data_8UL8
# 
_entry.id   8UL8 
# 
_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   8UL8         pdb_00008ul8 10.2210/pdb8ul8/pdb 
WWPDB D_1000278345 ?            ?                   
# 
_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                        8UL8 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-16 
_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           Y 
# 
_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 
;methyl 3-{(1R,3S,3aS,13R)-8-[(2S,3S,4R)-5-{[(S)-{[(S)-{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-2,3,4-trihydroxypentyl]-1-hydroxy-10,11-dimethyl-4,6-dioxo-2,3,4,5,6,8-hexahydro-1H-benzo[g]pyrrolo[2,1-e]pteridin-3-yl}benzoate (non-preferred name)
;
977.761   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        
;methyl 3-{(1R,3S,3aS,13R)-8-[(2S,3S,4R)-5-{[(S)-{[(S)-{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-2,3,4-trihydroxypentyl]-1-hydroxy-10,11-dimethyl-4,6-dioxo-2,3,4,5,6,8-hexahydro-1H-benzo[g]pyrrolo[2,1-e]pteridin-3-yl}benzoate (non-preferred name)
;
_pdbx_entity_nonpoly.comp_id     XRK 
# 
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 
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 
XRK non-polymer         . 
;methyl 3-{(1R,3S,3aS,13R)-8-[(2S,3S,4R)-5-{[(S)-{[(S)-{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-2,3,4-trihydroxypentyl]-1-hydroxy-10,11-dimethyl-4,6-dioxo-2,3,4,5,6,8-hexahydro-1H-benzo[g]pyrrolo[2,1-e]pteridin-3-yl}benzoate (non-preferred name)
;
? 'C38 H45 N9 O18 P2' 977.761 
# 
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        XRK 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   XRK 
_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          XRK 
_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      XRK 
_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                     8UL8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     118.527 
_cell.length_a_esd                 ? 
_cell.length_b                     178.972 
_cell.length_b_esd                 ? 
_cell.length_c                     235.142 
_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                         8UL8 
_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                   8UL8 
_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             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_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            293 
# 
_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         2022-02-02 
_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   0.965459 
_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 ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.965459 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8UL8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.82 
_reflns.d_resolution_low                               48.54 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     58656 
_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                           97.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.84 
_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                                0.129 
_reflns.pdbx_Rpim_I_all                                0.072 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       170896 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.978 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.106 
_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                                    2.82 
_reflns_shell.d_res_low                                     2.90 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           14116 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4666 
_reflns_shell.percent_possible_obs                          99.6 
_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                               3.0 
_reflns_shell.pdbx_chi_squared                              0.61 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.8 
_reflns_shell.pdbx_Rrim_I_all                               1.804 
_reflns_shell.pdbx_Rpim_I_all                               0.998 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.303 
_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                                  1.489 
_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                                 8UL8 
_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                            2.82 
_refine.ls_d_res_low                             48.54 
_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                     58364 
_refine.ls_number_reflns_R_free                  1996 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.49 
_refine.ls_percent_reflns_R_free                 3.42 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2251 
_refine.ls_R_factor_R_free                       0.2473 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2243 
_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                 ? 
_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                            0.55 
_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                       2.82 
_refine_hist.d_res_low                        48.54 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               6360 
_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         67 
_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' ? 0.012  ? 6496 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.696  ? 8818 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.502 ? 917  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.080  ? 989  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 1140 ? 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' 2.82 2.89  . . 144 4059 98.00 . . . . 0.4695 . . . . . . . . . . . 0.5709 
'X-RAY DIFFRACTION' 2.89 2.97  . . 144 4045 99.00 . . . . 0.4173 . . . . . . . . . . . 0.4346 
'X-RAY DIFFRACTION' 2.97 3.06  . . 145 4045 98.00 . . . . 0.3637 . . . . . . . . . . . 0.4118 
'X-RAY DIFFRACTION' 3.06 3.15  . . 144 4089 99.00 . . . . 0.3237 . . . . . . . . . . . 0.3179 
'X-RAY DIFFRACTION' 3.15 3.27  . . 144 4074 98.00 . . . . 0.2990 . . . . . . . . . . . 0.3352 
'X-RAY DIFFRACTION' 3.27 3.40  . . 144 4077 98.00 . . . . 0.2748 . . . . . . . . . . . 0.2922 
'X-RAY DIFFRACTION' 3.40 3.55  . . 141 3963 96.00 . . . . 0.2748 . . . . . . . . . . . 0.2870 
'X-RAY DIFFRACTION' 3.55 3.74  . . 135 3867 93.00 . . . . 0.2457 . . . . . . . . . . . 0.2760 
'X-RAY DIFFRACTION' 3.74 3.97  . . 145 4079 97.00 . . . . 0.2202 . . . . . . . . . . . 0.2600 
'X-RAY DIFFRACTION' 3.97 4.28  . . 143 4066 98.00 . . . . 0.2031 . . . . . . . . . . . 0.2311 
'X-RAY DIFFRACTION' 4.28 4.71  . . 143 4056 97.00 . . . . 0.1806 . . . . . . . . . . . 0.2093 
'X-RAY DIFFRACTION' 4.71 5.39  . . 144 4043 96.00 . . . . 0.1890 . . . . . . . . . . . 0.2008 
'X-RAY DIFFRACTION' 5.39 6.79  . . 140 3968 94.00 . . . . 0.2030 . . . . . . . . . . . 0.2293 
'X-RAY DIFFRACTION' 6.79 48.54 . . 140 3937 90.00 . . . . 0.1693 . . . . . . . . . . . 0.1810 
# 
_struct.entry_id                     8UL8 
_struct.title                        'LSD1-CoREST in complex with T15, short soaking' 
_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        8UL8 
_struct_keywords.text            
'Epigenetics, Histone demethylase, Drug resistance, Covalent inhibitor, OXIDOREDUCTASE, OXIDOREDUCTASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
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 8UL8 A 20 ? 871 ? O60341 1   ? 852 ? 1   852 
2 2 8UL8 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 8UL8 GLY A 1  ? UNP O60341 ? ? 'expression tag' -18 1  
1 8UL8 SER A 2  ? UNP O60341 ? ? 'expression tag' -17 2  
1 8UL8 SER A 3  ? UNP O60341 ? ? 'expression tag' -16 3  
1 8UL8 HIS A 4  ? UNP O60341 ? ? 'expression tag' -15 4  
1 8UL8 HIS A 5  ? UNP O60341 ? ? 'expression tag' -14 5  
1 8UL8 HIS A 6  ? UNP O60341 ? ? 'expression tag' -13 6  
1 8UL8 HIS A 7  ? UNP O60341 ? ? 'expression tag' -12 7  
1 8UL8 HIS A 8  ? UNP O60341 ? ? 'expression tag' -11 8  
1 8UL8 HIS A 9  ? UNP O60341 ? ? 'expression tag' -10 9  
1 8UL8 SER A 10 ? UNP O60341 ? ? 'expression tag' -9  10 
1 8UL8 SER A 11 ? UNP O60341 ? ? 'expression tag' -8  11 
1 8UL8 GLY A 12 ? UNP O60341 ? ? 'expression tag' -7  12 
1 8UL8 LEU A 13 ? UNP O60341 ? ? 'expression tag' -6  13 
1 8UL8 VAL A 14 ? UNP O60341 ? ? 'expression tag' -5  14 
1 8UL8 PRO A 15 ? UNP O60341 ? ? 'expression tag' -4  15 
1 8UL8 ARG A 16 ? UNP O60341 ? ? 'expression tag' -3  16 
1 8UL8 GLY A 17 ? UNP O60341 ? ? 'expression tag' -2  17 
1 8UL8 SER A 18 ? UNP O60341 ? ? 'expression tag' -1  18 
1 8UL8 HIS A 19 ? UNP O60341 ? ? 'expression tag' 0   19 
2 8UL8 GLY B 1  ? UNP Q9UKL0 ? ? 'expression tag' 297 20 
2 8UL8 PRO B 2  ? UNP Q9UKL0 ? ? 'expression tag' 298 21 
2 8UL8 LEU B 3  ? UNP Q9UKL0 ? ? 'expression tag' 299 22 
2 8UL8 GLY B 4  ? UNP Q9UKL0 ? ? 'expression tag' 300 23 
2 8UL8 SER B 5  ? UNP Q9UKL0 ? ? 'expression tag' 301 24 
2 8UL8 PRO B 6  ? UNP Q9UKL0 ? ? 'expression tag' 302 25 
2 8UL8 GLU B 7  ? UNP Q9UKL0 ? ? 'expression tag' 303 26 
2 8UL8 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)' 5290  ? 
1 MORE         -40   ? 
1 'SSA (A^2)'  37720 ? 
# 
_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_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 ? GLY A 221 ? PHE A 196 GLY A 202 1 ? 7  
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 PRO A 260 ? SER A 263 ? PRO A 241 SER A 244 5 ? 4  
HELX_P HELX_P7  AA7 ASP A 264 ? HIS A 278 ? ASP A 245 HIS A 259 1 ? 15 
HELX_P HELX_P8  AA8 GLY A 306 ? PHE A 319 ? GLY A 287 PHE A 300 1 ? 14 
HELX_P HELX_P9  AA9 ASN A 359 ? VAL A 368 ? ASN A 340 VAL A 349 1 ? 10 
HELX_P HELX_P10 AB1 PRO A 390 ? GLN A 414 ? PRO A 371 GLN A 395 1 ? 25 
HELX_P HELX_P11 AB2 SER A 426 ? VAL A 487 ? SER A 407 VAL A 468 1 ? 62 
HELX_P HELX_P12 AB3 ASP A 492 ? GLU A 524 ? ASP A 473 GLU A 505 1 ? 33 
HELX_P HELX_P13 AB4 GLU A 525 ? ASN A 533 ? GLU A 506 ASN A 514 1 ? 9  
HELX_P HELX_P14 AB5 SER A 541 ? ASN A 559 ? SER A 522 ASN A 540 1 ? 19 
HELX_P HELX_P15 AB6 ASP A 574 ? GLU A 578 ? ASP A 555 GLU A 559 5 ? 5  
HELX_P HELX_P16 AB7 SER A 591 ? GLU A 599 ? SER A 572 GLU A 580 1 ? 9  
HELX_P HELX_P17 AB8 PRO A 645 ? LYS A 650 ? PRO A 626 LYS A 631 1 ? 6  
HELX_P HELX_P18 AB9 PRO A 663 ? MET A 673 ? PRO A 644 MET A 654 1 ? 11 
HELX_P HELX_P19 AC1 ALA A 727 ? MET A 734 ? ALA A 708 MET A 715 1 ? 8  
HELX_P HELX_P20 AC2 GLU A 735 ? ILE A 737 ? GLU A 716 ILE A 718 5 ? 3  
HELX_P HELX_P21 AC3 SER A 738 ? GLY A 755 ? SER A 719 GLY A 736 1 ? 18 
HELX_P HELX_P22 AC4 SER A 756 ? VAL A 759 ? SER A 737 VAL A 740 5 ? 4  
HELX_P HELX_P23 AC5 SER A 788 ? GLN A 797 ? SER A 769 GLN A 778 1 ? 10 
HELX_P HELX_P24 AC6 GLY A 819 ? ILE A 823 ? GLY A 800 ILE A 804 5 ? 5  
HELX_P HELX_P25 AC7 THR A 829 ? LEU A 849 ? THR A 810 LEU A 830 1 ? 21 
HELX_P HELX_P26 AC8 ALA A 851 ? LEU A 855 ? ALA A 832 LEU A 836 5 ? 5  
HELX_P HELX_P27 AC9 SER B 21  ? ALA B 30  ? SER B 317 ALA B 326 1 ? 10 
HELX_P HELX_P28 AD1 THR B 33  ? LEU B 67  ? THR B 329 LEU B 363 1 ? 35 
HELX_P HELX_P29 AD2 ILE B 71  ? ARG B 75  ? ILE B 367 ARG B 371 5 ? 5  
HELX_P HELX_P30 AD3 THR B 88  ? TYR B 102 ? THR B 384 TYR B 398 1 ? 15 
HELX_P HELX_P31 AD4 ASP B 105 ? GLY B 114 ? ASP B 401 GLY B 410 1 ? 10 
HELX_P HELX_P32 AD5 SER B 117 ? TYR B 128 ? SER B 413 TYR B 424 1 ? 12 
HELX_P HELX_P33 AD6 ASN B 133 ? GLU B 144 ? ASN B 429 GLU B 440 1 ? 12 
# 
_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 2.55  
2 PRO 489 A . ? PRO 470 A PRO 490 A ? PRO 471 A 1 -0.39 
3 GLN 652 A . ? GLN 633 A PRO 653 A ? PRO 634 A 1 -4.77 
4 VAL 659 A . ? VAL 640 A PRO 660 A ? PRO 641 A 1 -2.05 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
AA6 ? 5 ? 
# 
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 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? 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 THR A 632 ? CYS A 637 ? THR A 613 CYS A 618 
AA4 2 GLY A 618 ? ASN A 625 ? GLY A 599 ASN A 606 
AA4 3 THR A 607 ? THR A 615 ? THR A 588 THR A 596 
AA4 4 GLN A 657 ? VAL A 659 ? GLN A 638 VAL A 640 
AA5 1 GLY A 674 ? PHE A 675 ? GLY A 655 PHE A 656 
AA5 2 SER A 781 ? TYR A 782 ? SER A 762 TYR A 763 
AA6 1 LEU A 696 ? GLY A 698 ? LEU A 677 GLY A 679 
AA6 2 GLU A 709 ? ASN A 715 ? GLU A 690 ASN A 696 
AA6 3 ILE A 721 ? VAL A 726 ? ILE A 702 VAL A 707 
AA6 4 ASN A 679 ? CYS A 684 ? ASN A 660 CYS A 665 
AA6 5 GLU A 764 ? VAL A 767 ? GLU A 745 VAL A 748 
# 
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 O CYS A 637 ? O CYS A 618 N CYS A 619 ? N CYS A 600 
AA4 2 3 O ILE A 622 ? O ILE A 603 N ARG A 610 ? N ARG A 591 
AA4 3 4 N VAL A 612 ? N VAL A 593 O GLN A 657 ? O GLN A 638 
AA5 1 2 N GLY A 674 ? N GLY A 655 O TYR A 782 ? O TYR A 763 
AA6 1 2 N PHE A 697 ? N PHE A 678 O PHE A 713 ? O PHE A 694 
AA6 2 3 N TRP A 714 ? N TRP A 695 O LEU A 723 ? O LEU A 704 
AA6 3 4 O LEU A 722 ? O LEU A 703 N LEU A 683 ? N LEU A 664 
AA6 4 5 N VAL A 682 ? N VAL A 663 O VAL A 766 ? O VAL A 747 
# 
_pdbx_entry_details.entry_id                   8UL8 
_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 NH2 A ARG 384 ? ? O   B LYS 312 ? ? 2.12 
2 1 OE2 B GLU 368 ? ? NH1 B ARG 371 ? ? 2.13 
3 1 OD2 A ASP 583 ? ? NZ  A LYS 585 ? ? 2.14 
4 1 NH1 A ARG 316 ? ? O12 A XRK 901 ? ? 2.17 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA A LYS 268 ? ? CB A LYS 268 ? ? CG  A LYS 268 ? ? 134.46 113.40 21.06  2.20 N 
2 1 C  A VAL 468 ? ? N  A LYS 469 ? ? CA  A LYS 469 ? ? 101.70 121.70 -20.00 2.50 Y 
3 1 CA A LEU 704 ? ? CB A LEU 704 ? ? CG  A LEU 704 ? ? 131.64 115.30 16.34  2.30 N 
4 1 CB B LEU 342 ? ? CG B LEU 342 ? ? CD2 B LEU 342 ? ? 98.55  111.00 -12.45 1.70 N 
5 1 NE B ARG 347 ? ? CZ B ARG 347 ? ? NH2 B ARG 347 ? ? 116.51 120.30 -3.79  0.50 N 
6 1 CD B LYS 412 ? ? CE B LYS 412 ? ? NZ  B LYS 412 ? ? 97.74  111.70 -13.96 2.30 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 MET A 332 ? ? -141.05 -9.78  
2  1 THR A 335 ? ? -88.11  47.29  
3  1 THR A 542 ? ? -170.57 147.02 
4  1 ALA A 597 ? ? -58.79  -9.95  
5  1 ARG A 668 ? ? -176.29 147.48 
6  1 ALA A 757 ? ? -137.11 -56.40 
7  1 TYR A 807 ? ? -145.37 47.90  
8  1 TYR B 398 ? ? -130.35 -83.54 
9  1 ARG B 400 ? ? 76.39   -15.08 
10 1 TYR B 424 ? ? -92.28  32.82  
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
XRK C4   C Y N 388 
XRK C14  C N N 389 
XRK C5   C Y N 390 
XRK C6   C Y N 391 
XRK C11  C Y N 392 
XRK C7   C Y N 393 
XRK C8   C N S 394 
XRK C9   C N N 395 
XRK C10  C N R 396 
XRK C12  C Y N 397 
XRK C13  C Y N 398 
XRK N1   N N N 399 
XRK N2   N N N 400 
XRK C3   C Y N 401 
XRK N3   N Y N 402 
XRK C1   C N N 403 
XRK C15  C Y N 404 
XRK C16  C N N 405 
XRK C17  C Y N 406 
XRK C18  C Y N 407 
XRK C19  C N N 408 
XRK C2   C N N 409 
XRK C20  C N S 410 
XRK C21  C N S 411 
XRK C22  C N R 412 
XRK C23  C N N 413 
XRK C24  C N N 414 
XRK C25  C N R 415 
XRK C26  C N R 416 
XRK C27  C Y N 417 
XRK C28  C Y N 418 
XRK C29  C Y N 419 
XRK C30  C Y N 420 
XRK C31  C Y N 421 
XRK C32  C N R 422 
XRK C33  C N S 423 
XRK C34  C N N 424 
XRK C35  C N N 425 
XRK C36  C N N 426 
XRK C37  C N S 427 
XRK C38  C Y N 428 
XRK N4   N Y N 429 
XRK N5   N N N 430 
XRK N6   N Y N 431 
XRK N7   N Y N 432 
XRK N8   N N N 433 
XRK N9   N N N 434 
XRK O1   O N N 435 
XRK O10  O N N 436 
XRK O11  O N N 437 
XRK O12  O N N 438 
XRK O13  O N N 439 
XRK O14  O N N 440 
XRK O15  O N N 441 
XRK O16  O N N 442 
XRK O17  O N N 443 
XRK O18  O N N 444 
XRK O2   O N N 445 
XRK O3   O N N 446 
XRK O4   O N N 447 
XRK O5   O N N 448 
XRK O6   O N N 449 
XRK O7   O N N 450 
XRK O8   O N N 451 
XRK O9   O N N 452 
XRK P1   P N N 453 
XRK P2   P N N 454 
XRK H1   H N N 455 
XRK H2   H N N 456 
XRK H3   H N N 457 
XRK H4   H N N 458 
XRK H5   H N N 459 
XRK H6   H N N 460 
XRK H7   H N N 461 
XRK H8   H N N 462 
XRK H9   H N N 463 
XRK H10  H N N 464 
XRK H11  H N N 465 
XRK H12  H N N 466 
XRK H13  H N N 467 
XRK H14  H N N 468 
XRK H15  H N N 469 
XRK H16  H N N 470 
XRK H17  H N N 471 
XRK H18  H N N 472 
XRK H19  H N N 473 
XRK H20  H N N 474 
XRK H21  H N N 475 
XRK H22  H N N 476 
XRK H23  H N N 477 
XRK H24  H N N 478 
XRK H25  H N N 479 
XRK H26  H N N 480 
XRK H27  H N N 481 
XRK H28  H N N 482 
XRK H29  H N N 483 
XRK H30  H N N 484 
XRK H31  H N N 485 
XRK H32  H N N 486 
XRK H33  H N N 487 
XRK H35  H N N 488 
XRK H36  H N N 489 
XRK H37  H N N 490 
XRK H39  H N N 491 
XRK H40  H N N 492 
XRK H41  H N N 493 
XRK H42  H N N 494 
XRK H43  H N N 495 
XRK H44  H N N 496 
XRK H45  H N N 497 
XRK H46  H N N 498 
XRK H47  H N N 499 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
XRK C14 C13  sing N N 374 
XRK C13 C12  doub Y N 375 
XRK C13 C15  sing Y N 376 
XRK O3  C10  sing N N 377 
XRK C12 C11  sing Y N 378 
XRK C10 C9   sing N N 379 
XRK C10 N1   sing N N 380 
XRK C16 C15  sing N N 381 
XRK C9  C8   sing N N 382 
XRK C15 C17  doub Y N 383 
XRK C11 N1   sing N N 384 
XRK C11 C18  doub Y N 385 
XRK N1  C37  sing N N 386 
XRK O18 C36  doub N N 387 
XRK C8  C37  sing N N 388 
XRK C8  C7   sing N N 389 
XRK C17 C18  sing Y N 390 
XRK C18 N2   sing N N 391 
XRK C37 C36  sing N N 392 
XRK C37 C34  sing N N 393 
XRK C36 N9   sing N N 394 
XRK C7  C38  doub Y N 395 
XRK C7  C6   sing Y N 396 
XRK C38 C3   sing Y N 397 
XRK C6  C5   doub Y N 398 
XRK N2  C34  sing N N 399 
XRK N2  C19  sing N N 400 
XRK C34 N8   doub N N 401 
XRK N9  C35  sing N N 402 
XRK O2  C2   doub N N 403 
XRK C3  C4   doub Y N 404 
XRK C3  C2   sing N N 405 
XRK C5  C4   sing Y N 406 
XRK O4  C20  sing N N 407 
XRK C2  O1   sing N N 408 
XRK C19 C20  sing N N 409 
XRK N8  C35  sing N N 410 
XRK C35 O17  doub N N 411 
XRK C20 C21  sing N N 412 
XRK O1  C1   sing N N 413 
XRK O15 C32  sing N N 414 
XRK C21 O5   sing N N 415 
XRK C21 C22  sing N N 416 
XRK C32 C33  sing N N 417 
XRK C32 C26  sing N N 418 
XRK O12 P2   doub N N 419 
XRK O6  C22  sing N N 420 
XRK O16 C33  sing N N 421 
XRK C27 N4   doub Y N 422 
XRK C27 N3   sing Y N 423 
XRK C33 C25  sing N N 424 
XRK O11 P2   sing N N 425 
XRK N4  C28  sing Y N 426 
XRK C22 C23  sing N N 427 
XRK P2  O13  sing N N 428 
XRK P2  O10  sing N N 429 
XRK N3  C26  sing N N 430 
XRK N3  C31  sing Y N 431 
XRK C26 O14  sing N N 432 
XRK C28 C31  doub Y N 433 
XRK C28 C29  sing Y N 434 
XRK C23 O7   sing N N 435 
XRK N5  C29  sing N N 436 
XRK C31 N7   sing Y N 437 
XRK O13 C24  sing N N 438 
XRK C25 O14  sing N N 439 
XRK C25 C24  sing N N 440 
XRK C29 N6   doub Y N 441 
XRK O10 P1   sing N N 442 
XRK O7  P1   sing N N 443 
XRK N7  C30  doub Y N 444 
XRK N6  C30  sing Y N 445 
XRK P1  O9   doub N N 446 
XRK P1  O8   sing N N 447 
XRK C4  H1   sing N N 448 
XRK C14 H2   sing N N 449 
XRK C14 H3   sing N N 450 
XRK C14 H4   sing N N 451 
XRK C5  H5   sing N N 452 
XRK C6  H6   sing N N 453 
XRK C8  H7   sing N N 454 
XRK C9  H8   sing N N 455 
XRK C9  H9   sing N N 456 
XRK C10 H10  sing N N 457 
XRK C12 H11  sing N N 458 
XRK C1  H12  sing N N 459 
XRK C1  H13  sing N N 460 
XRK C1  H14  sing N N 461 
XRK C16 H15  sing N N 462 
XRK C16 H16  sing N N 463 
XRK C16 H17  sing N N 464 
XRK C17 H18  sing N N 465 
XRK C19 H19  sing N N 466 
XRK C19 H20  sing N N 467 
XRK C20 H21  sing N N 468 
XRK C21 H22  sing N N 469 
XRK C22 H23  sing N N 470 
XRK C23 H24  sing N N 471 
XRK C23 H25  sing N N 472 
XRK C24 H26  sing N N 473 
XRK C24 H27  sing N N 474 
XRK C25 H28  sing N N 475 
XRK C26 H29  sing N N 476 
XRK C27 H30  sing N N 477 
XRK C30 H31  sing N N 478 
XRK C32 H32  sing N N 479 
XRK C33 H33  sing N N 480 
XRK C38 H35  sing N N 481 
XRK N5  H36  sing N N 482 
XRK N5  H37  sing N N 483 
XRK N9  H39  sing N N 484 
XRK O11 H40  sing N N 485 
XRK O15 H41  sing N N 486 
XRK O16 H42  sing N N 487 
XRK O3  H43  sing N N 488 
XRK O4  H44  sing N N 489 
XRK O5  H45  sing N N 490 
XRK O6  H46  sing N N 491 
XRK O8  H47  sing N N 492 
# 
_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                    8UL8 
_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]   0.008437 
_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]   0.005587 
_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]   0.004253 
_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 ? -16.216 38.686  98.415  1.00 139.87 ?  171 PRO A N   1 
ATOM   2    C CA  . PRO A 1 190 ? -16.310 38.630  99.885  1.00 138.23 ?  171 PRO A CA  1 
ATOM   3    C C   . PRO A 1 190 ? -17.635 39.235  100.398 1.00 136.35 ?  171 PRO A C   1 
ATOM   4    O O   . PRO A 1 190 ? -18.106 40.227  99.812  1.00 132.32 ?  171 PRO A O   1 
ATOM   5    C CB  . PRO A 1 190 ? -15.093 39.456  100.352 1.00 118.72 ?  171 PRO A CB  1 
