data_9EL7
# 
_entry.id   9EL7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9EL7         pdb_00009el7 10.2210/pdb9el7/pdb 
WWPDB D_1000290734 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-05 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EL7 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-04 
_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              andrea.mattevi@unipv.it 
_pdbx_contact_author.name_first         Andrea 
_pdbx_contact_author.name_last          Mattevi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9523-7128 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Caroli, J.'  1 0000-0001-8954-8045 
'Mattevi, A.' 2 0000-0002-9523-7128 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'to be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Distal drug resistance mutations promote covalent inhibitor-adduct Grob fragmentation in LSD1' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Caroli, J.'  1 0000-0001-8954-8045 
primary 'Mattevi, A.' 2 0000-0002-9523-7128 
# 
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 'Lysine-specific histone demethylase 1A' 95051.633 1 1.14.99.66 ? ? ? 
2 polymer     man 'REST corepressor 1' 16459.742 1 ?          ? ? ? 
3 non-polymer syn 
;[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl (2S,3S,4R)-5-[(4aS)-7,8-dimethyl-4a-[(1R)-1-{3-[(5-methyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl}-3-oxopropyl]-2,4-dioxo-3,4,4a,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl dihydrogen diphosphate (non-preferred name)
;
1060.876  1 ?          ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 
;BRAF35-HDAC complex protein BHC110,Flavin-containing amine oxidase domain-containing protein 2,[histone H3]-dimethyl-L-lysine(4) FAD-dependent demethylase 1A
;
2 'Protein CoREST' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GSSHHHHHHSSGLVPRGSHMLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPR
KKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEER
NAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLW
LDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFG
MDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQE
FNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQ
YKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANA
TPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAV
LCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAP
ILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPIT
PGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM
;
;GSSHHHHHHSSGLVPRGSHMLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPR
KKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEER
NAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLW
LDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFG
MDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQE
FNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQ
YKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANA
TPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAV
LCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAP
ILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPIT
PGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM
;
A ? 
2 'polypeptide(L)' no no 
;GPLGSPEFRAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGIEPYRLPEVI
QKCNARWTTEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAE
;
;GPLGSPEFRAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGIEPYRLPEVI
QKCNARWTTEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAE
;
B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        
;[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl (2S,3S,4R)-5-[(4aS)-7,8-dimethyl-4a-[(1R)-1-{3-[(5-methyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl}-3-oxopropyl]-2,4-dioxo-3,4,4a,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl dihydrogen diphosphate (non-preferred name)
;
_pdbx_entity_nonpoly.comp_id     A1BI4 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   SER n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  SER n 
1 11  SER n 
1 12  GLY n 
1 13  LEU n 
1 14  VAL n 
1 15  PRO n 
1 16  ARG n 
1 17  GLY n 
1 18  SER n 
1 19  HIS n 
1 20  MET n 
1 21  LEU n 
1 22  SER n 
1 23  GLY n 
1 24  LYS n 
1 25  LYS n 
1 26  ALA n 
1 27  ALA n 
1 28  ALA n 
1 29  ALA n 
1 30  ALA n 
1 31  ALA n 
1 32  ALA n 
1 33  ALA n 
1 34  ALA n 
1 35  ALA n 
1 36  ALA n 
1 37  ALA n 
1 38  THR n 
1 39  GLY n 
1 40  THR n 
1 41  GLU n 
1 42  ALA n 
1 43  GLY n 
1 44  PRO n 
1 45  GLY n 
1 46  THR n 
1 47  ALA n 
1 48  GLY n 
1 49  GLY n 
1 50  SER n 
1 51  GLU n 
1 52  ASN n 
1 53  GLY n 
1 54  SER n 
1 55  GLU n 
1 56  VAL n 
1 57  ALA n 
1 58  ALA n 
1 59  GLN n 
1 60  PRO n 
1 61  ALA n 
1 62  GLY n 
1 63  LEU n 
1 64  SER n 
1 65  GLY n 
1 66  PRO n 
1 67  ALA n 
1 68  GLU n 
1 69  VAL n 
1 70  GLY n 
1 71  PRO n 
1 72  GLY n 
1 73  ALA n 
1 74  VAL n 
1 75  GLY n 
1 76  GLU n 
1 77  ARG n 
1 78  THR n 
1 79  PRO n 
1 80  ARG n 
1 81  LYS n 
1 82  LYS n 
1 83  GLU n 
1 84  PRO n 
1 85  PRO n 
1 86  ARG n 
1 87  ALA n 
1 88  SER n 
1 89  PRO n 
1 90  PRO n 
1 91  GLY n 
1 92  GLY n 
1 93  LEU n 
1 94  ALA n 
1 95  GLU n 
1 96  PRO n 
1 97  PRO n 
1 98  GLY n 
1 99  SER n 
1 100 ALA n 
1 101 GLY n 
1 102 PRO n 
1 103 GLN n 
1 104 ALA n 
1 105 GLY n 
1 106 PRO n 
1 107 THR n 
1 108 VAL n 
1 109 VAL n 
1 110 PRO n 
1 111 GLY n 
1 112 SER n 
1 113 ALA n 
1 114 THR n 
1 115 PRO n 
1 116 MET n 
1 117 GLU n 
1 118 THR n 
1 119 GLY n 
1 120 ILE n 
1 121 ALA n 
1 122 GLU n 
1 123 THR n 
1 124 PRO n 
1 125 GLU n 
1 126 GLY n 
1 127 ARG n 
1 128 ARG n 
1 129 THR n 
1 130 SER n 
1 131 ARG n 
1 132 ARG n 
1 133 LYS n 
1 134 ARG n 
1 135 ALA n 
1 136 LYS n 
1 137 VAL n 
1 138 GLU n 
1 139 TYR n 
1 140 ARG n 
1 141 GLU n 
1 142 MET n 
1 143 ASP n 
1 144 GLU n 
1 145 SER n 
1 146 LEU n 
1 147 ALA n 
1 148 ASN n 
1 149 LEU n 
1 150 SER n 
1 151 GLU n 
1 152 ASP n 
1 153 GLU n 
1 154 TYR n 
1 155 TYR n 
1 156 SER n 
1 157 GLU n 
1 158 GLU n 
1 159 GLU n 
1 160 ARG n 
1 161 ASN n 
1 162 ALA n 
1 163 LYS n 
1 164 ALA n 
1 165 GLU n 
1 166 LYS n 
1 167 GLU n 
1 168 LYS n 
1 169 LYS n 
1 170 LEU n 
1 171 PRO n 
1 172 PRO n 
1 173 PRO n 
1 174 PRO n 
1 175 PRO n 
1 176 GLN n 
1 177 ALA n 
1 178 PRO n 
1 179 PRO n 
1 180 GLU n 
1 181 GLU n 
1 182 GLU n 
1 183 ASN n 
1 184 GLU n 
1 185 SER n 
1 186 GLU n 
1 187 PRO n 
1 188 GLU n 
1 189 GLU n 
1 190 PRO n 
1 191 SER n 
1 192 GLY n 
1 193 VAL n 
1 194 GLU n 
1 195 GLY n 
1 196 ALA n 
1 197 ALA n 
1 198 PHE n 
1 199 GLN n 
1 200 SER n 
1 201 ARG n 
1 202 LEU n 
1 203 PRO n 
1 204 HIS n 
1 205 ASP n 
1 206 ARG n 
1 207 MET n 
1 208 THR n 
1 209 SER n 
1 210 GLN n 
1 211 GLU n 
1 212 ALA n 
1 213 ALA n 
1 214 CYS n 
1 215 PHE n 
1 216 PRO n 
1 217 ASP n 
1 218 ILE n 
1 219 ILE n 
1 220 SER n 
1 221 GLY n 
1 222 PRO n 
1 223 GLN n 
1 224 GLN n 
1 225 THR n 
1 226 GLN n 
1 227 LYS n 
1 228 VAL n 
1 229 PHE n 
1 230 LEU n 
1 231 PHE n 
1 232 ILE n 
1 233 ARG n 
1 234 ASN n 
1 235 ARG n 
1 236 THR n 
1 237 LEU n 
1 238 GLN n 
1 239 LEU n 
1 240 TRP n 
1 241 LEU n 
1 242 ASP n 
1 243 ASN n 
1 244 PRO n 
1 245 LYS n 
1 246 ILE n 
1 247 GLN n 
1 248 LEU n 
1 249 THR n 
1 250 PHE n 
1 251 GLU n 
1 252 ALA n 
1 253 THR n 
1 254 LEU n 
1 255 GLN n 
1 256 GLN n 
1 257 LEU n 
1 258 GLU n 
1 259 ALA n 
1 260 PRO n 
1 261 TYR n 
1 262 ASN n 
1 263 SER n 
1 264 ASP n 
1 265 THR n 
1 266 VAL n 
1 267 LEU n 
1 268 VAL n 
1 269 HIS n 
1 270 ARG n 
1 271 VAL n 
1 272 HIS n 
1 273 SER n 
1 274 TYR n 
1 275 LEU n 
1 276 GLU n 
1 277 ARG n 
1 278 HIS n 
1 279 GLY n 
1 280 LEU n 
1 281 ILE n 
1 282 ASN n 
1 283 PHE n 
1 284 GLY n 
1 285 ILE n 
1 286 TYR n 
1 287 LYS n 
1 288 ARG n 
1 289 ILE n 
1 290 LYS n 
1 291 PRO n 
1 292 LEU n 
1 293 PRO n 
1 294 THR n 
1 295 LYS n 
1 296 LYS n 
1 297 THR n 
1 298 GLY n 
1 299 LYS n 
1 300 VAL n 
1 301 ILE n 
1 302 ILE n 
1 303 ILE n 
1 304 GLY n 
1 305 SER n 
1 306 GLY n 
1 307 VAL n 
1 308 SER n 
1 309 GLY n 
1 310 LEU n 
1 311 ALA n 
1 312 ALA n 
1 313 ALA n 
1 314 ARG n 
1 315 GLN n 
1 316 LEU n 
1 317 GLN n 
1 318 SER n 
1 319 PHE n 
1 320 GLY n 
1 321 MET n 
1 322 ASP n 
1 323 VAL n 
1 324 THR n 
1 325 LEU n 
1 326 LEU n 
1 327 GLU n 
1 328 ALA n 
1 329 ARG n 
1 330 ASP n 
1 331 ARG n 
1 332 VAL n 
1 333 GLY n 
1 334 GLY n 
1 335 ARG n 
1 336 VAL n 
1 337 ALA n 
1 338 THR n 
1 339 PHE n 
1 340 ARG n 
1 341 LYS n 
1 342 GLY n 
1 343 ASN n 
1 344 TYR n 
1 345 VAL n 
1 346 ALA n 
1 347 ASP n 
1 348 LEU n 
1 349 GLY n 
1 350 ALA n 
1 351 MET n 
1 352 VAL n 
1 353 VAL n 
1 354 THR n 
1 355 GLY n 
1 356 LEU n 
1 357 GLY n 
1 358 GLY n 
1 359 ASN n 
1 360 PRO n 
1 361 MET n 
1 362 ALA n 
1 363 VAL n 
1 364 VAL n 
1 365 SER n 
1 366 LYS n 
1 367 GLN n 
1 368 VAL n 
1 369 ASN n 
1 370 MET n 
1 371 GLU n 
1 372 LEU n 
1 373 ALA n 
1 374 LYS n 
1 375 ILE n 
1 376 LYS n 
1 377 GLN n 
1 378 LYS n 
1 379 CYS n 
1 380 PRO n 
1 381 LEU n 
1 382 TYR n 
1 383 GLU n 
1 384 ALA n 
1 385 ASN n 
1 386 GLY n 
1 387 GLN n 
1 388 ALA n 
1 389 VAL n 
1 390 PRO n 
1 391 LYS n 
1 392 GLU n 
1 393 LYS n 
1 394 ASP n 
1 395 GLU n 
1 396 MET n 
1 397 VAL n 
1 398 GLU n 
1 399 GLN n 
1 400 GLU n 
1 401 PHE n 
1 402 ASN n 
1 403 ARG n 
1 404 LEU n 
1 405 LEU n 
1 406 GLU n 
1 407 ALA n 
1 408 THR n 
1 409 SER n 
1 410 TYR n 
1 411 LEU n 
1 412 SER n 
1 413 HIS n 
1 414 GLN n 
1 415 LEU n 
1 416 ASP n 
1 417 PHE n 
1 418 ASN n 
1 419 VAL n 
1 420 LEU n 
1 421 ASN n 
1 422 ASN n 
1 423 LYS n 
1 424 PRO n 
1 425 VAL n 
1 426 SER n 
1 427 LEU n 
1 428 GLY n 
1 429 GLN n 
1 430 ALA n 
1 431 LEU n 
1 432 GLU n 
1 433 VAL n 
1 434 VAL n 
1 435 ILE n 
1 436 GLN n 
1 437 LEU n 
1 438 GLN n 
1 439 GLU n 
1 440 LYS n 
1 441 HIS n 
1 442 VAL n 
1 443 LYS n 
1 444 ASP n 
1 445 GLU n 
1 446 GLN n 
1 447 ILE n 
1 448 GLU n 
1 449 HIS n 
1 450 TRP n 
1 451 LYS n 
1 452 LYS n 
1 453 ILE n 
1 454 VAL n 
1 455 LYS n 
1 456 THR n 
1 457 GLN n 
1 458 GLU n 
1 459 GLU n 
1 460 LEU n 
1 461 LYS n 
1 462 GLU n 
1 463 LEU n 
1 464 LEU n 
1 465 ASN n 
1 466 LYS n 
1 467 MET n 
1 468 VAL n 
1 469 ASN n 
1 470 LEU n 
1 471 LYS n 
1 472 GLU n 
1 473 LYS n 
1 474 ILE n 
1 475 LYS n 
1 476 GLU n 
1 477 LEU n 
1 478 HIS n 
1 479 GLN n 
1 480 GLN n 
1 481 TYR n 
1 482 LYS n 
1 483 GLU n 
1 484 ALA n 
1 485 SER n 
1 486 GLU n 
1 487 VAL n 
1 488 LYS n 
1 489 PRO n 
1 490 PRO n 
1 491 ARG n 
1 492 ASP n 
1 493 ILE n 
1 494 THR n 
1 495 ALA n 
1 496 GLU n 
1 497 PHE n 
1 498 LEU n 
1 499 VAL n 
1 500 LYS n 
1 501 SER n 
1 502 LYS n 
1 503 HIS n 
1 504 ARG n 
1 505 ASP n 
1 506 LEU n 
1 507 THR n 
1 508 ALA n 
1 509 LEU n 
1 510 CYS n 
1 511 LYS n 
1 512 GLU n 
1 513 TYR n 
1 514 ASP n 
1 515 GLU n 
1 516 LEU n 
1 517 ALA n 
1 518 GLU n 
1 519 THR n 
1 520 GLN n 
1 521 GLY n 
1 522 LYS n 
1 523 LEU n 
1 524 GLU n 
1 525 GLU n 
1 526 LYS n 
1 527 LEU n 
1 528 GLN n 
1 529 GLU n 
1 530 LEU n 
1 531 GLU n 
1 532 ALA n 
1 533 ASN n 
1 534 PRO n 
1 535 PRO n 
1 536 SER n 
1 537 ASP n 
1 538 VAL n 
1 539 TYR n 
1 540 LEU n 
1 541 SER n 
1 542 SER n 
1 543 ARG n 
1 544 ASP n 
1 545 ARG n 
1 546 GLN n 
1 547 ILE n 
1 548 LEU n 
1 549 ASP n 
1 550 TRP n 
1 551 HIS n 
1 552 PHE n 
1 553 ALA n 
1 554 ASN n 
1 555 LEU n 
1 556 GLU n 
1 557 PHE n 
1 558 ALA n 
1 559 ASN n 
1 560 ALA n 
1 561 THR n 
1 562 PRO n 
1 563 LEU n 
1 564 SER n 
1 565 THR n 
1 566 LEU n 
1 567 SER n 
1 568 LEU n 
1 569 LYS n 
1 570 HIS n 
1 571 TRP n 
1 572 ASP n 
1 573 GLN n 
1 574 ASP n 
1 575 ASP n 
1 576 ASP n 
1 577 PHE n 
1 578 GLU n 
1 579 PHE n 
1 580 THR n 
1 581 GLY n 
1 582 SER n 
1 583 HIS n 
1 584 LEU n 
1 585 THR n 
1 586 VAL n 
1 587 ARG n 
1 588 ASN n 
1 589 GLY n 
1 590 TYR n 
1 591 SER n 
1 592 CYS n 
1 593 VAL n 
1 594 PRO n 
1 595 VAL n 
1 596 ALA n 
1 597 LEU n 
1 598 ALA n 
1 599 GLU n 
1 600 GLY n 
1 601 LEU n 
1 602 ASP n 
1 603 ILE n 
1 604 LYS n 
1 605 LEU n 
1 606 ASN n 
1 607 THR n 
1 608 ALA n 
1 609 VAL n 
1 610 ARG n 
1 611 GLN n 
1 612 VAL n 
1 613 ARG n 
1 614 TYR n 
1 615 THR n 
1 616 ALA n 
1 617 SER n 
1 618 GLY n 
1 619 CYS n 
1 620 GLU n 
1 621 VAL n 
1 622 ILE n 
1 623 ALA n 
1 624 VAL n 
1 625 ASN n 
1 626 THR n 
1 627 ARG n 
1 628 SER n 
1 629 THR n 
1 630 SER n 
1 631 GLN n 
1 632 THR n 
1 633 PHE n 
1 634 ILE n 
1 635 TYR n 
1 636 LYS n 
1 637 CYS n 
1 638 ASP n 
1 639 ALA n 
1 640 VAL n 
1 641 LEU n 
1 642 CYS n 
1 643 THR n 
1 644 LEU n 
1 645 PRO n 
1 646 LEU n 
1 647 GLY n 
1 648 VAL n 
1 649 LEU n 
1 650 LYS n 
1 651 GLN n 
1 652 GLN n 
1 653 PRO n 
1 654 PRO n 
1 655 ALA n 
1 656 VAL n 
1 657 GLN n 
1 658 PHE n 
1 659 VAL n 
1 660 PRO n 
1 661 PRO n 
1 662 LEU n 
1 663 PRO n 
1 664 GLU n 
1 665 TRP n 
1 666 LYS n 
1 667 THR n 
1 668 SER n 
1 669 ALA n 
1 670 VAL n 
1 671 GLN n 
1 672 ARG n 
1 673 MET n 
1 674 GLY n 
1 675 PHE n 
1 676 GLY n 
1 677 ASN n 
1 678 LEU n 
1 679 ASN n 
1 680 LYS n 
1 681 VAL n 
1 682 VAL n 
1 683 LEU n 
1 684 CYS n 
1 685 PHE n 
1 686 ASP n 
1 687 ARG n 
1 688 VAL n 
1 689 PHE n 
1 690 TRP n 
1 691 ASP n 
1 692 PRO n 
1 693 SER n 
1 694 VAL n 
1 695 ASN n 
1 696 LEU n 
1 697 PHE n 
1 698 GLY n 
1 699 HIS n 
1 700 VAL n 
1 701 GLY n 
1 702 SER n 
1 703 THR n 
1 704 THR n 
1 705 ALA n 
1 706 SER n 
1 707 ARG n 
1 708 GLY n 
1 709 GLU n 
1 710 LEU n 
1 711 PHE n 
1 712 LEU n 
1 713 PHE n 
1 714 TRP n 
1 715 ASN n 
1 716 LEU n 
1 717 TYR n 
1 718 LYS n 
1 719 ALA n 
1 720 PRO n 
1 721 ILE n 
1 722 LEU n 
1 723 LEU n 
1 724 ALA n 
1 725 LEU n 
1 726 VAL n 
1 727 ALA n 
1 728 GLY n 
1 729 GLU n 
1 730 ALA n 
1 731 ALA n 
1 732 GLY n 
1 733 ILE n 
1 734 MET n 
1 735 GLU n 
1 736 ASN n 
1 737 ILE n 
1 738 SER n 
1 739 ASP n 
1 740 ASP n 
1 741 VAL n 
1 742 ILE n 
1 743 VAL n 
1 744 GLY n 
1 745 ARG n 
1 746 CYS n 
1 747 LEU n 
1 748 ALA n 
1 749 ILE n 
1 750 LEU n 
1 751 LYS n 
1 752 GLY n 
1 753 ILE n 
1 754 PHE n 
1 755 GLY n 
1 756 SER n 
1 757 SER n 
1 758 ALA n 
1 759 VAL n 
1 760 PRO n 
1 761 GLN n 
1 762 PRO n 
1 763 LYS n 
1 764 GLU n 
1 765 THR n 
1 766 VAL n 
1 767 VAL n 
1 768 SER n 
1 769 ARG n 
1 770 TRP n 
1 771 ARG n 
1 772 ALA n 
1 773 ASP n 
1 774 PRO n 
1 775 TRP n 
1 776 ALA n 
1 777 ARG n 
1 778 GLY n 
1 779 SER n 
1 780 TYR n 
1 781 SER n 
1 782 TYR n 
1 783 VAL n 
1 784 ALA n 
1 785 ALA n 
1 786 GLY n 
1 787 SER n 
1 788 SER n 
1 789 GLY n 
1 790 ASN n 
1 791 ASP n 
1 792 TYR n 
1 793 ASP n 
1 794 LEU n 
1 795 MET n 
1 796 ALA n 
1 797 GLN n 
1 798 PRO n 
1 799 ILE n 
1 800 THR n 
1 801 PRO n 
1 802 GLY n 
1 803 PRO n 
1 804 SER n 
1 805 ILE n 
1 806 PRO n 
1 807 GLY n 
1 808 ALA n 
1 809 PRO n 
1 810 GLN n 
1 811 PRO n 
1 812 ILE n 
1 813 PRO n 
1 814 ARG n 
1 815 LEU n 
1 816 PHE n 
1 817 PHE n 
1 818 ALA n 
1 819 GLY n 
1 820 GLU n 
1 821 HIS n 
1 822 THR n 
1 823 ILE n 
1 824 ARG n 
1 825 ASN n 
1 826 TYR n 
1 827 PRO n 
1 828 ALA n 
1 829 THR n 
1 830 VAL n 
1 831 HIS n 
1 832 GLY n 
1 833 ALA n 
1 834 LEU n 
1 835 LEU n 
1 836 SER n 
1 837 GLY n 
1 838 LEU n 
1 839 ARG n 
1 840 GLU n 
1 841 ALA n 
1 842 GLY n 
1 843 ARG n 
1 844 ILE n 
1 845 ALA n 
1 846 ASP n 
1 847 GLN n 
1 848 PHE n 
1 849 LEU n 
1 850 GLY n 
1 851 ALA n 
1 852 MET n 
1 853 TYR n 
1 854 THR n 
1 855 LEU n 
1 856 PRO n 
1 857 ARG n 
1 858 GLN n 
1 859 ALA n 
1 860 THR n 
1 861 PRO n 
1 862 GLY n 
1 863 VAL n 
1 864 PRO n 
1 865 ALA n 
1 866 GLN n 
1 867 GLN n 
1 868 SER n 
1 869 PRO n 
1 870 SER n 
1 871 MET n 
2 1   GLY n 
2 2   PRO n 
2 3   LEU n 
2 4   GLY n 
2 5   SER n 
2 6   PRO n 
2 7   GLU n 
2 8   PHE n 
2 9   ARG n 
2 10  ALA n 
2 11  LYS n 
2 12  ARG n 
2 13  LYS n 
2 14  PRO n 
2 15  PRO n 
2 16  LYS n 
2 17  GLY n 
2 18  MET n 
2 19  PHE n 
2 20  LEU n 
2 21  SER n 
2 22  GLN n 
2 23  GLU n 
2 24  ASP n 
2 25  VAL n 
2 26  GLU n 
2 27  ALA n 
2 28  VAL n 
2 29  SER n 
2 30  ALA n 
2 31  ASN n 
2 32  ALA n 
2 33  THR n 
2 34  ALA n 
2 35  ALA n 
2 36  THR n 
2 37  THR n 
2 38  VAL n 
2 39  LEU n 
2 40  ARG n 
2 41  GLN n 
2 42  LEU n 
2 43  ASP n 
2 44  MET n 
2 45  GLU n 
2 46  LEU n 
2 47  VAL n 
2 48  SER n 
2 49  VAL n 
2 50  LYS n 
2 51  ARG n 
2 52  GLN n 
2 53  ILE n 
2 54  GLN n 
2 55  ASN n 
2 56  ILE n 
2 57  LYS n 
2 58  GLN n 
2 59  THR n 
2 60  ASN n 
2 61  SER n 
2 62  ALA n 
2 63  LEU n 
2 64  LYS n 
2 65  GLU n 
2 66  LYS n 
2 67  LEU n 
2 68  ASP n 
2 69  GLY n 
2 70  GLY n 
2 71  ILE n 
2 72  GLU n 
2 73  PRO n 
2 74  TYR n 
2 75  ARG n 
2 76  LEU n 
2 77  PRO n 
2 78  GLU n 
2 79  VAL n 
2 80  ILE n 
2 81  GLN n 
2 82  LYS n 
2 83  CYS n 
2 84  ASN n 
2 85  ALA n 
2 86  ARG n 
2 87  TRP n 
2 88  THR n 
2 89  THR n 
2 90  GLU n 
2 91  GLU n 
2 92  GLN n 
2 93  LEU n 
2 94  LEU n 
2 95  ALA n 
2 96  VAL n 
2 97  GLN n 
2 98  ALA n 
2 99  ILE n 
2 100 ARG n 
2 101 LYS n 
2 102 TYR n 
2 103 GLY n 
2 104 ARG n 
2 105 ASP n 
2 106 PHE n 
2 107 GLN n 
2 108 ALA n 
2 109 ILE n 
2 110 SER n 
2 111 ASP n 
2 112 VAL n 
2 113 ILE n 
2 114 GLY n 
2 115 ASN n 
2 116 LYS n 
2 117 SER n 
2 118 VAL n 
2 119 VAL n 
2 120 GLN n 
2 121 VAL n 
2 122 LYS n 
2 123 ASN n 
2 124 PHE n 
2 125 PHE n 
2 126 VAL n 
2 127 ASN n 
2 128 TYR n 
2 129 ARG n 
2 130 ARG n 
2 131 ARG n 
2 132 PHE n 
2 133 ASN n 
2 134 ILE n 
2 135 ASP n 
2 136 GLU n 
2 137 VAL n 
2 138 LEU n 
2 139 GLN n 
2 140 GLU n 
2 141 TRP n 
2 142 GLU n 
2 143 ALA n 
2 144 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 871 human ? 'KDM1A, AOF2, KDM1, KIAA0601, LSD1' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 144 human ? 'RCOR1, KIAA0071, RCOR'             ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1BI4 non-polymer         . 
;[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl (2S,3S,4R)-5-[(4aS)-7,8-dimethyl-4a-[(1R)-1-{3-[(5-methyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl}-3-oxopropyl]-2,4-dioxo-3,4,4a,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl dihydrogen diphosphate (non-preferred name)
;
? 'C40 H46 N12 O17 P2 S' 1060.876 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'           89.093   
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'       175.209  
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'          132.118  
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'           133.103  
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'         121.158  
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'         146.144  
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'           147.129  
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'           75.067   
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'       156.162  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'          131.173  
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'          131.173  
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'       147.195  
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'        149.211  
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'          165.189  
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'           115.130  
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'           105.093  
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'           119.119  
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'        204.225  
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'          181.189  
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'          117.146  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -18 ?   ?   ?   A . n 
A 1 2   SER 2   -17 ?   ?   ?   A . n 
A 1 3   SER 3   -16 ?   ?   ?   A . n 
A 1 4   HIS 4   -15 ?   ?   ?   A . n 
A 1 5   HIS 5   -14 ?   ?   ?   A . n 
A 1 6   HIS 6   -13 ?   ?   ?   A . n 
A 1 7   HIS 7   -12 ?   ?   ?   A . n 
A 1 8   HIS 8   -11 ?   ?   ?   A . n 
A 1 9   HIS 9   -10 ?   ?   ?   A . n 
A 1 10  SER 10  -9  ?   ?   ?   A . n 
A 1 11  SER 11  -8  ?   ?   ?   A . n 
A 1 12  GLY 12  -7  ?   ?   ?   A . n 
A 1 13  LEU 13  -6  ?   ?   ?   A . n 
A 1 14  VAL 14  -5  ?   ?   ?   A . n 
A 1 15  PRO 15  -4  ?   ?   ?   A . n 
A 1 16  ARG 16  -3  ?   ?   ?   A . n 
A 1 17  GLY 17  -2  ?   ?   ?   A . n 
A 1 18  SER 18  -1  ?   ?   ?   A . n 
A 1 19  HIS 19  0   ?   ?   ?   A . n 
A 1 20  MET 20  1   ?   ?   ?   A . n 
A 1 21  LEU 21  2   ?   ?   ?   A . n 
A 1 22  SER 22  3   ?   ?   ?   A . n 
A 1 23  GLY 23  4   ?   ?   ?   A . n 
A 1 24  LYS 24  5   ?   ?   ?   A . n 
A 1 25  LYS 25  6   ?   ?   ?   A . n 
A 1 26  ALA 26  7   ?   ?   ?   A . n 
A 1 27  ALA 27  8   ?   ?   ?   A . n 
A 1 28  ALA 28  9   ?   ?   ?   A . n 
A 1 29  ALA 29  10  ?   ?   ?   A . n 
A 1 30  ALA 30  11  ?   ?   ?   A . n 
A 1 31  ALA 31  12  ?   ?   ?   A . n 
A 1 32  ALA 32  13  ?   ?   ?   A . n 
A 1 33  ALA 33  14  ?   ?   ?   A . n 
A 1 34  ALA 34  15  ?   ?   ?   A . n 
A 1 35  ALA 35  16  ?   ?   ?   A . n 
A 1 36  ALA 36  17  ?   ?   ?   A . n 
A 1 37  ALA 37  18  ?   ?   ?   A . n 
A 1 38  THR 38  19  ?   ?   ?   A . n 
A 1 39  GLY 39  20  ?   ?   ?   A . n 
A 1 40  THR 40  21  ?   ?   ?   A . n 
A 1 41  GLU 41  22  ?   ?   ?   A . n 
A 1 42  ALA 42  23  ?   ?   ?   A . n 
A 1 43  GLY 43  24  ?   ?   ?   A . n 
A 1 44  PRO 44  25  ?   ?   ?   A . n 
A 1 45  GLY 45  26  ?   ?   ?   A . n 
A 1 46  THR 46  27  ?   ?   ?   A . n 
A 1 47  ALA 47  28  ?   ?   ?   A . n 
A 1 48  GLY 48  29  ?   ?   ?   A . n 
A 1 49  GLY 49  30  ?   ?   ?   A . n 
A 1 50  SER 50  31  ?   ?   ?   A . n 
A 1 51  GLU 51  32  ?   ?   ?   A . n 
A 1 52  ASN 52  33  ?   ?   ?   A . n 
A 1 53  GLY 53  34  ?   ?   ?   A . n 
A 1 54  SER 54  35  ?   ?   ?   A . n 
A 1 55  GLU 55  36  ?   ?   ?   A . n 
A 1 56  VAL 56  37  ?   ?   ?   A . n 
A 1 57  ALA 57  38  ?   ?   ?   A . n 
A 1 58  ALA 58  39  ?   ?   ?   A . n 
A 1 59  GLN 59  40  ?   ?   ?   A . n 
A 1 60  PRO 60  41  ?   ?   ?   A . n 
A 1 61  ALA 61  42  ?   ?   ?   A . n 
A 1 62  GLY 62  43  ?   ?   ?   A . n 
A 1 63  LEU 63  44  ?   ?   ?   A . n 
A 1 64  SER 64  45  ?   ?   ?   A . n 
A 1 65  GLY 65  46  ?   ?   ?   A . n 
A 1 66  PRO 66  47  ?   ?   ?   A . n 
A 1 67  ALA 67  48  ?   ?   ?   A . n 
A 1 68  GLU 68  49  ?   ?   ?   A . n 
A 1 69  VAL 69  50  ?   ?   ?   A . n 
A 1 70  GLY 70  51  ?   ?   ?   A . n 
A 1 71  PRO 71  52  ?   ?   ?   A . n 
A 1 72  GLY 72  53  ?   ?   ?   A . n 
A 1 73  ALA 73  54  ?   ?   ?   A . n 
A 1 74  VAL 74  55  ?   ?   ?   A . n 
A 1 75  GLY 75  56  ?   ?   ?   A . n 
A 1 76  GLU 76  57  ?   ?   ?   A . n 
A 1 77  ARG 77  58  ?   ?   ?   A . n 
A 1 78  THR 78  59  ?   ?   ?   A . n 
A 1 79  PRO 79  60  ?   ?   ?   A . n 
A 1 80  ARG 80  61  ?   ?   ?   A . n 
A 1 81  LYS 81  62  ?   ?   ?   A . n 
A 1 82  LYS 82  63  ?   ?   ?   A . n 
A 1 83  GLU 83  64  ?   ?   ?   A . n 
A 1 84  PRO 84  65  ?   ?   ?   A . n 
A 1 85  PRO 85  66  ?   ?   ?   A . n 
A 1 86  ARG 86  67  ?   ?   ?   A . n 
A 1 87  ALA 87  68  ?   ?   ?   A . n 
A 1 88  SER 88  69  ?   ?   ?   A . n 
A 1 89  PRO 89  70  ?   ?   ?   A . n 
A 1 90  PRO 90  71  ?   ?   ?   A . n 
A 1 91  GLY 91  72  ?   ?   ?   A . n 
A 1 92  GLY 92  73  ?   ?   ?   A . n 
A 1 93  LEU 93  74  ?   ?   ?   A . n 
A 1 94  ALA 94  75  ?   ?   ?   A . n 
A 1 95  GLU 95  76  ?   ?   ?   A . n 
A 1 96  PRO 96  77  ?   ?   ?   A . n 
A 1 97  PRO 97  78  ?   ?   ?   A . n 
A 1 98  GLY 98  79  ?   ?   ?   A . n 
A 1 99  SER 99  80  ?   ?   ?   A . n 
A 1 100 ALA 100 81  ?   ?   ?   A . n 
A 1 101 GLY 101 82  ?   ?   ?   A . n 
A 1 102 PRO 102 83  ?   ?   ?   A . n 
A 1 103 GLN 103 84  ?   ?   ?   A . n 
A 1 104 ALA 104 85  ?   ?   ?   A . n 
A 1 105 GLY 105 86  ?   ?   ?   A . n 
A 1 106 PRO 106 87  ?   ?   ?   A . n 
A 1 107 THR 107 88  ?   ?   ?   A . n 
A 1 108 VAL 108 89  ?   ?   ?   A . n 
A 1 109 VAL 109 90  ?   ?   ?   A . n 
A 1 110 PRO 110 91  ?   ?   ?   A . n 
A 1 111 GLY 111 92  ?   ?   ?   A . n 
A 1 112 SER 112 93  ?   ?   ?   A . n 
A 1 113 ALA 113 94  ?   ?   ?   A . n 
A 1 114 THR 114 95  ?   ?   ?   A . n 
A 1 115 PRO 115 96  ?   ?   ?   A . n 
A 1 116 MET 116 97  ?   ?   ?   A . n 
A 1 117 GLU 117 98  ?   ?   ?   A . n 
A 1 118 THR 118 99  ?   ?   ?   A . n 
A 1 119 GLY 119 100 ?   ?   ?   A . n 
A 1 120 ILE 120 101 ?   ?   ?   A . n 
A 1 121 ALA 121 102 ?   ?   ?   A . n 
A 1 122 GLU 122 103 ?   ?   ?   A . n 
A 1 123 THR 123 104 ?   ?   ?   A . n 
A 1 124 PRO 124 105 ?   ?   ?   A . n 
A 1 125 GLU 125 106 ?   ?   ?   A . n 
A 1 126 GLY 126 107 ?   ?   ?   A . n 
A 1 127 ARG 127 108 ?   ?   ?   A . n 
A 1 128 ARG 128 109 ?   ?   ?   A . n 
A 1 129 THR 129 110 ?   ?   ?   A . n 
A 1 130 SER 130 111 ?   ?   ?   A . n 
A 1 131 ARG 131 112 ?   ?   ?   A . n 
A 1 132 ARG 132 113 ?   ?   ?   A . n 
A 1 133 LYS 133 114 ?   ?   ?   A . n 
A 1 134 ARG 134 115 ?   ?   ?   A . n 
A 1 135 ALA 135 116 ?   ?   ?   A . n 
A 1 136 LYS 136 117 ?   ?   ?   A . n 
A 1 137 VAL 137 118 ?   ?   ?   A . n 
A 1 138 GLU 138 119 ?   ?   ?   A . n 
A 1 139 TYR 139 120 ?   ?   ?   A . n 
A 1 140 ARG 140 121 ?   ?   ?   A . n 
A 1 141 GLU 141 122 ?   ?   ?   A . n 
A 1 142 MET 142 123 ?   ?   ?   A . n 
A 1 143 ASP 143 124 ?   ?   ?   A . n 
A 1 144 GLU 144 125 ?   ?   ?   A . n 
A 1 145 SER 145 126 ?   ?   ?   A . n 
A 1 146 LEU 146 127 ?   ?   ?   A . n 
A 1 147 ALA 147 128 ?   ?   ?   A . n 
A 1 148 ASN 148 129 ?   ?   ?   A . n 
A 1 149 LEU 149 130 ?   ?   ?   A . n 
A 1 150 SER 150 131 ?   ?   ?   A . n 
A 1 151 GLU 151 132 ?   ?   ?   A . n 
A 1 152 ASP 152 133 ?   ?   ?   A . n 
A 1 153 GLU 153 134 ?   ?   ?   A . n 
A 1 154 TYR 154 135 ?   ?   ?   A . n 
A 1 155 TYR 155 136 ?   ?   ?   A . n 
A 1 156 SER 156 137 ?   ?   ?   A . n 
A 1 157 GLU 157 138 ?   ?   ?   A . n 
A 1 158 GLU 158 139 ?   ?   ?   A . n 
A 1 159 GLU 159 140 ?   ?   ?   A . n 
A 1 160 ARG 160 141 ?   ?   ?   A . n 
A 1 161 ASN 161 142 ?   ?   ?   A . n 
A 1 162 ALA 162 143 ?   ?   ?   A . n 
A 1 163 LYS 163 144 ?   ?   ?   A . n 
A 1 164 ALA 164 145 ?   ?   ?   A . n 
A 1 165 GLU 165 146 ?   ?   ?   A . n 
A 1 166 LYS 166 147 ?   ?   ?   A . n 
A 1 167 GLU 167 148 ?   ?   ?   A . n 
A 1 168 LYS 168 149 ?   ?   ?   A . n 
A 1 169 LYS 169 150 ?   ?   ?   A . n 
A 1 170 LEU 170 151 ?   ?   ?   A . n 
A 1 171 PRO 171 152 ?   ?   ?   A . n 
A 1 172 PRO 172 153 ?   ?   ?   A . n 
A 1 173 PRO 173 154 ?   ?   ?   A . n 
A 1 174 PRO 174 155 ?   ?   ?   A . n 
A 1 175 PRO 175 156 ?   ?   ?   A . n 
A 1 176 GLN 176 157 ?   ?   ?   A . n 
A 1 177 ALA 177 158 ?   ?   ?   A . n 
A 1 178 PRO 178 159 ?   ?   ?   A . n 
A 1 179 PRO 179 160 ?   ?   ?   A . n 
A 1 180 GLU 180 161 ?   ?   ?   A . n 
A 1 181 GLU 181 162 ?   ?   ?   A . n 
A 1 182 GLU 182 163 ?   ?   ?   A . n 
A 1 183 ASN 183 164 ?   ?   ?   A . n 
A 1 184 GLU 184 165 ?   ?   ?   A . n 
A 1 185 SER 185 166 ?   ?   ?   A . n 
A 1 186 GLU 186 167 ?   ?   ?   A . n 
A 1 187 PRO 187 168 ?   ?   ?   A . n 
A 1 188 GLU 188 169 ?   ?   ?   A . n 
A 1 189 GLU 189 170 ?   ?   ?   A . n 
A 1 190 PRO 190 171 171 PRO PRO A . n 
A 1 191 SER 191 172 172 SER SER A . n 
A 1 192 GLY 192 173 173 GLY GLY A . n 
A 1 193 VAL 193 174 174 VAL VAL A . n 
A 1 194 GLU 194 175 175 GLU GLU A . n 
A 1 195 GLY 195 176 176 GLY GLY A . n 
A 1 196 ALA 196 177 177 ALA ALA A . n 
A 1 197 ALA 197 178 178 ALA ALA A . n 
A 1 198 PHE 198 179 179 PHE PHE A . n 
A 1 199 GLN 199 180 180 GLN GLN A . n 
A 1 200 SER 200 181 181 SER SER A . n 
A 1 201 ARG 201 182 182 ARG ARG A . n 
A 1 202 LEU 202 183 183 LEU LEU A . n 
A 1 203 PRO 203 184 184 PRO PRO A . n 
A 1 204 HIS 204 185 185 HIS HIS A . n 
A 1 205 ASP 205 186 186 ASP ASP A . n 
A 1 206 ARG 206 187 187 ARG ARG A . n 
A 1 207 MET 207 188 188 MET MET A . n 
A 1 208 THR 208 189 189 THR THR A . n 
A 1 209 SER 209 190 190 SER SER A . n 
A 1 210 GLN 210 191 191 GLN GLN A . n 
A 1 211 GLU 211 192 192 GLU GLU A . n 
A 1 212 ALA 212 193 193 ALA ALA A . n 
A 1 213 ALA 213 194 194 ALA ALA A . n 
A 1 214 CYS 214 195 195 CYS CYS A . n 
A 1 215 PHE 215 196 196 PHE PHE A . n 
A 1 216 PRO 216 197 197 PRO PRO A . n 
A 1 217 ASP 217 198 198 ASP ASP A . n 
A 1 218 ILE 218 199 199 ILE ILE A . n 
A 1 219 ILE 219 200 200 ILE ILE A . n 
A 1 220 SER 220 201 201 SER SER A . n 
A 1 221 GLY 221 202 202 GLY GLY A . n 
A 1 222 PRO 222 203 203 PRO PRO A . n 
A 1 223 GLN 223 204 204 GLN GLN A . n 
A 1 224 GLN 224 205 205 GLN GLN A . n 
A 1 225 THR 225 206 206 THR THR A . n 
A 1 226 GLN 226 207 207 GLN GLN A . n 
A 1 227 LYS 227 208 208 LYS LYS A . n 
A 1 228 VAL 228 209 209 VAL VAL A . n 
A 1 229 PHE 229 210 210 PHE PHE A . n 
A 1 230 LEU 230 211 211 LEU LEU A . n 
A 1 231 PHE 231 212 212 PHE PHE A . n 
A 1 232 ILE 232 213 213 ILE ILE A . n 
A 1 233 ARG 233 214 214 ARG ARG A . n 
A 1 234 ASN 234 215 215 ASN ASN A . n 
A 1 235 ARG 235 216 216 ARG ARG A . n 
A 1 236 THR 236 217 217 THR THR A . n 
A 1 237 LEU 237 218 218 LEU LEU A . n 
A 1 238 GLN 238 219 219 GLN GLN A . n 
A 1 239 LEU 239 220 220 LEU LEU A . n 
A 1 240 TRP 240 221 221 TRP TRP A . n 
A 1 241 LEU 241 222 222 LEU LEU A . n 
A 1 242 ASP 242 223 223 ASP ASP A . n 
A 1 243 ASN 243 224 224 ASN ASN A . n 
A 1 244 PRO 244 225 225 PRO PRO A . n 
A 1 245 LYS 245 226 226 LYS LYS A . n 
A 1 246 ILE 246 227 227 ILE ILE A . n 
A 1 247 GLN 247 228 228 GLN GLN A . n 
A 1 248 LEU 248 229 229 LEU LEU A . n 
A 1 249 THR 249 230 230 THR THR A . n 
A 1 250 PHE 250 231 231 PHE PHE A . n 
A 1 251 GLU 251 232 232 GLU GLU A . n 
A 1 252 ALA 252 233 233 ALA ALA A . n 
A 1 253 THR 253 234 234 THR THR A . n 
A 1 254 LEU 254 235 235 LEU LEU A . n 
A 1 255 GLN 255 236 236 GLN GLN A . n 
A 1 256 GLN 256 237 237 GLN GLN A . n 
A 1 257 LEU 257 238 238 LEU LEU A . n 
A 1 258 GLU 258 239 239 GLU GLU A . n 
A 1 259 ALA 259 240 240 ALA ALA A . n 
A 1 260 PRO 260 241 241 PRO PRO A . n 
A 1 261 TYR 261 242 242 TYR TYR A . n 
A 1 262 ASN 262 243 243 ASN ASN A . n 
A 1 263 SER 263 244 244 SER SER A . n 
A 1 264 ASP 264 245 245 ASP ASP A . n 
A 1 265 THR 265 246 246 THR THR A . n 
A 1 266 VAL 266 247 247 VAL VAL A . n 
A 1 267 LEU 267 248 248 LEU LEU A . n 
A 1 268 VAL 268 249 249 VAL VAL A . n 
A 1 269 HIS 269 250 250 HIS HIS A . n 
A 1 270 ARG 270 251 251 ARG ARG A . n 
A 1 271 VAL 271 252 252 VAL VAL A . n 
A 1 272 HIS 272 253 253 HIS HIS A . n 
A 1 273 SER 273 254 254 SER SER A . n 
A 1 274 TYR 274 255 255 TYR TYR A . n 
A 1 275 LEU 275 256 256 LEU LEU A . n 
A 1 276 GLU 276 257 257 GLU GLU A . n 
A 1 277 ARG 277 258 258 ARG ARG A . n 
A 1 278 HIS 278 259 259 HIS HIS A . n 
A 1 279 GLY 279 260 260 GLY GLY A . n 
A 1 280 LEU 280 261 261 LEU LEU A . n 
A 1 281 ILE 281 262 262 ILE ILE A . n 
A 1 282 ASN 282 263 263 ASN ASN A . n 
A 1 283 PHE 283 264 264 PHE PHE A . n 
A 1 284 GLY 284 265 265 GLY GLY A . n 
A 1 285 ILE 285 266 266 ILE ILE A . n 
A 1 286 TYR 286 267 267 TYR TYR A . n 
A 1 287 LYS 287 268 268 LYS LYS A . n 
A 1 288 ARG 288 269 269 ARG ARG A . n 
A 1 289 ILE 289 270 270 ILE ILE A . n 
A 1 290 LYS 290 271 271 LYS LYS A . n 
A 1 291 PRO 291 272 272 PRO PRO A . n 
A 1 292 LEU 292 273 273 LEU LEU A . n 
A 1 293 PRO 293 274 274 PRO PRO A . n 
A 1 294 THR 294 275 275 THR THR A . n 
A 1 295 LYS 295 276 276 LYS LYS A . n 
A 1 296 LYS 296 277 277 LYS LYS A . n 
A 1 297 THR 297 278 278 THR THR A . n 
A 1 298 GLY 298 279 279 GLY GLY A . n 
A 1 299 LYS 299 280 280 LYS LYS A . n 
A 1 300 VAL 300 281 281 VAL VAL A . n 
A 1 301 ILE 301 282 282 ILE ILE A . n 
A 1 302 ILE 302 283 283 ILE ILE A . n 
A 1 303 ILE 303 284 284 ILE ILE A . n 
A 1 304 GLY 304 285 285 GLY GLY A . n 
A 1 305 SER 305 286 286 SER SER A . n 
A 1 306 GLY 306 287 287 GLY GLY A . n 
A 1 307 VAL 307 288 288 VAL VAL A . n 
A 1 308 SER 308 289 289 SER SER A . n 
A 1 309 GLY 309 290 290 GLY GLY A . n 
A 1 310 LEU 310 291 291 LEU LEU A . n 
A 1 311 ALA 311 292 292 ALA ALA A . n 
A 1 312 ALA 312 293 293 ALA ALA A . n 
A 1 313 ALA 313 294 294 ALA ALA A . n 
A 1 314 ARG 314 295 295 ARG ARG A . n 
A 1 315 GLN 315 296 296 GLN GLN A . n 
A 1 316 LEU 316 297 297 LEU LEU A . n 
A 1 317 GLN 317 298 298 GLN GLN A . n 
A 1 318 SER 318 299 299 SER SER A . n 
A 1 319 PHE 319 300 300 PHE PHE A . n 
A 1 320 GLY 320 301 301 GLY GLY A . n 
A 1 321 MET 321 302 302 MET MET A . n 
A 1 322 ASP 322 303 303 ASP ASP A . n 
A 1 323 VAL 323 304 304 VAL VAL A . n 
A 1 324 THR 324 305 305 THR THR A . n 
A 1 325 LEU 325 306 306 LEU LEU A . n 
A 1 326 LEU 326 307 307 LEU LEU A . n 
A 1 327 GLU 327 308 308 GLU GLU A . n 
A 1 328 ALA 328 309 309 ALA ALA A . n 
A 1 329 ARG 329 310 310 ARG ARG A . n 
A 1 330 ASP 330 311 311 ASP ASP A . n 
A 1 331 ARG 331 312 312 ARG ARG A . n 
A 1 332 VAL 332 313 313 VAL VAL A . n 
A 1 333 GLY 333 314 314 GLY GLY A . n 
A 1 334 GLY 334 315 315 GLY GLY A . n 
A 1 335 ARG 335 316 316 ARG ARG A . n 
A 1 336 VAL 336 317 317 VAL VAL A . n 
A 1 337 ALA 337 318 318 ALA ALA A . n 
A 1 338 THR 338 319 319 THR THR A . n 
A 1 339 PHE 339 320 320 PHE PHE A . n 
A 1 340 ARG 340 321 321 ARG ARG A . n 
A 1 341 LYS 341 322 322 LYS LYS A . n 
A 1 342 GLY 342 323 323 GLY GLY A . n 
A 1 343 ASN 343 324 324 ASN ASN A . n 
A 1 344 TYR 344 325 325 TYR TYR A . n 
A 1 345 VAL 345 326 326 VAL VAL A . n 
A 1 346 ALA 346 327 327 ALA ALA A . n 
A 1 347 ASP 347 328 328 ASP ASP A . n 
A 1 348 LEU 348 329 329 LEU LEU A . n 
A 1 349 GLY 349 330 330 GLY GLY A . n 
A 1 350 ALA 350 331 331 ALA ALA A . n 
A 1 351 MET 351 332 332 MET MET A . n 
A 1 352 VAL 352 333 333 VAL VAL A . n 
A 1 353 VAL 353 334 334 VAL VAL A . n 
A 1 354 THR 354 335 335 THR THR A . n 
A 1 355 GLY 355 336 336 GLY GLY A . n 
A 1 356 LEU 356 337 337 LEU LEU A . n 
A 1 357 GLY 357 338 338 GLY GLY A . n 
A 1 358 GLY 358 339 339 GLY GLY A . n 
A 1 359 ASN 359 340 340 ASN ASN A . n 
A 1 360 PRO 360 341 341 PRO PRO A . n 
A 1 361 MET 361 342 342 MET MET A . n 
A 1 362 ALA 362 343 343 ALA ALA A . n 
A 1 363 VAL 363 344 344 VAL VAL A . n 
A 1 364 VAL 364 345 345 VAL VAL A . n 
A 1 365 SER 365 346 346 SER SER A . n 
A 1 366 LYS 366 347 347 LYS LYS A . n 
A 1 367 GLN 367 348 348 GLN GLN A . n 
A 1 368 VAL 368 349 349 VAL VAL A . n 
A 1 369 ASN 369 350 350 ASN ASN A . n 
A 1 370 MET 370 351 351 MET MET A . n 
A 1 371 GLU 371 352 352 GLU GLU A . n 
A 1 372 LEU 372 353 353 LEU LEU A . n 
A 1 373 ALA 373 354 354 ALA ALA A . n 
A 1 374 LYS 374 355 355 LYS LYS A . n 
A 1 375 ILE 375 356 356 ILE ILE A . n 
A 1 376 LYS 376 357 357 LYS LYS A . n 
A 1 377 GLN 377 358 358 GLN GLN A . n 
A 1 378 LYS 378 359 359 LYS LYS A . n 
A 1 379 CYS 379 360 360 CYS CYS A . n 
A 1 380 PRO 380 361 361 PRO PRO A . n 
A 1 381 LEU 381 362 362 LEU LEU A . n 
A 1 382 TYR 382 363 363 TYR TYR A . n 
A 1 383 GLU 383 364 364 GLU GLU A . n 
A 1 384 ALA 384 365 365 ALA ALA A . n 
A 1 385 ASN 385 366 366 ASN ASN A . n 
A 1 386 GLY 386 367 367 GLY GLY A . n 
A 1 387 GLN 387 368 368 GLN GLN A . n 
A 1 388 ALA 388 369 369 ALA ALA A . n 
A 1 389 VAL 389 370 370 VAL VAL A . n 
A 1 390 PRO 390 371 371 PRO PRO A . n 
A 1 391 LYS 391 372 372 LYS LYS A . n 
A 1 392 GLU 392 373 373 GLU GLU A . n 
A 1 393 LYS 393 374 374 LYS LYS A . n 
A 1 394 ASP 394 375 375 ASP ASP A . n 
A 1 395 GLU 395 376 376 GLU GLU A . n 
A 1 396 MET 396 377 377 MET MET A . n 
A 1 397 VAL 397 378 378 VAL VAL A . n 
A 1 398 GLU 398 379 379 GLU GLU A . n 
A 1 399 GLN 399 380 380 GLN GLN A . n 
A 1 400 GLU 400 381 381 GLU GLU A . n 
A 1 401 PHE 401 382 382 PHE PHE A . n 
A 1 402 ASN 402 383 383 ASN ASN A . n 
A 1 403 ARG 403 384 384 ARG ARG A . n 
A 1 404 LEU 404 385 385 LEU LEU A . n 
A 1 405 LEU 405 386 386 LEU LEU A . n 
A 1 406 GLU 406 387 387 GLU GLU A . n 
A 1 407 ALA 407 388 388 ALA ALA A . n 
A 1 408 THR 408 389 389 THR THR A . n 
A 1 409 SER 409 390 390 SER SER A . n 
A 1 410 TYR 410 391 391 TYR TYR A . n 
A 1 411 LEU 411 392 392 LEU LEU A . n 
A 1 412 SER 412 393 393 SER SER A . n 
A 1 413 HIS 413 394 394 HIS HIS A . n 
A 1 414 GLN 414 395 395 GLN GLN A . n 
A 1 415 LEU 415 396 396 LEU LEU A . n 
A 1 416 ASP 416 397 397 ASP ASP A . n 
A 1 417 PHE 417 398 398 PHE PHE A . n 
A 1 418 ASN 418 399 399 ASN ASN A . n 
A 1 419 VAL 419 400 400 VAL VAL A . n 
A 1 420 LEU 420 401 401 LEU LEU A . n 
A 1 421 ASN 421 402 402 ASN ASN A . n 
A 1 422 ASN 422 403 403 ASN ASN A . n 
A 1 423 LYS 423 404 404 LYS LYS A . n 
A 1 424 PRO 424 405 405 PRO PRO A . n 
A 1 425 VAL 425 406 406 VAL VAL A . n 
A 1 426 SER 426 407 407 SER SER A . n 
A 1 427 LEU 427 408 408 LEU LEU A . n 
A 1 428 GLY 428 409 409 GLY GLY A . n 
A 1 429 GLN 429 410 410 GLN GLN A . n 
A 1 430 ALA 430 411 411 ALA ALA A . n 
A 1 431 LEU 431 412 412 LEU LEU A . n 
A 1 432 GLU 432 413 413 GLU GLU A . n 
A 1 433 VAL 433 414 414 VAL VAL A . n 
A 1 434 VAL 434 415 415 VAL VAL A . n 
A 1 435 ILE 435 416 416 ILE ILE A . n 
A 1 436 GLN 436 417 417 GLN GLN A . n 
A 1 437 LEU 437 418 418 LEU LEU A . n 
A 1 438 GLN 438 419 419 GLN GLN A . n 
A 1 439 GLU 439 420 420 GLU GLU A . n 
A 1 440 LYS 440 421 421 LYS LYS A . n 
A 1 441 HIS 441 422 422 HIS HIS A . n 
A 1 442 VAL 442 423 423 VAL VAL A . n 
A 1 443 LYS 443 424 424 LYS LYS A . n 
A 1 444 ASP 444 425 425 ASP ASP A . n 
A 1 445 GLU 445 426 426 GLU GLU A . n 
A 1 446 GLN 446 427 427 GLN GLN A . n 
A 1 447 ILE 447 428 428 ILE ILE A . n 
A 1 448 GLU 448 429 429 GLU GLU A . n 
A 1 449 HIS 449 430 430 HIS HIS A . n 
A 1 450 TRP 450 431 431 TRP TRP A . n 
A 1 451 LYS 451 432 432 LYS LYS A . n 
A 1 452 LYS 452 433 433 LYS LYS A . n 
A 1 453 ILE 453 434 434 ILE ILE A . n 
A 1 454 VAL 454 435 435 VAL VAL A . n 
A 1 455 LYS 455 436 436 LYS LYS A . n 
A 1 456 THR 456 437 437 THR THR A . n 
A 1 457 GLN 457 438 438 GLN GLN A . n 
A 1 458 GLU 458 439 439 GLU GLU A . n 
A 1 459 GLU 459 440 440 GLU GLU A . n 
A 1 460 LEU 460 441 441 LEU LEU A . n 
A 1 461 LYS 461 442 442 LYS LYS A . n 
A 1 462 GLU 462 443 443 GLU GLU A . n 
A 1 463 LEU 463 444 444 LEU LEU A . n 
A 1 464 LEU 464 445 445 LEU LEU A . n 
A 1 465 ASN 465 446 446 ASN ASN A . n 
A 1 466 LYS 466 447 447 LYS LYS A . n 
A 1 467 MET 467 448 448 MET MET A . n 
A 1 468 VAL 468 449 449 VAL VAL A . n 
A 1 469 ASN 469 450 450 ASN ASN A . n 
A 1 470 LEU 470 451 451 LEU LEU A . n 
A 1 471 LYS 471 452 452 LYS LYS A . n 
A 1 472 GLU 472 453 453 GLU GLU A . n 
A 1 473 LYS 473 454 454 LYS LYS A . n 
A 1 474 ILE 474 455 455 ILE ILE A . n 
A 1 475 LYS 475 456 456 LYS LYS A . n 
A 1 476 GLU 476 457 457 GLU GLU A . n 
A 1 477 LEU 477 458 458 LEU LEU A . n 
A 1 478 HIS 478 459 459 HIS HIS A . n 
A 1 479 GLN 479 460 460 GLN GLN A . n 
A 1 480 GLN 480 461 461 GLN GLN A . n 
A 1 481 TYR 481 462 462 TYR TYR A . n 
A 1 482 LYS 482 463 463 LYS LYS A . n 
A 1 483 GLU 483 464 464 GLU GLU A . n 
A 1 484 ALA 484 465 465 ALA ALA A . n 
A 1 485 SER 485 466 466 SER SER A . n 
A 1 486 GLU 486 467 467 GLU GLU A . n 
A 1 487 VAL 487 468 468 VAL VAL A . n 
A 1 488 LYS 488 469 469 LYS LYS A . n 
A 1 489 PRO 489 470 470 PRO PRO A . n 
A 1 490 PRO 490 471 471 PRO PRO A . n 
A 1 491 ARG 491 472 472 ARG ARG A . n 
A 1 492 ASP 492 473 473 ASP ASP A . n 
A 1 493 ILE 493 474 474 ILE ILE A . n 
A 1 494 THR 494 475 475 THR THR A . n 
A 1 495 ALA 495 476 476 ALA ALA A . n 
A 1 496 GLU 496 477 477 GLU GLU A . n 
A 1 497 PHE 497 478 478 PHE PHE A . n 
A 1 498 LEU 498 479 479 LEU LEU A . n 
A 1 499 VAL 499 480 480 VAL VAL A . n 
A 1 500 LYS 500 481 481 LYS LYS A . n 
A 1 501 SER 501 482 482 SER SER A . n 
A 1 502 LYS 502 483 483 LYS LYS A . n 
A 1 503 HIS 503 484 484 HIS HIS A . n 
A 1 504 ARG 504 485 485 ARG ARG A . n 
A 1 505 ASP 505 486 486 ASP ASP A . n 
A 1 506 LEU 506 487 487 LEU LEU A . n 
A 1 507 THR 507 488 488 THR THR A . n 
A 1 508 ALA 508 489 489 ALA ALA A . n 
A 1 509 LEU 509 490 490 LEU LEU A . n 
A 1 510 CYS 510 491 491 CYS CYS A . n 
A 1 511 LYS 511 492 492 LYS LYS A . n 
A 1 512 GLU 512 493 493 GLU GLU A . n 
A 1 513 TYR 513 494 494 TYR TYR A . n 
A 1 514 ASP 514 495 495 ASP ASP A . n 
A 1 515 GLU 515 496 496 GLU GLU A . n 
A 1 516 LEU 516 497 497 LEU LEU A . n 
A 1 517 ALA 517 498 498 ALA ALA A . n 
A 1 518 GLU 518 499 499 GLU GLU A . n 
A 1 519 THR 519 500 500 THR THR A . n 
A 1 520 GLN 520 501 501 GLN GLN A . n 
A 1 521 GLY 521 502 502 GLY GLY A . n 
A 1 522 LYS 522 503 503 LYS LYS A . n 
A 1 523 LEU 523 504 504 LEU LEU A . n 
A 1 524 GLU 524 505 505 GLU GLU A . n 
A 1 525 GLU 525 506 506 GLU GLU A . n 
A 1 526 LYS 526 507 507 LYS LYS A . n 
A 1 527 LEU 527 508 508 LEU LEU A . n 
A 1 528 GLN 528 509 509 GLN GLN A . n 
A 1 529 GLU 529 510 510 GLU GLU A . n 
A 1 530 LEU 530 511 511 LEU LEU A . n 
A 1 531 GLU 531 512 512 GLU GLU A . n 
A 1 532 ALA 532 513 513 ALA ALA A . n 
A 1 533 ASN 533 514 514 ASN ASN A . n 
A 1 534 PRO 534 515 515 PRO PRO A . n 
A 1 535 PRO 535 516 516 PRO PRO A . n 
A 1 536 SER 536 517 517 SER SER A . n 
A 1 537 ASP 537 518 518 ASP ASP A . n 
A 1 538 VAL 538 519 519 VAL VAL A . n 
A 1 539 TYR 539 520 520 TYR TYR A . n 
A 1 540 LEU 540 521 521 LEU LEU A . n 
A 1 541 SER 541 522 522 SER SER A . n 
A 1 542 SER 542 523 523 SER SER A . n 
A 1 543 ARG 543 524 524 ARG ARG A . n 
A 1 544 ASP 544 525 525 ASP ASP A . n 
A 1 545 ARG 545 526 526 ARG ARG A . n 
A 1 546 GLN 546 527 527 GLN GLN A . n 
A 1 547 ILE 547 528 528 ILE ILE A . n 
A 1 548 LEU 548 529 529 LEU LEU A . n 
A 1 549 ASP 549 530 530 ASP ASP A . n 
A 1 550 TRP 550 531 531 TRP TRP A . n 
A 1 551 HIS 551 532 532 HIS HIS A . n 
A 1 552 PHE 552 533 533 PHE PHE A . n 
A 1 553 ALA 553 534 534 ALA ALA A . n 
A 1 554 ASN 554 535 535 ASN ASN A . n 
A 1 555 LEU 555 536 536 LEU LEU A . n 
A 1 556 GLU 556 537 537 GLU GLU A . n 
A 1 557 PHE 557 538 538 PHE PHE A . n 
A 1 558 ALA 558 539 539 ALA ALA A . n 
A 1 559 ASN 559 540 540 ASN ASN A . n 
A 1 560 ALA 560 541 541 ALA ALA A . n 
A 1 561 THR 561 542 542 THR THR A . n 
A 1 562 PRO 562 543 543 PRO PRO A . n 
A 1 563 LEU 563 544 544 LEU LEU A . n 
A 1 564 SER 564 545 545 SER SER A . n 
A 1 565 THR 565 546 546 THR THR A . n 
A 1 566 LEU 566 547 547 LEU LEU A . n 
A 1 567 SER 567 548 548 SER SER A . n 
A 1 568 LEU 568 549 549 LEU LEU A . n 
A 1 569 LYS 569 550 550 LYS LYS A . n 
A 1 570 HIS 570 551 551 HIS HIS A . n 
A 1 571 TRP 571 552 552 TRP TRP A . n 
A 1 572 ASP 572 553 553 ASP ASP A . n 
A 1 573 GLN 573 554 554 GLN GLN A . n 
A 1 574 ASP 574 555 555 ASP ASP A . n 
A 1 575 ASP 575 556 556 ASP ASP A . n 
A 1 576 ASP 576 557 557 ASP ASP A . n 
A 1 577 PHE 577 558 558 PHE PHE A . n 
A 1 578 GLU 578 559 559 GLU GLU A . n 
A 1 579 PHE 579 560 560 PHE PHE A . n 
A 1 580 THR 580 561 561 THR THR A . n 
A 1 581 GLY 581 562 562 GLY GLY A . n 
A 1 582 SER 582 563 563 SER SER A . n 
A 1 583 HIS 583 564 564 HIS HIS A . n 
A 1 584 LEU 584 565 565 LEU LEU A . n 
A 1 585 THR 585 566 566 THR THR A . n 
A 1 586 VAL 586 567 567 VAL VAL A . n 
A 1 587 ARG 587 568 568 ARG ARG A . n 
A 1 588 ASN 588 569 569 ASN ASN A . n 
A 1 589 GLY 589 570 570 GLY GLY A . n 
A 1 590 TYR 590 571 571 TYR TYR A . n 
A 1 591 SER 591 572 572 SER SER A . n 
A 1 592 CYS 592 573 573 CYS CYS A . n 
A 1 593 VAL 593 574 574 VAL VAL A . n 
A 1 594 PRO 594 575 575 PRO PRO A . n 
A 1 595 VAL 595 576 576 VAL VAL A . n 
A 1 596 ALA 596 577 577 ALA ALA A . n 
A 1 597 LEU 597 578 578 LEU LEU A . n 
A 1 598 ALA 598 579 579 ALA ALA A . n 
A 1 599 GLU 599 580 580 GLU GLU A . n 
A 1 600 GLY 600 581 581 GLY GLY A . n 
A 1 601 LEU 601 582 582 LEU LEU A . n 
A 1 602 ASP 602 583 583 ASP ASP A . n 
A 1 603 ILE 603 584 584 ILE ILE A . n 
A 1 604 LYS 604 585 585 LYS LYS A . n 
A 1 605 LEU 605 586 586 LEU LEU A . n 
A 1 606 ASN 606 587 587 ASN ASN A . n 
A 1 607 THR 607 588 588 THR THR A . n 
A 1 608 ALA 608 589 589 ALA ALA A . n 
A 1 609 VAL 609 590 590 VAL VAL A . n 
A 1 610 ARG 610 591 591 ARG ARG A . n 
A 1 611 GLN 611 592 592 GLN GLN A . n 
A 1 612 VAL 612 593 593 VAL VAL A . n 
A 1 613 ARG 613 594 594 ARG ARG A . n 
A 1 614 TYR 614 595 595 TYR TYR A . n 
A 1 615 THR 615 596 596 THR THR A . n 
A 1 616 ALA 616 597 597 ALA ALA A . n 
A 1 617 SER 617 598 598 SER SER A . n 
A 1 618 GLY 618 599 599 GLY GLY A . n 
A 1 619 CYS 619 600 600 CYS CYS A . n 
A 1 620 GLU 620 601 601 GLU GLU A . n 
A 1 621 VAL 621 602 602 VAL VAL A . n 
A 1 622 ILE 622 603 603 ILE ILE A . n 
A 1 623 ALA 623 604 604 ALA ALA A . n 
A 1 624 VAL 624 605 605 VAL VAL A . n 
A 1 625 ASN 625 606 606 ASN ASN A . n 
A 1 626 THR 626 607 607 THR THR A . n 
A 1 627 ARG 627 608 608 ARG ARG A . n 
A 1 628 SER 628 609 609 SER SER A . n 
A 1 629 THR 629 610 610 THR THR A . n 
A 1 630 SER 630 611 611 SER SER A . n 
A 1 631 GLN 631 612 612 GLN GLN A . n 
A 1 632 THR 632 613 613 THR THR A . n 
A 1 633 PHE 633 614 614 PHE PHE A . n 
A 1 634 ILE 634 615 615 ILE ILE A . n 
A 1 635 TYR 635 616 616 TYR TYR A . n 
A 1 636 LYS 636 617 617 LYS LYS A . n 
A 1 637 CYS 637 618 618 CYS CYS A . n 
A 1 638 ASP 638 619 619 ASP ASP A . n 
A 1 639 ALA 639 620 620 ALA ALA A . n 
A 1 640 VAL 640 621 621 VAL VAL A . n 
A 1 641 LEU 641 622 622 LEU LEU A . n 
A 1 642 CYS 642 623 623 CYS CYS A . n 
A 1 643 THR 643 624 624 THR THR A . n 
A 1 644 LEU 644 625 625 LEU LEU A . n 
A 1 645 PRO 645 626 626 PRO PRO A . n 
A 1 646 LEU 646 627 627 LEU LEU A . n 
A 1 647 GLY 647 628 628 GLY GLY A . n 
A 1 648 VAL 648 629 629 VAL VAL A . n 
A 1 649 LEU 649 630 630 LEU LEU A . n 
A 1 650 LYS 650 631 631 LYS LYS A . n 
A 1 651 GLN 651 632 632 GLN GLN A . n 
A 1 652 GLN 652 633 633 GLN GLN A . n 
A 1 653 PRO 653 634 634 PRO PRO A . n 
A 1 654 PRO 654 635 635 PRO PRO A . n 
A 1 655 ALA 655 636 636 ALA ALA A . n 
A 1 656 VAL 656 637 637 VAL VAL A . n 
A 1 657 GLN 657 638 638 GLN GLN A . n 
A 1 658 PHE 658 639 639 PHE PHE A . n 
A 1 659 VAL 659 640 640 VAL VAL A . n 
A 1 660 PRO 660 641 641 PRO PRO A . n 
A 1 661 PRO 661 642 642 PRO PRO A . n 
A 1 662 LEU 662 643 643 LEU LEU A . n 
A 1 663 PRO 663 644 644 PRO PRO A . n 
A 1 664 GLU 664 645 645 GLU GLU A . n 
A 1 665 TRP 665 646 646 TRP TRP A . n 
A 1 666 LYS 666 647 647 LYS LYS A . n 
A 1 667 THR 667 648 648 THR THR A . n 
A 1 668 SER 668 649 649 SER SER A . n 
A 1 669 ALA 669 650 650 ALA ALA A . n 
A 1 670 VAL 670 651 651 VAL VAL A . n 
A 1 671 GLN 671 652 652 GLN GLN A . n 
A 1 672 ARG 672 653 653 ARG ARG A . n 
A 1 673 MET 673 654 654 MET MET A . n 
A 1 674 GLY 674 655 655 GLY GLY A . n 
A 1 675 PHE 675 656 656 PHE PHE A . n 
A 1 676 GLY 676 657 657 GLY GLY A . n 
A 1 677 ASN 677 658 658 ASN ASN A . n 
A 1 678 LEU 678 659 659 LEU LEU A . n 
A 1 679 ASN 679 660 660 ASN ASN A . n 
A 1 680 LYS 680 661 661 LYS LYS A . n 
A 1 681 VAL 681 662 662 VAL VAL A . n 
A 1 682 VAL 682 663 663 VAL VAL A . n 
A 1 683 LEU 683 664 664 LEU LEU A . n 
A 1 684 CYS 684 665 665 CYS CYS A . n 
A 1 685 PHE 685 666 666 PHE PHE A . n 
A 1 686 ASP 686 667 667 ASP ASP A . n 
A 1 687 ARG 687 668 668 ARG ARG A . n 
A 1 688 VAL 688 669 669 VAL VAL A . n 
A 1 689 PHE 689 670 670 PHE PHE A . n 
A 1 690 TRP 690 671 671 TRP TRP A . n 
A 1 691 ASP 691 672 672 ASP ASP A . n 
A 1 692 PRO 692 673 673 PRO PRO A . n 
A 1 693 SER 693 674 674 SER SER A . n 
A 1 694 VAL 694 675 675 VAL VAL A . n 
A 1 695 ASN 695 676 676 ASN ASN A . n 
A 1 696 LEU 696 677 677 LEU LEU A . n 
A 1 697 PHE 697 678 678 PHE PHE A . n 
A 1 698 GLY 698 679 679 GLY GLY A . n 
A 1 699 HIS 699 680 680 HIS HIS A . n 
A 1 700 VAL 700 681 681 VAL VAL A . n 
A 1 701 GLY 701 682 682 GLY GLY A . n 
A 1 702 SER 702 683 683 SER SER A . n 
A 1 703 THR 703 684 684 THR THR A . n 
A 1 704 THR 704 685 685 THR THR A . n 
A 1 705 ALA 705 686 686 ALA ALA A . n 
A 1 706 SER 706 687 687 SER SER A . n 
A 1 707 ARG 707 688 688 ARG ARG A . n 
A 1 708 GLY 708 689 689 GLY GLY A . n 
A 1 709 GLU 709 690 690 GLU GLU A . n 
A 1 710 LEU 710 691 691 LEU LEU A . n 
A 1 711 PHE 711 692 692 PHE PHE A . n 
A 1 712 LEU 712 693 693 LEU LEU A . n 
A 1 713 PHE 713 694 694 PHE PHE A . n 
A 1 714 TRP 714 695 695 TRP TRP A . n 
A 1 715 ASN 715 696 696 ASN ASN A . n 
A 1 716 LEU 716 697 697 LEU LEU A . n 
A 1 717 TYR 717 698 698 TYR TYR A . n 
A 1 718 LYS 718 699 699 LYS LYS A . n 
A 1 719 ALA 719 700 700 ALA ALA A . n 
A 1 720 PRO 720 701 701 PRO PRO A . n 
A 1 721 ILE 721 702 702 ILE ILE A . n 
A 1 722 LEU 722 703 703 LEU LEU A . n 
A 1 723 LEU 723 704 704 LEU LEU A . n 
A 1 724 ALA 724 705 705 ALA ALA A . n 
A 1 725 LEU 725 706 706 LEU LEU A . n 
A 1 726 VAL 726 707 707 VAL VAL A . n 
A 1 727 ALA 727 708 708 ALA ALA A . n 
A 1 728 GLY 728 709 709 GLY GLY A . n 
A 1 729 GLU 729 710 710 GLU GLU A . n 
A 1 730 ALA 730 711 711 ALA ALA A . n 
A 1 731 ALA 731 712 712 ALA ALA A . n 
A 1 732 GLY 732 713 713 GLY GLY A . n 
A 1 733 ILE 733 714 714 ILE ILE A . n 
A 1 734 MET 734 715 715 MET MET A . n 
A 1 735 GLU 735 716 716 GLU GLU A . n 
A 1 736 ASN 736 717 717 ASN ASN A . n 
A 1 737 ILE 737 718 718 ILE ILE A . n 
A 1 738 SER 738 719 719 SER SER A . n 
A 1 739 ASP 739 720 720 ASP ASP A . n 
A 1 740 ASP 740 721 721 ASP ASP A . n 
A 1 741 VAL 741 722 722 VAL VAL A . n 
A 1 742 ILE 742 723 723 ILE ILE A . n 
A 1 743 VAL 743 724 724 VAL VAL A . n 
A 1 744 GLY 744 725 725 GLY GLY A . n 
A 1 745 ARG 745 726 726 ARG ARG A . n 
A 1 746 CYS 746 727 727 CYS CYS A . n 
A 1 747 LEU 747 728 728 LEU LEU A . n 
A 1 748 ALA 748 729 729 ALA ALA A . n 
A 1 749 ILE 749 730 730 ILE ILE A . n 
A 1 750 LEU 750 731 731 LEU LEU A . n 
A 1 751 LYS 751 732 732 LYS LYS A . n 
A 1 752 GLY 752 733 733 GLY GLY A . n 
A 1 753 ILE 753 734 734 ILE ILE A . n 
A 1 754 PHE 754 735 735 PHE PHE A . n 
A 1 755 GLY 755 736 736 GLY GLY A . n 
A 1 756 SER 756 737 737 SER SER A . n 
A 1 757 SER 757 738 738 SER SER A . n 
A 1 758 ALA 758 739 739 ALA ALA A . n 
A 1 759 VAL 759 740 740 VAL VAL A . n 
A 1 760 PRO 760 741 741 PRO PRO A . n 
A 1 761 GLN 761 742 742 GLN GLN A . n 
A 1 762 PRO 762 743 743 PRO PRO A . n 
A 1 763 LYS 763 744 744 LYS LYS A . n 
A 1 764 GLU 764 745 745 GLU GLU A . n 
A 1 765 THR 765 746 746 THR THR A . n 
A 1 766 VAL 766 747 747 VAL VAL A . n 
A 1 767 VAL 767 748 748 VAL VAL A . n 
A 1 768 SER 768 749 749 SER SER A . n 
A 1 769 ARG 769 750 750 ARG ARG A . n 
A 1 770 TRP 770 751 751 TRP TRP A . n 
A 1 771 ARG 771 752 752 ARG ARG A . n 
A 1 772 ALA 772 753 753 ALA ALA A . n 
A 1 773 ASP 773 754 754 ASP ASP A . n 
A 1 774 PRO 774 755 755 PRO PRO A . n 
A 1 775 TRP 775 756 756 TRP TRP A . n 
A 1 776 ALA 776 757 757 ALA ALA A . n 
A 1 777 ARG 777 758 758 ARG ARG A . n 
A 1 778 GLY 778 759 759 GLY GLY A . n 
A 1 779 SER 779 760 760 SER SER A . n 
A 1 780 TYR 780 761 761 TYR TYR A . n 
A 1 781 SER 781 762 762 SER SER A . n 
A 1 782 TYR 782 763 763 TYR TYR A . n 
A 1 783 VAL 783 764 764 VAL VAL A . n 
A 1 784 ALA 784 765 765 ALA ALA A . n 
A 1 785 ALA 785 766 766 ALA ALA A . n 
A 1 786 GLY 786 767 767 GLY GLY A . n 
A 1 787 SER 787 768 768 SER SER A . n 
A 1 788 SER 788 769 769 SER SER A . n 
A 1 789 GLY 789 770 770 GLY GLY A . n 
A 1 790 ASN 790 771 771 ASN ASN A . n 
A 1 791 ASP 791 772 772 ASP ASP A . n 
A 1 792 TYR 792 773 773 TYR TYR A . n 
A 1 793 ASP 793 774 774 ASP ASP A . n 
A 1 794 LEU 794 775 775 LEU LEU A . n 
A 1 795 MET 795 776 776 MET MET A . n 
A 1 796 ALA 796 777 777 ALA ALA A . n 
A 1 797 GLN 797 778 778 GLN GLN A . n 
A 1 798 PRO 798 779 779 PRO PRO A . n 
A 1 799 ILE 799 780 780 ILE ILE A . n 
A 1 800 THR 800 781 781 THR THR A . n 
A 1 801 PRO 801 782 782 PRO PRO A . n 
A 1 802 GLY 802 783 783 GLY GLY A . n 
A 1 803 PRO 803 784 784 PRO PRO A . n 
A 1 804 SER 804 785 785 SER SER A . n 
A 1 805 ILE 805 786 786 ILE ILE A . n 
A 1 806 PRO 806 787 787 PRO PRO A . n 
A 1 807 GLY 807 788 788 GLY GLY A . n 
A 1 808 ALA 808 789 789 ALA ALA A . n 
A 1 809 PRO 809 790 790 PRO PRO A . n 
A 1 810 GLN 810 791 791 GLN GLN A . n 
A 1 811 PRO 811 792 792 PRO PRO A . n 
A 1 812 ILE 812 793 793 ILE ILE A . n 
A 1 813 PRO 813 794 794 PRO PRO A . n 
A 1 814 ARG 814 795 795 ARG ARG A . n 
A 1 815 LEU 815 796 796 LEU LEU A . n 
A 1 816 PHE 816 797 797 PHE PHE A . n 
A 1 817 PHE 817 798 798 PHE PHE A . n 
A 1 818 ALA 818 799 799 ALA ALA A . n 
A 1 819 GLY 819 800 800 GLY GLY A . n 
A 1 820 GLU 820 801 801 GLU GLU A . n 
A 1 821 HIS 821 802 802 HIS HIS A . n 
A 1 822 THR 822 803 803 THR THR A . n 
A 1 823 ILE 823 804 804 ILE ILE A . n 
A 1 824 ARG 824 805 805 ARG ARG A . n 
A 1 825 ASN 825 806 806 ASN ASN A . n 
A 1 826 TYR 826 807 807 TYR TYR A . n 
A 1 827 PRO 827 808 808 PRO PRO A . n 
A 1 828 ALA 828 809 809 ALA ALA A . n 
A 1 829 THR 829 810 810 THR THR A . n 
A 1 830 VAL 830 811 811 VAL VAL A . n 
A 1 831 HIS 831 812 812 HIS HIS A . n 
A 1 832 GLY 832 813 813 GLY GLY A . n 
A 1 833 ALA 833 814 814 ALA ALA A . n 
A 1 834 LEU 834 815 815 LEU LEU A . n 
A 1 835 LEU 835 816 816 LEU LEU A . n 
A 1 836 SER 836 817 817 SER SER A . n 
A 1 837 GLY 837 818 818 GLY GLY A . n 
A 1 838 LEU 838 819 819 LEU LEU A . n 
A 1 839 ARG 839 820 820 ARG ARG A . n 
A 1 840 GLU 840 821 821 GLU GLU A . n 
A 1 841 ALA 841 822 822 ALA ALA A . n 
A 1 842 GLY 842 823 823 GLY GLY A . n 
A 1 843 ARG 843 824 824 ARG ARG A . n 
A 1 844 ILE 844 825 825 ILE ILE A . n 
A 1 845 ALA 845 826 826 ALA ALA A . n 
A 1 846 ASP 846 827 827 ASP ASP A . n 
A 1 847 GLN 847 828 828 GLN GLN A . n 
A 1 848 PHE 848 829 829 PHE PHE A . n 
A 1 849 LEU 849 830 830 LEU LEU A . n 
A 1 850 GLY 850 831 831 GLY GLY A . n 
A 1 851 ALA 851 832 832 ALA ALA A . n 
A 1 852 MET 852 833 833 MET MET A . n 
A 1 853 TYR 853 834 834 TYR TYR A . n 
A 1 854 THR 854 835 835 THR THR A . n 
A 1 855 LEU 855 836 836 LEU LEU A . n 
A 1 856 PRO 856 837 ?   ?   ?   A . n 
A 1 857 ARG 857 838 ?   ?   ?   A . n 
A 1 858 GLN 858 839 ?   ?   ?   A . n 
A 1 859 ALA 859 840 ?   ?   ?   A . n 
A 1 860 THR 860 841 ?   ?   ?   A . n 
A 1 861 PRO 861 842 ?   ?   ?   A . n 
A 1 862 GLY 862 843 ?   ?   ?   A . n 
A 1 863 VAL 863 844 ?   ?   ?   A . n 
A 1 864 PRO 864 845 ?   ?   ?   A . n 
A 1 865 ALA 865 846 ?   ?   ?   A . n 
A 1 866 GLN 866 847 ?   ?   ?   A . n 
A 1 867 GLN 867 848 ?   ?   ?   A . n 
A 1 868 SER 868 849 ?   ?   ?   A . n 
A 1 869 PRO 869 850 ?   ?   ?   A . n 
A 1 870 SER 870 851 ?   ?   ?   A . n 
A 1 871 MET 871 852 ?   ?   ?   A . n 
B 2 1   GLY 1   297 ?   ?   ?   B . n 
B 2 2   PRO 2   298 ?   ?   ?   B . n 
B 2 3   LEU 3   299 ?   ?   ?   B . n 
B 2 4   GLY 4   300 ?   ?   ?   B . n 
B 2 5   SER 5   301 ?   ?   ?   B . n 
B 2 6   PRO 6   302 ?   ?   ?   B . n 
B 2 7   GLU 7   303 ?   ?   ?   B . n 
B 2 8   PHE 8   304 ?   ?   ?   B . n 
B 2 9   ARG 9   305 ?   ?   ?   B . n 
B 2 10  ALA 10  306 ?   ?   ?   B . n 
B 2 11  LYS 11  307 ?   ?   ?   B . n 
B 2 12  ARG 12  308 308 ARG ARG B . n 
B 2 13  LYS 13  309 309 LYS LYS B . n 
B 2 14  PRO 14  310 310 PRO PRO B . n 
B 2 15  PRO 15  311 311 PRO PRO B . n 
B 2 16  LYS 16  312 312 LYS LYS B . n 
B 2 17  GLY 17  313 313 GLY GLY B . n 
B 2 18  MET 18  314 314 MET MET B . n 
B 2 19  PHE 19  315 315 PHE PHE B . n 
B 2 20  LEU 20  316 316 LEU LEU B . n 
B 2 21  SER 21  317 317 SER SER B . n 
B 2 22  GLN 22  318 318 GLN GLN B . n 
B 2 23  GLU 23  319 319 GLU GLU B . n 
B 2 24  ASP 24  320 320 ASP ASP B . n 
B 2 25  VAL 25  321 321 VAL VAL B . n 
B 2 26  GLU 26  322 322 GLU GLU B . n 
B 2 27  ALA 27  323 323 ALA ALA B . n 
B 2 28  VAL 28  324 324 VAL VAL B . n 
B 2 29  SER 29  325 325 SER SER B . n 
B 2 30  ALA 30  326 326 ALA ALA B . n 
B 2 31  ASN 31  327 327 ASN ASN B . n 
B 2 32  ALA 32  328 328 ALA ALA B . n 
B 2 33  THR 33  329 329 THR THR B . n 
B 2 34  ALA 34  330 330 ALA ALA B . n 
B 2 35  ALA 35  331 331 ALA ALA B . n 
B 2 36  THR 36  332 332 THR THR B . n 
B 2 37  THR 37  333 333 THR THR B . n 
B 2 38  VAL 38  334 334 VAL VAL B . n 
B 2 39  LEU 39  335 335 LEU LEU B . n 
B 2 40  ARG 40  336 336 ARG ARG B . n 
B 2 41  GLN 41  337 337 GLN GLN B . n 
B 2 42  LEU 42  338 338 LEU LEU B . n 
B 2 43  ASP 43  339 339 ASP ASP B . n 
B 2 44  MET 44  340 340 MET MET B . n 
B 2 45  GLU 45  341 341 GLU GLU B . n 
B 2 46  LEU 46  342 342 LEU LEU B . n 
B 2 47  VAL 47  343 343 VAL VAL B . n 
B 2 48  SER 48  344 344 SER SER B . n 
B 2 49  VAL 49  345 345 VAL VAL B . n 
B 2 50  LYS 50  346 346 LYS LYS B . n 
B 2 51  ARG 51  347 347 ARG ARG B . n 
B 2 52  GLN 52  348 348 GLN GLN B . n 
B 2 53  ILE 53  349 349 ILE ILE B . n 
B 2 54  GLN 54  350 350 GLN GLN B . n 
B 2 55  ASN 55  351 351 ASN ASN B . n 
B 2 56  ILE 56  352 352 ILE ILE B . n 
B 2 57  LYS 57  353 353 LYS LYS B . n 
B 2 58  GLN 58  354 354 GLN GLN B . n 
B 2 59  THR 59  355 355 THR THR B . n 
B 2 60  ASN 60  356 356 ASN ASN B . n 
B 2 61  SER 61  357 357 SER SER B . n 
B 2 62  ALA 62  358 358 ALA ALA B . n 
B 2 63  LEU 63  359 359 LEU LEU B . n 
B 2 64  LYS 64  360 360 LYS LYS B . n 
B 2 65  GLU 65  361 361 GLU GLU B . n 
B 2 66  LYS 66  362 362 LYS LYS B . n 
B 2 67  LEU 67  363 363 LEU LEU B . n 
B 2 68  ASP 68  364 364 ASP ASP B . n 
B 2 69  GLY 69  365 365 GLY GLY B . n 
B 2 70  GLY 70  366 366 GLY GLY B . n 
B 2 71  ILE 71  367 367 ILE ILE B . n 
B 2 72  GLU 72  368 368 GLU GLU B . n 
B 2 73  PRO 73  369 369 PRO PRO B . n 
B 2 74  TYR 74  370 370 TYR TYR B . n 
B 2 75  ARG 75  371 371 ARG ARG B . n 
B 2 76  LEU 76  372 372 LEU LEU B . n 
B 2 77  PRO 77  373 373 PRO PRO B . n 
B 2 78  GLU 78  374 374 GLU GLU B . n 
B 2 79  VAL 79  375 375 VAL VAL B . n 
B 2 80  ILE 80  376 376 ILE ILE B . n 
B 2 81  GLN 81  377 377 GLN GLN B . n 
B 2 82  LYS 82  378 378 LYS LYS B . n 
B 2 83  CYS 83  379 379 CYS CYS B . n 
B 2 84  ASN 84  380 380 ASN ASN B . n 
B 2 85  ALA 85  381 381 ALA ALA B . n 
B 2 86  ARG 86  382 382 ARG ARG B . n 
B 2 87  TRP 87  383 383 TRP TRP B . n 
B 2 88  THR 88  384 384 THR THR B . n 
B 2 89  THR 89  385 385 THR THR B . n 
B 2 90  GLU 90  386 386 GLU GLU B . n 
B 2 91  GLU 91  387 387 GLU GLU B . n 
B 2 92  GLN 92  388 388 GLN GLN B . n 
B 2 93  LEU 93  389 389 LEU LEU B . n 
B 2 94  LEU 94  390 390 LEU LEU B . n 
B 2 95  ALA 95  391 391 ALA ALA B . n 
B 2 96  VAL 96  392 392 VAL VAL B . n 
B 2 97  GLN 97  393 393 GLN GLN B . n 
B 2 98  ALA 98  394 394 ALA ALA B . n 
B 2 99  ILE 99  395 395 ILE ILE B . n 
B 2 100 ARG 100 396 396 ARG ARG B . n 
B 2 101 LYS 101 397 397 LYS LYS B . n 
B 2 102 TYR 102 398 398 TYR TYR B . n 
B 2 103 GLY 103 399 399 GLY GLY B . n 
B 2 104 ARG 104 400 400 ARG ARG B . n 
B 2 105 ASP 105 401 401 ASP ASP B . n 
B 2 106 PHE 106 402 402 PHE PHE B . n 
B 2 107 GLN 107 403 403 GLN GLN B . n 
B 2 108 ALA 108 404 404 ALA ALA B . n 
B 2 109 ILE 109 405 405 ILE ILE B . n 
B 2 110 SER 110 406 406 SER SER B . n 
B 2 111 ASP 111 407 407 ASP ASP B . n 
B 2 112 VAL 112 408 408 VAL VAL B . n 
B 2 113 ILE 113 409 409 ILE ILE B . n 
B 2 114 GLY 114 410 410 GLY GLY B . n 
B 2 115 ASN 115 411 411 ASN ASN B . n 
B 2 116 LYS 116 412 412 LYS LYS B . n 
B 2 117 SER 117 413 413 SER SER B . n 
B 2 118 VAL 118 414 414 VAL VAL B . n 
B 2 119 VAL 119 415 415 VAL VAL B . n 
B 2 120 GLN 120 416 416 GLN GLN B . n 
B 2 121 VAL 121 417 417 VAL VAL B . n 
B 2 122 LYS 122 418 418 LYS LYS B . n 
B 2 123 ASN 123 419 419 ASN ASN B . n 
B 2 124 PHE 124 420 420 PHE PHE B . n 
B 2 125 PHE 125 421 421 PHE PHE B . n 
B 2 126 VAL 126 422 422 VAL VAL B . n 
B 2 127 ASN 127 423 423 ASN ASN B . n 
B 2 128 TYR 128 424 424 TYR TYR B . n 
B 2 129 ARG 129 425 425 ARG ARG B . n 
B 2 130 ARG 130 426 426 ARG ARG B . n 
B 2 131 ARG 131 427 427 ARG ARG B . n 
B 2 132 PHE 132 428 428 PHE PHE B . n 
B 2 133 ASN 133 429 429 ASN ASN B . n 
B 2 134 ILE 134 430 430 ILE ILE B . n 
B 2 135 ASP 135 431 431 ASP ASP B . n 
B 2 136 GLU 136 432 432 GLU GLU B . n 
B 2 137 VAL 137 433 433 VAL VAL B . n 
B 2 138 LEU 138 434 434 LEU LEU B . n 
B 2 139 GLN 139 435 435 GLN GLN B . n 
B 2 140 GLU 140 436 436 GLU GLU B . n 
B 2 141 TRP 141 437 437 TRP TRP B . n 
B 2 142 GLU 142 438 438 GLU GLU B . n 
B 2 143 ALA 143 439 439 ALA ALA B . n 
B 2 144 GLU 144 440 440 GLU GLU B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BI4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BI4 
_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        ? 
# 
_pdbx_nonpoly_scheme.asym_id         C 
_pdbx_nonpoly_scheme.entity_id       3 
_pdbx_nonpoly_scheme.mon_id          A1BI4 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     901 
_pdbx_nonpoly_scheme.auth_seq_num    901 
_pdbx_nonpoly_scheme.pdb_mon_id      A1BI4 
_pdbx_nonpoly_scheme.auth_mon_id     DRG 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
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  ? ? ? '(1.18.2_3874: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    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                     9EL7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     120.104 
_cell.length_a_esd                 ? 
_cell.length_b                     179.769 
_cell.length_b_esd                 ? 
_cell.length_c                     235.063 
_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                         9EL7 
_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                   9EL7 
_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             5.69 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          78.38 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.2 Na/K Tartrate, 100 mM ADA pH 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            300 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-09-21 
_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   0.96546 
_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                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.96546 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EL7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.87 
_reflns.d_resolution_low                               49.19 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     58387 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.04 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.127 
_reflns.pdbx_Rpim_I_all                                0.050 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       378415 
_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                              0.117 
_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                                    2.87 
_reflns_shell.d_res_low                                     2.97 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           39003 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5666 
_reflns_shell.percent_possible_obs                          100.0 
_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                               6.9 
_reflns_shell.pdbx_chi_squared                              0.72 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.3 
_reflns_shell.pdbx_Rrim_I_all                               1.736 
_reflns_shell.pdbx_Rpim_I_all                               0.659 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.606 
_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                                  1.605 
_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                                 9EL7 
_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                            2.87 
_refine.ls_d_res_low                             49.19 
_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                     58147 
_refine.ls_number_reflns_R_free                  1992 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.54 
_refine.ls_percent_reflns_R_free                 3.43 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2171 
_refine.ls_R_factor_R_free                       0.2424 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2162 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 27.57 
_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                            0.38 
_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                       2.87 
_refine_hist.d_res_low                        49.19 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               6365 
_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        6293 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         72 
_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' ? 0.010  ? 6501 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.329  ? 8823 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.374 ? 920  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.066  ? 988  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 1142 ? 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' 2.87 2.94  . . 141 3984 100.00 . . . . 0.3640 . . . . . . . . . . . 0.3808 
'X-RAY DIFFRACTION' 2.94 3.02  . . 142 3982 100.00 . . . . 0.3385 . . . . . . . . . . . 0.3785 
'X-RAY DIFFRACTION' 3.02 3.11  . . 140 3971 100.00 . . . . 0.3240 . . . . . . . . . . . 0.3755 
'X-RAY DIFFRACTION' 3.11 3.21  . . 142 3987 100.00 . . . . 0.3124 . . . . . . . . . . . 0.3111 
'X-RAY DIFFRACTION' 3.21 3.33  . . 142 4016 100.00 . . . . 0.2996 . . . . . . . . . . . 0.3295 
'X-RAY DIFFRACTION' 3.33 3.46  . . 141 3945 100.00 . . . . 0.2568 . . . . . . . . . . . 0.3071 
'X-RAY DIFFRACTION' 3.46 3.62  . . 141 3998 99.00  . . . . 0.2506 . . . . . . . . . . . 0.2489 
'X-RAY DIFFRACTION' 3.62 3.81  . . 141 3955 99.00  . . . . 0.2428 . . . . . . . . . . . 0.2610 
'X-RAY DIFFRACTION' 3.81 4.04  . . 141 3974 100.00 . . . . 0.2170 . . . . . . . . . . . 0.2535 
'X-RAY DIFFRACTION' 4.04 4.36  . . 142 3981 99.00  . . . . 0.2016 . . . . . . . . . . . 0.1924 
'X-RAY DIFFRACTION' 4.36 4.79  . . 141 4003 99.00  . . . . 0.1878 . . . . . . . . . . . 0.2413 
'X-RAY DIFFRACTION' 4.80 5.49  . . 144 4047 100.00 . . . . 0.1947 . . . . . . . . . . . 0.2159 
'X-RAY DIFFRACTION' 5.49 6.91  . . 145 4087 100.00 . . . . 0.1957 . . . . . . . . . . . 0.2185 
'X-RAY DIFFRACTION' 6.91 49.19 . . 149 4225 100.00 . . . . 0.1543 . . . . . . . . . . . 0.1864 
# 
_struct.entry_id                     9EL7 
_struct.title                        'LSD1-CoREST in complex with T105 enantiomer (1R,2S)' 
_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        9EL7 
_struct_keywords.text            'Epigenetics, Histone demethylase, Drug resistance, Covalent inhibitor, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP KDM1A_HUMAN O60341 ? 1 
;MLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPGGLAEPPGS
AGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPP
EEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEA
PYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATF
RKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNV
LNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLV
KSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEF
TGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFV
PPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISD
DVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAG
EHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM
;
1   
2 UNP RCOR1_HUMAN Q9UKL0 ? 2 
;RAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGIEPYRLPEVIQKCNARWT
TEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAE
;
308 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9EL7 A 20 ? 871 ? O60341 1   ? 852 ? 1   852 
2 2 9EL7 B 9  ? 144 ? Q9UKL0 308 ? 443 ? 305 440 
# 
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 9EL7 GLY A 1  ? UNP O60341 ? ? 'expression tag' -18 1  
1 9EL7 SER A 2  ? UNP O60341 ? ? 'expression tag' -17 2  
1 9EL7 SER A 3  ? UNP O60341 ? ? 'expression tag' -16 3  
1 9EL7 HIS A 4  ? UNP O60341 ? ? 'expression tag' -15 4  
1 9EL7 HIS A 5  ? UNP O60341 ? ? 'expression tag' -14 5  
1 9EL7 HIS A 6  ? UNP O60341 ? ? 'expression tag' -13 6  
1 9EL7 HIS A 7  ? UNP O60341 ? ? 'expression tag' -12 7  
1 9EL7 HIS A 8  ? UNP O60341 ? ? 'expression tag' -11 8  
1 9EL7 HIS A 9  ? UNP O60341 ? ? 'expression tag' -10 9  
1 9EL7 SER A 10 ? UNP O60341 ? ? 'expression tag' -9  10 
1 9EL7 SER A 11 ? UNP O60341 ? ? 'expression tag' -8  11 
1 9EL7 GLY A 12 ? UNP O60341 ? ? 'expression tag' -7  12 
1 9EL7 LEU A 13 ? UNP O60341 ? ? 'expression tag' -6  13 
1 9EL7 VAL A 14 ? UNP O60341 ? ? 'expression tag' -5  14 
1 9EL7 PRO A 15 ? UNP O60341 ? ? 'expression tag' -4  15 
1 9EL7 ARG A 16 ? UNP O60341 ? ? 'expression tag' -3  16 
1 9EL7 GLY A 17 ? UNP O60341 ? ? 'expression tag' -2  17 
1 9EL7 SER A 18 ? UNP O60341 ? ? 'expression tag' -1  18 
1 9EL7 HIS A 19 ? UNP O60341 ? ? 'expression tag' 0   19 
2 9EL7 GLY B 1  ? UNP Q9UKL0 ? ? 'expression tag' 297 20 
2 9EL7 PRO B 2  ? UNP Q9UKL0 ? ? 'expression tag' 298 21 
2 9EL7 LEU B 3  ? UNP Q9UKL0 ? ? 'expression tag' 299 22 
2 9EL7 GLY B 4  ? UNP Q9UKL0 ? ? 'expression tag' 300 23 
2 9EL7 SER B 5  ? UNP Q9UKL0 ? ? 'expression tag' 301 24 
2 9EL7 PRO B 6  ? UNP Q9UKL0 ? ? 'expression tag' 302 25 
2 9EL7 GLU B 7  ? UNP Q9UKL0 ? ? 'expression tag' 303 26 
2 9EL7 PHE B 8  ? UNP Q9UKL0 ? ? 'expression tag' 304 27 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7320  ? 
1 MORE         -43   ? 
1 'SSA (A^2)'  37640 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 192 ? SER A 200 ? GLY A 173 SER A 181 1 ? 9  
HELX_P HELX_P2  AA2 THR A 208 ? PHE A 215 ? THR A 189 PHE A 196 1 ? 8  
HELX_P HELX_P3  AA3 PHE A 215 ? SER A 220 ? PHE A 196 SER A 201 1 ? 6  
HELX_P HELX_P4  AA4 PRO A 222 ? ASN A 243 ? PRO A 203 ASN A 224 1 ? 22 
HELX_P HELX_P5  AA5 THR A 249 ? LEU A 257 ? THR A 230 LEU A 238 1 ? 9  
HELX_P HELX_P6  AA6 ASP A 264 ? HIS A 278 ? ASP A 245 HIS A 259 1 ? 15 
HELX_P HELX_P7  AA7 GLY A 306 ? PHE A 319 ? GLY A 287 PHE A 300 1 ? 14 
HELX_P HELX_P8  AA8 ASN A 359 ? VAL A 368 ? ASN A 340 VAL A 349 1 ? 10 
HELX_P HELX_P9  AA9 PRO A 390 ? GLN A 414 ? PRO A 371 GLN A 395 1 ? 25 
HELX_P HELX_P10 AB1 SER A 426 ? VAL A 487 ? SER A 407 VAL A 468 1 ? 62 
HELX_P HELX_P11 AB2 ASP A 492 ? ASN A 533 ? ASP A 473 ASN A 514 1 ? 42 
HELX_P HELX_P12 AB3 SER A 541 ? ASN A 559 ? SER A 522 ASN A 540 1 ? 19 
HELX_P HELX_P13 AB4 ASP A 574 ? GLU A 578 ? ASP A 555 GLU A 559 5 ? 5  
HELX_P HELX_P14 AB5 SER A 591 ? GLU A 599 ? SER A 572 GLU A 580 1 ? 9  
HELX_P HELX_P15 AB6 PRO A 645 ? GLN A 651 ? PRO A 626 GLN A 632 1 ? 7  
HELX_P HELX_P16 AB7 PRO A 663 ? MET A 673 ? PRO A 644 MET A 654 1 ? 11 
HELX_P HELX_P17 AB8 ALA A 727 ? GLU A 735 ? ALA A 708 GLU A 716 1 ? 9  
HELX_P HELX_P18 AB9 SER A 738 ? GLY A 755 ? SER A 719 GLY A 736 1 ? 18 
HELX_P HELX_P19 AC1 SER A 788 ? GLN A 797 ? SER A 769 GLN A 778 1 ? 10 
HELX_P HELX_P20 AC2 GLY A 819 ? ILE A 823 ? GLY A 800 ILE A 804 5 ? 5  
HELX_P HELX_P21 AC3 THR A 829 ? GLY A 850 ? THR A 810 GLY A 831 1 ? 22 
HELX_P HELX_P22 AC4 ALA A 851 ? LEU A 855 ? ALA A 832 LEU A 836 5 ? 5  
HELX_P HELX_P23 AC5 SER B 21  ? ALA B 30  ? SER B 317 ALA B 326 1 ? 10 
HELX_P HELX_P24 AC6 THR B 33  ? LEU B 67  ? THR B 329 LEU B 363 1 ? 35 
HELX_P HELX_P25 AC7 ILE B 71  ? ARG B 75  ? ILE B 367 ARG B 371 5 ? 5  
HELX_P HELX_P26 AC8 THR B 88  ? GLY B 103 ? THR B 384 GLY B 399 1 ? 16 
HELX_P HELX_P27 AC9 ASP B 105 ? GLY B 114 ? ASP B 401 GLY B 410 1 ? 10 
HELX_P HELX_P28 AD1 SER B 117 ? TYR B 128 ? SER B 413 TYR B 424 1 ? 12 
HELX_P HELX_P29 AD2 ASN B 133 ? ALA B 143 ? ASN B 429 ALA B 439 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
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 ALA 259 A . ? ALA 240 A PRO 260 A ? PRO 241 A 1 6.57  