ATOM   6    C CG  . PRO A 1 190 ? -14.187 39.568  99.127  1.00 111.86 ?  171 PRO A CG  1 
ATOM   7    C CD  . PRO A 1 190 ? -15.143 39.590  97.961  1.00 118.98 ?  171 PRO A CD  1 
ATOM   8    N N   . SER A 1 191 ? -18.218 38.659  101.460 1.00 131.44 ?  172 SER A N   1 
ATOM   9    C CA  . SER A 1 191 ? -19.559 39.036  101.910 1.00 131.58 ?  172 SER A CA  1 
ATOM   10   C C   . SER A 1 191 ? -19.631 39.141  103.434 1.00 123.13 ?  172 SER A C   1 
ATOM   11   O O   . SER A 1 191 ? -18.798 38.594  104.169 1.00 120.11 ?  172 SER A O   1 
ATOM   12   C CB  . SER A 1 191 ? -20.623 38.039  101.394 1.00 132.65 ?  172 SER A CB  1 
ATOM   13   O OG  . SER A 1 191 ? -20.773 36.908  102.248 1.00 122.86 ?  172 SER A OG  1 
ATOM   14   N N   . GLY A 1 192 ? -20.658 39.855  103.900 1.00 112.19 ?  173 GLY A N   1 
ATOM   15   C CA  . GLY A 1 192 ? -20.897 40.014  105.322 1.00 116.27 ?  173 GLY A CA  1 
ATOM   16   C C   . GLY A 1 192 ? -20.209 41.235  105.901 1.00 111.40 ?  173 GLY A C   1 
ATOM   17   O O   . GLY A 1 192 ? -20.123 42.278  105.237 1.00 104.24 ?  173 GLY A O   1 
ATOM   18   N N   . VAL A 1 193 ? -19.727 41.130  107.146 1.00 109.37 ?  174 VAL A N   1 
ATOM   19   C CA  . VAL A 1 193 ? -18.899 42.209  107.671 1.00 98.12  ?  174 VAL A CA  1 
ATOM   20   C C   . VAL A 1 193 ? -17.550 42.202  106.970 1.00 97.76  ?  174 VAL A C   1 
ATOM   21   O O   . VAL A 1 193 ? -16.990 43.260  106.674 1.00 100.31 ?  174 VAL A O   1 
ATOM   22   C CB  . VAL A 1 193 ? -18.740 42.134  109.211 1.00 96.88  ?  174 VAL A CB  1 
ATOM   23   C CG1 . VAL A 1 193 ? -20.090 42.105  109.930 1.00 98.90  ?  174 VAL A CG1 1 
ATOM   24   C CG2 . VAL A 1 193 ? -17.786 41.021  109.675 1.00 96.11  ?  174 VAL A CG2 1 
ATOM   25   N N   . GLU A 1 194 ? -17.028 41.012  106.658 1.00 101.32 ?  175 GLU A N   1 
ATOM   26   C CA  . GLU A 1 194 ? -15.725 40.920  106.011 1.00 101.51 ?  175 GLU A CA  1 
ATOM   27   C C   . GLU A 1 194 ? -15.737 41.543  104.620 1.00 98.58  ?  175 GLU A C   1 
ATOM   28   O O   . GLU A 1 194 ? -14.689 41.970  104.122 1.00 94.08  ?  175 GLU A O   1 
ATOM   29   C CB  . GLU A 1 194 ? -15.288 39.459  105.921 1.00 106.64 ?  175 GLU A CB  1 
ATOM   30   C CG  . GLU A 1 194 ? -14.908 38.808  107.242 1.00 109.09 ?  175 GLU A CG  1 
ATOM   31   C CD  . GLU A 1 194 ? -15.171 37.296  107.237 1.00 119.48 ?  175 GLU A CD  1 
ATOM   32   O OE1 . GLU A 1 194 ? -14.526 36.565  106.437 1.00 115.93 ?  175 GLU A OE1 1 
ATOM   33   O OE2 . GLU A 1 194 ? -16.022 36.843  108.036 1.00 116.52 ?  175 GLU A OE2 1 
ATOM   34   N N   . GLY A 1 195 ? -16.898 41.590  103.968 1.00 100.24 ?  176 GLY A N   1 
ATOM   35   C CA  . GLY A 1 195 ? -16.969 42.244  102.675 1.00 99.14  ?  176 GLY A CA  1 
ATOM   36   C C   . GLY A 1 195 ? -16.797 43.742  102.800 1.00 91.88  ?  176 GLY A C   1 
ATOM   37   O O   . GLY A 1 195 ? -16.135 44.378  101.971 1.00 86.41  ?  176 GLY A O   1 
ATOM   38   N N   . ALA A 1 196 ? -17.375 44.324  103.852 1.00 95.94  ?  177 ALA A N   1 
ATOM   39   C CA  . ALA A 1 196 ? -17.247 45.761  104.064 1.00 87.25  ?  177 ALA A CA  1 
ATOM   40   C C   . ALA A 1 196 ? -15.793 46.162  104.277 1.00 77.20  ?  177 ALA A C   1 
ATOM   41   O O   . ALA A 1 196 ? -15.364 47.210  103.794 1.00 80.33  ?  177 ALA A O   1 
ATOM   42   C CB  . ALA A 1 196 ? -18.111 46.196  105.245 1.00 83.43  ?  177 ALA A CB  1 
ATOM   43   N N   . ALA A 1 197 ? -15.014 45.338  104.979 1.00 77.28  ?  178 ALA A N   1 
ATOM   44   C CA  . ALA A 1 197 ? -13.593 45.641  105.135 1.00 80.12  ?  178 ALA A CA  1 
ATOM   45   C C   . ALA A 1 197 ? -12.851 45.505  103.811 1.00 82.17  ?  178 ALA A C   1 
ATOM   46   O O   . ALA A 1 197 ? -11.930 46.281  103.517 1.00 77.67  ?  178 ALA A O   1 
ATOM   47   C CB  . ALA A 1 197 ? -12.961 44.742  106.196 1.00 78.66  ?  178 ALA A CB  1 
ATOM   48   N N   . PHE A 1 198 ? -13.227 44.519  103.001 1.00 82.97  ?  179 PHE A N   1 
ATOM   49   C CA  . PHE A 1 198 ? -12.605 44.389  101.693 1.00 80.84  ?  179 PHE A CA  1 
ATOM   50   C C   . PHE A 1 198 ? -12.995 45.566  100.798 1.00 76.92  ?  179 PHE A C   1 
ATOM   51   O O   . PHE A 1 198 ? -12.146 46.155  100.110 1.00 71.38  ?  179 PHE A O   1 
ATOM   52   C CB  . PHE A 1 198 ? -12.996 43.046  101.061 1.00 78.37  ?  179 PHE A CB  1 
ATOM   53   C CG  . PHE A 1 198 ? -12.657 42.955  99.614  1.00 74.91  ?  179 PHE A CG  1 
ATOM   54   C CD1 . PHE A 1 198 ? -11.388 42.558  99.217  1.00 70.06  ?  179 PHE A CD1 1 
ATOM   55   C CD2 . PHE A 1 198 ? -13.593 43.330  98.648  1.00 72.47  ?  179 PHE A CD2 1 
ATOM   56   C CE1 . PHE A 1 198 ? -11.059 42.505  97.884  1.00 70.38  ?  179 PHE A CE1 1 
ATOM   57   C CE2 . PHE A 1 198 ? -13.275 43.301  97.314  1.00 73.16  ?  179 PHE A CE2 1 
ATOM   58   C CZ  . PHE A 1 198 ? -12.007 42.879  96.920  1.00 77.34  ?  179 PHE A CZ  1 
ATOM   59   N N   . GLN A 1 199 ? -14.285 45.916  100.792 1.00 74.09  ?  180 GLN A N   1 
ATOM   60   C CA  . GLN A 1 199 ? -14.791 47.016  99.984  1.00 74.04  ?  180 GLN A CA  1 
ATOM   61   C C   . GLN A 1 199 ? -14.288 48.366  100.487 1.00 79.78  ?  180 GLN A C   1 
ATOM   62   O O   . GLN A 1 199 ? -14.486 49.390  99.821  1.00 82.35  ?  180 GLN A O   1 
ATOM   63   C CB  . GLN A 1 199 ? -16.325 46.930  99.967  1.00 78.27  ?  180 GLN A CB  1 
ATOM   64   C CG  . GLN A 1 199 ? -17.103 48.088  99.327  1.00 83.48  ?  180 GLN A CG  1 
ATOM   65   C CD  . GLN A 1 199 ? -16.725 48.320  97.874  1.00 84.19  ?  180 GLN A CD  1 
ATOM   66   O OE1 . GLN A 1 199 ? -16.423 47.378  97.149  1.00 83.23  ?  180 GLN A OE1 1 
ATOM   67   N NE2 . GLN A 1 199 ? -16.749 49.583  97.441  1.00 87.02  ?  180 GLN A NE2 1 
ATOM   68   N N   . SER A 1 200 ? -13.610 48.384  101.634 1.00 81.25  ?  181 SER A N   1 
ATOM   69   C CA  . SER A 1 200 ? -12.980 49.577  102.183 1.00 75.55  ?  181 SER A CA  1 
ATOM   70   C C   . SER A 1 200 ? -11.453 49.484  102.144 1.00 75.42  ?  181 SER A C   1 
ATOM   71   O O   . SER A 1 200 ? -10.766 50.219  102.859 1.00 79.83  ?  181 SER A O   1 
ATOM   72   C CB  . SER A 1 200 ? -13.481 49.807  103.613 1.00 74.82  ?  181 SER A CB  1 
ATOM   73   O OG  . SER A 1 200 ? -14.828 50.262  103.612 1.00 72.74  ?  181 SER A OG  1 
ATOM   74   N N   . ARG A 1 201 ? -10.914 48.575  101.332 1.00 74.06  ?  182 ARG A N   1 
ATOM   75   C CA  . ARG A 1 201 ? -9.472  48.383  101.175 1.00 66.36  ?  182 ARG A CA  1 
ATOM   76   C C   . ARG A 1 201 ? -8.784  48.124  102.519 1.00 71.10  ?  182 ARG A C   1 
ATOM   77   O O   . ARG A 1 201 ? -7.690  48.624  102.788 1.00 73.01  ?  182 ARG A O   1 
ATOM   78   C CB  . ARG A 1 201 ? -8.862  49.572  100.441 1.00 63.75  ?  182 ARG A CB  1 
ATOM   79   C CG  . ARG A 1 201 ? -9.631  49.923  99.170  1.00 64.71  ?  182 ARG A CG  1 
ATOM   80   C CD  . ARG A 1 201 ? -9.436  51.378  98.768  1.00 69.16  ?  182 ARG A CD  1 
ATOM   81   N NE  . ARG A 1 201 ? -10.063 52.320  99.704  1.00 79.23  ?  182 ARG A NE  1 
ATOM   82   C CZ  . ARG A 1 201 ? -11.359 52.641  99.704  1.00 80.25  ?  182 ARG A CZ  1 
ATOM   83   N NH1 . ARG A 1 201 ? -12.182 52.108  98.810  1.00 82.57  ?  182 ARG A NH1 1 
ATOM   84   N NH2 . ARG A 1 201 ? -11.834 53.506  100.591 1.00 79.94  ?  182 ARG A NH2 1 
ATOM   85   N N   . LEU A 1 202 ? -9.408  47.277  103.357 1.00 75.26  ?  183 LEU A N   1 
ATOM   86   C CA  . LEU A 1 202 ? -8.941  47.036  104.738 1.00 75.82  ?  183 LEU A CA  1 
ATOM   87   C C   . LEU A 1 202 ? -8.930  45.560  105.109 1.00 73.88  ?  183 LEU A C   1 
ATOM   88   O O   . LEU A 1 202 ? -9.955  44.879  104.935 1.00 82.66  ?  183 LEU A O   1 
ATOM   89   C CB  . LEU A 1 202 ? -9.844  47.781  105.716 1.00 79.28  ?  183 LEU A CB  1 
ATOM   90   C CG  . LEU A 1 202 ? -9.733  49.291  105.761 1.00 75.84  ?  183 LEU A CG  1 
ATOM   91   C CD1 . LEU A 1 202 ? -10.970 49.836  106.439 1.00 78.37  ?  183 LEU A CD1 1 
ATOM   92   C CD2 . LEU A 1 202 ? -8.479  49.662  106.504 1.00 78.63  ?  183 LEU A CD2 1 
ATOM   93   N N   . PRO A 1 203 ? -7.835  45.045  105.667 1.00 71.54  ?  184 PRO A N   1 
ATOM   94   C CA  . PRO A 1 203 ? -7.826  43.640  106.116 1.00 72.29  ?  184 PRO A CA  1 
ATOM   95   C C   . PRO A 1 203 ? -8.848  43.415  107.221 1.00 83.07  ?  184 PRO A C   1 
ATOM   96   O O   . PRO A 1 203 ? -8.780  44.033  108.283 1.00 86.97  ?  184 PRO A O   1 
ATOM   97   C CB  . PRO A 1 203 ? -6.391  43.435  106.620 1.00 77.96  ?  184 PRO A CB  1 
ATOM   98   C CG  . PRO A 1 203 ? -5.865  44.796  106.894 1.00 76.38  ?  184 PRO A CG  1 
ATOM   99   C CD  . PRO A 1 203 ? -6.570  45.741  105.955 1.00 68.83  ?  184 PRO A CD  1 
ATOM   100  N N   . HIS A 1 204 ? -9.804  42.513  106.968 1.00 89.08  ?  185 HIS A N   1 
ATOM   101  C CA  . HIS A 1 204 ? -10.906 42.311  107.910 1.00 85.90  ?  185 HIS A CA  1 
ATOM   102  C C   . HIS A 1 204 ? -10.458 41.688  109.221 1.00 84.87  ?  185 HIS A C   1 
ATOM   103  O O   . HIS A 1 204 ? -11.168 41.830  110.219 1.00 86.94  ?  185 HIS A O   1 
ATOM   104  C CB  . HIS A 1 204 ? -12.016 41.443  107.297 1.00 91.55  ?  185 HIS A CB  1 
ATOM   105  C CG  . HIS A 1 204 ? -11.607 40.024  107.034 1.00 98.42  ?  185 HIS A CG  1 
ATOM   106  N ND1 . HIS A 1 204 ? -11.407 39.103  108.041 1.00 92.13  ?  185 HIS A ND1 1 
ATOM   107  C CD2 . HIS A 1 204 ? -11.361 39.370  105.873 1.00 103.12 ?  185 HIS A CD2 1 
ATOM   108  C CE1 . HIS A 1 204 ? -11.042 37.950  107.513 1.00 94.69  ?  185 HIS A CE1 1 
ATOM   109  N NE2 . HIS A 1 204 ? -11.014 38.082  106.199 1.00 99.75  ?  185 HIS A NE2 1 
ATOM   110  N N   . ASP A 1 205 ? -9.306  41.014  109.254 1.00 87.29  ?  186 ASP A N   1 
ATOM   111  C CA  . ASP A 1 205 ? -8.881  40.276  110.441 1.00 91.04  ?  186 ASP A CA  1 
ATOM   112  C C   . ASP A 1 205 ? -7.599  40.835  111.044 1.00 88.46  ?  186 ASP A C   1 
ATOM   113  O O   . ASP A 1 205 ? -6.908  40.145  111.800 1.00 86.29  ?  186 ASP A O   1 
ATOM   114  C CB  . ASP A 1 205 ? -8.715  38.790  110.113 1.00 97.62  ?  186 ASP A CB  1 
ATOM   115  C CG  . ASP A 1 205 ? -7.670  38.527  109.024 1.00 103.49 ?  186 ASP A CG  1 
ATOM   116  O OD1 . ASP A 1 205 ? -7.690  37.406  108.454 1.00 105.70 ?  186 ASP A OD1 1 
ATOM   117  O OD2 . ASP A 1 205 ? -6.843  39.426  108.728 1.00 100.69 ?  186 ASP A OD2 1 
ATOM   118  N N   . ARG A 1 206 ? -7.259  42.070  110.709 1.00 92.08  ?  187 ARG A N   1 
ATOM   119  C CA  . ARG A 1 206 ? -6.011  42.672  111.144 1.00 92.90  ?  187 ARG A CA  1 
ATOM   120  C C   . ARG A 1 206 ? -6.259  44.156  111.366 1.00 90.21  ?  187 ARG A C   1 
ATOM   121  O O   . ARG A 1 206 ? -7.067  44.781  110.668 1.00 82.16  ?  187 ARG A O   1 
ATOM   122  C CB  . ARG A 1 206 ? -4.906  42.514  110.095 1.00 96.36  ?  187 ARG A CB  1 
ATOM   123  C CG  . ARG A 1 206 ? -4.420  41.106  109.794 1.00 105.67 ?  187 ARG A CG  1 
ATOM   124  C CD  . ARG A 1 206 ? -3.652  41.117  108.449 1.00 108.94 ?  187 ARG A CD  1 
ATOM   125  N NE  . ARG A 1 206 ? -2.959  42.397  108.272 1.00 117.29 ?  187 ARG A NE  1 
ATOM   126  C CZ  . ARG A 1 206 ? -1.811  42.730  108.868 1.00 121.05 ?  187 ARG A CZ  1 
ATOM   127  N NH1 . ARG A 1 206 ? -1.276  43.934  108.658 1.00 113.41 ?  187 ARG A NH1 1 
ATOM   128  N NH2 . ARG A 1 206 ? -1.199  41.869  109.682 1.00 110.77 ?  187 ARG A NH2 1 
ATOM   129  N N   . MET A 1 207 ? -5.548  44.717  112.332 1.00 88.52  ?  188 MET A N   1 
ATOM   130  C CA  . MET A 1 207 ? -5.496  46.162  112.477 1.00 84.08  ?  188 MET A CA  1 
ATOM   131  C C   . MET A 1 207 ? -4.467  46.741  111.517 1.00 81.06  ?  188 MET A C   1 
ATOM   132  O O   . MET A 1 207 ? -3.393  46.158  111.318 1.00 84.81  ?  188 MET A O   1 
ATOM   133  C CB  . MET A 1 207 ? -5.156  46.513  113.922 1.00 83.45  ?  188 MET A CB  1 
ATOM   134  C CG  . MET A 1 207 ? -6.319  46.267  114.880 1.00 84.17  ?  188 MET A CG  1 
ATOM   135  S SD  . MET A 1 207 ? -5.996  46.852  116.553 1.00 90.41  ?  188 MET A SD  1 
ATOM   136  C CE  . MET A 1 207 ? -6.059  48.640  116.361 1.00 85.44  ?  188 MET A CE  1 
ATOM   137  N N   . THR A 1 208 ? -4.807  47.879  110.899 1.00 76.44  ?  189 THR A N   1 
ATOM   138  C CA  . THR A 1 208 ? -3.863  48.532  109.993 1.00 76.86  ?  189 THR A CA  1 
ATOM   139  C C   . THR A 1 208 ? -2.873  49.391  110.772 1.00 74.01  ?  189 THR A C   1 
ATOM   140  O O   . THR A 1 208 ? -3.047  49.671  111.958 1.00 77.95  ?  189 THR A O   1 
ATOM   141  C CB  . THR A 1 208 ? -4.574  49.399  108.949 1.00 76.47  ?  189 THR A CB  1 
ATOM   142  O OG1 . THR A 1 208 ? -5.085  50.602  109.553 1.00 76.90  ?  189 THR A OG1 1 
ATOM   143  C CG2 . THR A 1 208 ? -5.699  48.630  108.293 1.00 70.23  ?  189 THR A CG2 1 
ATOM   144  N N   . SER A 1 209 ? -1.807  49.804  110.089 1.00 73.86  ?  190 SER A N   1 
ATOM   145  C CA  . SER A 1 209 ? -0.876  50.742  110.710 1.00 80.40  ?  190 SER A CA  1 
ATOM   146  C C   . SER A 1 209 ? -1.578  52.021  111.144 1.00 79.60  ?  190 SER A C   1 
ATOM   147  O O   . SER A 1 209 ? -1.244  52.597  112.192 1.00 74.03  ?  190 SER A O   1 
ATOM   148  C CB  . SER A 1 209 ? 0.267   51.074  109.749 1.00 82.23  ?  190 SER A CB  1 
ATOM   149  O OG  . SER A 1 209 ? 1.306   51.791  110.406 1.00 70.83  ?  190 SER A OG  1 
ATOM   150  N N   . GLN A 1 210 ? -2.556  52.481  110.366 1.00 77.93  ?  191 GLN A N   1 
ATOM   151  C CA  . GLN A 1 210 ? -3.273  53.683  110.772 1.00 80.61  ?  191 GLN A CA  1 
ATOM   152  C C   . GLN A 1 210 ? -4.062  53.462  112.060 1.00 76.86  ?  191 GLN A C   1 
ATOM   153  O O   . GLN A 1 210 ? -4.045  54.311  112.953 1.00 73.22  ?  191 GLN A O   1 
ATOM   154  C CB  . GLN A 1 210 ? -4.190  54.154  109.651 1.00 80.91  ?  191 GLN A CB  1 
ATOM   155  C CG  . GLN A 1 210 ? -4.943  55.367  110.057 1.00 85.45  ?  191 GLN A CG  1 
ATOM   156  C CD  . GLN A 1 210 ? -5.229  56.278  108.898 1.00 99.05  ?  191 GLN A CD  1 
ATOM   157  O OE1 . GLN A 1 210 ? -5.912  55.894  107.942 1.00 99.69  ?  191 GLN A OE1 1 
ATOM   158  N NE2 . GLN A 1 210 ? -4.677  57.499  108.956 1.00 101.30 ?  191 GLN A NE2 1 
ATOM   159  N N   . GLU A 1 211 ? -4.756  52.327  112.175 1.00 79.86  ?  192 GLU A N   1 
ATOM   160  C CA  . GLU A 1 211 ? -5.528  52.045  113.378 1.00 73.58  ?  192 GLU A CA  1 
ATOM   161  C C   . GLU A 1 211 ? -4.630  51.824  114.582 1.00 72.51  ?  192 GLU A C   1 
ATOM   162  O O   . GLU A 1 211 ? -5.003  52.173  115.703 1.00 74.74  ?  192 GLU A O   1 
ATOM   163  C CB  . GLU A 1 211 ? -6.425  50.836  113.153 1.00 73.10  ?  192 GLU A CB  1 
ATOM   164  C CG  . GLU A 1 211 ? -7.352  51.030  111.988 1.00 79.52  ?  192 GLU A CG  1 
ATOM   165  C CD  . GLU A 1 211 ? -7.960  49.745  111.424 1.00 85.95  ?  192 GLU A CD  1 
ATOM   166  O OE1 . GLU A 1 211 ? -9.102  49.874  110.930 1.00 86.71  ?  192 GLU A OE1 1 
ATOM   167  O OE2 . GLU A 1 211 ? -7.330  48.642  111.452 1.00 77.54  ?  192 GLU A OE2 1 
ATOM   168  N N   . ALA A 1 212 ? -3.449  51.249  114.387 1.00 73.19  ?  193 ALA A N   1 
ATOM   169  C CA  . ALA A 1 212 ? -2.498  51.198  115.487 1.00 72.18  ?  193 ALA A CA  1 
ATOM   170  C C   . ALA A 1 212 ? -2.224  52.596  116.026 1.00 73.07  ?  193 ALA A C   1 
ATOM   171  O O   . ALA A 1 212 ? -2.176  52.804  117.242 1.00 71.18  ?  193 ALA A O   1 
ATOM   172  C CB  . ALA A 1 212 ? -1.194  50.536  115.040 1.00 71.07  ?  193 ALA A CB  1 
ATOM   173  N N   . ALA A 1 213 ? -2.061  53.574  115.132 1.00 76.03  ?  194 ALA A N   1 
ATOM   174  C CA  . ALA A 1 213 ? -1.677  54.908  115.571 1.00 74.68  ?  194 ALA A CA  1 
ATOM   175  C C   . ALA A 1 213 ? -2.761  55.567  116.423 1.00 74.09  ?  194 ALA A C   1 
ATOM   176  O O   . ALA A 1 213 ? -2.440  56.290  117.374 1.00 73.84  ?  194 ALA A O   1 
ATOM   177  C CB  . ALA A 1 213 ? -1.342  55.772  114.363 1.00 76.72  ?  194 ALA A CB  1 
ATOM   178  N N   . CYS A 1 214 ? -4.037  55.315  116.121 1.00 70.91  ?  195 CYS A N   1 
ATOM   179  C CA  . CYS A 1 214 ? -5.137  55.912  116.870 1.00 78.03  ?  195 CYS A CA  1 
ATOM   180  C C   . CYS A 1 214 ? -5.625  55.051  118.034 1.00 79.81  ?  195 CYS A C   1 
ATOM   181  O O   . CYS A 1 214 ? -6.291  55.565  118.936 1.00 83.39  ?  195 CYS A O   1 
ATOM   182  C CB  . CYS A 1 214 ? -6.311  56.188  115.934 1.00 82.04  ?  195 CYS A CB  1 
ATOM   183  S SG  . CYS A 1 214 ? -5.833  56.995  114.386 1.00 96.87  ?  195 CYS A SG  1 
ATOM   184  N N   . PHE A 1 215 ? -5.326  53.756  118.037 1.00 76.42  ?  196 PHE A N   1 
ATOM   185  C CA  . PHE A 1 215 ? -5.774  52.861  119.100 1.00 67.47  ?  196 PHE A CA  1 
ATOM   186  C C   . PHE A 1 215 ? -4.596  52.062  119.652 1.00 71.62  ?  196 PHE A C   1 
ATOM   187  O O   . PHE A 1 215 ? -4.638  50.833  119.724 1.00 67.89  ?  196 PHE A O   1 
ATOM   188  C CB  . PHE A 1 215 ? -6.866  51.939  118.583 1.00 64.73  ?  196 PHE A CB  1 
ATOM   189  C CG  . PHE A 1 215 ? -8.046  52.658  117.975 1.00 72.28  ?  196 PHE A CG  1 
ATOM   190  C CD1 . PHE A 1 215 ? -8.015  53.100  116.661 1.00 75.91  ?  196 PHE A CD1 1 
ATOM   191  C CD2 . PHE A 1 215 ? -9.202  52.862  118.706 1.00 74.53  ?  196 PHE A CD2 1 
ATOM   192  C CE1 . PHE A 1 215 ? -9.110  53.749  116.097 1.00 78.06  ?  196 PHE A CE1 1 
ATOM   193  C CE2 . PHE A 1 215 ? -10.302 53.506  118.153 1.00 76.20  ?  196 PHE A CE2 1 
ATOM   194  C CZ  . PHE A 1 215 ? -10.258 53.946  116.849 1.00 79.65  ?  196 PHE A CZ  1 
ATOM   195  N N   . PRO A 1 216 ? -3.533  52.741  120.089 1.00 73.14  ?  197 PRO A N   1 
ATOM   196  C CA  . PRO A 1 216 ? -2.370  52.012  120.617 1.00 72.80  ?  197 PRO A CA  1 
ATOM   197  C C   . PRO A 1 216 ? -2.677  51.203  121.853 1.00 75.95  ?  197 PRO A C   1 
ATOM   198  O O   . PRO A 1 216 ? -1.974  50.217  122.105 1.00 80.91  ?  197 PRO A O   1 
ATOM   199  C CB  . PRO A 1 216 ? -1.356  53.124  120.918 1.00 73.47  ?  197 PRO A CB  1 
ATOM   200  C CG  . PRO A 1 216 ? -2.158  54.320  121.110 1.00 69.66  ?  197 PRO A CG  1 
ATOM   201  C CD  . PRO A 1 216 ? -3.423  54.193  120.313 1.00 67.65  ?  197 PRO A CD  1 
ATOM   202  N N   . ASP A 1 217 ? -3.670  51.608  122.651 1.00 78.03  ?  198 ASP A N   1 
ATOM   203  C CA  . ASP A 1 217 ? -4.238  50.724  123.671 1.00 80.36  ?  198 ASP A CA  1 
ATOM   204  C C   . ASP A 1 217 ? -4.727  49.396  123.083 1.00 80.36  ?  198 ASP A C   1 
ATOM   205  O O   . ASP A 1 217 ? -4.259  48.321  123.481 1.00 82.65  ?  198 ASP A O   1 
ATOM   206  C CB  . ASP A 1 217 ? -5.361  51.444  124.416 1.00 80.37  ?  198 ASP A CB  1 
ATOM   207  C CG  . ASP A 1 217 ? -6.332  52.138  123.475 1.00 85.83  ?  198 ASP A CG  1 
ATOM   208  O OD1 . ASP A 1 217 ? -6.004  52.277  122.282 1.00 81.88  ?  198 ASP A OD1 1 
ATOM   209  O OD2 . ASP A 1 217 ? -7.452  52.486  123.902 1.00 97.08  ?  198 ASP A OD2 1 
ATOM   210  N N   . ILE A 1 218 ? -5.664  49.450  122.130 1.00 74.01  ?  199 ILE A N   1 
ATOM   211  C CA  . ILE A 1 218 ? -6.282  48.231  121.607 1.00 74.09  ?  199 ILE A CA  1 
ATOM   212  C C   . ILE A 1 218 ? -5.233  47.272  121.041 1.00 80.40  ?  199 ILE A C   1 
ATOM   213  O O   . ILE A 1 218 ? -5.200  46.090  121.394 1.00 88.79  ?  199 ILE A O   1 
ATOM   214  C CB  . ILE A 1 218 ? -7.338  48.583  120.550 1.00 72.33  ?  199 ILE A CB  1 
ATOM   215  C CG1 . ILE A 1 218 ? -8.346  49.592  121.119 1.00 67.96  ?  199 ILE A CG1 1 
ATOM   216  C CG2 . ILE A 1 218 ? -7.937  47.317  119.939 1.00 72.13  ?  199 ILE A CG2 1 
ATOM   217  C CD1 . ILE A 1 218 ? -8.965  49.206  122.412 1.00 74.93  ?  199 ILE A CD1 1 
ATOM   218  N N   . ILE A 1 219 ? -4.358  47.763  120.163 1.00 82.63  ?  200 ILE A N   1 
ATOM   219  C CA  . ILE A 1 219 ? -3.492  46.854  119.414 1.00 81.28  ?  200 ILE A CA  1 
ATOM   220  C C   . ILE A 1 219 ? -2.355  46.294  120.275 1.00 79.10  ?  200 ILE A C   1 
ATOM   221  O O   . ILE A 1 219 ? -1.876  45.186  120.019 1.00 91.09  ?  200 ILE A O   1 
ATOM   222  C CB  . ILE A 1 219 ? -2.953  47.540  118.140 1.00 84.76  ?  200 ILE A CB  1 
ATOM   223  C CG1 . ILE A 1 219 ? -2.154  46.546  117.294 1.00 78.35  ?  200 ILE A CG1 1 
ATOM   224  C CG2 . ILE A 1 219 ? -2.098  48.780  118.473 1.00 79.33  ?  200 ILE A CG2 1 
ATOM   225  C CD1 . ILE A 1 219 ? -1.948  46.975  115.882 1.00 77.58  ?  200 ILE A CD1 1 
ATOM   226  N N   . SER A 1 220 ? -1.896  47.002  121.295 1.00 74.89  ?  201 SER A N   1 
ATOM   227  C CA  . SER A 1 220 ? -0.933  46.379  122.199 1.00 83.30  ?  201 SER A CA  1 
ATOM   228  C C   . SER A 1 220 ? -1.611  45.581  123.306 1.00 85.00  ?  201 SER A C   1 
ATOM   229  O O   . SER A 1 220 ? -0.915  44.949  124.112 1.00 81.34  ?  201 SER A O   1 
ATOM   230  C CB  . SER A 1 220 ? -0.016  47.428  122.828 1.00 82.84  ?  201 SER A CB  1 
ATOM   231  O OG  . SER A 1 220 ? -0.786  48.404  123.505 1.00 82.46  ?  201 SER A OG  1 
ATOM   232  N N   . GLY A 1 221 ? -2.946  45.606  123.354 1.00 84.26  ?  202 GLY A N   1 
ATOM   233  C CA  . GLY A 1 221 ? -3.715  44.929  124.368 1.00 90.21  ?  202 GLY A CA  1 