2 PRO 489 A . ? PRO 470 A PRO 490 A ? PRO 471 A 1 23.63 
3 GLN 652 A . ? GLN 633 A PRO 653 A ? PRO 634 A 1 5.02  
4 VAL 659 A . ? VAL 640 A PRO 660 A ? PRO 641 A 1 0.34  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 6 ? 
AA5 ? 2 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA7 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 ASP A 602 ? LYS A 604 ? ASP A 583 LYS A 585 
AA1 2 ASP A 322 ? LEU A 326 ? ASP A 303 LEU A 307 
AA1 3 LYS A 299 ? ILE A 303 ? LYS A 280 ILE A 284 
AA1 4 ALA A 639 ? CYS A 642 ? ALA A 620 CYS A 623 
AA1 5 LEU A 815 ? PHE A 817 ? LEU A 796 PHE A 798 
AA2 1 THR A 338 ? LYS A 341 ? THR A 319 LYS A 322 
AA2 2 TYR A 344 ? ASP A 347 ? TYR A 325 ASP A 328 
AA3 1 VAL A 352 ? VAL A 353 ? VAL A 333 VAL A 334 
AA3 2 LEU A 584 ? VAL A 586 ? LEU A 565 VAL A 567 
AA3 3 LEU A 372 ? LYS A 374 ? LEU A 353 LYS A 355 
AA4 1 LEU A 381 ? TYR A 382 ? LEU A 362 TYR A 363 
AA4 2 LEU A 696 ? HIS A 699 ? LEU A 677 HIS A 680 
AA4 3 GLU A 709 ? TRP A 714 ? GLU A 690 TRP A 695 
AA4 4 ILE A 721 ? VAL A 726 ? ILE A 702 VAL A 707 
AA4 5 ASN A 679 ? CYS A 684 ? ASN A 660 CYS A 665 
AA4 6 THR A 765 ? VAL A 767 ? THR A 746 VAL A 748 
AA5 1 VAL A 419 ? LEU A 420 ? VAL A 400 LEU A 401 
AA5 2 LYS A 423 ? PRO A 424 ? LYS A 404 PRO A 405 
AA6 1 THR A 632 ? CYS A 637 ? THR A 613 CYS A 618 
AA6 2 GLY A 618 ? ASN A 625 ? GLY A 599 ASN A 606 
AA6 3 THR A 607 ? THR A 615 ? THR A 588 THR A 596 
AA6 4 GLN A 657 ? VAL A 659 ? GLN A 638 VAL A 640 
AA7 1 GLY A 674 ? PHE A 675 ? GLY A 655 PHE A 656 
AA7 2 SER A 781 ? TYR A 782 ? SER A 762 TYR A 763 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LYS A 604 ? O LYS A 585 N LEU A 325 ? N LEU A 306 
AA1 2 3 O ASP A 322 ? O ASP A 303 N VAL A 300 ? N VAL A 281 
AA1 3 4 N ILE A 301 ? N ILE A 282 O LEU A 641 ? O LEU A 622 
AA1 4 5 N CYS A 642 ? N CYS A 623 O PHE A 816 ? O PHE A 797 
AA2 1 2 N PHE A 339 ? N PHE A 320 O ALA A 346 ? O ALA A 327 
AA3 1 2 N VAL A 353 ? N VAL A 334 O LEU A 584 ? O LEU A 565 
AA3 2 3 O THR A 585 ? O THR A 566 N ALA A 373 ? N ALA A 354 
AA4 1 2 N TYR A 382 ? N TYR A 363 O GLY A 698 ? O GLY A 679 
AA4 2 3 N PHE A 697 ? N PHE A 678 O PHE A 713 ? O PHE A 694 
AA4 3 4 N TRP A 714 ? N TRP A 695 O LEU A 723 ? O LEU A 704 
AA4 4 5 O ALA A 724 ? O ALA A 705 N VAL A 681 ? N VAL A 662 
AA4 5 6 N VAL A 682 ? N VAL A 663 O VAL A 766 ? O VAL A 747 
AA5 1 2 N LEU A 420 ? N LEU A 401 O LYS A 423 ? O LYS A 404 
AA6 1 2 O PHE A 633 ? O PHE A 614 N ALA A 623 ? N ALA A 604 
AA6 2 3 O GLU A 620 ? O GLU A 601 N ARG A 613 ? N ARG A 594 
AA6 3 4 N VAL A 612 ? N VAL A 593 O VAL A 659 ? O VAL A 640 
AA7 1 2 N GLY A 674 ? N GLY A 655 O TYR A 782 ? O TYR A 763 
# 
_pdbx_entry_details.entry_id                   9EL7 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG  B SER 406 ? ? O   B LYS 412 ? ? 2.06 
2 1 O   A PHE 666 ? ? CG  A PRO 701 ? ? 2.17 
3 1 OD1 B ASN 327 ? ? N   B ALA 330 ? ? 2.19 
4 1 CE  A LYS 424 ? ? OD1 B ASP 339 ? ? 2.19 
# 
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 THR A 542 ? ? -170.99 147.31 
2 1 SER A 687 ? ? -92.41  31.93  
3 1 ALA A 757 ? ? -138.56 -55.68 
4 1 TYR A 807 ? ? -143.21 48.10  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    TYR 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     571 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.052 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A GLY -18 ? A GLY 1   
2   1 Y 1 A SER -17 ? A SER 2   
3   1 Y 1 A SER -16 ? A SER 3   
4   1 Y 1 A HIS -15 ? A HIS 4   
5   1 Y 1 A HIS -14 ? A HIS 5   
6   1 Y 1 A HIS -13 ? A HIS 6   
7   1 Y 1 A HIS -12 ? A HIS 7   
8   1 Y 1 A HIS -11 ? A HIS 8   
9   1 Y 1 A HIS -10 ? A HIS 9   
10  1 Y 1 A SER -9  ? A SER 10  
11  1 Y 1 A SER -8  ? A SER 11  
12  1 Y 1 A GLY -7  ? A GLY 12  
13  1 Y 1 A LEU -6  ? A LEU 13  
14  1 Y 1 A VAL -5  ? A VAL 14  
15  1 Y 1 A PRO -4  ? A PRO 15  
16  1 Y 1 A ARG -3  ? A ARG 16  
17  1 Y 1 A GLY -2  ? A GLY 17  
18  1 Y 1 A SER -1  ? A SER 18  
19  1 Y 1 A HIS 0   ? A HIS 19  
20  1 Y 1 A MET 1   ? A MET 20  
21  1 Y 1 A LEU 2   ? A LEU 21  
22  1 Y 1 A SER 3   ? A SER 22  
23  1 Y 1 A GLY 4   ? A GLY 23  
24  1 Y 1 A LYS 5   ? A LYS 24  
25  1 Y 1 A LYS 6   ? A LYS 25  
26  1 Y 1 A ALA 7   ? A ALA 26  
27  1 Y 1 A ALA 8   ? A ALA 27  
28  1 Y 1 A ALA 9   ? A ALA 28  
29  1 Y 1 A ALA 10  ? A ALA 29  
30  1 Y 1 A ALA 11  ? A ALA 30  
31  1 Y 1 A ALA 12  ? A ALA 31  
32  1 Y 1 A ALA 13  ? A ALA 32  
33  1 Y 1 A ALA 14  ? A ALA 33  
34  1 Y 1 A ALA 15  ? A ALA 34  
35  1 Y 1 A ALA 16  ? A ALA 35  
36  1 Y 1 A ALA 17  ? A ALA 36  
37  1 Y 1 A ALA 18  ? A ALA 37  
38  1 Y 1 A THR 19  ? A THR 38  
39  1 Y 1 A GLY 20  ? A GLY 39  
40  1 Y 1 A THR 21  ? A THR 40  
41  1 Y 1 A GLU 22  ? A GLU 41  
42  1 Y 1 A ALA 23  ? A ALA 42  
43  1 Y 1 A GLY 24  ? A GLY 43  
44  1 Y 1 A PRO 25  ? A PRO 44  
45  1 Y 1 A GLY 26  ? A GLY 45  
46  1 Y 1 A THR 27  ? A THR 46  
47  1 Y 1 A ALA 28  ? A ALA 47  
48  1 Y 1 A GLY 29  ? A GLY 48  
49  1 Y 1 A GLY 30  ? A GLY 49  
50  1 Y 1 A SER 31  ? A SER 50  
51  1 Y 1 A GLU 32  ? A GLU 51  
52  1 Y 1 A ASN 33  ? A ASN 52  
53  1 Y 1 A GLY 34  ? A GLY 53  
54  1 Y 1 A SER 35  ? A SER 54  
55  1 Y 1 A GLU 36  ? A GLU 55  
56  1 Y 1 A VAL 37  ? A VAL 56  
57  1 Y 1 A ALA 38  ? A ALA 57  
58  1 Y 1 A ALA 39  ? A ALA 58  
59  1 Y 1 A GLN 40  ? A GLN 59  
60  1 Y 1 A PRO 41  ? A PRO 60  
61  1 Y 1 A ALA 42  ? A ALA 61  
62  1 Y 1 A GLY 43  ? A GLY 62  
63  1 Y 1 A LEU 44  ? A LEU 63  
64  1 Y 1 A SER 45  ? A SER 64  
65  1 Y 1 A GLY 46  ? A GLY 65  
66  1 Y 1 A PRO 47  ? A PRO 66  
67  1 Y 1 A ALA 48  ? A ALA 67  
68  1 Y 1 A GLU 49  ? A GLU 68  
69  1 Y 1 A VAL 50  ? A VAL 69  
70  1 Y 1 A GLY 51  ? A GLY 70  
71  1 Y 1 A PRO 52  ? A PRO 71  
72  1 Y 1 A GLY 53  ? A GLY 72  
73  1 Y 1 A ALA 54  ? A ALA 73  
74  1 Y 1 A VAL 55  ? A VAL 74  
75  1 Y 1 A GLY 56  ? A GLY 75  
76  1 Y 1 A GLU 57  ? A GLU 76  
77  1 Y 1 A ARG 58  ? A ARG 77  
78  1 Y 1 A THR 59  ? A THR 78  
79  1 Y 1 A PRO 60  ? A PRO 79  
80  1 Y 1 A ARG 61  ? A ARG 80  
81  1 Y 1 A LYS 62  ? A LYS 81  
82  1 Y 1 A LYS 63  ? A LYS 82  
83  1 Y 1 A GLU 64  ? A GLU 83  
84  1 Y 1 A PRO 65  ? A PRO 84  
85  1 Y 1 A PRO 66  ? A PRO 85  
86  1 Y 1 A ARG 67  ? A ARG 86  
87  1 Y 1 A ALA 68  ? A ALA 87  
88  1 Y 1 A SER 69  ? A SER 88  
89  1 Y 1 A PRO 70  ? A PRO 89  
90  1 Y 1 A PRO 71  ? A PRO 90  
91  1 Y 1 A GLY 72  ? A GLY 91  
92  1 Y 1 A GLY 73  ? A GLY 92  
93  1 Y 1 A LEU 74  ? A LEU 93  
94  1 Y 1 A ALA 75  ? A ALA 94  
95  1 Y 1 A GLU 76  ? A GLU 95  
96  1 Y 1 A PRO 77  ? A PRO 96  
97  1 Y 1 A PRO 78  ? A PRO 97  
98  1 Y 1 A GLY 79  ? A GLY 98  
99  1 Y 1 A SER 80  ? A SER 99  
100 1 Y 1 A ALA 81  ? A ALA 100 
101 1 Y 1 A GLY 82  ? A GLY 101 
102 1 Y 1 A PRO 83  ? A PRO 102 
103 1 Y 1 A GLN 84  ? A GLN 103 
104 1 Y 1 A ALA 85  ? A ALA 104 
105 1 Y 1 A GLY 86  ? A GLY 105 
106 1 Y 1 A PRO 87  ? A PRO 106 
107 1 Y 1 A THR 88  ? A THR 107 
108 1 Y 1 A VAL 89  ? A VAL 108 
109 1 Y 1 A VAL 90  ? A VAL 109 
110 1 Y 1 A PRO 91  ? A PRO 110 
111 1 Y 1 A GLY 92  ? A GLY 111 
112 1 Y 1 A SER 93  ? A SER 112 
113 1 Y 1 A ALA 94  ? A ALA 113 
114 1 Y 1 A THR 95  ? A THR 114 
115 1 Y 1 A PRO 96  ? A PRO 115 
116 1 Y 1 A MET 97  ? A MET 116 
117 1 Y 1 A GLU 98  ? A GLU 117 
118 1 Y 1 A THR 99  ? A THR 118 
119 1 Y 1 A GLY 100 ? A GLY 119 
120 1 Y 1 A ILE 101 ? A ILE 120 
121 1 Y 1 A ALA 102 ? A ALA 121 
122 1 Y 1 A GLU 103 ? A GLU 122 
123 1 Y 1 A THR 104 ? A THR 123 
124 1 Y 1 A PRO 105 ? A PRO 124 
125 1 Y 1 A GLU 106 ? A GLU 125 
126 1 Y 1 A GLY 107 ? A GLY 126 
127 1 Y 1 A ARG 108 ? A ARG 127 
128 1 Y 1 A ARG 109 ? A ARG 128 
129 1 Y 1 A THR 110 ? A THR 129 
130 1 Y 1 A SER 111 ? A SER 130 
131 1 Y 1 A ARG 112 ? A ARG 131 
132 1 Y 1 A ARG 113 ? A ARG 132 
133 1 Y 1 A LYS 114 ? A LYS 133 
134 1 Y 1 A ARG 115 ? A ARG 134 
135 1 Y 1 A ALA 116 ? A ALA 135 
136 1 Y 1 A LYS 117 ? A LYS 136 
137 1 Y 1 A VAL 118 ? A VAL 137 
138 1 Y 1 A GLU 119 ? A GLU 138 
139 1 Y 1 A TYR 120 ? A TYR 139 
140 1 Y 1 A ARG 121 ? A ARG 140 
141 1 Y 1 A GLU 122 ? A GLU 141 
142 1 Y 1 A MET 123 ? A MET 142 
143 1 Y 1 A ASP 124 ? A ASP 143 
144 1 Y 1 A GLU 125 ? A GLU 144 
145 1 Y 1 A SER 126 ? A SER 145 
146 1 Y 1 A LEU 127 ? A LEU 146 
147 1 Y 1 A ALA 128 ? A ALA 147 
148 1 Y 1 A ASN 129 ? A ASN 148 
149 1 Y 1 A LEU 130 ? A LEU 149 
150 1 Y 1 A SER 131 ? A SER 150 
151 1 Y 1 A GLU 132 ? A GLU 151 
152 1 Y 1 A ASP 133 ? A ASP 152 
153 1 Y 1 A GLU 134 ? A GLU 153 
154 1 Y 1 A TYR 135 ? A TYR 154 
155 1 Y 1 A TYR 136 ? A TYR 155 
156 1 Y 1 A SER 137 ? A SER 156 
157 1 Y 1 A GLU 138 ? A GLU 157 
158 1 Y 1 A GLU 139 ? A GLU 158 
159 1 Y 1 A GLU 140 ? A GLU 159 
160 1 Y 1 A ARG 141 ? A ARG 160 
161 1 Y 1 A ASN 142 ? A ASN 161 
162 1 Y 1 A ALA 143 ? A ALA 162 
163 1 Y 1 A LYS 144 ? A LYS 163 
164 1 Y 1 A ALA 145 ? A ALA 164 
165 1 Y 1 A GLU 146 ? A GLU 165 
166 1 Y 1 A LYS 147 ? A LYS 166 
167 1 Y 1 A GLU 148 ? A GLU 167 
168 1 Y 1 A LYS 149 ? A LYS 168 
169 1 Y 1 A LYS 150 ? A LYS 169 
170 1 Y 1 A LEU 151 ? A LEU 170 
171 1 Y 1 A PRO 152 ? A PRO 171 
172 1 Y 1 A PRO 153 ? A PRO 172 
173 1 Y 1 A PRO 154 ? A PRO 173 
174 1 Y 1 A PRO 155 ? A PRO 174 
175 1 Y 1 A PRO 156 ? A PRO 175 
176 1 Y 1 A GLN 157 ? A GLN 176 
177 1 Y 1 A ALA 158 ? A ALA 177 
178 1 Y 1 A PRO 159 ? A PRO 178 
179 1 Y 1 A PRO 160 ? A PRO 179 
180 1 Y 1 A GLU 161 ? A GLU 180 
181 1 Y 1 A GLU 162 ? A GLU 181 
182 1 Y 1 A GLU 163 ? A GLU 182 
183 1 Y 1 A ASN 164 ? A ASN 183 
184 1 Y 1 A GLU 165 ? A GLU 184 
185 1 Y 1 A SER 166 ? A SER 185 
186 1 Y 1 A GLU 167 ? A GLU 186 
187 1 Y 1 A PRO 168 ? A PRO 187 
188 1 Y 1 A GLU 169 ? A GLU 188 
189 1 Y 1 A GLU 170 ? A GLU 189 
190 1 Y 1 A PRO 837 ? A PRO 856 
191 1 Y 1 A ARG 838 ? A ARG 857 
192 1 Y 1 A GLN 839 ? A GLN 858 
193 1 Y 1 A ALA 840 ? A ALA 859 
194 1 Y 1 A THR 841 ? A THR 860 
195 1 Y 1 A PRO 842 ? A PRO 861 
196 1 Y 1 A GLY 843 ? A GLY 862 
197 1 Y 1 A VAL 844 ? A VAL 863 
198 1 Y 1 A PRO 845 ? A PRO 864 
199 1 Y 1 A ALA 846 ? A ALA 865 
200 1 Y 1 A GLN 847 ? A GLN 866 
201 1 Y 1 A GLN 848 ? A GLN 867 
202 1 Y 1 A SER 849 ? A SER 868 
203 1 Y 1 A PRO 850 ? A PRO 869 
204 1 Y 1 A SER 851 ? A SER 870 
205 1 Y 1 A MET 852 ? A MET 871 
206 1 Y 1 B GLY 297 ? B GLY 1   
207 1 Y 1 B PRO 298 ? B PRO 2   
208 1 Y 1 B LEU 299 ? B LEU 3   
209 1 Y 1 B GLY 300 ? B GLY 4   
210 1 Y 1 B SER 301 ? B SER 5   
211 1 Y 1 B PRO 302 ? B PRO 6   
212 1 Y 1 B GLU 303 ? B GLU 7   
213 1 Y 1 B PHE 304 ? B PHE 8   
214 1 Y 1 B ARG 305 ? B ARG 9   
215 1 Y 1 B ALA 306 ? B ALA 10  
216 1 Y 1 B LYS 307 ? B LYS 11  
# 
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 
A1BI4 C4   C N N 1   
A1BI4 C14  C Y N 2   
A1BI4 C5   C Y N 3   
A1BI4 C6   C Y N 4   
A1BI4 C11  C N N 5   
A1BI4 C7   C Y N 6   
A1BI4 C8   C Y N 7   
A1BI4 C9   C Y N 8   
A1BI4 C10  C N R 9   
A1BI4 C12  C N N 10  
A1BI4 C13  C N S 11  
A1BI4 N1   N Y N 12  
A1BI4 N2   N Y N 13  
A1BI4 C3   C Y N 14  
A1BI4 N3   N N N 15  
A1BI4 C1   C N N 16  
A1BI4 C15  C Y N 17  
A1BI4 C16  C Y N 18  
A1BI4 C17  C N N 19  
A1BI4 C18  C Y N 20  
A1BI4 C19  C N N 21  
A1BI4 C2   C Y N 22  
A1BI4 C20  C Y N 23  
A1BI4 C21  C Y N 24  
A1BI4 C22  C N N 25  
A1BI4 C23  C N R 26  
A1BI4 C24  C N S 27  
A1BI4 C25  C N S 28  
A1BI4 C26  C N N 29  
A1BI4 C27  C N N 30  
A1BI4 C28  C N R 31  
A1BI4 C29  C N R 32  
A1BI4 C30  C Y N 33  
A1BI4 C31  C Y N 34  
A1BI4 C32  C Y N 35  
A1BI4 C33  C Y N 36  
A1BI4 C34  C Y N 37  
A1BI4 C35  C N R 38  
A1BI4 C36  C N S 39  
A1BI4 C37  C N N 40  
A1BI4 C38  C N N 41  
A1BI4 C39  C N N 42  
A1BI4 C40  C Y N 43  
A1BI4 N10  N Y N 44  
A1BI4 N11  N N N 45  
A1BI4 N12  N N N 46  
A1BI4 N4   N N N 47  
A1BI4 N5   N N N 48  
A1BI4 N6   N Y N 49  
A1BI4 N7   N Y N 50  
A1BI4 N8   N N N 51  
A1BI4 N9   N Y N 52  
A1BI4 O1   O N N 53  
A1BI4 O10  O N N 54  
A1BI4 O11  O N N 55  
A1BI4 O12  O N N 56  
A1BI4 O13  O N N 57  
A1BI4 O14  O N N 58  
A1BI4 O15  O N N 59  
A1BI4 O16  O N N 60  
A1BI4 O17  O N N 61  
A1BI4 O2   O N N 62  
A1BI4 O3   O N N 63  
A1BI4 O4   O N N 64  
A1BI4 O5   O N N 65  
A1BI4 O6   O N N 66  
A1BI4 O7   O N N 67  
A1BI4 O8   O N N 68  
A1BI4 O9   O N N 69  
A1BI4 P1   P N N 70  
A1BI4 P2   P N N 71  
A1BI4 S1   S Y N 72  
A1BI4 H1   H N N 73  
A1BI4 H2   H N N 74  
A1BI4 H3   H N N 75  
A1BI4 H4   H N N 76  
A1BI4 H5   H N N 77  
A1BI4 H6   H N N 78  
A1BI4 H7   H N N 79  
A1BI4 H8   H N N 80  
A1BI4 H9   H N N 81  
A1BI4 H10  H N N 82  
A1BI4 H11  H N N 83  
A1BI4 H12  H N N 84  
A1BI4 H13  H N N 85  
A1BI4 H14  H N N 86  
A1BI4 H15  H N N 87  
A1BI4 H16  H N N 88  
A1BI4 H17  H N N 89  
A1BI4 H18  H N N 90  
A1BI4 H19  H N N 91  
A1BI4 H20  H N N 92  
A1BI4 H21  H N N 93  
A1BI4 H22  H N N 94  
A1BI4 H23  H N N 95  
A1BI4 H24  H N N 96  
A1BI4 H25  H N N 97  
A1BI4 H26  H N N 98  
A1BI4 H27  H N N 99  
A1BI4 H28  H N N 100 
A1BI4 H29  H N N 101 
A1BI4 H30  H N N 102 
A1BI4 H31  H N N 103 
A1BI4 H32  H N N 104 
A1BI4 H33  H N N 105 
A1BI4 H34  H N N 106 
A1BI4 H36  H N N 107 
A1BI4 H38  H N N 108 
A1BI4 H39  H N N 109 
A1BI4 H40  H N N 110 
A1BI4 H41  H N N 111 
A1BI4 H42  H N N 112 
A1BI4 H43  H N N 113 
A1BI4 H44  H N N 114 
A1BI4 H45  H N N 115 
A1BI4 H46  H N N 116 
A1BI4 H47  H N N 117 
A1BI4 H48  H N N 118 
ALA   N    N N N 119 
ALA   CA   C N S 120 
ALA   C    C N N 121 
ALA   O    O N N 122 
ALA   CB   C N N 123 
ALA   OXT  O N N 124 
ALA   H    H N N 125 
ALA   H2   H N N 126 
ALA   HA   H N N 127 
ALA   HB1  H N N 128 
ALA   HB2  H N N 129 
ALA   HB3  H N N 130 
ALA   HXT  H N N 131 
ARG   N    N N N 132 
ARG   CA   C N S 133 
ARG   C    C N N 134 
ARG   O    O N N 135 
ARG   CB   C N N 136 
ARG   CG   C N N 137 
ARG   CD   C N N 138 
ARG   NE   N N N 139 
ARG   CZ   C N N 140 
ARG   NH1  N N N 141 
ARG   NH2  N N N 142 
ARG   OXT  O N N 143 
ARG   H    H N N 144 
ARG   H2   H N N 145 
ARG   HA   H N N 146 
ARG   HB2  H N N 147 
ARG   HB3  H N N 148 
ARG   HG2  H N N 149 
ARG   HG3  H N N 150 
ARG   HD2  H N N 151 
ARG   HD3  H N N 152 
ARG   HE   H N N 153 
ARG   HH11 H N N 154 
ARG   HH12 H N N 155 
ARG   HH21 H N N 156 
ARG   HH22 H N N 157 
ARG   HXT  H N N 158 
ASN   N    N N N 159 
ASN   CA   C N S 160 
ASN   C    C N N 161 
ASN   O    O N N 162 
ASN   CB   C N N 163 
ASN   CG   C N N 164 
ASN   OD1  O N N 165 
ASN   ND2  N N N 166 
ASN   OXT  O N N 167 
ASN   H    H N N 168 
ASN   H2   H N N 169 
ASN   HA   H N N 170 
ASN   HB2  H N N 171 
ASN   HB3  H N N 172 
ASN   HD21 H N N 173 
ASN   HD22 H N N 174 
ASN   HXT  H N N 175 
ASP   N    N N N 176 
ASP   CA   C N S 177 
ASP   C    C N N 178 
ASP   O    O N N 179 
ASP   CB   C N N 180 
ASP   CG   C N N 181 
ASP   OD1  O N N 182 
ASP   OD2  O N N 183 
ASP   OXT  O N N 184 
ASP   H    H N N 185 
ASP   H2   H N N 186 
ASP   HA   H N N 187 
ASP   HB2  H N N 188 
ASP   HB3  H N N 189 
ASP   HD2  H N N 190 
ASP   HXT  H N N 191 
CYS   N    N N N 192 
CYS   CA   C N R 193 
CYS   C    C N N 194 
CYS   O    O N N 195 
CYS   CB   C N N 196 
CYS   SG   S N N 197 
CYS   OXT  O N N 198 
CYS   H    H N N 199 
CYS   H2   H N N 200 
CYS   HA   H N N 201 
CYS   HB2  H N N 202 
CYS   HB3  H N N 203 
CYS   HG   H N N 204 
CYS   HXT  H N N 205 
GLN   N    N N N 206 
GLN   CA   C N S 207 
GLN   C    C N N 208 
GLN   O    O N N 209 
GLN   CB   C N N 210 
GLN   CG   C N N 211 
GLN   CD   C N N 212 
GLN   OE1  O N N 213 
GLN   NE2  N N N 214 
GLN   OXT  O N N 215 
GLN   H    H N N 216 
GLN   H2   H N N 217 
GLN   HA   H N N 218 
GLN   HB2  H N N 219 
GLN   HB3  H N N 220 
GLN   HG2  H N N 221 
GLN   HG3  H N N 222 
GLN   HE21 H N N 223 
GLN   HE22 H N N 224 
GLN   HXT  H N N 225 
GLU   N    N N N 226 
GLU   CA   C N S 227 
GLU   C    C N N 228 
GLU   O    O N N 229 
GLU   CB   C N N 230 
GLU   CG   C N N 231 
GLU   CD   C N N 232 
GLU   OE1  O N N 233 
GLU   OE2  O N N 234 
GLU   OXT  O N N 235 
GLU   H    H N N 236 
GLU   H2   H N N 237 
GLU   HA   H N N 238 
GLU   HB2  H N N 239 
GLU   HB3  H N N 240 
GLU   HG2  H N N 241 
GLU   HG3  H N N 242 
GLU   HE2  H N N 243 
GLU   HXT  H N N 244 
GLY   N    N N N 245 
GLY   CA   C N N 246 
GLY   C    C N N 247 
GLY   O    O N N 248 
GLY   OXT  O N N 249 
GLY   H    H N N 250 
GLY   H2   H N N 251 
GLY   HA2  H N N 252 
GLY   HA3  H N N 253 
GLY   HXT  H N N 254 
HIS   N    N N N 255 
HIS   CA   C N S 256 
HIS   C    C N N 257 
HIS   O    O N N 258 
HIS   CB   C N N 259 
HIS   CG   C Y N 260 
HIS   ND1  N Y N 261 
HIS   CD2  C Y N 262 
HIS   CE1  C Y N 263 
HIS   NE2  N Y N 264 
HIS   OXT  O N N 265 
HIS   H    H N N 266 
HIS   H2   H N N 267 
HIS   HA   H N N 268 
HIS   HB2  H N N 269 
HIS   HB3  H N N 270 
HIS   HD1  H N N 271 
HIS   HD2  H N N 272 
HIS   HE1  H N N 273 
HIS   HE2  H N N 274 
HIS   HXT  H N N 275 
ILE   N    N N N 276 
ILE   CA   C N S 277 
ILE   C    C N N 278 
ILE   O    O N N 279 
ILE   CB   C N S 280 
ILE   CG1  C N N 281 
ILE   CG2  C N N 282 
ILE   CD1  C N N 283 
ILE   OXT  O N N 284 
ILE   H    H N N 285 
ILE   H2   H N N 286 
ILE   HA   H N N 287 
ILE   HB   H N N 288 
ILE   HG12 H N N 289 
ILE   HG13 H N N 290 
ILE   HG21 H N N 291 
ILE   HG22 H N N 292 
ILE   HG23 H N N 293 
ILE   HD11 H N N 294 
ILE   HD12 H N N 295 
ILE   HD13 H N N 296 
ILE   HXT  H N N 297 
LEU   N    N N N 298 
LEU   CA   C N S 299 
LEU   C    C N N 300 
LEU   O    O N N 301 
LEU   CB   C N N 302 
LEU   CG   C N N 303 
LEU   CD1  C N N 304 
LEU   CD2  C N N 305 
LEU   OXT  O N N 306 
LEU   H    H N N 307 
LEU   H2   H N N 308 
LEU   HA   H N N 309 
LEU   HB2  H N N 310 
LEU   HB3  H N N 311 
LEU   HG   H N N 312 
LEU   HD11 H N N 313 
LEU   HD12 H N N 314 
LEU   HD13 H N N 315 
LEU   HD21 H N N 316 
LEU   HD22 H N N 317 
LEU   HD23 H N N 318 
LEU   HXT  H N N 319 
LYS   N    N N N 320 
LYS   CA   C N S 321 
LYS   C    C N N 322 
LYS   O    O N N 323 
LYS   CB   C N N 324 
LYS   CG   C N N 325 
LYS   CD   C N N 326 
LYS   CE   C N N 327 
LYS   NZ   N N N 328 
LYS   OXT  O N N 329 
LYS   H    H N N 330 
LYS   H2   H N N 331 
LYS   HA   H N N 332 
LYS   HB2  H N N 333 
LYS   HB3  H N N 334 
LYS   HG2  H N N 335 
LYS   HG3  H N N 336 
LYS   HD2  H N N 337 
LYS   HD3  H N N 338 
LYS   HE2  H N N 339 
LYS   HE3  H N N 340 
LYS   HZ1  H N N 341 
LYS   HZ2  H N N 342 
LYS   HZ3  H N N 343 
LYS   HXT  H N N 344 
MET   N    N N N 345 
MET   CA   C N S 346 
MET   C    C N N 347 
MET   O    O N N 348 
MET   CB   C N N 349 
MET   CG   C N N 350 
MET   SD   S N N 351 
MET   CE   C N N 352 
MET   OXT  O N N 353 
MET   H    H N N 354 
MET   H2   H N N 355 
MET   HA   H N N 356 
MET   HB2  H N N 357 
MET   HB3  H N N 358 
MET   HG2  H N N 359 
MET   HG3  H N N 360 
MET   HE1  H N N 361 
MET   HE2  H N N 362 
MET   HE3  H N N 363 
MET   HXT  H N N 364 
PHE   N    N N N 365 
PHE   CA   C N S 366 
PHE   C    C N N 367 
PHE   O    O N N 368 
PHE   CB   C N N 369 
PHE   CG   C Y N 370 
PHE   CD1  C Y N 371 
PHE   CD2  C Y N 372 
PHE   CE1  C Y N 373 
PHE   CE2  C Y N 374 
PHE   CZ   C Y N 375 
PHE   OXT  O N N 376 
PHE   H    H N N 377 
PHE   H2   H N N 378 
PHE   HA   H N N 379 
PHE   HB2  H N N 380 
PHE   HB3  H N N 381 
PHE   HD1  H N N 382 
PHE   HD2  H N N 383 
PHE   HE1  H N N 384 
PHE   HE2  H N N 385 
PHE   HZ   H N N 386 
PHE   HXT  H N N 387 
PRO   N    N N N 388 
PRO   CA   C N S 389 
PRO   C    C N N 390 
PRO   O    O N N 391 
PRO   CB   C N N 392 
PRO   CG   C N N 393 
PRO   CD   C N N 394 
PRO   OXT  O N N 395 
PRO   H    H N N 396 
PRO   HA   H N N 397 
PRO   HB2  H N N 398 
PRO   HB3  H N N 399 
PRO   HG2  H N N 400 
PRO   HG3  H N N 401 
PRO   HD2  H N N 402 
PRO   HD3  H N N 403 
PRO   HXT  H N N 404 
SER   N    N N N 405 
SER   CA   C N S 406 
SER   C    C N N 407 
SER   O    O N N 408 
SER   CB   C N N 409 
SER   OG   O N N 410 
SER   OXT  O N N 411 
SER   H    H N N 412 
SER   H2   H N N 413 
SER   HA   H N N 414 
SER   HB2  H N N 415 
SER   HB3  H N N 416 
SER   HG   H N N 417 
SER   HXT  H N N 418 
THR   N    N N N 419 
THR   CA   C N S 420 
THR   C    C N N 421 
THR   O    O N N 422 
THR   CB   C N R 423 
THR   OG1  O N N 424 
THR   CG2  C N N 425 
THR   OXT  O N N 426 
THR   H    H N N 427 
THR   H2   H N N 428 
THR   HA   H N N 429 
THR   HB   H N N 430 
THR   HG1  H N N 431 
THR   HG21 H N N 432 
THR   HG22 H N N 433 
THR   HG23 H N N 434 
THR   HXT  H N N 435 
TRP   N    N N N 436 
TRP   CA   C N S 437 
TRP   C    C N N 438 
TRP   O    O N N 439 
TRP   CB   C N N 440 
TRP   CG   C Y N 441 
TRP   CD1  C Y N 442 
TRP   CD2  C Y N 443 
TRP   NE1  N Y N 444 
TRP   CE2  C Y N 445 
TRP   CE3  C Y N 446 
TRP   CZ2  C Y N 447 
TRP   CZ3  C Y N 448 
TRP   CH2  C Y N 449 
TRP   OXT  O N N 450 
TRP   H    H N N 451 
TRP   H2   H N N 452 
TRP   HA   H N N 453 
TRP   HB2  H N N 454 
TRP   HB3  H N N 455 
TRP   HD1  H N N 456 
TRP   HE1  H N N 457 
TRP   HE3  H N N 458 
TRP   HZ2  H N N 459 
TRP   HZ3  H N N 460 
TRP   HH2  H N N 461 
TRP   HXT  H N N 462 
TYR   N    N N N 463 
TYR   CA   C N S 464 
TYR   C    C N N 465 
TYR   O    O N N 466 
TYR   CB   C N N 467 
TYR   CG   C Y N 468 
TYR   CD1  C Y N 469 
TYR   CD2  C Y N 470 
TYR   CE1  C Y N 471 
TYR   CE2  C Y N 472 
TYR   CZ   C Y N 473 
TYR   OH   O N N 474 
TYR   OXT  O N N 475 
TYR   H    H N N 476 
TYR   H2   H N N 477 
TYR   HA   H N N 478 
TYR   HB2  H N N 479 
TYR   HB3  H N N 480 
TYR   HD1  H N N 481 
TYR   HD2  H N N 482 
TYR   HE1  H N N 483 
TYR   HE2  H N N 484 
TYR   HH   H N N 485 
TYR   HXT  H N N 486 
VAL   N    N N N 487 
VAL   CA   C N S 488 
VAL   C    C N N 489 
VAL   O    O N N 490 
VAL   CB   C N N 491 
VAL   CG1  C N N 492 
VAL   CG2  C N N 493 
VAL   OXT  O N N 494 
VAL   H    H N N 495 
VAL   H2   H N N 496 
VAL   HA   H N N 497 
VAL   HB   H N N 498 
VAL   HG11 H N N 499 
VAL   HG12 H N N 500 
VAL   HG13 H N N 501 
VAL   HG21 H N N 502 
VAL   HG22 H N N 503 
VAL   HG23 H N N 504 
VAL   HXT  H N N 505 
# 
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 
A1BI4 C1  C2   sing N N 1   
A1BI4 N1  C2   doub Y N 2   
A1BI4 N1  N2   sing Y N 3   
A1BI4 C2  S1   sing Y N 4   
A1BI4 N2  C3   doub Y N 5   
A1BI4 C17 C16  sing N N 6   
A1BI4 S1  C3   sing Y N 7   
A1BI4 C7  C6   doub Y N 8   
A1BI4 C7  C8   sing Y N 9   
A1BI4 C3  N3   sing N N 10  
A1BI4 C6  C5   sing Y N 11  
A1BI4 C16 C15  doub Y N 12  
A1BI4 C16 C18  sing Y N 13  
A1BI4 C15 C14  sing Y N 14  
A1BI4 C8  C9   doub Y N 15  
A1BI4 N3  C4   sing N N 16  
A1BI4 C5  C4   sing N N 17  
A1BI4 C5  C40  doub Y N 18  
A1BI4 C19 C18  sing N N 19  
A1BI4 C18 C20  doub Y N 20  
A1BI4 C4  O1   doub N N 21  
A1BI4 C14 N4   sing N N 22  
A1BI4 C14 C21  doub Y N 23  
A1BI4 N4  C13  sing N N 24  
A1BI4 C9  C40  sing Y N 25  
A1BI4 C9  C10  sing N N 26  
A1BI4 O17 C39  doub N N 27  
A1BI4 C20 C21  sing Y N 28  
A1BI4 C21 N5   sing N N 29  
A1BI4 C11 C10  sing N N 30  
A1BI4 C11 C12  sing N N 31  
A1BI4 C10 C13  sing N N 32  
A1BI4 C13 C39  sing N N 33  
A1BI4 C13 C37  sing N N 34  
A1BI4 C12 O2   doub N N 35  
A1BI4 C39 N12  sing N N 36  
A1BI4 N5  C37  sing N N 37  
A1BI4 N5  C22  sing N N 38  
A1BI4 C37 N11  doub N N 39  
A1BI4 N12 C38  sing N N 40  
A1BI4 C22 C23  sing N N 41  
A1BI4 N11 C38  sing N N 42  
A1BI4 O3  C23  sing N N 43  
A1BI4 C38 O16  doub N N 44  
A1BI4 C23 C24  sing N N 45  
A1BI4 O14 C35  sing N N 46  
A1BI4 C24 C25  sing N N 47  
A1BI4 C24 O4   sing N N 48  
A1BI4 C35 C36  sing N N 49  
A1BI4 C35 C29  sing N N 50  
A1BI4 O11 P2   doub N N 51  
A1BI4 C25 O5   sing N N 52  
A1BI4 C25 C26  sing N N 53  
A1BI4 C30 N7   doub Y N 54  
A1BI4 C30 N6   sing Y N 55  
A1BI4 C36 O15  sing N N 56  
A1BI4 C36 C28  sing N N 57  
A1BI4 N7  C31  sing Y N 58  
A1BI4 O10 P2   sing N N 59  
A1BI4 P2  O9   sing N N 60  
A1BI4 P2  O12  sing N N 61  
A1BI4 N6  C29  sing N N 62  
A1BI4 N6  C34  sing Y N 63  
A1BI4 C29 O13  sing N N 64  
A1BI4 C31 C34  doub Y N 65  
A1BI4 C31 C32  sing Y N 66  
A1BI4 C26 O6   sing N N 67  
A1BI4 N8  C32  sing N N 68  
A1BI4 C34 N10  sing Y N 69  
A1BI4 C32 N9   doub Y N 70  
A1BI4 C28 O13  sing N N 71  
A1BI4 C28 C27  sing N N 72  
A1BI4 O9  P1   sing N N 73  
A1BI4 O12 C27  sing N N 74  
A1BI4 O6  P1   sing N N 75  
A1BI4 N10 C33  doub Y N 76  
A1BI4 N9  C33  sing Y N 77  
A1BI4 P1  O7   doub N N 78  
A1BI4 P1  O8   sing N N 79  
A1BI4 C6  H1   sing N N 80  
A1BI4 C11 H2   sing N N 81  
A1BI4 C11 H3   sing N N 82  
A1BI4 C7  H4   sing N N 83  
A1BI4 C8  H5   sing N N 84  
A1BI4 C10 H6   sing N N 85  
A1BI4 C12 H7   sing N N 86  
A1BI4 N3  H8   sing N N 87  
A1BI4 C1  H9   sing N N 88  
A1BI4 C1  H10  sing N N 89  
A1BI4 C1  H11  sing N N 90  
A1BI4 C15 H12  sing N N 91  
A1BI4 C17 H13  sing N N 92  
A1BI4 C17 H14  sing N N 93  
A1BI4 C17 H15  sing N N 94  
A1BI4 C19 H16  sing N N 95  
A1BI4 C19 H17  sing N N 96  
A1BI4 C19 H18  sing N N 97  
A1BI4 C20 H19  sing N N 98  
A1BI4 C22 H20  sing N N 99  
A1BI4 C22 H21  sing N N 100 
A1BI4 C23 H22  sing N N 101 
A1BI4 C24 H23  sing N N 102 
A1BI4 C25 H24  sing N N 103 
A1BI4 C26 H25  sing N N 104 
A1BI4 C26 H26  sing N N 105 
A1BI4 C27 H27  sing N N 106 
A1BI4 C27 H28  sing N N 107 
A1BI4 C28 H29  sing N N 108 
A1BI4 C29 H30  sing N N 109 
A1BI4 C30 H31  sing N N 110 
A1BI4 C33 H32  sing N N 111 
A1BI4 C35 H33  sing N N 112 
A1BI4 C36 H34  sing N N 113 
A1BI4 C40 H36  sing N N 114 
A1BI4 N12 H38  sing N N 115 
A1BI4 N4  H39  sing N N 116 
A1BI4 N8  H40  sing N N 117 
A1BI4 N8  H41  sing N N 118 
A1BI4 O10 H42  sing N N 119 
A1BI4 O14 H43  sing N N 120 
A1BI4 O15 H44  sing N N 121 
A1BI4 O3  H45  sing N N 122 
A1BI4 O4  H46  sing N N 123 
A1BI4 O5  H47  sing N N 124 
A1BI4 O8  H48  sing N N 125 
ALA   N   CA   sing N N 126 
ALA   N   H    sing N N 127 
ALA   N   H2   sing N N 128 
ALA   CA  C    sing N N 129 
ALA   CA  CB   sing N N 130 
ALA   CA  HA   sing N N 131 
ALA   C   O    doub N N 132 
ALA   C   OXT  sing N N 133 
ALA   CB  HB1  sing N N 134 
ALA   CB  HB2  sing N N 135 
ALA   CB  HB3  sing N N 136 
ALA   OXT HXT  sing N N 137 
ARG   N   CA   sing N N 138 
ARG   N   H    sing N N 139 
ARG   N   H2   sing N N 140 
ARG   CA  C    sing N N 141 
ARG   CA  CB   sing N N 142 
ARG   CA  HA   sing N N 143 
ARG   C   O    doub N N 144 
ARG   C   OXT  sing N N 145 
ARG   CB  CG   sing N N 146 
ARG   CB  HB2  sing N N 147 
ARG   CB  HB3  sing N N 148 
ARG   CG  CD   sing N N 149 
ARG   CG  HG2  sing N N 150 
ARG   CG  HG3  sing N N 151 
ARG   CD  NE   sing N N 152 
ARG   CD  HD2  sing N N 153 
ARG   CD  HD3  sing N N 154 
ARG   NE  CZ   sing N N 155 
ARG   NE  HE   sing N N 156 
ARG   CZ  NH1  sing N N 157 
ARG   CZ  NH2  doub N N 158 
ARG   NH1 HH11 sing N N 159 
ARG   NH1 HH12 sing N N 160 
ARG   NH2 HH21 sing N N 161 
ARG   NH2 HH22 sing N N 162 
ARG   OXT HXT  sing N N 163 
ASN   N   CA   sing N N 164 
ASN   N   H    sing N N 165 
ASN   N   H2   sing N N 166 
ASN   CA  C    sing N N 167 
ASN   CA  CB   sing N N 168 
ASN   CA  HA   sing N N 169 
ASN   C   O    doub N N 170 
ASN   C   OXT  sing N N 171 
ASN   CB  CG   sing N N 172 
ASN   CB  HB2  sing N N 173 
ASN   CB  HB3  sing N N 174 
ASN   CG  OD1  doub N N 175 
ASN   CG  ND2  sing N N 176 
ASN   ND2 HD21 sing N N 177 
ASN   ND2 HD22 sing N N 178 
ASN   OXT HXT  sing N N 179 
ASP   N   CA   sing N N 180 
ASP   N   H    sing N N 181 
ASP   N   H2   sing N N 182 
ASP   CA  C    sing N N 183 
ASP   CA  CB   sing N N 184 
ASP   CA  HA   sing N N 185 
ASP   C   O    doub N N 186 
ASP   C   OXT  sing N N 187 
ASP   CB  CG   sing N N 188 
ASP   CB  HB2  sing N N 189 
ASP   CB  HB3  sing N N 190 
ASP   CG  OD1  doub N N 191 
ASP   CG  OD2  sing N N 192 
ASP   OD2 HD2  sing N N 193 
ASP   OXT HXT  sing N N 194 
CYS   N   CA   sing N N 195 
CYS   N   H    sing N N 196 
CYS   N   H2   sing N N 197 
CYS   CA  C    sing N N 198 
CYS   CA  CB   sing N N 199 
CYS   CA  HA   sing N N 200 
CYS   C   O    doub N N 201 
CYS   C   OXT  sing N N 202 
CYS   CB  SG   sing N N 203 
CYS   CB  HB2  sing N N 204 
CYS   CB  HB3  sing N N 205 
CYS   SG  HG   sing N N 206 
CYS   OXT HXT  sing N N 207 
GLN   N   CA   sing N N 208 
GLN   N   H    sing N N 209 
GLN   N   H2   sing N N 210 
GLN   CA  C    sing N N 211 
GLN   CA  CB   sing N N 212 
GLN   CA  HA   sing N N 213 
GLN   C   O    doub N N 214 
GLN   C   OXT  sing N N 215 
GLN   CB  CG   sing N N 216 
GLN   CB  HB2  sing N N 217 
GLN   CB  HB3  sing N N 218 
GLN   CG  CD   sing N N 219 
GLN   CG  HG2  sing N N 220 
GLN   CG  HG3  sing N N 221 
GLN   CD  OE1  doub N N 222 
GLN   CD  NE2  sing N N 223 
GLN   NE2 HE21 sing N N 224 
GLN   NE2 HE22 sing N N 225 
GLN   OXT HXT  sing N N 226 
GLU   N   CA   sing N N 227 
GLU   N   H    sing N N 228 
GLU   N   H2   sing N N 229 
GLU   CA  C    sing N N 230 
GLU   CA  CB   sing N N 231 
GLU   CA  HA   sing N N 232 
GLU   C   O    doub N N 233 
GLU   C   OXT  sing N N 234 
GLU   CB  CG   sing N N 235 
GLU   CB  HB2  sing N N 236 
GLU   CB  HB3  sing N N 237 
GLU   CG  CD   sing N N 238 
GLU   CG  HG2  sing N N 239 
GLU   CG  HG3  sing N N 240 
GLU   CD  OE1  doub N N 241 
GLU   CD  OE2  sing N N 242 
GLU   OE2 HE2  sing N N 243 
GLU   OXT HXT  sing N N 244 
GLY   N   CA   sing N N 245 
GLY   N   H    sing N N 246 
GLY   N   H2   sing N N 247 
GLY   CA  C    sing N N 248 
GLY   CA  HA2  sing N N 249 
GLY   CA  HA3  sing N N 250 
GLY   C   O    doub N N 251 
GLY   C   OXT  sing N N 252 
GLY   OXT HXT  sing N N 253 
HIS   N   CA   sing N N 254 
HIS   N   H    sing N N 255 
HIS   N   H2   sing N N 256 
HIS   CA  C    sing N N 257 
HIS   CA  CB   sing N N 258 
HIS   CA  HA   sing N N 259 
HIS   C   O    doub N N 260 
HIS   C   OXT  sing N N 261 
HIS   CB  CG   sing N N 262 
HIS   CB  HB2  sing N N 263 
HIS   CB  HB3  sing N N 264 
HIS   CG  ND1  sing Y N 265 
HIS   CG  CD2  doub Y N 266 
HIS   ND1 CE1  doub Y N 267 
HIS   ND1 HD1  sing N N 268 
HIS   CD2 NE2  sing Y N 269 
HIS   CD2 HD2  sing N N 270 
HIS   CE1 NE2  sing Y N 271 
HIS   CE1 HE1  sing N N 272 
HIS   NE2 HE2  sing N N 273 
HIS   OXT HXT  sing N N 274 
ILE   N   CA   sing N N 275 
ILE   N   H    sing N N 276 
ILE   N   H2   sing N N 277 
ILE   CA  C    sing N N 278 
ILE   CA  CB   sing N N 279 
ILE   CA  HA   sing N N 280 
ILE   C   O    doub N N 281 
ILE   C   OXT  sing N N 282 
ILE   CB  CG1  sing N N 283 
ILE   CB  CG2  sing N N 284 
ILE   CB  HB   sing N N 285 
ILE   CG1 CD1  sing N N 286 
ILE   CG1 HG12 sing N N 287 
ILE   CG1 HG13 sing N N 288 
ILE   CG2 HG21 sing N N 289 
ILE   CG2 HG22 sing N N 290 
ILE   CG2 HG23 sing N N 291 
ILE   CD1 HD11 sing N N 292 
ILE   CD1 HD12 sing N N 293 
ILE   CD1 HD13 sing N N 294 
ILE   OXT HXT  sing N N 295 
LEU   N   CA   sing N N 296 
LEU   N   H    sing N N 297 
LEU   N   H2   sing N N 298 
LEU   CA  C    sing N N 299 
LEU   CA  CB   sing N N 300 
LEU   CA  HA   sing N N 301 
LEU   C   O    doub N N 302 
LEU   C   OXT  sing N N 303 
LEU   CB  CG   sing N N 304 
LEU   CB  HB2  sing N N 305 
LEU   CB  HB3  sing N N 306 
LEU   CG  CD1  sing N N 307 
LEU   CG  CD2  sing N N 308 
LEU   CG  HG   sing N N 309 
LEU   CD1 HD11 sing N N 310 
LEU   CD1 HD12 sing N N 311 
LEU   CD1 HD13 sing N N 312 
LEU   CD2 HD21 sing N N 313 
LEU   CD2 HD22 sing N N 314 
LEU   CD2 HD23 sing N N 315 
LEU   OXT HXT  sing N N 316 
LYS   N   CA   sing N N 317 
LYS   N   H    sing N N 318 
LYS   N   H2   sing N N 319 
LYS   CA  C    sing N N 320 
LYS   CA  CB   sing N N 321 
LYS   CA  HA   sing N N 322 
LYS   C   O    doub N N 323 
LYS   C   OXT  sing N N 324 
LYS   CB  CG   sing N N 325 
LYS   CB  HB2  sing N N 326 
LYS   CB  HB3  sing N N 327 
LYS   CG  CD   sing N N 328 
LYS   CG  HG2  sing N N 329 
LYS   CG  HG3  sing N N 330 
LYS   CD  CE   sing N N 331 
LYS   CD  HD2  sing N N 332 
LYS   CD  HD3  sing N N 333 
LYS   CE  NZ   sing N N 334 
LYS   CE  HE2  sing N N 335 
LYS   CE  HE3  sing N N 336 
LYS   NZ  HZ1  sing N N 337 
LYS   NZ  HZ2  sing N N 338 
LYS   NZ  HZ3  sing N N 339 
LYS   OXT HXT  sing N N 340 
MET   N   CA   sing N N 341 
MET   N   H    sing N N 342 
MET   N   H2   sing N N 343 
MET   CA  C    sing N N 344 
MET   CA  CB   sing N N 345 
MET   CA  HA   sing N N 346 
MET   C   O    doub N N 347 
MET   C   OXT  sing N N 348 
MET   CB  CG   sing N N 349 
MET   CB  HB2  sing N N 350 
MET   CB  HB3  sing N N 351 
MET   CG  SD   sing N N 352 
MET   CG  HG2  sing N N 353 
MET   CG  HG3  sing N N 354 
MET   SD  CE   sing N N 355 
MET   CE  HE1  sing N N 356 
MET   CE  HE2  sing N N 357 
MET   CE  HE3  sing N N 358 
MET   OXT HXT  sing N N 359 
PHE   N   CA   sing N N 360 
PHE   N   H    sing N N 361 
PHE   N   H2   sing N N 362 
PHE   CA  C    sing N N 363 
PHE   CA  CB   sing N N 364 
PHE   CA  HA   sing N N 365 
PHE   C   O    doub N N 366 
PHE   C   OXT  sing N N 367 
PHE   CB  CG   sing N N 368 
PHE   CB  HB2  sing N N 369 
PHE   CB  HB3  sing N N 370 
PHE   CG  CD1  doub Y N 371 
PHE   CG  CD2  sing Y N 372 
PHE   CD1 CE1  sing Y N 373 
PHE   CD1 HD1  sing N N 374 
PHE   CD2 CE2  doub Y N 375 
PHE   CD2 HD2  sing N N 376 
PHE   CE1 CZ   doub Y N 377 
PHE   CE1 HE1  sing N N 378 
PHE   CE2 CZ   sing Y N 379 
PHE   CE2 HE2  sing N N 380 
PHE   CZ  HZ   sing N N 381 
PHE   OXT HXT  sing N N 382 
PRO   N   CA   sing N N 383 
PRO   N   CD   sing N N 384 
PRO   N   H    sing N N 385 
PRO   CA  C    sing N N 386 
PRO   CA  CB   sing N N 387 
PRO   CA  HA   sing N N 388 
PRO   C   O    doub N N 389 
PRO   C   OXT  sing N N 390 
PRO   CB  CG   sing N N 391 
PRO   CB  HB2  sing N N 392 
PRO   CB  HB3  sing N N 393 
PRO   CG  CD   sing N N 394 
PRO   CG  HG2  sing N N 395 
PRO   CG  HG3  sing N N 396 
PRO   CD  HD2  sing N N 397 
PRO   CD  HD3  sing N N 398 
PRO   OXT HXT  sing N N 399 
SER   N   CA   sing N N 400 
SER   N   H    sing N N 401 
SER   N   H2   sing N N 402 
SER   CA  C    sing N N 403 
SER   CA  CB   sing N N 404 
SER   CA  HA   sing N N 405 
SER   C   O    doub N N 406 
SER   C   OXT  sing N N 407 
SER   CB  OG   sing N N 408 
SER   CB  HB2  sing N N 409 
SER   CB  HB3  sing N N 410 
SER   OG  HG   sing N N 411 
SER   OXT HXT  sing N N 412 
THR   N   CA   sing N N 413 
THR   N   H    sing N N 414 
THR   N   H2   sing N N 415 
THR   CA  C    sing N N 416 
THR   CA  CB   sing N N 417 
THR   CA  HA   sing N N 418 
THR   C   O    doub N N 419 
THR   C   OXT  sing N N 420 
THR   CB  OG1  sing N N 421 
THR   CB  CG2  sing N N 422 
THR   CB  HB   sing N N 423 
THR   OG1 HG1  sing N N 424 
THR   CG2 HG21 sing N N 425 
THR   CG2 HG22 sing N N 426 
THR   CG2 HG23 sing N N 427 
THR   OXT HXT  sing N N 428 
TRP   N   CA   sing N N 429 
TRP   N   H    sing N N 430 
TRP   N   H2   sing N N 431 
TRP   CA  C    sing N N 432 
TRP   CA  CB   sing N N 433 
TRP   CA  HA   sing N N 434 
TRP   C   O    doub N N 435 
TRP   C   OXT  sing N N 436 
TRP   CB  CG   sing N N 437 
TRP   CB  HB2  sing N N 438 
TRP   CB  HB3  sing N N 439 
TRP   CG  CD1  doub Y N 440 
TRP   CG  CD2  sing Y N 441 
TRP   CD1 NE1  sing Y N 442 
TRP   CD1 HD1  sing N N 443 
TRP   CD2 CE2  doub Y N 444 
TRP   CD2 CE3  sing Y N 445 
TRP   NE1 CE2  sing Y N 446 
TRP   NE1 HE1  sing N N 447 
TRP   CE2 CZ2  sing Y N 448 
TRP   CE3 CZ3  doub Y N 449 
TRP   CE3 HE3  sing N N 450 
TRP   CZ2 CH2  doub Y N 451 
TRP   CZ2 HZ2  sing N N 452 
TRP   CZ3 CH2  sing Y N 453 
TRP   CZ3 HZ3  sing N N 454 
TRP   CH2 HH2  sing N N 455 
TRP   OXT HXT  sing N N 456 
TYR   N   CA   sing N N 457 
TYR   N   H    sing N N 458 
TYR   N   H2   sing N N 459 
TYR   CA  C    sing N N 460 
TYR   CA  CB   sing N N 461 
TYR   CA  HA   sing N N 462 
TYR   C   O    doub N N 463 
TYR   C   OXT  sing N N 464 
TYR   CB  CG   sing N N 465 
TYR   CB  HB2  sing N N 466 
TYR   CB  HB3  sing N N 467 
TYR   CG  CD1  doub Y N 468 
TYR   CG  CD2  sing Y N 469 
TYR   CD1 CE1  sing Y N 470 
TYR   CD1 HD1  sing N N 471 
TYR   CD2 CE2  doub Y N 472 
TYR   CD2 HD2  sing N N 473 
TYR   CE1 CZ   doub Y N 474 
TYR   CE1 HE1  sing N N 475 
TYR   CE2 CZ   sing Y N 476 
TYR   CE2 HE2  sing N N 477 
TYR   CZ  OH   sing N N 478 
TYR   OH  HH   sing N N 479 
TYR   OXT HXT  sing N N 480 
VAL   N   CA   sing N N 481 
VAL   N   H    sing N N 482 
VAL   N   H2   sing N N 483 
VAL   CA  C    sing N N 484 
VAL   CA  CB   sing N N 485 
VAL   CA  HA   sing N N 486 
VAL   C   O    doub N N 487 
VAL   C   OXT  sing N N 488 
VAL   CB  CG1  sing N N 489 
VAL   CB  CG2  sing N N 490 
VAL   CB  HB   sing N N 491 
VAL   CG1 HG11 sing N N 492 
VAL   CG1 HG12 sing N N 493 
VAL   CG1 HG13 sing N N 494 
VAL   CG2 HG21 sing N N 495 
VAL   CG2 HG22 sing N N 496 
VAL   CG2 HG23 sing N N 497 
VAL   OXT HXT  sing N N 498 
# 
_pdbx_audit_support.funding_organization   'Italian Association for Cancer Research' 
_pdbx_audit_support.country                Italy 
_pdbx_audit_support.grant_number           IG19808 
_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   2v1d 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EL7 
_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]   0.008326 
_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]   0.005563 
_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]   0.004254 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . PRO   A 1 190 ? -16.444 38.758  98.469  1.00 134.69 ?  171 PRO   A N   1 
ATOM   2    C CA  . PRO   A 1 190 ? -16.557 38.645  99.931  1.00 133.89 ?  171 PRO   A CA  1 
ATOM   3    C C   . PRO   A 1 190 ? -17.962 39.078  100.372 1.00 130.27 ?  171 PRO   A C   1 
ATOM   4    O O   . PRO   A 1 190 ? -18.602 39.766  99.615  1.00 131.51 ?  171 PRO   A O   1 
ATOM   5    C CB  . PRO   A 1 190 ? -15.454 39.566  100.469 1.00 117.20 ?  171 PRO   A CB  1 
ATOM   6    C CG  . PRO   A 1 190 ? -14.459 39.613  99.348  1.00 112.47 ?  171 PRO   A CG  1 
ATOM   7    C CD  . PRO   A 1 190 ? -15.335 39.652  98.118  1.00 114.59 ?  171 PRO   A CD  1 
ATOM   8    N N   . SER   A 1 191 ? -18.399 38.677  101.569 1.00 124.73 ?  172 SER   A N   1 
ATOM   9    C CA  . SER   A 1 191 ? -19.777 39.024  102.000 1.00 122.75 ?  172 SER   A CA  1 
ATOM   10   C C   . SER   A 1 191 ? -19.855 39.366  103.487 1.00 118.24 ?  172 SER   A C   1 
ATOM   11   O O   . SER   A 1 191 ? -19.010 38.899  104.252 1.00 120.62 ?  172 SER   A O   1 
ATOM   12   C CB  . SER   A 1 191 ? -20.717 37.900  101.669 1.00 127.24 ?  172 SER   A CB  1 
ATOM   13   O OG  . SER   A 1 191 ? -20.301 36.697  102.292 1.00 119.32 ?  172 SER   A OG  1 
ATOM   14   N N   . GLY   A 1 192 ? -20.887 40.120  103.865 1.00 104.71 ?  173 GLY   A N   1 
ATOM   15   C CA  . GLY   A 1 192 ? -21.116 40.483  105.274 1.00 112.30 ?  173 GLY   A CA  1 
ATOM   16   C C   . GLY   A 1 192 ? -20.222 41.603  105.753 1.00 105.44 ?  173 GLY   A C   1 
ATOM   17   O O   . GLY   A 1 192 ? -19.868 42.459  104.958 1.00 94.49  ?  173 GLY   A O   1 
ATOM   18   N N   . VAL   A 1 193 ? -19.910 41.614  107.044 1.00 101.16 ?  174 VAL   A N   1 
ATOM   19   C CA  . VAL   A 1 193 ? -19.029 42.674  107.592 1.00 88.51  ?  174 VAL   A CA  1 
ATOM   20   C C   . VAL   A 1 193 ? -17.657 42.547  106.953 1.00 92.15  ?  174 VAL   A C   1 
ATOM   21   O O   . VAL   A 1 193 ? -17.159 43.544  106.508 1.00 99.20  ?  174 VAL   A O   1 
ATOM   22   C CB  . VAL   A 1 193 ? -19.009 42.714  109.126 1.00 88.82  ?  174 VAL   A CB  1 
ATOM   23   C CG1 . VAL   A 1 193 ? -20.414 42.770  109.676 1.00 89.06  ?  174 VAL   A CG1 1 
ATOM   24   C CG2 . VAL   A 1 193 ? -18.231 41.582  109.758 1.00 96.07  ?  174 VAL   A CG2 1 
ATOM   25   N N   . GLU   A 1 194 ? -17.158 41.339  106.726 1.00 96.99  ?  175 GLU   A N   1 
ATOM   26   C CA  . GLU   A 1 194 ? -15.830 41.152  106.096 1.00 102.19 ?  175 GLU   A CA  1 
ATOM   27   C C   . GLU   A 1 194 ? -15.834 41.775  104.692 1.00 97.52  ?  175 GLU   A C   1 
ATOM   28   O O   . GLU   A 1 194 ? -14.812 42.291  104.292 1.00 87.20  ?  175 GLU   A O   1 
ATOM   29   C CB  . GLU   A 1 194 ? -15.428 39.679  106.159 1.00 101.04 ?  175 GLU   A CB  1 
ATOM   30   C CG  . GLU   A 1 194 ? -16.578 38.772  106.548 1.00 112.26 ?  175 GLU   A CG  1 
ATOM   31   C CD  . GLU   A 1 194 ? -16.214 37.529  107.337 1.00 122.82 ?  175 GLU   A CD  1 
ATOM   32   O OE1 . GLU   A 1 194 ? -15.037 37.372  107.686 1.00 121.84 ?  175 GLU   A OE1 1 
ATOM   33   O OE2 . GLU   A 1 194 ? -17.117 36.723  107.600 1.00 121.95 ?  175 GLU   A OE2 1 
ATOM   34   N N   . GLY   A 1 195 ? -16.937 41.697  103.955 1.00 98.57  ?  176 GLY   A N   1 
ATOM   35   C CA  . GLY   A 1 195 ? -17.037 42.339  102.638 1.00 93.73  ?  176 GLY   A CA  1 
ATOM   36   C C   . GLY   A 1 195 ? -16.887 43.833  102.751 1.00 82.29  ?  176 GLY   A C   1 
ATOM   37   O O   . GLY   A 1 195 ? -16.319 44.409  101.859 1.00 80.85  ?  176 GLY   A O   1 
ATOM   38   N N   . ALA   A 1 196 ? -17.426 44.442  103.799 1.00 91.81  ?  177 ALA   A N   1 
ATOM   39   C CA  . ALA   A 1 196 ? -17.307 45.902  103.997 1.00 85.02  ?  177 ALA   A CA  1 
ATOM   40   C C   . ALA   A 1 196 ? -15.841 46.295  104.161 1.00 74.55  ?  177 ALA   A C   1 
ATOM   41   O O   . ALA   A 1 196 ? -15.446 47.302  103.633 1.00 74.70  ?  177 ALA   A O   1 
ATOM   42   C CB  . ALA   A 1 196 ? -18.121 46.315  105.179 1.00 77.44  ?  177 ALA   A CB  1 
ATOM   43   N N   . ALA   A 1 197 ? -15.055 45.491  104.857 1.00 71.07  ?  178 ALA   A N   1 
ATOM   44   C CA  . ALA   A 1 197 ? -13.620 45.784  105.036 1.00 74.66  ?  178 ALA   A CA  1 
ATOM   45   C C   . ALA   A 1 197 ? -12.907 45.762  103.691 1.00 75.56  ?  178 ALA   A C   1 
ATOM   46   O O   . ALA   A 1 197 ? -11.953 46.500  103.504 1.00 69.76  ?  178 ALA   A O   1 
ATOM   47   C CB  . ALA   A 1 197 ? -13.015 44.773  105.956 1.00 69.88  ?  178 ALA   A CB  1 
ATOM   48   N N   . PHE   A 1 198 ? -13.293 44.839  102.834 1.00 75.84  ?  179 PHE   A N   1 
ATOM   49   C CA  . PHE   A 1 198 ? -12.668 44.736  101.507 1.00 75.20  ?  179 PHE   A CA  1 
ATOM   50   C C   . PHE   A 1 198 ? -13.102 45.943  100.688 1.00 71.53  ?  179 PHE   A C   1 
ATOM   51   O O   . PHE   A 1 198 ? -12.289 46.543  100.034 1.00 66.95  ?  179 PHE   A O   1 
ATOM   52   C CB  . PHE   A 1 198 ? -13.058 43.397  100.892 1.00 70.04  ?  179 PHE   A CB  1 
ATOM   53   C CG  . PHE   A 1 198 ? -12.835 43.299  99.415  1.00 71.88  ?  179 PHE   A CG  1 
ATOM   54   C CD1 . PHE   A 1 198 ? -11.641 42.835  98.919  1.00 71.75  ?  179 PHE   A CD1 1 
ATOM   55   C CD2 . PHE   A 1 198 ? -13.822 43.667  98.530  1.00 72.75  ?  179 PHE   A CD2 1 
ATOM   56   C CE1 . PHE   A 1 198 ? -11.436 42.758  97.559  1.00 77.94  ?  179 PHE   A CE1 1 
ATOM   57   C CE2 . PHE   A 1 198 ? -13.616 43.593  97.171  1.00 68.88  ?  179 PHE   A CE2 1 
ATOM   58   C CZ  . PHE   A 1 198 ? -12.419 43.143  96.693  1.00 72.96  ?  179 PHE   A CZ  1 
ATOM   59   N N   . GLN   A 1 199 ? -14.365 46.303  100.762 1.00 65.38  ?  180 GLN   A N   1 
ATOM   60   C CA  . GLN   A 1 199 ? -14.826 47.432  99.973  1.00 68.86  ?  180 GLN   A CA  1 
ATOM   61   C C   . GLN   A 1 199 ? -14.232 48.758  100.454 1.00 75.88  ?  180 GLN   A C   1 
ATOM   62   O O   . GLN   A 1 199 ? -14.301 49.766  99.737  1.00 78.76  ?  180 GLN   A O   1 
ATOM   63   C CB  . GLN   A 1 199 ? -16.356 47.451  100.004 1.00 73.01  ?  180 GLN   A CB  1 
ATOM   64   C CG  . GLN   A 1 199 ? -17.018 48.521  99.142  1.00 80.13  ?  180 GLN   A CG  1 
ATOM   65   C CD  . GLN   A 1 199 ? -16.519 48.518  97.702  1.00 82.96  ?  180 GLN   A CD  1 
ATOM   66   O OE1 . GLN   A 1 199 ? -16.040 47.500  97.197  1.00 80.50  ?  180 GLN   A OE1 1 
ATOM   67   N NE2 . GLN   A 1 199 ? -16.616 49.671  97.038  1.00 85.21  ?  180 GLN   A NE2 1 
ATOM   68   N N   . SER   A 1 200 ? -13.628 48.776  101.638 1.00 76.74  ?  181 SER   A N   1 
ATOM   69   C CA  . SER   A 1 200 ? -12.936 49.942  102.165 1.00 74.25  ?  181 SER   A CA  1 
ATOM   70   C C   . SER   A 1 200 ? -11.413 49.822  102.042 1.00 70.79  ?  181 SER   A C   1 
ATOM   71   O O   . SER   A 1 200 ? -10.681 50.617  102.639 1.00 78.89  ?  181 SER   A O   1 
ATOM   72   C CB  . SER   A 1 200 ? -13.351 50.160  103.628 1.00 74.06  ?  181 SER   A CB  1 
ATOM   73   O OG  . SER   A 1 200 ? -14.707 50.577  103.718 1.00 75.15  ?  181 SER   A OG  1 
ATOM   74   N N   . ARG   A 1 201 ? -10.927 48.844  101.292 1.00 66.33  ?  182 ARG   A N   1 
ATOM   75   C CA  . ARG   A 1 201 ? -9.501  48.591  101.105 1.00 57.42  ?  182 ARG   A CA  1 
ATOM   76   C C   . ARG   A 1 201 ? -8.781  48.321  102.417 1.00 59.40  ?  182 ARG   A C   1 
ATOM   77   O O   . ARG   A 1 201 ? -7.588  48.620  102.537 1.00 58.92  ?  182 ARG   A O   1 
ATOM   78   C CB  . ARG   A 1 201 ? -8.828  49.727  100.339 1.00 53.97  ?  182 ARG   A CB  1 
ATOM   79   C CG  . ARG   A 1 201 ? -9.625  50.176  99.131  1.00 56.90  ?  182 ARG   A CG  1 
ATOM   80   C CD  . ARG   A 1 201 ? -9.421  51.648  98.876  1.00 67.23  ?  182 ARG   A CD  1 
ATOM   81   N NE  . ARG   A 1 201 ? -10.094 52.441  99.904  1.00 71.14  ?  182 ARG   A NE  1 
ATOM   82   C CZ  . ARG   A 1 201 ? -11.313 52.947  99.762  1.00 75.03  ?  182 ARG   A CZ  1 
ATOM   83   N NH1 . ARG   A 1 201 ? -11.984 52.764  98.625  1.00 69.16  ?  182 ARG   A NH1 1 
ATOM   84   N NH2 . ARG   A 1 201 ? -11.860 53.640  100.754 1.00 79.82  ?  182 ARG   A NH2 1 
ATOM   85   N N   . LEU   A 1 202 ? -9.477  47.689  103.387 1.00 65.38  ?  183 LEU   A N   1 
ATOM   86   C CA  . LEU   A 1 202 ? -8.910  47.326  104.694 1.00 64.70  ?  183 LEU   A CA  1 
ATOM   87   C C   . LEU   A 1 202 ? -8.962  45.825  104.942 1.00 65.76  ?  183 LEU   A C   1 
ATOM   88   O O   . LEU   A 1 202 ? -9.974  45.184  104.639 1.00 73.84  ?  183 LEU   A O   1 
ATOM   89   C CB  . LEU   A 1 202 ? -9.656  48.010  105.850 1.00 67.88  ?  183 LEU   A CB  1 
ATOM   90   C CG  . LEU   A 1 202 ? -9.800  49.524  105.839 1.00 64.94  ?  183 LEU   A CG  1 
ATOM   91   C CD1 . LEU   A 1 202 ? -11.095 49.922  106.518 1.00 63.85  ?  183 LEU   A CD1 1 
ATOM   92   C CD2 . LEU   A 1 202 ? -8.598  50.103  106.526 1.00 69.34  ?  183 LEU   A CD2 1 
ATOM   93   N N   . PRO   A 1 203 ? -7.924  45.246  105.549 1.00 64.68  ?  184 PRO   A N   1 
ATOM   94   C CA  . PRO   A 1 203 ? -8.012  43.841  105.988 1.00 64.09  ?  184 PRO   A CA  1 
ATOM   95   C C   . PRO   A 1 203 ? -9.034  43.699  107.107 1.00 73.97  ?  184 PRO   A C   1 
ATOM   96   O O   . PRO   A 1 203 ? -9.028  44.488  108.057 1.00 75.92  ?  184 PRO   A O   1 
ATOM   97   C CB  . PRO   A 1 203 ? -6.595  43.537  106.486 1.00 66.94  ?  184 PRO   A CB  1 
ATOM   98   C CG  . PRO   A 1 203 ? -6.068  44.857  106.917 1.00 69.74  ?  184 PRO   A CG  1 
ATOM   99   C CD  . PRO   A 1 203 ? -6.680  45.898  106.002 1.00 59.63  ?  184 PRO   A CD  1 
ATOM   100  N N   . HIS   A 1 204 ? -9.911  42.686  107.005 1.00 78.34  ?  185 HIS   A N   1 
ATOM   101  C CA  . HIS   A 1 204 ? -10.909 42.508  108.063 1.00 76.95  ?  185 HIS   A CA  1 
ATOM   102  C C   . HIS   A 1 204 ? -10.339 41.953  109.347 1.00 72.30  ?  185 HIS   A C   1 
ATOM   103  O O   . HIS   A 1 204 ? -10.970 42.119  110.392 1.00 75.13  ?  185 HIS   A O   1 
ATOM   104  C CB  . HIS   A 1 204 ? -12.064 41.592  107.655 1.00 82.06  ?  185 HIS   A CB  1 
ATOM   105  C CG  . HIS   A 1 204 ? -11.646 40.210  107.261 1.00 93.81  ?  185 HIS   A CG  1 
ATOM   106  N ND1 . HIS   A 1 204 ? -11.262 39.252  108.180 1.00 92.50  ?  185 HIS   A ND1 1 
ATOM   107  C CD2 . HIS   A 1 204 ? -11.667 39.588  106.058 1.00 94.29  ?  185 HIS   A CD2 1 
ATOM   108  C CE1 . HIS   A 1 204 ? -10.969 38.134  107.543 1.00 92.20  ?  185 HIS   A CE1 1 
ATOM   109  N NE2 . HIS   A 1 204 ? -11.222 38.307  106.258 1.00 96.54  ?  185 HIS   A NE2 1 
ATOM   110  N N   . ASP   A 1 205 ? -9.172  41.325  109.302 1.00 70.29  ?  186 ASP   A N   1 
ATOM   111  C CA  . ASP   A 1 205 ? -8.707  40.508  110.416 1.00 78.03  ?  186 ASP   A CA  1 
ATOM   112  C C   . ASP   A 1 205 ? -7.450  41.048  111.082 1.00 78.06  ?  186 ASP   A C   1 
ATOM   113  O O   . ASP   A 1 205 ? -6.867  40.378  111.951 1.00 74.90  ?  186 ASP   A O   1 
ATOM   114  C CB  . ASP   A 1 205 ? -8.503  39.062  109.938 1.00 87.54  ?  186 ASP   A CB  1 
ATOM   115  C CG  . ASP   A 1 205 ? -7.401  38.914  108.865 1.00 93.34  ?  186 ASP   A CG  1 
ATOM   116  O OD1 . ASP   A 1 205 ? -7.440  37.877  108.169 1.00 96.55  ?  186 ASP   A OD1 1 
ATOM   117  O OD2 . ASP   A 1 205 ? -6.509  39.786  108.727 1.00 95.33  ?  186 ASP   A OD2 1 
ATOM   118  N N   . ARG   A 1 206 ? -7.024  42.245  110.707 1.00 79.77  ?  187 ARG   A N   1 
ATOM   119  C CA  . ARG   A 1 206 ? -5.839  42.857  111.278 1.00 83.33  ?  187 ARG   A CA  1 
ATOM   120  C C   . ARG   A 1 206 ? -6.103  44.354  111.342 1.00 80.19  ?  187 ARG   A C   1 
ATOM   121  O O   . ARG   A 1 206 ? -6.927  44.883  110.587 1.00 73.25  ?  187 ARG   A O   1 
ATOM   122  C CB  . ARG   A 1 206 ? -4.613  42.512  110.423 1.00 83.10  ?  187 ARG   A CB  1 
ATOM   123  C CG  . ARG   A 1 206 ? -3.228  42.790  111.011 1.00 92.63  ?  187 ARG   A CG  1 
ATOM   124  C CD  . ARG   A 1 206 ? -2.178  42.279  110.016 1.00 91.97  ?  187 ARG   A CD  1 
ATOM   125  N NE  . ARG   A 1 206 ? -2.417  42.862  108.696 1.00 98.59  ?  187 ARG   A NE  1 
ATOM   126  C CZ  . ARG   A 1 206 ? -2.932  42.199  107.657 1.00 99.62  ?  187 ARG   A CZ  1 
ATOM   127  N NH1 . ARG   A 1 206 ? -3.279  40.917  107.784 1.00 97.98  ?  187 ARG   A NH1 1 
ATOM   128  N NH2 . ARG   A 1 206 ? -3.126  42.827  106.498 1.00 89.50  ?  187 ARG   A NH2 1 
ATOM   129  N N   . MET   A 1 207 ? -5.447  45.038  112.267 1.00 81.25  ?  188 MET   A N   1 
ATOM   130  C CA  . MET   A 1 207 ? -5.545  46.488  112.264 1.00 77.64  ?  188 MET   A CA  1 
ATOM   131  C C   . MET   A 1 207 ? -4.377  47.084  111.500 1.00 74.21  ?  188 MET   A C   1 
ATOM   132  O O   . MET   A 1 207 ? -3.247  46.574  111.562 1.00 73.06  ?  188 MET   A O   1 
ATOM   133  C CB  . MET   A 1 207 ? -5.635  47.069  113.679 1.00 74.87  ?  188 MET   A CB  1 
ATOM   134  C CG  . MET   A 1 207 ? -6.811  46.529  114.509 1.00 78.99  ?  188 MET   A CG  1 
ATOM   135  S SD  . MET   A 1 207 ? -6.974  47.340  116.130 1.00 86.69  ?  188 MET   A SD  1 
ATOM   136  C CE  . MET   A 1 207 ? -5.328  47.086  116.656 1.00 74.47  ?  188 MET   A CE  1 
ATOM   137  N N   . THR   A 1 208 ? -4.685  48.148  110.745 1.00 71.29  ?  189 THR   A N   1 
ATOM   138  C CA  . THR   A 1 208 ? -3.739  48.850  109.890 1.00 65.64  ?  189 THR   A CA  1 
ATOM   139  C C   . THR   A 1 208 ? -2.816  49.729  110.723 1.00 65.52  ?  189 THR   A C   1 
ATOM   140  O O   . THR   A 1 208 ? -3.035  49.968  111.910 1.00 70.29  ?  189 THR   A O   1 
ATOM   141  C CB  . THR   A 1 208 ? -4.466  49.700  108.837 1.00 66.42  ?  189 THR   A CB  1 
ATOM   142  O OG1 . THR   A 1 208 ? -4.996  50.904  109.424 1.00 70.92  ?  189 THR   A OG1 1 
ATOM   143  C CG2 . THR   A 1 208 ? -5.587  48.934  108.189 1.00 59.36  ?  189 THR   A CG2 1 
ATOM   144  N N   . SER   A 1 209 ? -1.766  50.217  110.075 1.00 72.12  ?  190 SER   A N   1 
ATOM   145  C CA  . SER   A 1 209 ? -0.872  51.173  110.721 1.00 72.67  ?  190 SER   A CA  1 
ATOM   146  C C   . SER   A 1 209 ? -1.607  52.451  111.125 1.00 69.93  ?  190 SER   A C   1 
ATOM   147  O O   . SER   A 1 209 ? -1.298  53.048  112.166 1.00 62.95  ?  190 SER   A O   1 
ATOM   148  C CB  . SER   A 1 209 ? 0.285   51.495  109.774 1.00 71.40  ?  190 SER   A CB  1 
ATOM   149  O OG  . SER   A 1 209 ? 1.363   52.083  110.464 1.00 72.21  ?  190 SER   A OG  1 
ATOM   150  N N   . GLN   A 1 210 ? -2.577  52.887  110.317 1.00 71.01  ?  191 GLN   A N   1 
ATOM   151  C CA  . GLN   A 1 210 ? -3.328  54.089  110.661 1.00 71.46  ?  191 GLN   A CA  1 
ATOM   152  C C   . GLN   A 1 210 ? -4.061  53.918  111.982 1.00 70.96  ?  191 GLN   A C   1 
ATOM   153  O O   . GLN   A 1 210 ? -4.079  54.831  112.814 1.00 72.85  ?  191 GLN   A O   1 
ATOM   154  C CB  . GLN   A 1 210 ? -4.311  54.435  109.541 1.00 72.88  ?  191 GLN   A CB  1 
ATOM   155  C CG  . GLN   A 1 210 ? -4.718  55.890  109.543 1.00 80.61  ?  191 GLN   A CG  1 
ATOM   156  C CD  . GLN   A 1 210 ? -5.636  56.275  108.385 1.00 85.99  ?  191 GLN   A CD  1 
ATOM   157  O OE1 . GLN   A 1 210 ? -5.967  55.452  107.517 1.00 94.84  ?  191 GLN   A OE1 1 
ATOM   158  N NE2 . GLN   A 1 210 ? -6.072  57.536  108.382 1.00 81.77  ?  191 GLN   A NE2 1 
ATOM   159  N N   . GLU   A 1 211 ? -4.657  52.743  112.196 1.00 72.13  ?  192 GLU   A N   1 
ATOM   160  C CA  . GLU   A 1 211 ? -5.471  52.497  113.379 1.00 66.23  ?  192 GLU   A CA  1 
ATOM   161  C C   . GLU   A 1 211 ? -4.598  52.273  114.602 1.00 61.86  ?  192 GLU   A C   1 
ATOM   162  O O   . GLU   A 1 211 ? -4.921  52.738  115.696 1.00 61.90  ?  192 GLU   A O   1 
ATOM   163  C CB  . GLU   A 1 211 ? -6.393  51.305  113.117 1.00 66.26  ?  192 GLU   A CB  1 
ATOM   164  C CG  . GLU   A 1 211 ? -7.036  51.413  111.743 1.00 76.41  ?  192 GLU   A CG  1 
ATOM   165  C CD  . GLU   A 1 211 ? -7.976  50.271  111.334 1.00 79.18  ?  192 GLU   A CD  1 
ATOM   166  O OE1 . GLU   A 1 211 ? -9.100  50.642  110.896 1.00 76.71  ?  192 GLU   A OE1 1 
ATOM   167  O OE2 . GLU   A 1 211 ? -7.590  49.055  111.377 1.00 65.51  ?  192 GLU   A OE2 1 
ATOM   168  N N   . ALA   A 1 212 ? -3.479  51.578  114.431 1.00 59.96  ?  193 ALA   A N   1 
ATOM   169  C CA  . ALA   A 1 212 ? -2.517  51.470  115.514 1.00 60.78  ?  193 ALA   A CA  1 
ATOM   170  C C   . ALA   A 1 212 ? -2.128  52.843  116.045 1.00 64.10  ?  193 ALA   A C   1 
ATOM   171  O O   . ALA   A 1 212 ? -1.876  53.007  117.246 1.00 62.70  ?  193 ALA   A O   1 
ATOM   172  C CB  . ALA   A 1 212 ? -1.278  50.713  115.034 1.00 61.32  ?  193 ALA   A CB  1 
ATOM   173  N N   . ALA   A 1 213 ? -2.080  53.844  115.171 1.00 68.30  ?  194 ALA   A N   1 
ATOM   174  C CA  . ALA   A 1 213 ? -1.710  55.174  115.627 1.00 68.78  ?  194 ALA   A CA  1 
ATOM   175  C C   . ALA   A 1 213 ? -2.832  55.812  116.442 1.00 65.06  ?  194 ALA   A C   1 
ATOM   176  O O   . ALA   A 1 213 ? -2.573  56.440  117.467 1.00 68.96  ?  194 ALA   A O   1 
ATOM   177  C CB  . ALA   A 1 213 ? -1.335  56.034  114.432 1.00 66.58  ?  194 ALA   A CB  1 
ATOM   178  N N   . CYS   A 1 214 ? -4.079  55.635  116.027 1.00 63.08  ?  195 CYS   A N   1 
ATOM   179  C CA  . CYS   A 1 214 ? -5.202  56.200  116.756 1.00 66.17  ?  195 CYS   A CA  1 
ATOM   180  C C   . CYS   A 1 214 ? -5.689  55.350  117.924 1.00 70.55  ?  195 CYS   A C   1 
ATOM   181  O O   . CYS   A 1 214 ? -6.421  55.860  118.774 1.00 72.25  ?  195 CYS   A O   1 
ATOM   182  C CB  . CYS   A 1 214 ? -6.365  56.412  115.805 1.00 71.20  ?  195 CYS   A CB  1 
ATOM   183  S SG  . CYS   A 1 214 ? -5.913  57.465  114.463 1.00 89.02  ?  195 CYS   A SG  1 
ATOM   184  N N   . PHE   A 1 215 ? -5.358  54.063  117.966 1.00 72.42  ?  196 PHE   A N   1 
ATOM   185  C CA  . PHE   A 1 215 ? -5.810  53.182  119.042 1.00 63.46  ?  196 PHE   A CA  1 
ATOM   186  C C   . PHE   A 1 215 ? -4.632  52.379  119.570 1.00 62.65  ?  196 PHE   A C   1 
ATOM   187  O O   . PHE   A 1 215 ? -4.685  51.153  119.641 1.00 61.64  ?  196 PHE   A O   1 
ATOM   188  C CB  . PHE   A 1 215 ? -6.916  52.251  118.564 1.00 61.57  ?  196 PHE   A CB  1 
ATOM   189  C CG  . PHE   A 1 215 ? -8.099  52.956  117.967 1.00 65.07  ?  196 PHE   A CG  1 
ATOM   190  C CD1 . PHE   A 1 215 ? -8.089  53.375  116.660 1.00 63.01  ?  196 PHE   A CD1 1 
ATOM   191  C CD2 . PHE   A 1 215 ? -9.241  53.170  118.711 1.00 71.86  ?  196 PHE   A CD2 1 
ATOM   192  C CE1 . PHE   A 1 215 ? -9.189  54.009  116.111 1.00 68.72  ?  196 PHE   A CE1 1 
ATOM   193  C CE2 . PHE   A 1 215 ? -10.352 53.809  118.160 1.00 71.87  ?  196 PHE   A CE2 1 
ATOM   194  C CZ  . PHE   A 1 215 ? -10.323 54.228  116.865 1.00 68.25  ?  196 PHE   A CZ  1 
ATOM   195  N N   . PRO   A 1 216 ? -3.541  53.042  119.945 1.00 65.12  ?  197 PRO   A N   1 
ATOM   196  C CA  . PRO   A 1 216 ? -2.378  52.291  120.433 1.00 65.93  ?  197 PRO   A CA  1 
ATOM   197  C C   . PRO   A 1 216 ? -2.681  51.504  121.675 1.00 71.15  ?  197 PRO   A C   1 
ATOM   198  O O   . PRO   A 1 216 ? -1.933  50.572  121.993 1.00 77.22  ?  197 PRO   A O   1 
ATOM   199  C CB  . PRO   A 1 216 ? -1.338  53.385  120.714 1.00 69.19  ?  197 PRO   A CB  1 
ATOM   200  C CG  . PRO   A 1 216 ? -2.153  54.544  121.090 1.00 64.72  ?  197 PRO   A CG  1 
ATOM   201  C CD  . PRO   A 1 216 ? -3.385  54.486  120.192 1.00 66.23  ?  197 PRO   A CD  1 
ATOM   202  N N   . ASP   A 1 217 ? -3.746  51.856  122.403 1.00 71.06  ?  198 ASP   A N   1 
ATOM   203  C CA  . ASP   A 1 217 ? -4.150  51.047  123.551 1.00 73.90  ?  198 ASP   A CA  1 
ATOM   204  C C   . ASP   A 1 217 ? -4.612  49.657  123.110 1.00 74.30  ?  198 ASP   A C   1 
ATOM   205  O O   . ASP   A 1 217 ? -4.247  48.649  123.728 1.00 78.78  ?  198 ASP   A O   1 
ATOM   206  C CB  . ASP   A 1 217 ? -5.245  51.769  124.336 1.00 68.11  ?  198 ASP   A CB  1 
ATOM   207  C CG  . ASP   A 1 217 ? -6.362  52.277  123.442 1.00 71.58  ?  198 ASP   A CG  1 
ATOM   208  O OD1 . ASP   A 1 217 ? -6.589  51.663  122.396 1.00 80.15  ?  198 ASP   A OD1 1 
ATOM   209  O OD2 . ASP   A 1 217 ? -7.022  53.282  123.761 1.00 81.81  ?  198 ASP   A OD2 1 
ATOM   210  N N   . ILE   A 1 218 ? -5.372  49.586  122.018 1.00 69.78  ?  199 ILE   A N   1 
ATOM   211  C CA  . ILE   A 1 218 ? -6.017  48.347  121.604 1.00 68.49  ?  199 ILE   A CA  1 
ATOM   212  C C   . ILE   A 1 218 ? -5.030  47.402  120.922 1.00 76.79  ?  199 ILE   A C   1 
ATOM   213  O O   . ILE   A 1 218 ? -4.955  46.214  121.260 1.00 83.24  ?  199 ILE   A O   1 
ATOM   214  C CB  . ILE   A 1 218 ? -7.212  48.685  120.708 1.00 60.77  ?  199 ILE   A CB  1 
ATOM   215  C CG1 . ILE   A 1 218 ? -8.316  49.250  121.591 1.00 58.56  ?  199 ILE   A CG1 1 
ATOM   216  C CG2 . ILE   A 1 218 ? -7.643  47.468  119.905 1.00 65.29  ?  199 ILE   A CG2 1 
ATOM   217  C CD1 . ILE   A 1 218 ? -9.464  49.817  120.848 1.00 64.93  ?  199 ILE   A CD1 1 
ATOM   218  N N   . ILE   A 1 219 ? -4.252  47.905  119.958 1.00 79.61  ?  200 ILE   A N   1 
ATOM   219  C CA  . ILE   A 1 219 ? -3.267  47.057  119.289 1.00 76.99  ?  200 ILE   A CA  1 
ATOM   220  C C   . ILE   A 1 219 ? -2.218  46.515  120.256 1.00 76.78  ?  200 ILE   A C   1 
ATOM   221  O O   . ILE   A 1 219 ? -1.744  45.389  120.077 1.00 83.72  ?  200 ILE   A O   1 
ATOM   222  C CB  . ILE   A 1 219 ? -2.605  47.801  118.104 1.00 78.00  ?  200 ILE   A CB  1 
ATOM   223  C CG1 . ILE   A 1 219 ? -1.798  46.805  117.272 1.00 75.48  ?  200 ILE   A CG1 1 
ATOM   224  C CG2 . ILE   A 1 219 ? -1.788  49.021  118.536 1.00 69.12  ?  200 ILE   A CG2 1 
ATOM   225  C CD1 . ILE   A 1 219 ? -1.716  47.156  115.836 1.00 67.65  ?  200 ILE   A CD1 1 
ATOM   226  N N   . SER   A 1 220 ? -1.838  47.279  121.291 1.00 70.25  ?  201 SER   A N   1 
ATOM   227  C CA  . SER   A 1 220 ? -0.811  46.777  122.204 1.00 74.08  ?  201 SER   A CA  1 
ATOM   228  C C   . SER   A 1 220 ? -1.376  45.848  123.265 1.00 77.67  ?  201 SER   A C   1 
ATOM   229  O O   . SER   A 1 220 ? -0.599  45.259  124.028 1.00 77.20  ?  201 SER   A O   1 
ATOM   230  C CB  . SER   A 1 220 ? -0.074  47.929  122.899 1.00 79.25  ?  201 SER   A CB  1 
ATOM   231  O OG  . SER   A 1 220 ? -0.933  48.676  123.755 1.00 80.54  ?  201 SER   A OG  1 
ATOM   232  N N   . GLY   A 1 221 ? -2.699  45.714  123.321 1.00 78.20  ?  202 GLY   A N   1 
ATOM   233  C CA  . GLY   A 1 221 ? -3.365  45.010  124.382 1.00 84.99  ?  202 GLY   A CA  1 
ATOM   234  C C   . GLY   A 1 221 ? -3.814  43.617  123.996 1.00 90.87  ?  202 GLY   A C   1 
ATOM   235  O O   . GLY   A 1 221 ? -3.282  42.990  123.070 1.00 86.06  ?  202 GLY   A O   1 
ATOM   236  N N   . PRO   A 1 222 ? -4.801  43.108  124.735 1.00 96.18  ?  203 PRO   A N   1 
ATOM   237  C CA  . PRO   A 1 222 ? -5.274  41.727  124.534 1.00 96.69  ?  203 PRO   A CA  1 
ATOM   238  C C   . PRO   A 1 222 ? -5.896  41.482  123.160 1.00 95.98  ?  203 PRO   A C   1 
ATOM   239  O O   . PRO   A 1 222 ? -6.768  42.232  122.702 1.00 90.29  ?  203 PRO   A O   1 
ATOM   240  C CB  . PRO   A 1 222 ? -6.309  41.549  125.653 1.00 94.26  ?  203 PRO   A CB  1 
ATOM   241  C CG  . PRO   A 1 222 ? -6.565  42.940  126.221 1.00 87.91  ?  203 PRO   A CG  1 
ATOM   242  C CD  . PRO   A 1 222 ? -5.299  43.684  125.996 1.00 91.95  ?  203 PRO   A CD  1 
ATOM   243  N N   . GLN   A 1 223 ? -5.469  40.378  122.530 1.00 92.19  ?  204 GLN   A N   1 
ATOM   244  C CA  . GLN   A 1 223 ? -5.949  40.014  121.199 1.00 92.92  ?  204 GLN   A CA  1 
ATOM   245  C C   . GLN   A 1 223 ? -7.471  39.930  121.124 1.00 94.55  ?  204 GLN   A C   1 
ATOM   246  O O   . GLN   A 1 223 ? -8.044  40.036  120.031 1.00 90.77  ?  204 GLN   A O   1 
ATOM   247  C CB  . GLN   A 1 223 ? -5.337  38.676  120.773 1.00 97.75  ?  204 GLN   A CB  1 
ATOM   248  C CG  . GLN   A 1 223 ? -4.004  38.798  120.040 1.00 102.05 ?  204 GLN   A CG  1 
ATOM   249  C CD  . GLN   A 1 223 ? -4.172  38.946  118.533 1.00 108.47 ?  204 GLN   A CD  1 
ATOM   250  O OE1 . GLN   A 1 223 ? -5.292  39.058  118.025 1.00 104.60 ?  204 GLN   A OE1 1 
ATOM   251  N NE2 . GLN   A 1 223 ? -3.053  38.948  117.810 1.00 113.60 ?  204 GLN   A NE2 1 
ATOM   252  N N   . GLN   A 1 224 ? -8.146  39.743  122.256 1.00 100.27 ?  205 GLN   A N   1 
ATOM   253  C CA  . GLN   A 1 224 ? -9.601  39.667  122.214 1.00 100.38 ?  205 GLN   A CA  1 
ATOM   254  C C   . GLN   A 1 224 ? -10.205 41.030  121.909 1.00 93.48  ?  205 GLN   A C   1 
ATOM   255  O O   . GLN   A 1 224 ? -11.069 41.152  121.031 1.00 93.17  ?  205 GLN   A O   1 
ATOM   256  C CB  . GLN   A 1 224 ? -10.151 39.104  123.527 1.00 102.95 ?  205 GLN   A CB  1 
ATOM   257  C CG  . GLN   A 1 224 ? -11.665 39.285  123.677 1.00 106.57 ?  205 GLN   A CG  1 
ATOM   258  C CD  . GLN   A 1 224 ? -12.453 38.681  122.507 1.00 114.70 ?  205 GLN   A CD  1 
ATOM   259  O OE1 . GLN   A 1 224 ? -12.105 37.614  121.985 1.00 118.29 ?  205 GLN   A OE1 1 
ATOM   260  N NE2 . GLN   A 1 224 ? -13.520 39.367  122.092 1.00 107.68 ?  205 GLN   A NE2 1 
ATOM   261  N N   . THR   A 1 225 ? -9.756  42.071  122.617 1.00 91.93  ?  206 THR   A N   1 
ATOM   262  C CA  . THR   A 1 225 ? -10.284 43.410  122.361 1.00 96.75  ?  206 THR   A CA  1 
ATOM   263  C C   . THR   A 1 225 ? -10.027 43.830  120.919 1.00 89.56  ?  206 THR   A C   1 
ATOM   264  O O   . THR   A 1 225 ? -10.856 44.518  120.311 1.00 82.55  ?  206 THR   A O   1 
ATOM   265  C CB  . THR   A 1 225 ? -9.671  44.427  123.331 1.00 99.30  ?  206 THR   A CB  1 
ATOM   266  O OG1 . THR   A 1 225 ? -8.240  44.430  123.187 1.00 100.36 ?  206 THR   A OG1 1 
ATOM   267  C CG2 . THR   A 1 225 ? -10.036 44.070  124.780 1.00 91.65  ?  206 THR   A CG2 1 
ATOM   268  N N   . GLN   A 1 226 ? -8.887  43.404  120.351 1.00 88.60  ?  207 GLN   A N   1 
ATOM   269  C CA  . GLN   A 1 226 ? -8.595  43.685  118.947 1.00 84.68  ?  207 GLN   A CA  1 
ATOM   270  C C   . GLN   A 1 226 ? -9.706  43.175  118.033 1.00 85.70  ?  207 GLN   A C   1 
ATOM   271  O O   . GLN   A 1 226 ? -10.125 43.881  117.100 1.00 80.29  ?  207 GLN   A O   1 
ATOM   272  C CB  . GLN   A 1 226 ? -7.251  43.073  118.544 1.00 76.76  ?  207 GLN   A CB  1 
ATOM   273  C CG  . GLN   A 1 226 ? -6.067  43.509  119.389 1.00 79.57  ?  207 GLN   A CG  1 
ATOM   274  C CD  . GLN   A 1 226 ? -4.735  43.160  118.737 1.00 83.36  ?  207 GLN   A CD  1 
ATOM   275  O OE1 . GLN   A 1 226 ? -4.655  43.003  117.514 1.00 81.64  ?  207 GLN   A OE1 1 
ATOM   276  N NE2 . GLN   A 1 226 ? -3.683  43.039  119.550 1.00 74.27  ?  207 GLN   A NE2 1 
ATOM   277  N N   . LYS   A 1 227 ? -10.204 41.953  118.286 1.00 83.20  ?  208 LYS   A N   1 
ATOM   278  C CA  . LYS   A 1 227 ? -11.281 41.428  117.449 1.00 85.25  ?  208 LYS   A CA  1 
ATOM   279  C C   . LYS   A 1 227 ? -12.578 42.190  117.682 1.00 84.84  ?  208 LYS   A C   1 
ATOM   280  O O   . LYS   A 1 227 ? -13.415 42.307  116.770 1.00 80.13  ?  208 LYS   A O   1 
ATOM   281  C CB  . LYS   A 1 227 ? -11.490 39.933  117.702 1.00 91.42  ?  208 LYS   A CB  1 
ATOM   282  C CG  . LYS   A 1 227 ? -10.228 39.088  117.573 1.00 99.60  ?  208 LYS   A CG  1 
ATOM   283  C CD  . LYS   A 1 227 ? -10.536 37.581  117.462 1.00 96.50  ?  208 LYS   A CD  1 
ATOM   284  C CE  . LYS   A 1 227 ? -9.266  36.755  117.713 1.00 93.55  ?  208 LYS   A CE  1 
ATOM   285  N NZ  . LYS   A 1 227 ? -9.185  35.498  116.907 1.00 99.21  ?  208 LYS   A NZ  1 
ATOM   286  N N   . VAL   A 1 228 ? -12.756 42.715  118.894 1.00 83.01  ?  209 VAL   A N   1 
ATOM   287  C CA  . VAL   A 1 228 ? -13.938 43.514  119.189 1.00 86.76  ?  209 VAL   A CA  1 
ATOM   288  C C   . VAL   A 1 228 ? -13.923 44.773  118.334 1.00 87.54  ?  209 VAL   A C   1 
ATOM   289  O O   . VAL   A 1 228 ? -14.830 45.021  117.527 1.00 87.17  ?  209 VAL   A O   1 
ATOM   290  C CB  . VAL   A 1 228 ? -13.985 43.856  120.688 1.00 88.33  ?  209 VAL   A CB  1 
ATOM   291  C CG1 . VAL   A 1 228 ? -15.212 44.724  121.014 1.00 77.58  ?  209 VAL   A CG1 1 
ATOM   292  C CG2 . VAL   A 1 228 ? -13.896 42.583  121.532 1.00 85.98  ?  209 VAL   A CG2 1 
ATOM   293  N N   . PHE   A 1 229 ? -12.874 45.582  118.507 1.00 84.23  ?  210 PHE   A N   1 
ATOM   294  C CA  . PHE   A 1 229 ? -12.607 46.737  117.663 1.00 79.62  ?  210 PHE   A CA  1 
ATOM   295  C C   . PHE   A 1 229 ? -12.838 46.425  116.193 1.00 80.59  ?  210 PHE   A C   1 
ATOM   296  O O   . PHE   A 1 229 ? -13.606 47.114  115.505 1.00 73.57  ?  210 PHE   A O   1 
ATOM   297  C CB  . PHE   A 1 229 ? -11.159 47.188  117.881 1.00 78.44  ?  210 PHE   A CB  1 
ATOM   298  C CG  . PHE   A 1 229 ? -10.699 48.207  116.889 1.00 80.12  ?  210 PHE   A CG  1 
ATOM   299  C CD1 . PHE   A 1 229 ? -10.803 49.553  117.174 1.00 79.47  ?  210 PHE   A CD1 1 
ATOM   300  C CD2 . PHE   A 1 229 ? -10.192 47.827  115.659 1.00 82.87  ?  210 PHE   A CD2 1 
ATOM   301  C CE1 . PHE   A 1 229 ? -10.403 50.502  116.257 1.00 77.66  ?  210 PHE   A CE1 1 
ATOM   302  C CE2 . PHE   A 1 229 ? -9.797  48.768  114.736 1.00 80.61  ?  210 PHE   A CE2 1 
ATOM   303  C CZ  . PHE   A 1 229 ? -9.900  50.109  115.040 1.00 75.93  ?  210 PHE   A CZ  1 
ATOM   304  N N   . LEU   A 1 230 ? -12.137 45.389  115.702 1.00 78.01  ?  211 LEU   A N   1 
ATOM   305  C CA  . LEU   A 1 230 ? -12.174 45.072  114.278 1.00 76.86  ?  211 LEU   A CA  1 
ATOM   306  C C   . LEU   A 1 230 ? -13.596 44.839  113.815 1.00 77.74  ?  211 LEU   A C   1 
ATOM   307  O O   . LEU   A 1 230 ? -14.003 45.351  112.761 1.00 77.66  ?  211 LEU   A O   1 
ATOM   308  C CB  . LEU   A 1 230 ? -11.306 43.855  113.966 1.00 70.10  ?  211 LEU   A CB  1 
ATOM   309  C CG  . LEU   A 1 230 ? -9.793  44.049  113.925 1.00 70.59  ?  211 LEU   A CG  1 
ATOM   310  C CD1 . LEU   A 1 230 ? -9.048  42.756  114.032 1.00 70.74  ?  211 LEU   A CD1 1 
ATOM   311  C CD2 . LEU   A 1 230 ? -9.425  44.698  112.649 1.00 71.72  ?  211 LEU   A CD2 1 
ATOM   312  N N   . PHE   A 1 231 ? -14.382 44.098  114.606 1.00 81.52  ?  212 PHE   A N   1 
ATOM   313  C CA  . PHE   A 1 231 ? -15.783 43.912  114.248 1.00 86.89  ?  212 PHE   A CA  1 
ATOM   314  C C   . PHE   A 1 231 ? -16.531 45.240  114.273 1.00 84.42  ?  212 PHE   A C   1 
ATOM   315  O O   . PHE   A 1 231 ? -17.365 45.517  113.394 1.00 78.81  ?  212 PHE   A O   1 
ATOM   316  C CB  . PHE   A 1 231 ? -16.473 42.906  115.176 1.00 84.93  ?  212 PHE   A CB  1 
ATOM   317  C CG  . PHE   A 1 231 ? -17.943 42.773  114.879 1.00 91.40  ?  212 PHE   A CG  1 
ATOM   318  C CD1 . PHE   A 1 231 ? -18.378 42.019  113.799 1.00 97.28  ?  212 PHE   A CD1 1 
ATOM   319  C CD2 . PHE   A 1 231 ? -18.884 43.478  115.612 1.00 95.45  ?  212 PHE   A CD2 1 
ATOM   320  C CE1 . PHE   A 1 231 ? -19.728 41.929  113.485 1.00 95.23  ?  212 PHE   A CE1 1 
ATOM   321  C CE2 . PHE   A 1 231 ? -20.238 43.394  115.301 1.00 100.79 ?  212 PHE   A CE2 1 
ATOM   322  C CZ  . PHE   A 1 231 ? -20.657 42.616  114.237 1.00 97.64  ?  212 PHE   A CZ  1 
ATOM   323  N N   . ILE   A 1 232 ? -16.257 46.066  115.287 1.00 80.41  ?  213 ILE   A N   1 
ATOM   324  C CA  . ILE   A 1 232 ? -16.919 47.356  115.383 1.00 78.71  ?  213 ILE   A CA  1 
ATOM   325  C C   . ILE   A 1 232 ? -16.629 48.178  114.137 1.00 77.82  ?  213 ILE   A C   1 
ATOM   326  O O   . ILE   A 1 232 ? -17.546 48.715  113.503 1.00 73.28  ?  213 ILE   A O   1 
ATOM   327  C CB  . ILE   A 1 232 ? -16.491 48.071  116.674 1.00 84.70  ?  213 ILE   A CB  1 
ATOM   328  C CG1 . ILE   A 1 232 ? -16.872 47.212  117.879 1.00 80.79  ?  213 ILE   A CG1 1 
ATOM   329  C CG2 . ILE   A 1 232 ? -17.130 49.455  116.768 1.00 78.90  ?  213 ILE   A CG2 1 
ATOM   330  C CD1 . ILE   A 1 232 ? -16.096 47.532  119.118 1.00 81.25  ?  213 ILE   A CD1 1 
ATOM   331  N N   . ARG   A 1 233 ? -15.353 48.235  113.734 1.00 79.13  ?  214 ARG   A N   1 
ATOM   332  C CA  . ARG   A 1 233 ? -14.992 48.921  112.496 1.00 77.10  ?  214 ARG   A CA  1 
ATOM   333  C C   . ARG   A 1 233 ? -15.793 48.368  111.330 1.00 80.34  ?  214 ARG   A C   1 
ATOM   334  O O   . ARG   A 1 233 ? -16.470 49.116  110.605 1.00 75.79  ?  214 ARG   A O   1 
ATOM   335  C CB  . ARG   A 1 233 ? -13.489 48.793  112.193 1.00 76.83  ?  214 ARG   A CB  1 
ATOM   336  C CG  . ARG   A 1 233 ? -13.249 48.810  110.663 1.00 75.77  ?  214 ARG   A CG  1 
ATOM   337  C CD  . ARG   A 1 233 ? -11.888 49.220  110.113 1.00 74.10  ?  214 ARG   A CD  1 
ATOM   338  N NE  . ARG   A 1 233 ? -10.702 48.418  110.442 1.00 69.60  ?  214 ARG   A NE  1 
ATOM   339  C CZ  . ARG   A 1 233 ? -10.443 47.212  109.951 1.00 71.07  ?  214 ARG   A CZ  1 
ATOM   340  N NH1 . ARG   A 1 233 ? -11.319 46.608  109.168 1.00 76.28  ?  214 ARG   A NH1 1 
ATOM   341  N NH2 . ARG   A 1 233 ? -9.318  46.593  110.261 1.00 73.28  ?  214 ARG   A NH2 1 
ATOM   342  N N   . ASN   A 1 234 ? -15.727 47.038  111.150 1.00 80.52  ?  215 ASN   A N   1 
ATOM   343  C CA  . ASN   A 1 234 ? -16.269 46.414  109.947 1.00 77.86  ?  215 ASN   A CA  1 
ATOM   344  C C   . ASN   A 1 234 ? -17.773 46.631  109.855 1.00 80.94  ?  215 ASN   A C   1 
ATOM   345  O O   . ASN   A 1 234 ? -18.303 46.934  108.774 1.00 74.62  ?  215 ASN   A O   1 
ATOM   346  C CB  . ASN   A 1 234 ? -15.918 44.928  109.938 1.00 77.91  ?  215 ASN   A CB  1 
ATOM   347  C CG  . ASN   A 1 234 ? -14.423 44.689  109.833 1.00 82.11  ?  215 ASN   A CG  1 
ATOM   348  O OD1 . ASN   A 1 234 ? -13.685 45.590  109.446 1.00 82.77  ?  215 ASN   A OD1 1 
ATOM   349  N ND2 . ASN   A 1 234 ? -13.966 43.479  110.178 1.00 78.76  ?  215 ASN   A ND2 1 
ATOM   350  N N   . ARG   A 1 235 ? -18.471 46.535  110.997 1.00 82.67  ?  216 ARG   A N   1 
ATOM   351  C CA  . ARG   A 1 235 ? -19.923 46.652  111.003 1.00 82.21  ?  216 ARG   A CA  1 
ATOM   352  C C   . ARG   A 1 235 ? -20.382 48.091  110.813 1.00 79.44  ?  216 ARG   A C   1 
ATOM   353  O O   . ARG   A 1 235 ? -21.460 48.324  110.245 1.00 78.08  ?  216 ARG   A O   1 
ATOM   354  C CB  . ARG   A 1 235 ? -20.481 46.050  112.298 1.00 85.14  ?  216 ARG   A CB  1 
ATOM   355  C CG  . ARG   A 1 235 ? -22.004 46.127  112.428 1.00 93.12  ?  216 ARG   A CG  1 
ATOM   356  C CD  . ARG   A 1 235 ? -22.753 45.493  111.254 1.00 88.76  ?  216 ARG   A CD  1 
ATOM   357  N NE  . ARG   A 1 235 ? -24.201 45.641  111.420 1.00 96.27  ?  216 ARG   A NE  1 
ATOM   358  C CZ  . ARG   A 1 235 ? -25.085 45.602  110.422 1.00 100.33 ?  216 ARG   A CZ  1 
ATOM   359  N NH1 . ARG   A 1 235 ? -24.683 45.440  109.168 1.00 94.58  ?  216 ARG   A NH1 1 
ATOM   360  N NH2 . ARG   A 1 235 ? -26.378 45.755  110.675 1.00 103.33 ?  216 ARG   A NH2 1 
ATOM   361  N N   . THR   A 1 236 ? -19.576 49.063  111.238 1.00 80.52  ?  217 THR   A N   1 
ATOM   362  C CA  . THR   A 1 236 ? -19.880 50.453  110.917 1.00 80.70  ?  217 THR   A CA  1 
ATOM   363  C C   . THR   A 1 236 ? -19.661 50.734  109.438 1.00 81.35  ?  217 THR   A C   1 
ATOM   364  O O   . THR   A 1 236 ? -20.497 51.375  108.780 1.00 75.87  ?  217 THR   A O   1 
ATOM   365  C CB  . THR   A 1 236 ? -19.018 51.376  111.754 1.00 77.51  ?  217 THR   A CB  1 
ATOM   366  O OG1 . THR   A 1 236 ? -19.029 50.915  113.107 1.00 82.90  ?  217 THR   A OG1 1 
ATOM   367  C CG2 . THR   A 1 236 ? -19.546 52.780  111.668 1.00 77.76  ?  217 THR   A CG2 1 
ATOM   368  N N   . LEU   A 1 237 ? -18.521 50.281  108.909 1.00 78.13  ?  218 LEU   A N   1 
ATOM   369  C CA  . LEU   A 1 237 ? -18.296 50.381  107.478 1.00 76.48  ?  218 LEU   A CA  1 
ATOM   370  C C   . LEU   A 1 237 ? -19.467 49.798  106.715 1.00 81.13  ?  218 LEU   A C   1 
ATOM   371  O O   . LEU   A 1 237 ? -19.954 50.405  105.751 1.00 77.76  ?  218 LEU   A O   1 
ATOM   372  C CB  . LEU   A 1 237 ? -17.006 49.670  107.098 1.00 71.47  ?  218 LEU   A CB  1 
ATOM   373  C CG  . LEU   A 1 237 ? -15.744 50.309  107.632 1.00 75.39  ?  218 LEU   A CG  1 
ATOM   374  C CD1 . LEU   A 1 237 ? -14.582 49.359  107.468 1.00 72.87  ?  218 LEU   A CD1 1 
ATOM   375  C CD2 . LEU   A 1 237 ? -15.501 51.629  106.899 1.00 72.53  ?  218 LEU   A CD2 1 
ATOM   376  N N   . GLN   A 1 238 ? -19.945 48.623  107.153 1.00 82.04  ?  219 GLN   A N   1 
ATOM   377  C CA  . GLN   A 1 238 ? -21.080 47.990  106.494 1.00 80.62  ?  219 GLN   A CA  1 
ATOM   378  C C   . GLN   A 1 238 ? -22.258 48.943  106.451 1.00 83.84  ?  219 GLN   A C   1 
ATOM   379  O O   . GLN   A 1 238 ? -22.723 49.322  105.369 1.00 86.63  ?  219 GLN   A O   1 
ATOM   380  C CB  . GLN   A 1 238 ? -21.446 46.690  107.207 1.00 85.54  ?  219 GLN   A CB  1 
ATOM   381  C CG  . GLN   A 1 238 ? -22.589 45.891  106.562 1.00 92.14  ?  219 GLN   A CG  1 
ATOM   382  C CD  . GLN   A 1 238 ? -22.659 44.437  107.049 1.00 100.99 ?  219 GLN   A CD  1 
ATOM   383  O OE1 . GLN   A 1 238 ? -21.913 44.029  107.950 1.00 96.27  ?  219 GLN   A OE1 1 
ATOM   384  N NE2 . GLN   A 1 238 ? -23.533 43.643  106.425 1.00 101.41 ?  219 GLN   A NE2 1 
ATOM   385  N N   . LEU   A 1 239 ? -22.687 49.420  107.622 1.00 83.13  ?  220 LEU   A N   1 
ATOM   386  C CA  . LEU   A 1 239 ? -23.829 50.325  107.687 1.00 86.68  ?  220 LEU   A CA  1 
ATOM   387  C C   . LEU   A 1 239 ? -23.724 51.452  106.664 1.00 88.21  ?  220 LEU   A C   1 
ATOM   388  O O   . LEU   A 1 239 ? -24.630 51.641  105.838 1.00 86.66  ?  220 LEU   A O   1 
ATOM   389  C CB  . LEU   A 1 239 ? -23.959 50.878  109.096 1.00 83.97  ?  220 LEU   A CB  1 
ATOM   390  C CG  . LEU   A 1 239 ? -24.532 49.743  109.933 1.00 86.59  ?  220 LEU   A CG  1 
ATOM   391  C CD1 . LEU   A 1 239 ? -24.142 49.865  111.388 1.00 90.19  ?  220 LEU   A CD1 1 
ATOM   392  C CD2 . LEU   A 1 239 ? -26.041 49.649  109.732 1.00 94.03  ?  220 LEU   A CD2 1 
ATOM   393  N N   . TRP   A 1 240 ? -22.606 52.190  106.684 1.00 80.89  ?  221 TRP   A N   1 
ATOM   394  C CA  . TRP   A 1 240 ? -22.410 53.254  105.705 1.00 82.43  ?  221 TRP   A CA  1 
ATOM   395  C C   . TRP   A 1 240 ? -22.554 52.723  104.281 1.00 84.52  ?  221 TRP   A C   1 
ATOM   396  O O   . TRP   A 1 240 ? -23.253 53.314  103.447 1.00 81.48  ?  221 TRP   A O   1 
ATOM   397  C CB  . TRP   A 1 240 ? -21.037 53.909  105.900 1.00 79.59  ?  221 TRP   A CB  1 
ATOM   398  C CG  . TRP   A 1 240 ? -20.596 54.738  104.702 1.00 82.18  ?  221 TRP   A CG  1 
ATOM   399  C CD1 . TRP   A 1 240 ? -19.540 54.484  103.869 1.00 79.69  ?  221 TRP   A CD1 1 
ATOM   400  C CD2 . TRP   A 1 240 ? -21.221 55.926  104.195 1.00 79.80  ?  221 TRP   A CD2 1 
ATOM   401  N NE1 . TRP   A 1 240 ? -19.471 55.437  102.884 1.00 73.51  ?  221 TRP   A NE1 1 
ATOM   402  C CE2 . TRP   A 1 240 ? -20.487 56.335  103.062 1.00 76.41  ?  221 TRP   A CE2 1 
ATOM   403  C CE3 . TRP   A 1 240 ? -22.323 56.683  104.591 1.00 80.94  ?  221 TRP   A CE3 1 
ATOM   404  C CZ2 . TRP   A 1 240 ? -20.814 57.472  102.329 1.00 79.58  ?  221 TRP   A CZ2 1 
ATOM   405  C CZ3 . TRP   A 1 240 ? -22.650 57.808  103.857 1.00 84.74  ?  221 TRP   A CZ3 1 
ATOM   406  C CH2 . TRP   A 1 240 ? -21.897 58.192  102.737 1.00 83.52  ?  221 TRP   A CH2 1 
ATOM   407  N N   . LEU   A 1 241 ? -21.922 51.580  103.998 1.00 83.32  ?  222 LEU   A N   1 
ATOM   408  C CA  . LEU   A 1 241 ? -21.829 51.105  102.620 1.00 83.27  ?  222 LEU   A CA  1 
ATOM   409  C C   . LEU   A 1 241 ? -23.182 50.656  102.080 1.00 90.81  ?  222 LEU   A C   1 
ATOM   410  O O   . LEU   A 1 241 ? -23.519 50.942  100.919 1.00 84.86  ?  222 LEU   A O   1 
ATOM   411  C CB  . LEU   A 1 241 ? -20.805 49.983  102.538 1.00 73.55  ?  222 LEU   A CB  1 
ATOM   412  C CG  . LEU   A 1 241 ? -19.374 50.504  102.455 1.00 77.51  ?  222 LEU   A CG  1 
ATOM   413  C CD1 . LEU   A 1 241 ? -18.354 49.371  102.546 1.00 76.27  ?  222 LEU   A CD1 1 
ATOM   414  C CD2 . LEU   A 1 241 ? -19.200 51.303  101.164 1.00 72.52  ?  222 LEU   A CD2 1 
ATOM   415  N N   . ASP   A 1 242 ? -23.972 49.956  102.905 1.00 96.04  ?  223 ASP   A N   1 
ATOM   416  C CA  . ASP   A 1 242 ? -25.279 49.472  102.462 1.00 100.91 ?  223 ASP   A CA  1 
ATOM   417  C C   . ASP   A 1 242 ? -26.269 50.602  102.241 1.00 100.60 ?  223 ASP   A C   1 
ATOM   418  O O   . ASP   A 1 242 ? -27.309 50.382  101.610 1.00 107.61 ?  223 ASP   A O   1 
ATOM   419  C CB  . ASP   A 1 242 ? -25.845 48.447  103.452 1.00 101.46 ?  223 ASP   A CB  1 
ATOM   420  C CG  . ASP   A 1 242 ? -24.920 47.231  103.637 1.00 111.82 ?  223 ASP   A CG  1 
ATOM   421  O OD1 . ASP   A 1 242 ? -25.285 46.117  103.187 1.00 118.11 ?  223 ASP   A OD1 1 
ATOM   422  O OD2 . ASP   A 1 242 ? -23.816 47.376  104.199 1.00 106.30 ?  223 ASP   A OD2 1 
ATOM   423  N N   . ASN   A 1 243 ? -25.967 51.795  102.724 1.00 96.19  ?  224 ASN   A N   1 
ATOM   424  C CA  . ASN   A 1 243 ? -26.742 52.950  102.316 1.00 96.02  ?  224 ASN   A CA  1 
ATOM   425  C C   . ASN   A 1 243 ? -25.888 54.201  102.476 1.00 96.57  ?  224 ASN   A C   1 
ATOM   426  O O   . ASN   A 1 243 ? -25.722 54.709  103.593 1.00 95.57  ?  224 ASN   A O   1 
ATOM   427  C CB  . ASN   A 1 243 ? -28.035 53.047  103.121 1.00 95.30  ?  224 ASN   A CB  1 
ATOM   428  C CG  . ASN   A 1 243 ? -28.865 54.247  102.729 1.00 106.39 ?  224 ASN   A CG  1 
ATOM   429  O OD1 . ASN   A 1 243 ? -28.794 54.732  101.585 1.00 105.00 ?  224 ASN   A OD1 1 
ATOM   430  N ND2 . ASN   A 1 243 ? -29.664 54.738  103.674 1.00 107.12 ?  224 ASN   A ND2 1 
ATOM   431  N N   . PRO   A 1 244 ? -25.318 54.715  101.395 1.00 95.70  ?  225 PRO   A N   1 
ATOM   432  C CA  . PRO   A 1 244 ? -24.413 55.850  101.526 1.00 86.89  ?  225 PRO   A CA  1 
ATOM   433  C C   . PRO   A 1 244 ? -25.042 57.126  101.020 1.00 91.97  ?  225 PRO   A C   1 
ATOM   434  O O   . PRO   A 1 244 ? -24.317 58.058  100.656 1.00 94.80  ?  225 PRO   A O   1 
ATOM   435  C CB  . PRO   A 1 244 ? -23.230 55.442  100.645 1.00 84.89  ?  225 PRO   A CB  1 
ATOM   436  C CG  . PRO   A 1 244 ? -23.828 54.395  99.656  1.00 87.99  ?  225 PRO   A CG  1 
ATOM   437  C CD  . PRO   A 1 244 ? -25.277 54.192  100.023 1.00 93.88  ?  225 PRO   A CD  1 
ATOM   438  N N   . LYS   A 1 245 ? -26.370 57.188  100.946 1.00 92.80  ?  226 LYS   A N   1 
ATOM   439  C CA  . LYS   A 1 245 ? -27.001 58.445  100.562 1.00 93.25  ?  226 LYS   A CA  1 
ATOM   440  C C   . LYS   A 1 245 ? -27.413 59.292  101.765 1.00 95.14  ?  226 LYS   A C   1 
ATOM   441  O O   . LYS   A 1 245 ? -27.904 60.412  101.575 1.00 92.36  ?  226 LYS   A O   1 
ATOM   442  C CB  . LYS   A 1 245 ? -28.212 58.194  99.655  1.00 90.51  ?  226 LYS   A CB  1 
ATOM   443  C CG  . LYS   A 1 245 ? -27.862 57.859  98.208  1.00 91.40  ?  226 LYS   A CG  1 
ATOM   444  C CD  . LYS   A 1 245 ? -29.078 57.945  97.269  1.00 89.98  ?  226 LYS   A CD  1 
ATOM   445  C CE  . LYS   A 1 245 ? -30.274 57.124  97.784  1.00 104.08 ?  226 LYS   A CE  1 
ATOM   446  N NZ  . LYS   A 1 245 ? -29.969 55.685  98.153  1.00 104.65 ?  226 LYS   A NZ  1 
ATOM   447  N N   . ILE   A 1 246 ? -27.213 58.801  102.993 1.00 93.12  ?  227 ILE   A N   1 
ATOM   448  C CA  . ILE   A 1 246 ? -27.544 59.554  104.202 1.00 94.70  ?  227 ILE   A CA  1 
ATOM   449  C C   . ILE   A 1 246 ? -26.451 59.362  105.248 1.00 92.61  ?  227 ILE   A C   1 
ATOM   450  O O   . ILE   A 1 246 ? -25.895 58.267  105.393 1.00 90.52  ?  227 ILE   A O   1 
ATOM   451  C CB  . ILE   A 1 246 ? -28.912 59.145  104.789 1.00 95.28  ?  227 ILE   A CB  1 
ATOM   452  C CG1 . ILE   A 1 246 ? -28.935 57.642  105.105 1.00 95.47  ?  227 ILE   A CG1 1 
ATOM   453  C CG2 . ILE   A 1 246 ? -30.048 59.593  103.865 1.00 92.18  ?  227 ILE   A CG2 1 
ATOM   454  C CD1 . ILE   A 1 246 ? -30.206 57.170  105.767 1.00 98.95  ?  227 ILE   A CD1 1 
ATOM   455  N N   . GLN   A 1 247 ? -26.173 60.434  105.994 1.00 86.69  ?  228 GLN   A N   1 
ATOM   456  C CA  . GLN   A 1 247 ? -25.130 60.416  107.006 1.00 84.93  ?  228 GLN   A CA  1 
ATOM   457  C C   . GLN   A 1 247 ? -25.341 59.273  107.990 1.00 83.37  ?  228 GLN   A C   1 
ATOM   458  O O   . GLN   A 1 247 ? -26.472 58.909  108.312 1.00 87.15  ?  228 GLN   A O   1 
ATOM   459  C CB  . GLN   A 1 247 ? -25.110 61.755  107.741 1.00 90.02  ?  228 GLN   A CB  1 
ATOM   460  C CG  . GLN   A 1 247 ? -24.239 61.776  108.991 1.00 93.85  ?  228 GLN   A CG  1 
ATOM   461  C CD  . GLN   A 1 247 ? -24.054 63.168  109.559 1.00 89.86  ?  228 GLN   A CD  1 
ATOM   462  O OE1 . GLN   A 1 247 ? -24.941 64.022  109.463 1.00 88.09  ?  228 GLN   A OE1 1 
ATOM   463  N NE2 . GLN   A 1 247 ? -22.888 63.404  110.151 1.00 91.43  ?  228 GLN   A NE2 1 
ATOM   464  N N   . LEU   A 1 248 ? -24.242 58.694  108.453 1.00 76.91  ?  229 LEU   A N   1 
ATOM   465  C CA  . LEU   A 1 248 ? -24.290 57.624  109.439 1.00 83.50  ?  229 LEU   A CA  1 
ATOM   466  C C   . LEU   A 1 248 ? -23.854 58.202  110.780 1.00 89.64  ?  229 LEU   A C   1 
ATOM   467  O O   . LEU   A 1 248 ? -22.664 58.269  111.095 1.00 86.60  ?  229 LEU   A O   1 
ATOM   468  C CB  . LEU   A 1 248 ? -23.416 56.452  109.028 1.00 80.70  ?  229 LEU   A CB  1 
ATOM   469  C CG  . LEU   A 1 248 ? -23.481 55.340  110.075 1.00 82.32  ?  229 LEU   A CG  1 
ATOM   470  C CD1 . LEU   A 1 248 ? -24.643 54.417  109.788 1.00 86.00  ?  229 LEU   A CD1 1 
ATOM   471  C CD2 . LEU   A 1 248 ? -22.173 54.573  110.167 1.00 78.13  ?  229 LEU   A CD2 1 
ATOM   472  N N   . THR   A 1 249 ? -24.835 58.606  111.581 1.00 93.73  ?  230 THR   A N   1 
ATOM   473  C CA  . THR   A 1 249 ? -24.573 59.170  112.893 1.00 88.92  ?  230 THR   A CA  1 
ATOM   474  C C   . THR   A 1 249 ? -24.179 58.075  113.873 1.00 90.06  ?  230 THR   A C   1 
ATOM   475  O O   . THR   A 1 249 ? -24.442 56.888  113.663 1.00 92.19  ?  230 THR   A O   1 
ATOM   476  C CB  . THR   A 1 249 ? -25.795 59.916  113.398 1.00 91.94  ?  230 THR   A CB  1 
ATOM   477  O OG1 . THR   A 1 249 ? -26.876 58.987  113.586 1.00 93.04  ?  230 THR   A OG1 1 
ATOM   478  C CG2 . THR   A 1 249 ? -26.187 60.987  112.384 1.00 92.22  ?  230 THR   A CG2 1 
ATOM   479  N N   . PHE   A 1 250 ? -23.545 58.499  114.966 1.00 86.00  ?  231 PHE   A N   1 
ATOM   480  C CA  . PHE   A 1 250 ? -22.971 57.559  115.929 1.00 90.40  ?  231 PHE   A CA  1 
ATOM   481  C C   . PHE   A 1 250 ? -24.060 56.785  116.664 1.00 96.84  ?  231 PHE   A C   1 
ATOM   482  O O   . PHE   A 1 250 ? -24.024 55.547  116.745 1.00 96.18  ?  231 PHE   A O   1 
ATOM   483  C CB  . PHE   A 1 250 ? -22.093 58.335  116.910 1.00 84.70  ?  231 PHE   A CB  1 
ATOM   484  C CG  . PHE   A 1 250 ? -21.883 57.657  118.224 1.00 87.49  ?  231 PHE   A CG  1 
ATOM   485  C CD1 . PHE   A 1 250 ? -21.197 56.451  118.309 1.00 90.34  ?  231 PHE   A CD1 1 
ATOM   486  C CD2 . PHE   A 1 250 ? -22.324 58.251  119.388 1.00 89.86  ?  231 PHE   A CD2 1 
ATOM   487  C CE1 . PHE   A 1 250 ? -20.984 55.838  119.543 1.00 92.84  ?  231 PHE   A CE1 1 
ATOM   488  C CE2 . PHE   A 1 250 ? -22.109 57.648  120.620 1.00 85.20  ?  231 PHE   A CE2 1 
ATOM   489  C CZ  . PHE   A 1 250 ? -21.439 56.443  120.701 1.00 86.16  ?  231 PHE   A CZ  1 
ATOM   490  N N   . GLU   A 1 251 ? -25.080 57.530  117.073 1.00 102.74 ?  232 GLU   A N   1 
ATOM   491  C CA  . GLU   A 1 251 ? -26.257 56.951  117.754 1.00 100.17 ?  232 GLU   A CA  1 
ATOM   492  C C   . GLU   A 1 251 ? -26.819 55.883  116.837 1.00 102.47 ?  232 GLU   A C   1 
ATOM   493  O O   . GLU   A 1 251 ? -26.907 54.732  117.260 1.00 105.03 ?  232 GLU   A O   1 
ATOM   494  C CB  . GLU   A 1 251 ? -27.329 58.015  117.924 1.00 102.75 ?  232 GLU   A CB  1 
ATOM   495  C CG  . GLU   A 1 251 ? -26.830 59.228  118.663 1.00 107.65 ?  232 GLU   A CG  1 
ATOM   496  C CD  . GLU   A 1 251 ? -25.863 60.028  117.825 1.00 111.43 ?  232 GLU   A CD  1 
ATOM   497  O OE1 . GLU   A 1 251 ? -25.374 61.051  118.304 1.00 121.22 ?  232 GLU   A OE1 1 
ATOM   498  O OE2 . GLU   A 1 251 ? -25.605 59.604  116.702 1.00 110.97 ?  232 GLU   A OE2 1 
ATOM   499  N N   . ALA   A 1 252 ? -26.979 56.227  115.566 1.00 96.06  ?  233 ALA   A N   1 
ATOM   500  C CA  . ALA   A 1 252 ? -27.532 55.265  114.596 1.00 99.34  ?  233 ALA   A CA  1 
ATOM   501  C C   . ALA   A 1 252 ? -26.617 54.051  114.523 1.00 98.18  ?  233 ALA   A C   1 
ATOM   502  O O   . ALA   A 1 252 ? -27.116 52.952  114.509 1.00 102.04 ?  233 ALA   A O   1 
ATOM   503  C CB  . ALA   A 1 252 ? -27.671 55.924  113.260 1.00 98.26  ?  233 ALA   A CB  1 
ATOM   504  N N   . THR   A 1 253 ? -25.309 54.250  114.516 1.00 96.19  ?  234 THR   A N   1 
ATOM   505  C CA  . THR   A 1 253 ? -24.406 53.085  114.500 1.00 98.47  ?  234 THR   A CA  1 
ATOM   506  C C   . THR   A 1 253 ? -24.629 52.288  115.779 1.00 100.10 ?  234 THR   A C   1 
ATOM   507  O O   . THR   A 1 253 ? -24.760 51.080  115.702 1.00 101.51 ?  234 THR   A O   1 
ATOM   508  C CB  . THR   A 1 253 ? -22.954 53.560  114.468 1.00 91.72  ?  234 THR   A CB  1 
ATOM   509  O OG1 . THR   A 1 253 ? -22.906 54.591  113.492 1.00 89.78  ?  234 THR   A OG1 1 
ATOM   510  C CG2 . THR   A 1 253 ? -21.972 52.479  114.104 1.00 90.76  ?  234 THR   A CG2 1 
ATOM   511  N N   . LEU   A 1 254 ? -24.737 52.963  116.913 1.00 102.93 ?  235 LEU   A N   1 
ATOM   512  C CA  . LEU   A 1 254 ? -24.882 52.212  118.178 1.00 105.96 ?  235 LEU   A CA  1 
ATOM   513  C C   . LEU   A 1 254 ? -26.171 51.401  118.187 1.00 105.29 ?  235 LEU   A C   1 
ATOM   514  O O   . LEU   A 1 254 ? -26.142 50.289  118.689 1.00 104.10 ?  235 LEU   A O   1 
ATOM   515  C CB  . LEU   A 1 254 ? -24.834 53.168  119.365 1.00 99.38  ?  235 LEU   A CB  1 
ATOM   516  C CG  . LEU   A 1 254 ? -24.526 52.455  120.671 1.00 96.49  ?  235 LEU   A CG  1 
ATOM   517  C CD1 . LEU   A 1 254 ? -23.929 51.101  120.374 1.00 98.52  ?  235 LEU   A CD1 1 
ATOM   518  C CD2 . LEU   A 1 254 ? -23.583 53.259  121.528 1.00 91.08  ?  235 LEU   A CD2 1 
ATOM   519  N N   . GLN   A 1 255 ? -27.256 51.943  117.655 1.00 102.79 ?  236 GLN   A N   1 
ATOM   520  C CA  . GLN   A 1 255 ? -28.513 51.175  117.735 1.00 104.91 ?  236 GLN   A CA  1 
ATOM   521  C C   . GLN   A 1 255 ? -28.369 49.850  117.001 1.00 109.66 ?  236 GLN   A C   1 
ATOM   522  O O   . GLN   A 1 255 ? -28.583 48.825  117.632 1.00 111.03 ?  236 GLN   A O   1 
ATOM   523  C CB  . GLN   A 1 255 ? -29.639 51.982  117.109 1.00 102.55 ?  236 GLN   A CB  1 
ATOM   524  C CG  . GLN   A 1 255 ? -30.123 53.105  118.006 1.00 113.78 ?  236 GLN   A CG  1 
ATOM   525  C CD  . GLN   A 1 255 ? -30.137 52.700  119.460 1.00 124.81 ?  236 GLN   A CD  1 
ATOM   526  O OE1 . GLN   A 1 255 ? -30.215 51.523  119.800 1.00 123.61 ?  236 GLN   A OE1 1 
ATOM   527  N NE2 . GLN   A 1 255 ? -30.069 53.684  120.341 1.00 122.74 ?  236 GLN   A NE2 1 
ATOM   528  N N   . GLN   A 1 256 ? -27.843 49.860  115.781 1.00 107.44 ?  237 GLN   A N   1 
ATOM   529  C CA  . GLN   A 1 256 ? -27.712 48.609  114.992 1.00 106.43 ?  237 GLN   A CA  1 
ATOM   530  C C   . GLN   A 1 256 ? -26.667 47.686  115.604 1.00 106.66 ?  237 GLN   A C   1 
ATOM   531  O O   . GLN   A 1 256 ? -26.747 46.495  115.382 1.00 114.08 ?  237 GLN   A O   1 
ATOM   532  C CB  . GLN   A 1 256 ? -27.496 48.881  113.514 1.00 102.07 ?  237 GLN   A CB  1 
ATOM   533  C CG  . GLN   A 1 256 ? -28.770 48.794  112.706 1.00 110.12 ?  237 GLN   A CG  1 
ATOM   534  C CD  . GLN   A 1 256 ? -29.027 50.122  112.048 1.00 117.72 ?  237 GLN   A CD  1 
ATOM   535  O OE1 . GLN   A 1 256 ? -28.576 51.154  112.524 1.00 105.95 ?  237 GLN   A OE1 1 
ATOM   536  N NE2 . GLN   A 1 256 ? -29.748 50.105  110.941 1.00 118.61 ?  237 GLN   A NE2 1 
ATOM   537  N N   . LEU   A 1 257 ? -25.681 48.234  116.296 1.00 103.28 ?  238 LEU   A N   1 
ATOM   538  C CA  . LEU   A 1 257 ? -24.673 47.394  116.972 1.00 111.69 ?  238 LEU   A CA  1 
ATOM   539  C C   . LEU   A 1 257 ? -25.368 46.569  118.057 1.00 116.19 ?  238 LEU   A C   1 
ATOM   540  O O   . LEU   A 1 257 ? -26.271 47.085  118.721 1.00 113.08 ?  238 LEU   A O   1 
ATOM   541  C CB  . LEU   A 1 257 ? -23.637 48.333  117.583 1.00 112.95 ?  238 LEU   A CB  1 
ATOM   542  C CG  . LEU   A 1 257 ? -22.210 48.071  117.131 1.00 110.78 ?  238 LEU   A CG  1 
ATOM   543  C CD1 . LEU   A 1 257 ? -21.246 48.227  118.290 1.00 104.13 ?  238 LEU   A CD1 1 
ATOM   544  C CD2 . LEU   A 1 257 ? -22.122 46.671  116.569 1.00 107.89 ?  238 LEU   A CD2 1 
ATOM   545  N N   . GLU   A 1 258 ? -24.902 45.346  118.275 1.00 121.12 ?  239 GLU   A N   1 
ATOM   546  C CA  . GLU   A 1 258 ? -25.534 44.443  119.263 1.00 113.04 ?  239 GLU   A CA  1 
ATOM   547  C C   . GLU   A 1 258 ? -24.518 44.047  120.328 1.00 112.84 ?  239 GLU   A C   1 
ATOM   548  O O   . GLU   A 1 258 ? -23.337 44.284  120.144 1.00 117.82 ?  239 GLU   A O   1 
ATOM   549  C CB  . GLU   A 1 258 ? -25.987 43.158  118.583 1.00 119.96 ?  239 GLU   A CB  1 
ATOM   550  C CG  . GLU   A 1 258 ? -25.750 43.151  117.085 1.00 130.99 ?  239 GLU   A CG  1 
ATOM   551  C CD  . GLU   A 1 258 ? -24.348 42.819  116.606 1.00 131.62 ?  239 GLU   A CD  1 
ATOM   552  O OE1 . GLU   A 1 258 ? -23.672 42.012  117.253 1.00 124.51 ?  239 GLU   A OE1 1 
ATOM   553  O OE2 . GLU   A 1 258 ? -23.951 43.362  115.571 1.00 128.22 ?  239 GLU   A OE2 1 
ATOM   554  N N   . ALA   A 1 259 ? -25.000 43.506  121.438 1.00 110.26 ?  240 ALA   A N   1 
ATOM   555  C CA  . ALA   A 1 259 ? -24.111 43.040  122.516 1.00 107.17 ?  240 ALA   A CA  1 
ATOM   556  C C   . ALA   A 1 259 ? -23.386 41.790  122.048 1.00 107.77 ?  240 ALA   A C   1 
ATOM   557  O O   . ALA   A 1 259 ? -23.925 41.043  121.256 1.00 107.56 ?  240 ALA   A O   1 
ATOM   558  C CB  . ALA   A 1 259 ? -24.920 42.755  123.746 1.00 103.01 ?  240 ALA   A CB  1 
ATOM   559  N N   . PRO   A 1 260 ? -22.154 41.551  122.507 1.00 105.72 ?  241 PRO   A N   1 
ATOM   560  C CA  . PRO   A 1 260 ? -21.550 42.372  123.540 1.00 106.45 ?  241 PRO   A CA  1 
ATOM   561  C C   . PRO   A 1 260 ? -20.782 43.564  122.963 1.00 112.94 ?  241 PRO   A C   1 
ATOM   562  O O   . PRO   A 1 260 ? -20.192 44.311  123.698 1.00 113.16 ?  241 PRO   A O   1 
ATOM   563  C CB  . PRO   A 1 260 ? -20.537 41.390  124.112 1.00 101.00 ?  241 PRO   A CB  1 
ATOM   564  C CG  . PRO   A 1 260 ? -20.083 40.624  122.912 1.00 101.95 ?  241 PRO   A CG  1 
ATOM   565  C CD  . PRO   A 1 260 ? -21.336 40.432  122.098 1.00 97.17  ?  241 PRO   A CD  1 
ATOM   566  N N   . TYR   A 1 261 ? -20.820 43.689  121.644 1.00 112.44 ?  242 TYR   A N   1 
ATOM   567  C CA  . TYR   A 1 261 ? -20.130 44.735  120.859 1.00 112.43 ?  242 TYR   A CA  1 
ATOM   568  C C   . TYR   A 1 261 ? -20.655 46.124  121.212 1.00 110.32 ?  242 TYR   A C   1 
ATOM   569  O O   . TYR   A 1 261 ? -19.865 47.052  121.181 1.00 110.23 ?  242 TYR   A O   1 
ATOM   570  C CB  . TYR   A 1 261 ? -20.217 44.369  119.381 1.00 110.76 ?  242 TYR   A CB  1 
ATOM   571  C CG  . TYR   A 1 261 ? -19.583 43.040  119.080 1.00 103.98 ?  242 TYR   A CG  1 
ATOM   572  C CD1 . TYR   A 1 261 ? -18.363 42.707  119.622 1.00 98.86  ?  242 TYR   A CD1 1 
ATOM   573  C CD2 . TYR   A 1 261 ? -20.199 42.115  118.267 1.00 104.55 ?  242 TYR   A CD2 1 
ATOM   574  C CE1 . TYR   A 1 261 ? -17.759 41.496  119.353 1.00 97.28  ?  242 TYR   A CE1 1 
ATOM   575  C CE2 . TYR   A 1 261 ? -19.612 40.895  117.991 1.00 102.04 ?  242 TYR   A CE2 1 