ATOM   234  C C   . GLY A 1 221 ? -4.006  43.482  124.028 1.00 97.25  ?  202 GLY A C   1 
ATOM   235  O O   . GLY A 1 221 ? -3.463  42.918  123.070 1.00 96.94  ?  202 GLY A O   1 
ATOM   236  N N   . PRO A 1 222 ? -4.860  42.848  124.837 1.00 102.16 ?  203 PRO A N   1 
ATOM   237  C CA  . PRO A 1 222 ? -5.205  41.438  124.603 1.00 101.78 ?  203 PRO A CA  1 
ATOM   238  C C   . PRO A 1 222 ? -5.952  41.205  123.291 1.00 104.46 ?  203 PRO A C   1 
ATOM   239  O O   . PRO A 1 222 ? -6.785  42.013  122.856 1.00 97.52  ?  203 PRO A O   1 
ATOM   240  C CB  . PRO A 1 222 ? -6.079  41.088  125.813 1.00 100.24 ?  203 PRO A CB  1 
ATOM   241  C CG  . PRO A 1 222 ? -6.552  42.426  126.354 1.00 94.86  ?  203 PRO A CG  1 
ATOM   242  C CD  . PRO A 1 222 ? -5.409  43.348  126.110 1.00 94.46  ?  203 PRO A CD  1 
ATOM   243  N N   . GLN A 1 223 ? -5.648  40.054  122.672 1.00 103.65 ?  204 GLN A N   1 
ATOM   244  C CA  . GLN A 1 223 ? -6.208  39.708  121.368 1.00 100.03 ?  204 GLN A CA  1 
ATOM   245  C C   . GLN A 1 223 ? -7.730  39.694  121.352 1.00 102.95 ?  204 GLN A C   1 
ATOM   246  O O   . GLN A 1 223 ? -8.329  39.764  120.273 1.00 98.41  ?  204 GLN A O   1 
ATOM   247  C CB  . GLN A 1 223 ? -5.695  38.346  120.916 1.00 104.45 ?  204 GLN A CB  1 
ATOM   248  C CG  . GLN A 1 223 ? -4.199  38.311  120.723 1.00 114.76 ?  204 GLN A CG  1 
ATOM   249  C CD  . GLN A 1 223 ? -3.788  38.622  119.285 1.00 119.70 ?  204 GLN A CD  1 
ATOM   250  O OE1 . GLN A 1 223 ? -4.633  38.775  118.387 1.00 105.57 ?  204 GLN A OE1 1 
ATOM   251  N NE2 . GLN A 1 223 ? -2.478  38.729  119.064 1.00 120.88 ?  204 GLN A NE2 1 
ATOM   252  N N   . GLN A 1 224 ? -8.380  39.589  122.510 1.00 109.50 ?  205 GLN A N   1 
ATOM   253  C CA  . GLN A 1 224 ? -9.834  39.565  122.456 1.00 109.83 ?  205 GLN A CA  1 
ATOM   254  C C   . GLN A 1 224 ? -10.380 40.948  122.151 1.00 105.01 ?  205 GLN A C   1 
ATOM   255  O O   . GLN A 1 224 ? -11.281 41.081  121.315 1.00 105.17 ?  205 GLN A O   1 
ATOM   256  C CB  . GLN A 1 224 ? -10.440 39.010  123.746 1.00 108.71 ?  205 GLN A CB  1 
ATOM   257  C CG  . GLN A 1 224 ? -11.949 38.714  123.605 1.00 114.50 ?  205 GLN A CG  1 
ATOM   258  C CD  . GLN A 1 224 ? -12.290 37.897  122.322 1.00 118.40 ?  205 GLN A CD  1 
ATOM   259  O OE1 . GLN A 1 224 ? -11.827 36.760  122.136 1.00 111.44 ?  205 GLN A OE1 1 
ATOM   260  N NE2 . GLN A 1 224 ? -13.130 38.476  121.457 1.00 115.76 ?  205 GLN A NE2 1 
ATOM   261  N N   . THR A 1 225 ? -9.822  41.989  122.783 1.00 103.48 ?  206 THR A N   1 
ATOM   262  C CA  . THR A 1 225 ? -10.282 43.348  122.492 1.00 105.81 ?  206 THR A CA  1 
ATOM   263  C C   . THR A 1 225 ? -10.133 43.663  121.006 1.00 96.86  ?  206 THR A C   1 
ATOM   264  O O   . THR A 1 225 ? -11.012 44.301  120.411 1.00 89.09  ?  206 THR A O   1 
ATOM   265  C CB  . THR A 1 225 ? -9.527  44.386  123.344 1.00 105.48 ?  206 THR A CB  1 
ATOM   266  O OG1 . THR A 1 225 ? -8.111  44.287  123.115 1.00 102.60 ?  206 THR A OG1 1 
ATOM   267  C CG2 . THR A 1 225 ? -9.825  44.187  124.852 1.00 98.55  ?  206 THR A CG2 1 
ATOM   268  N N   . GLN A 1 226 ? -9.053  43.170  120.380 1.00 97.02  ?  207 GLN A N   1 
ATOM   269  C CA  . GLN A 1 226 ? -8.809  43.453  118.965 1.00 92.50  ?  207 GLN A CA  1 
ATOM   270  C C   . GLN A 1 226 ? -9.951  42.944  118.083 1.00 91.97  ?  207 GLN A C   1 
ATOM   271  O O   . GLN A 1 226 ? -10.446 43.688  117.225 1.00 89.55  ?  207 GLN A O   1 
ATOM   272  C CB  . GLN A 1 226 ? -7.464  42.873  118.517 1.00 79.08  ?  207 GLN A CB  1 
ATOM   273  C CG  . GLN A 1 226 ? -6.301  43.205  119.436 1.00 82.90  ?  207 GLN A CG  1 
ATOM   274  C CD  . GLN A 1 226 ? -4.961  42.996  118.757 1.00 85.59  ?  207 GLN A CD  1 
ATOM   275  O OE1 . GLN A 1 226 ? -4.900  42.816  117.543 1.00 90.68  ?  207 GLN A OE1 1 
ATOM   276  N NE2 . GLN A 1 226 ? -3.882  42.990  119.536 1.00 82.14  ?  207 GLN A NE2 1 
ATOM   277  N N   . LYS A 1 227 ? -10.399 41.687  118.296 1.00 93.54  ?  208 LYS A N   1 
ATOM   278  C CA  . LYS A 1 227 ? -11.512 41.143  117.518 1.00 92.66  ?  208 LYS A CA  1 
ATOM   279  C C   . LYS A 1 227 ? -12.785 41.952  117.733 1.00 90.92  ?  208 LYS A C   1 
ATOM   280  O O   . LYS A 1 227 ? -13.613 42.082  116.817 1.00 87.13  ?  208 LYS A O   1 
ATOM   281  C CB  . LYS A 1 227 ? -11.786 39.682  117.878 1.00 100.84 ?  208 LYS A CB  1 
ATOM   282  C CG  . LYS A 1 227 ? -10.752 38.697  117.533 1.00 102.99 ?  208 LYS A CG  1 
ATOM   283  C CD  . LYS A 1 227 ? -11.358 37.314  117.699 1.00 106.59 ?  208 LYS A CD  1 
ATOM   284  C CE  . LYS A 1 227 ? -10.397 36.136  117.446 1.00 102.90 ?  208 LYS A CE  1 
ATOM   285  N NZ  . LYS A 1 227 ? -9.193  36.186  118.444 1.00 108.34 ?  208 LYS A NZ  1 
ATOM   286  N N   . VAL A 1 228 ? -12.982 42.462  118.953 1.00 92.48  ?  209 VAL A N   1 
ATOM   287  C CA  . VAL A 1 228 ? -14.142 43.307  119.222 1.00 95.31  ?  209 VAL A CA  1 
ATOM   288  C C   . VAL A 1 228 ? -14.059 44.544  118.347 1.00 94.09  ?  209 VAL A C   1 
ATOM   289  O O   . VAL A 1 228 ? -14.951 44.838  117.538 1.00 92.82  ?  209 VAL A O   1 
ATOM   290  C CB  . VAL A 1 228 ? -14.196 43.699  120.713 1.00 97.84  ?  209 VAL A CB  1 
ATOM   291  C CG1 . VAL A 1 228 ? -15.460 44.517  121.026 1.00 88.78  ?  209 VAL A CG1 1 
ATOM   292  C CG2 . VAL A 1 228 ? -13.965 42.495  121.651 1.00 97.95  ?  209 VAL A CG2 1 
ATOM   293  N N   . PHE A 1 229 ? -12.944 45.258  118.486 1.00 91.89  ?  210 PHE A N   1 
ATOM   294  C CA  . PHE A 1 229 ? -12.645 46.432  117.684 1.00 88.76  ?  210 PHE A CA  1 
ATOM   295  C C   . PHE A 1 229 ? -12.821 46.148  116.197 1.00 88.79  ?  210 PHE A C   1 
ATOM   296  O O   . PHE A 1 229 ? -13.569 46.846  115.498 1.00 83.88  ?  210 PHE A O   1 
ATOM   297  C CB  . PHE A 1 229 ? -11.210 46.867  117.980 1.00 86.41  ?  210 PHE A CB  1 
ATOM   298  C CG  . PHE A 1 229 ? -10.658 47.801  116.972 1.00 93.85  ?  210 PHE A CG  1 
ATOM   299  C CD1 . PHE A 1 229 ? -11.243 49.043  116.754 1.00 93.92  ?  210 PHE A CD1 1 
ATOM   300  C CD2 . PHE A 1 229 ? -9.616  47.396  116.150 1.00 95.26  ?  210 PHE A CD2 1 
ATOM   301  C CE1 . PHE A 1 229 ? -10.747 49.901  115.787 1.00 89.73  ?  210 PHE A CE1 1 
ATOM   302  C CE2 . PHE A 1 229 ? -9.127  48.236  115.164 1.00 92.00  ?  210 PHE A CE2 1 
ATOM   303  C CZ  . PHE A 1 229 ? -9.690  49.498  114.990 1.00 90.25  ?  210 PHE A CZ  1 
ATOM   304  N N   . LEU A 1 230 ? -12.124 45.112  115.703 1.00 87.37  ?  211 LEU A N   1 
ATOM   305  C CA  . LEU A 1 230 ? -12.181 44.783  114.284 1.00 81.78  ?  211 LEU A CA  1 
ATOM   306  C C   . LEU A 1 230 ? -13.614 44.548  113.838 1.00 84.85  ?  211 LEU A C   1 
ATOM   307  O O   . LEU A 1 230 ? -14.011 44.999  112.757 1.00 85.40  ?  211 LEU A O   1 
ATOM   308  C CB  . LEU A 1 230 ? -11.314 43.564  113.984 1.00 78.31  ?  211 LEU A CB  1 
ATOM   309  C CG  . LEU A 1 230 ? -9.804  43.748  114.120 1.00 81.40  ?  211 LEU A CG  1 
ATOM   310  C CD1 . LEU A 1 230 ? -9.038  42.438  114.055 1.00 80.38  ?  211 LEU A CD1 1 
ATOM   311  C CD2 . LEU A 1 230 ? -9.313  44.673  113.055 1.00 81.21  ?  211 LEU A CD2 1 
ATOM   312  N N   . PHE A 1 231 ? -14.416 43.865  114.668 1.00 88.16  ?  212 PHE A N   1 
ATOM   313  C CA  . PHE A 1 231 ? -15.822 43.667  114.320 1.00 90.11  ?  212 PHE A CA  1 
ATOM   314  C C   . PHE A 1 231 ? -16.577 44.992  114.316 1.00 87.35  ?  212 PHE A C   1 
ATOM   315  O O   . PHE A 1 231 ? -17.427 45.233  113.443 1.00 80.04  ?  212 PHE A O   1 
ATOM   316  C CB  . PHE A 1 231 ? -16.492 42.672  115.277 1.00 89.61  ?  212 PHE A CB  1 
ATOM   317  C CG  . PHE A 1 231 ? -17.982 42.530  115.043 1.00 94.88  ?  212 PHE A CG  1 
ATOM   318  C CD1 . PHE A 1 231 ? -18.898 43.284  115.768 1.00 100.45 ?  212 PHE A CD1 1 
ATOM   319  C CD2 . PHE A 1 231 ? -18.465 41.681  114.061 1.00 98.84  ?  212 PHE A CD2 1 
ATOM   320  C CE1 . PHE A 1 231 ? -20.268 43.175  115.528 1.00 103.05 ?  212 PHE A CE1 1 
ATOM   321  C CE2 . PHE A 1 231 ? -19.831 41.566  113.819 1.00 100.43 ?  212 PHE A CE2 1 
ATOM   322  C CZ  . PHE A 1 231 ? -20.731 42.315  114.552 1.00 103.29 ?  212 PHE A CZ  1 
ATOM   323  N N   . ILE A 1 232 ? -16.285 45.857  115.291 1.00 85.23  ?  213 ILE A N   1 
ATOM   324  C CA  . ILE A 1 232 ? -16.989 47.128  115.382 1.00 87.75  ?  213 ILE A CA  1 
ATOM   325  C C   . ILE A 1 232 ? -16.691 47.986  114.162 1.00 85.48  ?  213 ILE A C   1 
ATOM   326  O O   . ILE A 1 232 ? -17.599 48.576  113.566 1.00 82.14  ?  213 ILE A O   1 
ATOM   327  C CB  . ILE A 1 232 ? -16.615 47.854  116.679 1.00 90.67  ?  213 ILE A CB  1 
ATOM   328  C CG1 . ILE A 1 232 ? -16.937 46.975  117.882 1.00 86.51  ?  213 ILE A CG1 1 
ATOM   329  C CG2 . ILE A 1 232 ? -17.338 49.202  116.740 1.00 90.17  ?  213 ILE A CG2 1 
ATOM   330  C CD1 . ILE A 1 232 ? -16.286 47.452  119.152 1.00 87.62  ?  213 ILE A CD1 1 
ATOM   331  N N   . ARG A 1 233 ? -15.413 48.074  113.779 1.00 84.72  ?  214 ARG A N   1 
ATOM   332  C CA  . ARG A 1 233 ? -15.055 48.716  112.520 1.00 82.29  ?  214 ARG A CA  1 
ATOM   333  C C   . ARG A 1 233 ? -15.841 48.110  111.353 1.00 88.30  ?  214 ARG A C   1 
ATOM   334  O O   . ARG A 1 233 ? -16.566 48.819  110.635 1.00 84.57  ?  214 ARG A O   1 
ATOM   335  C CB  . ARG A 1 233 ? -13.543 48.609  112.262 1.00 79.45  ?  214 ARG A CB  1 
ATOM   336  C CG  . ARG A 1 233 ? -13.289 48.568  110.757 1.00 80.70  ?  214 ARG A CG  1 
ATOM   337  C CD  . ARG A 1 233 ? -11.938 48.940  110.206 1.00 82.61  ?  214 ARG A CD  1 
ATOM   338  N NE  . ARG A 1 233 ? -10.786 48.119  110.584 1.00 77.36  ?  214 ARG A NE  1 
ATOM   339  C CZ  . ARG A 1 233 ? -10.494 46.944  110.036 1.00 77.93  ?  214 ARG A CZ  1 
ATOM   340  N NH1 . ARG A 1 233 ? -11.308 46.402  109.141 1.00 80.61  ?  214 ARG A NH1 1 
ATOM   341  N NH2 . ARG A 1 233 ? -9.399  46.292  110.399 1.00 81.77  ?  214 ARG A NH2 1 
ATOM   342  N N   . ASN A 1 234 ? -15.711 46.786  111.155 1.00 87.75  ?  215 ASN A N   1 
ATOM   343  C CA  . ASN A 1 234 ? -16.311 46.148  109.986 1.00 80.23  ?  215 ASN A CA  1 
ATOM   344  C C   . ASN A 1 234 ? -17.822 46.314  109.993 1.00 85.87  ?  215 ASN A C   1 
ATOM   345  O O   . ASN A 1 234 ? -18.430 46.598  108.950 1.00 82.07  ?  215 ASN A O   1 
ATOM   346  C CB  . ASN A 1 234 ? -15.919 44.679  109.943 1.00 81.25  ?  215 ASN A CB  1 
ATOM   347  C CG  . ASN A 1 234 ? -14.422 44.488  109.850 1.00 85.39  ?  215 ASN A CG  1 
ATOM   348  O OD1 . ASN A 1 234 ? -13.703 45.416  109.495 1.00 87.59  ?  215 ASN A OD1 1 
ATOM   349  N ND2 . ASN A 1 234 ? -13.939 43.287  110.177 1.00 82.69  ?  215 ASN A ND2 1 
ATOM   350  N N   . ARG A 1 235 ? -18.438 46.186  111.178 1.00 89.55  ?  216 ARG A N   1 
ATOM   351  C CA  . ARG A 1 235 ? -19.881 46.360  111.297 1.00 90.61  ?  216 ARG A CA  1 
ATOM   352  C C   . ARG A 1 235 ? -20.299 47.782  110.939 1.00 87.01  ?  216 ARG A C   1 
ATOM   353  O O   . ARG A 1 235 ? -21.302 47.991  110.241 1.00 85.72  ?  216 ARG A O   1 
ATOM   354  C CB  . ARG A 1 235 ? -20.331 45.998  112.712 1.00 92.81  ?  216 ARG A CB  1 
ATOM   355  C CG  . ARG A 1 235 ? -21.849 45.949  112.891 1.00 99.74  ?  216 ARG A CG  1 
ATOM   356  C CD  . ARG A 1 235 ? -22.545 44.925  111.987 1.00 99.54  ?  216 ARG A CD  1 
ATOM   357  N NE  . ARG A 1 235 ? -23.998 45.103  112.034 1.00 99.34  ?  216 ARG A NE  1 
ATOM   358  C CZ  . ARG A 1 235 ? -24.755 45.399  110.977 1.00 101.15 ?  216 ARG A CZ  1 
ATOM   359  N NH1 . ARG A 1 235 ? -24.203 45.535  109.779 1.00 99.60  ?  216 ARG A NH1 1 
ATOM   360  N NH2 . ARG A 1 235 ? -26.068 45.557  111.111 1.00 97.54  ?  216 ARG A NH2 1 
ATOM   361  N N   . THR A 1 236 ? -19.535 48.774  111.396 1.00 86.36  ?  217 THR A N   1 
ATOM   362  C CA  . THR A 1 236 ? -19.861 50.159  111.070 1.00 85.97  ?  217 THR A CA  1 
ATOM   363  C C   . THR A 1 236 ? -19.710 50.415  109.580 1.00 88.16  ?  217 THR A C   1 
ATOM   364  O O   . THR A 1 236 ? -20.570 51.057  108.953 1.00 83.53  ?  217 THR A O   1 
ATOM   365  C CB  . THR A 1 236 ? -18.967 51.114  111.849 1.00 79.16  ?  217 THR A CB  1 
ATOM   366  O OG1 . THR A 1 236 ? -18.908 50.694  113.210 1.00 85.00  ?  217 THR A OG1 1 
ATOM   367  C CG2 . THR A 1 236 ? -19.533 52.511  111.792 1.00 81.98  ?  217 THR A CG2 1 
ATOM   368  N N   . LEU A 1 237 ? -18.601 49.932  108.998 1.00 87.88  ?  218 LEU A N   1 
ATOM   369  C CA  . LEU A 1 237 ? -18.376 50.106  107.567 1.00 83.09  ?  218 LEU A CA  1 
ATOM   370  C C   . LEU A 1 237 ? -19.526 49.523  106.769 1.00 88.09  ?  218 LEU A C   1 
ATOM   371  O O   . LEU A 1 237 ? -20.036 50.165  105.838 1.00 83.72  ?  218 LEU A O   1 
ATOM   372  C CB  . LEU A 1 237 ? -17.062 49.462  107.158 1.00 73.80  ?  218 LEU A CB  1 
ATOM   373  C CG  . LEU A 1 237 ? -15.823 50.047  107.797 1.00 77.22  ?  218 LEU A CG  1 
ATOM   374  C CD1 . LEU A 1 237 ? -14.719 49.050  107.728 1.00 76.97  ?  218 LEU A CD1 1 
ATOM   375  C CD2 . LEU A 1 237 ? -15.444 51.317  107.054 1.00 76.13  ?  218 LEU A CD2 1 
ATOM   376  N N   . GLN A 1 238 ? -19.958 48.307  107.147 1.00 85.27  ?  219 GLN A N   1 
ATOM   377  C CA  . GLN A 1 238 ? -21.122 47.686  106.528 1.00 86.93  ?  219 GLN A CA  1 
ATOM   378  C C   . GLN A 1 238 ? -22.313 48.631  106.533 1.00 92.35  ?  219 GLN A C   1 
ATOM   379  O O   . GLN A 1 238 ? -22.872 48.950  105.476 1.00 94.18  ?  219 GLN A O   1 
ATOM   380  C CB  . GLN A 1 238 ? -21.475 46.394  107.252 1.00 95.74  ?  219 GLN A CB  1 
ATOM   381  C CG  . GLN A 1 238 ? -22.425 45.491  106.470 1.00 102.59 ?  219 GLN A CG  1 
ATOM   382  C CD  . GLN A 1 238 ? -22.658 44.145  107.160 1.00 110.40 ?  219 GLN A CD  1 
ATOM   383  O OE1 . GLN A 1 238 ? -21.792 43.640  107.890 1.00 106.65 ?  219 GLN A OE1 1 
ATOM   384  N NE2 . GLN A 1 238 ? -23.823 43.552  106.913 1.00 112.89 ?  219 GLN A NE2 1 
ATOM   385  N N   . LEU A 1 239 ? -22.705 49.102  107.722 1.00 90.28  ?  220 LEU A N   1 
ATOM   386  C CA  . LEU A 1 239 ? -23.859 49.988  107.845 1.00 89.53  ?  220 LEU A CA  1 
ATOM   387  C C   . LEU A 1 239 ? -23.783 51.150  106.865 1.00 90.62  ?  220 LEU A C   1 
ATOM   388  O O   . LEU A 1 239 ? -24.761 51.462  106.172 1.00 92.02  ?  220 LEU A O   1 
ATOM   389  C CB  . LEU A 1 239 ? -23.954 50.493  109.281 1.00 91.57  ?  220 LEU A CB  1 
ATOM   390  C CG  . LEU A 1 239 ? -24.396 49.366  110.203 1.00 93.17  ?  220 LEU A CG  1 
ATOM   391  C CD1 . LEU A 1 239 ? -24.340 49.817  111.643 1.00 95.85  ?  220 LEU A CD1 1 
ATOM   392  C CD2 . LEU A 1 239 ? -25.796 48.911  109.821 1.00 94.24  ?  220 LEU A CD2 1 
ATOM   393  N N   . TRP A 1 240 ? -22.612 51.794  106.779 1.00 86.23  ?  221 TRP A N   1 
ATOM   394  C CA  . TRP A 1 240 ? -22.452 52.896  105.835 1.00 89.74  ?  221 TRP A CA  1 
ATOM   395  C C   . TRP A 1 240 ? -22.566 52.401  104.396 1.00 89.63  ?  221 TRP A C   1 
ATOM   396  O O   . TRP A 1 240 ? -23.247 53.012  103.558 1.00 86.45  ?  221 TRP A O   1 
ATOM   397  C CB  . TRP A 1 240 ? -21.106 53.595  106.067 1.00 85.74  ?  221 TRP A CB  1 
ATOM   398  C CG  . TRP A 1 240 ? -20.604 54.398  104.877 1.00 83.68  ?  221 TRP A CG  1 
ATOM   399  C CD1 . TRP A 1 240 ? -19.519 54.118  104.097 1.00 81.40  ?  221 TRP A CD1 1 
ATOM   400  C CD2 . TRP A 1 240 ? -21.177 55.598  104.340 1.00 83.75  ?  221 TRP A CD2 1 
ATOM   401  N NE1 . TRP A 1 240 ? -19.383 55.062  103.109 1.00 75.57  ?  221 TRP A NE1 1 
ATOM   402  C CE2 . TRP A 1 240 ? -20.391 55.977  103.233 1.00 78.84  ?  221 TRP A CE2 1 
ATOM   403  C CE3 . TRP A 1 240 ? -22.278 56.383  104.684 1.00 85.15  ?  221 TRP A CE3 1 
ATOM   404  C CZ2 . TRP A 1 240 ? -20.666 57.107  102.478 1.00 81.64  ?  221 TRP A CZ2 1 
ATOM   405  C CZ3 . TRP A 1 240 ? -22.549 57.504  103.927 1.00 87.17  ?  221 TRP A CZ3 1 
ATOM   406  C CH2 . TRP A 1 240 ? -21.746 57.856  102.839 1.00 84.59  ?  221 TRP A CH2 1 
ATOM   407  N N   . LEU A 1 241 ? -21.924 51.277  104.101 1.00 87.85  ?  222 LEU A N   1 
ATOM   408  C CA  . LEU A 1 241 ? -21.906 50.793  102.732 1.00 88.48  ?  222 LEU A CA  1 
ATOM   409  C C   . LEU A 1 241 ? -23.294 50.386  102.252 1.00 96.80  ?  222 LEU A C   1 
ATOM   410  O O   . LEU A 1 241 ? -23.596 50.526  101.055 1.00 92.82  ?  222 LEU A O   1 
ATOM   411  C CB  . LEU A 1 241 ? -20.931 49.635  102.617 1.00 83.27  ?  222 LEU A CB  1 
ATOM   412  C CG  . LEU A 1 241 ? -19.499 50.173  102.608 1.00 84.38  ?  222 LEU A CG  1 
ATOM   413  C CD1 . LEU A 1 241 ? -18.452 49.047  102.622 1.00 78.97  ?  222 LEU A CD1 1 
ATOM   414  C CD2 . LEU A 1 241 ? -19.299 51.155  101.448 1.00 77.45  ?  222 LEU A CD2 1 
ATOM   415  N N   . ASP A 1 242 ? -24.157 49.876  103.149 1.00 100.95 ?  223 ASP A N   1 
ATOM   416  C CA  . ASP A 1 242 ? -25.401 49.333  102.628 1.00 103.91 ?  223 ASP A CA  1 
ATOM   417  C C   . ASP A 1 242 ? -26.335 50.461  102.216 1.00 105.23 ?  223 ASP A C   1 
ATOM   418  O O   . ASP A 1 242 ? -27.205 50.276  101.352 1.00 111.20 ?  223 ASP A O   1 
ATOM   419  C CB  . ASP A 1 242 ? -26.094 48.420  103.642 1.00 107.08 ?  223 ASP A CB  1 
ATOM   420  C CG  . ASP A 1 242 ? -25.219 47.273  104.115 1.00 116.19 ?  223 ASP A CG  1 
ATOM   421  O OD1 . ASP A 1 242 ? -24.137 47.022  103.550 1.00 112.42 ?  223 ASP A OD1 1 
ATOM   422  O OD2 . ASP A 1 242 ? -25.691 46.533  105.021 1.00 119.33 ?  223 ASP A OD2 1 
ATOM   423  N N   . ASN A 1 243 ? -26.155 51.637  102.813 1.00 100.29 ?  224 ASN A N   1 
ATOM   424  C CA  . ASN A 1 243 ? -26.922 52.818  102.434 1.00 102.73 ?  224 ASN A CA  1 
ATOM   425  C C   . ASN A 1 243 ? -26.014 54.032  102.537 1.00 102.25 ?  224 ASN A C   1 
ATOM   426  O O   . ASN A 1 243 ? -25.910 54.666  103.594 1.00 103.32 ?  224 ASN A O   1 
ATOM   427  C CB  . ASN A 1 243 ? -28.164 52.976  103.306 1.00 101.86 ?  224 ASN A CB  1 
ATOM   428  C CG  . ASN A 1 243 ? -29.047 54.118  102.843 1.00 109.71 ?  224 ASN A CG  1 
ATOM   429  O OD1 . ASN A 1 243 ? -28.955 54.579  101.690 1.00 103.67 ?  224 ASN A OD1 1 
ATOM   430  N ND2 . ASN A 1 243 ? -29.906 54.593  103.740 1.00 111.92 ?  224 ASN A ND2 1 
ATOM   431  N N   . PRO A 1 244 ? -25.323 54.380  101.455 1.00 100.58 ?  225 PRO A N   1 
ATOM   432  C CA  . PRO A 1 244 ? -24.426 55.538  101.506 1.00 93.77  ?  225 PRO A CA  1 
ATOM   433  C C   . PRO A 1 244 ? -25.085 56.810  101.002 1.00 95.62  ?  225 PRO A C   1 
ATOM   434  O O   . PRO A 1 244 ? -24.382 57.744  100.607 1.00 94.26  ?  225 PRO A O   1 
ATOM   435  C CB  . PRO A 1 244 ? -23.270 55.120  100.589 1.00 88.94  ?  225 PRO A CB  1 
ATOM   436  C CG  . PRO A 1 244 ? -23.814 53.916  99.775  1.00 91.93  ?  225 PRO A CG  1 
ATOM   437  C CD  . PRO A 1 244 ? -25.247 53.709  100.151 1.00 97.08  ?  225 PRO A CD  1 
ATOM   438  N N   . LYS A 1 245 ? -26.418 56.871  100.972 1.00 96.00  ?  226 LYS A N   1 
ATOM   439  C CA  . LYS A 1 245 ? -27.080 58.118  100.604 1.00 98.80  ?  226 LYS A CA  1 
ATOM   440  C C   . LYS A 1 245 ? -27.520 58.940  101.819 1.00 100.33 ?  226 LYS A C   1 
ATOM   441  O O   . LYS A 1 245 ? -27.996 60.072  101.651 1.00 95.23  ?  226 LYS A O   1 
ATOM   442  C CB  . LYS A 1 245 ? -28.273 57.840  99.676  1.00 98.99  ?  226 LYS A CB  1 
ATOM   443  C CG  . LYS A 1 245 ? -27.861 57.360  98.282  1.00 95.67  ?  226 LYS A CG  1 
ATOM   444  C CD  . LYS A 1 245 ? -29.052 57.055  97.370  1.00 94.87  ?  226 LYS A CD  1 
ATOM   445  C CE  . LYS A 1 245 ? -29.562 58.320  96.679  1.00 100.76 ?  226 LYS A CE  1 
ATOM   446  N NZ  . LYS A 1 245 ? -29.989 58.085  95.266  1.00 106.43 ?  226 LYS A NZ  1 
ATOM   447  N N   . ILE A 1 246 ? -27.349 58.411  103.033 1.00 98.38  ?  227 ILE A N   1 
ATOM   448  C CA  . ILE A 1 246 ? -27.635 59.126  104.269 1.00 98.90  ?  227 ILE A CA  1 
ATOM   449  C C   . ILE A 1 246 ? -26.419 59.032  105.185 1.00 98.63  ?  227 ILE A C   1 
ATOM   450  O O   . ILE A 1 246 ? -25.658 58.059  105.143 1.00 98.11  ?  227 ILE A O   1 
ATOM   451  C CB  . ILE A 1 246 ? -28.894 58.571  104.982 1.00 102.21 ?  227 ILE A CB  1 
ATOM   452  C CG1 . ILE A 1 246 ? -28.614 57.175  105.561 1.00 100.11 ?  227 ILE A CG1 1 
ATOM   453  C CG2 . ILE A 1 246 ? -30.087 58.551  104.031 1.00 97.28  ?  227 ILE A CG2 1 
ATOM   454  C CD1 . ILE A 1 246 ? -29.619 56.720  106.598 1.00 105.24 ?  227 ILE A CD1 1 
ATOM   455  N N   . GLN A 1 247 ? -26.243 60.053  106.022 1.00 95.67  ?  228 GLN A N   1 
ATOM   456  C CA  . GLN A 1 247 ? -25.169 60.046  107.005 1.00 89.59  ?  228 GLN A CA  1 
ATOM   457  C C   . GLN A 1 247 ? -25.332 58.883  107.976 1.00 87.87  ?  228 GLN A C   1 
ATOM   458  O O   . GLN A 1 247 ? -26.443 58.445  108.272 1.00 92.55  ?  228 GLN A O   1 
ATOM   459  C CB  . GLN A 1 247 ? -25.157 61.370  107.765 1.00 98.52  ?  228 GLN A CB  1 
ATOM   460  C CG  . GLN A 1 247 ? -24.026 61.512  108.766 1.00 102.81 ?  228 GLN A CG  1 
ATOM   461  C CD  . GLN A 1 247 ? -24.088 62.811  109.550 1.00 98.38  ?  228 GLN A CD  1 
ATOM   462  O OE1 . GLN A 1 247 ? -25.004 63.616  109.376 1.00 97.56  ?  228 GLN A OE1 1 
ATOM   463  N NE2 . GLN A 1 247 ? -23.106 63.016  110.424 1.00 95.44  ?  228 GLN A NE2 1 
ATOM   464  N N   . LEU A 1 248 ? -24.213 58.370  108.466 1.00 84.95  ?  229 LEU A N   1 
ATOM   465  C CA  . LEU A 1 248 ? -24.220 57.339  109.499 1.00 89.29  ?  229 LEU A CA  1 
ATOM   466  C C   . LEU A 1 248 ? -23.774 57.962  110.815 1.00 93.88  ?  229 LEU A C   1 
ATOM   467  O O   . LEU A 1 248 ? -22.577 58.166  111.042 1.00 91.98  ?  229 LEU A O   1 
ATOM   468  C CB  . LEU A 1 248 ? -23.321 56.164  109.145 1.00 85.98  ?  229 LEU A CB  1 
ATOM   469  C CG  . LEU A 1 248 ? -23.749 54.927  109.939 1.00 88.14  ?  229 LEU A CG  1 
ATOM   470  C CD1 . LEU A 1 248 ? -24.935 54.215  109.275 1.00 91.14  ?  229 LEU A CD1 1 
ATOM   471  C CD2 . LEU A 1 248 ? -22.581 53.988  110.160 1.00 86.00  ?  229 LEU A CD2 1 
ATOM   472  N N   . THR A 1 249 ? -24.739 58.230  111.692 1.00 101.12 ?  230 THR A N   1 
ATOM   473  C CA  . THR A 1 249 ? -24.462 58.822  112.994 1.00 98.75  ?  230 THR A CA  1 
ATOM   474  C C   . THR A 1 249 ? -24.009 57.762  113.987 1.00 94.48  ?  230 THR A C   1 
ATOM   475  O O   . THR A 1 249 ? -24.314 56.575  113.854 1.00 96.60  ?  230 THR A O   1 
ATOM   476  C CB  . THR A 1 249 ? -25.697 59.512  113.559 1.00 99.59  ?  230 THR A CB  1 
ATOM   477  O OG1 . THR A 1 249 ? -26.716 58.525  113.796 1.00 97.53  ?  230 THR A OG1 1 
ATOM   478  C CG2 . THR A 1 249 ? -26.202 60.583  112.579 1.00 97.83  ?  230 THR A CG2 1 
ATOM   479  N N   . PHE A 1 250 ? -23.274 58.220  115.001 1.00 93.27  ?  231 PHE A N   1 
ATOM   480  C CA  . PHE A 1 250 ? -22.843 57.333  116.078 1.00 93.79  ?  231 PHE A CA  1 
ATOM   481  C C   . PHE A 1 250 ? -24.036 56.656  116.738 1.00 100.47 ?  231 PHE A C   1 
ATOM   482  O O   . PHE A 1 250 ? -23.984 55.465  117.071 1.00 99.44  ?  231 PHE A O   1 
ATOM   483  C CB  . PHE A 1 250 ? -22.036 58.135  117.099 1.00 88.09  ?  231 PHE A CB  1 
ATOM   484  C CG  . PHE A 1 250 ? -21.815 57.430  118.395 1.00 90.45  ?  231 PHE A CG  1 
ATOM   485  C CD1 . PHE A 1 250 ? -21.329 56.131  118.429 1.00 93.32  ?  231 PHE A CD1 1 
ATOM   486  C CD2 . PHE A 1 250 ? -22.083 58.073  119.591 1.00 92.77  ?  231 PHE A CD2 1 
ATOM   487  C CE1 . PHE A 1 250 ? -21.135 55.479  119.640 1.00 95.84  ?  231 PHE A CE1 1 
ATOM   488  C CE2 . PHE A 1 250 ? -21.878 57.434  120.802 1.00 89.60  ?  231 PHE A CE2 1 
ATOM   489  C CZ  . PHE A 1 250 ? -21.405 56.137  120.833 1.00 91.65  ?  231 PHE A CZ  1 
ATOM   490  N N   . GLU A 1 251 ? -25.127 57.402  116.922 1.00 104.31 ?  232 GLU A N   1 
ATOM   491  C CA  . GLU A 1 251 ? -26.332 56.837  117.513 1.00 101.37 ?  232 GLU A CA  1 
ATOM   492  C C   . GLU A 1 251 ? -26.893 55.727  116.632 1.00 103.69 ?  232 GLU A C   1 
ATOM   493  O O   . GLU A 1 251 ? -27.040 54.582  117.080 1.00 107.41 ?  232 GLU A O   1 
ATOM   494  C CB  . GLU A 1 251 ? -27.373 57.936  117.760 1.00 102.50 ?  232 GLU A CB  1 
ATOM   495  C CG  . GLU A 1 251 ? -26.932 59.101  118.689 1.00 110.98 ?  232 GLU A CG  1 
ATOM   496  C CD  . GLU A 1 251 ? -25.804 60.015  118.141 1.00 116.98 ?  232 GLU A CD  1 
ATOM   497  O OE1 . GLU A 1 251 ? -25.225 60.794  118.943 1.00 113.56 ?  232 GLU A OE1 1 
ATOM   498  O OE2 . GLU A 1 251 ? -25.513 59.984  116.916 1.00 113.86 ?  232 GLU A OE2 1 
ATOM   499  N N   . ALA A 1 252 ? -27.186 56.045  115.361 1.00 103.24 ?  233 ALA A N   1 
ATOM   500  C CA  . ALA A 1 252 ? -27.646 55.024  114.418 1.00 102.97 ?  233 ALA A CA  1 
ATOM   501  C C   . ALA A 1 252 ? -26.732 53.799  114.436 1.00 99.24  ?  233 ALA A C   1 
ATOM   502  O O   . ALA A 1 252 ? -27.199 52.658  114.334 1.00 97.04  ?  233 ALA A O   1 
ATOM   503  C CB  . ALA A 1 252 ? -27.736 55.615  113.006 1.00 97.94  ?  233 ALA A CB  1 
ATOM   504  N N   . THR A 1 253 ? -25.428 54.023  114.602 1.00 99.34  ?  234 THR A N   1 
ATOM   505  C CA  . THR A 1 253 ? -24.461 52.934  114.587 1.00 98.99  ?  234 THR A CA  1 
ATOM   506  C C   . THR A 1 253 ? -24.621 52.055  115.816 1.00 103.28 ?  234 THR A C   1 
ATOM   507  O O   . THR A 1 253 ? -24.941 50.864  115.708 1.00 105.69 ?  234 THR A O   1 
ATOM   508  C CB  . THR A 1 253 ? -23.037 53.499  114.519 1.00 95.44  ?  234 THR A CB  1 
ATOM   509  O OG1 . THR A 1 253 ? -22.889 54.304  113.345 1.00 97.75  ?  234 THR A OG1 1 
ATOM   510  C CG2 . THR A 1 253 ? -22.015 52.378  114.469 1.00 92.83  ?  234 THR A CG2 1 
ATOM   511  N N   . LEU A 1 254 ? -24.388 52.639  116.999 1.00 107.43 ?  235 LEU A N   1 
ATOM   512  C CA  . LEU A 1 254 ? -24.476 51.906  118.262 1.00 107.86 ?  235 LEU A CA  1 
ATOM   513  C C   . LEU A 1 254 ? -25.808 51.196  118.406 1.00 109.46 ?  235 LEU A C   1 
ATOM   514  O O   . LEU A 1 254 ? -25.890 50.145  119.056 1.00 110.60 ?  235 LEU A O   1 
ATOM   515  C CB  . LEU A 1 254 ? -24.268 52.868  119.441 1.00 102.53 ?  235 LEU A CB  1 
ATOM   516  C CG  . LEU A 1 254 ? -24.286 52.294  120.857 1.00 96.62  ?  235 LEU A CG  1 
ATOM   517  C CD1 . LEU A 1 254 ? -23.300 51.152  120.981 1.00 101.57 ?  235 LEU A CD1 1 
ATOM   518  C CD2 . LEU A 1 254 ? -23.942 53.381  121.846 1.00 93.33  ?  235 LEU A CD2 1 
ATOM   519  N N   . GLN A 1 255 ? -26.861 51.743  117.795 1.00 109.63 ?  236 GLN A N   1 
ATOM   520  C CA  . GLN A 1 255 ? -28.164 51.109  117.917 1.00 112.37 ?  236 GLN A CA  1 
ATOM   521  C C   . GLN A 1 255 ? -28.185 49.741  117.245 1.00 114.37 ?  236 GLN A C   1 
ATOM   522  O O   . GLN A 1 255 ? -28.799 48.802  117.769 1.00 117.15 ?  236 GLN A O   1 
ATOM   523  C CB  . GLN A 1 255 ? -29.260 52.019  117.358 1.00 110.40 ?  236 GLN A CB  1 
ATOM   524  C CG  . GLN A 1 255 ? -30.655 51.539  117.749 1.00 122.73 ?  236 GLN A CG  1 
ATOM   525  C CD  . GLN A 1 255 ? -30.787 51.191  119.254 1.00 134.48 ?  236 GLN A CD  1 
ATOM   526  O OE1 . GLN A 1 255 ? -30.101 51.764  120.118 1.00 131.54 ?  236 GLN A OE1 1 
ATOM   527  N NE2 . GLN A 1 255 ? -31.646 50.215  119.557 1.00 128.08 ?  236 GLN A NE2 1 
ATOM   528  N N   . GLN A 1 256 ? -27.497 49.589  116.111 1.00 112.02 ?  237 GLN A N   1 
ATOM   529  C CA  . GLN A 1 256 ? -27.682 48.367  115.345 1.00 107.33 ?  237 GLN A CA  1 
ATOM   530  C C   . GLN A 1 256 ? -26.609 47.337  115.664 1.00 108.90 ?  237 GLN A C   1 
ATOM   531  O O   . GLN A 1 256 ? -26.758 46.164  115.303 1.00 107.81 ?  237 GLN A O   1 
ATOM   532  C CB  . GLN A 1 256 ? -27.708 48.652  113.854 1.00 96.45  ?  237 GLN A CB  1 
ATOM   533  C CG  . GLN A 1 256 ? -28.680 49.754  113.527 1.00 105.82 ?  237 GLN A CG  1 
ATOM   534  C CD  . GLN A 1 256 ? -28.975 49.896  112.059 1.00 111.23 ?  237 GLN A CD  1 
ATOM   535  O OE1 . GLN A 1 256 ? -28.583 49.044  111.256 1.00 115.48 ?  237 GLN A OE1 1 
ATOM   536  N NE2 . GLN A 1 256 ? -29.472 51.075  111.678 1.00 107.33 ?  237 GLN A NE2 1 
ATOM   537  N N   . LEU A 1 257 ? -25.542 47.750  116.344 1.00 107.17 ?  238 LEU A N   1 
ATOM   538  C CA  . LEU A 1 257 ? -24.682 46.805  117.038 1.00 114.61 ?  238 LEU A CA  1 
ATOM   539  C C   . LEU A 1 257 ? -25.450 46.074  118.134 1.00 121.97 ?  238 LEU A C   1 
ATOM   540  O O   . LEU A 1 257 ? -26.277 46.663  118.842 1.00 121.41 ?  238 LEU A O   1 
ATOM   541  C CB  . LEU A 1 257 ? -23.494 47.526  117.659 1.00 114.12 ?  238 LEU A CB  1 
ATOM   542  C CG  . LEU A 1 257 ? -22.296 47.801  116.771 1.00 108.56 ?  238 LEU A CG  1 
ATOM   543  C CD1 . LEU A 1 257 ? -21.364 48.677  117.539 1.00 110.65 ?  238 LEU A CD1 1 
ATOM   544  C CD2 . LEU A 1 257 ? -21.606 46.506  116.404 1.00 111.00 ?  238 LEU A CD2 1 
ATOM   545  N N   . GLU A 1 258 ? -25.150 44.784  118.287 1.00 120.92 ?  239 GLU A N   1 
ATOM   546  C CA  . GLU A 1 258 ? -25.689 43.986  119.375 1.00 119.44 ?  239 GLU A CA  1 
ATOM   547  C C   . GLU A 1 258 ? -24.565 43.633  120.348 1.00 120.30 ?  239 GLU A C   1 
ATOM   548  O O   . GLU A 1 258 ? -23.370 43.691  120.019 1.00 121.28 ?  239 GLU A O   1 
ATOM   549  C CB  . GLU A 1 258 ? -26.401 42.731  118.849 1.00 120.43 ?  239 GLU A CB  1 
ATOM   550  C CG  . GLU A 1 258 ? -27.636 43.074  117.972 1.00 128.48 ?  239 GLU A CG  1 
ATOM   551  C CD  . GLU A 1 258 ? -28.441 41.895  117.552 1.00 138.13 ?  239 GLU A CD  1 
ATOM   552  O OE1 . GLU A 1 258 ? -28.018 40.757  117.847 1.00 136.18 ?  239 GLU A OE1 1 
ATOM   553  O OE2 . GLU A 1 258 ? -29.393 42.079  116.730 1.00 134.35 ?  239 GLU A OE2 1 
ATOM   554  N N   . ALA A 1 259 ? -24.969 43.312  121.579 1.00 116.12 ?  240 ALA A N   1 
ATOM   555  C CA  . ALA A 1 259 ? -24.019 42.925  122.598 1.00 110.08 ?  240 ALA A CA  1 
ATOM   556  C C   . ALA A 1 259 ? -23.313 41.641  122.172 1.00 109.37 ?  240 ALA A C   1 
ATOM   557  O O   . ALA A 1 259 ? -23.832 40.882  121.351 1.00 108.77 ?  240 ALA A O   1 
ATOM   558  C CB  . ALA A 1 259 ? -24.729 42.738  123.935 1.00 107.61 ?  240 ALA A CB  1 
ATOM   559  N N   . PRO A 1 260 ? -22.106 41.382  122.699 1.00 109.06 ?  241 PRO A N   1 
ATOM   560  C CA  . PRO A 1 260 ? -21.332 42.133  123.698 1.00 108.52 ?  241 PRO A CA  1 
ATOM   561  C C   . PRO A 1 260 ? -20.676 43.395  123.129 1.00 110.66 ?  241 PRO A C   1 
ATOM   562  O O   . PRO A 1 260 ? -19.995 44.142  123.840 1.00 102.62 ?  241 PRO A O   1 
ATOM   563  C CB  . PRO A 1 260 ? -20.271 41.119  124.123 1.00 105.98 ?  241 PRO A CB  1 
ATOM   564  C CG  . PRO A 1 260 ? -19.995 40.349  122.857 1.00 102.66 ?  241 PRO A CG  1 
ATOM   565  C CD  . PRO A 1 260 ? -21.335 40.243  122.157 1.00 102.30 ?  241 PRO A CD  1 
ATOM   566  N N   . TYR A 1 261 ? -20.902 43.622  121.833 1.00 114.94 ?  242 TYR A N   1 
ATOM   567  C CA  . TYR A 1 261 ? -20.138 44.632  121.112 1.00 115.56 ?  242 TYR A CA  1 
ATOM   568  C C   . TYR A 1 261 ? -20.603 46.047  121.446 1.00 116.11 ?  242 TYR A C   1 
ATOM   569  O O   . TYR A 1 261 ? -19.777 46.969  121.489 1.00 110.54 ?  242 TYR A O   1 
ATOM   570  C CB  . TYR A 1 261 ? -20.207 44.347  119.607 1.00 110.92 ?  242 TYR A CB  1 
ATOM   571  C CG  . TYR A 1 261 ? -19.596 43.008  119.238 1.00 107.59 ?  242 TYR A CG  1 
ATOM   572  C CD1 . TYR A 1 261 ? -18.224 42.794  119.357 1.00 106.09 ?  242 TYR A CD1 1 
ATOM   573  C CD2 . TYR A 1 261 ? -20.386 41.955  118.783 1.00 110.92 ?  242 TYR A CD2 1 
ATOM   574  C CE1 . TYR A 1 261 ? -17.647 41.568  119.022 1.00 106.51 ?  242 TYR A CE1 1 
ATOM   575  C CE2 . TYR A 1 261 ? -19.819 40.717  118.443 1.00 110.25 ?  242 TYR A CE2 1 
ATOM   576  C CZ  . TYR A 1 261 ? -18.447 40.530  118.564 1.00 109.62 ?  242 TYR A CZ  1 
ATOM   577  O OH  . TYR A 1 261 ? -17.877 39.309  118.230 1.00 104.01 ?  242 TYR A OH  1 
ATOM   578  N N   . ASN A 1 262 ? -21.899 46.242  121.715 1.00 117.14 ?  243 ASN A N   1 
ATOM   579  C CA  . ASN A 1 262 ? -22.406 47.548  122.122 1.00 114.35 ?  243 ASN A CA  1 
ATOM   580  C C   . ASN A 1 262 ? -22.324 47.772  123.632 1.00 108.04 ?  243 ASN A C   1 
ATOM   581  O O   . ASN A 1 262 ? -22.999 48.668  124.149 1.00 103.90 ?  243 ASN A O   1 
ATOM   582  C CB  . ASN A 1 262 ? -23.846 47.755  121.627 1.00 112.44 ?  243 ASN A CB  1 
ATOM   583  C CG  . ASN A 1 262 ? -24.853 46.823  122.285 1.00 113.91 ?  243 ASN A CG  1 
ATOM   584  O OD1 . ASN A 1 262 ? -24.509 45.985  123.122 1.00 112.03 ?  243 ASN A OD1 1 
ATOM   585  N ND2 . ASN A 1 262 ? -26.120 46.978  121.907 1.00 112.30 ?  243 ASN A ND2 1 
ATOM   586  N N   . SER A 1 263 ? -21.507 46.982  124.342 1.00 110.14 ?  244 SER A N   1 
ATOM   587  C CA  . SER A 1 263 ? -21.368 47.136  125.790 1.00 112.89 ?  244 SER A CA  1 
ATOM   588  C C   . SER A 1 263 ? -20.499 48.332  126.157 1.00 110.11 ?  244 SER A C   1 
ATOM   589  O O   . SER A 1 263 ? -20.740 48.982  127.185 1.00 110.09 ?  244 SER A O   1 
ATOM   590  C CB  . SER A 1 263 ? -20.783 45.864  126.414 1.00 112.16 ?  244 SER A CB  1 
ATOM   591  O OG  . SER A 1 263 ? -19.362 45.885  126.405 1.00 108.21 ?  244 SER A OG  1 
ATOM   592  N N   . ASP A 1 264 ? -19.491 48.631  125.338 1.00 110.11 ?  245 ASP A N   1 
ATOM   593  C CA  . ASP A 1 264 ? -18.617 49.780  125.544 1.00 105.06 ?  245 ASP A CA  1 
ATOM   594  C C   . ASP A 1 264 ? -19.021 50.881  124.570 1.00 98.53  ?  245 ASP A C   1 
ATOM   595  O O   . ASP A 1 264 ? -18.785 50.768  123.362 1.00 97.14  ?  245 ASP A O   1 
ATOM   596  C CB  . ASP A 1 264 ? -17.151 49.393  125.355 1.00 97.60  ?  245 ASP A CB  1 
ATOM   597  C CG  . ASP A 1 264 ? -16.204 50.503  125.775 1.00 98.14  ?  245 ASP A CG  1 
ATOM   598  O OD1 . ASP A 1 264 ? -16.690 51.629  126.026 1.00 92.44  ?  245 ASP A OD1 1 
ATOM   599  O OD2 . ASP A 1 264 ? -14.983 50.243  125.873 1.00 99.42  ?  245 ASP A OD2 1 
ATOM   600  N N   . THR A 1 265 ? -19.619 51.949  125.092 1.00 93.30  ?  246 THR A N   1 
ATOM   601  C CA  . THR A 1 265 ? -20.011 53.035  124.208 1.00 96.84  ?  246 THR A CA  1 
ATOM   602  C C   . THR A 1 265 ? -18.802 53.825  123.726 1.00 96.06  ?  246 THR A C   1 
ATOM   603  O O   . THR A 1 265 ? -18.764 54.239  122.561 1.00 96.72  ?  246 THR A O   1 
ATOM   604  C CB  . THR A 1 265 ? -21.017 53.961  124.890 1.00 98.63  ?  246 THR A CB  1 
ATOM   605  O OG1 . THR A 1 265 ? -20.496 54.406  126.151 1.00 99.65  ?  246 THR A OG1 1 
ATOM   606  C CG2 . THR A 1 265 ? -22.330 53.238  125.090 1.00 98.45  ?  246 THR A CG2 1 
ATOM   607  N N   . VAL A 1 266 ? -17.805 54.057  124.589 1.00 92.94  ?  247 VAL A N   1 
ATOM   608  C CA  . VAL A 1 266 ? -16.690 54.884  124.137 1.00 96.36  ?  247 VAL A CA  1 
ATOM   609  C C   . VAL A 1 266 ? -15.901 54.173  123.040 1.00 92.36  ?  247 VAL A C   1 
ATOM   610  O O   . VAL A 1 266 ? -15.523 54.797  122.040 1.00 90.51  ?  247 VAL A O   1 
ATOM   611  C CB  . VAL A 1 266 ? -15.797 55.356  125.307 1.00 91.90  ?  247 VAL A CB  1 
ATOM   612  C CG1 . VAL A 1 266 ? -16.556 56.348  126.135 1.00 87.75  ?  247 VAL A CG1 1 
ATOM   613  C CG2 . VAL A 1 266 ? -15.366 54.214  126.182 1.00 91.27  ?  247 VAL A CG2 1 
ATOM   614  N N   . LEU A 1 267 ? -15.693 52.857  123.160 1.00 93.19  ?  248 LEU A N   1 
ATOM   615  C CA  . LEU A 1 267 ? -15.005 52.145  122.081 1.00 90.24  ?  248 LEU A CA  1 
ATOM   616  C C   . LEU A 1 267 ? -15.772 52.278  120.770 1.00 89.87  ?  248 LEU A C   1 
ATOM   617  O O   . LEU A 1 267 ? -15.187 52.603  119.733 1.00 88.37  ?  248 LEU A O   1 
ATOM   618  C CB  . LEU A 1 267 ? -14.790 50.676  122.436 1.00 85.01  ?  248 LEU A CB  1 
ATOM   619  C CG  . LEU A 1 267 ? -13.870 49.993  121.426 1.00 87.95  ?  248 LEU A CG  1 
ATOM   620  C CD1 . LEU A 1 267 ? -12.613 50.839  121.220 1.00 85.84  ?  248 LEU A CD1 1 
ATOM   621  C CD2 . LEU A 1 267 ? -13.479 48.617  121.902 1.00 78.43  ?  248 LEU A CD2 1 
ATOM   622  N N   . VAL A 1 268 ? -17.089 52.057  120.797 1.00 90.53  ?  249 VAL A N   1 
ATOM   623  C CA  . VAL A 1 268 ? -17.887 52.320  119.603 1.00 87.37  ?  249 VAL A CA  1 
ATOM   624  C C   . VAL A 1 268 ? -17.769 53.779  119.191 1.00 82.40  ?  249 VAL A C   1 
ATOM   625  O O   . VAL A 1 268 ? -17.461 54.079  118.037 1.00 85.72  ?  249 VAL A O   1 
ATOM   626  C CB  . VAL A 1 268 ? -19.353 51.900  119.803 1.00 88.26  ?  249 VAL A CB  1 
ATOM   627  C CG1 . VAL A 1 268 ? -20.191 52.394  118.653 1.00 90.81  ?  249 VAL A CG1 1 
ATOM   628  C CG2 . VAL A 1 268 ? -19.434 50.402  119.806 1.00 92.14  ?  249 VAL A CG2 1 
ATOM   629  N N   . HIS A 1 269 ? -18.010 54.711  120.116 1.00 89.88  ?  250 HIS A N   1 
ATOM   630  C CA  . HIS A 1 269 ? -17.875 56.125  119.755 1.00 91.47  ?  250 HIS A CA  1 
ATOM   631  C C   . HIS A 1 269 ? -16.493 56.422  119.207 1.00 89.78  ?  250 HIS A C   1 
ATOM   632  O O   . HIS A 1 269 ? -16.337 57.262  118.311 1.00 82.92  ?  250 HIS A O   1 
ATOM   633  C CB  . HIS A 1 269 ? -18.139 57.046  120.944 1.00 84.09  ?  250 HIS A CB  1 
ATOM   634  C CG  . HIS A 1 269 ? -18.060 58.502  120.590 1.00 87.70  ?  250 HIS A CG  1 
ATOM   635  N ND1 . HIS A 1 269 ? -18.964 59.114  119.747 1.00 86.18  ?  250 HIS A ND1 1 
ATOM   636  C CD2 . HIS A 1 269 ? -17.156 59.457  120.928 1.00 88.98  ?  250 HIS A CD2 1 
ATOM   637  C CE1 . HIS A 1 269 ? -18.642 60.391  119.607 1.00 83.58  ?  250 HIS A CE1 1 
ATOM   638  N NE2 . HIS A 1 269 ? -17.547 60.623  120.310 1.00 83.54  ?  250 HIS A NE2 1 
ATOM   639  N N   . ARG A 1 270 ? -15.482 55.725  119.714 1.00 90.17  ?  251 ARG A N   1 
ATOM   640  C CA  . ARG A 1 270 ? -14.129 56.028  119.293 1.00 87.09  ?  251 ARG A CA  1 
ATOM   641  C C   . ARG A 1 270 ? -13.828 55.447  117.911 1.00 85.96  ?  251 ARG A C   1 
ATOM   642  O O   . ARG A 1 270 ? -13.153 56.096  117.106 1.00 85.54  ?  251 ARG A O   1 
ATOM   643  C CB  . ARG A 1 270 ? -13.166 55.532  120.369 1.00 82.07  ?  251 ARG A CB  1 
ATOM   644  C CG  . ARG A 1 270 ? -12.001 56.389  120.427 1.00 89.79  ?  251 ARG A CG  1 
ATOM   645  C CD  . ARG A 1 270 ? -11.207 56.220  121.657 1.00 90.48  ?  251 ARG A CD  1 
ATOM   646  N NE  . ARG A 1 270 ? -10.792 54.851  121.858 1.00 79.62  ?  251 ARG A NE  1 
ATOM   647  C CZ  . ARG A 1 270 ? -9.517  54.508  122.018 1.00 87.00  ?  251 ARG A CZ  1 
ATOM   648  N NH1 . ARG A 1 270 ? -8.561  55.424  121.907 1.00 90.69  ?  251 ARG A NH1 1 
ATOM   649  N NH2 . ARG A 1 270 ? -9.184  53.250  122.242 1.00 80.09  ?  251 ARG A NH2 1 
ATOM   650  N N   . VAL A 1 271 ? -14.359 54.261  117.607 1.00 85.31  ?  252 VAL A N   1 
ATOM   651  C CA  . VAL A 1 271 ? -14.234 53.694  116.271 1.00 75.90  ?  252 VAL A CA  1 
ATOM   652  C C   . VAL A 1 271 ? -14.973 54.553  115.262 1.00 79.16  ?  252 VAL A C   1 
ATOM   653  O O   . VAL A 1 271 ? -14.408 54.965  114.244 1.00 83.85  ?  252 VAL A O   1 
ATOM   654  C CB  . VAL A 1 271 ? -14.758 52.249  116.253 1.00 82.48  ?  252 VAL A CB  1 
ATOM   655  C CG1 . VAL A 1 271 ? -15.064 51.808  114.831 1.00 81.25  ?  252 VAL A CG1 1 
ATOM   656  C CG2 . VAL A 1 271 ? -13.760 51.313  116.910 1.00 83.08  ?  252 VAL A CG2 1 
ATOM   657  N N   . HIS A 1 272 ? -16.252 54.827  115.519 1.00 82.13  ?  253 HIS A N   1 
ATOM   658  C CA  . HIS A 1 272 ? -17.042 55.583  114.551 1.00 80.19  ?  253 HIS A CA  1 
ATOM   659  C C   . HIS A 1 272 ? -16.375 56.900  114.218 1.00 81.22  ?  253 HIS A C   1 
ATOM   660  O O   . HIS A 1 272 ? -16.389 57.343  113.064 1.00 83.44  ?  253 HIS A O   1 
ATOM   661  C CB  . HIS A 1 272 ? -18.448 55.840  115.082 1.00 76.36  ?  253 HIS A CB  1 
ATOM   662  C CG  . HIS A 1 272 ? -19.261 56.752  114.219 1.00 79.94  ?  253 HIS A CG  1 
ATOM   663  N ND1 . HIS A 1 272 ? -19.062 58.118  114.175 1.00 83.53  ?  253 HIS A ND1 1 
ATOM   664  C CD2 . HIS A 1 272 ? -20.280 56.493  113.364 1.00 84.23  ?  253 HIS A CD2 1 
ATOM   665  C CE1 . HIS A 1 272 ? -19.926 58.660  113.333 1.00 85.35  ?  253 HIS A CE1 1 
ATOM   666  N NE2 . HIS A 1 272 ? -20.674 57.695  112.825 1.00 86.78  ?  253 HIS A NE2 1 
ATOM   667  N N   . SER A 1 273 ? -15.781 57.544  115.212 1.00 83.81  ?  254 SER A N   1 
ATOM   668  C CA  . SER A 1 273 ? -15.177 58.839  114.944 1.00 86.50  ?  254 SER A CA  1 
ATOM   669  C C   . SER A 1 273 ? -13.958 58.699  114.038 1.00 83.27  ?  254 SER A C   1 
ATOM   670  O O   . SER A 1 273 ? -13.803 59.478  113.091 1.00 85.30  ?  254 SER A O   1 
ATOM   671  C CB  . SER A 1 273 ? -14.841 59.538  116.261 1.00 83.45  ?  254 SER A CB  1 
ATOM   672  O OG  . SER A 1 273 ? -16.045 59.987  116.875 1.00 75.20  ?  254 SER A OG  1 
ATOM   673  N N   . TYR A 1 274 ? -13.101 57.700  114.300 1.00 80.09  ?  255 TYR A N   1 
ATOM   674  C CA  . TYR A 1 274 ? -11.957 57.412  113.431 1.00 80.00  ?  255 TYR A CA  1 
ATOM   675  C C   . TYR A 1 274 ? -12.393 57.217  111.985 1.00 76.15  ?  255 TYR A C   1 
ATOM   676  O O   . TYR A 1 274 ? -11.848 57.833  111.060 1.00 72.95  ?  255 TYR A O   1 
ATOM   677  C CB  . TYR A 1 274 ? -11.223 56.173  113.949 1.00 83.21  ?  255 TYR A CB  1 
ATOM   678  C CG  . TYR A 1 274 ? -10.485 55.360  112.905 1.00 81.11  ?  255 TYR A CG  1 
ATOM   679  C CD1 . TYR A 1 274 ? -9.218  55.723  112.443 1.00 80.65  ?  255 TYR A CD1 1 
ATOM   680  C CD2 . TYR A 1 274 ? -11.072 54.220  112.376 1.00 82.45  ?  255 TYR A CD2 1 
ATOM   681  C CE1 . TYR A 1 274 ? -8.543  54.959  111.469 1.00 78.52  ?  255 TYR A CE1 1 
ATOM   682  C CE2 . TYR A 1 274 ? -10.422 53.451  111.415 1.00 92.39  ?  255 TYR A CE2 1 
ATOM   683  C CZ  . TYR A 1 274 ? -9.160  53.820  110.953 1.00 96.51  ?  255 TYR A CZ  1 
ATOM   684  O OH  . TYR A 1 274 ? -8.543  53.019  109.984 1.00 102.13 ?  255 TYR A OH  1 
ATOM   685  N N   . LEU A 1 275 ? -13.395 56.371  111.779 1.00 77.67  ?  256 LEU A N   1 
ATOM   686  C CA  . LEU A 1 275 ? -13.893 56.135  110.434 1.00 77.81  ?  256 LEU A CA  1 
ATOM   687  C C   . LEU A 1 275 ? -14.369 57.432  109.790 1.00 73.19  ?  256 LEU A C   1 
ATOM   688  O O   . LEU A 1 275 ? -14.080 57.706  108.625 1.00 71.48  ?  256 LEU A O   1 
ATOM   689  C CB  . LEU A 1 275 ? -15.022 55.109  110.481 1.00 76.66  ?  256 LEU A CB  1 
ATOM   690  C CG  . LEU A 1 275 ? -14.704 53.757  111.114 1.00 76.93  ?  256 LEU A CG  1 