ATOM   576  C CZ  . TYR   A 1 261 ? -18.385 40.584  118.534 1.00 101.27 ?  242 TYR   A CZ  1 
ATOM   577  O OH  . TYR   A 1 261 ? -17.793 39.389  118.270 1.00 98.23  ?  242 TYR   A OH  1 
ATOM   578  N N   . ASN   A 1 262 ? -21.929 46.255  121.570 1.00 111.83 ?  243 ASN   A N   1 
ATOM   579  C CA  . ASN   A 1 262 ? -22.484 47.594  121.890 1.00 110.73 ?  243 ASN   A CA  1 
ATOM   580  C C   . ASN   A 1 262 ? -22.377 47.908  123.384 1.00 107.32 ?  243 ASN   A C   1 
ATOM   581  O O   . ASN   A 1 262 ? -23.074 48.804  123.825 1.00 98.87  ?  243 ASN   A O   1 
ATOM   582  C CB  . ASN   A 1 262 ? -23.920 47.746  121.415 1.00 109.68 ?  243 ASN   A CB  1 
ATOM   583  C CG  . ASN   A 1 262 ? -24.866 46.971  122.290 1.00 111.27 ?  243 ASN   A CG  1 
ATOM   584  O OD1 . ASN   A 1 262 ? -24.427 46.181  123.109 1.00 106.04 ?  243 ASN   A OD1 1 
ATOM   585  N ND2 . ASN   A 1 262 ? -26.155 47.189  122.113 1.00 110.16 ?  243 ASN   A ND2 1 
ATOM   586  N N   . SER   A 1 263 ? -21.599 47.140  124.135 1.00 106.85 ?  244 SER   A N   1 
ATOM   587  C CA  . SER   A 1 263 ? -21.436 47.390  125.583 1.00 107.15 ?  244 SER   A CA  1 
ATOM   588  C C   . SER   A 1 263 ? -20.620 48.652  125.822 1.00 104.60 ?  244 SER   A C   1 
ATOM   589  O O   . SER   A 1 263 ? -21.124 49.565  126.454 1.00 110.99 ?  244 SER   A O   1 
ATOM   590  C CB  . SER   A 1 263 ? -20.750 46.237  126.216 1.00 109.23 ?  244 SER   A CB  1 
ATOM   591  O OG  . SER   A 1 263 ? -19.555 45.955  125.526 1.00 104.96 ?  244 SER   A OG  1 
ATOM   592  N N   . ASP   A 1 264 ? -19.383 48.652  125.345 1.00 107.12 ?  245 ASP   A N   1 
ATOM   593  C CA  . ASP   A 1 264 ? -18.409 49.734  125.524 1.00 101.32 ?  245 ASP   A CA  1 
ATOM   594  C C   . ASP   A 1 264 ? -18.787 50.884  124.605 1.00 91.22  ?  245 ASP   A C   1 
ATOM   595  O O   . ASP   A 1 264 ? -18.409 50.929  123.434 1.00 90.57  ?  245 ASP   A O   1 
ATOM   596  C CB  . ASP   A 1 264 ? -16.989 49.257  125.246 1.00 95.63  ?  245 ASP   A CB  1 
ATOM   597  C CG  . ASP   A 1 264 ? -15.948 50.305  125.608 1.00 97.37  ?  245 ASP   A CG  1 
ATOM   598  O OD1 . ASP   A 1 264 ? -16.336 51.479  125.855 1.00 92.52  ?  245 ASP   A OD1 1 
ATOM   599  O OD2 . ASP   A 1 264 ? -14.747 49.948  125.661 1.00 95.25  ?  245 ASP   A OD2 1 
ATOM   600  N N   . THR   A 1 265 ? -19.519 51.842  125.165 1.00 90.16  ?  246 THR   A N   1 
ATOM   601  C CA  . THR   A 1 265 ? -20.073 52.916  124.356 1.00 91.02  ?  246 THR   A CA  1 
ATOM   602  C C   . THR   A 1 265 ? -18.985 53.853  123.817 1.00 92.36  ?  246 THR   A C   1 
ATOM   603  O O   . THR   A 1 265 ? -19.176 54.471  122.759 1.00 88.47  ?  246 THR   A O   1 
ATOM   604  C CB  . THR   A 1 265 ? -21.119 53.669  125.185 1.00 94.08  ?  246 THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 265 ? -21.734 54.695  124.398 1.00 98.09  ?  246 THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 265 ? -20.491 54.287  126.443 1.00 92.22  ?  246 THR   A CG2 1 
ATOM   607  N N   . VAL   A 1 266 ? -17.830 53.953  124.491 1.00 88.92  ?  247 VAL   A N   1 
ATOM   608  C CA  . VAL   A 1 266 ? -16.807 54.892  124.030 1.00 87.35  ?  247 VAL   A CA  1 
ATOM   609  C C   . VAL   A 1 266 ? -15.941 54.275  122.928 1.00 88.27  ?  247 VAL   A C   1 
ATOM   610  O O   . VAL   A 1 266 ? -15.568 54.957  121.962 1.00 84.98  ?  247 VAL   A O   1 
ATOM   611  C CB  . VAL   A 1 266 ? -15.961 55.395  125.213 1.00 81.31  ?  247 VAL   A CB  1 
ATOM   612  C CG1 . VAL   A 1 266 ? -16.845 56.150  126.162 1.00 81.64  ?  247 VAL   A CG1 1 
ATOM   613  C CG2 . VAL   A 1 266 ? -15.260 54.258  125.915 1.00 88.72  ?  247 VAL   A CG2 1 
ATOM   614  N N   . LEU   A 1 267 ? -15.605 52.985  123.046 1.00 87.85  ?  248 LEU   A N   1 
ATOM   615  C CA  . LEU   A 1 267 ? -14.992 52.277  121.926 1.00 83.15  ?  248 LEU   A CA  1 
ATOM   616  C C   . LEU   A 1 267 ? -15.760 52.530  120.634 1.00 81.80  ?  248 LEU   A C   1 
ATOM   617  O O   . LEU   A 1 267 ? -15.167 52.786  119.584 1.00 80.38  ?  248 LEU   A O   1 
ATOM   618  C CB  . LEU   A 1 267 ? -14.929 50.779  122.212 1.00 81.28  ?  248 LEU   A CB  1 
ATOM   619  C CG  . LEU   A 1 267 ? -14.052 50.039  121.208 1.00 75.77  ?  248 LEU   A CG  1 
ATOM   620  C CD1 . LEU   A 1 267 ? -12.799 50.840  120.978 1.00 79.77  ?  248 LEU   A CD1 1 
ATOM   621  C CD2 . LEU   A 1 267 ? -13.698 48.653  121.677 1.00 71.42  ?  248 LEU   A CD2 1 
ATOM   622  N N   . VAL   A 1 268 ? -17.089 52.477  120.698 1.00 82.26  ?  249 VAL   A N   1 
ATOM   623  C CA  . VAL   A 1 268 ? -17.881 52.730  119.503 1.00 80.79  ?  249 VAL   A CA  1 
ATOM   624  C C   . VAL   A 1 268 ? -17.811 54.203  119.114 1.00 77.76  ?  249 VAL   A C   1 
ATOM   625  O O   . VAL   A 1 268 ? -17.787 54.539  117.928 1.00 79.66  ?  249 VAL   A O   1 
ATOM   626  C CB  . VAL   A 1 268 ? -19.325 52.245  119.715 1.00 82.61  ?  249 VAL   A CB  1 
ATOM   627  C CG1 . VAL   A 1 268 ? -20.232 52.715  118.604 1.00 82.25  ?  249 VAL   A CG1 1 
ATOM   628  C CG2 . VAL   A 1 268 ? -19.341 50.743  119.772 1.00 86.86  ?  249 VAL   A CG2 1 
ATOM   629  N N   . HIS   A 1 269 ? -17.757 55.108  120.089 1.00 82.45  ?  250 HIS   A N   1 
ATOM   630  C CA  . HIS   A 1 269 ? -17.635 56.516  119.714 1.00 84.26  ?  250 HIS   A CA  1 
ATOM   631  C C   . HIS   A 1 269 ? -16.274 56.800  119.090 1.00 85.54  ?  250 HIS   A C   1 
ATOM   632  O O   . HIS   A 1 269 ? -16.186 57.534  118.095 1.00 82.06  ?  250 HIS   A O   1 
ATOM   633  C CB  . HIS   A 1 269 ? -17.876 57.437  120.910 1.00 79.09  ?  250 HIS   A CB  1 
ATOM   634  C CG  . HIS   A 1 269 ? -17.984 58.888  120.536 1.00 84.29  ?  250 HIS   A CG  1 
ATOM   635  N ND1 . HIS   A 1 269 ? -19.112 59.426  119.951 1.00 85.42  ?  250 HIS   A ND1 1 
ATOM   636  C CD2 . HIS   A 1 269 ? -17.097 59.908  120.647 1.00 83.92  ?  250 HIS   A CD2 1 
ATOM   637  C CE1 . HIS   A 1 269 ? -18.921 60.716  119.729 1.00 82.30  ?  250 HIS   A CE1 1 
ATOM   638  N NE2 . HIS   A 1 269 ? -17.706 61.033  120.141 1.00 85.04  ?  250 HIS   A NE2 1 
ATOM   639  N N   . ARG   A 1 270 ? -15.203 56.222  119.650 1.00 80.11  ?  251 ARG   A N   1 
ATOM   640  C CA  . ARG   A 1 270 ? -13.884 56.376  119.044 1.00 77.81  ?  251 ARG   A CA  1 
ATOM   641  C C   . ARG   A 1 270 ? -13.870 55.854  117.610 1.00 78.42  ?  251 ARG   A C   1 
ATOM   642  O O   . ARG   A 1 270 ? -13.487 56.575  116.683 1.00 80.55  ?  251 ARG   A O   1 
ATOM   643  C CB  . ARG   A 1 270 ? -12.833 55.649  119.872 1.00 74.16  ?  251 ARG   A CB  1 
ATOM   644  C CG  . ARG   A 1 270 ? -12.396 56.370  121.077 1.00 66.60  ?  251 ARG   A CG  1 
ATOM   645  C CD  . ARG   A 1 270 ? -11.539 55.465  121.880 1.00 69.16  ?  251 ARG   A CD  1 
ATOM   646  N NE  . ARG   A 1 270 ? -10.129 55.557  121.527 1.00 75.34  ?  251 ARG   A NE  1 
ATOM   647  C CZ  . ARG   A 1 270 ? -9.206  54.678  121.923 1.00 82.11  ?  251 ARG   A CZ  1 
ATOM   648  N NH1 . ARG   A 1 270 ? -9.549  53.631  122.675 1.00 72.93  ?  251 ARG   A NH1 1 
ATOM   649  N NH2 . ARG   A 1 270 ? -7.935  54.838  121.568 1.00 84.99  ?  251 ARG   A NH2 1 
ATOM   650  N N   . VAL   A 1 271 ? -14.292 54.600  117.413 1.00 77.01  ?  252 VAL   A N   1 
ATOM   651  C CA  . VAL   A 1 271 ? -14.246 53.987  116.090 1.00 67.84  ?  252 VAL   A CA  1 
ATOM   652  C C   . VAL   A 1 271 ? -15.000 54.838  115.082 1.00 71.94  ?  252 VAL   A C   1 
ATOM   653  O O   . VAL   A 1 271 ? -14.469 55.198  114.027 1.00 74.32  ?  252 VAL   A O   1 
ATOM   654  C CB  . VAL   A 1 271 ? -14.797 52.554  116.145 1.00 72.23  ?  252 VAL   A CB  1 
ATOM   655  C CG1 . VAL   A 1 271 ? -15.227 52.093  114.762 1.00 74.58  ?  252 VAL   A CG1 1 
ATOM   656  C CG2 . VAL   A 1 271 ? -13.748 51.615  116.725 1.00 72.07  ?  252 VAL   A CG2 1 
ATOM   657  N N   . HIS   A 1 272 ? -16.242 55.196  115.402 1.00 75.91  ?  253 HIS   A N   1 
ATOM   658  C CA  . HIS   A 1 272 ? -17.035 55.986  114.465 1.00 72.58  ?  253 HIS   A CA  1 
ATOM   659  C C   . HIS   A 1 272 ? -16.354 57.307  114.158 1.00 77.72  ?  253 HIS   A C   1 
ATOM   660  O O   . HIS   A 1 272 ? -16.378 57.780  113.016 1.00 81.16  ?  253 HIS   A O   1 
ATOM   661  C CB  . HIS   A 1 272 ? -18.434 56.228  115.029 1.00 71.50  ?  253 HIS   A CB  1 
ATOM   662  C CG  . HIS   A 1 272 ? -19.298 57.099  114.172 1.00 70.83  ?  253 HIS   A CG  1 
ATOM   663  N ND1 . HIS   A 1 272 ? -19.139 58.467  114.096 1.00 77.65  ?  253 HIS   A ND1 1 
ATOM   664  C CD2 . HIS   A 1 272 ? -20.354 56.801  113.378 1.00 78.97  ?  253 HIS   A CD2 1 
ATOM   665  C CE1 . HIS   A 1 272 ? -20.044 58.971  113.274 1.00 80.22  ?  253 HIS   A CE1 1 
ATOM   666  N NE2 . HIS   A 1 272 ? -20.799 57.982  112.830 1.00 81.70  ?  253 HIS   A NE2 1 
ATOM   667  N N   . SER   A 1 273 ? -15.736 57.922  115.162 1.00 77.82  ?  254 SER   A N   1 
ATOM   668  C CA  . SER   A 1 273 ? -15.128 59.223  114.924 1.00 78.06  ?  254 SER   A CA  1 
ATOM   669  C C   . SER   A 1 273 ? -13.893 59.090  114.046 1.00 77.16  ?  254 SER   A C   1 
ATOM   670  O O   . SER   A 1 273 ? -13.642 59.947  113.192 1.00 80.76  ?  254 SER   A O   1 
ATOM   671  C CB  . SER   A 1 273 ? -14.803 59.899  116.254 1.00 79.23  ?  254 SER   A CB  1 
ATOM   672  O OG  . SER   A 1 273 ? -16.013 60.298  116.889 1.00 78.59  ?  254 SER   A OG  1 
ATOM   673  N N   . TYR   A 1 274 ? -13.133 58.005  114.218 1.00 74.78  ?  255 TYR   A N   1 
ATOM   674  C CA  . TYR   A 1 274 ? -11.986 57.738  113.353 1.00 73.54  ?  255 TYR   A CA  1 
ATOM   675  C C   . TYR   A 1 274 ? -12.416 57.558  111.903 1.00 69.51  ?  255 TYR   A C   1 
ATOM   676  O O   . TYR   A 1 274 ? -11.864 58.188  110.993 1.00 69.14  ?  255 TYR   A O   1 
ATOM   677  C CB  . TYR   A 1 274 ? -11.249 56.502  113.854 1.00 75.23  ?  255 TYR   A CB  1 
ATOM   678  C CG  . TYR   A 1 274 ? -10.314 55.860  112.858 1.00 78.12  ?  255 TYR   A CG  1 
ATOM   679  C CD1 . TYR   A 1 274 ? -8.969  56.214  112.820 1.00 80.23  ?  255 TYR   A CD1 1 
ATOM   680  C CD2 . TYR   A 1 274 ? -10.762 54.865  111.985 1.00 78.71  ?  255 TYR   A CD2 1 
ATOM   681  C CE1 . TYR   A 1 274 ? -8.090  55.609  111.922 1.00 85.06  ?  255 TYR   A CE1 1 
ATOM   682  C CE2 . TYR   A 1 274 ? -9.903  54.262  111.080 1.00 81.43  ?  255 TYR   A CE2 1 
ATOM   683  C CZ  . TYR   A 1 274 ? -8.561  54.638  111.051 1.00 85.54  ?  255 TYR   A CZ  1 
ATOM   684  O OH  . TYR   A 1 274 ? -7.680  54.047  110.160 1.00 91.39  ?  255 TYR   A OH  1 
ATOM   685  N N   . LEU   A 1 275 ? -13.410 56.705  111.669 1.00 67.61  ?  256 LEU   A N   1 
ATOM   686  C CA  . LEU   A 1 275 ? -13.872 56.485  110.305 1.00 71.11  ?  256 LEU   A CA  1 
ATOM   687  C C   . LEU   A 1 275 ? -14.432 57.763  109.699 1.00 68.87  ?  256 LEU   A C   1 
ATOM   688  O O   . LEU   A 1 275 ? -14.292 58.007  108.499 1.00 71.40  ?  256 LEU   A O   1 
ATOM   689  C CB  . LEU   A 1 275 ? -14.919 55.370  110.270 1.00 71.64  ?  256 LEU   A CB  1 
ATOM   690  C CG  . LEU   A 1 275 ? -14.540 54.051  110.951 1.00 70.70  ?  256 LEU   A CG  1 
ATOM   691  C CD1 . LEU   A 1 275 ? -15.741 53.126  110.982 1.00 73.20  ?  256 LEU   A CD1 1 
ATOM   692  C CD2 . LEU   A 1 275 ? -13.358 53.372  110.268 1.00 69.31  ?  256 LEU   A CD2 1 
ATOM   693  N N   . GLU   A 1 276 ? -15.075 58.592  110.503 1.00 71.33  ?  257 GLU   A N   1 
ATOM   694  C CA  . GLU   A 1 276 ? -15.663 59.792  109.935 1.00 73.01  ?  257 GLU   A CA  1 
ATOM   695  C C   . GLU   A 1 276 ? -14.572 60.772  109.542 1.00 66.81  ?  257 GLU   A C   1 
ATOM   696  O O   . GLU   A 1 276 ? -14.641 61.413  108.482 1.00 60.28  ?  257 GLU   A O   1 
ATOM   697  C CB  . GLU   A 1 276 ? -16.632 60.404  110.944 1.00 77.60  ?  257 GLU   A CB  1 
ATOM   698  C CG  . GLU   A 1 276 ? -17.807 61.122  110.321 1.00 83.67  ?  257 GLU   A CG  1 
ATOM   699  C CD  . GLU   A 1 276 ? -18.521 62.019  111.309 1.00 86.37  ?  257 GLU   A CD  1 
ATOM   700  O OE1 . GLU   A 1 276 ? -19.699 62.380  111.051 1.00 90.84  ?  257 GLU   A OE1 1 
ATOM   701  O OE2 . GLU   A 1 276 ? -17.895 62.358  112.342 1.00 90.00  ?  257 GLU   A OE2 1 
ATOM   702  N N   . ARG   A 1 277 ? -13.538 60.855  110.377 1.00 66.81  ?  258 ARG   A N   1 
ATOM   703  C CA  . ARG   A 1 277 ? -12.471 61.825  110.185 1.00 66.22  ?  258 ARG   A CA  1 
ATOM   704  C C   . ARG   A 1 277 ? -11.708 61.509  108.922 1.00 72.35  ?  258 ARG   A C   1 
ATOM   705  O O   . ARG   A 1 277 ? -11.467 62.389  108.081 1.00 70.38  ?  258 ARG   A O   1 
ATOM   706  C CB  . ARG   A 1 277 ? -11.536 61.804  111.399 1.00 69.73  ?  258 ARG   A CB  1 
ATOM   707  C CG  . ARG   A 1 277 ? -10.441 62.855  111.412 1.00 66.29  ?  258 ARG   A CG  1 
ATOM   708  C CD  . ARG   A 1 277 ? -10.979 64.208  110.972 1.00 70.65  ?  258 ARG   A CD  1 
ATOM   709  N NE  . ARG   A 1 277 ? -11.886 64.834  111.936 1.00 65.59  ?  258 ARG   A NE  1 
ATOM   710  C CZ  . ARG   A 1 277 ? -11.467 65.517  112.997 1.00 68.29  ?  258 ARG   A CZ  1 
ATOM   711  N NH1 . ARG   A 1 277 ? -10.165 65.643  113.236 1.00 67.74  ?  258 ARG   A NH1 1 
ATOM   712  N NH2 . ARG   A 1 277 ? -12.343 66.065  113.828 1.00 68.59  ?  258 ARG   A NH2 1 
ATOM   713  N N   . HIS   A 1 278 ? -11.351 60.239  108.760 1.00 71.43  ?  259 HIS   A N   1 
ATOM   714  C CA  . HIS   A 1 278 ? -10.536 59.823  107.644 1.00 68.54  ?  259 HIS   A CA  1 
ATOM   715  C C   . HIS   A 1 278 ? -11.352 59.365  106.460 1.00 66.27  ?  259 HIS   A C   1 
ATOM   716  O O   . HIS   A 1 278 ? -10.823 58.663  105.595 1.00 72.28  ?  259 HIS   A O   1 
ATOM   717  C CB  . HIS   A 1 278 ? -9.567  58.759  108.105 1.00 66.57  ?  259 HIS   A CB  1 
ATOM   718  C CG  . HIS   A 1 278 ? -8.647  59.257  109.158 1.00 67.43  ?  259 HIS   A CG  1 
ATOM   719  N ND1 . HIS   A 1 278 ? -8.559  58.687  110.406 1.00 73.05  ?  259 HIS   A ND1 1 
ATOM   720  C CD2 . HIS   A 1 278 ? -7.830  60.336  109.175 1.00 77.65  ?  259 HIS   A CD2 1 
ATOM   721  C CE1 . HIS   A 1 278 ? -7.676  59.354  111.130 1.00 83.26  ?  259 HIS   A CE1 1 
ATOM   722  N NE2 . HIS   A 1 278 ? -7.227  60.367  110.410 1.00 85.52  ?  259 HIS   A NE2 1 
ATOM   723  N N   . GLY   A 1 279 ? -12.614 59.774  106.388 1.00 65.79  ?  260 GLY   A N   1 
ATOM   724  C CA  . GLY   A 1 279 ? -13.382 59.628  105.169 1.00 68.36  ?  260 GLY   A CA  1 
ATOM   725  C C   . GLY   A 1 279 ? -13.718 58.218  104.758 1.00 67.51  ?  260 GLY   A C   1 
ATOM   726  O O   . GLY   A 1 279 ? -14.024 57.992  103.594 1.00 74.45  ?  260 GLY   A O   1 
ATOM   727  N N   . LEU   A 1 280 ? -13.643 57.248  105.668 1.00 72.44  ?  261 LEU   A N   1 
ATOM   728  C CA  . LEU   A 1 280 ? -14.105 55.902  105.350 1.00 72.31  ?  261 LEU   A CA  1 
ATOM   729  C C   . LEU   A 1 280 ? -15.626 55.794  105.371 1.00 74.64  ?  261 LEU   A C   1 
ATOM   730  O O   . LEU   A 1 280 ? -16.188 54.941  104.677 1.00 70.58  ?  261 LEU   A O   1 
ATOM   731  C CB  . LEU   A 1 280 ? -13.471 54.906  106.313 1.00 67.35  ?  261 LEU   A CB  1 
ATOM   732  C CG  . LEU   A 1 280 ? -12.030 54.677  105.862 1.00 68.39  ?  261 LEU   A CG  1 
ATOM   733  C CD1 . LEU   A 1 280 ? -11.221 53.878  106.877 1.00 69.51  ?  261 LEU   A CD1 1 
ATOM   734  C CD2 . LEU   A 1 280 ? -12.037 53.988  104.499 1.00 68.58  ?  261 LEU   A CD2 1 
ATOM   735  N N   . ILE   A 1 281 ? -16.299 56.659  106.133 1.00 78.53  ?  262 ILE   A N   1 
ATOM   736  C CA  . ILE   A 1 281 ? -17.748 56.796  106.116 1.00 76.50  ?  262 ILE   A CA  1 
ATOM   737  C C   . ILE   A 1 281 ? -18.068 58.275  105.971 1.00 72.56  ?  262 ILE   A C   1 
ATOM   738  O O   . ILE   A 1 281 ? -17.222 59.137  106.215 1.00 74.32  ?  262 ILE   A O   1 
ATOM   739  C CB  . ILE   A 1 281 ? -18.392 56.225  107.390 1.00 78.23  ?  262 ILE   A CB  1 
ATOM   740  C CG1 . ILE   A 1 281 ? -18.134 57.167  108.565 1.00 79.10  ?  262 ILE   A CG1 1 
ATOM   741  C CG2 . ILE   A 1 281 ? -17.826 54.835  107.706 1.00 75.54  ?  262 ILE   A CG2 1 
ATOM   742  C CD1 . ILE   A 1 281 ? -18.552 56.595  109.898 1.00 74.80  ?  262 ILE   A CD1 1 
ATOM   743  N N   . ASN   A 1 282 ? -19.304 58.563  105.561 1.00 73.01  ?  263 ASN   A N   1 
ATOM   744  C CA  . ASN   A 1 282 ? -19.805 59.941  105.475 1.00 78.80  ?  263 ASN   A CA  1 
ATOM   745  C C   . ASN   A 1 282 ? -18.873 60.804  104.637 1.00 74.06  ?  263 ASN   A C   1 
ATOM   746  O O   . ASN   A 1 282 ? -18.388 61.854  105.073 1.00 77.97  ?  263 ASN   A O   1 
ATOM   747  C CB  . ASN   A 1 282 ? -19.990 60.571  106.862 1.00 83.52  ?  263 ASN   A CB  1 
ATOM   748  C CG  . ASN   A 1 282 ? -20.917 59.783  107.766 1.00 82.65  ?  263 ASN   A CG  1 
ATOM   749  O OD1 . ASN   A 1 282 ? -21.940 59.245  107.337 1.00 87.48  ?  263 ASN   A OD1 1 
ATOM   750  N ND2 . ASN   A 1 282 ? -20.562 59.721  109.038 1.00 83.28  ?  263 ASN   A ND2 1 
ATOM   751  N N   . PHE   A 1 283 ? -18.580 60.320  103.441 1.00 74.94  ?  264 PHE   A N   1 
ATOM   752  C CA  . PHE   A 1 283 ? -17.804 61.058  102.461 1.00 67.76  ?  264 PHE   A CA  1 
ATOM   753  C C   . PHE   A 1 283 ? -18.610 61.116  101.182 1.00 68.91  ?  264 PHE   A C   1 
ATOM   754  O O   . PHE   A 1 283 ? -19.399 60.214  100.885 1.00 77.66  ?  264 PHE   A O   1 
ATOM   755  C CB  . PHE   A 1 283 ? -16.423 60.410  102.195 1.00 62.79  ?  264 PHE   A CB  1 
ATOM   756  C CG  . PHE   A 1 283 ? -16.488 59.063  101.485 1.00 71.14  ?  264 PHE   A CG  1 
ATOM   757  C CD1 . PHE   A 1 283 ? -16.580 58.978  100.099 1.00 71.37  ?  264 PHE   A CD1 1 
ATOM   758  C CD2 . PHE   A 1 283 ? -16.447 57.879  102.209 1.00 73.68  ?  264 PHE   A CD2 1 
ATOM   759  C CE1 . PHE   A 1 283 ? -16.640 57.742  99.451  1.00 62.50  ?  264 PHE   A CE1 1 
ATOM   760  C CE2 . PHE   A 1 283 ? -16.486 56.641  101.567 1.00 73.14  ?  264 PHE   A CE2 1 
ATOM   761  C CZ  . PHE   A 1 283 ? -16.593 56.576  100.182 1.00 65.73  ?  264 PHE   A CZ  1 
ATOM   762  N N   . GLY   A 1 284 ? -18.404 62.161  100.417 1.00 62.14  ?  265 GLY   A N   1 
ATOM   763  C CA  . GLY   A 1 284 ? -19.064 62.187  99.134  1.00 67.58  ?  265 GLY   A CA  1 
ATOM   764  C C   . GLY   A 1 284 ? -20.234 63.136  99.112  1.00 73.20  ?  265 GLY   A C   1 
ATOM   765  O O   . GLY   A 1 284 ? -20.087 64.323  99.428  1.00 79.42  ?  265 GLY   A O   1 
ATOM   766  N N   . ILE   A 1 285 ? -21.406 62.641  98.731  1.00 74.43  ?  266 ILE   A N   1 
ATOM   767  C CA  . ILE   A 1 285 ? -22.608 63.460  98.665  1.00 74.23  ?  266 ILE   A CA  1 
ATOM   768  C C   . ILE   A 1 285 ? -23.701 62.713  99.404  1.00 80.85  ?  266 ILE   A C   1 
ATOM   769  O O   . ILE   A 1 285 ? -24.371 61.844  98.833  1.00 88.20  ?  266 ILE   A O   1 
ATOM   770  C CB  . ILE   A 1 285 ? -23.027 63.778  97.240  1.00 68.21  ?  266 ILE   A CB  1 
ATOM   771  C CG1 . ILE   A 1 285 ? -21.924 64.595  96.583  1.00 75.79  ?  266 ILE   A CG1 1 
ATOM   772  C CG2 . ILE   A 1 285 ? -24.287 64.572  97.275  1.00 70.22  ?  266 ILE   A CG2 1 
ATOM   773  C CD1 . ILE   A 1 285 ? -21.944 64.576  95.083  1.00 77.61  ?  266 ILE   A CD1 1 
ATOM   774  N N   . TYR   A 1 286 ? -23.879 63.054  100.672 1.00 85.80  ?  267 TYR   A N   1 
ATOM   775  C CA  . TYR   A 1 286 ? -24.853 62.455  101.558 1.00 82.52  ?  267 TYR   A CA  1 
ATOM   776  C C   . TYR   A 1 286 ? -25.757 63.558  102.085 1.00 93.66  ?  267 TYR   A C   1 
ATOM   777  O O   . TYR   A 1 286 ? -25.379 64.736  102.082 1.00 95.79  ?  267 TYR   A O   1 
ATOM   778  C CB  . TYR   A 1 286 ? -24.116 61.685  102.677 1.00 84.98  ?  267 TYR   A CB  1 
ATOM   779  C CG  . TYR   A 1 286 ? -22.932 62.403  103.336 1.00 85.07  ?  267 TYR   A CG  1 
ATOM   780  C CD1 . TYR   A 1 286 ? -21.707 62.503  102.679 1.00 85.73  ?  267 TYR   A CD1 1 
ATOM   781  C CD2 . TYR   A 1 286 ? -22.994 62.865  104.649 1.00 87.79  ?  267 TYR   A CD2 1 
ATOM   782  C CE1 . TYR   A 1 286 ? -20.602 63.135  103.265 1.00 90.17  ?  267 TYR   A CE1 1 
ATOM   783  C CE2 . TYR   A 1 286 ? -21.875 63.489  105.261 1.00 89.13  ?  267 TYR   A CE2 1 
ATOM   784  C CZ  . TYR   A 1 286 ? -20.678 63.621  104.562 1.00 88.98  ?  267 TYR   A CZ  1 
ATOM   785  O OH  . TYR   A 1 286 ? -19.548 64.225  105.127 1.00 78.31  ?  267 TYR   A OH  1 
ATOM   786  N N   . LYS   A 1 287 ? -26.983 63.197  102.464 1.00 97.34  ?  268 LYS   A N   1 
ATOM   787  C CA  . LYS   A 1 287 ? -27.805 64.136  103.217 1.00 102.40 ?  268 LYS   A CA  1 
ATOM   788  C C   . LYS   A 1 287 ? -27.434 64.034  104.688 1.00 101.30 ?  268 LYS   A C   1 
ATOM   789  O O   . LYS   A 1 287 ? -27.132 62.945  105.192 1.00 94.87  ?  268 LYS   A O   1 
ATOM   790  C CB  . LYS   A 1 287 ? -29.311 63.895  103.030 1.00 105.24 ?  268 LYS   A CB  1 
ATOM   791  C CG  . LYS   A 1 287 ? -30.154 64.950  103.809 1.00 116.08 ?  268 LYS   A CG  1 
ATOM   792  C CD  . LYS   A 1 287 ? -31.643 64.616  104.027 1.00 115.27 ?  268 LYS   A CD  1 
ATOM   793  C CE  . LYS   A 1 287 ? -32.507 65.036  102.837 1.00 115.71 ?  268 LYS   A CE  1 
ATOM   794  N NZ  . LYS   A 1 287 ? -32.753 66.525  102.837 1.00 109.32 ?  268 LYS   A NZ  1 
ATOM   795  N N   . ARG   A 1 288 ? -27.416 65.184  105.359 1.00 104.09 ?  269 ARG   A N   1 
ATOM   796  C CA  . ARG   A 1 288 ? -27.126 65.236  106.779 1.00 103.15 ?  269 ARG   A CA  1 
ATOM   797  C C   . ARG   A 1 288 ? -28.401 64.967  107.563 1.00 106.59 ?  269 ARG   A C   1 
ATOM   798  O O   . ARG   A 1 288 ? -29.467 65.484  107.210 1.00 110.27 ?  269 ARG   A O   1 
ATOM   799  C CB  . ARG   A 1 288 ? -26.583 66.611  107.142 1.00 105.08 ?  269 ARG   A CB  1 
ATOM   800  C CG  . ARG   A 1 288 ? -25.149 66.829  106.766 1.00 110.71 ?  269 ARG   A CG  1 
ATOM   801  C CD  . ARG   A 1 288 ? -24.665 68.181  107.247 1.00 120.22 ?  269 ARG   A CD  1 
ATOM   802  N NE  . ARG   A 1 288 ? -25.163 69.281  106.419 1.00 128.52 ?  269 ARG   A NE  1 
ATOM   803  C CZ  . ARG   A 1 288 ? -24.531 69.734  105.337 1.00 130.24 ?  269 ARG   A CZ  1 
ATOM   804  N NH1 . ARG   A 1 288 ? -23.394 69.157  104.959 1.00 127.36 ?  269 ARG   A NH1 1 
ATOM   805  N NH2 . ARG   A 1 288 ? -25.030 70.747  104.632 1.00 125.72 ?  269 ARG   A NH2 1 
ATOM   806  N N   . ILE   A 1 289 ? -28.303 64.157  108.621 1.00 106.42 ?  270 ILE   A N   1 
ATOM   807  C CA  . ILE   A 1 289 ? -29.289 64.268  109.690 1.00 114.73 ?  270 ILE   A CA  1 
ATOM   808  C C   . ILE   A 1 289 ? -28.984 65.568  110.424 1.00 117.54 ?  270 ILE   A C   1 
ATOM   809  O O   . ILE   A 1 289 ? -29.782 66.515  110.403 1.00 114.98 ?  270 ILE   A O   1 
ATOM   810  C CB  . ILE   A 1 289 ? -29.271 63.082  110.669 1.00 108.96 ?  270 ILE   A CB  1 
ATOM   811  C CG1 . ILE   A 1 289 ? -29.649 61.777  109.966 1.00 110.61 ?  270 ILE   A CG1 1 
ATOM   812  C CG2 . ILE   A 1 289 ? -30.200 63.400  111.849 1.00 111.22 ?  270 ILE   A CG2 1 
ATOM   813  C CD1 . ILE   A 1 289 ? -29.392 60.518  110.805 1.00 113.98 ?  270 ILE   A CD1 1 
ATOM   814  N N   . LYS   A 1 290 ? -27.827 65.567  111.088 1.00 114.25 ?  271 LYS   A N   1 
ATOM   815  C CA  . LYS   A 1 290 ? -27.327 66.703  111.900 1.00 116.12 ?  271 LYS   A CA  1 
ATOM   816  C C   . LYS   A 1 290 ? -26.884 67.844  110.994 1.00 120.68 ?  271 LYS   A C   1 
ATOM   817  O O   . LYS   A 1 290 ? -25.820 67.724  110.399 1.00 119.54 ?  271 LYS   A O   1 
ATOM   818  C CB  . LYS   A 1 290 ? -26.094 66.263  112.684 1.00 112.12 ?  271 LYS   A CB  1 
ATOM   819  C CG  . LYS   A 1 290 ? -26.193 64.877  113.289 1.00 111.19 ?  271 LYS   A CG  1 
ATOM   820  C CD  . LYS   A 1 290 ? -25.338 64.717  114.512 1.00 107.96 ?  271 LYS   A CD  1 
ATOM   821  C CE  . LYS   A 1 290 ? -24.288 65.798  114.628 1.00 116.84 ?  271 LYS   A CE  1 
ATOM   822  N NZ  . LYS   A 1 290 ? -23.241 65.439  115.616 1.00 108.50 ?  271 LYS   A NZ  1 
ATOM   823  N N   . PRO   A 1 291 ? -27.590 68.990  110.950 1.00 123.17 ?  272 PRO   A N   1 
ATOM   824  C CA  . PRO   A 1 291 ? -27.211 70.099  110.110 1.00 121.75 ?  272 PRO   A CA  1 
ATOM   825  C C   . PRO   A 1 291 ? -25.929 70.734  110.647 1.00 123.41 ?  272 PRO   A C   1 
ATOM   826  O O   . PRO   A 1 291 ? -25.653 70.679  111.812 1.00 117.37 ?  272 PRO   A O   1 
ATOM   827  C CB  . PRO   A 1 291 ? -28.401 71.053  110.169 1.00 114.68 ?  272 PRO   A CB  1 
ATOM   828  C CG  . PRO   A 1 291 ? -29.505 70.172  110.652 1.00 116.15 ?  272 PRO   A CG  1 
ATOM   829  C CD  . PRO   A 1 291 ? -28.808 69.299  111.670 1.00 121.52 ?  272 PRO   A CD  1 
ATOM   830  N N   . LEU   A 1 292 ? -25.227 71.405  109.751 1.00 125.01 ?  273 LEU   A N   1 
ATOM   831  C CA  . LEU   A 1 292 ? -23.904 71.974  110.057 1.00 124.33 ?  273 LEU   A CA  1 
ATOM   832  C C   . LEU   A 1 292 ? -23.975 72.915  111.246 1.00 129.16 ?  273 LEU   A C   1 
ATOM   833  O O   . LEU   A 1 292 ? -24.901 73.707  111.322 1.00 128.29 ?  273 LEU   A O   1 
ATOM   834  C CB  . LEU   A 1 292 ? -23.491 72.784  108.835 1.00 123.90 ?  273 LEU   A CB  1 
ATOM   835  C CG  . LEU   A 1 292 ? -22.558 72.047  107.893 1.00 124.54 ?  273 LEU   A CG  1 
ATOM   836  C CD1 . LEU   A 1 292 ? -21.726 73.036  107.103 1.00 115.45 ?  273 LEU   A CD1 1 
ATOM   837  C CD2 . LEU   A 1 292 ? -21.680 71.109  108.691 1.00 109.95 ?  273 LEU   A CD2 1 
ATOM   838  N N   . PRO   A 1 293 ? -22.974 72.884  112.142 1.00 132.62 ?  274 PRO   A N   1 
ATOM   839  C CA  . PRO   A 1 293 ? -22.902 73.815  113.243 1.00 129.07 ?  274 PRO   A CA  1 
ATOM   840  C C   . PRO   A 1 293 ? -22.767 75.182  112.571 1.00 127.29 ?  274 PRO   A C   1 
ATOM   841  O O   . PRO   A 1 293 ? -21.952 75.350  111.705 1.00 121.59 ?  274 PRO   A O   1 
ATOM   842  C CB  . PRO   A 1 293 ? -21.581 73.462  113.921 1.00 128.30 ?  274 PRO   A CB  1 
ATOM   843  C CG  . PRO   A 1 293 ? -20.805 72.761  112.844 1.00 127.59 ?  274 PRO   A CG  1 
ATOM   844  C CD  . PRO   A 1 293 ? -21.864 71.951  112.135 1.00 132.57 ?  274 PRO   A CD  1 
ATOM   845  N N   . THR   A 1 294 ? -23.495 76.152  113.097 1.00 130.26 ?  275 THR   A N   1 
ATOM   846  C CA  . THR   A 1 294 ? -23.584 77.485  112.469 1.00 129.80 ?  275 THR   A CA  1 
ATOM   847  C C   . THR   A 1 294 ? -22.219 78.157  112.384 1.00 124.19 ?  275 THR   A C   1 
ATOM   848  O O   . THR   A 1 294 ? -22.009 78.855  111.392 1.00 115.24 ?  275 THR   A O   1 
ATOM   849  C CB  . THR   A 1 294 ? -24.632 78.337  113.184 1.00 126.97 ?  275 THR   A CB  1 
ATOM   850  O OG1 . THR   A 1 294 ? -24.278 79.696  112.938 1.00 139.48 ?  275 THR   A OG1 1 
ATOM   851  C CG2 . THR   A 1 294 ? -24.697 78.060  114.669 1.00 120.39 ?  275 THR   A CG2 1 
ATOM   852  N N   . LYS   A 1 295 ? -21.360 78.004  113.389 1.00 119.59 ?  276 LYS   A N   1 
ATOM   853  C CA  . LYS   A 1 295 ? -20.063 78.717  113.285 1.00 112.75 ?  276 LYS   A CA  1 
ATOM   854  C C   . LYS   A 1 295 ? -18.919 77.764  112.980 1.00 105.17 ?  276 LYS   A C   1 
ATOM   855  O O   . LYS   A 1 295 ? -18.727 76.806  113.709 1.00 101.82 ?  276 LYS   A O   1 
ATOM   856  C CB  . LYS   A 1 295 ? -19.755 79.566  114.515 1.00 118.19 ?  276 LYS   A CB  1 
ATOM   857  C CG  . LYS   A 1 295 ? -19.155 80.940  114.227 1.00 114.58 ?  276 LYS   A CG  1 
ATOM   858  C CD  . LYS   A 1 295 ? -18.639 81.157  112.810 1.00 112.45 ?  276 LYS   A CD  1 
ATOM   859  C CE  . LYS   A 1 295 ? -19.693 81.064  111.725 1.00 117.38 ?  276 LYS   A CE  1 
ATOM   860  N NZ  . LYS   A 1 295 ? -19.265 81.699  110.457 1.00 105.33 ?  276 LYS   A NZ  1 
ATOM   861  N N   . LYS   A 1 296 ? -18.213 78.084  111.906 1.00 103.39 ?  277 LYS   A N   1 
ATOM   862  C CA  . LYS   A 1 296 ? -17.045 77.358  111.383 1.00 94.37  ?  277 LYS   A CA  1 
ATOM   863  C C   . LYS   A 1 296 ? -15.827 77.689  112.232 1.00 87.15  ?  277 LYS   A C   1 
ATOM   864  O O   . LYS   A 1 296 ? -15.806 78.730  112.841 1.00 89.78  ?  277 LYS   A O   1 
ATOM   865  C CB  . LYS   A 1 296 ? -16.828 77.845  109.955 1.00 89.88  ?  277 LYS   A CB  1 
ATOM   866  C CG  . LYS   A 1 296 ? -18.072 77.831  109.088 1.00 87.55  ?  277 LYS   A CG  1 
ATOM   867  C CD  . LYS   A 1 296 ? -17.891 78.608  107.821 1.00 85.98  ?  277 LYS   A CD  1 
ATOM   868  C CE  . LYS   A 1 296 ? -19.053 78.467  106.865 1.00 101.01 ?  277 LYS   A CE  1 
ATOM   869  N NZ  . LYS   A 1 296 ? -19.345 79.743  106.176 1.00 97.37  ?  277 LYS   A NZ  1 
ATOM   870  N N   . THR   A 1 297 ? -14.858 76.798  112.256 1.00 75.59  ?  278 THR   A N   1 
ATOM   871  C CA  . THR   A 1 297 ? -13.631 77.055  113.019 1.00 74.11  ?  278 THR   A CA  1 
ATOM   872  C C   . THR   A 1 297 ? -12.471 76.881  112.060 1.00 75.42  ?  278 THR   A C   1 
ATOM   873  O O   . THR   A 1 297 ? -12.474 75.916  111.375 1.00 78.39  ?  278 THR   A O   1 
ATOM   874  C CB  . THR   A 1 297 ? -13.489 75.980  114.086 1.00 76.00  ?  278 THR   A CB  1 
ATOM   875  O OG1 . THR   A 1 297 ? -14.751 75.926  114.730 1.00 81.70  ?  278 THR   A OG1 1 
ATOM   876  C CG2 . THR   A 1 297 ? -12.448 76.306  115.122 1.00 80.81  ?  278 THR   A CG2 1 
ATOM   877  N N   . GLY   A 1 298 ? -11.581 77.847  111.925 1.00 77.75  ?  279 GLY   A N   1 
ATOM   878  C CA  . GLY   A 1 298 ? -10.411 77.659  111.049 1.00 70.86  ?  279 GLY   A CA  1 
ATOM   879  C C   . GLY   A 1 298 ? -10.646 78.014  109.601 1.00 69.15  ?  279 GLY   A C   1 
ATOM   880  O O   . GLY   A 1 298 ? -11.737 77.857  109.120 1.00 71.90  ?  279 GLY   A O   1 
ATOM   881  N N   . LYS   A 1 299 ? -9.617  78.465  108.907 1.00 62.72  ?  280 LYS   A N   1 
ATOM   882  C CA  . LYS   A 1 299 ? -9.812  78.796  107.499 1.00 65.45  ?  280 LYS   A CA  1 
ATOM   883  C C   . LYS   A 1 299 ? -8.788  78.068  106.632 1.00 69.80  ?  280 LYS   A C   1 
ATOM   884  O O   . LYS   A 1 299 ? -7.581  78.149  106.893 1.00 70.76  ?  280 LYS   A O   1 
ATOM   885  C CB  . LYS   A 1 299 ? -9.699  80.305  107.291 1.00 59.71  ?  280 LYS   A CB  1 
ATOM   886  C CG  . LYS   A 1 299 ? -9.960  80.785  105.876 1.00 71.62  ?  280 LYS   A CG  1 
ATOM   887  C CD  . LYS   A 1 299 ? -11.160 80.059  105.224 1.00 78.73  ?  280 LYS   A CD  1 
ATOM   888  C CE  . LYS   A 1 299 ? -11.696 80.746  103.929 1.00 68.78  ?  280 LYS   A CE  1 
ATOM   889  N NZ  . LYS   A 1 299 ? -10.624 81.485  103.173 1.00 69.43  ?  280 LYS   A NZ  1 
ATOM   890  N N   . VAL   A 1 300 ? -9.263  77.384  105.584 1.00 61.51  ?  281 VAL   A N   1 
ATOM   891  C CA  . VAL   A 1 300 ? -8.400  76.665  104.652 1.00 60.69  ?  281 VAL   A CA  1 
ATOM   892  C C   . VAL   A 1 300 ? -8.645  77.180  103.247 1.00 59.08  ?  281 VAL   A C   1 
ATOM   893  O O   . VAL   A 1 300 ? -9.798  77.271  102.806 1.00 61.81  ?  281 VAL   A O   1 
ATOM   894  C CB  . VAL   A 1 300 ? -8.630  75.142  104.684 1.00 61.92  ?  281 VAL   A CB  1 
ATOM   895  C CG1 . VAL   A 1 300 ? -7.938  74.513  103.529 1.00 56.43  ?  281 VAL   A CG1 1 
ATOM   896  C CG2 . VAL   A 1 300 ? -8.089  74.538  105.950 1.00 61.83  ?  281 VAL   A CG2 1 
ATOM   897  N N   . ILE   A 1 301 ? -7.556  77.483  102.543 1.00 56.20  ?  282 ILE   A N   1 
ATOM   898  C CA  . ILE   A 1 301 ? -7.565  77.750  101.110 1.00 53.81  ?  282 ILE   A CA  1 
ATOM   899  C C   . ILE   A 1 301 ? -7.093  76.500  100.368 1.00 61.61  ?  282 ILE   A C   1 
ATOM   900  O O   . ILE   A 1 301 ? -6.049  75.915  100.708 1.00 56.35  ?  282 ILE   A O   1 
ATOM   901  C CB  . ILE   A 1 301 ? -6.674  78.952  100.770 1.00 56.25  ?  282 ILE   A CB  1 
ATOM   902  C CG1 . ILE   A 1 301 ? -7.429  80.244  101.059 1.00 59.76  ?  282 ILE   A CG1 1 
ATOM   903  C CG2 . ILE   A 1 301 ? -6.188  78.885  99.321  1.00 54.00  ?  282 ILE   A CG2 1 
ATOM   904  C CD1 . ILE   A 1 301 ? -8.714  80.393  100.231 1.00 60.45  ?  282 ILE   A CD1 1 
ATOM   905  N N   . ILE   A 1 302 ? -7.850  76.108  99.338  1.00 58.44  ?  283 ILE   A N   1 
ATOM   906  C CA  . ILE   A 1 302 ? -7.591  74.903  98.553  1.00 57.50  ?  283 ILE   A CA  1 
ATOM   907  C C   . ILE   A 1 302 ? -7.266  75.309  97.118  1.00 57.53  ?  283 ILE   A C   1 
ATOM   908  O O   . ILE   A 1 302 ? -8.112  75.897  96.430  1.00 60.76  ?  283 ILE   A O   1 
ATOM   909  C CB  . ILE   A 1 302 ? -8.797  73.957  98.574  1.00 56.60  ?  283 ILE   A CB  1 
ATOM   910  C CG1 . ILE   A 1 302 ? -8.908  73.274  99.931  1.00 57.57  ?  283 ILE   A CG1 1 
ATOM   911  C CG2 . ILE   A 1 302 ? -8.648  72.917  97.514  1.00 57.10  ?  283 ILE   A CG2 1 
ATOM   912  C CD1 . ILE   A 1 302 ? -9.982  72.202  99.957  1.00 59.17  ?  283 ILE   A CD1 1 
ATOM   913  N N   . ILE   A 1 303 ? -6.059  74.983  96.652  1.00 50.53  ?  284 ILE   A N   1 
ATOM   914  C CA  . ILE   A 1 303 ? -5.670  75.327  95.289  1.00 50.61  ?  284 ILE   A CA  1 
ATOM   915  C C   . ILE   A 1 303 ? -6.097  74.202  94.349  1.00 49.85  ?  284 ILE   A C   1 
ATOM   916  O O   . ILE   A 1 303 ? -5.625  73.063  94.450  1.00 47.45  ?  284 ILE   A O   1 
ATOM   917  C CB  . ILE   A 1 303 ? -4.167  75.606  95.185  1.00 50.74  ?  284 ILE   A CB  1 
ATOM   918  C CG1 . ILE   A 1 303 ? -3.770  76.712  96.162  1.00 50.35  ?  284 ILE   A CG1 1 
ATOM   919  C CG2 . ILE   A 1 303 ? -3.813  76.030  93.759  1.00 42.34  ?  284 ILE   A CG2 1 
ATOM   920  C CD1 . ILE   A 1 303 ? -2.277  77.031  96.166  1.00 41.65  ?  284 ILE   A CD1 1 
ATOM   921  N N   . GLY   A 1 304 ? -7.001  74.523  93.435  1.00 51.27  ?  285 GLY   A N   1 
ATOM   922  C CA  . GLY   A 1 304 ? -7.464  73.580  92.437  1.00 50.10  ?  285 GLY   A CA  1 
ATOM   923  C C   . GLY   A 1 304 ? -8.798  72.979  92.821  1.00 50.86  ?  285 GLY   A C   1 
ATOM   924  O O   . GLY   A 1 304 ? -8.977  72.553  93.964  1.00 48.98  ?  285 GLY   A O   1 
ATOM   925  N N   . SER   A 1 305 ? -9.750  72.939  91.897  1.00 51.16  ?  286 SER   A N   1 
ATOM   926  C CA  . SER   A 1 305 ? -11.009 72.241  92.135  1.00 58.08  ?  286 SER   A CA  1 
ATOM   927  C C   . SER   A 1 305 ? -11.131 71.019  91.232  1.00 60.91  ?  286 SER   A C   1 
ATOM   928  O O   . SER   A 1 305 ? -12.195 70.732  90.677  1.00 59.07  ?  286 SER   A O   1 
ATOM   929  C CB  . SER   A 1 305 ? -12.204 73.164  91.942  1.00 58.52  ?  286 SER   A CB  1 
ATOM   930  O OG  . SER   A 1 305 ? -12.272 73.573  90.586  1.00 65.03  ?  286 SER   A OG  1 
ATOM   931  N N   . GLY   A 1 306 ? -10.030 70.296  91.063  1.00 57.46  ?  287 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 306 ? -10.117 68.950  90.580  1.00 57.59  ?  287 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 306 ? -10.773 68.074  91.631  1.00 55.77  ?  287 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 306 ? -11.221 68.519  92.683  1.00 57.33  ?  287 GLY   A O   1 
ATOM   935  N N   . VAL   A 1 307 ? -10.812 66.781  91.337  1.00 59.91  ?  288 VAL   A N   1 
ATOM   936  C CA  . VAL   A 1 307 ? -11.463 65.863  92.253  1.00 53.77  ?  288 VAL   A CA  1 
ATOM   937  C C   . VAL   A 1 307 ? -10.760 65.880  93.598  1.00 55.54  ?  288 VAL   A C   1 
ATOM   938  O O   . VAL   A 1 307 ? -11.416 65.881  94.646  1.00 57.84  ?  288 VAL   A O   1 
ATOM   939  C CB  . VAL   A 1 307 ? -11.522 64.450  91.637  1.00 56.46  ?  288 VAL   A CB  1 
ATOM   940  C CG1 . VAL   A 1 307 ? -11.886 63.378  92.687  1.00 50.85  ?  288 VAL   A CG1 1 
ATOM   941  C CG2 . VAL   A 1 307 ? -12.515 64.446  90.488  1.00 50.87  ?  288 VAL   A CG2 1 
ATOM   942  N N   . SER   A 1 308 ? -9.424  65.906  93.611  1.00 53.54  ?  289 SER   A N   1 
ATOM   943  C CA  . SER   A 1 308 ? -8.764  65.832  94.912  1.00 56.25  ?  289 SER   A CA  1 
ATOM   944  C C   . SER   A 1 308 ? -9.097  67.072  95.736  1.00 60.18  ?  289 SER   A C   1 
ATOM   945  O O   . SER   A 1 308 ? -9.479  66.962  96.912  1.00 54.33  ?  289 SER   A O   1 
ATOM   946  C CB  . SER   A 1 308 ? -7.250  65.635  94.775  1.00 48.68  ?  289 SER   A CB  1 
ATOM   947  O OG  . SER   A 1 308 ? -6.659  66.637  93.997  1.00 53.89  ?  289 SER   A OG  1 
ATOM   948  N N   . GLY   A 1 309 ? -9.028  68.258  95.106  1.00 58.59  ?  290 GLY   A N   1 
ATOM   949  C CA  . GLY   A 1 309 ? -9.506  69.479  95.733  1.00 55.44  ?  290 GLY   A CA  1 
ATOM   950  C C   . GLY   A 1 309 ? -10.928 69.376  96.267  1.00 58.04  ?  290 GLY   A C   1 
ATOM   951  O O   . GLY   A 1 309 ? -11.159 69.566  97.466  1.00 61.85  ?  290 GLY   A O   1 
ATOM   952  N N   . LEU   A 1 310 ? -11.885 69.062  95.388  1.00 54.44  ?  291 LEU   A N   1 
ATOM   953  C CA  . LEU   A 1 310 ? -13.283 68.977  95.794  1.00 50.90  ?  291 LEU   A CA  1 
ATOM   954  C C   . LEU   A 1 310 ? -13.461 67.998  96.945  1.00 56.69  ?  291 LEU   A C   1 
ATOM   955  O O   . LEU   A 1 310 ? -14.183 68.269  97.911  1.00 62.08  ?  291 LEU   A O   1 
ATOM   956  C CB  . LEU   A 1 310 ? -14.125 68.568  94.595  1.00 48.43  ?  291 LEU   A CB  1 
ATOM   957  C CG  . LEU   A 1 310 ? -14.129 69.594  93.474  1.00 55.51  ?  291 LEU   A CG  1 
ATOM   958  C CD1 . LEU   A 1 310 ? -14.460 68.952  92.176  1.00 59.04  ?  291 LEU   A CD1 1 
ATOM   959  C CD2 . LEU   A 1 310 ? -15.201 70.607  93.765  1.00 67.04  ?  291 LEU   A CD2 1 
ATOM   960  N N   . ALA   A 1 311 ? -12.808 66.850  96.870  1.00 56.25  ?  292 ALA   A N   1 
ATOM   961  C CA  . ALA   A 1 311 ? -13.072 65.853  97.894  1.00 57.98  ?  292 ALA   A CA  1 
ATOM   962  C C   . ALA   A 1 311 ? -12.610 66.328  99.265  1.00 60.35  ?  292 ALA   A C   1 
ATOM   963  O O   . ALA   A 1 311 ? -13.250 66.012  100.275 1.00 62.92  ?  292 ALA   A O   1 
ATOM   964  C CB  . ALA   A 1 311 ? -12.407 64.527  97.524  1.00 58.44  ?  292 ALA   A CB  1 
ATOM   965  N N   . ALA   A 1 312 ? -11.512 67.082  99.332  1.00 59.76  ?  293 ALA   A N   1 
ATOM   966  C CA  . ALA   A 1 312 ? -11.104 67.629  100.622 1.00 62.89  ?  293 ALA   A CA  1 
ATOM   967  C C   . ALA   A 1 312 ? -12.042 68.751  101.051 1.00 62.93  ?  293 ALA   A C   1 
ATOM   968  O O   . ALA   A 1 312 ? -12.499 68.787  102.201 1.00 60.90  ?  293 ALA   A O   1 
ATOM   969  C CB  . ALA   A 1 312 ? -9.665  68.131  100.561 1.00 55.83  ?  293 ALA   A CB  1 
ATOM   970  N N   . ALA   A 1 313 ? -12.342 69.671  100.126 1.00 58.91  ?  294 ALA   A N   1 
ATOM   971  C CA  . ALA   A 1 313 ? -13.215 70.790  100.442 1.00 57.16  ?  294 ALA   A CA  1 
ATOM   972  C C   . ALA   A 1 313 ? -14.507 70.312  101.079 1.00 62.38  ?  294 ALA   A C   1 
ATOM   973  O O   . ALA   A 1 313 ? -14.942 70.872  102.092 1.00 68.12  ?  294 ALA   A O   1 
ATOM   974  C CB  . ALA   A 1 313 ? -13.513 71.602  99.186  1.00 56.25  ?  294 ALA   A CB  1 
ATOM   975  N N   . ARG   A 1 314 ? -15.120 69.259  100.525 1.00 56.80  ?  295 ARG   A N   1 
ATOM   976  C CA  . ARG   A 1 314 ? -16.373 68.780  101.095 1.00 57.93  ?  295 ARG   A CA  1 
ATOM   977  C C   . ARG   A 1 314 ? -16.148 68.220  102.481 1.00 61.07  ?  295 ARG   A C   1 
ATOM   978  O O   . ARG   A 1 314 ? -16.937 68.473  103.402 1.00 61.64  ?  295 ARG   A O   1 
ATOM   979  C CB  . ARG   A 1 314 ? -17.014 67.720  100.209 1.00 59.61  ?  295 ARG   A CB  1 
ATOM   980  C CG  . ARG   A 1 314 ? -17.816 68.297  99.087  1.00 64.21  ?  295 ARG   A CG  1 
ATOM   981  C CD  . ARG   A 1 314 ? -18.626 67.227  98.441  1.00 62.93  ?  295 ARG   A CD  1 
ATOM   982  N NE  . ARG   A 1 314 ? -19.839 66.903  99.169  1.00 61.56  ?  295 ARG   A NE  1 
ATOM   983  C CZ  . ARG   A 1 314 ? -21.012 67.492  98.939  1.00 71.32  ?  295 ARG   A CZ  1 
ATOM   984  N NH1 . ARG   A 1 314 ? -22.083 67.118  99.646  1.00 74.95  ?  295 ARG   A NH1 1 
ATOM   985  N NH2 . ARG   A 1 314 ? -21.111 68.464  98.020  1.00 57.88  ?  295 ARG   A NH2 1 
ATOM   986  N N   . GLN   A 1 315 ? -15.069 67.463  102.652 1.00 62.11  ?  296 GLN   A N   1 
ATOM   987  C CA  . GLN   A 1 315 ? -14.806 66.887  103.960 1.00 65.61  ?  296 GLN   A CA  1 
ATOM   988  C C   . GLN   A 1 315 ? -14.578 67.981  104.987 1.00 67.32  ?  296 GLN   A C   1 
ATOM   989  O O   . GLN   A 1 315 ? -15.071 67.897  106.114 1.00 68.74  ?  296 GLN   A O   1 
ATOM   990  C CB  . GLN   A 1 315 ? -13.606 65.947  103.888 1.00 58.02  ?  296 GLN   A CB  1 
ATOM   991  C CG  . GLN   A 1 315 ? -13.920 64.633  103.250 1.00 59.08  ?  296 GLN   A CG  1 
ATOM   992  C CD  . GLN   A 1 315 ? -14.999 63.886  103.974 1.00 65.02  ?  296 GLN   A CD  1 
ATOM   993  O OE1 . GLN   A 1 315 ? -16.193 64.083  103.704 1.00 68.35  ?  296 GLN   A OE1 1 
ATOM   994  N NE2 . GLN   A 1 315 ? -14.597 63.029  104.921 1.00 64.89  ?  296 GLN   A NE2 1 
ATOM   995  N N   . LEU   A 1 316 ? -13.842 69.027  104.606 1.00 68.72  ?  297 LEU   A N   1 
ATOM   996  C CA  . LEU   A 1 316 ? -13.492 70.065  105.562 1.00 66.46  ?  297 LEU   A CA  1 
ATOM   997  C C   . LEU   A 1 316 ? -14.732 70.846  105.978 1.00 70.51  ?  297 LEU   A C   1 
ATOM   998  O O   . LEU   A 1 316 ? -15.008 70.996  107.179 1.00 71.31  ?  297 LEU   A O   1 
ATOM   999  C CB  . LEU   A 1 316 ? -12.418 70.974  104.964 1.00 59.74  ?  297 LEU   A CB  1 
ATOM   1000 C CG  . LEU   A 1 316 ? -11.031 70.332  104.873 1.00 53.72  ?  297 LEU   A CG  1 
ATOM   1001 C CD1 . LEU   A 1 316 ? -10.053 71.251  104.168 1.00 50.00  ?  297 LEU   A CD1 1 
ATOM   1002 C CD2 . LEU   A 1 316 ? -10.505 69.920  106.234 1.00 52.05  ?  297 LEU   A CD2 1 
ATOM   1003 N N   . GLN   A 1 317 ? -15.500 71.335  104.999 1.00 60.28  ?  298 GLN   A N   1 
ATOM   1004 C CA  . GLN   A 1 317 ? -16.821 71.874  105.297 1.00 60.99  ?  298 GLN   A CA  1 
ATOM   1005 C C   . GLN   A 1 317 ? -17.620 70.919  106.191 1.00 71.01  ?  298 GLN   A C   1 
ATOM   1006 O O   . GLN   A 1 317 ? -18.113 71.311  107.254 1.00 75.33  ?  298 GLN   A O   1 
ATOM   1007 C CB  . GLN   A 1 317 ? -17.549 72.148  103.994 1.00 61.35  ?  298 GLN   A CB  1 
ATOM   1008 C CG  . GLN   A 1 317 ? -18.603 73.185  104.072 1.00 69.52  ?  298 GLN   A CG  1 
ATOM   1009 C CD  . GLN   A 1 317 ? -19.458 73.229  102.816 1.00 79.24  ?  298 GLN   A CD  1 
ATOM   1010 O OE1 . GLN   A 1 317 ? -20.119 72.241  102.469 1.00 86.00  ?  298 GLN   A OE1 1 
ATOM   1011 N NE2 . GLN   A 1 317 ? -19.454 74.379  102.127 1.00 65.27  ?  298 GLN   A NE2 1 
ATOM   1012 N N   . SER   A 1 318 ? -17.735 69.648  105.787 1.00 76.10  ?  299 SER   A N   1 
ATOM   1013 C CA  . SER   A 1 318 ? -18.349 68.617  106.632 1.00 69.62  ?  299 SER   A CA  1 
ATOM   1014 C C   . SER   A 1 318 ? -17.878 68.691  108.083 1.00 68.79  ?  299 SER   A C   1 
ATOM   1015 O O   . SER   A 1 318 ? -18.629 68.356  109.002 1.00 71.51  ?  299 SER   A O   1 
ATOM   1016 C CB  . SER   A 1 318 ? -18.036 67.231  106.033 1.00 73.45  ?  299 SER   A CB  1 
ATOM   1017 O OG  . SER   A 1 318 ? -18.469 66.126  106.823 1.00 80.92  ?  299 SER   A OG  1 
ATOM   1018 N N   . PHE   A 1 319 ? -16.644 69.119  108.314 1.00 68.90  ?  300 PHE   A N   1 
ATOM   1019 C CA  . PHE   A 1 319 ? -16.053 69.092  109.643 1.00 68.30  ?  300 PHE   A CA  1 
ATOM   1020 C C   . PHE   A 1 319 ? -16.202 70.416  110.373 1.00 75.43  ?  300 PHE   A C   1 
ATOM   1021 O O   . PHE   A 1 319 ? -15.700 70.555  111.494 1.00 70.75  ?  300 PHE   A O   1 
ATOM   1022 C CB  . PHE   A 1 319 ? -14.569 68.746  109.559 1.00 66.52  ?  300 PHE   A CB  1 
ATOM   1023 C CG  . PHE   A 1 319 ? -14.284 67.381  109.040 1.00 66.53  ?  300 PHE   A CG  1 
ATOM   1024 C CD1 . PHE   A 1 319 ? -15.306 66.467  108.829 1.00 70.18  ?  300 PHE   A CD1 1 
ATOM   1025 C CD2 . PHE   A 1 319 ? -12.977 67.007  108.752 1.00 65.88  ?  300 PHE   A CD2 1 
ATOM   1026 C CE1 . PHE   A 1 319 ? -15.032 65.199  108.338 1.00 67.72  ?  300 PHE   A CE1 1 
ATOM   1027 C CE2 . PHE   A 1 319 ? -12.692 65.748  108.273 1.00 65.36  ?  300 PHE   A CE2 1 
ATOM   1028 C CZ  . PHE   A 1 319 ? -13.725 64.836  108.068 1.00 67.22  ?  300 PHE   A CZ  1 
ATOM   1029 N N   . GLY   A 1 320 ? -16.846 71.396  109.752 1.00 75.35  ?  301 GLY   A N   1 
ATOM   1030 C CA  . GLY   A 1 320 ? -17.006 72.690  110.368 1.00 67.47  ?  301 GLY   A CA  1 
ATOM   1031 C C   . GLY   A 1 320 ? -15.856 73.641  110.127 1.00 74.84  ?  301 GLY   A C   1 
ATOM   1032 O O   . GLY   A 1 320 ? -15.527 74.441  111.008 1.00 84.06  ?  301 GLY   A O   1 
ATOM   1033 N N   . MET   A 1 321 ? -15.216 73.581  108.968 1.00 72.87  ?  302 MET   A N   1 
ATOM   1034 C CA  . MET   A 1 321 ? -14.207 74.579  108.667 1.00 68.70  ?  302 MET   A CA  1 
ATOM   1035 C C   . MET   A 1 321 ? -14.687 75.480  107.549 1.00 69.37  ?  302 MET   A C   1 
ATOM   1036 O O   . MET   A 1 321 ? -15.657 75.172  106.848 1.00 70.67  ?  302 MET   A O   1 
ATOM   1037 C CB  . MET   A 1 321 ? -12.859 73.950  108.315 1.00 63.62  ?  302 MET   A CB  1 
ATOM   1038 C CG  . MET   A 1 321 ? -12.314 73.123  109.457 1.00 69.60  ?  302 MET   A CG  1 
ATOM   1039 S SD  . MET   A 1 321 ? -10.626 72.541  109.219 1.00 74.09  ?  302 MET   A SD  1 
ATOM   1040 C CE  . MET   A 1 321 ? -9.674  74.060  109.138 1.00 61.78  ?  302 MET   A CE  1 
ATOM   1041 N N   . ASP   A 1 322 ? -14.024 76.628  107.436 1.00 64.61  ?  303 ASP   A N   1 
ATOM   1042 C CA  . ASP   A 1 322 ? -14.289 77.564  106.357 1.00 72.77  ?  303 ASP   A CA  1 
ATOM   1043 C C   . ASP   A 1 322 ? -13.342 77.200  105.221 1.00 70.50  ?  303 ASP   A C   1 
ATOM   1044 O O   . ASP   A 1 322 ? -12.115 77.195  105.401 1.00 66.00  ?  303 ASP   A O   1 
ATOM   1045 C CB  . ASP   A 1 322 ? -14.107 79.015  106.825 1.00 70.45  ?  303 ASP   A CB  1 
ATOM   1046 C CG  . ASP   A 1 322 ? -14.556 80.068  105.774 1.00 84.73  ?  303 ASP   A CG  1 
ATOM   1047 O OD1 . ASP   A 1 322 ? -14.730 79.749  104.559 1.00 92.59  ?  303 ASP   A OD1 1 
ATOM   1048 O OD2 . ASP   A 1 322 ? -14.741 81.243  106.172 1.00 91.89  ?  303 ASP   A OD2 1 
ATOM   1049 N N   . VAL   A 1 323 ? -13.904 76.865  104.064 1.00 63.97  ?  304 VAL   A N   1 
ATOM   1050 C CA  . VAL   A 1 323 ? -13.107 76.382  102.947 1.00 64.84  ?  304 VAL   A CA  1 
ATOM   1051 C C   . VAL   A 1 323 ? -13.411 77.207  101.712 1.00 60.38  ?  304 VAL   A C   1 
ATOM   1052 O O   . VAL   A 1 323 ? -14.577 77.413  101.363 1.00 63.67  ?  304 VAL   A O   1 
ATOM   1053 C CB  . VAL   A 1 323 ? -13.372 74.896  102.658 1.00 58.91  ?  304 VAL   A CB  1 
ATOM   1054 C CG1 . VAL   A 1 323 ? -12.385 74.405  101.660 1.00 61.48  ?  304 VAL   A CG1 1 
ATOM   1055 C CG2 . VAL   A 1 323 ? -13.271 74.090  103.931 1.00 64.80  ?  304 VAL   A CG2 1 
ATOM   1056 N N   . THR   A 1 324 ? -12.364 77.633  101.026 1.00 58.73  ?  305 THR   A N   1 
ATOM   1057 C CA  . THR   A 1 324 ? -12.505 78.274  99.733  1.00 59.79  ?  305 THR   A CA  1 
ATOM   1058 C C   . THR   A 1 324 ? -11.531 77.615  98.763  1.00 61.27  ?  305 THR   A C   1 
ATOM   1059 O O   . THR   A 1 324 ? -10.366 77.374  99.111  1.00 57.80  ?  305 THR   A O   1 
ATOM   1060 C CB  . THR   A 1 324 ? -12.271 79.793  99.861  1.00 60.52  ?  305 THR   A CB  1 
ATOM   1061 O OG1 . THR   A 1 324 ? -13.388 80.375  100.545 1.00 69.86  ?  305 THR   A OG1 1 
ATOM   1062 C CG2 . THR   A 1 324 ? -12.109 80.478  98.496  1.00 57.84  ?  305 THR   A CG2 1 
ATOM   1063 N N   . LEU   A 1 325 ? -12.022 77.301  97.560  1.00 59.87  ?  306 LEU   A N   1 
ATOM   1064 C CA  . LEU   A 1 325 ? -11.212 76.728  96.495  1.00 61.16  ?  306 LEU   A CA  1 
ATOM   1065 C C   . LEU   A 1 325 ? -10.927 77.789  95.454  1.00 55.12  ?  306 LEU   A C   1 
ATOM   1066 O O   . LEU   A 1 325 ? -11.833 78.518  95.049  1.00 57.88  ?  306 LEU   A O   1 
ATOM   1067 C CB  . LEU   A 1 325 ? -11.912 75.547  95.815  1.00 58.77  ?  306 LEU   A CB  1 
ATOM   1068 C CG  . LEU   A 1 325 ? -12.256 74.342  96.679  1.00 54.82  ?  306 LEU   A CG  1 
ATOM   1069 C CD1 . LEU   A 1 325 ? -13.639 74.546  97.261  1.00 60.31  ?  306 LEU   A CD1 1 
ATOM   1070 C CD2 . LEU   A 1 325 ? -12.230 73.086  95.859  1.00 51.88  ?  306 LEU   A CD2 1 
ATOM   1071 N N   . LEU   A 1 326 ? -9.673  77.852  95.008  1.00 53.60  ?  307 LEU   A N   1 
ATOM   1072 C CA  . LEU   A 1 326 ? -9.272  78.695  93.892  1.00 53.42  ?  307 LEU   A CA  1 
ATOM   1073 C C   . LEU   A 1 326 ? -8.999  77.817  92.681  1.00 60.14  ?  307 LEU   A C   1 
ATOM   1074 O O   . LEU   A 1 326 ? -8.290  76.812  92.786  1.00 60.54  ?  307 LEU   A O   1 
ATOM   1075 C CB  . LEU   A 1 326 ? -8.032  79.519  94.239  1.00 52.74  ?  307 LEU   A CB  1 
ATOM   1076 C CG  . LEU   A 1 326 ? -8.035  80.171  95.631  1.00 59.42  ?  307 LEU   A CG  1 
ATOM   1077 C CD1 . LEU   A 1 326 ? -6.854  81.111  95.800  1.00 47.65  ?  307 LEU   A CD1 1 
ATOM   1078 C CD2 . LEU   A 1 326 ? -9.351  80.896  95.985  1.00 57.10  ?  307 LEU   A CD2 1 
ATOM   1079 N N   . GLU   A 1 327 ? -9.547  78.204  91.534  1.00 62.57  ?  308 GLU   A N   1 
ATOM   1080 C CA  . GLU   A 1 327 ? -9.491  77.396  90.322  1.00 58.82  ?  308 GLU   A CA  1 
ATOM   1081 C C   . GLU   A 1 327 ? -9.110  78.281  89.152  1.00 60.45  ?  308 GLU   A C   1 
ATOM   1082 O O   . GLU   A 1 327 ? -9.797  79.270  88.875  1.00 63.58  ?  308 GLU   A O   1 
ATOM   1083 C CB  . GLU   A 1 327 ? -10.833 76.703  90.062  1.00 60.28  ?  308 GLU   A CB  1 
ATOM   1084 C CG  . GLU   A 1 327 ? -10.880 75.920  88.753  1.00 63.10  ?  308 GLU   A CG  1 
ATOM   1085 C CD  . GLU   A 1 327 ? -9.750  74.878  88.628  1.00 63.12  ?  308 GLU   A CD  1 
ATOM   1086 O OE1 . GLU   A 1 327 ? -8.952  75.013  87.662  1.00 57.14  ?  308 GLU   A OE1 1 
ATOM   1087 O OE2 . GLU   A 1 327 ? -9.628  73.972  89.516  1.00 58.34  ?  308 GLU   A OE2 1 
ATOM   1088 N N   . ALA   A 1 328 ? -8.009  77.933  88.480  1.00 57.53  ?  309 ALA   A N   1 
ATOM   1089 C CA  . ALA   A 1 328 ? -7.573  78.707  87.325  1.00 53.49  ?  309 ALA   A CA  1 
ATOM   1090 C C   . ALA   A 1 328 ? -8.606  78.639  86.207  1.00 61.82  ?  309 ALA   A C   1 
ATOM   1091 O O   . ALA   A 1 328 ? -8.899  79.650  85.554  1.00 63.82  ?  309 ALA   A O   1 
ATOM   1092 C CB  . ALA   A 1 328 ? -6.209  78.201  86.845  1.00 48.38  ?  309 ALA   A CB  1 
ATOM   1093 N N   . ARG   A 1 329 ? -9.186  77.457  85.992  1.00 66.08  ?  310 ARG   A N   1 
ATOM   1094 C CA  . ARG   A 1 329 ? -10.099 77.236  84.883  1.00 66.33  ?  310 ARG   A CA  1 
ATOM   1095 C C   . ARG   A 1 329 ? -11.429 77.944  85.129  1.00 70.07  ?  310 ARG   A C   1 
ATOM   1096 O O   . ARG   A 1 329 ? -11.739 78.390  86.242  1.00 69.68  ?  310 ARG   A O   1 
ATOM   1097 C CB  . ARG   A 1 329 ? -10.357 75.743  84.681  1.00 63.62  ?  310 ARG   A CB  1 
ATOM   1098 C CG  . ARG   A 1 329 ? -9.154  74.966  84.167  1.00 66.62  ?  310 ARG   A CG  1 
ATOM   1099 C CD  . ARG   A 1 329 ? -9.571  73.554  83.748  1.00 64.72  ?  310 ARG   A CD  1 
ATOM   1100 N NE  . ARG   A 1 329 ? -8.486  72.611  83.971  1.00 62.11  ?  310 ARG   A NE  1 
ATOM   1101 C CZ  . ARG   A 1 329 ? -7.551  72.331  83.075  1.00 58.45  ?  310 ARG   A CZ  1 
ATOM   1102 N NH1 . ARG   A 1 329 ? -7.587  72.902  81.882  1.00 58.55  ?  310 ARG   A NH1 1 
ATOM   1103 N NH2 . ARG   A 1 329 ? -6.587  71.474  83.379  1.00 61.90  ?  310 ARG   A NH2 1 
ATOM   1104 N N   . ASP   A 1 330 ? -12.225 78.036  84.059  1.00 71.44  ?  311 ASP   A N   1 
ATOM   1105 C CA  . ASP   A 1 330 ? -13.624 78.424  84.150  1.00 66.00  ?  311 ASP   A CA  1 
ATOM   1106 C C   . ASP   A 1 330 ? -14.546 77.239  84.450  1.00 64.22  ?  311 ASP   A C   1 
ATOM   1107 O O   . ASP   A 1 330 ? -15.739 77.312  84.138  1.00 63.54  ?  311 ASP   A O   1 
ATOM   1108 C CB  . ASP   A 1 330 ? -14.062 79.124  82.864  1.00 65.79  ?  311 ASP   A CB  1 
ATOM   1109 C CG  . ASP   A 1 330 ? -13.677 78.335  81.597  1.00 84.69  ?  311 ASP   A CG  1 
ATOM   1110 O OD1 . ASP   A 1 330 ? -13.024 77.271  81.760  1.00 77.74  ?  311 ASP   A OD1 1 
ATOM   1111 O OD2 . ASP   A 1 330 ? -14.017 78.781  80.450  1.00 81.01  ?  311 ASP   A OD2 1 
ATOM   1112 N N   . ARG   A 1 331 ? -14.031 76.164  85.057  1.00 59.67  ?  312 ARG   A N   1 
ATOM   1113 C CA  . ARG   A 1 331 ? -14.868 75.003  85.350  1.00 63.43  ?  312 ARG   A CA  1 
ATOM   1114 C C   . ARG   A 1 331 ? -14.213 74.155  86.425  1.00 63.70  ?  312 ARG   A C   1 
ATOM   1115 O O   . ARG   A 1 331 ? -12.986 74.163  86.578  1.00 70.43  ?  312 ARG   A O   1 
ATOM   1116 C CB  . ARG   A 1 331 ? -15.092 74.125  84.116  1.00 63.72  ?  312 ARG   A CB  1 
ATOM   1117 C CG  . ARG   A 1 331 ? -13.799 73.698  83.473  1.00 61.55  ?  312 ARG   A CG  1 
ATOM   1118 C CD  . ARG   A 1 331 ? -13.986 72.710  82.343  1.00 61.68  ?  312 ARG   A CD  1 
ATOM   1119 N NE  . ARG   A 1 331 ? -12.690 72.198  81.915  1.00 61.16  ?  312 ARG   A NE  1 
ATOM   1120 C CZ  . ARG   A 1 331 ? -12.064 71.211  82.544  1.00 60.52  ?  312 ARG   A CZ  1 
ATOM   1121 N NH1 . ARG   A 1 331 ? -12.654 70.639  83.591  1.00 58.66  ?  312 ARG   A NH1 1 
ATOM   1122 N NH2 . ARG   A 1 331 ? -10.868 70.788  82.131  1.00 57.52  ?  312 ARG   A NH2 1 
ATOM   1123 N N   . VAL   A 1 332 ? -15.036 73.381  87.132  1.00 56.69  ?  313 VAL   A N   1 
ATOM   1124 C CA  . VAL   A 1 332 ? -14.505 72.400  88.071  1.00 63.11  ?  313 VAL   A CA  1 
ATOM   1125 C C   . VAL   A 1 332 ? -14.017 71.167  87.309  1.00 64.22  ?  313 VAL   A C   1 
ATOM   1126 O O   . VAL   A 1 332 ? -14.046 71.134  86.075  1.00 64.63  ?  313 VAL   A O   1 
ATOM   1127 C CB  . VAL   A 1 332 ? -15.563 72.020  89.115  1.00 58.02  ?  313 VAL   A CB  1 
ATOM   1128 C CG1 . VAL   A 1 332 ? -15.943 73.231  89.892  1.00 55.67  ?  313 VAL   A CG1 1 
ATOM   1129 C CG2 . VAL   A 1 332 ? -16.774 71.442  88.434  1.00 61.71  ?  313 VAL   A CG2 1 
ATOM   1130 N N   . GLY   A 1 333 ? -13.543 70.150  88.032  1.00 64.36  ?  314 GLY   A N   1 
ATOM   1131 C CA  . GLY   A 1 333 ? -13.223 68.869  87.448  1.00 57.72  ?  314 GLY   A CA  1 
ATOM   1132 C C   . GLY   A 1 333 ? -11.772 68.650  87.068  1.00 54.75  ?  314 GLY   A C   1 
ATOM   1133 O O   . GLY   A 1 333 ? -11.289 67.519  87.144  1.00 65.56  ?  314 GLY   A O   1 
ATOM   1134 N N   . GLY   A 1 334 ? -11.065 69.679  86.660  1.00 60.06  ?  315 GLY   A N   1 
ATOM   1135 C CA  . GLY   A 1 334 ? -9.657  69.476  86.391  1.00 59.71  ?  315 GLY   A CA  1 
ATOM   1136 C C   . GLY   A 1 334 ? -9.478  68.590  85.184  1.00 56.76  ?  315 GLY   A C   1 
ATOM   1137 O O   . GLY   A 1 334 ? -10.066 68.814  84.117  1.00 57.36  ?  315 GLY   A O   1 
ATOM   1138 N N   . ARG   A 1 335 ? -8.655  67.560  85.360  1.00 61.50  ?  316 ARG   A N   1 
ATOM   1139 C CA  . ARG   A 1 335 ? -8.407  66.532  84.353  1.00 52.97  ?  316 ARG   A CA  1 
ATOM   1140 C C   . ARG   A 1 335 ? -9.585  65.567  84.188  1.00 58.75  ?  316 ARG   A C   1 
ATOM   1141 O O   . ARG   A 1 335 ? -9.472  64.591  83.442  1.00 62.77  ?  316 ARG   A O   1 
ATOM   1142 C CB  . ARG   A 1 335 ? -7.133  65.782  84.725  1.00 46.97  ?  316 ARG   A CB  1 
ATOM   1143 C CG  . ARG   A 1 335 ? -5.902  66.460  84.210  1.00 40.66  ?  316 ARG   A CG  1 
ATOM   1144 C CD  . ARG   A 1 335 ? -4.676  65.843  84.833  1.00 46.97  ?  316 ARG   A CD  1 
ATOM   1145 N NE  . ARG   A 1 335 ? -4.528  66.127  86.258  1.00 48.56  ?  316 ARG   A NE  1 
ATOM   1146 C CZ  . ARG   A 1 335 ? -3.525  65.674  87.008  1.00 54.63  ?  316 ARG   A CZ  1 
ATOM   1147 N NH1 . ARG   A 1 335 ? -2.592  64.884  86.482  1.00 56.71  ?  316 ARG   A NH1 1 
ATOM   1148 N NH2 . ARG   A 1 335 ? -3.458  65.994  88.295  1.00 62.64  ?  316 ARG   A NH2 1 
ATOM   1149 N N   . VAL   A 1 336 ? -10.699 65.796  84.882  1.00 60.58  ?  317 VAL   A N   1 
ATOM   1150 C CA  . VAL   A 1 336 ? -11.995 65.263  84.470  1.00 53.54  ?  317 VAL   A CA  1 
ATOM   1151 C C   . VAL   A 1 336 ? -12.629 66.348  83.602  1.00 63.39  ?  317 VAL   A C   1 
ATOM   1152 O O   . VAL   A 1 336 ? -13.219 67.319  84.080  1.00 67.30  ?  317 VAL   A O   1 
ATOM   1153 C CB  . VAL   A 1 336 ? -12.861 64.879  85.654  1.00 51.75  ?  317 VAL   A CB  1 
ATOM   1154 C CG1 . VAL   A 1 336 ? -14.263 64.581  85.178  1.00 56.44  ?  317 VAL   A CG1 1 
ATOM   1155 C CG2 . VAL   A 1 336 ? -12.241 63.688  86.364  1.00 54.45  ?  317 VAL   A CG2 1 
ATOM   1156 N N   . ALA   A 1 337 ? -12.447 66.207  82.304  1.00 65.85  ?  318 ALA   A N   1 
ATOM   1157 C CA  . ALA   A 1 337 ? -13.029 67.084  81.310  1.00 63.32  ?  318 ALA   A CA  1 
ATOM   1158 C C   . ALA   A 1 337 ? -14.065 66.296  80.523  1.00 73.28  ?  318 ALA   A C   1 
ATOM   1159 O O   . ALA   A 1 337 ? -13.897 65.094  80.291  1.00 82.18  ?  318 ALA   A O   1 
ATOM   1160 C CB  . ALA   A 1 337 ? -11.947 67.620  80.375  1.00 59.99  ?  318 ALA   A CB  1 
ATOM   1161 N N   . THR   A 1 338 ? -15.137 66.966  80.127  1.00 71.15  ?  319 THR   A N   1 
ATOM   1162 C CA  . THR   A 1 338 ? -16.195 66.352  79.347  1.00 68.73  ?  319 THR   A CA  1 
ATOM   1163 C C   . THR   A 1 338 ? -16.596 67.307  78.241  1.00 75.67  ?  319 THR   A C   1 
ATOM   1164 O O   . THR   A 1 338 ? -16.847 68.486  78.499  1.00 76.32  ?  319 THR   A O   1 
ATOM   1165 C CB  . THR   A 1 338 ? -17.401 66.027  80.206  1.00 70.17  ?  319 THR   A CB  1 
ATOM   1166 O OG1 . THR   A 1 338 ? -17.078 64.946  81.079  1.00 73.84  ?  319 THR   A OG1 1 
ATOM   1167 C CG2 . THR   A 1 338 ? -18.551 65.624  79.352  1.00 74.93  ?  319 THR   A CG2 1 
ATOM   1168 N N   . PHE   A 1 339 ? -16.639 66.798  77.012  1.00 84.79  ?  320 PHE   A N   1 
ATOM   1169 C CA  . PHE   A 1 339 ? -17.130 67.560  75.876  1.00 80.61  ?  320 PHE   A CA  1 
ATOM   1170 C C   . PHE   A 1 339 ? -18.645 67.427  75.820  1.00 83.08  ?  320 PHE   A C   1 
ATOM   1171 O O   . PHE   A 1 339 ? -19.181 66.326  76.008  1.00 80.45  ?  320 PHE   A O   1 
ATOM   1172 C CB  . PHE   A 1 339 ? -16.498 67.064  74.577  1.00 83.62  ?  320 PHE   A CB  1 
ATOM   1173 C CG  . PHE   A 1 339 ? -17.014 67.764  73.353  1.00 89.41  ?  320 PHE   A CG  1 
ATOM   1174 C CD1 . PHE   A 1 339 ? -16.684 69.089  73.110  1.00 86.50  ?  320 PHE   A CD1 1 
ATOM   1175 C CD2 . PHE   A 1 339 ? -17.842 67.105  72.458  1.00 85.29  ?  320 PHE   A CD2 1 
ATOM   1176 C CE1 . PHE   A 1 339 ? -17.166 69.745  71.996  1.00 90.91  ?  320 PHE   A CE1 1 
ATOM   1177 C CE2 . PHE   A 1 339 ? -18.323 67.752  71.346  1.00 91.73  ?  320 PHE   A CE2 1 
ATOM   1178 C CZ  . PHE   A 1 339 ? -17.981 69.079  71.109  1.00 93.59  ?  320 PHE   A CZ  1 
ATOM   1179 N N   . ARG   A 1 340 ? -19.330 68.552  75.597  1.00 78.38  ?  321 ARG   A N   1 
ATOM   1180 C CA  . ARG   A 1 340 ? -20.777 68.565  75.409  1.00 76.66  ?  321 ARG   A CA  1 
ATOM   1181 C C   . ARG   A 1 340 ? -21.134 69.549  74.305  1.00 88.58  ?  321 ARG   A C   1 
ATOM   1182 O O   . ARG   A 1 340 ? -20.785 70.734  74.370  1.00 91.01  ?  321 ARG   A O   1 
ATOM   1183 C CB  . ARG   A 1 340 ? -21.513 68.917  76.701  1.00 68.72  ?  321 ARG   A CB  1 
ATOM   1184 C CG  . ARG   A 1 340 ? -21.540 67.797  77.713  1.00 72.95  ?  321 ARG   A CG  1 
ATOM   1185 C CD  . ARG   A 1 340 ? -21.760 68.309  79.135  1.00 75.31  ?  321 ARG   A CD  1 
ATOM   1186 N NE  . ARG   A 1 340 ? -21.487 67.284  80.137  1.00 76.19  ?  321 ARG   A NE  1 
ATOM   1187 C CZ  . ARG   A 1 340 ? -22.195 66.164  80.285  1.00 88.01  ?  321 ARG   A CZ  1 
ATOM   1188 N NH1 . ARG   A 1 340 ? -23.253 65.938  79.503  1.00 92.55  ?  321 ARG   A NH1 1 
ATOM   1189 N NH2 . ARG   A 1 340 ? -21.853 65.269  81.221  1.00 82.69  ?  321 ARG   A NH2 1 
ATOM   1190 N N   . LYS   A 1 341 ? -21.808 69.040  73.280  1.00 94.99  ?  322 LYS   A N   1 
ATOM   1191 C CA  . LYS   A 1 341 ? -22.423 69.865  72.246  1.00 96.98  ?  322 LYS   A CA  1 
ATOM   1192 C C   . LYS   A 1 341 ? -23.598 69.056  71.717  1.00 99.11  ?  322 LYS   A C   1 
ATOM   1193 O O   . LYS   A 1 341 ? -23.417 67.913  71.285  1.00 99.78  ?  322 LYS   A O   1 
ATOM   1194 C CB  . LYS   A 1 341 ? -21.423 70.226  71.139  1.00 89.23  ?  322 LYS   A CB  1 
ATOM   1195 C CG  . LYS   A 1 341 ? -21.715 71.546  70.437  1.00 94.95  ?  322 LYS   A CG  1 
ATOM   1196 C CD  . LYS   A 1 341 ? -20.655 71.895  69.384  1.00 96.81  ?  322 LYS   A CD  1 
ATOM   1197 C CE  . LYS   A 1 341 ? -20.587 73.405  69.127  1.00 104.53 ?  322 LYS   A CE  1 
ATOM   1198 N NZ  . LYS   A 1 341 ? -20.078 73.786  67.760  1.00 104.23 ?  322 LYS   A NZ  1 
ATOM   1199 N N   . GLY   A 1 342 ? -24.798 69.624  71.797  1.00 94.59  ?  323 GLY   A N   1 
ATOM   1200 C CA  . GLY   A 1 342 ? -25.987 68.827  71.561  1.00 95.68  ?  323 GLY   A CA  1 
ATOM   1201 C C   . GLY   A 1 342 ? -25.997 67.616  72.469  1.00 98.83  ?  323 GLY   A C   1 
ATOM   1202 O O   . GLY   A 1 342 ? -25.668 67.704  73.656  1.00 96.41  ?  323 GLY   A O   1 
ATOM   1203 N N   . ASN   A 1 343 ? -26.360 66.461  71.899  1.00 102.19 ?  324 ASN   A N   1 
ATOM   1204 C CA  . ASN   A 1 343 ? -26.331 65.177  72.593  1.00 98.01  ?  324 ASN   A CA  1 
ATOM   1205 C C   . ASN   A 1 343 ? -25.000 64.463  72.428  1.00 100.06 ?  324 ASN   A C   1 
ATOM   1206 O O   . ASN   A 1 343 ? -24.860 63.311  72.868  1.00 96.98  ?  324 ASN   A O   1 
ATOM   1207 C CB  . ASN   A 1 343 ? -27.464 64.288  72.089  1.00 104.53 ?  324 ASN   A CB  1 
ATOM   1208 C CG  . ASN   A 1 343 ? -28.731 65.074  71.828  1.00 113.85 ?  324 ASN   A CG  1 
ATOM   1209 O OD1 . ASN   A 1 343 ? -29.118 65.939  72.627  1.00 110.43 ?  324 ASN   A OD1 1 
ATOM   1210 N ND2 . ASN   A 1 343 ? -29.354 64.824  70.674  1.00 117.39 ?  324 ASN   A ND2 1 
ATOM   1211 N N   . TYR   A 1 344 ? -24.033 65.116  71.789  1.00 99.71  ?  325 TYR   A N   1 
ATOM   1212 C CA  . TYR   A 1 344 ? -22.665 64.623  71.790  1.00 102.66 ?  325 TYR   A CA  1 
ATOM   1213 C C   . TYR   A 1 344 ? -22.045 64.809  73.173  1.00 98.18  ?  325 TYR   A C   1 
ATOM   1214 O O   . TYR   A 1 344 ? -22.073 65.909  73.737  1.00 93.16  ?  325 TYR   A O   1 
ATOM   1215 C CB  . TYR   A 1 344 ? -21.844 65.360  70.738  1.00 102.45 ?  325 TYR   A CB  1 
ATOM   1216 C CG  . TYR   A 1 344 ? -22.263 65.095  69.308  1.00 108.53 ?  325 TYR   A CG  1 
ATOM   1217 C CD1 . TYR   A 1 344 ? -22.890 63.904  68.946  1.00 106.89 ?  325 TYR   A CD1 1 
ATOM   1218 C CD2 . TYR   A 1 344 ? -22.042 66.052  68.317  1.00 116.14 ?  325 TYR   A CD2 1 
ATOM   1219 C CE1 . TYR   A 1 344 ? -23.270 63.670  67.631  1.00 105.70 ?  325 TYR   A CE1 1 
ATOM   1220 C CE2 . TYR   A 1 344 ? -22.421 65.829  67.000  1.00 114.53 ?  325 TYR   A CE2 1 
ATOM   1221 C CZ  . TYR   A 1 344 ? -23.031 64.636  66.661  1.00 110.76 ?  325 TYR   A CZ  1 
ATOM   1222 O OH  . TYR   A 1 344 ? -23.397 64.432  65.345  1.00 113.87 ?  325 TYR   A OH  1 
ATOM   1223 N N   . VAL   A 1 345 ? -21.489 63.725  73.714  1.00 96.61  ?  326 VAL   A N   1 
ATOM   1224 C CA  . VAL   A 1 345 ? -20.864 63.673  75.031  1.00 84.98  ?  326 VAL   A CA  1 
ATOM   1225 C C   . VAL   A 1 345 ? -19.634 62.782  74.968  1.00 88.56  ?  326 VAL   A C   1 
ATOM   1226 O O   . VAL   A 1 345 ? -19.735 61.605  74.614  1.00 97.44  ?  326 VAL   A O   1 
ATOM   1227 C CB  . VAL   A 1 345 ? -21.864 63.163  76.081  1.00 85.11  ?  326 VAL   A CB  1 
ATOM   1228 C CG1 . VAL   A 1 345 ? -21.159 62.848  77.390  1.00 89.24  ?  326 VAL   A CG1 1 
ATOM   1229 C CG2 . VAL   A 1 345 ? -22.954 64.203  76.301  1.00 90.55  ?  326 VAL   A CG2 1 
ATOM   1230 N N   . ALA   A 1 346 ? -18.471 63.325  75.317  1.00 87.40  ?  327 ALA   A N   1 
ATOM   1231 C CA  . ALA   A 1 346 ? -17.225 62.565  75.213  1.00 86.24  ?  327 ALA   A CA  1 
ATOM   1232 C C   . ALA   A 1 346 ? -16.191 63.133  76.179  1.00 81.79  ?  327 ALA   A C   1 
ATOM   1233 O O   . ALA   A 1 346 ? -15.881 64.328  76.113  1.00 83.25  ?  327 ALA   A O   1 
ATOM   1234 C CB  . ALA   A 1 346 ? -16.706 62.605  73.776  1.00 80.21  ?  327 ALA   A CB  1 
ATOM   1235 N N   . ASP   A 1 347 ? -15.652 62.284  77.058  1.00 73.01  ?  328 ASP   A N   1 
ATOM   1236 C CA  . ASP   A 1 347 ? -14.614 62.704  77.996  1.00 72.71  ?  328 ASP   A CA  1 
ATOM   1237 C C   . ASP   A 1 347 ? -13.283 62.937  77.291  1.00 72.99  ?  328 ASP   A C   1 
ATOM   1238 O O   . ASP   A 1 347 ? -12.766 62.052  76.615  1.00 73.32  ?  328 ASP   A O   1 
ATOM   1239 C CB  . ASP   A 1 347 ? -14.413 61.647  79.076  1.00 74.32  ?  328 ASP   A CB  1 
ATOM   1240 C CG  . ASP   A 1 347 ? -15.559 61.584  80.062  1.00 82.78  ?  328 ASP   A CG  1 
ATOM   1241 O OD1 . ASP   A 1 347 ? -15.865 62.619  80.695  1.00 77.67  ?  328 ASP   A OD1 1 
ATOM   1242 O OD2 . ASP   A 1 347 ? -16.169 60.488  80.182  1.00 88.22  ?  328 ASP   A OD2 1 
ATOM   1243 N N   . LEU   A 1 348 ? -12.693 64.110  77.491  1.00 76.53  ?  329 LEU   A N   1 
ATOM   1244 C CA  . LEU   A 1 348 ? -11.316 64.307  77.074  1.00 67.48  ?  329 LEU   A CA  1 
ATOM   1245 C C   . LEU   A 1 348 ? -10.318 63.887  78.149  1.00 69.61  ?  329 LEU   A C   1 
ATOM   1246 O O   . LEU   A 1 348 ? -9.112  63.857  77.880  1.00 64.35  ?  329 LEU   A O   1 
ATOM   1247 C CB  . LEU   A 1 348 ? -11.087 65.767  76.717  1.00 71.63  ?  329 LEU   A CB  1 
ATOM   1248 C CG  . LEU   A 1 348 ? -11.548 66.228  75.333  1.00 84.72  ?  329 LEU   A CG  1 
ATOM   1249 C CD1 . LEU   A 1 348 ? -10.798 65.473  74.239  1.00 84.42  ?  329 LEU   A CD1 1 
ATOM   1250 C CD2 . LEU   A 1 348 ? -13.061 66.101  75.158  1.00 82.02  ?  329 LEU   A CD2 1 
ATOM   1251 N N   . GLY   A 1 349 ? -10.800 63.563  79.332  1.00 67.31  ?  330 GLY   A N   1 
ATOM   1252 C CA  . GLY   A 1 349 ? -9.875  63.185  80.402  1.00 62.67  ?  330 GLY   A CA  1 
ATOM   1253 C C   . GLY   A 1 349 ? -10.200 61.825  80.931  1.00 63.86  ?  330 GLY   A C   1 
ATOM   1254 O O   . GLY   A 1 349 ? -10.377 60.957  80.153  1.00 71.16  ?  330 GLY   A O   1 
ATOM   1255 N N   . ALA   A 1 350 ? -10.389 61.693  82.227  1.00 65.63  ?  331 ALA   A N   1 
ATOM   1256 C CA  . ALA   A 1 350 ? -10.669 60.374  82.805  1.00 66.06  ?  331 ALA   A CA  1 
ATOM   1257 C C   . ALA   A 1 350 ? -11.964 59.840  82.215  1.00 70.96  ?  331 ALA   A C   1 
ATOM   1258 O O   . ALA   A 1 350 ? -12.912 60.590  82.073  1.00 74.65  ?  331 ALA   A O   1 
ATOM   1259 C CB  . ALA   A 1 350 ? -10.774 60.512  84.285  1.00 59.93  ?  331 ALA   A CB  1 
ATOM   1260 N N   . MET   A 1 351 ? -11.977 58.572  81.845  1.00 73.20  ?  332 MET   A N   1 
ATOM   1261 C CA  . MET   A 1 351 ? -13.209 58.060  81.227  1.00 74.12  ?  332 MET   A CA  1 
ATOM   1262 C C   . MET   A 1 351 ? -13.564 56.686  81.756  1.00 74.15  ?  332 MET   A C   1 
ATOM   1263 O O   . MET   A 1 351 ? -14.653 56.263  81.511  1.00 77.43  ?  332 MET   A O   1 
ATOM   1264 C CB  . MET   A 1 351 ? -12.957 57.936  79.733  1.00 78.54  ?  332 MET   A CB  1 
ATOM   1265 C CG  . MET   A 1 351 ? -13.877 57.015  79.040  1.00 82.23  ?  332 MET   A CG  1 
ATOM   1266 S SD  . MET   A 1 351 ? -13.717 57.455  77.343  1.00 102.23 ?  332 MET   A SD  1 
ATOM   1267 C CE  . MET   A 1 351 ? -12.092 56.800  76.991  1.00 84.84  ?  332 MET   A CE  1 
ATOM   1268 N N   . VAL   A 1 352 ? -12.686 56.045  82.498  1.00 65.79  ?  333 VAL   A N   1 
ATOM   1269 C CA  . VAL   A 1 352 ? -13.008 54.647  82.869  1.00 71.75  ?  333 VAL   A CA  1 
ATOM   1270 C C   . VAL   A 1 352 ? -12.964 54.444  84.372  1.00 67.24  ?  333 VAL   A C   1 
ATOM   1271 O O   . VAL   A 1 352 ? -12.041 54.904  84.978  1.00 67.30  ?  333 VAL   A O   1 
ATOM   1272 C CB  . VAL   A 1 352 ? -11.990 53.723  82.194  1.00 75.52  ?  333 VAL   A CB  1 
ATOM   1273 C CG1 . VAL   A 1 352 ? -12.155 52.291  82.619  1.00 74.20  ?  333 VAL   A CG1 1 
ATOM   1274 C CG2 . VAL   A 1 352 ? -12.052 53.835  80.694  1.00 68.74  ?  333 VAL   A CG2 1 
ATOM   1275 N N   . VAL   A 1 353 ? -13.946 53.738  84.910  1.00 65.26  ?  334 VAL   A N   1 
ATOM   1276 C CA  . VAL   A 1 353 ? -13.971 53.364  86.344  1.00 61.81  ?  334 VAL   A CA  1 
ATOM   1277 C C   . VAL   A 1 353 ? -13.340 51.985  86.397  1.00 68.36  ?  334 VAL   A C   1 
ATOM   1278 O O   . VAL   A 1 353 ? -13.982 51.035  86.096  1.00 72.72  ?  334 VAL   A O   1 
ATOM   1279 C CB  . VAL   A 1 353 ? -15.405 53.337  86.861  1.00 57.92  ?  334 VAL   A CB  1 
ATOM   1280 C CG1 . VAL   A 1 353 ? -15.459 52.875  88.290  1.00 58.09  ?  334 VAL   A CG1 1 
ATOM   1281 C CG2 . VAL   A 1 353 ? -16.026 54.700  86.734  1.00 62.99  ?  334 VAL   A CG2 1 
ATOM   1282 N N   . THR   A 1 354 ? -12.117 51.902  86.857  1.00 67.16  ?  335 THR   A N   1 
ATOM   1283 C CA  . THR   A 1 354 ? -11.411 50.636  86.731  1.00 63.27  ?  335 THR   A CA  1 
ATOM   1284 C C   . THR   A 1 354 ? -11.852 49.593  87.753  1.00 68.26  ?  335 THR   A C   1 
ATOM   1285 O O   . THR   A 1 354 ? -11.019 49.038  88.487  1.00 70.62  ?  335 THR   A O   1 
ATOM   1286 C CB  . THR   A 1 354 ? -9.907  50.872  86.816  1.00 63.04  ?  335 THR   A CB  1 
ATOM   1287 O OG1 . THR   A 1 354 ? -9.510  51.053  88.181  1.00 70.27  ?  335 THR   A OG1 1 
ATOM   1288 C CG2 . THR   A 1 354 ? -9.551  52.104  86.021  1.00 71.23  ?  335 THR   A CG2 1 
ATOM   1289 N N   . GLY   A 1 355 ? -13.154 49.294  87.793  1.00 63.72  ?  336 GLY   A N   1 
ATOM   1290 C CA  . GLY   A 1 355 ? -13.628 48.161  88.581  1.00 73.29  ?  336 GLY   A CA  1 
ATOM   1291 C C   . GLY   A 1 355 ? -14.086 48.525  89.975  1.00 70.44  ?  336 GLY   A C   1 
ATOM   1292 O O   . GLY   A 1 355 ? -13.388 49.273  90.660  1.00 74.77  ?  336 GLY   A O   1 
ATOM   1293 N N   . LEU   A 1 356 ? -15.242 48.022  90.418  1.00 67.36  ?  337 LEU   A N   1 
ATOM   1294 C CA  . LEU   A 1 356 ? -15.852 48.515  91.655  1.00 67.74  ?  337 LEU   A CA  1 
ATOM   1295 C C   . LEU   A 1 356 ? -15.474 47.717  92.903  1.00 69.06  ?  337 LEU   A C   1 
ATOM   1296 O O   . LEU   A 1 356 ? -15.987 48.013  93.990  1.00 71.51  ?  337 LEU   A O   1 
ATOM   1297 C CB  . LEU   A 1 356 ? -17.377 48.538  91.539  1.00 57.38  ?  337 LEU   A CB  1 
ATOM   1298 C CG  . LEU   A 1 356 ? -18.032 49.024  90.256  1.00 61.16  ?  337 LEU   A CG  1 
ATOM   1299 C CD1 . LEU   A 1 356 ? -19.529 49.147  90.481  1.00 60.94  ?  337 LEU   A CD1 1 
ATOM   1300 C CD2 . LEU   A 1 356 ? -17.455 50.347  89.825  1.00 70.49  ?  337 LEU   A CD2 1 
ATOM   1301 N N   . GLY   A 1 357 ? -14.600 46.728  92.793  1.00 66.24  ?  338 GLY   A N   1 
ATOM   1302 C CA  . GLY   A 1 357 ? -14.266 45.935  93.956  1.00 67.29  ?  338 GLY   A CA  1 
ATOM   1303 C C   . GLY   A 1 357 ? -13.250 46.633  94.823  1.00 72.20  ?  338 GLY   A C   1 
ATOM   1304 O O   . GLY   A 1 357 ? -12.047 46.558  94.550  1.00 75.62  ?  338 GLY   A O   1 
ATOM   1305 N N   . GLY   A 1 358 ? -13.727 47.310  95.871  1.00 76.75  ?  339 GLY   A N   1 
ATOM   1306 C CA  . GLY   A 1 358 ? -12.893 48.138  96.722  1.00 73.67  ?  339 GLY   A CA  1 
ATOM   1307 C C   . GLY   A 1 358 ? -12.686 49.549  96.221  1.00 67.43  ?  339 GLY   A C   1 
ATOM   1308 O O   . GLY   A 1 358 ? -11.859 50.272  96.779  1.00 73.10  ?  339 GLY   A O   1 
ATOM   1309 N N   . ASN   A 1 359 ? -13.398 49.950  95.198  1.00 65.92  ?  340 ASN   A N   1 
ATOM   1310 C CA  . ASN   A 1 359 ? -13.267 51.267  94.606  1.00 68.32  ?  340 ASN   A CA  1 
ATOM   1311 C C   . ASN   A 1 359 ? -14.183 52.241  95.337  1.00 74.10  ?  340 ASN   A C   1 
ATOM   1312 O O   . ASN   A 1 359 ? -15.383 51.971  95.462  1.00 75.33  ?  340 ASN   A O   1 
ATOM   1313 C CB  . ASN   A 1 359 ? -13.631 51.196  93.121  1.00 68.49  ?  340 ASN   A CB  1 
ATOM   1314 C CG  . ASN   A 1 359 ? -13.353 52.485  92.371  1.00 70.40  ?  340 ASN   A CG  1 
ATOM   1315 O OD1 . ASN   A 1 359 ? -13.540 53.577  92.900  1.00 71.34  ?  340 ASN   A OD1 1 
ATOM   1316 N ND2 . ASN   A 1 359 ? -12.931 52.362  91.116  1.00 72.61  ?  340 ASN   A ND2 1 
ATOM   1317 N N   . PRO   A 1 360 ? -13.666 53.377  95.826  1.00 73.55  ?  341 PRO   A N   1 
ATOM   1318 C CA  . PRO   A 1 360 ? -14.555 54.359  96.459  1.00 71.27  ?  341 PRO   A CA  1 
ATOM   1319 C C   . PRO   A 1 360 ? -15.496 55.017  95.476  1.00 69.79  ?  341 PRO   A C   1 
ATOM   1320 O O   . PRO   A 1 360 ? -16.535 55.536  95.903  1.00 71.04  ?  341 PRO   A O   1 
ATOM   1321 C CB  . PRO   A 1 360 ? -13.582 55.369  97.075  1.00 65.91  ?  341 PRO   A CB  1 
ATOM   1322 C CG  . PRO   A 1 360 ? -12.424 55.337  96.161  1.00 68.91  ?  341 PRO   A CG  1 
ATOM   1323 C CD  . PRO   A 1 360 ? -12.288 53.887  95.730  1.00 70.04  ?  341 PRO   A CD  1 
ATOM   1324 N N   . MET   A 1 361 ? -15.183 54.997  94.176  1.00 67.48  ?  342 MET   A N   1 
ATOM   1325 C CA  . MET   A 1 361 ? -16.135 55.497  93.187  1.00 71.15  ?  342 MET   A CA  1 
ATOM   1326 C C   . MET   A 1 361 ? -17.428 54.699  93.193  1.00 72.52  ?  342 MET   A C   1 
ATOM   1327 O O   . MET   A 1 361 ? -18.451 55.204  92.713  1.00 72.02  ?  342 MET   A O   1 
ATOM   1328 C CB  . MET   A 1 361 ? -15.543 55.455  91.784  1.00 67.38  ?  342 MET   A CB  1 
ATOM   1329 C CG  . MET   A 1 361 ? -14.326 56.318  91.599  1.00 68.85  ?  342 MET   A CG  1 
ATOM   1330 S SD  . MET   A 1 361 ? -14.592 58.043  92.019  1.00 71.51  ?  342 MET   A SD  1 
ATOM   1331 C CE  . MET   A 1 361 ? -15.863 58.473  90.826  1.00 71.81  ?  342 MET   A CE  1 
ATOM   1332 N N   . ALA   A 1 362 ? -17.388 53.454  93.684  1.00 68.90  ?  343 ALA   A N   1 
ATOM   1333 C CA  . ALA   A 1 362 ? -18.607 52.680  93.885  1.00 69.07  ?  343 ALA   A CA  1 
ATOM   1334 C C   . ALA   A 1 362 ? -19.589 53.437  94.770  1.00 82.01  ?  343 ALA   A C   1 
ATOM   1335 O O   . ALA   A 1 362 ? -20.752 53.638  94.401  1.00 83.22  ?  343 ALA   A O   1 
ATOM   1336 C CB  . ALA   A 1 362 ? -18.263 51.334  94.509  1.00 68.17  ?  343 ALA   A CB  1 
ATOM   1337 N N   . VAL   A 1 363 ? -19.127 53.865  95.952  1.00 82.99  ?  344 VAL   A N   1 
ATOM   1338 C CA  . VAL   A 1 363 ? -19.942 54.698  96.832  1.00 73.85  ?  344 VAL   A CA  1 
ATOM   1339 C C   . VAL   A 1 363 ? -20.438 55.933  96.099  1.00 76.16  ?  344 VAL   A C   1 
ATOM   1340 O O   . VAL   A 1 363 ? -21.588 56.356  96.258  1.00 80.69  ?  344 VAL   A O   1 
ATOM   1341 C CB  . VAL   A 1 363 ? -19.135 55.090  98.074  1.00 72.87  ?  344 VAL   A CB  1 
ATOM   1342 C CG1 . VAL   A 1 363 ? -19.965 55.995  98.957  1.00 78.71  ?  344 VAL   A CG1 1 
ATOM   1343 C CG2 . VAL   A 1 363 ? -18.686 53.856  98.806  1.00 76.78  ?  344 VAL   A CG2 1 
ATOM   1344 N N   . VAL   A 1 364 ? -19.577 56.540  95.290  1.00 72.35  ?  345 VAL   A N   1 
ATOM   1345 C CA  . VAL   A 1 364 ? -19.992 57.752  94.606  1.00 72.76  ?  345 VAL   A CA  1 
ATOM   1346 C C   . VAL   A 1 364 ? -21.081 57.459  93.590  1.00 74.57  ?  345 VAL   A C   1 
ATOM   1347 O O   . VAL   A 1 364 ? -21.949 58.302  93.344  1.00 78.07  ?  345 VAL   A O   1 
ATOM   1348 C CB  . VAL   A 1 364 ? -18.767 58.422  93.968  1.00 74.35  ?  345 VAL   A CB  1 
ATOM   1349 C CG1 . VAL   A 1 364 ? -19.166 59.717  93.257  1.00 70.40  ?  345 VAL   A CG1 1 
ATOM   1350 C CG2 . VAL   A 1 364 ? -17.707 58.672  95.049  1.00 69.10  ?  345 VAL   A CG2 1 
ATOM   1351 N N   . SER   A 1 365 ? -21.068 56.264  92.994  1.00 85.08  ?  346 SER   A N   1 
ATOM   1352 C CA  . SER   A 1 365 ? -22.031 55.931  91.943  1.00 86.35  ?  346 SER   A CA  1 
ATOM   1353 C C   . SER   A 1 365 ? -23.424 55.710  92.501  1.00 81.90  ?  346 SER   A C   1 
ATOM   1354 O O   . SER   A 1 365 ? -24.416 55.949  91.805  1.00 84.19  ?  346 SER   A O   1 
ATOM   1355 C CB  . SER   A 1 365 ? -21.567 54.691  91.180  1.00 81.42  ?  346 SER   A CB  1 
ATOM   1356 O OG  . SER   A 1 365 ? -21.256 53.639  92.072  1.00 84.17  ?  346 SER   A OG  1 
ATOM   1357 N N   . LYS   A 1 366 ? -23.497 55.402  93.775  1.00 78.06  ?  347 LYS   A N   1 
ATOM   1358 C CA  . LYS   A 1 366 ? -24.841 55.290  94.351  1.00 80.22  ?  347 LYS   A CA  1 
ATOM   1359 C C   . LYS   A 1 366 ? -25.305 56.711  94.670  1.00 85.11  ?  347 LYS   A C   1 
ATOM   1360 O O   . LYS   A 1 366 ? -26.491 56.949  94.654  1.00 87.82  ?  347 LYS   A O   1 
ATOM   1361 C CB  . LYS   A 1 366 ? -24.781 54.342  95.543  1.00 79.80  ?  347 LYS   A CB  1 
ATOM   1362 C CG  . LYS   A 1 366 ? -24.106 53.014  95.249  1.00 81.19  ?  347 LYS   A CG  1 
ATOM   1363 C CD  . LYS   A 1 366 ? -24.166 52.044  96.397  1.00 91.52  ?  347 LYS   A CD  1 
ATOM   1364 C CE  . LYS   A 1 366 ? -23.059 51.012  96.380  1.00 94.26  ?  347 LYS   A CE  1 
ATOM   1365 N NZ  . LYS   A 1 366 ? -22.198 51.069  97.586  1.00 87.04  ?  347 LYS   A NZ  1 
ATOM   1366 N N   . GLN   A 1 367 ? -24.374 57.627  94.903  1.00 83.55  ?  348 GLN   A N   1 
ATOM   1367 C CA  . GLN   A 1 367 ? -24.725 59.020  95.270  1.00 81.21  ?  348 GLN   A CA  1 
ATOM   1368 C C   . GLN   A 1 367 ? -24.963 59.915  94.058  1.00 83.52  ?  348 GLN   A C   1 
ATOM   1369 O O   . GLN   A 1 367 ? -25.578 60.941  94.238  1.00 83.41  ?  348 GLN   A O   1 
ATOM   1370 C CB  . GLN   A 1 367 ? -23.599 59.647  96.083  1.00 76.60  ?  348 GLN   A CB  1 
ATOM   1371 C CG  . GLN   A 1 367 ? -23.307 58.928  97.382  1.00 78.32  ?  348 GLN   A CG  1 
ATOM   1372 C CD  . GLN   A 1 367 ? -22.146 59.532  98.119  1.00 76.69  ?  348 GLN   A CD  1 
ATOM   1373 O OE1 . GLN   A 1 367 ? -21.460 60.403  97.628  1.00 70.91  ?  348 GLN   A OE1 1 
ATOM   1374 N NE2 . GLN   A 1 367 ? -21.923 59.076  99.327  1.00 77.80  ?  348 GLN   A NE2 1 
ATOM   1375 N N   . VAL   A 1 368 ? -24.462 59.572  92.880  1.00 89.72  ?  349 VAL   A N   1 
ATOM   1376 C CA  . VAL   A 1 368 ? -24.638 60.477  91.709  1.00 89.86  ?  349 VAL   A CA  1 
ATOM   1377 C C   . VAL   A 1 368 ? -25.219 59.671  90.564  1.00 98.09  ?  349 VAL   A C   1 
ATOM   1378 O O   . VAL   A 1 368 ? -24.813 58.567  90.409  1.00 98.20  ?  349 VAL   A O   1 
ATOM   1379 C CB  . VAL   A 1 368 ? -23.286 61.031  91.255  1.00 82.76  ?  349 VAL   A CB  1 
ATOM   1380 C CG1 . VAL   A 1 368 ? -23.450 62.175  90.286  1.00 89.45  ?  349 VAL   A CG1 1 
ATOM   1381 C CG2 . VAL   A 1 368 ? -22.435 61.458  92.420  1.00 81.39  ?  349 VAL   A CG2 1 
ATOM   1382 N N   . ASN   A 1 369 ? -25.994 60.266  89.674  1.00 104.19 ?  350 ASN   A N   1 
ATOM   1383 C CA  . ASN   A 1 369 ? -26.550 59.413  88.600  1.00 110.23 ?  350 ASN   A CA  1 
ATOM   1384 C C   . ASN   A 1 369 ? -25.464 59.195  87.557  1.00 110.01 ?  350 ASN   A C   1 
ATOM   1385 O O   . ASN   A 1 369 ? -25.381 59.971  86.607  1.00 111.36 ?  350 ASN   A O   1 
ATOM   1386 C CB  . ASN   A 1 369 ? -27.686 60.121  87.878  1.00 117.68 ?  350 ASN   A CB  1 
ATOM   1387 C CG  . ASN   A 1 369 ? -27.327 61.562  87.593  1.00 128.50 ?  350 ASN   A CG  1 
ATOM   1388 O OD1 . ASN   A 1 369 ? -27.049 62.330  88.511  1.00 119.59 ?  350 ASN   A OD1 1 
ATOM   1389 N ND2 . ASN   A 1 369 ? -27.300 61.926  86.324  1.00 129.28 ?  350 ASN   A ND2 1 
ATOM   1390 N N   . MET   A 1 370 ? -24.661 58.159  87.751  1.00 108.27 ?  351 MET   A N   1 
ATOM   1391 C CA  . MET   A 1 370 ? -23.615 57.840  86.765  1.00 102.93 ?  351 MET   A CA  1 
ATOM   1392 C C   . MET   A 1 370 ? -24.161 56.665  85.968  1.00 111.91 ?  351 MET   A C   1 
ATOM   1393 O O   . MET   A 1 370 ? -24.621 55.706  86.594  1.00 111.52 ?  351 MET   A O   1 
ATOM   1394 C CB  . MET   A 1 370 ? -22.339 57.379  87.464  1.00 102.46 ?  351 MET   A CB  1 
ATOM   1395 C CG  . MET   A 1 370 ? -21.644 58.438  88.269  1.00 100.64 ?  351 MET   A CG  1 
ATOM   1396 S SD  . MET   A 1 370 ? -19.874 58.174  88.327  1.00 89.01  ?  351 MET   A SD  1 
ATOM   1397 C CE  . MET   A 1 370 ? -19.722 57.157  89.778  1.00 76.50  ?  351 MET   A CE  1 
ATOM   1398 N N   . GLU   A 1 371 ? -24.183 56.786  84.645  1.00 108.80 ?  352 GLU   A N   1 
ATOM   1399 C CA  . GLU   A 1 371 ? -24.635 55.676  83.782  1.00 103.67 ?  352 GLU   A CA  1 
ATOM   1400 C C   . GLU   A 1 371 ? -23.389 54.856  83.503  1.00 94.79  ?  352 GLU   A C   1 
ATOM   1401 O O   . GLU   A 1 371 ? -22.634 55.229  82.620  1.00 95.67  ?  352 GLU   A O   1 
ATOM   1402 C CB  . GLU   A 1 371 ? -25.198 56.246  82.490  1.00 110.83 ?  352 GLU   A CB  1 
ATOM   1403 C CG  . GLU   A 1 371 ? -26.552 56.891  82.675  1.00 118.69 ?  352 GLU   A CG  1 
ATOM   1404 C CD  . GLU   A 1 371 ? -27.440 56.732  81.458  1.00 129.00 ?  352 GLU   A CD  1 
ATOM   1405 O OE1 . GLU   A 1 371 ? -28.609 57.172  81.500  1.00 128.46 ?  352 GLU   A OE1 1 
ATOM   1406 O OE2 . GLU   A 1 371 ? -26.954 56.159  80.472  1.00 129.95 ?  352 GLU   A OE2 1 
ATOM   1407 N N   . LEU   A 1 372 ? -23.217 53.779  84.250  1.00 86.04  ?  353 LEU   A N   1 
ATOM   1408 C CA  . LEU   A 1 372 ? -22.002 52.970  84.195  1.00 91.60  ?  353 LEU   A CA  1 
ATOM   1409 C C   . LEU   A 1 372 ? -22.185 51.781  83.242  1.00 92.11  ?  353 LEU   A C   1 
ATOM   1410 O O   . LEU   A 1 372 ? -22.897 50.818  83.560  1.00 86.56  ?  353 LEU   A O   1 
ATOM   1411 C CB  . LEU   A 1 372 ? -21.634 52.498  85.599  1.00 87.94  ?  353 LEU   A CB  1 
ATOM   1412 C CG  . LEU   A 1 372 ? -21.051 53.534  86.553  1.00 82.88  ?  353 LEU   A CG  1 
ATOM   1413 C CD1 . LEU   A 1 372 ? -20.390 52.843  87.709  1.00 78.41  ?  353 LEU   A CD1 1 
ATOM   1414 C CD2 . LEU   A 1 372 ? -20.057 54.397  85.825  1.00 83.20  ?  353 LEU   A CD2 1 
ATOM   1415 N N   . ALA   A 1 373 ? -21.500 51.829  82.094  1.00 93.36  ?  354 ALA   A N   1 
ATOM   1416 C CA  . ALA   A 1 373 ? -21.646 50.862  81.007  1.00 83.36  ?  354 ALA   A CA  1 
ATOM   1417 C C   . ALA   A 1 373 ? -20.386 50.009  80.875  1.00 89.58  ?  354 ALA   A C   1 
ATOM   1418 O O   . ALA   A 1 373 ? -19.290 50.548  80.681  1.00 89.89  ?  354 ALA   A O   1 
ATOM   1419 C CB  . ALA   A 1 373 ? -21.924 51.589  79.695  1.00 85.16  ?  354 ALA   A CB  1 
ATOM   1420 N N   . LYS   A 1 374 ? -20.553 48.682  80.936  1.00 94.64  ?  355 LYS   A N   1 
ATOM   1421 C CA  . LYS   A 1 374 ? -19.432 47.744  80.880  1.00 91.27  ?  355 LYS   A CA  1 
ATOM   1422 C C   . LYS   A 1 374 ? -18.660 47.847  79.562  1.00 87.13  ?  355 LYS   A C   1 
ATOM   1423 O O   . LYS   A 1 374 ? -19.127 48.404  78.562  1.00 90.03  ?  355 LYS   A O   1 
ATOM   1424 C CB  . LYS   A 1 374 ? -19.922 46.310  81.071  1.00 92.86  ?  355 LYS   A CB  1 
ATOM   1425 C CG  . LYS   A 1 374 ? -20.686 46.102  82.366  1.00 101.51 ?  355 LYS   A CG  1 
ATOM   1426 C CD  . LYS   A 1 374 ? -20.660 44.648  82.839  1.00 109.34 ?  355 LYS   A CD  1 
ATOM   1427 C CE  . LYS   A 1 374 ? -22.080 44.068  82.908  1.00 113.66 ?  355 LYS   A CE  1 
ATOM   1428 N NZ  . LYS   A 1 374 ? -22.132 42.730  83.569  1.00 109.80 ?  355 LYS   A NZ  1 
ATOM   1429 N N   . ILE   A 1 375 ? -17.449 47.303  79.580  1.00 83.79  ?  356 ILE   A N   1 
ATOM   1430 C CA  . ILE   A 1 375 ? -16.524 47.383  78.455  1.00 95.66  ?  356 ILE   A CA  1 
ATOM   1431 C C   . ILE   A 1 375 ? -16.310 45.980  77.906  1.00 106.37 ?  356 ILE   A C   1 
ATOM   1432 O O   . ILE   A 1 375 ? -15.844 45.086  78.628  1.00 105.81 ?  356 ILE   A O   1 
ATOM   1433 C CB  . ILE   A 1 375 ? -15.186 48.021  78.858  1.00 97.68  ?  356 ILE   A CB  1 
ATOM   1434 C CG1 . ILE   A 1 375 ? -15.335 49.530  79.068  1.00 92.27  ?  356 ILE   A CG1 1 
ATOM   1435 C CG2 . ILE   A 1 375 ? -14.109 47.703  77.840  1.00 98.85  ?  356 ILE   A CG2 1 
ATOM   1436 C CD1 . ILE   A 1 375 ? -13.992 50.256  79.109  1.00 93.08  ?  356 ILE   A CD1 1 
ATOM   1437 N N   . LYS   A 1 376 ? -16.654 45.790  76.628  1.00 105.82 ?  357 LYS   A N   1 
ATOM   1438 C CA  . LYS   A 1 376 ? -16.420 44.531  75.927  1.00 109.57 ?  357 LYS   A CA  1 
ATOM   1439 C C   . LYS   A 1 376 ? -14.956 44.494  75.499  1.00 109.31 ?  357 LYS   A C   1 
ATOM   1440 O O   . LYS   A 1 376 ? -14.544 45.241  74.601  1.00 105.69 ?  357 LYS   A O   1 
ATOM   1441 C CB  . LYS   A 1 376 ? -17.354 44.405  74.724  1.00 116.72 ?  357 LYS   A CB  1 
ATOM   1442 C CG  . LYS   A 1 376 ? -18.819 44.083  75.051  1.00 116.47 ?  357 LYS   A CG  1 
ATOM   1443 C CD  . LYS   A 1 376 ? -19.689 44.232  73.797  1.00 125.51 ?  357 LYS   A CD  1 
ATOM   1444 C CE  . LYS   A 1 376 ? -21.171 43.959  74.053  1.00 128.99 ?  357 LYS   A CE  1 
ATOM   1445 N NZ  . LYS   A 1 376 ? -22.003 44.352  72.868  1.00 125.58 ?  357 LYS   A NZ  1 
ATOM   1446 N N   . GLN   A 1 377 ? -14.172 43.615  76.131  1.00 107.21 ?  358 GLN   A N   1 
ATOM   1447 C CA  . GLN   A 1 377 ? -12.719 43.714  76.041  1.00 110.38 ?  358 GLN   A CA  1 
ATOM   1448 C C   . GLN   A 1 377 ? -12.170 43.301  74.675  1.00 107.34 ?  358 GLN   A C   1 
ATOM   1449 O O   . GLN   A 1 377 ? -10.971 43.478  74.434  1.00 110.33 ?  358 GLN   A O   1 
ATOM   1450 C CB  . GLN   A 1 377 ? -12.054 42.880  77.158  1.00 118.34 ?  358 GLN   A CB  1 
ATOM   1451 C CG  . GLN   A 1 377 ? -12.773 42.848  78.551  1.00 120.37 ?  358 GLN   A CG  1 
ATOM   1452 C CD  . GLN   A 1 377 ? -12.427 44.023  79.500  1.00 133.34 ?  358 GLN   A CD  1 
ATOM   1453 O OE1 . GLN   A 1 377 ? -11.818 45.030  79.099  1.00 130.39 ?  358 GLN   A OE1 1 
ATOM   1454 N NE2 . GLN   A 1 377 ? -12.819 43.881  80.775  1.00 129.89 ?  358 GLN   A NE2 1 
ATOM   1455 N N   . LYS   A 1 378 ? -13.008 42.790  73.772  1.00 107.65 ?  359 LYS   A N   1 
ATOM   1456 C CA  . LYS   A 1 378 ? -12.535 42.283  72.486  1.00 102.53 ?  359 LYS   A CA  1 
ATOM   1457 C C   . LYS   A 1 378 ? -12.117 43.428  71.565  1.00 96.98  ?  359 LYS   A C   1 
ATOM   1458 O O   . LYS   A 1 378 ? -12.898 44.354  71.327  1.00 94.98  ?  359 LYS   A O   1 
ATOM   1459 C CB  . LYS   A 1 378 ? -13.639 41.445  71.834  1.00 101.62 ?  359 LYS   A CB  1 
ATOM   1460 C CG  . LYS   A 1 378 ? -13.500 41.236  70.321  1.00 105.62 ?  359 LYS   A CG  1 
ATOM   1461 C CD  . LYS   A 1 378 ? -14.402 40.097  69.813  1.00 107.38 ?  359 LYS   A CD  1 
ATOM   1462 C CE  . LYS   A 1 378 ? -14.805 40.304  68.347  1.00 105.70 ?  359 LYS   A CE  1 
ATOM   1463 N NZ  . LYS   A 1 378 ? -15.943 39.433  67.912  1.00 98.36  ?  359 LYS   A NZ  1 
ATOM   1464 N N   . CYS   A 1 379 ? -10.896 43.362  71.035  1.00 93.78  ?  360 CYS   A N   1 
ATOM   1465 C CA  . CYS   A 1 379 ? -10.353 44.432  70.195  1.00 90.54  ?  360 CYS   A CA  1 
ATOM   1466 C C   . CYS   A 1 379 ? -9.732  43.885  68.909  1.00 88.77  ?  360 CYS   A C   1 
ATOM   1467 O O   . CYS   A 1 379 ? -8.628  43.312  68.958  1.00 90.41  ?  360 CYS   A O   1 
ATOM   1468 C CB  . CYS   A 1 379 ? -9.314  45.257  70.956  1.00 91.37  ?  360 CYS   A CB  1 
ATOM   1469 S SG  . CYS   A 1 379 ? -8.728  46.782  70.077  1.00 91.93  ?  360 CYS   A SG  1 
ATOM   1470 N N   . PRO   A 1 380 ? -10.382 44.064  67.759  1.00 85.95  ?  361 PRO   A N   1 
ATOM   1471 C CA  . PRO   A 1 380 ? -9.793  43.676  66.464  1.00 86.45  ?  361 PRO   A CA  1 
ATOM   1472 C C   . PRO   A 1 380 ? -8.678  44.603  66.024  1.00 86.51  ?  361 PRO   A C   1 
ATOM   1473 O O   . PRO   A 1 380 ? -8.899  45.800  65.801  1.00 88.84  ?  361 PRO   A O   1 
ATOM   1474 C CB  . PRO   A 1 380 ? -10.986 43.753  65.501  1.00 84.45  ?  361 PRO   A CB  1 
ATOM   1475 C CG  . PRO   A 1 380 ? -11.935 44.648  66.115  1.00 87.84  ?  361 PRO   A CG  1 
ATOM   1476 C CD  . PRO   A 1 380 ? -11.810 44.382  67.611  1.00 94.23  ?  361 PRO   A CD  1 
ATOM   1477 N N   . LEU   A 1 381 ? -7.490  44.039  65.812  1.00 89.39  ?  362 LEU   A N   1 
ATOM   1478 C CA  . LEU   A 1 381 ? -6.369  44.750  65.206  1.00 90.71  ?  362 LEU   A CA  1 
ATOM   1479 C C   . LEU   A 1 381 ? -6.548  44.845  63.685  1.00 86.61  ?  362 LEU   A C   1 
ATOM   1480 O O   . LEU   A 1 381 ? -6.895  43.855  63.037  1.00 96.90  ?  362 LEU   A O   1 
ATOM   1481 C CB  . LEU   A 1 381 ? -5.072  44.014  65.546  1.00 85.95  ?  362 LEU   A CB  1 
ATOM   1482 C CG  . LEU   A 1 381 ? -4.418  44.382  66.870  1.00 83.86  ?  362 LEU   A CG  1 
ATOM   1483 C CD1 . LEU   A 1 381 ? -3.992  45.790  66.731  1.00 79.27  ?  362 LEU   A CD1 1 
ATOM   1484 C CD2 . LEU   A 1 381 ? -5.372  44.242  68.054  1.00 86.10  ?  362 LEU   A CD2 1 
ATOM   1485 N N   . TYR   A 1 382 ? -6.335  46.029  63.111  1.00 76.91  ?  363 TYR   A N   1 
ATOM   1486 C CA  . TYR   A 1 382 ? -6.476  46.232  61.666  1.00 82.91  ?  363 TYR   A CA  1 
ATOM   1487 C C   . TYR   A 1 382 ? -5.207  46.860  61.130  1.00 87.61  ?  363 TYR   A C   1 
ATOM   1488 O O   . TYR   A 1 382 ? -4.928  48.023  61.422  1.00 88.85  ?  363 TYR   A O   1 
ATOM   1489 C CB  . TYR   A 1 382 ? -7.647  47.141  61.294  1.00 86.72  ?  363 TYR   A CB  1 
ATOM   1490 C CG  . TYR   A 1 382 ? -9.019  46.555  61.447  1.00 96.77  ?  363 TYR   A CG  1 
ATOM   1491 C CD1 . TYR   A 1 382 ? -9.298  45.590  62.400  1.00 100.92 ?  363 TYR   A CD1 1 
ATOM   1492 C CD2 . TYR   A 1 382 ? -10.017 46.900  60.571  1.00 97.48  ?  363 TYR   A CD2 1 
ATOM   1493 C CE1 . TYR   A 1 382 ? -10.567 45.048  62.515  1.00 102.25 ?  363 TYR   A CE1 1 
ATOM   1494 C CE2 . TYR   A 1 382 ? -11.272 46.359  60.667  1.00 101.20 ?  363 TYR   A CE2 1 
ATOM   1495 C CZ  . TYR   A 1 382 ? -11.548 45.437  61.636  1.00 104.16 ?  363 TYR   A CZ  1 
ATOM   1496 O OH  . TYR   A 1 382 ? -12.819 44.912  61.710  1.00 115.93 ?  363 TYR   A OH  1 
ATOM   1497 N N   . GLU   A 1 383 ? -4.485  46.141  60.281  1.00 99.19  ?  364 GLU   A N   1 
ATOM   1498 C CA  . GLU   A 1 383 ? -3.131  46.574  60.001  1.00 93.12  ?  364 GLU   A CA  1 
ATOM   1499 C C   . GLU   A 1 383 ? -3.177  47.730  58.991  1.00 91.31  ?  364 GLU   A C   1 
ATOM   1500 O O   . GLU   A 1 383 ? -4.253  48.180  58.572  1.00 95.15  ?  364 GLU   A O   1 
ATOM   1501 C CB  . GLU   A 1 383 ? -2.315  45.370  59.553  1.00 102.21 ?  364 GLU   A CB  1 
ATOM   1502 C CG  . GLU   A 1 383 ? -0.814  45.532  59.573  1.00 106.32 ?  364 GLU   A CG  1 
ATOM   1503 C CD  . GLU   A 1 383 ? -0.156  44.215  59.217  1.00 119.37 ?  364 GLU   A CD  1 
ATOM   1504 O OE1 . GLU   A 1 383 ? -0.900  43.252  58.918  1.00 114.47 ?  364 GLU   A OE1 1 
ATOM   1505 O OE2 . GLU   A 1 383 ? 1.094   44.116  59.321  1.00 125.12 ?  364 GLU   A OE2 1 
ATOM   1506 N N   . ALA   A 1 384 ? -2.005  48.269  58.643  1.00 90.29  ?  365 ALA   A N   1 
ATOM   1507 C CA  . ALA   A 1 384 ? -1.991  49.565  57.957  1.00 87.46  ?  365 ALA   A CA  1 
ATOM   1508 C C   . ALA   A 1 384 ? -2.647  49.523  56.580  1.00 96.79  ?  365 ALA   A C   1 
ATOM   1509 O O   . ALA   A 1 384 ? -3.047  50.575  56.071  1.00 96.89  ?  365 ALA   A O   1 
ATOM   1510 C CB  . ALA   A 1 384 ? -0.561  50.094  57.830  1.00 81.77  ?  365 ALA   A CB  1 
ATOM   1511 N N   . ASN   A 1 385 ? -2.746  48.341  55.960  1.00 105.32 ?  366 ASN   A N   1 
ATOM   1512 C CA  . ASN   A 1 385 ? -3.483  48.199  54.703  1.00 96.81  ?  366 ASN   A CA  1 
ATOM   1513 C C   . ASN   A 1 385 ? -4.954  48.582  54.866  1.00 103.14 ?  366 ASN   A C   1 
ATOM   1514 O O   . ASN   A 1 385 ? -5.504  49.344  54.061  1.00 104.56 ?  366 ASN   A O   1 
ATOM   1515 C CB  . ASN   A 1 385 ? -3.322  46.765  54.181  1.00 92.11  ?  366 ASN   A CB  1 
ATOM   1516 C CG  . ASN   A 1 385 ? -4.006  45.692  55.078  1.00 106.93 ?  366 ASN   A CG  1 
ATOM   1517 O OD1 . ASN   A 1 385 ? -5.028  45.934  55.720  1.00 103.09 ?  366 ASN   A OD1 1 
ATOM   1518 N ND2 . ASN   A 1 385 ? -3.428  44.490  55.098  1.00 111.81 ?  366 ASN   A ND2 1 
ATOM   1519 N N   . GLY   A 1 386 ? -5.599  48.075  55.917  1.00 101.52 ?  367 GLY   A N   1 
ATOM   1520 C CA  . GLY   A 1 386 ? -7.011  48.284  56.164  1.00 98.52  ?  367 GLY   A CA  1 
ATOM   1521 C C   . GLY   A 1 386 ? -7.750  46.989  56.447  1.00 103.94 ?  367 GLY   A C   1 
ATOM   1522 O O   . GLY   A 1 386 ? -8.983  46.949  56.363  1.00 108.21 ?  367 GLY   A O   1 
ATOM   1523 N N   . GLN   A 1 387 ? -7.016  45.924  56.791  1.00 101.47 ?  368 GLN   A N   1 
ATOM   1524 C CA  . GLN   A 1 387 ? -7.582  44.587  56.919  1.00 98.53  ?  368 GLN   A CA  1 
ATOM   1525 C C   . GLN   A 1 387 ? -7.088  43.909  58.186  1.00 93.95  ?  368 GLN   A C   1 
ATOM   1526 O O   . GLN   A 1 387 ? -5.922  44.041  58.573  1.00 94.66  ?  368 GLN   A O   1 
ATOM   1527 C CB  . GLN   A 1 387 ? -7.225  43.704  55.716  1.00 106.68 ?  368 GLN   A CB  1 
ATOM   1528 C CG  . GLN   A 1 387 ? -8.179  43.800  54.525  1.00 107.91 ?  368 GLN   A CG  1 
ATOM   1529 C CD  . GLN   A 1 387 ? -7.799  42.824  53.426  1.00 116.83 ?  368 GLN   A CD  1 
ATOM   1530 O OE1 . GLN   A 1 387 ? -6.692  42.887  52.881  1.00 116.86 ?  368 GLN   A OE1 1 
ATOM   1531 N NE2 . GLN   A 1 387 ? -8.706  41.899  53.110  1.00 119.32 ?  368 GLN   A NE2 1 
ATOM   1532 N N   . ALA   A 1 388 ? -7.986  43.136  58.795  1.00 88.56  ?  369 ALA   A N   1 
ATOM   1533 C CA  . ALA   A 1 388 ? -7.753  42.509  60.089  1.00 95.73  ?  369 ALA   A CA  1 
ATOM   1534 C C   . ALA   A 1 388 ? -6.448  41.729  60.153  1.00 94.40  ?  369 ALA   A C   1 
ATOM   1535 O O   . ALA   A 1 388 ? -5.926  41.267  59.136  1.00 100.34 ?  369 ALA   A O   1 
ATOM   1536 C CB  . ALA   A 1 388 ? -8.916  41.580  60.446  1.00 97.04  ?  369 ALA   A CB  1 
ATOM   1537 N N   . VAL   A 1 389 ? -5.903  41.589  61.349  1.00 91.09  ?  370 VAL   A N   1 
ATOM   1538 C CA  . VAL   A 1 389 ? -4.811  40.653  61.546  1.00 96.52  ?  370 VAL   A CA  1 
ATOM   1539 C C   . VAL   A 1 389 ? -5.474  39.310  61.816  1.00 103.11 ?  370 VAL   A C   1 
ATOM   1540 O O   . VAL   A 1 389 ? -6.379  39.221  62.659  1.00 104.13 ?  370 VAL   A O   1 
ATOM   1541 C CB  . VAL   A 1 389 ? -3.876  41.100  62.679  1.00 97.21  ?  370 VAL   A CB  1 
ATOM   1542 C CG1 . VAL   A 1 389 ? -2.900  39.981  63.052  1.00 100.69 ?  370 VAL   A CG1 1 
ATOM   1543 C CG2 . VAL   A 1 389 ? -3.129  42.362  62.263  1.00 95.78  ?  370 VAL   A CG2 1 
ATOM   1544 N N   . PRO   A 1 390 ? -5.090  38.262  61.094  1.00 103.23 ?  371 PRO   A N   1 
ATOM   1545 C CA  . PRO   A 1 390 ? -5.734  36.956  61.274  1.00 97.15  ?  371 PRO   A CA  1 
ATOM   1546 C C   . PRO   A 1 390 ? -5.587  36.431  62.694  1.00 98.84  ?  371 PRO   A C   1 
ATOM   1547 O O   . PRO   A 1 390 ? -4.512  36.508  63.291  1.00 101.14 ?  371 PRO   A O   1 
ATOM   1548 C CB  . PRO   A 1 390 ? -4.992  36.069  60.274  1.00 105.75 ?  371 PRO   A CB  1 
ATOM   1549 C CG  . PRO   A 1 390 ? -4.512  37.041  59.208  1.00 103.14 ?  371 PRO   A CG  1 
ATOM   1550 C CD  . PRO   A 1 390 ? -4.193  38.303  59.924  1.00 100.97 ?  371 PRO   A CD  1 
ATOM   1551 N N   . LYS   A 1 391 ? -6.683  35.860  63.217  1.00 98.18  ?  372 LYS   A N   1 
ATOM   1552 C CA  . LYS   A 1 391 ? -6.709  35.343  64.585  1.00 100.78 ?  372 LYS   A CA  1 
ATOM   1553 C C   . LYS   A 1 391 ? -5.547  34.412  64.891  1.00 106.05 ?  372 LYS   A C   1 
ATOM   1554 O O   . LYS   A 1 391 ? -5.263  34.163  66.062  1.00 108.18 ?  372 LYS   A O   1 
ATOM   1555 C CB  . LYS   A 1 391 ? -8.016  34.584  64.874  1.00 102.23 ?  372 LYS   A CB  1 
ATOM   1556 C CG  . LYS   A 1 391 ? -9.294  35.329  64.496  1.00 109.93 ?  372 LYS   A CG  1 
ATOM   1557 C CD  . LYS   A 1 391 ? -10.546 34.663  65.085  1.00 111.52 ?  372 LYS   A CD  1 
ATOM   1558 C CE  . LYS   A 1 391 ? -11.400 35.676  65.856  1.00 111.60 ?  372 LYS   A CE  1 
ATOM   1559 N NZ  . LYS   A 1 391 ? -12.701 35.116  66.315  1.00 108.06 ?  372 LYS   A NZ  1 
ATOM   1560 N N   . GLU   A 1 392 ? -4.900  33.846  63.871  1.00 114.92 ?  373 GLU   A N   1 
ATOM   1561 C CA  . GLU   A 1 392 ? -3.683  33.075  64.102  1.00 114.44 ?  373 GLU   A CA  1 
ATOM   1562 C C   . GLU   A 1 392 ? -2.600  33.962  64.695  1.00 106.85 ?  373 GLU   A C   1 
ATOM   1563 O O   . GLU   A 1 392 ? -1.956  33.619  65.699  1.00 99.89  ?  373 GLU   A O   1 
ATOM   1564 C CB  . GLU   A 1 392 ? -3.206  32.474  62.779  1.00 115.32 ?  373 GLU   A CB  1 
ATOM   1565 C CG  . GLU   A 1 392 ? -3.724  31.083  62.491  1.00 126.22 ?  373 GLU   A CG  1 
ATOM   1566 C CD  . GLU   A 1 392 ? -2.894  30.007  63.160  1.00 129.74 ?  373 GLU   A CD  1 
ATOM   1567 O OE1 . GLU   A 1 392 ? -1.716  30.278  63.490  1.00 126.99 ?  373 GLU   A OE1 1 
ATOM   1568 O OE2 . GLU   A 1 392 ? -3.418  28.887  63.344  1.00 132.52 ?  373 GLU   A OE2 1 
ATOM   1569 N N   . LYS   A 1 393 ? -2.416  35.128  64.085  1.00 100.08 ?  374 LYS   A N   1 
ATOM   1570 C CA  . LYS   A 1 393 ? -1.281  36.006  64.282  1.00 98.53  ?  374 LYS   A CA  1 
ATOM   1571 C C   . LYS   A 1 393 ? -1.538  36.989  65.418  1.00 103.70 ?  374 LYS   A C   1 
ATOM   1572 O O   . LYS   A 1 393 ? -0.655  37.211  66.256  1.00 100.35 ?  374 LYS   A O   1 
ATOM   1573 C CB  . LYS   A 1 393 ? -1.000  36.713  62.957  1.00 93.96  ?  374 LYS   A CB  1 
ATOM   1574 C CG  . LYS   A 1 393 ? 0.290   37.460  62.873  1.00 103.83 ?  374 LYS   A CG  1 
ATOM   1575 C CD  . LYS   A 1 393 ? 0.672   37.627  61.414  1.00 102.93 ?  374 LYS   A CD  1 
ATOM   1576 C CE  . LYS   A 1 393 ? 2.158   37.809  61.291  1.00 106.42 ?  374 LYS   A CE  1 
ATOM   1577 N NZ  . LYS   A 1 393 ? 2.901   36.571  61.730  1.00 107.52 ?  374 LYS   A NZ  1 
ATOM   1578 N N   . ASP   A 1 394 ? -2.752  37.553  65.471  1.00 103.28 ?  375 ASP   A N   1 
ATOM   1579 C CA  . ASP   A 1 394 ? -3.192  38.332  66.625  1.00 98.72  ?  375 ASP   A CA  1 
ATOM   1580 C C   . ASP   A 1 394 ? -2.870  37.618  67.933  1.00 95.59  ?  375 ASP   A C   1 
ATOM   1581 O O   . ASP   A 1 394 ? -2.337  38.220  68.869  1.00 100.92 ?  375 ASP   A O   1 
ATOM   1582 C CB  . ASP   A 1 394 ? -4.697  38.607  66.532  1.00 99.61  ?  375 ASP   A CB  1 
ATOM   1583 C CG  . ASP   A 1 394 ? -5.139  39.812  67.377  1.00 108.56 ?  375 ASP   A CG  1 
ATOM   1584 O OD1 . ASP   A 1 394 ? -4.690  39.968  68.540  1.00 106.97 ?  375 ASP   A OD1 1 
ATOM   1585 O OD2 . ASP   A 1 394 ? -5.960  40.607  66.870  1.00 107.85 ?  375 ASP   A OD2 1 
ATOM   1586 N N   . GLU   A 1 395 ? -3.174  36.330  68.015  1.00 89.15  ?  376 GLU   A N   1 
ATOM   1587 C CA  . GLU   A 1 395 ? -3.009  35.664  69.296  1.00 95.81  ?  376 GLU   A CA  1 
ATOM   1588 C C   . GLU   A 1 395 ? -1.565  35.331  69.603  1.00 93.26  ?  376 GLU   A C   1 
ATOM   1589 O O   . GLU   A 1 395 ? -1.188  35.306  70.779  1.00 89.47  ?  376 GLU   A O   1 
ATOM   1590 C CB  . GLU   A 1 395 ? -3.852  34.392  69.372  1.00 98.85  ?  376 GLU   A CB  1 
ATOM   1591 C CG  . GLU   A 1 395 ? -5.263  34.578  68.877  1.00 106.68 ?  376 GLU   A CG  1 
ATOM   1592 C CD  . GLU   A 1 395 ? -6.266  33.654  69.540  1.00 114.02 ?  376 GLU   A CD  1 
ATOM   1593 O OE1 . GLU   A 1 395 ? -7.354  34.145  69.917  1.00 120.80 ?  376 GLU   A OE1 1 
ATOM   1594 O OE2 . GLU   A 1 395 ? -5.969  32.448  69.696  1.00 114.17 ?  376 GLU   A OE2 1 
ATOM   1595 N N   . MET   A 1 396 ? -0.734  35.051  68.614  1.00 96.54  ?  377 MET   A N   1 
ATOM   1596 C CA  . MET   A 1 396 ? 0.581   34.644  69.071  1.00 103.52 ?  377 MET   A CA  1 
ATOM   1597 C C   . MET   A 1 396 ? 1.489   35.839  69.301  1.00 94.51  ?  377 MET   A C   1 
ATOM   1598 O O   . MET   A 1 396 ? 2.418   35.739  70.116  1.00 92.97  ?  377 MET   A O   1 
ATOM   1599 C CB  . MET   A 1 396 ? 1.240   33.633  68.120  1.00 108.86 ?  377 MET   A CB  1 
ATOM   1600 C CG  . MET   A 1 396 ? 1.653   34.080  66.724  1.00 105.81 ?  377 MET   A CG  1 
ATOM   1601 S SD  . MET   A 1 396 ? 3.233   34.989  66.772  1.00 120.70 ?  377 MET   A SD  1 
ATOM   1602 C CE  . MET   A 1 396 ? 4.388   33.742  67.391  1.00 103.64 ?  377 MET   A CE  1 
ATOM   1603 N N   . VAL   A 1 397 ? 1.237   36.965  68.623  1.00 91.24  ?  378 VAL   A N   1 
ATOM   1604 C CA  . VAL   A 1 397 ? 1.959   38.189  68.959  1.00 89.70  ?  378 VAL   A CA  1 
ATOM   1605 C C   . VAL   A 1 397 ? 1.576   38.649  70.359  1.00 87.03  ?  378 VAL   A C   1 
ATOM   1606 O O   . VAL   A 1 397 ? 2.439   38.833  71.225  1.00 85.38  ?  378 VAL   A O   1 
ATOM   1607 C CB  . VAL   A 1 397 ? 1.704   39.281  67.909  1.00 84.52  ?  378 VAL   A CB  1 
ATOM   1608 C CG1 . VAL   A 1 397 ? 2.547   40.497  68.212  1.00 83.20  ?  378 VAL   A CG1 1 
ATOM   1609 C CG2 . VAL   A 1 397 ? 2.039   38.769  66.537  1.00 91.27  ?  378 VAL   A CG2 1 
ATOM   1610 N N   . GLU   A 1 398 ? 0.271   38.800  70.612  1.00 84.10  ?  379 GLU   A N   1 
ATOM   1611 C CA  . GLU   A 1 398 ? -0.203  39.096  71.962  1.00 87.45  ?  379 GLU   A CA  1 
ATOM   1612 C C   . GLU   A 1 398 ? 0.441   38.189  73.012  1.00 83.84  ?  379 GLU   A C   1 
ATOM   1613 O O   . GLU   A 1 398 ? 0.800   38.654  74.100  1.00 82.31  ?  379 GLU   A O   1 
ATOM   1614 C CB  . GLU   A 1 398 ? -1.729  38.986  72.018  1.00 92.33  ?  379 GLU   A CB  1 
ATOM   1615 C CG  . GLU   A 1 398 ? -2.341  39.297  73.388  1.00 89.94  ?  379 GLU   A CG  1 
ATOM   1616 C CD  . GLU   A 1 398 ? -3.704  39.975  73.293  1.00 94.64  ?  379 GLU   A CD  1 
ATOM   1617 O OE1 . GLU   A 1 398 ? -4.048  40.494  72.200  1.00 94.81  ?  379 GLU   A OE1 1 
ATOM   1618 O OE2 . GLU   A 1 398 ? -4.432  39.982  74.316  1.00 93.46  ?  379 GLU   A OE2 1 
ATOM   1619 N N   . GLN   A 1 399 ? 0.610   36.894  72.705  1.00 87.90  ?  380 GLN   A N   1 
ATOM   1620 C CA  . GLN   A 1 399 ? 1.239   35.996  73.674  1.00 86.84  ?  380 GLN   A CA  1 
ATOM   1621 C C   . GLN   A 1 399 ? 2.733   36.268  73.807  1.00 83.32  ?  380 GLN   A C   1 
ATOM   1622 O O   . GLN   A 1 399 ? 3.309   36.058  74.882  1.00 78.05  ?  380 GLN   A O   1 
ATOM   1623 C CB  . GLN   A 1 399 ? 1.023   34.531  73.295  1.00 91.79  ?  380 GLN   A CB  1 
ATOM   1624 C CG  . GLN   A 1 399 ? 1.944   33.592  74.097  1.00 101.96 ?  380 GLN   A CG  1 
ATOM   1625 C CD  . GLN   A 1 399 ? 1.933   32.141  73.644  1.00 107.38 ?  380 GLN   A CD  1 
ATOM   1626 O OE1 . GLN   A 1 399 ? 1.297   31.793  72.643  1.00 107.33 ?  380 GLN   A OE1 1 
ATOM   1627 N NE2 . GLN   A 1 399 ? 2.663   31.287  74.374  1.00 100.81 ?  380 GLN   A NE2 1 
ATOM   1628 N N   . GLU   A 1 400 ? 3.382   36.728  72.734  1.00 82.49  ?  381 GLU   A N   1 
ATOM   1629 C CA  . GLU   A 1 400 ? 4.802   37.046  72.838  1.00 83.05  ?  381 GLU   A CA  1 
ATOM   1630 C C   . GLU   A 1 400 ? 5.000   38.321  73.638  1.00 79.97  ?  381 GLU   A C   1 
ATOM   1631 O O   . GLU   A 1 400 ? 5.861   38.378  74.533  1.00 74.68  ?  381 GLU   A O   1 
ATOM   1632 C CB  . GLU   A 1 400 ? 5.422   37.161  71.442  1.00 77.49  ?  381 GLU   A CB  1 
ATOM   1633 C CG  . GLU   A 1 400 ? 6.919   36.837  71.365  1.00 77.07  ?  381 GLU   A CG  1 
ATOM   1634 C CD  . GLU   A 1 400 ? 7.295   35.457  71.938  1.00 87.91  ?  381 GLU   A CD  1 
ATOM   1635 O OE1 . GLU   A 1 400 ? 6.417   34.572  72.090  1.00 92.87  ?  381 GLU   A OE1 1 
ATOM   1636 O OE2 . GLU   A 1 400 ? 8.494   35.243  72.219  1.00 88.68  ?  381 GLU   A OE2 1 
ATOM   1637 N N   . PHE   A 1 401 ? 4.187   39.339  73.336  1.00 79.21  ?  382 PHE   A N   1 
ATOM   1638 C CA  . PHE   A 1 401 ? 4.080   40.545  74.145  1.00 76.31  ?  382 PHE   A CA  1 
ATOM   1639 C C   . PHE   A 1 401 ? 4.040   40.218  75.633  1.00 78.09  ?  382 PHE   A C   1 
ATOM   1640 O O   . PHE   A 1 401 ? 4.880   40.691  76.417  1.00 74.65  ?  382 PHE   A O   1 
ATOM   1641 C CB  . PHE   A 1 401 ? 2.827   41.325  73.737  1.00 79.94  ?  382 PHE   A CB  1 
ATOM   1642 C CG  . PHE   A 1 401 ? 2.483   42.454  74.681  1.00 85.87  ?  382 PHE   A CG  1 
ATOM   1643 C CD1 . PHE   A 1 401 ? 3.302   43.575  74.773  1.00 81.43  ?  382 PHE   A CD1 1 
ATOM   1644 C CD2 . PHE   A 1 401 ? 1.350   42.388  75.481  1.00 81.22  ?  382 PHE   A CD2 1 
ATOM   1645 C CE1 . PHE   A 1 401 ? 2.999   44.595  75.628  1.00 75.81  ?  382 PHE   A CE1 1 
ATOM   1646 C CE2 . PHE   A 1 401 ? 1.047   43.406  76.337  1.00 81.35  ?  382 PHE   A CE2 1 
ATOM   1647 C CZ  . PHE   A 1 401 ? 1.873   44.511  76.417  1.00 78.67  ?  382 PHE   A CZ  1 
ATOM   1648 N N   . ASN   A 1 402 ? 3.075   39.391  76.040  1.00 72.76  ?  383 ASN   A N   1 
ATOM   1649 C CA  . ASN   A 1 402 ? 2.962   39.085  77.459  1.00 72.51  ?  383 ASN   A CA  1 
ATOM   1650 C C   . ASN   A 1 402 ? 4.198   38.358  77.952  1.00 73.75  ?  383 ASN   A C   1 
ATOM   1651 O O   . ASN   A 1 402 ? 4.653   38.586  79.078  1.00 75.77  ?  383 ASN   A O   1 
ATOM   1652 C CB  . ASN   A 1 402 ? 1.695   38.282  77.730  1.00 66.32  ?  383 ASN   A CB  1 
ATOM   1653 C CG  . ASN   A 1 402 ? 0.437   39.066  77.399  1.00 82.08  ?  383 ASN   A CG  1 
ATOM   1654 O OD1 . ASN   A 1 402 ? -0.418  38.602  76.643  1.00 83.63  ?  383 ASN   A OD1 1 
ATOM   1655 N ND2 . ASN   A 1 402 ? 0.328   40.282  77.951  1.00 90.37  ?  383 ASN   A ND2 1 
ATOM   1656 N N   . ARG   A 1 403 ? 4.802   37.566  77.089  1.00 76.07  ?  384 ARG   A N   1 
ATOM   1657 C CA  . ARG   A 1 403 ? 5.982   36.801  77.534  1.00 78.57  ?  384 ARG   A CA  1 
ATOM   1658 C C   . ARG   A 1 403 ? 7.150   37.756  77.661  1.00 71.94  ?  384 ARG   A C   1 
ATOM   1659 O O   . ARG   A 1 403 ? 7.908   37.621  78.585  1.00 65.96  ?  384 ARG   A O   1 
ATOM   1660 C CB  . ARG   A 1 403 ? 6.213   35.648  76.570  1.00 87.07  ?  384 ARG   A CB  1 
ATOM   1661 C CG  . ARG   A 1 403 ? 5.045   34.682  76.542  1.00 89.46  ?  384 ARG   A CG  1 
ATOM   1662 C CD  . ARG   A 1 403 ? 4.749   34.266  75.127  1.00 99.10  ?  384 ARG   A CD  1 
ATOM   1663 N NE  . ARG   A 1 403 ? 5.884   33.480  74.699  1.00 105.34 ?  384 ARG   A NE  1 
ATOM   1664 C CZ  . ARG   A 1 403 ? 6.270   32.372  75.295  1.00 107.48 ?  384 ARG   A CZ  1 
ATOM   1665 N NH1 . ARG   A 1 403 ? 5.600   31.912  76.334  1.00 104.59 ?  384 ARG   A NH1 1 
ATOM   1666 N NH2 . ARG   A 1 403 ? 7.329   31.727  74.853  1.00 98.75  ?  384 ARG   A NH2 1 
ATOM   1667 N N   . LEU   A 1 404 ? 7.284   38.664  76.717  1.00 66.93  ?  385 LEU   A N   1 
ATOM   1668 C CA  . LEU   A 1 404 ? 8.319   39.684  76.826  1.00 71.59  ?  385 LEU   A CA  1 
ATOM   1669 C C   . LEU   A 1 404 ? 8.210   40.480  78.130  1.00 74.30  ?  385 LEU   A C   1 
ATOM   1670 O O   . LEU   A 1 404 ? 9.232   40.863  78.721  1.00 69.53  ?  385 LEU   A O   1 
ATOM   1671 C CB  . LEU   A 1 404 ? 8.228   40.605  75.617  1.00 68.54  ?  385 LEU   A CB  1 
ATOM   1672 C CG  . LEU   A 1 404 ? 8.788   39.938  74.365  1.00 69.06  ?  385 LEU   A CG  1 
ATOM   1673 C CD1 . LEU   A 1 404 ? 8.521   40.739  73.087  1.00 61.37  ?  385 LEU   A CD1 1 
ATOM   1674 C CD2 . LEU   A 1 404 ? 10.266  39.743  74.579  1.00 70.55  ?  385 LEU   A CD2 1 
ATOM   1675 N N   . LEU   A 1 405 ? 6.992   40.729  78.610  1.00 70.33  ?  386 LEU   A N   1 
ATOM   1676 C CA  . LEU   A 1 405 ? 6.844   41.411  79.890  1.00 65.50  ?  386 LEU   A CA  1 
ATOM   1677 C C   . LEU   A 1 405 ? 7.404   40.580  81.039  1.00 69.30  ?  386 LEU   A C   1 
ATOM   1678 O O   . LEU   A 1 405 ? 8.283   41.048  81.775  1.00 68.05  ?  386 LEU   A O   1 
ATOM   1679 C CB  . LEU   A 1 405 ? 5.381   41.756  80.121  1.00 69.67  ?  386 LEU   A CB  1 
ATOM   1680 C CG  . LEU   A 1 405 ? 5.175   43.147  79.557  1.00 66.40  ?  386 LEU   A CG  1 
ATOM   1681 C CD1 . LEU   A 1 405 ? 3.711   43.507  79.403  1.00 68.38  ?  386 LEU   A CD1 1 
ATOM   1682 C CD2 . LEU   A 1 405 ? 5.901   44.095  80.461  1.00 66.51  ?  386 LEU   A CD2 1 
ATOM   1683 N N   . GLU   A 1 406 ? 6.908   39.338  81.215  1.00 68.83  ?  387 GLU   A N   1 
ATOM   1684 C CA  . GLU   A 1 406 ? 7.435   38.465  82.270  1.00 70.15  ?  387 GLU   A CA  1 
ATOM   1685 C C   . GLU   A 1 406 ? 8.955   38.433  82.242  1.00 69.72  ?  387 GLU   A C   1 
ATOM   1686 O O   . GLU   A 1 406 ? 9.613   38.420  83.292  1.00 65.04  ?  387 GLU   A O   1 
ATOM   1687 C CB  . GLU   A 1 406 ? 6.941   37.029  82.112  1.00 78.27  ?  387 GLU   A CB  1 
ATOM   1688 C CG  . GLU   A 1 406 ? 5.462   36.726  82.214  1.00 89.28  ?  387 GLU   A CG  1 
ATOM   1689 C CD  . GLU   A 1 406 ? 5.165   35.267  81.785  1.00 106.89 ?  387 GLU   A CD  1 
ATOM   1690 O OE1 . GLU   A 1 406 ? 4.302   35.069  80.890  1.00 98.88  ?  387 GLU   A OE1 1 
ATOM   1691 O OE2 . GLU   A 1 406 ? 5.804   34.322  82.338  1.00 104.28 ?  387 GLU   A OE2 1 
ATOM   1692 N N   . ALA   A 1 407 ? 9.520   38.394  81.028  1.00 71.02  ?  388 ALA   A N   1 
ATOM   1693 C CA  . ALA   A 1 407 ? 10.964  38.339  80.845  1.00 69.79  ?  388 ALA   A CA  1 
ATOM   1694 C C   . ALA   A 1 407 ? 11.662  39.548  81.471  1.00 71.67  ?  388 ALA   A C   1 
ATOM   1695 O O   . ALA   A 1 407 ? 12.672  39.398  82.178  1.00 68.09  ?  388 ALA   A O   1 
ATOM   1696 C CB  . ALA   A 1 407 ? 11.266  38.236  79.355  1.00 71.98  ?  388 ALA   A CB  1 
ATOM   1697 N N   . THR   A 1 408 ? 11.140  40.759  81.223  1.00 72.23  ?  389 THR   A N   1 
ATOM   1698 C CA  . THR   A 1 408 ? 11.719  41.943  81.859  1.00 70.79  ?  389 THR   A CA  1 
ATOM   1699 C C   . THR   A 1 408 ? 11.642  41.830  83.367  1.00 68.43  ?  389 THR   A C   1 
ATOM   1700 O O   . THR   A 1 408 ? 12.575  42.227  84.075  1.00 69.13  ?  389 THR   A O   1 
ATOM   1701 C CB  . THR   A 1 408 ? 11.014  43.214  81.400  1.00 69.02  ?  389 THR   A CB  1 
ATOM   1702 O OG1 . THR   A 1 408 ? 9.598   43.022  81.485  1.00 75.93  ?  389 THR   A OG1 1 
ATOM   1703 C CG2 . THR   A 1 408 ? 11.395  43.541  79.956  1.00 66.48  ?  389 THR   A CG2 1 
ATOM   1704 N N   . SER   A 1 409 ? 10.540  41.270  83.873  1.00 68.05  ?  390 SER   A N   1 
ATOM   1705 C CA  . SER   A 1 409 ? 10.404  41.093  85.313  1.00 66.52  ?  390 SER   A CA  1 
ATOM   1706 C C   . SER   A 1 409 ? 11.446  40.121  85.836  1.00 73.65  ?  390 SER   A C   1 
ATOM   1707 O O   . SER   A 1 409 ? 12.037  40.345  86.903  1.00 73.19  ?  390 SER   A O   1 
ATOM   1708 C CB  . SER   A 1 409 ? 8.999   40.619  85.645  1.00 58.54  ?  390 SER   A CB  1 
ATOM   1709 O OG  . SER   A 1 409 ? 8.852   40.548  87.039  1.00 62.39  ?  390 SER   A OG  1 
ATOM   1710 N N   . TYR   A 1 410 ? 11.686  39.039  85.086  1.00 72.21  ?  391 TYR   A N   1 
ATOM   1711 C CA  . TYR   A 1 410 ? 12.780  38.125  85.385  1.00 76.62  ?  391 TYR   A CA  1 
ATOM   1712 C C   . TYR   A 1 410 ? 14.119  38.865  85.422  1.00 79.46  ?  391 TYR   A C   1 
ATOM   1713 O O   . TYR   A 1 410 ? 14.860  38.777  86.409  1.00 78.08  ?  391 TYR   A O   1 
ATOM   1714 C CB  . TYR   A 1 410 ? 12.798  36.992  84.347  1.00 87.43  ?  391 TYR   A CB  1 
ATOM   1715 C CG  . TYR   A 1 410 ? 13.843  35.925  84.614  1.00 90.35  ?  391 TYR   A CG  1 
ATOM   1716 C CD1 . TYR   A 1 410 ? 13.615  34.921  85.537  1.00 93.93  ?  391 TYR   A CD1 1 
ATOM   1717 C CD2 . TYR   A 1 410 ? 15.076  35.955  83.968  1.00 88.90  ?  391 TYR   A CD2 1 
ATOM   1718 C CE1 . TYR   A 1 410 ? 14.581  33.974  85.809  1.00 100.74 ?  391 TYR   A CE1 1 
ATOM   1719 C CE2 . TYR   A 1 410 ? 16.045  35.016  84.229  1.00 93.10  ?  391 TYR   A CE2 1 
ATOM   1720 C CZ  . TYR   A 1 410 ? 15.794  34.023  85.144  1.00 100.16 ?  391 TYR   A CZ  1 
ATOM   1721 O OH  . TYR   A 1 410 ? 16.763  33.078  85.393  1.00 104.79 ?  391 TYR   A OH  1 
ATOM   1722 N N   . LEU   A 1 411 ? 14.455  39.588  84.341  1.00 73.66  ?  392 LEU   A N   1 
ATOM   1723 C CA  . LEU   A 1 411 ? 15.621  40.475  84.367  1.00 78.32  ?  392 LEU   A CA  1 
ATOM   1724 C C   . LEU   A 1 411 ? 15.666  41.341  85.618  1.00 81.11  ?  392 LEU   A C   1 
ATOM   1725 O O   . LEU   A 1 411 ? 16.729  41.513  86.225  1.00 82.71  ?  392 LEU   A O   1 
ATOM   1726 C CB  . LEU   A 1 411 ? 15.648  41.400  83.152  1.00 76.73  ?  392 LEU   A CB  1 
ATOM   1727 C CG  . LEU   A 1 411 ? 16.332  41.040  81.852  1.00 76.68  ?  392 LEU   A CG  1 
ATOM   1728 C CD1 . LEU   A 1 411 ? 16.023  42.090  80.817  1.00 69.14  ?  392 LEU   A CD1 1 
ATOM   1729 C CD2 . LEU   A 1 411 ? 17.813  41.060  82.125  1.00 83.48  ?  392 LEU   A CD2 1 
ATOM   1730 N N   . SER   A 1 412 ? 14.533  41.954  85.978  1.00 78.04  ?  393 SER   A N   1 
ATOM   1731 C CA  . SER   A 1 412 ? 14.527  42.888  87.099  1.00 82.73  ?  393 SER   A CA  1 
ATOM   1732 C C   . SER   A 1 412 ? 14.732  42.157  88.425  1.00 83.24  ?  393 SER   A C   1 
ATOM   1733 O O   . SER   A 1 412 ? 15.724  42.391  89.129  1.00 78.75  ?  393 SER   A O   1 
ATOM   1734 C CB  . SER   A 1 412 ? 13.221  43.697  87.105  1.00 78.88  ?  393 SER   A CB  1 
ATOM   1735 O OG  . SER   A 1 412 ? 13.194  44.603  88.203  1.00 76.69  ?  393 SER   A OG  1 
ATOM   1736 N N   . HIS   A 1 413 ? 13.821  41.235  88.767  1.00 82.19  ?  394 HIS   A N   1 
ATOM   1737 C CA  . HIS   A 1 413 ? 13.792  40.674  90.115  1.00 91.68  ?  394 HIS   A CA  1 
ATOM   1738 C C   . HIS   A 1 413 ? 14.714  39.473  90.307  1.00 94.21  ?  394 HIS   A C   1 
ATOM   1739 O O   . HIS   A 1 413 ? 15.163  39.245  91.435  1.00 96.23  ?  394 HIS   A O   1 
ATOM   1740 C CB  . HIS   A 1 413 ? 12.355  40.301  90.520  1.00 88.22  ?  394 HIS   A CB  1 
ATOM   1741 C CG  . HIS   A 1 413 ? 11.410  41.469  90.520  1.00 93.51  ?  394 HIS   A CG  1 
ATOM   1742 N ND1 . HIS   A 1 413 ? 10.336  41.560  89.660  1.00 93.86  ?  394 HIS   A ND1 1 
ATOM   1743 C CD2 . HIS   A 1 413 ? 11.407  42.617  91.245  1.00 99.69  ?  394 HIS   A CD2 1 
ATOM   1744 C CE1 . HIS   A 1 413 ? 9.699   42.702  89.865  1.00 98.33  ?  394 HIS   A CE1 1 
ATOM   1745 N NE2 . HIS   A 1 413 ? 10.331  43.365  90.819  1.00 104.11 ?  394 HIS   A NE2 1 
ATOM   1746 N N   . GLN   A 1 414 ? 15.046  38.715  89.259  1.00 97.74  ?  395 GLN   A N   1 
ATOM   1747 C CA  . GLN   A 1 414 ? 15.872  37.538  89.500  1.00 98.55  ?  395 GLN   A CA  1 
ATOM   1748 C C   . GLN   A 1 414 ? 17.350  37.785  89.184  1.00 94.97  ?  395 GLN   A C   1 
ATOM   1749 O O   . GLN   A 1 414 ? 18.221  37.221  89.852  1.00 95.45  ?  395 GLN   A O   1 
ATOM   1750 C CB  . GLN   A 1 414 ? 15.427  36.349  88.652  1.00 97.89  ?  395 GLN   A CB  1 
ATOM   1751 C CG  . GLN   A 1 414 ? 13.932  35.968  88.529  1.00 105.65 ?  395 GLN   A CG  1 
ATOM   1752 C CD  . GLN   A 1 414 ? 13.085  35.871  89.768  1.00 107.40 ?  395 GLN   A CD  1 
ATOM   1753 O OE1 . GLN   A 1 414 ? 12.059  36.566  89.864  1.00 107.87 ?  395 GLN   A OE1 1 
ATOM   1754 N NE2 . GLN   A 1 414 ? 13.551  35.122  90.769  1.00 115.77 ?  395 GLN   A NE2 1 
ATOM   1755 N N   . LEU   A 1 415 ? 17.657  38.577  88.146  1.00 88.83  ?  396 LEU   A N   1 
ATOM   1756 C CA  . LEU   A 1 415 ? 19.031  38.870  87.733  1.00 89.69  ?  396 LEU   A CA  1 
ATOM   1757 C C   . LEU   A 1 415 ? 19.526  40.261  88.150  1.00 95.68  ?  396 LEU   A C   1 
ATOM   1758 O O   . LEU   A 1 415 ? 20.641  40.638  87.763  1.00 92.41  ?  396 LEU   A O   1 
ATOM   1759 C CB  . LEU   A 1 415 ? 19.175  38.734  86.210  1.00 90.00  ?  396 LEU   A CB  1 
ATOM   1760 C CG  . LEU   A 1 415 ? 18.644  37.490  85.477  1.00 92.41  ?  396 LEU   A CG  1 
ATOM   1761 C CD1 . LEU   A 1 415 ? 18.763  37.622  83.962  1.00 85.53  ?  396 LEU   A CD1 1 
ATOM   1762 C CD2 . LEU   A 1 415 ? 19.362  36.249  85.915  1.00 92.93  ?  396 LEU   A CD2 1 
ATOM   1763 N N   . ASP   A 1 416 ? 18.728  41.021  88.913  1.00 96.65  ?  397 ASP   A N   1 
ATOM   1764 C CA  . ASP   A 1 416 ? 19.034  42.391  89.375  1.00 94.77  ?  397 ASP   A CA  1 
ATOM   1765 C C   . ASP   A 1 416 ? 19.653  43.262  88.271  1.00 94.09  ?  397 ASP   A C   1 
ATOM   1766 O O   . ASP   A 1 416 ? 20.655  43.957  88.467  1.00 103.26 ?  397 ASP   A O   1 
ATOM   1767 C CB  . ASP   A 1 416 ? 19.920  42.366  90.630  1.00 95.26  ?  397 ASP   A CB  1 
ATOM   1768 C CG  . ASP   A 1 416 ? 19.739  43.619  91.525  1.00 110.46 ?  397 ASP   A CG  1 
ATOM   1769 O OD1 . ASP   A 1 416 ? 19.322  44.698  91.023  1.00 113.11 ?  397 ASP   A OD1 1 
ATOM   1770 O OD2 . ASP   A 1 416 ? 20.001  43.511  92.750  1.00 123.38 ?  397 ASP   A OD2 1 
ATOM   1771 N N   . PHE   A 1 417 ? 19.021  43.250  87.099  1.00 85.18  ?  398 PHE   A N   1 
ATOM   1772 C CA  . PHE   A 1 417 ? 19.481  44.062  85.968  1.00 88.41  ?  398 PHE   A CA  1 
ATOM   1773 C C   . PHE   A 1 417 ? 18.820  45.445  86.040  1.00 86.24  ?  398 PHE   A C   1 
ATOM   1774 O O   . PHE   A 1 417 ? 17.983  45.828  85.220  1.00 82.89  ?  398 PHE   A O   1 
ATOM   1775 C CB  . PHE   A 1 417 ? 19.186  43.344  84.650  1.00 81.99  ?  398 PHE   A CB  1 
ATOM   1776 C CG  . PHE   A 1 417 ? 19.564  44.123  83.414  1.00 77.90  ?  398 PHE   A CG  1 
ATOM   1777 C CD1 . PHE   A 1 417 ? 20.885  44.453  83.151  1.00 81.47  ?  398 PHE   A CD1 1 
ATOM   1778 C CD2 . PHE   A 1 417 ? 18.589  44.517  82.504  1.00 78.88  ?  398 PHE   A CD2 1 
ATOM   1779 C CE1 . PHE   A 1 417 ? 21.231  45.172  81.993  1.00 86.18  ?  398 PHE   A CE1 1 
ATOM   1780 C CE2 . PHE   A 1 417 ? 18.925  45.247  81.346  1.00 77.07  ?  398 PHE   A CE2 1 
ATOM   1781 C CZ  . PHE   A 1 417 ? 20.247  45.570  81.091  1.00 75.94  ?  398 PHE   A CZ  1 
ATOM   1782 N N   . ASN   A 1 418 ? 19.168  46.185  87.078  1.00 85.31  ?  399 ASN   A N   1 
ATOM   1783 C CA  . ASN   A 1 418 ? 18.456  47.462  87.279  1.00 85.38  ?  399 ASN   A CA  1 
ATOM   1784 C C   . ASN   A 1 418 ? 19.361  48.675  87.145  1.00 86.39  ?  399 ASN   A C   1 
ATOM   1785 O O   . ASN   A 1 418 ? 18.858  49.759  87.317  1.00 84.63  ?  399 ASN   A O   1 
ATOM   1786 C CB  . ASN   A 1 418 ? 17.696  47.435  88.592  1.00 82.73  ?  399 ASN   A CB  1 
ATOM   1787 C CG  . ASN   A 1 418 ? 16.622  46.384  88.549  1.00 84.67  ?  399 ASN   A CG  1 
ATOM   1788 O OD1 . ASN   A 1 418 ? 15.870  46.325  87.598  1.00 76.03  ?  399 ASN   A OD1 1 
ATOM   1789 N ND2 . ASN   A 1 418 ? 16.563  45.540  89.554  1.00 89.13  ?  399 ASN   A ND2 1 
ATOM   1790 N N   . VAL   A 1 419 ? 20.648  48.499  86.895  1.00 91.54  ?  400 VAL   A N   1 
ATOM   1791 C CA  . VAL   A 1 419 ? 21.499  49.700  86.680  1.00 89.92  ?  400 VAL   A CA  1 
ATOM   1792 C C   . VAL   A 1 419 ? 22.403  49.439  85.483  1.00 92.57  ?  400 VAL   A C   1 
ATOM   1793 O O   . VAL   A 1 419 ? 22.911  48.345  85.404  1.00 97.58  ?  400 VAL   A O   1 
ATOM   1794 C CB  . VAL   A 1 419 ? 22.326  50.022  87.928  1.00 94.33  ?  400 VAL   A CB  1 
ATOM   1795 C CG1 . VAL   A 1 419 ? 23.425  51.015  87.613  1.00 96.46  ?  400 VAL   A CG1 1 
ATOM   1796 C CG2 . VAL   A 1 419 ? 21.456  50.538  89.052  1.00 86.18  ?  400 VAL   A CG2 1 
ATOM   1797 N N   . LEU   A 1 420 ? 22.529  50.387  84.561  1.00 92.80  ?  401 LEU   A N   1 
ATOM   1798 C CA  . LEU   A 1 420 ? 23.446  50.192  83.417  1.00 93.23  ?  401 LEU   A CA  1 
ATOM   1799 C C   . LEU   A 1 420 ? 24.229  51.473  83.174  1.00 98.35  ?  401 LEU   A C   1 
ATOM   1800 O O   . LEU   A 1 420 ? 23.594  52.452  82.853  1.00 97.96  ?  401 LEU   A O   1 
ATOM   1801 C CB  . LEU   A 1 420 ? 22.611  49.881  82.185  1.00 92.54  ?  401 LEU   A CB  1 
ATOM   1802 C CG  . LEU   A 1 420 ? 23.332  49.033  81.155  1.00 96.76  ?  401 LEU   A CG  1 
ATOM   1803 C CD1 . LEU   A 1 420 ? 23.697  47.706  81.768  1.00 94.53  ?  401 LEU   A CD1 1 
ATOM   1804 C CD2 . LEU   A 1 420 ? 22.469  48.829  79.931  1.00 93.95  ?  401 LEU   A CD2 1 
ATOM   1805 N N   . ASN   A 1 421 ? 25.555  51.423  83.269  1.00 99.71  ?  402 ASN   A N   1 
ATOM   1806 C CA  . ASN   A 1 421 ? 26.447  52.589  83.037  1.00 108.17 ?  402 ASN   A CA  1 
ATOM   1807 C C   . ASN   A 1 421 ? 26.089  53.753  83.954  1.00 106.24 ?  402 ASN   A C   1 
ATOM   1808 O O   . ASN   A 1 421 ? 26.014  54.868  83.438  1.00 103.68 ?  402 ASN   A O   1 
ATOM   1809 C CB  . ASN   A 1 421 ? 26.469  53.056  81.582  1.00 109.12 ?  402 ASN   A CB  1 
ATOM   1810 C CG  . ASN   A 1 421 ? 26.597  51.916  80.601  1.00 117.61 ?  402 ASN   A CG  1 
ATOM   1811 O OD1 . ASN   A 1 421 ? 27.300  50.943  80.855  1.00 121.29 ?  402 ASN   A OD1 1 
ATOM   1812 N ND2 . ASN   A 1 421 ? 25.919  52.033  79.475  1.00 115.83 ?  402 ASN   A ND2 1 
ATOM   1813 N N   . ASN   A 1 422 ? 25.773  53.450  85.217  1.00 104.36 ?  403 ASN   A N   1 
ATOM   1814 C CA  . ASN   A 1 422 ? 25.424  54.367  86.341  1.00 105.29 ?  403 ASN   A CA  1 
ATOM   1815 C C   . ASN   A 1 422 ? 24.003  54.910  86.223  1.00 102.80 ?  403 ASN   A C   1 
ATOM   1816 O O   . ASN   A 1 422 ? 23.620  55.692  87.077  1.00 105.39 ?  403 ASN   A O   1 
ATOM   1817 C CB  . ASN   A 1 422 ? 26.375  55.547  86.533  1.00 110.44 ?  403 ASN   A CB  1 
ATOM   1818 C CG  . ASN   A 1 422 ? 27.786  55.128  86.848  1.00 115.87 ?  403 ASN   A CG  1 
ATOM   1819 O OD1 . ASN   A 1 422 ? 28.416  54.428  86.068  1.00 115.83 ?  403 ASN   A OD1 1 
ATOM   1820 N ND2 . ASN   A 1 422 ? 28.291  55.573  87.981  1.00 115.14 ?  403 ASN   A ND2 1 
ATOM   1821 N N   . LYS   A 1 423 ? 23.230  54.462  85.249  1.00 98.56  ?  404 LYS   A N   1 
ATOM   1822 C CA  . LYS   A 1 423 ? 21.874  54.999  85.071  1.00 88.72  ?  404 LYS   A CA  1 
ATOM   1823 C C   . LYS   A 1 423 ? 20.899  53.870  85.329  1.00 87.77  ?  404 LYS   A C   1 
ATOM   1824 O O   . LYS   A 1 423 ? 21.219  52.751  85.025  1.00 86.28  ?  404 LYS   A O   1 
ATOM   1825 C CB  . LYS   A 1 423 ? 21.727  55.505  83.643  1.00 89.68  ?  404 LYS   A CB  1 
ATOM   1826 C CG  . LYS   A 1 423 ? 22.949  56.211  83.092  1.00 91.46  ?  404 LYS   A CG  1 
ATOM   1827 C CD  . LYS   A 1 423 ? 22.594  57.181  82.001  1.00 94.17  ?  404 LYS   A CD  1 
ATOM   1828 C CE  . LYS   A 1 423 ? 23.229  56.841  80.673  1.00 96.67  ?  404 LYS   A CE  1 
ATOM   1829 N NZ  . LYS   A 1 423 ? 22.470  57.415  79.539  1.00 100.25 ?  404 LYS   A NZ  1 
ATOM   1830 N N   . PRO   A 1 424 ? 19.739  54.142  85.926  1.00 84.87  ?  405 PRO   A N   1 
ATOM   1831 C CA  . PRO   A 1 424 ? 18.769  53.118  86.199  1.00 76.93  ?  405 PRO   A CA  1 
ATOM   1832 C C   . PRO   A 1 424 ? 18.199  52.633  84.874  1.00 72.38  ?  405 PRO   A C   1 
ATOM   1833 O O   . PRO   A 1 424 ? 18.006  53.403  84.018  1.00 77.96  ?  405 PRO   A O   1 
ATOM   1834 C CB  . PRO   A 1 424 ? 17.686  53.907  86.901  1.00 69.35  ?  405 PRO   A CB  1 
ATOM   1835 C CG  . PRO   A 1 424 ? 17.821  55.233  86.272  1.00 77.45  ?  405 PRO   A CG  1 
ATOM   1836 C CD  . PRO   A 1 424 ? 19.307  55.455  86.315  1.00 82.03  ?  405 PRO   A CD  1 
ATOM   1837 N N   . VAL   A 1 425 ? 17.937  51.344  84.796  1.00 70.77  ?  406 VAL   A N   1 
ATOM   1838 C CA  . VAL   A 1 425 ? 17.416  50.716  83.562  1.00 69.71  ?  406 VAL   A CA  1 
ATOM   1839 C C   . VAL   A 1 425 ? 15.957  51.077  83.379  1.00 63.14  ?  406 VAL   A C   1 
ATOM   1840 O O   . VAL   A 1 425 ? 15.236  51.038  84.335  1.00 63.21  ?  406 VAL   A O   1 
ATOM   1841 C CB  . VAL   A 1 425 ? 17.581  49.200  83.676  1.00 67.24  ?  406 VAL   A CB  1 
ATOM   1842 C CG1 . VAL   A 1 425 ? 16.956  48.480  82.513  1.00 59.45  ?  406 VAL   A CG1 1 
ATOM   1843 C CG2 . VAL   A 1 425 ? 19.033  48.832  83.777  1.00 71.10  ?  406 VAL   A CG2 1 
ATOM   1844 N N   . SER   A 1 426 ? 15.568  51.385  82.159  1.00 57.89  ?  407 SER   A N   1 
ATOM   1845 C CA  . SER   A 1 426 ? 14.150  51.661  81.868  1.00 63.54  ?  407 SER   A CA  1 
ATOM   1846 C C   . SER   A 1 426 ? 13.469  50.372  81.433  1.00 64.79  ?  407 SER   A C   1 
ATOM   1847 O O   . SER   A 1 426 ? 14.118  49.383  81.296  1.00 64.40  ?  407 SER   A O   1 
ATOM   1848 C CB  . SER   A 1 426 ? 14.051  52.659  80.796  1.00 61.05  ?  407 SER   A CB  1 
ATOM   1849 O OG  . SER   A 1 426 ? 14.293  52.042  79.566  1.00 63.09  ?  407 SER   A OG  1 
ATOM   1850 N N   . LEU   A 1 427 ? 12.164  50.396  81.282  1.00 63.26  ?  408 LEU   A N   1 
ATOM   1851 C CA  . LEU   A 1 427 ? 11.457  49.230  80.782  1.00 57.29  ?  408 LEU   A CA  1 
ATOM   1852 C C   . LEU   A 1 427 ? 11.749  49.019  79.308  1.00 64.22  ?  408 LEU   A C   1 
ATOM   1853 O O   . LEU   A 1 427 ? 11.953  47.879  78.868  1.00 67.13  ?  408 LEU   A O   1 
ATOM   1854 C CB  . LEU   A 1 427 ? 9.959   49.388  81.011  1.00 55.71  ?  408 LEU   A CB  1 
ATOM   1855 C CG  . LEU   A 1 427 ? 9.096   48.211  80.568  1.00 57.26  ?  408 LEU   A CG  1 
ATOM   1856 C CD1 . LEU   A 1 427 ? 9.414   47.012  81.411  1.00 60.21  ?  408 LEU   A CD1 1 
ATOM   1857 C CD2 . LEU   A 1 427 ? 7.622   48.543  80.687  1.00 54.29  ?  408 LEU   A CD2 1 
ATOM   1858 N N   . GLY   A 1 428 ? 11.774  50.108  78.533  1.00 62.49  ?  409 GLY   A N   1 
ATOM   1859 C CA  . GLY   A 1 428 ? 12.032  49.996  77.106  1.00 59.84  ?  409 GLY   A CA  1 
ATOM   1860 C C   . GLY   A 1 428 ? 13.393  49.398  76.799  1.00 65.43  ?  409 GLY   A C   1 
ATOM   1861 O O   . GLY   A 1 428 ? 13.514  48.534  75.926  1.00 65.08  ?  409 GLY   A O   1 
ATOM   1862 N N   . GLN   A 1 429 ? 14.433  49.841  77.512  1.00 60.25  ?  410 GLN   A N   1 
ATOM   1863 C CA  . GLN   A 1 429 ? 15.728  49.183  77.401  1.00 62.54  ?  410 GLN   A CA  1 
ATOM   1864 C C   . GLN   A 1 429 ? 15.605  47.691  77.654  1.00 65.67  ?  410 GLN   A C   1 
ATOM   1865 O O   . GLN   A 1 429 ? 16.027  46.871  76.834  1.00 72.27  ?  410 GLN   A O   1 
ATOM   1866 C CB  . GLN   A 1 429 ? 16.719  49.771  78.390  1.00 63.02  ?  410 GLN   A CB  1 
ATOM   1867 C CG  . GLN   A 1 429 ? 17.242  51.105  78.017  1.00 67.98  ?  410 GLN   A CG  1 
ATOM   1868 C CD  . GLN   A 1 429 ? 17.971  51.728  79.174  1.00 74.70  ?  410 GLN   A CD  1 
ATOM   1869 O OE1 . GLN   A 1 429 ? 18.574  51.023  79.995  1.00 70.71  ?  410 GLN   A OE1 1 
ATOM   1870 N NE2 . GLN   A 1 429 ? 17.904  53.058  79.270  1.00 87.29  ?  410 GLN   A NE2 1 
ATOM   1871 N N   . ALA   A 1 430 ? 15.035  47.321  78.798  1.00 66.63  ?  411 ALA   A N   1 
ATOM   1872 C CA  . ALA   A 1 430 ? 14.937  45.913  79.148  1.00 61.49  ?  411 ALA   A CA  1 
ATOM   1873 C C   . ALA   A 1 430 ? 14.160  45.132  78.103  1.00 63.14  ?  411 ALA   A C   1 
ATOM   1874 O O   . ALA   A 1 430 ? 14.468  43.964  77.857  1.00 67.67  ?  411 ALA   A O   1 
ATOM   1875 C CB  . ALA   A 1 430 ? 14.296  45.760  80.522  1.00 59.29  ?  411 ALA   A CB  1 
ATOM   1876 N N   . LEU   A 1 431 ? 13.171  45.752  77.459  1.00 62.19  ?  412 LEU   A N   1 
ATOM   1877 C CA  . LEU   A 1 431 ? 12.474  45.063  76.372  1.00 67.78  ?  412 LEU   A CA  1 
ATOM   1878 C C   . LEU   A 1 431 ? 13.389  44.822  75.175  1.00 71.77  ?  412 LEU   A C   1 
ATOM   1879 O O   . LEU   A 1 431 ? 13.358  43.744  74.568  1.00 72.54  ?  412 LEU   A O   1 
ATOM   1880 C CB  . LEU   A 1 431 ? 11.249  45.852  75.930  1.00 62.27  ?  412 LEU   A CB  1 
ATOM   1881 C CG  . LEU   A 1 431 ? 10.079  45.633  76.871  1.00 64.26  ?  412 LEU   A CG  1 
ATOM   1882 C CD1 . LEU   A 1 431 ? 8.924   46.467  76.395  1.00 63.47  ?  412 LEU   A CD1 1 
ATOM   1883 C CD2 . LEU   A 1 431 ? 9.719   44.157  76.941  1.00 60.44  ?  412 LEU   A CD2 1 
ATOM   1884 N N   . GLU   A 1 432 ? 14.189  45.822  74.803  1.00 74.07  ?  413 GLU   A N   1 
ATOM   1885 C CA  . GLU   A 1 432 ? 15.158  45.628  73.736  1.00 67.83  ?  413 GLU   A CA  1 
ATOM   1886 C C   . GLU   A 1 432 ? 16.109  44.491  74.068  1.00 72.21  ?  413 GLU   A C   1 
ATOM   1887 O O   . GLU   A 1 432 ? 16.272  43.552  73.279  1.00 79.48  ?  413 GLU   A O   1 
ATOM   1888 C CB  . GLU   A 1 432 ? 15.920  46.912  73.495  1.00 68.11  ?  413 GLU   A CB  1 
ATOM   1889 C CG  . GLU   A 1 432 ? 15.212  47.786  72.507  1.00 87.05  ?  413 GLU   A CG  1 
ATOM   1890 C CD  . GLU   A 1 432 ? 15.984  49.049  72.205  1.00 101.55 ?  413 GLU   A CD  1 
ATOM   1891 O OE1 . GLU   A 1 432 ? 16.506  49.136  71.062  1.00 115.13 ?  413 GLU   A OE1 1 
ATOM   1892 O OE2 . GLU   A 1 432 ? 16.068  49.937  73.099  1.00 99.52  ?  413 GLU   A OE2 1 
ATOM   1893 N N   . VAL   A 1 433 ? 16.724  44.540  75.245  1.00 62.08  ?  414 VAL   A N   1 
ATOM   1894 C CA  . VAL   A 1 433 ? 17.612  43.460  75.652  1.00 68.19  ?  414 VAL   A CA  1 
ATOM   1895 C C   . VAL   A 1 433 ? 16.925  42.104  75.521  1.00 75.86  ?  414 VAL   A C   1 
ATOM   1896 O O   . VAL   A 1 433 ? 17.513  41.138  75.020  1.00 80.21  ?  414 VAL   A O   1 
ATOM   1897 C CB  . VAL   A 1 433 ? 18.121  43.686  77.080  1.00 67.17  ?  414 VAL   A CB  1 
ATOM   1898 C CG1 . VAL   A 1 433 ? 18.613  42.357  77.662  1.00 66.44  ?  414 VAL   A CG1 1 
ATOM   1899 C CG2 . VAL   A 1 433 ? 19.226  44.716  77.053  1.00 61.76  ?  414 VAL   A CG2 1 
ATOM   1900 N N   . VAL   A 1 434 ? 15.673  42.001  75.963  1.00 76.10  ?  415 VAL   A N   1 
ATOM   1901 C CA  . VAL   A 1 434 ? 15.023  40.697  75.895  1.00 73.13  ?  415 VAL   A CA  1 
ATOM   1902 C C   . VAL   A 1 434 ? 14.748  40.312  74.443  1.00 74.62  ?  415 VAL   A C   1 
ATOM   1903 O O   . VAL   A 1 434 ? 14.884  39.143  74.068  1.00 76.11  ?  415 VAL   A O   1 
ATOM   1904 C CB  . VAL   A 1 434 ? 13.751  40.671  76.757  1.00 68.14  ?  415 VAL   A CB  1 
ATOM   1905 C CG1 . VAL   A 1 434 ? 12.987  39.389  76.532  1.00 66.76  ?  415 VAL   A CG1 1 
ATOM   1906 C CG2 . VAL   A 1 434 ? 14.134  40.765  78.214  1.00 66.75  ?  415 VAL   A CG2 1 
ATOM   1907 N N   . ILE   A 1 435 ? 14.401  41.279  73.588  1.00 73.13  ?  416 ILE   A N   1 
ATOM   1908 C CA  . ILE   A 1 435 ? 14.168  40.932  72.188  1.00 74.92  ?  416 ILE   A CA  1 
ATOM   1909 C C   . ILE   A 1 435 ? 15.465  40.492  71.525  1.00 79.75  ?  416 ILE   A C   1 
ATOM   1910 O O   . ILE   A 1 435 ? 15.520  39.446  70.871  1.00 83.20  ?  416 ILE   A O   1 
ATOM   1911 C CB  . ILE   A 1 435 ? 13.512  42.087  71.416  1.00 70.44  ?  416 ILE   A CB  1 
ATOM   1912 C CG1 . ILE   A 1 435 ? 12.028  42.193  71.783  1.00 73.30  ?  416 ILE   A CG1 1 
ATOM   1913 C CG2 . ILE   A 1 435 ? 13.678  41.859  69.933  1.00 65.65  ?  416 ILE   A CG2 1 
ATOM   1914 C CD1 . ILE   A 1 435 ? 11.316  43.371  71.159  1.00 69.53  ?  416 ILE   A CD1 1 
ATOM   1915 N N   . GLN   A 1 436 ? 16.535  41.274  71.695  1.00 82.14  ?  417 GLN   A N   1 
ATOM   1916 C CA  . GLN   A 1 436 ? 17.827  40.884  71.133  1.00 82.07  ?  417 GLN   A CA  1 
ATOM   1917 C C   . GLN   A 1 436 ? 18.203  39.463  71.548  1.00 83.63  ?  417 GLN   A C   1 
ATOM   1918 O O   . GLN   A 1 436 ? 18.496  38.617  70.698  1.00 87.22  ?  417 GLN   A O   1 
ATOM   1919 C CB  . GLN   A 1 436 ? 18.904  41.891  71.545  1.00 76.29  ?  417 GLN   A CB  1 
ATOM   1920 C CG  . GLN   A 1 436 ? 18.846  43.157  70.695  1.00 84.35  ?  417 GLN   A CG  1 
ATOM   1921 C CD  . GLN   A 1 436 ? 19.308  44.422  71.422  1.00 91.46  ?  417 GLN   A CD  1 
ATOM   1922 O OE1 . GLN   A 1 436 ? 19.857  44.367  72.532  1.00 88.24  ?  417 GLN   A OE1 1 
ATOM   1923 N NE2 . GLN   A 1 436 ? 19.072  45.578  70.792  1.00 92.63  ?  417 GLN   A NE2 1 
ATOM   1924 N N   . LEU   A 1 437 ? 18.147  39.163  72.846  1.00 76.22  ?  418 LEU   A N   1 
ATOM   1925 C CA  . LEU   A 1 437 ? 18.514  37.824  73.286  1.00 74.75  ?  418 LEU   A CA  1 
ATOM   1926 C C   . LEU   A 1 437 ? 17.602  36.747  72.718  1.00 82.00  ?  418 LEU   A C   1 
ATOM   1927 O O   . LEU   A 1 437 ? 18.002  35.577  72.677  1.00 81.80  ?  418 LEU   A O   1 
ATOM   1928 C CB  . LEU   A 1 437 ? 18.539  37.750  74.815  1.00 72.54  ?  418 LEU   A CB  1 
ATOM   1929 C CG  . LEU   A 1 437 ? 19.710  38.541  75.396  1.00 77.35  ?  418 LEU   A CG  1 
ATOM   1930 C CD1 . LEU   A 1 437 ? 20.148  38.062  76.767  1.00 81.47  ?  418 LEU   A CD1 1 
ATOM   1931 C CD2 . LEU   A 1 437 ? 20.861  38.467  74.429  1.00 81.77  ?  418 LEU   A CD2 1 
ATOM   1932 N N   . GLN   A 1 438 ? 16.388  37.099  72.290  1.00 79.07  ?  419 GLN   A N   1 
ATOM   1933 C CA  . GLN   A 1 438 ? 15.573  36.116  71.594  1.00 81.32  ?  419 GLN   A CA  1 
ATOM   1934 C C   . GLN   A 1 438 ? 15.935  36.056  70.114  1.00 89.27  ?  419 GLN   A C   1 
ATOM   1935 O O   . GLN   A 1 438 ? 15.915  34.973  69.518  1.00 92.17  ?  419 GLN   A O   1 
ATOM   1936 C CB  . GLN   A 1 438 ? 14.083  36.413  71.773  1.00 75.12  ?  419 GLN   A CB  1 
ATOM   1937 C CG  . GLN   A 1 438 ? 13.602  36.375  73.206  1.00 76.29  ?  419 GLN   A CG  1 
ATOM   1938 C CD  . GLN   A 1 438 ? 14.164  35.223  74.027  1.00 83.37  ?  419 GLN   A CD  1 
ATOM   1939 O OE1 . GLN   A 1 438 ? 15.091  35.395  74.833  1.00 77.88  ?  419 GLN   A OE1 1 
ATOM   1940 N NE2 . GLN   A 1 438 ? 13.565  34.043  73.863  1.00 91.28  ?  419 GLN   A NE2 1 
ATOM   1941 N N   . GLU   A 1 439 ? 16.436  37.161  69.594  1.00 87.72  ?  420 GLU   A N   1 
ATOM   1942 C CA  . GLU   A 1 439 ? 16.899  37.130  68.195  1.00 89.89  ?  420 GLU   A CA  1 
ATOM   1943 C C   . GLU   A 1 439 ? 18.235  36.401  68.194  1.00 90.10  ?  420 GLU   A C   1 
ATOM   1944 O O   . GLU   A 1 439 ? 18.507  35.669  67.268  1.00 88.89  ?  420 GLU   A O   1 
ATOM   1945 C CB  . GLU   A 1 439 ? 17.030  38.547  67.662  1.00 82.78  ?  420 GLU   A CB  1 
ATOM   1946 C CG  . GLU   A 1 439 ? 15.749  39.025  67.043  1.00 86.37  ?  420 GLU   A CG  1 
ATOM   1947 C CD  . GLU   A 1 439 ? 15.837  40.434  66.518  1.00 101.19 ?  420 GLU   A CD  1 
ATOM   1948 O OE1 . GLU   A 1 439 ? 16.823  41.096  66.820  1.00 99.39  ?  420 GLU   A OE1 1 
ATOM   1949 O OE2 . GLU   A 1 439 ? 14.917  40.847  65.812  1.00 110.56 ?  420 GLU   A OE2 1 
ATOM   1950 N N   . LYS   A 1 440 ? 19.040  36.614  69.221  1.00 89.13  ?  421 LYS   A N   1 
ATOM   1951 C CA  . LYS   A 1 440 ? 20.338  35.915  69.273  1.00 85.05  ?  421 LYS   A CA  1 
ATOM   1952 C C   . LYS   A 1 440 ? 20.074  34.427  69.392  1.00 86.79  ?  421 LYS   A C   1 
ATOM   1953 O O   . LYS   A 1 440 ? 20.639  33.679  68.649  1.00 94.60  ?  421 LYS   A O   1 
ATOM   1954 C CB  . LYS   A 1 440 ? 21.152  36.348  70.487  1.00 81.21  ?  421 LYS   A CB  1 
ATOM   1955 C CG  . LYS   A 1 440 ? 21.993  35.250  71.104  1.00 80.72  ?  421 LYS   A CG  1 
ATOM   1956 C CD  . LYS   A 1 440 ? 23.112  35.776  71.925  1.00 81.25  ?  421 LYS   A CD  1 
ATOM   1957 C CE  . LYS   A 1 440 ? 24.088  34.691  72.299  1.00 86.74  ?  421 LYS   A CE  1 
ATOM   1958 N NZ  . LYS   A 1 440 ? 24.131  34.480  73.761  1.00 97.95  ?  421 LYS   A NZ  1 
ATOM   1959 N N   . HIS   A 1 441 ? 19.130  34.030  70.220  1.00 89.63  ?  422 HIS   A N   1 
ATOM   1960 C CA  . HIS   A 1 441 ? 18.893  32.583  70.407  1.00 88.85  ?  422 HIS   A CA  1 
ATOM   1961 C C   . HIS   A 1 441 ? 18.436  31.957  69.102  1.00 88.52  ?  422 HIS   A C   1 
ATOM   1962 O O   . HIS   A 1 441 ? 18.844  30.868  68.832  1.00 94.74  ?  422 HIS   A O   1 
ATOM   1963 C CB  . HIS   A 1 441 ? 17.901  32.348  71.528  1.00 86.69  ?  422 HIS   A CB  1 
ATOM   1964 C CG  . HIS   A 1 441 ? 17.502  30.929  71.676  1.00 92.69  ?  422 HIS   A CG  1 
ATOM   1965 N ND1 . HIS   A 1 441 ? 16.423  30.405  71.027  1.00 94.61  ?  422 HIS   A ND1 1 
ATOM   1966 C CD2 . HIS   A 1 441 ? 18.017  29.939  72.420  1.00 90.26  ?  422 HIS   A CD2 1 
ATOM   1967 C CE1 . HIS   A 1 441 ? 16.285  29.149  71.355  1.00 88.52  ?  422 HIS   A CE1 1 
ATOM   1968 N NE2 . HIS   A 1 441 ? 17.244  28.845  72.206  1.00 93.14  ?  422 HIS   A NE2 1 
ATOM   1969 N N   . VAL   A 1 442 ? 17.618  32.636  68.323  1.00 86.36  ?  423 VAL   A N   1 
ATOM   1970 C CA  . VAL   A 1 442 ? 17.174  32.019  67.054  1.00 85.08  ?  423 VAL   A CA  1 
ATOM   1971 C C   . VAL   A 1 442 ? 18.398  31.764  66.185  1.00 95.20  ?  423 VAL   A C   1 
ATOM   1972 O O   . VAL   A 1 442 ? 18.544  30.651  65.722  1.00 97.89  ?  423 VAL   A O   1 
ATOM   1973 C CB  . VAL   A 1 442 ? 16.192  32.954  66.347  1.00 85.38  ?  423 VAL   A CB  1 
ATOM   1974 C CG1 . VAL   A 1 442 ? 16.309  32.843  64.848  1.00 92.22  ?  423 VAL   A CG1 1 
ATOM   1975 C CG2 . VAL   A 1 442 ? 14.775  32.680  66.784  1.00 83.91  ?  423 VAL   A CG2 1 
ATOM   1976 N N   . LYS   A 1 443 ? 19.304  32.728  66.080  1.00 95.02  ?  424 LYS   A N   1 
ATOM   1977 C CA  . LYS   A 1 443 ? 20.502  32.530  65.237  1.00 91.89  ?  424 LYS   A CA  1 
ATOM   1978 C C   . LYS   A 1 443 ? 21.315  31.382  65.816  1.00 93.61  ?  424 LYS   A C   1 
ATOM   1979 O O   . LYS   A 1 443 ? 21.614  30.466  65.092  1.00 98.08  ?  424 LYS   A O   1 
ATOM   1980 C CB  . LYS   A 1 443 ? 21.311  33.822  65.186  1.00 86.11  ?  424 LYS   A CB  1 
ATOM   1981 C CG  . LYS   A 1 443 ? 20.665  34.921  64.365  1.00 85.33  ?  424 LYS   A CG  1 
ATOM   1982 C CD  . LYS   A 1 443 ? 21.476  36.173  64.322  1.00 93.03  ?  424 LYS   A CD  1 
ATOM   1983 C CE  . LYS   A 1 443 ? 21.083  37.076  63.180  1.00 91.23  ?  424 LYS   A CE  1 
ATOM   1984 N NZ  . LYS   A 1 443 ? 19.754  36.710  62.653  1.00 85.52  ?  424 LYS   A NZ  1 
ATOM   1985 N N   . ASP   A 1 444 ? 21.472  31.346  67.125  1.00 89.63  ?  425 ASP   A N   1 
ATOM   1986 C CA  . ASP   A 1 444 ? 22.265  30.284  67.774  1.00 93.35  ?  425 ASP   A CA  1 
ATOM   1987 C C   . ASP   A 1 444 ? 21.661  28.919  67.462  1.00 99.48  ?  425 ASP   A C   1 
ATOM   1988 O O   . ASP   A 1 444 ? 22.407  27.985  67.242  1.00 93.93  ?  425 ASP   A O   1 
ATOM   1989 C CB  . ASP   A 1 444 ? 22.184  30.452  69.283  1.00 89.90  ?  425 ASP   A CB  1 
ATOM   1990 C CG  . ASP   A 1 444 ? 23.373  31.174  69.859  1.00 99.76  ?  425 ASP   A CG  1 
ATOM   1991 O OD1 . ASP   A 1 444 ? 23.595  31.053  71.056  1.00 110.38 ?  425 ASP   A OD1 1 
ATOM   1992 O OD2 . ASP   A 1 444 ? 24.065  31.828  69.100  1.00 111.08 ?  425 ASP   A OD2 1 
ATOM   1993 N N   . GLU   A 1 445 ? 20.344  28.800  67.480  1.00 99.87  ?  426 GLU   A N   1 
ATOM   1994 C CA  . GLU   A 1 445 ? 19.720  27.495  67.184  1.00 98.24  ?  426 GLU   A CA  1 
ATOM   1995 C C   . GLU   A 1 445 ? 20.054  27.112  65.756  1.00 95.25  ?  426 GLU   A C   1 
ATOM   1996 O O   . GLU   A 1 445 ? 20.423  25.984  65.538  1.00 102.04 ?  426 GLU   A O   1 
ATOM   1997 C CB  . GLU   A 1 445 ? 18.203  27.616  67.222  1.00 99.64  ?  426 GLU   A CB  1 
ATOM   1998 C CG  . GLU   A 1 445 ? 17.615  27.411  68.594  1.00 97.38  ?  426 GLU   A CG  1 
ATOM   1999 C CD  . GLU   A 1 445 ? 17.877  26.062  69.219  1.00 103.73 ?  426 GLU   A CD  1 
ATOM   2000 O OE1 . GLU   A 1 445 ? 18.892  25.925  69.902  1.00 109.10 ?  426 GLU   A OE1 1 
ATOM   2001 O OE2 . GLU   A 1 445 ? 17.048  25.173  69.038  1.00 108.31 ?  426 GLU   A OE2 1 
ATOM   2002 N N   . GLN   A 1 446 ? 19.985  28.058  64.832  1.00 97.27  ?  427 GLN   A N   1 
ATOM   2003 C CA  . GLN   A 1 446 ? 20.227  27.718  63.416  1.00 96.14  ?  427 GLN   A CA  1 
ATOM   2004 C C   . GLN   A 1 446 ? 21.646  27.186  63.271  1.00 95.37  ?  427 GLN   A C   1 
ATOM   2005 O O   . GLN   A 1 446 ? 21.835  26.147  62.670  1.00 93.15  ?  427 GLN   A O   1 
ATOM   2006 C CB  . GLN   A 1 446 ? 20.029  28.969  62.571  1.00 87.70  ?  427 GLN   A CB  1 
ATOM   2007 C CG  . GLN   A 1 446 ? 18.705  28.990  61.839  1.00 87.31  ?  427 GLN   A CG  1 
ATOM   2008 C CD  . GLN   A 1 446 ? 18.286  30.384  61.464  1.00 103.02 ?  427 GLN   A CD  1 
ATOM   2009 O OE1 . GLN   A 1 446 ? 19.105  31.268  61.281  1.00 105.91 ?  427 GLN   A OE1 1 
ATOM   2010 N NE2 . GLN   A 1 446 ? 16.989  30.596  61.344  1.00 107.71 ?  427 GLN   A NE2 1 
ATOM   2011 N N   . ILE   A 1 447 ? 22.595  27.845  63.903  1.00 95.68  ?  428 ILE   A N   1 
ATOM   2012 C CA  . ILE   A 1 447 ? 23.998  27.406  63.775  1.00 90.76  ?  428 ILE   A CA  1 
ATOM   2013 C C   . ILE   A 1 447 ? 24.143  25.993  64.314  1.00 92.86  ?  428 ILE   A C   1 
ATOM   2014 O O   . ILE   A 1 447 ? 24.580  25.154  63.576  1.00 95.35  ?  428 ILE   A O   1 
ATOM   2015 C CB  . ILE   A 1 447 ? 24.823  28.370  64.620  1.00 89.79  ?  428 ILE   A CB  1 
ATOM   2016 C CG1 . ILE   A 1 447 ? 25.044  29.685  63.887  1.00 89.99  ?  428 ILE   A CG1 1 
ATOM   2017 C CG2 . ILE   A 1 447 ? 26.119  27.730  65.040  1.00 100.09 ?  428 ILE   A CG2 1 
ATOM   2018 C CD1 . ILE   A 1 447 ? 26.070  30.549  64.531  1.00 100.34 ?  428 ILE   A CD1 1 
ATOM   2019 N N   . GLU   A 1 448 ? 23.624  25.706  65.492  1.00 98.62  ?  429 GLU   A N   1 
ATOM   2020 C CA  . GLU   A 1 448 ? 23.860  24.365  66.070  1.00 97.08  ?  429 GLU   A CA  1 
ATOM   2021 C C   . GLU   A 1 448 ? 23.186  23.301  65.213  1.00 96.26  ?  429 GLU   A C   1 
ATOM   2022 O O   . GLU   A 1 448 ? 23.582  22.160  65.280  1.00 95.64  ?  429 GLU   A O   1 
ATOM   2023 C CB  . GLU   A 1 448 ? 23.436  24.341  67.533  1.00 90.91  ?  429 GLU   A CB  1 
ATOM   2024 C CG  . GLU   A 1 448 ? 22.426  23.275  67.857  1.00 102.07 ?  429 GLU   A CG  1 
ATOM   2025 C CD  . GLU   A 1 448 ? 22.533  22.818  69.296  1.00 113.72 ?  429 GLU   A CD  1 
ATOM   2026 O OE1 . GLU   A 1 448 ? 23.622  22.960  69.863  1.00 119.81 ?  429 GLU   A OE1 1 
ATOM   2027 O OE2 . GLU   A 1 448 ? 21.535  22.328  69.841  1.00 116.90 ?  429 GLU   A OE2 1 
ATOM   2028 N N   . HIS   A 1 449 ? 22.193  23.683  64.439  1.00 91.69  ?  430 HIS   A N   1 
ATOM   2029 C CA  . HIS   A 1 449 ? 21.504  22.730  63.574  1.00 92.37  ?  430 HIS   A CA  1 
ATOM   2030 C C   . HIS   A 1 449 ? 22.327  22.414  62.332  1.00 96.88  ?  430 HIS   A C   1 
ATOM   2031 O O   . HIS   A 1 449 ? 22.650  21.251  62.067  1.00 100.95 ?  430 HIS   A O   1 
ATOM   2032 C CB  . HIS   A 1 449 ? 20.137  23.292  63.189  1.00 95.55  ?  430 HIS   A CB  1 
ATOM   2033 C CG  . HIS   A 1 449 ? 19.466  22.585  62.052  1.00 91.86  ?  430 HIS   A CG  1 
ATOM   2034 N ND1 . HIS   A 1 449 ? 19.519  23.048  60.753  1.00 93.90  ?  430 HIS   A ND1 1 
ATOM   2035 C CD2 . HIS   A 1 449 ? 18.665  21.494  62.029  1.00 95.27  ?  430 HIS   A CD2 1 
ATOM   2036 C CE1 . HIS   A 1 449 ? 18.802  22.258  59.974  1.00 93.50  ?  430 HIS   A CE1 1 
ATOM   2037 N NE2 . HIS   A 1 449 ? 18.273  21.307  60.724  1.00 98.65  ?  430 HIS   A NE2 1 
ATOM   2038 N N   . TRP   A 1 450 ? 22.671  23.443  61.550  1.00 97.55  ?  431 TRP   A N   1 
ATOM   2039 C CA  . TRP   A 1 450 ? 23.536  23.231  60.395  1.00 91.72  ?  431 TRP   A CA  1 
ATOM   2040 C C   . TRP   A 1 450 ? 24.899  22.674  60.803  1.00 95.27  ?  431 TRP   A C   1 
ATOM   2041 O O   . TRP   A 1 450 ? 25.508  21.922  60.037  1.00 101.42 ?  431 TRP   A O   1 
ATOM   2042 C CB  . TRP   A 1 450 ? 23.714  24.529  59.614  1.00 85.88  ?  431 TRP   A CB  1 
ATOM   2043 C CG  . TRP   A 1 450 ? 22.442  25.130  59.048  1.00 96.34  ?  431 TRP   A CG  1 
ATOM   2044 C CD1 . TRP   A 1 450 ? 21.733  26.178  59.563  1.00 98.95  ?  431 TRP   A CD1 1 
ATOM   2045 C CD2 . TRP   A 1 450 ? 21.758  24.745  57.843  1.00 99.57  ?  431 TRP   A CD2 1 
ATOM   2046 N NE1 . TRP   A 1 450 ? 20.649  26.462  58.765  1.00 98.29  ?  431 TRP   A NE1 1 
ATOM   2047 C CE2 . TRP   A 1 450 ? 20.641  25.599  57.703  1.00 100.58 ?  431 TRP   A CE2 1 
ATOM   2048 C CE3 . TRP   A 1 450 ? 21.978  23.765  56.873  1.00 97.33  ?  431 TRP   A CE3 1 
ATOM   2049 C CZ2 . TRP   A 1 450 ? 19.748  25.500  56.634  1.00 101.51 ?  431 TRP   A CZ2 1 
ATOM   2050 C CZ3 . TRP   A 1 450 ? 21.090  23.672  55.808  1.00 108.35 ?  431 TRP   A CZ3 1 
ATOM   2051 C CH2 . TRP   A 1 450 ? 19.990  24.536  55.697  1.00 107.77 ?  431 TRP   A CH2 1 
ATOM   2052 N N   . LYS   A 1 451 ? 25.392  23.011  61.999  1.00 94.51  ?  432 LYS   A N   1 
ATOM   2053 C CA  . LYS   A 1 451 ? 26.672  22.469  62.446  1.00 91.38  ?  432 LYS   A CA  1 
ATOM   2054 C C   . LYS   A 1 451 ? 26.606  20.967  62.684  1.00 95.80  ?  432 LYS   A C   1 
ATOM   2055 O O   . LYS   A 1 451 ? 27.629  20.284  62.568  1.00 100.71 ?  432 LYS   A O   1 
ATOM   2056 C CB  . LYS   A 1 451 ? 27.152  23.166  63.720  1.00 92.23  ?  432 LYS   A CB  1 
ATOM   2057 C CG  . LYS   A 1 451 ? 28.023  24.390  63.465  1.00 100.10 ?  432 LYS   A CG  1 
ATOM   2058 C CD  . LYS   A 1 451 ? 29.100  24.531  64.535  1.00 105.12 ?  432 LYS   A CD  1 
ATOM   2059 C CE  . LYS   A 1 451 ? 29.775  25.899  64.474  1.00 108.69 ?  432 LYS   A CE  1 
ATOM   2060 N NZ  . LYS   A 1 451 ? 30.650  26.116  65.665  1.00 111.55 ?  432 LYS   A NZ  1 
ATOM   2061 N N   . LYS   A 1 452 ? 25.447  20.428  63.054  1.00 96.36  ?  433 LYS   A N   1 
ATOM   2062 C CA  . LYS   A 1 452 ? 25.356  18.979  63.128  1.00 93.10  ?  433 LYS   A CA  1 
ATOM   2063 C C   . LYS   A 1 452 ? 24.954  18.370  61.796  1.00 94.85  ?  433 LYS   A C   1 
ATOM   2064 O O   . LYS   A 1 452 ? 24.939  17.144  61.670  1.00 99.12  ?  433 LYS   A O   1 
ATOM   2065 C CB  . LYS   A 1 452 ? 24.416  18.521  64.272  1.00 95.02  ?  433 LYS   A CB  1 
ATOM   2066 C CG  . LYS   A 1 452 ? 22.904  18.796  64.189  1.00 100.36 ?  433 LYS   A CG  1 
ATOM   2067 C CD  . LYS   A 1 452 ? 22.332  18.894  65.643  1.00 110.99 ?  433 LYS   A CD  1 
ATOM   2068 C CE  . LYS   A 1 452 ? 20.851  18.480  65.791  1.00 111.63 ?  433 LYS   A CE  1 
ATOM   2069 N NZ  . LYS   A 1 452 ? 19.852  19.517  65.335  1.00 110.44 ?  433 LYS   A NZ  1 
ATOM   2070 N N   . ILE   A 1 453 ? 24.682  19.188  60.782  1.00 91.07  ?  434 ILE   A N   1 
ATOM   2071 C CA  . ILE   A 1 453 ? 24.639  18.662  59.424  1.00 91.89  ?  434 ILE   A CA  1 
ATOM   2072 C C   . ILE   A 1 453 ? 26.055  18.444  58.895  1.00 97.70  ?  434 ILE   A C   1 
ATOM   2073 O O   . ILE   A 1 453 ? 26.374  17.372  58.369  1.00 100.67 ?  434 ILE   A O   1 
ATOM   2074 C CB  . ILE   A 1 453 ? 23.821  19.583  58.498  1.00 94.15  ?  434 ILE   A CB  1 
ATOM   2075 C CG1 . ILE   A 1 453 ? 22.322  19.351  58.702  1.00 91.92  ?  434 ILE   A CG1 1 
ATOM   2076 C CG2 . ILE   A 1 453 ? 24.211  19.365  57.036  1.00 88.76  ?  434 ILE   A CG2 1 
ATOM   2077 C CD1 . ILE   A 1 453 ? 21.433  20.200  57.829  1.00 93.88  ?  434 ILE   A CD1 1 
ATOM   2078 N N   . VAL   A 1 454 ? 26.936  19.445  59.031  1.00 96.53  ?  435 VAL   A N   1 
ATOM   2079 C CA  . VAL   A 1 454 ? 28.302  19.268  58.541  1.00 91.35  ?  435 VAL   A CA  1 
ATOM   2080 C C   . VAL   A 1 454 ? 28.994  18.118  59.265  1.00 94.88  ?  435 VAL   A C   1 
ATOM   2081 O O   . VAL   A 1 454 ? 29.712  17.334  58.637  1.00 102.83 ?  435 VAL   A O   1 
ATOM   2082 C CB  . VAL   A 1 454 ? 29.126  20.564  58.649  1.00 85.05  ?  435 VAL   A CB  1 
ATOM   2083 C CG1 . VAL   A 1 454 ? 28.722  21.537  57.612  1.00 86.61  ?  435 VAL   A CG1 1 
ATOM   2084 C CG2 . VAL   A 1 454 ? 28.994  21.166  60.004  1.00 94.70  ?  435 VAL   A CG2 1 
ATOM   2085 N N   . LYS   A 1 455 ? 28.813  17.998  60.586  1.00 88.66  ?  436 LYS   A N   1 
ATOM   2086 C CA  . LYS   A 1 455 ? 29.430  16.875  61.289  1.00 94.72  ?  436 LYS   A CA  1 
ATOM   2087 C C   . LYS   A 1 455 ? 29.034  15.549  60.657  1.00 102.93 ?  436 LYS   A C   1 
ATOM   2088 O O   . LYS   A 1 455 ? 29.871  14.645  60.497  1.00 101.99 ?  436 LYS   A O   1 
ATOM   2089 C CB  . LYS   A 1 455 ? 29.071  16.869  62.780  1.00 90.12  ?  436 LYS   A CB  1 
ATOM   2090 C CG  . LYS   A 1 455 ? 29.279  15.476  63.404  1.00 93.82  ?  436 LYS   A CG  1 
ATOM   2091 C CD  . LYS   A 1 455 ? 29.323  15.431  64.919  1.00 103.33 ?  436 LYS   A CD  1 
ATOM   2092 C CE  . LYS   A 1 455 ? 30.552  16.152  65.461  1.00 106.77 ?  436 LYS   A CE  1 
ATOM   2093 N NZ  . LYS   A 1 455 ? 30.895  15.655  66.828  1.00 111.17 ?  436 LYS   A NZ  1 
ATOM   2094 N N   . THR   A 1 456 ? 27.768  15.423  60.267  1.00 102.59 ?  437 THR   A N   1 
ATOM   2095 C CA  . THR   A 1 456 ? 27.289  14.167  59.719  1.00 103.56 ?  437 THR   A CA  1 
ATOM   2096 C C   . THR   A 1 456 ? 27.533  14.066  58.210  1.00 100.49 ?  437 THR   A C   1 
ATOM   2097 O O   . THR   A 1 456 ? 27.732  12.958  57.703  1.00 105.04 ?  437 THR   A O   1 
ATOM   2098 C CB  . THR   A 1 456 ? 25.810  13.974  60.100  1.00 103.65 ?  437 THR   A CB  1 
ATOM   2099 O OG1 . THR   A 1 456 ? 25.402  12.621  59.873  1.00 115.45 ?  437 THR   A OG1 1 
ATOM   2100 C CG2 . THR   A 1 456 ? 24.915  14.882  59.320  1.00 99.63  ?  437 THR   A CG2 1 
ATOM   2101 N N   . GLN   A 1 457 ? 27.610  15.179  57.477  1.00 98.47  ?  438 GLN   A N   1 
ATOM   2102 C CA  . GLN   A 1 457 ? 28.133  15.082  56.116  1.00 95.89  ?  438 GLN   A CA  1 
ATOM   2103 C C   . GLN   A 1 457 ? 29.637  15.075  56.030  1.00 96.54  ?  438 GLN   A C   1 
ATOM   2104 O O   . GLN   A 1 457 ? 30.169  15.147  54.926  1.00 101.56 ?  438 GLN   A O   1 
ATOM   2105 C CB  . GLN   A 1 457 ? 27.615  16.192  55.207  1.00 89.15  ?  438 GLN   A CB  1 
ATOM   2106 C CG  . GLN   A 1 457 ? 26.322  15.795  54.629  1.00 91.59  ?  438 GLN   A CG  1 
ATOM   2107 C CD  . GLN   A 1 457 ? 25.892  16.629  53.466  1.00 99.85  ?  438 GLN   A CD  1 
ATOM   2108 O OE1 . GLN   A 1 457 ? 26.306  17.775  53.324  1.00 98.53  ?  438 GLN   A OE1 1 
ATOM   2109 N NE2 . GLN   A 1 457 ? 25.078  16.045  52.592  1.00 109.35 ?  438 GLN   A NE2 1 
ATOM   2110 N N   . GLU   A 1 458 ? 30.352  15.014  57.134  1.00 98.43  ?  439 GLU   A N   1 
ATOM   2111 C CA  . GLU   A 1 458 ? 31.761  14.706  57.016  1.00 99.85  ?  439 GLU   A CA  1 
ATOM   2112 C C   . GLU   A 1 458 ? 32.041  13.266  57.381  1.00 97.84  ?  439 GLU   A C   1 
ATOM   2113 O O   . GLU   A 1 458 ? 32.974  12.679  56.836  1.00 101.53 ?  439 GLU   A O   1 
ATOM   2114 C CB  . GLU   A 1 458 ? 32.603  15.653  57.876  1.00 101.83 ?  439 GLU   A CB  1 
ATOM   2115 C CG  . GLU   A 1 458 ? 32.953  16.953  57.142  1.00 100.05 ?  439 GLU   A CG  1 
ATOM   2116 C CD  . GLU   A 1 458 ? 33.763  17.938  57.989  1.00 113.23 ?  439 GLU   A CD  1 
ATOM   2117 O OE1 . GLU   A 1 458 ? 34.292  18.921  57.417  1.00 121.60 ?  439 GLU   A OE1 1 
ATOM   2118 O OE2 . GLU   A 1 458 ? 33.878  17.734  59.221  1.00 108.84 ?  439 GLU   A OE2 1 
ATOM   2119 N N   . GLU   A 1 459 ? 31.240  12.691  58.282  1.00 100.99 ?  440 GLU   A N   1 
ATOM   2120 C CA  . GLU   A 1 459 ? 31.183  11.240  58.414  1.00 103.37 ?  440 GLU   A CA  1 
ATOM   2121 C C   . GLU   A 1 459 ? 30.861  10.598  57.066  1.00 100.35 ?  440 GLU   A C   1 
ATOM   2122 O O   . GLU   A 1 459 ? 31.472  9.598   56.677  1.00 100.06 ?  440 GLU   A O   1 
ATOM   2123 C CB  . GLU   A 1 459 ? 30.124  10.850  59.448  1.00 102.46 ?  440 GLU   A CB  1 
ATOM   2124 C CG  . GLU   A 1 459 ? 30.435  11.201  60.895  1.00 113.11 ?  440 GLU   A CG  1 
ATOM   2125 C CD  . GLU   A 1 459 ? 29.466  10.526  61.873  1.00 130.28 ?  440 GLU   A CD  1 
ATOM   2126 O OE1 . GLU   A 1 459 ? 28.246  10.506  61.582  1.00 128.19 ?  440 GLU   A OE1 1 
ATOM   2127 O OE2 . GLU   A 1 459 ? 29.916  10.025  62.933  1.00 134.57 ?  440 GLU   A OE2 1 
ATOM   2128 N N   . LEU   A 1 460 ? 29.897  11.163  56.340  1.00 96.05  ?  441 LEU   A N   1 
ATOM   2129 C CA  . LEU   A 1 460 ? 29.579  10.668  55.006  1.00 93.51  ?  441 LEU   A CA  1 
ATOM   2130 C C   . LEU   A 1 460 ? 30.775  10.780  54.068  1.00 100.14 ?  441 LEU   A C   1 
ATOM   2131 O O   . LEU   A 1 460 ? 31.072  9.841   53.318  1.00 101.67 ?  441 LEU   A O   1 
ATOM   2132 C CB  . LEU   A 1 460 ? 28.408  11.450  54.428  1.00 94.31  ?  441 LEU   A CB  1 
ATOM   2133 C CG  . LEU   A 1 460 ? 27.947  11.025  53.039  1.00 92.66  ?  441 LEU   A CG  1 
ATOM   2134 C CD1 . LEU   A 1 460 ? 27.378  9.625   53.128  1.00 97.16  ?  441 LEU   A CD1 1 
ATOM   2135 C CD2 . LEU   A 1 460 ? 26.960  12.012  52.401  1.00 90.76  ?  441 LEU   A CD2 1 
ATOM   2136 N N   . LYS   A 1 461 ? 31.451  11.934  54.074  1.00 99.45  ?  442 LYS   A N   1 
ATOM   2137 C CA  . LYS   A 1 461 ? 32.635  12.114  53.237  1.00 95.13  ?  442 LYS   A CA  1 
ATOM   2138 C C   . LYS   A 1 461 ? 33.669  11.022  53.496  1.00 96.24  ?  442 LYS   A C   1 
ATOM   2139 O O   . LYS   A 1 461 ? 34.139  10.365  52.564  1.00 101.09 ?  442 LYS   A O   1 
ATOM   2140 C CB  . LYS   A 1 461 ? 33.245  13.491  53.486  1.00 90.94  ?  442 LYS   A CB  1 
ATOM   2141 C CG  . LYS   A 1 461 ? 34.406  13.878  52.588  1.00 84.20  ?  442 LYS   A CG  1 
ATOM   2142 C CD  . LYS   A 1 461 ? 34.982  15.185  53.099  1.00 93.19  ?  442 LYS   A CD  1 
ATOM   2143 C CE  . LYS   A 1 461 ? 36.235  15.630  52.373  1.00 97.49  ?  442 LYS   A CE  1 
ATOM   2144 N NZ  . LYS   A 1 461 ? 36.818  16.852  53.012  1.00 96.25  ?  442 LYS   A NZ  1 
ATOM   2145 N N   . GLU   A 1 462 ? 34.032  10.804  54.758  1.00 90.36  ?  443 GLU   A N   1 
ATOM   2146 C CA  . GLU   A 1 462 ? 35.026  9.784   55.043  1.00 94.84  ?  443 GLU   A CA  1 
ATOM   2147 C C   . GLU   A 1 462 ? 34.493  8.381   54.807  1.00 96.74  ?  443 GLU   A C   1 
ATOM   2148 O O   . GLU   A 1 462 ? 35.280  7.455   54.584  1.00 91.83  ?  443 GLU   A O   1 
ATOM   2149 C CB  . GLU   A 1 462 ? 35.545  9.944   56.470  1.00 94.10  ?  443 GLU   A CB  1 
ATOM   2150 C CG  . GLU   A 1 462 ? 36.272  11.272  56.646  1.00 107.40 ?  443 GLU   A CG  1 
ATOM   2151 C CD  . GLU   A 1 462 ? 37.414  11.192  57.640  1.00 115.53 ?  443 GLU   A CD  1 
ATOM   2152 O OE1 . GLU   A 1 462 ? 37.284  10.418  58.614  1.00 115.92 ?  443 GLU   A OE1 1 
ATOM   2153 O OE2 . GLU   A 1 462 ? 38.438  11.895  57.445  1.00 118.17 ?  443 GLU   A OE2 1 
ATOM   2154 N N   . LEU   A 1 463 ? 33.177  8.203   54.828  1.00 97.23  ?  444 LEU   A N   1 
ATOM   2155 C CA  . LEU   A 1 463 ? 32.626  6.911   54.453  1.00 92.32  ?  444 LEU   A CA  1 
ATOM   2156 C C   . LEU   A 1 463 ? 32.795  6.662   52.966  1.00 94.64  ?  444 LEU   A C   1 
ATOM   2157 O O   . LEU   A 1 463 ? 33.154  5.557   52.551  1.00 98.76  ?  444 LEU   A O   1 
ATOM   2158 C CB  . LEU   A 1 463 ? 31.156  6.834   54.816  1.00 92.20  ?  444 LEU   A CB  1 
ATOM   2159 C CG  . LEU   A 1 463 ? 30.721  5.387   54.904  1.00 93.48  ?  444 LEU   A CG  1 
ATOM   2160 C CD1 . LEU   A 1 463 ? 31.297  4.785   56.173  1.00 93.91  ?  444 LEU   A CD1 1 
ATOM   2161 C CD2 . LEU   A 1 463 ? 29.218  5.298   54.874  1.00 93.65  ?  444 LEU   A CD2 1 
ATOM   2162 N N   . LEU   A 1 464 ? 32.523  7.670   52.145  1.00 95.66  ?  445 LEU   A N   1 
ATOM   2163 C CA  . LEU   A 1 464 ? 32.671  7.489   50.709  1.00 92.07  ?  445 LEU   A CA  1 
ATOM   2164 C C   . LEU   A 1 464 ? 34.126  7.217   50.341  1.00 94.71  ?  445 LEU   A C   1 
ATOM   2165 O O   . LEU   A 1 464 ? 34.414  6.284   49.585  1.00 99.47  ?  445 LEU   A O   1 
ATOM   2166 C CB  . LEU   A 1 464 ? 32.125  8.708   49.966  1.00 92.65  ?  445 LEU   A CB  1 
ATOM   2167 C CG  . LEU   A 1 464 ? 30.629  8.973   50.164  1.00 92.68  ?  445 LEU   A CG  1 
ATOM   2168 C CD1 . LEU   A 1 464 ? 30.072  9.822   49.024  1.00 93.49  ?  445 LEU   A CD1 1 
ATOM   2169 C CD2 . LEU   A 1 464 ? 29.857  7.675   50.293  1.00 85.98  ?  445 LEU   A CD2 1 
ATOM   2170 N N   . ASN   A 1 465 ? 35.065  7.998   50.884  1.00 93.97  ?  446 ASN   A N   1 
ATOM   2171 C CA  . ASN   A 1 465 ? 36.474  7.736   50.604  1.00 93.90  ?  446 ASN   A CA  1 
ATOM   2172 C C   . ASN   A 1 465 ? 36.853  6.301   50.946  1.00 93.98  ?  446 ASN   A C   1 
ATOM   2173 O O   . ASN   A 1 465 ? 37.509  5.617   50.155  1.00 96.33  ?  446 ASN   A O   1 
ATOM   2174 C CB  . ASN   A 1 465 ? 37.374  8.733   51.333  1.00 86.71  ?  446 ASN   A CB  1 
ATOM   2175 C CG  . ASN   A 1 465 ? 37.659  9.968   50.490  1.00 94.86  ?  446 ASN   A CG  1 
ATOM   2176 O OD1 . ASN   A 1 465 ? 37.100  11.036  50.718  1.00 105.02 ?  446 ASN   A OD1 1 
ATOM   2177 N ND2 . ASN   A 1 465 ? 38.547  9.825   49.513  1.00 97.70  ?  446 ASN   A ND2 1 
ATOM   2178 N N   . LYS   A 1 466 ? 36.416  5.809   52.101  1.00 92.54  ?  447 LYS   A N   1 
ATOM   2179 C CA  . LYS   A 1 466 ? 36.709  4.422   52.443  1.00 90.40  ?  447 LYS   A CA  1 
ATOM   2180 C C   . LYS   A 1 466 ? 36.057  3.446   51.462  1.00 93.02  ?  447 LYS   A C   1 
ATOM   2181 O O   . LYS   A 1 466 ? 36.525  2.311   51.327  1.00 94.45  ?  447 LYS   A O   1 
ATOM   2182 C CB  . LYS   A 1 466 ? 36.268  4.160   53.887  1.00 84.33  ?  447 LYS   A CB  1 
ATOM   2183 C CG  . LYS   A 1 466 ? 36.654  2.821   54.459  1.00 91.08  ?  447 LYS   A CG  1 
ATOM   2184 C CD  . LYS   A 1 466 ? 36.536  2.796   55.980  1.00 94.65  ?  447 LYS   A CD  1 
ATOM   2185 C CE  . LYS   A 1 466 ? 37.899  2.947   56.673  1.00 98.59  ?  447 LYS   A CE  1 
ATOM   2186 N NZ  . LYS   A 1 466 ? 38.593  1.640   56.936  1.00 100.11 ?  447 LYS   A NZ  1 
ATOM   2187 N N   . MET   A 1 467 ? 35.028  3.883   50.733  1.00 89.83  ?  448 MET   A N   1 
ATOM   2188 C CA  . MET   A 1 467 ? 34.324  3.018   49.797  1.00 88.56  ?  448 MET   A CA  1 
ATOM   2189 C C   . MET   A 1 467 ? 34.852  3.102   48.368  1.00 90.88  ?  448 MET   A C   1 
ATOM   2190 O O   . MET   A 1 467 ? 34.779  2.110   47.638  1.00 92.84  ?  448 MET   A O   1 
ATOM   2191 C CB  . MET   A 1 467 ? 32.829  3.333   49.813  1.00 90.68  ?  448 MET   A CB  1 
ATOM   2192 C CG  . MET   A 1 467 ? 32.101  2.751   51.011  1.00 95.71  ?  448 MET   A CG  1 
ATOM   2193 S SD  . MET   A 1 467 ? 30.383  3.307   51.125  1.00 110.37 ?  448 MET   A SD  1 
ATOM   2194 C CE  . MET   A 1 467 ? 29.647  2.737   49.590  1.00 95.91  ?  448 MET   A CE  1 
ATOM   2195 N N   . VAL   A 1 468 ? 35.344  4.257   47.923  1.00 93.11  ?  449 VAL   A N   1 
ATOM   2196 C CA  . VAL   A 1 468 ? 36.199  4.274   46.737  1.00 91.36  ?  449 VAL   A CA  1 
ATOM   2197 C C   . VAL   A 1 468 ? 37.383  3.338   46.925  1.00 94.25  ?  449 VAL   A C   1 
ATOM   2198 O O   . VAL   A 1 468 ? 37.612  2.424   46.125  1.00 101.46 ?  449 VAL   A O   1 
ATOM   2199 C CB  . VAL   A 1 468 ? 36.680  5.698   46.420  1.00 92.29  ?  449 VAL   A CB  1 
ATOM   2200 C CG1 . VAL   A 1 468 ? 37.815  5.617   45.424  1.00 101.50 ?  449 VAL   A CG1 1 
ATOM   2201 C CG2 . VAL   A 1 468 ? 35.551  6.522   45.810  1.00 85.22  ?  449 VAL   A CG2 1 
ATOM   2202 N N   . ASN   A 1 469 ? 38.156  3.555   47.989  1.00 92.98  ?  450 ASN   A N   1 
ATOM   2203 C CA  . ASN   A 1 469 ? 39.386  2.803   48.177  1.00 93.17  ?  450 ASN   A CA  1 
ATOM   2204 C C   . ASN   A 1 469 ? 39.126  1.325   48.436  1.00 95.82  ?  450 ASN   A C   1 
ATOM   2205 O O   . ASN   A 1 469 ? 40.072  0.529   48.424  1.00 95.70  ?  450 ASN   A O   1 
ATOM   2206 C CB  . ASN   A 1 469 ? 40.206  3.431   49.307  1.00 84.99  ?  450 ASN   A CB  1 
ATOM   2207 C CG  . ASN   A 1 469 ? 40.875  4.729   48.877  1.00 91.69  ?  450 ASN   A CG  1 
ATOM   2208 O OD1 . ASN   A 1 469 ? 40.402  5.406   47.961  1.00 97.07  ?  450 ASN   A OD1 1 
ATOM   2209 N ND2 . ASN   A 1 469 ? 41.980  5.081   49.530  1.00 99.64  ?  450 ASN   A ND2 1 
ATOM   2210 N N   . LEU   A 1 470 ? 37.876  0.939   48.663  1.00 93.18  ?  451 LEU   A N   1 
ATOM   2211 C CA  . LEU   A 1 470 ? 37.565  -0.476  48.737  1.00 90.57  ?  451 LEU   A CA  1 
ATOM   2212 C C   . LEU   A 1 470 ? 37.112  -1.002  47.388  1.00 87.88  ?  451 LEU   A C   1 
ATOM   2213 O O   . LEU   A 1 470 ? 37.523  -2.092  46.988  1.00 90.07  ?  451 LEU   A O   1 
ATOM   2214 C CB  . LEU   A 1 470 ? 36.492  -0.741  49.793  1.00 82.90  ?  451 LEU   A CB  1 
ATOM   2215 C CG  . LEU   A 1 470 ? 36.801  -2.037  50.517  1.00 88.42  ?  451 LEU   A CG  1 
ATOM   2216 C CD1 . LEU   A 1 470 ? 38.237  -1.986  51.035  1.00 88.27  ?  451 LEU   A CD1 1 
ATOM   2217 C CD2 . LEU   A 1 470 ? 35.820  -2.274  51.638  1.00 94.43  ?  451 LEU   A CD2 1 
ATOM   2218 N N   . LYS   A 1 471 ? 36.290  -0.235  46.668  1.00 86.96  ?  452 LYS   A N   1 
ATOM   2219 C CA  . LYS   A 1 471 ? 35.862  -0.650  45.339  1.00 85.19  ?  452 LYS   A CA  1 
ATOM   2220 C C   . LYS   A 1 471 ? 37.040  -0.764  44.382  1.00 92.37  ?  452 LYS   A C   1 
ATOM   2221 O O   . LYS   A 1 471 ? 36.919  -1.425  43.349  1.00 95.24  ?  452 LYS   A O   1 
ATOM   2222 C CB  . LYS   A 1 471 ? 34.818  0.322   44.771  1.00 83.10  ?  452 LYS   A CB  1 
ATOM   2223 C CG  . LYS   A 1 471 ? 34.115  -0.166  43.502  1.00 86.36  ?  452 LYS   A CG  1 
ATOM   2224 C CD  . LYS   A 1 471 ? 33.466  0.970   42.720  1.00 93.93  ?  452 LYS   A CD  1 
ATOM   2225 C CE  . LYS   A 1 471 ? 33.113  0.541   41.299  1.00 95.93  ?  452 LYS   A CE  1 
ATOM   2226 N NZ  . LYS   A 1 471 ? 32.809  1.697   40.414  1.00 100.66 ?  452 LYS   A NZ  1 
ATOM   2227 N N   . GLU   A 1 472 ? 38.185  -0.157  44.698  1.00 94.74  ?  453 GLU   A N   1 
ATOM   2228 C CA  . GLU   A 1 472 ? 39.326  -0.309  43.803  1.00 89.57  ?  453 GLU   A CA  1 
ATOM   2229 C C   . GLU   A 1 472 ? 40.110  -1.579  44.116  1.00 89.69  ?  453 GLU   A C   1 
ATOM   2230 O O   . GLU   A 1 472 ? 40.497  -2.306  43.194  1.00 92.69  ?  453 GLU   A O   1 
ATOM   2231 C CB  . GLU   A 1 472 ? 40.215  0.933   43.853  1.00 87.22  ?  453 GLU   A CB  1 
ATOM   2232 C CG  . GLU   A 1 472 ? 39.479  2.207   43.421  1.00 103.42 ?  453 GLU   A CG  1 
ATOM   2233 C CD  . GLU   A 1 472 ? 38.777  2.086   42.045  1.00 117.33 ?  453 GLU   A CD  1 
ATOM   2234 O OE1 . GLU   A 1 472 ? 39.257  1.323   41.171  1.00 112.22 ?  453 GLU   A OE1 1 
ATOM   2235 O OE2 . GLU   A 1 472 ? 37.746  2.778   41.832  1.00 120.14 ?  453 GLU   A OE2 1 
ATOM   2236 N N   . LYS   A 1 473 ? 40.335  -1.868  45.403  1.00 86.87  ?  454 LYS   A N   1 
ATOM   2237 C CA  . LYS   A 1 473 ? 40.835  -3.182  45.799  1.00 89.84  ?  454 LYS   A CA  1 
ATOM   2238 C C   . LYS   A 1 473 ? 39.983  -4.306  45.224  1.00 87.23  ?  454 LYS   A C   1 
ATOM   2239 O O   . LYS   A 1 473 ? 40.506  -5.325  44.762  1.00 84.79  ?  454 LYS   A O   1 
ATOM   2240 C CB  . LYS   A 1 473 ? 40.872  -3.311  47.320  1.00 87.75  ?  454 LYS   A CB  1 
ATOM   2241 C CG  . LYS   A 1 473 ? 41.885  -2.460  48.049  1.00 88.86  ?  454 LYS   A CG  1 
ATOM   2242 C CD  . LYS   A 1 473 ? 41.762  -2.814  49.540  1.00 106.10 ?  454 LYS   A CD  1 
ATOM   2243 C CE  . LYS   A 1 473 ? 42.667  -2.001  50.496  1.00 108.91 ?  454 LYS   A CE  1 
ATOM   2244 N NZ  . LYS   A 1 473 ? 42.431  -2.328  51.958  1.00 98.20  ?  454 LYS   A NZ  1 
ATOM   2245 N N   . ILE   A 1 474 ? 38.668  -4.137  45.242  1.00 84.59  ?  455 ILE   A N   1 
ATOM   2246 C CA  . ILE   A 1 474 ? 37.794  -5.206  44.792  1.00 80.53  ?  455 ILE   A CA  1 
ATOM   2247 C C   . ILE   A 1 474 ? 37.856  -5.353  43.279  1.00 85.66  ?  455 ILE   A C   1 
ATOM   2248 O O   . ILE   A 1 474 ? 37.960  -6.473  42.763  1.00 88.85  ?  455 ILE   A O   1 
ATOM   2249 C CB  . ILE   A 1 474 ? 36.365  -4.975  45.311  1.00 84.64  ?  455 ILE   A CB  1 
ATOM   2250 C CG1 . ILE   A 1 474 ? 36.358  -5.021  46.852  1.00 86.71  ?  455 ILE   A CG1 1 
ATOM   2251 C CG2 . ILE   A 1 474 ? 35.419  -5.990  44.729  1.00 91.31  ?  455 ILE   A CG2 1 
ATOM   2252 C CD1 . ILE   A 1 474 ? 34.967  -5.029  47.468  1.00 89.71  ?  455 ILE   A CD1 1 
ATOM   2253 N N   . LYS   A 1 475 ? 37.851  -4.231  42.545  1.00 88.71  ?  456 LYS   A N   1 
ATOM   2254 C CA  . LYS   A 1 475 ? 38.004  -4.276  41.093  1.00 85.60  ?  456 LYS   A CA  1 
ATOM   2255 C C   . LYS   A 1 475 ? 39.330  -4.951  40.712  1.00 88.52  ?  456 LYS   A C   1 
ATOM   2256 O O   . LYS   A 1 475 ? 39.427  -5.608  39.666  1.00 88.73  ?  456 LYS   A O   1 
ATOM   2257 C CB  . LYS   A 1 475 ? 37.874  -2.841  40.535  1.00 78.79  ?  456 LYS   A CB  1 
ATOM   2258 C CG  . LYS   A 1 475 ? 37.668  -2.781  39.007  1.00 93.31  ?  456 LYS   A CG  1 
ATOM   2259 C CD  . LYS   A 1 475 ? 37.588  -1.400  38.268  1.00 99.94  ?  456 LYS   A CD  1 
ATOM   2260 C CE  . LYS   A 1 475 ? 36.251  -0.688  38.493  1.00 110.08 ?  456 LYS   A CE  1 
ATOM   2261 N NZ  . LYS   A 1 475 ? 35.994  0.546   37.673  1.00 110.30 ?  456 LYS   A NZ  1 
ATOM   2262 N N   . GLU   A 1 476 ? 40.322  -4.885  41.591  1.00 85.87  ?  457 GLU   A N   1 
ATOM   2263 C CA  . GLU   A 1 476 ? 41.643  -5.442  41.345  1.00 84.52  ?  457 GLU   A CA  1 
ATOM   2264 C C   . GLU   A 1 476 ? 41.764  -6.913  41.754  1.00 88.51  ?  457 GLU   A C   1 
ATOM   2265 O O   . GLU   A 1 476 ? 42.202  -7.739  40.948  1.00 90.18  ?  457 GLU   A O   1 
ATOM   2266 C CB  . GLU   A 1 476 ? 42.677  -4.607  42.086  1.00 85.16  ?  457 GLU   A CB  1 
ATOM   2267 C CG  . GLU   A 1 476 ? 44.094  -4.921  41.737  1.00 92.49  ?  457 GLU   A CG  1 
ATOM   2268 C CD  . GLU   A 1 476 ? 45.044  -4.354  42.762  1.00 106.00 ?  457 GLU   A CD  1 
ATOM   2269 O OE1 . GLU   A 1 476 ? 45.518  -3.210  42.570  1.00 115.81 ?  457 GLU   A OE1 1 
ATOM   2270 O OE2 . GLU   A 1 476 ? 45.289  -5.044  43.779  1.00 108.79 ?  457 GLU   A OE2 1 
ATOM   2271 N N   . LEU   A 1 477 ? 41.421  -7.264  43.001  1.00 85.36  ?  458 LEU   A N   1 
ATOM   2272 C CA  . LEU   A 1 477 ? 41.439  -8.675  43.378  1.00 83.48  ?  458 LEU   A CA  1 
ATOM   2273 C C   . LEU   A 1 477 ? 40.590  -9.515  42.446  1.00 87.29  ?  458 LEU   A C   1 
ATOM   2274 O O   . LEU   A 1 477 ? 40.918  -10.678 42.202  1.00 92.19  ?  458 LEU   A O   1 
ATOM   2275 C CB  . LEU   A 1 477 ? 40.948  -8.898  44.801  1.00 85.03  ?  458 LEU   A CB  1 
ATOM   2276 C CG  . LEU   A 1 477 ? 42.012  -9.188  45.845  1.00 91.48  ?  458 LEU   A CG  1 
ATOM   2277 C CD1 . LEU   A 1 477 ? 42.959  -7.997  46.006  1.00 98.38  ?  458 LEU   A CD1 1 
ATOM   2278 C CD2 . LEU   A 1 477 ? 41.308  -9.514  47.151  1.00 92.46  ?  458 LEU   A CD2 1 
ATOM   2279 N N   . HIS   A 1 478 ? 39.486  -8.970  41.939  1.00 81.15  ?  459 HIS   A N   1 
ATOM   2280 C CA  . HIS   A 1 478 ? 38.722  -9.699  40.942  1.00 78.16  ?  459 HIS   A CA  1 
ATOM   2281 C C   . HIS   A 1 478 ? 39.612  -10.082 39.774  1.00 83.00  ?  459 HIS   A C   1 
ATOM   2282 O O   . HIS   A 1 478 ? 39.700  -11.255 39.396  1.00 86.56  ?  459 HIS   A O   1 
ATOM   2283 C CB  . HIS   A 1 478 ? 37.555  -8.856  40.466  1.00 83.17  ?  459 HIS   A CB  1 
ATOM   2284 C CG  . HIS   A 1 478 ? 36.581  -9.602  39.615  1.00 81.97  ?  459 HIS   A CG  1 
ATOM   2285 N ND1 . HIS   A 1 478 ? 35.714  -10.543 40.130  1.00 80.63  ?  459 HIS   A ND1 1 
ATOM   2286 C CD2 . HIS   A 1 478 ? 36.321  -9.531  38.287  1.00 76.12  ?  459 HIS   A CD2 1 
ATOM   2287 C CE1 . HIS   A 1 478 ? 34.957  -11.016 39.154  1.00 82.00  ?  459 HIS   A CE1 1 
ATOM   2288 N NE2 . HIS   A 1 478 ? 35.307  -10.419 38.027  1.00 76.51  ?  459 HIS   A NE2 1 
ATOM   2289 N N   . GLN   A 1 479 ? 40.288  -9.088  39.196  1.00 86.78  ?  460 GLN   A N   1 
ATOM   2290 C CA  . GLN   A 1 479 ? 41.227  -9.350  38.114  1.00 86.94  ?  460 GLN   A CA  1 
ATOM   2291 C C   . GLN   A 1 479 ? 42.210  -10.441 38.499  1.00 84.12  ?  460 GLN   A C   1 
ATOM   2292 O O   . GLN   A 1 479 ? 42.452  -11.375 37.729  1.00 89.63  ?  460 GLN   A O   1 
ATOM   2293 C CB  . GLN   A 1 479 ? 41.982  -8.076  37.739  1.00 86.36  ?  460 GLN   A CB  1 
ATOM   2294 C CG  . GLN   A 1 479 ? 42.844  -8.265  36.519  1.00 90.35  ?  460 GLN   A CG  1 
ATOM   2295 C CD  . GLN   A 1 479 ? 42.058  -8.861  35.358  1.00 103.40 ?  460 GLN   A CD  1 
ATOM   2296 O OE1 . GLN   A 1 479 ? 40.945  -8.416  35.057  1.00 107.52 ?  460 GLN   A OE1 1 
ATOM   2297 N NE2 . GLN   A 1 479 ? 42.620  -9.890  34.715  1.00 101.67 ?  460 GLN   A NE2 1 
ATOM   2298 N N   . GLN   A 1 480 ? 42.783  -10.347 39.693  1.00 76.06  ?  461 GLN   A N   1 
ATOM   2299 C CA  . GLN   A 1 480 ? 43.735  -11.365 40.101  1.00 78.03  ?  461 GLN   A CA  1 
ATOM   2300 C C   . GLN   A 1 480 ? 43.062  -12.728 40.205  1.00 83.48  ?  461 GLN   A C   1 
ATOM   2301 O O   . GLN   A 1 480 ? 43.650  -13.748 39.827  1.00 81.69  ?  461 GLN   A O   1 
ATOM   2302 C CB  . GLN   A 1 480 ? 44.392  -10.960 41.413  1.00 75.59  ?  461 GLN   A CB  1 
ATOM   2303 C CG  . GLN   A 1 480 ? 45.085  -9.622  41.320  1.00 77.47  ?  461 GLN   A CG  1 
ATOM   2304 C CD  . GLN   A 1 480 ? 45.876  -9.275  42.564  1.00 86.19  ?  461 GLN   A CD  1 
ATOM   2305 O OE1 . GLN   A 1 480 ? 45.934  -10.046 43.529  1.00 88.28  ?  461 GLN   A OE1 1 
ATOM   2306 N NE2 . GLN   A 1 480 ? 46.489  -8.102  42.551  1.00 90.08  ?  461 GLN   A NE2 1 
ATOM   2307 N N   . TYR   A 1 481 ? 41.815  -12.763 40.680  1.00 83.80  ?  462 TYR   A N   1 
ATOM   2308 C CA  . TYR   A 1 481 ? 41.127  -14.038 40.832  1.00 74.35  ?  462 TYR   A CA  1 
ATOM   2309 C C   . TYR   A 1 481 ? 40.791  -14.645 39.481  1.00 80.35  ?  462 TYR   A C   1 
ATOM   2310 O O   . TYR   A 1 481 ? 40.981  -15.851 39.278  1.00 81.88  ?  462 TYR   A O   1 
ATOM   2311 C CB  . TYR   A 1 481 ? 39.861  -13.872 41.665  1.00 73.98  ?  462 TYR   A CB  1 
ATOM   2312 C CG  . TYR   A 1 481 ? 38.902  -15.051 41.584  1.00 79.42  ?  462 TYR   A CG  1 
ATOM   2313 C CD1 . TYR   A 1 481 ? 37.831  -15.047 40.687  1.00 77.61  ?  462 TYR   A CD1 1 
ATOM   2314 C CD2 . TYR   A 1 481 ? 39.059  -16.165 42.412  1.00 75.36  ?  462 TYR   A CD2 1 
ATOM   2315 C CE1 . TYR   A 1 481 ? 36.951  -16.115 40.613  1.00 76.01  ?  462 TYR   A CE1 1 
ATOM   2316 C CE2 . TYR   A 1 481 ? 38.184  -17.240 42.345  1.00 74.51  ?  462 TYR   A CE2 1 
ATOM   2317 C CZ  . TYR   A 1 481 ? 37.128  -17.210 41.444  1.00 80.36  ?  462 TYR   A CZ  1 
ATOM   2318 O OH  . TYR   A 1 481 ? 36.245  -18.275 41.368  1.00 79.36  ?  462 TYR   A OH  1 
ATOM   2319 N N   . LYS   A 1 482 ? 40.284  -13.851 38.535  1.00 80.46  ?  463 LYS   A N   1 
ATOM   2320 C CA  . LYS   A 1 482 ? 39.925  -14.493 37.276  1.00 86.07  ?  463 LYS   A CA  1 
ATOM   2321 C C   . LYS   A 1 482 ? 41.175  -14.918 36.496  1.00 87.23  ?  463 LYS   A C   1 
ATOM   2322 O O   . LYS   A 1 482 ? 41.143  -15.950 35.817  1.00 86.64  ?  463 LYS   A O   1 
ATOM   2323 C CB  . LYS   A 1 482 ? 38.977  -13.615 36.443  1.00 77.35  ?  463 LYS   A CB  1 
ATOM   2324 C CG  . LYS   A 1 482 ? 39.561  -12.402 35.781  1.00 88.00  ?  463 LYS   A CG  1 
ATOM   2325 C CD  . LYS   A 1 482 ? 38.657  -11.960 34.604  1.00 102.06 ?  463 LYS   A CD  1 
ATOM   2326 C CE  . LYS   A 1 482 ? 39.072  -10.585 34.047  1.00 104.52 ?  463 LYS   A CE  1 
ATOM   2327 N NZ  . LYS   A 1 482 ? 38.412  -10.190 32.770  1.00 106.58 ?  463 LYS   A NZ  1 
ATOM   2328 N N   . GLU   A 1 483 ? 42.296  -14.197 36.643  1.00 79.91  ?  464 GLU   A N   1 
ATOM   2329 C CA  . GLU   A 1 483 ? 43.563  -14.662 36.076  1.00 75.77  ?  464 GLU   A CA  1 
ATOM   2330 C C   . GLU   A 1 483 ? 44.001  -15.989 36.690  1.00 81.13  ?  464 GLU   A C   1 
ATOM   2331 O O   . GLU   A 1 483 ? 44.506  -16.876 35.993  1.00 80.74  ?  464 GLU   A O   1 
ATOM   2332 C CB  . GLU   A 1 483 ? 44.658  -13.622 36.288  1.00 73.24  ?  464 GLU   A CB  1 
ATOM   2333 C CG  . GLU   A 1 483 ? 44.705  -12.525 35.244  1.00 90.28  ?  464 GLU   A CG  1 
ATOM   2334 C CD  . GLU   A 1 483 ? 45.754  -11.452 35.557  1.00 98.53  ?  464 GLU   A CD  1 
ATOM   2335 O OE1 . GLU   A 1 483 ? 45.767  -10.397 34.871  1.00 95.73  ?  464 GLU   A OE1 1 
ATOM   2336 O OE2 . GLU   A 1 483 ? 46.570  -11.674 36.484  1.00 102.88 ?  464 GLU   A OE2 1 
ATOM   2337 N N   . ALA   A 1 484 ? 43.862  -16.133 37.999  1.00 79.24  ?  465 ALA   A N   1 
ATOM   2338 C CA  . ALA   A 1 484 ? 44.275  -17.375 38.618  1.00 73.69  ?  465 ALA   A CA  1 
ATOM   2339 C C   . ALA   A 1 484 ? 43.323  -18.511 38.293  1.00 81.53  ?  465 ALA   A C   1 
ATOM   2340 O O   . ALA   A 1 484 ? 43.693  -19.676 38.468  1.00 79.50  ?  465 ALA   A O   1 
ATOM   2341 C CB  . ALA   A 1 484 ? 44.390  -17.197 40.130  1.00 73.72  ?  465 ALA   A CB  1 
ATOM   2342 N N   . SER   A 1 485 ? 42.107  -18.200 37.837  1.00 83.45  ?  466 SER   A N   1 
ATOM   2343 C CA  . SER   A 1 485 ? 41.168  -19.211 37.367  1.00 85.48  ?  466 SER   A CA  1 
ATOM   2344 C C   . SER   A 1 485 ? 41.378  -19.566 35.902  1.00 87.14  ?  466 SER   A C   1 
ATOM   2345 O O   . SER   A 1 485 ? 40.974  -20.659 35.475  1.00 86.07  ?  466 SER   A O   1 
ATOM   2346 C CB  . SER   A 1 485 ? 39.728  -18.725 37.552  1.00 84.26  ?  466 SER   A CB  1 
ATOM   2347 O OG  . SER   A 1 485 ? 39.394  -18.650 38.920  1.00 84.56  ?  466 SER   A OG  1 
ATOM   2348 N N   . GLU   A 1 486 ? 41.891  -18.622 35.133  1.00 90.87  ?  467 GLU   A N   1 
ATOM   2349 C CA  . GLU   A 1 486 ? 42.099  -18.924 33.703  1.00 86.65  ?  467 GLU   A CA  1 
ATOM   2350 C C   . GLU   A 1 486 ? 43.215  -19.956 33.609  1.00 83.88  ?  467 GLU   A C   1 
ATOM   2351 O O   . GLU   A 1 486 ? 43.334  -20.580 32.586  1.00 98.32  ?  467 GLU   A O   1 
ATOM   2352 C CB  . GLU   A 1 486 ? 42.284  -17.640 32.894  1.00 96.56  ?  467 GLU   A CB  1 
ATOM   2353 C CG  . GLU   A 1 486 ? 41.556  -16.457 33.500  1.00 101.92 ?  467 GLU   A CG  1 
ATOM   2354 C CD  . GLU   A 1 486 ? 40.425  -15.860 32.689  1.00 113.75 ?  467 GLU   A CD  1 
ATOM   2355 O OE1 . GLU   A 1 486 ? 40.662  -14.869 31.987  1.00 125.29 ?  467 GLU   A OE1 1 
ATOM   2356 O OE2 . GLU   A 1 486 ? 39.307  -16.372 32.789  1.00 106.39 ?  467 GLU   A OE2 1 
ATOM   2357 N N   . VAL   A 1 487 ? 43.964  -20.181 34.671  1.00 72.80  ?  468 VAL   A N   1 
ATOM   2358 C CA  . VAL   A 1 487 ? 44.989  -21.239 34.534  1.00 73.80  ?  468 VAL   A CA  1 
ATOM   2359 C C   . VAL   A 1 487 ? 44.185  -22.512 34.634  1.00 76.02  ?  468 VAL   A C   1 
ATOM   2360 O O   . VAL   A 1 487 ? 43.757  -22.812 35.692  1.00 77.23  ?  468 VAL   A O   1 
ATOM   2361 C CB  . VAL   A 1 487 ? 45.974  -21.186 35.696  1.00 63.93  ?  468 VAL   A CB  1 
ATOM   2362 C CG1 . VAL   A 1 487 ? 46.565  -22.542 35.957  1.00 58.94  ?  468 VAL   A CG1 1 
ATOM   2363 C CG2 . VAL   A 1 487 ? 47.063  -20.185 35.430  1.00 66.46  ?  468 VAL   A CG2 1 
ATOM   2364 N N   . LYS   A 1 488 ? 44.038  -23.238 33.544  1.00 84.22  ?  469 LYS   A N   1 
ATOM   2365 C CA  . LYS   A 1 488 ? 43.175  -24.432 33.563  1.00 81.68  ?  469 LYS   A CA  1 
ATOM   2366 C C   . LYS   A 1 488 ? 43.811  -25.548 34.366  1.00 81.43  ?  469 LYS   A C   1 
ATOM   2367 O O   . LYS   A 1 488 ? 45.016  -25.648 34.393  1.00 78.77  ?  469 LYS   A O   1 
ATOM   2368 C CB  . LYS   A 1 488 ? 42.870  -24.879 32.138  1.00 86.71  ?  469 LYS   A CB  1 
ATOM   2369 C CG  . LYS   A 1 488 ? 41.934  -23.949 31.390  1.00 94.93  ?  469 LYS   A CG  1 
ATOM   2370 C CD  . LYS   A 1 488 ? 41.100  -23.104 32.323  1.00 98.64  ?  469 LYS   A CD  1 
ATOM   2371 C CE  . LYS   A 1 488 ? 39.915  -23.845 32.908  1.00 105.97 ?  469 LYS   A CE  1 
ATOM   2372 N NZ  . LYS   A 1 488 ? 38.639  -23.135 32.669  1.00 106.26 ?  469 LYS   A NZ  1 
ATOM   2373 N N   . PRO   A 1 489 ? 42.993  -26.400 34.992  1.00 82.86  ?  470 PRO   A N   1 
ATOM   2374 C CA  . PRO   A 1 489 ? 43.448  -27.526 35.751  1.00 79.25  ?  470 PRO   A CA  1 
ATOM   2375 C C   . PRO   A 1 489 ? 43.958  -28.601 34.799  1.00 80.87  ?  470 PRO   A C   1 
ATOM   2376 O O   . PRO   A 1 489 ? 43.527  -28.667 33.702  1.00 80.26  ?  470 PRO   A O   1 
ATOM   2377 C CB  . PRO   A 1 489 ? 42.168  -28.059 36.374  1.00 79.16  ?  470 PRO   A CB  1 
ATOM   2378 C CG  . PRO   A 1 489 ? 41.273  -26.894 36.360  1.00 77.45  ?  470 PRO   A CG  1 
ATOM   2379 C CD  . PRO   A 1 489 ? 41.563  -26.306 35.009  1.00 86.53  ?  470 PRO   A CD  1 
ATOM   2380 N N   . PRO   A 1 490 ? 44.884  -29.463 35.233  1.00 84.69  ?  471 PRO   A N   1 
ATOM   2381 C CA  . PRO   A 1 490 ? 45.082  -29.774 36.631  1.00 81.04  ?  471 PRO   A CA  1 
ATOM   2382 C C   . PRO   A 1 490 ? 46.222  -28.889 37.127  1.00 82.06  ?  471 PRO   A C   1 
ATOM   2383 O O   . PRO   A 1 490 ? 47.097  -28.620 36.367  1.00 82.96  ?  471 PRO   A O   1 
ATOM   2384 C CB  . PRO   A 1 490 ? 45.524  -31.228 36.567  1.00 77.19  ?  471 PRO   A CB  1 
ATOM   2385 C CG  . PRO   A 1 490 ? 45.798  -31.499 35.110  1.00 85.02  ?  471 PRO   A CG  1 
ATOM   2386 C CD  . PRO   A 1 490 ? 45.824  -30.167 34.410  1.00 75.67  ?  471 PRO   A CD  1 
ATOM   2387 N N   . ARG   A 1 491 ? 46.149  -28.429 38.368  1.00 74.50  ?  472 ARG   A N   1 
ATOM   2388 C CA  . ARG   A 1 491 ? 47.196  -27.496 38.824  1.00 69.98  ?  472 ARG   A CA  1 
ATOM   2389 C C   . ARG   A 1 491 ? 47.804  -27.982 40.119  1.00 65.83  ?  472 ARG   A C   1 
ATOM   2390 O O   . ARG   A 1 491 ? 47.172  -28.724 40.809  1.00 78.94  ?  472 ARG   A O   1 
ATOM   2391 C CB  . ARG   A 1 491 ? 46.592  -26.123 39.096  1.00 67.41  ?  472 ARG   A CB  1 
ATOM   2392 C CG  . ARG   A 1 491 ? 45.092  -26.047 38.911  1.00 69.77  ?  472 ARG   A CG  1 
ATOM   2393 C CD  . ARG   A 1 491 ? 44.655  -24.614 39.035  1.00 76.05  ?  472 ARG   A CD  1 
ATOM   2394 N NE  . ARG   A 1 491 ? 43.302  -24.588 39.536  1.00 81.03  ?  472 ARG   A NE  1 
ATOM   2395 C CZ  . ARG   A 1 491 ? 42.323  -23.920 38.981  1.00 80.71  ?  472 ARG   A CZ  1 
ATOM   2396 N NH1 . ARG   A 1 491 ? 42.549  -23.205 37.909  1.00 72.55  ?  472 ARG   A NH1 1 
ATOM   2397 N NH2 . ARG   A 1 491 ? 41.116  -23.960 39.489  1.00 86.60  ?  472 ARG   A NH2 1 
ATOM   2398 N N   . ASP   A 1 492 ? 49.016  -27.544 40.404  1.00 62.55  ?  473 ASP   A N   1 
ATOM   2399 C CA  . ASP   A 1 492 ? 49.681  -27.932 41.659  1.00 66.25  ?  473 ASP   A CA  1 
ATOM   2400 C C   . ASP   A 1 492 ? 49.048  -27.161 42.804  1.00 69.42  ?  473 ASP   A C   1 
ATOM   2401 O O   . ASP   A 1 492 ? 48.575  -26.092 42.582  1.00 70.61  ?  473 ASP   A O   1 
ATOM   2402 C CB  . ASP   A 1 492 ? 51.191  -27.784 41.551  1.00 64.96  ?  473 ASP   A CB  1 
ATOM   2403 C CG  . ASP   A 1 492 ? 51.656  -26.356 41.597  1.00 79.94  ?  473 ASP   A CG  1 
ATOM   2404 O OD1 . ASP   A 1 492 ? 52.850  -26.145 41.716  1.00 83.02  ?  473 ASP   A OD1 1 
ATOM   2405 O OD2 . ASP   A 1 492 ? 50.816  -25.491 41.519  1.00 76.70  ?  473 ASP   A OD2 1 
ATOM   2406 N N   . ILE   A 1 493 ? 49.133  -27.692 44.005  1.00 71.63  ?  474 ILE   A N   1 
ATOM   2407 C CA  . ILE   A 1 493 ? 48.472  -27.081 45.183  1.00 71.78  ?  474 ILE   A CA  1 
ATOM   2408 C C   . ILE   A 1 493 ? 48.767  -25.597 45.358  1.00 69.01  ?  474 ILE   A C   1 
ATOM   2409 O O   . ILE   A 1 493 ? 47.887  -24.927 45.842  1.00 70.43  ?  474 ILE   A O   1 
ATOM   2410 C CB  . ILE   A 1 493 ? 48.739  -27.912 46.438  1.00 68.39  ?  474 ILE   A CB  1 
ATOM   2411 C CG1 . ILE   A 1 493 ? 47.430  -28.229 47.143  1.00 67.70  ?  474 ILE   A CG1 1 
ATOM   2412 C CG2 . ILE   A 1 493 ? 49.711  -27.230 47.359  1.00 66.96  ?  474 ILE   A CG2 1 
ATOM   2413 C CD1 . ILE   A 1 493 ? 46.301  -28.375 46.194  1.00 74.76  ?  474 ILE   A CD1 1 
ATOM   2414 N N   . THR   A 1 494 ? 49.918  -25.081 44.954  1.00 68.51  ?  475 THR   A N   1 
ATOM   2415 C CA  . THR   A 1 494 ? 50.084  -23.648 45.187  1.00 70.17  ?  475 THR   A CA  1 
ATOM   2416 C C   . THR   A 1 494 ? 49.257  -22.835 44.196  1.00 69.87  ?  475 THR   A C   1 
ATOM   2417 O O   . THR   A 1 494 ? 48.768  -21.752 44.537  1.00 73.15  ?  475 THR   A O   1 
ATOM   2418 C CB  . THR   A 1 494 ? 51.556  -23.221 45.122  1.00 66.62  ?  475 THR   A CB  1 
ATOM   2419 O OG1 . THR   A 1 494 ? 52.001  -23.206 43.765  1.00 76.33  ?  475 THR   A OG1 1 
ATOM   2420 C CG2 . THR   A 1 494 ? 52.444  -24.156 45.938  1.00 65.57  ?  475 THR   A CG2 1 
ATOM   2421 N N   . ALA   A 1 495 ? 49.072  -23.349 42.979  1.00 70.01  ?  476 ALA   A N   1 
ATOM   2422 C CA  . ALA   A 1 495 ? 48.123  -22.752 42.048  1.00 64.00  ?  476 ALA   A CA  1 
ATOM   2423 C C   . ALA   A 1 495 ? 46.691  -22.880 42.555  1.00 71.82  ?  476 ALA   A C   1 
ATOM   2424 O O   . ALA   A 1 495 ? 45.870  -21.971 42.371  1.00 68.76  ?  476 ALA   A O   1 
ATOM   2425 C CB  . ALA   A 1 495 ? 48.259  -23.421 40.691  1.00 64.05  ?  476 ALA   A CB  1 
ATOM   2426 N N   . GLU   A 1 496 ? 46.365  -24.017 43.171  1.00 77.11  ?  477 GLU   A N   1 
ATOM   2427 C CA  . GLU   A 1 496 ? 45.033  -24.192 43.731  1.00 73.59  ?  477 GLU   A CA  1 
ATOM   2428 C C   . GLU   A 1 496 ? 44.820  -23.251 44.905  1.00 73.65  ?  477 GLU   A C   1 
ATOM   2429 O O   . GLU   A 1 496 ? 43.747  -22.654 45.043  1.00 77.89  ?  477 GLU   A O   1 
ATOM   2430 C CB  . GLU   A 1 496 ? 44.831  -25.653 44.139  1.00 70.32  ?  477 GLU   A CB  1 
ATOM   2431 C CG  . GLU   A 1 496 ? 43.366  -26.059 44.295  1.00 79.32  ?  477 GLU   A CG  1 
ATOM   2432 C CD  . GLU   A 1 496 ? 42.573  -26.024 42.991  1.00 84.78  ?  477 GLU   A CD  1 
ATOM   2433 O OE1 . GLU   A 1 496 ? 43.159  -26.197 41.895  1.00 81.89  ?  477 GLU   A OE1 1 
ATOM   2434 O OE2 . GLU   A 1 496 ? 41.346  -25.808 43.065  1.00 90.88  ?  477 GLU   A OE2 1 
ATOM   2435 N N   . PHE   A 1 497 ? 45.851  -23.100 45.710  1.00 73.93  ?  478 PHE   A N   1 
ATOM   2436 C CA  . PHE   A 1 497 ? 45.742  -22.228 46.893  1.00 74.09  ?  478 PHE   A CA  1 
ATOM   2437 C C   . PHE   A 1 497 ? 45.504  -20.813 46.430  1.00 77.61  ?  478 PHE   A C   1 
ATOM   2438 O O   . PHE   A 1 497 ? 44.762  -20.106 47.044  1.00 84.21  ?  478 PHE   A O   1 
ATOM   2439 C CB  . PHE   A 1 497 ? 47.086  -22.143 47.588  1.00 76.21  ?  478 PHE   A CB  1 
ATOM   2440 C CG  . PHE   A 1 497 ? 47.100  -21.228 48.774  1.00 80.47  ?  478 PHE   A CG  1 
ATOM   2441 C CD1 . PHE   A 1 497 ? 46.229  -21.421 49.817  1.00 82.46  ?  478 PHE   A CD1 1 
ATOM   2442 C CD2 . PHE   A 1 497 ? 48.008  -20.201 48.860  1.00 82.65  ?  478 PHE   A CD2 1 
ATOM   2443 C CE1 . PHE   A 1 497 ? 46.260  -20.595 50.920  1.00 87.07  ?  478 PHE   A CE1 1 
ATOM   2444 C CE2 . PHE   A 1 497 ? 48.033  -19.370 49.961  1.00 87.70  ?  478 PHE   A CE2 1 
ATOM   2445 C CZ  . PHE   A 1 497 ? 47.158  -19.569 50.987  1.00 88.23  ?  478 PHE   A CZ  1 
ATOM   2446 N N   . LEU   A 1 498 ? 46.152  -20.419 45.358  1.00 77.00  ?  479 LEU   A N   1 
ATOM   2447 C CA  . LEU   A 1 498 ? 45.980  -19.022 44.929  1.00 74.57  ?  479 LEU   A CA  1 
ATOM   2448 C C   . LEU   A 1 498 ? 44.536  -18.777 44.544  1.00 74.54  ?  479 LEU   A C   1 
ATOM   2449 O O   . LEU   A 1 498 ? 44.033  -17.749 44.848  1.00 80.63  ?  479 LEU   A O   1 
ATOM   2450 C CB  . LEU   A 1 498 ? 46.893  -18.753 43.744  1.00 69.79  ?  479 LEU   A CB  1 
ATOM   2451 C CG  . LEU   A 1 498 ? 47.059  -17.278 43.434  1.00 69.47  ?  479 LEU   A CG  1 
ATOM   2452 C CD1 . LEU   A 1 498 ? 48.162  -16.694 44.271  1.00 71.08  ?  479 LEU   A CD1 1 
ATOM   2453 C CD2 . LEU   A 1 498 ? 47.350  -17.074 41.977  1.00 56.86  ?  479 LEU   A CD2 1 
ATOM   2454 N N   . VAL   A 1 499 ? 43.919  -19.690 43.834  1.00 76.54  ?  480 VAL   A N   1 
ATOM   2455 C CA  . VAL   A 1 499 ? 42.517  -19.405 43.464  1.00 81.38  ?  480 VAL   A CA  1 
ATOM   2456 C C   . VAL   A 1 499 ? 41.689  -19.347 44.734  1.00 80.41  ?  480 VAL   A C   1 
ATOM   2457 O O   . VAL   A 1 499 ? 40.920  -18.441 44.879  1.00 81.62  ?  480 VAL   A O   1 
ATOM   2458 C CB  . VAL   A 1 499 ? 41.992  -20.471 42.502  1.00 81.72  ?  480 VAL   A CB  1 
ATOM   2459 C CG1 . VAL   A 1 499 ? 40.485  -20.549 42.541  1.00 80.85  ?  480 VAL   A CG1 1 
ATOM   2460 C CG2 . VAL   A 1 499 ? 42.457  -20.187 41.097  1.00 82.41  ?  480 VAL   A CG2 1 
ATOM   2461 N N   . LYS   A 1 500 ? 41.875  -20.291 45.633  1.00 78.76  ?  481 LYS   A N   1 
ATOM   2462 C CA  . LYS   A 1 500 ? 41.061  -20.263 46.864  1.00 84.99  ?  481 LYS   A CA  1 
ATOM   2463 C C   . LYS   A 1 500 ? 41.411  -19.038 47.695  1.00 86.31  ?  481 LYS   A C   1 
ATOM   2464 O O   . LYS   A 1 500 ? 40.507  -18.414 48.211  1.00 87.84  ?  481 LYS   A O   1 
ATOM   2465 C CB  . LYS   A 1 500 ? 41.312  -21.518 47.688  1.00 83.52  ?  481 LYS   A CB  1 
ATOM   2466 C CG  . LYS   A 1 500 ? 41.053  -22.817 46.957  1.00 81.98  ?  481 LYS   A CG  1 
ATOM   2467 C CD  . LYS   A 1 500 ? 39.670  -23.326 47.170  1.00 91.24  ?  481 LYS   A CD  1 
ATOM   2468 C CE  . LYS   A 1 500 ? 39.436  -24.655 46.500  1.00 91.19  ?  481 LYS   A CE  1 
ATOM   2469 N NZ  . LYS   A 1 500 ? 40.006  -25.745 47.312  1.00 93.75  ?  481 LYS   A NZ  1 
ATOM   2470 N N   . SER   A 1 501 ? 42.687  -18.708 47.811  1.00 84.46  ?  482 SER   A N   1 
ATOM   2471 C CA  . SER   A 1 501 ? 43.024  -17.561 48.678  1.00 83.23  ?  482 SER   A CA  1 
ATOM   2472 C C   . SER   A 1 501 ? 42.392  -16.295 48.123  1.00 84.94  ?  482 SER   A C   1 
ATOM   2473 O O   . SER   A 1 501 ? 41.706  -15.644 48.845  1.00 91.16  ?  482 SER   A O   1 
ATOM   2474 C CB  . SER   A 1 501 ? 44.499  -17.440 48.817  1.00 82.75  ?  482 SER   A CB  1 
ATOM   2475 O OG  . SER   A 1 501 ? 44.964  -16.142 48.515  1.00 94.16  ?  482 SER   A OG  1 
ATOM   2476 N N   . LYS   A 1 502 ? 42.510  -16.049 46.832  1.00 81.20  ?  483 LYS   A N   1 
ATOM   2477 C CA  . LYS   A 1 502 ? 41.943  -14.811 46.257  1.00 82.05  ?  483 LYS   A CA  1 
ATOM   2478 C C   . LYS   A 1 502 ? 40.431  -14.821 46.414  1.00 82.85  ?  483 LYS   A C   1 
ATOM   2479 O O   . LYS   A 1 502 ? 39.873  -13.771 46.581  1.00 86.92  ?  483 LYS   A O   1 
ATOM   2480 C CB  . LYS   A 1 502 ? 42.381  -14.612 44.808  1.00 80.25  ?  483 LYS   A CB  1 
ATOM   2481 C CG  . LYS   A 1 502 ? 43.871  -14.412 44.605  1.00 74.66  ?  483 LYS   A CG  1 
ATOM   2482 C CD  . LYS   A 1 502 ? 44.317  -13.002 44.808  1.00 88.99  ?  483 LYS   A CD  1 
ATOM   2483 C CE  . LYS   A 1 502 ? 45.810  -12.821 44.648  1.00 90.12  ?  483 LYS   A CE  1 
ATOM   2484 N NZ  . LYS   A 1 502 ? 46.475  -12.352 45.886  1.00 89.88  ?  483 LYS   A NZ  1 
ATOM   2485 N N   . HIS   A 1 503 ? 39.790  -15.964 46.264  1.00 81.50  ?  484 HIS   A N   1 
ATOM   2486 C CA  . HIS   A 1 503 ? 38.327  -16.016 46.442  1.00 84.99  ?  484 HIS   A CA  1 
ATOM   2487 C C   . HIS   A 1 503 ? 37.973  -15.643 47.869  1.00 90.16  ?  484 HIS   A C   1 
ATOM   2488 O O   . HIS   A 1 503 ? 37.045  -14.894 48.068  1.00 90.96  ?  484 HIS   A O   1 
ATOM   2489 C CB  . HIS   A 1 503 ? 37.885  -17.454 46.277  1.00 84.33  ?  484 HIS   A CB  1 
ATOM   2490 C CG  . HIS   A 1 503 ? 36.414  -17.617 46.274  1.00 88.76  ?  484 HIS   A CG  1 
ATOM   2491 N ND1 . HIS   A 1 503 ? 35.654  -17.283 45.198  1.00 87.14  ?  484 HIS   A ND1 1 
ATOM   2492 C CD2 . HIS   A 1 503 ? 35.572  -18.091 47.202  1.00 93.22  ?  484 HIS   A CD2 1 
ATOM   2493 C CE1 . HIS   A 1 503 ? 34.403  -17.549 45.448  1.00 93.09  ?  484 HIS   A CE1 1 
ATOM   2494 N NE2 . HIS   A 1 503 ? 34.330  -18.041 46.663  1.00 103.54 ?  484 HIS   A NE2 1 
ATOM   2495 N N   . ARG   A 1 504 ? 38.699  -16.166 48.836  1.00 88.51  ?  485 ARG   A N   1 
ATOM   2496 C CA  . ARG   A 1 504 ? 38.318  -15.839 50.221  1.00 87.43  ?  485 ARG   A CA  1 
ATOM   2497 C C   . ARG   A 1 504 ? 38.498  -14.350 50.445  1.00 90.36  ?  485 ARG   A C   1 
ATOM   2498 O O   . ARG   A 1 504 ? 37.578  -13.708 50.902  1.00 91.27  ?  485 ARG   A O   1 
ATOM   2499 C CB  . ARG   A 1 504 ? 39.245  -16.574 51.175  1.00 87.87  ?  485 ARG   A CB  1 
ATOM   2500 C CG  . ARG   A 1 504 ? 39.019  -16.198 52.624  1.00 98.57  ?  485 ARG   A CG  1 
ATOM   2501 C CD  . ARG   A 1 504 ? 40.012  -15.150 53.029  1.00 97.96  ?  485 ARG   A CD  1 
ATOM   2502 N NE  . ARG   A 1 504 ? 39.598  -14.647 54.315  1.00 104.10 ?  485 ARG   A NE  1 
ATOM   2503 C CZ  . ARG   A 1 504 ? 39.868  -13.436 54.745  1.00 104.77 ?  485 ARG   A CZ  1 
ATOM   2504 N NH1 . ARG   A 1 504 ? 39.446  -13.052 55.931  1.00 115.07 ?  485 ARG   A NH1 1 
ATOM   2505 N NH2 . ARG   A 1 504 ? 40.562  -12.612 53.991  1.00 95.84  ?  485 ARG   A NH2 1 