ATOM   691  C CD1 . LEU A 1 275 ? -15.944 52.900  111.039 1.00 83.23  ?  256 LEU A CD1 1 
ATOM   692  C CD2 . LEU A 1 275 ? -13.564 53.048  110.425 1.00 71.16  ?  256 LEU A CD2 1 
ATOM   693  N N   . GLU A 1 276 ? -15.121 58.236  110.531 1.00 78.46  ?  257 GLU A N   1 
ATOM   694  C CA  . GLU A 1 276 ? -15.701 59.424  109.930 1.00 77.02  ?  257 GLU A CA  1 
ATOM   695  C C   . GLU A 1 276 ? -14.611 60.410  109.560 1.00 73.93  ?  257 GLU A C   1 
ATOM   696  O O   . GLU A 1 276 ? -14.685 61.076  108.516 1.00 74.66  ?  257 GLU A O   1 
ATOM   697  C CB  . GLU A 1 276 ? -16.719 60.039  110.891 1.00 82.28  ?  257 GLU A CB  1 
ATOM   698  C CG  . GLU A 1 276 ? -17.214 61.427  110.491 1.00 89.01  ?  257 GLU A CG  1 
ATOM   699  C CD  . GLU A 1 276 ? -18.625 61.750  111.001 1.00 94.21  ?  257 GLU A CD  1 
ATOM   700  O OE1 . GLU A 1 276 ? -19.171 60.970  111.810 1.00 91.92  ?  257 GLU A OE1 1 
ATOM   701  O OE2 . GLU A 1 276 ? -19.190 62.789  110.581 1.00 99.43  ?  257 GLU A OE2 1 
ATOM   702  N N   . ARG A 1 277 ? -13.564 60.464  110.384 1.00 73.54  ?  258 ARG A N   1 
ATOM   703  C CA  . ARG A 1 277 ? -12.459 61.386  110.162 1.00 75.83  ?  258 ARG A CA  1 
ATOM   704  C C   . ARG A 1 277 ? -11.722 61.058  108.869 1.00 78.38  ?  258 ARG A C   1 
ATOM   705  O O   . ARG A 1 277 ? -11.559 61.908  107.984 1.00 72.64  ?  258 ARG A O   1 
ATOM   706  C CB  . ARG A 1 277 ? -11.499 61.340  111.357 1.00 74.80  ?  258 ARG A CB  1 
ATOM   707  C CG  . ARG A 1 277 ? -10.268 62.181  111.101 1.00 80.38  ?  258 ARG A CG  1 
ATOM   708  C CD  . ARG A 1 277 ? -10.686 63.625  111.117 1.00 81.32  ?  258 ARG A CD  1 
ATOM   709  N NE  . ARG A 1 277 ? -10.528 64.250  112.417 1.00 74.89  ?  258 ARG A NE  1 
ATOM   710  C CZ  . ARG A 1 277 ? -11.366 65.156  112.886 1.00 73.09  ?  258 ARG A CZ  1 
ATOM   711  N NH1 . ARG A 1 277 ? -12.490 65.408  112.223 1.00 71.07  ?  258 ARG A NH1 1 
ATOM   712  N NH2 . ARG A 1 277 ? -11.150 65.707  114.067 1.00 77.26  ?  258 ARG A NH2 1 
ATOM   713  N N   . HIS A 1 278 ? -11.264 59.817  108.742 1.00 75.17  ?  259 HIS A N   1 
ATOM   714  C CA  . HIS A 1 278 ? -10.468 59.433  107.594 1.00 72.68  ?  259 HIS A CA  1 
ATOM   715  C C   . HIS A 1 278 ? -11.304 59.024  106.395 1.00 74.21  ?  259 HIS A C   1 
ATOM   716  O O   . HIS A 1 278 ? -10.828 58.255  105.552 1.00 74.91  ?  259 HIS A O   1 
ATOM   717  C CB  . HIS A 1 278 ? -9.502  58.342  108.009 1.00 75.70  ?  259 HIS A CB  1 
ATOM   718  C CG  . HIS A 1 278 ? -8.709  58.721  109.207 1.00 78.30  ?  259 HIS A CG  1 
ATOM   719  N ND1 . HIS A 1 278 ? -7.934  59.859  109.242 1.00 86.11  ?  259 HIS A ND1 1 
ATOM   720  C CD2 . HIS A 1 278 ? -8.582  58.139  110.419 1.00 80.45  ?  259 HIS A CD2 1 
ATOM   721  C CE1 . HIS A 1 278 ? -7.343  59.948  110.419 1.00 89.49  ?  259 HIS A CE1 1 
ATOM   722  N NE2 . HIS A 1 278 ? -7.716  58.912  111.150 1.00 86.63  ?  259 HIS A NE2 1 
ATOM   723  N N   . GLY A 1 279 ? -12.520 59.560  106.279 1.00 76.67  ?  260 GLY A N   1 
ATOM   724  C CA  . GLY A 1 279 ? -13.332 59.402  105.080 1.00 73.14  ?  260 GLY A CA  1 
ATOM   725  C C   . GLY A 1 279 ? -13.582 57.974  104.663 1.00 76.18  ?  260 GLY A C   1 
ATOM   726  O O   . GLY A 1 279 ? -13.617 57.686  103.461 1.00 82.40  ?  260 GLY A O   1 
ATOM   727  N N   . LEU A 1 280 ? -13.705 57.055  105.624 1.00 77.52  ?  261 LEU A N   1 
ATOM   728  C CA  . LEU A 1 280 ? -14.119 55.693  105.318 1.00 73.29  ?  261 LEU A CA  1 
ATOM   729  C C   . LEU A 1 280 ? -15.628 55.545  105.360 1.00 74.40  ?  261 LEU A C   1 
ATOM   730  O O   . LEU A 1 280 ? -16.174 54.655  104.698 1.00 70.76  ?  261 LEU A O   1 
ATOM   731  C CB  . LEU A 1 280 ? -13.465 54.717  106.292 1.00 68.96  ?  261 LEU A CB  1 
ATOM   732  C CG  . LEU A 1 280 ? -12.001 54.486  105.914 1.00 73.71  ?  261 LEU A CG  1 
ATOM   733  C CD1 . LEU A 1 280 ? -11.253 53.724  106.998 1.00 73.49  ?  261 LEU A CD1 1 
ATOM   734  C CD2 . LEU A 1 280 ? -11.896 53.768  104.555 1.00 72.79  ?  261 LEU A CD2 1 
ATOM   735  N N   . ILE A 1 281 ? -16.303 56.420  106.111 1.00 80.91  ?  262 ILE A N   1 
ATOM   736  C CA  . ILE A 1 281 ? -17.754 56.510  106.189 1.00 76.80  ?  262 ILE A CA  1 
ATOM   737  C C   . ILE A 1 281 ? -18.114 57.985  106.076 1.00 78.98  ?  262 ILE A C   1 
ATOM   738  O O   . ILE A 1 281 ? -17.294 58.863  106.370 1.00 82.03  ?  262 ILE A O   1 
ATOM   739  C CB  . ILE A 1 281 ? -18.294 55.896  107.494 1.00 77.90  ?  262 ILE A CB  1 
ATOM   740  C CG1 . ILE A 1 281 ? -17.724 56.642  108.700 1.00 80.43  ?  262 ILE A CG1 1 
ATOM   741  C CG2 . ILE A 1 281 ? -17.900 54.404  107.607 1.00 76.03  ?  262 ILE A CG2 1 
ATOM   742  C CD1 . ILE A 1 281 ? -18.371 56.258  110.004 1.00 82.69  ?  262 ILE A CD1 1 
ATOM   743  N N   . ASN A 1 282 ? -19.335 58.261  105.618 1.00 78.88  ?  263 ASN A N   1 
ATOM   744  C CA  . ASN A 1 282 ? -19.834 59.632  105.429 1.00 82.97  ?  263 ASN A CA  1 
ATOM   745  C C   . ASN A 1 282 ? -18.830 60.478  104.647 1.00 78.99  ?  263 ASN A C   1 
ATOM   746  O O   . ASN A 1 282 ? -18.308 61.485  105.137 1.00 83.43  ?  263 ASN A O   1 
ATOM   747  C CB  . ASN A 1 282 ? -20.151 60.324  106.764 1.00 87.72  ?  263 ASN A CB  1 
ATOM   748  C CG  . ASN A 1 282 ? -20.862 59.425  107.760 1.00 84.29  ?  263 ASN A CG  1 
ATOM   749  O OD1 . ASN A 1 282 ? -21.978 58.968  107.525 1.00 88.51  ?  263 ASN A OD1 1 
ATOM   750  N ND2 . ASN A 1 282 ? -20.207 59.165  108.883 1.00 82.44  ?  263 ASN A ND2 1 
ATOM   751  N N   . PHE A 1 283 ? -18.542 60.033  103.425 1.00 80.79  ?  264 PHE A N   1 
ATOM   752  C CA  . PHE A 1 283 ? -17.817 60.827  102.438 1.00 77.14  ?  264 PHE A CA  1 
ATOM   753  C C   . PHE A 1 283 ? -18.629 60.870  101.151 1.00 76.74  ?  264 PHE A C   1 
ATOM   754  O O   . PHE A 1 283 ? -19.457 59.997  100.885 1.00 80.06  ?  264 PHE A O   1 
ATOM   755  C CB  . PHE A 1 283 ? -16.404 60.274  102.163 1.00 69.75  ?  264 PHE A CB  1 
ATOM   756  C CG  . PHE A 1 283 ? -16.391 58.904  101.532 1.00 78.18  ?  264 PHE A CG  1 
ATOM   757  C CD1 . PHE A 1 283 ? -16.485 58.749  100.145 1.00 78.69  ?  264 PHE A CD1 1 
ATOM   758  C CD2 . PHE A 1 283 ? -16.265 57.760  102.325 1.00 79.86  ?  264 PHE A CD2 1 
ATOM   759  C CE1 . PHE A 1 283 ? -16.465 57.474  99.560  1.00 75.36  ?  264 PHE A CE1 1 
ATOM   760  C CE2 . PHE A 1 283 ? -16.229 56.483  101.754 1.00 76.03  ?  264 PHE A CE2 1 
ATOM   761  C CZ  . PHE A 1 283 ? -16.339 56.340  100.368 1.00 78.58  ?  264 PHE A CZ  1 
ATOM   762  N N   . GLY A 1 284 ? -18.391 61.883  100.348 1.00 67.45  ?  265 GLY A N   1 
ATOM   763  C CA  . GLY A 1 284 ? -19.095 62.006  99.088  1.00 70.58  ?  265 GLY A CA  1 
ATOM   764  C C   . GLY A 1 284 ? -20.318 62.881  99.233  1.00 78.28  ?  265 GLY A C   1 
ATOM   765  O O   . GLY A 1 284 ? -20.223 64.014  99.711  1.00 85.81  ?  265 GLY A O   1 
ATOM   766  N N   . ILE A 1 285 ? -21.473 62.361  98.826  1.00 81.89  ?  266 ILE A N   1 
ATOM   767  C CA  . ILE A 1 285 ? -22.736 63.103  98.854  1.00 82.74  ?  266 ILE A CA  1 
ATOM   768  C C   . ILE A 1 285 ? -23.800 62.285  99.581  1.00 86.72  ?  266 ILE A C   1 
ATOM   769  O O   . ILE A 1 285 ? -24.282 61.278  99.048  1.00 93.48  ?  266 ILE A O   1 
ATOM   770  C CB  . ILE A 1 285 ? -23.221 63.467  97.448  1.00 76.10  ?  266 ILE A CB  1 
ATOM   771  C CG1 . ILE A 1 285 ? -22.255 64.451  96.788  1.00 78.91  ?  266 ILE A CG1 1 
ATOM   772  C CG2 . ILE A 1 285 ? -24.609 64.037  97.549  1.00 83.95  ?  266 ILE A CG2 1 
ATOM   773  C CD1 . ILE A 1 285 ? -22.529 64.703  95.341  1.00 83.94  ?  266 ILE A CD1 1 
ATOM   774  N N   . TYR A 1 286 ? -24.204 62.753  100.766 1.00 92.14  ?  267 TYR A N   1 
ATOM   775  C CA  . TYR A 1 286 ? -25.150 62.118  101.678 1.00 94.32  ?  267 TYR A CA  1 
ATOM   776  C C   . TYR A 1 286 ? -26.017 63.237  102.256 1.00 100.72 ?  267 TYR A C   1 
ATOM   777  O O   . TYR A 1 286 ? -25.505 64.351  102.411 1.00 102.48 ?  267 TYR A O   1 
ATOM   778  C CB  . TYR A 1 286 ? -24.375 61.331  102.783 1.00 93.16  ?  267 TYR A CB  1 
ATOM   779  C CG  . TYR A 1 286 ? -23.136 62.017  103.370 1.00 95.67  ?  267 TYR A CG  1 
ATOM   780  C CD1 . TYR A 1 286 ? -21.922 62.010  102.693 1.00 91.72  ?  267 TYR A CD1 1 
ATOM   781  C CD2 . TYR A 1 286 ? -23.179 62.652  104.616 1.00 98.08  ?  267 TYR A CD2 1 
ATOM   782  C CE1 . TYR A 1 286 ? -20.777 62.643  103.230 1.00 95.59  ?  267 TYR A CE1 1 
ATOM   783  C CE2 . TYR A 1 286 ? -22.033 63.281  105.166 1.00 96.82  ?  267 TYR A CE2 1 
ATOM   784  C CZ  . TYR A 1 286 ? -20.832 63.273  104.467 1.00 97.19  ?  267 TYR A CZ  1 
ATOM   785  O OH  . TYR A 1 286 ? -19.679 63.879  104.976 1.00 89.53  ?  267 TYR A OH  1 
ATOM   786  N N   . LYS A 1 287 ? -27.322 63.020  102.530 1.00 101.46 ?  268 LYS A N   1 
ATOM   787  C CA  . LYS A 1 287 ? -27.948 64.080  103.319 1.00 109.86 ?  268 LYS A CA  1 
ATOM   788  C C   . LYS A 1 287 ? -27.472 63.903  104.759 1.00 110.78 ?  268 LYS A C   1 
ATOM   789  O O   . LYS A 1 287 ? -27.346 62.770  105.253 1.00 99.17  ?  268 LYS A O   1 
ATOM   790  C CB  . LYS A 1 287 ? -29.487 64.156  103.408 1.00 111.20 ?  268 LYS A CB  1 
ATOM   791  C CG  . LYS A 1 287 ? -30.563 64.385  102.436 1.00 117.54 ?  268 LYS A CG  1 
ATOM   792  C CD  . LYS A 1 287 ? -31.937 64.836  103.353 1.00 122.70 ?  268 LYS A CD  1 
ATOM   793  C CE  . LYS A 1 287 ? -32.313 66.357  103.153 1.00 117.73 ?  268 LYS A CE  1 
ATOM   794  N NZ  . LYS A 1 287 ? -33.213 66.339  101.880 1.00 118.95 ?  268 LYS A NZ  1 
ATOM   795  N N   . ARG A 1 288 ? -27.197 65.024  105.432 1.00 115.52 ?  269 ARG A N   1 
ATOM   796  C CA  . ARG A 1 288 ? -26.906 64.913  106.853 1.00 114.33 ?  269 ARG A CA  1 
ATOM   797  C C   . ARG A 1 288 ? -28.187 64.731  107.643 1.00 117.48 ?  269 ARG A C   1 
ATOM   798  O O   . ARG A 1 288 ? -29.286 65.025  107.169 1.00 120.59 ?  269 ARG A O   1 
ATOM   799  C CB  . ARG A 1 288 ? -26.178 66.137  107.411 1.00 113.99 ?  269 ARG A CB  1 
ATOM   800  C CG  . ARG A 1 288 ? -24.672 66.037  107.461 1.00 117.72 ?  269 ARG A CG  1 
ATOM   801  C CD  . ARG A 1 288 ? -24.095 67.427  107.503 1.00 128.78 ?  269 ARG A CD  1 
ATOM   802  N NE  . ARG A 1 288 ? -24.553 68.153  106.317 1.00 138.01 ?  269 ARG A NE  1 
ATOM   803  C CZ  . ARG A 1 288 ? -24.054 68.010  105.087 1.00 136.37 ?  269 ARG A CZ  1 
ATOM   804  N NH1 . ARG A 1 288 ? -23.058 67.160  104.844 1.00 128.27 ?  269 ARG A NH1 1 
ATOM   805  N NH2 . ARG A 1 288 ? -24.562 68.722  104.087 1.00 133.58 ?  269 ARG A NH2 1 
ATOM   806  N N   . ILE A 1 289 ? -28.036 64.269  108.879 1.00 120.17 ?  270 ILE A N   1 
ATOM   807  C CA  . ILE A 1 289 ? -29.145 64.243  109.835 1.00 122.61 ?  270 ILE A CA  1 
ATOM   808  C C   . ILE A 1 289 ? -29.054 65.434  110.776 1.00 125.70 ?  270 ILE A C   1 
ATOM   809  O O   . ILE A 1 289 ? -29.997 66.221  110.913 1.00 127.81 ?  270 ILE A O   1 
ATOM   810  C CB  . ILE A 1 289 ? -29.144 62.914  110.623 1.00 117.17 ?  270 ILE A CB  1 
ATOM   811  C CG1 . ILE A 1 289 ? -28.962 61.738  109.664 1.00 110.90 ?  270 ILE A CG1 1 
ATOM   812  C CG2 . ILE A 1 289 ? -30.463 62.746  111.363 1.00 111.18 ?  270 ILE A CG2 1 
ATOM   813  C CD1 . ILE A 1 289 ? -29.969 61.641  108.538 1.00 108.69 ?  270 ILE A CD1 1 
ATOM   814  N N   . LYS A 1 290 ? -27.878 65.586  111.388 1.00 126.32 ?  271 LYS A N   1 
ATOM   815  C CA  . LYS A 1 290 ? -27.412 66.736  112.147 1.00 130.03 ?  271 LYS A CA  1 
ATOM   816  C C   . LYS A 1 290 ? -26.964 67.823  111.174 1.00 130.66 ?  271 LYS A C   1 
ATOM   817  O O   . LYS A 1 290 ? -25.914 67.666  110.535 1.00 130.23 ?  271 LYS A O   1 
ATOM   818  C CB  . LYS A 1 290 ? -26.253 66.309  113.052 1.00 125.20 ?  271 LYS A CB  1 
ATOM   819  C CG  . LYS A 1 290 ? -26.501 64.979  113.753 1.00 121.20 ?  271 LYS A CG  1 
ATOM   820  C CD  . LYS A 1 290 ? -25.386 64.631  114.727 1.00 120.31 ?  271 LYS A CD  1 
ATOM   821  C CE  . LYS A 1 290 ? -25.640 63.274  115.380 1.00 116.80 ?  271 LYS A CE  1 
ATOM   822  N NZ  . LYS A 1 290 ? -24.554 62.873  116.324 1.00 113.56 ?  271 LYS A NZ  1 
ATOM   823  N N   . PRO A 1 291 ? -27.721 68.913  111.003 1.00 134.10 ?  272 PRO A N   1 
ATOM   824  C CA  . PRO A 1 291 ? -27.257 69.987  110.116 1.00 133.56 ?  272 PRO A CA  1 
ATOM   825  C C   . PRO A 1 291 ? -25.967 70.612  110.637 1.00 133.44 ?  272 PRO A C   1 
ATOM   826  O O   . PRO A 1 291 ? -25.542 70.416  111.782 1.00 126.41 ?  272 PRO A O   1 
ATOM   827  C CB  . PRO A 1 291 ? -28.427 70.983  110.103 1.00 128.02 ?  272 PRO A CB  1 
ATOM   828  C CG  . PRO A 1 291 ? -29.620 70.171  110.501 1.00 125.10 ?  272 PRO A CG  1 
ATOM   829  C CD  . PRO A 1 291 ? -29.079 69.183  111.509 1.00 130.51 ?  272 PRO A CD  1 
ATOM   830  N N   . LEU A 1 292 ? -25.341 71.392  109.757 1.00 136.70 ?  273 LEU A N   1 
ATOM   831  C CA  . LEU A 1 292 ? -23.948 71.791  109.933 1.00 136.86 ?  273 LEU A CA  1 
ATOM   832  C C   . LEU A 1 292 ? -23.757 72.688  111.160 1.00 139.15 ?  273 LEU A C   1 
ATOM   833  O O   . LEU A 1 292 ? -24.654 73.461  111.519 1.00 135.22 ?  273 LEU A O   1 
ATOM   834  C CB  . LEU A 1 292 ? -23.460 72.522  108.682 1.00 139.25 ?  273 LEU A CB  1 
ATOM   835  C CG  . LEU A 1 292 ? -23.029 71.653  107.498 1.00 138.46 ?  273 LEU A CG  1 
ATOM   836  C CD1 . LEU A 1 292 ? -22.637 72.527  106.287 1.00 124.88 ?  273 LEU A CD1 1 
ATOM   837  C CD2 . LEU A 1 292 ? -21.905 70.690  107.913 1.00 125.34 ?  273 LEU A CD2 1 
ATOM   838  N N   . PRO A 1 293 ? -22.593 72.604  111.814 1.00 141.27 ?  274 PRO A N   1 
ATOM   839  C CA  . PRO A 1 293 ? -22.261 73.571  112.869 1.00 132.47 ?  274 PRO A CA  1 
ATOM   840  C C   . PRO A 1 293 ? -22.421 75.001  112.372 1.00 130.69 ?  274 PRO A C   1 
ATOM   841  O O   . PRO A 1 293 ? -21.950 75.365  111.287 1.00 125.57 ?  274 PRO A O   1 
ATOM   842  C CB  . PRO A 1 293 ? -20.803 73.255  113.222 1.00 128.85 ?  274 PRO A CB  1 
ATOM   843  C CG  . PRO A 1 293 ? -20.396 72.062  112.426 1.00 129.18 ?  274 PRO A CG  1 
ATOM   844  C CD  . PRO A 1 293 ? -21.555 71.580  111.609 1.00 137.37 ?  274 PRO A CD  1 
ATOM   845  N N   . THR A 1 294 ? -23.105 75.816  113.181 1.00 134.57 ?  275 THR A N   1 
ATOM   846  C CA  . THR A 1 294 ? -23.492 77.158  112.749 1.00 134.00 ?  275 THR A CA  1 
ATOM   847  C C   . THR A 1 294 ? -22.270 78.029  112.471 1.00 129.44 ?  275 THR A C   1 
ATOM   848  O O   . THR A 1 294 ? -22.251 78.798  111.498 1.00 116.24 ?  275 THR A O   1 
ATOM   849  C CB  . THR A 1 294 ? -24.417 77.790  113.801 1.00 135.83 ?  275 THR A CB  1 
ATOM   850  O OG1 . THR A 1 294 ? -24.841 79.091  113.362 1.00 142.58 ?  275 THR A OG1 1 
ATOM   851  C CG2 . THR A 1 294 ? -23.746 77.870  115.197 1.00 120.39 ?  275 THR A CG2 1 
ATOM   852  N N   . LYS A 1 295 ? -21.231 77.906  113.301 1.00 127.34 ?  276 LYS A N   1 
ATOM   853  C CA  . LYS A 1 295 ? -19.977 78.604  113.082 1.00 121.49 ?  276 LYS A CA  1 
ATOM   854  C C   . LYS A 1 295 ? -18.845 77.618  112.842 1.00 116.05 ?  276 LYS A C   1 
ATOM   855  O O   . LYS A 1 295 ? -18.804 76.512  113.401 1.00 114.83 ?  276 LYS A O   1 
ATOM   856  C CB  . LYS A 1 295 ? -19.621 79.539  114.242 1.00 125.52 ?  276 LYS A CB  1 
ATOM   857  C CG  . LYS A 1 295 ? -20.240 80.916  114.081 1.00 124.09 ?  276 LYS A CG  1 
ATOM   858  C CD  . LYS A 1 295 ? -19.888 81.860  115.212 1.00 122.19 ?  276 LYS A CD  1 
ATOM   859  C CE  . LYS A 1 295 ? -20.658 83.161  115.039 1.00 121.07 ?  276 LYS A CE  1 
ATOM   860  N NZ  . LYS A 1 295 ? -20.294 84.215  116.019 1.00 118.34 ?  276 LYS A NZ  1 
ATOM   861  N N   . LYS A 1 296 ? -17.918 78.074  112.017 1.00 109.56 ?  277 LYS A N   1 
ATOM   862  C CA  . LYS A 1 296 ? -16.857 77.288  111.426 1.00 101.84 ?  277 LYS A CA  1 
ATOM   863  C C   . LYS A 1 296 ? -15.562 77.520  112.205 1.00 96.13  ?  277 LYS A C   1 
ATOM   864  O O   . LYS A 1 296 ? -15.390 78.538  112.868 1.00 103.50 ?  277 LYS A O   1 
ATOM   865  C CB  . LYS A 1 296 ? -16.753 77.688  109.945 1.00 96.31  ?  277 LYS A CB  1 
ATOM   866  C CG  . LYS A 1 296 ? -18.090 77.395  109.197 1.00 92.78  ?  277 LYS A CG  1 
ATOM   867  C CD  . LYS A 1 296 ? -18.117 77.654  107.658 1.00 94.24  ?  277 LYS A CD  1 
ATOM   868  C CE  . LYS A 1 296 ? -18.206 79.153  107.224 1.00 107.95 ?  277 LYS A CE  1 
ATOM   869  N NZ  . LYS A 1 296 ? -19.561 79.848  107.356 1.00 104.56 ?  277 LYS A NZ  1 
ATOM   870  N N   . THR A 1 297 ? -14.663 76.546  112.158 1.00 89.39  ?  278 THR A N   1 
ATOM   871  C CA  . THR A 1 297 ? -13.435 76.596  112.941 1.00 88.25  ?  278 THR A CA  1 
ATOM   872  C C   . THR A 1 297 ? -12.228 76.461  112.022 1.00 86.37  ?  278 THR A C   1 
ATOM   873  O O   . THR A 1 297 ? -12.170 75.532  111.211 1.00 85.62  ?  278 THR A O   1 
ATOM   874  C CB  . THR A 1 297 ? -13.436 75.474  113.972 1.00 91.74  ?  278 THR A CB  1 
ATOM   875  O OG1 . THR A 1 297 ? -14.753 75.370  114.525 1.00 94.62  ?  278 THR A OG1 1 
ATOM   876  C CG2 . THR A 1 297 ? -12.420 75.745  115.065 1.00 87.26  ?  278 THR A CG2 1 
ATOM   877  N N   . GLY A 1 298 ? -11.257 77.364  112.158 1.00 88.33  ?  279 GLY A N   1 
ATOM   878  C CA  . GLY A 1 298 ? -10.100 77.367  111.269 1.00 82.98  ?  279 GLY A CA  1 
ATOM   879  C C   . GLY A 1 298 ? -10.451 77.662  109.819 1.00 78.91  ?  279 GLY A C   1 
ATOM   880  O O   . GLY A 1 298 ? -11.610 77.500  109.423 1.00 79.28  ?  279 GLY A O   1 
ATOM   881  N N   . LYS A 1 299 ? -9.480  78.115  109.015 1.00 74.20  ?  280 LYS A N   1 
ATOM   882  C CA  . LYS A 1 299 ? -9.721  78.387  107.596 1.00 78.30  ?  280 LYS A CA  1 
ATOM   883  C C   . LYS A 1 299 ? -8.676  77.734  106.695 1.00 78.21  ?  280 LYS A C   1 
ATOM   884  O O   . LYS A 1 299 ? -7.473  77.880  106.942 1.00 73.93  ?  280 LYS A O   1 
ATOM   885  C CB  . LYS A 1 299 ? -9.745  79.860  107.266 1.00 67.91  ?  280 LYS A CB  1 
ATOM   886  C CG  . LYS A 1 299 ? -10.090 79.952  105.825 1.00 83.08  ?  280 LYS A CG  1 
ATOM   887  C CD  . LYS A 1 299 ? -10.139 81.361  105.228 1.00 102.88 ?  280 LYS A CD  1 
ATOM   888  C CE  . LYS A 1 299 ? -10.410 81.257  103.661 1.00 90.88  ?  280 LYS A CE  1 
ATOM   889  N NZ  . LYS A 1 299 ? -11.739 80.450  103.382 1.00 85.01  ?  280 LYS A NZ  1 
ATOM   890  N N   . VAL A 1 300 ? -9.140  77.049  105.630 1.00 74.03  ?  281 VAL A N   1 
ATOM   891  C CA  . VAL A 1 300 ? -8.280  76.262  104.745 1.00 71.68  ?  281 VAL A CA  1 
ATOM   892  C C   . VAL A 1 300 ? -8.489  76.732  103.314 1.00 65.23  ?  281 VAL A C   1 
ATOM   893  O O   . VAL A 1 300 ? -9.629  76.746  102.832 1.00 64.17  ?  281 VAL A O   1 
ATOM   894  C CB  . VAL A 1 300 ? -8.591  74.752  104.781 1.00 66.71  ?  281 VAL A CB  1 
ATOM   895  C CG1 . VAL A 1 300 ? -7.505  74.037  104.059 1.00 57.26  ?  281 VAL A CG1 1 
ATOM   896  C CG2 . VAL A 1 300 ? -8.908  74.207  106.191 1.00 71.98  ?  281 VAL A CG2 1 
ATOM   897  N N   . ILE A 1 301 ? -7.392  77.069  102.618 1.00 58.47  ?  282 ILE A N   1 
ATOM   898  C CA  . ILE A 1 301 ? -7.427  77.334  101.179 1.00 63.18  ?  282 ILE A CA  1 
ATOM   899  C C   . ILE A 1 301 ? -7.010  76.069  100.421 1.00 69.73  ?  282 ILE A C   1 
ATOM   900  O O   . ILE A 1 301 ? -6.022  75.399  100.786 1.00 61.70  ?  282 ILE A O   1 
ATOM   901  C CB  . ILE A 1 301 ? -6.526  78.527  100.804 1.00 62.61  ?  282 ILE A CB  1 
ATOM   902  C CG1 . ILE A 1 301 ? -7.200  79.837  101.184 1.00 68.52  ?  282 ILE A CG1 1 
ATOM   903  C CG2 . ILE A 1 301 ? -6.182  78.517  99.335  1.00 57.45  ?  282 ILE A CG2 1 
ATOM   904  C CD1 . ILE A 1 301 ? -8.467  80.139  100.378 1.00 71.97  ?  282 ILE A CD1 1 
ATOM   905  N N   . ILE A 1 302 ? -7.759  75.748  99.356  1.00 64.90  ?  283 ILE A N   1 
ATOM   906  C CA  . ILE A 1 302 ? -7.576  74.536  98.558  1.00 60.15  ?  283 ILE A CA  1 
ATOM   907  C C   . ILE A 1 302 ? -7.264  74.927  97.118  1.00 57.64  ?  283 ILE A C   1 
ATOM   908  O O   . ILE A 1 302 ? -8.107  75.523  96.436  1.00 59.99  ?  283 ILE A O   1 
ATOM   909  C CB  . ILE A 1 302 ? -8.821  73.649  98.613  1.00 56.54  ?  283 ILE A CB  1 
ATOM   910  C CG1 . ILE A 1 302 ? -8.933  73.036  100.002 1.00 60.32  ?  283 ILE A CG1 1 
ATOM   911  C CG2 . ILE A 1 302 ? -8.748  72.595  97.556  1.00 59.37  ?  283 ILE A CG2 1 
ATOM   912  C CD1 . ILE A 1 302 ? -10.007 71.971  100.108 1.00 65.84  ?  283 ILE A CD1 1 
ATOM   913  N N   . ILE A 1 303 ? -6.068  74.595  96.644  1.00 53.01  ?  284 ILE A N   1 
ATOM   914  C CA  . ILE A 1 303 ? -5.683  74.966  95.289  1.00 52.36  ?  284 ILE A CA  1 
ATOM   915  C C   . ILE A 1 303 ? -6.106  73.852  94.349  1.00 55.59  ?  284 ILE A C   1 
ATOM   916  O O   . ILE A 1 303 ? -5.678  72.703  94.495  1.00 55.71  ?  284 ILE A O   1 
ATOM   917  C CB  . ILE A 1 303 ? -4.183  75.246  95.179  1.00 52.79  ?  284 ILE A CB  1 
ATOM   918  C CG1 . ILE A 1 303 ? -3.806  76.366  96.153  1.00 53.00  ?  284 ILE A CG1 1 