ATOM   2506 N N   . ASP   A 1 505 ? 39.616  -13.812 49.998  1.00 90.67  ?  486 ASP   A N   1 
ATOM   2507 C CA  . ASP   A 1 505 ? 39.898  -12.377 50.193  1.00 86.67  ?  486 ASP   A CA  1 
ATOM   2508 C C   . ASP   A 1 505 ? 38.855  -11.554 49.470  1.00 87.36  ?  486 ASP   A C   1 
ATOM   2509 O O   . ASP   A 1 505 ? 38.442  -10.559 49.999  1.00 88.15  ?  486 ASP   A O   1 
ATOM   2510 C CB  . ASP   A 1 505 ? 41.268  -12.034 49.634  1.00 87.88  ?  486 ASP   A CB  1 
ATOM   2511 C CG  . ASP   A 1 505 ? 42.361  -12.657 50.460  1.00 93.04  ?  486 ASP   A CG  1 
ATOM   2512 O OD1 . ASP   A 1 505 ? 42.026  -13.159 51.508  1.00 95.71  ?  486 ASP   A OD1 1 
ATOM   2513 O OD2 . ASP   A 1 505 ? 43.521  -12.613 50.058  1.00 93.53  ?  486 ASP   A OD2 1 
ATOM   2514 N N   . LEU   A 1 506 ? 38.469  -11.954 48.281  1.00 86.76  ?  487 LEU   A N   1 
ATOM   2515 C CA  . LEU   A 1 506 ? 37.486  -11.101 47.601  1.00 90.02  ?  487 LEU   A CA  1 
ATOM   2516 C C   . LEU   A 1 506 ? 36.179  -11.113 48.381  1.00 89.18  ?  487 LEU   A C   1 
ATOM   2517 O O   . LEU   A 1 506 ? 35.666  -10.051 48.631  1.00 92.06  ?  487 LEU   A O   1 
ATOM   2518 C CB  . LEU   A 1 506 ? 37.315  -11.582 46.169  1.00 85.22  ?  487 LEU   A CB  1 
ATOM   2519 C CG  . LEU   A 1 506 ? 36.716  -10.532 45.259  1.00 84.46  ?  487 LEU   A CG  1 
ATOM   2520 C CD1 . LEU   A 1 506 ? 36.897  -10.926 43.820  1.00 93.61  ?  487 LEU   A CD1 1 
ATOM   2521 C CD2 . LEU   A 1 506 ? 35.251  -10.389 45.574  1.00 93.75  ?  487 LEU   A CD2 1 
ATOM   2522 N N   . THR   A 1 507 ? 35.672  -12.271 48.776  1.00 90.97  ?  488 THR   A N   1 
ATOM   2523 C CA  . THR   A 1 507 ? 34.407  -12.250 49.517  1.00 94.40  ?  488 THR   A CA  1 
ATOM   2524 C C   . THR   A 1 507 ? 34.525  -11.469 50.830  1.00 92.29  ?  488 THR   A C   1 
ATOM   2525 O O   . THR   A 1 507 ? 33.556  -10.828 51.255  1.00 90.88  ?  488 THR   A O   1 
ATOM   2526 C CB  . THR   A 1 507 ? 33.901  -13.669 49.797  1.00 83.95  ?  488 THR   A CB  1 
ATOM   2527 O OG1 . THR   A 1 507 ? 34.908  -14.408 50.492  1.00 86.05  ?  488 THR   A OG1 1 
ATOM   2528 C CG2 . THR   A 1 507 ? 33.539  -14.381 48.497  1.00 86.14  ?  488 THR   A CG2 1 
ATOM   2529 N N   . ALA   A 1 508 ? 35.696  -11.498 51.477  1.00 88.10  ?  489 ALA   A N   1 
ATOM   2530 C CA  . ALA   A 1 508 ? 35.923  -10.667 52.658  1.00 84.83  ?  489 ALA   A CA  1 
ATOM   2531 C C   . ALA   A 1 508 ? 35.757  -9.180  52.325  1.00 94.44  ?  489 ALA   A C   1 
ATOM   2532 O O   . ALA   A 1 508 ? 34.862  -8.504  52.848  1.00 99.30  ?  489 ALA   A O   1 
ATOM   2533 C CB  . ALA   A 1 508 ? 37.310  -10.956 53.244  1.00 77.24  ?  489 ALA   A CB  1 
ATOM   2534 N N   . LEU   A 1 509 ? 36.606  -8.654  51.446  1.00 89.77  ?  490 LEU   A N   1 
ATOM   2535 C CA  . LEU   A 1 509 ? 36.428  -7.280  50.996  1.00 88.43  ?  490 LEU   A CA  1 
ATOM   2536 C C   . LEU   A 1 509 ? 35.031  -7.012  50.458  1.00 93.07  ?  490 LEU   A C   1 
ATOM   2537 O O   . LEU   A 1 509 ? 34.555  -5.878  50.539  1.00 101.21 ?  490 LEU   A O   1 
ATOM   2538 C CB  . LEU   A 1 509 ? 37.480  -6.937  49.953  1.00 87.68  ?  490 LEU   A CB  1 
ATOM   2539 C CG  . LEU   A 1 509 ? 38.775  -6.405  50.552  1.00 85.02  ?  490 LEU   A CG  1 
ATOM   2540 C CD1 . LEU   A 1 509 ? 39.527  -7.418  51.408  1.00 86.78  ?  490 LEU   A CD1 1 
ATOM   2541 C CD2 . LEU   A 1 509 ? 39.631  -5.922  49.367  1.00 86.45  ?  490 LEU   A CD2 1 
ATOM   2542 N N   . CYS   A 1 510 ? 34.353  -8.011  49.901  1.00 93.62  ?  491 CYS   A N   1 
ATOM   2543 C CA  . CYS   A 1 510 ? 32.992  -7.735  49.457  1.00 96.18  ?  491 CYS   A CA  1 
ATOM   2544 C C   . CYS   A 1 510 ? 32.022  -7.632  50.624  1.00 97.80  ?  491 CYS   A C   1 
ATOM   2545 O O   . CYS   A 1 510 ? 30.977  -6.983  50.497  1.00 97.36  ?  491 CYS   A O   1 
ATOM   2546 C CB  . CYS   A 1 510 ? 32.519  -8.791  48.462  1.00 93.86  ?  491 CYS   A CB  1 
ATOM   2547 S SG  . CYS   A 1 510 ? 32.982  -8.390  46.779  1.00 96.21  ?  491 CYS   A SG  1 
ATOM   2548 N N   . LYS   A 1 511 ? 32.342  -8.235  51.762  1.00 96.67  ?  492 LYS   A N   1 
ATOM   2549 C CA  . LYS   A 1 511 ? 31.443  -8.085  52.894  1.00 101.55 ?  492 LYS   A CA  1 
ATOM   2550 C C   . LYS   A 1 511 ? 31.622  -6.712  53.539  1.00 103.74 ?  492 LYS   A C   1 
ATOM   2551 O O   . LYS   A 1 511 ? 30.634  -6.053  53.880  1.00 105.35 ?  492 LYS   A O   1 
ATOM   2552 C CB  . LYS   A 1 511 ? 31.664  -9.221  53.897  1.00 96.09  ?  492 LYS   A CB  1 
ATOM   2553 C CG  . LYS   A 1 511 ? 30.386  -9.670  54.595  1.00 104.49 ?  492 LYS   A CG  1 
ATOM   2554 C CD  . LYS   A 1 511 ? 30.676  -10.605 55.760  1.00 104.41 ?  492 LYS   A CD  1 
ATOM   2555 C CE  . LYS   A 1 511 ? 31.456  -9.886  56.848  1.00 113.31 ?  492 LYS   A CE  1 
ATOM   2556 N NZ  . LYS   A 1 511 ? 31.410  -10.598 58.153  1.00 114.81 ?  492 LYS   A NZ  1 
ATOM   2557 N N   . GLU   A 1 512 ? 32.872  -6.256  53.681  1.00 100.62 ?  493 GLU   A N   1 
ATOM   2558 C CA  . GLU   A 1 512 ? 33.134  -4.912  54.190  1.00 97.17  ?  493 GLU   A CA  1 
ATOM   2559 C C   . GLU   A 1 512 ? 32.375  -3.857  53.400  1.00 95.95  ?  493 GLU   A C   1 
ATOM   2560 O O   . GLU   A 1 512 ? 31.686  -3.014  53.983  1.00 102.42 ?  493 GLU   A O   1 
ATOM   2561 C CB  . GLU   A 1 512 ? 34.626  -4.607  54.139  1.00 93.68  ?  493 GLU   A CB  1 
ATOM   2562 C CG  . GLU   A 1 512 ? 35.487  -5.501  54.986  1.00 100.33 ?  493 GLU   A CG  1 
ATOM   2563 C CD  . GLU   A 1 512 ? 36.859  -4.888  55.215  1.00 108.87 ?  493 GLU   A CD  1 
ATOM   2564 O OE1 . GLU   A 1 512 ? 37.169  -3.863  54.555  1.00 102.14 ?  493 GLU   A OE1 1 
ATOM   2565 O OE2 . GLU   A 1 512 ? 37.626  -5.436  56.038  1.00 112.95 ?  493 GLU   A OE2 1 
ATOM   2566 N N   . TYR   A 1 513 ? 32.505  -3.877  52.068  1.00 91.64  ?  494 TYR   A N   1 
ATOM   2567 C CA  . TYR   A 1 513 ? 31.842  -2.866  51.247  1.00 90.86  ?  494 TYR   A CA  1 
ATOM   2568 C C   . TYR   A 1 513 ? 30.331  -2.929  51.392  1.00 97.60  ?  494 TYR   A C   1 
ATOM   2569 O O   . TYR   A 1 513 ? 29.648  -1.918  51.199  1.00 103.64 ?  494 TYR   A O   1 
ATOM   2570 C CB  . TYR   A 1 513 ? 32.228  -3.012  49.775  1.00 82.56  ?  494 TYR   A CB  1 
ATOM   2571 C CG  . TYR   A 1 513 ? 31.567  -2.003  48.842  1.00 81.98  ?  494 TYR   A CG  1 
ATOM   2572 C CD1 . TYR   A 1 513 ? 32.252  -0.870  48.417  1.00 80.47  ?  494 TYR   A CD1 1 
ATOM   2573 C CD2 . TYR   A 1 513 ? 30.268  -2.195  48.364  1.00 79.00  ?  494 TYR   A CD2 1 
ATOM   2574 C CE1 . TYR   A 1 513 ? 31.657  0.054   47.561  1.00 79.88  ?  494 TYR   A CE1 1 
ATOM   2575 C CE2 . TYR   A 1 513 ? 29.668  -1.279  47.507  1.00 77.05  ?  494 TYR   A CE2 1 
ATOM   2576 C CZ  . TYR   A 1 513 ? 30.365  -0.158  47.109  1.00 79.97  ?  494 TYR   A CZ  1 
ATOM   2577 O OH  . TYR   A 1 513 ? 29.771  0.755   46.259  1.00 83.06  ?  494 TYR   A OH  1 
ATOM   2578 N N   . ASP   A 1 514 ? 29.780  -4.092  51.725  1.00 98.95  ?  495 ASP   A N   1 
ATOM   2579 C CA  . ASP   A 1 514 ? 28.339  -4.129  51.940  1.00 101.99 ?  495 ASP   A CA  1 
ATOM   2580 C C   . ASP   A 1 514 ? 27.962  -3.497  53.278  1.00 103.25 ?  495 ASP   A C   1 
ATOM   2581 O O   . ASP   A 1 514 ? 27.029  -2.687  53.342  1.00 100.83 ?  495 ASP   A O   1 
ATOM   2582 C CB  . ASP   A 1 514 ? 27.840  -5.568  51.816  1.00 103.50 ?  495 ASP   A CB  1 
ATOM   2583 C CG  . ASP   A 1 514 ? 27.800  -6.030  50.371  1.00 105.13 ?  495 ASP   A CG  1 
ATOM   2584 O OD1 . ASP   A 1 514 ? 27.777  -5.135  49.499  1.00 102.90 ?  495 ASP   A OD1 1 
ATOM   2585 O OD2 . ASP   A 1 514 ? 27.795  -7.258  50.102  1.00 104.23 ?  495 ASP   A OD2 1 
ATOM   2586 N N   . GLU   A 1 515 ? 28.737  -3.790  54.315  1.00 103.19 ?  496 GLU   A N   1 
ATOM   2587 C CA  . GLU   A 1 515 ? 28.485  -3.189  55.643  1.00 100.96 ?  496 GLU   A CA  1 
ATOM   2588 C C   . GLU   A 1 515 ? 28.558  -1.676  55.497  1.00 103.38 ?  496 GLU   A C   1 
ATOM   2589 O O   . GLU   A 1 515 ? 27.674  -0.997  55.988  1.00 106.97 ?  496 GLU   A O   1 
ATOM   2590 C CB  . GLU   A 1 515 ? 29.536  -3.665  56.631  1.00 95.37  ?  496 GLU   A CB  1 
ATOM   2591 C CG  . GLU   A 1 515 ? 29.708  -5.163  56.595  1.00 114.06 ?  496 GLU   A CG  1 
ATOM   2592 C CD  . GLU   A 1 515 ? 30.038  -5.803  57.927  1.00 125.04 ?  496 GLU   A CD  1 
ATOM   2593 O OE1 . GLU   A 1 515 ? 30.994  -5.347  58.570  1.00 126.08 ?  496 GLU   A OE1 1 
ATOM   2594 O OE2 . GLU   A 1 515 ? 29.340  -6.757  58.310  1.00 122.96 ?  496 GLU   A OE2 1 
ATOM   2595 N N   . LEU   A 1 516 ? 29.539  -1.176  54.761  1.00 99.53  ?  497 LEU   A N   1 
ATOM   2596 C CA  . LEU   A 1 516 ? 29.649  0.287   54.576  1.00 95.54  ?  497 LEU   A CA  1 
ATOM   2597 C C   . LEU   A 1 516 ? 28.427  0.812   53.839  1.00 101.50 ?  497 LEU   A C   1 
ATOM   2598 O O   . LEU   A 1 516 ? 27.960  1.869   54.184  1.00 107.12 ?  497 LEU   A O   1 
ATOM   2599 C CB  . LEU   A 1 516 ? 30.934  0.627   53.837  1.00 92.61  ?  497 LEU   A CB  1 
ATOM   2600 C CG  . LEU   A 1 516 ? 32.109  0.814   54.776  1.00 92.43  ?  497 LEU   A CG  1 
ATOM   2601 C CD1 . LEU   A 1 516 ? 32.072  -0.256  55.840  1.00 95.33  ?  497 LEU   A CD1 1 
ATOM   2602 C CD2 . LEU   A 1 516 ? 33.408  0.753   54.017  1.00 95.31  ?  497 LEU   A CD2 1 
ATOM   2603 N N   . ALA   A 1 517 ? 27.902  0.084   52.869  1.00 101.73 ?  498 ALA   A N   1 
ATOM   2604 C CA  . ALA   A 1 517 ? 26.706  0.581   52.160  1.00 102.85 ?  498 ALA   A CA  1 
ATOM   2605 C C   . ALA   A 1 517 ? 25.535  0.697   53.128  1.00 105.53 ?  498 ALA   A C   1 
ATOM   2606 O O   . ALA   A 1 517 ? 24.715  1.578   52.921  1.00 103.24 ?  498 ALA   A O   1 
ATOM   2607 C CB  . ALA   A 1 517 ? 26.366  -0.321  51.018  1.00 101.13 ?  498 ALA   A CB  1 
ATOM   2608 N N   . GLU   A 1 518 ? 25.396  -0.231  54.070  1.00 105.31 ?  499 GLU   A N   1 
ATOM   2609 C CA  . GLU   A 1 518 ? 24.302  -0.086  55.051  1.00 113.04 ?  499 GLU   A CA  1 
ATOM   2610 C C   . GLU   A 1 518 ? 24.545  1.209   55.819  1.00 111.82 ?  499 GLU   A C   1 
ATOM   2611 O O   . GLU   A 1 518 ? 23.691  2.085   55.790  1.00 108.67 ?  499 GLU   A O   1 
ATOM   2612 C CB  . GLU   A 1 518 ? 24.415  -1.200  56.083  1.00 110.18 ?  499 GLU   A CB  1 
ATOM   2613 C CG  . GLU   A 1 518 ? 23.858  -2.514  55.595  1.00 120.37 ?  499 GLU   A CG  1 
ATOM   2614 C CD  . GLU   A 1 518 ? 22.358  -2.639  55.742  1.00 127.15 ?  499 GLU   A CD  1 
ATOM   2615 O OE1 . GLU   A 1 518 ? 21.818  -2.098  56.717  1.00 128.98 ?  499 GLU   A OE1 1 
ATOM   2616 O OE2 . GLU   A 1 518 ? 21.740  -3.279  54.884  1.00 131.31 ?  499 GLU   A OE2 1 
ATOM   2617 N N   . THR   A 1 519 ? 25.771  1.408   56.283  1.00 108.12 ?  500 THR   A N   1 
ATOM   2618 C CA  . THR   A 1 519 ? 26.097  2.615   57.068  1.00 102.22 ?  500 THR   A CA  1 
ATOM   2619 C C   . THR   A 1 519 ? 25.877  3.847   56.206  1.00 99.75  ?  500 THR   A C   1 
ATOM   2620 O O   . THR   A 1 519 ? 25.378  4.812   56.701  1.00 102.05 ?  500 THR   A O   1 
ATOM   2621 C CB  . THR   A 1 519 ? 27.534  2.560   57.564  1.00 100.09 ?  500 THR   A CB  1 
ATOM   2622 O OG1 . THR   A 1 519 ? 27.542  1.730   58.719  1.00 98.78  ?  500 THR   A OG1 1 
ATOM   2623 C CG2 . THR   A 1 519 ? 28.053  3.929   57.920  1.00 101.69 ?  500 THR   A CG2 1 
ATOM   2624 N N   . GLN   A 1 520 ? 26.230  3.810   54.937  1.00 99.25  ?  501 GLN   A N   1 
ATOM   2625 C CA  . GLN   A 1 520 ? 25.967  5.007   54.117  1.00 107.41 ?  501 GLN   A CA  1 
ATOM   2626 C C   . GLN   A 1 520 ? 24.464  5.269   54.052  1.00 110.89 ?  501 GLN   A C   1 
ATOM   2627 O O   . GLN   A 1 520 ? 24.076  6.426   54.113  1.00 111.62 ?  501 GLN   A O   1 
ATOM   2628 C CB  . GLN   A 1 520 ? 26.447  4.797   52.689  1.00 105.04 ?  501 GLN   A CB  1 
ATOM   2629 C CG  . GLN   A 1 520 ? 25.911  5.847   51.741  1.00 96.86  ?  501 GLN   A CG  1 
ATOM   2630 C CD  . GLN   A 1 520 ? 26.162  5.441   50.319  1.00 101.66 ?  501 GLN   A CD  1 
ATOM   2631 O OE1 . GLN   A 1 520 ? 26.538  4.318   50.047  1.00 112.51 ?  501 GLN   A OE1 1 
ATOM   2632 N NE2 . GLN   A 1 520 ? 25.945  6.354   49.397  1.00 100.33 ?  501 GLN   A NE2 1 
ATOM   2633 N N   . GLY   A 1 521 ? 23.644  4.234   53.911  1.00 108.76 ?  502 GLY   A N   1 
ATOM   2634 C CA  . GLY   A 1 521 ? 22.203  4.490   53.786  1.00 107.72 ?  502 GLY   A CA  1 
ATOM   2635 C C   . GLY   A 1 521 ? 21.663  5.180   55.015  1.00 110.41 ?  502 GLY   A C   1 
ATOM   2636 O O   . GLY   A 1 521 ? 20.895  6.117   54.853  1.00 113.19 ?  502 GLY   A O   1 
ATOM   2637 N N   . LYS   A 1 522 ? 22.081  4.740   56.196  1.00 105.62 ?  503 LYS   A N   1 
ATOM   2638 C CA  . LYS   A 1 522 ? 21.606  5.356   57.452  1.00 106.84 ?  503 LYS   A CA  1 
ATOM   2639 C C   . LYS   A 1 522 ? 21.954  6.836   57.440  1.00 113.28 ?  503 LYS   A C   1 
ATOM   2640 O O   . LYS   A 1 522 ? 21.044  7.667   57.454  1.00 113.79 ?  503 LYS   A O   1 
ATOM   2641 C CB  . LYS   A 1 522 ? 22.369  4.773   58.634  1.00 102.68 ?  503 LYS   A CB  1 
ATOM   2642 C CG  . LYS   A 1 522 ? 22.150  3.293   58.860  1.00 104.55 ?  503 LYS   A CG  1 
ATOM   2643 C CD  . LYS   A 1 522 ? 23.083  2.755   59.899  1.00 114.45 ?  503 LYS   A CD  1 
ATOM   2644 C CE  . LYS   A 1 522 ? 23.808  3.844   60.657  1.00 114.21 ?  503 LYS   A CE  1 
ATOM   2645 N NZ  . LYS   A 1 522 ? 24.504  3.300   61.848  1.00 109.65 ?  503 LYS   A NZ  1 
ATOM   2646 N N   . LEU   A 1 523 ? 23.245  7.135   57.434  1.00 110.23 ?  504 LEU   A N   1 
ATOM   2647 C CA  . LEU   A 1 523 ? 23.661  8.529   57.468  1.00 99.91  ?  504 LEU   A CA  1 
ATOM   2648 C C   . LEU   A 1 523 ? 23.051  9.320   56.326  1.00 101.56 ?  504 LEU   A C   1 
ATOM   2649 O O   . LEU   A 1 523 ? 22.828  10.523  56.458  1.00 107.85 ?  504 LEU   A O   1 
ATOM   2650 C CB  . LEU   A 1 523 ? 25.190  8.630   57.434  1.00 92.93  ?  504 LEU   A CB  1 
ATOM   2651 C CG  . LEU   A 1 523 ? 25.959  8.537   58.764  1.00 100.91 ?  504 LEU   A CG  1 
ATOM   2652 C CD1 . LEU   A 1 523 ? 25.499  7.385   59.685  1.00 101.46 ?  504 LEU   A CD1 1 
ATOM   2653 C CD2 . LEU   A 1 523 ? 27.464  8.468   58.522  1.00 101.81 ?  504 LEU   A CD2 1 
ATOM   2654 N N   . GLU   A 1 524 ? 22.759  8.674   55.210  1.00 105.34 ?  505 GLU   A N   1 
ATOM   2655 C CA  . GLU   A 1 524 ? 22.146  9.390   54.101  1.00 112.44 ?  505 GLU   A CA  1 
ATOM   2656 C C   . GLU   A 1 524 ? 20.693  9.746   54.408  1.00 112.88 ?  505 GLU   A C   1 
ATOM   2657 O O   . GLU   A 1 524 ? 20.144  10.677  53.802  1.00 109.88 ?  505 GLU   A O   1 
ATOM   2658 C CB  . GLU   A 1 524 ? 22.296  8.537   52.831  1.00 112.89 ?  505 GLU   A CB  1 
ATOM   2659 C CG  . GLU   A 1 524 ? 22.138  9.211   51.484  1.00 110.34 ?  505 GLU   A CG  1 
ATOM   2660 C CD  . GLU   A 1 524 ? 22.607  8.295   50.344  1.00 115.21 ?  505 GLU   A CD  1 
ATOM   2661 O OE1 . GLU   A 1 524 ? 22.900  7.111   50.633  1.00 116.20 ?  505 GLU   A OE1 1 
ATOM   2662 O OE2 . GLU   A 1 524 ? 22.697  8.755   49.178  1.00 108.84 ?  505 GLU   A OE2 1 
ATOM   2663 N N   . GLU   A 1 525 ? 20.152  9.103   55.443  1.00 110.12 ?  506 GLU   A N   1 
ATOM   2664 C CA  . GLU   A 1 525 ? 18.748  9.353   55.851  1.00 112.77 ?  506 GLU   A CA  1 
ATOM   2665 C C   . GLU   A 1 525 ? 18.711  10.432  56.929  1.00 114.25 ?  506 GLU   A C   1 
ATOM   2666 O O   . GLU   A 1 525 ? 17.869  11.317  56.835  1.00 113.58 ?  506 GLU   A O   1 
ATOM   2667 C CB  . GLU   A 1 525 ? 18.052  8.059   56.257  1.00 114.08 ?  506 GLU   A CB  1 
ATOM   2668 C CG  . GLU   A 1 525 ? 18.605  7.419   57.508  1.00 119.11 ?  506 GLU   A CG  1 
ATOM   2669 C CD  . GLU   A 1 525 ? 17.802  6.187   57.878  1.00 126.77 ?  506 GLU   A CD  1 
ATOM   2670 O OE1 . GLU   A 1 525 ? 18.022  5.639   58.965  1.00 125.25 ?  506 GLU   A OE1 1 
ATOM   2671 O OE2 . GLU   A 1 525 ? 16.955  5.787   57.065  1.00 135.93 ?  506 GLU   A OE2 1 
ATOM   2672 N N   . LYS   A 1 526 ? 19.690  10.459  57.828  1.00 110.80 ?  507 LYS   A N   1 
ATOM   2673 C CA  . LYS   A 1 526 ? 19.721  11.521  58.860  1.00 105.99 ?  507 LYS   A CA  1 
ATOM   2674 C C   . LYS   A 1 526 ? 19.834  12.872  58.169  1.00 107.67 ?  507 LYS   A C   1 
ATOM   2675 O O   . LYS   A 1 526 ? 19.150  13.774  58.573  1.00 114.54 ?  507 LYS   A O   1 
ATOM   2676 C CB  . LYS   A 1 526 ? 20.912  11.343  59.788  1.00 101.18 ?  507 LYS   A CB  1 
ATOM   2677 C CG  . LYS   A 1 526 ? 20.926  10.010  60.499  1.00 111.84 ?  507 LYS   A CG  1 
ATOM   2678 C CD  . LYS   A 1 526 ? 21.725  10.068  61.764  1.00 119.56 ?  507 LYS   A CD  1 
ATOM   2679 C CE  . LYS   A 1 526 ? 22.592  11.303  61.824  1.00 124.03 ?  507 LYS   A CE  1 
ATOM   2680 N NZ  . LYS   A 1 526 ? 23.610  11.202  62.895  1.00 126.40 ?  507 LYS   A NZ  1 
ATOM   2681 N N   . LEU   A 1 527 ? 20.624  12.994  57.111  1.00 110.59 ?  508 LEU   A N   1 
ATOM   2682 C CA  . LEU   A 1 527 ? 20.703  14.270  56.370  1.00 110.88 ?  508 LEU   A CA  1 
ATOM   2683 C C   . LEU   A 1 527 ? 19.318  14.616  55.817  1.00 115.05 ?  508 LEU   A C   1 
ATOM   2684 O O   . LEU   A 1 527 ? 18.987  15.792  55.783  1.00 120.47 ?  508 LEU   A O   1 
ATOM   2685 C CB  . LEU   A 1 527 ? 21.703  14.102  55.225  1.00 113.02 ?  508 LEU   A CB  1 
ATOM   2686 C CG  . LEU   A 1 527 ? 23.172  13.991  55.623  1.00 108.62 ?  508 LEU   A CG  1 
ATOM   2687 C CD1 . LEU   A 1 527 ? 23.997  15.025  54.893  1.00 103.76 ?  508 LEU   A CD1 1 
ATOM   2688 C CD2 . LEU   A 1 527 ? 23.356  14.141  57.117  1.00 103.37 ?  508 LEU   A CD2 1 
ATOM   2689 N N   . GLN   A 1 528 ? 18.564  13.644  55.319  1.00 118.80 ?  509 GLN   A N   1 
ATOM   2690 C CA  . GLN   A 1 528 ? 17.216  13.966  54.802  1.00 122.00 ?  509 GLN   A CA  1 
ATOM   2691 C C   . GLN   A 1 528 ? 16.323  14.473  55.937  1.00 119.53 ?  509 GLN   A C   1 
ATOM   2692 O O   . GLN   A 1 528 ? 15.593  15.443  55.731  1.00 114.34 ?  509 GLN   A O   1 
ATOM   2693 C CB  . GLN   A 1 528 ? 16.597  12.702  54.221  1.00 122.77 ?  509 GLN   A CB  1 
ATOM   2694 C CG  . GLN   A 1 528 ? 15.451  12.986  53.273  1.00 129.90 ?  509 GLN   A CG  1 
ATOM   2695 C CD  . GLN   A 1 528 ? 15.823  12.573  51.875  1.00 134.68 ?  509 GLN   A CD  1 
ATOM   2696 O OE1 . GLN   A 1 528 ? 15.569  11.449  51.455  1.00 132.28 ?  509 GLN   A OE1 1 
ATOM   2697 N NE2 . GLN   A 1 528 ? 16.449  13.483  51.151  1.00 134.00 ?  509 GLN   A NE2 1 
ATOM   2698 N N   . GLU   A 1 529 ? 16.344  13.807  57.086  1.00 114.92 ?  510 GLU   A N   1 
ATOM   2699 C CA  . GLU   A 1 529 ? 15.460  14.276  58.174  1.00 111.42 ?  510 GLU   A CA  1 
ATOM   2700 C C   . GLU   A 1 529 ? 15.949  15.615  58.711  1.00 119.73 ?  510 GLU   A C   1 
ATOM   2701 O O   . GLU   A 1 529 ? 15.136  16.531  58.798  1.00 121.19 ?  510 GLU   A O   1 
ATOM   2702 C CB  . GLU   A 1 529 ? 15.222  13.190  59.214  1.00 109.54 ?  510 GLU   A CB  1 
ATOM   2703 C CG  . GLU   A 1 529 ? 16.439  12.841  60.020  1.00 117.40 ?  510 GLU   A CG  1 
ATOM   2704 C CD  . GLU   A 1 529 ? 16.541  13.688  61.263  1.00 128.08 ?  510 GLU   A CD  1 
ATOM   2705 O OE1 . GLU   A 1 529 ? 15.919  14.754  61.274  1.00 129.72 ?  510 GLU   A OE1 1 
ATOM   2706 O OE2 . GLU   A 1 529 ? 17.258  13.295  62.190  1.00 129.17 ?  510 GLU   A OE2 1 
ATOM   2707 N N   . LEU   A 1 530 ? 17.259  15.771  58.893  1.00 118.51 ?  511 LEU   A N   1 
ATOM   2708 C CA  . LEU   A 1 530 ? 17.799  17.027  59.459  1.00 106.22 ?  511 LEU   A CA  1 
ATOM   2709 C C   . LEU   A 1 530 ? 17.440  18.161  58.523  1.00 108.35 ?  511 LEU   A C   1 
ATOM   2710 O O   . LEU   A 1 530 ? 16.929  19.140  58.986  1.00 117.87 ?  511 LEU   A O   1 
ATOM   2711 C CB  . LEU   A 1 530 ? 19.312  16.901  59.555  1.00 103.12 ?  511 LEU   A CB  1 
ATOM   2712 C CG  . LEU   A 1 530 ? 19.776  16.124  60.771  1.00 109.36 ?  511 LEU   A CG  1 
ATOM   2713 C CD1 . LEU   A 1 530 ? 21.091  16.656  61.288  1.00 107.59 ?  511 LEU   A CD1 1 
ATOM   2714 C CD2 . LEU   A 1 530 ? 18.728  16.217  61.846  1.00 113.01 ?  511 LEU   A CD2 1 
ATOM   2715 N N   . GLU   A 1 531 ? 17.580  17.960  57.222  1.00 107.47 ?  512 GLU   A N   1 
ATOM   2716 C CA  . GLU   A 1 531 ? 17.234  19.016  56.247  1.00 117.49 ?  512 GLU   A CA  1 
ATOM   2717 C C   . GLU   A 1 531 ? 15.747  19.334  56.345  1.00 116.41 ?  512 GLU   A C   1 
ATOM   2718 O O   . GLU   A 1 531 ? 15.399  20.480  56.129  1.00 114.71 ?  512 GLU   A O   1 
ATOM   2719 C CB  . GLU   A 1 531 ? 17.534  18.545  54.831  1.00 126.00 ?  512 GLU   A CB  1 
ATOM   2720 C CG  . GLU   A 1 531 ? 17.464  19.661  53.817  1.00 114.30 ?  512 GLU   A CG  1 
ATOM   2721 C CD  . GLU   A 1 531 ? 18.775  20.413  53.723  1.00 130.00 ?  512 GLU   A CD  1 
ATOM   2722 O OE1 . GLU   A 1 531 ? 19.741  19.942  54.323  1.00 128.01 ?  512 GLU   A OE1 1 
ATOM   2723 O OE2 . GLU   A 1 531 ? 18.822  21.460  53.057  1.00 143.20 ?  512 GLU   A OE2 1 
ATOM   2724 N N   . ALA   A 1 532 ? 14.916  18.316  56.553  1.00 117.26 ?  513 ALA   A N   1 
ATOM   2725 C CA  . ALA   A 1 532 ? 13.451  18.447  56.670  1.00 120.00 ?  513 ALA   A CA  1 
ATOM   2726 C C   . ALA   A 1 532 ? 13.025  19.046  58.014  1.00 117.06 ?  513 ALA   A C   1 
ATOM   2727 O O   . ALA   A 1 532 ? 11.878  19.465  58.114  1.00 115.58 ?  513 ALA   A O   1 
ATOM   2728 C CB  . ALA   A 1 532 ? 12.826  17.099  56.459  1.00 112.81 ?  513 ALA   A CB  1 
ATOM   2729 N N   . ASN   A 1 533 ? 13.906  19.137  59.005  1.00 114.55 ?  514 ASN   A N   1 
ATOM   2730 C CA  . ASN   A 1 533 ? 13.461  19.673  60.316  1.00 111.20 ?  514 ASN   A CA  1 
ATOM   2731 C C   . ASN   A 1 533 ? 14.332  20.864  60.702  1.00 110.17 ?  514 ASN   A C   1 
ATOM   2732 O O   . ASN   A 1 533 ? 14.965  20.828  61.757  1.00 109.06 ?  514 ASN   A O   1 
ATOM   2733 C CB  . ASN   A 1 533 ? 13.630  18.606  61.392  1.00 112.15 ?  514 ASN   A CB  1 
ATOM   2734 C CG  . ASN   A 1 533 ? 12.511  17.598  61.389  1.00 119.87 ?  514 ASN   A CG  1 
ATOM   2735 O OD1 . ASN   A 1 533 ? 11.624  17.663  60.548  1.00 117.15 ?  514 ASN   A OD1 1 
ATOM   2736 N ND2 . ASN   A 1 533 ? 12.535  16.680  62.337  1.00 117.79 ?  514 ASN   A ND2 1 
ATOM   2737 N N   . PRO   A 1 534 ? 14.286  21.981  59.959  1.00 107.82 ?  515 PRO   A N   1 
ATOM   2738 C CA  . PRO   A 1 534 ? 15.121  23.111  60.250  1.00 103.17 ?  515 PRO   A CA  1 
ATOM   2739 C C   . PRO   A 1 534 ? 14.382  23.922  61.300  1.00 111.76 ?  515 PRO   A C   1 
ATOM   2740 O O   . PRO   A 1 534 ? 13.197  24.024  61.211  1.00 113.41 ?  515 PRO   A O   1 
ATOM   2741 C CB  . PRO   A 1 534 ? 15.039  23.902  58.955  1.00 102.25 ?  515 PRO   A CB  1 
ATOM   2742 C CG  . PRO   A 1 534 ? 13.622  23.722  58.552  1.00 100.06 ?  515 PRO   A CG  1 
ATOM   2743 C CD  . PRO   A 1 534 ? 13.332  22.288  58.915  1.00 108.75 ?  515 PRO   A CD  1 
ATOM   2744 N N   . PRO   A 1 535 ? 15.086  24.610  62.212  1.00 111.33 ?  516 PRO   A N   1 
ATOM   2745 C CA  . PRO   A 1 535 ? 14.461  25.406  63.241  1.00 105.96 ?  516 PRO   A CA  1 
ATOM   2746 C C   . PRO   A 1 535 ? 13.978  26.752  62.688  1.00 107.99 ?  516 PRO   A C   1 
ATOM   2747 O O   . PRO   A 1 535 ? 14.268  27.094  61.574  1.00 103.36 ?  516 PRO   A O   1 
ATOM   2748 C CB  . PRO   A 1 535 ? 15.586  25.538  64.260  1.00 102.72 ?  516 PRO   A CB  1 
ATOM   2749 C CG  . PRO   A 1 535 ? 16.796  25.645  63.410  1.00 97.63  ?  516 PRO   A CG  1 
ATOM   2750 C CD  . PRO   A 1 535 ? 16.526  24.687  62.278  1.00 109.33 ?  516 PRO   A CD  1 
ATOM   2751 N N   . SER   A 1 536 ? 13.264  27.497  63.519  1.00 111.09 ?  517 SER   A N   1 
ATOM   2752 C CA  . SER   A 1 536 ? 12.636  28.766  63.079  1.00 105.27 ?  517 SER   A CA  1 
ATOM   2753 C C   . SER   A 1 536 ? 13.664  29.709  62.466  1.00 98.58  ?  517 SER   A C   1 
ATOM   2754 O O   . SER   A 1 536 ? 14.740  29.867  63.010  1.00 94.51  ?  517 SER   A O   1 
ATOM   2755 C CB  . SER   A 1 536 ? 11.878  29.416  64.199  1.00 110.69 ?  517 SER   A CB  1 
ATOM   2756 O OG  . SER   A 1 536 ? 12.309  28.952  65.472  1.00 121.30 ?  517 SER   A OG  1 
ATOM   2757 N N   . ASP   A 1 537 ? 13.301  30.246  61.314  1.00 96.06  ?  518 ASP   A N   1 
ATOM   2758 C CA  . ASP   A 1 537 ? 14.118  31.164  60.493  1.00 100.79 ?  518 ASP   A CA  1 
ATOM   2759 C C   . ASP   A 1 537 ? 14.336  32.507  61.180  1.00 105.63 ?  518 ASP   A C   1 
ATOM   2760 O O   . ASP   A 1 537 ? 15.445  33.007  61.125  1.00 101.66 ?  518 ASP   A O   1 
ATOM   2761 C CB  . ASP   A 1 537 ? 13.369  31.400  59.189  1.00 104.91 ?  518 ASP   A CB  1 
ATOM   2762 C CG  . ASP   A 1 537 ? 14.156  32.205  58.187  1.00 115.38 ?  518 ASP   A CG  1 
ATOM   2763 O OD1 . ASP   A 1 537 ? 15.073  32.915  58.612  1.00 114.44 ?  518 ASP   A OD1 1 
ATOM   2764 O OD2 . ASP   A 1 537 ? 13.834  32.110  56.999  1.00 124.81 ?  518 ASP   A OD2 1 
ATOM   2765 N N   . VAL   A 1 538 ? 13.294  33.050  61.806  1.00 109.55 ?  519 VAL   A N   1 
ATOM   2766 C CA  . VAL   A 1 538 ? 13.335  34.403  62.428  1.00 97.06  ?  519 VAL   A CA  1 
ATOM   2767 C C   . VAL   A 1 538 ? 12.652  34.379  63.785  1.00 95.31  ?  519 VAL   A C   1 
ATOM   2768 O O   . VAL   A 1 538 ? 11.908  33.447  64.046  1.00 93.08  ?  519 VAL   A O   1 
ATOM   2769 C CB  . VAL   A 1 538 ? 12.549  35.384  61.552  1.00 95.93  ?  519 VAL   A CB  1 
ATOM   2770 C CG1 . VAL   A 1 538 ? 13.349  35.850  60.357  1.00 106.08 ?  519 VAL   A CG1 1 
ATOM   2771 C CG2 . VAL   A 1 538 ? 11.236  34.775  61.114  1.00 87.66  ?  519 VAL   A CG2 1 
ATOM   2772 N N   . TYR   A 1 539 ? 12.932  35.383  64.612  1.00 98.06  ?  520 TYR   A N   1 
ATOM   2773 C CA  . TYR   A 1 539 ? 12.199  35.521  65.889  1.00 92.43  ?  520 TYR   A CA  1 
ATOM   2774 C C   . TYR   A 1 539 ? 10.918  36.272  65.567  1.00 88.73  ?  520 TYR   A C   1 
ATOM   2775 O O   . TYR   A 1 539 ? 9.858   35.824  65.956  1.00 85.93  ?  520 TYR   A O   1 
ATOM   2776 C CB  . TYR   A 1 539 ? 12.945  36.381  66.899  1.00 91.26  ?  520 TYR   A CB  1 
ATOM   2777 C CG  . TYR   A 1 539 ? 12.140  36.609  68.147  1.00 92.15  ?  520 TYR   A CG  1 
ATOM   2778 C CD1 . TYR   A 1 539 ? 11.488  35.561  68.747  1.00 94.94  ?  520 TYR   A CD1 1 
ATOM   2779 C CD2 . TYR   A 1 539 ? 12.007  37.854  68.719  1.00 91.24  ?  520 TYR   A CD2 1 
ATOM   2780 C CE1 . TYR   A 1 539 ? 10.746  35.735  69.896  1.00 93.95  ?  520 TYR   A CE1 1 
ATOM   2781 C CE2 . TYR   A 1 539 ? 11.259  38.050  69.863  1.00 86.34  ?  520 TYR   A CE2 1 
ATOM   2782 C CZ  . TYR   A 1 539 ? 10.623  36.983  70.452  1.00 89.48  ?  520 TYR   A CZ  1 
ATOM   2783 O OH  . TYR   A 1 539 ? 9.870   37.122  71.569  1.00 85.47  ?  520 TYR   A OH  1 
ATOM   2784 N N   . LEU   A 1 540 ? 11.018  37.388  64.875  1.00 84.61  ?  521 LEU   A N   1 
ATOM   2785 C CA  . LEU   A 1 540 ? 9.758   38.078  64.555  1.00 85.76  ?  521 LEU   A CA  1 
ATOM   2786 C C   . LEU   A 1 540 ? 9.900   38.689  63.179  1.00 87.57  ?  521 LEU   A C   1 
ATOM   2787 O O   . LEU   A 1 540 ? 10.939  39.255  62.915  1.00 87.65  ?  521 LEU   A O   1 
ATOM   2788 C CB  . LEU   A 1 540 ? 9.540   39.164  65.600  1.00 94.48  ?  521 LEU   A CB  1 
ATOM   2789 C CG  . LEU   A 1 540 ? 8.776   38.726  66.840  1.00 94.55  ?  521 LEU   A CG  1 
ATOM   2790 C CD1 . LEU   A 1 540 ? 8.992   39.708  67.962  1.00 95.10  ?  521 LEU   A CD1 1 
ATOM   2791 C CD2 . LEU   A 1 540 ? 7.307   38.626  66.538  1.00 91.54  ?  521 LEU   A CD2 1 
ATOM   2792 N N   . SER   A 1 541 ? 8.887   38.539  62.343  1.00 84.36  ?  522 SER   A N   1 
ATOM   2793 C CA  . SER   A 1 541 ? 8.980   39.137  60.999  1.00 88.41  ?  522 SER   A CA  1 
ATOM   2794 C C   . SER   A 1 541 ? 8.671   40.618  61.096  1.00 90.52  ?  522 SER   A C   1 
ATOM   2795 O O   . SER   A 1 541 ? 7.996   40.997  62.017  1.00 93.87  ?  522 SER   A O   1 
ATOM   2796 C CB  . SER   A 1 541 ? 8.064   38.465  60.050  1.00 93.90  ?  522 SER   A CB  1 
ATOM   2797 O OG  . SER   A 1 541 ? 6.817   39.115  60.008  1.00 89.59  ?  522 SER   A OG  1 
ATOM   2798 N N   . SER   A 1 542 ? 8.978   41.377  60.057  1.00 88.30  ?  523 SER   A N   1 
ATOM   2799 C CA  . SER   A 1 542 ? 8.712   42.833  60.063  1.00 95.01  ?  523 SER   A CA  1 
ATOM   2800 C C   . SER   A 1 542 ? 7.217   43.085  60.261  1.00 96.45  ?  523 SER   A C   1 
ATOM   2801 O O   . SER   A 1 542 ? 6.869   44.052  60.897  1.00 96.96  ?  523 SER   A O   1 
ATOM   2802 C CB  . SER   A 1 542 ? 9.148   43.415  58.780  1.00 97.25  ?  523 SER   A CB  1 
ATOM   2803 O OG  . SER   A 1 542 ? 8.160   43.164  57.805  1.00 110.46 ?  523 SER   A OG  1 
ATOM   2804 N N   . ARG   A 1 543 ? 6.363   42.303  59.627  1.00 97.19  ?  524 ARG   A N   1 
ATOM   2805 C CA  . ARG   A 1 543 ? 4.920   42.434  59.894  1.00 97.28  ?  524 ARG   A CA  1 
ATOM   2806 C C   . ARG   A 1 543 ? 4.692   42.061  61.354  1.00 92.45  ?  524 ARG   A C   1 
ATOM   2807 O O   . ARG   A 1 543 ? 4.011   42.784  62.025  1.00 97.23  ?  524 ARG   A O   1 
ATOM   2808 C CB  . ARG   A 1 543 ? 4.183   41.424  59.016  1.00 105.89 ?  524 ARG   A CB  1 
ATOM   2809 C CG  . ARG   A 1 543 ? 2.692   41.655  58.865  1.00 103.53 ?  524 ARG   A CG  1 
ATOM   2810 C CD  . ARG   A 1 543 ? 2.019   40.318  58.690  1.00 114.38 ?  524 ARG   A CD  1 
ATOM   2811 N NE  . ARG   A 1 543 ? 0.730   40.397  58.030  1.00 118.87 ?  524 ARG   A NE  1 
ATOM   2812 C CZ  . ARG   A 1 543 ? 0.472   41.159  56.981  1.00 122.06 ?  524 ARG   A CZ  1 
ATOM   2813 N NH1 . ARG   A 1 543 ? -0.735  41.161  56.447  1.00 122.15 ?  524 ARG   A NH1 1 
ATOM   2814 N NH2 . ARG   A 1 543 ? 1.417   41.923  56.472  1.00 121.07 ?  524 ARG   A NH2 1 
ATOM   2815 N N   . ASP   A 1 544 ? 5.312   40.996  61.843  1.00 91.66  ?  525 ASP   A N   1 
ATOM   2816 C CA  . ASP   A 1 544 ? 5.047   40.592  63.243  1.00 90.64  ?  525 ASP   A CA  1 
ATOM   2817 C C   . ASP   A 1 544 ? 5.502   41.680  64.205  1.00 92.32  ?  525 ASP   A C   1 
ATOM   2818 O O   . ASP   A 1 544 ? 4.721   42.063  65.041  1.00 91.77  ?  525 ASP   A O   1 
ATOM   2819 C CB  . ASP   A 1 544 ? 5.757   39.293  63.589  1.00 97.34  ?  525 ASP   A CB  1 
ATOM   2820 C CG  . ASP   A 1 544 ? 5.359   38.140  62.700  1.00 107.03 ?  525 ASP   A CG  1 
ATOM   2821 O OD1 . ASP   A 1 544 ? 4.609   38.375  61.750  1.00 107.08 ?  525 ASP   A OD1 1 
ATOM   2822 O OD2 . ASP   A 1 544 ? 5.812   37.020  62.973  1.00 99.60  ?  525 ASP   A OD2 1 
ATOM   2823 N N   . ARG   A 1 545 ? 6.675   42.267  64.001  1.00 91.90  ?  526 ARG   A N   1 
ATOM   2824 C CA  . ARG   A 1 545 ? 7.159   43.311  64.940  1.00 90.28  ?  526 ARG   A CA  1 
ATOM   2825 C C   . ARG   A 1 545 ? 6.213   44.506  64.934  1.00 87.37  ?  526 ARG   A C   1 
ATOM   2826 O O   . ARG   A 1 545 ? 6.023   45.092  65.974  1.00 88.85  ?  526 ARG   A O   1 
ATOM   2827 C CB  . ARG   A 1 545 ? 8.597   43.733  64.664  1.00 86.94  ?  526 ARG   A CB  1 
ATOM   2828 C CG  . ARG   A 1 545 ? 9.065   44.849  65.583  1.00 96.34  ?  526 ARG   A CG  1 
ATOM   2829 C CD  . ARG   A 1 545 ? 10.141  44.377  66.536  1.00 98.43  ?  526 ARG   A CD  1 
ATOM   2830 N NE  . ARG   A 1 545 ? 10.663  45.317  67.525  1.00 104.21 ?  526 ARG   A NE  1 
ATOM   2831 C CZ  . ARG   A 1 545 ? 10.118  46.471  67.902  1.00 103.25 ?  526 ARG   A CZ  1 
ATOM   2832 N NH1 . ARG   A 1 545 ? 8.995   46.905  67.364  1.00 92.57  ?  526 ARG   A NH1 1 
ATOM   2833 N NH2 . ARG   A 1 545 ? 10.718  47.202  68.819  1.00 105.54 ?  526 ARG   A NH2 1 
ATOM   2834 N N   . GLN   A 1 546 ? 5.654   44.860  63.788  1.00 84.22  ?  527 GLN   A N   1 
ATOM   2835 C CA  . GLN   A 1 546 ? 4.671   45.954  63.724  1.00 78.08  ?  527 GLN   A CA  1 
ATOM   2836 C C   . GLN   A 1 546 ? 3.467   45.588  64.581  1.00 82.33  ?  527 GLN   A C   1 
ATOM   2837 O O   . GLN   A 1 546 ? 2.927   46.472  65.186  1.00 90.22  ?  527 GLN   A O   1 
ATOM   2838 C CB  . GLN   A 1 546 ? 4.228   46.169  62.288  1.00 80.01  ?  527 GLN   A CB  1 
ATOM   2839 C CG  . GLN   A 1 546 ? 5.296   46.811  61.429  1.00 89.92  ?  527 GLN   A CG  1 
ATOM   2840 C CD  . GLN   A 1 546 ? 4.802   47.062  60.031  1.00 93.58  ?  527 GLN   A CD  1 
ATOM   2841 O OE1 . GLN   A 1 546 ? 3.984   46.326  59.504  1.00 97.54  ?  527 GLN   A OE1 1 
ATOM   2842 N NE2 . GLN   A 1 546 ? 5.292   48.121  59.423  1.00 86.96  ?  527 GLN   A NE2 1 
ATOM   2843 N N   . ILE   A 1 547 ? 3.014   44.345  64.586  1.00 75.16  ?  528 ILE   A N   1 
ATOM   2844 C CA  . ILE   A 1 547 ? 1.865   44.078  65.484  1.00 80.54  ?  528 ILE   A CA  1 
ATOM   2845 C C   . ILE   A 1 547 ? 2.351   44.261  66.915  1.00 79.41  ?  528 ILE   A C   1 
ATOM   2846 O O   . ILE   A 1 547 ? 1.667   44.916  67.654  1.00 76.98  ?  528 ILE   A O   1 
ATOM   2847 C CB  . ILE   A 1 547 ? 1.255   42.699  65.244  1.00 82.35  ?  528 ILE   A CB  1 
ATOM   2848 C CG1 . ILE   A 1 547 ? 0.256   42.741  64.096  1.00 87.89  ?  528 ILE   A CG1 1 
ATOM   2849 C CG2 . ILE   A 1 547 ? 0.585   42.216  66.505  1.00 78.73  ?  528 ILE   A CG2 1 
ATOM   2850 C CD1 . ILE   A 1 547 ? 0.883   42.651  62.745  1.00 93.27  ?  528 ILE   A CD1 1 
ATOM   2851 N N   . LEU   A 1 548 ? 3.472   43.650  67.275  1.00 80.43  ?  529 LEU   A N   1 
ATOM   2852 C CA  . LEU   A 1 548 ? 4.067   43.845  68.591  1.00 74.14  ?  529 LEU   A CA  1 
ATOM   2853 C C   . LEU   A 1 548 ? 4.137   45.326  68.937  1.00 79.87  ?  529 LEU   A C   1 
ATOM   2854 O O   . LEU   A 1 548 ? 3.958   45.718  70.098  1.00 75.63  ?  529 LEU   A O   1 
ATOM   2855 C CB  . LEU   A 1 548 ? 5.461   43.239  68.618  1.00 71.76  ?  529 LEU   A CB  1 
ATOM   2856 C CG  . LEU   A 1 548 ? 6.060   43.192  70.011  1.00 72.64  ?  529 LEU   A CG  1 
ATOM   2857 C CD1 . LEU   A 1 548 ? 5.115   42.413  70.913  1.00 73.41  ?  529 LEU   A CD1 1 
ATOM   2858 C CD2 . LEU   A 1 548 ? 7.454   42.570  69.969  1.00 70.38  ?  529 LEU   A CD2 1 
ATOM   2859 N N   . ASP   A 1 549 ? 4.397   46.167  67.938  1.00 78.21  ?  530 ASP   A N   1 
ATOM   2860 C CA  . ASP   A 1 549 ? 4.475   47.593  68.197  1.00 72.24  ?  530 ASP   A CA  1 
ATOM   2861 C C   . ASP   A 1 549 ? 3.168   48.149  68.713  1.00 74.98  ?  530 ASP   A C   1 
ATOM   2862 O O   . ASP   A 1 549 ? 3.173   49.121  69.471  1.00 77.57  ?  530 ASP   A O   1 
ATOM   2863 C CB  . ASP   A 1 549 ? 4.862   48.338  66.939  1.00 78.99  ?  530 ASP   A CB  1 
ATOM   2864 C CG  . ASP   A 1 549 ? 6.304   48.661  66.918  1.00 84.89  ?  530 ASP   A CG  1 
ATOM   2865 O OD1 . ASP   A 1 549 ? 6.952   48.401  67.966  1.00 76.13  ?  530 ASP   A OD1 1 
ATOM   2866 O OD2 . ASP   A 1 549 ? 6.779   49.177  65.877  1.00 88.13  ?  530 ASP   A OD2 1 
ATOM   2867 N N   . TRP   A 1 550 ? 2.044   47.581  68.289  1.00 73.86  ?  531 TRP   A N   1 
ATOM   2868 C CA  . TRP   A 1 550 ? 0.769   48.087  68.764  1.00 66.50  ?  531 TRP   A CA  1 
ATOM   2869 C C   . TRP   A 1 550 ? 0.551   47.705  70.219  1.00 68.92  ?  531 TRP   A C   1 
ATOM   2870 O O   . TRP   A 1 550 ? 0.030   48.503  71.008  1.00 72.77  ?  531 TRP   A O   1 
ATOM   2871 C CB  . TRP   A 1 550 ? -0.344  47.572  67.871  1.00 65.89  ?  531 TRP   A CB  1 
ATOM   2872 C CG  . TRP   A 1 550 ? -1.693  48.023  68.231  1.00 65.05  ?  531 TRP   A CG  1 
ATOM   2873 C CD1 . TRP   A 1 550 ? -2.438  48.995  67.601  1.00 64.46  ?  531 TRP   A CD1 1 
ATOM   2874 C CD2 . TRP   A 1 550 ? -2.512  47.491  69.276  1.00 59.31  ?  531 TRP   A CD2 1 
ATOM   2875 N NE1 . TRP   A 1 550 ? -3.669  49.102  68.214  1.00 66.76  ?  531 TRP   A NE1 1 
ATOM   2876 C CE2 . TRP   A 1 550 ? -3.736  48.192  69.244  1.00 65.79  ?  531 TRP   A CE2 1 
ATOM   2877 C CE3 . TRP   A 1 550 ? -2.327  46.491  70.239  1.00 68.18  ?  531 TRP   A CE3 1 
ATOM   2878 C CZ2 . TRP   A 1 550 ? -4.768  47.931  70.148  1.00 67.40  ?  531 TRP   A CZ2 1 
ATOM   2879 C CZ3 . TRP   A 1 550 ? -3.346  46.233  71.143  1.00 71.32  ?  531 TRP   A CZ3 1 
ATOM   2880 C CH2 . TRP   A 1 550 ? -4.555  46.951  71.089  1.00 71.56  ?  531 TRP   A CH2 1 
ATOM   2881 N N   . HIS   A 1 551 ? 0.961   46.503  70.604  1.00 65.15  ?  532 HIS   A N   1 
ATOM   2882 C CA  . HIS   A 1 551 ? 0.859   46.135  72.004  1.00 71.18  ?  532 HIS   A CA  1 
ATOM   2883 C C   . HIS   A 1 551 ? 1.769   46.986  72.887  1.00 73.83  ?  532 HIS   A C   1 
ATOM   2884 O O   . HIS   A 1 551 ? 1.485   47.147  74.080  1.00 73.96  ?  532 HIS   A O   1 
ATOM   2885 C CB  . HIS   A 1 551 ? 1.172   44.653  72.176  1.00 77.91  ?  532 HIS   A CB  1 
ATOM   2886 C CG  . HIS   A 1 551 ? 0.045   43.754  71.778  1.00 83.29  ?  532 HIS   A CG  1 
ATOM   2887 N ND1 . HIS   A 1 551 ? -0.319  43.552  70.463  1.00 84.24  ?  532 HIS   A ND1 1 
ATOM   2888 C CD2 . HIS   A 1 551 ? -0.799  43.000  72.520  1.00 87.98  ?  532 HIS   A CD2 1 
ATOM   2889 C CE1 . HIS   A 1 551 ? -1.341  42.716  70.412  1.00 88.34  ?  532 HIS   A CE1 1 
ATOM   2890 N NE2 . HIS   A 1 551 ? -1.647  42.360  71.647  1.00 88.96  ?  532 HIS   A NE2 1 
ATOM   2891 N N   . PHE   A 1 552 ? 2.846   47.543  72.333  1.00 71.07  ?  533 PHE   A N   1 
ATOM   2892 C CA  . PHE   A 1 552 ? 3.638   48.491  73.106  1.00 68.83  ?  533 PHE   A CA  1 
ATOM   2893 C C   . PHE   A 1 552 ? 2.955   49.852  73.161  1.00 66.57  ?  533 PHE   A C   1 
ATOM   2894 O O   . PHE   A 1 552 ? 2.894   50.472  74.224  1.00 62.29  ?  533 PHE   A O   1 
ATOM   2895 C CB  . PHE   A 1 552 ? 5.046   48.614  72.525  1.00 66.76  ?  533 PHE   A CB  1 
ATOM   2896 C CG  . PHE   A 1 552 ? 5.894   47.391  72.730  1.00 67.65  ?  533 PHE   A CG  1 
ATOM   2897 C CD1 . PHE   A 1 552 ? 6.771   46.959  71.729  1.00 70.43  ?  533 PHE   A CD1 1 
ATOM   2898 C CD2 . PHE   A 1 552 ? 5.816   46.663  73.910  1.00 70.95  ?  533 PHE   A CD2 1 
ATOM   2899 C CE1 . PHE   A 1 552 ? 7.566   45.831  71.896  1.00 58.81  ?  533 PHE   A CE1 1 
ATOM   2900 C CE2 . PHE   A 1 552 ? 6.613   45.516  74.092  1.00 75.57  ?  533 PHE   A CE2 1 
ATOM   2901 C CZ  . PHE   A 1 552 ? 7.492   45.107  73.077  1.00 67.77  ?  533 PHE   A CZ  1 
ATOM   2902 N N   . ALA   A 1 553 ? 2.427   50.324  72.031  1.00 68.03  ?  534 ALA   A N   1 
ATOM   2903 C CA  . ALA   A 1 553 ? 1.633   51.546  72.042  1.00 66.71  ?  534 ALA   A CA  1 
ATOM   2904 C C   . ALA   A 1 553 ? 0.518   51.469  73.078  1.00 66.90  ?  534 ALA   A C   1 
ATOM   2905 O O   . ALA   A 1 553 ? 0.294   52.428  73.820  1.00 75.70  ?  534 ALA   A O   1 
ATOM   2906 C CB  . ALA   A 1 553 ? 1.056   51.829  70.653  1.00 66.62  ?  534 ALA   A CB  1 
ATOM   2907 N N   . ASN   A 1 554 ? -0.177  50.334  73.165  1.00 66.78  ?  535 ASN   A N   1 
ATOM   2908 C CA  . ASN   A 1 554 ? -1.203  50.203  74.196  1.00 68.20  ?  535 ASN   A CA  1 
ATOM   2909 C C   . ASN   A 1 554 ? -0.618  50.403  75.589  1.00 63.65  ?  535 ASN   A C   1 
ATOM   2910 O O   . ASN   A 1 554 ? -1.221  51.073  76.428  1.00 64.96  ?  535 ASN   A O   1 
ATOM   2911 C CB  . ASN   A 1 554 ? -1.889  48.837  74.111  1.00 70.34  ?  535 ASN   A CB  1 
ATOM   2912 C CG  . ASN   A 1 554 ? -3.288  48.851  74.728  1.00 69.71  ?  535 ASN   A CG  1 
ATOM   2913 O OD1 . ASN   A 1 554 ? -4.106  49.716  74.410  1.00 73.33  ?  535 ASN   A OD1 1 
ATOM   2914 N ND2 . ASN   A 1 554 ? -3.560  47.907  75.617  1.00 61.52  ?  535 ASN   A ND2 1 
ATOM   2915 N N   . LEU   A 1 555 ? 0.547   49.810  75.855  1.00 64.16  ?  536 LEU   A N   1 
ATOM   2916 C CA  . LEU   A 1 555 ? 1.184   49.915  77.163  1.00 57.27  ?  536 LEU   A CA  1 
ATOM   2917 C C   . LEU   A 1 555 ? 1.735   51.315  77.399  1.00 63.40  ?  536 LEU   A C   1 
ATOM   2918 O O   . LEU   A 1 555 ? 1.876   51.753  78.542  1.00 62.36  ?  536 LEU   A O   1 
ATOM   2919 C CB  . LEU   A 1 555 ? 2.302   48.883  77.264  1.00 48.35  ?  536 LEU   A CB  1 
ATOM   2920 C CG  . LEU   A 1 555 ? 2.988   48.778  78.605  1.00 54.85  ?  536 LEU   A CG  1 
ATOM   2921 C CD1 . LEU   A 1 555 ? 2.057   48.097  79.577  1.00 58.21  ?  536 LEU   A CD1 1 
ATOM   2922 C CD2 . LEU   A 1 555 ? 4.315   48.029  78.519  1.00 55.26  ?  536 LEU   A CD2 1 
ATOM   2923 N N   . GLU   A 1 556 ? 2.065   52.023  76.334  1.00 62.43  ?  537 GLU   A N   1 
ATOM   2924 C CA  . GLU   A 1 556 ? 2.480   53.398  76.485  1.00 60.77  ?  537 GLU   A CA  1 
ATOM   2925 C C   . GLU   A 1 556 ? 1.283   54.270  76.799  1.00 66.98  ?  537 GLU   A C   1 
ATOM   2926 O O   . GLU   A 1 556 ? 1.401   55.258  77.541  1.00 68.36  ?  537 GLU   A O   1 
ATOM   2927 C CB  . GLU   A 1 556 ? 3.198   53.859  75.214  1.00 62.36  ?  537 GLU   A CB  1 
ATOM   2928 C CG  . GLU   A 1 556 ? 4.595   53.285  75.190  1.00 62.42  ?  537 GLU   A CG  1 
ATOM   2929 C CD  . GLU   A 1 556 ? 5.440   53.679  74.000  1.00 66.88  ?  537 GLU   A CD  1 
ATOM   2930 O OE1 . GLU   A 1 556 ? 4.887   53.991  72.906  1.00 64.61  ?  537 GLU   A OE1 1 
ATOM   2931 O OE2 . GLU   A 1 556 ? 6.683   53.663  74.193  1.00 66.43  ?  537 GLU   A OE2 1 
ATOM   2932 N N   . PHE   A 1 557 ? 0.131   53.923  76.227  1.00 64.18  ?  538 PHE   A N   1 
ATOM   2933 C CA  . PHE   A 1 557 ? -1.112  54.590  76.592  1.00 65.80  ?  538 PHE   A CA  1 
ATOM   2934 C C   . PHE   A 1 557 ? -1.466  54.359  78.064  1.00 65.58  ?  538 PHE   A C   1 
ATOM   2935 O O   . PHE   A 1 557 ? -1.809  55.298  78.783  1.00 67.43  ?  538 PHE   A O   1 
ATOM   2936 C CB  . PHE   A 1 557 ? -2.220  54.116  75.658  1.00 66.96  ?  538 PHE   A CB  1 
ATOM   2937 C CG  . PHE   A 1 557 ? -3.558  54.052  76.301  1.00 78.89  ?  538 PHE   A CG  1 
ATOM   2938 C CD1 . PHE   A 1 557 ? -4.207  55.207  76.703  1.00 74.79  ?  538 PHE   A CD1 1 
ATOM   2939 C CD2 . PHE   A 1 557 ? -4.163  52.809  76.529  1.00 77.12  ?  538 PHE   A CD2 1 
ATOM   2940 C CE1 . PHE   A 1 557 ? -5.438  55.126  77.327  1.00 84.32  ?  538 PHE   A CE1 1 
ATOM   2941 C CE2 . PHE   A 1 557 ? -5.404  52.724  77.141  1.00 83.33  ?  538 PHE   A CE2 1 
ATOM   2942 C CZ  . PHE   A 1 557 ? -6.046  53.887  77.538  1.00 90.88  ?  538 PHE   A CZ  1 
ATOM   2943 N N   . ALA   A 1 558 ? -1.365  53.118  78.539  1.00 61.26  ?  539 ALA   A N   1 
ATOM   2944 C CA  . ALA   A 1 558 ? -1.688  52.835  79.934  1.00 60.67  ?  539 ALA   A CA  1 
ATOM   2945 C C   . ALA   A 1 558 ? -0.897  53.719  80.894  1.00 61.03  ?  539 ALA   A C   1 
ATOM   2946 O O   . ALA   A 1 558 ? -1.423  54.160  81.924  1.00 64.04  ?  539 ALA   A O   1 
ATOM   2947 C CB  . ALA   A 1 558 ? -1.412  51.369  80.246  1.00 60.51  ?  539 ALA   A CB  1 
ATOM   2948 N N   . ASN   A 1 559 ? 0.370   53.966  80.586  1.00 54.24  ?  540 ASN   A N   1 
ATOM   2949 C CA  . ASN   A 1 559 ? 1.255   54.689  81.474  1.00 53.18  ?  540 ASN   A CA  1 
ATOM   2950 C C   . ASN   A 1 559 ? 1.542   56.088  80.967  1.00 54.21  ?  540 ASN   A C   1 
ATOM   2951 O O   . ASN   A 1 559 ? 2.376   56.798  81.538  1.00 53.22  ?  540 ASN   A O   1 
ATOM   2952 C CB  . ASN   A 1 559 ? 2.532   53.885  81.683  1.00 49.56  ?  540 ASN   A CB  1 
ATOM   2953 C CG  . ASN   A 1 559 ? 2.241   52.530  82.274  1.00 60.02  ?  540 ASN   A CG  1 
ATOM   2954 O OD1 . ASN   A 1 559 ? 2.235   52.341  83.504  1.00 65.47  ?  540 ASN   A OD1 1 
ATOM   2955 N ND2 . ASN   A 1 559 ? 1.935   51.577  81.402  1.00 63.17  ?  540 ASN   A ND2 1 
ATOM   2956 N N   . ALA   A 1 560 ? 0.842   56.508  79.929  1.00 57.89  ?  541 ALA   A N   1 
ATOM   2957 C CA  . ALA   A 1 560 ? 0.983   57.847  79.360  1.00 66.19  ?  541 ALA   A CA  1 
ATOM   2958 C C   . ALA   A 1 560 ? 2.449   58.270  79.173  1.00 56.79  ?  541 ALA   A C   1 
ATOM   2959 O O   . ALA   A 1 560 ? 2.831   59.384  79.492  1.00 57.28  ?  541 ALA   A O   1 
ATOM   2960 C CB  . ALA   A 1 560 ? 0.225   58.863  80.219  1.00 63.69  ?  541 ALA   A CB  1 
ATOM   2961 N N   . THR   A 1 561 ? 3.275   57.382  78.635  1.00 61.13  ?  542 THR   A N   1 
ATOM   2962 C CA  . THR   A 1 561 ? 4.674   57.754  78.446  1.00 57.36  ?  542 THR   A CA  1 
ATOM   2963 C C   . THR   A 1 561 ? 5.426   56.708  77.620  1.00 58.94  ?  542 THR   A C   1 
ATOM   2964 O O   . THR   A 1 561 ? 5.101   55.518  77.671  1.00 53.30  ?  542 THR   A O   1 
ATOM   2965 C CB  . THR   A 1 561 ? 5.387   57.963  79.791  1.00 49.24  ?  542 THR   A CB  1 
ATOM   2966 O OG1 . THR   A 1 561 ? 6.724   58.421  79.554  1.00 48.80  ?  542 THR   A OG1 1 
ATOM   2967 C CG2 . THR   A 1 561 ? 5.453   56.674  80.581  1.00 53.63  ?  542 THR   A CG2 1 
ATOM   2968 N N   . PRO   A 1 562 ? 6.404   57.141  76.827  1.00 55.39  ?  543 PRO   A N   1 
ATOM   2969 C CA  . PRO   A 1 562 ? 7.339   56.217  76.181  1.00 51.57  ?  543 PRO   A CA  1 
ATOM   2970 C C   . PRO   A 1 562 ? 7.976   55.223  77.142  1.00 57.56  ?  543 PRO   A C   1 
ATOM   2971 O O   . PRO   A 1 562 ? 8.470   55.599  78.211  1.00 55.58  ?  543 PRO   A O   1 
ATOM   2972 C CB  . PRO   A 1 562 ? 8.387   57.168  75.605  1.00 55.89  ?  543 PRO   A CB  1 
ATOM   2973 C CG  . PRO   A 1 562 ? 7.584   58.411  75.269  1.00 55.84  ?  543 PRO   A CG  1 
ATOM   2974 C CD  . PRO   A 1 562 ? 6.601   58.533  76.383  1.00 57.07  ?  543 PRO   A CD  1 
ATOM   2975 N N   . LEU   A 1 563 ? 8.027   53.941  76.728  1.00 54.11  ?  544 LEU   A N   1 
ATOM   2976 C CA  . LEU   A 1 563 ? 8.565   52.935  77.635  1.00 52.85  ?  544 LEU   A CA  1 
ATOM   2977 C C   . LEU   A 1 563 ? 10.037  53.145  77.972  1.00 54.41  ?  544 LEU   A C   1 
ATOM   2978 O O   . LEU   A 1 563 ? 10.553  52.466  78.869  1.00 61.66  ?  544 LEU   A O   1 
ATOM   2979 C CB  . LEU   A 1 563 ? 8.345   51.528  77.086  1.00 56.58  ?  544 LEU   A CB  1 
ATOM   2980 C CG  . LEU   A 1 563 ? 6.980   51.176  76.490  1.00 59.76  ?  544 LEU   A CG  1 
ATOM   2981 C CD1 . LEU   A 1 563 ? 7.050   49.802  75.872  1.00 65.24  ?  544 LEU   A CD1 1 
ATOM   2982 C CD2 . LEU   A 1 563 ? 5.874   51.180  77.552  1.00 61.07  ?  544 LEU   A CD2 1 
ATOM   2983 N N   . SER   A 1 564 ? 10.721  54.074  77.323  1.00 53.39  ?  545 SER   A N   1 
ATOM   2984 C CA  . SER   A 1 564 ? 12.095  54.348  77.712  1.00 53.91  ?  545 SER   A CA  1 
ATOM   2985 C C   . SER   A 1 564 ? 12.191  55.204  78.959  1.00 61.00  ?  545 SER   A C   1 
ATOM   2986 O O   . SER   A 1 564 ? 13.302  55.365  79.486  1.00 64.02  ?  545 SER   A O   1 
ATOM   2987 C CB  . SER   A 1 564 ? 12.830  55.058  76.589  1.00 57.28  ?  545 SER   A CB  1 
ATOM   2988 O OG  . SER   A 1 564 ? 12.192  56.293  76.317  1.00 70.26  ?  545 SER   A OG  1 
ATOM   2989 N N   . THR   A 1 565 ? 11.076  55.793  79.415  1.00 56.47  ?  546 THR   A N   1 
ATOM   2990 C CA  . THR   A 1 565 ? 11.075  56.587  80.639  1.00 55.11  ?  546 THR   A CA  1 
ATOM   2991 C C   . THR   A 1 565 ? 10.621  55.804  81.866  1.00 58.88  ?  546 THR   A C   1 
ATOM   2992 O O   . THR   A 1 565 ? 10.980  56.192  82.986  1.00 56.91  ?  546 THR   A O   1 
ATOM   2993 C CB  . THR   A 1 565 ? 10.175  57.824  80.501  1.00 55.36  ?  546 THR   A CB  1 
ATOM   2994 O OG1 . THR   A 1 565 ? 8.796   57.435  80.576  1.00 52.96  ?  546 THR   A OG1 1 
ATOM   2995 C CG2 . THR   A 1 565 ? 10.434  58.577  79.204  1.00 51.04  ?  546 THR   A CG2 1 
ATOM   2996 N N   . LEU   A 1 566 ? 9.857   54.714  81.686  1.00 58.58  ?  547 LEU   A N   1 
ATOM   2997 C CA  . LEU   A 1 566 ? 9.344   53.946  82.819  1.00 55.60  ?  547 LEU   A CA  1 
ATOM   2998 C C   . LEU   A 1 566 ? 10.470  53.249  83.571  1.00 57.83  ?  547 LEU   A C   1 
ATOM   2999 O O   . LEU   A 1 566 ? 11.379  52.682  82.968  1.00 61.76  ?  547 LEU   A O   1 
ATOM   3000 C CB  . LEU   A 1 566 ? 8.319   52.920  82.352  1.00 50.89  ?  547 LEU   A CB  1 
ATOM   3001 C CG  . LEU   A 1 566 ? 6.962   53.577  82.121  1.00 55.29  ?  547 LEU   A CG  1 
ATOM   3002 C CD1 . LEU   A 1 566 ? 5.950   52.661  81.465  1.00 55.90  ?  547 LEU   A CD1 1 
ATOM   3003 C CD2 . LEU   A 1 566 ? 6.432   54.055  83.452  1.00 58.89  ?  547 LEU   A CD2 1 
ATOM   3004 N N   . SER   A 1 567 ? 10.426  53.323  84.895  1.00 55.94  ?  548 SER   A N   1 
ATOM   3005 C CA  . SER   A 1 567 ? 11.339  52.544  85.716  1.00 57.89  ?  548 SER   A CA  1 
ATOM   3006 C C   . SER   A 1 567 ? 11.084  51.059  85.515  1.00 62.78  ?  548 SER   A C   1 
ATOM   3007 O O   . SER   A 1 567 ? 9.964   50.587  85.727  1.00 65.65  ?  548 SER   A O   1 
ATOM   3008 C CB  . SER   A 1 567 ? 11.152  52.910  87.181  1.00 58.71  ?  548 SER   A CB  1 
ATOM   3009 O OG  . SER   A 1 567 ? 11.714  51.936  88.032  1.00 54.44  ?  548 SER   A OG  1 
ATOM   3010 N N   . LEU   A 1 568 ? 12.118  50.314  85.117  1.00 62.31  ?  549 LEU   A N   1 
ATOM   3011 C CA  . LEU   A 1 568 ? 11.946  48.870  84.982  1.00 64.61  ?  549 LEU   A CA  1 
ATOM   3012 C C   . LEU   A 1 568 ? 11.544  48.248  86.314  1.00 60.03  ?  549 LEU   A C   1 
ATOM   3013 O O   . LEU   A 1 568 ? 10.572  47.493  86.390  1.00 57.17  ?  549 LEU   A O   1 
ATOM   3014 C CB  . LEU   A 1 568 ? 13.222  48.211  84.453  1.00 66.62  ?  549 LEU   A CB  1 
ATOM   3015 C CG  . LEU   A 1 568 ? 13.200  46.690  84.645  1.00 56.29  ?  549 LEU   A CG  1 
ATOM   3016 C CD1 . LEU   A 1 568 ? 12.360  46.068  83.561  1.00 57.61  ?  549 LEU   A CD1 1 
ATOM   3017 C CD2 . LEU   A 1 568 ? 14.583  46.088  84.671  1.00 59.24  ?  549 LEU   A CD2 1 
ATOM   3018 N N   . LYS   A 1 569 ? 12.248  48.597  87.388  1.00 57.60  ?  550 LYS   A N   1 
ATOM   3019 C CA  . LYS   A 1 569 ? 11.984  47.952  88.666  1.00 55.03  ?  550 LYS   A CA  1 
ATOM   3020 C C   . LYS   A 1 569 ? 10.555  48.218  89.143  1.00 60.75  ?  550 LYS   A C   1 
ATOM   3021 O O   . LYS   A 1 569 ? 9.846   47.290  89.554  1.00 64.58  ?  550 LYS   A O   1 
ATOM   3022 C CB  . LYS   A 1 569 ? 13.020  48.408  89.696  1.00 54.62  ?  550 LYS   A CB  1 
ATOM   3023 C CG  . LYS   A 1 569 ? 12.977  47.599  90.971  1.00 68.75  ?  550 LYS   A CG  1 
ATOM   3024 C CD  . LYS   A 1 569 ? 14.199  47.878  91.878  1.00 72.45  ?  550 LYS   A CD  1 
ATOM   3025 C CE  . LYS   A 1 569 ? 14.073  47.116  93.204  1.00 85.04  ?  550 LYS   A CE  1 
ATOM   3026 N NZ  . LYS   A 1 569 ? 14.072  45.618  92.991  1.00 94.39  ?  550 LYS   A NZ  1 
ATOM   3027 N N   . HIS   A 1 570 ? 10.086  49.473  89.029  1.00 66.71  ?  551 HIS   A N   1 
ATOM   3028 C CA  . HIS   A 1 570 ? 8.941   49.949  89.805  1.00 61.85  ?  551 HIS   A CA  1 
ATOM   3029 C C   . HIS   A 1 570 ? 7.700   50.362  89.018  1.00 61.55  ?  551 HIS   A C   1 
ATOM   3030 O O   . HIS   A 1 570 ? 6.723   50.786  89.645  1.00 58.86  ?  551 HIS   A O   1 
ATOM   3031 C CB  . HIS   A 1 570 ? 9.359   51.158  90.628  1.00 56.84  ?  551 HIS   A CB  1 
ATOM   3032 C CG  . HIS   A 1 570 ? 10.378  50.858  91.662  1.00 57.21  ?  551 HIS   A CG  1 
ATOM   3033 N ND1 . HIS   A 1 570 ? 10.135  50.009  92.715  1.00 67.42  ?  551 HIS   A ND1 1 
ATOM   3034 C CD2 . HIS   A 1 570 ? 11.648  51.300  91.811  1.00 59.92  ?  551 HIS   A CD2 1 
ATOM   3035 C CE1 . HIS   A 1 570 ? 11.216  49.938  93.472  1.00 71.46  ?  551 HIS   A CE1 1 
ATOM   3036 N NE2 . HIS   A 1 570 ? 12.148  50.716  92.947  1.00 62.44  ?  551 HIS   A NE2 1 
ATOM   3037 N N   . TRP   A 1 571 ? 7.707   50.286  87.682  1.00 57.95  ?  552 TRP   A N   1 
ATOM   3038 C CA  . TRP   A 1 571 ? 6.623   50.871  86.891  1.00 55.84  ?  552 TRP   A CA  1 
ATOM   3039 C C   . TRP   A 1 571 ? 5.255   50.271  87.191  1.00 58.69  ?  552 TRP   A C   1 
ATOM   3040 O O   . TRP   A 1 571 ? 4.233   50.879  86.856  1.00 60.90  ?  552 TRP   A O   1 
ATOM   3041 C CB  . TRP   A 1 571 ? 6.905   50.709  85.392  1.00 60.09  ?  552 TRP   A CB  1 
ATOM   3042 C CG  . TRP   A 1 571 ? 6.734   49.282  84.903  1.00 68.23  ?  552 TRP   A CG  1 
ATOM   3043 C CD1 . TRP   A 1 571 ? 7.640   48.248  85.025  1.00 60.12  ?  552 TRP   A CD1 1 
ATOM   3044 C CD2 . TRP   A 1 571 ? 5.578   48.724  84.244  1.00 63.34  ?  552 TRP   A CD2 1 
ATOM   3045 N NE1 . TRP   A 1 571 ? 7.112   47.104  84.482  1.00 58.05  ?  552 TRP   A NE1 1 
ATOM   3046 C CE2 . TRP   A 1 571 ? 5.857   47.366  83.992  1.00 56.78  ?  552 TRP   A CE2 1 
ATOM   3047 C CE3 . TRP   A 1 571 ? 4.341   49.244  83.838  1.00 61.53  ?  552 TRP   A CE3 1 
ATOM   3048 C CZ2 . TRP   A 1 571 ? 4.955   46.525  83.347  1.00 53.79  ?  552 TRP   A CZ2 1 
ATOM   3049 C CZ3 . TRP   A 1 571 ? 3.439   48.394  83.192  1.00 61.76  ?  552 TRP   A CZ3 1 
ATOM   3050 C CH2 . TRP   A 1 571 ? 3.754   47.050  82.963  1.00 51.80  ?  552 TRP   A CH2 1 
ATOM   3051 N N   . ASP   A 1 572 ? 5.200   49.083  87.778  1.00 63.47  ?  553 ASP   A N   1 
ATOM   3052 C CA  . ASP   A 1 572 ? 3.932   48.392  87.973  1.00 69.73  ?  553 ASP   A CA  1 
ATOM   3053 C C   . ASP   A 1 572 ? 3.655   48.194  89.454  1.00 70.68  ?  553 ASP   A C   1 
ATOM   3054 O O   . ASP   A 1 572 ? 2.858   47.330  89.827  1.00 80.80  ?  553 ASP   A O   1 
ATOM   3055 C CB  . ASP   A 1 572 ? 3.917   47.056  87.200  1.00 72.00  ?  553 ASP   A CB  1 
ATOM   3056 C CG  . ASP   A 1 572 ? 5.032   46.061  87.657  1.00 77.96  ?  553 ASP   A CG  1 
ATOM   3057 O OD1 . ASP   A 1 572 ? 6.105   46.498  88.175  1.00 75.26  ?  553 ASP   A OD1 1 
ATOM   3058 O OD2 . ASP   A 1 572 ? 4.831   44.828  87.488  1.00 74.76  ?  553 ASP   A OD2 1 
ATOM   3059 N N   . GLN   A 1 573 ? 4.301   48.996  90.307  1.00 73.32  ?  554 GLN   A N   1 
ATOM   3060 C CA  . GLN   A 1 573 ? 4.225   48.820  91.759  1.00 73.66  ?  554 GLN   A CA  1 
ATOM   3061 C C   . GLN   A 1 573 ? 2.814   48.976  92.309  1.00 72.35  ?  554 GLN   A C   1 
ATOM   3062 O O   . GLN   A 1 573 ? 2.557   48.560  93.443  1.00 73.45  ?  554 GLN   A O   1 
ATOM   3063 C CB  . GLN   A 1 573 ? 5.179   49.800  92.446  1.00 68.30  ?  554 GLN   A CB  1 
ATOM   3064 C CG  . GLN   A 1 573 ? 4.951   51.265  92.075  1.00 69.25  ?  554 GLN   A CG  1 
ATOM   3065 C CD  . GLN   A 1 573 ? 4.097   52.043  93.061  1.00 65.19  ?  554 GLN   A CD  1 
ATOM   3066 O OE1 . GLN   A 1 573 ? 4.217   51.881  94.275  1.00 67.97  ?  554 GLN   A OE1 1 
ATOM   3067 N NE2 . GLN   A 1 573 ? 3.217   52.893  92.533  1.00 66.03  ?  554 GLN   A NE2 1 
ATOM   3068 N N   . ASP   A 1 574 ? 1.891   49.520  91.524  1.00 75.40  ?  555 ASP   A N   1 
ATOM   3069 C CA  . ASP   A 1 574 ? 0.516   49.698  91.952  1.00 75.96  ?  555 ASP   A CA  1 
ATOM   3070 C C   . ASP   A 1 574 ? -0.414  48.572  91.483  1.00 84.41  ?  555 ASP   A C   1 
ATOM   3071 O O   . ASP   A 1 574 ? -1.626  48.653  91.734  1.00 82.92  ?  555 ASP   A O   1 
ATOM   3072 C CB  . ASP   A 1 574 ? -0.011  51.070  91.483  1.00 72.06  ?  555 ASP   A CB  1 
ATOM   3073 C CG  . ASP   A 1 574 ? -0.100  51.210  89.960  1.00 78.50  ?  555 ASP   A CG  1 
ATOM   3074 O OD1 . ASP   A 1 574 ? 0.712   50.615  89.208  1.00 85.72  ?  555 ASP   A OD1 1 
ATOM   3075 O OD2 . ASP   A 1 574 ? -1.003  51.948  89.508  1.00 84.61  ?  555 ASP   A OD2 1 
ATOM   3076 N N   . ASP   A 1 575 ? 0.108   47.520  90.817  1.00 91.75  ?  556 ASP   A N   1 
ATOM   3077 C CA  . ASP   A 1 575 ? -0.783  46.430  90.408  1.00 91.41  ?  556 ASP   A CA  1 
ATOM   3078 C C   . ASP   A 1 575 ? -1.357  45.638  91.566  1.00 89.83  ?  556 ASP   A C   1 
ATOM   3079 O O   . ASP   A 1 575 ? -2.361  44.951  91.362  1.00 93.27  ?  556 ASP   A O   1 
ATOM   3080 C CB  . ASP   A 1 575 ? -0.146  45.397  89.445  1.00 86.91  ?  556 ASP   A CB  1 
ATOM   3081 C CG  . ASP   A 1 575 ? -0.080  45.868  87.987  1.00 106.61 ?  556 ASP   A CG  1 
ATOM   3082 O OD1 . ASP   A 1 575 ? -0.414  47.043  87.680  1.00 112.83 ?  556 ASP   A OD1 1 
ATOM   3083 O OD2 . ASP   A 1 575 ? 0.183   45.008  87.115  1.00 112.52 ?  556 ASP   A OD2 1 
ATOM   3084 N N   . ASP   A 1 576 ? -0.785  45.688  92.760  1.00 83.81  ?  557 ASP   A N   1 
ATOM   3085 C CA  . ASP   A 1 576 ? -1.308  44.734  93.721  1.00 82.71  ?  557 ASP   A CA  1 
ATOM   3086 C C   . ASP   A 1 576 ? -2.537  45.275  94.418  1.00 77.49  ?  557 ASP   A C   1 
ATOM   3087 O O   . ASP   A 1 576 ? -3.107  44.591  95.267  1.00 82.91  ?  557 ASP   A O   1 
ATOM   3088 C CB  . ASP   A 1 576 ? -0.253  44.341  94.740  1.00 90.32  ?  557 ASP   A CB  1 
ATOM   3089 C CG  . ASP   A 1 576 ? 1.048   43.984  94.063  1.00 113.10 ?  557 ASP   A CG  1 
ATOM   3090 O OD1 . ASP   A 1 576 ? 1.044   43.928  92.797  1.00 119.43 ?  557 ASP   A OD1 1 
ATOM   3091 O OD2 . ASP   A 1 576 ? 1.985   43.572  94.793  1.00 122.58 ?  557 ASP   A OD2 1 
ATOM   3092 N N   . PHE   A 1 577 ? -2.962  46.482  94.049  1.00 79.43  ?  558 PHE   A N   1 
ATOM   3093 C CA  . PHE   A 1 577 ? -4.136  47.134  94.608  1.00 68.99  ?  558 PHE   A CA  1 
ATOM   3094 C C   . PHE   A 1 577 ? -5.174  47.380  93.532  1.00 67.90  ?  558 PHE   A C   1 
ATOM   3095 O O   . PHE   A 1 577 ? -6.063  48.213  93.708  1.00 70.12  ?  558 PHE   A O   1 
ATOM   3096 C CB  . PHE   A 1 577 ? -3.752  48.440  95.305  1.00 64.04  ?  558 PHE   A CB  1 
ATOM   3097 C CG  . PHE   A 1 577 ? -2.467  48.357  96.104  1.00 61.07  ?  558 PHE   A CG  1 
ATOM   3098 C CD1 . PHE   A 1 577 ? -2.488  48.066  97.457  1.00 61.51  ?  558 PHE   A CD1 1 
ATOM   3099 C CD2 . PHE   A 1 577 ? -1.240  48.612  95.513  1.00 64.30  ?  558 PHE   A CD2 1 
ATOM   3100 C CE1 . PHE   A 1 577 ? -1.313  48.002  98.209  1.00 54.47  ?  558 PHE   A CE1 1 
ATOM   3101 C CE2 . PHE   A 1 577 ? -0.062  48.544  96.268  1.00 62.01  ?  558 PHE   A CE2 1 
ATOM   3102 C CZ  . PHE   A 1 577 ? -0.111  48.235  97.617  1.00 51.86  ?  558 PHE   A CZ  1 
ATOM   3103 N N   . GLU   A 1 578 ? -5.053  46.675  92.411  1.00 77.78  ?  559 GLU   A N   1 
ATOM   3104 C CA  . GLU   A 1 578 ? -6.052  46.723  91.355  1.00 74.31  ?  559 GLU   A CA  1 
ATOM   3105 C C   . GLU   A 1 578 ? -7.413  46.361  91.946  1.00 67.79  ?  559 GLU   A C   1 
ATOM   3106 O O   . GLU   A 1 578 ? -7.518  45.566  92.884  1.00 68.41  ?  559 GLU   A O   1 
ATOM   3107 C CB  . GLU   A 1 578 ? -5.638  45.755  90.236  1.00 90.27  ?  559 GLU   A CB  1 
ATOM   3108 C CG  . GLU   A 1 578 ? -6.017  46.081  88.770  1.00 102.37 ?  559 GLU   A CG  1 
ATOM   3109 C CD  . GLU   A 1 578 ? -5.690  44.901  87.789  1.00 117.75 ?  559 GLU   A CD  1 
ATOM   3110 O OE1 . GLU   A 1 578 ? -5.202  43.824  88.240  1.00 109.92 ?  559 GLU   A OE1 1 
ATOM   3111 O OE2 . GLU   A 1 578 ? -5.927  45.052  86.563  1.00 120.26 ?  559 GLU   A OE2 1 
ATOM   3112 N N   . PHE   A 1 579 ? -8.459  46.989  91.434  1.00 68.18  ?  560 PHE   A N   1 
ATOM   3113 C CA  . PHE   A 1 579 ? -9.800  46.636  91.878  1.00 71.79  ?  560 PHE   A CA  1 
ATOM   3114 C C   . PHE   A 1 579 ? -10.326 45.417  91.111  1.00 74.50  ?  560 PHE   A C   1 
ATOM   3115 O O   . PHE   A 1 579 ? -9.940  45.161  89.961  1.00 80.39  ?  560 PHE   A O   1 
ATOM   3116 C CB  . PHE   A 1 579 ? -10.754 47.810  91.672  1.00 73.35  ?  560 PHE   A CB  1 
ATOM   3117 C CG  . PHE   A 1 579 ? -10.412 49.031  92.483  1.00 76.03  ?  560 PHE   A CG  1 
ATOM   3118 C CD1 . PHE   A 1 579 ? -9.993  48.908  93.800  1.00 70.88  ?  560 PHE   A CD1 1 
ATOM   3119 C CD2 . PHE   A 1 579 ? -10.517 50.314  91.921  1.00 67.19  ?  560 PHE   A CD2 1 
ATOM   3120 C CE1 . PHE   A 1 579 ? -9.683  50.029  94.542  1.00 66.73  ?  560 PHE   A CE1 1 
ATOM   3121 C CE2 . PHE   A 1 579 ? -10.214 51.434  92.660  1.00 60.74  ?  560 PHE   A CE2 1 
ATOM   3122 C CZ  . PHE   A 1 579 ? -9.791  51.295  93.965  1.00 65.17  ?  560 PHE   A CZ  1 
ATOM   3123 N N   . THR   A 1 580 ? -11.248 44.683  91.740  1.00 65.49  ?  561 THR   A N   1 
ATOM   3124 C CA  . THR   A 1 580 ? -11.876 43.537  91.092  1.00 71.52  ?  561 THR   A CA  1 
ATOM   3125 C C   . THR   A 1 580 ? -13.124 43.982  90.332  1.00 74.05  ?  561 THR   A C   1 
ATOM   3126 O O   . THR   A 1 580 ? -13.856 44.867  90.783  1.00 73.23  ?  561 THR   A O   1 
ATOM   3127 C CB  . THR   A 1 580 ? -12.299 42.477  92.097  1.00 64.46  ?  561 THR   A CB  1 
ATOM   3128 O OG1 . THR   A 1 580 ? -13.398 42.982  92.847  1.00 73.26  ?  561 THR   A OG1 1 
ATOM   3129 C CG2 . THR   A 1 580 ? -11.136 42.151  93.057  1.00 61.49  ?  561 THR   A CG2 1 
ATOM   3130 N N   . GLY   A 1 581 ? -13.372 43.353  89.189  1.00 75.42  ?  562 GLY   A N   1 
ATOM   3131 C CA  . GLY   A 1 581 ? -14.580 43.580  88.421  1.00 66.38  ?  562 GLY   A CA  1 
ATOM   3132 C C   . GLY   A 1 581 ? -14.290 44.236  87.085  1.00 73.81  ?  562 GLY   A C   1 
ATOM   3133 O O   . GLY   A 1 581 ? -13.176 44.669  86.789  1.00 74.42  ?  562 GLY   A O   1 
ATOM   3134 N N   . SER   A 1 582 ? -15.340 44.282  86.273  1.00 71.46  ?  563 SER   A N   1 
ATOM   3135 C CA  . SER   A 1 582 ? -15.224 44.823  84.931  1.00 72.69  ?  563 SER   A CA  1 
ATOM   3136 C C   . SER   A 1 582 ? -14.931 46.304  85.009  1.00 73.47  ?  563 SER   A C   1 
ATOM   3137 O O   . SER   A 1 582 ? -15.457 46.999  85.868  1.00 77.93  ?  563 SER   A O   1 
ATOM   3138 C CB  . SER   A 1 582 ? -16.521 44.606  84.146  1.00 84.57  ?  563 SER   A CB  1 
ATOM   3139 O OG  . SER   A 1 582 ? -16.600 43.308  83.593  1.00 103.90 ?  563 SER   A OG  1 
ATOM   3140 N N   . HIS   A 1 583 ? -14.077 46.780  84.120  1.00 72.75  ?  564 HIS   A N   1 
ATOM   3141 C CA  . HIS   A 1 583 ? -13.911 48.205  83.910  1.00 60.91  ?  564 HIS   A CA  1 
ATOM   3142 C C   . HIS   A 1 583 ? -15.169 48.766  83.255  1.00 73.50  ?  564 HIS   A C   1 
ATOM   3143 O O   . HIS   A 1 583 ? -15.897 48.052  82.567  1.00 85.33  ?  564 HIS   A O   1 
ATOM   3144 C CB  . HIS   A 1 583 ? -12.666 48.416  83.054  1.00 59.24  ?  564 HIS   A CB  1 
ATOM   3145 C CG  . HIS   A 1 583 ? -11.393 48.183  83.807  1.00 61.07  ?  564 HIS   A CG  1 
ATOM   3146 N ND1 . HIS   A 1 583 ? -11.331 47.350  84.910  1.00 60.81  ?  564 HIS   A ND1 1 
ATOM   3147 C CD2 . HIS   A 1 583 ? -10.116 48.549  83.541  1.00 63.62  ?  564 HIS   A CD2 1 
ATOM   3148 C CE1 . HIS   A 1 583 ? -10.087 47.293  85.350  1.00 61.30  ?  564 HIS   A CE1 1 
ATOM   3149 N NE2 . HIS   A 1 583 ? -9.329  48.005  84.534  1.00 73.80  ?  564 HIS   A NE2 1 
ATOM   3150 N N   . LEU   A 1 584 ? -15.460 50.043  83.512  1.00 78.73  ?  565 LEU   A N   1 
ATOM   3151 C CA  . LEU   A 1 584 ? -16.696 50.652  83.033  1.00 75.39  ?  565 LEU   A CA  1 
ATOM   3152 C C   . LEU   A 1 584 ? -16.408 52.032  82.484  1.00 75.21  ?  565 LEU   A C   1 
ATOM   3153 O O   . LEU   A 1 584 ? -15.372 52.628  82.768  1.00 76.42  ?  565 LEU   A O   1 
ATOM   3154 C CB  . LEU   A 1 584 ? -17.756 50.811  84.120  1.00 75.82  ?  565 LEU   A CB  1 
ATOM   3155 C CG  . LEU   A 1 584 ? -18.271 49.565  84.823  1.00 82.26  ?  565 LEU   A CG  1 
ATOM   3156 C CD1 . LEU   A 1 584 ? -17.318 49.181  85.882  1.00 74.43  ?  565 LEU   A CD1 1 
ATOM   3157 C CD2 . LEU   A 1 584 ? -19.610 49.837  85.433  1.00 91.28  ?  565 LEU   A CD2 1 
ATOM   3158 N N   . THR   A 1 585 ? -17.347 52.541  81.700  1.00 75.34  ?  566 THR   A N   1 
ATOM   3159 C CA  . THR   A 1 585 ? -17.307 53.915  81.247  1.00 76.86  ?  566 THR   A CA  1 
ATOM   3160 C C   . THR   A 1 585 ? -18.523 54.632  81.804  1.00 84.73  ?  566 THR   A C   1 
ATOM   3161 O O   . THR   A 1 585 ? -19.412 54.015  82.401  1.00 82.28  ?  566 THR   A O   1 
ATOM   3162 C CB  . THR   A 1 585 ? -17.260 54.023  79.715  1.00 79.62  ?  566 THR   A CB  1 
ATOM   3163 O OG1 . THR   A 1 585 ? -18.539 53.707  79.151  1.00 81.40  ?  566 THR   A OG1 1 
ATOM   3164 C CG2 . THR   A 1 585 ? -16.199 53.104  79.160  1.00 77.70  ?  566 THR   A CG2 1 
ATOM   3165 N N   . VAL   A 1 586 ? -18.533 55.951  81.617  1.00 84.85  ?  567 VAL   A N   1 
ATOM   3166 C CA  . VAL   A 1 586 ? -19.555 56.829  82.167  1.00 84.11  ?  567 VAL   A CA  1 
ATOM   3167 C C   . VAL   A 1 586 ? -20.278 57.422  80.973  1.00 89.07  ?  567 VAL   A C   1 
ATOM   3168 O O   . VAL   A 1 586 ? -19.752 58.319  80.301  1.00 92.75  ?  567 VAL   A O   1 
ATOM   3169 C CB  . VAL   A 1 586 ? -18.961 57.921  83.059  1.00 86.26  ?  567 VAL   A CB  1 
ATOM   3170 C CG1 . VAL   A 1 586 ? -20.017 58.963  83.374  1.00 93.87  ?  567 VAL   A CG1 1 
ATOM   3171 C CG2 . VAL   A 1 586 ? -18.396 57.322  84.341  1.00 76.61  ?  567 VAL   A CG2 1 
ATOM   3172 N N   . ARG   A 1 587 ? -21.483 56.924  80.695  1.00 94.97  ?  568 ARG   A N   1 
ATOM   3173 C CA  . ARG   A 1 587 ? -22.102 57.246  79.414  1.00 102.98 ?  568 ARG   A CA  1 
ATOM   3174 C C   . ARG   A 1 587 ? -22.655 58.663  79.370  1.00 100.89 ?  568 ARG   A C   1 
ATOM   3175 O O   . ARG   A 1 587 ? -22.745 59.245  78.280  1.00 98.83  ?  568 ARG   A O   1 
ATOM   3176 C CB  . ARG   A 1 587 ? -23.198 56.236  79.080  1.00 105.01 ?  568 ARG   A CB  1 
ATOM   3177 C CG  . ARG   A 1 587 ? -22.659 54.997  78.390  1.00 109.79 ?  568 ARG   A CG  1 
ATOM   3178 C CD  . ARG   A 1 587 ? -23.774 54.076  77.931  1.00 119.03 ?  568 ARG   A CD  1 
ATOM   3179 N NE  . ARG   A 1 587 ? -23.918 54.028  76.477  1.00 123.58 ?  568 ARG   A NE  1 
ATOM   3180 C CZ  . ARG   A 1 587 ? -24.680 53.137  75.849  1.00 123.69 ?  568 ARG   A CZ  1 
ATOM   3181 N NH1 . ARG   A 1 587 ? -25.345 52.235  76.557  1.00 122.64 ?  568 ARG   A NH1 1 
ATOM   3182 N NH2 . ARG   A 1 587 ? -24.769 53.129  74.523  1.00 124.58 ?  568 ARG   A NH2 1 
ATOM   3183 N N   . ASN   A 1 588 ? -23.019 59.233  80.521  1.00 98.79  ?  569 ASN   A N   1 
ATOM   3184 C CA  . ASN   A 1 588 ? -23.512 60.603  80.572  1.00 97.18  ?  569 ASN   A CA  1 
ATOM   3185 C C   . ASN   A 1 588 ? -22.407 61.631  80.792  1.00 96.27  ?  569 ASN   A C   1 
ATOM   3186 O O   . ASN   A 1 588 ? -22.718 62.811  80.999  1.00 98.17  ?  569 ASN   A O   1 
ATOM   3187 C CB  . ASN   A 1 588 ? -24.581 60.755  81.655  1.00 98.70  ?  569 ASN   A CB  1 
ATOM   3188 C CG  . ASN   A 1 588 ? -24.188 60.096  82.954  1.00 107.46 ?  569 ASN   A CG  1 
ATOM   3189 O OD1 . ASN   A 1 588 ? -23.203 59.354  83.007  1.00 106.31 ?  569 ASN   A OD1 1 
ATOM   3190 N ND2 . ASN   A 1 588 ? -24.939 60.379  84.023  1.00 108.19 ?  569 ASN   A ND2 1 
ATOM   3191 N N   . GLY   A 1 589 ? -21.135 61.223  80.722  1.00 91.18  ?  570 GLY   A N   1 
ATOM   3192 C CA  . GLY   A 1 589 ? -20.015 62.143  80.879  1.00 84.63  ?  570 GLY   A CA  1 
ATOM   3193 C C   . GLY   A 1 589 ? -19.494 62.160  82.312  1.00 90.40  ?  570 GLY   A C   1 
ATOM   3194 O O   . GLY   A 1 589 ? -20.285 62.281  83.262  1.00 94.87  ?  570 GLY   A O   1 
ATOM   3195 N N   . TYR   A 1 590 ? -18.176 62.046  82.501  1.00 79.34  ?  571 TYR   A N   1 
ATOM   3196 C CA  . TYR   A 1 590 ? -17.630 61.869  83.840  1.00 74.37  ?  571 TYR   A CA  1 
ATOM   3197 C C   . TYR   A 1 590 ? -17.567 63.181  84.601  1.00 77.39  ?  571 TYR   A C   1 
ATOM   3198 O O   . TYR   A 1 590 ? -17.515 63.159  85.835  1.00 75.56  ?  571 TYR   A O   1 
ATOM   3199 C CB  . TYR   A 1 590 ? -16.271 61.158  83.702  1.00 72.54  ?  571 TYR   A CB  1 
ATOM   3200 C CG  . TYR   A 1 590 ? -15.648 60.506  84.934  1.00 72.01  ?  571 TYR   A CG  1 
ATOM   3201 C CD1 . TYR   A 1 590 ? -16.414 60.158  86.041  1.00 71.40  ?  571 TYR   A CD1 1 
ATOM   3202 C CD2 . TYR   A 1 590 ? -14.429 59.841  84.797  1.00 66.50  ?  571 TYR   A CD2 1 
ATOM   3203 C CE1 . TYR   A 1 590 ? -15.867 59.435  87.102  1.00 63.54  ?  571 TYR   A CE1 1 
ATOM   3204 C CE2 . TYR   A 1 590 ? -13.892 59.081  85.821  1.00 62.27  ?  571 TYR   A CE2 1 
ATOM   3205 C CZ  . TYR   A 1 590 ? -14.611 58.879  86.976  1.00 67.30  ?  571 TYR   A CZ  1 
ATOM   3206 O OH  . TYR   A 1 590 ? -14.056 58.107  87.994  1.00 65.61  ?  571 TYR   A OH  1 
ATOM   3207 N N   . SER   A 1 591 ? -17.657 64.314  83.892  1.00 76.17  ?  572 SER   A N   1 
ATOM   3208 C CA  . SER   A 1 591 ? -17.807 65.599  84.552  1.00 72.69  ?  572 SER   A CA  1 
ATOM   3209 C C   . SER   A 1 591 ? -18.997 65.619  85.494  1.00 75.25  ?  572 SER   A C   1 
ATOM   3210 O O   . SER   A 1 591 ? -19.047 66.456  86.402  1.00 77.54  ?  572 SER   A O   1 
ATOM   3211 C CB  . SER   A 1 591 ? -17.976 66.707  83.522  1.00 70.82  ?  572 SER   A CB  1 
ATOM   3212 O OG  . SER   A 1 591 ? -19.337 66.817  83.151  1.00 73.22  ?  572 SER   A OG  1 
ATOM   3213 N N   . CYS   A 1 592 ? -19.965 64.726  85.300  1.00 79.31  ?  573 CYS   A N   1 
ATOM   3214 C CA  . CYS   A 1 592 ? -21.120 64.711  86.181  1.00 75.77  ?  573 CYS   A CA  1 
ATOM   3215 C C   . CYS   A 1 592 ? -20.709 64.551  87.636  1.00 73.08  ?  573 CYS   A C   1 
ATOM   3216 O O   . CYS   A 1 592 ? -21.468 64.949  88.526  1.00 77.58  ?  573 CYS   A O   1 
ATOM   3217 C CB  . CYS   A 1 592 ? -22.090 63.595  85.756  1.00 85.94  ?  573 CYS   A CB  1 
ATOM   3218 S SG  . CYS   A 1 592 ? -21.678 61.880  86.295  1.00 89.13  ?  573 CYS   A SG  1 
ATOM   3219 N N   . VAL   A 1 593 ? -19.516 64.016  87.894  1.00 74.33  ?  574 VAL   A N   1 
ATOM   3220 C CA  . VAL   A 1 593 ? -19.059 63.703  89.251  1.00 71.32  ?  574 VAL   A CA  1 
ATOM   3221 C C   . VAL   A 1 593 ? -18.476 64.933  89.935  1.00 70.47  ?  574 VAL   A C   1 
ATOM   3222 O O   . VAL   A 1 593 ? -18.987 65.317  90.993  1.00 72.67  ?  574 VAL   A O   1 
ATOM   3223 C CB  . VAL   A 1 593 ? -18.054 62.541  89.252  1.00 69.50  ?  574 VAL   A CB  1 
ATOM   3224 C CG1 . VAL   A 1 593 ? -17.254 62.531  90.545  1.00 59.55  ?  574 VAL   A CG1 1 
ATOM   3225 C CG2 . VAL   A 1 593 ? -18.785 61.229  89.083  1.00 69.22  ?  574 VAL   A CG2 1 
ATOM   3226 N N   . PRO   A 1 594 ? -17.420 65.573  89.418  1.00 67.71  ?  575 PRO   A N   1 
ATOM   3227 C CA  . PRO   A 1 594 ? -16.971 66.813  90.058  1.00 67.13  ?  575 PRO   A CA  1 
ATOM   3228 C C   . PRO   A 1 594 ? -18.084 67.822  90.237  1.00 73.68  ?  575 PRO   A C   1 
ATOM   3229 O O   . PRO   A 1 594 ? -18.227 68.403  91.328  1.00 77.46  ?  575 PRO   A O   1 
ATOM   3230 C CB  . PRO   A 1 594 ? -15.881 67.322  89.108  1.00 63.10  ?  575 PRO   A CB  1 
ATOM   3231 C CG  . PRO   A 1 594 ? -16.043 66.577  87.887  1.00 67.32  ?  575 PRO   A CG  1 
ATOM   3232 C CD  . PRO   A 1 594 ? -16.528 65.238  88.303  1.00 68.42  ?  575 PRO   A CD  1 
ATOM   3233 N N   . VAL   A 1 595 ? -18.887 68.048  89.199  1.00 69.13  ?  576 VAL   A N   1 
ATOM   3234 C CA  . VAL   A 1 595 ? -19.968 69.018  89.328  1.00 69.44  ?  576 VAL   A CA  1 
ATOM   3235 C C   . VAL   A 1 595 ? -20.833 68.674  90.530  1.00 69.74  ?  576 VAL   A C   1 
ATOM   3236 O O   . VAL   A 1 595 ? -21.169 69.539  91.347  1.00 74.57  ?  576 VAL   A O   1 
ATOM   3237 C CB  . VAL   A 1 595 ? -20.792 69.071  88.038  1.00 60.99  ?  576 VAL   A CB  1 
ATOM   3238 C CG1 . VAL   A 1 595 ? -22.017 69.908  88.263  1.00 61.72  ?  576 VAL   A CG1 1 
ATOM   3239 C CG2 . VAL   A 1 595 ? -19.945 69.629  86.939  1.00 55.29  ?  576 VAL   A CG2 1 
ATOM   3240 N N   . ALA   A 1 596 ? -21.167 67.396  90.681  1.00 65.95  ?  577 ALA   A N   1 
ATOM   3241 C CA  . ALA   A 1 596 ? -21.949 66.984  91.839  1.00 71.68  ?  577 ALA   A CA  1 
ATOM   3242 C C   . ALA   A 1 596 ? -21.239 67.359  93.134  1.00 77.06  ?  577 ALA   A C   1 
ATOM   3243 O O   . ALA   A 1 596 ? -21.845 67.939  94.043  1.00 82.63  ?  577 ALA   A O   1 
ATOM   3244 C CB  . ALA   A 1 596 ? -22.225 65.480  91.784  1.00 71.77  ?  577 ALA   A CB  1 
ATOM   3245 N N   . LEU   A 1 597 ? -19.943 67.053  93.227  1.00 74.78  ?  578 LEU   A N   1 
ATOM   3246 C CA  . LEU   A 1 597 ? -19.195 67.360  94.441  1.00 68.32  ?  578 LEU   A CA  1 
ATOM   3247 C C   . LEU   A 1 597 ? -19.137 68.858  94.693  1.00 74.59  ?  578 LEU   A C   1 
ATOM   3248 O O   . LEU   A 1 597 ? -19.215 69.305  95.848  1.00 78.41  ?  578 LEU   A O   1 
ATOM   3249 C CB  . LEU   A 1 597 ? -17.788 66.792  94.341  1.00 63.78  ?  578 LEU   A CB  1 
ATOM   3250 C CG  . LEU   A 1 597 ? -17.662 65.279  94.368  1.00 60.93  ?  578 LEU   A CG  1 
ATOM   3251 C CD1 . LEU   A 1 597 ? -16.207 64.940  94.255  1.00 60.40  ?  578 LEU   A CD1 1 
ATOM   3252 C CD2 . LEU   A 1 597 ? -18.249 64.686  95.645  1.00 57.32  ?  578 LEU   A CD2 1 
ATOM   3253 N N   . ALA   A 1 598 ? -19.016 69.651  93.622  1.00 69.30  ?  579 ALA   A N   1 
ATOM   3254 C CA  . ALA   A 1 598 ? -18.872 71.093  93.756  1.00 71.91  ?  579 ALA   A CA  1 
ATOM   3255 C C   . ALA   A 1 598 ? -20.095 71.762  94.371  1.00 78.99  ?  579 ALA   A C   1 
ATOM   3256 O O   . ALA   A 1 598 ? -20.013 72.936  94.761  1.00 82.32  ?  579 ALA   A O   1 
ATOM   3257 C CB  . ALA   A 1 598 ? -18.577 71.711  92.392  1.00 68.60  ?  579 ALA   A CB  1 
ATOM   3258 N N   . GLU   A 1 599 ? -21.214 71.055  94.477  1.00 79.93  ?  580 GLU   A N   1 
ATOM   3259 C CA  . GLU   A 1 599 ? -22.437 71.669  94.972  1.00 84.61  ?  580 GLU   A CA  1 
ATOM   3260 C C   . GLU   A 1 599 ? -22.264 72.088  96.425  1.00 84.25  ?  580 GLU   A C   1 
ATOM   3261 O O   . GLU   A 1 599 ? -21.933 71.264  97.286  1.00 84.04  ?  580 GLU   A O   1 
ATOM   3262 C CB  . GLU   A 1 599 ? -23.607 70.703  94.831  1.00 90.12  ?  580 GLU   A CB  1 
ATOM   3263 C CG  . GLU   A 1 599 ? -24.937 71.278  95.288  1.00 99.47  ?  580 GLU   A CG  1 
ATOM   3264 C CD  . GLU   A 1 599 ? -25.872 70.202  95.822  1.00 110.09 ?  580 GLU   A CD  1 
ATOM   3265 O OE1 . GLU   A 1 599 ? -27.075 70.201  95.452  1.00 115.46 ?  580 GLU   A OE1 1 
ATOM   3266 O OE2 . GLU   A 1 599 ? -25.392 69.350  96.610  1.00 107.19 ?  580 GLU   A OE2 1 
ATOM   3267 N N   . GLY   A 1 600 ? -22.488 73.369  96.693  1.00 85.90  ?  581 GLY   A N   1 
ATOM   3268 C CA  . GLY   A 1 600 ? -22.471 73.863  98.049  1.00 80.97  ?  581 GLY   A CA  1 
ATOM   3269 C C   . GLY   A 1 600 ? -21.125 74.324  98.546  1.00 77.18  ?  581 GLY   A C   1 
ATOM   3270 O O   . GLY   A 1 600 ? -20.920 74.380  99.764  1.00 84.81  ?  581 GLY   A O   1 
ATOM   3271 N N   . LEU   A 1 601 ? -20.207 74.667  97.655  1.00 69.05  ?  582 LEU   A N   1 
ATOM   3272 C CA  . LEU   A 1 601 ? -18.858 75.020  98.051  1.00 64.76  ?  582 LEU   A CA  1 
ATOM   3273 C C   . LEU   A 1 601 ? -18.452 76.354  97.451  1.00 62.57  ?  582 LEU   A C   1 
ATOM   3274 O O   . LEU   A 1 601 ? -18.870 76.718  96.348  1.00 61.50  ?  582 LEU   A O   1 
ATOM   3275 C CB  . LEU   A 1 601 ? -17.833 73.964  97.626  1.00 66.91  ?  582 LEU   A CB  1 
ATOM   3276 C CG  . LEU   A 1 601 ? -17.954 72.527  98.078  1.00 69.42  ?  582 LEU   A CG  1 
ATOM   3277 C CD1 . LEU   A 1 601 ? -16.756 71.802  97.534  1.00 74.35  ?  582 LEU   A CD1 1 
ATOM   3278 C CD2 . LEU   A 1 601 ? -18.008 72.390  99.587  1.00 67.82  ?  582 LEU   A CD2 1 
ATOM   3279 N N   . ASP   A 1 602 ? -17.589 77.058  98.176  1.00 70.20  ?  583 ASP   A N   1 
ATOM   3280 C CA  . ASP   A 1 602 ? -17.121 78.377  97.751  1.00 68.73  ?  583 ASP   A CA  1 
ATOM   3281 C C   . ASP   A 1 602 ? -15.994 78.187  96.744  1.00 65.70  ?  583 ASP   A C   1 
ATOM   3282 O O   . ASP   A 1 602 ? -14.857 77.877  97.113  1.00 68.15  ?  583 ASP   A O   1 
ATOM   3283 C CB  . ASP   A 1 602 ? -16.661 79.199  98.949  1.00 58.10  ?  583 ASP   A CB  1 
ATOM   3284 C CG  . ASP   A 1 602 ? -16.510 80.657  98.616  1.00 79.01  ?  583 ASP   A CG  1 
ATOM   3285 O OD1 . ASP   A 1 602 ? -15.724 81.346  99.316  1.00 86.00  ?  583 ASP   A OD1 1 
ATOM   3286 O OD2 . ASP   A 1 602 ? -17.174 81.120  97.646  1.00 83.09  ?  583 ASP   A OD2 1 
ATOM   3287 N N   . ILE   A 1 603 ? -16.290 78.383  95.466  1.00 58.19  ?  584 ILE   A N   1 
ATOM   3288 C CA  . ILE   A 1 603 ? -15.309 78.123  94.428  1.00 62.80  ?  584 ILE   A CA  1 
ATOM   3289 C C   . ILE   A 1 603 ? -15.110 79.401  93.623  1.00 61.73  ?  584 ILE   A C   1 
ATOM   3290 O O   . ILE   A 1 603 ? -16.048 79.881  92.979  1.00 68.46  ?  584 ILE   A O   1 
ATOM   3291 C CB  . ILE   A 1 603 ? -15.737 76.946  93.536  1.00 63.45  ?  584 ILE   A CB  1 
ATOM   3292 C CG1 . ILE   A 1 603 ? -16.189 75.778  94.408  1.00 58.58  ?  584 ILE   A CG1 1 
ATOM   3293 C CG2 . ILE   A 1 603 ? -14.604 76.454  92.710  1.00 59.70  ?  584 ILE   A CG2 1 
ATOM   3294 C CD1 . ILE   A 1 603 ? -17.082 74.824  93.702  1.00 61.32  ?  584 ILE   A CD1 1 
ATOM   3295 N N   . LYS   A 1 604 ? -13.896 79.957  93.664  1.00 58.21  ?  585 LYS   A N   1 
ATOM   3296 C CA  . LYS   A 1 604 ? -13.530 81.104  92.834  1.00 61.56  ?  585 LYS   A CA  1 
ATOM   3297 C C   . LYS   A 1 604 ? -12.948 80.594  91.520  1.00 57.96  ?  585 LYS   A C   1 
ATOM   3298 O O   . LYS   A 1 604 ? -11.803 80.132  91.501  1.00 59.42  ?  585 LYS   A O   1 
ATOM   3299 C CB  . LYS   A 1 604 ? -12.500 82.000  93.535  1.00 62.31  ?  585 LYS   A CB  1 
ATOM   3300 C CG  . LYS   A 1 604 ? -12.849 82.548  94.929  1.00 62.37  ?  585 LYS   A CG  1 
ATOM   3301 C CD  . LYS   A 1 604 ? -14.222 83.217  94.987  1.00 71.97  ?  585 LYS   A CD  1 
ATOM   3302 C CE  . LYS   A 1 604 ? -14.699 83.409  96.430  1.00 77.71  ?  585 LYS   A CE  1 
ATOM   3303 N NZ  . LYS   A 1 604 ? -16.127 82.956  96.598  1.00 76.82  ?  585 LYS   A NZ  1 
ATOM   3304 N N   . LEU   A 1 605 ? -13.709 80.693  90.416  1.00 59.08  ?  586 LEU   A N   1 
ATOM   3305 C CA  . LEU   A 1 605 ? -13.160 80.291  89.113  1.00 60.17  ?  586 LEU   A CA  1 
ATOM   3306 C C   . LEU   A 1 605 ? -12.436 81.463  88.455  1.00 61.40  ?  586 LEU   A C   1 
ATOM   3307 O O   . LEU   A 1 605 ? -12.553 82.618  88.871  1.00 68.06  ?  586 LEU   A O   1 
ATOM   3308 C CB  . LEU   A 1 605 ? -14.235 79.717  88.169  1.00 50.48  ?  586 LEU   A CB  1 
ATOM   3309 C CG  . LEU   A 1 605 ? -15.232 78.694  88.778  1.00 59.95  ?  586 LEU   A CG  1 
ATOM   3310 C CD1 . LEU   A 1 605 ? -16.298 78.106  87.845  1.00 51.46  ?  586 LEU   A CD1 1 
ATOM   3311 C CD2 . LEU   A 1 605 ? -14.492 77.536  89.433  1.00 67.38  ?  586 LEU   A CD2 1 
ATOM   3312 N N   . ASN   A 1 606 ? -11.649 81.149  87.435  1.00 60.07  ?  587 ASN   A N   1 
ATOM   3313 C CA  . ASN   A 1 606 ? -10.832 82.149  86.737  1.00 67.07  ?  587 ASN   A CA  1 
ATOM   3314 C C   . ASN   A 1 606 ? -9.893  82.875  87.693  1.00 64.64  ?  587 ASN   A C   1 
ATOM   3315 O O   . ASN   A 1 606 ? -9.609  84.063  87.542  1.00 68.80  ?  587 ASN   A O   1 
ATOM   3316 C CB  . ASN   A 1 606 ? -11.715 83.133  85.986  1.00 70.25  ?  587 ASN   A CB  1 
ATOM   3317 C CG  . ASN   A 1 606 ? -12.680 82.432  85.108  1.00 70.35  ?  587 ASN   A CG  1 
ATOM   3318 O OD1 . ASN   A 1 606 ? -12.285 81.822  84.105  1.00 77.22  ?  587 ASN   A OD1 1 
ATOM   3319 N ND2 . ASN   A 1 606 ? -13.947 82.436  85.504  1.00 62.92  ?  587 ASN   A ND2 1 
ATOM   3320 N N   . THR   A 1 607 ? -9.393  82.134  88.669  1.00 62.32  ?  588 THR   A N   1 
ATOM   3321 C CA  . THR   A 1 607 ? -8.550  82.651  89.736  1.00 58.23  ?  588 THR   A CA  1 
ATOM   3322 C C   . THR   A 1 607 ? -7.270  81.822  89.696  1.00 55.64  ?  588 THR   A C   1 
ATOM   3323 O O   . THR   A 1 607 ? -7.255  80.667  90.134  1.00 52.30  ?  588 THR   A O   1 
ATOM   3324 C CB  . THR   A 1 607 ? -9.266  82.504  91.067  1.00 62.29  ?  588 THR   A CB  1 
ATOM   3325 O OG1 . THR   A 1 607 ? -10.661 82.813  90.899  1.00 53.20  ?  588 THR   A OG1 1 
ATOM   3326 C CG2 . THR   A 1 607 ? -8.621  83.392  92.129  1.00 59.86  ?  588 THR   A CG2 1 
ATOM   3327 N N   . ALA   A 1 608 ? -6.206  82.378  89.153  1.00 53.47  ?  589 ALA   A N   1 
ATOM   3328 C CA  . ALA   A 1 608 ? -4.965  81.636  88.997  1.00 48.91  ?  589 ALA   A CA  1 
ATOM   3329 C C   . ALA   A 1 608 ? -4.067  81.942  90.189  1.00 53.28  ?  589 ALA   A C   1 
ATOM   3330 O O   . ALA   A 1 608 ? -3.540  83.057  90.315  1.00 55.39  ?  589 ALA   A O   1 
ATOM   3331 C CB  . ALA   A 1 608 ? -4.284  81.993  87.680  1.00 51.21  ?  589 ALA   A CB  1 
ATOM   3332 N N   . VAL   A 1 609 ? -3.905  80.957  91.076  1.00 49.42  ?  590 VAL   A N   1 
ATOM   3333 C CA  . VAL   A 1 609 ? -2.934  81.113  92.143  1.00 49.45  ?  590 VAL   A CA  1 
ATOM   3334 C C   . VAL   A 1 609 ? -1.571  81.336  91.527  1.00 51.61  ?  590 VAL   A C   1 
ATOM   3335 O O   . VAL   A 1 609 ? -1.202  80.726  90.513  1.00 56.43  ?  590 VAL   A O   1 
ATOM   3336 C CB  . VAL   A 1 609 ? -2.932  79.912  93.101  1.00 51.90  ?  590 VAL   A CB  1 
ATOM   3337 C CG1 . VAL   A 1 609 ? -1.686  79.945  94.026  1.00 45.98  ?  590 VAL   A CG1 1 
ATOM   3338 C CG2 . VAL   A 1 609 ? -4.215  79.920  93.934  1.00 46.18  ?  590 VAL   A CG2 1 
ATOM   3339 N N   . ARG   A 1 610 ? -0.826  82.253  92.117  1.00 53.59  ?  591 ARG   A N   1 
ATOM   3340 C CA  . ARG   A 1 610 ? 0.400   82.689  91.487  1.00 55.21  ?  591 ARG   A CA  1 
ATOM   3341 C C   . ARG   A 1 610 ? 1.550   82.778  92.476  1.00 53.35  ?  591 ARG   A C   1 
ATOM   3342 O O   . ARG   A 1 610 ? 2.699   82.559  92.073  1.00 52.22  ?  591 ARG   A O   1 
ATOM   3343 C CB  . ARG   A 1 610 ? 0.127   84.038  90.795  1.00 56.59  ?  591 ARG   A CB  1 
ATOM   3344 C CG  . ARG   A 1 610 ? 1.270   84.801  90.222  1.00 63.89  ?  591 ARG   A CG  1 
ATOM   3345 C CD  . ARG   A 1 610 ? 0.711   85.627  89.036  1.00 79.20  ?  591 ARG   A CD  1 
ATOM   3346 N NE  . ARG   A 1 610 ? 0.072   84.806  88.007  1.00 82.27  ?  591 ARG   A NE  1 
ATOM   3347 C CZ  . ARG   A 1 610 ? -0.086  85.174  86.733  1.00 97.57  ?  591 ARG   A CZ  1 
ATOM   3348 N NH1 . ARG   A 1 610 ? 0.283   86.399  86.341  1.00 84.71  ?  591 ARG   A NH1 1 
ATOM   3349 N NH2 . ARG   A 1 610 ? -0.658  84.328  85.863  1.00 96.59  ?  591 ARG   A NH2 1 
ATOM   3350 N N   . GLN   A 1 611 ? 1.272   82.971  93.771  1.00 49.83  ?  592 GLN   A N   1 
ATOM   3351 C CA  . GLN   A 1 611 ? 2.253   82.836  94.836  1.00 50.99  ?  592 GLN   A CA  1 
ATOM   3352 C C   . GLN   A 1 611 ? 1.604   82.228  96.077  1.00 52.10  ?  592 GLN   A C   1 
ATOM   3353 O O   . GLN   A 1 611 ? 0.438   82.509  96.375  1.00 50.45  ?  592 GLN   A O   1 
ATOM   3354 C CB  . GLN   A 1 611 ? 2.832   84.191  95.177  1.00 60.75  ?  592 GLN   A CB  1 
ATOM   3355 C CG  . GLN   A 1 611 ? 4.137   84.146  95.885  1.00 62.71  ?  592 GLN   A CG  1 
ATOM   3356 C CD  . GLN   A 1 611 ? 4.693   85.525  96.070  1.00 57.34  ?  592 GLN   A CD  1 
ATOM   3357 O OE1 . GLN   A 1 611 ? 4.521   86.137  97.117  1.00 60.24  ?  592 GLN   A OE1 1 
ATOM   3358 N NE2 . GLN   A 1 611 ? 5.352   86.035  95.037  1.00 62.76  ?  592 GLN   A NE2 1 
ATOM   3359 N N   . VAL   A 1 612 ? 2.373   81.413  96.814  1.00 48.08  ?  593 VAL   A N   1 
ATOM   3360 C CA  . VAL   A 1 612 ? 1.918   80.808  98.077  1.00 54.99  ?  593 VAL   A CA  1 
ATOM   3361 C C   . VAL   A 1 612 ? 2.895   81.190  99.190  1.00 57.18  ?  593 VAL   A C   1 
ATOM   3362 O O   . VAL   A 1 612 ? 4.075   80.798  99.154  1.00 53.09  ?  593 VAL   A O   1 
ATOM   3363 C CB  . VAL   A 1 612 ? 1.790   79.272  97.995  1.00 51.57  ?  593 VAL   A CB  1 
ATOM   3364 C CG1 . VAL   A 1 612 ? 1.305   78.729  99.294  1.00 47.70  ?  593 VAL   A CG1 1 
ATOM   3365 C CG2 . VAL   A 1 612 ? 0.823   78.869  96.937  1.00 51.90  ?  593 VAL   A CG2 1 
ATOM   3366 N N   . ARG   A 1 613 ? 2.394   81.936  100.185 1.00 54.58  ?  594 ARG   A N   1 
ATOM   3367 C CA  . ARG   A 1 613 ? 3.177   82.400  101.325 1.00 49.38  ?  594 ARG   A CA  1 
ATOM   3368 C C   . ARG   A 1 613 ? 2.700   81.690  102.589 1.00 57.39  ?  594 ARG   A C   1 
ATOM   3369 O O   . ARG   A 1 613 ? 1.511   81.760  102.942 1.00 57.63  ?  594 ARG   A O   1 
ATOM   3370 C CB  . ARG   A 1 613 ? 3.033   83.901  101.502 1.00 58.30  ?  594 ARG   A CB  1 
ATOM   3371 C CG  . ARG   A 1 613 ? 3.589   84.730  100.382 1.00 64.63  ?  594 ARG   A CG  1 
ATOM   3372 C CD  . ARG   A 1 613 ? 3.650   86.239  100.728 1.00 58.95  ?  594 ARG   A CD  1 
ATOM   3373 N NE  . ARG   A 1 613 ? 4.803   86.795  100.042 1.00 57.52  ?  594 ARG   A NE  1 
ATOM   3374 C CZ  . ARG   A 1 613 ? 5.923   87.174  100.640 1.00 60.81  ?  594 ARG   A CZ  1 
ATOM   3375 N NH1 . ARG   A 1 613 ? 6.028   87.116  101.969 1.00 63.61  ?  594 ARG   A NH1 1 
ATOM   3376 N NH2 . ARG   A 1 613 ? 6.924   87.639  99.899  1.00 61.85  ?  594 ARG   A NH2 1 
ATOM   3377 N N   . TYR   A 1 614 ? 3.620   81.023  103.282 1.00 52.35  ?  595 TYR   A N   1 
ATOM   3378 C CA  . TYR   A 1 614 ? 3.266   80.285  104.490 1.00 59.51  ?  595 TYR   A CA  1 
ATOM   3379 C C   . TYR   A 1 614 ? 4.298   80.601  105.573 1.00 61.34  ?  595 TYR   A C   1 
ATOM   3380 O O   . TYR   A 1 614 ? 5.511   80.608  105.310 1.00 62.44  ?  595 TYR   A O   1 
ATOM   3381 C CB  . TYR   A 1 614 ? 3.159   78.760  104.212 1.00 56.35  ?  595 TYR   A CB  1 
ATOM   3382 C CG  . TYR   A 1 614 ? 4.416   78.157  103.622 1.00 51.37  ?  595 TYR   A CG  1 
ATOM   3383 C CD1 . TYR   A 1 614 ? 4.740   78.340  102.286 1.00 50.16  ?  595 TYR   A CD1 1 
ATOM   3384 C CD2 . TYR   A 1 614 ? 5.299   77.440  104.417 1.00 49.04  ?  595 TYR   A CD2 1 
ATOM   3385 C CE1 . TYR   A 1 614 ? 5.904   77.818  101.753 1.00 49.02  ?  595 TYR   A CE1 1 
ATOM   3386 C CE2 . TYR   A 1 614 ? 6.466   76.913  103.893 1.00 50.06  ?  595 TYR   A CE2 1 
ATOM   3387 C CZ  . TYR   A 1 614 ? 6.759   77.103  102.563 1.00 51.22  ?  595 TYR   A CZ  1 
ATOM   3388 O OH  . TYR   A 1 614 ? 7.924   76.590  102.048 1.00 54.68  ?  595 TYR   A OH  1 
ATOM   3389 N N   . THR   A 1 615 ? 3.820   80.903  106.778 1.00 56.85  ?  596 THR   A N   1 
ATOM   3390 C CA  . THR   A 1 615 ? 4.699   81.306  107.868 1.00 62.88  ?  596 THR   A CA  1 
ATOM   3391 C C   . THR   A 1 615 ? 4.190   80.696  109.160 1.00 60.66  ?  596 THR   A C   1 
ATOM   3392 O O   . THR   A 1 615 ? 3.114   80.087  109.203 1.00 54.55  ?  596 THR   A O   1 
ATOM   3393 C CB  . THR   A 1 615 ? 4.760   82.829  108.042 1.00 64.15  ?  596 THR   A CB  1 
ATOM   3394 O OG1 . THR   A 1 615 ? 3.469   83.309  108.461 1.00 64.32  ?  596 THR   A OG1 1 
ATOM   3395 C CG2 . THR   A 1 615 ? 5.219   83.534  106.750 1.00 57.98  ?  596 THR   A CG2 1 
ATOM   3396 N N   . ALA   A 1 616 ? 4.955   80.920  110.234 1.00 61.15  ?  597 ALA   A N   1 
ATOM   3397 C CA  . ALA   A 1 616 ? 4.619   80.328  111.522 1.00 55.31  ?  597 ALA   A CA  1 
ATOM   3398 C C   . ALA   A 1 616 ? 3.253   80.757  112.020 1.00 52.29  ?  597 ALA   A C   1 
ATOM   3399 O O   . ALA   A 1 616 ? 2.668   80.070  112.853 1.00 54.11  ?  597 ALA   A O   1 
ATOM   3400 C CB  . ALA   A 1 616 ? 5.678   80.677  112.554 1.00 55.81  ?  597 ALA   A CB  1 
ATOM   3401 N N   . SER   A 1 617 ? 2.708   81.850  111.513 1.00 63.13  ?  598 SER   A N   1 
ATOM   3402 C CA  . SER   A 1 617 ? 1.460   82.357  112.054 1.00 66.54  ?  598 SER   A CA  1 
ATOM   3403 C C   . SER   A 1 617 ? 0.294   82.228  111.093 1.00 67.23  ?  598 SER   A C   1 
ATOM   3404 O O   . SER   A 1 617 ? -0.855  82.437  111.510 1.00 65.62  ?  598 SER   A O   1 
ATOM   3405 C CB  . SER   A 1 617 ? 1.650   83.813  112.510 1.00 70.26  ?  598 SER   A CB  1 
ATOM   3406 O OG  . SER   A 1 617 ? 2.202   84.608  111.478 1.00 76.12  ?  598 SER   A OG  1 
ATOM   3407 N N   . GLY   A 1 618 ? 0.549   81.839  109.847 1.00 63.95  ?  599 GLY   A N   1 
ATOM   3408 C CA  . GLY   A 1 618 ? -0.528  81.566  108.913 1.00 61.18  ?  599 GLY   A CA  1 
ATOM   3409 C C   . GLY   A 1 618 ? -0.038  81.690  107.474 1.00 64.51  ?  599 GLY   A C   1 
ATOM   3410 O O   . GLY   A 1 618 ? 1.171   81.651  107.199 1.00 60.52  ?  599 GLY   A O   1 
ATOM   3411 N N   . CYS   A 1 619 ? -1.006  81.853  106.568 1.00 62.78  ?  600 CYS   A N   1 
ATOM   3412 C CA  . CYS   A 1 619 ? -0.734  81.736  105.145 1.00 59.97  ?  600 CYS   A CA  1 
ATOM   3413 C C   . CYS   A 1 619 ? -1.456  82.831  104.402 1.00 59.40  ?  600 CYS   A C   1 
ATOM   3414 O O   . CYS   A 1 619 ? -2.582  83.197  104.756 1.00 58.87  ?  600 CYS   A O   1 
ATOM   3415 C CB  . CYS   A 1 619 ? -1.218  80.395  104.581 1.00 58.78  ?  600 CYS   A CB  1 
ATOM   3416 S SG  . CYS   A 1 619 ? -0.348  78.992  105.252 1.00 65.06  ?  600 CYS   A SG  1 
ATOM   3417 N N   . GLU   A 1 620 ? -0.820  83.312  103.346 1.00 57.48  ?  601 GLU   A N   1 
ATOM   3418 C CA  . GLU   A 1 620 ? -1.504  84.105  102.339 1.00 63.77  ?  601 GLU   A CA  1 
ATOM   3419 C C   . GLU   A 1 620 ? -1.221  83.552  100.946 1.00 61.92  ?  601 GLU   A C   1 
ATOM   3420 O O   . GLU   A 1 620 ? -0.073  83.237  100.604 1.00 57.95  ?  601 GLU   A O   1 
ATOM   3421 C CB  . GLU   A 1 620 ? -1.181  85.618  102.506 1.00 72.06  ?  601 GLU   A CB  1 
ATOM   3422 C CG  . GLU   A 1 620 ? 0.307   86.034  102.549 1.00 74.94  ?  601 GLU   A CG  1 
ATOM   3423 C CD  . GLU   A 1 620 ? 0.520   87.558  102.797 1.00 94.72  ?  601 GLU   A CD  1 
ATOM   3424 O OE1 . GLU   A 1 620 ? -0.475  88.332  102.845 1.00 95.66  ?  601 GLU   A OE1 1 
ATOM   3425 O OE2 . GLU   A 1 620 ? 1.687   87.963  103.059 1.00 99.11  ?  601 GLU   A OE2 1 
ATOM   3426 N N   . VAL   A 1 621 ? -2.298  83.376  100.181 1.00 57.81  ?  602 VAL   A N   1 
ATOM   3427 C CA  . VAL   A 1 621 ? -2.257  82.928  98.796  1.00 58.88  ?  602 VAL   A CA  1 
ATOM   3428 C C   . VAL   A 1 621 ? -2.564  84.134  97.931  1.00 57.96  ?  602 VAL   A C   1 
ATOM   3429 O O   . VAL   A 1 621 ? -3.588  84.795  98.141  1.00 63.27  ?  602 VAL   A O   1 
ATOM   3430 C CB  . VAL   A 1 621 ? -3.281  81.804  98.536  1.00 59.09  ?  602 VAL   A CB  1 
ATOM   3431 C CG1 . VAL   A 1 621 ? -3.300  81.411  97.066  1.00 54.67  ?  602 VAL   A CG1 1 
ATOM   3432 C CG2 . VAL   A 1 621 ? -3.015  80.585  99.438  1.00 62.49  ?  602 VAL   A CG2 1 
ATOM   3433 N N   . ILE   A 1 622 ? -1.696  84.414  96.962  1.00 56.24  ?  603 ILE   A N   1 
ATOM   3434 C CA  . ILE   A 1 622 ? -1.860  85.531  96.032  1.00 57.70  ?  603 ILE   A CA  1 
ATOM   3435 C C   . ILE   A 1 622 ? -2.263  84.984  94.670  1.00 60.95  ?  603 ILE   A C   1 
ATOM   3436 O O   . ILE   A 1 622 ? -1.481  84.262  94.034  1.00 62.26  ?  603 ILE   A O   1 
ATOM   3437 C CB  . ILE   A 1 622 ? -0.565  86.335  95.898  1.00 60.73  ?  603 ILE   A CB  1 
ATOM   3438 C CG1 . ILE   A 1 622 ? -0.244  87.054  97.198  1.00 66.60  ?  603 ILE   A CG1 1 
ATOM   3439 C CG2 . ILE   A 1 622 ? -0.649  87.277  94.727  1.00 57.21  ?  603 ILE   A CG2 1 
ATOM   3440 C CD1 . ILE   A 1 622 ? 1.078   87.781  97.156  1.00 69.20  ?  603 ILE   A CD1 1 
ATOM   3441 N N   . ALA   A 1 623 ? -3.458  85.351  94.197  1.00 62.69  ?  604 ALA   A N   1 
ATOM   3442 C CA  . ALA   A 1 623 ? -3.934  84.922  92.883  1.00 63.87  ?  604 ALA   A CA  1 
ATOM   3443 C C   . ALA   A 1 623 ? -4.369  86.125  92.044  1.00 69.51  ?  604 ALA   A C   1 
ATOM   3444 O O   . ALA   A 1 623 ? -4.570  87.228  92.565  1.00 69.60  ?  604 ALA   A O   1 
ATOM   3445 C CB  . ALA   A 1 623 ? -5.093  83.931  93.010  1.00 58.78  ?  604 ALA   A CB  1 
ATOM   3446 N N   . VAL   A 1 624 ? -4.518  85.902  90.728  1.00 68.63  ?  605 VAL   A N   1 
ATOM   3447 C CA  . VAL   A 1 624 ? -4.988  86.926  89.797  1.00 66.68  ?  605 VAL   A CA  1 
ATOM   3448 C C   . VAL   A 1 624 ? -6.154  86.385  88.982  1.00 65.91  ?  605 VAL   A C   1 
ATOM   3449 O O   . VAL   A 1 624 ? -6.388  85.177  88.912  1.00 67.17  ?  605 VAL   A O   1 
ATOM   3450 C CB  . VAL   A 1 624 ? -3.884  87.416  88.844  1.00 70.23  ?  605 VAL   A CB  1 
ATOM   3451 C CG1 . VAL   A 1 624 ? -2.631  87.766  89.627  1.00 68.46  ?  605 VAL   A CG1 1 
ATOM   3452 C CG2 . VAL   A 1 624 ? -3.611  86.381  87.757  1.00 65.87  ?  605 VAL   A CG2 1 
ATOM   3453 N N   . ASN   A 1 625 ? -6.893  87.307  88.369  1.00 70.01  ?  606 ASN   A N   1 
ATOM   3454 C CA  . ASN   A 1 625 ? -7.972  86.951  87.452  1.00 79.83  ?  606 ASN   A CA  1 
ATOM   3455 C C   . ASN   A 1 625 ? -7.413  86.532  86.082  1.00 76.88  ?  606 ASN   A C   1 
ATOM   3456 O O   . ASN   A 1 625 ? -6.592  87.239  85.483  1.00 75.25  ?  606 ASN   A O   1 
ATOM   3457 C CB  . ASN   A 1 625 ? -8.938  88.134  87.315  1.00 83.21  ?  606 ASN   A CB  1 
ATOM   3458 C CG  . ASN   A 1 625 ? -10.238 87.761  86.615  1.00 82.26  ?  606 ASN   A CG  1 
ATOM   3459 O OD1 . ASN   A 1 625 ? -11.006 86.927  87.099  1.00 80.92  ?  606 ASN   A OD1 1 
ATOM   3460 N ND2 . ASN   A 1 625 ? -10.490 88.388  85.475  1.00 81.54  ?  606 ASN   A ND2 1 
ATOM   3461 N N   . THR   A 1 626 ? -7.852  85.372  85.586  1.00 73.26  ?  607 THR   A N   1 
ATOM   3462 C CA  . THR   A 1 626 ? -7.306  84.868  84.326  1.00 75.08  ?  607 THR   A CA  1 
ATOM   3463 C C   . THR   A 1 626 ? -7.700  85.736  83.145  1.00 82.36  ?  607 THR   A C   1 
ATOM   3464 O O   . THR   A 1 626 ? -6.987  85.755  82.138  1.00 86.08  ?  607 THR   A O   1 
ATOM   3465 C CB  . THR   A 1 626 ? -7.769  83.440  84.073  1.00 75.11  ?  607 THR   A CB  1 
ATOM   3466 O OG1 . THR   A 1 626 ? -9.204  83.392  84.100  1.00 78.70  ?  607 THR   A OG1 1 
ATOM   3467 C CG2 . THR   A 1 626 ? -7.211  82.503  85.146  1.00 67.48  ?  607 THR   A CG2 1 
ATOM   3468 N N   . ARG   A 1 627 ? -8.802  86.474  83.259  1.00 85.68  ?  608 ARG   A N   1 
ATOM   3469 C CA  . ARG   A 1 627 ? -9.270  87.304  82.158  1.00 83.96  ?  608 ARG   A CA  1 
ATOM   3470 C C   . ARG   A 1 627 ? -8.480  88.617  82.069  1.00 93.33  ?  608 ARG   A C   1 
ATOM   3471 O O   . ARG   A 1 627 ? -7.833  88.891  81.048  1.00 100.13 ?  608 ARG   A O   1 
ATOM   3472 C CB  . ARG   A 1 627 ? -10.778 87.511  82.313  1.00 78.97  ?  608 ARG   A CB  1 
ATOM   3473 C CG  . ARG   A 1 627 ? -11.510 86.154  82.330  1.00 79.06  ?  608 ARG   A CG  1 
ATOM   3474 C CD  . ARG   A 1 627 ? -12.898 86.218  82.947  1.00 76.56  ?  608 ARG   A CD  1 
ATOM   3475 N NE  . ARG   A 1 627 ? -12.860 86.147  84.406  1.00 85.09  ?  608 ARG   A NE  1 
ATOM   3476 C CZ  . ARG   A 1 627 ? -13.934 85.987  85.183  1.00 90.87  ?  608 ARG   A CZ  1 
ATOM   3477 N NH1 . ARG   A 1 627 ? -15.139 85.878  84.636  1.00 93.90  ?  608 ARG   A NH1 1 
ATOM   3478 N NH2 . ARG   A 1 627 ? -13.805 85.936  86.510  1.00 86.45  ?  608 ARG   A NH2 1 
ATOM   3479 N N   . SER   A 1 628 ? -8.479  89.429  83.137  1.00 86.67  ?  609 SER   A N   1 
ATOM   3480 C CA  . SER   A 1 628 ? -7.576  90.584  83.230  1.00 89.83  ?  609 SER   A CA  1 
ATOM   3481 C C   . SER   A 1 628 ? -6.558  90.295  84.330  1.00 88.67  ?  609 SER   A C   1 
ATOM   3482 O O   . SER   A 1 628 ? -6.874  90.393  85.523  1.00 84.95  ?  609 SER   A O   1 
ATOM   3483 C CB  . SER   A 1 628 ? -8.336  91.886  83.495  1.00 95.28  ?  609 SER   A CB  1 
ATOM   3484 O OG  . SER   A 1 628 ? -9.228  91.763  84.593  1.00 94.23  ?  609 SER   A OG  1 
ATOM   3485 N N   . THR   A 1 629 ? -5.326  89.951  83.925  1.00 88.52  ?  610 THR   A N   1 
ATOM   3486 C CA  . THR   A 1 629 ? -4.331  89.493  84.895  1.00 87.08  ?  610 THR   A CA  1 
ATOM   3487 C C   . THR   A 1 629 ? -3.842  90.596  85.830  1.00 89.23  ?  610 THR   A C   1 
ATOM   3488 O O   . THR   A 1 629 ? -3.100  90.297  86.772  1.00 88.84  ?  610 THR   A O   1 
ATOM   3489 C CB  . THR   A 1 629 ? -3.114  88.872  84.199  1.00 82.41  ?  610 THR   A CB  1 
ATOM   3490 O OG1 . THR   A 1 629 ? -2.264  89.908  83.685  1.00 89.41  ?  610 THR   A OG1 1 
ATOM   3491 C CG2 . THR   A 1 629 ? -3.550  87.969  83.083  1.00 86.04  ?  610 THR   A CG2 1 
ATOM   3492 N N   . SER   A 1 630 ? -4.227  91.853  85.606  1.00 90.16  ?  611 SER   A N   1 
ATOM   3493 C CA  . SER   A 1 630 ? -3.788  92.912  86.504  1.00 77.34  ?  611 SER   A CA  1 
ATOM   3494 C C   . SER   A 1 630 ? -4.513  92.833  87.839  1.00 80.58  ?  611 SER   A C   1 
ATOM   3495 O O   . SER   A 1 630 ? -3.890  92.960  88.897  1.00 82.67  ?  611 SER   A O   1 
ATOM   3496 C CB  . SER   A 1 630 ? -4.025  94.248  85.843  1.00 79.12  ?  611 SER   A CB  1 
ATOM   3497 O OG  . SER   A 1 630 ? -3.417  94.230  84.570  1.00 100.63 ?  611 SER   A OG  1 
ATOM   3498 N N   . GLN   A 1 631 ? -5.824  92.605  87.802  1.00 78.50  ?  612 GLN   A N   1 
ATOM   3499 C CA  . GLN   A 1 631 ? -6.648  92.502  89.000  1.00 67.73  ?  612 GLN   A CA  1 
ATOM   3500 C C   . GLN   A 1 631 ? -6.182  91.360  89.912  1.00 74.02  ?  612 GLN   A C   1 
ATOM   3501 O O   . GLN   A 1 631 ? -6.120  90.202  89.494  1.00 81.25  ?  612 GLN   A O   1 
ATOM   3502 C CB  . GLN   A 1 631 ? -8.085  92.299  88.559  1.00 71.69  ?  612 GLN   A CB  1 
ATOM   3503 C CG  . GLN   A 1 631 ? -9.048  91.965  89.648  1.00 82.51  ?  612 GLN   A CG  1 
ATOM   3504 C CD  . GLN   A 1 631 ? -10.451 91.917  89.095  1.00 98.60  ?  612 GLN   A CD  1 
ATOM   3505 O OE1 . GLN   A 1 631 ? -10.640 91.949  87.872  1.00 95.61  ?  612 GLN   A OE1 1 
ATOM   3506 N NE2 . GLN   A 1 631 ? -11.446 91.837  89.980  1.00 103.39 ?  612 GLN   A NE2 1 
ATOM   3507 N N   . THR   A 1 632 ? -5.886  91.680  91.169  1.00 69.49  ?  613 THR   A N   1 
ATOM   3508 C CA  . THR   A 1 632 ? -5.065  90.846  92.037  1.00 63.17  ?  613 THR   A CA  1 
ATOM   3509 C C   . THR   A 1 632 ? -5.815  90.517  93.325  1.00 62.18  ?  613 THR   A C   1 
ATOM   3510 O O   . THR   A 1 632 ? -6.565  91.347  93.846  1.00 70.14  ?  613 THR   A O   1 
ATOM   3511 C CB  . THR   A 1 632 ? -3.738  91.568  92.342  1.00 60.07  ?  613 THR   A CB  1 
ATOM   3512 O OG1 . THR   A 1 632 ? -2.853  91.484  91.205  1.00 60.94  ?  613 THR   A OG1 1 
ATOM   3513 C CG2 . THR   A 1 632 ? -3.071  90.977  93.536  1.00 58.02  ?  613 THR   A CG2 1 
ATOM   3514 N N   . PHE   A 1 633 ? -5.628  89.303  93.843  1.00 63.13  ?  614 PHE   A N   1 
ATOM   3515 C CA  . PHE   A 1 633 ? -6.370  88.864  95.019  1.00 63.93  ?  614 PHE   A CA  1 
ATOM   3516 C C   . PHE   A 1 633 ? -5.454  88.344  96.124  1.00 63.28  ?  614 PHE   A C   1 
ATOM   3517 O O   . PHE   A 1 633 ? -4.403  87.738  95.883  1.00 64.87  ?  614 PHE   A O   1 
ATOM   3518 C CB  . PHE   A 1 633 ? -7.389  87.792  94.668  1.00 63.88  ?  614 PHE   A CB  1 
ATOM   3519 C CG  . PHE   A 1 633 ? -8.495  88.279  93.794  1.00 69.79  ?  614 PHE   A CG  1 
ATOM   3520 C CD1 . PHE   A 1 633 ? -9.703  88.693  94.343  1.00 67.73  ?  614 PHE   A CD1 1 
ATOM   3521 C CD2 . PHE   A 1 633 ? -8.334  88.325  92.414  1.00 74.82  ?  614 PHE   A CD2 1 
ATOM   3522 C CE1 . PHE   A 1 633 ? -10.736 89.132  93.523  1.00 74.00  ?  614 PHE   A CE1 1 
ATOM   3523 C CE2 . PHE   A 1 633 ? -9.354  88.771  91.591  1.00 74.48  ?  614 PHE   A CE2 1 
ATOM   3524 C CZ  . PHE   A 1 633 ? -10.556 89.169  92.144  1.00 74.01  ?  614 PHE   A CZ  1 
ATOM   3525 N N   . ILE   A 1 634 ? -5.891  88.582  97.349  1.00 56.63  ?  615 ILE   A N   1 
ATOM   3526 C CA  . ILE   A 1 634 ? -5.210  88.135  98.551  1.00 61.55  ?  615 ILE   A CA  1 
ATOM   3527 C C   . ILE   A 1 634 ? -6.167  87.291  99.366  1.00 64.38  ?  615 ILE   A C   1 
ATOM   3528 O O   . ILE   A 1 634 ? -7.268  87.748  99.710  1.00 69.68  ?  615 ILE   A O   1 
ATOM   3529 C CB  . ILE   A 1 634 ? -4.713  89.318  99.393  1.00 66.73  ?  615 ILE   A CB  1 
ATOM   3530 C CG1 . ILE   A 1 634 ? -3.523  90.041  98.759  1.00 57.43  ?  615 ILE   A CG1 1 
ATOM   3531 C CG2 . ILE   A 1 634 ? -4.458  88.842  100.801 1.00 71.63  ?  615 ILE   A CG2 1 
ATOM   3532 C CD1 . ILE   A 1 634 ? -2.303  89.224  98.791  1.00 65.06  ?  615 ILE   A CD1 1 
ATOM   3533 N N   . TYR   A 1 635 ? -5.744  86.072  99.685  1.00 60.79  ?  616 TYR   A N   1 
ATOM   3534 C CA  . TYR   A 1 635 ? -6.487  85.198  100.576 1.00 62.41  ?  616 TYR   A CA  1 
ATOM   3535 C C   . TYR   A 1 635 ? -5.584  84.826  101.738 1.00 64.22  ?  616 TYR   A C   1 
ATOM   3536 O O   . TYR   A 1 635 ? -4.403  84.516  101.543 1.00 65.45  ?  616 TYR   A O   1 
ATOM   3537 C CB  . TYR   A 1 635 ? -6.982  83.951  99.851  1.00 58.21  ?  616 TYR   A CB  1 
ATOM   3538 C CG  . TYR   A 1 635 ? -7.926  84.282  98.712  1.00 62.05  ?  616 TYR   A CG  1 
ATOM   3539 C CD1 . TYR   A 1 635 ? -7.434  84.604  97.435  1.00 54.77  ?  616 TYR   A CD1 1 
ATOM   3540 C CD2 . TYR   A 1 635 ? -9.308  84.298  98.910  1.00 56.44  ?  616 TYR   A CD2 1 
ATOM   3541 C CE1 . TYR   A 1 635 ? -8.292  84.911  96.397  1.00 49.51  ?  616 TYR   A CE1 1 
ATOM   3542 C CE2 . TYR   A 1 635 ? -10.174 84.607  97.875  1.00 49.49  ?  616 TYR   A CE2 1 
ATOM   3543 C CZ  . TYR   A 1 635 ? -9.663  84.916  96.628  1.00 54.57  ?  616 TYR   A CZ  1 
ATOM   3544 O OH  . TYR   A 1 635 ? -10.550 85.228  95.616  1.00 72.70  ?  616 TYR   A OH  1 
ATOM   3545 N N   . LYS   A 1 636 ? -6.131  84.873  102.938 1.00 62.92  ?  617 LYS   A N   1 
ATOM   3546 C CA  . LYS   A 1 636 ? -5.364  84.584  104.130 1.00 64.56  ?  617 LYS   A CA  1 
ATOM   3547 C C   . LYS   A 1 636 ? -6.018  83.414  104.851 1.00 56.44  ?  617 LYS   A C   1 
ATOM   3548 O O   . LYS   A 1 636 ? -7.245  83.257  104.830 1.00 62.88  ?  617 LYS   A O   1 
ATOM   3549 C CB  . LYS   A 1 636 ? -5.254  85.872  104.984 1.00 70.95  ?  617 LYS   A CB  1 
ATOM   3550 C CG  . LYS   A 1 636 ? -4.329  86.879  104.280 1.00 67.46  ?  617 LYS   A CG  1 
ATOM   3551 C CD  . LYS   A 1 636 ? -4.188  88.214  104.982 1.00 84.63  ?  617 LYS   A CD  1 
ATOM   3552 C CE  . LYS   A 1 636 ? -3.257  89.132  104.151 1.00 78.25  ?  617 LYS   A CE  1 
ATOM   3553 N NZ  . LYS   A 1 636 ? -3.089  90.479  104.778 1.00 82.88  ?  617 LYS   A NZ  1 
ATOM   3554 N N   . CYS   A 1 637 ? -5.197  82.537  105.417 1.00 51.53  ?  618 CYS   A N   1 
ATOM   3555 C CA  . CYS   A 1 637 ? -5.764  81.298  105.935 1.00 58.51  ?  618 CYS   A CA  1 
ATOM   3556 C C   . CYS   A 1 637 ? -4.795  80.656  106.909 1.00 59.31  ?  618 CYS   A C   1 
ATOM   3557 O O   . CYS   A 1 637 ? -3.596  80.979  106.940 1.00 52.53  ?  618 CYS   A O   1 
ATOM   3558 C CB  . CYS   A 1 637 ? -6.087  80.321  104.805 1.00 60.23  ?  618 CYS   A CB  1 
ATOM   3559 S SG  . CYS   A 1 637 ? -4.623  80.093  103.698 1.00 63.63  ?  618 CYS   A SG  1 
ATOM   3560 N N   . ASP   A 1 638 ? -5.349  79.736  107.707 1.00 60.60  ?  619 ASP   A N   1 
ATOM   3561 C CA  . ASP   A 1 638 ? -4.531  78.941  108.616 1.00 63.18  ?  619 ASP   A CA  1 
ATOM   3562 C C   . ASP   A 1 638 ? -3.703  77.890  107.890 1.00 61.89  ?  619 ASP   A C   1 
ATOM   3563 O O   . ASP   A 1 638 ? -2.649  77.495  108.401 1.00 57.60  ?  619 ASP   A O   1 
ATOM   3564 C CB  . ASP   A 1 638 ? -5.400  78.246  109.656 1.00 63.73  ?  619 ASP   A CB  1 
ATOM   3565 C CG  . ASP   A 1 638 ? -6.243  79.217  110.454 1.00 71.69  ?  619 ASP   A CG  1 
ATOM   3566 O OD1 . ASP   A 1 638 ? -7.496  79.184  110.272 1.00 63.54  ?  619 ASP   A OD1 1 
ATOM   3567 O OD2 . ASP   A 1 638 ? -5.641  79.993  111.255 1.00 73.51  ?  619 ASP   A OD2 1 
ATOM   3568 N N   . ALA   A 1 639 ? -4.159  77.430  106.717 1.00 65.69  ?  620 ALA   A N   1 
ATOM   3569 C CA  . ALA   A 1 639 ? -3.537  76.312  106.012 1.00 62.78  ?  620 ALA   A CA  1 
ATOM   3570 C C   . ALA   A 1 639 ? -3.907  76.349  104.535 1.00 60.56  ?  620 ALA   A C   1 
ATOM   3571 O O   . ALA   A 1 639 ? -5.049  76.670  104.179 1.00 60.66  ?  620 ALA   A O   1 
ATOM   3572 C CB  . ALA   A 1 639 ? -3.960  74.963  106.607 1.00 56.39  ?  620 ALA   A CB  1 
ATOM   3573 N N   . VAL   A 1 640 ? -2.942  75.992  103.688 1.00 56.73  ?  621 VAL   A N   1 
ATOM   3574 C CA  . VAL   A 1 640 ? -3.164  75.811  102.254 1.00 62.82  ?  621 VAL   A CA  1 
ATOM   3575 C C   . VAL   A 1 640 ? -3.089  74.325  101.891 1.00 61.73  ?  621 VAL   A C   1 
ATOM   3576 O O   . VAL   A 1 640 ? -2.150  73.615  102.296 1.00 54.11  ?  621 VAL   A O   1 
ATOM   3577 C CB  . VAL   A 1 640 ? -2.141  76.596  101.429 1.00 56.79  ?  621 VAL   A CB  1 
ATOM   3578 C CG1 . VAL   A 1 640 ? -2.577  76.625  99.983  1.00 54.82  ?  621 VAL   A CG1 1 
ATOM   3579 C CG2 . VAL   A 1 640 ? -1.971  77.966  102.007 1.00 57.78  ?  621 VAL   A CG2 1 
ATOM   3580 N N   . LEU   A 1 641 ? -4.060  73.863  101.102 1.00 55.53  ?  622 LEU   A N   1 
ATOM   3581 C CA  . LEU   A 1 641 ? -4.047  72.515  100.546 1.00 53.03  ?  622 LEU   A CA  1 
ATOM   3582 C C   . LEU   A 1 641 ? -3.782  72.641  99.053  1.00 52.01  ?  622 LEU   A C   1 
ATOM   3583 O O   . LEU   A 1 641 ? -4.660  73.068  98.294  1.00 55.25  ?  622 LEU   A O   1 
ATOM   3584 C CB  . LEU   A 1 641 ? -5.359  71.785  100.814 1.00 53.90  ?  622 LEU   A CB  1 
ATOM   3585 C CG  . LEU   A 1 641 ? -5.360  70.425  100.134 1.00 53.54  ?  622 LEU   A CG  1 
ATOM   3586 C CD1 . LEU   A 1 641 ? -4.238  69.569  100.697 1.00 48.42  ?  622 LEU   A CD1 1 
ATOM   3587 C CD2 . LEU   A 1 641 ? -6.697  69.765  100.332 1.00 53.79  ?  622 LEU   A CD2 1 
ATOM   3588 N N   . CYS   A 1 642 ? -2.568  72.298  98.642  1.00 49.51  ?  623 CYS   A N   1 
ATOM   3589 C CA  . CYS   A 1 642 ? -2.151  72.367  97.248  1.00 48.74  ?  623 CYS   A CA  1 
ATOM   3590 C C   . CYS   A 1 642 ? -2.566  71.091  96.516  1.00 52.85  ?  623 CYS   A C   1 
ATOM   3591 O O   . CYS   A 1 642 ? -2.178  69.991  96.926  1.00 56.26  ?  623 CYS   A O   1 
ATOM   3592 C CB  . CYS   A 1 642 ? -0.638  72.535  97.192  1.00 47.86  ?  623 CYS   A CB  1 
ATOM   3593 S SG  . CYS   A 1 642 ? 0.033   72.614  95.520  1.00 56.81  ?  623 CYS   A SG  1 
ATOM   3594 N N   . THR   A 1 643 ? -3.364  71.218  95.445  1.00 49.88  ?  624 THR   A N   1 
ATOM   3595 C CA  . THR   A 1 643 ? -3.594  70.080  94.555  1.00 52.25  ?  624 THR   A CA  1 
ATOM   3596 C C   . THR   A 1 643 ? -3.188  70.440  93.130  1.00 51.19  ?  624 THR   A C   1 
ATOM   3597 O O   . THR   A 1 643 ? -3.791  69.989  92.162  1.00 52.74  ?  624 THR   A O   1 
ATOM   3598 C CB  . THR   A 1 643 ? -5.043  69.565  94.608  1.00 50.33  ?  624 THR   A CB  1 
ATOM   3599 O OG1 . THR   A 1 643 ? -5.917  70.305  93.742  1.00 49.85  ?  624 THR   A OG1 1 
ATOM   3600 C CG2 . THR   A 1 643 ? -5.563  69.695  96.008  1.00 49.51  ?  624 THR   A CG2 1 
ATOM   3601 N N   . LEU   A 1 644 ? -2.178  71.276  93.004  1.00 53.86  ?  625 LEU   A N   1 
ATOM   3602 C CA  . LEU   A 1 644 ? -1.632  71.586  91.700  1.00 48.42  ?  625 LEU   A CA  1 
ATOM   3603 C C   . LEU   A 1 644 ? -1.140  70.303  91.049  1.00 50.78  ?  625 LEU   A C   1 
ATOM   3604 O O   . LEU   A 1 644 ? -0.467  69.500  91.703  1.00 50.21  ?  625 LEU   A O   1 
ATOM   3605 C CB  . LEU   A 1 644 ? -0.481  72.585  91.828  1.00 48.93  ?  625 LEU   A CB  1 
ATOM   3606 C CG  . LEU   A 1 644 ? -0.912  74.006  92.206  1.00 53.33  ?  625 LEU   A CG  1 
ATOM   3607 C CD1 . LEU   A 1 644 ? 0.297   74.867  92.515  1.00 48.79  ?  625 LEU   A CD1 1 
ATOM   3608 C CD2 . LEU   A 1 644 ? -1.770  74.635  91.074  1.00 46.92  ?  625 LEU   A CD2 1 
ATOM   3609 N N   . PRO   A 1 645 ? -1.462  70.066  89.788  1.00 56.85  ?  626 PRO   A N   1 
ATOM   3610 C CA  . PRO   A 1 645 ? -0.925  68.900  89.097  1.00 49.81  ?  626 PRO   A CA  1 
ATOM   3611 C C   . PRO   A 1 645 ? 0.594   68.898  89.092  1.00 53.42  ?  626 PRO   A C   1 
ATOM   3612 O O   . PRO   A 1 645 ? 1.238   69.952  89.002  1.00 51.33  ?  626 PRO   A O   1 
ATOM   3613 C CB  . PRO   A 1 645 ? -1.478  69.063  87.686  1.00 48.11  ?  626 PRO   A CB  1 
ATOM   3614 C CG  . PRO   A 1 645 ? -2.720  69.821  87.878  1.00 49.45  ?  626 PRO   A CG  1 
ATOM   3615 C CD  . PRO   A 1 645 ? -2.398  70.818  88.935  1.00 52.27  ?  626 PRO   A CD  1 
ATOM   3616 N N   . LEU   A 1 646 ? 1.157   67.679  89.169  1.00 54.44  ?  627 LEU   A N   1 
ATOM   3617 C CA  . LEU   A 1 646 ? 2.609   67.513  89.204  1.00 49.33  ?  627 LEU   A CA  1 
ATOM   3618 C C   . LEU   A 1 646 ? 3.271   68.240  88.047  1.00 55.44  ?  627 LEU   A C   1 
ATOM   3619 O O   . LEU   A 1 646 ? 4.361   68.811  88.199  1.00 56.15  ?  627 LEU   A O   1 
ATOM   3620 C CB  . LEU   A 1 646 ? 2.976   66.038  89.163  1.00 48.91  ?  627 LEU   A CB  1 
ATOM   3621 C CG  . LEU   A 1 646 ? 4.452   65.686  88.926  1.00 49.82  ?  627 LEU   A CG  1 
ATOM   3622 C CD1 . LEU   A 1 646 ? 5.395   66.205  89.989  1.00 46.70  ?  627 LEU   A CD1 1 
ATOM   3623 C CD2 . LEU   A 1 646 ? 4.598   64.183  88.835  1.00 54.98  ?  627 LEU   A CD2 1 
ATOM   3624 N N   . GLY   A 1 647 ? 2.611   68.253  86.886  1.00 54.91  ?  628 GLY   A N   1 
ATOM   3625 C CA  . GLY   A 1 647 ? 3.151   68.982  85.749  1.00 51.87  ?  628 GLY   A CA  1 
ATOM   3626 C C   . GLY   A 1 647 ? 3.278   70.466  86.012  1.00 53.00  ?  628 GLY   A C   1 
ATOM   3627 O O   . GLY   A 1 647 ? 4.238   71.102  85.572  1.00 56.26  ?  628 GLY   A O   1 
ATOM   3628 N N   . VAL   A 1 648 ? 2.312   71.039  86.732  1.00 58.05  ?  629 VAL   A N   1 
ATOM   3629 C CA  . VAL   A 1 648 ? 2.400   72.449  87.096  1.00 54.43  ?  629 VAL   A CA  1 
ATOM   3630 C C   . VAL   A 1 648 ? 3.553   72.670  88.066  1.00 53.43  ?  629 VAL   A C   1 
ATOM   3631 O O   . VAL   A 1 648 ? 4.369   73.579  87.878  1.00 54.34  ?  629 VAL   A O   1 
ATOM   3632 C CB  . VAL   A 1 648 ? 1.068   72.934  87.683  1.00 45.21  ?  629 VAL   A CB  1 
ATOM   3633 C CG1 . VAL   A 1 648 ? 1.278   74.228  88.447  1.00 41.41  ?  629 VAL   A CG1 1 
ATOM   3634 C CG2 . VAL   A 1 648 ? 0.036   73.069  86.571  1.00 42.57  ?  629 VAL   A CG2 1 
ATOM   3635 N N   . LEU   A 1 649 ? 3.651   71.822  89.104  1.00 49.08  ?  630 LEU   A N   1 
ATOM   3636 C CA  . LEU   A 1 649 ? 4.755   71.937  90.055  1.00 46.32  ?  630 LEU   A CA  1 
ATOM   3637 C C   . LEU   A 1 649 ? 6.099   71.766  89.376  1.00 52.75  ?  630 LEU   A C   1 
ATOM   3638 O O   . LEU   A 1 649 ? 7.118   72.208  89.916  1.00 52.86  ?  630 LEU   A O   1 
ATOM   3639 C CB  . LEU   A 1 649 ? 4.633   70.897  91.167  1.00 51.94  ?  630 LEU   A CB  1 
ATOM   3640 C CG  . LEU   A 1 649 ? 3.344   70.839  91.998  1.00 54.22  ?  630 LEU   A CG  1 
ATOM   3641 C CD1 . LEU   A 1 649 ? 3.311   69.580  92.900  1.00 43.58  ?  630 LEU   A CD1 1 
ATOM   3642 C CD2 . LEU   A 1 649 ? 3.192   72.112  92.810  1.00 42.57  ?  630 LEU   A CD2 1 
ATOM   3643 N N   . LYS   A 1 650 ? 6.127   71.116  88.209  1.00 56.11  ?  631 LYS   A N   1 
ATOM   3644 C CA  . LYS   A 1 650 ? 7.384   70.833  87.540  1.00 51.06  ?  631 LYS   A CA  1 
ATOM   3645 C C   . LYS   A 1 650 ? 7.847   72.001  86.692  1.00 55.58  ?  631 LYS   A C   1 
ATOM   3646 O O   . LYS   A 1 650 ? 9.030   72.061  86.330  1.00 56.89  ?  631 LYS   A O   1 
ATOM   3647 C CB  . LYS   A 1 650 ? 7.230   69.602  86.659  1.00 51.27  ?  631 LYS   A CB  1 
ATOM   3648 C CG  . LYS   A 1 650 ? 7.514   68.260  87.297  1.00 52.40  ?  631 LYS   A CG  1 
ATOM   3649 C CD  . LYS   A 1 650 ? 7.401   67.163  86.223  1.00 43.97  ?  631 LYS   A CD  1 
ATOM   3650 C CE  . LYS   A 1 650 ? 7.796   65.801  86.747  1.00 48.43  ?  631 LYS   A CE  1 
ATOM   3651 N NZ  . LYS   A 1 650 ? 9.251   65.684  87.076  1.00 50.80  ?  631 LYS   A NZ  1 
ATOM   3652 N N   . GLN   A 1 651 ? 6.933   72.924  86.392  1.00 56.23  ?  632 GLN   A N   1 
ATOM   3653 C CA  . GLN   A 1 651 ? 7.157   73.993  85.426  1.00 54.74  ?  632 GLN   A CA  1 
ATOM   3654 C C   . GLN   A 1 651 ? 8.355   74.862  85.811  1.00 63.88  ?  632 GLN   A C   1 
ATOM   3655 O O   . GLN   A 1 651 ? 8.475   75.309  86.957  1.00 66.15  ?  632 GLN   A O   1 
ATOM   3656 C CB  . GLN   A 1 651 ? 5.864   74.807  85.331  1.00 52.10  ?  632 GLN   A CB  1 
ATOM   3657 C CG  . GLN   A 1 651 ? 5.751   75.796  84.201  1.00 66.47  ?  632 GLN   A CG  1 
ATOM   3658 C CD  . GLN   A 1 651 ? 4.329   76.383  84.055  1.00 72.55  ?  632 GLN   A CD  1 
ATOM   3659 O OE1 . GLN   A 1 651 ? 4.114   77.336  83.311  1.00 78.65  ?  632 GLN   A OE1 1 
ATOM   3660 N NE2 . GLN   A 1 651 ? 3.357   75.786  84.737  1.00 70.21  ?  632 GLN   A NE2 1 
ATOM   3661 N N   . GLN   A 1 652 ? 9.266   75.064  84.857  1.00 72.85  ?  633 GLN   A N   1 
ATOM   3662 C CA  . GLN   A 1 652 ? 10.384  76.006  85.006  1.00 75.21  ?  633 GLN   A CA  1 
ATOM   3663 C C   . GLN   A 1 652 ? 10.394  76.944  83.802  1.00 86.51  ?  633 GLN   A C   1 
ATOM   3664 O O   . GLN   A 1 652 ? 10.502  76.472  82.642  1.00 88.14  ?  633 GLN   A O   1 
ATOM   3665 C CB  . GLN   A 1 652 ? 11.727  75.288  85.143  1.00 69.46  ?  633 GLN   A CB  1 
ATOM   3666 C CG  . GLN   A 1 652 ? 11.910  74.575  86.455  1.00 70.16  ?  633 GLN   A CG  1 
ATOM   3667 C CD  . GLN   A 1 652 ? 11.635  75.465  87.645  1.00 80.48  ?  633 GLN   A CD  1 
ATOM   3668 O OE1 . GLN   A 1 652 ? 12.092  76.613  87.701  1.00 83.19  ?  633 GLN   A OE1 1 
ATOM   3669 N NE2 . GLN   A 1 652 ? 10.885  74.938  88.617  1.00 80.96  ?  633 GLN   A NE2 1 
ATOM   3670 N N   . PRO   A 1 653 ? 10.292  78.270  84.005  1.00 84.06  ?  634 PRO   A N   1 
ATOM   3671 C CA  . PRO   A 1 653 ? 10.274  78.915  85.320  1.00 75.89  ?  634 PRO   A CA  1 
ATOM   3672 C C   . PRO   A 1 653 ? 8.915   78.730  85.988  1.00 74.93  ?  634 PRO   A C   1 
ATOM   3673 O O   . PRO   A 1 653 ? 7.927   78.479  85.274  1.00 76.04  ?  634 PRO   A O   1 
ATOM   3674 C CB  . PRO   A 1 653 ? 10.539  80.391  84.992  1.00 70.47  ?  634 PRO   A CB  1 
ATOM   3675 C CG  . PRO   A 1 653 ? 10.745  80.445  83.477  1.00 78.24  ?  634 PRO   A CG  1 
ATOM   3676 C CD  . PRO   A 1 653 ? 10.040  79.254  82.943  1.00 81.30  ?  634 PRO   A CD  1 
ATOM   3677 N N   . PRO   A 1 654 ? 8.880   78.840  87.313  1.00 61.98  ?  635 PRO   A N   1 
ATOM   3678 C CA  . PRO   A 1 654 ? 7.675   78.476  88.070  1.00 61.14  ?  635 PRO   A CA  1 
ATOM   3679 C C   . PRO   A 1 654 ? 6.439   79.239  87.634  1.00 56.49  ?  635 PRO   A C   1 
ATOM   3680 O O   . PRO   A 1 654 ? 6.490   80.441  87.410  1.00 66.38  ?  635 PRO   A O   1 
ATOM   3681 C CB  . PRO   A 1 654 ? 8.057   78.827  89.506  1.00 59.35  ?  635 PRO   A CB  1 
ATOM   3682 C CG  . PRO   A 1 654 ? 9.528   78.579  89.527  1.00 68.54  ?  635 PRO   A CG  1 
ATOM   3683 C CD  . PRO   A 1 654 ? 10.051  78.994  88.183  1.00 60.34  ?  635 PRO   A CD  1 
ATOM   3684 N N   . ALA   A 1 655 ? 5.319   78.528  87.521  1.00 58.34  ?  636 ALA   A N   1 
ATOM   3685 C CA  . ALA   A 1 655 ? 4.033   79.192  87.368  1.00 51.97  ?  636 ALA   A CA  1 
ATOM   3686 C C   . ALA   A 1 655 ? 3.455   79.611  88.702  1.00 60.02  ?  636 ALA   A C   1 
ATOM   3687 O O   . ALA   A 1 655 ? 2.533   80.442  88.726  1.00 60.38  ?  636 ALA   A O   1 
ATOM   3688 C CB  . ALA   A 1 655 ? 3.030   78.277  86.673  1.00 57.38  ?  636 ALA   A CB  1 
ATOM   3689 N N   . VAL   A 1 656 ? 3.945   79.012  89.799  1.00 57.35  ?  637 VAL   A N   1 
ATOM   3690 C CA  . VAL   A 1 656 ? 3.517   79.319  91.161  1.00 51.21  ?  637 VAL   A CA  1 
ATOM   3691 C C   . VAL   A 1 656 ? 4.755   79.368  92.033  1.00 52.43  ?  637 VAL   A C   1 
ATOM   3692 O O   . VAL   A 1 656 ? 5.597   78.470  91.958  1.00 51.74  ?  637 VAL   A O   1 
ATOM   3693 C CB  . VAL   A 1 656 ? 2.526   78.292  91.731  1.00 42.96  ?  637 VAL   A CB  1 
ATOM   3694 C CG1 . VAL   A 1 656 ? 2.252   78.616  93.180  1.00 47.30  ?  637 VAL   A CG1 1 
ATOM   3695 C CG2 . VAL   A 1 656 ? 1.258   78.327  90.969  1.00 46.14  ?  637 VAL   A CG2 1 
ATOM   3696 N N   . GLN   A 1 657 ? 4.870   80.406  92.866  1.00 60.03  ?  638 GLN   A N   1 
ATOM   3697 C CA  . GLN   A 1 657 ? 6.128   80.644  93.546  1.00 57.22  ?  638 GLN   A CA  1 
ATOM   3698 C C   . GLN   A 1 657 ? 5.854   80.273  95.004  1.00 61.24  ?  638 GLN   A C   1 
ATOM   3699 O O   . GLN   A 1 657 ? 4.804   80.661  95.556  1.00 58.18  ?  638 GLN   A O   1 
ATOM   3700 C CB  . GLN   A 1 657 ? 6.518   82.100  93.526  1.00 53.21  ?  638 GLN   A CB  1 
ATOM   3701 C CG  . GLN   A 1 657 ? 8.022   82.421  93.372  1.00 72.23  ?  638 GLN   A CG  1 
ATOM   3702 C CD  . GLN   A 1 657 ? 8.343   83.761  93.990  1.00 80.07  ?  638 GLN   A CD  1 
ATOM   3703 O OE1 . GLN   A 1 657 ? 7.750   84.102  95.014  1.00 78.67  ?  638 GLN   A OE1 1 
ATOM   3704 N NE2 . GLN   A 1 657 ? 8.970   84.634  93.201  1.00 108.64 ?  638 GLN   A NE2 1 
ATOM   3705 N N   . PHE   A 1 658 ? 6.757   79.528  95.643  1.00 53.97  ?  639 PHE   A N   1 
ATOM   3706 C CA  . PHE   A 1 658 ? 6.536   79.210  97.049  1.00 52.91  ?  639 PHE   A CA  1 
ATOM   3707 C C   . PHE   A 1 658 ? 7.414   80.095  97.936  1.00 52.81  ?  639 PHE   A C   1 
ATOM   3708 O O   . PHE   A 1 658 ? 8.615   80.285  97.670  1.00 50.62  ?  639 PHE   A O   1 
ATOM   3709 C CB  . PHE   A 1 658 ? 6.743   77.714  97.314  1.00 52.89  ?  639 PHE   A CB  1 
ATOM   3710 C CG  . PHE   A 1 658 ? 5.554   76.860  96.884  1.00 49.52  ?  639 PHE   A CG  1 
ATOM   3711 C CD1 . PHE   A 1 658 ? 4.396   76.780  97.668  1.00 49.90  ?  639 PHE   A CD1 1 
ATOM   3712 C CD2 . PHE   A 1 658 ? 5.584   76.177  95.676  1.00 48.56  ?  639 PHE   A CD2 1 
ATOM   3713 C CE1 . PHE   A 1 658 ? 3.310   76.013  97.252  1.00 50.51  ?  639 PHE   A CE1 1 
ATOM   3714 C CE2 . PHE   A 1 658 ? 4.505   75.425  95.244  1.00 43.26  ?  639 PHE   A CE2 1 
ATOM   3715 C CZ  . PHE   A 1 658 ? 3.364   75.340  96.019  1.00 44.93  ?  639 PHE   A CZ  1 
ATOM   3716 N N   . VAL   A 1 659 ? 6.795   80.682  98.955  1.00 47.17  ?  640 VAL   A N   1 
ATOM   3717 C CA  . VAL   A 1 659 ? 7.501   81.608  99.836  1.00 48.30  ?  640 VAL   A CA  1 
ATOM   3718 C C   . VAL   A 1 659 ? 7.281   81.173  101.279 1.00 51.12  ?  640 VAL   A C   1 
ATOM   3719 O O   . VAL   A 1 659 ? 6.179   81.349  101.839 1.00 55.09  ?  640 VAL   A O   1 
ATOM   3720 C CB  . VAL   A 1 659 ? 7.058   83.067  99.606  1.00 58.00  ?  640 VAL   A CB  1 
ATOM   3721 C CG1 . VAL   A 1 659 ? 7.453   83.934  100.780 1.00 54.56  ?  640 VAL   A CG1 1 
ATOM   3722 C CG2 . VAL   A 1 659 ? 7.673   83.632  98.328  1.00 49.07  ?  640 VAL   A CG2 1 
ATOM   3723 N N   . PRO   A 1 660 ? 8.296   80.586  101.923 1.00 50.44  ?  641 PRO   A N   1 
ATOM   3724 C CA  . PRO   A 1 660 ? 9.636   80.317  101.371 1.00 45.34  ?  641 PRO   A CA  1 
ATOM   3725 C C   . PRO   A 1 660 ? 9.663   79.143  100.387 1.00 52.62  ?  641 PRO   A C   1 
ATOM   3726 O O   . PRO   A 1 660 ? 8.685   78.367  100.293 1.00 52.08  ?  641 PRO   A O   1 
ATOM   3727 C CB  . PRO   A 1 660 ? 10.464  80.002  102.619 1.00 39.46  ?  641 PRO   A CB  1 
ATOM   3728 C CG  . PRO   A 1 660 ? 9.470   79.502  103.625 1.00 42.44  ?  641 PRO   A CG  1 
ATOM   3729 C CD  . PRO   A 1 660 ? 8.144   80.122  103.319 1.00 47.33  ?  641 PRO   A CD  1 
ATOM   3730 N N   . PRO   A 1 661 ? 10.768  78.995  99.659  1.00 50.63  ?  642 PRO   A N   1 
ATOM   3731 C CA  . PRO   A 1 661 ? 10.851  77.913  98.677  1.00 46.64  ?  642 PRO   A CA  1 
ATOM   3732 C C   . PRO   A 1 661 ? 10.655  76.556  99.338  1.00 53.18  ?  642 PRO   A C   1 
ATOM   3733 O O   . PRO   A 1 661 ? 11.101  76.325  100.468 1.00 51.80  ?  642 PRO   A O   1 
ATOM   3734 C CB  . PRO   A 1 661 ? 12.271  78.050  98.122  1.00 43.30  ?  642 PRO   A CB  1 
ATOM   3735 C CG  . PRO   A 1 661 ? 12.700  79.361  98.470  1.00 41.72  ?  642 PRO   A CG  1 
ATOM   3736 C CD  . PRO   A 1 661 ? 12.059  79.675  99.789  1.00 43.37  ?  642 PRO   A CD  1 
ATOM   3737 N N   . LEU   A 1 662 ? 9.986   75.659  98.612  1.00 57.33  ?  643 LEU   A N   1 
ATOM   3738 C CA  . LEU   A 1 662 ? 9.872   74.263  99.015  1.00 50.21  ?  643 LEU   A CA  1 
ATOM   3739 C C   . LEU   A 1 662 ? 11.251  73.683  99.347  1.00 49.53  ?  643 LEU   A C   1 
ATOM   3740 O O   . LEU   A 1 662 ? 12.242  73.988  98.664  1.00 47.88  ?  643 LEU   A O   1 
ATOM   3741 C CB  . LEU   A 1 662 ? 9.209   73.462  97.885  1.00 47.48  ?  643 LEU   A CB  1 
ATOM   3742 C CG  . LEU   A 1 662 ? 7.802   73.995  97.571  1.00 48.81  ?  643 LEU   A CG  1 
ATOM   3743 C CD1 . LEU   A 1 662 ? 7.025   73.126  96.606  1.00 39.31  ?  643 LEU   A CD1 1 
ATOM   3744 C CD2 . LEU   A 1 662 ? 7.004   74.170  98.848  1.00 44.88  ?  643 LEU   A CD2 1 
ATOM   3745 N N   . PRO   A 1 663 ? 11.361  72.852  100.377 1.00 45.90  ?  644 PRO   A N   1 
ATOM   3746 C CA  . PRO   A 1 663 ? 12.650  72.220  100.670 1.00 44.28  ?  644 PRO   A CA  1 
ATOM   3747 C C   . PRO   A 1 663 ? 13.127  71.327  99.537  1.00 54.07  ?  644 PRO   A C   1 
ATOM   3748 O O   . PRO   A 1 663 ? 12.338  70.818  98.729  1.00 53.05  ?  644 PRO   A O   1 
ATOM   3749 C CB  . PRO   A 1 663 ? 12.372  71.398  101.931 1.00 45.52  ?  644 PRO   A CB  1 
ATOM   3750 C CG  . PRO   A 1 663 ? 10.882  71.296  102.037 1.00 47.31  ?  644 PRO   A CG  1 
ATOM   3751 C CD  . PRO   A 1 663 ? 10.327  72.527  101.378 1.00 50.01  ?  644 PRO   A CD  1 
ATOM   3752 N N   . GLU   A 1 664 ? 14.456  71.133  99.516  1.00 60.60  ?  645 GLU   A N   1 
ATOM   3753 C CA  . GLU   A 1 664 ? 15.122  70.269  98.537  1.00 57.73  ?  645 GLU   A CA  1 
ATOM   3754 C C   . GLU   A 1 664 ? 14.441  68.909  98.436  1.00 63.54  ?  645 GLU   A C   1 
ATOM   3755 O O   . GLU   A 1 664 ? 14.231  68.396  97.333  1.00 63.69  ?  645 GLU   A O   1 
ATOM   3756 C CB  . GLU   A 1 664 ? 16.600  70.112  98.922  1.00 63.27  ?  645 GLU   A CB  1 
ATOM   3757 C CG  . GLU   A 1 664 ? 17.605  69.567  97.865  1.00 74.61  ?  645 GLU   A CG  1 
ATOM   3758 C CD  . GLU   A 1 664 ? 17.633  68.059  97.787  1.00 100.17 ?  645 GLU   A CD  1 
ATOM   3759 O OE1 . GLU   A 1 664 ? 17.251  67.403  98.773  1.00 110.45 ?  645 GLU   A OE1 1 
ATOM   3760 O OE2 . GLU   A 1 664 ? 18.155  67.511  96.784  1.00 109.91 ?  645 GLU   A OE2 1 
ATOM   3761 N N   . TRP   A 1 665 ? 14.079  68.302  99.576  1.00 56.19  ?  646 TRP   A N   1 
ATOM   3762 C CA  . TRP   A 1 665 ? 13.521  66.960  99.484  1.00 51.59  ?  646 TRP   A CA  1 
ATOM   3763 C C   . TRP   A 1 665 ? 12.188  66.965  98.759  1.00 53.14  ?  646 TRP   A C   1 
ATOM   3764 O O   . TRP   A 1 665 ? 11.836  65.981  98.096  1.00 64.38  ?  646 TRP   A O   1 
ATOM   3765 C CB  . TRP   A 1 665 ? 13.363  66.294  100.854 1.00 45.98  ?  646 TRP   A CB  1 
ATOM   3766 C CG  . TRP   A 1 665 ? 12.538  67.014  101.792 1.00 47.36  ?  646 TRP   A CG  1 
ATOM   3767 C CD1 . TRP   A 1 665 ? 12.964  67.870  102.753 1.00 50.10  ?  646 TRP   A CD1 1 
ATOM   3768 C CD2 . TRP   A 1 665 ? 11.111  66.947  101.913 1.00 48.62  ?  646 TRP   A CD2 1 
ATOM   3769 N NE1 . TRP   A 1 665 ? 11.891  68.360  103.464 1.00 44.72  ?  646 TRP   A NE1 1 
ATOM   3770 C CE2 . TRP   A 1 665 ? 10.741  67.810  102.971 1.00 42.29  ?  646 TRP   A CE2 1 
ATOM   3771 C CE3 . TRP   A 1 665 ? 10.107  66.258  101.223 1.00 50.90  ?  646 TRP   A CE3 1 
ATOM   3772 C CZ2 . TRP   A 1 665 ? 9.419   68.014  103.351 1.00 40.91  ?  646 TRP   A CZ2 1 
ATOM   3773 C CZ3 . TRP   A 1 665 ? 8.772   66.460  101.619 1.00 51.19  ?  646 TRP   A CZ3 1 
ATOM   3774 C CH2 . TRP   A 1 665 ? 8.452   67.330  102.676 1.00 47.29  ?  646 TRP   A CH2 1 
ATOM   3775 N N   . LYS   A 1 666 ? 11.436  68.045  98.847  1.00 50.56  ?  647 LYS   A N   1 
ATOM   3776 C CA  . LYS   A 1 666 ? 10.215  68.067  98.060  1.00 51.09  ?  647 LYS   A CA  1 
ATOM   3777 C C   . LYS   A 1 666 ? 10.519  68.349  96.591  1.00 52.43  ?  647 LYS   A C   1 
ATOM   3778 O O   . LYS   A 1 666 ? 10.031  67.635  95.707  1.00 57.54  ?  647 LYS   A O   1 
ATOM   3779 C CB  . LYS   A 1 666 ? 9.227   69.081  98.635  1.00 47.80  ?  647 LYS   A CB  1 
ATOM   3780 C CG  . LYS   A 1 666 ? 8.028   69.363  97.753  1.00 47.64  ?  647 LYS   A CG  1 
ATOM   3781 C CD  . LYS   A 1 666 ? 6.939   68.364  97.997  1.00 51.32  ?  647 LYS   A CD  1 
ATOM   3782 C CE  . LYS   A 1 666 ? 6.630   68.220  99.481  1.00 49.30  ?  647 LYS   A CE  1 
ATOM   3783 N NZ  . LYS   A 1 666 ? 5.230   67.724  99.719  1.00 49.38  ?  647 LYS   A NZ  1 
ATOM   3784 N N   . THR   A 1 667 ? 11.333  69.367  96.302  1.00 52.53  ?  648 THR   A N   1 
ATOM   3785 C CA  . THR   A 1 667 ? 11.561  69.724  94.899  1.00 57.81  ?  648 THR   A CA  1 
ATOM   3786 C C   . THR   A 1 667 ? 12.210  68.579  94.143  1.00 57.55  ?  648 THR   A C   1 
ATOM   3787 O O   . THR   A 1 667 ? 11.936  68.396  92.952  1.00 57.49  ?  648 THR   A O   1 
ATOM   3788 C CB  . THR   A 1 667 ? 12.444  70.976  94.750  1.00 54.34  ?  648 THR   A CB  1 
ATOM   3789 O OG1 . THR   A 1 667 ? 13.807  70.631  95.040  1.00 60.19  ?  648 THR   A OG1 1 
ATOM   3790 C CG2 . THR   A 1 667 ? 12.001  72.107  95.656  1.00 38.50  ?  648 THR   A CG2 1 
ATOM   3791 N N   . SER   A 1 668 ? 13.055  67.789  94.826  1.00 59.59  ?  649 SER   A N   1 
ATOM   3792 C CA  . SER   A 1 668 ? 13.757  66.693  94.162  1.00 54.91  ?  649 SER   A CA  1 
ATOM   3793 C C   . SER   A 1 668 ? 12.819  65.553  93.833  1.00 55.78  ?  649 SER   A C   1 
ATOM   3794 O O   . SER   A 1 668 ? 12.903  64.978  92.745  1.00 55.95  ?  649 SER   A O   1 
ATOM   3795 C CB  . SER   A 1 668 ? 14.903  66.199  95.016  1.00 52.09  ?  649 SER   A CB  1 
ATOM   3796 O OG  . SER   A 1 668 ? 15.854  67.234  95.133  1.00 69.01  ?  649 SER   A OG  1 
ATOM   3797 N N   . ALA   A 1 669 ? 11.905  65.222  94.742  1.00 54.50  ?  650 ALA   A N   1 
ATOM   3798 C CA  . ALA   A 1 669 ? 10.822  64.327  94.359  1.00 50.98  ?  650 ALA   A CA  1 
ATOM   3799 C C   . ALA   A 1 669 ? 10.097  64.847  93.123  1.00 54.46  ?  650 ALA   A C   1 
ATOM   3800 O O   . ALA   A 1 669 ? 9.788   64.074  92.213  1.00 59.10  ?  650 ALA   A O   1 
ATOM   3801 C CB  . ALA   A 1 669 ? 9.846   64.151  95.514  1.00 51.60  ?  650 ALA   A CB  1 
ATOM   3802 N N   . VAL   A 1 670 ? 9.847   66.156  93.056  1.00 51.18  ?  651 VAL   A N   1 
ATOM   3803 C CA  . VAL   A 1 670 ? 9.130   66.714  91.911  1.00 52.90  ?  651 VAL   A CA  1 
ATOM   3804 C C   . VAL   A 1 670 ? 9.909   66.483  90.615  1.00 55.25  ?  651 VAL   A C   1 
ATOM   3805 O O   . VAL   A 1 670 ? 9.328   66.089  89.590  1.00 53.07  ?  651 VAL   A O   1 
ATOM   3806 C CB  . VAL   A 1 670 ? 8.821   68.210  92.144  1.00 52.69  ?  651 VAL   A CB  1 
ATOM   3807 C CG1 . VAL   A 1 670 ? 8.271   68.856  90.884  1.00 45.66  ?  651 VAL   A CG1 1 
ATOM   3808 C CG2 . VAL   A 1 670 ? 7.817   68.387  93.289  1.00 48.58  ?  651 VAL   A CG2 1 
ATOM   3809 N N   . GLN   A 1 671 ? 11.232  66.687  90.630  1.00 50.83  ?  652 GLN   A N   1 
ATOM   3810 C CA  . GLN   A 1 671 ? 11.974  66.445  89.390  1.00 57.66  ?  652 GLN   A CA  1 
ATOM   3811 C C   . GLN   A 1 671 ? 12.054  64.961  89.047  1.00 53.31  ?  652 GLN   A C   1 
ATOM   3812 O O   . GLN   A 1 671 ? 11.954  64.589  87.879  1.00 56.02  ?  652 GLN   A O   1 
ATOM   3813 C CB  . GLN   A 1 671 ? 13.365  67.060  89.465  1.00 62.15  ?  652 GLN   A CB  1 
ATOM   3814 C CG  . GLN   A 1 671 ? 13.327  68.472  90.026  1.00 75.74  ?  652 GLN   A CG  1 
ATOM   3815 C CD  . GLN   A 1 671 ? 14.674  69.201  89.968  1.00 89.39  ?  652 GLN   A CD  1 
ATOM   3816 O OE1 . GLN   A 1 671 ? 15.629  68.755  89.309  1.00 93.97  ?  652 GLN   A OE1 1 
ATOM   3817 N NE2 . GLN   A 1 671 ? 14.764  70.315  90.701  1.00 83.14  ?  652 GLN   A NE2 1 
ATOM   3818 N N   . ARG   A 1 672 ? 12.209  64.098  90.049  1.00 56.92  ?  653 ARG   A N   1 
ATOM   3819 C CA  . ARG   A 1 672 ? 12.360  62.674  89.787  1.00 50.31  ?  653 ARG   A CA  1 
ATOM   3820 C C   . ARG   A 1 672 ? 11.099  62.074  89.196  1.00 58.02  ?  653 ARG   A C   1 
ATOM   3821 O O   . ARG   A 1 672 ? 11.175  61.195  88.322  1.00 64.78  ?  653 ARG   A O   1 
ATOM   3822 C CB  . ARG   A 1 672 ? 12.721  61.929  91.066  1.00 49.16  ?  653 ARG   A CB  1 
ATOM   3823 C CG  . ARG   A 1 672 ? 14.146  62.124  91.430  1.00 54.89  ?  653 ARG   A CG  1 
ATOM   3824 C CD  . ARG   A 1 672 ? 14.607  61.156  92.461  1.00 49.62  ?  653 ARG   A CD  1 
ATOM   3825 N NE  . ARG   A 1 672 ? 13.766  61.159  93.641  1.00 49.03  ?  653 ARG   A NE  1 
ATOM   3826 C CZ  . ARG   A 1 672 ? 14.008  61.919  94.694  1.00 55.90  ?  653 ARG   A CZ  1 
ATOM   3827 N NH1 . ARG   A 1 672 ? 15.051  62.747  94.654  1.00 64.48  ?  653 ARG   A NH1 1 
ATOM   3828 N NH2 . ARG   A 1 672 ? 13.207  61.872  95.762  1.00 52.42  ?  653 ARG   A NH2 1 
ATOM   3829 N N   . MET   A 1 673 ? 9.934   62.495  89.677  1.00 51.06  ?  654 MET   A N   1 
ATOM   3830 C CA  . MET   A 1 673 ? 8.721   61.834  89.228  1.00 56.34  ?  654 MET   A CA  1 
ATOM   3831 C C   . MET   A 1 673 ? 8.496   62.083  87.737  1.00 56.86  ?  654 MET   A C   1 
ATOM   3832 O O   . MET   A 1 673 ? 9.002   63.037  87.147  1.00 55.44  ?  654 MET   A O   1 
ATOM   3833 C CB  . MET   A 1 673 ? 7.523   62.304  90.035  1.00 51.50  ?  654 MET   A CB  1 
ATOM   3834 C CG  . MET   A 1 673 ? 7.687   61.981  91.512  1.00 59.19  ?  654 MET   A CG  1 
ATOM   3835 S SD  . MET   A 1 673 ? 6.134   62.006  92.419  1.00 72.18  ?  654 MET   A SD  1 
ATOM   3836 C CE  . MET   A 1 673 ? 5.122   61.225  91.131  1.00 64.49  ?  654 MET   A CE  1 
ATOM   3837 N N   . GLY   A 1 674 ? 7.772   61.166  87.112  1.00 52.41  ?  655 GLY   A N   1 
ATOM   3838 C CA  . GLY   A 1 674 ? 7.411   61.302  85.724  1.00 47.41  ?  655 GLY   A CA  1 
ATOM   3839 C C   . GLY   A 1 674 ? 6.021   61.896  85.622  1.00 50.76  ?  655 GLY   A C   1 
ATOM   3840 O O   . GLY   A 1 674 ? 5.112   61.510  86.360  1.00 50.87  ?  655 GLY   A O   1 
ATOM   3841 N N   . PHE   A 1 675 ? 5.832   62.780  84.655  1.00 50.86  ?  656 PHE   A N   1 
ATOM   3842 C CA  . PHE   A 1 675 ? 4.488   63.309  84.345  1.00 54.22  ?  656 PHE   A CA  1 
ATOM   3843 C C   . PHE   A 1 675 ? 4.286   63.103  82.855  1.00 54.20  ?  656 PHE   A C   1 
ATOM   3844 O O   . PHE   A 1 675 ? 4.863   63.808  82.072  1.00 53.46  ?  656 PHE   A O   1 
ATOM   3845 C CB  . PHE   A 1 675 ? 4.324   64.771  84.728  1.00 49.62  ?  656 PHE   A CB  1 
ATOM   3846 C CG  . PHE   A 1 675 ? 2.893   65.190  84.892  1.00 48.87  ?  656 PHE   A CG  1 
ATOM   3847 C CD1 . PHE   A 1 675 ? 2.018   64.438  85.625  1.00 52.43  ?  656 PHE   A CD1 1 
ATOM   3848 C CD2 . PHE   A 1 675 ? 2.419   66.331  84.313  1.00 45.59  ?  656 PHE   A CD2 1 
ATOM   3849 C CE1 . PHE   A 1 675 ? 0.705   64.826  85.775  1.00 49.86  ?  656 PHE   A CE1 1 
ATOM   3850 C CE2 . PHE   A 1 675 ? 1.106   66.712  84.463  1.00 48.21  ?  656 PHE   A CE2 1 
ATOM   3851 C CZ  . PHE   A 1 675 ? 0.248   65.958  85.193  1.00 43.49  ?  656 PHE   A CZ  1 
ATOM   3852 N N   . GLY   A 1 676 ? 3.442   62.147  82.517  1.00 54.46  ?  657 GLY   A N   1 
ATOM   3853 C CA  . GLY   A 1 676 ? 3.226   61.709  81.135  1.00 55.34  ?  657 GLY   A CA  1 
ATOM   3854 C C   . GLY   A 1 676 ? 2.241   62.507  80.337  1.00 54.54  ?  657 GLY   A C   1 
ATOM   3855 O O   . GLY   A 1 676 ? 1.711   63.454  80.826  1.00 55.10  ?  657 GLY   A O   1 
ATOM   3856 N N   . ASN   A 1 677 ? 2.063   62.081  79.100  1.00 59.01  ?  658 ASN   A N   1 
ATOM   3857 C CA  . ASN   A 1 677 ? 1.151   62.737  78.150  1.00 59.56  ?  658 ASN   A CA  1 
ATOM   3858 C C   . ASN   A 1 677 ? 0.340   61.694  77.397  1.00 56.31  ?  658 ASN   A C   1 
ATOM   3859 O O   . ASN   A 1 677 ? 0.850   60.656  77.102  1.00 61.04  ?  658 ASN   A O   1 
ATOM   3860 C CB  . ASN   A 1 677 ? 1.948   63.549  77.154  1.00 56.04  ?  658 ASN   A CB  1 
ATOM   3861 C CG  . ASN   A 1 677 ? 1.067   64.539  76.463  1.00 61.46  ?  658 ASN   A CG  1 
ATOM   3862 O OD1 . ASN   A 1 677 ? -0.118  64.575  76.713  1.00 58.52  ?  658 ASN   A OD1 1 
ATOM   3863 N ND2 . ASN   A 1 677 ? 1.651   65.329  75.603  1.00 60.08  ?  658 ASN   A ND2 1 
ATOM   3864 N N   . LEU   A 1 678 ? -0.896  62.029  77.096  1.00 57.36  ?  659 LEU   A N   1 
ATOM   3865 C CA  . LEU   A 1 678 ? -1.849  61.161  76.388  1.00 54.07  ?  659 LEU   A CA  1 
ATOM   3866 C C   . LEU   A 1 678 ? -2.823  62.101  75.715  1.00 65.24  ?  659 LEU   A C   1 
ATOM   3867 O O   . LEU   A 1 678 ? -3.206  63.023  76.361  1.00 73.42  ?  659 LEU   A O   1 
ATOM   3868 C CB  . LEU   A 1 678 ? -2.589  60.438  77.496  1.00 51.67  ?  659 LEU   A CB  1 
ATOM   3869 C CG  . LEU   A 1 678 ? -3.035  59.028  77.208  1.00 63.90  ?  659 LEU   A CG  1 
ATOM   3870 C CD1 . LEU   A 1 678 ? -3.825  58.523  78.382  1.00 63.01  ?  659 LEU   A CD1 1 
ATOM   3871 C CD2 . LEU   A 1 678 ? -3.893  59.014  75.984  1.00 69.89  ?  659 LEU   A CD2 1 
ATOM   3872 N N   . ASN   A 1 679 ? -3.286  61.843  74.507  1.00 66.41  ?  660 ASN   A N   1 
ATOM   3873 C CA  . ASN   A 1 679 ? -4.229  62.839  73.943  1.00 66.45  ?  660 ASN   A CA  1 
ATOM   3874 C C   . ASN   A 1 679 ? -5.404  62.134  73.294  1.00 67.70  ?  660 ASN   A C   1 
ATOM   3875 O O   . ASN   A 1 679 ? -5.240  61.015  72.937  1.00 74.35  ?  660 ASN   A O   1 
ATOM   3876 C CB  . ASN   A 1 679 ? -3.507  63.835  73.059  1.00 63.59  ?  660 ASN   A CB  1 
ATOM   3877 C CG  . ASN   A 1 679 ? -2.533  64.636  73.874  1.00 66.56  ?  660 ASN   A CG  1 
ATOM   3878 O OD1 . ASN   A 1 679 ? -1.389  64.784  73.478  1.00 60.74  ?  660 ASN   A OD1 1 
ATOM   3879 N ND2 . ASN   A 1 679 ? -2.985  65.155  74.995  1.00 68.75  ?  660 ASN   A ND2 1 
ATOM   3880 N N   . LYS   A 1 680 ? -6.556  62.776  73.196  1.00 60.85  ?  661 LYS   A N   1 
ATOM   3881 C CA  . LYS   A 1 680 ? -7.695  62.081  72.568  1.00 68.08  ?  661 LYS   A CA  1 
ATOM   3882 C C   . LYS   A 1 680 ? -8.261  62.932  71.447  1.00 72.87  ?  661 LYS   A C   1 
ATOM   3883 O O   . LYS   A 1 680 ? -8.215  64.122  71.567  1.00 72.66  ?  661 LYS   A O   1 
ATOM   3884 C CB  . LYS   A 1 680 ? -8.849  61.936  73.548  1.00 58.35  ?  661 LYS   A CB  1 
ATOM   3885 C CG  . LYS   A 1 680 ? -8.533  61.203  74.827  1.00 60.47  ?  661 LYS   A CG  1 
ATOM   3886 C CD  . LYS   A 1 680 ? -9.743  60.581  75.413  1.00 59.59  ?  661 LYS   A CD  1 
ATOM   3887 C CE  . LYS   A 1 680 ? -9.667  60.492  76.908  1.00 61.79  ?  661 LYS   A CE  1 
ATOM   3888 N NZ  . LYS   A 1 680 ? -9.703  59.096  77.371  1.00 78.80  ?  661 LYS   A NZ  1 
ATOM   3889 N N   . VAL   A 1 681 ? -8.742  62.293  70.390  1.00 78.83  ?  662 VAL   A N   1 
ATOM   3890 C CA  . VAL   A 1 681 ? -9.433  62.961  69.288  1.00 77.64  ?  662 VAL   A CA  1 
ATOM   3891 C C   . VAL   A 1 681 ? -10.874 62.477  69.282  1.00 78.77  ?  662 VAL   A C   1 
ATOM   3892 O O   . VAL   A 1 681 ? -11.130 61.265  69.211  1.00 77.67  ?  662 VAL   A O   1 
ATOM   3893 C CB  . VAL   A 1 681 ? -8.772  62.684  67.933  1.00 75.72  ?  662 VAL   A CB  1 
ATOM   3894 C CG1 . VAL   A 1 681 ? -9.557  63.384  66.844  1.00 79.05  ?  662 VAL   A CG1 1 
ATOM   3895 C CG2 . VAL   A 1 681 ? -7.319  63.127  67.929  1.00 72.90  ?  662 VAL   A CG2 1 
ATOM   3896 N N   . VAL   A 1 682 ? -11.816 63.414  69.357  1.00 78.86  ?  663 VAL   A N   1 
ATOM   3897 C CA  . VAL   A 1 682 ? -13.235 63.083  69.350  1.00 87.07  ?  663 VAL   A CA  1 
ATOM   3898 C C   . VAL   A 1 682 ? -13.780 63.319  67.954  1.00 91.47  ?  663 VAL   A C   1 
ATOM   3899 O O   . VAL   A 1 682 ? -13.621 64.415  67.397  1.00 90.23  ?  663 VAL   A O   1 
ATOM   3900 C CB  . VAL   A 1 682 ? -14.020 63.907  70.380  1.00 91.17  ?  663 VAL   A CB  1 
ATOM   3901 C CG1 . VAL   A 1 682 ? -15.409 63.305  70.544  1.00 91.25  ?  663 VAL   A CG1 1 
ATOM   3902 C CG2 . VAL   A 1 682 ? -13.295 63.924  71.686  1.00 92.59  ?  663 VAL   A CG2 1 
ATOM   3903 N N   . LEU   A 1 683 ? -14.434 62.295  67.395  1.00 97.57  ?  664 LEU   A N   1 
ATOM   3904 C CA  . LEU   A 1 683 ? -15.002 62.332  66.051  1.00 93.82  ?  664 LEU   A CA  1 
ATOM   3905 C C   . LEU   A 1 683 ? -16.499 62.047  66.139  1.00 96.08  ?  664 LEU   A C   1 
ATOM   3906 O O   . LEU   A 1 683 ? -16.913 60.960  66.575  1.00 90.33  ?  664 LEU   A O   1 
ATOM   3907 C CB  . LEU   A 1 683 ? -14.281 61.335  65.140  1.00 88.62  ?  664 LEU   A CB  1 
ATOM   3908 C CG  . LEU   A 1 683 ? -12.793 61.685  64.980  1.00 80.77  ?  664 LEU   A CG  1 
ATOM   3909 C CD1 . LEU   A 1 683 ? -11.952 60.511  64.485  1.00 78.73  ?  664 LEU   A CD1 1 
ATOM   3910 C CD2 . LEU   A 1 683 ? -12.617 62.890  64.086  1.00 82.48  ?  664 LEU   A CD2 1 
ATOM   3911 N N   . CYS   A 1 684 ? -17.299 63.036  65.735  1.00 98.63  ?  665 CYS   A N   1 
ATOM   3912 C CA  . CYS   A 1 684 ? -18.751 63.001  65.831  1.00 107.64 ?  665 CYS   A CA  1 
ATOM   3913 C C   . CYS   A 1 684 ? -19.360 62.668  64.481  1.00 109.36 ?  665 CYS   A C   1 
ATOM   3914 O O   . CYS   A 1 684 ? -19.033 63.293  63.464  1.00 110.21 ?  665 CYS   A O   1 
ATOM   3915 C CB  . CYS   A 1 684 ? -19.294 64.342  66.311  1.00 110.71 ?  665 CYS   A CB  1 
ATOM   3916 S SG  . CYS   A 1 684 ? -18.619 64.903  67.866  1.00 111.17 ?  665 CYS   A SG  1 
ATOM   3917 N N   . PHE   A 1 685 ? -20.261 61.701  64.485  1.00 110.54 ?  666 PHE   A N   1 
ATOM   3918 C CA  . PHE   A 1 685 ? -20.909 61.268  63.263  1.00 112.34 ?  666 PHE   A CA  1 
ATOM   3919 C C   . PHE   A 1 685 ? -22.427 61.267  63.468  1.00 114.63 ?  666 PHE   A C   1 
ATOM   3920 O O   . PHE   A 1 685 ? -22.930 61.413  64.586  1.00 111.71 ?  666 PHE   A O   1 
ATOM   3921 C CB  . PHE   A 1 685 ? -20.343 59.917  62.794  1.00 113.17 ?  666 PHE   A CB  1 
ATOM   3922 C CG  . PHE   A 1 685 ? -18.859 59.992  62.442  1.00 106.39 ?  666 PHE   A CG  1 
ATOM   3923 C CD1 . PHE   A 1 685 ? -18.392 60.996  61.587  1.00 104.07 ?  666 PHE   A CD1 1 
ATOM   3924 C CD2 . PHE   A 1 685 ? -17.942 59.093  62.979  1.00 100.67 ?  666 PHE   A CD2 1 
ATOM   3925 C CE1 . PHE   A 1 685 ? -17.028 61.101  61.279  1.00 102.15 ?  666 PHE   A CE1 1 
ATOM   3926 C CE2 . PHE   A 1 685 ? -16.603 59.189  62.673  1.00 98.81  ?  666 PHE   A CE2 1 
ATOM   3927 C CZ  . PHE   A 1 685 ? -16.140 60.185  61.826  1.00 98.27  ?  666 PHE   A CZ  1 
ATOM   3928 N N   . ASP   A 1 686 ? -23.143 61.207  62.338  1.00 120.70 ?  667 ASP   A N   1 
ATOM   3929 C CA  . ASP   A 1 686 ? -24.583 60.990  62.244  1.00 116.49 ?  667 ASP   A CA  1 
ATOM   3930 C C   . ASP   A 1 686 ? -24.958 59.511  62.291  1.00 115.85 ?  667 ASP   A C   1 
ATOM   3931 O O   . ASP   A 1 686 ? -25.971 59.129  62.903  1.00 113.80 ?  667 ASP   A O   1 
ATOM   3932 C CB  . ASP   A 1 686 ? -25.108 61.613  60.951  1.00 106.86 ?  667 ASP   A CB  1 
ATOM   3933 C CG  . ASP   A 1 686 ? -24.173 61.398  59.788  1.00 119.51 ?  667 ASP   A CG  1 
ATOM   3934 O OD1 . ASP   A 1 686 ? -22.953 61.156  60.098  1.00 123.58 ?  667 ASP   A OD1 1 
ATOM   3935 O OD2 . ASP   A 1 686 ? -24.620 61.290  58.621  1.00 126.89 ?  667 ASP   A OD2 1 
ATOM   3936 N N   . ARG   A 1 687 ? -24.145 58.659  61.674  1.00 110.23 ?  668 ARG   A N   1 
ATOM   3937 C CA  . ARG   A 1 687 ? -24.484 57.257  61.544  1.00 112.18 ?  668 ARG   A CA  1 
ATOM   3938 C C   . ARG   A 1 687 ? -23.319 56.388  61.987  1.00 108.24 ?  668 ARG   A C   1 
ATOM   3939 O O   . ARG   A 1 687 ? -22.196 56.522  61.485  1.00 106.72 ?  668 ARG   A O   1 
ATOM   3940 C CB  . ARG   A 1 687 ? -24.895 56.960  60.106  1.00 117.31 ?  668 ARG   A CB  1 
ATOM   3941 C CG  . ARG   A 1 687 ? -23.926 57.445  59.037  1.00 118.10 ?  668 ARG   A CG  1 
ATOM   3942 C CD  . ARG   A 1 687 ? -24.600 57.343  57.675  1.00 128.40 ?  668 ARG   A CD  1 
ATOM   3943 N NE  . ARG   A 1 687 ? -23.701 57.564  56.543  1.00 134.70 ?  668 ARG   A NE  1 
ATOM   3944 C CZ  . ARG   A 1 687 ? -23.476 58.745  55.972  1.00 128.67 ?  668 ARG   A CZ  1 
ATOM   3945 N NH1 . ARG   A 1 687 ? -24.071 59.840  56.441  1.00 119.18 ?  668 ARG   A NH1 1 
ATOM   3946 N NH2 . ARG   A 1 687 ? -22.650 58.828  54.931  1.00 120.68 ?  668 ARG   A NH2 1 
ATOM   3947 N N   . VAL   A 1 688 ? -23.605 55.498  62.927  1.00 102.04 ?  669 VAL   A N   1 
ATOM   3948 C CA  . VAL   A 1 688 ? -22.754 54.352  63.194  1.00 104.88 ?  669 VAL   A CA  1 
ATOM   3949 C C   . VAL   A 1 688 ? -22.417 53.696  61.854  1.00 109.00 ?  669 VAL   A C   1 
ATOM   3950 O O   . VAL   A 1 688 ? -23.305 53.268  61.108  1.00 111.13 ?  669 VAL   A O   1 
ATOM   3951 C CB  . VAL   A 1 688 ? -23.438 53.363  64.161  1.00 105.22 ?  669 VAL   A CB  1 
ATOM   3952 C CG1 . VAL   A 1 688 ? -22.697 52.031  64.181  1.00 108.10 ?  669 VAL   A CG1 1 
ATOM   3953 C CG2 . VAL   A 1 688 ? -23.525 53.948  65.563  1.00 106.02 ?  669 VAL   A CG2 1 
ATOM   3954 N N   . PHE   A 1 689 ? -21.133 53.651  61.518  1.00 108.08 ?  670 PHE   A N   1 
ATOM   3955 C CA  . PHE   A 1 689 ? -20.664 53.020  60.294  1.00 100.14 ?  670 PHE   A CA  1 
ATOM   3956 C C   . PHE   A 1 689 ? -19.542 52.053  60.633  1.00 98.29  ?  670 PHE   A C   1 
ATOM   3957 O O   . PHE   A 1 689 ? -18.603 51.870  59.861  1.00 100.92 ?  670 PHE   A O   1 
ATOM   3958 C CB  . PHE   A 1 689 ? -20.232 54.083  59.289  1.00 99.44  ?  670 PHE   A CB  1 
ATOM   3959 C CG  . PHE   A 1 689 ? -18.977 54.806  59.655  1.00 107.56 ?  670 PHE   A CG  1 
ATOM   3960 C CD1 . PHE   A 1 689 ? -18.989 55.864  60.554  1.00 109.50 ?  670 PHE   A CD1 1 
ATOM   3961 C CD2 . PHE   A 1 689 ? -17.797 54.519  58.985  1.00 113.57 ?  670 PHE   A CD2 1 
ATOM   3962 C CE1 . PHE   A 1 689 ? -17.801 56.547  60.859  1.00 109.07 ?  670 PHE   A CE1 1 
ATOM   3963 C CE2 . PHE   A 1 689 ? -16.621 55.201  59.268  1.00 114.66 ?  670 PHE   A CE2 1 
ATOM   3964 C CZ  . PHE   A 1 689 ? -16.620 56.217  60.199  1.00 108.69 ?  670 PHE   A CZ  1 
ATOM   3965 N N   . TRP   A 1 690 ? -19.655 51.440  61.809  1.00 93.40  ?  671 TRP   A N   1 
ATOM   3966 C CA  . TRP   A 1 690 ? -18.665 50.561  62.402  1.00 97.82  ?  671 TRP   A CA  1 
ATOM   3967 C C   . TRP   A 1 690 ? -19.417 49.424  63.062  1.00 95.12  ?  671 TRP   A C   1 
ATOM   3968 O O   . TRP   A 1 690 ? -20.647 49.426  63.128  1.00 92.22  ?  671 TRP   A O   1 
ATOM   3969 C CB  . TRP   A 1 690 ? -17.793 51.282  63.444  1.00 105.75 ?  671 TRP   A CB  1 
ATOM   3970 C CG  . TRP   A 1 690 ? -18.576 52.071  64.505  1.00 104.28 ?  671 TRP   A CG  1 
ATOM   3971 C CD1 . TRP   A 1 690 ? -19.194 51.562  65.614  1.00 104.01 ?  671 TRP   A CD1 1 
ATOM   3972 C CD2 . TRP   A 1 690 ? -18.787 53.495  64.548  1.00 96.13  ?  671 TRP   A CD2 1 
ATOM   3973 N NE1 . TRP   A 1 690 ? -19.789 52.569  66.318  1.00 105.33 ?  671 TRP   A NE1 1 
ATOM   3974 C CE2 . TRP   A 1 690 ? -19.551 53.768  65.696  1.00 99.64  ?  671 TRP   A CE2 1 
ATOM   3975 C CE3 . TRP   A 1 690 ? -18.416 54.559  63.717  1.00 96.50  ?  671 TRP   A CE3 1 
ATOM   3976 C CZ2 . TRP   A 1 690 ? -19.948 55.068  66.043  1.00 104.68 ?  671 TRP   A CZ2 1 
ATOM   3977 C CZ3 . TRP   A 1 690 ? -18.808 55.850  64.062  1.00 98.70  ?  671 TRP   A CZ3 1 
ATOM   3978 C CH2 . TRP   A 1 690 ? -19.566 56.091  65.212  1.00 103.92 ?  671 TRP   A CH2 1 
ATOM   3979 N N   . ASP   A 1 691 ? -18.681 48.470  63.592  1.00 95.22  ?  672 ASP   A N   1 
ATOM   3980 C CA  . ASP   A 1 691 ? -19.368 47.370  64.249  1.00 105.25 ?  672 ASP   A CA  1 
ATOM   3981 C C   . ASP   A 1 691 ? -19.803 47.817  65.642  1.00 113.78 ?  672 ASP   A C   1 
ATOM   3982 O O   . ASP   A 1 691 ? -18.957 48.024  66.525  1.00 112.61 ?  672 ASP   A O   1 
ATOM   3983 C CB  . ASP   A 1 691 ? -18.467 46.141  64.320  1.00 107.78 ?  672 ASP   A CB  1 
ATOM   3984 C CG  . ASP   A 1 691 ? -19.175 44.935  64.903  1.00 117.18 ?  672 ASP   A CG  1 
ATOM   3985 O OD1 . ASP   A 1 691 ? -20.239 45.113  65.543  1.00 113.10 ?  672 ASP   A OD1 1 
ATOM   3986 O OD2 . ASP   A 1 691 ? -18.652 43.806  64.742  1.00 121.94 ?  672 ASP   A OD2 1 
ATOM   3987 N N   . PRO   A 1 692 ? -21.111 47.946  65.886  1.00 114.87 ?  673 PRO   A N   1 
ATOM   3988 C CA  . PRO   A 1 692 ? -21.568 48.502  67.170  1.00 114.14 ?  673 PRO   A CA  1 
ATOM   3989 C C   . PRO   A 1 692 ? -21.412 47.554  68.343  1.00 110.29 ?  673 PRO   A C   1 
ATOM   3990 O O   . PRO   A 1 692 ? -21.452 48.014  69.491  1.00 116.47 ?  673 PRO   A O   1 
ATOM   3991 C CB  . PRO   A 1 692 ? -23.047 48.816  66.909  1.00 111.80 ?  673 PRO   A CB  1 
ATOM   3992 C CG  . PRO   A 1 692 ? -23.172 48.831  65.413  1.00 111.21 ?  673 PRO   A CG  1 
ATOM   3993 C CD  . PRO   A 1 692 ? -22.228 47.775  64.951  1.00 111.25 ?  673 PRO   A CD  1 
ATOM   3994 N N   . SER   A 1 693 ? -21.256 46.254  68.107  1.00 107.91 ?  674 SER   A N   1 
ATOM   3995 C CA  . SER   A 1 693 ? -20.919 45.356  69.208  1.00 120.11 ?  674 SER   A CA  1 
ATOM   3996 C C   . SER   A 1 693 ? -19.423 45.333  69.488  1.00 118.47 ?  674 SER   A C   1 
ATOM   3997 O O   . SER   A 1 693 ? -18.985 44.651  70.427  1.00 113.71 ?  674 SER   A O   1 
ATOM   3998 C CB  . SER   A 1 693 ? -21.422 43.935  68.925  1.00 117.17 ?  674 SER   A CB  1 
ATOM   3999 O OG  . SER   A 1 693 ? -20.718 43.349  67.844  1.00 114.20 ?  674 SER   A OG  1 
ATOM   4000 N N   . VAL   A 1 694 ? -18.642 46.053  68.687  1.00 112.35 ?  675 VAL   A N   1 
ATOM   4001 C CA  . VAL   A 1 694 ? -17.240 46.315  68.980  1.00 114.39 ?  675 VAL   A CA  1 
ATOM   4002 C C   . VAL   A 1 694 ? -17.152 47.676  69.671  1.00 116.62 ?  675 VAL   A C   1 
ATOM   4003 O O   . VAL   A 1 694 ? -17.464 48.720  69.078  1.00 111.75 ?  675 VAL   A O   1 
ATOM   4004 C CB  . VAL   A 1 694 ? -16.384 46.256  67.709  1.00 111.43 ?  675 VAL   A CB  1 
ATOM   4005 C CG1 . VAL   A 1 694 ? -15.098 47.046  67.873  1.00 105.84 ?  675 VAL   A CG1 1 
ATOM   4006 C CG2 . VAL   A 1 694 ? -16.048 44.813  67.406  1.00 109.80 ?  675 VAL   A CG2 1 
ATOM   4007 N N   . ASN   A 1 695 ? -16.753 47.658  70.948  1.00 111.18 ?  676 ASN   A N   1 
ATOM   4008 C CA  . ASN   A 1 695 ? -16.515 48.909  71.660  1.00 110.53 ?  676 ASN   A CA  1 
ATOM   4009 C C   . ASN   A 1 695 ? -15.254 49.597  71.150  1.00 106.35 ?  676 ASN   A C   1 
ATOM   4010 O O   . ASN   A 1 695 ? -15.255 50.806  70.881  1.00 104.93 ?  676 ASN   A O   1 
ATOM   4011 C CB  . ASN   A 1 695 ? -16.420 48.650  73.164  1.00 105.39 ?  676 ASN   A CB  1 
ATOM   4012 C CG  . ASN   A 1 695 ? -17.768 48.411  73.797  1.00 107.00 ?  676 ASN   A CG  1 
ATOM   4013 O OD1 . ASN   A 1 695 ? -17.883 47.692  74.797  1.00 105.43 ?  676 ASN   A OD1 1 
ATOM   4014 N ND2 . ASN   A 1 695 ? -18.803 49.025  73.227  1.00 107.38 ?  676 ASN   A ND2 1 
ATOM   4015 N N   . LEU   A 1 696 ? -14.173 48.833  70.989  1.00 101.86 ?  677 LEU   A N   1 
ATOM   4016 C CA  . LEU   A 1 696 ? -12.875 49.381  70.632  1.00 97.45  ?  677 LEU   A CA  1 
ATOM   4017 C C   . LEU   A 1 696 ? -12.204 48.515  69.575  1.00 95.13  ?  677 LEU   A C   1 
ATOM   4018 O O   . LEU   A 1 696 ? -12.377 47.295  69.545  1.00 99.93  ?  677 LEU   A O   1 
ATOM   4019 C CB  . LEU   A 1 696 ? -11.973 49.500  71.862  1.00 97.83  ?  677 LEU   A CB  1 
ATOM   4020 C CG  . LEU   A 1 696 ? -11.451 48.199  72.468  1.00 99.27  ?  677 LEU   A CG  1 
ATOM   4021 C CD1 . LEU   A 1 696 ? -10.302 48.502  73.409  1.00 107.49 ?  677 LEU   A CD1 1 
ATOM   4022 C CD2 . LEU   A 1 696 ? -12.539 47.422  73.204  1.00 105.67 ?  677 LEU   A CD2 1 
ATOM   4023 N N   . PHE   A 1 697 ? -11.432 49.163  68.705  1.00 89.19  ?  678 PHE   A N   1 
ATOM   4024 C CA  . PHE   A 1 697 ? -10.684 48.461  67.673  1.00 85.31  ?  678 PHE   A CA  1 
ATOM   4025 C C   . PHE   A 1 697 ? -9.386  49.206  67.379  1.00 85.86  ?  678 PHE   A C   1 
ATOM   4026 O O   . PHE   A 1 697 ? -9.329  50.439  67.440  1.00 83.58  ?  678 PHE   A O   1 
ATOM   4027 C CB  . PHE   A 1 697 ? -11.525 48.286  66.402  1.00 78.12  ?  678 PHE   A CB  1 
ATOM   4028 C CG  . PHE   A 1 697 ? -11.841 49.566  65.670  1.00 71.61  ?  678 PHE   A CG  1 
ATOM   4029 C CD1 . PHE   A 1 697 ? -13.104 50.133  65.761  1.00 77.13  ?  678 PHE   A CD1 1 
ATOM   4030 C CD2 . PHE   A 1 697 ? -10.907 50.167  64.838  1.00 72.28  ?  678 PHE   A CD2 1 
ATOM   4031 C CE1 . PHE   A 1 697 ? -13.418 51.303  65.062  1.00 76.44  ?  678 PHE   A CE1 1 
ATOM   4032 C CE2 . PHE   A 1 697 ? -11.212 51.340  64.131  1.00 74.91  ?  678 PHE   A CE2 1 
ATOM   4033 C CZ  . PHE   A 1 697 ? -12.466 51.906  64.243  1.00 74.16  ?  678 PHE   A CZ  1 
ATOM   4034 N N   . GLY   A 1 698 ? -8.340  48.448  67.047  1.00 85.64  ?  679 GLY   A N   1 
ATOM   4035 C CA  . GLY   A 1 698 ? -7.019  49.008  66.867  1.00 81.54  ?  679 GLY   A CA  1 
ATOM   4036 C C   . GLY   A 1 698 ? -6.661  49.285  65.418  1.00 78.52  ?  679 GLY   A C   1 
ATOM   4037 O O   . GLY   A 1 698 ? -7.294  48.785  64.499  1.00 83.79  ?  679 GLY   A O   1 
ATOM   4038 N N   . HIS   A 1 699 ? -5.643  50.121  65.234  1.00 76.67  ?  680 HIS   A N   1 
ATOM   4039 C CA  . HIS   A 1 699 ? -4.998  50.350  63.951  1.00 73.97  ?  680 HIS   A CA  1 
ATOM   4040 C C   . HIS   A 1 699 ? -3.510  50.179  64.165  1.00 82.16  ?  680 HIS   A C   1 
ATOM   4041 O O   . HIS   A 1 699 ? -2.944  50.790  65.077  1.00 77.07  ?  680 HIS   A O   1 
ATOM   4042 C CB  . HIS   A 1 699 ? -5.266  51.743  63.397  1.00 76.30  ?  680 HIS   A CB  1 
ATOM   4043 C CG  . HIS   A 1 699 ? -4.194  52.240  62.471  1.00 84.82  ?  680 HIS   A CG  1 
ATOM   4044 N ND1 . HIS   A 1 699 ? -3.191  53.093  62.881  1.00 87.39  ?  680 HIS   A ND1 1 
ATOM   4045 C CD2 . HIS   A 1 699 ? -3.970  52.010  61.154  1.00 88.53  ?  680 HIS   A CD2 1 
ATOM   4046 C CE1 . HIS   A 1 699 ? -2.403  53.376  61.858  1.00 88.04  ?  680 HIS   A CE1 1 
ATOM   4047 N NE2 . HIS   A 1 699 ? -2.854  52.730  60.798  1.00 90.11  ?  680 HIS   A NE2 1 
ATOM   4048 N N   . VAL   A 1 700 ? -2.879  49.352  63.336  1.00 87.54  ?  681 VAL   A N   1 
ATOM   4049 C CA  . VAL   A 1 700 ? -1.461  49.064  63.491  1.00 83.40  ?  681 VAL   A CA  1 
ATOM   4050 C C   . VAL   A 1 700 ? -0.657  50.074  62.697  1.00 82.54  ?  681 VAL   A C   1 
ATOM   4051 O O   . VAL   A 1 700 ? -0.954  50.343  61.532  1.00 83.83  ?  681 VAL   A O   1 
ATOM   4052 C CB  . VAL   A 1 700 ? -1.138  47.634  63.061  1.00 79.66  ?  681 VAL   A CB  1 
ATOM   4053 C CG1 . VAL   A 1 700 ? 0.357   47.403  63.184  1.00 83.34  ?  681 VAL   A CG1 1 
ATOM   4054 C CG2 . VAL   A 1 700 ? -1.901  46.675  63.944  1.00 79.27  ?  681 VAL   A CG2 1 
ATOM   4055 N N   . GLY   A 1 701 ? 0.337   50.661  63.342  1.00 89.06  ?  682 GLY   A N   1 
ATOM   4056 C CA  . GLY   A 1 701 ? 1.118   51.686  62.696  1.00 92.18  ?  682 GLY   A CA  1 
ATOM   4057 C C   . GLY   A 1 701 ? 2.150   51.105  61.759  1.00 96.90  ?  682 GLY   A C   1 
ATOM   4058 O O   . GLY   A 1 701 ? 2.462   49.912  61.791  1.00 95.21  ?  682 GLY   A O   1 
ATOM   4059 N N   . SER   A 1 702 ? 2.686   51.984  60.915  1.00 95.71  ?  683 SER   A N   1 
ATOM   4060 C CA  . SER   A 1 702 ? 3.726   51.602  59.967  1.00 92.66  ?  683 SER   A CA  1 
ATOM   4061 C C   . SER   A 1 702 ? 5.103   51.485  60.618  1.00 93.28  ?  683 SER   A C   1 
ATOM   4062 O O   . SER   A 1 702 ? 5.919   50.663  60.190  1.00 91.80  ?  683 SER   A O   1 
ATOM   4063 C CB  . SER   A 1 702 ? 3.768   52.627  58.837  1.00 97.21  ?  683 SER   A CB  1 
ATOM   4064 O OG  . SER   A 1 702 ? 3.986   53.929  59.381  1.00 107.82 ?  683 SER   A OG  1 
ATOM   4065 N N   . THR   A 1 703 ? 5.389   52.284  61.641  1.00 96.23  ?  684 THR   A N   1 
ATOM   4066 C CA  . THR   A 1 703 ? 6.729   52.349  62.201  1.00 92.00  ?  684 THR   A CA  1 
ATOM   4067 C C   . THR   A 1 703 ? 6.692   52.115  63.698  1.00 87.83  ?  684 THR   A C   1 
ATOM   4068 O O   . THR   A 1 703 ? 5.651   52.253  64.341  1.00 89.58  ?  684 THR   A O   1 
ATOM   4069 C CB  . THR   A 1 703 ? 7.369   53.700  61.936  1.00 91.08  ?  684 THR   A CB  1 
ATOM   4070 O OG1 . THR   A 1 703 ? 7.066   54.093  60.592  1.00 94.33  ?  684 THR   A OG1 1 
ATOM   4071 C CG2 . THR   A 1 703 ? 8.893   53.631  62.150  1.00 89.41  ?  684 THR   A CG2 1 
ATOM   4072 N N   . THR   A 1 704 ? 7.852   51.733  64.239  1.00 85.37  ?  685 THR   A N   1 
ATOM   4073 C CA  . THR   A 1 704 ? 8.072   51.847  65.672  1.00 78.93  ?  685 THR   A CA  1 
ATOM   4074 C C   . THR   A 1 704 ? 7.855   53.282  66.125  1.00 83.36  ?  685 THR   A C   1 
ATOM   4075 O O   . THR   A 1 704 ? 7.101   53.538  67.074  1.00 79.63  ?  685 THR   A O   1 
ATOM   4076 C CB  . THR   A 1 704 ? 9.479   51.366  66.022  1.00 81.63  ?  685 THR   A CB  1 
ATOM   4077 O OG1 . THR   A 1 704 ? 9.614   49.983  65.672  1.00 87.99  ?  685 THR   A OG1 1 
ATOM   4078 C CG2 . THR   A 1 704 ? 9.755   51.519  67.486  1.00 77.05  ?  685 THR   A CG2 1 
ATOM   4079 N N   . ALA   A 1 705 ? 8.467   54.235  65.413  1.00 86.05  ?  686 ALA   A N   1 
ATOM   4080 C CA  . ALA   A 1 705 ? 8.382   55.638  65.801  1.00 73.31  ?  686 ALA   A CA  1 
ATOM   4081 C C   . ALA   A 1 705 ? 6.937   56.088  65.938  1.00 78.70  ?  686 ALA   A C   1 
ATOM   4082 O O   . ALA   A 1 705 ? 6.552   56.656  66.966  1.00 88.52  ?  686 ALA   A O   1 
ATOM   4083 C CB  . ALA   A 1 705 ? 9.116   56.512  64.793  1.00 80.24  ?  686 ALA   A CB  1 
ATOM   4084 N N   . SER   A 1 706 ? 6.109   55.834  64.924  1.00 74.06  ?  687 SER   A N   1 
ATOM   4085 C CA  . SER   A 1 706 ? 4.725   56.286  64.981  1.00 75.31  ?  687 SER   A CA  1 
ATOM   4086 C C   . SER   A 1 706 ? 3.781   55.238  65.556  1.00 74.67  ?  687 SER   A C   1 
ATOM   4087 O O   . SER   A 1 706 ? 2.603   55.197  65.167  1.00 76.49  ?  687 SER   A O   1 
ATOM   4088 C CB  . SER   A 1 706 ? 4.246   56.714  63.598  1.00 79.00  ?  687 SER   A CB  1 
ATOM   4089 O OG  . SER   A 1 706 ? 4.145   55.573  62.761  1.00 97.35  ?  687 SER   A OG  1 
ATOM   4090 N N   . ARG   A 1 707 ? 4.263   54.417  66.473  1.00 69.45  ?  688 ARG   A N   1 
ATOM   4091 C CA  . ARG   A 1 707 ? 3.377   53.328  66.929  1.00 70.74  ?  688 ARG   A CA  1 
ATOM   4092 C C   . ARG   A 1 707 ? 2.171   53.847  67.690  1.00 76.44  ?  688 ARG   A C   1 
ATOM   4093 O O   . ARG   A 1 707 ? 1.181   53.153  67.717  1.00 72.43  ?  688 ARG   A O   1 
ATOM   4094 C CB  . ARG   A 1 707 ? 4.112   52.264  67.732  1.00 68.18  ?  688 ARG   A CB  1 
ATOM   4095 C CG  . ARG   A 1 707 ? 5.007   52.784  68.832  1.00 65.79  ?  688 ARG   A CG  1 
ATOM   4096 C CD  . ARG   A 1 707 ? 5.305   51.588  69.687  1.00 68.24  ?  688 ARG   A CD  1 
ATOM   4097 N NE  . ARG   A 1 707 ? 6.090   51.967  70.829  1.00 63.90  ?  688 ARG   A NE  1 
ATOM   4098 C CZ  . ARG   A 1 707 ? 7.094   51.275  71.288  1.00 66.26  ?  688 ARG   A CZ  1 
ATOM   4099 N NH1 . ARG   A 1 707 ? 7.444   50.161  70.695  1.00 76.49  ?  688 ARG   A NH1 1 
ATOM   4100 N NH2 . ARG   A 1 707 ? 7.754   51.696  72.331  1.00 64.75  ?  688 ARG   A NH2 1 
ATOM   4101 N N   . GLY   A 1 708 ? 2.257   55.014  68.297  1.00 80.28  ?  689 GLY   A N   1 
ATOM   4102 C CA  . GLY   A 1 708 ? 1.093   55.458  69.073  1.00 72.35  ?  689 GLY   A CA  1 
ATOM   4103 C C   . GLY   A 1 708 ? 0.218   56.427  68.326  1.00 72.66  ?  689 GLY   A C   1 
ATOM   4104 O O   . GLY   A 1 708 ? -0.764  56.844  68.874  1.00 71.18  ?  689 GLY   A O   1 
ATOM   4105 N N   . GLU   A 1 709 ? 0.519   56.711  67.078  1.00 73.22  ?  690 GLU   A N   1 
ATOM   4106 C CA  . GLU   A 1 709 ? -0.296  57.732  66.403  1.00 70.00  ?  690 GLU   A CA  1 
ATOM   4107 C C   . GLU   A 1 709 ? -1.630  57.132  66.001  1.00 73.41  ?  690 GLU   A C   1 
ATOM   4108 O O   . GLU   A 1 709 ? -1.654  56.317  65.124  1.00 81.83  ?  690 GLU   A O   1 
ATOM   4109 C CB  . GLU   A 1 709 ? 0.428   58.130  65.135  1.00 71.26  ?  690 GLU   A CB  1 
ATOM   4110 C CG  . GLU   A 1 709 ? -0.237  59.256  64.423  1.00 74.11  ?  690 GLU   A CG  1 
ATOM   4111 C CD  . GLU   A 1 709 ? 0.734   59.912  63.485  1.00 93.53  ?  690 GLU   A CD  1 
ATOM   4112 O OE1 . GLU   A 1 709 ? 1.895   60.056  63.864  1.00 90.73  ?  690 GLU   A OE1 1 
ATOM   4113 O OE2 . GLU   A 1 709 ? 0.322   60.248  62.386  1.00 103.74 ?  690 GLU   A OE2 1 
ATOM   4114 N N   . LEU   A 1 710 ? -2.685  57.555  66.673  1.00 72.61  ?  691 LEU   A N   1 
ATOM   4115 C CA  . LEU   A 1 710 ? -4.062  57.112  66.393  1.00 71.77  ?  691 LEU   A CA  1 
ATOM   4116 C C   . LEU   A 1 710 ? -4.124  55.598  66.342  1.00 71.80  ?  691 LEU   A C   1 
ATOM   4117 O O   . LEU   A 1 710 ? -4.717  55.102  65.441  1.00 79.36  ?  691 LEU   A O   1 
ATOM   4118 C CB  . LEU   A 1 710 ? -4.516  57.759  65.094  1.00 71.19  ?  691 LEU   A CB  1 
ATOM   4119 C CG  . LEU   A 1 710 ? -4.673  59.263  65.213  1.00 73.19  ?  691 LEU   A CG  1 
ATOM   4120 C CD1 . LEU   A 1 710 ? -4.177  59.956  63.975  1.00 74.70  ?  691 LEU   A CD1 1 
ATOM   4121 C CD2 . LEU   A 1 710 ? -6.116  59.617  65.468  1.00 75.18  ?  691 LEU   A CD2 1 
ATOM   4122 N N   . PHE   A 1 711 ? -3.594  54.923  67.343  1.00 67.46  ?  692 PHE   A N   1 
ATOM   4123 C CA  . PHE   A 1 711 ? -3.529  53.450  67.317  1.00 67.96  ?  692 PHE   A CA  1 
ATOM   4124 C C   . PHE   A 1 711 ? -4.742  52.773  67.944  1.00 73.17  ?  692 PHE   A C   1 
ATOM   4125 O O   . PHE   A 1 711 ? -4.730  51.565  67.994  1.00 75.30  ?  692 PHE   A O   1 
ATOM   4126 C CB  . PHE   A 1 711 ? -2.328  53.013  68.132  1.00 70.28  ?  692 PHE   A CB  1 
ATOM   4127 C CG  . PHE   A 1 711 ? -2.624  52.949  69.598  1.00 70.15  ?  692 PHE   A CG  1 
ATOM   4128 C CD1 . PHE   A 1 711 ? -2.814  54.096  70.321  1.00 70.98  ?  692 PHE   A CD1 1 
ATOM   4129 C CD2 . PHE   A 1 711 ? -2.729  51.743  70.244  1.00 69.99  ?  692 PHE   A CD2 1 
ATOM   4130 C CE1 . PHE   A 1 711 ? -3.097  54.034  71.665  1.00 70.85  ?  692 PHE   A CE1 1 
ATOM   4131 C CE2 . PHE   A 1 711 ? -3.004  51.682  71.592  1.00 70.57  ?  692 PHE   A CE2 1 
ATOM   4132 C CZ  . PHE   A 1 711 ? -3.191  52.830  72.295  1.00 68.55  ?  692 PHE   A CZ  1 
ATOM   4133 N N   . LEU   A 1 712 ? -5.732  53.496  68.433  1.00 74.12  ?  693 LEU   A N   1 
ATOM   4134 C CA  . LEU   A 1 712 ? -6.864  52.781  69.064  1.00 70.25  ?  693 LEU   A CA  1 
ATOM   4135 C C   . LEU   A 1 712 ? -8.099  53.655  68.963  1.00 75.32  ?  693 LEU   A C   1 
ATOM   4136 O O   . LEU   A 1 712 ? -7.943  54.844  68.970  1.00 77.41  ?  693 LEU   A O   1 
ATOM   4137 C CB  . LEU   A 1 712 ? -6.500  52.499  70.512  1.00 65.32  ?  693 LEU   A CB  1 
ATOM   4138 C CG  . LEU   A 1 712 ? -7.580  51.828  71.335  1.00 77.48  ?  693 LEU   A CG  1 
ATOM   4139 C CD1 . LEU   A 1 712 ? -8.132  50.635  70.613  1.00 85.76  ?  693 LEU   A CD1 1 
ATOM   4140 C CD2 . LEU   A 1 712 ? -7.019  51.394  72.661  1.00 76.12  ?  693 LEU   A CD2 1 
ATOM   4141 N N   . PHE   A 1 713 ? -9.264  53.049  68.774  1.00 75.31  ?  694 PHE   A N   1 
ATOM   4142 C CA  . PHE   A 1 713 ? -10.513 53.759  68.550  1.00 77.81  ?  694 PHE   A CA  1 
ATOM   4143 C C   . PHE   A 1 713 ? -11.584 53.231  69.492  1.00 88.31  ?  694 PHE   A C   1 
ATOM   4144 O O   . PHE   A 1 713 ? -11.675 52.022  69.738  1.00 86.65  ?  694 PHE   A O   1 
ATOM   4145 C CB  . PHE   A 1 713 ? -10.995 53.629  67.103  1.00 69.10  ?  694 PHE   A CB  1 
ATOM   4146 C CG  . PHE   A 1 713 ? -10.201 54.434  66.112  1.00 69.64  ?  694 PHE   A CG  1 
ATOM   4147 C CD1 . PHE   A 1 713 ? -8.927  54.030  65.723  1.00 68.19  ?  694 PHE   A CD1 1 
ATOM   4148 C CD2 . PHE   A 1 713 ? -10.737 55.597  65.548  1.00 71.10  ?  694 PHE   A CD2 1 
ATOM   4149 C CE1 . PHE   A 1 713 ? -8.190  54.779  64.790  1.00 70.83  ?  694 PHE   A CE1 1 
ATOM   4150 C CE2 . PHE   A 1 713 ? -10.009 56.352  64.609  1.00 68.12  ?  694 PHE   A CE2 1 
ATOM   4151 C CZ  . PHE   A 1 713 ? -8.737  55.946  64.233  1.00 68.57  ?  694 PHE   A CZ  1 
ATOM   4152 N N   . TRP   A 1 714 ? -12.391 54.161  70.000  1.00 90.24  ?  695 TRP   A N   1 
ATOM   4153 C CA  . TRP   A 1 714 ? -13.426 53.940  71.010  1.00 92.93  ?  695 TRP   A CA  1 
ATOM   4154 C C   . TRP   A 1 714 ? -14.792 54.396  70.511  1.00 95.96  ?  695 TRP   A C   1 
ATOM   4155 O O   . TRP   A 1 714 ? -14.958 55.539  70.071  1.00 92.45  ?  695 TRP   A O   1 
ATOM   4156 C CB  . TRP   A 1 714 ? -13.034 54.634  72.329  1.00 96.04  ?  695 TRP   A CB  1 
ATOM   4157 C CG  . TRP   A 1 714 ? -12.352 53.813  73.461  1.00 99.49  ?  695 TRP   A CG  1 
ATOM   4158 C CD1 . TRP   A 1 714 ? -12.485 52.479  73.690  1.00 107.64 ?  695 TRP   A CD1 1 
ATOM   4159 C CD2 . TRP   A 1 714 ? -11.356 54.274  74.411  1.00 103.16 ?  695 TRP   A CD2 1 
ATOM   4160 N NE1 . TRP   A 1 714 ? -11.746 52.104  74.796  1.00 113.87 ?  695 TRP   A NE1 1 
ATOM   4161 C CE2 . TRP   A 1 714 ? -11.020 53.177  75.233  1.00 108.63 ?  695 TRP   A CE2 1 
ATOM   4162 C CE3 . TRP   A 1 714 ? -10.742 55.509  74.659  1.00 101.99 ?  695 TRP   A CE3 1 
ATOM   4163 C CZ2 . TRP   A 1 714 ? -10.097 53.278  76.283  1.00 115.72 ?  695 TRP   A CZ2 1 
ATOM   4164 C CZ3 . TRP   A 1 714 ? -9.820  55.612  75.708  1.00 95.40  ?  695 TRP   A CZ3 1 
ATOM   4165 C CH2 . TRP   A 1 714 ? -9.517  54.505  76.508  1.00 109.64 ?  695 TRP   A CH2 1 
ATOM   4166 N N   . ASN   A 1 715 ? -15.732 53.462  70.512  1.00 97.02  ?  696 ASN   A N   1 
ATOM   4167 C CA  . ASN   A 1 715 ? -17.175 53.671  70.624  1.00 106.34 ?  696 ASN   A CA  1 
ATOM   4168 C C   . ASN   A 1 715 ? -17.666 52.966  71.876  1.00 112.96 ?  696 ASN   A C   1 
ATOM   4169 O O   . ASN   A 1 715 ? -17.786 51.735  71.913  1.00 114.88 ?  696 ASN   A O   1 
ATOM   4170 C CB  . ASN   A 1 715 ? -17.918 53.293  69.327  1.00 110.61 ?  696 ASN   A CB  1 
ATOM   4171 C CG  . ASN   A 1 715 ? -19.464 53.017  69.514  1.00 118.40 ?  696 ASN   A CG  1 
ATOM   4172 O OD1 . ASN   A 1 715 ? -19.941 52.542  70.558  1.00 128.34 ?  696 ASN   A OD1 1 
ATOM   4173 N ND2 . ASN   A 1 715 ? -20.243 53.549  68.585  1.00 116.54 ?  696 ASN   A ND2 1 
ATOM   4174 N N   . LEU   A 1 716 ? -17.987 53.802  72.852  1.00 113.52 ?  697 LEU   A N   1 
ATOM   4175 C CA  . LEU   A 1 716 ? -18.510 53.405  74.174  1.00 113.46 ?  697 LEU   A CA  1 
ATOM   4176 C C   . LEU   A 1 716 ? -19.866 54.087  74.325  1.00 116.32 ?  697 LEU   A C   1 
ATOM   4177 O O   . LEU   A 1 716 ? -20.747 53.544  74.997  1.00 113.70 ?  697 LEU   A O   1 
ATOM   4178 C CB  . LEU   A 1 716 ? -17.528 53.939  75.214  1.00 106.69 ?  697 LEU   A CB  1 
ATOM   4179 C CG  . LEU   A 1 716 ? -16.302 53.072  75.483  1.00 105.69 ?  697 LEU   A CG  1 
ATOM   4180 C CD1 . LEU   A 1 716 ? -16.688 51.618  75.629  1.00 102.18 ?  697 LEU   A CD1 1 
ATOM   4181 C CD2 . LEU   A 1 716 ? -15.246 53.233  74.410  1.00 100.24 ?  697 LEU   A CD2 1 
ATOM   4182 N N   . TYR   A 1 717 ? -19.991 55.258  73.711  1.00 117.31 ?  698 TYR   A N   1 
ATOM   4183 C CA  . TYR   A 1 717 ? -21.226 56.066  73.766  1.00 117.96 ?  698 TYR   A CA  1 
ATOM   4184 C C   . TYR   A 1 717 ? -22.281 55.475  72.838  1.00 122.89 ?  698 TYR   A C   1 
ATOM   4185 O O   . TYR   A 1 717 ? -21.937 54.864  71.824  1.00 123.13 ?  698 TYR   A O   1 
ATOM   4186 C CB  . TYR   A 1 717 ? -20.889 57.529  73.491  1.00 117.27 ?  698 TYR   A CB  1 
ATOM   4187 C CG  . TYR   A 1 717 ? -19.766 58.056  74.346  1.00 116.58 ?  698 TYR   A CG  1 
ATOM   4188 C CD1 . TYR   A 1 717 ? -18.517 58.312  73.815  1.00 109.01 ?  698 TYR   A CD1 1 
ATOM   4189 C CD2 . TYR   A 1 717 ? -19.948 58.281  75.696  1.00 112.86 ?  698 TYR   A CD2 1 
ATOM   4190 C CE1 . TYR   A 1 717 ? -17.485 58.786  74.600  1.00 102.62 ?  698 TYR   A CE1 1 
ATOM   4191 C CE2 . TYR   A 1 717 ? -18.925 58.750  76.496  1.00 105.95 ?  698 TYR   A CE2 1 
ATOM   4192 C CZ  . TYR   A 1 717 ? -17.690 59.007  75.945  1.00 102.64 ?  698 TYR   A CZ  1 
ATOM   4193 O OH  . TYR   A 1 717 ? -16.684 59.464  76.734  1.00 91.30  ?  698 TYR   A OH  1 
ATOM   4194 N N   . LYS   A 1 718 ? -23.538 55.670  73.218  1.00 124.50 ?  699 LYS   A N   1 
ATOM   4195 C CA  . LYS   A 1 718 ? -24.718 55.186  72.466  1.00 127.58 ?  699 LYS   A CA  1 
ATOM   4196 C C   . LYS   A 1 718 ? -24.765 55.867  71.103  1.00 125.18 ?  699 LYS   A C   1 
ATOM   4197 O O   . LYS   A 1 718 ? -25.051 55.193  70.116  1.00 117.33 ?  699 LYS   A O   1 
ATOM   4198 C CB  . LYS   A 1 718 ? -25.968 55.629  73.223  1.00 121.89 ?  699 LYS   A CB  1 
ATOM   4199 C CG  . LYS   A 1 718 ? -25.789 56.890  74.053  1.00 125.32 ?  699 LYS   A CG  1 
ATOM   4200 C CD  . LYS   A 1 718 ? -26.250 56.716  75.482  1.00 129.33 ?  699 LYS   A CD  1 
ATOM   4201 C CE  . LYS   A 1 718 ? -26.427 58.028  76.210  1.00 125.60 ?  699 LYS   A CE  1 
ATOM   4202 N NZ  . LYS   A 1 718 ? -27.081 57.847  77.524  1.00 127.20 ?  699 LYS   A NZ  1 
ATOM   4203 N N   . ALA   A 1 719 ? -24.434 57.156  71.080  1.00 120.77 ?  700 ALA   A N   1 
ATOM   4204 C CA  . ALA   A 1 719 ? -24.475 58.019  69.881  1.00 117.72 ?  700 ALA   A CA  1 
ATOM   4205 C C   . ALA   A 1 719 ? -23.321 57.732  68.924  1.00 113.14 ?  700 ALA   A C   1 
ATOM   4206 O O   . ALA   A 1 719 ? -22.399 57.006  69.272  1.00 114.76 ?  700 ALA   A O   1 
ATOM   4207 C CB  . ALA   A 1 719 ? -24.474 59.459  70.302  1.00 115.98 ?  700 ALA   A CB  1 
ATOM   4208 N N   . PRO   A 1 720 ? -23.303 58.351  67.737  1.00 107.36 ?  701 PRO   A N   1 
ATOM   4209 C CA  . PRO   A 1 720 ? -22.290 58.083  66.748  1.00 108.48 ?  701 PRO   A CA  1 
ATOM   4210 C C   . PRO   A 1 720 ? -21.048 58.895  67.096  1.00 107.05 ?  701 PRO   A C   1 
ATOM   4211 O O   . PRO   A 1 720 ? -20.811 59.919  66.508  1.00 99.19  ?  701 PRO   A O   1 
ATOM   4212 C CB  . PRO   A 1 720 ? -22.924 58.727  65.526  1.00 113.81 ?  701 PRO   A CB  1 
ATOM   4213 C CG  . PRO   A 1 720 ? -23.497 59.965  66.103  1.00 113.66 ?  701 PRO   A CG  1 
ATOM   4214 C CD  . PRO   A 1 720 ? -24.176 59.430  67.341  1.00 112.74 ?  701 PRO   A CD  1 
ATOM   4215 N N   . ILE   A 1 721 ? -20.277 58.378  68.044  1.00 108.13 ?  702 ILE   A N   1 
ATOM   4216 C CA  . ILE   A 1 721 ? -19.046 59.084  68.464  1.00 102.86 ?  702 ILE   A CA  1 
ATOM   4217 C C   . ILE   A 1 721 ? -17.914 58.078  68.545  1.00 96.69  ?  702 ILE   A C   1 
ATOM   4218 O O   . ILE   A 1 721 ? -17.990 57.170  69.347  1.00 99.55  ?  702 ILE   A O   1 
ATOM   4219 C CB  . ILE   A 1 721 ? -19.254 59.776  69.820  1.00 104.74 ?  702 ILE   A CB  1 
ATOM   4220 C CG1 . ILE   A 1 721 ? -19.589 61.257  69.659  1.00 104.98 ?  702 ILE   A CG1 1 
ATOM   4221 C CG2 . ILE   A 1 721 ? -18.038 59.590  70.696  1.00 100.84 ?  702 ILE   A CG2 1 
ATOM   4222 C CD1 . ILE   A 1 721 ? -18.805 61.944  68.574  1.00 101.69 ?  702 ILE   A CD1 1 
ATOM   4223 N N   . LEU   A 1 722 ? -16.981 58.207  67.628  1.00 91.95  ?  703 LEU   A N   1 
ATOM   4224 C CA  . LEU   A 1 722 ? -15.705 57.508  67.663  1.00 98.57  ?  703 LEU   A CA  1 
ATOM   4225 C C   . LEU   A 1 722 ? -14.609 58.412  68.206  1.00 97.38  ?  703 LEU   A C   1 
ATOM   4226 O O   . LEU   A 1 722 ? -14.488 59.582  67.820  1.00 88.40  ?  703 LEU   A O   1 
ATOM   4227 C CB  . LEU   A 1 722 ? -15.261 56.963  66.303  1.00 95.55  ?  703 LEU   A CB  1 
ATOM   4228 C CG  . LEU   A 1 722 ? -15.808 55.592  65.918  1.00 95.96  ?  703 LEU   A CG  1 
ATOM   4229 C CD1 . LEU   A 1 722 ? -15.206 55.167  64.589  1.00 98.64  ?  703 LEU   A CD1 1 
ATOM   4230 C CD2 . LEU   A 1 722 ? -15.521 54.570  67.019  1.00 92.16  ?  703 LEU   A CD2 1 
ATOM   4231 N N   . LEU   A 1 723 ? -13.771 57.819  69.056  1.00 93.28  ?  704 LEU   A N   1 
ATOM   4232 C CA  . LEU   A 1 723 ? -12.805 58.529  69.877  1.00 89.25  ?  704 LEU   A CA  1 
ATOM   4233 C C   . LEU   A 1 723 ? -11.454 57.836  69.708  1.00 84.68  ?  704 LEU   A C   1 
ATOM   4234 O O   . LEU   A 1 723 ? -11.356 56.621  69.910  1.00 84.79  ?  704 LEU   A O   1 
ATOM   4235 C CB  . LEU   A 1 723 ? -13.326 58.523  71.320  1.00 87.89  ?  704 LEU   A CB  1 
ATOM   4236 C CG  . LEU   A 1 723 ? -12.788 59.296  72.508  1.00 89.81  ?  704 LEU   A CG  1 
ATOM   4237 C CD1 . LEU   A 1 723 ? -13.944 59.593  73.440  1.00 88.42  ?  704 LEU   A CD1 1 
ATOM   4238 C CD2 . LEU   A 1 723 ? -11.794 58.420  73.204  1.00 93.76  ?  704 LEU   A CD2 1 
ATOM   4239 N N   . ALA   A 1 724 ? -10.430 58.596  69.298  1.00 79.52  ?  705 ALA   A N   1 
ATOM   4240 C CA  . ALA   A 1 724 ? -9.146  58.052  68.842  1.00 77.12  ?  705 ALA   A CA  1 
ATOM   4241 C C   . ALA   A 1 724 ? -7.977  58.499  69.721  1.00 79.53  ?  705 ALA   A C   1 
ATOM   4242 O O   . ALA   A 1 724 ? -7.805  59.700  69.967  1.00 79.12  ?  705 ALA   A O   1 
ATOM   4243 C CB  . ALA   A 1 724 ? -8.872  58.480  67.400  1.00 73.72  ?  705 ALA   A CB  1 
ATOM   4244 N N   . LEU   A 1 725 ? -7.125  57.550  70.119  1.00 70.58  ?  706 LEU   A N   1 
ATOM   4245 C CA  . LEU   A 1 725 ? -6.044  57.817  71.062  1.00 69.32  ?  706 LEU   A CA  1 
ATOM   4246 C C   . LEU   A 1 725 ? -4.713  58.128  70.389  1.00 71.06  ?  706 LEU   A C   1 
ATOM   4247 O O   . LEU   A 1 725 ? -4.431  57.667  69.286  1.00 76.07  ?  706 LEU   A O   1 
ATOM   4248 C CB  . LEU   A 1 725 ? -5.839  56.647  72.013  1.00 66.76  ?  706 LEU   A CB  1 
ATOM   4249 C CG  . LEU   A 1 725 ? -6.876  56.682  73.124  1.00 82.85  ?  706 LEU   A CG  1 
ATOM   4250 C CD1 . LEU   A 1 725 ? -8.217  56.243  72.569  1.00 88.90  ?  706 LEU   A CD1 1 
ATOM   4251 C CD2 . LEU   A 1 725 ? -6.452  55.843  74.322  1.00 79.97  ?  706 LEU   A CD2 1 
ATOM   4252 N N   . VAL   A 1 726 ? -3.881  58.901  71.085  1.00 68.86  ?  707 VAL   A N   1 
ATOM   4253 C CA  . VAL   A 1 726 ? -2.530  59.240  70.639  1.00 67.46  ?  707 VAL   A CA  1 
ATOM   4254 C C   . VAL   A 1 726 ? -1.579  59.067  71.817  1.00 67.97  ?  707 VAL   A C   1 
ATOM   4255 O O   . VAL   A 1 726 ? -1.530  59.930  72.700  1.00 68.75  ?  707 VAL   A O   1 
ATOM   4256 C CB  . VAL   A 1 726 ? -2.450  60.668  70.098  1.00 62.58  ?  707 VAL   A CB  1 
ATOM   4257 C CG1 . VAL   A 1 726 ? -1.036  60.974  69.602  1.00 62.76  ?  707 VAL   A CG1 1 
ATOM   4258 C CG2 . VAL   A 1 726 ? -3.476  60.871  69.005  1.00 65.91  ?  707 VAL   A CG2 1 
ATOM   4259 N N   . ALA   A 1 727 ? -0.799  57.981  71.819  1.00 64.96  ?  708 ALA   A N   1 
ATOM   4260 C CA  . ALA   A 1 727 ? 0.036   57.612  72.958  1.00 63.89  ?  708 ALA   A CA  1 
ATOM   4261 C C   . ALA   A 1 727 ? 1.518   57.801  72.648  1.00 56.72  ?  708 ALA   A C   1 
ATOM   4262 O O   . ALA   A 1 727 ? 1.901   58.287  71.588  1.00 58.58  ?  708 ALA   A O   1 
ATOM   4263 C CB  . ALA   A 1 727 ? -0.233  56.161  73.369  1.00 70.81  ?  708 ALA   A CB  1 
ATOM   4264 N N   . GLY   A 1 728 ? 2.352   57.402  73.602  1.00 59.20  ?  709 GLY   A N   1 
ATOM   4265 C CA  . GLY   A 1 728 ? 3.792   57.282  73.477  1.00 56.16  ?  709 GLY   A CA  1 
ATOM   4266 C C   . GLY   A 1 728 ? 4.425   58.534  72.920  1.00 56.43  ?  709 GLY   A C   1 
ATOM   4267 O O   . GLY   A 1 728 ? 3.941   59.646  73.132  1.00 65.66  ?  709 GLY   A O   1 
ATOM   4268 N N   . GLU   A 1 729 ? 5.517   58.358  72.168  1.00 59.92  ?  710 GLU   A N   1 
ATOM   4269 C CA  . GLU   A 1 729 ? 6.205   59.524  71.629  1.00 56.78  ?  710 GLU   A CA  1 
ATOM   4270 C C   . GLU   A 1 729 ? 5.324   60.313  70.681  1.00 57.44  ?  710 GLU   A C   1 
ATOM   4271 O O   . GLU   A 1 729 ? 5.598   61.493  70.445  1.00 61.69  ?  710 GLU   A O   1 
ATOM   4272 C CB  . GLU   A 1 729 ? 7.505   59.135  70.928  1.00 48.80  ?  710 GLU   A CB  1 
ATOM   4273 C CG  . GLU   A 1 729 ? 8.410   58.233  71.753  1.00 58.83  ?  710 GLU   A CG  1 
ATOM   4274 C CD  . GLU   A 1 729 ? 9.452   59.018  72.546  1.00 70.20  ?  710 GLU   A CD  1 
ATOM   4275 O OE1 . GLU   A 1 729 ? 9.312   60.257  72.629  1.00 76.99  ?  710 GLU   A OE1 1 
ATOM   4276 O OE2 . GLU   A 1 729 ? 10.404  58.416  73.095  1.00 73.66  ?  710 GLU   A OE2 1 
ATOM   4277 N N   . ALA   A 1 730 ? 4.261   59.703  70.156  1.00 57.51  ?  711 ALA   A N   1 
ATOM   4278 C CA  . ALA   A 1 730 ? 3.392   60.413  69.223  1.00 62.01  ?  711 ALA   A CA  1 
ATOM   4279 C C   . ALA   A 1 730 ? 2.661   61.563  69.910  1.00 67.83  ?  711 ALA   A C   1 
ATOM   4280 O O   . ALA   A 1 730 ? 2.474   62.634  69.312  1.00 64.93  ?  711 ALA   A O   1 
ATOM   4281 C CB  . ALA   A 1 730 ? 2.394   59.444  68.588  1.00 58.63  ?  711 ALA   A CB  1 
ATOM   4282 N N   . ALA   A 1 731 ? 2.248   61.355  71.167  1.00 66.61  ?  712 ALA   A N   1 
ATOM   4283 C CA  . ALA   A 1 731 ? 1.446   62.341  71.884  1.00 65.53  ?  712 ALA   A CA  1 
ATOM   4284 C C   . ALA   A 1 731 ? 2.106   63.711  71.857  1.00 68.34  ?  712 ALA   A C   1 
ATOM   4285 O O   . ALA   A 1 731 ? 1.512   64.703  71.410  1.00 63.19  ?  712 ALA   A O   1 
ATOM   4286 C CB  . ALA   A 1 731 ? 1.236   61.882  73.324  1.00 59.65  ?  712 ALA   A CB  1 
ATOM   4287 N N   . GLY   A 1 732 ? 3.357   63.768  72.323  1.00 68.55  ?  713 GLY   A N   1 
ATOM   4288 C CA  . GLY   A 1 732 ? 4.065   65.031  72.382  1.00 68.63  ?  713 GLY   A CA  1 
ATOM   4289 C C   . GLY   A 1 732 ? 4.183   65.725  71.045  1.00 65.74  ?  713 GLY   A C   1 
ATOM   4290 O O   . GLY   A 1 732 ? 4.176   66.957  70.986  1.00 74.30  ?  713 GLY   A O   1 
ATOM   4291 N N   . ILE   A 1 733 ? 4.259   64.956  69.958  1.00 70.50  ?  714 ILE   A N   1 
ATOM   4292 C CA  . ILE   A 1 733 ? 4.505   65.523  68.629  1.00 71.48  ?  714 ILE   A CA  1 
ATOM   4293 C C   . ILE   A 1 733 ? 3.211   65.909  67.919  1.00 67.49  ?  714 ILE   A C   1 
ATOM   4294 O O   . ILE   A 1 733 ? 3.167   66.922  67.226  1.00 71.38  ?  714 ILE   A O   1 
ATOM   4295 C CB  . ILE   A 1 733 ? 5.347   64.549  67.780  1.00 68.88  ?  714 ILE   A CB  1 
ATOM   4296 C CG1 . ILE   A 1 733 ? 6.622   64.174  68.537  1.00 69.21  ?  714 ILE   A CG1 1 
ATOM   4297 C CG2 . ILE   A 1 733 ? 5.766   65.215  66.505  1.00 68.19  ?  714 ILE   A CG2 1 
ATOM   4298 C CD1 . ILE   A 1 733 ? 7.360   62.995  67.980  1.00 62.74  ?  714 ILE   A CD1 1 
ATOM   4299 N N   . MET   A 1 734 ? 2.130   65.144  68.079  1.00 69.97  ?  715 MET   A N   1 
ATOM   4300 C CA  . MET   A 1 734 ? 0.868   65.538  67.462  1.00 66.73  ?  715 MET   A CA  1 
ATOM   4301 C C   . MET   A 1 734 ? 0.336   66.854  68.003  1.00 73.50  ?  715 MET   A C   1 
ATOM   4302 O O   . MET   A 1 734 ? -0.553  67.443  67.381  1.00 80.04  ?  715 MET   A O   1 
ATOM   4303 C CB  . MET   A 1 734 ? -0.194  64.459  67.655  1.00 70.91  ?  715 MET   A CB  1 
ATOM   4304 C CG  . MET   A 1 734 ? 0.062   63.171  66.881  1.00 82.77  ?  715 MET   A CG  1 
ATOM   4305 S SD  . MET   A 1 734 ? 0.140   63.396  65.085  1.00 110.26 ?  715 MET   A SD  1 
ATOM   4306 C CE  . MET   A 1 734 ? -1.370  62.564  64.575  1.00 96.24  ?  715 MET   A CE  1 
ATOM   4307 N N   . GLU   A 1 735 ? 0.838   67.336  69.145  1.00 76.85  ?  716 GLU   A N   1 
ATOM   4308 C CA  . GLU   A 1 735 ? 0.303   68.587  69.678  1.00 77.72  ?  716 GLU   A CA  1 
ATOM   4309 C C   . GLU   A 1 735 ? 0.710   69.797  68.840  1.00 78.50  ?  716 GLU   A C   1 
ATOM   4310 O O   . GLU   A 1 735 ? 0.025   70.825  68.901  1.00 78.01  ?  716 GLU   A O   1 
ATOM   4311 C CB  . GLU   A 1 735 ? 0.741   68.794  71.126  1.00 69.56  ?  716 GLU   A CB  1 
ATOM   4312 C CG  . GLU   A 1 735 ? 0.481   67.653  72.071  1.00 74.40  ?  716 GLU   A CG  1 
ATOM   4313 C CD  . GLU   A 1 735 ? 0.061   68.137  73.468  1.00 74.83  ?  716 GLU   A CD  1 
ATOM   4314 O OE1 . GLU   A 1 735 ? 0.387   69.304  73.812  1.00 73.24  ?  716 GLU   A OE1 1 
ATOM   4315 O OE2 . GLU   A 1 735 ? -0.516  67.330  74.248  1.00 68.28  ?  716 GLU   A OE2 1 
ATOM   4316 N N   . ASN   A 1 736 ? 1.816   69.697  68.092  1.00 75.95  ?  717 ASN   A N   1 
ATOM   4317 C CA  . ASN   A 1 736 ? 2.267   70.692  67.123  1.00 80.90  ?  717 ASN   A CA  1 
ATOM   4318 C C   . ASN   A 1 736 ? 1.699   70.507  65.728  1.00 85.01  ?  717 ASN   A C   1 
ATOM   4319 O O   . ASN   A 1 736 ? 2.298   70.989  64.762  1.00 94.71  ?  717 ASN   A O   1 
ATOM   4320 C CB  . ASN   A 1 736 ? 3.793   70.700  67.042  1.00 81.07  ?  717 ASN   A CB  1 
ATOM   4321 C CG  . ASN   A 1 736 ? 4.425   71.416  68.187  1.00 88.75  ?  717 ASN   A CG  1 
ATOM   4322 O OD1 . ASN   A 1 736 ? 5.021   70.812  69.069  1.00 86.02  ?  717 ASN   A OD1 1 
ATOM   4323 N ND2 . ASN   A 1 736 ? 4.405   72.751  68.110  1.00 104.75 ?  717 ASN   A ND2 1 
ATOM   4324 N N   . ILE   A 1 737 ? 0.568   69.844  65.596  1.00 80.66  ?  718 ILE   A N   1 
ATOM   4325 C CA  . ILE   A 1 737 ? -0.056  69.620  64.305  1.00 87.95  ?  718 ILE   A CA  1 
ATOM   4326 C C   . ILE   A 1 737 ? -1.489  70.127  64.431  1.00 89.56  ?  718 ILE   A C   1 
ATOM   4327 O O   . ILE   A 1 737 ? -2.123  69.926  65.472  1.00 87.13  ?  718 ILE   A O   1 
ATOM   4328 C CB  . ILE   A 1 737 ? 0.012   68.116  63.910  1.00 85.62  ?  718 ILE   A CB  1 
ATOM   4329 C CG1 . ILE   A 1 737 ? 1.454   67.578  63.866  1.00 83.33  ?  718 ILE   A CG1 1 
ATOM   4330 C CG2 . ILE   A 1 737 ? -0.584  67.881  62.596  1.00 83.32  ?  718 ILE   A CG2 1 
ATOM   4331 C CD1 . ILE   A 1 737 ? 2.382   68.251  62.864  1.00 91.59  ?  718 ILE   A CD1 1 
ATOM   4332 N N   . SER   A 1 738 ? -1.993  70.732  63.367  1.00 89.59  ?  719 SER   A N   1 
ATOM   4333 C CA  . SER   A 1 738 ? -3.350  71.318  63.378  1.00 91.74  ?  719 SER   A CA  1 
ATOM   4334 C C   . SER   A 1 738 ? -4.427  70.249  63.528  1.00 90.87  ?  719 SER   A C   1 
ATOM   4335 O O   . SER   A 1 738 ? -4.228  69.135  63.117  1.00 87.27  ?  719 SER   A O   1 
ATOM   4336 C CB  . SER   A 1 738 ? -3.561  72.133  62.148  1.00 99.63  ?  719 SER   A CB  1 
ATOM   4337 O OG  . SER   A 1 738 ? -4.333  71.430  61.191  1.00 104.46 ?  719 SER   A OG  1 
ATOM   4338 N N   . ASP   A 1 739 ? -5.591  70.643  64.007  1.00 92.59  ?  720 ASP   A N   1 
ATOM   4339 C CA  . ASP   A 1 739 ? -6.694  69.678  64.186  1.00 92.53  ?  720 ASP   A CA  1 
ATOM   4340 C C   . ASP   A 1 739 ? -7.115  69.115  62.832  1.00 100.17 ?  720 ASP   A C   1 
ATOM   4341 O O   . ASP   A 1 739 ? -7.418  67.925  62.749  1.00 94.66  ?  720 ASP   A O   1 
ATOM   4342 C CB  . ASP   A 1 739 ? -7.858  70.374  64.873  1.00 97.79  ?  720 ASP   A CB  1 
ATOM   4343 C CG  . ASP   A 1 739 ? -7.402  71.295  65.980  1.00 103.33 ?  720 ASP   A CG  1 
ATOM   4344 O OD1 . ASP   A 1 739 ? -6.660  70.830  66.836  1.00 105.57 ?  720 ASP   A OD1 1 
ATOM   4345 O OD2 . ASP   A 1 739 ? -7.792  72.463  65.966  1.00 104.29 ?  720 ASP   A OD2 1 
ATOM   4346 N N   . ASP   A 1 740 ? -7.155  69.958  61.808  1.00 103.57 ?  721 ASP   A N   1 
ATOM   4347 C CA  . ASP   A 1 740 ? -7.589  69.486  60.473  1.00 102.17 ?  721 ASP   A CA  1 
ATOM   4348 C C   . ASP   A 1 740 ? -6.620  68.420  59.981  1.00 98.54  ?  721 ASP   A C   1 
ATOM   4349 O O   . ASP   A 1 740 ? -7.066  67.428  59.438  1.00 97.39  ?  721 ASP   A O   1 
ATOM   4350 C CB  . ASP   A 1 740 ? -7.769  70.664  59.526  1.00 103.91 ?  721 ASP   A CB  1 
ATOM   4351 C CG  . ASP   A 1 740 ? -8.735  71.677  60.099  1.00 116.55 ?  721 ASP   A CG  1 
ATOM   4352 O OD1 . ASP   A 1 740 ? -8.319  72.827  60.298  1.00 124.64 ?  721 ASP   A OD1 1 
ATOM   4353 O OD2 . ASP   A 1 740 ? -9.883  71.295  60.366  1.00 115.44 ?  721 ASP   A OD2 1 
ATOM   4354 N N   . VAL   A 1 741 ? -5.326  68.608  60.167  1.00 90.99  ?  722 VAL   A N   1 
ATOM   4355 C CA  . VAL   A 1 741 ? -4.442  67.512  59.709  1.00 85.02  ?  722 VAL   A CA  1 
ATOM   4356 C C   . VAL   A 1 741 ? -4.731  66.277  60.553  1.00 85.56  ?  722 VAL   A C   1 
ATOM   4357 O O   . VAL   A 1 741 ? -4.909  65.217  59.999  1.00 92.88  ?  722 VAL   A O   1 
ATOM   4358 C CB  . VAL   A 1 741 ? -2.975  67.916  59.835  1.00 87.72  ?  722 VAL   A CB  1 
ATOM   4359 C CG1 . VAL   A 1 741 ? -2.071  66.749  59.531  1.00 80.74  ?  722 VAL   A CG1 1 
ATOM   4360 C CG2 . VAL   A 1 741 ? -2.657  69.088  58.941  1.00 82.51  ?  722 VAL   A CG2 1 
ATOM   4361 N N   . ILE   A 1 742 ? -4.865  66.450  61.856  1.00 90.09  ?  723 ILE   A N   1 
ATOM   4362 C CA  . ILE   A 1 742 ? -5.081  65.284  62.749  1.00 90.42  ?  723 ILE   A CA  1 
ATOM   4363 C C   . ILE   A 1 742 ? -6.401  64.629  62.394  1.00 91.86  ?  723 ILE   A C   1 
ATOM   4364 O O   . ILE   A 1 742 ? -6.467  63.417  62.366  1.00 86.60  ?  723 ILE   A O   1 
ATOM   4365 C CB  . ILE   A 1 742 ? -5.029  65.720  64.217  1.00 90.77  ?  723 ILE   A CB  1 
ATOM   4366 C CG1 . ILE   A 1 742 ? -3.665  66.311  64.557  1.00 88.58  ?  723 ILE   A CG1 1 
ATOM   4367 C CG2 . ILE   A 1 742 ? -5.366  64.559  65.124  1.00 82.28  ?  723 ILE   A CG2 1 
ATOM   4368 C CD1 . ILE   A 1 742 ? -3.520  66.699  65.992  1.00 83.54  ?  723 ILE   A CD1 1 
ATOM   4369 N N   . VAL   A 1 743 ? -7.431  65.413  62.133  1.00 95.35  ?  724 VAL   A N   1 
ATOM   4370 C CA  . VAL   A 1 743 ? -8.704  64.741  61.762  1.00 103.02 ?  724 VAL   A CA  1 
ATOM   4371 C C   . VAL   A 1 743 ? -8.529  64.044  60.410  1.00 100.16 ?  724 VAL   A C   1 
ATOM   4372 O O   . VAL   A 1 743 ? -9.029  62.932  60.253  1.00 95.44  ?  724 VAL   A O   1 
ATOM   4373 C CB  . VAL   A 1 743 ? -9.924  65.669  61.856  1.00 100.95 ?  724 VAL   A CB  1 
ATOM   4374 C CG1 . VAL   A 1 743 ? -10.083 66.195  63.259  1.00 92.81  ?  724 VAL   A CG1 1 
ATOM   4375 C CG2 . VAL   A 1 743 ? -9.852  66.827  60.891  1.00 99.08  ?  724 VAL   A CG2 1 
ATOM   4376 N N   . GLY   A 1 744 ? -7.739  64.657  59.539  1.00 92.25  ?  725 GLY   A N   1 
ATOM   4377 C CA  . GLY   A 1 744 ? -7.465  64.061  58.227  1.00 87.76  ?  725 GLY   A CA  1 
ATOM   4378 C C   . GLY   A 1 744 ? -6.901  62.673  58.390  1.00 90.79  ?  725 GLY   A C   1 
ATOM   4379 O O   . GLY   A 1 744 ? -7.512  61.736  57.912  1.00 88.47  ?  725 GLY   A O   1 
ATOM   4380 N N   . ARG   A 1 745 ? -5.851  62.533  59.183  1.00 84.06  ?  726 ARG   A N   1 
ATOM   4381 C CA  . ARG   A 1 745 ? -5.205  61.217  59.339  1.00 78.70  ?  726 ARG   A CA  1 
ATOM   4382 C C   . ARG   A 1 745 ? -6.189  60.198  59.896  1.00 83.92  ?  726 ARG   A C   1 
ATOM   4383 O O   . ARG   A 1 745 ? -6.087  59.065  59.509  1.00 84.30  ?  726 ARG   A O   1 
ATOM   4384 C CB  . ARG   A 1 745 ? -3.980  61.348  60.232  1.00 79.75  ?  726 ARG   A CB  1 
ATOM   4385 C CG  . ARG   A 1 745 ? -3.019  62.428  59.776  1.00 77.28  ?  726 ARG   A CG  1 
ATOM   4386 C CD  . ARG   A 1 745 ? -1.660  62.217  60.390  1.00 85.44  ?  726 ARG   A CD  1 
ATOM   4387 N NE  . ARG   A 1 745 ? -0.787  63.344  60.159  1.00 90.82  ?  726 ARG   A NE  1 
ATOM   4388 C CZ  . ARG   A 1 745 ? 0.446   63.416  60.612  1.00 93.50  ?  726 ARG   A CZ  1 
ATOM   4389 N NH1 . ARG   A 1 745 ? 0.930   62.423  61.323  1.00 92.28  ?  726 ARG   A NH1 1 
ATOM   4390 N NH2 . ARG   A 1 745 ? 1.196   64.465  60.360  1.00 85.99  ?  726 ARG   A NH2 1 
ATOM   4391 N N   . CYS   A 1 746 ? -7.048  60.570  60.834  1.00 88.11  ?  727 CYS   A N   1 
ATOM   4392 C CA  . CYS   A 1 746 ? -8.031  59.595  61.362  1.00 92.58  ?  727 CYS   A CA  1 
ATOM   4393 C C   . CYS   A 1 746 ? -8.995  59.202  60.258  1.00 91.00  ?  727 CYS   A C   1 
ATOM   4394 O O   . CYS   A 1 746 ? -9.345  58.043  60.160  1.00 88.47  ?  727 CYS   A O   1 
ATOM   4395 C CB  . CYS   A 1 746 ? -8.849  60.190  62.490  1.00 95.67  ?  727 CYS   A CB  1 
ATOM   4396 S SG  . CYS   A 1 746 ? -7.914  61.428  63.404  1.00 104.46 ?  727 CYS   A SG  1 
ATOM   4397 N N   . LEU   A 1 747 ? -9.401  60.157  59.439  1.00 96.17  ?  728 LEU   A N   1 
ATOM   4398 C CA  . LEU   A 1 747 ? -10.351 59.800  58.366  1.00 100.46 ?  728 LEU   A CA  1 
ATOM   4399 C C   . LEU   A 1 747 ? -9.675  58.797  57.443  1.00 98.14  ?  728 LEU   A C   1 
ATOM   4400 O O   . LEU   A 1 747 ? -10.256 57.746  57.199  1.00 94.58  ?  728 LEU   A O   1 
ATOM   4401 C CB  . LEU   A 1 747 ? -10.717 61.084  57.631  1.00 96.33  ?  728 LEU   A CB  1 
ATOM   4402 C CG  . LEU   A 1 747 ? -11.599 62.013  58.453  1.00 98.29  ?  728 LEU   A CG  1 
ATOM   4403 C CD1 . LEU   A 1 747 ? -12.135 63.150  57.616  1.00 97.25  ?  728 LEU   A CD1 1 
ATOM   4404 C CD2 . LEU   A 1 747 ? -12.736 61.238  59.080  1.00 100.68 ?  728 LEU   A CD2 1 
ATOM   4405 N N   . ALA   A 1 748 ? -8.427  59.061  57.088  1.00 93.56  ?  729 ALA   A N   1 
ATOM   4406 C CA  . ALA   A 1 748 ? -7.700  58.142  56.207  1.00 86.53  ?  729 ALA   A CA  1 
ATOM   4407 C C   . ALA   A 1 748 ? -7.618  56.785  56.884  1.00 92.51  ?  729 ALA   A C   1 
ATOM   4408 O O   . ALA   A 1 748 ? -7.986  55.821  56.248  1.00 104.74 ?  729 ALA   A O   1 
ATOM   4409 C CB  . ALA   A 1 748 ? -6.327  58.689  55.969  1.00 79.99  ?  729 ALA   A CB  1 
ATOM   4410 N N   . ILE   A 1 749 ? -7.285  56.732  58.165  1.00 89.73  ?  730 ILE   A N   1 
ATOM   4411 C CA  . ILE   A 1 749 ? -7.171  55.398  58.809  1.00 92.85  ?  730 ILE   A CA  1 
ATOM   4412 C C   . ILE   A 1 749 ? -8.538  54.742  58.796  1.00 97.29  ?  730 ILE   A C   1 
ATOM   4413 O O   . ILE   A 1 749 ? -8.640  53.597  58.405  1.00 101.24 ?  730 ILE   A O   1 
ATOM   4414 C CB  . ILE   A 1 749 ? -6.652  55.520  60.242  1.00 88.53  ?  730 ILE   A CB  1 
ATOM   4415 C CG1 . ILE   A 1 749 ? -5.229  56.068  60.289  1.00 93.59  ?  730 ILE   A CG1 1 
ATOM   4416 C CG2 . ILE   A 1 749 ? -6.738  54.177  60.925  1.00 77.65  ?  730 ILE   A CG2 1 
ATOM   4417 C CD1 . ILE   A 1 749 ? -4.261  55.143  60.973  1.00 88.42  ?  730 ILE   A CD1 1 
ATOM   4418 N N   . LEU   A 1 750 ? -9.564  55.506  59.123  1.00 97.32  ?  731 LEU   A N   1 
ATOM   4419 C CA  . LEU   A 1 750 ? -10.929 54.945  59.144  1.00 104.00 ?  731 LEU   A CA  1 
ATOM   4420 C C   . LEU   A 1 750 ? -11.321 54.522  57.735  1.00 110.43 ?  731 LEU   A C   1 
ATOM   4421 O O   . LEU   A 1 750 ? -11.931 53.451  57.589  1.00 105.85 ?  731 LEU   A O   1 
ATOM   4422 C CB  . LEU   A 1 750 ? -11.866 56.028  59.664  1.00 100.79 ?  731 LEU   A CB  1 
ATOM   4423 C CG  . LEU   A 1 750 ? -11.802 56.236  61.166  1.00 95.24  ?  731 LEU   A CG  1 
ATOM   4424 C CD1 . LEU   A 1 750 ? -12.855 57.222  61.599  1.00 92.64  ?  731 LEU   A CD1 1 
ATOM   4425 C CD2 . LEU   A 1 750 ? -11.971 54.921  61.891  1.00 88.99  ?  731 LEU   A CD2 1 
ATOM   4426 N N   . LYS   A 1 751 ? -10.962 55.325  56.736  1.00 104.56 ?  732 LYS   A N   1 
ATOM   4427 C CA  . LYS   A 1 751 ? -11.350 54.969  55.356  1.00 104.49 ?  732 LYS   A CA  1 
ATOM   4428 C C   . LYS   A 1 751 ? -10.745 53.613  55.017  1.00 107.74 ?  732 LYS   A C   1 
ATOM   4429 O O   . LYS   A 1 751 ? -11.486 52.767  54.603  1.00 108.59 ?  732 LYS   A O   1 
ATOM   4430 C CB  . LYS   A 1 751 ? -10.824 56.014  54.376  1.00 103.25 ?  732 LYS   A CB  1 
ATOM   4431 C CG  . LYS   A 1 751 ? -11.754 57.191  54.146  1.00 101.10 ?  732 LYS   A CG  1 
ATOM   4432 C CD  . LYS   A 1 751 ? -11.115 58.307  53.370  1.00 87.93  ?  732 LYS   A CD  1 
ATOM   4433 C CE  . LYS   A 1 751 ? -12.019 59.512  53.244  1.00 97.04  ?  732 LYS   A CE  1 
ATOM   4434 N NZ  . LYS   A 1 751 ? -13.342 59.275  53.865  1.00 99.34  ?  732 LYS   A NZ  1 
ATOM   4435 N N   . GLY   A 1 752 ? -9.479  53.380  55.322  1.00 103.46 ?  733 GLY   A N   1 