ATOM   919  C CG2 . ILE A 1 303 ? -3.834  75.635  93.725  1.00 43.89  ?  284 ILE A CG2 1 
ATOM   920  C CD1 . ILE A 1 303 ? -2.349  76.696  96.144  1.00 47.07  ?  284 ILE A CD1 1 
ATOM   921  N N   . GLY A 1 304 ? -6.969  74.186  93.402  1.00 55.95  ?  285 GLY A N   1 
ATOM   922  C CA  . GLY A 1 304 ? -7.403  73.243  92.393  1.00 57.86  ?  285 GLY A CA  1 
ATOM   923  C C   . GLY A 1 304 ? -8.718  72.604  92.772  1.00 64.20  ?  285 GLY A C   1 
ATOM   924  O O   . GLY A 1 304 ? -8.900  72.233  93.939  1.00 58.69  ?  285 GLY A O   1 
ATOM   925  N N   . SER A 1 305 ? -9.653  72.467  91.822  1.00 64.23  ?  286 SER A N   1 
ATOM   926  C CA  . SER A 1 305 ? -10.893 71.754  92.124  1.00 67.26  ?  286 SER A CA  1 
ATOM   927  C C   . SER A 1 305 ? -11.001 70.489  91.284  1.00 69.54  ?  286 SER A C   1 
ATOM   928  O O   . SER A 1 305 ? -12.081 70.120  90.795  1.00 63.74  ?  286 SER A O   1 
ATOM   929  C CB  . SER A 1 305 ? -12.126 72.634  91.942  1.00 68.82  ?  286 SER A CB  1 
ATOM   930  O OG  . SER A 1 305 ? -12.514 72.652  90.585  1.00 73.15  ?  286 SER A OG  1 
ATOM   931  N N   . GLY A 1 306 ? -9.870  69.804  91.125  1.00 64.44  ?  287 GLY A N   1 
ATOM   932  C CA  . GLY A 1 306 ? -9.892  68.454  90.648  1.00 60.70  ?  287 GLY A CA  1 
ATOM   933  C C   . GLY A 1 306 ? -10.692 67.593  91.603  1.00 65.27  ?  287 GLY A C   1 
ATOM   934  O O   . GLY A 1 306 ? -11.236 68.040  92.616  1.00 60.48  ?  287 GLY A O   1 
ATOM   935  N N   . VAL A 1 307 ? -10.781 66.311  91.264  1.00 70.73  ?  288 VAL A N   1 
ATOM   936  C CA  . VAL A 1 307 ? -11.515 65.440  92.164  1.00 62.65  ?  288 VAL A CA  1 
ATOM   937  C C   . VAL A 1 307 ? -10.839 65.431  93.519  1.00 56.89  ?  288 VAL A C   1 
ATOM   938  O O   . VAL A 1 307 ? -11.513 65.438  94.554  1.00 59.48  ?  288 VAL A O   1 
ATOM   939  C CB  . VAL A 1 307 ? -11.665 64.036  91.557  1.00 61.62  ?  288 VAL A CB  1 
ATOM   940  C CG1 . VAL A 1 307 ? -12.116 63.022  92.614  1.00 54.75  ?  288 VAL A CG1 1 
ATOM   941  C CG2 . VAL A 1 307 ? -12.661 64.116  90.424  1.00 57.00  ?  288 VAL A CG2 1 
ATOM   942  N N   . SER A 1 308 ? -9.503  65.488  93.545  1.00 53.10  ?  289 SER A N   1 
ATOM   943  C CA  . SER A 1 308 ? -8.840  65.415  94.843  1.00 59.00  ?  289 SER A CA  1 
ATOM   944  C C   . SER A 1 308 ? -9.131  66.672  95.669  1.00 62.51  ?  289 SER A C   1 
ATOM   945  O O   . SER A 1 308 ? -9.440  66.580  96.872  1.00 51.57  ?  289 SER A O   1 
ATOM   946  C CB  . SER A 1 308 ? -7.335  65.168  94.676  1.00 52.98  ?  289 SER A CB  1 
ATOM   947  O OG  . SER A 1 308 ? -6.574  66.357  94.512  1.00 55.44  ?  289 SER A OG  1 
ATOM   948  N N   . GLY A 1 309 ? -9.082  67.849  95.028  1.00 65.76  ?  290 GLY A N   1 
ATOM   949  C CA  . GLY A 1 309 ? -9.536  69.071  95.668  1.00 62.67  ?  290 GLY A CA  1 
ATOM   950  C C   . GLY A 1 309 ? -10.931 68.897  96.251  1.00 64.48  ?  290 GLY A C   1 
ATOM   951  O O   . GLY A 1 309 ? -11.113 68.884  97.477  1.00 61.66  ?  290 GLY A O   1 
ATOM   952  N N   . LEU A 1 310 ? -11.916 68.714  95.363  1.00 63.72  ?  291 LEU A N   1 
ATOM   953  C CA  . LEU A 1 310 ? -13.308 68.608  95.783  1.00 60.79  ?  291 LEU A CA  1 
ATOM   954  C C   . LEU A 1 310 ? -13.479 67.620  96.923  1.00 59.07  ?  291 LEU A C   1 
ATOM   955  O O   . LEU A 1 310 ? -14.193 67.889  97.892  1.00 63.92  ?  291 LEU A O   1 
ATOM   956  C CB  . LEU A 1 310 ? -14.170 68.198  94.596  1.00 60.93  ?  291 LEU A CB  1 
ATOM   957  C CG  . LEU A 1 310 ? -14.224 69.217  93.472  1.00 60.05  ?  291 LEU A CG  1 
ATOM   958  C CD1 . LEU A 1 310 ? -14.647 68.566  92.183  1.00 62.48  ?  291 LEU A CD1 1 
ATOM   959  C CD2 . LEU A 1 310 ? -15.201 70.314  93.855  1.00 72.87  ?  291 LEU A CD2 1 
ATOM   960  N N   . ALA A 1 311 ? -12.822 66.476  96.836  1.00 60.85  ?  292 ALA A N   1 
ATOM   961  C CA  . ALA A 1 311 ? -13.065 65.460  97.849  1.00 66.31  ?  292 ALA A CA  1 
ATOM   962  C C   . ALA A 1 311 ? -12.624 65.935  99.231  1.00 62.82  ?  292 ALA A C   1 
ATOM   963  O O   . ALA A 1 311 ? -13.316 65.681  100.219 1.00 68.21  ?  292 ALA A O   1 
ATOM   964  C CB  . ALA A 1 311 ? -12.370 64.150  97.470  1.00 64.43  ?  292 ALA A CB  1 
ATOM   965  N N   . ALA A 1 312 ? -11.483 66.626  99.330  1.00 62.67  ?  293 ALA A N   1 
ATOM   966  C CA  . ALA A 1 312 ? -11.087 67.189  100.624 1.00 66.12  ?  293 ALA A CA  1 
ATOM   967  C C   . ALA A 1 312 ? -12.030 68.312  101.055 1.00 67.46  ?  293 ALA A C   1 
ATOM   968  O O   . ALA A 1 312 ? -12.505 68.337  102.199 1.00 67.27  ?  293 ALA A O   1 
ATOM   969  C CB  . ALA A 1 312 ? -9.651  67.704  100.571 1.00 56.80  ?  293 ALA A CB  1 
ATOM   970  N N   . ALA A 1 313 ? -12.300 69.254  100.149 1.00 64.95  ?  294 ALA A N   1 
ATOM   971  C CA  . ALA A 1 313 ? -13.198 70.359  100.450 1.00 63.66  ?  294 ALA A CA  1 
ATOM   972  C C   . ALA A 1 313 ? -14.523 69.866  101.030 1.00 68.64  ?  294 ALA A C   1 
ATOM   973  O O   . ALA A 1 313 ? -14.978 70.392  102.055 1.00 69.48  ?  294 ALA A O   1 
ATOM   974  C CB  . ALA A 1 313 ? -13.424 71.198  99.187  1.00 60.85  ?  294 ALA A CB  1 
ATOM   975  N N   . ARG A 1 314 ? -15.158 68.862  100.383 1.00 64.14  ?  295 ARG A N   1 
ATOM   976  C CA  . ARG A 1 314 ? -16.379 68.246  100.922 1.00 64.97  ?  295 ARG A CA  1 
ATOM   977  C C   . ARG A 1 314 ? -16.180 67.841  102.369 1.00 67.43  ?  295 ARG A C   1 
ATOM   978  O O   . ARG A 1 314 ? -17.002 68.143  103.243 1.00 64.90  ?  295 ARG A O   1 
ATOM   979  C CB  . ARG A 1 314 ? -16.770 66.984  100.143 1.00 69.48  ?  295 ARG A CB  1 
ATOM   980  C CG  . ARG A 1 314 ? -17.382 67.152  98.775  1.00 75.76  ?  295 ARG A CG  1 
ATOM   981  C CD  . ARG A 1 314 ? -18.635 67.872  98.902  1.00 73.99  ?  295 ARG A CD  1 
ATOM   982  N NE  . ARG A 1 314 ? -19.700 67.039  99.420  1.00 63.81  ?  295 ARG A NE  1 
ATOM   983  C CZ  . ARG A 1 314 ? -20.946 67.121  98.976  1.00 73.96  ?  295 ARG A CZ  1 
ATOM   984  N NH1 . ARG A 1 314 ? -21.886 66.363  99.524  1.00 79.73  ?  295 ARG A NH1 1 
ATOM   985  N NH2 . ARG A 1 314 ? -21.258 68.010  98.026  1.00 67.59  ?  295 ARG A NH2 1 
ATOM   986  N N   . GLN A 1 315 ? -15.088 67.121  102.621 1.00 64.14  ?  296 GLN A N   1 
ATOM   987  C CA  . GLN A 1 315 ? -14.818 66.610  103.950 1.00 67.23  ?  296 GLN A CA  1 
ATOM   988  C C   . GLN A 1 315 ? -14.535 67.732  104.936 1.00 71.92  ?  296 GLN A C   1 
ATOM   989  O O   . GLN A 1 315 ? -14.973 67.660  106.086 1.00 74.54  ?  296 GLN A O   1 
ATOM   990  C CB  . GLN A 1 315 ? -13.645 65.641  103.898 1.00 65.16  ?  296 GLN A CB  1 
ATOM   991  C CG  . GLN A 1 315 ? -13.974 64.337  103.240 1.00 68.12  ?  296 GLN A CG  1 
ATOM   992  C CD  . GLN A 1 315 ? -14.988 63.541  104.014 1.00 72.10  ?  296 GLN A CD  1 
ATOM   993  O OE1 . GLN A 1 315 ? -16.193 63.621  103.736 1.00 78.06  ?  296 GLN A OE1 1 
ATOM   994  N NE2 . GLN A 1 315 ? -14.516 62.753  104.984 1.00 69.64  ?  296 GLN A NE2 1 
ATOM   995  N N   . LEU A 1 316 ? -13.770 68.756  104.531 1.00 68.50  ?  297 LEU A N   1 
ATOM   996  C CA  . LEU A 1 316 ? -13.394 69.786  105.495 1.00 66.07  ?  297 LEU A CA  1 
ATOM   997  C C   . LEU A 1 316 ? -14.618 70.582  105.912 1.00 71.52  ?  297 LEU A C   1 
ATOM   998  O O   . LEU A 1 316 ? -14.896 70.722  107.108 1.00 78.67  ?  297 LEU A O   1 
ATOM   999  C CB  . LEU A 1 316 ? -12.293 70.692  104.940 1.00 56.50  ?  297 LEU A CB  1 
ATOM   1000 C CG  . LEU A 1 316 ? -10.959 69.949  104.880 1.00 57.00  ?  297 LEU A CG  1 
ATOM   1001 C CD1 . LEU A 1 316 ? -9.847  70.749  104.218 1.00 51.65  ?  297 LEU A CD1 1 
ATOM   1002 C CD2 . LEU A 1 316 ? -10.559 69.434  106.266 1.00 54.20  ?  297 LEU A CD2 1 
ATOM   1003 N N   . GLN A 1 317 ? -15.394 71.056  104.940 1.00 66.89  ?  298 GLN A N   1 
ATOM   1004 C CA  . GLN A 1 317 ? -16.713 71.589  105.241 1.00 63.61  ?  298 GLN A CA  1 
ATOM   1005 C C   . GLN A 1 317 ? -17.513 70.632  106.122 1.00 71.80  ?  298 GLN A C   1 
ATOM   1006 O O   . GLN A 1 317 ? -18.089 71.032  107.136 1.00 80.75  ?  298 GLN A O   1 
ATOM   1007 C CB  . GLN A 1 317 ? -17.445 71.862  103.943 1.00 63.39  ?  298 GLN A CB  1 
ATOM   1008 C CG  . GLN A 1 317 ? -18.609 72.768  104.100 1.00 76.03  ?  298 GLN A CG  1 
ATOM   1009 C CD  . GLN A 1 317 ? -19.423 72.874  102.836 1.00 83.36  ?  298 GLN A CD  1 
ATOM   1010 O OE1 . GLN A 1 317 ? -20.043 71.888  102.407 1.00 85.76  ?  298 GLN A OE1 1 
ATOM   1011 N NE2 . GLN A 1 317 ? -19.415 74.071  102.210 1.00 66.38  ?  298 GLN A NE2 1 
ATOM   1012 N N   . SER A 1 318 ? -17.537 69.353  105.766 1.00 79.38  ?  299 SER A N   1 
ATOM   1013 C CA  . SER A 1 318 ? -18.183 68.341  106.604 1.00 78.50  ?  299 SER A CA  1 
ATOM   1014 C C   . SER A 1 318 ? -17.711 68.363  108.061 1.00 77.30  ?  299 SER A C   1 
ATOM   1015 O O   . SER A 1 318 ? -18.418 67.867  108.942 1.00 77.61  ?  299 SER A O   1 
ATOM   1016 C CB  . SER A 1 318 ? -17.924 66.957  105.987 1.00 79.64  ?  299 SER A CB  1 
ATOM   1017 O OG  . SER A 1 318 ? -18.423 65.892  106.777 1.00 93.65  ?  299 SER A OG  1 
ATOM   1018 N N   . PHE A 1 319 ? -16.529 68.900  108.344 1.00 75.86  ?  300 PHE A N   1 
ATOM   1019 C CA  . PHE A 1 319 ? -15.966 68.840  109.684 1.00 79.81  ?  300 PHE A CA  1 
ATOM   1020 C C   . PHE A 1 319 ? -16.093 70.176  110.416 1.00 87.81  ?  300 PHE A C   1 
ATOM   1021 O O   . PHE A 1 319 ? -15.504 70.358  111.492 1.00 86.64  ?  300 PHE A O   1 
ATOM   1022 C CB  . PHE A 1 319 ? -14.498 68.406  109.619 1.00 76.93  ?  300 PHE A CB  1 
ATOM   1023 C CG  . PHE A 1 319 ? -14.281 67.012  109.089 1.00 81.52  ?  300 PHE A CG  1 
ATOM   1024 C CD1 . PHE A 1 319 ? -15.348 66.221  108.669 1.00 89.97  ?  300 PHE A CD1 1 
ATOM   1025 C CD2 . PHE A 1 319 ? -12.996 66.509  108.972 1.00 83.76  ?  300 PHE A CD2 1 
ATOM   1026 C CE1 . PHE A 1 319 ? -15.133 64.948  108.162 1.00 81.87  ?  300 PHE A CE1 1 
ATOM   1027 C CE2 . PHE A 1 319 ? -12.771 65.249  108.481 1.00 74.76  ?  300 PHE A CE2 1 
ATOM   1028 C CZ  . PHE A 1 319 ? -13.839 64.463  108.080 1.00 81.88  ?  300 PHE A CZ  1 
ATOM   1029 N N   . GLY A 1 320 ? -16.858 71.105  109.859 1.00 79.95  ?  301 GLY A N   1 
ATOM   1030 C CA  . GLY A 1 320 ? -16.995 72.405  110.456 1.00 78.72  ?  301 GLY A CA  1 
ATOM   1031 C C   . GLY A 1 320 ? -15.806 73.298  110.209 1.00 87.70  ?  301 GLY A C   1 
ATOM   1032 O O   . GLY A 1 320 ? -15.387 74.035  111.114 1.00 97.45  ?  301 GLY A O   1 
ATOM   1033 N N   . MET A 1 321 ? -15.229 73.252  109.017 1.00 79.26  ?  302 MET A N   1 
ATOM   1034 C CA  . MET A 1 321 ? -14.173 74.187  108.692 1.00 73.51  ?  302 MET A CA  1 
ATOM   1035 C C   . MET A 1 321 ? -14.634 75.094  107.576 1.00 76.63  ?  302 MET A C   1 
ATOM   1036 O O   . MET A 1 321 ? -15.624 74.817  106.885 1.00 77.78  ?  302 MET A O   1 
ATOM   1037 C CB  . MET A 1 321 ? -12.882 73.491  108.298 1.00 66.99  ?  302 MET A CB  1 
ATOM   1038 C CG  . MET A 1 321 ? -12.241 72.807  109.462 1.00 72.26  ?  302 MET A CG  1 
ATOM   1039 S SD  . MET A 1 321 ? -10.553 72.279  109.117 1.00 73.60  ?  302 MET A SD  1 
ATOM   1040 C CE  . MET A 1 321 ? -9.516  73.612  109.762 1.00 72.80  ?  302 MET A CE  1 
ATOM   1041 N N   . ASP A 1 322 ? -13.901 76.197  107.438 1.00 75.08  ?  303 ASP A N   1 
ATOM   1042 C CA  . ASP A 1 322 ? -14.145 77.184  106.397 1.00 78.80  ?  303 ASP A CA  1 
ATOM   1043 C C   . ASP A 1 322 ? -13.246 76.836  105.219 1.00 80.90  ?  303 ASP A C   1 
ATOM   1044 O O   . ASP A 1 322 ? -12.012 76.911  105.326 1.00 76.72  ?  303 ASP A O   1 
ATOM   1045 C CB  . ASP A 1 322 ? -13.859 78.590  106.920 1.00 89.06  ?  303 ASP A CB  1 
ATOM   1046 C CG  . ASP A 1 322 ? -14.534 79.687  106.094 1.00 97.80  ?  303 ASP A CG  1 
ATOM   1047 O OD1 . ASP A 1 322 ? -15.097 79.366  105.018 1.00 105.11 ?  303 ASP A OD1 1 
ATOM   1048 O OD2 . ASP A 1 322 ? -14.492 80.870  106.527 1.00 96.66  ?  303 ASP A OD2 1 
ATOM   1049 N N   . VAL A 1 323 ? -13.854 76.453  104.097 1.00 78.72  ?  304 VAL A N   1 
ATOM   1050 C CA  . VAL A 1 323 ? -13.104 75.949  102.952 1.00 78.47  ?  304 VAL A CA  1 
ATOM   1051 C C   . VAL A 1 323 ? -13.410 76.785  101.721 1.00 72.99  ?  304 VAL A C   1 
ATOM   1052 O O   . VAL A 1 323 ? -14.579 76.976  101.370 1.00 76.22  ?  304 VAL A O   1 
ATOM   1053 C CB  . VAL A 1 323 ? -13.422 74.475  102.675 1.00 70.28  ?  304 VAL A CB  1 
ATOM   1054 C CG1 . VAL A 1 323 ? -12.522 73.970  101.598 1.00 67.41  ?  304 VAL A CG1 1 
ATOM   1055 C CG2 . VAL A 1 323 ? -13.241 73.682  103.921 1.00 71.06  ?  304 VAL A CG2 1 
ATOM   1056 N N   . THR A 1 324 ? -12.354 77.249  101.053 1.00 67.83  ?  305 THR A N   1 
ATOM   1057 C CA  . THR A 1 324 ? -12.443 77.899  99.754  1.00 73.35  ?  305 THR A CA  1 
ATOM   1058 C C   . THR A 1 324 ? -11.469 77.225  98.799  1.00 72.64  ?  305 THR A C   1 
ATOM   1059 O O   . THR A 1 324 ? -10.311 76.964  99.166  1.00 67.00  ?  305 THR A O   1 
ATOM   1060 C CB  . THR A 1 324 ? -12.144 79.415  99.847  1.00 73.84  ?  305 THR A CB  1 
ATOM   1061 O OG1 . THR A 1 324 ? -13.236 80.070  100.497 1.00 86.22  ?  305 THR A OG1 1 
ATOM   1062 C CG2 . THR A 1 324 ? -11.943 80.050  98.451  1.00 72.37  ?  305 THR A CG2 1 
ATOM   1063 N N   . LEU A 1 325 ? -11.942 76.945  97.577  1.00 62.79  ?  306 LEU A N   1 
ATOM   1064 C CA  . LEU A 1 325 ? -11.111 76.364  96.535  1.00 64.11  ?  306 LEU A CA  1 
ATOM   1065 C C   . LEU A 1 325 ? -10.839 77.416  95.475  1.00 62.12  ?  306 LEU A C   1 
ATOM   1066 O O   . LEU A 1 325 ? -11.775 78.063  94.994  1.00 65.12  ?  306 LEU A O   1 
ATOM   1067 C CB  . LEU A 1 325 ? -11.776 75.148  95.883  1.00 65.63  ?  306 LEU A CB  1 
ATOM   1068 C CG  . LEU A 1 325 ? -12.234 73.990  96.758  1.00 59.96  ?  306 LEU A CG  1 
ATOM   1069 C CD1 . LEU A 1 325 ? -13.612 74.303  97.295  1.00 68.30  ?  306 LEU A CD1 1 
ATOM   1070 C CD2 . LEU A 1 325 ? -12.286 72.735  95.956  1.00 61.61  ?  306 LEU A CD2 1 
ATOM   1071 N N   . LEU A 1 326 ? -9.569  77.575  95.104  1.00 55.76  ?  307 LEU A N   1 
ATOM   1072 C CA  . LEU A 1 326 ? -9.187  78.423  93.983  1.00 59.10  ?  307 LEU A CA  1 
ATOM   1073 C C   . LEU A 1 326 ? -8.941  77.532  92.773  1.00 63.89  ?  307 LEU A C   1 
ATOM   1074 O O   . LEU A 1 326 ? -8.174  76.566  92.855  1.00 57.74  ?  307 LEU A O   1 
ATOM   1075 C CB  . LEU A 1 326 ? -7.934  79.247  94.306  1.00 56.23  ?  307 LEU A CB  1 
ATOM   1076 C CG  . LEU A 1 326 ? -7.901  79.826  95.729  1.00 62.01  ?  307 LEU A CG  1 
ATOM   1077 C CD1 . LEU A 1 326 ? -6.591  80.522  96.012  1.00 55.52  ?  307 LEU A CD1 1 
ATOM   1078 C CD2 . LEU A 1 326 ? -9.086  80.756  96.030  1.00 60.84  ?  307 LEU A CD2 1 
ATOM   1079 N N   . GLU A 1 327 ? -9.577  77.847  91.648  1.00 64.18  ?  308 GLU A N   1 
ATOM   1080 C CA  . GLU A 1 327 ? -9.487  76.945  90.517  1.00 59.64  ?  308 GLU A CA  1 
ATOM   1081 C C   . GLU A 1 327 ? -9.122  77.782  89.303  1.00 59.56  ?  308 GLU A C   1 
ATOM   1082 O O   . GLU A 1 327 ? -9.785  78.787  89.035  1.00 63.54  ?  308 GLU A O   1 
ATOM   1083 C CB  . GLU A 1 327 ? -10.814 76.233  90.249  1.00 61.38  ?  308 GLU A CB  1 
ATOM   1084 C CG  . GLU A 1 327 ? -10.563 74.796  89.770  1.00 71.10  ?  308 GLU A CG  1 
ATOM   1085 C CD  . GLU A 1 327 ? -9.907  74.675  88.425  1.00 72.83  ?  308 GLU A CD  1 
ATOM   1086 O OE1 . GLU A 1 327 ? -10.070 75.531  87.533  1.00 69.60  ?  308 GLU A OE1 1 
ATOM   1087 O OE2 . GLU A 1 327 ? -9.156  73.704  88.292  1.00 71.68  ?  308 GLU A OE2 1 
ATOM   1088 N N   . ALA A 1 328 ? -8.090  77.371  88.559  1.00 58.83  ?  309 ALA A N   1 
ATOM   1089 C CA  . ALA A 1 328 ? -7.625  78.190  87.436  1.00 57.86  ?  309 ALA A CA  1 
ATOM   1090 C C   . ALA A 1 328 ? -8.600  78.150  86.253  1.00 66.58  ?  309 ALA A C   1 
ATOM   1091 O O   . ALA A 1 328 ? -8.802  79.161  85.567  1.00 62.87  ?  309 ALA A O   1 
ATOM   1092 C CB  . ALA A 1 328 ? -6.227  77.744  87.001  1.00 47.68  ?  309 ALA A CB  1 
ATOM   1093 N N   . ARG A 1 329 ? -9.209  76.993  85.993  1.00 74.42  ?  310 ARG A N   1 
ATOM   1094 C CA  . ARG A 1 329 ? -10.139 76.851  84.884  1.00 69.36  ?  310 ARG A CA  1 
ATOM   1095 C C   . ARG A 1 329 ? -11.472 77.519  85.207  1.00 70.63  ?  310 ARG A C   1 
ATOM   1096 O O   . ARG A 1 329 ? -11.752 77.941  86.341  1.00 70.49  ?  310 ARG A O   1 
ATOM   1097 C CB  . ARG A 1 329 ? -10.394 75.378  84.570  1.00 67.33  ?  310 ARG A CB  1 
ATOM   1098 C CG  . ARG A 1 329 ? -9.170  74.610  84.115  1.00 70.91  ?  310 ARG A CG  1 
ATOM   1099 C CD  . ARG A 1 329 ? -9.552  73.149  83.925  1.00 66.20  ?  310 ARG A CD  1 
ATOM   1100 N NE  . ARG A 1 329 ? -8.475  72.214  84.229  1.00 63.84  ?  310 ARG A NE  1 
ATOM   1101 C CZ  . ARG A 1 329 ? -7.569  71.797  83.345  1.00 62.29  ?  310 ARG A CZ  1 
ATOM   1102 N NH1 . ARG A 1 329 ? -7.622  72.244  82.094  1.00 54.30  ?  310 ARG A NH1 1 
ATOM   1103 N NH2 . ARG A 1 329 ? -6.622  70.915  83.716  1.00 61.76  ?  310 ARG A NH2 1 
ATOM   1104 N N   . ASP A 1 330 ? -12.309 77.584  84.179  1.00 71.97  ?  311 ASP A N   1 
ATOM   1105 C CA  . ASP A 1 330 ? -13.701 77.980  84.278  1.00 71.07  ?  311 ASP A CA  1 
ATOM   1106 C C   . ASP A 1 330 ? -14.616 76.801  84.549  1.00 70.26  ?  311 ASP A C   1 
ATOM   1107 O O   . ASP A 1 330 ? -15.814 76.871  84.255  1.00 71.15  ?  311 ASP A O   1 
ATOM   1108 C CB  . ASP A 1 330 ? -14.096 78.671  82.991  1.00 70.60  ?  311 ASP A CB  1 
ATOM   1109 C CG  . ASP A 1 330 ? -13.582 77.912  81.776  1.00 87.50  ?  311 ASP A CG  1 
ATOM   1110 O OD1 . ASP A 1 330 ? -14.339 77.811  80.779  1.00 104.47 ?  311 ASP A OD1 1 
ATOM   1111 O OD2 . ASP A 1 330 ? -12.438 77.381  81.837  1.00 90.27  ?  311 ASP A OD2 1 
ATOM   1112 N N   . ARG A 1 331 ? -14.086 75.709  85.088  1.00 65.54  ?  312 ARG A N   1 
ATOM   1113 C CA  . ARG A 1 331 ? -14.937 74.568  85.372  1.00 63.57  ?  312 ARG A CA  1 
ATOM   1114 C C   . ARG A 1 331 ? -14.261 73.731  86.435  1.00 64.11  ?  312 ARG A C   1 
ATOM   1115 O O   . ARG A 1 331 ? -13.031 73.737  86.564  1.00 65.42  ?  312 ARG A O   1 
ATOM   1116 C CB  . ARG A 1 331 ? -15.191 73.715  84.126  1.00 65.77  ?  312 ARG A CB  1 
ATOM   1117 C CG  . ARG A 1 331 ? -13.923 73.088  83.592  1.00 64.41  ?  312 ARG A CG  1 
ATOM   1118 C CD  . ARG A 1 331 ? -14.127 72.164  82.411  1.00 62.44  ?  312 ARG A CD  1 
ATOM   1119 N NE  . ARG A 1 331 ? -12.836 71.613  82.021  1.00 58.93  ?  312 ARG A NE  1 
ATOM   1120 C CZ  . ARG A 1 331 ? -12.201 70.662  82.706  1.00 60.37  ?  312 ARG A CZ  1 
ATOM   1121 N NH1 . ARG A 1 331 ? -12.765 70.123  83.794  1.00 57.51  ?  312 ARG A NH1 1 
ATOM   1122 N NH2 . ARG A 1 331 ? -11.011 70.228  82.289  1.00 56.66  ?  312 ARG A NH2 1 
ATOM   1123 N N   . VAL A 1 332 ? -15.077 73.005  87.186  1.00 60.74  ?  313 VAL A N   1 
ATOM   1124 C CA  . VAL A 1 332 ? -14.548 72.019  88.116  1.00 70.12  ?  313 VAL A CA  1 
ATOM   1125 C C   . VAL A 1 332 ? -14.086 70.771  87.363  1.00 64.84  ?  313 VAL A C   1 
ATOM   1126 O O   . VAL A 1 332 ? -14.416 70.588  86.188  1.00 69.25  ?  313 VAL A O   1 
ATOM   1127 C CB  . VAL A 1 332 ? -15.612 71.674  89.171  1.00 71.43  ?  313 VAL A CB  1 
ATOM   1128 C CG1 . VAL A 1 332 ? -15.785 72.824  90.127  1.00 66.63  ?  313 VAL A CG1 1 
ATOM   1129 C CG2 . VAL A 1 332 ? -16.927 71.389  88.475  1.00 71.35  ?  313 VAL A CG2 1 
ATOM   1130 N N   . GLY A 1 333 ? -13.322 69.897  88.032  1.00 68.57  ?  314 GLY A N   1 
ATOM   1131 C CA  . GLY A 1 333 ? -13.073 68.538  87.577  1.00 60.34  ?  314 GLY A CA  1 
ATOM   1132 C C   . GLY A 1 333 ? -11.640 68.262  87.162  1.00 57.93  ?  314 GLY A C   1 
ATOM   1133 O O   . GLY A 1 333 ? -11.188 67.118  87.258  1.00 61.26  ?  314 GLY A O   1 
ATOM   1134 N N   . GLY A 1 334 ? -10.916 69.271  86.727  1.00 66.29  ?  315 GLY A N   1 
ATOM   1135 C CA  . GLY A 1 334 ? -9.530  69.020  86.362  1.00 62.64  ?  315 GLY A CA  1 
ATOM   1136 C C   . GLY A 1 334 ? -9.452  68.114  85.155  1.00 53.02  ?  315 GLY A C   1 
ATOM   1137 O O   . GLY A 1 334 ? -10.090 68.354  84.125  1.00 54.27  ?  315 GLY A O   1 
ATOM   1138 N N   . ARG A 1 335 ? -8.675  67.047  85.294  1.00 59.82  ?  316 ARG A N   1 
ATOM   1139 C CA  . ARG A 1 335 ? -8.498  66.018  84.269  1.00 53.82  ?  316 ARG A CA  1 
ATOM   1140 C C   . ARG A 1 335 ? -9.700  65.084  84.166  1.00 55.81  ?  316 ARG A C   1 
ATOM   1141 O O   . ARG A 1 335 ? -9.635  64.104  83.439  1.00 62.93  ?  316 ARG A O   1 
ATOM   1142 C CB  . ARG A 1 335 ? -7.202  65.240  84.552  1.00 46.35  ?  316 ARG A CB  1 
ATOM   1143 C CG  . ARG A 1 335 ? -6.123  66.229  84.635  1.00 43.64  ?  316 ARG A CG  1 
ATOM   1144 C CD  . ARG A 1 335 ? -4.680  65.887  84.585  1.00 40.98  ?  316 ARG A CD  1 
ATOM   1145 N NE  . ARG A 1 335 ? -4.148  65.019  85.641  1.00 52.42  ?  316 ARG A NE  1 
ATOM   1146 C CZ  . ARG A 1 335 ? -3.845  65.322  86.899  1.00 46.09  ?  316 ARG A CZ  1 
ATOM   1147 N NH1 . ARG A 1 335 ? -4.122  66.490  87.426  1.00 53.12  ?  316 ARG A NH1 1 
ATOM   1148 N NH2 . ARG A 1 335 ? -3.285  64.393  87.649  1.00 59.27  ?  316 ARG A NH2 1 
ATOM   1149 N N   . VAL A 1 336 ? -10.781 65.346  84.894  1.00 55.34  ?  317 VAL A N   1 
ATOM   1150 C CA  . VAL A 1 336 ? -12.085 64.829  84.522  1.00 51.39  ?  317 VAL A CA  1 
ATOM   1151 C C   . VAL A 1 336 ? -12.768 65.910  83.686  1.00 64.57  ?  317 VAL A C   1 
ATOM   1152 O O   . VAL A 1 336 ? -13.522 66.749  84.197  1.00 68.70  ?  317 VAL A O   1 
ATOM   1153 C CB  . VAL A 1 336 ? -12.903 64.428  85.751  1.00 48.08  ?  317 VAL A CB  1 
ATOM   1154 C CG1 . VAL A 1 336 ? -14.234 63.896  85.337  1.00 61.28  ?  317 VAL A CG1 1 
ATOM   1155 C CG2 . VAL A 1 336 ? -12.146 63.409  86.556  1.00 51.08  ?  317 VAL A CG2 1 
ATOM   1156 N N   . ALA A 1 337 ? -12.432 65.938  82.398  1.00 64.94  ?  318 ALA A N   1 
ATOM   1157 C CA  . ALA A 1 337 ? -13.073 66.758  81.382  1.00 58.19  ?  318 ALA A CA  1 
ATOM   1158 C C   . ALA A 1 337 ? -14.141 65.943  80.647  1.00 72.68  ?  318 ALA A C   1 
ATOM   1159 O O   . ALA A 1 337 ? -13.963 64.744  80.409  1.00 81.52  ?  318 ALA A O   1 
ATOM   1160 C CB  . ALA A 1 337 ? -12.018 67.246  80.397  1.00 55.42  ?  318 ALA A CB  1 
ATOM   1161 N N   . THR A 1 338 ? -15.247 66.590  80.289  1.00 74.42  ?  319 THR A N   1 
ATOM   1162 C CA  . THR A 1 338 ? -16.333 65.943  79.553  1.00 69.03  ?  319 THR A CA  1 
ATOM   1163 C C   . THR A 1 338 ? -16.839 66.886  78.479  1.00 77.26  ?  319 THR A C   1 
ATOM   1164 O O   . THR A 1 338 ? -17.426 67.929  78.786  1.00 85.62  ?  319 THR A O   1 
ATOM   1165 C CB  . THR A 1 338 ? -17.481 65.539  80.464  1.00 74.74  ?  319 THR A CB  1 
ATOM   1166 O OG1 . THR A 1 338 ? -17.069 64.451  81.299  1.00 80.06  ?  319 THR A OG1 1 
ATOM   1167 C CG2 . THR A 1 338 ? -18.675 65.127  79.642  1.00 80.04  ?  319 THR A CG2 1 
ATOM   1168 N N   . PHE A 1 339 ? -16.622 66.513  77.226  1.00 84.26  ?  320 PHE A N   1 
ATOM   1169 C CA  . PHE A 1 339 ? -17.173 67.267  76.113  1.00 81.70  ?  320 PHE A CA  1 
ATOM   1170 C C   . PHE A 1 339 ? -18.678 67.060  76.059  1.00 83.32  ?  320 PHE A C   1 
ATOM   1171 O O   . PHE A 1 339 ? -19.177 65.950  76.286  1.00 85.44  ?  320 PHE A O   1 
ATOM   1172 C CB  . PHE A 1 339 ? -16.516 66.820  74.815  1.00 84.22  ?  320 PHE A CB  1 
ATOM   1173 C CG  . PHE A 1 339 ? -17.093 67.440  73.585  1.00 89.69  ?  320 PHE A CG  1 
ATOM   1174 C CD1 . PHE A 1 339 ? -16.750 68.734  73.222  1.00 86.35  ?  320 PHE A CD1 1 
ATOM   1175 C CD2 . PHE A 1 339 ? -17.942 66.710  72.762  1.00 89.91  ?  320 PHE A CD2 1 
ATOM   1176 C CE1 . PHE A 1 339 ? -17.274 69.309  72.072  1.00 89.60  ?  320 PHE A CE1 1 
ATOM   1177 C CE2 . PHE A 1 339 ? -18.462 67.272  71.616  1.00 91.16  ?  320 PHE A CE2 1 
ATOM   1178 C CZ  . PHE A 1 339 ? -18.123 68.579  71.266  1.00 94.19  ?  320 PHE A CZ  1 
ATOM   1179 N N   . ARG A 1 340 ? -19.405 68.144  75.797  1.00 78.49  ?  321 ARG A N   1 
ATOM   1180 C CA  . ARG A 1 340 ? -20.856 68.097  75.725  1.00 77.21  ?  321 ARG A CA  1 
ATOM   1181 C C   . ARG A 1 340 ? -21.294 69.070  74.652  1.00 86.33  ?  321 ARG A C   1 
ATOM   1182 O O   . ARG A 1 340 ? -20.829 70.212  74.617  1.00 91.83  ?  321 ARG A O   1 
ATOM   1183 C CB  . ARG A 1 340 ? -21.502 68.428  77.070  1.00 70.37  ?  321 ARG A CB  1 
ATOM   1184 C CG  . ARG A 1 340 ? -21.581 67.221  78.021  1.00 79.39  ?  321 ARG A CG  1 
ATOM   1185 C CD  . ARG A 1 340 ? -22.008 67.591  79.449  1.00 74.06  ?  321 ARG A CD  1 
ATOM   1186 N NE  . ARG A 1 340 ? -21.480 66.669  80.451  1.00 74.84  ?  321 ARG A NE  1 
ATOM   1187 C CZ  . ARG A 1 340 ? -22.122 65.570  80.856  1.00 86.64  ?  321 ARG A CZ  1 
ATOM   1188 N NH1 . ARG A 1 340 ? -23.312 65.286  80.331  1.00 86.55  ?  321 ARG A NH1 1 
ATOM   1189 N NH2 . ARG A 1 340 ? -21.584 64.748  81.772  1.00 78.89  ?  321 ARG A NH2 1 
ATOM   1190 N N   . LYS A 1 341 ? -22.153 68.595  73.754  1.00 94.68  ?  322 LYS A N   1 
ATOM   1191 C CA  . LYS A 1 341 ? -22.657 69.391  72.641  1.00 92.95  ?  322 LYS A CA  1 
ATOM   1192 C C   . LYS A 1 341 ? -23.791 68.599  72.003  1.00 94.52  ?  322 LYS A C   1 
ATOM   1193 O O   . LYS A 1 341 ? -23.593 67.452  71.585  1.00 96.24  ?  322 LYS A O   1 
ATOM   1194 C CB  . LYS A 1 341 ? -21.528 69.722  71.654  1.00 81.95  ?  322 LYS A CB  1 
ATOM   1195 C CG  . LYS A 1 341 ? -21.940 70.588  70.494  1.00 83.55  ?  322 LYS A CG  1 
ATOM   1196 C CD  . LYS A 1 341 ? -20.747 71.296  69.847  1.00 84.32  ?  322 LYS A CD  1 
ATOM   1197 C CE  . LYS A 1 341 ? -21.220 72.616  69.205  1.00 95.47  ?  322 LYS A CE  1 
ATOM   1198 N NZ  . LYS A 1 341 ? -20.280 73.231  68.211  1.00 101.23 ?  322 LYS A NZ  1 
ATOM   1199 N N   . GLY A 1 342 ? -24.988 69.179  71.968  1.00 94.60  ?  323 GLY A N   1 
ATOM   1200 C CA  . GLY A 1 342 ? -26.156 68.395  71.610  1.00 98.17  ?  323 GLY A CA  1 
ATOM   1201 C C   . GLY A 1 342 ? -26.260 67.162  72.479  1.00 100.18 ?  323 GLY A C   1 
ATOM   1202 O O   . GLY A 1 342 ? -26.085 67.227  73.703  1.00 99.79  ?  323 GLY A O   1 
ATOM   1203 N N   . ASN A 1 343 ? -26.536 66.015  71.838  1.00 100.18 ?  324 ASN A N   1 
ATOM   1204 C CA  . ASN A 1 343 ? -26.514 64.712  72.501  1.00 99.78  ?  324 ASN A CA  1 
ATOM   1205 C C   . ASN A 1 343 ? -25.124 64.105  72.565  1.00 97.85  ?  324 ASN A C   1 
ATOM   1206 O O   . ASN A 1 343 ? -24.958 63.036  73.170  1.00 93.70  ?  324 ASN A O   1 
ATOM   1207 C CB  . ASN A 1 343 ? -27.421 63.707  71.789  1.00 110.11 ?  324 ASN A CB  1 
ATOM   1208 C CG  . ASN A 1 343 ? -28.851 64.171  71.702  1.00 124.27 ?  324 ASN A CG  1 
ATOM   1209 O OD1 . ASN A 1 343 ? -29.272 65.069  72.442  1.00 125.79 ?  324 ASN A OD1 1 
ATOM   1210 N ND2 . ASN A 1 343 ? -29.620 63.554  70.802  1.00 130.25 ?  324 ASN A ND2 1 
ATOM   1211 N N   . TYR A 1 344 ? -24.138 64.739  71.939  1.00 95.80  ?  325 TYR A N   1 
ATOM   1212 C CA  . TYR A 1 344 ? -22.777 64.226  71.969  1.00 96.45  ?  325 TYR A CA  1 
ATOM   1213 C C   . TYR A 1 344 ? -22.162 64.453  73.350  1.00 97.55  ?  325 TYR A C   1 
ATOM   1214 O O   . TYR A 1 344 ? -22.131 65.584  73.852  1.00 96.89  ?  325 TYR A O   1 
ATOM   1215 C CB  . TYR A 1 344 ? -21.951 64.901  70.877  1.00 92.88  ?  325 TYR A CB  1 
ATOM   1216 C CG  . TYR A 1 344 ? -22.425 64.600  69.467  1.00 99.18  ?  325 TYR A CG  1 
ATOM   1217 C CD1 . TYR A 1 344 ? -22.210 65.507  68.431  1.00 103.94 ?  325 TYR A CD1 1 
ATOM   1218 C CD2 . TYR A 1 344 ? -23.073 63.404  69.166  1.00 99.61  ?  325 TYR A CD2 1 
ATOM   1219 C CE1 . TYR A 1 344 ? -22.642 65.234  67.137  1.00 105.34 ?  325 TYR A CE1 1 
ATOM   1220 C CE2 . TYR A 1 344 ? -23.513 63.122  67.881  1.00 95.96  ?  325 TYR A CE2 1 
ATOM   1221 C CZ  . TYR A 1 344 ? -23.293 64.034  66.868  1.00 104.41 ?  325 TYR A CZ  1 
ATOM   1222 O OH  . TYR A 1 344 ? -23.726 63.750  65.583  1.00 106.60 ?  325 TYR A OH  1 
ATOM   1223 N N   . VAL A 1 345 ? -21.683 63.375  73.964  1.00 90.56  ?  326 VAL A N   1 
ATOM   1224 C CA  . VAL A 1 345 ? -21.033 63.408  75.267  1.00 83.12  ?  326 VAL A CA  1 
ATOM   1225 C C   . VAL A 1 345 ? -19.836 62.473  75.191  1.00 86.77  ?  326 VAL A C   1 
ATOM   1226 O O   . VAL A 1 345 ? -19.982 61.314  74.791  1.00 97.50  ?  326 VAL A O   1 
ATOM   1227 C CB  . VAL A 1 345 ? -22.005 62.967  76.381  1.00 87.48  ?  326 VAL A CB  1 
ATOM   1228 C CG1 . VAL A 1 345 ? -21.275 62.639  77.680  1.00 90.22  ?  326 VAL A CG1 1 
ATOM   1229 C CG2 . VAL A 1 345 ? -23.112 64.003  76.579  1.00 85.98  ?  326 VAL A CG2 1 
ATOM   1230 N N   . ALA A 1 346 ? -18.652 62.961  75.547  1.00 83.05  ?  327 ALA A N   1 
ATOM   1231 C CA  . ALA A 1 346 ? -17.466 62.104  75.456  1.00 85.03  ?  327 ALA A CA  1 
ATOM   1232 C C   . ALA A 1 346 ? -16.380 62.658  76.349  1.00 79.21  ?  327 ALA A C   1 
ATOM   1233 O O   . ALA A 1 346 ? -16.076 63.849  76.229  1.00 81.71  ?  327 ALA A O   1 
ATOM   1234 C CB  . ALA A 1 346 ? -16.974 62.046  73.991  1.00 81.55  ?  327 ALA A CB  1 
ATOM   1235 N N   . ASP A 1 347 ? -15.778 61.843  77.215  1.00 68.55  ?  328 ASP A N   1 
ATOM   1236 C CA  . ASP A 1 347 ? -14.882 62.527  78.119  1.00 75.84  ?  328 ASP A CA  1 
ATOM   1237 C C   . ASP A 1 347 ? -13.537 62.674  77.414  1.00 75.41  ?  328 ASP A C   1 
ATOM   1238 O O   . ASP A 1 347 ? -13.072 61.760  76.722  1.00 69.64  ?  328 ASP A O   1 
ATOM   1239 C CB  . ASP A 1 347 ? -14.625 61.831  79.453  1.00 78.05  ?  328 ASP A CB  1 
ATOM   1240 C CG  . ASP A 1 347 ? -15.846 61.405  80.128  1.00 86.88  ?  328 ASP A CG  1 
ATOM   1241 O OD1 . ASP A 1 347 ? -16.820 61.026  79.488  1.00 101.28 ?  328 ASP A OD1 1 
ATOM   1242 O OD2 . ASP A 1 347 ? -15.932 61.828  81.312  1.00 88.10  ?  328 ASP A OD2 1 
ATOM   1243 N N   . LEU A 1 348 ? -12.872 63.807  77.653  1.00 77.30  ?  329 LEU A N   1 
ATOM   1244 C CA  . LEU A 1 348 ? -11.513 64.017  77.185  1.00 66.08  ?  329 LEU A CA  1 
ATOM   1245 C C   . LEU A 1 348 ? -10.468 63.601  78.205  1.00 65.34  ?  329 LEU A C   1 
ATOM   1246 O O   . LEU A 1 348 ? -9.281  63.565  77.863  1.00 59.17  ?  329 LEU A O   1 
ATOM   1247 C CB  . LEU A 1 348 ? -11.305 65.479  76.847  1.00 77.22  ?  329 LEU A CB  1 
ATOM   1248 C CG  . LEU A 1 348 ? -11.766 65.996  75.489  1.00 82.77  ?  329 LEU A CG  1 
ATOM   1249 C CD1 . LEU A 1 348 ? -11.023 65.218  74.402  1.00 81.53  ?  329 LEU A CD1 1 
ATOM   1250 C CD2 . LEU A 1 348 ? -13.286 65.860  75.374  1.00 79.75  ?  329 LEU A CD2 1 
ATOM   1251 N N   . GLY A 1 349 ? -10.882 63.311  79.442  1.00 64.23  ?  330 GLY A N   1 
ATOM   1252 C CA  . GLY A 1 349 ? -9.963  62.960  80.498  1.00 62.80  ?  330 GLY A CA  1 
ATOM   1253 C C   . GLY A 1 349 ? -10.213 61.546  80.940  1.00 64.85  ?  330 GLY A C   1 
ATOM   1254 O O   . GLY A 1 349 ? -10.345 60.670  80.090  1.00 73.91  ?  330 GLY A O   1 
ATOM   1255 N N   . ALA A 1 350 ? -10.279 61.293  82.239  1.00 60.17  ?  331 ALA A N   1 
ATOM   1256 C CA  . ALA A 1 350 ? -10.684 59.977  82.706  1.00 65.51  ?  331 ALA A CA  1 
ATOM   1257 C C   . ALA A 1 350 ? -12.019 59.570  82.081  1.00 67.99  ?  331 ALA A C   1 
ATOM   1258 O O   . ALA A 1 350 ? -12.899 60.403  81.860  1.00 73.45  ?  331 ALA A O   1 
ATOM   1259 C CB  . ALA A 1 350 ? -10.783 59.968  84.231  1.00 62.30  ?  331 ALA A CB  1 
ATOM   1260 N N   . MET A 1 351 ? -12.145 58.279  81.761  1.00 71.03  ?  332 MET A N   1 
ATOM   1261 C CA  . MET A 1 351 ? -13.372 57.707  81.209  1.00 73.86  ?  332 MET A CA  1 
ATOM   1262 C C   . MET A 1 351 ? -13.685 56.324  81.752  1.00 70.85  ?  332 MET A C   1 
ATOM   1263 O O   . MET A 1 351 ? -14.800 55.843  81.531  1.00 74.26  ?  332 MET A O   1 
ATOM   1264 C CB  . MET A 1 351 ? -13.303 57.630  79.668  1.00 79.43  ?  332 MET A CB  1 
ATOM   1265 C CG  . MET A 1 351 ? -12.342 56.588  79.104  1.00 76.55  ?  332 MET A CG  1 
ATOM   1266 S SD  . MET A 1 351 ? -12.120 56.747  77.293  1.00 102.33 ?  332 MET A SD  1 
ATOM   1267 C CE  . MET A 1 351 ? -10.522 55.922  77.034  1.00 72.85  ?  332 MET A CE  1 
ATOM   1268 N N   . VAL A 1 352 ? -12.774 55.689  82.483  1.00 64.45  ?  333 VAL A N   1 
ATOM   1269 C CA  . VAL A 1 352 ? -12.904 54.297  82.880  1.00 68.72  ?  333 VAL A CA  1 
ATOM   1270 C C   . VAL A 1 352 ? -12.884 54.208  84.394  1.00 69.67  ?  333 VAL A C   1 
ATOM   1271 O O   . VAL A 1 352 ? -11.964 54.729  85.036  1.00 72.71  ?  333 VAL A O   1 
ATOM   1272 C CB  . VAL A 1 352 ? -11.775 53.426  82.297  1.00 70.84  ?  333 VAL A CB  1 
ATOM   1273 C CG1 . VAL A 1 352 ? -11.833 52.035  82.911  1.00 68.82  ?  333 VAL A CG1 1 
ATOM   1274 C CG2 . VAL A 1 352 ? -11.867 53.359  80.786  1.00 68.76  ?  333 VAL A CG2 1 
ATOM   1275 N N   . VAL A 1 353 ? -13.879 53.527  84.954  1.00 73.23  ?  334 VAL A N   1 
ATOM   1276 C CA  . VAL A 1 353 ? -13.875 53.111  86.353  1.00 68.42  ?  334 VAL A CA  1 
ATOM   1277 C C   . VAL A 1 353 ? -13.285 51.713  86.377  1.00 67.73  ?  334 VAL A C   1 
ATOM   1278 O O   . VAL A 1 353 ? -13.822 50.810  85.740  1.00 75.01  ?  334 VAL A O   1 
ATOM   1279 C CB  . VAL A 1 353 ? -15.296 53.134  86.944  1.00 66.54  ?  334 VAL A CB  1 
ATOM   1280 C CG1 . VAL A 1 353 ? -15.284 52.935  88.451  1.00 61.90  ?  334 VAL A CG1 1 
ATOM   1281 C CG2 . VAL A 1 353 ? -15.995 54.440  86.596  1.00 68.69  ?  334 VAL A CG2 1 
ATOM   1282 N N   . THR A 1 354 ? -12.182 51.526  87.091  1.00 67.80  ?  335 THR A N   1 
ATOM   1283 C CA  . THR A 1 354 ? -11.434 50.279  86.956  1.00 70.39  ?  335 THR A CA  1 
ATOM   1284 C C   . THR A 1 354 ? -11.938 49.203  87.906  1.00 76.90  ?  335 THR A C   1 
ATOM   1285 O O   . THR A 1 354 ? -11.158 48.523  88.578  1.00 81.74  ?  335 THR A O   1 
ATOM   1286 C CB  . THR A 1 354 ? -9.945  50.521  87.158  1.00 72.11  ?  335 THR A CB  1 
ATOM   1287 O OG1 . THR A 1 354 ? -9.653  50.672  88.551  1.00 71.11  ?  335 THR A OG1 1 
ATOM   1288 C CG2 . THR A 1 354 ? -9.541  51.766  86.434  1.00 76.52  ?  335 THR A CG2 1 
ATOM   1289 N N   . GLY A 1 355 ? -13.250 49.015  87.960  1.00 74.06  ?  336 GLY A N   1 
ATOM   1290 C CA  . GLY A 1 355 ? -13.755 47.834  88.640  1.00 81.52  ?  336 GLY A CA  1 
ATOM   1291 C C   . GLY A 1 355 ? -14.162 48.128  90.061  1.00 78.58  ?  336 GLY A C   1 
ATOM   1292 O O   . GLY A 1 355 ? -13.373 48.706  90.809  1.00 80.45  ?  336 GLY A O   1 
ATOM   1293 N N   . LEU A 1 356 ? -15.387 47.751  90.442  1.00 74.57  ?  337 LEU A N   1 
ATOM   1294 C CA  . LEU A 1 356 ? -15.980 48.206  91.694  1.00 73.88  ?  337 LEU A CA  1 
ATOM   1295 C C   . LEU A 1 356 ? -15.536 47.401  92.920  1.00 78.33  ?  337 LEU A C   1 
ATOM   1296 O O   . LEU A 1 356 ? -16.011 47.679  94.030  1.00 75.38  ?  337 LEU A O   1 
ATOM   1297 C CB  . LEU A 1 356 ? -17.506 48.185  91.590  1.00 66.15  ?  337 LEU A CB  1 
ATOM   1298 C CG  . LEU A 1 356 ? -18.176 48.861  90.401  1.00 66.65  ?  337 LEU A CG  1 
ATOM   1299 C CD1 . LEU A 1 356 ? -19.698 48.761  90.515  1.00 60.58  ?  337 LEU A CD1 1 
ATOM   1300 C CD2 . LEU A 1 356 ? -17.747 50.304  90.320  1.00 73.73  ?  337 LEU A CD2 1 
ATOM   1301 N N   . GLY A 1 357 ? -14.628 46.442  92.766  1.00 76.56  ?  338 GLY A N   1 
ATOM   1302 C CA  . GLY A 1 357 ? -14.222 45.624  93.892  1.00 76.51  ?  338 GLY A CA  1 
ATOM   1303 C C   . GLY A 1 357 ? -13.299 46.309  94.879  1.00 76.32  ?  338 GLY A C   1 
ATOM   1304 O O   . GLY A 1 357 ? -12.083 46.084  94.866  1.00 77.95  ?  338 GLY A O   1 
ATOM   1305 N N   . GLY A 1 358 ? -13.871 47.113  95.771  1.00 76.84  ?  339 GLY A N   1 
ATOM   1306 C CA  . GLY A 1 358 ? -13.088 47.850  96.740  1.00 75.88  ?  339 GLY A CA  1 
ATOM   1307 C C   . GLY A 1 358 ? -12.735 49.244  96.288  1.00 76.15  ?  339 GLY A C   1 
ATOM   1308 O O   . GLY A 1 358 ? -11.832 49.867  96.859  1.00 73.07  ?  339 GLY A O   1 
ATOM   1309 N N   . ASN A 1 359 ? -13.391 49.728  95.292  1.00 75.30  ?  340 ASN A N   1 
ATOM   1310 C CA  . ASN A 1 359 ? -13.221 51.031  94.696  1.00 71.32  ?  340 ASN A CA  1 
ATOM   1311 C C   . ASN A 1 359 ? -14.102 52.026  95.433  1.00 79.20  ?  340 ASN A C   1 
ATOM   1312 O O   . ASN A 1 359 ? -15.305 51.771  95.599  1.00 79.17  ?  340 ASN A O   1 
ATOM   1313 C CB  . ASN A 1 359 ? -13.590 50.976  93.218  1.00 71.02  ?  340 ASN A CB  1 
ATOM   1314 C CG  . ASN A 1 359 ? -13.285 52.265  92.479  1.00 74.71  ?  340 ASN A CG  1 
ATOM   1315 O OD1 . ASN A 1 359 ? -13.266 53.345  93.064  1.00 79.58  ?  340 ASN A OD1 1 
ATOM   1316 N ND2 . ASN A 1 359 ? -12.994 52.151  91.188  1.00 76.44  ?  340 ASN A ND2 1 
ATOM   1317 N N   . PRO A 1 360 ? -13.542 53.142  95.913  1.00 78.98  ?  341 PRO A N   1 
ATOM   1318 C CA  . PRO A 1 360 ? -14.389 54.186  96.503  1.00 75.00  ?  341 PRO A CA  1 
ATOM   1319 C C   . PRO A 1 360 ? -15.377 54.771  95.519  1.00 72.68  ?  341 PRO A C   1 
ATOM   1320 O O   . PRO A 1 360 ? -16.413 55.290  95.955  1.00 76.10  ?  341 PRO A O   1 
ATOM   1321 C CB  . PRO A 1 360 ? -13.378 55.238  96.975  1.00 75.70  ?  341 PRO A CB  1 
ATOM   1322 C CG  . PRO A 1 360 ? -12.158 54.979  96.147  1.00 72.88  ?  341 PRO A CG  1 
ATOM   1323 C CD  . PRO A 1 360 ? -12.116 53.493  95.989  1.00 74.39  ?  341 PRO A CD  1 
ATOM   1324 N N   . MET A 1 361 ? -15.093 54.656  94.233  1.00 69.06  ?  342 MET A N   1 
ATOM   1325 C CA  . MET A 1 361 ? -16.030 55.222  93.238  1.00 74.11  ?  342 MET A CA  1 
ATOM   1326 C C   . MET A 1 361 ? -17.303 54.391  93.232  1.00 76.64  ?  342 MET A C   1 
ATOM   1327 O O   . MET A 1 361 ? -18.320 54.852  92.749  1.00 73.12  ?  342 MET A O   1 
ATOM   1328 C CB  . MET A 1 361 ? -15.412 55.190  91.851  1.00 69.71  ?  342 MET A CB  1 
ATOM   1329 C CG  . MET A 1 361 ? -14.164 55.977  91.781  1.00 74.65  ?  342 MET A CG  1 
ATOM   1330 S SD  . MET A 1 361 ? -14.489 57.655  92.230  1.00 82.07  ?  342 MET A SD  1 
ATOM   1331 C CE  . MET A 1 361 ? -15.970 57.961  91.288  1.00 79.66  ?  342 MET A CE  1 
ATOM   1332 N N   . ALA A 1 362 ? -17.214 53.183  93.751  1.00 76.09  ?  343 ALA A N   1 
ATOM   1333 C CA  . ALA A 1 362 ? -18.396 52.320  93.827  1.00 74.28  ?  343 ALA A CA  1 
ATOM   1334 C C   . ALA A 1 362 ? -19.427 53.061  94.654  1.00 83.12  ?  343 ALA A C   1 
ATOM   1335 O O   . ALA A 1 362 ? -20.526 53.243  94.197  1.00 85.25  ?  343 ALA A O   1 
ATOM   1336 C CB  . ALA A 1 362 ? -17.988 51.071  94.526  1.00 76.04  ?  343 ALA A CB  1 
ATOM   1337 N N   . VAL A 1 363 ? -19.018 53.491  95.838  1.00 85.20  ?  344 VAL A N   1 
ATOM   1338 C CA  . VAL A 1 363 ? -19.897 54.223  96.782  1.00 78.66  ?  344 VAL A CA  1 
ATOM   1339 C C   . VAL A 1 363 ? -20.374 55.497  96.120  1.00 79.93  ?  344 VAL A C   1 
ATOM   1340 O O   . VAL A 1 363 ? -21.534 55.784  96.198  1.00 85.60  ?  344 VAL A O   1 
ATOM   1341 C CB  . VAL A 1 363 ? -19.117 54.590  98.040  1.00 77.00  ?  344 VAL A CB  1 
ATOM   1342 C CG1 . VAL A 1 363 ? -19.922 55.537  98.891  1.00 76.30  ?  344 VAL A CG1 1 
ATOM   1343 C CG2 . VAL A 1 363 ? -18.729 53.362  98.822  1.00 74.81  ?  344 VAL A CG2 1 
ATOM   1344 N N   . VAL A 1 364 ? -19.490 56.209  95.444  1.00 75.88  ?  345 VAL A N   1 
ATOM   1345 C CA  . VAL A 1 364 ? -19.903 57.482  94.802  1.00 79.77  ?  345 VAL A CA  1 
ATOM   1346 C C   . VAL A 1 364 ? -20.899 57.213  93.691  1.00 81.29  ?  345 VAL A C   1 
ATOM   1347 O O   . VAL A 1 364 ? -21.763 58.028  93.498  1.00 86.50  ?  345 VAL A O   1 
ATOM   1348 C CB  . VAL A 1 364 ? -18.706 58.245  94.245  1.00 81.22  ?  345 VAL A CB  1 
ATOM   1349 C CG1 . VAL A 1 364 ? -19.169 59.494  93.538  1.00 72.79  ?  345 VAL A CG1 1 
ATOM   1350 C CG2 . VAL A 1 364 ? -17.735 58.588  95.347  1.00 80.37  ?  345 VAL A CG2 1 
ATOM   1351 N N   . SER A 1 365 ? -20.771 56.098  92.988  1.00 85.39  ?  346 SER A N   1 
ATOM   1352 C CA  . SER A 1 365 ? -21.719 55.762  91.904  1.00 89.41  ?  346 SER A CA  1 
ATOM   1353 C C   . SER A 1 365 ? -23.145 55.655  92.447  1.00 88.38  ?  346 SER A C   1 
ATOM   1354 O O   . SER A 1 365 ? -24.066 56.044  91.748  1.00 93.29  ?  346 SER A O   1 
ATOM   1355 C CB  . SER A 1 365 ? -21.304 54.501  91.264  1.00 87.21  ?  346 SER A CB  1 
ATOM   1356 O OG  . SER A 1 365 ? -21.785 53.416  92.017  1.00 86.52  ?  346 SER A OG  1 
ATOM   1357 N N   . LYS A 1 366 ? -23.335 55.109  93.635  1.00 85.82  ?  347 LYS A N   1 
ATOM   1358 C CA  . LYS A 1 366 ? -24.705 55.044  94.170  1.00 85.90  ?  347 LYS A CA  1 
ATOM   1359 C C   . LYS A 1 366 ? -25.148 56.434  94.606  1.00 86.56  ?  347 LYS A C   1 
ATOM   1360 O O   . LYS A 1 366 ? -26.319 56.705  94.524  1.00 88.24  ?  347 LYS A O   1 
ATOM   1361 C CB  . LYS A 1 366 ? -24.723 54.117  95.377  1.00 86.03  ?  347 LYS A CB  1 
ATOM   1362 C CG  . LYS A 1 366 ? -23.953 52.826  95.195  1.00 85.86  ?  347 LYS A CG  1 
ATOM   1363 C CD  . LYS A 1 366 ? -24.626 51.676  95.867  1.00 95.27  ?  347 LYS A CD  1 
ATOM   1364 C CE  . LYS A 1 366 ? -23.676 50.837  96.688  1.00 103.08 ?  347 LYS A CE  1 
ATOM   1365 N NZ  . LYS A 1 366 ? -24.369 49.655  97.248  1.00 100.93 ?  347 LYS A NZ  1 
ATOM   1366 N N   . GLN A 1 367 ? -24.227 57.277  95.047  1.00 88.09  ?  348 GLN A N   1 
ATOM   1367 C CA  . GLN A 1 367 ? -24.602 58.616  95.537  1.00 89.21  ?  348 GLN A CA  1 
ATOM   1368 C C   . GLN A 1 367 ? -25.001 59.481  94.350  1.00 89.97  ?  348 GLN A C   1 
ATOM   1369 O O   . GLN A 1 367 ? -25.892 60.290  94.497  1.00 93.76  ?  348 GLN A O   1 
ATOM   1370 C CB  . GLN A 1 367 ? -23.433 59.218  96.301  1.00 85.66  ?  348 GLN A CB  1 
ATOM   1371 C CG  . GLN A 1 367 ? -23.132 58.517  97.611  1.00 84.32  ?  348 GLN A CG  1 
ATOM   1372 C CD  . GLN A 1 367 ? -21.948 59.179  98.252  1.00 81.38  ?  348 GLN A CD  1 
ATOM   1373 O OE1 . GLN A 1 367 ? -21.354 60.072  97.686  1.00 84.87  ?  348 GLN A OE1 1 
ATOM   1374 N NE2 . GLN A 1 367 ? -21.593 58.750  99.440  1.00 82.77  ?  348 GLN A NE2 1 
ATOM   1375 N N   . VAL A 1 368 ? -24.354 59.302  93.210  1.00 92.41  ?  349 VAL A N   1 