ATOM   4436 C CA  . GLY   A 1 752 ? -8.923  52.067  54.972  1.00 102.41 ?  733 GLY   A CA  1 
ATOM   4437 C C   . GLY   A 1 752 ? -9.637  50.945  55.687  1.00 103.30 ?  733 GLY   A C   1 
ATOM   4438 O O   . GLY   A 1 752 ? -10.010 50.002  55.034  1.00 115.34 ?  733 GLY   A O   1 
ATOM   4439 N N   . ILE   A 1 753 ? -9.903  51.073  56.974  1.00 101.97 ?  734 ILE   A N   1 
ATOM   4440 C CA  . ILE   A 1 753 ? -10.578 49.929  57.646  1.00 110.02 ?  734 ILE   A CA  1 
ATOM   4441 C C   . ILE   A 1 753 ? -12.021 49.771  57.164  1.00 111.65 ?  734 ILE   A C   1 
ATOM   4442 O O   . ILE   A 1 753 ? -12.524 48.657  57.255  1.00 112.56 ?  734 ILE   A O   1 
ATOM   4443 C CB  . ILE   A 1 753 ? -10.500 49.972  59.183  1.00 107.04 ?  734 ILE   A CB  1 
ATOM   4444 C CG1 . ILE   A 1 753 ? -9.072  49.808  59.704  1.00 105.81 ?  734 ILE   A CG1 1 
ATOM   4445 C CG2 . ILE   A 1 753 ? -11.369 48.875  59.745  1.00 101.76 ?  734 ILE   A CG2 1 
ATOM   4446 C CD1 . ILE   A 1 753 ? -8.914  50.107  61.191  1.00 103.68 ?  734 ILE   A CD1 1 
ATOM   4447 N N   . PHE   A 1 754 ? -12.701 50.844  56.762  1.00 112.52 ?  735 PHE   A N   1 
ATOM   4448 C CA  . PHE   A 1 754 ? -14.146 50.654  56.460  1.00 115.05 ?  735 PHE   A CA  1 
ATOM   4449 C C   . PHE   A 1 754 ? -14.525 50.934  55.004  1.00 110.70 ?  735 PHE   A C   1 
ATOM   4450 O O   . PHE   A 1 754 ? -15.680 50.713  54.647  1.00 106.35 ?  735 PHE   A O   1 
ATOM   4451 C CB  . PHE   A 1 754 ? -14.987 51.507  57.414  1.00 108.91 ?  735 PHE   A CB  1 
ATOM   4452 C CG  . PHE   A 1 754 ? -15.032 51.007  58.833  1.00 103.33 ?  735 PHE   A CG  1 
ATOM   4453 C CD1 . PHE   A 1 754 ? -15.830 49.941  59.182  1.00 105.19 ?  735 PHE   A CD1 1 
ATOM   4454 C CD2 . PHE   A 1 754 ? -14.272 51.599  59.818  1.00 100.33 ?  735 PHE   A CD2 1 
ATOM   4455 C CE1 . PHE   A 1 754 ? -15.864 49.469  60.480  1.00 104.54 ?  735 PHE   A CE1 1 
ATOM   4456 C CE2 . PHE   A 1 754 ? -14.308 51.124  61.114  1.00 98.40  ?  735 PHE   A CE2 1 
ATOM   4457 C CZ  . PHE   A 1 754 ? -15.104 50.064  61.446  1.00 96.86  ?  735 PHE   A CZ  1 
ATOM   4458 N N   . GLY   A 1 755 ? -13.582 51.368  54.185  1.00 102.83 ?  736 GLY   A N   1 
ATOM   4459 C CA  . GLY   A 1 755 ? -13.898 51.700  52.787  1.00 100.77 ?  736 GLY   A CA  1 
ATOM   4460 C C   . GLY   A 1 755 ? -13.999 53.197  52.646  1.00 103.24 ?  736 GLY   A C   1 
ATOM   4461 O O   . GLY   A 1 755 ? -14.521 53.803  53.543  1.00 106.46 ?  736 GLY   A O   1 
ATOM   4462 N N   . SER   A 1 756 ? -13.641 53.745  51.490  1.00 103.07 ?  737 SER   A N   1 
ATOM   4463 C CA  . SER   A 1 756 ? -13.611 55.211  51.271  1.00 101.24 ?  737 SER   A CA  1 
ATOM   4464 C C   . SER   A 1 756 ? -14.997 55.844  51.155  1.00 104.17 ?  737 SER   A C   1 
ATOM   4465 O O   . SER   A 1 756 ? -15.072 57.065  51.129  1.00 104.67 ?  737 SER   A O   1 
ATOM   4466 C CB  . SER   A 1 756 ? -12.768 55.558  50.098  1.00 101.30 ?  737 SER   A CB  1 
ATOM   4467 O OG  . SER   A 1 756 ? -12.903 56.937  49.810  1.00 103.78 ?  737 SER   A OG  1 
ATOM   4468 N N   . SER   A 1 757 ? -16.038 55.029  51.164  1.00 108.20 ?  738 SER   A N   1 
ATOM   4469 C CA  . SER   A 1 757 ? -17.390 55.587  50.959  1.00 112.58 ?  738 SER   A CA  1 
ATOM   4470 C C   . SER   A 1 757 ? -18.142 55.672  52.278  1.00 110.82 ?  738 SER   A C   1 
ATOM   4471 O O   . SER   A 1 757 ? -18.919 56.600  52.438  1.00 109.98 ?  738 SER   A O   1 
ATOM   4472 C CB  . SER   A 1 757 ? -18.137 54.732  49.994  1.00 113.26 ?  738 SER   A CB  1 
ATOM   4473 O OG  . SER   A 1 757 ? -17.962 53.366  50.321  1.00 109.27 ?  738 SER   A OG  1 
ATOM   4474 N N   . ALA   A 1 758 ? -17.883 54.752  53.196  1.00 108.27 ?  739 ALA   A N   1 
ATOM   4475 C CA  . ALA   A 1 758 ? -18.636 54.731  54.469  1.00 112.34 ?  739 ALA   A CA  1 
ATOM   4476 C C   . ALA   A 1 758 ? -18.235 55.847  55.445  1.00 118.34 ?  739 ALA   A C   1 
ATOM   4477 O O   . ALA   A 1 758 ? -18.960 56.016  56.404  1.00 112.47 ?  739 ALA   A O   1 
ATOM   4478 C CB  . ALA   A 1 758 ? -18.541 53.370  55.098  1.00 103.65 ?  739 ALA   A CB  1 
ATOM   4479 N N   . VAL   A 1 759 ? -17.139 56.573  55.222  1.00 119.62 ?  740 VAL   A N   1 
ATOM   4480 C CA  . VAL   A 1 759 ? -16.689 57.603  56.202  1.00 111.74 ?  740 VAL   A CA  1 
ATOM   4481 C C   . VAL   A 1 759 ? -17.158 59.009  55.813  1.00 109.56 ?  740 VAL   A C   1 
ATOM   4482 O O   . VAL   A 1 759 ? -16.550 59.639  54.952  1.00 104.19 ?  740 VAL   A O   1 
ATOM   4483 C CB  . VAL   A 1 759 ? -15.163 57.508  56.351  1.00 112.37 ?  740 VAL   A CB  1 
ATOM   4484 C CG1 . VAL   A 1 759 ? -14.671 58.623  57.246  1.00 112.37 ?  740 VAL   A CG1 1 
ATOM   4485 C CG2 . VAL   A 1 759 ? -14.716 56.187  56.951  1.00 109.66 ?  740 VAL   A CG2 1 
ATOM   4486 N N   . PRO   A 1 760 ? -18.177 59.566  56.489  1.00 111.38 ?  741 PRO   A N   1 
ATOM   4487 C CA  . PRO   A 1 760 ? -18.683 60.894  56.196  1.00 109.76 ?  741 PRO   A CA  1 
ATOM   4488 C C   . PRO   A 1 760 ? -17.811 61.937  56.878  1.00 108.46 ?  741 PRO   A C   1 
ATOM   4489 O O   . PRO   A 1 760 ? -17.198 61.610  57.824  1.00 117.00 ?  741 PRO   A O   1 
ATOM   4490 C CB  . PRO   A 1 760 ? -19.993 60.969  56.975  1.00 102.63 ?  741 PRO   A CB  1 
ATOM   4491 C CG  . PRO   A 1 760 ? -20.246 59.568  57.424  1.00 110.01 ?  741 PRO   A CG  1 
ATOM   4492 C CD  . PRO   A 1 760 ? -18.870 58.988  57.609  1.00 112.35 ?  741 PRO   A CD  1 
ATOM   4493 N N   . GLN   A 1 761 ? -17.825 63.179  56.418  1.00 105.34 ?  742 GLN   A N   1 
ATOM   4494 C CA  . GLN   A 1 761 ? -17.037 64.178  57.172  1.00 111.47 ?  742 GLN   A CA  1 
ATOM   4495 C C   . GLN   A 1 761 ? -17.669 64.308  58.554  1.00 119.58 ?  742 GLN   A C   1 
ATOM   4496 O O   . GLN   A 1 761 ? -18.899 64.378  58.636  1.00 117.05 ?  742 GLN   A O   1 
ATOM   4497 C CB  . GLN   A 1 761 ? -17.029 65.521  56.457  1.00 102.61 ?  742 GLN   A CB  1 
ATOM   4498 C CG  . GLN   A 1 761 ? -15.644 66.125  56.353  1.00 118.25 ?  742 GLN   A CG  1 
ATOM   4499 C CD  . GLN   A 1 761 ? -14.678 65.171  55.701  1.00 116.59 ?  742 GLN   A CD  1 
ATOM   4500 O OE1 . GLN   A 1 761 ? -15.006 64.028  55.411  1.00 113.69 ?  742 GLN   A OE1 1 
ATOM   4501 N NE2 . GLN   A 1 761 ? -13.467 65.637  55.465  1.00 111.38 ?  742 GLN   A NE2 1 
ATOM   4502 N N   . PRO   A 1 762 ? -16.885 64.361  59.644  1.00 118.18 ?  743 PRO   A N   1 
ATOM   4503 C CA  . PRO   A 1 762 ? -17.444 64.466  60.981  1.00 107.32 ?  743 PRO   A CA  1 
ATOM   4504 C C   . PRO   A 1 762 ? -17.998 65.872  61.192  1.00 107.41 ?  743 PRO   A C   1 
ATOM   4505 O O   . PRO   A 1 762 ? -17.458 66.778  60.640  1.00 105.38 ?  743 PRO   A O   1 
ATOM   4506 C CB  . PRO   A 1 762 ? -16.192 64.339  61.830  1.00 107.13 ?  743 PRO   A CB  1 
ATOM   4507 C CG  . PRO   A 1 762 ? -15.157 64.978  60.976  1.00 107.97 ?  743 PRO   A CG  1 
ATOM   4508 C CD  . PRO   A 1 762 ? -15.439 64.378  59.626  1.00 112.83 ?  743 PRO   A CD  1 
ATOM   4509 N N   . LYS   A 1 763 ? -19.036 66.000  62.006  1.00 105.73 ?  744 LYS   A N   1 
ATOM   4510 C CA  . LYS   A 1 763 ? -19.633 67.329  62.269  1.00 112.56 ?  744 LYS   A CA  1 
ATOM   4511 C C   . LYS   A 1 763 ? -18.757 68.126  63.241  1.00 114.09 ?  744 LYS   A C   1 
ATOM   4512 O O   . LYS   A 1 763 ? -18.208 69.147  62.814  1.00 105.02 ?  744 LYS   A O   1 
ATOM   4513 C CB  . LYS   A 1 763 ? -21.037 67.140  62.833  1.00 114.49 ?  744 LYS   A CB  1 
ATOM   4514 C CG  . LYS   A 1 763 ? -21.577 65.724  62.715  1.00 122.65 ?  744 LYS   A CG  1 
ATOM   4515 C CD  . LYS   A 1 763 ? -22.905 65.520  63.419  1.00 126.01 ?  744 LYS   A CD  1 
ATOM   4516 C CE  . LYS   A 1 763 ? -24.100 65.945  62.585  1.00 122.22 ?  744 LYS   A CE  1 
ATOM   4517 N NZ  . LYS   A 1 763 ? -25.365 66.010  63.361  1.00 114.93 ?  744 LYS   A NZ  1 
ATOM   4518 N N   . GLU   A 1 764 ? -18.633 67.659  64.490  1.00 116.72 ?  745 GLU   A N   1 
ATOM   4519 C CA  . GLU   A 1 764 ? -17.864 68.309  65.538  1.00 111.97 ?  745 GLU   A CA  1 
ATOM   4520 C C   . GLU   A 1 764 ? -16.588 67.504  65.746  1.00 103.88 ?  745 GLU   A C   1 
ATOM   4521 O O   . GLU   A 1 764 ? -16.621 66.266  65.738  1.00 92.95  ?  745 GLU   A O   1 
ATOM   4522 C CB  . GLU   A 1 764 ? -18.694 68.394  66.828  1.00 112.24 ?  745 GLU   A CB  1 
ATOM   4523 C CG  . GLU   A 1 764 ? -19.939 69.251  66.655  1.00 106.72 ?  745 GLU   A CG  1 
ATOM   4524 C CD  . GLU   A 1 764 ? -19.587 70.686  66.314  1.00 108.99 ?  745 GLU   A CD  1 
ATOM   4525 O OE1 . GLU   A 1 764 ? -18.479 71.114  66.704  1.00 112.61 ?  745 GLU   A OE1 1 
ATOM   4526 O OE2 . GLU   A 1 764 ? -20.406 71.394  65.681  1.00 114.50 ?  745 GLU   A OE2 1 
ATOM   4527 N N   . THR   A 1 765 ? -15.462 68.211  65.851  1.00 103.65 ?  746 THR   A N   1 
ATOM   4528 C CA  . THR   A 1 765 ? -14.159 67.622  66.123  1.00 97.12  ?  746 THR   A CA  1 
ATOM   4529 C C   . THR   A 1 765 ? -13.491 68.417  67.232  1.00 95.83  ?  746 THR   A C   1 
ATOM   4530 O O   . THR   A 1 765 ? -13.511 69.656  67.212  1.00 95.22  ?  746 THR   A O   1 
ATOM   4531 C CB  . THR   A 1 765 ? -13.292 67.636  64.882  1.00 93.56  ?  746 THR   A CB  1 
ATOM   4532 O OG1 . THR   A 1 765 ? -13.405 68.929  64.273  1.00 101.13 ?  746 THR   A OG1 1 
ATOM   4533 C CG2 . THR   A 1 765 ? -13.756 66.579  63.930  1.00 93.55  ?  746 THR   A CG2 1 
ATOM   4534 N N   . VAL   A 1 766 ? -12.934 67.696  68.210  1.00 92.82  ?  747 VAL   A N   1 
ATOM   4535 C CA  . VAL   A 1 766 ? -12.188 68.257  69.329  1.00 83.88  ?  747 VAL   A CA  1 
ATOM   4536 C C   . VAL   A 1 766 ? -10.895 67.462  69.448  1.00 82.90  ?  747 VAL   A C   1 
ATOM   4537 O O   . VAL   A 1 766 ? -10.909 66.228  69.337  1.00 81.31  ?  747 VAL   A O   1 
ATOM   4538 C CB  . VAL   A 1 766 ? -12.971 68.139  70.648  1.00 88.54  ?  747 VAL   A CB  1 
ATOM   4539 C CG1 . VAL   A 1 766 ? -12.216 68.827  71.752  1.00 85.68  ?  747 VAL   A CG1 1 
ATOM   4540 C CG2 . VAL   A 1 766 ? -14.392 68.616  70.496  1.00 93.27  ?  747 VAL   A CG2 1 
ATOM   4541 N N   . VAL   A 1 767 ? -9.783  68.145  69.713  1.00 79.44  ?  748 VAL   A N   1 
ATOM   4542 C CA  . VAL   A 1 767 ? -8.495  67.467  69.866  1.00 77.70  ?  748 VAL   A CA  1 
ATOM   4543 C C   . VAL   A 1 767 ? -7.821  67.958  71.147  1.00 73.31  ?  748 VAL   A C   1 
ATOM   4544 O O   . VAL   A 1 767 ? -7.438  69.133  71.245  1.00 76.03  ?  748 VAL   A O   1 
ATOM   4545 C CB  . VAL   A 1 767 ? -7.590  67.687  68.645  1.00 75.91  ?  748 VAL   A CB  1 
ATOM   4546 C CG1 . VAL   A 1 767 ? -6.159  67.330  68.969  1.00 74.11  ?  748 VAL   A CG1 1 
ATOM   4547 C CG2 . VAL   A 1 767 ? -8.083  66.849  67.507  1.00 81.72  ?  748 VAL   A CG2 1 
ATOM   4548 N N   . SER   A 1 768 ? -7.646  67.062  72.118  1.00 65.18  ?  749 SER   A N   1 
ATOM   4549 C CA  . SER   A 1 768 ? -6.985  67.460  73.354  1.00 64.89  ?  749 SER   A CA  1 
ATOM   4550 C C   . SER   A 1 768 ? -5.497  67.720  73.113  1.00 65.01  ?  749 SER   A C   1 
ATOM   4551 O O   . SER   A 1 768 ? -4.879  67.145  72.212  1.00 68.20  ?  749 SER   A O   1 
ATOM   4552 C CB  . SER   A 1 768 ? -7.154  66.396  74.438  1.00 55.72  ?  749 SER   A CB  1 
ATOM   4553 O OG  . SER   A 1 768 ? -6.265  65.324  74.233  1.00 61.35  ?  749 SER   A OG  1 
ATOM   4554 N N   . ARG   A 1 769 ? -4.915  68.621  73.924  1.00 61.37  ?  750 ARG   A N   1 
ATOM   4555 C CA  . ARG   A 1 769 ? -3.466  68.899  73.882  1.00 66.80  ?  750 ARG   A CA  1 
ATOM   4556 C C   . ARG   A 1 769 ? -3.002  69.139  75.333  1.00 67.64  ?  750 ARG   A C   1 
ATOM   4557 O O   . ARG   A 1 769 ? -2.654  70.263  75.744  1.00 67.27  ?  750 ARG   A O   1 
ATOM   4558 C CB  . ARG   A 1 769 ? -3.124  70.074  72.952  1.00 65.02  ?  750 ARG   A CB  1 
ATOM   4559 C CG  . ARG   A 1 769 ? -3.644  69.933  71.515  1.00 67.74  ?  750 ARG   A CG  1 
ATOM   4560 C CD  . ARG   A 1 769 ? -3.447  71.191  70.676  1.00 76.64  ?  750 ARG   A CD  1 
ATOM   4561 N NE  . ARG   A 1 769 ? -2.056  71.667  70.634  1.00 84.85  ?  750 ARG   A NE  1 
ATOM   4562 C CZ  . ARG   A 1 769 ? -1.606  72.793  71.214  1.00 87.50  ?  750 ARG   A CZ  1 
ATOM   4563 N NH1 . ARG   A 1 769 ? -2.431  73.589  71.905  1.00 79.21  ?  750 ARG   A NH1 1 
ATOM   4564 N NH2 . ARG   A 1 769 ? -0.317  73.135  71.106  1.00 82.16  ?  750 ARG   A NH2 1 
ATOM   4565 N N   . TRP   A 1 770 ? -2.980  68.041  76.111  1.00 63.28  ?  751 TRP   A N   1 
ATOM   4566 C CA  . TRP   A 1 770 ? -2.834  68.125  77.560  1.00 57.85  ?  751 TRP   A CA  1 
ATOM   4567 C C   . TRP   A 1 770 ? -1.460  68.638  77.971  1.00 61.55  ?  751 TRP   A C   1 
ATOM   4568 O O   . TRP   A 1 770 ? -1.346  69.361  78.965  1.00 62.24  ?  751 TRP   A O   1 
ATOM   4569 C CB  . TRP   A 1 770 ? -3.093  66.771  78.202  1.00 53.88  ?  751 TRP   A CB  1 
ATOM   4570 C CG  . TRP   A 1 770 ? -4.535  66.420  78.343  1.00 57.41  ?  751 TRP   A CG  1 
ATOM   4571 C CD1 . TRP   A 1 770 ? -5.213  65.441  77.668  1.00 63.41  ?  751 TRP   A CD1 1 
ATOM   4572 C CD2 . TRP   A 1 770 ? -5.476  67.007  79.240  1.00 61.34  ?  751 TRP   A CD2 1 
ATOM   4573 N NE1 . TRP   A 1 770 ? -6.522  65.389  78.084  1.00 60.64  ?  751 TRP   A NE1 1 
ATOM   4574 C CE2 . TRP   A 1 770 ? -6.714  66.348  79.041  1.00 59.60  ?  751 TRP   A CE2 1 
ATOM   4575 C CE3 . TRP   A 1 770 ? -5.397  68.028  80.199  1.00 59.44  ?  751 TRP   A CE3 1 
ATOM   4576 C CZ2 . TRP   A 1 770 ? -7.865  66.690  79.748  1.00 58.11  ?  751 TRP   A CZ2 1 
ATOM   4577 C CZ3 . TRP   A 1 770 ? -6.533  68.356  80.906  1.00 54.95  ?  751 TRP   A CZ3 1 
ATOM   4578 C CH2 . TRP   A 1 770 ? -7.756  67.688  80.677  1.00 59.72  ?  751 TRP   A CH2 1 
ATOM   4579 N N   . ARG   A 1 771 ? -0.396  68.271  77.250  1.00 59.81  ?  752 ARG   A N   1 
ATOM   4580 C CA  . ARG   A 1 771 ? 0.896   68.844  77.619  1.00 59.01  ?  752 ARG   A CA  1 
ATOM   4581 C C   . ARG   A 1 771 ? 0.897   70.362  77.433  1.00 59.52  ?  752 ARG   A C   1 
ATOM   4582 O O   . ARG   A 1 771 ? 1.555   71.087  78.187  1.00 54.33  ?  752 ARG   A O   1 
ATOM   4583 C CB  . ARG   A 1 771 ? 2.022   68.195  76.821  1.00 54.71  ?  752 ARG   A CB  1 
ATOM   4584 C CG  . ARG   A 1 771 ? 3.424   68.468  77.362  1.00 47.49  ?  752 ARG   A CG  1 
ATOM   4585 C CD  . ARG   A 1 771 ? 3.706   67.715  78.686  1.00 51.67  ?  752 ARG   A CD  1 
ATOM   4586 N NE  . ARG   A 1 771 ? 4.241   66.368  78.492  1.00 58.19  ?  752 ARG   A NE  1 
ATOM   4587 C CZ  . ARG   A 1 771 ? 4.401   65.481  79.469  1.00 55.51  ?  752 ARG   A CZ  1 
ATOM   4588 N NH1 . ARG   A 1 771 ? 4.069   65.803  80.703  1.00 60.31  ?  752 ARG   A NH1 1 
ATOM   4589 N NH2 . ARG   A 1 771 ? 4.873   64.268  79.222  1.00 64.94  ?  752 ARG   A NH2 1 
ATOM   4590 N N   . ALA   A 1 772 ? 0.127   70.861  76.498  1.00 64.48  ?  753 ALA   A N   1 
ATOM   4591 C CA  . ALA   A 1 772 ? 0.189   72.311  76.264  1.00 63.70  ?  753 ALA   A CA  1 
ATOM   4592 C C   . ALA   A 1 772 ? -0.696  73.049  77.250  1.00 66.25  ?  753 ALA   A C   1 
ATOM   4593 O O   . ALA   A 1 772 ? -0.484  74.225  77.457  1.00 62.54  ?  753 ALA   A O   1 
ATOM   4594 C CB  . ALA   A 1 772 ? -0.243  72.582  74.865  1.00 66.96  ?  753 ALA   A CB  1 
ATOM   4595 N N   . ASP   A 1 773 ? -1.668  72.364  77.817  1.00 64.91  ?  754 ASP   A N   1 
ATOM   4596 C CA  . ASP   A 1 773 ? -2.559  73.060  78.761  1.00 59.40  ?  754 ASP   A CA  1 
ATOM   4597 C C   . ASP   A 1 773 ? -1.707  73.535  79.917  1.00 59.75  ?  754 ASP   A C   1 
ATOM   4598 O O   . ASP   A 1 773 ? -1.074  72.731  80.522  1.00 68.02  ?  754 ASP   A O   1 
ATOM   4599 C CB  . ASP   A 1 773 ? -3.621  72.096  79.259  1.00 62.27  ?  754 ASP   A CB  1 
ATOM   4600 C CG  . ASP   A 1 773 ? -4.579  72.761  80.197  1.00 62.50  ?  754 ASP   A CG  1 
ATOM   4601 O OD1 . ASP   A 1 773 ? -4.296  73.857  80.577  1.00 59.18  ?  754 ASP   A OD1 1 
ATOM   4602 O OD2 . ASP   A 1 773 ? -5.574  72.166  80.524  1.00 61.07  ?  754 ASP   A OD2 1 
ATOM   4603 N N   . PRO   A 1 774 ? -1.767  74.806  80.316  1.00 60.10  ?  755 PRO   A N   1 
ATOM   4604 C CA  . PRO   A 1 774 ? -0.947  75.296  81.393  1.00 62.58  ?  755 PRO   A CA  1 
ATOM   4605 C C   . PRO   A 1 774 ? -1.492  74.974  82.782  1.00 59.86  ?  755 PRO   A C   1 
ATOM   4606 O O   . PRO   A 1 774 ? -0.841  75.236  83.709  1.00 58.66  ?  755 PRO   A O   1 
ATOM   4607 C CB  . PRO   A 1 774 ? -1.006  76.787  81.134  1.00 56.41  ?  755 PRO   A CB  1 
ATOM   4608 C CG  . PRO   A 1 774 ? -2.369  76.990  80.629  1.00 57.86  ?  755 PRO   A CG  1 
ATOM   4609 C CD  . PRO   A 1 774 ? -2.586  75.817  79.719  1.00 57.95  ?  755 PRO   A CD  1 
ATOM   4610 N N   . TRP   A 1 775 ? -2.701  74.457  82.861  1.00 55.40  ?  756 TRP   A N   1 
ATOM   4611 C CA  . TRP   A 1 775 ? -3.285  74.090  84.165  1.00 54.87  ?  756 TRP   A CA  1 
ATOM   4612 C C   . TRP   A 1 775 ? -3.092  72.602  84.412  1.00 63.00  ?  756 TRP   A C   1 
ATOM   4613 O O   . TRP   A 1 775 ? -3.731  72.086  85.282  1.00 61.03  ?  756 TRP   A O   1 
ATOM   4614 C CB  . TRP   A 1 775 ? -4.749  74.477  84.190  1.00 54.49  ?  756 TRP   A CB  1 
ATOM   4615 C CG  . TRP   A 1 775 ? -4.982  75.891  83.775  1.00 64.36  ?  756 TRP   A CG  1 
ATOM   4616 C CD1 . TRP   A 1 775 ? -5.921  76.340  82.908  1.00 62.45  ?  756 TRP   A CD1 1 
ATOM   4617 C CD2 . TRP   A 1 775 ? -4.286  77.052  84.227  1.00 62.43  ?  756 TRP   A CD2 1 
ATOM   4618 N NE1 . TRP   A 1 775 ? -5.841  77.691  82.779  1.00 56.72  ?  756 TRP   A NE1 1 
ATOM   4619 C CE2 . TRP   A 1 775 ? -4.846  78.152  83.575  1.00 58.15  ?  756 TRP   A CE2 1 
ATOM   4620 C CE3 . TRP   A 1 775 ? -3.239  77.271  85.110  1.00 61.45  ?  756 TRP   A CE3 1 
ATOM   4621 C CZ2 . TRP   A 1 775 ? -4.405  79.444  83.781  1.00 57.32  ?  756 TRP   A CZ2 1 
ATOM   4622 C CZ3 . TRP   A 1 775 ? -2.794  78.550  85.313  1.00 61.64  ?  756 TRP   A CZ3 1 
ATOM   4623 C CH2 . TRP   A 1 775 ? -3.367  79.619  84.652  1.00 57.84  ?  756 TRP   A CH2 1 
ATOM   4624 N N   . ALA   A 1 776 ? -2.344  71.939  83.542  1.00 62.51  ?  757 ALA   A N   1 
ATOM   4625 C CA  . ALA   A 1 776 ? -2.038  70.506  83.658  1.00 51.26  ?  757 ALA   A CA  1 
ATOM   4626 C C   . ALA   A 1 776 ? -0.584  70.248  83.307  1.00 51.68  ?  757 ALA   A C   1 
ATOM   4627 O O   . ALA   A 1 776 ? 0.062   69.616  84.072  1.00 51.79  ?  757 ALA   A O   1 
ATOM   4628 C CB  . ALA   A 1 776 ? -2.933  69.744  82.752  1.00 53.41  ?  757 ALA   A CB  1 
ATOM   4629 N N   . ARG   A 1 777 ? -0.167  70.665  82.125  1.00 52.36  ?  758 ARG   A N   1 
ATOM   4630 C CA  . ARG   A 1 777 ? 1.191   70.468  81.563  1.00 52.53  ?  758 ARG   A CA  1 
ATOM   4631 C C   . ARG   A 1 777 ? 1.518   68.992  81.482  1.00 56.52  ?  758 ARG   A C   1 
ATOM   4632 O O   . ARG   A 1 777 ? 2.660   68.665  81.635  1.00 54.87  ?  758 ARG   A O   1 
ATOM   4633 C CB  . ARG   A 1 777 ? 2.275   71.168  82.368  1.00 57.41  ?  758 ARG   A CB  1 
ATOM   4634 C CG  . ARG   A 1 777 ? 1.986   72.630  82.612  1.00 60.74  ?  758 ARG   A CG  1 
ATOM   4635 C CD  . ARG   A 1 777 ? 2.918   73.405  81.746  1.00 65.60  ?  758 ARG   A CD  1 
ATOM   4636 N NE  . ARG   A 1 777 ? 2.241   74.623  81.389  1.00 83.32  ?  758 ARG   A NE  1 
ATOM   4637 C CZ  . ARG   A 1 777 ? 2.851   75.638  80.831  1.00 84.93  ?  758 ARG   A CZ  1 
ATOM   4638 N NH1 . ARG   A 1 777 ? 4.137   75.555  80.565  1.00 84.44  ?  758 ARG   A NH1 1 
ATOM   4639 N NH2 . ARG   A 1 777 ? 2.185   76.731  80.551  1.00 80.15  ?  758 ARG   A NH2 1 
ATOM   4640 N N   . GLY   A 1 778 ? 0.532   68.183  81.138  1.00 51.89  ?  759 GLY   A N   1 
ATOM   4641 C CA  . GLY   A 1 778 ? 0.645   66.741  81.061  1.00 51.35  ?  759 GLY   A CA  1 
ATOM   4642 C C   . GLY   A 1 778 ? -0.691  66.109  81.398  1.00 53.86  ?  759 GLY   A C   1 
ATOM   4643 O O   . GLY   A 1 778 ? -1.676  66.792  81.660  1.00 55.84  ?  759 GLY   A O   1 
ATOM   4644 N N   . SER   A 1 779 ? -0.707  64.774  81.378  1.00 48.97  ?  760 SER   A N   1 
ATOM   4645 C CA  . SER   A 1 779 ? -1.925  64.020  81.644  1.00 51.03  ?  760 SER   A CA  1 
ATOM   4646 C C   . SER   A 1 779 ? -1.943  63.371  83.019  1.00 54.74  ?  760 SER   A C   1 
ATOM   4647 O O   . SER   A 1 779 ? -2.915  63.548  83.753  1.00 57.32  ?  760 SER   A O   1 
ATOM   4648 C CB  . SER   A 1 779 ? -2.126  62.950  80.570  1.00 55.77  ?  760 SER   A CB  1 
ATOM   4649 O OG  . SER   A 1 779 ? -1.131  61.943  80.684  1.00 63.23  ?  760 SER   A OG  1 
ATOM   4650 N N   . TYR   A 1 780 ? -0.917  62.601  83.390  1.00 52.04  ?  761 TYR   A N   1 
ATOM   4651 C CA  . TYR   A 1 780 ? -0.864  62.057  84.742  1.00 52.55  ?  761 TYR   A CA  1 
ATOM   4652 C C   . TYR   A 1 780 ? 0.503   61.446  85.031  1.00 55.25  ?  761 TYR   A C   1 
ATOM   4653 O O   . TYR   A 1 780 ? 1.352   61.303  84.151  1.00 56.90  ?  761 TYR   A O   1 
ATOM   4654 C CB  . TYR   A 1 780 ? -1.957  61.031  84.998  1.00 57.03  ?  761 TYR   A CB  1 
ATOM   4655 C CG  . TYR   A 1 780 ? -2.178  59.996  83.942  1.00 61.37  ?  761 TYR   A CG  1 
ATOM   4656 C CD1 . TYR   A 1 780 ? -1.454  58.811  83.954  1.00 63.15  ?  761 TYR   A CD1 1 
ATOM   4657 C CD2 . TYR   A 1 780 ? -3.150  60.172  82.957  1.00 63.12  ?  761 TYR   A CD2 1 
ATOM   4658 C CE1 . TYR   A 1 780 ? -1.674  57.824  83.008  1.00 63.74  ?  761 TYR   A CE1 1 
ATOM   4659 C CE2 . TYR   A 1 780 ? -3.371  59.192  81.994  1.00 67.67  ?  761 TYR   A CE2 1 
ATOM   4660 C CZ  . TYR   A 1 780 ? -2.624  58.020  82.033  1.00 68.03  ?  761 TYR   A CZ  1 
ATOM   4661 O OH  . TYR   A 1 780 ? -2.819  57.034  81.112  1.00 68.71  ?  761 TYR   A OH  1 
ATOM   4662 N N   . SER   A 1 781 ? 0.708   61.105  86.293  1.00 55.16  ?  762 SER   A N   1 
ATOM   4663 C CA  . SER   A 1 781 ? 2.038   60.751  86.742  1.00 56.07  ?  762 SER   A CA  1 
ATOM   4664 C C   . SER   A 1 781 ? 2.380   59.319  86.340  1.00 55.92  ?  762 SER   A C   1 
ATOM   4665 O O   . SER   A 1 781 ? 1.516   58.523  85.979  1.00 57.19  ?  762 SER   A O   1 
ATOM   4666 C CB  . SER   A 1 781 ? 2.137   60.918  88.255  1.00 56.24  ?  762 SER   A CB  1 
ATOM   4667 O OG  . SER   A 1 781 ? 1.204   60.063  88.888  1.00 58.78  ?  762 SER   A OG  1 
ATOM   4668 N N   . TYR   A 1 782 ? 3.672   59.012  86.382  1.00 52.82  ?  763 TYR   A N   1 
ATOM   4669 C CA  . TYR   A 1 782 ? 4.187   57.703  86.027  1.00 48.94  ?  763 TYR   A CA  1 
ATOM   4670 C C   . TYR   A 1 782 ? 5.482   57.529  86.778  1.00 56.42  ?  763 TYR   A C   1 
ATOM   4671 O O   . TYR   A 1 782 ? 6.138   58.513  87.127  1.00 61.94  ?  763 TYR   A O   1 
ATOM   4672 C CB  . TYR   A 1 782 ? 4.424   57.529  84.530  1.00 45.31  ?  763 TYR   A CB  1 
ATOM   4673 C CG  . TYR   A 1 782 ? 5.615   58.264  83.956  1.00 51.12  ?  763 TYR   A CG  1 
ATOM   4674 C CD1 . TYR   A 1 782 ? 6.924   57.815  84.159  1.00 53.10  ?  763 TYR   A CD1 1 
ATOM   4675 C CD2 . TYR   A 1 782 ? 5.431   59.391  83.148  1.00 50.03  ?  763 TYR   A CD2 1 
ATOM   4676 C CE1 . TYR   A 1 782 ? 8.015   58.501  83.589  1.00 51.86  ?  763 TYR   A CE1 1 
ATOM   4677 C CE2 . TYR   A 1 782 ? 6.501   60.063  82.588  1.00 47.76  ?  763 TYR   A CE2 1 
ATOM   4678 C CZ  . TYR   A 1 782 ? 7.793   59.625  82.810  1.00 48.44  ?  763 TYR   A CZ  1 
ATOM   4679 O OH  . TYR   A 1 782 ? 8.859   60.332  82.256  1.00 51.03  ?  763 TYR   A OH  1 
ATOM   4680 N N   . VAL   A 1 783 ? 5.850   56.272  87.037  1.00 60.98  ?  764 VAL   A N   1 
ATOM   4681 C CA  . VAL   A 1 783 ? 7.007   56.030  87.893  1.00 58.06  ?  764 VAL   A CA  1 
ATOM   4682 C C   . VAL   A 1 783 ? 8.218   56.089  86.980  1.00 58.05  ?  764 VAL   A C   1 
ATOM   4683 O O   . VAL   A 1 783 ? 8.559   55.113  86.303  1.00 57.24  ?  764 VAL   A O   1 
ATOM   4684 C CB  . VAL   A 1 783 ? 6.911   54.696  88.634  1.00 58.54  ?  764 VAL   A CB  1 
ATOM   4685 C CG1 . VAL   A 1 783 ? 8.106   54.548  89.599  1.00 54.66  ?  764 VAL   A CG1 1 
ATOM   4686 C CG2 . VAL   A 1 783 ? 5.567   54.562  89.319  1.00 58.48  ?  764 VAL   A CG2 1 
ATOM   4687 N N   . ALA   A 1 784 ? 8.850   57.258  86.912  1.00 60.03  ?  765 ALA   A N   1 
ATOM   4688 C CA  . ALA   A 1 784 ? 9.990   57.441  86.034  1.00 53.87  ?  765 ALA   A CA  1 
ATOM   4689 C C   . ALA   A 1 784 ? 11.130  56.535  86.461  1.00 56.40  ?  765 ALA   A C   1 
ATOM   4690 O O   . ALA   A 1 784 ? 11.253  56.162  87.634  1.00 54.38  ?  765 ALA   A O   1 
ATOM   4691 C CB  . ALA   A 1 784 ? 10.449  58.891  86.057  1.00 56.83  ?  765 ALA   A CB  1 
ATOM   4692 N N   . ALA   A 1 785 ? 11.946  56.154  85.484  1.00 57.49  ?  766 ALA   A N   1 
ATOM   4693 C CA  . ALA   A 1 785 ? 13.203  55.500  85.802  1.00 63.24  ?  766 ALA   A CA  1 
ATOM   4694 C C   . ALA   A 1 785 ? 14.006  56.408  86.724  1.00 63.64  ?  766 ALA   A C   1 
ATOM   4695 O O   . ALA   A 1 785 ? 14.132  57.611  86.471  1.00 69.98  ?  766 ALA   A O   1 
ATOM   4696 C CB  . ALA   A 1 785 ? 13.971  55.185  84.519  1.00 60.28  ?  766 ALA   A CB  1 
ATOM   4697 N N   . GLY   A 1 786 ? 14.519  55.842  87.815  1.00 63.07  ?  767 GLY   A N   1 
ATOM   4698 C CA  . GLY   A 1 786 ? 15.127  56.634  88.862  1.00 59.95  ?  767 GLY   A CA  1 
ATOM   4699 C C   . GLY   A 1 786 ? 14.169  57.077  89.947  1.00 61.44  ?  767 GLY   A C   1 
ATOM   4700 O O   . GLY   A 1 786 ? 14.613  57.514  91.022  1.00 62.06  ?  767 GLY   A O   1 
ATOM   4701 N N   . SER   A 1 787 ? 12.870  56.990  89.710  1.00 61.17  ?  768 SER   A N   1 
ATOM   4702 C CA  . SER   A 1 787 ? 11.913  57.262  90.763  1.00 58.87  ?  768 SER   A CA  1 
ATOM   4703 C C   . SER   A 1 787 ? 11.538  55.942  91.424  1.00 61.45  ?  768 SER   A C   1 
ATOM   4704 O O   . SER   A 1 787 ? 12.055  54.870  91.092  1.00 63.63  ?  768 SER   A O   1 
ATOM   4705 C CB  . SER   A 1 787 ? 10.681  57.991  90.206  1.00 62.56  ?  768 SER   A CB  1 
ATOM   4706 O OG  . SER   A 1 787 ? 9.936   58.669  91.213  1.00 57.84  ?  768 SER   A OG  1 
ATOM   4707 N N   . SER   A 1 788 ? 10.621  56.024  92.369  1.00 56.85  ?  769 SER   A N   1 
ATOM   4708 C CA  . SER   A 1 788 ? 10.098  54.851  93.037  1.00 58.46  ?  769 SER   A CA  1 
ATOM   4709 C C   . SER   A 1 788 ? 8.788   55.262  93.672  1.00 56.58  ?  769 SER   A C   1 
ATOM   4710 O O   . SER   A 1 788 ? 8.376   56.415  93.592  1.00 61.68  ?  769 SER   A O   1 
ATOM   4711 C CB  . SER   A 1 788 ? 11.076  54.308  94.082  1.00 61.85  ?  769 SER   A CB  1 
ATOM   4712 O OG  . SER   A 1 788 ? 11.020  55.066  95.272  1.00 57.56  ?  769 SER   A OG  1 
ATOM   4713 N N   . GLY   A 1 789 ? 8.129   54.312  94.313  1.00 61.67  ?  770 GLY   A N   1 
ATOM   4714 C CA  . GLY   A 1 789 ? 6.916   54.681  94.994  1.00 59.47  ?  770 GLY   A CA  1 
ATOM   4715 C C   . GLY   A 1 789 ? 7.144   55.551  96.208  1.00 61.98  ?  770 GLY   A C   1 
ATOM   4716 O O   . GLY   A 1 789 ? 6.199   56.201  96.664  1.00 66.69  ?  770 GLY   A O   1 
ATOM   4717 N N   . ASN   A 1 790 ? 8.368   55.580  96.752  1.00 57.47  ?  771 ASN   A N   1 
ATOM   4718 C CA  . ASN   A 1 790 ? 8.596   56.432  97.917  1.00 62.32  ?  771 ASN   A CA  1 
ATOM   4719 C C   . ASN   A 1 790 ? 8.447   57.913  97.580  1.00 59.59  ?  771 ASN   A C   1 
ATOM   4720 O O   . ASN   A 1 790 ? 8.051   58.702  98.445  1.00 57.88  ?  771 ASN   A O   1 
ATOM   4721 C CB  . ASN   A 1 790 ? 9.962   56.158  98.540  1.00 65.60  ?  771 ASN   A CB  1 
ATOM   4722 C CG  . ASN   A 1 790 ? 9.911   55.028  99.550  1.00 84.66  ?  771 ASN   A CG  1 
ATOM   4723 O OD1 . ASN   A 1 790 ? 10.307  53.900  99.257  1.00 87.31  ?  771 ASN   A OD1 1 
ATOM   4724 N ND2 . ASN   A 1 790 ? 9.371   55.318  100.747 1.00 93.47  ?  771 ASN   A ND2 1 
ATOM   4725 N N   . ASP   A 1 791 ? 8.738   58.301  96.334  1.00 56.62  ?  772 ASP   A N   1 
ATOM   4726 C CA  . ASP   A 1 791 ? 8.567   59.682  95.909  1.00 50.02  ?  772 ASP   A CA  1 
ATOM   4727 C C   . ASP   A 1 791 ? 7.119   60.114  95.975  1.00 55.54  ?  772 ASP   A C   1 
ATOM   4728 O O   . ASP   A 1 791 ? 6.829   61.288  96.243  1.00 55.46  ?  772 ASP   A O   1 
ATOM   4729 C CB  . ASP   A 1 791 ? 9.076   59.854  94.491  1.00 47.04  ?  772 ASP   A CB  1 
ATOM   4730 C CG  . ASP   A 1 791 ? 10.553  60.006  94.445  1.00 52.94  ?  772 ASP   A CG  1 
ATOM   4731 O OD1 . ASP   A 1 791 ? 11.149  60.261  95.517  1.00 52.18  ?  772 ASP   A OD1 1 
ATOM   4732 O OD2 . ASP   A 1 791 ? 11.118  59.870  93.342  1.00 58.55  ?  772 ASP   A OD2 1 
ATOM   4733 N N   . TYR   A 1 792 ? 6.194   59.195  95.704  1.00 57.04  ?  773 TYR   A N   1 
ATOM   4734 C CA  . TYR   A 1 792 ? 4.792   59.546  95.846  1.00 56.20  ?  773 TYR   A CA  1 
ATOM   4735 C C   . TYR   A 1 792 ? 4.478   59.886  97.306  1.00 59.51  ?  773 TYR   A C   1 
ATOM   4736 O O   . TYR   A 1 792 ? 3.661   60.774  97.575  1.00 62.30  ?  773 TYR   A O   1 
ATOM   4737 C CB  . TYR   A 1 792 ? 3.921   58.405  95.316  1.00 52.01  ?  773 TYR   A CB  1 
ATOM   4738 C CG  . TYR   A 1 792 ? 3.863   58.277  93.798  1.00 59.16  ?  773 TYR   A CG  1 
ATOM   4739 C CD1 . TYR   A 1 792 ? 4.787   57.512  93.100  1.00 62.33  ?  773 TYR   A CD1 1 
ATOM   4740 C CD2 . TYR   A 1 792 ? 2.861   58.888  93.064  1.00 61.26  ?  773 TYR   A CD2 1 
ATOM   4741 C CE1 . TYR   A 1 792 ? 4.719   57.371  91.699  1.00 64.77  ?  773 TYR   A CE1 1 
ATOM   4742 C CE2 . TYR   A 1 792 ? 2.784   58.759  91.675  1.00 62.45  ?  773 TYR   A CE2 1 
ATOM   4743 C CZ  . TYR   A 1 792 ? 3.711   57.995  90.989  1.00 69.05  ?  773 TYR   A CZ  1 
ATOM   4744 O OH  . TYR   A 1 792 ? 3.629   57.868  89.593  1.00 68.51  ?  773 TYR   A OH  1 
ATOM   4745 N N   . ASP   A 1 793 ? 5.163   59.243  98.260  1.00 57.44  ?  774 ASP   A N   1 
ATOM   4746 C CA  . ASP   A 1 793 ? 4.945   59.564  99.666  1.00 55.97  ?  774 ASP   A CA  1 
ATOM   4747 C C   . ASP   A 1 793 ? 5.554   60.907  100.047 1.00 56.52  ?  774 ASP   A C   1 
ATOM   4748 O O   . ASP   A 1 793 ? 4.882   61.745  100.661 1.00 55.72  ?  774 ASP   A O   1 
ATOM   4749 C CB  . ASP   A 1 793 ? 5.505   58.479  100.571 1.00 57.01  ?  774 ASP   A CB  1 
ATOM   4750 C CG  . ASP   A 1 793 ? 4.599   57.282  100.648 1.00 66.70  ?  774 ASP   A CG  1 
ATOM   4751 O OD1 . ASP   A 1 793 ? 5.108   56.141  100.815 1.00 70.00  ?  774 ASP   A OD1 1 
ATOM   4752 O OD2 . ASP   A 1 793 ? 3.374   57.487  100.426 1.00 73.97  ?  774 ASP   A OD2 1 
ATOM   4753 N N   . LEU   A 1 794 ? 6.841   61.099  99.750  1.00 52.99  ?  775 LEU   A N   1 
ATOM   4754 C CA  . LEU   A 1 794 ? 7.440   62.427  99.794  1.00 51.45  ?  775 LEU   A CA  1 
ATOM   4755 C C   . LEU   A 1 794 ? 6.484   63.510  99.298  1.00 57.61  ?  775 LEU   A C   1 
ATOM   4756 O O   . LEU   A 1 794 ? 6.268   64.513  99.991  1.00 57.38  ?  775 LEU   A O   1 
ATOM   4757 C CB  . LEU   A 1 794 ? 8.711   62.450  98.962  1.00 50.88  ?  775 LEU   A CB  1 
ATOM   4758 C CG  . LEU   A 1 794 ? 9.864   61.639  99.530  1.00 48.37  ?  775 LEU   A CG  1 
ATOM   4759 C CD1 . LEU   A 1 794 ? 11.062  61.744  98.592  1.00 51.88  ?  775 LEU   A CD1 1 
ATOM   4760 C CD2 . LEU   A 1 794 ? 10.213  62.108  100.909 1.00 42.04  ?  775 LEU   A CD2 1 
ATOM   4761 N N   . MET   A 1 795 ? 5.883   63.333  98.109  1.00 52.47  ?  776 MET   A N   1 
ATOM   4762 C CA  . MET   A 1 795 ? 4.960   64.367  97.640  1.00 54.09  ?  776 MET   A CA  1 
ATOM   4763 C C   . MET   A 1 795 ? 3.828   64.605  98.615  1.00 54.74  ?  776 MET   A C   1 
ATOM   4764 O O   . MET   A 1 795 ? 3.298   65.716  98.672  1.00 59.63  ?  776 MET   A O   1 
ATOM   4765 C CB  . MET   A 1 795 ? 4.344   64.038  96.281  1.00 61.61  ?  776 MET   A CB  1 
ATOM   4766 C CG  . MET   A 1 795 ? 5.331   63.999  95.151  1.00 63.31  ?  776 MET   A CG  1 
ATOM   4767 S SD  . MET   A 1 795 ? 5.971   65.613  94.745  1.00 67.34  ?  776 MET   A SD  1 
ATOM   4768 C CE  . MET   A 1 795 ? 4.613   66.705  95.187  1.00 64.26  ?  776 MET   A CE  1 
ATOM   4769 N N   . ALA   A 1 796 ? 3.438   63.594  99.383  1.00 54.33  ?  777 ALA   A N   1 
ATOM   4770 C CA  . ALA   A 1 796 ? 2.295   63.781  100.261 1.00 55.41  ?  777 ALA   A CA  1 
ATOM   4771 C C   . ALA   A 1 796 ? 2.646   64.461  101.588 1.00 54.48  ?  777 ALA   A C   1 
ATOM   4772 O O   . ALA   A 1 796 ? 1.724   64.820  102.331 1.00 56.47  ?  777 ALA   A O   1 
ATOM   4773 C CB  . ALA   A 1 796 ? 1.606   62.432  100.509 1.00 47.85  ?  777 ALA   A CB  1 
ATOM   4774 N N   . GLN   A 1 797 ? 3.936   64.669  101.894 1.00 51.74  ?  778 GLN   A N   1 
ATOM   4775 C CA  . GLN   A 1 797 ? 4.327   65.218  103.200 1.00 53.93  ?  778 GLN   A CA  1 
ATOM   4776 C C   . GLN   A 1 797 ? 3.942   66.693  103.294 1.00 60.52  ?  778 GLN   A C   1 
ATOM   4777 O O   . GLN   A 1 797 ? 4.185   67.453  102.346 1.00 60.28  ?  778 GLN   A O   1 
ATOM   4778 C CB  . GLN   A 1 797 ? 5.832   65.070  103.401 1.00 58.40  ?  778 GLN   A CB  1 
ATOM   4779 C CG  . GLN   A 1 797 ? 6.277   63.766  104.088 1.00 70.84  ?  778 GLN   A CG  1 
ATOM   4780 C CD  . GLN   A 1 797 ? 5.777   63.649  105.513 1.00 88.68  ?  778 GLN   A CD  1 
ATOM   4781 O OE1 . GLN   A 1 797 ? 6.043   64.533  106.335 1.00 84.42  ?  778 GLN   A OE1 1 
ATOM   4782 N NE2 . GLN   A 1 797 ? 5.062   62.550  105.824 1.00 89.06  ?  778 GLN   A NE2 1 
ATOM   4783 N N   . PRO   A 1 798 ? 3.337   67.137  104.394 1.00 57.74  ?  779 PRO   A N   1 
ATOM   4784 C CA  . PRO   A 1 798 ? 3.081   68.575  104.553 1.00 60.12  ?  779 PRO   A CA  1 
ATOM   4785 C C   . PRO   A 1 798 ? 4.373   69.327  104.822 1.00 58.44  ?  779 PRO   A C   1 
ATOM   4786 O O   . PRO   A 1 798 ? 5.357   68.744  105.277 1.00 61.94  ?  779 PRO   A O   1 
ATOM   4787 C CB  . PRO   A 1 798 ? 2.142   68.643  105.758 1.00 57.60  ?  779 PRO   A CB  1 
ATOM   4788 C CG  . PRO   A 1 798 ? 2.402   67.376  106.479 1.00 56.62  ?  779 PRO   A CG  1 
ATOM   4789 C CD  . PRO   A 1 798 ? 2.689   66.348  105.443 1.00 55.59  ?  779 PRO   A CD  1 
ATOM   4790 N N   . ILE   A 1 799 ? 4.325   70.634  104.622 1.00 51.73  ?  780 ILE   A N   1 
ATOM   4791 C CA  . ILE   A 1 799 ? 5.516   71.476  104.874 1.00 57.53  ?  780 ILE   A CA  1 
ATOM   4792 C C   . ILE   A 1 799 ? 5.293   72.330  106.111 1.00 59.27  ?  780 ILE   A C   1 
ATOM   4793 O O   . ILE   A 1 799 ? 4.259   72.902  106.254 1.00 56.70  ?  780 ILE   A O   1 
ATOM   4794 C CB  . ILE   A 1 799 ? 5.812   72.315  103.643 1.00 58.69  ?  780 ILE   A CB  1 
ATOM   4795 C CG1 . ILE   A 1 799 ? 5.797   71.422  102.416 1.00 57.23  ?  780 ILE   A CG1 1 
ATOM   4796 C CG2 . ILE   A 1 799 ? 7.144   72.989  103.799 1.00 53.95  ?  780 ILE   A CG2 1 
ATOM   4797 C CD1 . ILE   A 1 799 ? 7.147   71.179  101.879 1.00 60.96  ?  780 ILE   A CD1 1 
ATOM   4798 N N   . THR   A 1 800 ? 6.267   72.355  106.994 1.00 62.56  ?  781 THR   A N   1 
ATOM   4799 C CA  . THR   A 1 800 ? 6.132   73.152  108.218 1.00 63.75  ?  781 THR   A CA  1 
ATOM   4800 C C   . THR   A 1 800 ? 7.117   74.298  108.130 1.00 61.82  ?  781 THR   A C   1 
ATOM   4801 O O   . THR   A 1 800 ? 8.291   74.042  108.051 1.00 61.63  ?  781 THR   A O   1 
ATOM   4802 C CB  . THR   A 1 800 ? 6.467   72.296  109.427 1.00 58.98  ?  781 THR   A CB  1 
ATOM   4803 O OG1 . THR   A 1 800 ? 5.473   71.287  109.494 1.00 66.30  ?  781 THR   A OG1 1 
ATOM   4804 C CG2 . THR   A 1 800 ? 6.374   73.086  110.698 1.00 68.54  ?  781 THR   A CG2 1 
ATOM   4805 N N   . PRO   A 1 801 ? 6.667   75.552  108.232 1.00 61.99  ?  782 PRO   A N   1 
ATOM   4806 C CA  . PRO   A 1 801 ? 7.534   76.700  108.108 1.00 58.97  ?  782 PRO   A CA  1 
ATOM   4807 C C   . PRO   A 1 801 ? 8.416   76.925  109.330 1.00 65.10  ?  782 PRO   A C   1 
ATOM   4808 O O   . PRO   A 1 801 ? 8.167   76.386  110.320 1.00 66.11  ?  782 PRO   A O   1 
ATOM   4809 C CB  . PRO   A 1 801 ? 6.529   77.830  108.118 1.00 58.83  ?  782 PRO   A CB  1 
ATOM   4810 C CG  . PRO   A 1 801 ? 5.465   77.303  108.992 1.00 59.27  ?  782 PRO   A CG  1 
ATOM   4811 C CD  . PRO   A 1 801 ? 5.295   75.910  108.476 1.00 58.99  ?  782 PRO   A CD  1 
ATOM   4812 N N   . GLY   A 1 802 ? 9.433   77.757  109.206 1.00 61.67  ?  783 GLY   A N   1 
ATOM   4813 C CA  . GLY   A 1 802 ? 10.314  78.040  110.347 1.00 65.61  ?  783 GLY   A CA  1 
ATOM   4814 C C   . GLY   A 1 802 ? 9.664   78.938  111.375 1.00 66.45  ?  783 GLY   A C   1 
ATOM   4815 O O   . GLY   A 1 802 ? 8.690   79.582  111.079 1.00 64.62  ?  783 GLY   A O   1 
ATOM   4816 N N   . PRO   A 1 803 ? 10.199  79.051  112.595 1.00 69.68  ?  784 PRO   A N   1 
ATOM   4817 C CA  . PRO   A 1 803 ? 9.588   79.894  113.593 1.00 71.62  ?  784 PRO   A CA  1 
ATOM   4818 C C   . PRO   A 1 803 ? 9.752   81.358  113.183 1.00 78.91  ?  784 PRO   A C   1 
ATOM   4819 O O   . PRO   A 1 803 ? 10.748  81.690  112.629 1.00 73.61  ?  784 PRO   A O   1 
ATOM   4820 C CB  . PRO   A 1 803 ? 10.471  79.600  114.789 1.00 71.06  ?  784 PRO   A CB  1 
ATOM   4821 C CG  . PRO   A 1 803 ? 11.799  79.362  114.170 1.00 69.48  ?  784 PRO   A CG  1 
ATOM   4822 C CD  . PRO   A 1 803 ? 11.460  78.482  113.000 1.00 65.91  ?  784 PRO   A CD  1 
ATOM   4823 N N   . SER   A 1 804 ? 8.740   82.179  113.431 1.00 79.82  ?  785 SER   A N   1 
ATOM   4824 C CA  . SER   A 1 804 ? 8.811   83.610  113.060 1.00 82.33  ?  785 SER   A CA  1 
ATOM   4825 C C   . SER   A 1 804 ? 9.878   84.299  113.903 1.00 90.92  ?  785 SER   A C   1 
ATOM   4826 O O   . SER   A 1 804 ? 10.688  85.031  113.363 1.00 87.19  ?  785 SER   A O   1 
ATOM   4827 C CB  . SER   A 1 804 ? 7.481   84.252  113.263 1.00 87.21  ?  785 SER   A CB  1 
ATOM   4828 O OG  . SER   A 1 804 ? 6.721   84.243  112.068 1.00 76.21  ?  785 SER   A OG  1 
ATOM   4829 N N   . ILE   A 1 805 ? 9.889   84.004  115.194 1.00 96.65  ?  786 ILE   A N   1 
ATOM   4830 C CA  . ILE   A 1 805 ? 10.870  84.606  116.129 1.00 94.32  ?  786 ILE   A CA  1 
ATOM   4831 C C   . ILE   A 1 805 ? 11.855  83.499  116.438 1.00 96.11  ?  786 ILE   A C   1 
ATOM   4832 O O   . ILE   A 1 805 ? 11.404  82.458  116.820 1.00 96.89  ?  786 ILE   A O   1 
ATOM   4833 C CB  . ILE   A 1 805 ? 10.139  85.008  117.412 1.00 94.60  ?  786 ILE   A CB  1 
ATOM   4834 C CG1 . ILE   A 1 805 ? 8.744   85.538  117.102 1.00 99.76  ?  786 ILE   A CG1 1 
ATOM   4835 C CG2 . ILE   A 1 805 ? 10.951  86.006  118.202 1.00 93.12  ?  786 ILE   A CG2 1 
ATOM   4836 C CD1 . ILE   A 1 805 ? 7.634   84.712  117.695 1.00 96.59  ?  786 ILE   A CD1 1 
ATOM   4837 N N   . PRO   A 1 806 ? 13.177  83.677  116.326 1.00 101.21 ?  787 PRO   A N   1 
ATOM   4838 C CA  . PRO   A 1 806 ? 14.090  82.589  116.618 1.00 102.38 ?  787 PRO   A CA  1 
ATOM   4839 C C   . PRO   A 1 806 ? 13.925  82.190  118.085 1.00 97.76  ?  787 PRO   A C   1 
ATOM   4840 O O   . PRO   A 1 806 ? 13.826  83.049  118.924 1.00 87.90  ?  787 PRO   A O   1 
ATOM   4841 C CB  . PRO   A 1 806 ? 15.468  83.203  116.384 1.00 98.04  ?  787 PRO   A CB  1 
ATOM   4842 C CG  . PRO   A 1 806 ? 15.223  84.674  116.541 1.00 102.03 ?  787 PRO   A CG  1 
ATOM   4843 C CD  . PRO   A 1 806 ? 13.850  84.898  115.952 1.00 98.70  ?  787 PRO   A CD  1 
ATOM   4844 N N   . GLY   A 1 807 ? 13.919  80.885  118.335 1.00 94.81  ?  788 GLY   A N   1 
ATOM   4845 C CA  . GLY   A 1 807 ? 13.743  80.358  119.696 1.00 93.27  ?  788 GLY   A CA  1 
ATOM   4846 C C   . GLY   A 1 807 ? 12.285  80.193  120.053 1.00 86.65  ?  788 GLY   A C   1 
ATOM   4847 O O   . GLY   A 1 807 ? 11.999  79.935  121.209 1.00 80.76  ?  788 GLY   A O   1 
ATOM   4848 N N   . ALA   A 1 808 ? 11.392  80.433  119.110 1.00 82.81  ?  789 ALA   A N   1 
ATOM   4849 C CA  . ALA   A 1 808 ? 9.973   80.191  119.405 1.00 77.40  ?  789 ALA   A CA  1 
ATOM   4850 C C   . ALA   A 1 808 ? 9.726   78.701  119.242 1.00 86.12  ?  789 ALA   A C   1 
ATOM   4851 O O   . ALA   A 1 808 ? 10.433  78.066  118.481 1.00 89.01  ?  789 ALA   A O   1 
ATOM   4852 C CB  . ALA   A 1 808 ? 9.100   80.980  118.491 1.00 81.39  ?  789 ALA   A CB  1 
ATOM   4853 N N   . PRO   A 1 809 ? 8.675   78.130  119.840 1.00 77.85  ?  790 PRO   A N   1 
ATOM   4854 C CA  . PRO   A 1 809 ? 8.439   76.721  119.745 1.00 75.02  ?  790 PRO   A CA  1 
ATOM   4855 C C   . PRO   A 1 809 ? 8.128   76.312  118.309 1.00 81.88  ?  790 PRO   A C   1 
ATOM   4856 O O   . PRO   A 1 809 ? 7.534   77.055  117.600 1.00 79.27  ?  790 PRO   A O   1 
ATOM   4857 C CB  . PRO   A 1 809 ? 7.196   76.546  120.600 1.00 75.97  ?  790 PRO   A CB  1 
ATOM   4858 C CG  . PRO   A 1 809 ? 6.517   77.853  120.481 1.00 77.18  ?  790 PRO   A CG  1 
ATOM   4859 C CD  . PRO   A 1 809 ? 7.661   78.822  120.587 1.00 79.83  ?  790 PRO   A CD  1 
ATOM   4860 N N   . GLN   A 1 810 ? 8.473   75.078  117.969 1.00 81.27  ?  791 GLN   A N   1 
ATOM   4861 C CA  . GLN   A 1 810 ? 8.273   74.580  116.593 1.00 83.58  ?  791 GLN   A CA  1 
ATOM   4862 C C   . GLN   A 1 810 ? 6.806   74.688  116.201 1.00 78.99  ?  791 GLN   A C   1 
ATOM   4863 O O   . GLN   A 1 810 ? 5.948   74.166  116.898 1.00 75.63  ?  791 GLN   A O   1 
ATOM   4864 C CB  . GLN   A 1 810 ? 8.635   73.106  116.553 1.00 81.24  ?  791 GLN   A CB  1 
ATOM   4865 C CG  . GLN   A 1 810 ? 7.925   72.362  115.448 1.00 83.93  ?  791 GLN   A CG  1 
ATOM   4866 C CD  . GLN   A 1 810 ? 8.932   72.089  114.372 1.00 89.50  ?  791 GLN   A CD  1 
ATOM   4867 O OE1 . GLN   A 1 810 ? 9.949   72.755  114.292 1.00 87.59  ?  791 GLN   A OE1 1 
ATOM   4868 N NE2 . GLN   A 1 810 ? 8.664   71.094  113.553 1.00 103.62 ?  791 GLN   A NE2 1 
ATOM   4869 N N   . PRO   A 1 811 ? 6.506   75.275  115.040 1.00 79.95  ?  792 PRO   A N   1 
ATOM   4870 C CA  . PRO   A 1 811 ? 5.147   75.446  114.611 1.00 80.71  ?  792 PRO   A CA  1 
ATOM   4871 C C   . PRO   A 1 811 ? 4.496   74.254  113.916 1.00 76.37  ?  792 PRO   A C   1 
ATOM   4872 O O   . PRO   A 1 811 ? 5.124   73.312  113.643 1.00 66.85  ?  792 PRO   A O   1 
ATOM   4873 C CB  . PRO   A 1 811 ? 5.229   76.644  113.670 1.00 66.22  ?  792 PRO   A CB  1 
ATOM   4874 C CG  . PRO   A 1 811 ? 6.603   76.563  113.110 1.00 69.22  ?  792 PRO   A CG  1 
ATOM   4875 C CD  . PRO   A 1 811 ? 7.462   75.862  114.131 1.00 73.24  ?  792 PRO   A CD  1 
ATOM   4876 N N   . ILE   A 1 812 ? 3.205   74.419  113.680 1.00 72.84  ?  793 ILE   A N   1 
ATOM   4877 C CA  . ILE   A 1 812 ? 2.246   73.522  113.001 1.00 64.83  ?  793 ILE   A CA  1 
ATOM   4878 C C   . ILE   A 1 812 ? 2.571   73.483  111.518 1.00 66.72  ?  793 ILE   A C   1 
ATOM   4879 O O   . ILE   A 1 812 ? 3.138   74.414  111.023 1.00 64.56  ?  793 ILE   A O   1 
ATOM   4880 C CB  . ILE   A 1 812 ? 0.878   74.189  113.156 1.00 71.00  ?  793 ILE   A CB  1 
ATOM   4881 C CG1 . ILE   A 1 812 ? 0.697   74.772  114.552 1.00 79.62  ?  793 ILE   A CG1 1 
ATOM   4882 C CG2 . ILE   A 1 812 ? -0.228  73.228  112.815 1.00 73.96  ?  793 ILE   A CG2 1 
ATOM   4883 C CD1 . ILE   A 1 812 ? 1.349   76.104  114.746 1.00 77.60  ?  793 ILE   A CD1 1 
ATOM   4884 N N   . PRO   A 1 813 ? 2.254   72.405  110.796 1.00 75.70  ?  794 PRO   A N   1 
ATOM   4885 C CA  . PRO   A 1 813 ? 2.447   72.376  109.368 1.00 67.59  ?  794 PRO   A CA  1 
ATOM   4886 C C   . PRO   A 1 813 ? 1.375   73.273  108.753 1.00 62.73  ?  794 PRO   A C   1 
ATOM   4887 O O   . PRO   A 1 813 ? 0.306   73.241  109.227 1.00 60.46  ?  794 PRO   A O   1 
ATOM   4888 C CB  . PRO   A 1 813 ? 2.141   70.916  109.090 1.00 55.90  ?  794 PRO   A CB  1 
ATOM   4889 C CG  . PRO   A 1 813 ? 2.495   70.260  110.363 1.00 55.73  ?  794 PRO   A CG  1 
ATOM   4890 C CD  . PRO   A 1 813 ? 1.792   71.154  111.336 1.00 73.21  ?  794 PRO   A CD  1 
ATOM   4891 N N   . ARG   A 1 814 ? 1.705   74.033  107.717 1.00 57.78  ?  795 ARG   A N   1 
ATOM   4892 C CA  . ARG   A 1 814 ? 0.712   74.958  107.128 1.00 59.86  ?  795 ARG   A CA  1 
ATOM   4893 C C   . ARG   A 1 814 ? 0.415   74.638  105.670 1.00 52.68  ?  795 ARG   A C   1 
ATOM   4894 O O   . ARG   A 1 814 ? -0.635  74.996  105.226 1.00 48.01  ?  795 ARG   A O   1 
ATOM   4895 C CB  . ARG   A 1 814 ? 1.281   76.369  107.193 1.00 58.39  ?  795 ARG   A CB  1 
ATOM   4896 C CG  . ARG   A 1 814 ? 1.585   76.856  108.594 1.00 57.09  ?  795 ARG   A CG  1 
ATOM   4897 C CD  . ARG   A 1 814 ? 0.410   77.645  109.083 1.00 58.61  ?  795 ARG   A CD  1 
ATOM   4898 N NE  . ARG   A 1 814 ? 0.556   77.993  110.468 1.00 62.09  ?  795 ARG   A NE  1 
ATOM   4899 C CZ  . ARG   A 1 814 ? -0.446  78.344  111.227 1.00 61.69  ?  795 ARG   A CZ  1 
ATOM   4900 N NH1 . ARG   A 1 814 ? -1.664  78.379  110.741 1.00 57.17  ?  795 ARG   A NH1 1 
ATOM   4901 N NH2 . ARG   A 1 814 ? -0.238  78.658  112.476 1.00 63.72  ?  795 ARG   A NH2 1 
ATOM   4902 N N   . LEU   A 1 815 ? 1.320   73.954  104.988 1.00 52.88  ?  796 LEU   A N   1 
ATOM   4903 C CA  . LEU   A 1 815 ? 1.176   73.643  103.546 1.00 53.51  ?  796 LEU   A CA  1 
ATOM   4904 C C   . LEU   A 1 815 ? 1.002   72.143  103.342 1.00 55.20  ?  796 LEU   A C   1 
ATOM   4905 O O   . LEU   A 1 815 ? 1.922   71.432  103.610 1.00 51.14  ?  796 LEU   A O   1 
ATOM   4906 C CB  . LEU   A 1 815 ? 2.446   74.133  102.866 1.00 50.76  ?  796 LEU   A CB  1 
ATOM   4907 C CG  . LEU   A 1 815 ? 2.467   74.027  101.358 1.00 49.67  ?  796 LEU   A CG  1 
ATOM   4908 C CD1 . LEU   A 1 815 ? 1.153   74.480  100.801 1.00 50.74  ?  796 LEU   A CD1 1 
ATOM   4909 C CD2 . LEU   A 1 815 ? 3.599   74.842  100.803 1.00 42.27  ?  796 LEU   A CD2 1 
ATOM   4910 N N   . PHE   A 1 816 ? -0.143  71.738  102.802 1.00 53.75  ?  797 PHE   A N   1 
ATOM   4911 C CA  . PHE   A 1 816 ? -0.540  70.343  102.588 1.00 51.58  ?  797 PHE   A CA  1 
ATOM   4912 C C   . PHE   A 1 816 ? -0.757  70.047  101.096 1.00 51.23  ?  797 PHE   A C   1 
ATOM   4913 O O   . PHE   A 1 816 ? -1.153  70.918  100.322 1.00 53.06  ?  797 PHE   A O   1 
ATOM   4914 C CB  . PHE   A 1 816 ? -1.834  70.036  103.365 1.00 49.26  ?  797 PHE   A CB  1 
ATOM   4915 C CG  . PHE   A 1 816 ? -1.727  70.258  104.844 1.00 51.90  ?  797 PHE   A CG  1 
ATOM   4916 C CD1 . PHE   A 1 816 ? -1.860  71.535  105.381 1.00 61.53  ?  797 PHE   A CD1 1 
ATOM   4917 C CD2 . PHE   A 1 816 ? -1.527  69.195  105.711 1.00 54.10  ?  797 PHE   A CD2 1 
ATOM   4918 C CE1 . PHE   A 1 816 ? -1.764  71.753  106.760 1.00 53.81  ?  797 PHE   A CE1 1 
ATOM   4919 C CE2 . PHE   A 1 816 ? -1.431  69.386  107.070 1.00 52.12  ?  797 PHE   A CE2 1 
ATOM   4920 C CZ  . PHE   A 1 816 ? -1.547  70.665  107.604 1.00 58.91  ?  797 PHE   A CZ  1 
ATOM   4921 N N   . PHE   A 1 817 ? -0.536  68.797  100.683 1.00 61.58  ?  798 PHE   A N   1 
ATOM   4922 C CA  . PHE   A 1 817 ? -0.577  68.426  99.265  1.00 51.14  ?  798 PHE   A CA  1 
ATOM   4923 C C   . PHE   A 1 817 ? -1.492  67.232  99.015  1.00 51.82  ?  798 PHE   A C   1 
ATOM   4924 O O   . PHE   A 1 817 ? -1.477  66.246  99.761  1.00 48.29  ?  798 PHE   A O   1 
ATOM   4925 C CB  . PHE   A 1 817 ? 0.794   68.054  98.759  1.00 47.49  ?  798 PHE   A CB  1 
ATOM   4926 C CG  . PHE   A 1 817 ? 1.768   69.156  98.801  1.00 52.29  ?  798 PHE   A CG  1 
ATOM   4927 C CD1 . PHE   A 1 817 ? 1.998   69.933  97.681  1.00 56.37  ?  798 PHE   A CD1 1 
ATOM   4928 C CD2 . PHE   A 1 817 ? 2.469   69.424  99.959  1.00 54.40  ?  798 PHE   A CD2 1 
ATOM   4929 C CE1 . PHE   A 1 817 ? 2.921   70.956  97.709  1.00 47.95  ?  798 PHE   A CE1 1 
ATOM   4930 C CE2 . PHE   A 1 817 ? 3.391   70.467  99.999  1.00 55.29  ?  798 PHE   A CE2 1 
ATOM   4931 C CZ  . PHE   A 1 817 ? 3.622   71.223  98.875  1.00 49.12  ?  798 PHE   A CZ  1 
ATOM   4932 N N   . ALA   A 1 818 ? -2.267  67.304  97.941  1.00 48.51  ?  799 ALA   A N   1 
ATOM   4933 C CA  . ALA   A 1 818 ? -3.104  66.186  97.540  1.00 49.02  ?  799 ALA   A CA  1 
ATOM   4934 C C   . ALA   A 1 818 ? -3.112  66.140  96.021  1.00 49.30  ?  799 ALA   A C   1 
ATOM   4935 O O   . ALA   A 1 818 ? -2.465  66.958  95.361  1.00 50.82  ?  799 ALA   A O   1 
ATOM   4936 C CB  . ALA   A 1 818 ? -4.522  66.288  98.121  1.00 46.92  ?  799 ALA   A CB  1 
ATOM   4937 N N   . GLY   A 1 819 ? -3.822  65.165  95.469  1.00 52.49  ?  800 GLY   A N   1 
ATOM   4938 C CA  . GLY   A 1 819 ? -3.810  64.961  94.036  1.00 59.04  ?  800 GLY   A CA  1 
ATOM   4939 C C   . GLY   A 1 819 ? -3.197  63.611  93.661  1.00 57.09  ?  800 GLY   A C   1 
ATOM   4940 O O   . GLY   A 1 819 ? -2.495  62.959  94.456  1.00 50.03  ?  800 GLY   A O   1 
ATOM   4941 N N   . GLU   A 1 820 ? -3.463  63.200  92.398  1.00 51.37  ?  801 GLU   A N   1 
ATOM   4942 C CA  . GLU   A 1 820 ? -3.093  61.862  91.945  1.00 48.89  ?  801 GLU   A CA  1 
ATOM   4943 C C   . GLU   A 1 820 ? -1.602  61.610  92.081  1.00 50.01  ?  801 GLU   A C   1 
ATOM   4944 O O   . GLU   A 1 820 ? -1.198  60.485  92.380  1.00 51.20  ?  801 GLU   A O   1 
ATOM   4945 C CB  . GLU   A 1 820 ? -3.553  61.617  90.505  1.00 48.55  ?  801 GLU   A CB  1 
ATOM   4946 C CG  . GLU   A 1 820 ? -2.996  62.537  89.441  1.00 54.68  ?  801 GLU   A CG  1 
ATOM   4947 C CD  . GLU   A 1 820 ? -1.678  62.055  88.855  1.00 53.39  ?  801 GLU   A CD  1 
ATOM   4948 O OE1 . GLU   A 1 820 ? -1.182  60.984  89.267  1.00 47.31  ?  801 GLU   A OE1 1 
ATOM   4949 O OE2 . GLU   A 1 820 ? -1.146  62.745  87.953  1.00 56.98  ?  801 GLU   A OE2 1 
ATOM   4950 N N   . HIS   A 1 821 ? -0.781  62.618  91.914  1.00 44.51  ?  802 HIS   A N   1 
ATOM   4951 C CA  . HIS   A 1 821 ? 0.645   62.361  92.128  1.00 47.63  ?  802 HIS   A CA  1 
ATOM   4952 C C   . HIS   A 1 821 ? 1.001   62.185  93.608  1.00 51.48  ?  802 HIS   A C   1 
ATOM   4953 O O   . HIS   A 1 821 ? 2.208   62.138  93.891  1.00 53.05  ?  802 HIS   A O   1 
ATOM   4954 C CB  . HIS   A 1 821 ? 1.482   63.494  91.536  1.00 48.78  ?  802 HIS   A CB  1 
ATOM   4955 C CG  . HIS   A 1 821 ? 1.124   64.825  92.102  1.00 52.34  ?  802 HIS   A CG  1 
ATOM   4956 N ND1 . HIS   A 1 821 ? -0.149  65.344  92.009  1.00 54.33  ?  802 HIS   A ND1 1 
ATOM   4957 C CD2 . HIS   A 1 821 ? 1.833   65.700  92.846  1.00 47.95  ?  802 HIS   A CD2 1 
ATOM   4958 C CE1 . HIS   A 1 821 ? -0.204  66.490  92.654  1.00 49.54  ?  802 HIS   A CE1 1 
ATOM   4959 N NE2 . HIS   A 1 821 ? 0.989   66.733  93.165  1.00 53.01  ?  802 HIS   A NE2 1 
ATOM   4960 N N   . THR   A 1 822 ? 0.075   62.087  94.568  1.00 51.88  ?  803 THR   A N   1 
ATOM   4961 C CA  . THR   A 1 822 ? 0.438   62.008  95.984  1.00 53.30  ?  803 THR   A CA  1 
ATOM   4962 C C   . THR   A 1 822 ? 0.012   60.716  96.666  1.00 54.36  ?  803 THR   A C   1 
ATOM   4963 O O   . THR   A 1 822 ? 0.190   60.602  97.881  1.00 60.22  ?  803 THR   A O   1 
ATOM   4964 C CB  . THR   A 1 822 ? -0.172  63.179  96.790  1.00 53.81  ?  803 THR   A CB  1 
ATOM   4965 O OG1 . THR   A 1 822 ? -1.606  63.209  96.630  1.00 49.20  ?  803 THR   A OG1 1 
ATOM   4966 C CG2 . THR   A 1 822 ? 0.439   64.527  96.371  1.00 50.64  ?  803 THR   A CG2 1 
ATOM   4967 N N   . ILE   A 1 823 ? -0.568  59.760  95.950  1.00 52.54  ?  804 ILE   A N   1 
ATOM   4968 C CA  . ILE   A 1 823 ? -1.130  58.557  96.566  1.00 48.09  ?  804 ILE   A CA  1 
ATOM   4969 C C   . ILE   A 1 823 ? -0.441  57.353  95.919  1.00 52.07  ?  804 ILE   A C   1 
ATOM   4970 O O   . ILE   A 1 823 ? -0.797  56.865  94.840  1.00 51.65  ?  804 ILE   A O   1 
ATOM   4971 C CB  . ILE   A 1 823 ? -2.662  58.517  96.469  1.00 44.52  ?  804 ILE   A CB  1 
ATOM   4972 C CG1 . ILE   A 1 823 ? -3.238  57.375  97.280  1.00 42.04  ?  804 ILE   A CG1 1 
ATOM   4973 C CG2 . ILE   A 1 823 ? -3.206  58.579  95.028  1.00 45.31  ?  804 ILE   A CG2 1 
ATOM   4974 C CD1 . ILE   A 1 823 ? -4.630  57.680  97.749  1.00 42.65  ?  804 ILE   A CD1 1 
ATOM   4975 N N   . ARG   A 1 824 ? 0.617   56.897  96.588  1.00 58.31  ?  805 ARG   A N   1 
ATOM   4976 C CA  . ARG   A 1 824 ? 1.466   55.790  96.152  1.00 53.44  ?  805 ARG   A CA  1 
ATOM   4977 C C   . ARG   A 1 824 ? 0.698   54.578  95.637  1.00 54.80  ?  805 ARG   A C   1 
ATOM   4978 O O   . ARG   A 1 824 ? 0.991   54.063  94.557  1.00 58.62  ?  805 ARG   A O   1 
ATOM   4979 C CB  . ARG   A 1 824 ? 2.350   55.410  97.335  1.00 53.86  ?  805 ARG   A CB  1 
ATOM   4980 C CG  . ARG   A 1 824 ? 3.092   54.172  97.221  1.00 60.47  ?  805 ARG   A CG  1 
ATOM   4981 C CD  . ARG   A 1 824 ? 3.988   53.984  98.442  1.00 57.59  ?  805 ARG   A CD  1 
ATOM   4982 N NE  . ARG   A 1 824 ? 5.069   53.073  98.082  1.00 61.17  ?  805 ARG   A NE  1 
ATOM   4983 C CZ  . ARG   A 1 824 ? 6.281   53.112  98.606  1.00 62.29  ?  805 ARG   A CZ  1 
ATOM   4984 N NH1 . ARG   A 1 824 ? 6.558   54.004  99.543  1.00 68.83  ?  805 ARG   A NH1 1 
ATOM   4985 N NH2 . ARG   A 1 824 ? 7.210   52.257  98.199  1.00 65.22  ?  805 ARG   A NH2 1 
ATOM   4986 N N   . ASN   A 1 825 ? -0.294  54.100  96.383  1.00 60.12  ?  806 ASN   A N   1 
ATOM   4987 C CA  . ASN   A 1 825 ? -0.972  52.875  95.954  1.00 57.54  ?  806 ASN   A CA  1 
ATOM   4988 C C   . ASN   A 1 825 ? -2.036  53.078  94.879  1.00 58.25  ?  806 ASN   A C   1 
ATOM   4989 O O   . ASN   A 1 825 ? -2.556  52.069  94.375  1.00 59.60  ?  806 ASN   A O   1 
ATOM   4990 C CB  . ASN   A 1 825 ? -1.578  52.162  97.160  1.00 46.51  ?  806 ASN   A CB  1 
ATOM   4991 C CG  . ASN   A 1 825 ? -0.512  51.669  98.107  1.00 58.49  ?  806 ASN   A CG  1 
ATOM   4992 O OD1 . ASN   A 1 825 ? 0.688   51.745  97.790  1.00 62.43  ?  806 ASN   A OD1 1 
ATOM   4993 N ND2 . ASN   A 1 825 ? -0.921  51.158  99.268  1.00 52.73  ?  806 ASN   A ND2 1 
ATOM   4994 N N   . TYR   A 1 826 ? -2.402  54.331  94.525  1.00 44.28  ?  807 TYR   A N   1 
ATOM   4995 C CA  . TYR   A 1 826 ? -3.419  54.498  93.489  1.00 45.92  ?  807 TYR   A CA  1 
ATOM   4996 C C   . TYR   A 1 826 ? -3.121  55.700  92.598  1.00 51.47  ?  807 TYR   A C   1 
ATOM   4997 O O   . TYR   A 1 826 ? -4.039  56.488  92.314  1.00 47.07  ?  807 TYR   A O   1 
ATOM   4998 C CB  . TYR   A 1 826 ? -4.831  54.644  94.088  1.00 44.86  ?  807 TYR   A CB  1 
ATOM   4999 C CG  . TYR   A 1 826 ? -5.180  53.559  95.094  1.00 55.63  ?  807 TYR   A CG  1 
ATOM   5000 C CD1 . TYR   A 1 826 ? -6.012  52.497  94.752  1.00 60.82  ?  807 TYR   A CD1 1 
ATOM   5001 C CD2 . TYR   A 1 826 ? -4.670  53.587  96.383  1.00 52.72  ?  807 TYR   A CD2 1 
ATOM   5002 C CE1 . TYR   A 1 826 ? -6.314  51.493  95.659  1.00 54.61  ?  807 TYR   A CE1 1 
ATOM   5003 C CE2 . TYR   A 1 826 ? -4.953  52.586  97.277  1.00 61.96  ?  807 TYR   A CE2 1 
ATOM   5004 C CZ  . TYR   A 1 826 ? -5.779  51.539  96.915  1.00 59.17  ?  807 TYR   A CZ  1 
ATOM   5005 O OH  . TYR   A 1 826 ? -6.059  50.558  97.845  1.00 62.74  ?  807 TYR   A OH  1 
ATOM   5006 N N   . PRO   A 1 827 ? -1.894  55.860  92.094  1.00 49.30  ?  808 PRO   A N   1 
ATOM   5007 C CA  . PRO   A 1 827 ? -1.587  57.062  91.327  1.00 48.45  ?  808 PRO   A CA  1 
ATOM   5008 C C   . PRO   A 1 827 ? -2.326  57.069  90.004  1.00 49.27  ?  808 PRO   A C   1 
ATOM   5009 O O   . PRO   A 1 827 ? -2.911  56.076  89.582  1.00 55.40  ?  808 PRO   A O   1 
ATOM   5010 C CB  . PRO   A 1 827 ? -0.067  57.008  91.136  1.00 47.42  ?  808 PRO   A CB  1 
ATOM   5011 C CG  . PRO   A 1 827 ? 0.321   55.654  91.388  1.00 51.85  ?  808 PRO   A CG  1 
ATOM   5012 C CD  . PRO   A 1 827 ? -0.751  54.935  92.127  1.00 53.83  ?  808 PRO   A CD  1 
ATOM   5013 N N   . ALA   A 1 828 ? -2.362  58.258  89.414  1.00 51.75  ?  809 ALA   A N   1 
ATOM   5014 C CA  . ALA   A 1 828 ? -2.860  58.515  88.070  1.00 46.58  ?  809 ALA   A CA  1 
ATOM   5015 C C   . ALA   A 1 828 ? -4.251  57.932  87.820  1.00 53.84  ?  809 ALA   A C   1 
ATOM   5016 O O   . ALA   A 1 828 ? -4.559  57.431  86.740  1.00 62.21  ?  809 ALA   A O   1 
ATOM   5017 C CB  . ALA   A 1 828 ? -1.857  58.021  87.059  1.00 45.67  ?  809 ALA   A CB  1 
ATOM   5018 N N   . THR   A 1 829 ? -5.126  58.034  88.810  1.00 52.83  ?  810 THR   A N   1 
ATOM   5019 C CA  . THR   A 1 829 ? -6.519  57.642  88.639  1.00 55.71  ?  810 THR   A CA  1 
ATOM   5020 C C   . THR   A 1 829 ? -7.422  58.637  89.352  1.00 55.81  ?  810 THR   A C   1 
ATOM   5021 O O   . THR   A 1 829 ? -6.978  59.394  90.219  1.00 54.41  ?  810 THR   A O   1 
ATOM   5022 C CB  . THR   A 1 829 ? -6.789  56.280  89.238  1.00 57.48  ?  810 THR   A CB  1 
ATOM   5023 O OG1 . THR   A 1 829 ? -6.662  56.397  90.664  1.00 56.59  ?  810 THR   A OG1 1 
ATOM   5024 C CG2 . THR   A 1 829 ? -5.800  55.250  88.720  1.00 58.54  ?  810 THR   A CG2 1 
ATOM   5025 N N   . VAL   A 1 830 ? -8.710  58.609  89.019  1.00 53.17  ?  811 VAL   A N   1 
ATOM   5026 C CA  . VAL   A 1 830 ? -9.644  59.467  89.737  1.00 49.80  ?  811 VAL   A CA  1 
ATOM   5027 C C   . VAL   A 1 830 ? -9.818  58.987  91.169  1.00 51.75  ?  811 VAL   A C   1 
ATOM   5028 O O   . VAL   A 1 830 ? -9.708  59.775  92.113  1.00 56.13  ?  811 VAL   A O   1 
ATOM   5029 C CB  . VAL   A 1 830 ? -10.988 59.559  89.008  1.00 49.64  ?  811 VAL   A CB  1 
ATOM   5030 C CG1 . VAL   A 1 830 ? -12.047 59.952  89.984  1.00 47.37  ?  811 VAL   A CG1 1 
ATOM   5031 C CG2 . VAL   A 1 830 ? -10.904 60.580  87.899  1.00 50.70  ?  811 VAL   A CG2 1 
ATOM   5032 N N   . HIS   A 1 831 ? -10.071 57.692  91.368  1.00 51.20  ?  812 HIS   A N   1 
ATOM   5033 C CA  . HIS   A 1 831 ? -10.231 57.220  92.740  1.00 51.45  ?  812 HIS   A CA  1 
ATOM   5034 C C   . HIS   A 1 831 ? -9.008  57.567  93.580  1.00 56.82  ?  812 HIS   A C   1 
ATOM   5035 O O   . HIS   A 1 831 ? -9.126  57.808  94.786  1.00 57.90  ?  812 HIS   A O   1 
ATOM   5036 C CB  . HIS   A 1 831 ? -10.503 55.704  92.821  1.00 57.42  ?  812 HIS   A CB  1 
ATOM   5037 C CG  . HIS   A 1 831 ? -9.488  54.837  92.124  1.00 57.40  ?  812 HIS   A CG  1 
ATOM   5038 N ND1 . HIS   A 1 831 ? -9.537  54.566  90.769  1.00 51.09  ?  812 HIS   A ND1 1 
ATOM   5039 C CD2 . HIS   A 1 831 ? -8.361  54.232  92.587  1.00 50.76  ?  812 HIS   A CD2 1 
ATOM   5040 C CE1 . HIS   A 1 831 ? -8.510  53.798  90.444  1.00 55.43  ?  812 HIS   A CE1 1 
ATOM   5041 N NE2 . HIS   A 1 831 ? -7.767  53.601  91.523  1.00 53.83  ?  812 HIS   A NE2 1 
ATOM   5042 N N   . GLY   A 1 832 ? -7.825  57.612  92.968  1.00 56.98  ?  813 GLY   A N   1 
ATOM   5043 C CA  . GLY   A 1 832 ? -6.643  57.958  93.737  1.00 54.29  ?  813 GLY   A CA  1 
ATOM   5044 C C   . GLY   A 1 832 ? -6.662  59.412  94.165  1.00 52.74  ?  813 GLY   A C   1 
ATOM   5045 O O   . GLY   A 1 832 ? -6.401  59.732  95.329  1.00 54.71  ?  813 GLY   A O   1 
ATOM   5046 N N   . ALA   A 1 833 ? -6.973  60.314  93.231  1.00 47.35  ?  814 ALA   A N   1 
ATOM   5047 C CA  . ALA   A 1 833 ? -7.080  61.722  93.590  1.00 52.08  ?  814 ALA   A CA  1 
ATOM   5048 C C   . ALA   A 1 833 ? -8.079  61.892  94.721  1.00 53.60  ?  814 ALA   A C   1 
ATOM   5049 O O   . ALA   A 1 833 ? -7.770  62.480  95.762  1.00 52.02  ?  814 ALA   A O   1 
ATOM   5050 C CB  . ALA   A 1 833 ? -7.484  62.566  92.371  1.00 52.34  ?  814 ALA   A CB  1 
ATOM   5051 N N   . LEU   A 1 834 ? -9.259  61.302  94.558  1.00 56.11  ?  815 LEU   A N   1 
ATOM   5052 C CA  . LEU   A 1 834 ? -10.287 61.383  95.580  1.00 51.75  ?  815 LEU   A CA  1 
ATOM   5053 C C   . LEU   A 1 834 ? -9.783  60.878  96.919  1.00 51.82  ?  815 LEU   A C   1 
ATOM   5054 O O   . LEU   A 1 834 ? -9.922  61.550  97.944  1.00 57.94  ?  815 LEU   A O   1 
ATOM   5055 C CB  . LEU   A 1 834 ? -11.506 60.599  95.133  1.00 53.24  ?  815 LEU   A CB  1 
ATOM   5056 C CG  . LEU   A 1 834 ? -12.690 60.628  96.080  1.00 54.93  ?  815 LEU   A CG  1 
ATOM   5057 C CD1 . LEU   A 1 834 ? -13.951 60.785  95.247  1.00 63.47  ?  815 LEU   A CD1 1 
ATOM   5058 C CD2 . LEU   A 1 834 ? -12.738 59.333  96.853  1.00 55.61  ?  815 LEU   A CD2 1 
ATOM   5059 N N   . LEU   A 1 835 ? -9.185  59.702  96.944  1.00 52.02  ?  816 LEU   A N   1 
ATOM   5060 C CA  . LEU   A 1 835 ? -8.700  59.243  98.232  1.00 54.49  ?  816 LEU   A CA  1 
ATOM   5061 C C   . LEU   A 1 835 ? -7.689  60.227  98.808  1.00 51.91  ?  816 LEU   A C   1 
ATOM   5062 O O   . LEU   A 1 835 ? -7.656  60.425  100.027 1.00 52.97  ?  816 LEU   A O   1 
ATOM   5063 C CB  . LEU   A 1 835 ? -8.107  57.837  98.118  1.00 52.87  ?  816 LEU   A CB  1 
ATOM   5064 C CG  . LEU   A 1 835 ? -9.122  56.734  97.810  1.00 53.84  ?  816 LEU   A CG  1 
ATOM   5065 C CD1 . LEU   A 1 835 ? -8.386  55.478  97.458  1.00 63.45  ?  816 LEU   A CD1 1 
ATOM   5066 C CD2 . LEU   A 1 835 ? -10.028 56.447  98.965  1.00 57.55  ?  816 LEU   A CD2 1 
ATOM   5067 N N   . SER   A 1 836 ? -6.890  60.892  97.961  1.00 48.99  ?  817 SER   A N   1 
ATOM   5068 C CA  . SER   A 1 836 ? -5.868  61.771  98.529  1.00 53.86  ?  817 SER   A CA  1 
ATOM   5069 C C   . SER   A 1 836 ? -6.507  63.011  99.138  1.00 53.33  ?  817 SER   A C   1 
ATOM   5070 O O   . SER   A 1 836 ? -6.087  63.470  100.209 1.00 51.49  ?  817 SER   A O   1 
ATOM   5071 C CB  . SER   A 1 836 ? -4.798  62.140  97.492  1.00 50.95  ?  817 SER   A CB  1 
ATOM   5072 O OG  . SER   A 1 836 ? -5.227  63.109  96.554  1.00 50.94  ?  817 SER   A OG  1 
ATOM   5073 N N   . GLY   A 1 837 ? -7.552  63.534  98.496  1.00 52.92  ?  818 GLY   A N   1 
ATOM   5074 C CA  . GLY   A 1 837 ? -8.335  64.588  99.119  1.00 51.79  ?  818 GLY   A CA  1 
ATOM   5075 C C   . GLY   A 1 837 ? -8.868  64.167  100.475 1.00 56.50  ?  818 GLY   A C   1 
ATOM   5076 O O   . GLY   A 1 837 ? -8.694  64.877  101.468 1.00 61.02  ?  818 GLY   A O   1 
ATOM   5077 N N   . LEU   A 1 838 ? -9.502  62.991  100.541 1.00 53.89  ?  819 LEU   A N   1 
ATOM   5078 C CA  . LEU   A 1 838 ? -10.031 62.522  101.813 1.00 47.19  ?  819 LEU   A CA  1 
ATOM   5079 C C   . LEU   A 1 838 ? -8.929  62.452  102.857 1.00 51.53  ?  819 LEU   A C   1 
ATOM   5080 O O   . LEU   A 1 838 ? -9.141  62.803  104.025 1.00 58.78  ?  819 LEU   A O   1 
ATOM   5081 C CB  . LEU   A 1 838 ? -10.686 61.154  101.643 1.00 49.31  ?  819 LEU   A CB  1 
ATOM   5082 C CG  . LEU   A 1 838 ? -11.916 61.119  100.749 1.00 54.58  ?  819 LEU   A CG  1 
ATOM   5083 C CD1 . LEU   A 1 838 ? -12.716 59.805  100.884 1.00 60.32  ?  819 LEU   A CD1 1 
ATOM   5084 C CD2 . LEU   A 1 838 ? -12.756 62.302  101.076 1.00 49.96  ?  819 LEU   A CD2 1 
ATOM   5085 N N   . ARG   A 1 839 ? -7.741  62.014  102.443 1.00 50.74  ?  820 ARG   A N   1 
ATOM   5086 C CA  . ARG   A 1 839 ? -6.627  61.847  103.365 1.00 45.46  ?  820 ARG   A CA  1 
ATOM   5087 C C   . ARG   A 1 839 ? -6.239  63.178  103.997 1.00 54.30  ?  820 ARG   A C   1 
ATOM   5088 O O   . ARG   A 1 839 ? -6.206  63.303  105.225 1.00 56.41  ?  820 ARG   A O   1 
ATOM   5089 C CB  . ARG   A 1 839 ? -5.445  61.227  102.625 1.00 42.02  ?  820 ARG   A CB  1 
ATOM   5090 C CG  . ARG   A 1 839 ? -4.191  61.123  103.446 1.00 38.84  ?  820 ARG   A CG  1 
ATOM   5091 C CD  . ARG   A 1 839 ? -2.958  60.886  102.589 1.00 44.57  ?  820 ARG   A CD  1 
ATOM   5092 N NE  . ARG   A 1 839 ? -2.565  62.058  101.795 1.00 53.94  ?  820 ARG   A NE  1 
ATOM   5093 C CZ  . ARG   A 1 839 ? -2.284  62.047  100.490 1.00 56.36  ?  820 ARG   A CZ  1 
ATOM   5094 N NH1 . ARG   A 1 839 ? -2.358  60.933  99.780  1.00 56.99  ?  820 ARG   A NH1 1 
ATOM   5095 N NH2 . ARG   A 1 839 ? -1.934  63.162  99.877  1.00 60.00  ?  820 ARG   A NH2 1 
ATOM   5096 N N   . GLU   A 1 840 ? -5.963  64.197  103.176 1.00 55.19  ?  821 GLU   A N   1 
ATOM   5097 C CA  . GLU   A 1 840 ? -5.496  65.463  103.733 1.00 55.85  ?  821 GLU   A CA  1 
ATOM   5098 C C   . GLU   A 1 840 ? -6.574  66.133  104.569 1.00 60.93  ?  821 GLU   A C   1 
ATOM   5099 O O   . GLU   A 1 840 ? -6.265  66.737  105.606 1.00 61.64  ?  821 GLU   A O   1 
ATOM   5100 C CB  . GLU   A 1 840 ? -5.010  66.397  102.629 1.00 51.90  ?  821 GLU   A CB  1 
ATOM   5101 C CG  . GLU   A 1 840 ? -3.881  65.749  101.872 1.00 58.91  ?  821 GLU   A CG  1 
ATOM   5102 C CD  . GLU   A 1 840 ? -2.607  65.554  102.714 1.00 62.14  ?  821 GLU   A CD  1 
ATOM   5103 O OE1 . GLU   A 1 840 ? -2.154  66.484  103.404 1.00 58.18  ?  821 GLU   A OE1 1 
ATOM   5104 O OE2 . GLU   A 1 840 ? -2.094  64.407  102.740 1.00 64.25  ?  821 GLU   A OE2 1 
ATOM   5105 N N   . ALA   A 1 841 ? -7.842  66.030  104.156 1.00 55.71  ?  822 ALA   A N   1 
ATOM   5106 C CA  . ALA   A 1 841 ? -8.882  66.661  104.955 1.00 55.17  ?  822 ALA   A CA  1 
ATOM   5107 C C   . ALA   A 1 841 ? -8.940  66.037  106.334 1.00 54.86  ?  822 ALA   A C   1 
ATOM   5108 O O   . ALA   A 1 841 ? -9.170  66.720  107.331 1.00 63.59  ?  822 ALA   A O   1 
ATOM   5109 C CB  . ALA   A 1 841 ? -10.237 66.577  104.272 1.00 53.71  ?  822 ALA   A CB  1 
ATOM   5110 N N   . GLY   A 1 842 ? -8.687  64.751  106.426 1.00 56.71  ?  823 GLY   A N   1 
ATOM   5111 C CA  . GLY   A 1 842 ? -8.616  64.165  107.746 1.00 61.38  ?  823 GLY   A CA  1 
ATOM   5112 C C   . GLY   A 1 842 ? -7.368  64.597  108.476 1.00 60.32  ?  823 GLY   A C   1 
ATOM   5113 O O   . GLY   A 1 842 ? -7.346  64.644  109.706 1.00 63.63  ?  823 GLY   A O   1 
ATOM   5114 N N   . ARG   A 1 843 ? -6.308  64.908  107.741 1.00 55.38  ?  824 ARG   A N   1 
ATOM   5115 C CA  . ARG   A 1 843 ? -5.087  65.276  108.436 1.00 54.74  ?  824 ARG   A CA  1 
ATOM   5116 C C   . ARG   A 1 843 ? -5.140  66.725  108.877 1.00 61.67  ?  824 ARG   A C   1 
ATOM   5117 O O   . ARG   A 1 843 ? -4.728  67.050  109.995 1.00 61.36  ?  824 ARG   A O   1 
ATOM   5118 C CB  . ARG   A 1 843 ? -3.876  65.037  107.550 1.00 49.40  ?  824 ARG   A CB  1 
ATOM   5119 C CG  . ARG   A 1 843 ? -2.695  65.813  108.011 1.00 57.17  ?  824 ARG   A CG  1 
ATOM   5120 C CD  . ARG   A 1 843 ? -1.415  65.131  107.673 1.00 66.83  ?  824 ARG   A CD  1 
ATOM   5121 N NE  . ARG   A 1 843 ? -1.370  64.692  106.283 1.00 66.70  ?  824 ARG   A NE  1 
ATOM   5122 C CZ  . ARG   A 1 843 ? -0.391  63.929  105.807 1.00 67.03  ?  824 ARG   A CZ  1 
ATOM   5123 N NH1 . ARG   A 1 843 ? 0.603   63.558  106.621 1.00 65.56  ?  824 ARG   A NH1 1 
ATOM   5124 N NH2 . ARG   A 1 843 ? -0.399  63.541  104.538 1.00 58.99  ?  824 ARG   A NH2 1 
ATOM   5125 N N   . ILE   A 1 844 ? -5.653  67.601  108.008 1.00 61.60  ?  825 ILE   A N   1 
ATOM   5126 C CA  . ILE   A 1 844 ? -5.793  69.008  108.358 1.00 61.10  ?  825 ILE   A CA  1 
ATOM   5127 C C   . ILE   A 1 844 ? -6.733  69.152  109.546 1.00 59.45  ?  825 ILE   A C   1 
ATOM   5128 O O   . ILE   A 1 844 ? -6.406  69.815  110.533 1.00 64.59  ?  825 ILE   A O   1 
ATOM   5129 C CB  . ILE   A 1 844 ? -6.260  69.828  107.133 1.00 64.75  ?  825 ILE   A CB  1 
ATOM   5130 C CG1 . ILE   A 1 844 ? -5.093  70.028  106.156 1.00 55.71  ?  825 ILE   A CG1 1 
ATOM   5131 C CG2 . ILE   A 1 844 ? -6.792  71.194  107.545 1.00 54.13  ?  825 ILE   A CG2 1 
ATOM   5132 C CD1 . ILE   A 1 844 ? -5.527  70.329  104.778 1.00 53.37  ?  825 ILE   A CD1 1 
ATOM   5133 N N   . ALA   A 1 845 ? -7.890  68.492  109.494 1.00 58.40  ?  826 ALA   A N   1 
ATOM   5134 C CA  . ALA   A 1 845 ? -8.810  68.539  110.627 1.00 62.43  ?  826 ALA   A CA  1 
ATOM   5135 C C   . ALA   A 1 845 ? -8.151  68.050  111.912 1.00 64.19  ?  826 ALA   A C   1 
ATOM   5136 O O   . ALA   A 1 845 ? -8.316  68.662  112.974 1.00 66.32  ?  826 ALA   A O   1 
ATOM   5137 C CB  . ALA   A 1 845 ? -10.057 67.717  110.335 1.00 64.25  ?  826 ALA   A CB  1 
ATOM   5138 N N   . ASP   A 1 846 ? -7.399  66.952  111.842 1.00 65.54  ?  827 ASP   A N   1 
ATOM   5139 C CA  . ASP   A 1 846 ? -6.687  66.469  113.027 1.00 70.55  ?  827 ASP   A CA  1 
ATOM   5140 C C   . ASP   A 1 846 ? -5.786  67.554  113.593 1.00 68.77  ?  827 ASP   A C   1 
ATOM   5141 O O   . ASP   A 1 846 ? -5.613  67.671  114.810 1.00 76.83  ?  827 ASP   A O   1 
ATOM   5142 C CB  . ASP   A 1 846 ? -5.858  65.230  112.670 1.00 66.19  ?  827 ASP   A CB  1 
ATOM   5143 C CG  . ASP   A 1 846 ? -6.637  63.938  112.814 1.00 76.53  ?  827 ASP   A CG  1 
ATOM   5144 O OD1 . ASP   A 1 846 ? -7.881  64.010  113.002 1.00 73.19  ?  827 ASP   A OD1 1 
ATOM   5145 O OD2 . ASP   A 1 846 ? -6.009  62.850  112.692 1.00 84.74  ?  827 ASP   A OD2 1 
ATOM   5146 N N   . GLN   A 1 847 ? -5.284  68.403  112.730 1.00 64.05  ?  828 GLN   A N   1 
ATOM   5147 C CA  . GLN   A 1 847 ? -4.325  69.396  113.234 1.00 66.83  ?  828 GLN   A CA  1 
ATOM   5148 C C   . GLN   A 1 847 ? -5.026  70.632  113.760 1.00 71.86  ?  828 GLN   A C   1 
ATOM   5149 O O   . GLN   A 1 847 ? -4.578  71.156  114.739 1.00 68.95  ?  828 GLN   A O   1 
ATOM   5150 C CB  . GLN   A 1 847 ? -3.452  69.860  112.089 1.00 70.01  ?  828 GLN   A CB  1 
ATOM   5151 C CG  . GLN   A 1 847 ? -2.566  71.008  112.494 1.00 74.77  ?  828 GLN   A CG  1 
ATOM   5152 C CD  . GLN   A 1 847 ? -1.204  70.478  112.822 1.00 85.15  ?  828 GLN   A CD  1 
ATOM   5153 O OE1 . GLN   A 1 847 ? -0.386  70.259  111.949 1.00 83.10  ?  828 GLN   A OE1 1 
ATOM   5154 N NE2 . GLN   A 1 847 ? -0.957  70.250  114.092 1.00 90.03  ?  828 GLN   A NE2 1 
ATOM   5155 N N   . PHE   A 1 848 ? -6.063  71.093  113.083 1.00 72.25  ?  829 PHE   A N   1 
ATOM   5156 C CA  . PHE   A 1 848 ? -6.703  72.354  113.504 1.00 66.12  ?  829 PHE   A CA  1 
ATOM   5157 C C   . PHE   A 1 848 ? -7.920  72.127  114.384 1.00 70.28  ?  829 PHE   A C   1 
ATOM   5158 O O   . PHE   A 1 848 ? -8.317  73.055  115.039 1.00 71.64  ?  829 PHE   A O   1 
ATOM   5159 C CB  . PHE   A 1 848 ? -6.952  73.205  112.269 1.00 64.86  ?  829 PHE   A CB  1 
ATOM   5160 C CG  . PHE   A 1 848 ? -5.656  73.623  111.643 1.00 67.13  ?  829 PHE   A CG  1 
ATOM   5161 C CD1 . PHE   A 1 848 ? -4.957  74.702  112.123 1.00 66.00  ?  829 PHE   A CD1 1 
ATOM   5162 C CD2 . PHE   A 1 848 ? -5.088  72.886  110.642 1.00 68.66  ?  829 PHE   A CD2 1 
ATOM   5163 C CE1 . PHE   A 1 848 ? -3.743  75.065  111.583 1.00 59.26  ?  829 PHE   A CE1 1 
ATOM   5164 C CE2 . PHE   A 1 848 ? -3.872  73.251  110.107 1.00 68.16  ?  829 PHE   A CE2 1 
ATOM   5165 C CZ  . PHE   A 1 848 ? -3.205  74.340  110.571 1.00 64.02  ?  829 PHE   A CZ  1 
ATOM   5166 N N   . LEU   A 1 849 ? -8.490  70.936  114.396 1.00 71.95  ?  830 LEU   A N   1 
ATOM   5167 C CA  . LEU   A 1 849 ? -9.670  70.747  115.264 1.00 67.59  ?  830 LEU   A CA  1 
ATOM   5168 C C   . LEU   A 1 849 ? -9.330  69.798  116.395 1.00 72.78  ?  830 LEU   A C   1 
ATOM   5169 O O   . LEU   A 1 849 ? -10.153 69.615  117.251 1.00 77.65  ?  830 LEU   A O   1 
ATOM   5170 C CB  . LEU   A 1 849 ? -10.799 70.156  114.436 1.00 60.15  ?  830 LEU   A CB  1 
ATOM   5171 C CG  . LEU   A 1 849 ? -11.161 70.956  113.206 1.00 65.74  ?  830 LEU   A CG  1 
ATOM   5172 C CD1 . LEU   A 1 849 ? -12.498 70.513  112.674 1.00 63.19  ?  830 LEU   A CD1 1 
ATOM   5173 C CD2 . LEU   A 1 849 ? -11.198 72.418  113.550 1.00 64.91  ?  830 LEU   A CD2 1 
ATOM   5174 N N   . GLY   A 1 850 ? -8.231  69.079  116.277 1.00 73.57  ?  831 GLY   A N   1 
ATOM   5175 C CA  . GLY   A 1 850 ? -7.808  68.148  117.331 1.00 79.31  ?  831 GLY   A CA  1 
ATOM   5176 C C   . GLY   A 1 850 ? -8.389  66.764  117.163 1.00 81.21  ?  831 GLY   A C   1 
ATOM   5177 O O   . GLY   A 1 850 ? -9.506  66.632  116.720 1.00 80.41  ?  831 GLY   A O   1 
ATOM   5178 N N   . ALA   A 1 851 ? -7.665  65.751  117.601 1.00 86.86  ?  832 ALA   A N   1 
ATOM   5179 C CA  . ALA   A 1 851 ? -8.208  64.389  117.481 1.00 95.00  ?  832 ALA   A CA  1 
ATOM   5180 C C   . ALA   A 1 851 ? -8.637  63.965  118.875 1.00 103.81 ?  832 ALA   A C   1 
ATOM   5181 O O   . ALA   A 1 851 ? -7.778  63.606  119.660 1.00 102.65 ?  832 ALA   A O   1 
ATOM   5182 C CB  . ALA   A 1 851 ? -7.133  63.482  116.965 1.00 86.64  ?  832 ALA   A CB  1 
ATOM   5183 N N   . MET   A 1 852 ? -9.934  63.924  119.135 1.00 105.77 ?  833 MET   A N   1 
ATOM   5184 C CA  . MET   A 1 852 ? -10.371 63.585  120.506 1.00 106.76 ?  833 MET   A CA  1 
ATOM   5185 C C   . MET   A 1 852 ? -10.588 62.082  120.619 1.00 102.72 ?  833 MET   A C   1 
ATOM   5186 O O   . MET   A 1 852 ? -10.828 61.614  121.714 1.00 108.96 ?  833 MET   A O   1 
ATOM   5187 C CB  . MET   A 1 852 ? -11.672 64.319  120.828 1.00 111.11 ?  833 MET   A CB  1 
ATOM   5188 C CG  . MET   A 1 852 ? -11.743 65.703  120.214 1.00 108.44 ?  833 MET   A CG  1 
ATOM   5189 S SD  . MET   A 1 852 ? -10.584 66.842  120.994 1.00 125.19 ?  833 MET   A SD  1 
ATOM   5190 C CE  . MET   A 1 852 ? -11.380 68.416  120.693 1.00 99.78  ?  833 MET   A CE  1 
ATOM   5191 N N   . TYR   A 1 853 ? -10.442 61.362  119.520 1.00 99.07  ?  834 TYR   A N   1 
ATOM   5192 C CA  . TYR   A 1 853 ? -10.720 59.910  119.486 1.00 98.18  ?  834 TYR   A CA  1 
ATOM   5193 C C   . TYR   A 1 853 ? -9.444  59.090  119.659 1.00 93.35  ?  834 TYR   A C   1 
ATOM   5194 O O   . TYR   A 1 853 ? -9.484  57.914  119.377 1.00 85.47  ?  834 TYR   A O   1 
ATOM   5195 C CB  . TYR   A 1 853 ? -11.335 59.591  118.127 1.00 92.75  ?  834 TYR   A CB  1 
ATOM   5196 C CG  . TYR   A 1 853 ? -10.458 60.024  116.986 1.00 97.08  ?  834 TYR   A CG  1 
ATOM   5197 C CD1 . TYR   A 1 853 ? -10.774 61.119  116.208 1.00 94.45  ?  834 TYR   A CD1 1 
ATOM   5198 C CD2 . TYR   A 1 853 ? -9.281  59.360  116.721 1.00 89.14  ?  834 TYR   A CD2 1 
ATOM   5199 C CE1 . TYR   A 1 853 ? -9.955  61.528  115.176 1.00 88.20  ?  834 TYR   A CE1 1 
ATOM   5200 C CE2 . TYR   A 1 853 ? -8.452  59.756  115.694 1.00 88.30  ?  834 TYR   A CE2 1 
ATOM   5201 C CZ  . TYR   A 1 853 ? -8.789  60.843  114.923 1.00 90.88  ?  834 TYR   A CZ  1 
ATOM   5202 O OH  . TYR   A 1 853 ? -7.964  61.230  113.918 1.00 85.37  ?  834 TYR   A OH  1 
ATOM   5203 N N   . THR   A 1 854 ? -8.361  59.676  120.144 1.00 97.23  ?  835 THR   A N   1 
ATOM   5204 C CA  . THR   A 1 854 ? -7.134  58.894  120.254 1.00 92.87  ?  835 THR   A CA  1 
ATOM   5205 C C   . THR   A 1 854 ? -6.815  58.470  121.696 1.00 100.97 ?  835 THR   A C   1 
ATOM   5206 O O   . THR   A 1 854 ? -5.724  57.942  121.945 1.00 99.03  ?  835 THR   A O   1 
ATOM   5207 C CB  . THR   A 1 854 ? -5.962  59.681  119.637 1.00 97.38  ?  835 THR   A CB  1 
ATOM   5208 O OG1 . THR   A 1 854 ? -5.983  61.040  120.105 1.00 102.87 ?  835 THR   A OG1 1 
ATOM   5209 C CG2 . THR   A 1 854 ? -6.047  59.685  118.092 1.00 82.17  ?  835 THR   A CG2 1 
ATOM   5210 N N   . LEU   A 1 855 ? -7.763  58.646  122.634 1.00 110.81 ?  836 LEU   A N   1 
ATOM   5211 C CA  . LEU   A 1 855 ? -7.567  58.448  124.089 1.00 100.21 ?  836 LEU   A CA  1 
ATOM   5212 C C   . LEU   A 1 855 ? -8.211  57.145  124.599 1.00 94.63  ?  836 LEU   A C   1 
ATOM   5213 O O   . LEU   A 1 855 ? -7.946  56.670  125.716 1.00 93.99  ?  836 LEU   A O   1 
ATOM   5214 C CB  . LEU   A 1 855 ? -8.151  59.640  124.863 1.00 105.36 ?  836 LEU   A CB  1 
ATOM   5215 C CG  . LEU   A 1 855 ? -7.428  60.997  124.932 1.00 110.67 ?  836 LEU   A CG  1 
ATOM   5216 C CD1 . LEU   A 1 855 ? -7.328  61.656  123.541 1.00 94.60  ?  836 LEU   A CD1 1 
ATOM   5217 C CD2 . LEU   A 1 855 ? -8.108  61.938  125.965 1.00 101.13 ?  836 LEU   A CD2 1 
ATOM   5218 N N   . ARG   B 2 12  ? 10.718  32.849  89.376  1.00 110.15 ?  308 ARG   B N   1 
ATOM   5219 C CA  . ARG   B 2 12  ? 12.130  32.523  89.710  1.00 123.44 ?  308 ARG   B CA  1 
ATOM   5220 C C   . ARG   B 2 12  ? 12.774  31.771  88.545  1.00 123.56 ?  308 ARG   B C   1 
ATOM   5221 O O   . ARG   B 2 12  ? 13.956  31.418  88.637  1.00 124.61 ?  308 ARG   B O   1 
ATOM   5222 C CB  . ARG   B 2 12  ? 12.218  31.699  90.994  1.00 132.86 ?  308 ARG   B CB  1 
ATOM   5223 C CG  . ARG   B 2 12  ? 13.635  31.280  91.356  1.00 134.66 ?  308 ARG   B CG  1 
ATOM   5224 C CD  . ARG   B 2 12  ? 14.441  32.400  91.987  1.00 139.47 ?  308 ARG   B CD  1 
ATOM   5225 N NE  . ARG   B 2 12  ? 15.123  32.018  93.212  1.00 147.96 ?  308 ARG   B NE  1 
ATOM   5226 C CZ  . ARG   B 2 12  ? 15.111  32.728  94.330  1.00 137.61 ?  308 ARG   B CZ  1 
ATOM   5227 N NH1 . ARG   B 2 12  ? 14.445  33.866  94.388  1.00 131.15 ?  308 ARG   B NH1 1 
ATOM   5228 N NH2 . ARG   B 2 12  ? 15.765  32.295  95.390  1.00 139.48 ?  308 ARG   B NH2 1 
ATOM   5229 N N   . LYS   B 2 13  ? 11.990  31.495  87.512  1.00 118.56 ?  309 LYS   B N   1 
ATOM   5230 C CA  . LYS   B 2 13  ? 12.505  30.849  86.287  1.00 112.40 ?  309 LYS   B CA  1 
ATOM   5231 C C   . LYS   B 2 13  ? 11.968  31.685  85.132  1.00 110.36 ?  309 LYS   B C   1 
ATOM   5232 O O   . LYS   B 2 13  ? 10.824  32.121  85.207  1.00 110.33 ?  309 LYS   B O   1 
ATOM   5233 C CB  . LYS   B 2 13  ? 12.001  29.409  86.202  1.00 109.97 ?  309 LYS   B CB  1 
ATOM   5234 C CG  . LYS   B 2 13  ? 12.876  28.450  85.409  1.00 120.07 ?  309 LYS   B CG  1 
ATOM   5235 C CD  . LYS   B 2 13  ? 12.803  27.007  85.893  1.00 123.28 ?  309 LYS   B CD  1 
ATOM   5236 C CE  . LYS   B 2 13  ? 13.932  26.125  85.388  1.00 117.66 ?  309 LYS   B CE  1 
ATOM   5237 N NZ  . LYS   B 2 13  ? 14.159  24.930  86.237  1.00 110.57 ?  309 LYS   B NZ  1 
ATOM   5238 N N   . PRO   B 2 14  ? 12.720  31.904  84.047  1.00 101.84 ?  310 PRO   B N   1 
ATOM   5239 C CA  . PRO   B 2 14  ? 12.229  32.693  82.944  1.00 95.32  ?  310 PRO   B CA  1 
ATOM   5240 C C   . PRO   B 2 14  ? 11.080  31.997  82.229  1.00 93.70  ?  310 PRO   B C   1 
ATOM   5241 O O   . PRO   B 2 14  ? 11.017  30.833  82.205  1.00 103.80 ?  310 PRO   B O   1 
ATOM   5242 C CB  . PRO   B 2 14  ? 13.399  32.709  81.972  1.00 91.36  ?  310 PRO   B CB  1 
ATOM   5243 C CG  . PRO   B 2 14  ? 14.224  31.540  82.382  1.00 93.49  ?  310 PRO   B CG  1 
ATOM   5244 C CD  . PRO   B 2 14  ? 14.083  31.472  83.880  1.00 98.11  ?  310 PRO   B CD  1 
ATOM   5245 N N   . PRO   B 2 15  ? 10.243  32.717  81.479  1.00 93.21  ?  311 PRO   B N   1 
ATOM   5246 C CA  . PRO   B 2 15  ? 9.110   32.113  80.816  1.00 95.22  ?  311 PRO   B CA  1 
ATOM   5247 C C   . PRO   B 2 15  ? 9.534   31.065  79.789  1.00 102.18 ?  311 PRO   B C   1 
ATOM   5248 O O   . PRO   B 2 15  ? 10.565  31.195  79.196  1.00 104.62 ?  311 PRO   B O   1 
ATOM   5249 C CB  . PRO   B 2 15  ? 8.532   33.260  79.994  1.00 92.00  ?  311 PRO   B CB  1 
ATOM   5250 C CG  . PRO   B 2 15  ? 8.994   34.471  80.712  1.00 86.26  ?  311 PRO   B CG  1 
ATOM   5251 C CD  . PRO   B 2 15  ? 10.378  34.120  81.195  1.00 91.73  ?  311 PRO   B CD  1 
ATOM   5252 N N   . LYS   B 2 16  ? 8.684   30.070  79.569  1.00 108.32 ?  312 LYS   B N   1 
ATOM   5253 C CA  . LYS   B 2 16  ? 9.033   29.023  78.587  1.00 111.75 ?  312 LYS   B CA  1 
ATOM   5254 C C   . LYS   B 2 16  ? 9.223   29.681  77.222  1.00 113.44 ?  312 LYS   B C   1 
ATOM   5255 O O   . LYS   B 2 16  ? 8.394   30.524  76.833  1.00 109.26 ?  312 LYS   B O   1 
ATOM   5256 C CB  . LYS   B 2 16  ? 7.924   27.974  78.529  1.00 114.00 ?  312 LYS   B CB  1 
ATOM   5257 C CG  . LYS   B 2 16  ? 7.982   26.929  79.631  1.00 116.83 ?  312 LYS   B CG  1 
ATOM   5258 C CD  . LYS   B 2 16  ? 9.037   27.230  80.668  1.00 117.59 ?  312 LYS   B CD  1 
ATOM   5259 C CE  . LYS   B 2 16  ? 9.501   25.995  81.412  1.00 119.81 ?  312 LYS   B CE  1 
ATOM   5260 N NZ  . LYS   B 2 16  ? 8.470   25.493  82.350  1.00 114.80 ?  312 LYS   B NZ  1 
ATOM   5261 N N   . GLY   B 2 17  ? 10.298  29.300  76.539  1.00 107.12 ?  313 GLY   B N   1 
ATOM   5262 C CA  . GLY   B 2 17  ? 10.594  29.877  75.221  1.00 106.82 ?  313 GLY   B CA  1 
ATOM   5263 C C   . GLY   B 2 17  ? 11.560  31.034  75.329  1.00 111.52 ?  313 GLY   B C   1 
ATOM   5264 O O   . GLY   B 2 17  ? 12.245  31.310  74.345  1.00 115.26 ?  313 GLY   B O   1 
ATOM   5265 N N   . MET   B 2 18  ? 11.632  31.690  76.480  1.00 94.39  ?  314 MET   B N   1 
ATOM   5266 C CA  . MET   B 2 18  ? 12.572  32.800  76.566  1.00 89.98  ?  314 MET   B CA  1 
ATOM   5267 C C   . MET   B 2 18  ? 13.926  32.304  77.048  1.00 89.60  ?  314 MET   B C   1 
ATOM   5268 O O   . MET   B 2 18  ? 14.017  31.411  77.900  1.00 85.91  ?  314 MET   B O   1 
ATOM   5269 C CB  . MET   B 2 18  ? 12.066  33.876  77.523  1.00 93.58  ?  314 MET   B CB  1 
ATOM   5270 C CG  . MET   B 2 18  ? 10.688  34.419  77.238  1.00 83.94  ?  314 MET   B CG  1 
ATOM   5271 S SD  . MET   B 2 18  ? 10.824  35.780  76.096  1.00 83.79  ?  314 MET   B SD  1 
ATOM   5272 C CE  . MET   B 2 18  ? 9.403   35.530  75.054  1.00 81.34  ?  314 MET   B CE  1 
ATOM   5273 N N   . PHE   B 2 19  ? 14.987  32.899  76.525  1.00 83.84  ?  315 PHE   B N   1 
ATOM   5274 C CA  . PHE   B 2 19  ? 16.326  32.421  76.841  1.00 95.05  ?  315 PHE   B CA  1 
ATOM   5275 C C   . PHE   B 2 19  ? 17.135  33.571  77.423  1.00 95.21  ?  315 PHE   B C   1 
ATOM   5276 O O   . PHE   B 2 19  ? 17.565  34.478  76.703  1.00 92.72  ?  315 PHE   B O   1 
ATOM   5277 C CB  . PHE   B 2 19  ? 16.968  31.806  75.606  1.00 95.73  ?  315 PHE   B CB  1 
ATOM   5278 C CG  . PHE   B 2 19  ? 16.619  30.362  75.428  1.00 98.57  ?  315 PHE   B CG  1 
ATOM   5279 C CD1 . PHE   B 2 19  ? 15.419  29.993  74.818  1.00 94.00  ?  315 PHE   B CD1 1 
ATOM   5280 C CD2 . PHE   B 2 19  ? 17.462  29.368  75.921  1.00 103.93 ?  315 PHE   B CD2 1 
ATOM   5281 C CE1 . PHE   B 2 19  ? 15.078  28.653  74.673  1.00 94.43  ?  315 PHE   B CE1 1 
ATOM   5282 C CE2 . PHE   B 2 19  ? 17.136  28.016  75.778  1.00 104.20 ?  315 PHE   B CE2 1 
ATOM   5283 C CZ  . PHE   B 2 19  ? 15.943  27.658  75.152  1.00 101.22 ?  315 PHE   B CZ  1 
ATOM   5284 N N   . LEU   B 2 20  ? 17.345  33.531  78.733  1.00 93.14  ?  316 LEU   B N   1 
ATOM   5285 C CA  . LEU   B 2 20  ? 17.903  34.672  79.441  1.00 94.72  ?  316 LEU   B CA  1 
ATOM   5286 C C   . LEU   B 2 20  ? 18.800  34.078  80.517  1.00 103.80 ?  316 LEU   B C   1 
ATOM   5287 O O   . LEU   B 2 20  ? 18.297  33.543  81.513  1.00 104.67 ?  316 LEU   B O   1 
ATOM   5288 C CB  . LEU   B 2 20  ? 16.798  35.505  80.091  1.00 93.52  ?  316 LEU   B CB  1 
ATOM   5289 C CG  . LEU   B 2 20  ? 15.540  35.982  79.343  1.00 89.64  ?  316 LEU   B CG  1 
ATOM   5290 C CD1 . LEU   B 2 20  ? 14.685  36.814  80.287  1.00 88.60  ?  316 LEU   B CD1 1 
ATOM   5291 C CD2 . LEU   B 2 20  ? 15.704  36.611  77.944  1.00 92.78  ?  316 LEU   B CD2 1 
ATOM   5292 N N   . SER   B 2 21  ? 20.108  34.111  80.323  1.00 107.15 ?  317 SER   B N   1 
ATOM   5293 C CA  . SER   B 2 21  ? 21.001  33.746  81.410  1.00 110.49 ?  317 SER   B CA  1 
ATOM   5294 C C   . SER   B 2 21  ? 21.809  34.976  81.765  1.00 112.42 ?  317 SER   B C   1 
ATOM   5295 O O   . SER   B 2 21  ? 21.869  35.935  80.988  1.00 106.53 ?  317 SER   B O   1 
ATOM   5296 C CB  . SER   B 2 21  ? 21.942  32.589  81.049  1.00 117.56 ?  317 SER   B CB  1 
ATOM   5297 O OG  . SER   B 2 21  ? 23.068  33.058  80.323  1.00 117.16 ?  317 SER   B OG  1 
ATOM   5298 N N   . GLN   B 2 22  ? 22.420  34.947  82.953  1.00 114.07 ?  318 GLN   B N   1 
ATOM   5299 C CA  . GLN   B 2 22  ? 23.296  36.048  83.336  1.00 118.83 ?  318 GLN   B CA  1 
ATOM   5300 C C   . GLN   B 2 22  ? 24.321  36.290  82.238  1.00 117.04 ?  318 GLN   B C   1 
ATOM   5301 O O   . GLN   B 2 22  ? 24.387  37.384  81.661  1.00 110.87 ?  318 GLN   B O   1 
ATOM   5302 C CB  . GLN   B 2 22  ? 23.992  35.742  84.669  1.00 122.08 ?  318 GLN   B CB  1 
ATOM   5303 C CG  . GLN   B 2 22  ? 25.015  36.802  85.125  1.00 125.36 ?  318 GLN   B CG  1 
ATOM   5304 C CD  . GLN   B 2 22  ? 24.516  38.243  84.978  1.00 128.34 ?  318 GLN   B CD  1 
ATOM   5305 O OE1 . GLN   B 2 22  ? 24.718  38.883  83.944  1.00 129.64 ?  318 GLN   B OE1 1 
ATOM   5306 N NE2 . GLN   B 2 22  ? 23.887  38.766  86.032  1.00 120.10 ?  318 GLN   B NE2 1 
ATOM   5307 N N   . GLU   B 2 23  ? 25.036  35.218  81.863  1.00 122.78 ?  319 GLU   B N   1 
ATOM   5308 C CA  . GLU   B 2 23  ? 26.248  35.309  81.056  1.00 121.33 ?  319 GLU   B CA  1 
ATOM   5309 C C   . GLU   B 2 23  ? 25.952  36.150  79.819  1.00 116.88 ?  319 GLU   B C   1 
ATOM   5310 O O   . GLU   B 2 23  ? 26.716  37.048  79.444  1.00 112.88 ?  319 GLU   B O   1 
ATOM   5311 C CB  . GLU   B 2 23  ? 26.652  33.914  80.572  1.00 125.55 ?  319 GLU   B CB  1 
ATOM   5312 C CG  . GLU   B 2 23  ? 28.150  33.609  80.393  1.00 128.79 ?  319 GLU   B CG  1 
ATOM   5313 C CD  . GLU   B 2 23  ? 28.341  32.480  79.404  1.00 137.09 ?  319 GLU   B CD  1 
ATOM   5314 O OE1 . GLU   B 2 23  ? 27.413  32.323  78.563  1.00 137.25 ?  319 GLU   B OE1 1 
ATOM   5315 O OE2 . GLU   B 2 23  ? 29.266  31.650  79.624  1.00 144.49 ?  319 GLU   B OE2 1 
ATOM   5316 N N   . ASP   B 2 24  ? 24.807  35.858  79.191  1.00 113.97 ?  320 ASP   B N   1 
ATOM   5317 C CA  . ASP   B 2 24  ? 24.377  36.470  77.939  1.00 110.21 ?  320 ASP   B CA  1 
ATOM   5318 C C   . ASP   B 2 24  ? 24.310  37.991  78.033  1.00 114.12 ?  320 ASP   B C   1 
ATOM   5319 O O   . ASP   B 2 24  ? 24.614  38.701  77.064  1.00 109.00 ?  320 ASP   B O   1 
ATOM   5320 C CB  . ASP   B 2 24  ? 22.986  35.934  77.587  1.00 111.81 ?  320 ASP   B CB  1 
ATOM   5321 C CG  . ASP   B 2 24  ? 23.013  34.546  76.970  1.00 116.66 ?  320 ASP   B CG  1 
ATOM   5322 O OD1 . ASP   B 2 24  ? 21.970  33.850  77.060  1.00 114.61 ?  320 ASP   B OD1 1 
ATOM   5323 O OD2 . ASP   B 2 24  ? 24.053  34.164  76.384  1.00 116.15 ?  320 ASP   B OD2 1 
ATOM   5324 N N   . VAL   B 2 25  ? 23.883  38.509  79.183  1.00 117.79 ?  321 VAL   B N   1 
ATOM   5325 C CA  . VAL   B 2 25  ? 23.280  39.835  79.184  1.00 110.58 ?  321 VAL   B CA  1 
ATOM   5326 C C   . VAL   B 2 25  ? 24.335  40.938  79.154  1.00 111.32 ?  321 VAL   B C   1 
ATOM   5327 O O   . VAL   B 2 25  ? 24.195  41.906  78.395  1.00 107.75 ?  321 VAL   B O   1 
ATOM   5328 C CB  . VAL   B 2 25  ? 22.308  39.969  80.369  1.00 107.23 ?  321 VAL   B CB  1 
ATOM   5329 C CG1 . VAL   B 2 25  ? 21.549  41.270  80.271  1.00 103.11 ?  321 VAL   B CG1 1 
ATOM   5330 C CG2 . VAL   B 2 25  ? 21.319  38.828  80.337  1.00 102.86 ?  321 VAL   B CG2 1 
ATOM   5331 N N   . GLU   B 2 26  ? 25.413  40.827  79.949  1.00 111.25 ?  322 GLU   B N   1 
ATOM   5332 C CA  . GLU   B 2 26  ? 26.470  41.834  79.822  1.00 118.23 ?  322 GLU   B CA  1 
ATOM   5333 C C   . GLU   B 2 26  ? 27.069  41.812  78.430  1.00 116.75 ?  322 GLU   B C   1 
ATOM   5334 O O   . GLU   B 2 26  ? 27.480  42.857  77.913  1.00 115.91 ?  322 GLU   B O   1 
ATOM   5335 C CB  . GLU   B 2 26  ? 27.603  41.635  80.832  1.00 118.61 ?  322 GLU   B CB  1 
ATOM   5336 C CG  . GLU   B 2 26  ? 27.172  41.391  82.237  1.00 122.30 ?  322 GLU   B CG  1 
ATOM   5337 C CD  . GLU   B 2 26  ? 27.020  39.918  82.491  1.00 126.84 ?  322 GLU   B CD  1 
ATOM   5338 O OE1 . GLU   B 2 26  ? 26.297  39.273  81.696  1.00 123.31 ?  322 GLU   B OE1 1 
ATOM   5339 O OE2 . GLU   B 2 26  ? 27.607  39.413  83.480  1.00 130.55 ?  322 GLU   B OE2 1 
ATOM   5340 N N   . ALA   B 2 27  ? 27.128  40.629  77.816  1.00 115.67 ?  323 ALA   B N   1 
ATOM   5341 C CA  . ALA   B 2 27  ? 27.648  40.515  76.461  1.00 116.48 ?  323 ALA   B CA  1 
ATOM   5342 C C   . ALA   B 2 27  ? 26.911  41.431  75.494  1.00 116.40 ?  323 ALA   B C   1 
ATOM   5343 O O   . ALA   B 2 27  ? 27.514  41.961  74.549  1.00 120.34 ?  323 ALA   B O   1 
ATOM   5344 C CB  . ALA   B 2 27  ? 27.552  39.063  75.993  1.00 116.23 ?  323 ALA   B CB  1 
ATOM   5345 N N   . VAL   B 2 28  ? 25.619  41.654  75.725  1.00 112.47 ?  324 VAL   B N   1 
ATOM   5346 C CA  . VAL   B 2 28  ? 24.795  42.366  74.760  1.00 112.82 ?  324 VAL   B CA  1 
ATOM   5347 C C   . VAL   B 2 28  ? 24.539  43.800  75.202  1.00 112.03 ?  324 VAL   B C   1 
ATOM   5348 O O   . VAL   B 2 28  ? 24.067  44.623  74.395  1.00 107.14 ?  324 VAL   B O   1 
ATOM   5349 C CB  . VAL   B 2 28  ? 23.488  41.580  74.552  1.00 108.58 ?  324 VAL   B CB  1 
ATOM   5350 C CG1 . VAL   B 2 28  ? 22.613  42.200  73.466  1.00 106.02 ?  324 VAL   B CG1 1 
ATOM   5351 C CG2 . VAL   B 2 28  ? 23.828  40.129  74.295  1.00 103.15 ?  324 VAL   B CG2 1 
ATOM   5352 N N   . SER   B 2 29  ? 24.880  44.131  76.449  1.00 115.34 ?  325 SER   B N   1 
ATOM   5353 C CA  . SER   B 2 29  ? 24.775  45.469  77.010  1.00 114.95 ?  325 SER   B CA  1 
ATOM   5354 C C   . SER   B 2 29  ? 26.121  46.184  77.126  1.00 115.77 ?  325 SER   B C   1 
ATOM   5355 O O   . SER   B 2 29  ? 26.137  47.402  77.346  1.00 118.52 ?  325 SER   B O   1 
ATOM   5356 C CB  . SER   B 2 29  ? 24.117  45.391  78.395  1.00 108.06 ?  325 SER   B CB  1 
ATOM   5357 O OG  . SER   B 2 29  ? 24.948  44.710  79.326  1.00 102.36 ?  325 SER   B OG  1 
ATOM   5358 N N   . ALA   B 2 30  ? 27.242  45.467  76.955  1.00 114.35 ?  326 ALA   B N   1 
ATOM   5359 C CA  . ALA   B 2 30  ? 28.567  45.977  77.306  1.00 111.46 ?  326 ALA   B CA  1 
ATOM   5360 C C   . ALA   B 2 30  ? 28.961  47.242  76.559  1.00 114.60 ?  326 ALA   B C   1 
ATOM   5361 O O   . ALA   B 2 30  ? 29.939  47.884  76.968  1.00 117.11 ?  326 ALA   B O   1 
ATOM   5362 C CB  . ALA   B 2 30  ? 29.635  44.909  77.071  1.00 113.60 ?  326 ALA   B CB  1 
ATOM   5363 N N   . ASN   B 2 31  ? 28.258  47.616  75.492  1.00 105.12 ?  327 ASN   B N   1 
ATOM   5364 C CA  . ASN   B 2 31  ? 28.541  48.902  74.866  1.00 108.91 ?  327 ASN   B CA  1 
ATOM   5365 C C   . ASN   B 2 31  ? 27.285  49.316  74.103  1.00 109.64 ?  327 ASN   B C   1 
ATOM   5366 O O   . ASN   B 2 31  ? 26.236  48.671  74.214  1.00 108.18 ?  327 ASN   B O   1 
ATOM   5367 C CB  . ASN   B 2 31  ? 29.826  48.816  74.018  1.00 114.32 ?  327 ASN   B CB  1 
ATOM   5368 C CG  . ASN   B 2 31  ? 29.646  48.081  72.689  1.00 120.18 ?  327 ASN   B CG  1 
ATOM   5369 O OD1 . ASN   B 2 31  ? 28.543  47.958  72.161  1.00 123.55 ?  327 ASN   B OD1 1 
ATOM   5370 N ND2 . ASN   B 2 31  ? 30.730  47.490  72.208  1.00 125.08 ?  327 ASN   B ND2 1 
ATOM   5371 N N   . ALA   B 2 32  ? 27.392  50.382  73.304  1.00 106.91 ?  328 ALA   B N   1 
ATOM   5372 C CA  . ALA   B 2 32  ? 26.200  50.939  72.668  1.00 110.68 ?  328 ALA   B CA  1 
ATOM   5373 C C   . ALA   B 2 32  ? 25.687  50.041  71.553  1.00 116.28 ?  328 ALA   B C   1 
ATOM   5374 O O   . ALA   B 2 32  ? 24.471  49.929  71.354  1.00 117.55 ?  328 ALA   B O   1 
ATOM   5375 C CB  . ALA   B 2 32  ? 26.483  52.341  72.129  1.00 102.98 ?  328 ALA   B CB  1 
ATOM   5376 N N   . THR   B 2 33  ? 26.596  49.400  70.810  1.00 119.45 ?  329 THR   B N   1 
ATOM   5377 C CA  . THR   B 2 33  ? 26.234  48.535  69.689  1.00 118.24 ?  329 THR   B CA  1 
ATOM   5378 C C   . THR   B 2 33  ? 26.730  47.097  69.865  1.00 114.18 ?  329 THR   B C   1 
ATOM   5379 O O   . THR   B 2 33  ? 26.757  46.336  68.890  1.00 111.21 ?  329 THR   B O   1 
ATOM   5380 C CB  . THR   B 2 33  ? 26.753  49.129  68.375  1.00 116.63 ?  329 THR   B CB  1 
ATOM   5381 O OG1 . THR   B 2 33  ? 28.073  49.654  68.581  1.00 115.50 ?  329 THR   B OG1 1 
ATOM   5382 C CG2 . THR   B 2 33  ? 25.823  50.232  67.856  1.00 107.54 ?  329 THR   B CG2 1 
ATOM   5383 N N   . ALA   B 2 34  ? 27.105  46.700  71.093  1.00 114.22 ?  330 ALA   B N   1 
ATOM   5384 C CA  . ALA   B 2 34  ? 27.503  45.318  71.367  1.00 108.36 ?  330 ALA   B CA  1 
ATOM   5385 C C   . ALA   B 2 34  ? 26.412  44.333  71.002  1.00 110.98 ?  330 ALA   B C   1 
ATOM   5386 O O   . ALA   B 2 34  ? 26.705  43.158  70.765  1.00 111.39 ?  330 ALA   B O   1 
ATOM   5387 C CB  . ALA   B 2 34  ? 27.878  45.134  72.841  1.00 103.98 ?  330 ALA   B CB  1 
ATOM   5388 N N   . ALA   B 2 35  ? 25.160  44.783  70.951  1.00 111.99 ?  331 ALA   B N   1 
ATOM   5389 C CA  . ALA   B 2 35  ? 24.100  43.918  70.457  1.00 105.26 ?  331 ALA   B CA  1 
ATOM   5390 C C   . ALA   B 2 35  ? 24.215  43.708  68.955  1.00 104.47 ?  331 ALA   B C   1 
ATOM   5391 O O   . ALA   B 2 35  ? 24.024  42.591  68.465  1.00 105.60 ?  331 ALA   B O   1 
ATOM   5392 C CB  . ALA   B 2 35  ? 22.736  44.505  70.803  1.00 105.94 ?  331 ALA   B CB  1 
ATOM   5393 N N   . THR   B 2 36  ? 24.372  44.796  68.227  1.00 108.11 ?  332 THR   B N   1 
ATOM   5394 C CA  . THR   B 2 36  ? 24.397  44.654  66.759  1.00 109.24 ?  332 THR   B CA  1 
ATOM   5395 C C   . THR   B 2 36  ? 25.625  43.842  66.391  1.00 107.74 ?  332 THR   B C   1 
ATOM   5396 O O   . THR   B 2 36  ? 25.529  42.986  65.537  1.00 106.59 ?  332 THR   B O   1 
ATOM   5397 C CB  . THR   B 2 36  ? 24.344  46.028  66.096  1.00 109.91 ?  332 THR   B CB  1 
ATOM   5398 O OG1 . THR   B 2 36  ? 23.277  46.695  66.757  1.00 112.08 ?  332 THR   B OG1 1 
ATOM   5399 C CG2 . THR   B 2 36  ? 24.022  45.959  64.626  1.00 110.15 ?  332 THR   B CG2 1 
ATOM   5400 N N   . THR   B 2 37  ? 26.735  44.098  67.057  1.00 108.24 ?  333 THR   B N   1 
ATOM   5401 C CA  . THR   B 2 37  ? 27.943  43.338  66.699  1.00 106.28 ?  333 THR   B CA  1 
ATOM   5402 C C   . THR   B 2 37  ? 27.712  41.858  66.968  1.00 107.19 ?  333 THR   B C   1 
ATOM   5403 O O   . THR   B 2 37  ? 27.844  41.084  66.038  1.00 108.37 ?  333 THR   B O   1 
ATOM   5404 C CB  . THR   B 2 37  ? 29.088  43.767  67.612  1.00 108.38 ?  333 THR   B CB  1 
ATOM   5405 O OG1 . THR   B 2 37  ? 29.630  44.971  67.083  1.00 99.86  ?  333 THR   B OG1 1 
ATOM   5406 C CG2 . THR   B 2 37  ? 30.166  42.720  67.738  1.00 105.68 ?  333 THR   B CG2 1 
ATOM   5407 N N   . VAL   B 2 38  ? 27.182  41.516  68.135  1.00 105.58 ?  334 VAL   B N   1 
ATOM   5408 C CA  . VAL   B 2 38  ? 27.054  40.080  68.508  1.00 102.95 ?  334 VAL   B CA  1 
ATOM   5409 C C   . VAL   B 2 38  ? 26.144  39.367  67.520  1.00 102.01 ?  334 VAL   B C   1 
ATOM   5410 O O   . VAL   B 2 38  ? 26.431  38.249  67.169  1.00 102.63 ?  334 VAL   B O   1 
ATOM   5411 C CB  . VAL   B 2 38  ? 26.547  39.921  69.944  1.00 97.22  ?  334 VAL   B CB  1 
ATOM   5412 C CG1 . VAL   B 2 38  ? 25.628  38.733  70.058  1.00 100.87 ?  334 VAL   B CG1 1 
ATOM   5413 C CG2 . VAL   B 2 38  ? 27.698  39.777  70.914  1.00 97.85  ?  334 VAL   B CG2 1 
ATOM   5414 N N   . LEU   B 2 39  ? 25.061  39.999  67.123  1.00 100.04 ?  335 LEU   B N   1 
ATOM   5415 C CA  . LEU   B 2 39  ? 24.165  39.372  66.135  1.00 100.27 ?  335 LEU   B CA  1 
ATOM   5416 C C   . LEU   B 2 39  ? 24.886  39.248  64.798  1.00 108.11 ?  335 LEU   B C   1 
ATOM   5417 O O   . LEU   B 2 39  ? 24.583  38.320  64.077  1.00 110.79 ?  335 LEU   B O   1 
ATOM   5418 C CB  . LEU   B 2 39  ? 22.906  40.219  66.001  1.00 106.18 ?  335 LEU   B CB  1 
ATOM   5419 C CG  . LEU   B 2 39  ? 22.072  40.332  67.271  1.00 100.29 ?  335 LEU   B CG  1 
ATOM   5420 C CD1 . LEU   B 2 39  ? 20.649  40.705  66.932  1.00 96.17  ?  335 LEU   B CD1 1 
ATOM   5421 C CD2 . LEU   B 2 39  ? 22.102  39.032  68.040  1.00 97.01  ?  335 LEU   B CD2 1 
ATOM   5422 N N   . ARG   B 2 40  ? 25.715  40.213  64.421  1.00 109.01 ?  336 ARG   B N   1 
ATOM   5423 C CA  . ARG   B 2 40  ? 26.386  40.071  63.107  1.00 108.60 ?  336 ARG   B CA  1 
ATOM   5424 C C   . ARG   B 2 40  ? 27.339  38.881  63.098  1.00 110.57 ?  336 ARG   B C   1 
ATOM   5425 O O   . ARG   B 2 40  ? 27.275  38.128  62.145  1.00 118.09 ?  336 ARG   B O   1 
ATOM   5426 C CB  . ARG   B 2 40  ? 27.062  41.360  62.657  1.00 108.13 ?  336 ARG   B CB  1 
ATOM   5427 C CG  . ARG   B 2 40  ? 26.356  41.996  61.473  1.00 119.56 ?  336 ARG   B CG  1 
ATOM   5428 C CD  . ARG   B 2 40  ? 27.267  42.926  60.706  1.00 128.27 ?  336 ARG   B CD  1 
ATOM   5429 N NE  . ARG   B 2 40  ? 27.274  44.257  61.288  1.00 131.91 ?  336 ARG   B NE  1 
ATOM   5430 C CZ  . ARG   B 2 40  ? 26.638  45.299  60.779  1.00 133.97 ?  336 ARG   B CZ  1 
ATOM   5431 N NH1 . ARG   B 2 40  ? 26.710  46.472  61.380  1.00 128.92 ?  336 ARG   B NH1 1 
ATOM   5432 N NH2 . ARG   B 2 40  ? 25.937  45.164  59.669  1.00 136.95 ?  336 ARG   B NH2 1 
ATOM   5433 N N   . GLN   B 2 41  ? 28.099  38.654  64.166  1.00 108.01 ?  337 GLN   B N   1 
ATOM   5434 C CA  . GLN   B 2 41  ? 29.056  37.518  64.165  1.00 111.52 ?  337 GLN   B CA  1 
ATOM   5435 C C   . GLN   B 2 41  ? 28.292  36.218  63.961  1.00 110.06 ?  337 GLN   B C   1 
ATOM   5436 O O   . GLN   B 2 41  ? 28.725  35.399  63.177  1.00 110.92 ?  337 GLN   B O   1 
ATOM   5437 C CB  . GLN   B 2 41  ? 29.713  37.366  65.527  1.00 108.05 ?  337 GLN   B CB  1 
ATOM   5438 C CG  . GLN   B 2 41  ? 31.216  37.521  65.475  1.00 114.26 ?  337 GLN   B CG  1 
ATOM   5439 C CD  . GLN   B 2 41  ? 31.513  38.956  65.139  1.00 130.72 ?  337 GLN   B CD  1 
ATOM   5440 O OE1 . GLN   B 2 41  ? 30.711  39.625  64.500  1.00 133.21 ?  337 GLN   B OE1 1 
ATOM   5441 N NE2 . GLN   B 2 41  ? 32.650  39.448  65.597  1.00 131.59 ?  337 GLN   B NE2 1 
ATOM   5442 N N   . LEU   B 2 42  ? 27.177  36.049  64.648  1.00 108.06 ?  338 LEU   B N   1 
ATOM   5443 C CA  . LEU   B 2 42  ? 26.366  34.843  64.419  1.00 105.98 ?  338 LEU   B CA  1 
ATOM   5444 C C   . LEU   B 2 42  ? 25.831  34.898  62.994  1.00 105.52 ?  338 LEU   B C   1 
ATOM   5445 O O   . LEU   B 2 42  ? 25.869  33.887  62.329  1.00 107.14 ?  338 LEU   B O   1 
ATOM   5446 C CB  . LEU   B 2 42  ? 25.240  34.843  65.445  1.00 99.42  ?  338 LEU   B CB  1 
ATOM   5447 C CG  . LEU   B 2 42  ? 25.735  34.900  66.879  1.00 99.93  ?  338 LEU   B CG  1 
ATOM   5448 C CD1 . LEU   B 2 42  ? 24.945  33.961  67.757  1.00 95.41  ?  338 LEU   B CD1 1 
ATOM   5449 C CD2 . LEU   B 2 42  ? 27.201  34.539  66.920  1.00 99.76  ?  338 LEU   B CD2 1 
ATOM   5450 N N   . ASP   B 2 43  ? 25.392  36.061  62.533  1.00 102.11 ?  339 ASP   B N   1 
ATOM   5451 C CA  . ASP   B 2 43  ? 24.826  36.115  61.168  1.00 109.55 ?  339 ASP   B CA  1 
ATOM   5452 C C   . ASP   B 2 43  ? 25.917  35.724  60.180  1.00 110.91 ?  339 ASP   B C   1 
ATOM   5453 O O   . ASP   B 2 43  ? 25.637  34.956  59.280  1.00 109.80 ?  339 ASP   B O   1 
ATOM   5454 C CB  . ASP   B 2 43  ? 24.310  37.515  60.849  1.00 112.40 ?  339 ASP   B CB  1 
ATOM   5455 C CG  . ASP   B 2 43  ? 22.819  37.586  60.576  1.00 114.88 ?  339 ASP   B CG  1 
ATOM   5456 O OD1 . ASP   B 2 43  ? 22.066  36.867  61.235  1.00 115.77 ?  339 ASP   B OD1 1 
ATOM   5457 O OD2 . ASP   B 2 43  ? 22.422  38.383  59.723  1.00 119.61 ?  339 ASP   B OD2 1 
ATOM   5458 N N   . MET   B 2 44  ? 27.121  36.248  60.342  1.00 111.79 ?  340 MET   B N   1 
ATOM   5459 C CA  . MET   B 2 44  ? 28.170  35.869  59.374  1.00 107.10 ?  340 MET   B CA  1 
ATOM   5460 C C   . MET   B 2 44  ? 28.559  34.406  59.548  1.00 107.69 ?  340 MET   B C   1 
ATOM   5461 O O   . MET   B 2 44  ? 28.552  33.694  58.559  1.00 110.81 ?  340 MET   B O   1 
ATOM   5462 C CB  . MET   B 2 44  ? 29.391  36.772  59.510  1.00 106.60 ?  340 MET   B CB  1 
ATOM   5463 C CG  . MET   B 2 44  ? 29.159  38.109  58.852  1.00 110.17 ?  340 MET   B CG  1 
ATOM   5464 S SD  . MET   B 2 44  ? 30.620  39.144  58.807  1.00 126.16 ?  340 MET   B SD  1 
ATOM   5465 C CE  . MET   B 2 44  ? 31.268  38.859  60.449  1.00 114.66 ?  340 MET   B CE  1 
ATOM   5466 N N   . GLU   B 2 45  ? 28.767  33.957  60.776  1.00 102.01 ?  341 GLU   B N   1 
ATOM   5467 C CA  . GLU   B 2 45  ? 29.213  32.559  60.974  1.00 100.10 ?  341 GLU   B CA  1 
ATOM   5468 C C   . GLU   B 2 45  ? 28.157  31.612  60.427  1.00 100.89 ?  341 GLU   B C   1 
ATOM   5469 O O   . GLU   B 2 45  ? 28.439  30.451  60.251  1.00 97.52  ?  341 GLU   B O   1 
ATOM   5470 C CB  . GLU   B 2 45  ? 29.457  32.277  62.446  1.00 102.10 ?  341 GLU   B CB  1 
ATOM   5471 C CG  . GLU   B 2 45  ? 29.122  30.858  62.822  1.00 106.43 ?  341 GLU   B CG  1 
ATOM   5472 C CD  . GLU   B 2 45  ? 30.084  30.211  63.794  1.00 118.76 ?  341 GLU   B CD  1 
ATOM   5473 O OE1 . GLU   B 2 45  ? 30.790  29.279  63.392  1.00 121.19 ?  341 GLU   B OE1 1 
ATOM   5474 O OE2 . GLU   B 2 45  ? 30.110  30.637  64.952  1.00 123.54 ?  341 GLU   B OE2 1 
ATOM   5475 N N   . LEU   B 2 46  ? 26.976  32.123  60.142  1.00 102.31 ?  342 LEU   B N   1 
ATOM   5476 C CA  . LEU   B 2 46  ? 25.949  31.246  59.613  1.00 100.11 ?  342 LEU   B CA  1 
ATOM   5477 C C   . LEU   B 2 46  ? 26.139  31.047  58.114  1.00 98.38  ?  342 LEU   B C   1 
ATOM   5478 O O   . LEU   B 2 46  ? 25.810  29.977  57.595  1.00 96.75  ?  342 LEU   B O   1 
ATOM   5479 C CB  . LEU   B 2 46  ? 24.552  31.805  59.890  1.00 104.04 ?  342 LEU   B CB  1 
ATOM   5480 C CG  . LEU   B 2 46  ? 23.472  30.732  59.714  1.00 98.95  ?  342 LEU   B CG  1 
ATOM   5481 C CD1 . LEU   B 2 46  ? 23.636  29.714  60.866  1.00 98.32  ?  342 LEU   B CD1 1 
ATOM   5482 C CD2 . LEU   B 2 46  ? 22.043  31.257  59.615  1.00 99.29  ?  342 LEU   B CD2 1 
ATOM   5483 N N   . VAL   B 2 47  ? 26.670  32.049  57.400  1.00 96.92  ?  343 VAL   B N   1 
ATOM   5484 C CA  . VAL   B 2 47  ? 27.018  31.833  55.996  1.00 99.86  ?  343 VAL   B CA  1 
ATOM   5485 C C   . VAL   B 2 47  ? 28.253  30.944  55.888  1.00 96.87  ?  343 VAL   B C   1 
ATOM   5486 O O   . VAL   B 2 47  ? 28.279  29.991  55.102  1.00 95.73  ?  343 VAL   B O   1 
ATOM   5487 C CB  . VAL   B 2 47  ? 27.193  33.175  55.253  1.00 96.08  ?  343 VAL   B CB  1 
ATOM   5488 C CG1 . VAL   B 2 47  ? 25.941  34.017  55.391  1.00 87.55  ?  343 VAL   B CG1 1 
ATOM   5489 C CG2 . VAL   B 2 47  ? 28.400  33.973  55.749  1.00 96.52  ?  343 VAL   B CG2 1 
ATOM   5490 N N   . SER   B 2 48  ? 29.267  31.210  56.717  1.00 94.56  ?  344 SER   B N   1 
ATOM   5491 C CA  . SER   B 2 48  ? 30.471  30.400  56.846  1.00 93.74  ?  344 SER   B CA  1 
ATOM   5492 C C   . SER   B 2 48  ? 30.141  28.914  56.780  1.00 98.70  ?  344 SER   B C   1 
ATOM   5493 O O   . SER   B 2 48  ? 30.804  28.149  56.072  1.00 106.74 ?  344 SER   B O   1 
ATOM   5494 C CB  . SER   B 2 48  ? 31.181  30.749  58.159  1.00 99.32  ?  344 SER   B CB  1 
ATOM   5495 O OG  . SER   B 2 48  ? 32.316  29.938  58.410  1.00 105.80 ?  344 SER   B OG  1 
ATOM   5496 N N   . VAL   B 2 49  ? 29.097  28.505  57.486  1.00 96.34  ?  345 VAL   B N   1 
ATOM   5497 C CA  . VAL   B 2 49  ? 28.768  27.093  57.548  1.00 93.28  ?  345 VAL   B CA  1 
ATOM   5498 C C   . VAL   B 2 49  ? 27.833  26.659  56.425  1.00 93.28  ?  345 VAL   B C   1 
ATOM   5499 O O   . VAL   B 2 49  ? 27.890  25.507  55.993  1.00 99.10  ?  345 VAL   B O   1 
ATOM   5500 C CB  . VAL   B 2 49  ? 28.196  26.762  58.932  1.00 91.54  ?  345 VAL   B CB  1 
ATOM   5501 C CG1 . VAL   B 2 49  ? 27.670  25.330  58.979  1.00 93.67  ?  345 VAL   B CG1 1 
ATOM   5502 C CG2 . VAL   B 2 49  ? 29.281  26.955  59.981  1.00 97.93  ?  345 VAL   B CG2 1 
ATOM   5503 N N   . LYS   B 2 50  ? 26.994  27.546  55.904  1.00 93.26  ?  346 LYS   B N   1 
ATOM   5504 C CA  . LYS   B 2 50  ? 26.154  27.112  54.796  1.00 95.26  ?  346 LYS   B CA  1 
ATOM   5505 C C   . LYS   B 2 50  ? 26.989  26.764  53.573  1.00 97.82  ?  346 LYS   B C   1 
ATOM   5506 O O   . LYS   B 2 50  ? 26.753  25.732  52.939  1.00 102.40 ?  346 LYS   B O   1 
ATOM   5507 C CB  . LYS   B 2 50  ? 25.090  28.155  54.449  1.00 99.38  ?  346 LYS   B CB  1 
ATOM   5508 C CG  . LYS   B 2 50  ? 24.081  28.401  55.552  1.00 103.06 ?  346 LYS   B CG  1 
ATOM   5509 C CD  . LYS   B 2 50  ? 23.005  29.394  55.112  1.00 112.93 ?  346 LYS   B CD  1 
ATOM   5510 C CE  . LYS   B 2 50  ? 21.752  28.704  54.595  1.00 108.42 ?  346 LYS   B CE  1 
ATOM   5511 N NZ  . LYS   B 2 50  ? 20.889  28.287  55.744  1.00 111.04 ?  346 LYS   B NZ  1 
ATOM   5512 N N   . ARG   B 2 51  ? 27.985  27.589  53.238  1.00 98.27  ?  347 ARG   B N   1 
ATOM   5513 C CA  . ARG   B 2 51  ? 28.864  27.258  52.117  1.00 101.70 ?  347 ARG   B CA  1 
ATOM   5514 C C   . ARG   B 2 51  ? 29.681  26.001  52.377  1.00 101.52 ?  347 ARG   B C   1 
ATOM   5515 O O   . ARG   B 2 51  ? 29.867  25.182  51.468  1.00 105.72 ?  347 ARG   B O   1 
ATOM   5516 C CB  . ARG   B 2 51  ? 29.791  28.421  51.801  1.00 102.45 ?  347 ARG   B CB  1 
ATOM   5517 C CG  . ARG   B 2 51  ? 30.651  28.810  52.973  1.00 100.63 ?  347 ARG   B CG  1 
ATOM   5518 C CD  . ARG   B 2 51  ? 31.433  30.017  52.587  1.00 111.69 ?  347 ARG   B CD  1 
ATOM   5519 N NE  . ARG   B 2 51  ? 30.473  30.987  52.077  1.00 122.51 ?  347 ARG   B NE  1 
ATOM   5520 C CZ  . ARG   B 2 51  ? 30.769  32.192  51.609  1.00 123.57 ?  347 ARG   B CZ  1 
ATOM   5521 N NH1 . ARG   B 2 51  ? 32.010  32.661  51.701  1.00 120.32 ?  347 ARG   B NH1 1 
ATOM   5522 N NH2 . ARG   B 2 51  ? 29.795  32.954  51.112  1.00 122.51 ?  347 ARG   B NH2 1 
ATOM   5523 N N   . GLN   B 2 52  ? 30.197  25.832  53.595  1.00 92.86  ?  348 GLN   B N   1 
ATOM   5524 C CA  . GLN   B 2 52  ? 30.923  24.606  53.881  1.00 97.45  ?  348 GLN   B CA  1 
ATOM   5525 C C   . GLN   B 2 52  ? 30.031  23.381  53.687  1.00 100.32 ?  348 GLN   B C   1 
ATOM   5526 O O   . GLN   B 2 52  ? 30.541  22.290  53.402  1.00 101.97 ?  348 GLN   B O   1 
ATOM   5527 C CB  . GLN   B 2 52  ? 31.502  24.687  55.285  1.00 96.58  ?  348 GLN   B CB  1 
ATOM   5528 C CG  . GLN   B 2 52  ? 32.074  23.404  55.822  1.00 105.91 ?  348 GLN   B CG  1 
ATOM   5529 C CD  . GLN   B 2 52  ? 32.508  23.546  57.272  1.00 119.87 ?  348 GLN   B CD  1 
ATOM   5530 O OE1 . GLN   B 2 52  ? 32.114  24.495  57.968  1.00 112.61 ?  348 GLN   B OE1 1 
ATOM   5531 N NE2 . GLN   B 2 52  ? 33.332  22.607  57.736  1.00 123.25 ?  348 GLN   B NE2 1 
ATOM   5532 N N   . ILE   B 2 53  ? 28.709  23.558  53.768  1.00 96.55  ?  349 ILE   B N   1 
ATOM   5533 C CA  . ILE   B 2 53  ? 27.784  22.479  53.439  1.00 94.62  ?  349 ILE   B CA  1 
ATOM   5534 C C   . ILE   B 2 53  ? 27.703  22.279  51.935  1.00 96.00  ?  349 ILE   B C   1 
ATOM   5535 O O   . ILE   B 2 53  ? 27.811  21.151  51.449  1.00 103.73 ?  349 ILE   B O   1 
ATOM   5536 C CB  . ILE   B 2 53  ? 26.394  22.749  54.035  1.00 96.93  ?  349 ILE   B CB  1 
ATOM   5537 C CG1 . ILE   B 2 53  ? 26.443  22.534  55.544  1.00 96.79  ?  349 ILE   B CG1 1 
ATOM   5538 C CG2 . ILE   B 2 53  ? 25.348  21.869  53.387  1.00 97.82  ?  349 ILE   B CG2 1 
ATOM   5539 C CD1 . ILE   B 2 53  ? 25.130  22.575  56.220  1.00 95.17  ?  349 ILE   B CD1 1 
ATOM   5540 N N   . GLN   B 2 54  ? 27.458  23.352  51.175  1.00 95.74  ?  350 GLN   B N   1 
ATOM   5541 C CA  . GLN   B 2 54  ? 27.460  23.220  49.717  1.00 101.95 ?  350 GLN   B CA  1 
ATOM   5542 C C   . GLN   B 2 54  ? 28.718  22.521  49.245  1.00 101.73 ?  350 GLN   B C   1 
ATOM   5543 O O   . GLN   B 2 54  ? 28.682  21.693  48.328  1.00 101.73 ?  350 GLN   B O   1 
ATOM   5544 C CB  . GLN   B 2 54  ? 27.352  24.584  49.025  1.00 99.44  ?  350 GLN   B CB  1 
ATOM   5545 C CG  . GLN   B 2 54  ? 26.075  25.355  49.244  1.00 106.64 ?  350 GLN   B CG  1 
ATOM   5546 C CD  . GLN   B 2 54  ? 24.820  24.650  48.719  1.00 116.18 ?  350 GLN   B CD  1 
ATOM   5547 O OE1 . GLN   B 2 54  ? 24.637  23.438  48.884  1.00 114.66 ?  350 GLN   B OE1 1 
ATOM   5548 N NE2 . GLN   B 2 54  ? 23.948  25.423  48.071  1.00 115.21 ?  350 GLN   B NE2 1 
ATOM   5549 N N   . ASN   B 2 55  ? 29.833  22.818  49.893  1.00 102.03 ?  351 ASN   B N   1 
ATOM   5550 C CA  . ASN   B 2 55  ? 31.112  22.341  49.413  1.00 102.61 ?  351 ASN   B CA  1 
ATOM   5551 C C   . ASN   B 2 55  ? 31.352  20.886  49.819  1.00 98.76  ?  351 ASN   B C   1 
ATOM   5552 O O   . ASN   B 2 55  ? 31.976  20.129  49.090  1.00 97.97  ?  351 ASN   B O   1 
ATOM   5553 C CB  . ASN   B 2 55  ? 32.166  23.372  49.855  1.00 99.56  ?  351 ASN   B CB  1 
ATOM   5554 C CG  . ASN   B 2 55  ? 33.578  23.030  49.444  1.00 101.86 ?  351 ASN   B CG  1 
ATOM   5555 O OD1 . ASN   B 2 55  ? 33.886  21.891  49.107  1.00 111.34 ?  351 ASN   B OD1 1 
ATOM   5556 N ND2 . ASN   B 2 55  ? 34.424  24.044  49.371  1.00 114.18 ?  351 ASN   B ND2 1 
ATOM   5557 N N   . ILE   B 2 56  ? 30.776  20.426  50.915  1.00 98.41  ?  352 ILE   B N   1 
ATOM   5558 C CA  . ILE   B 2 56  ? 30.856  18.989  51.178  1.00 90.19  ?  352 ILE   B CA  1 
ATOM   5559 C C   . ILE   B 2 56  ? 29.660  18.245  50.582  1.00 90.39  ?  352 ILE   B C   1 
ATOM   5560 O O   . ILE   B 2 56  ? 29.674  17.021  50.486  1.00 92.72  ?  352 ILE   B O   1 
ATOM   5561 C CB  . ILE   B 2 56  ? 31.056  18.741  52.683  1.00 90.00  ?  352 ILE   B CB  1 
ATOM   5562 C CG1 . ILE   B 2 56  ? 32.380  19.373  53.080  1.00 96.86  ?  352 ILE   B CG1 1 
ATOM   5563 C CG2 . ILE   B 2 56  ? 31.134  17.296  52.980  1.00 86.62  ?  352 ILE   B CG2 1 
ATOM   5564 C CD1 . ILE   B 2 56  ? 32.640  19.448  54.560  1.00 100.54 ?  352 ILE   B CD1 1 
ATOM   5565 N N   . LYS   B 2 57  ? 28.617  18.944  50.140  1.00 95.10  ?  353 LYS   B N   1 
ATOM   5566 C CA  . LYS   B 2 57  ? 27.662  18.327  49.212  1.00 92.98  ?  353 LYS   B CA  1 
ATOM   5567 C C   . LYS   B 2 57  ? 28.351  17.997  47.889  1.00 91.86  ?  353 LYS   B C   1 
ATOM   5568 O O   . LYS   B 2 57  ? 28.263  16.869  47.408  1.00 92.99  ?  353 LYS   B O   1 
ATOM   5569 C CB  . LYS   B 2 57  ? 26.446  19.232  48.899  1.00 93.92  ?  353 LYS   B CB  1 
ATOM   5570 C CG  . LYS   B 2 57  ? 25.396  19.595  50.015  1.00 103.27 ?  353 LYS   B CG  1 
ATOM   5571 C CD  . LYS   B 2 57  ? 24.356  18.532  50.487  1.00 104.02 ?  353 LYS   B CD  1 
ATOM   5572 C CE  . LYS   B 2 57  ? 23.546  19.083  51.660  1.00 111.58 ?  353 LYS   B CE  1 
ATOM   5573 N NZ  . LYS   B 2 57  ? 22.490  18.149  52.000  1.00 111.76 ?  353 LYS   B NZ  1 
ATOM   5574 N N   . GLN   B 2 58  ? 29.113  18.961  47.337  1.00 95.15  ?  354 GLN   B N   1 
ATOM   5575 C CA  . GLN   B 2 58  ? 29.821  18.800  46.064  1.00 96.45  ?  354 GLN   B CA  1 
ATOM   5576 C C   . GLN   B 2 58  ? 30.872  17.688  46.142  1.00 94.14  ?  354 GLN   B C   1 
ATOM   5577 O O   . GLN   B 2 58  ? 30.876  16.772  45.316  1.00 88.46  ?  354 GLN   B O   1 
ATOM   5578 C CB  . GLN   B 2 58  ? 30.452  20.142  45.706  1.00 94.23  ?  354 GLN   B CB  1 
ATOM   5579 C CG  . GLN   B 2 58  ? 29.483  21.209  45.201  1.00 101.64 ?  354 GLN   B CG  1 
ATOM   5580 C CD  . GLN   B 2 58  ? 29.210  21.094  43.728  1.00 113.53 ?  354 GLN   B CD  1 
ATOM   5581 O OE1 . GLN   B 2 58  ? 29.950  20.418  43.015  1.00 118.38 ?  354 GLN   B OE1 1 
ATOM   5582 N NE2 . GLN   B 2 58  ? 28.200  21.828  43.239  1.00 110.98 ?  354 GLN   B NE2 1 
ATOM   5583 N N   . THR   B 2 59  ? 31.811  17.788  47.089  1.00 88.62  ?  355 THR   B N   1 
ATOM   5584 C CA  . THR   B 2 59  ? 32.720  16.682  47.373  1.00 87.82  ?  355 THR   B CA  1 
ATOM   5585 C C   . THR   B 2 59  ? 31.992  15.345  47.458  1.00 92.97  ?  355 THR   B C   1 
ATOM   5586 O O   . THR   B 2 59  ? 32.371  14.376  46.789  1.00 95.41  ?  355 THR   B O   1 
ATOM   5587 C CB  . THR   B 2 59  ? 33.490  16.961  48.663  1.00 93.82  ?  355 THR   B CB  1 
ATOM   5588 O OG1 . THR   B 2 59  ? 34.393  18.058  48.455  1.00 94.32  ?  355 THR   B OG1 1 
ATOM   5589 C CG2 . THR   B 2 59  ? 34.221  15.709  49.180  1.00 89.21  ?  355 THR   B CG2 1 
ATOM   5590 N N   . ASN   B 2 60  ? 30.944  15.262  48.274  1.00 90.51  ?  356 ASN   B N   1 
ATOM   5591 C CA  . ASN   B 2 60  ? 30.299  13.966  48.423  1.00 84.39  ?  356 ASN   B CA  1 
ATOM   5592 C C   . ASN   B 2 60  ? 29.509  13.588  47.175  1.00 88.15  ?  356 ASN   B C   1 
ATOM   5593 O O   . ASN   B 2 60  ? 29.295  12.402  46.923  1.00 92.70  ?  356 ASN   B O   1 
ATOM   5594 C CB  . ASN   B 2 60  ? 29.403  13.948  49.656  1.00 82.51  ?  356 ASN   B CB  1 
ATOM   5595 C CG  . ASN   B 2 60  ? 30.195  13.847  50.941  1.00 90.61  ?  356 ASN   B CG  1 
ATOM   5596 O OD1 . ASN   B 2 60  ? 31.376  13.515  50.931  1.00 89.84  ?  356 ASN   B OD1 1 
ATOM   5597 N ND2 . ASN   B 2 60  ? 29.539  14.115  52.062  1.00 95.90  ?  356 ASN   B ND2 1 
ATOM   5598 N N   . SER   B 2 61  ? 29.084  14.566  46.373  1.00 88.25  ?  357 SER   B N   1 
ATOM   5599 C CA  . SER   B 2 61  ? 28.320  14.239  45.172  1.00 87.11  ?  357 SER   B CA  1 
ATOM   5600 C C   . SER   B 2 61  ? 29.210  13.602  44.110  1.00 93.22  ?  357 SER   B C   1 
ATOM   5601 O O   . SER   B 2 61  ? 28.778  12.692  43.390  1.00 92.47  ?  357 SER   B O   1 
ATOM   5602 C CB  . SER   B 2 61  ? 27.641  15.491  44.623  1.00 83.25  ?  357 SER   B CB  1 
ATOM   5603 O OG  . SER   B 2 61  ? 27.072  15.239  43.353  1.00 91.32  ?  357 SER   B OG  1 
ATOM   5604 N N   . ALA   B 2 62  ? 30.455  14.071  44.000  1.00 93.05  ?  358 ALA   B N   1 
ATOM   5605 C CA  . ALA   B 2 62  ? 31.411  13.460  43.085  1.00 90.35  ?  358 ALA   B CA  1 
ATOM   5606 C C   . ALA   B 2 62  ? 31.800  12.053  43.544  1.00 95.44  ?  358 ALA   B C   1 
ATOM   5607 O O   . ALA   B 2 62  ? 31.728  11.090  42.765  1.00 91.44  ?  358 ALA   B O   1 
ATOM   5608 C CB  . ALA   B 2 62  ? 32.642  14.357  42.960  1.00 79.93  ?  358 ALA   B CB  1 
ATOM   5609 N N   . LEU   B 2 63  ? 32.217  11.917  44.811  1.00 92.55  ?  359 LEU   B N   1 
ATOM   5610 C CA  . LEU   B 2 63  ? 32.564  10.605  45.355  1.00 91.92  ?  359 LEU   B CA  1 
ATOM   5611 C C   . LEU   B 2 63  ? 31.436  9.599   45.141  1.00 96.05  ?  359 LEU   B C   1 
ATOM   5612 O O   . LEU   B 2 63  ? 31.685  8.414   44.891  1.00 95.36  ?  359 LEU   B O   1 
ATOM   5613 C CB  . LEU   B 2 63  ? 32.897  10.721  46.847  1.00 90.06  ?  359 LEU   B CB  1 
ATOM   5614 C CG  . LEU   B 2 63  ? 34.348  10.994  47.251  1.00 93.26  ?  359 LEU   B CG  1 
ATOM   5615 C CD1 . LEU   B 2 63  ? 34.775  12.386  46.821  1.00 95.72  ?  359 LEU   B CD1 1 
ATOM   5616 C CD2 . LEU   B 2 63  ? 34.549  10.817  48.759  1.00 92.96  ?  359 LEU   B CD2 1 
ATOM   5617 N N   . LYS   B 2 64  ? 30.183  10.053  45.222  1.00 100.31 ?  360 LYS   B N   1 
ATOM   5618 C CA  . LYS   B 2 64  ? 29.074  9.134   44.995  1.00 98.33  ?  360 LYS   B CA  1 
ATOM   5619 C C   . LYS   B 2 64  ? 29.047  8.652   43.553  1.00 94.65  ?  360 LYS   B C   1 
ATOM   5620 O O   . LYS   B 2 64  ? 28.717  7.489   43.296  1.00 99.65  ?  360 LYS   B O   1 
ATOM   5621 C CB  . LYS   B 2 64  ? 27.738  9.789   45.374  1.00 99.93  ?  360 LYS   B CB  1 
ATOM   5622 C CG  . LYS   B 2 64  ? 27.119  9.281   46.703  1.00 97.57  ?  360 LYS   B CG  1 
ATOM   5623 C CD  . LYS   B 2 64  ? 25.760  9.955   47.005  1.00 108.04 ?  360 LYS   B CD  1 
ATOM   5624 C CE  . LYS   B 2 64  ? 24.701  9.645   45.933  1.00 112.78 ?  360 LYS   B CE  1 
ATOM   5625 N NZ  . LYS   B 2 64  ? 23.482  10.517  46.024  1.00 113.42 ?  360 LYS   B NZ  1 
ATOM   5626 N N   . GLU   B 2 65  ? 29.417  9.512   42.602  1.00 95.43  ?  361 GLU   B N   1 
ATOM   5627 C CA  . GLU   B 2 65  ? 29.343  9.103   41.205  1.00 99.62  ?  361 GLU   B CA  1 
ATOM   5628 C C   . GLU   B 2 65  ? 30.411  8.068   40.854  1.00 103.50 ?  361 GLU   B C   1 
ATOM   5629 O O   . GLU   B 2 65  ? 30.151  7.164   40.049  1.00 105.26 ?  361 GLU   B O   1 
ATOM   5630 C CB  . GLU   B 2 65  ? 29.442  10.323  40.290  1.00 94.44  ?  361 GLU   B CB  1 
ATOM   5631 C CG  . GLU   B 2 65  ? 29.427  9.950   38.823  1.00 112.24 ?  361 GLU   B CG  1 
ATOM   5632 C CD  . GLU   B 2 65  ? 28.744  10.994  37.948  1.00 122.36 ?  361 GLU   B CD  1 
ATOM   5633 O OE1 . GLU   B 2 65  ? 27.843  10.601  37.174  1.00 125.59 ?  361 GLU   B OE1 1 
ATOM   5634 O OE2 . GLU   B 2 65  ? 29.114  12.187  38.041  1.00 121.19 ?  361 GLU   B OE2 1 
ATOM   5635 N N   . LYS   B 2 66  ? 31.597  8.160   41.465  1.00 100.85 ?  362 LYS   B N   1 
ATOM   5636 C CA  . LYS   B 2 66  ? 32.620  7.141   41.263  1.00 91.08  ?  362 LYS   B CA  1 
ATOM   5637 C C   . LYS   B 2 66  ? 32.146  5.755   41.664  1.00 95.38  ?  362 LYS   B C   1 
ATOM   5638 O O   . LYS   B 2 66  ? 32.681  4.761   41.164  1.00 109.63 ?  362 LYS   B O   1 
ATOM   5639 C CB  . LYS   B 2 66  ? 33.888  7.489   42.044  1.00 86.57  ?  362 LYS   B CB  1 
ATOM   5640 C CG  . LYS   B 2 66  ? 34.649  8.668   41.463  1.00 89.93  ?  362 LYS   B CG  1 
ATOM   5641 C CD  . LYS   B 2 66  ? 35.971  8.872   42.181  1.00 89.20  ?  362 LYS   B CD  1 
ATOM   5642 C CE  . LYS   B 2 66  ? 36.776  10.012  41.560  1.00 99.71  ?  362 LYS   B CE  1 
ATOM   5643 N NZ  . LYS   B 2 66  ? 38.088  10.205  42.264  1.00 100.84 ?  362 LYS   B NZ  1 
ATOM   5644 N N   . LEU   B 2 67  ? 31.152  5.660   42.540  1.00 95.35  ?  363 LEU   B N   1 
ATOM   5645 C CA  . LEU   B 2 67  ? 30.666  4.374   43.016  1.00 95.50  ?  363 LEU   B CA  1 
ATOM   5646 C C   . LEU   B 2 67  ? 29.471  3.865   42.213  1.00 106.13 ?  363 LEU   B C   1 
ATOM   5647 O O   . LEU   B 2 67  ? 28.658  3.091   42.745  1.00 107.84 ?  363 LEU   B O   1 
ATOM   5648 C CB  . LEU   B 2 67  ? 30.331  4.467   44.503  1.00 88.75  ?  363 LEU   B CB  1 
ATOM   5649 C CG  . LEU   B 2 67  ? 31.467  4.046   45.431  1.00 91.45  ?  363 LEU   B CG  1 
ATOM   5650 C CD1 . LEU   B 2 67  ? 32.716  4.813   45.110  1.00 90.32  ?  363 LEU   B CD1 1 
ATOM   5651 C CD2 . LEU   B 2 67  ? 31.089  4.269   46.876  1.00 91.78  ?  363 LEU   B CD2 1 
ATOM   5652 N N   . ASP   B 2 68  ? 29.384  4.304   40.962  1.00 106.65 ?  364 ASP   B N   1 
ATOM   5653 C CA  . ASP   B 2 68  ? 28.283  3.867   40.072  1.00 111.81 ?  364 ASP   B CA  1 
ATOM   5654 C C   . ASP   B 2 68  ? 28.313  2.347   39.987  1.00 117.32 ?  364 ASP   B C   1 
ATOM   5655 O O   . ASP   B 2 68  ? 29.382  1.785   39.758  1.00 118.76 ?  364 ASP   B O   1 
ATOM   5656 C CB  . ASP   B 2 68  ? 28.447  4.422   38.660  1.00 114.62 ?  364 ASP   B CB  1 
ATOM   5657 C CG  . ASP   B 2 68  ? 29.452  3.640   37.834  1.00 122.67 ?  364 ASP   B CG  1 
ATOM   5658 O OD1 . ASP   B 2 68  ? 30.588  3.495   38.297  1.00 115.14 ?  364 ASP   B OD1 1 
ATOM   5659 O OD2 . ASP   B 2 68  ? 29.073  3.124   36.778  1.00 133.84 ?  364 ASP   B OD2 1 
ATOM   5660 N N   . GLY   B 2 69  ? 27.208  1.701   40.341  1.00 115.57 ?  365 GLY   B N   1 
ATOM   5661 C CA  . GLY   B 2 69  ? 27.076  0.238   40.224  1.00 114.06 ?  365 GLY   B CA  1 
ATOM   5662 C C   . GLY   B 2 69  ? 27.696  -0.539  41.363  1.00 107.76 ?  365 GLY   B C   1 
ATOM   5663 O O   . GLY   B 2 69  ? 27.600  -1.753  41.348  1.00 107.73 ?  365 GLY   B O   1 
ATOM   5664 N N   . GLY   B 2 70  ? 28.309  0.134   42.323  1.00 106.88 ?  366 GLY   B N   1 
ATOM   5665 C CA  . GLY   B 2 70  ? 28.910  -0.576  43.456  1.00 103.79 ?  366 GLY   B CA  1 
ATOM   5666 C C   . GLY   B 2 70  ? 29.891  -1.626  43.004  1.00 98.30  ?  366 GLY   B C   1 
ATOM   5667 O O   . GLY   B 2 70  ? 30.706  -1.350  42.148  1.00 103.10 ?  366 GLY   B O   1 
ATOM   5668 N N   . ILE   B 2 71  ? 29.752  -2.814  43.562  1.00 94.17  ?  367 ILE   B N   1 
ATOM   5669 C CA  . ILE   B 2 71  ? 30.662  -3.942  43.268  1.00 96.49  ?  367 ILE   B CA  1 
ATOM   5670 C C   . ILE   B 2 71  ? 29.829  -5.073  42.690  1.00 99.64  ?  367 ILE   B C   1 
ATOM   5671 O O   . ILE   B 2 71  ? 30.128  -6.201  42.983  1.00 97.08  ?  367 ILE   B O   1 
ATOM   5672 C CB  . ILE   B 2 71  ? 31.320  -4.360  44.580  1.00 87.35  ?  367 ILE   B CB  1 
ATOM   5673 C CG1 . ILE   B 2 71  ? 30.287  -4.896  45.560  1.00 85.11  ?  367 ILE   B CG1 1 
ATOM   5674 C CG2 . ILE   B 2 71  ? 32.046  -3.181  45.170  1.00 85.47  ?  367 ILE   B CG2 1 
ATOM   5675 C CD1 . ILE   B 2 71  ? 30.862  -5.205  46.905  1.00 86.77  ?  367 ILE   B CD1 1 
ATOM   5676 N N   . GLU   B 2 72  ? 28.790  -4.757  41.930  1.00 99.24  ?  368 GLU   B N   1 
ATOM   5677 C CA  . GLU   B 2 72  ? 27.914  -5.826  41.401  1.00 101.17 ?  368 GLU   B CA  1 
ATOM   5678 C C   . GLU   B 2 72  ? 28.677  -6.757  40.464  1.00 98.96  ?  368 GLU   B C   1 
ATOM   5679 O O   . GLU   B 2 72  ? 28.549  -7.957  40.609  1.00 98.79  ?  368 GLU   B O   1 
ATOM   5680 C CB  . GLU   B 2 72  ? 26.700  -5.219  40.713  1.00 103.79 ?  368 GLU   B CB  1 
ATOM   5681 C CG  . GLU   B 2 72  ? 25.454  -5.339  41.559  1.00 108.41 ?  368 GLU   B CG  1 
ATOM   5682 C CD  . GLU   B 2 72  ? 25.739  -5.873  42.947  1.00 117.28 ?  368 GLU   B CD  1 
ATOM   5683 O OE1 . GLU   B 2 72  ? 25.295  -6.971  43.265  1.00 123.77 ?  368 GLU   B OE1 1 
ATOM   5684 O OE2 . GLU   B 2 72  ? 26.426  -5.194  43.699  1.00 116.90 ?  368 GLU   B OE2 1 
ATOM   5685 N N   . PRO   B 2 73  ? 29.535  -6.271  39.558  1.00 96.90  ?  369 PRO   B N   1 
ATOM   5686 C CA  . PRO   B 2 73  ? 30.258  -7.137  38.640  1.00 97.78  ?  369 PRO   B CA  1 
ATOM   5687 C C   . PRO   B 2 73  ? 31.394  -7.959  39.250  1.00 94.28  ?  369 PRO   B C   1 
ATOM   5688 O O   . PRO   B 2 73  ? 31.953  -8.742  38.557  1.00 95.28  ?  369 PRO   B O   1 
ATOM   5689 C CB  . PRO   B 2 73  ? 30.928  -6.144  37.693  1.00 100.61 ?  369 PRO   B CB  1 
ATOM   5690 C CG  . PRO   B 2 73  ? 30.118  -4.906  37.836  1.00 92.88  ?  369 PRO   B CG  1 
ATOM   5691 C CD  . PRO   B 2 73  ? 29.799  -4.877  39.307  1.00 95.61  ?  369 PRO   B CD  1 
ATOM   5692 N N   . TYR   B 2 74  ? 31.767  -7.663  40.484  1.00 86.98  ?  370 TYR   B N   1 
ATOM   5693 C CA  . TYR   B 2 74  ? 32.907  -8.308  41.160  1.00 83.96  ?  370 TYR   B CA  1 
ATOM   5694 C C   . TYR   B 2 74  ? 32.443  -9.311  42.209  1.00 89.30  ?  370 TYR   B C   1 
ATOM   5695 O O   . TYR   B 2 74  ? 33.216  -9.642  43.073  1.00 86.50  ?  370 TYR   B O   1 
ATOM   5696 C CB  . TYR   B 2 74  ? 33.788  -7.209  41.738  1.00 89.03  ?  370 TYR   B CB  1 
ATOM   5697 C CG  . TYR   B 2 74  ? 34.026  -6.071  40.784  1.00 90.45  ?  370 TYR   B CG  1 
ATOM   5698 C CD1 . TYR   B 2 74  ? 34.344  -6.306  39.468  1.00 93.33  ?  370 TYR   B CD1 1 
ATOM   5699 C CD2 . TYR   B 2 74  ? 33.950  -4.761  41.191  1.00 91.87  ?  370 TYR   B CD2 1 
ATOM   5700 C CE1 . TYR   B 2 74  ? 34.575  -5.278  38.578  1.00 95.79  ?  370 TYR   B CE1 1 
ATOM   5701 C CE2 . TYR   B 2 74  ? 34.185  -3.717  40.320  1.00 92.71  ?  370 TYR   B CE2 1 
ATOM   5702 C CZ  . TYR   B 2 74  ? 34.501  -3.977  39.008  1.00 94.89  ?  370 TYR   B CZ  1 
ATOM   5703 O OH  . TYR   B 2 74  ? 34.728  -2.966  38.134  1.00 97.12  ?  370 TYR   B OH  1 
ATOM   5704 N N   . ARG   B 2 75  ? 31.207  -9.771  42.147  1.00 93.42  ?  371 ARG   B N   1 
ATOM   5705 C CA  . ARG   B 2 75  ? 30.777  -10.728 43.193  1.00 99.79  ?  371 ARG   B CA  1 
ATOM   5706 C C   . ARG   B 2 75  ? 30.860  -12.165 42.673  1.00 99.54  ?  371 ARG   B C   1 
ATOM   5707 O O   . ARG   B 2 75  ? 30.575  -12.368 41.504  1.00 94.11  ?  371 ARG   B O   1 
ATOM   5708 C CB  . ARG   B 2 75  ? 29.374  -10.352 43.666  1.00 104.87 ?  371 ARG   B CB  1 
ATOM   5709 C CG  . ARG   B 2 75  ? 29.037  -10.873 45.052  1.00 102.39 ?  371 ARG   B CG  1 
ATOM   5710 C CD  . ARG   B 2 75  ? 28.866  -9.789  46.089  1.00 113.46 ?  371 ARG   B CD  1 
ATOM   5711 N NE  . ARG   B 2 75  ? 28.311  -8.572  45.536  1.00 119.17 ?  371 ARG   B NE  1 
ATOM   5712 C CZ  . ARG   B 2 75  ? 27.776  -7.618  46.274  1.00 121.09 ?  371 ARG   B CZ  1 
ATOM   5713 N NH1 . ARG   B 2 75  ? 27.724  -7.747  47.586  1.00 110.72 ?  371 ARG   B NH1 1 
ATOM   5714 N NH2 . ARG   B 2 75  ? 27.294  -6.536  45.705  1.00 121.06 ?  371 ARG   B NH2 1 
ATOM   5715 N N   . LEU   B 2 76  ? 31.258  -13.104 43.533  1.00 98.78  ?  372 LEU   B N   1 
ATOM   5716 C CA  . LEU   B 2 76  ? 31.382  -14.489 43.208  1.00 102.90 ?  372 LEU   B CA  1 
ATOM   5717 C C   . LEU   B 2 76  ? 30.205  -15.214 43.821  1.00 110.55 ?  372 LEU   B C   1 
ATOM   5718 O O   . LEU   B 2 76  ? 29.835  -14.912 44.964  1.00 111.75 ?  372 LEU   B O   1 
ATOM   5719 C CB  . LEU   B 2 76  ? 32.696  -15.040 43.767  1.00 103.71 ?  372 LEU   B CB  1 
ATOM   5720 C CG  . LEU   B 2 76  ? 33.895  -14.134 43.470  1.00 98.90  ?  372 LEU   B CG  1 
ATOM   5721 C CD1 . LEU   B 2 76  ? 35.119  -14.557 44.287  1.00 91.11  ?  372 LEU   B CD1 1 
ATOM   5722 C CD2 . LEU   B 2 76  ? 34.211  -14.065 41.955  1.00 87.72  ?  372 LEU   B CD2 1 
ATOM   5723 N N   . PRO   B 2 77  ? 29.576  -16.130 43.099  1.00 111.93 ?  373 PRO   B N   1 
ATOM   5724 C CA  . PRO   B 2 77  ? 28.505  -16.938 43.694  1.00 111.12 ?  373 PRO   B CA  1 
ATOM   5725 C C   . PRO   B 2 77  ? 28.884  -17.609 45.014  1.00 118.28 ?  373 PRO   B C   1 
ATOM   5726 O O   . PRO   B 2 77  ? 30.061  -17.680 45.388  1.00 116.80 ?  373 PRO   B O   1 
ATOM   5727 C CB  . PRO   B 2 77  ? 28.207  -17.970 42.596  1.00 113.41 ?  373 PRO   B CB  1 
ATOM   5728 C CG  . PRO   B 2 77  ? 29.265  -17.748 41.515  1.00 107.36 ?  373 PRO   B CG  1 
ATOM   5729 C CD  . PRO   B 2 77  ? 29.667  -16.332 41.646  1.00 106.10 ?  373 PRO   B CD  1 
ATOM   5730 N N   . GLU   B 2 78  ? 27.868  -18.101 45.723  1.00 125.74 ?  374 GLU   B N   1 
ATOM   5731 C CA  . GLU   B 2 78  ? 28.018  -18.685 47.052  1.00 132.63 ?  374 GLU   B CA  1 
ATOM   5732 C C   . GLU   B 2 78  ? 28.368  -20.169 46.943  1.00 140.03 ?  374 GLU   B C   1 
ATOM   5733 O O   . GLU   B 2 78  ? 27.619  -20.946 46.335  1.00 139.05 ?  374 GLU   B O   1 
ATOM   5734 C CB  . GLU   B 2 78  ? 26.725  -18.493 47.848  1.00 135.98 ?  374 GLU   B CB  1 
ATOM   5735 C CG  . GLU   B 2 78  ? 26.791  -18.888 49.322  1.00 140.97 ?  374 GLU   B CG  1 
ATOM   5736 C CD  . GLU   B 2 78  ? 27.898  -18.174 50.079  1.00 150.27 ?  374 GLU   B CD  1 
ATOM   5737 O OE1 . GLU   B 2 78  ? 29.012  -18.743 50.175  1.00 154.03 ?  374 GLU   B OE1 1 
ATOM   5738 O OE2 . GLU   B 2 78  ? 27.653  -17.049 50.579  1.00 146.02 ?  374 GLU   B OE2 1 
ATOM   5739 N N   . VAL   B 2 79  ? 29.493  -20.563 47.540  1.00 143.97 ?  375 VAL   B N   1 
ATOM   5740 C CA  . VAL   B 2 79  ? 29.904  -21.967 47.574  1.00 144.57 ?  375 VAL   B CA  1 
ATOM   5741 C C   . VAL   B 2 79  ? 29.112  -22.668 48.676  1.00 145.62 ?  375 VAL   B C   1 
ATOM   5742 O O   . VAL   B 2 79  ? 29.341  -22.438 49.868  1.00 142.99 ?  375 VAL   B O   1 
ATOM   5743 C CB  . VAL   B 2 79  ? 31.415  -22.114 47.797  1.00 145.80 ?  375 VAL   B CB  1 
ATOM   5744 C CG1 . VAL   B 2 79  ? 31.843  -23.572 47.608  1.00 135.31 ?  375 VAL   B CG1 1 
ATOM   5745 C CG2 . VAL   B 2 79  ? 32.201  -21.181 46.871  1.00 137.15 ?  375 VAL   B CG2 1 
ATOM   5746 N N   . ILE   B 2 80  ? 28.182  -23.530 48.279  1.00 142.72 ?  376 ILE   B N   1 
ATOM   5747 C CA  . ILE   B 2 80  ? 27.294  -24.231 49.205  1.00 141.73 ?  376 ILE   B CA  1 
ATOM   5748 C C   . ILE   B 2 80  ? 27.936  -25.595 49.430  1.00 142.76 ?  376 ILE   B C   1 
ATOM   5749 O O   . ILE   B 2 80  ? 27.699  -26.544 48.679  1.00 144.10 ?  376 ILE   B O   1 
ATOM   5750 C CB  . ILE   B 2 80  ? 25.882  -24.361 48.638  1.00 142.58 ?  376 ILE   B CB  1 
ATOM   5751 C CG1 . ILE   B 2 80  ? 25.388  -23.011 48.112  1.00 142.87 ?  376 ILE   B CG1 1 
ATOM   5752 C CG2 . ILE   B 2 80  ? 24.937  -24.935 49.691  1.00 138.97 ?  376 ILE   B CG2 1 
ATOM   5753 C CD1 . ILE   B 2 80  ? 24.204  -23.116 47.159  1.00 138.67 ?  376 ILE   B CD1 1 
ATOM   5754 N N   . GLN   B 2 81  ? 28.765  -25.715 50.463  1.00 139.29 ?  377 GLN   B N   1 
ATOM   5755 C CA  . GLN   B 2 81  ? 29.591  -26.911 50.585  1.00 139.27 ?  377 GLN   B CA  1 
ATOM   5756 C C   . GLN   B 2 81  ? 29.434  -27.554 51.955  1.00 138.01 ?  377 GLN   B C   1 
ATOM   5757 O O   . GLN   B 2 81  ? 29.730  -26.927 52.980  1.00 132.21 ?  377 GLN   B O   1 
ATOM   5758 C CB  . GLN   B 2 81  ? 31.056  -26.590 50.288  1.00 137.83 ?  377 GLN   B CB  1 
ATOM   5759 C CG  . GLN   B 2 81  ? 31.923  -27.827 50.160  1.00 132.64 ?  377 GLN   B CG  1 
ATOM   5760 C CD  . GLN   B 2 81  ? 33.386  -27.477 50.029  1.00 129.99 ?  377 GLN   B CD  1 
ATOM   5761 O OE1 . GLN   B 2 81  ? 33.904  -26.649 50.775  1.00 121.28 ?  377 GLN   B OE1 1 
ATOM   5762 N NE2 . GLN   B 2 81  ? 34.068  -28.118 49.081  1.00 125.29 ?  377 GLN   B NE2 1 
ATOM   5763 N N   . LYS   B 2 82  ? 28.980  -28.813 51.953  1.00 136.55 ?  378 LYS   B N   1 
ATOM   5764 C CA  . LYS   B 2 82  ? 28.789  -29.589 53.174  1.00 133.49 ?  378 LYS   B CA  1 
ATOM   5765 C C   . LYS   B 2 82  ? 30.139  -29.918 53.807  1.00 130.46 ?  378 LYS   B C   1 
ATOM   5766 O O   . LYS   B 2 82  ? 31.064  -30.372 53.124  1.00 129.85 ?  378 LYS   B O   1 
ATOM   5767 C CB  . LYS   B 2 82  ? 28.018  -30.880 52.866  1.00 133.00 ?  378 LYS   B CB  1 
ATOM   5768 C CG  . LYS   B 2 82  ? 26.513  -30.712 52.599  1.00 128.67 ?  378 LYS   B CG  1 
ATOM   5769 C CD  . LYS   B 2 82  ? 25.774  -32.054 52.720  1.00 130.79 ?  378 LYS   B CD  1 
ATOM   5770 C CE  . LYS   B 2 82  ? 24.248  -31.903 52.611  1.00 132.18 ?  378 LYS   B CE  1 
ATOM   5771 N NZ  . LYS   B 2 82  ? 23.518  -33.219 52.705  1.00 119.14 ?  378 LYS   B NZ  1 
ATOM   5772 N N   . CYS   B 2 83  ? 30.236  -29.722 55.123  1.00 126.14 ?  379 CYS   B N   1 
ATOM   5773 C CA  . CYS   B 2 83  ? 31.508  -29.724 55.849  1.00 123.00 ?  379 CYS   B CA  1 
ATOM   5774 C C   . CYS   B 2 83  ? 31.926  -31.143 56.249  1.00 124.88 ?  379 CYS   B C   1 
ATOM   5775 O O   . CYS   B 2 83  ? 31.475  -31.680 57.264  1.00 124.05 ?  379 CYS   B O   1 
ATOM   5776 C CB  . CYS   B 2 83  ? 31.399  -28.816 57.068  1.00 121.64 ?  379 CYS   B CB  1 
ATOM   5777 S SG  . CYS   B 2 83  ? 32.709  -29.041 58.286  1.00 128.38 ?  379 CYS   B SG  1 
ATOM   5778 N N   . ASN   B 2 84  ? 32.831  -31.724 55.457  1.00 128.62 ?  380 ASN   B N   1 
ATOM   5779 C CA  . ASN   B 2 84  ? 33.502  -33.005 55.677  1.00 121.60 ?  380 ASN   B CA  1 
ATOM   5780 C C   . ASN   B 2 84  ? 34.350  -32.993 56.964  1.00 121.57 ?  380 ASN   B C   1 
ATOM   5781 O O   . ASN   B 2 84  ? 34.628  -31.948 57.567  1.00 121.51 ?  380 ASN   B O   1 
ATOM   5782 C CB  . ASN   B 2 84  ? 34.341  -33.335 54.432  1.00 118.84 ?  380 ASN   B CB  1 
ATOM   5783 C CG  . ASN   B 2 84  ? 35.000  -34.717 54.468  1.00 128.66 ?  380 ASN   B CG  1 
ATOM   5784 O OD1 . ASN   B 2 84  ? 34.997  -35.428 55.484  1.00 129.17 ?  380 ASN   B OD1 1 
ATOM   5785 N ND2 . ASN   B 2 84  ? 35.481  -35.146 53.294  1.00 132.98 ?  380 ASN   B ND2 1 
ATOM   5786 N N   . ALA   B 2 85  ? 34.750  -34.201 57.384  1.00 121.25 ?  381 ALA   B N   1 
ATOM   5787 C CA  . ALA   B 2 85  ? 35.517  -34.458 58.599  1.00 118.54 ?  381 ALA   B CA  1 
ATOM   5788 C C   . ALA   B 2 85  ? 36.920  -34.995 58.350  1.00 117.59 ?  381 ALA   B C   1 
ATOM   5789 O O   . ALA   B 2 85  ? 37.809  -34.747 59.169  1.00 110.66 ?  381 ALA   B O   1 
ATOM   5790 C CB  . ALA   B 2 85  ? 34.775  -35.471 59.484  1.00 115.34 ?  381 ALA   B CB  1 
ATOM   5791 N N   . ARG   B 2 86  ? 37.130  -35.751 57.268  1.00 121.31 ?  382 ARG   B N   1 
ATOM   5792 C CA  . ARG   B 2 86  ? 38.445  -36.274 56.910  1.00 119.44 ?  382 ARG   B CA  1 
ATOM   5793 C C   . ARG   B 2 86  ? 39.267  -35.247 56.132  1.00 120.80 ?  382 ARG   B C   1 
ATOM   5794 O O   . ARG   B 2 86  ? 38.746  -34.481 55.309  1.00 119.91 ?  382 ARG   B O   1 
ATOM   5795 C CB  . ARG   B 2 86  ? 38.321  -37.554 56.077  1.00 120.01 ?  382 ARG   B CB  1 
ATOM   5796 C CG  . ARG   B 2 86  ? 37.964  -38.801 56.878  1.00 131.71 ?  382 ARG   B CG  1 
ATOM   5797 C CD  . ARG   B 2 86  ? 37.380  -39.902 55.996  1.00 136.52 ?  382 ARG   B CD  1 
ATOM   5798 N NE  . ARG   B 2 86  ? 37.009  -41.079 56.780  1.00 134.58 ?  382 ARG   B NE  1 
ATOM   5799 C CZ  . ARG   B 2 86  ? 37.509  -42.299 56.594  1.00 141.79 ?  382 ARG   B CZ  1 
ATOM   5800 N NH1 . ARG   B 2 86  ? 38.401  -42.521 55.634  1.00 139.71 ?  382 ARG   B NH1 1 
ATOM   5801 N NH2 . ARG   B 2 86  ? 37.107  -43.305 57.364  1.00 141.90 ?  382 ARG   B NH2 1 
ATOM   5802 N N   . TRP   B 2 87  ? 40.580  -35.265 56.381  1.00 114.67 ?  383 TRP   B N   1 
ATOM   5803 C CA  . TRP   B 2 87  ? 41.543  -34.395 55.710  1.00 106.82 ?  383 TRP   B CA  1 
ATOM   5804 C C   . TRP   B 2 87  ? 42.164  -35.126 54.523  1.00 109.12 ?  383 TRP   B C   1 
ATOM   5805 O O   . TRP   B 2 87  ? 42.992  -36.025 54.711  1.00 107.93 ?  383 TRP   B O   1 
ATOM   5806 C CB  . TRP   B 2 87  ? 42.636  -33.957 56.681  1.00 103.84 ?  383 TRP   B CB  1 
ATOM   5807 C CG  . TRP   B 2 87  ? 42.114  -33.082 57.745  1.00 112.04 ?  383 TRP   B CG  1 
ATOM   5808 C CD1 . TRP   B 2 87  ? 41.437  -33.472 58.853  1.00 115.27 ?  383 TRP   B CD1 1 
ATOM   5809 C CD2 . TRP   B 2 87  ? 42.184  -31.648 57.796  1.00 111.61 ?  383 TRP   B CD2 1 
ATOM   5810 N NE1 . TRP   B 2 87  ? 41.091  -32.373 59.604  1.00 116.87 ?  383 TRP   B NE1 1 
ATOM   5811 C CE2 . TRP   B 2 87  ? 41.535  -31.242 58.973  1.00 109.62 ?  383 TRP   B CE2 1 
ATOM   5812 C CE3 . TRP   B 2 87  ? 42.730  -30.670 56.957  1.00 108.86 ?  383 TRP   B CE3 1 
ATOM   5813 C CZ2 . TRP   B 2 87  ? 41.420  -29.905 59.339  1.00 112.67 ?  383 TRP   B CZ2 1 
ATOM   5814 C CZ3 . TRP   B 2 87  ? 42.616  -29.335 57.326  1.00 106.72 ?  383 TRP   B CZ3 1 
ATOM   5815 C CH2 . TRP   B 2 87  ? 41.965  -28.968 58.505  1.00 110.23 ?  383 TRP   B CH2 1 
ATOM   5816 N N   . THR   B 2 88  ? 41.799  -34.726 53.304  1.00 104.64 ?  384 THR   B N   1 
ATOM   5817 C CA  . THR   B 2 88  ? 42.515  -35.258 52.159  1.00 96.81  ?  384 THR   B CA  1 
ATOM   5818 C C   . THR   B 2 88  ? 43.949  -34.737 52.190  1.00 97.09  ?  384 THR   B C   1 
ATOM   5819 O O   . THR   B 2 88  ? 44.258  -33.729 52.837  1.00 96.49  ?  384 THR   B O   1 
ATOM   5820 C CB  . THR   B 2 88  ? 41.865  -34.835 50.850  1.00 97.73  ?  384 THR   B CB  1 
ATOM   5821 O OG1 . THR   B 2 88  ? 42.073  -33.440 50.646  1.00 103.06 ?  384 THR   B OG1 1 
ATOM   5822 C CG2 . THR   B 2 88  ? 40.372  -35.060 50.947  1.00 106.66 ?  384 THR   B CG2 1 
ATOM   5823 N N   . THR   B 2 89  ? 44.836  -35.418 51.466  1.00 96.43  ?  385 THR   B N   1 
ATOM   5824 C CA  . THR   B 2 89  ? 46.195  -34.899 51.349  1.00 92.42  ?  385 THR   B CA  1 
ATOM   5825 C C   . THR   B 2 89  ? 46.176  -33.484 50.765  1.00 89.08  ?  385 THR   B C   1 
ATOM   5826 O O   . THR   B 2 89  ? 46.946  -32.610 51.185  1.00 84.52  ?  385 THR   B O   1 
ATOM   5827 C CB  . THR   B 2 89  ? 47.035  -35.812 50.468  1.00 88.18  ?  385 THR   B CB  1 
ATOM   5828 O OG1 . THR   B 2 89  ? 46.955  -37.161 50.962  1.00 89.87  ?  385 THR   B OG1 1 
ATOM   5829 C CG2 . THR   B 2 89  ? 48.497  -35.333 50.520  1.00 72.32  ?  385 THR   B CG2 1 
ATOM   5830 N N   . GLU   B 2 90  ? 45.290  -33.243 49.794  1.00 88.78  ?  386 GLU   B N   1 
ATOM   5831 C CA  . GLU   B 2 90  ? 45.056  -31.898 49.281  1.00 88.13  ?  386 GLU   B CA  1 
ATOM   5832 C C   . GLU   B 2 90  ? 44.747  -30.912 50.398  1.00 90.04  ?  386 GLU   B C   1 
ATOM   5833 O O   . GLU   B 2 90  ? 45.341  -29.829 50.483  1.00 86.22  ?  386 GLU   B O   1 
ATOM   5834 C CB  . GLU   B 2 90  ? 43.896  -31.919 48.287  1.00 95.16  ?  386 GLU   B CB  1 
ATOM   5835 C CG  . GLU   B 2 90  ? 43.303  -30.528 48.026  1.00 102.61 ?  386 GLU   B CG  1 
ATOM   5836 C CD  . GLU   B 2 90  ? 42.132  -30.542 47.045  1.00 118.82 ?  386 GLU   B CD  1 
ATOM   5837 O OE1 . GLU   B 2 90  ? 41.460  -31.600 46.931  1.00 121.33 ?  386 GLU   B OE1 1 
ATOM   5838 O OE2 . GLU   B 2 90  ? 41.878  -29.482 46.412  1.00 118.25 ?  386 GLU   B OE2 1 
ATOM   5839 N N   . GLU   B 2 91  ? 43.773  -31.253 51.240  1.00 94.10  ?  387 GLU   B N   1 
ATOM   5840 C CA  . GLU   B 2 91  ? 43.247  -30.257 52.164  1.00 92.17  ?  387 GLU   B CA  1 
ATOM   5841 C C   . GLU   B 2 91  ? 44.288  -29.934 53.229  1.00 84.78  ?  387 GLU   B C   1 
ATOM   5842 O O   . GLU   B 2 91  ? 44.409  -28.775 53.650  1.00 84.91  ?  387 GLU   B O   1 
ATOM   5843 C CB  . GLU   B 2 91  ? 41.917  -30.768 52.737  1.00 98.47  ?  387 GLU   B CB  1 
ATOM   5844 C CG  . GLU   B 2 91  ? 40.844  -30.918 51.621  1.00 103.51 ?  387 GLU   B CG  1 
ATOM   5845 C CD  . GLU   B 2 91  ? 39.577  -31.623 52.063  1.00 110.03 ?  387 GLU   B CD  1 
ATOM   5846 O OE1 . GLU   B 2 91  ? 39.483  -32.046 53.240  1.00 107.73 ?  387 GLU   B OE1 1 
ATOM   5847 O OE2 . GLU   B 2 91  ? 38.688  -31.796 51.186  1.00 110.90 ?  387 GLU   B OE2 1 
ATOM   5848 N N   . GLN   B 2 92  ? 45.116  -30.919 53.603  1.00 82.11  ?  388 GLN   B N   1 
ATOM   5849 C CA  . GLN   B 2 92  ? 46.269  -30.616 54.448  1.00 84.66  ?  388 GLN   B CA  1 
ATOM   5850 C C   . GLN   B 2 92  ? 47.145  -29.542 53.809  1.00 82.11  ?  388 GLN   B C   1 
ATOM   5851 O O   . GLN   B 2 92  ? 47.595  -28.606 54.482  1.00 79.08  ?  388 GLN   B O   1 
ATOM   5852 C CB  . GLN   B 2 92  ? 47.075  -31.892 54.713  1.00 89.65  ?  388 GLN   B CB  1 
ATOM   5853 C CG  . GLN   B 2 92  ? 46.322  -32.925 55.570  1.00 90.26  ?  388 GLN   B CG  1 
ATOM   5854 C CD  . GLN   B 2 92  ? 46.966  -34.295 55.589  1.00 88.29  ?  388 GLN   B CD  1 
ATOM   5855 O OE1 . GLN   B 2 92  ? 48.183  -34.423 55.636  1.00 82.26  ?  388 GLN   B OE1 1 
ATOM   5856 N NE2 . GLN   B 2 92  ? 46.142  -35.330 55.548  1.00 101.22 ?  388 GLN   B NE2 1 
ATOM   5857 N N   . LEU   B 2 93  ? 47.360  -29.636 52.494  1.00 88.53  ?  389 LEU   B N   1 
ATOM   5858 C CA  . LEU   B 2 93  ? 48.319  -28.752 51.839  1.00 77.23  ?  389 LEU   B CA  1 
ATOM   5859 C C   . LEU   B 2 93  ? 47.763  -27.344 51.703  1.00 78.06  ?  389 LEU   B C   1 
ATOM   5860 O O   . LEU   B 2 93  ? 48.478  -26.371 51.964  1.00 79.67  ?  389 LEU   B O   1 
ATOM   5861 C CB  . LEU   B 2 93  ? 48.715  -29.325 50.480  1.00 73.20  ?  389 LEU   B CB  1 
ATOM   5862 C CG  . LEU   B 2 93  ? 49.848  -30.355 50.589  1.00 71.37  ?  389 LEU   B CG  1 
ATOM   5863 C CD1 . LEU   B 2 93  ? 49.945  -31.147 49.312  1.00 66.11  ?  389 LEU   B CD1 1 
ATOM   5864 C CD2 . LEU   B 2 93  ? 51.204  -29.770 50.982  1.00 65.49  ?  389 LEU   B CD2 1 
ATOM   5865 N N   . LEU   B 2 94  ? 46.489  -27.208 51.315  1.00 79.11  ?  390 LEU   B N   1 
ATOM   5866 C CA  . LEU   B 2 94  ? 45.853  -25.898 51.397  1.00 80.89  ?  390 LEU   B CA  1 
ATOM   5867 C C   . LEU   B 2 94  ? 46.015  -25.306 52.792  1.00 83.35  ?  390 LEU   B C   1 
ATOM   5868 O O   . LEU   B 2 94  ? 46.319  -24.117 52.942  1.00 81.86  ?  390 LEU   B O   1 
ATOM   5869 C CB  . LEU   B 2 94  ? 44.371  -25.991 51.034  1.00 76.80  ?  390 LEU   B CB  1 
ATOM   5870 C CG  . LEU   B 2 94  ? 44.047  -26.409 49.609  1.00 81.27  ?  390 LEU   B CG  1 
ATOM   5871 C CD1 . LEU   B 2 94  ? 42.688  -27.059 49.539  1.00 88.10  ?  390 LEU   B CD1 1 
ATOM   5872 C CD2 . LEU   B 2 94  ? 44.119  -25.217 48.686  1.00 77.83  ?  390 LEU   B CD2 1 
ATOM   5873 N N   . ALA   B 2 95  ? 45.843  -26.134 53.824  1.00 84.50  ?  391 ALA   B N   1 
ATOM   5874 C CA  . ALA   B 2 95  ? 45.937  -25.688 55.206  1.00 81.79  ?  391 ALA   B CA  1 
ATOM   5875 C C   . ALA   B 2 95  ? 47.260  -24.982 55.479  1.00 82.79  ?  391 ALA   B C   1 
ATOM   5876 O O   . ALA   B 2 95  ? 47.264  -23.769 55.713  1.00 86.68  ?  391 ALA   B O   1 
ATOM   5877 C CB  . ALA   B 2 95  ? 45.747  -26.868 56.156  1.00 85.84  ?  391 ALA   B CB  1 
ATOM   5878 N N   . VAL   B 2 96  ? 48.377  -25.718 55.446  1.00 77.15  ?  392 VAL   B N   1 
ATOM   5879 C CA  . VAL   B 2 96  ? 49.705  -25.135 55.642  1.00 78.80  ?  392 VAL   B CA  1 
ATOM   5880 C C   . VAL   B 2 96  ? 49.857  -23.814 54.898  1.00 88.23  ?  392 VAL   B C   1 
ATOM   5881 O O   . VAL   B 2 96  ? 50.289  -22.804 55.470  1.00 93.12  ?  392 VAL   B O   1 
ATOM   5882 C CB  . VAL   B 2 96  ? 50.811  -26.097 55.193  1.00 82.01  ?  392 VAL   B CB  1 
ATOM   5883 C CG1 . VAL   B 2 96  ? 52.108  -25.313 54.903  1.00 75.85  ?  392 VAL   B CG1 1 
ATOM   5884 C CG2 . VAL   B 2 96  ? 51.029  -27.159 56.246  1.00 88.80  ?  392 VAL   B CG2 1 
ATOM   5885 N N   . GLN   B 2 97  ? 49.507  -23.807 53.615  1.00 83.60  ?  393 GLN   B N   1 
ATOM   5886 C CA  . GLN   B 2 97  ? 49.654  -22.582 52.841  1.00 85.83  ?  393 GLN   B CA  1 
ATOM   5887 C C   . GLN   B 2 97  ? 48.811  -21.458 53.423  1.00 89.31  ?  393 GLN   B C   1 
ATOM   5888 O O   . GLN   B 2 97  ? 49.270  -20.311 53.516  1.00 89.05  ?  393 GLN   B O   1 
ATOM   5889 C CB  . GLN   B 2 97  ? 49.269  -22.845 51.400  1.00 79.16  ?  393 GLN   B CB  1 
ATOM   5890 C CG  . GLN   B 2 97  ? 50.441  -23.183 50.552  1.00 72.36  ?  393 GLN   B CG  1 
ATOM   5891 C CD  . GLN   B 2 97  ? 49.990  -23.542 49.183  1.00 77.25  ?  393 GLN   B CD  1 
ATOM   5892 O OE1 . GLN   B 2 97  ? 49.395  -24.603 48.964  1.00 73.14  ?  393 GLN   B OE1 1 
ATOM   5893 N NE2 . GLN   B 2 97  ? 50.199  -22.626 48.245  1.00 82.83  ?  393 GLN   B NE2 1 
ATOM   5894 N N   . ALA   B 2 98  ? 47.574  -21.778 53.821  1.00 88.02  ?  394 ALA   B N   1 
ATOM   5895 C CA  . ALA   B 2 98  ? 46.721  -20.801 54.483  1.00 87.51  ?  394 ALA   B CA  1 
ATOM   5896 C C   . ALA   B 2 98  ? 47.374  -20.261 55.746  1.00 91.13  ?  394 ALA   B C   1 
ATOM   5897 O O   . ALA   B 2 98  ? 47.196  -19.085 56.088  1.00 91.90  ?  394 ALA   B O   1 
ATOM   5898 C CB  . ALA   B 2 98  ? 45.363  -21.424 54.808  1.00 85.05  ?  394 ALA   B CB  1 
ATOM   5899 N N   . ILE   B 2 99  ? 48.151  -21.086 56.442  1.00 85.68  ?  395 ILE   B N   1 
ATOM   5900 C CA  . ILE   B 2 99  ? 48.749  -20.617 57.682  1.00 86.17  ?  395 ILE   B CA  1 
ATOM   5901 C C   . ILE   B 2 99  ? 49.858  -19.620 57.380  1.00 90.66  ?  395 ILE   B C   1 
ATOM   5902 O O   . ILE   B 2 99  ? 49.902  -18.543 57.972  1.00 101.01 ?  395 ILE   B O   1 
ATOM   5903 C CB  . ILE   B 2 99  ? 49.254  -21.799 58.522  1.00 90.63  ?  395 ILE   B CB  1 
ATOM   5904 C CG1 . ILE   B 2 99  ? 48.067  -22.529 59.177  1.00 87.45  ?  395 ILE   B CG1 1 
ATOM   5905 C CG2 . ILE   B 2 99  ? 50.177  -21.323 59.607  1.00 95.78  ?  395 ILE   B CG2 1 
ATOM   5906 C CD1 . ILE   B 2 99  ? 48.493  -23.729 59.973  1.00 88.66  ?  395 ILE   B CD1 1 
ATOM   5907 N N   . ARG   B 2 100 ? 50.748  -19.931 56.422  1.00 90.49  ?  396 ARG   B N   1 
ATOM   5908 C CA  . ARG   B 2 100 ? 51.782  -18.955 56.060  1.00 94.33  ?  396 ARG   B CA  1 
ATOM   5909 C C   . ARG   B 2 100 ? 51.180  -17.700 55.466  1.00 91.43  ?  396 ARG   B C   1 
ATOM   5910 O O   . ARG   B 2 100 ? 51.861  -16.678 55.438  1.00 90.22  ?  396 ARG   B O   1 
ATOM   5911 C CB  . ARG   B 2 100 ? 52.845  -19.565 55.113  1.00 88.01  ?  396 ARG   B CB  1 
ATOM   5912 C CG  . ARG   B 2 100 ? 53.968  -18.650 54.469  1.00 87.93  ?  396 ARG   B CG  1 
ATOM   5913 C CD  . ARG   B 2 100 ? 54.815  -17.917 55.514  1.00 96.19  ?  396 ARG   B CD  1 
ATOM   5914 N NE  . ARG   B 2 100 ? 56.037  -17.306 54.975  1.00 98.26  ?  396 ARG   B NE  1 
ATOM   5915 C CZ  . ARG   B 2 100 ? 56.083  -16.176 54.291  1.00 103.12 ?  396 ARG   B CZ  1 
ATOM   5916 N NH1 . ARG   B 2 100 ? 54.934  -15.602 53.984  1.00 109.66 ?  396 ARG   B NH1 1 
ATOM   5917 N NH2 . ARG   B 2 100 ? 57.238  -15.710 53.800  1.00 105.54 ?  396 ARG   B NH2 1 
ATOM   5918 N N   . LYS   B 2 101 ? 49.911  -17.715 55.054  1.00 88.57  ?  397 LYS   B N   1 
ATOM   5919 C CA  . LYS   B 2 101 ? 49.347  -16.478 54.548  1.00 93.85  ?  397 LYS   B CA  1 
ATOM   5920 C C   . LYS   B 2 101 ? 48.448  -15.786 55.550  1.00 97.35  ?  397 LYS   B C   1 
ATOM   5921 O O   . LYS   B 2 101 ? 48.298  -14.563 55.481  1.00 92.28  ?  397 LYS   B O   1 
ATOM   5922 C CB  . LYS   B 2 101 ? 48.576  -16.709 53.240  1.00 93.38  ?  397 LYS   B CB  1 
ATOM   5923 C CG  . LYS   B 2 101 ? 48.028  -15.395 52.653  1.00 90.75  ?  397 LYS   B CG  1 
ATOM   5924 C CD  . LYS   B 2 101 ? 47.351  -15.517 51.305  1.00 85.72  ?  397 LYS   B CD  1 
ATOM   5925 C CE  . LYS   B 2 101 ? 47.342  -14.165 50.584  1.00 91.21  ?  397 LYS   B CE  1 
ATOM   5926 N NZ  . LYS   B 2 101 ? 48.698  -13.512 50.574  1.00 99.71  ?  397 LYS   B NZ  1 
ATOM   5927 N N   . TYR   B 2 102 ? 47.881  -16.524 56.494  1.00 100.22 ?  398 TYR   B N   1 
ATOM   5928 C CA  . TYR   B 2 102 ? 46.905  -15.947 57.398  1.00 102.49 ?  398 TYR   B CA  1 
ATOM   5929 C C   . TYR   B 2 102 ? 47.270  -16.012 58.879  1.00 105.38 ?  398 TYR   B C   1 
ATOM   5930 O O   . TYR   B 2 102 ? 46.697  -15.244 59.659  1.00 110.05 ?  398 TYR   B O   1 
ATOM   5931 C CB  . TYR   B 2 102 ? 45.538  -16.611 57.175  1.00 98.81  ?  398 TYR   B CB  1 
ATOM   5932 C CG  . TYR   B 2 102 ? 44.938  -16.248 55.837  1.00 94.82  ?  398 TYR   B CG  1 
ATOM   5933 C CD1 . TYR   B 2 102 ? 44.583  -14.939 55.552  1.00 88.37  ?  398 TYR   B CD1 1 
ATOM   5934 C CD2 . TYR   B 2 102 ? 44.743  -17.212 54.853  1.00 94.86  ?  398 TYR   B CD2 1 
ATOM   5935 C CE1 . TYR   B 2 102 ? 44.027  -14.596 54.337  1.00 91.97  ?  398 TYR   B CE1 1 
ATOM   5936 C CE2 . TYR   B 2 102 ? 44.194  -16.879 53.631  1.00 91.41  ?  398 TYR   B CE2 1 
ATOM   5937 C CZ  . TYR   B 2 102 ? 43.838  -15.566 53.380  1.00 96.56  ?  398 TYR   B CZ  1 
ATOM   5938 O OH  . TYR   B 2 102 ? 43.295  -15.214 52.169  1.00 97.89  ?  398 TYR   B OH  1 
ATOM   5939 N N   . GLY   B 2 103 ? 48.239  -16.833 59.242  1.00 103.06 ?  399 GLY   B N   1 
ATOM   5940 C CA  . GLY   B 2 103 ? 48.632  -16.893 60.656  1.00 106.76 ?  399 GLY   B CA  1 
ATOM   5941 C C   . GLY   B 2 103 ? 47.617  -17.624 61.510  1.00 111.65 ?  399 GLY   B C   1 
ATOM   5942 O O   . GLY   B 2 103 ? 47.557  -18.842 61.420  1.00 106.21 ?  399 GLY   B O   1 
ATOM   5943 N N   . ARG   B 2 104 ? 46.872  -16.905 62.349  1.00 114.65 ?  400 ARG   B N   1 
ATOM   5944 C CA  . ARG   B 2 104 ? 45.915  -17.572 63.263  1.00 112.46 ?  400 ARG   B CA  1 
ATOM   5945 C C   . ARG   B 2 104 ? 44.468  -17.251 62.908  1.00 109.58 ?  400 ARG   B C   1 
ATOM   5946 O O   . ARG   B 2 104 ? 43.595  -17.652 63.665  1.00 108.04 ?  400 ARG   B O   1 
ATOM   5947 C CB  . ARG   B 2 104 ? 46.193  -17.145 64.702  1.00 109.94 ?  400 ARG   B CB  1 
ATOM   5948 C CG  . ARG   B 2 104 ? 47.657  -17.229 65.103  1.00 109.06 ?  400 ARG   B CG  1 
ATOM   5949 C CD  . ARG   B 2 104 ? 47.802  -17.735 66.520  1.00 107.67 ?  400 ARG   B CD  1 
ATOM   5950 N NE  . ARG   B 2 104 ? 49.174  -18.070 66.838  1.00 103.30 ?  400 ARG   B NE  1 
ATOM   5951 C CZ  . ARG   B 2 104 ? 50.200  -17.272 66.627  1.00 99.54  ?  400 ARG   B CZ  1 
ATOM   5952 N NH1 . ARG   B 2 104 ? 50.006  -16.084 66.094  1.00 87.74  ?  400 ARG   B NH1 1 
ATOM   5953 N NH2 . ARG   B 2 104 ? 51.414  -17.664 66.950  1.00 96.29  ?  400 ARG   B NH2 1 
ATOM   5954 N N   . ASP   B 2 105 ? 44.190  -16.647 61.765  1.00 104.67 ?  401 ASP   B N   1 
ATOM   5955 C CA  . ASP   B 2 105 ? 42.765  -16.316 61.532  1.00 102.51 ?  401 ASP   B CA  1 
ATOM   5956 C C   . ASP   B 2 105 ? 42.052  -17.579 61.060  1.00 103.11 ?  401 ASP   B C   1 
ATOM   5957 O O   . ASP   B 2 105 ? 41.747  -17.688 59.885  1.00 105.39 ?  401 ASP   B O   1 
ATOM   5958 C CB  . ASP   B 2 105 ? 42.634  -15.125 60.586  1.00 96.51  ?  401 ASP   B CB  1 
ATOM   5959 C CG  . ASP   B 2 105 ? 41.230  -14.861 60.079  1.00 105.92 ?  401 ASP   B CG  1 
ATOM   5960 O OD1 . ASP   B 2 105 ? 41.062  -13.870 59.369  1.00 97.90  ?  401 ASP   B OD1 1 
ATOM   5961 O OD2 . ASP   B 2 105 ? 40.322  -15.640 60.392  1.00 108.97 ?  401 ASP   B OD2 1 
ATOM   5962 N N   . PHE   B 2 106 ? 41.576  -18.384 61.995  1.00 93.86  ?  402 PHE   B N   1 
ATOM   5963 C CA  . PHE   B 2 106 ? 40.933  -19.666 61.642  1.00 101.27 ?  402 PHE   B CA  1 
ATOM   5964 C C   . PHE   B 2 106 ? 39.710  -19.456 60.757  1.00 101.68 ?  402 PHE   B C   1 
ATOM   5965 O O   . PHE   B 2 106 ? 39.444  -20.305 59.931  1.00 105.18 ?  402 PHE   B O   1 
ATOM   5966 C CB  . PHE   B 2 106 ? 40.612  -20.450 62.907  1.00 107.48 ?  402 PHE   B CB  1 
ATOM   5967 C CG  . PHE   B 2 106 ? 41.757  -20.470 63.878  1.00 116.33 ?  402 PHE   B CG  1 
ATOM   5968 C CD1 . PHE   B 2 106 ? 41.571  -20.151 65.206  1.00 118.93 ?  402 PHE   B CD1 1 
ATOM   5969 C CD2 . PHE   B 2 106 ? 43.026  -20.805 63.457  1.00 119.69 ?  402 PHE   B CD2 1 
ATOM   5970 C CE1 . PHE   B 2 106 ? 42.635  -20.166 66.090  1.00 120.55 ?  402 PHE   B CE1 1 
ATOM   5971 C CE2 . PHE   B 2 106 ? 44.091  -20.810 64.341  1.00 117.49 ?  402 PHE   B CE2 1 
ATOM   5972 C CZ  . PHE   B 2 106 ? 43.893  -20.492 65.658  1.00 117.40 ?  402 PHE   B CZ  1 
ATOM   5973 N N   . GLN   B 2 107 ? 38.950  -18.390 60.949  1.00 98.29  ?  403 GLN   B N   1 
ATOM   5974 C CA  . GLN   B 2 107 ? 37.771  -18.209 60.082  1.00 101.20 ?  403 GLN   B CA  1 
ATOM   5975 C C   . GLN   B 2 107 ? 38.232  -18.099 58.631  1.00 106.54 ?  403 GLN   B C   1 
ATOM   5976 O O   . GLN   B 2 107 ? 37.628  -18.744 57.777  1.00 106.27 ?  403 GLN   B O   1 
ATOM   5977 C CB  . GLN   B 2 107 ? 37.067  -16.921 60.477  1.00 97.02  ?  403 GLN   B CB  1 
ATOM   5978 C CG  . GLN   B 2 107 ? 35.718  -16.784 59.813  1.00 97.92  ?  403 GLN   B CG  1 
ATOM   5979 C CD  . GLN   B 2 107 ? 35.195  -18.158 59.514  1.00 109.57 ?  403 GLN   B CD  1 
ATOM   5980 O OE1 . GLN   B 2 107 ? 34.463  -18.742 60.296  1.00 109.75 ?  403 GLN   B OE1 1 
ATOM   5981 N NE2 . GLN   B 2 107 ? 35.590  -18.691 58.378  1.00 116.85 ?  403 GLN   B NE2 1 
ATOM   5982 N N   . ALA   B 2 108 ? 39.281  -17.332 58.362  1.00 106.30 ?  404 ALA   B N   1 
ATOM   5983 C CA  . ALA   B 2 108 ? 39.728  -17.223 56.963  1.00 102.54 ?  404 ALA   B CA  1 
ATOM   5984 C C   . ALA   B 2 108 ? 40.202  -18.589 56.492  1.00 101.91 ?  404 ALA   B C   1 
ATOM   5985 O O   . ALA   B 2 108 ? 39.763  -19.031 55.440  1.00 102.09 ?  404 ALA   B O   1 
ATOM   5986 C CB  . ALA   B 2 108 ? 40.834  -16.225 56.872  1.00 98.66  ?  404 ALA   B CB  1 
ATOM   5987 N N   . ILE   B 2 109 ? 41.025  -19.243 57.297  1.00 93.83  ?  405 ILE   B N   1 
ATOM   5988 C CA  . ILE   B 2 109 ? 41.568  -20.574 56.921  1.00 90.72  ?  405 ILE   B CA  1 
ATOM   5989 C C   . ILE   B 2 109 ? 40.433  -21.523 56.573  1.00 93.65  ?  405 ILE   B C   1 
ATOM   5990 O O   . ILE   B 2 109 ? 40.517  -22.186 55.567  1.00 95.79  ?  405 ILE   B O   1 
ATOM   5991 C CB  . ILE   B 2 109 ? 42.411  -21.123 58.063  1.00 84.25  ?  405 ILE   B CB  1 
ATOM   5992 C CG1 . ILE   B 2 109 ? 43.592  -20.205 58.333  1.00 86.31  ?  405 ILE   B CG1 1 
ATOM   5993 C CG2 . ILE   B 2 109 ? 42.871  -22.514 57.729  1.00 84.50  ?  405 ILE   B CG2 1 
ATOM   5994 C CD1 . ILE   B 2 109 ? 44.790  -20.943 58.813  1.00 88.67  ?  405 ILE   B CD1 1 
ATOM   5995 N N   . SER   B 2 110 ? 39.387  -21.547 57.372  1.00 99.46  ?  406 SER   B N   1 
ATOM   5996 C CA  . SER   B 2 110 ? 38.282  -22.464 57.029  1.00 103.53 ?  406 SER   B CA  1 
ATOM   5997 C C   . SER   B 2 110 ? 37.691  -22.026 55.697  1.00 101.13 ?  406 SER   B C   1 
ATOM   5998 O O   . SER   B 2 110 ? 37.354  -22.869 54.898  1.00 101.85 ?  406 SER   B O   1 
ATOM   5999 C CB  . SER   B 2 110 ? 37.239  -22.461 58.092  1.00 106.06 ?  406 SER   B CB  1 
ATOM   6000 O OG  . SER   B 2 110 ? 36.163  -23.298 57.719  1.00 108.36 ?  406 SER   B OG  1 
ATOM   6001 N N   . ASP   B 2 111 ? 37.599  -20.733 55.458  1.00 99.96  ?  407 ASP   B N   1 
ATOM   6002 C CA  . ASP   B 2 111 ? 36.986  -20.334 54.198  1.00 105.17 ?  407 ASP   B CA  1 
ATOM   6003 C C   . ASP   B 2 111 ? 37.806  -20.800 53.007  1.00 102.97 ?  407 ASP   B C   1 
ATOM   6004 O O   . ASP   B 2 111 ? 37.246  -21.094 51.945  1.00 106.42 ?  407 ASP   B O   1 
ATOM   6005 C CB  . ASP   B 2 111 ? 36.819  -18.818 54.158  1.00 109.60 ?  407 ASP   B CB  1 
ATOM   6006 C CG  . ASP   B 2 111 ? 35.803  -18.319 55.161  1.00 110.35 ?  407 ASP   B CG  1 
ATOM   6007 O OD1 . ASP   B 2 111 ? 34.828  -19.056 55.438  1.00 109.84 ?  407 ASP   B OD1 1 
ATOM   6008 O OD2 . ASP   B 2 111 ? 36.002  -17.202 55.696  1.00 108.81 ?  407 ASP   B OD2 1 
ATOM   6009 N N   . VAL   B 2 112 ? 39.127  -20.857 53.164  1.00 101.03 ?  408 VAL   B N   1 
ATOM   6010 C CA  . VAL   B 2 112 ? 39.999  -21.294 52.082  1.00 93.87  ?  408 VAL   B CA  1 
ATOM   6011 C C   . VAL   B 2 112 ? 39.779  -22.773 51.795  1.00 95.36  ?  408 VAL   B C   1 
ATOM   6012 O O   . VAL   B 2 112 ? 39.445  -23.165 50.670  1.00 98.47  ?  408 VAL   B O   1 
ATOM   6013 C CB  . VAL   B 2 112 ? 41.464  -20.998 52.437  1.00 93.99  ?  408 VAL   B CB  1 
ATOM   6014 C CG1 . VAL   B 2 112 ? 42.403  -21.820 51.580  1.00 95.47  ?  408 VAL   B CG1 1 
ATOM   6015 C CG2 . VAL   B 2 112 ? 41.743  -19.529 52.272  1.00 91.41  ?  408 VAL   B CG2 1 
ATOM   6016 N N   . ILE   B 2 113 ? 39.943  -23.613 52.818  1.00 92.23  ?  409 ILE   B N   1 
ATOM   6017 C CA  . ILE   B 2 113 ? 39.756  -25.047 52.632  1.00 89.95  ?  409 ILE   B CA  1 
ATOM   6018 C C   . ILE   B 2 113 ? 38.330  -25.349 52.195  1.00 98.96  ?  409 ILE   B C   1 
ATOM   6019 O O   . ILE   B 2 113 ? 38.096  -26.195 51.324  1.00 105.90 ?  409 ILE   B O   1 
ATOM   6020 C CB  . ILE   B 2 113 ? 40.133  -25.794 53.914  1.00 82.35  ?  409 ILE   B CB  1 
ATOM   6021 C CG1 . ILE   B 2 113 ? 41.478  -25.275 54.408  1.00 81.09  ?  409 ILE   B CG1 1 
ATOM   6022 C CG2 . ILE   B 2 113 ? 40.182  -27.276 53.645  1.00 92.02  ?  409 ILE   B CG2 1 
ATOM   6023 C CD1 . ILE   B 2 113 ? 42.068  -26.079 55.521  1.00 91.46  ?  409 ILE   B CD1 1 
ATOM   6024 N N   . GLY   B 2 114 ? 37.363  -24.649 52.769  1.00 102.96 ?  410 GLY   B N   1 
ATOM   6025 C CA  . GLY   B 2 114 ? 35.991  -24.695 52.303  1.00 107.62 ?  410 GLY   B CA  1 
ATOM   6026 C C   . GLY   B 2 114 ? 35.099  -25.663 53.036  1.00 112.69 ?  410 GLY   B C   1 
ATOM   6027 O O   . GLY   B 2 114 ? 33.988  -25.301 53.431  1.00 117.66 ?  410 GLY   B O   1 
ATOM   6028 N N   . ASN   B 2 115 ? 35.615  -26.877 53.197  1.00 108.32 ?  411 ASN   B N   1 
ATOM   6029 C CA  . ASN   B 2 115 ? 34.839  -27.959 53.836  1.00 114.06 ?  411 ASN   B CA  1 
ATOM   6030 C C   . ASN   B 2 115 ? 35.439  -28.336 55.182  1.00 112.95 ?  411 ASN   B C   1 
ATOM   6031 O O   . ASN   B 2 115 ? 35.395  -29.491 55.528  1.00 118.09 ?  411 ASN   B O   1 
ATOM   6032 C CB  . ASN   B 2 115 ? 34.642  -29.143 52.899  1.00 116.45 ?  411 ASN   B CB  1 
ATOM   6033 C CG  . ASN   B 2 115 ? 35.782  -30.128 52.932  1.00 117.80 ?  411 ASN   B CG  1 
ATOM   6034 O OD1 . ASN   B 2 115 ? 36.845  -29.839 53.460  1.00 114.80 ?  411 ASN   B OD1 1 
ATOM   6035 N ND2 . ASN   B 2 115 ? 35.566  -31.296 52.358  1.00 116.66 ?  411 ASN   B ND2 1 
ATOM   6036 N N   . LYS   B 2 116 ? 36.011  -27.369 55.868  1.00 108.18 ?  412 LYS   B N   1 
ATOM   6037 C CA  . LYS   B 2 116 ? 36.512  -27.650 57.220  1.00 110.85 ?  412 LYS   B CA  1 
ATOM   6038 C C   . LYS   B 2 116 ? 36.024  -26.513 58.101  1.00 119.08 ?  412 LYS   B C   1 
ATOM   6039 O O   . LYS   B 2 116 ? 36.101  -25.357 57.686  1.00 118.22 ?  412 LYS   B O   1 
ATOM   6040 C CB  . LYS   B 2 116 ? 38.032  -27.753 57.243  1.00 108.17 ?  412 LYS   B CB  1 
ATOM   6041 C CG  . LYS   B 2 116 ? 38.566  -29.154 57.465  1.00 110.23 ?  412 LYS   B CG  1 
ATOM   6042 C CD  . LYS   B 2 116 ? 38.508  -29.947 56.210  1.00 111.64 ?  412 LYS   B CD  1 
ATOM   6043 C CE  . LYS   B 2 116 ? 38.063  -31.366 56.426  1.00 109.85 ?  412 LYS   B CE  1 
ATOM   6044 N NZ  . LYS   B 2 116 ? 39.229  -32.264 56.513  1.00 107.03 ?  412 LYS   B NZ  1 
ATOM   6045 N N   . SER   B 2 117 ? 35.473  -26.864 59.248  1.00 120.11 ?  413 SER   B N   1 
ATOM   6046 C CA  . SER   B 2 117 ? 34.980  -25.852 60.212  1.00 120.67 ?  413 SER   B CA  1 
ATOM   6047 C C   . SER   B 2 117 ? 36.143  -25.315 61.041  1.00 116.69 ?  413 SER   B C   1 
ATOM   6048 O O   . SER   B 2 117 ? 37.183  -25.949 61.060  1.00 114.15 ?  413 SER   B O   1 
ATOM   6049 C CB  . SER   B 2 117 ? 33.894  -26.423 61.065  1.00 121.34 ?  413 SER   B CB  1 
ATOM   6050 O OG  . SER   B 2 117 ? 34.317  -26.587 62.404  1.00 121.61 ?  413 SER   B OG  1 
ATOM   6051 N N   . VAL   B 2 118 ? 35.917  -24.230 61.771  1.00 112.15 ?  414 VAL   B N   1 
ATOM   6052 C CA  . VAL   B 2 118 ? 37.016  -23.610 62.561  1.00 113.81 ?  414 VAL   B CA  1 
ATOM   6053 C C   . VAL   B 2 118 ? 37.546  -24.568 63.617  1.00 114.73 ?  414 VAL   B C   1 
ATOM   6054 O O   . VAL   B 2 118 ? 38.728  -24.485 63.937  1.00 109.87 ?  414 VAL   B O   1 
ATOM   6055 C CB  . VAL   B 2 118 ? 36.563  -22.317 63.242  1.00 109.39 ?  414 VAL   B CB  1 
ATOM   6056 C CG1 . VAL   B 2 118 ? 37.755  -21.515 63.716  1.00 102.15 ?  414 VAL   B CG1 1 
ATOM   6057 C CG2 . VAL   B 2 118 ? 35.673  -21.495 62.338  1.00 110.28 ?  414 VAL   B CG2 1 
ATOM   6058 N N   . VAL   B 2 119 ? 36.678  -25.349 64.239  1.00 117.53 ?  415 VAL   B N   1 
ATOM   6059 C CA  . VAL   B 2 119 ? 37.219  -26.209 65.322  1.00 122.95 ?  415 VAL   B CA  1 
ATOM   6060 C C   . VAL   B 2 119 ? 38.197  -27.236 64.759  1.00 121.00 ?  415 VAL   B C   1 
ATOM   6061 O O   . VAL   B 2 119 ? 39.277  -27.365 65.352  1.00 117.22 ?  415 VAL   B O   1 
ATOM   6062 C CB  . VAL   B 2 119 ? 36.115  -26.852 66.178  1.00 123.95 ?  415 VAL   B CB  1 
ATOM   6063 C CG1 . VAL   B 2 119 ? 35.112  -27.620 65.342  1.00 119.02 ?  415 VAL   B CG1 1 
ATOM   6064 C CG2 . VAL   B 2 119 ? 36.706  -27.741 67.255  1.00 115.65 ?  415 VAL   B CG2 1 
ATOM   6065 N N   . GLN   B 2 120 ? 37.871  -27.903 63.650  1.00 117.07 ?  416 GLN   B N   1 
ATOM   6066 C CA  . GLN   B 2 120 ? 38.880  -28.898 63.215  1.00 117.50 ?  416 GLN   B CA  1 
ATOM   6067 C C   . GLN   B 2 120 ? 40.090  -28.115 62.753  1.00 115.19 ?  416 GLN   B C   1 
ATOM   6068 O O   . GLN   B 2 120 ? 41.193  -28.643 62.883  1.00 114.88 ?  416 GLN   B O   1 
ATOM   6069 C CB  . GLN   B 2 120 ? 38.391  -29.955 62.232  1.00 111.42 ?  416 GLN   B CB  1 
ATOM   6070 C CG  . GLN   B 2 120 ? 37.723  -29.383 61.013  1.00 114.41 ?  416 GLN   B CG  1 
ATOM   6071 C CD  . GLN   B 2 120 ? 36.304  -29.114 61.402  1.00 118.24 ?  416 GLN   B CD  1 
ATOM   6072 O OE1 . GLN   B 2 120 ? 36.055  -28.426 62.379  1.00 120.20 ?  416 GLN   B OE1 1 
ATOM   6073 N NE2 . GLN   B 2 120 ? 35.377  -29.639 60.625  1.00 110.55 ?  416 GLN   B NE2 1 
ATOM   6074 N N   . VAL   B 2 121 ? 39.862  -26.898 62.267  1.00 110.69 ?  417 VAL   B N   1 
ATOM   6075 C CA  . VAL   B 2 121 ? 41.040  -26.098 61.951  1.00 110.24 ?  417 VAL   B CA  1 
ATOM   6076 C C   . VAL   B 2 121 ? 41.929  -25.942 63.185  1.00 113.97 ?  417 VAL   B C   1 
ATOM   6077 O O   . VAL   B 2 121 ? 43.151  -26.119 63.100  1.00 109.18 ?  417 VAL   B O   1 
ATOM   6078 C CB  . VAL   B 2 121 ? 40.635  -24.736 61.359  1.00 109.80 ?  417 VAL   B CB  1 
ATOM   6079 C CG1 . VAL   B 2 121 ? 41.843  -23.808 61.300  1.00 102.66 ?  417 VAL   B CG1 1 
ATOM   6080 C CG2 . VAL   B 2 121 ? 40.020  -24.917 59.972  1.00 107.58 ?  417 VAL   B CG2 1 
ATOM   6081 N N   . LYS   B 2 122 ? 41.341  -25.627 64.354  1.00 117.77 ?  418 LYS   B N   1 
ATOM   6082 C CA  . LYS   B 2 122 ? 42.133  -25.602 65.590  1.00 116.95 ?  418 LYS   B CA  1 
ATOM   6083 C C   . LYS   B 2 122 ? 42.724  -26.962 65.895  1.00 112.89 ?  418 LYS   B C   1 
ATOM   6084 O O   . LYS   B 2 122 ? 43.884  -27.069 66.312  1.00 108.83 ?  418 LYS   B O   1 
ATOM   6085 C CB  . LYS   B 2 122 ? 41.315  -25.164 66.798  1.00 119.27 ?  418 LYS   B CB  1 
ATOM   6086 C CG  . LYS   B 2 122 ? 41.406  -23.714 67.108  1.00 120.92 ?  418 LYS   B CG  1 
ATOM   6087 C CD  . LYS   B 2 122 ? 40.438  -22.994 66.255  1.00 127.01 ?  418 LYS   B CD  1 
ATOM   6088 C CE  . LYS   B 2 122 ? 39.043  -23.327 66.732  1.00 132.66 ?  418 LYS   B CE  1 
ATOM   6089 N NZ  . LYS   B 2 122 ? 38.060  -22.565 65.940  1.00 130.14 ?  418 LYS   B NZ  1 
ATOM   6090 N N   . ASN   B 2 123 ? 41.901  -27.986 65.811  1.00 111.53 ?  419 ASN   B N   1 
ATOM   6091 C CA  . ASN   B 2 123 ? 42.407  -29.334 66.156  1.00 120.79 ?  419 ASN   B CA  1 
ATOM   6092 C C   . ASN   B 2 123 ? 43.570  -29.633 65.220  1.00 120.45 ?  419 ASN   B C   1 
ATOM   6093 O O   . ASN   B 2 123 ? 44.637  -30.075 65.679  1.00 114.51 ?  419 ASN   B O   1 
ATOM   6094 C CB  . ASN   B 2 123 ? 41.287  -30.362 66.043  1.00 125.82 ?  419 ASN   B CB  1 
ATOM   6095 C CG  . ASN   B 2 123 ? 40.269  -30.202 67.148  1.00 128.19 ?  419 ASN   B CG  1 
ATOM   6096 O OD1 . ASN   B 2 123 ? 40.578  -29.646 68.206  1.00 128.02 ?  419 ASN   B OD1 1 
ATOM   6097 N ND2 . ASN   B 2 123 ? 39.072  -30.701 66.912  1.00 122.14 ?  419 ASN   B ND2 1 
ATOM   6098 N N   . PHE   B 2 124 ? 43.420  -29.164 63.993  1.00 121.18 ?  420 PHE   B N   1 
ATOM   6099 C CA  . PHE   B 2 124 ? 44.451  -29.425 62.971  1.00 117.06 ?  420 PHE   B CA  1 
ATOM   6100 C C   . PHE   B 2 124 ? 45.780  -28.826 63.400  1.00 114.82 ?  420 PHE   B C   1 
ATOM   6101 O O   . PHE   B 2 124 ? 46.781  -29.494 63.218  1.00 117.09 ?  420 PHE   B O   1 
ATOM   6102 C CB  . PHE   B 2 124 ? 44.033  -28.812 61.641  1.00 111.66 ?  420 PHE   B CB  1 
ATOM   6103 C CG  . PHE   B 2 124 ? 45.053  -29.015 60.559  1.00 112.21 ?  420 PHE   B CG  1 
ATOM   6104 C CD1 . PHE   B 2 124 ? 44.861  -29.961 59.575  1.00 108.99 ?  420 PHE   B CD1 1 
ATOM   6105 C CD2 . PHE   B 2 124 ? 46.211  -28.267 60.541  1.00 108.92 ?  420 PHE   B CD2 1 
ATOM   6106 C CE1 . PHE   B 2 124 ? 45.810  -30.139 58.590  1.00 103.98 ?  420 PHE   B CE1 1 
ATOM   6107 C CE2 . PHE   B 2 124 ? 47.157  -28.447 59.553  1.00 101.89 ?  420 PHE   B CE2 1 
ATOM   6108 C CZ  . PHE   B 2 124 ? 46.954  -29.388 58.585  1.00 102.42 ?  420 PHE   B CZ  1 
ATOM   6109 N N   . PHE   B 2 125 ? 45.783  -27.628 63.968  1.00 110.17 ?  421 PHE   B N   1 
ATOM   6110 C CA  . PHE   B 2 125 ? 47.095  -27.041 64.316  1.00 112.91 ?  421 PHE   B CA  1 
ATOM   6111 C C   . PHE   B 2 125 ? 47.803  -27.927 65.327  1.00 117.18 ?  421 PHE   B C   1 
ATOM   6112 O O   . PHE   B 2 125 ? 48.992  -28.189 65.184  1.00 113.55 ?  421 PHE   B O   1 
ATOM   6113 C CB  . PHE   B 2 125 ? 46.892  -25.748 65.094  1.00 110.23 ?  421 PHE   B CB  1 
ATOM   6114 C CG  . PHE   B 2 125 ? 46.741  -24.512 64.256  1.00 107.31 ?  421 PHE   B CG  1 
ATOM   6115 C CD1 . PHE   B 2 125 ? 45.627  -24.333 63.464  1.00 107.91 ?  421 PHE   B CD1 1 
ATOM   6116 C CD2 . PHE   B 2 125 ? 47.701  -23.522 64.287  1.00 103.96 ?  421 PHE   B CD2 1 
ATOM   6117 C CE1 . PHE   B 2 125 ? 45.486  -23.184 62.711  1.00 110.73 ?  421 PHE   B CE1 1 
ATOM   6118 C CE2 . PHE   B 2 125 ? 47.557  -22.374 63.534  1.00 104.94 ?  421 PHE   B CE2 1 
ATOM   6119 C CZ  . PHE   B 2 125 ? 46.449  -22.210 62.748  1.00 109.74 ?  421 PHE   B CZ  1 
ATOM   6120 N N   . VAL   B 2 126 ? 47.067  -28.353 66.343  1.00 118.25 ?  422 VAL   B N   1 
ATOM   6121 C CA  . VAL   B 2 126 ? 47.700  -29.197 67.388  1.00 117.78 ?  422 VAL   B CA  1 
ATOM   6122 C C   . VAL   B 2 126 ? 48.012  -30.582 66.839  1.00 119.56 ?  422 VAL   B C   1 
ATOM   6123 O O   . VAL   B 2 126 ? 49.093  -31.082 67.105  1.00 124.01 ?  422 VAL   B O   1 
ATOM   6124 C CB  . VAL   B 2 126 ? 46.836  -29.253 68.653  1.00 118.42 ?  422 VAL   B CB  1 
ATOM   6125 C CG1 . VAL   B 2 126 ? 47.621  -29.825 69.816  1.00 110.12 ?  422 VAL   B CG1 1 
ATOM   6126 C CG2 . VAL   B 2 126 ? 46.312  -27.873 69.000  1.00 113.69 ?  422 VAL   B CG2 1 
ATOM   6127 N N   . ASN   B 2 127 ? 47.095  -31.146 66.067  1.00 117.55 ?  423 ASN   B N   1 
ATOM   6128 C CA  . ASN   B 2 127 ? 47.273  -32.539 65.596  1.00 118.73 ?  423 ASN   B CA  1 
ATOM   6129 C C   . ASN   B 2 127 ? 48.492  -32.712 64.699  1.00 118.42 ?  423 ASN   B C   1 
ATOM   6130 O O   . ASN   B 2 127 ? 49.220  -33.671 64.897  1.00 118.52 ?  423 ASN   B O   1 
ATOM   6131 C CB  . ASN   B 2 127 ? 46.055  -32.996 64.813  1.00 120.48 ?  423 ASN   B CB  1 
ATOM   6132 C CG  . ASN   B 2 127 ? 44.895  -33.281 65.728  1.00 120.53 ?  423 ASN   B CG  1 
ATOM   6133 O OD1 . ASN   B 2 127 ? 43.756  -32.968 65.411  1.00 118.46 ?  423 ASN   B OD1 1 
ATOM   6134 N ND2 . ASN   B 2 127 ? 45.189  -33.865 66.870  1.00 120.36 ?  423 ASN   B ND2 1 
ATOM   6135 N N   . TYR   B 2 128 ? 48.721  -31.797 63.772  1.00 120.39 ?  424 TYR   B N   1 
ATOM   6136 C CA  . TYR   B 2 128 ? 49.829  -31.994 62.810  1.00 122.71 ?  424 TYR   B CA  1 
ATOM   6137 C C   . TYR   B 2 128 ? 50.993  -31.080 63.158  1.00 117.93 ?  424 TYR   B C   1 
ATOM   6138 O O   . TYR   B 2 128 ? 51.887  -30.919 62.344  1.00 113.18 ?  424 TYR   B O   1 
ATOM   6139 C CB  . TYR   B 2 128 ? 49.316  -31.732 61.397  1.00 109.21 ?  424 TYR   B CB  1 
ATOM   6140 C CG  . TYR   B 2 128 ? 48.340  -32.764 60.907  1.00 110.09 ?  424 TYR   B CG  1 
ATOM   6141 C CD1 . TYR   B 2 128 ? 48.778  -33.924 60.311  1.00 109.89 ?  424 TYR   B CD1 1 
ATOM   6142 C CD2 . TYR   B 2 128 ? 46.981  -32.589 61.045  1.00 110.90 ?  424 TYR   B CD2 1 
ATOM   6143 C CE1 . TYR   B 2 128 ? 47.894  -34.887 59.865  1.00 110.53 ?  424 TYR   B CE1 1 
ATOM   6144 C CE2 . TYR   B 2 128 ? 46.082  -33.540 60.600  1.00 111.96 ?  424 TYR   B CE2 1 
ATOM   6145 C CZ  . TYR   B 2 128 ? 46.541  -34.700 60.018  1.00 114.43 ?  424 TYR   B CZ  1 
ATOM   6146 O OH  . TYR   B 2 128 ? 45.677  -35.653 59.577  1.00 117.77 ?  424 TYR   B OH  1 
ATOM   6147 N N   . ARG   B 2 129 ? 51.052  -30.636 64.403  1.00 120.77 ?  425 ARG   B N   1 
ATOM   6148 C CA  . ARG   B 2 129 ? 52.031  -29.597 64.803  1.00 122.06 ?  425 ARG   B CA  1 
ATOM   6149 C C   . ARG   B 2 129 ? 53.470  -30.006 64.503  1.00 117.55 ?  425 ARG   B C   1 
ATOM   6150 O O   . ARG   B 2 129 ? 54.226  -29.141 64.094  1.00 108.42 ?  425 ARG   B O   1 
ATOM   6151 C CB  . ARG   B 2 129 ? 51.825  -29.253 66.280  1.00 127.10 ?  425 ARG   B CB  1 
ATOM   6152 C CG  . ARG   B 2 129 ? 53.034  -28.640 66.969  1.00 125.34 ?  425 ARG   B CG  1 
ATOM   6153 C CD  . ARG   B 2 129 ? 53.051  -29.084 68.418  1.00 128.88 ?  425 ARG   B CD  1 
ATOM   6154 N NE  . ARG   B 2 129 ? 53.724  -28.155 69.306  1.00 133.05 ?  425 ARG   B NE  1 
ATOM   6155 C CZ  . ARG   B 2 129 ? 53.599  -26.840 69.244  1.00 136.54 ?  425 ARG   B CZ  1 
ATOM   6156 N NH1 . ARG   B 2 129 ? 52.825  -26.287 68.325  1.00 134.49 ?  425 ARG   B NH1 1 
ATOM   6157 N NH2 . ARG   B 2 129 ? 54.250  -26.079 70.103  1.00 132.03 ?  425 ARG   B NH2 1 
ATOM   6158 N N   . ARG   B 2 130 ? 53.838  -31.264 64.688  1.00 122.15 ?  426 ARG   B N   1 
ATOM   6159 C CA  . ARG   B 2 130 ? 55.256  -31.612 64.442  1.00 120.21 ?  426 ARG   B CA  1 
ATOM   6160 C C   . ARG   B 2 130 ? 55.492  -32.044 62.994  1.00 117.30 ?  426 ARG   B C   1 
ATOM   6161 O O   . ARG   B 2 130 ? 56.567  -31.733 62.490  1.00 110.24 ?  426 ARG   B O   1 
ATOM   6162 C CB  . ARG   B 2 130 ? 55.699  -32.719 65.399  1.00 124.07 ?  426 ARG   B CB  1 
ATOM   6163 C CG  . ARG   B 2 130 ? 56.162  -32.224 66.761  1.00 133.00 ?  426 ARG   B CG  1 
ATOM   6164 C CD  . ARG   B 2 130 ? 55.793  -33.199 67.865  1.00 144.95 ?  426 ARG   B CD  1 
ATOM   6165 N NE  . ARG   B 2 130 ? 56.427  -32.940 69.151  1.00 147.82 ?  426 ARG   B NE  1 
ATOM   6166 C CZ  . ARG   B 2 130 ? 57.735  -32.989 69.383  1.00 151.78 ?  426 ARG   B CZ  1 
ATOM   6167 N NH1 . ARG   B 2 130 ? 58.577  -33.282 68.408  1.00 153.67 ?  426 ARG   B NH1 1 
ATOM   6168 N NH2 . ARG   B 2 130 ? 58.196  -32.741 70.594  1.00 147.39 ?  426 ARG   B NH2 1 
ATOM   6169 N N   . ARG   B 2 131 ? 54.542  -32.730 62.354  1.00 115.92 ?  427 ARG   B N   1 
ATOM   6170 C CA  . ARG   B 2 131 ? 54.811  -33.219 61.009  1.00 109.21 ?  427 ARG   B CA  1 
ATOM   6171 C C   . ARG   B 2 131 ? 54.754  -32.123 59.954  1.00 108.70 ?  427 ARG   B C   1 
ATOM   6172 O O   . ARG   B 2 131 ? 55.333  -32.291 58.874  1.00 108.21 ?  427 ARG   B O   1 
ATOM   6173 C CB  . ARG   B 2 131 ? 53.813  -34.327 60.676  1.00 108.16 ?  427 ARG   B CB  1 
ATOM   6174 C CG  . ARG   B 2 131 ? 53.793  -35.463 61.690  1.00 108.70 ?  427 ARG   B CG  1 
ATOM   6175 C CD  . ARG   B 2 131 ? 52.677  -36.462 61.415  1.00 105.71 ?  427 ARG   B CD  1 
ATOM   6176 N NE  . ARG   B 2 131 ? 51.416  -36.069 62.038  1.00 111.87 ?  427 ARG   B NE  1 
ATOM   6177 C CZ  . ARG   B 2 131 ? 50.264  -36.708 61.860  1.00 112.07 ?  427 ARG   B CZ  1 
ATOM   6178 N NH1 . ARG   B 2 131 ? 50.205  -37.778 61.076  1.00 101.82 ?  427 ARG   B NH1 1 
ATOM   6179 N NH2 . ARG   B 2 131 ? 49.170  -36.289 62.483  1.00 117.52 ?  427 ARG   B NH2 1 
ATOM   6180 N N   . PHE   B 2 132 ? 54.065  -31.017 60.231  1.00 105.56 ?  428 PHE   B N   1 
ATOM   6181 C CA  . PHE   B 2 132 ? 53.965  -29.909 59.293  1.00 98.01  ?  428 PHE   B CA  1 
ATOM   6182 C C   . PHE   B 2 132 ? 54.645  -28.657 59.810  1.00 96.94  ?  428 PHE   B C   1 
ATOM   6183 O O   . PHE   B 2 132 ? 54.368  -27.566 59.304  1.00 96.40  ?  428 PHE   B O   1 
ATOM   6184 C CB  . PHE   B 2 132 ? 52.501  -29.601 58.968  1.00 96.79  ?  428 PHE   B CB  1 
ATOM   6185 C CG  . PHE   B 2 132 ? 51.861  -30.598 58.047  1.00 96.35  ?  428 PHE   B CG  1 
ATOM   6186 C CD1 . PHE   B 2 132 ? 50.480  -30.694 57.960  1.00 90.57  ?  428 PHE   B CD1 1 
ATOM   6187 C CD2 . PHE   B 2 132 ? 52.644  -31.450 57.275  1.00 94.53  ?  428 PHE   B CD2 1 
ATOM   6188 C CE1 . PHE   B 2 132 ? 49.885  -31.616 57.116  1.00 88.57  ?  428 PHE   B CE1 1 
ATOM   6189 C CE2 . PHE   B 2 132 ? 52.063  -32.373 56.426  1.00 87.00  ?  428 PHE   B CE2 1 
ATOM   6190 C CZ  . PHE   B 2 132 ? 50.677  -32.456 56.346  1.00 87.39  ?  428 PHE   B CZ  1 
ATOM   6191 N N   . ASN   B 2 133 ? 55.502  -28.785 60.824  1.00 99.40  ?  429 ASN   B N   1 
ATOM   6192 C CA  . ASN   B 2 133 ? 56.306  -27.672 61.325  1.00 99.08  ?  429 ASN   B CA  1 
ATOM   6193 C C   . ASN   B 2 133 ? 55.479  -26.399 61.502  1.00 101.17 ?  429 ASN   B C   1 
ATOM   6194 O O   . ASN   B 2 133 ? 55.942  -25.296 61.198  1.00 104.12 ?  429 ASN   B O   1 
ATOM   6195 C CB  . ASN   B 2 133 ? 57.486  -27.415 60.396  1.00 94.49  ?  429 ASN   B CB  1 
ATOM   6196 C CG  . ASN   B 2 133 ? 58.603  -28.393 60.609  1.00 100.72 ?  429 ASN   B CG  1 
ATOM   6197 O OD1 . ASN   B 2 133 ? 58.632  -29.458 59.992  1.00 104.24 ?  429 ASN   B OD1 1 
ATOM   6198 N ND2 . ASN   B 2 133 ? 59.541  -28.042 61.475  1.00 106.14 ?  429 ASN   B ND2 1 
ATOM   6199 N N   . ILE   B 2 134 ? 54.231  -26.592 61.893  1.00 101.05 ?  430 ILE   B N   1 
ATOM   6200 C CA  . ILE   B 2 134 ? 53.245  -25.498 62.095  1.00 98.81  ?  430 ILE   B CA  1 
ATOM   6201 C C   . ILE   B 2 134 ? 53.902  -24.381 62.889  1.00 106.62 ?  430 ILE   B C   1 
ATOM   6202 O O   . ILE   B 2 134 ? 53.594  -23.224 62.660  1.00 106.30 ?  430 ILE   B O   1 
ATOM   6203 C CB  . ILE   B 2 134 ? 52.020  -26.048 62.829  1.00 88.92  ?  430 ILE   B CB  1 
ATOM   6204 C CG1 . ILE   B 2 134 ? 51.252  -27.065 61.981  1.00 101.03 ?  430 ILE   B CG1 1 
ATOM   6205 C CG2 . ILE   B 2 134 ? 51.130  -24.913 63.265  1.00 95.97  ?  430 ILE   B CG2 1 
ATOM   6206 C CD1 . ILE   B 2 134 ? 50.175  -27.855 62.725  1.00 114.47 ?  430 ILE   B CD1 1 
ATOM   6207 N N   . ASP   B 2 135 ? 54.802  -24.743 63.785  1.00 111.94 ?  431 ASP   B N   1 
ATOM   6208 C CA  . ASP   B 2 135 ? 55.476  -23.701 64.589  1.00 113.04 ?  431 ASP   B CA  1 
ATOM   6209 C C   . ASP   B 2 135 ? 56.343  -22.837 63.684  1.00 112.37 ?  431 ASP   B C   1 
ATOM   6210 O O   . ASP   B 2 135 ? 56.187  -21.618 63.697  1.00 112.20 ?  431 ASP   B O   1 
ATOM   6211 C CB  . ASP   B 2 135 ? 56.385  -24.350 65.626  1.00 119.21 ?  431 ASP   B CB  1 
ATOM   6212 C CG  . ASP   B 2 135 ? 55.694  -24.591 66.950  1.00 130.63 ?  431 ASP   B CG  1 
ATOM   6213 O OD1 . ASP   B 2 135 ? 54.544  -24.143 67.094  1.00 128.17 ?  431 ASP   B OD1 1 
ATOM   6214 O OD2 . ASP   B 2 135 ? 56.313  -25.219 67.821  1.00 136.65 ?  431 ASP   B OD2 1 
ATOM   6215 N N   . GLU   B 2 136 ? 57.131  -23.466 62.820  1.00 110.39 ?  432 GLU   B N   1 
ATOM   6216 C CA  . GLU   B 2 136 ? 58.061  -22.681 61.976  1.00 107.99 ?  432 GLU   B CA  1 
ATOM   6217 C C   . GLU   B 2 136 ? 57.257  -21.783 61.059  1.00 107.43 ?  432 GLU   B C   1 
ATOM   6218 O O   . GLU   B 2 136 ? 57.568  -20.609 60.969  1.00 113.58 ?  432 GLU   B O   1 
ATOM   6219 C CB  . GLU   B 2 136 ? 58.903  -23.591 61.093  1.00 101.29 ?  432 GLU   B CB  1 
ATOM   6220 C CG  . GLU   B 2 136 ? 59.644  -24.660 61.851  1.00 109.03 ?  432 GLU   B CG  1 
ATOM   6221 C CD  . GLU   B 2 136 ? 61.022  -24.877 61.276  1.00 107.84 ?  432 GLU   B CD  1 
ATOM   6222 O OE1 . GLU   B 2 136 ? 61.636  -23.893 60.918  1.00 108.17 ?  432 GLU   B OE1 1 
ATOM   6223 O OE2 . GLU   B 2 136 ? 61.468  -26.020 61.196  1.00 115.61 ?  432 GLU   B OE2 1 
ATOM   6224 N N   . VAL   B 2 137 ? 56.182  -22.317 60.507  1.00 103.20 ?  433 VAL   B N   1 
ATOM   6225 C CA  . VAL   B 2 137 ? 55.363  -21.559 59.533  1.00 108.87 ?  433 VAL   B CA  1 
ATOM   6226 C C   . VAL   B 2 137 ? 54.866  -20.287 60.203  1.00 110.88 ?  433 VAL   B C   1 
ATOM   6227 O O   . VAL   B 2 137 ? 55.078  -19.220 59.647  1.00 110.38 ?  433 VAL   B O   1 
ATOM   6228 C CB  . VAL   B 2 137 ? 54.180  -22.436 59.113  1.00 100.44 ?  433 VAL   B CB  1 
ATOM   6229 C CG1 . VAL   B 2 137 ? 52.970  -21.603 58.770  1.00 98.56  ?  433 VAL   B CG1 1 
ATOM   6230 C CG2 . VAL   B 2 137 ? 54.554  -23.354 57.975  1.00 94.34  ?  433 VAL   B CG2 1 
ATOM   6231 N N   . LEU   B 2 138 ? 54.376  -20.383 61.429  1.00 110.69 ?  434 LEU   B N   1 
ATOM   6232 C CA  . LEU   B 2 138 ? 53.875  -19.168 62.097  1.00 109.46 ?  434 LEU   B CA  1 
ATOM   6233 C C   . LEU   B 2 138 ? 55.009  -18.164 62.282  1.00 114.11 ?  434 LEU   B C   1 
ATOM   6234 O O   . LEU   B 2 138 ? 54.778  -16.986 62.009  1.00 113.61 ?  434 LEU   B O   1 
ATOM   6235 C CB  . LEU   B 2 138 ? 53.201  -19.589 63.394  1.00 102.78 ?  434 LEU   B CB  1 
ATOM   6236 C CG  . LEU   B 2 138 ? 51.846  -20.234 63.136  1.00 103.96 ?  434 LEU   B CG  1 
ATOM   6237 C CD1 . LEU   B 2 138 ? 51.417  -21.118 64.280  1.00 96.85  ?  434 LEU   B CD1 1 
ATOM   6238 C CD2 . LEU   B 2 138 ? 50.798  -19.180 62.852  1.00 101.85 ?  434 LEU   B CD2 1 
ATOM   6239 N N   . GLN   B 2 139 ? 56.216  -18.620 62.620  1.00 116.93 ?  435 GLN   B N   1 
ATOM   6240 C CA  . GLN   B 2 139 ? 57.335  -17.664 62.789  1.00 116.19 ?  435 GLN   B CA  1 
ATOM   6241 C C   . GLN   B 2 139 ? 57.555  -16.936 61.470  1.00 114.95 ?  435 GLN   B C   1 
ATOM   6242 O O   . GLN   B 2 139 ? 57.621  -15.706 61.492  1.00 116.57 ?  435 GLN   B O   1 
ATOM   6243 C CB  . GLN   B 2 139 ? 58.635  -18.404 63.056  1.00 116.93 ?  435 GLN   B CB  1 
ATOM   6244 C CG  . GLN   B 2 139 ? 58.527  -19.453 64.141  1.00 116.67 ?  435 GLN   B CG  1 
ATOM   6245 C CD  . GLN   B 2 139 ? 59.890  -20.017 64.435  1.00 119.17 ?  435 GLN   B CD  1 
ATOM   6246 O OE1 . GLN   B 2 139 ? 60.893  -19.582 63.883  1.00 132.97 ?  435 GLN   B OE1 1 
ATOM   6247 N NE2 . GLN   B 2 139 ? 59.936  -21.003 65.310  1.00 113.89 ?  435 GLN   B NE2 1 
ATOM   6248 N N   . GLU   B 2 140 ? 57.544  -17.666 60.354  1.00 114.68 ?  436 GLU   B N   1 
ATOM   6249 C CA  . GLU   B 2 140 ? 57.723  -17.024 59.031  1.00 115.76 ?  436 GLU   B CA  1 
ATOM   6250 C C   . GLU   B 2 140 ? 56.572  -16.045 58.812  1.00 112.81 ?  436 GLU   B C   1 
ATOM   6251 O O   . GLU   B 2 140 ? 56.835  -14.954 58.328  1.00 103.49 ?  436 GLU   B O   1 
ATOM   6252 C CB  . GLU   B 2 140 ? 57.797  -18.079 57.933  1.00 112.36 ?  436 GLU   B CB  1 
ATOM   6253 C CG  . GLU   B 2 140 ? 58.662  -17.662 56.761  1.00 118.48 ?  436 GLU   B CG  1 
ATOM   6254 C CD  . GLU   B 2 140 ? 60.136  -17.969 56.934  1.00 117.63 ?  436 GLU   B CD  1 
ATOM   6255 O OE1 . GLU   B 2 140 ? 60.536  -18.197 58.072  1.00 118.00 ?  436 GLU   B OE1 1 
ATOM   6256 O OE2 . GLU   B 2 140 ? 60.875  -17.977 55.933  1.00 119.76 ?  436 GLU   B OE2 1 
ATOM   6257 N N   . TRP   B 2 141 ? 55.345  -16.413 59.179  1.00 114.25 ?  437 TRP   B N   1 
ATOM   6258 C CA  . TRP   B 2 141 ? 54.209  -15.472 59.023  1.00 114.13 ?  437 TRP   B CA  1 
ATOM   6259 C C   . TRP   B 2 141 ? 54.402  -14.256 59.914  1.00 119.09 ?  437 TRP   B C   1 
ATOM   6260 O O   . TRP   B 2 141 ? 54.036  -13.165 59.498  1.00 118.14 ?  437 TRP   B O   1 
ATOM   6261 C CB  . TRP   B 2 141 ? 52.864  -16.100 59.353  1.00 112.74 ?  437 TRP   B CB  1 
ATOM   6262 C CG  . TRP   B 2 141 ? 51.778  -15.085 59.198  1.00 114.15 ?  437 TRP   B CG  1 
ATOM   6263 C CD1 . TRP   B 2 141 ? 51.261  -14.625 58.027  1.00 114.59 ?  437 TRP   B CD1 1 
ATOM   6264 C CD2 . TRP   B 2 141 ? 51.109  -14.357 60.235  1.00 118.27 ?  437 TRP   B CD2 1 
ATOM   6265 N NE1 . TRP   B 2 141 ? 50.305  -13.680 58.262  1.00 116.39 ?  437 TRP   B NE1 1 
ATOM   6266 C CE2 . TRP   B 2 141 ? 50.186  -13.499 59.608  1.00 117.97 ?  437 TRP   B CE2 1 
ATOM   6267 C CE3 . TRP   B 2 141 ? 51.182  -14.358 61.627  1.00 119.48 ?  437 TRP   B CE3 1 
ATOM   6268 C CZ2 . TRP   B 2 141 ? 49.347  -12.653 60.321  1.00 117.81 ?  437 TRP   B CZ2 1 
ATOM   6269 C CZ3 . TRP   B 2 141 ? 50.349  -13.524 62.334  1.00 117.63 ?  437 TRP   B CZ3 1 
ATOM   6270 C CH2 . TRP   B 2 141 ? 49.445  -12.685 61.690  1.00 118.00 ?  437 TRP   B CH2 1 
ATOM   6271 N N   . GLU   B 2 142 ? 54.944  -14.452 61.111  1.00 118.40 ?  438 GLU   B N   1 
ATOM   6272 C CA  . GLU   B 2 142 ? 55.098  -13.306 62.035  1.00 122.77 ?  438 GLU   B CA  1 
ATOM   6273 C C   . GLU   B 2 142 ? 55.984  -12.237 61.387  1.00 122.59 ?  438 GLU   B C   1 
ATOM   6274 O O   . GLU   B 2 142 ? 55.594  -11.064 61.423  1.00 118.39 ?  438 GLU   B O   1 
ATOM   6275 C CB  . GLU   B 2 142 ? 55.620  -13.782 63.392  1.00 122.75 ?  438 GLU   B CB  1 
ATOM   6276 C CG  . GLU   B 2 142 ? 54.559  -13.783 64.484  1.00 127.26 ?  438 GLU   B CG  1 
ATOM   6277 C CD  . GLU   B 2 142 ? 54.679  -14.847 65.565  1.00 128.71 ?  438 GLU   B CD  1 
ATOM   6278 O OE1 . GLU   B 2 142 ? 55.751  -15.454 65.689  1.00 120.61 ?  438 GLU   B OE1 1 
ATOM   6279 O OE2 . GLU   B 2 142 ? 53.696  -15.061 66.286  1.00 127.61 ?  438 GLU   B OE2 1 
ATOM   6280 N N   . ALA   B 2 143 ? 57.065  -12.611 60.709  1.00 117.97 ?  439 ALA   B N   1 
ATOM   6281 C CA  . ALA   B 2 143 ? 57.934  -11.574 60.114  1.00 117.88 ?  439 ALA   B CA  1 
ATOM   6282 C C   . ALA   B 2 143 ? 57.391  -11.087 58.768  1.00 125.46 ?  439 ALA   B C   1 
ATOM   6283 O O   . ALA   B 2 143 ? 58.081  -11.298 57.773  1.00 124.98 ?  439 ALA   B O   1 
ATOM   6284 C CB  . ALA   B 2 143 ? 59.315  -12.142 59.944  1.00 106.68 ?  439 ALA   B CB  1 
ATOM   6285 N N   . GLU   B 2 144 ? 56.261  -10.374 58.770  1.00 125.64 ?  440 GLU   B N   1 
ATOM   6286 C CA  . GLU   B 2 144 ? 55.612  -9.824  57.551  1.00 120.63 ?  440 GLU   B CA  1 
ATOM   6287 C C   . GLU   B 2 144 ? 54.416  -8.982  57.995  1.00 118.44 ?  440 GLU   B C   1 
ATOM   6288 O O   . GLU   B 2 144 ? 53.360  -9.595  58.222  1.00 117.65 ?  440 GLU   B O   1 
ATOM   6289 C CB  . GLU   B 2 144 ? 55.103  -10.941 56.638  1.00 119.60 ?  440 GLU   B CB  1 
ATOM   6290 C CG  . GLU   B 2 144 ? 55.714  -10.921 55.244  1.00 120.68 ?  440 GLU   B CG  1 
ATOM   6291 C CD  . GLU   B 2 144 ? 55.001  -11.716 54.158  1.00 122.95 ?  440 GLU   B CD  1 
ATOM   6292 O OE1 . GLU   B 2 144 ? 54.003  -11.215 53.608  1.00 119.89 ?  440 GLU   B OE1 1 
ATOM   6293 O OE2 . GLU   B 2 144 ? 55.459  -12.827 53.851  1.00 110.41 ?  440 GLU   B OE2 1 
HETATM 6294 C C4  . A1BI4 C 3 .   ? -7.582  51.554  81.686  1.00 112.60 ?  901 A1BI4 A C4  1 
HETATM 6295 C C14 . A1BI4 C 3 .   ? -7.333  59.553  81.883  1.00 65.43  ?  901 A1BI4 A C14 1 
HETATM 6296 C C5  . A1BI4 C 3 .   ? -7.809  52.994  81.335  1.00 97.12  ?  901 A1BI4 A C5  1 
HETATM 6297 C C6  . A1BI4 C 3 .   ? -8.310  53.465  80.124  1.00 95.23  ?  901 A1BI4 A C6  1 
HETATM 6298 C C11 . A1BI4 C 3 .   ? -5.638  56.553  83.095  1.00 75.65  ?  901 A1BI4 A C11 1 
HETATM 6299 C C7  . A1BI4 C 3 .   ? -8.445  54.820  79.893  1.00 92.96  ?  901 A1BI4 A C7  1 
HETATM 6300 C C8  . A1BI4 C 3 .   ? -8.069  55.716  80.877  1.00 92.15  ?  901 A1BI4 A C8  1 
HETATM 6301 C C9  . A1BI4 C 3 .   ? -7.585  55.286  82.110  1.00 91.42  ?  901 A1BI4 A C9  1 
HETATM 6302 C C10 . A1BI4 C 3 .   ? -7.162  56.288  83.183  1.00 81.96  ?  901 A1BI4 A C10 1 
HETATM 6303 C C12 . A1BI4 C 3 .   ? -4.734  55.399  83.389  1.00 78.13  ?  901 A1BI4 A C12 1 
HETATM 6304 C C13 . A1BI4 C 3 .   ? -8.083  57.592  83.245  1.00 73.62  ?  901 A1BI4 A C13 1 
HETATM 6305 N N1  . A1BI4 C 3 .   ? -9.879  50.632  77.884  1.00 110.45 ?  901 A1BI4 A N1  1 
HETATM 6306 N N2  . A1BI4 C 3 .   ? -9.162  51.142  78.959  1.00 110.96 ?  901 A1BI4 A N2  1 
HETATM 6307 C C3  . A1BI4 C 3 .   ? -9.052  50.277  79.935  1.00 108.58 ?  901 A1BI4 A C3  1 
HETATM 6308 N N3  . A1BI4 C 3 .   ? -8.328  50.516  81.088  1.00 107.38 ?  901 A1BI4 A N3  1 
HETATM 6309 C C1  . A1BI4 C 3 .   ? -10.783 48.535  76.975  1.00 118.61 ?  901 A1BI4 A C1  1 
HETATM 6310 C C15 . A1BI4 C 3 .   ? -7.174  60.120  80.616  1.00 64.12  ?  901 A1BI4 A C15 1 
HETATM 6311 C C16 . A1BI4 C 3 .   ? -6.621  61.361  80.470  1.00 66.46  ?  901 A1BI4 A C16 1 
HETATM 6312 C C17 . A1BI4 C 3 .   ? -6.463  61.950  79.096  1.00 64.54  ?  901 A1BI4 A C17 1 
HETATM 6313 C C18 . A1BI4 C 3 .   ? -6.211  62.093  81.638  1.00 69.67  ?  901 A1BI4 A C18 1 
HETATM 6314 C C19 . A1BI4 C 3 .   ? -5.602  63.464  81.495  1.00 58.72  ?  901 A1BI4 A C19 1 
HETATM 6315 C C2  . A1BI4 C 3 .   ? -10.195 49.391  78.049  1.00 120.24 ?  901 A1BI4 A C2  1 
HETATM 6316 C C20 . A1BI4 C 3 .   ? -6.355  61.525  82.882  1.00 67.92  ?  901 A1BI4 A C20 1 
HETATM 6317 C C21 . A1BI4 C 3 .   ? -6.926  60.258  83.046  1.00 68.55  ?  901 A1BI4 A C21 1 
HETATM 6318 C C22 . A1BI4 C 3 .   ? -6.529  60.251  85.573  1.00 60.70  ?  901 A1BI4 A C22 1 
HETATM 6319 C C23 . A1BI4 C 3 .   ? -6.847  61.725  85.847  1.00 60.68  ?  901 A1BI4 A C23 1 
HETATM 6320 C C24 . A1BI4 C 3 .   ? -6.367  62.187  87.231  1.00 62.34  ?  901 A1BI4 A C24 1 
HETATM 6321 C C25 . A1BI4 C 3 .   ? -7.026  63.476  87.733  1.00 59.82  ?  901 A1BI4 A C25 1 
HETATM 6322 C C26 . A1BI4 C 3 .   ? -6.436  63.913  89.051  1.00 58.91  ?  901 A1BI4 A C26 1 
HETATM 6323 C C27 . A1BI4 C 3 .   ? -5.990  70.222  89.754  1.00 51.04  ?  901 A1BI4 A C27 1 
HETATM 6324 C C28 . A1BI4 C 3 .   ? -6.640  71.551  89.487  1.00 47.94  ?  901 A1BI4 A C28 1 
HETATM 6325 C C29 . A1BI4 C 3 .   ? -6.056  73.643  88.780  1.00 53.25  ?  901 A1BI4 A C29 1 
HETATM 6326 C C30 . A1BI4 C 3 .   ? -3.759  74.370  87.991  1.00 50.40  ?  901 A1BI4 A C30 1 
HETATM 6327 C C31 . A1BI4 C 3 .   ? -3.597  76.290  88.894  1.00 51.02  ?  901 A1BI4 A C31 1 
HETATM 6328 C C32 . A1BI4 C 3 .   ? -3.238  77.567  89.375  1.00 48.67  ?  901 A1BI4 A C32 1 
HETATM 6329 C C33 . A1BI4 C 3 .   ? -5.303  77.601  90.431  1.00 47.57  ?  901 A1BI4 A C33 1 
HETATM 6330 C C34 . A1BI4 C 3 .   ? -4.836  75.800  89.259  1.00 48.63  ?  901 A1BI4 A C34 1 
HETATM 6331 C C35 . A1BI4 C 3 .   ? -6.421  72.898  87.504  1.00 52.63  ?  901 A1BI4 A C35 1 
HETATM 6332 C C36 . A1BI4 C 3 .   ? -7.251  71.750  88.093  1.00 49.06  ?  901 A1BI4 A C36 1 
HETATM 6333 C C37 . A1BI4 C 3 .   ? -7.807  58.450  84.474  1.00 67.43  ?  901 A1BI4 A C37 1 
HETATM 6334 C C38 . A1BI4 C 3 .   ? -9.234  57.264  85.758  1.00 67.37  ?  901 A1BI4 A C38 1 
HETATM 6335 C C39 . A1BI4 C 3 .   ? -9.510  57.099  83.400  1.00 72.62  ?  901 A1BI4 A C39 1 
HETATM 6336 C C40 . A1BI4 C 3 .   ? -7.451  53.917  82.320  1.00 87.59  ?  901 A1BI4 A C40 1 
HETATM 6337 N N10 . A1BI4 C 3 .   ? -5.751  76.416  90.028  1.00 50.45  ?  901 A1BI4 A N10 1 
HETATM 6338 N N11 . A1BI4 C 3 .   ? -8.221  58.115  85.656  1.00 65.24  ?  901 A1BI4 A N11 1 
HETATM 6339 N N12 . A1BI4 C 3 .   ? -9.905  56.798  84.670  1.00 71.83  ?  901 A1BI4 A N12 1 
HETATM 6340 N N4  . A1BI4 C 3 .   ? -7.906  58.319  81.995  1.00 66.72  ?  901 A1BI4 A N4  1 
HETATM 6341 N N5  . A1BI4 C 3 .   ? -7.105  59.645  84.332  1.00 65.04  ?  901 A1BI4 A N5  1 
HETATM 6342 N N6  . A1BI4 C 3 .   ? -4.935  74.566  88.672  1.00 50.13  ?  901 A1BI4 A N6  1 
HETATM 6343 N N7  . A1BI4 C 3 .   ? -2.925  75.375  88.099  1.00 47.60  ?  901 A1BI4 A N7  1 
HETATM 6344 N N8  . A1BI4 C 3 .   ? -2.082  78.163  89.096  1.00 49.27  ?  901 A1BI4 A N8  1 
HETATM 6345 N N9  . A1BI4 C 3 .   ? -4.132  78.204  90.165  1.00 45.19  ?  901 A1BI4 A N9  1 
HETATM 6346 O O1  . A1BI4 C 3 .   ? -6.728  51.253  82.513  1.00 112.51 ?  901 A1BI4 A O1  1 
HETATM 6347 O O10 . A1BI4 C 3 .   ? -7.962  67.286  88.282  1.00 51.95  ?  901 A1BI4 A O10 1 
HETATM 6348 O O11 . A1BI4 C 3 .   ? -5.740  68.484  87.548  1.00 45.21  -1 901 A1BI4 A O11 1 
HETATM 6349 O O12 . A1BI4 C 3 .   ? -7.009  69.209  89.601  1.00 60.93  ?  901 A1BI4 A O12 1 
HETATM 6350 O O13 . A1BI4 C 3 .   ? -5.657  72.599  89.630  1.00 54.22  ?  901 A1BI4 A O13 1 
HETATM 6351 O O14 . A1BI4 C 3 .   ? -7.096  73.646  86.514  1.00 53.68  ?  901 A1BI4 A O14 1 
HETATM 6352 O O15 . A1BI4 C 3 .   ? -8.607  72.142  88.240  1.00 53.47  ?  901 A1BI4 A O15 1 
HETATM 6353 O O16 . A1BI4 C 3 .   ? -9.618  56.913  86.854  1.00 57.83  ?  901 A1BI4 A O16 1 
HETATM 6354 O O17 . A1BI4 C 3 .   ? -10.283 56.980  82.469  1.00 74.20  ?  901 A1BI4 A O17 1 
HETATM 6355 O O2  . A1BI4 C 3 .   ? -4.368  55.033  84.477  1.00 83.93  ?  901 A1BI4 A O2  1 
HETATM 6356 O O3  . A1BI4 C 3 .   ? -8.214  62.043  85.657  1.00 59.41  ?  901 A1BI4 A O3  1 
HETATM 6357 O O4  . A1BI4 C 3 .   ? -6.551  61.174  88.213  1.00 55.71  ?  901 A1BI4 A O4  1 
HETATM 6358 O O5  . A1BI4 C 3 .   ? -8.441  63.305  87.863  1.00 57.70  ?  901 A1BI4 A O5  1 
HETATM 6359 O O6  . A1BI4 C 3 .   ? -7.175  65.017  89.623  1.00 61.56  ?  901 A1BI4 A O6  1 
HETATM 6360 O O7  . A1BI4 C 3 .   ? -5.247  65.329  91.281  1.00 48.46  ?  901 A1BI4 A O7  1 
HETATM 6361 O O8  . A1BI4 C 3 .   ? -7.496  66.603  91.437  1.00 59.59  -1 901 A1BI4 A O8  1 
HETATM 6362 O O9  . A1BI4 C 3 .   ? -5.814  67.060  89.570  1.00 50.75  ?  901 A1BI4 A O9  1 
HETATM 6363 P P1  . A1BI4 C 3 .   ? -6.400  66.008  90.616  1.00 53.38  ?  901 A1BI4 A P1  1 
HETATM 6364 P P2  . A1BI4 C 3 .   ? -6.680  67.996  88.610  1.00 52.37  ?  901 A1BI4 A P2  1 
HETATM 6365 S S1  . A1BI4 C 3 .   ? -9.878  48.783  79.640  1.00 127.01 ?  901 A1BI4 A S1  1 
# 