ATOM   1376 C CA  . VAL A 1 368 ? -24.711 60.129  92.031  1.00 93.87  ?  349 VAL A CA  1 
ATOM   1377 C C   . VAL A 1 368 ? -25.264 59.223  90.947  1.00 106.71 ?  349 VAL A C   1 
ATOM   1378 O O   . VAL A 1 368 ? -24.858 58.071  90.883  1.00 105.85 ?  349 VAL A O   1 
ATOM   1379 C CB  . VAL A 1 368 ? -23.473 60.850  91.510  1.00 86.83  ?  349 VAL A CB  1 
ATOM   1380 C CG1 . VAL A 1 368 ? -23.852 61.990  90.596  1.00 95.71  ?  349 VAL A CG1 1 
ATOM   1381 C CG2 . VAL A 1 368 ? -22.651 61.349  92.666  1.00 87.78  ?  349 VAL A CG2 1 
ATOM   1382 N N   . ASN A 1 369 ? -26.150 59.750  90.113  1.00 113.82 ?  350 ASN A N   1 
ATOM   1383 C CA  . ASN A 1 369 ? -26.712 58.916  89.032  1.00 122.26 ?  350 ASN A CA  1 
ATOM   1384 C C   . ASN A 1 369 ? -25.652 58.862  87.950  1.00 121.42 ?  350 ASN A C   1 
ATOM   1385 O O   . ASN A 1 369 ? -25.629 59.747  87.102  1.00 120.12 ?  350 ASN A O   1 
ATOM   1386 C CB  . ASN A 1 369 ? -27.962 59.529  88.409  1.00 131.02 ?  350 ASN A CB  1 
ATOM   1387 C CG  . ASN A 1 369 ? -28.249 58.962  87.036  1.00 135.04 ?  350 ASN A CG  1 
ATOM   1388 O OD1 . ASN A 1 369 ? -28.135 57.760  86.826  1.00 132.21 ?  350 ASN A OD1 1 
ATOM   1389 N ND2 . ASN A 1 369 ? -28.620 59.816  86.098  1.00 130.19 ?  350 ASN A ND2 1 
ATOM   1390 N N   . MET A 1 370 ? -24.797 57.857  88.039  1.00 114.47 ?  351 MET A N   1 
ATOM   1391 C CA  . MET A 1 370 ? -23.737 57.637  87.043  1.00 110.84 ?  351 MET A CA  1 
ATOM   1392 C C   . MET A 1 370 ? -24.222 56.440  86.250  1.00 117.28 ?  351 MET A C   1 
ATOM   1393 O O   . MET A 1 370 ? -24.637 55.482  86.888  1.00 119.10 ?  351 MET A O   1 
ATOM   1394 C CB  . MET A 1 370 ? -22.464 57.215  87.767  1.00 103.69 ?  351 MET A CB  1 
ATOM   1395 C CG  . MET A 1 370 ? -21.336 58.188  87.646  1.00 104.57 ?  351 MET A CG  1 
ATOM   1396 S SD  . MET A 1 370 ? -19.933 57.578  88.579  1.00 100.85 ?  351 MET A SD  1 
ATOM   1397 C CE  . MET A 1 370 ? -20.769 56.724  89.910  1.00 75.50  ?  351 MET A CE  1 
ATOM   1398 N N   . GLU A 1 371 ? -24.241 56.522  84.927  1.00 114.17 ?  352 GLU A N   1 
ATOM   1399 C CA  . GLU A 1 371 ? -24.664 55.338  84.153  1.00 110.78 ?  352 GLU A CA  1 
ATOM   1400 C C   . GLU A 1 371 ? -23.396 54.546  83.884  1.00 102.63 ?  352 GLU A C   1 
ATOM   1401 O O   . GLU A 1 371 ? -22.604 54.982  83.066  1.00 98.06  ?  352 GLU A O   1 
ATOM   1402 C CB  . GLU A 1 371 ? -25.283 55.782  82.836  1.00 118.49 ?  352 GLU A CB  1 
ATOM   1403 C CG  . GLU A 1 371 ? -26.755 56.101  82.956  1.00 130.29 ?  352 GLU A CG  1 
ATOM   1404 C CD  . GLU A 1 371 ? -27.534 55.898  81.671  1.00 142.62 ?  352 GLU A CD  1 
ATOM   1405 O OE1 . GLU A 1 371 ? -28.783 55.972  81.710  1.00 138.11 ?  352 GLU A OE1 1 
ATOM   1406 O OE2 . GLU A 1 371 ? -26.888 55.671  80.633  1.00 139.35 ?  352 GLU A OE2 1 
ATOM   1407 N N   . LEU A 1 372 ? -23.248 53.410  84.546  1.00 98.52  ?  353 LEU A N   1 
ATOM   1408 C CA  . LEU A 1 372 ? -22.021 52.602  84.401  1.00 95.17  ?  353 LEU A CA  1 
ATOM   1409 C C   . LEU A 1 372 ? -22.264 51.441  83.451  1.00 90.49  ?  353 LEU A C   1 
ATOM   1410 O O   . LEU A 1 372 ? -22.998 50.533  83.803  1.00 89.33  ?  353 LEU A O   1 
ATOM   1411 C CB  . LEU A 1 372 ? -21.647 52.080  85.782  1.00 91.63  ?  353 LEU A CB  1 
ATOM   1412 C CG  . LEU A 1 372 ? -20.849 53.067  86.611  1.00 89.76  ?  353 LEU A CG  1 
ATOM   1413 C CD1 . LEU A 1 372 ? -19.924 52.334  87.546  1.00 81.39  ?  353 LEU A CD1 1 
ATOM   1414 C CD2 . LEU A 1 372 ? -20.056 53.955  85.690  1.00 84.71  ?  353 LEU A CD2 1 
ATOM   1415 N N   . ALA A 1 373 ? -21.648 51.501  82.284  1.00 91.77  ?  354 ALA A N   1 
ATOM   1416 C CA  . ALA A 1 373 ? -21.749 50.429  81.311  1.00 86.72  ?  354 ALA A CA  1 
ATOM   1417 C C   . ALA A 1 373 ? -20.432 49.671  81.310  1.00 91.00  ?  354 ALA A C   1 
ATOM   1418 O O   . ALA A 1 373 ? -19.386 50.258  81.015  1.00 88.31  ?  354 ALA A O   1 
ATOM   1419 C CB  . ALA A 1 373 ? -22.051 50.974  79.918  1.00 91.15  ?  354 ALA A CB  1 
ATOM   1420 N N   . LYS A 1 374 ? -20.488 48.379  81.660  1.00 95.33  ?  355 LYS A N   1 
ATOM   1421 C CA  . LYS A 1 374 ? -19.335 47.503  81.536  1.00 93.59  ?  355 LYS A CA  1 
ATOM   1422 C C   . LYS A 1 374 ? -18.815 47.574  80.116  1.00 95.02  ?  355 LYS A C   1 
ATOM   1423 O O   . LYS A 1 374 ? -19.576 47.747  79.157  1.00 93.37  ?  355 LYS A O   1 
ATOM   1424 C CB  . LYS A 1 374 ? -19.679 46.048  81.882  1.00 96.12  ?  355 LYS A CB  1 
ATOM   1425 C CG  . LYS A 1 374 ? -19.940 45.790  83.371  1.00 107.93 ?  355 LYS A CG  1 
ATOM   1426 C CD  . LYS A 1 374 ? -20.503 44.377  83.663  1.00 112.30 ?  355 LYS A CD  1 
ATOM   1427 C CE  . LYS A 1 374 ? -19.416 43.287  83.742  1.00 119.73 ?  355 LYS A CE  1 
ATOM   1428 N NZ  . LYS A 1 374 ? -18.663 43.246  85.051  1.00 106.96 ?  355 LYS A NZ  1 
ATOM   1429 N N   . ILE A 1 375 ? -17.499 47.482  79.982  1.00 96.22  ?  356 ILE A N   1 
ATOM   1430 C CA  . ILE A 1 375 ? -16.927 47.271  78.657  1.00 102.85 ?  356 ILE A CA  1 
ATOM   1431 C C   . ILE A 1 375 ? -17.174 45.818  78.276  1.00 111.44 ?  356 ILE A C   1 
ATOM   1432 O O   . ILE A 1 375 ? -17.476 44.954  79.119  1.00 115.32 ?  356 ILE A O   1 
ATOM   1433 C CB  . ILE A 1 375 ? -15.407 47.541  78.579  1.00 102.68 ?  356 ILE A CB  1 
ATOM   1434 C CG1 . ILE A 1 375 ? -14.734 46.376  79.362  1.00 105.14 ?  356 ILE A CG1 1 
ATOM   1435 C CG2 . ILE A 1 375 ? -15.016 48.942  79.070  1.00 85.84  ?  356 ILE A CG2 1 
ATOM   1436 C CD1 . ILE A 1 375 ? -13.375 46.249  79.134  1.00 110.23 ?  356 ILE A CD1 1 
ATOM   1437 N N   . LYS A 1 376 ? -16.955 45.540  77.005  1.00 110.09 ?  357 LYS A N   1 
ATOM   1438 C CA  . LYS A 1 376 ? -16.721 44.196  76.523  1.00 108.46 ?  357 LYS A CA  1 
ATOM   1439 C C   . LYS A 1 376 ? -15.256 44.092  76.101  1.00 107.74 ?  357 LYS A C   1 
ATOM   1440 O O   . LYS A 1 376 ? -14.759 44.923  75.325  1.00 97.90  ?  357 LYS A O   1 
ATOM   1441 C CB  . LYS A 1 376 ? -17.676 43.877  75.367  1.00 108.31 ?  357 LYS A CB  1 
ATOM   1442 C CG  . LYS A 1 376 ? -19.149 44.058  75.720  1.00 109.24 ?  357 LYS A CG  1 
ATOM   1443 C CD  . LYS A 1 376 ? -20.098 43.532  74.646  1.00 111.06 ?  357 LYS A CD  1 
ATOM   1444 C CE  . LYS A 1 376 ? -21.413 44.322  74.643  1.00 108.61 ?  357 LYS A CE  1 
ATOM   1445 N NZ  . LYS A 1 376 ? -22.127 44.214  73.339  1.00 110.45 ?  357 LYS A NZ  1 
ATOM   1446 N N   . GLN A 1 377 ? -14.574 43.057  76.599  1.00 108.80 ?  358 GLN A N   1 
ATOM   1447 C CA  . GLN A 1 377 ? -13.117 43.000  76.497  1.00 108.94 ?  358 GLN A CA  1 
ATOM   1448 C C   . GLN A 1 377 ? -12.589 42.754  75.063  1.00 106.86 ?  358 GLN A C   1 
ATOM   1449 O O   . GLN A 1 377 ? -11.443 43.117  74.786  1.00 98.63  ?  358 GLN A O   1 
ATOM   1450 C CB  . GLN A 1 377 ? -12.577 41.922  77.456  1.00 112.79 ?  358 GLN A CB  1 
ATOM   1451 C CG  . GLN A 1 377 ? -12.662 42.201  78.998  1.00 124.74 ?  358 GLN A CG  1 
ATOM   1452 C CD  . GLN A 1 377 ? -11.815 43.383  79.517  1.00 134.59 ?  358 GLN A CD  1 
ATOM   1453 O OE1 . GLN A 1 377 ? -12.121 43.970  80.575  1.00 136.21 ?  358 GLN A OE1 1 
ATOM   1454 N NE2 . GLN A 1 377 ? -10.763 43.743  78.773  1.00 127.23 ?  358 GLN A NE2 1 
ATOM   1455 N N   . LYS A 1 378 ? -13.380 42.176  74.142  1.00 108.87 ?  359 LYS A N   1 
ATOM   1456 C CA  . LYS A 1 378 ? -12.913 41.834  72.782  1.00 99.78  ?  359 LYS A CA  1 
ATOM   1457 C C   . LYS A 1 378 ? -12.422 43.051  71.998  1.00 93.70  ?  359 LYS A C   1 
ATOM   1458 O O   . LYS A 1 378 ? -13.155 44.032  71.819  1.00 94.87  ?  359 LYS A O   1 
ATOM   1459 C CB  . LYS A 1 378 ? -14.035 41.143  71.987  1.00 98.97  ?  359 LYS A CB  1 
ATOM   1460 C CG  . LYS A 1 378 ? -13.671 40.678  70.527  1.00 104.54 ?  359 LYS A CG  1 
ATOM   1461 C CD  . LYS A 1 378 ? -14.850 40.011  69.756  1.00 112.71 ?  359 LYS A CD  1 
ATOM   1462 C CE  . LYS A 1 378 ? -14.379 39.477  68.410  1.00 117.53 ?  359 LYS A CE  1 
ATOM   1463 N NZ  . LYS A 1 378 ? -14.501 40.425  67.340  1.00 109.25 ?  359 LYS A NZ  1 
ATOM   1464 N N   . CYS A 1 379 ? -11.193 42.954  71.493  1.00 88.32  ?  360 CYS A N   1 
ATOM   1465 C CA  . CYS A 1 379 ? -10.543 44.030  70.748  1.00 89.53  ?  360 CYS A CA  1 
ATOM   1466 C C   . CYS A 1 379 ? -9.948  43.473  69.456  1.00 85.48  ?  360 CYS A C   1 
ATOM   1467 O O   . CYS A 1 379 ? -8.842  42.901  69.467  1.00 85.72  ?  360 CYS A O   1 
ATOM   1468 C CB  . CYS A 1 379 ? -9.469  44.700  71.601  1.00 91.97  ?  360 CYS A CB  1 
ATOM   1469 S SG  . CYS A 1 379 ? -8.775  46.200  70.855  1.00 86.61  ?  360 CYS A SG  1 
ATOM   1470 N N   . PRO A 1 380 ? -10.658 43.602  68.334  1.00 80.55  ?  361 PRO A N   1 
ATOM   1471 C CA  . PRO A 1 380 ? -10.118 43.172  67.036  1.00 76.51  ?  361 PRO A CA  1 
ATOM   1472 C C   . PRO A 1 380 ? -9.066  44.126  66.490  1.00 75.84  ?  361 PRO A C   1 
ATOM   1473 O O   . PRO A 1 380 ? -9.331  45.311  66.303  1.00 78.94  ?  361 PRO A O   1 
ATOM   1474 C CB  . PRO A 1 380 ? -11.352 43.161  66.124  1.00 75.45  ?  361 PRO A CB  1 
ATOM   1475 C CG  . PRO A 1 380 ? -12.310 44.045  66.750  1.00 79.64  ?  361 PRO A CG  1 
ATOM   1476 C CD  . PRO A 1 380 ? -12.092 43.903  68.249  1.00 87.85  ?  361 PRO A CD  1 
ATOM   1477 N N   . LEU A 1 381 ? -7.899  43.585  66.157  1.00 80.87  ?  362 LEU A N   1 
ATOM   1478 C CA  . LEU A 1 381 ? -6.822  44.346  65.539  1.00 79.77  ?  362 LEU A CA  1 
ATOM   1479 C C   . LEU A 1 381 ? -6.955  44.384  64.015  1.00 78.66  ?  362 LEU A C   1 
ATOM   1480 O O   . LEU A 1 381 ? -7.525  43.483  63.400  1.00 82.72  ?  362 LEU A O   1 
ATOM   1481 C CB  . LEU A 1 381 ? -5.476  43.752  65.958  1.00 78.59  ?  362 LEU A CB  1 
ATOM   1482 C CG  . LEU A 1 381 ? -4.887  44.349  67.235  1.00 82.08  ?  362 LEU A CG  1 
ATOM   1483 C CD1 . LEU A 1 381 ? -5.881  44.322  68.408  1.00 81.21  ?  362 LEU A CD1 1 
ATOM   1484 C CD2 . LEU A 1 381 ? -3.647  43.540  67.588  1.00 86.63  ?  362 LEU A CD2 1 
ATOM   1485 N N   . TYR A 1 382 ? -6.533  45.486  63.420  1.00 74.98  ?  363 TYR A N   1 
ATOM   1486 C CA  . TYR A 1 382 ? -6.589  45.660  61.958  1.00 79.45  ?  363 TYR A CA  1 
ATOM   1487 C C   . TYR A 1 382 ? -5.280  46.304  61.572  1.00 88.20  ?  363 TYR A C   1 
ATOM   1488 O O   . TYR A 1 382 ? -4.940  47.258  62.203  1.00 89.04  ?  363 TYR A O   1 
ATOM   1489 C CB  . TYR A 1 382 ? -7.671  46.666  61.594  1.00 81.33  ?  363 TYR A CB  1 
ATOM   1490 C CG  . TYR A 1 382 ? -9.054  46.136  61.815  1.00 84.41  ?  363 TYR A CG  1 
ATOM   1491 C CD1 . TYR A 1 382 ? -9.756  45.544  60.798  1.00 88.92  ?  363 TYR A CD1 1 
ATOM   1492 C CD2 . TYR A 1 382 ? -9.643  46.195  63.053  1.00 84.77  ?  363 TYR A CD2 1 
ATOM   1493 C CE1 . TYR A 1 382 ? -11.015 45.021  61.005  1.00 94.50  ?  363 TYR A CE1 1 
ATOM   1494 C CE2 . TYR A 1 382 ? -10.895 45.672  63.284  1.00 88.36  ?  363 TYR A CE2 1 
ATOM   1495 C CZ  . TYR A 1 382 ? -11.585 45.089  62.253  1.00 93.90  ?  363 TYR A CZ  1 
ATOM   1496 O OH  . TYR A 1 382 ? -12.825 44.588  62.475  1.00 98.56  ?  363 TYR A OH  1 
ATOM   1497 N N   . GLU A 1 383 ? -4.584  45.802  60.564  1.00 96.98  ?  364 GLU A N   1 
ATOM   1498 C CA  . GLU A 1 383 ? -3.279  46.418  60.228  1.00 95.07  ?  364 GLU A CA  1 
ATOM   1499 C C   . GLU A 1 383 ? -3.475  47.608  59.290  1.00 91.64  ?  364 GLU A C   1 
ATOM   1500 O O   . GLU A 1 383 ? -4.580  47.816  58.833  1.00 94.66  ?  364 GLU A O   1 
ATOM   1501 C CB  . GLU A 1 383 ? -2.226  45.355  59.921  1.00 97.17  ?  364 GLU A CB  1 
ATOM   1502 C CG  . GLU A 1 383 ? -2.124  44.935  58.478  1.00 108.07 ?  364 GLU A CG  1 
ATOM   1503 C CD  . GLU A 1 383 ? -0.994  45.660  57.776  1.00 118.58 ?  364 GLU A CD  1 
ATOM   1504 O OE1 . GLU A 1 383 ? -0.507  46.638  58.390  1.00 109.07 ?  364 GLU A OE1 1 
ATOM   1505 O OE2 . GLU A 1 383 ? -0.685  45.338  56.615  1.00 114.12 ?  364 GLU A OE2 1 
ATOM   1506 N N   . ALA A 1 384 ? -2.399  48.292  58.923  1.00 92.23  ?  365 ALA A N   1 
ATOM   1507 C CA  . ALA A 1 384 ? -2.434  49.509  58.087  1.00 95.86  ?  365 ALA A CA  1 
ATOM   1508 C C   . ALA A 1 384 ? -3.156  49.267  56.760  1.00 100.64 ?  365 ALA A C   1 
ATOM   1509 O O   . ALA A 1 384 ? -3.835  50.175  56.302  1.00 97.74  ?  365 ALA A O   1 
ATOM   1510 C CB  . ALA A 1 384 ? -1.031  49.993  57.870  1.00 86.98  ?  365 ALA A CB  1 
ATOM   1511 N N   . ASN A 1 385 ? -3.030  48.095  56.146  1.00 104.19 ?  366 ASN A N   1 
ATOM   1512 C CA  . ASN A 1 385 ? -3.796  47.824  54.906  1.00 102.53 ?  366 ASN A CA  1 
ATOM   1513 C C   . ASN A 1 385 ? -5.299  47.896  55.196  1.00 104.24 ?  366 ASN A C   1 
ATOM   1514 O O   . ASN A 1 385 ? -6.005  48.406  54.344  1.00 107.66 ?  366 ASN A O   1 
ATOM   1515 C CB  . ASN A 1 385 ? -3.366  46.520  54.246  1.00 98.47  ?  366 ASN A CB  1 
ATOM   1516 C CG  . ASN A 1 385 ? -3.565  45.321  55.137  1.00 106.37 ?  366 ASN A CG  1 
ATOM   1517 O OD1 . ASN A 1 385 ? -4.509  45.268  55.902  1.00 106.00 ?  366 ASN A OD1 1 
ATOM   1518 N ND2 . ASN A 1 385 ? -2.679  44.349  55.045  1.00 108.80 ?  366 ASN A ND2 1 
ATOM   1519 N N   . GLY A 1 386 ? -5.764  47.439  56.358  1.00 98.67  ?  367 GLY A N   1 
ATOM   1520 C CA  . GLY A 1 386 ? -7.190  47.489  56.715  1.00 94.49  ?  367 GLY A CA  1 
ATOM   1521 C C   . GLY A 1 386 ? -7.762  46.104  56.875  1.00 103.12 ?  367 GLY A C   1 
ATOM   1522 O O   . GLY A 1 386 ? -8.934  45.975  57.218  1.00 100.32 ?  367 GLY A O   1 
ATOM   1523 N N   . GLN A 1 387 ? -6.942  45.094  56.634  1.00 102.91 ?  368 GLN A N   1 
ATOM   1524 C CA  . GLN A 1 387 ? -7.410  43.706  56.797  1.00 99.75  ?  368 GLN A CA  1 
ATOM   1525 C C   . GLN A 1 387 ? -7.384  43.398  58.280  1.00 90.43  ?  368 GLN A C   1 
ATOM   1526 O O   . GLN A 1 387 ? -6.492  43.860  58.940  1.00 91.04  ?  368 GLN A O   1 
ATOM   1527 C CB  . GLN A 1 387 ? -6.485  42.733  56.071  1.00 105.54 ?  368 GLN A CB  1 
ATOM   1528 C CG  . GLN A 1 387 ? -6.353  42.991  54.578  1.00 112.69 ?  368 GLN A CG  1 
ATOM   1529 C CD  . GLN A 1 387 ? -7.632  42.797  53.806  1.00 114.81 ?  368 GLN A CD  1 
ATOM   1530 O OE1 . GLN A 1 387 ? -8.730  42.983  54.319  1.00 118.23 ?  368 GLN A OE1 1 
ATOM   1531 N NE2 . GLN A 1 387 ? -7.492  42.430  52.546  1.00 108.54 ?  368 GLN A NE2 1 
ATOM   1532 N N   . ALA A 1 388 ? -8.332  42.612  58.751  1.00 87.04  ?  369 ALA A N   1 
ATOM   1533 C CA  . ALA A 1 388 ? -8.340  42.226  60.168  1.00 86.88  ?  369 ALA A CA  1 
ATOM   1534 C C   . ALA A 1 388 ? -7.173  41.283  60.423  1.00 90.99  ?  369 ALA A C   1 
ATOM   1535 O O   . ALA A 1 388 ? -6.839  40.508  59.557  1.00 98.49  ?  369 ALA A O   1 
ATOM   1536 C CB  . ALA A 1 388 ? -9.646  41.565  60.477  1.00 87.59  ?  369 ALA A CB  1 
ATOM   1537 N N   . VAL A 1 389 ? -6.550  41.363  61.581  1.00 88.03  ?  370 VAL A N   1 
ATOM   1538 C CA  . VAL A 1 389 ? -5.440  40.414  61.819  1.00 90.31  ?  370 VAL A CA  1 
ATOM   1539 C C   . VAL A 1 389 ? -6.076  39.055  62.062  1.00 99.48  ?  370 VAL A C   1 
ATOM   1540 O O   . VAL A 1 389 ? -7.068  39.011  62.753  1.00 100.46 ?  370 VAL A O   1 
ATOM   1541 C CB  . VAL A 1 389 ? -4.575  40.870  62.996  1.00 90.13  ?  370 VAL A CB  1 
ATOM   1542 C CG1 . VAL A 1 389 ? -3.748  39.736  63.551  1.00 94.87  ?  370 VAL A CG1 1 
ATOM   1543 C CG2 . VAL A 1 389 ? -3.677  42.013  62.586  1.00 82.75  ?  370 VAL A CG2 1 
ATOM   1544 N N   . PRO A 1 390 ? -5.533  37.959  61.508  1.00 101.85 ?  371 PRO A N   1 
ATOM   1545 C CA  . PRO A 1 390 ? -6.095  36.629  61.682  1.00 96.16  ?  371 PRO A CA  1 
ATOM   1546 C C   . PRO A 1 390 ? -6.037  36.169  63.136  1.00 99.53  ?  371 PRO A C   1 
ATOM   1547 O O   . PRO A 1 390 ? -5.052  36.395  63.749  1.00 100.84 ?  371 PRO A O   1 
ATOM   1548 C CB  . PRO A 1 390 ? -5.096  35.760  60.931  1.00 96.32  ?  371 PRO A CB  1 
ATOM   1549 C CG  . PRO A 1 390 ? -4.529  36.679  59.903  1.00 101.67 ?  371 PRO A CG  1 
ATOM   1550 C CD  . PRO A 1 390 ? -4.368  37.975  60.649  1.00 99.44  ?  371 PRO A CD  1 
ATOM   1551 N N   . LYS A 1 391 ? -7.013  35.379  63.570  1.00 91.56  ?  372 LYS A N   1 
ATOM   1552 C CA  . LYS A 1 391 ? -7.105  34.965  64.986  1.00 97.48  ?  372 LYS A CA  1 
ATOM   1553 C C   . LYS A 1 391 ? -5.840  34.241  65.423  1.00 102.71 ?  372 LYS A C   1 
ATOM   1554 O O   . LYS A 1 391 ? -5.417  34.452  66.534  1.00 107.64 ?  372 LYS A O   1 
ATOM   1555 C CB  . LYS A 1 391 ? -8.205  33.917  65.145  1.00 100.42 ?  372 LYS A CB  1 
ATOM   1556 C CG  . LYS A 1 391 ? -9.569  34.430  65.574  1.00 103.79 ?  372 LYS A CG  1 
ATOM   1557 C CD  . LYS A 1 391 ? -10.215 33.563  66.628  1.00 104.64 ?  372 LYS A CD  1 
ATOM   1558 C CE  . LYS A 1 391 ? -11.459 34.173  67.236  1.00 110.75 ?  372 LYS A CE  1 
ATOM   1559 N NZ  . LYS A 1 391 ? -11.925 33.393  68.406  1.00 105.97 ?  372 LYS A NZ  1 
ATOM   1560 N N   . GLU A 1 392 ? -5.280  33.377  64.600  1.00 107.57 ?  373 GLU A N   1 
ATOM   1561 C CA  . GLU A 1 392 ? -4.088  32.647  65.086  1.00 110.73 ?  373 GLU A CA  1 
ATOM   1562 C C   . GLU A 1 392 ? -2.950  33.622  65.347  1.00 103.70 ?  373 GLU A C   1 
ATOM   1563 O O   . GLU A 1 392 ? -2.269  33.436  66.331  1.00 104.42 ?  373 GLU A O   1 
ATOM   1564 C CB  . GLU A 1 392 ? -3.652  31.592  64.074  1.00 120.50 ?  373 GLU A CB  1 
ATOM   1565 C CG  . GLU A 1 392 ? -4.764  30.646  63.660  1.00 121.56 ?  373 GLU A CG  1 
ATOM   1566 C CD  . GLU A 1 392 ? -4.233  29.340  63.106  1.00 131.26 ?  373 GLU A CD  1 
ATOM   1567 O OE1 . GLU A 1 392 ? -3.050  29.062  63.345  1.00 133.28 ?  373 GLU A OE1 1 
ATOM   1568 O OE2 . GLU A 1 392 ? -4.996  28.614  62.440  1.00 130.24 ?  373 GLU A OE2 1 
ATOM   1569 N N   . LYS A 1 393 ? -2.731  34.591  64.469  1.00 96.44  ?  374 LYS A N   1 
ATOM   1570 C CA  . LYS A 1 393 ? -1.590  35.513  64.690  1.00 101.63 ?  374 LYS A CA  1 
ATOM   1571 C C   . LYS A 1 393 ? -1.816  36.368  65.930  1.00 103.96 ?  374 LYS A C   1 
ATOM   1572 O O   . LYS A 1 393 ? -0.890  36.523  66.717  1.00 100.66 ?  374 LYS A O   1 
ATOM   1573 C CB  . LYS A 1 393 ? -1.330  36.389  63.470  1.00 95.71  ?  374 LYS A CB  1 
ATOM   1574 C CG  . LYS A 1 393 ? 0.142   36.574  63.158  1.00 100.27 ?  374 LYS A CG  1 
ATOM   1575 C CD  . LYS A 1 393 ? 0.381   37.424  61.950  1.00 103.12 ?  374 LYS A CD  1 
ATOM   1576 C CE  . LYS A 1 393 ? 1.367   36.813  60.982  1.00 113.89 ?  374 LYS A CE  1 
ATOM   1577 N NZ  . LYS A 1 393 ? 2.212   35.787  61.635  1.00 113.87 ?  374 LYS A NZ  1 
ATOM   1578 N N   . ASP A 1 394 ? -3.038  36.841  66.118  1.00 101.13 ?  375 ASP A N   1 
ATOM   1579 C CA  . ASP A 1 394 ? -3.334  37.727  67.261  1.00 97.21  ?  375 ASP A CA  1 
ATOM   1580 C C   . ASP A 1 394 ? -3.014  36.982  68.545  1.00 95.78  ?  375 ASP A C   1 
ATOM   1581 O O   . ASP A 1 394 ? -2.332  37.529  69.379  1.00 100.94 ?  375 ASP A O   1 
ATOM   1582 C CB  . ASP A 1 394 ? -4.837  37.962  67.315  1.00 100.31 ?  375 ASP A CB  1 
ATOM   1583 C CG  . ASP A 1 394 ? -5.265  39.365  67.680  1.00 112.93 ?  375 ASP A CG  1 
ATOM   1584 O OD1 . ASP A 1 394 ? -4.631  39.968  68.552  1.00 112.97 ?  375 ASP A OD1 1 
ATOM   1585 O OD2 . ASP A 1 394 ? -6.248  39.826  67.097  1.00 110.46 ?  375 ASP A OD2 1 
ATOM   1586 N N   . GLU A 1 395 ? -3.456  35.746  68.656  1.00 93.51  ?  376 GLU A N   1 
ATOM   1587 C CA  . GLU A 1 395 ? -3.210  34.984  69.893  1.00 91.66  ?  376 GLU A CA  1 
ATOM   1588 C C   . GLU A 1 395 ? -1.722  34.734  70.060  1.00 90.65  ?  376 GLU A C   1 
ATOM   1589 O O   . GLU A 1 395 ? -1.255  34.771  71.178  1.00 90.20  ?  376 GLU A O   1 
ATOM   1590 C CB  . GLU A 1 395 ? -3.973  33.671  69.840  1.00 101.27 ?  376 GLU A CB  1 
ATOM   1591 C CG  . GLU A 1 395 ? -5.460  33.870  69.697  1.00 104.12 ?  376 GLU A CG  1 
ATOM   1592 C CD  . GLU A 1 395 ? -6.275  32.675  70.136  1.00 121.09 ?  376 GLU A CD  1 
ATOM   1593 O OE1 . GLU A 1 395 ? -5.765  31.557  70.015  1.00 122.92 ?  376 GLU A OE1 1 
ATOM   1594 O OE2 . GLU A 1 395 ? -7.407  32.869  70.597  1.00 124.37 ?  376 GLU A OE2 1 
ATOM   1595 N N   . MET A 1 396 ? -1.024  34.453  68.973  1.00 94.99  ?  377 MET A N   1 
ATOM   1596 C CA  . MET A 1 396 ? 0.409   34.106  69.078  1.00 101.53 ?  377 MET A CA  1 
ATOM   1597 C C   . MET A 1 396 ? 1.195   35.276  69.645  1.00 95.27  ?  377 MET A C   1 
ATOM   1598 O O   . MET A 1 396 ? 1.944   35.086  70.579  1.00 93.76  ?  377 MET A O   1 
ATOM   1599 C CB  . MET A 1 396 ? 0.967   33.777  67.698  1.00 106.62 ?  377 MET A CB  1 
ATOM   1600 C CG  . MET A 1 396 ? 2.345   33.187  67.747  1.00 108.75 ?  377 MET A CG  1 
ATOM   1601 S SD  . MET A 1 396 ? 3.575   34.390  67.255  1.00 135.23 ?  377 MET A SD  1 
ATOM   1602 C CE  . MET A 1 396 ? 3.115   34.629  65.543  1.00 115.90 ?  377 MET A CE  1 
ATOM   1603 N N   . VAL A 1 397 ? 1.015   36.437  69.049  1.00 92.40  ?  378 VAL A N   1 
ATOM   1604 C CA  . VAL A 1 397 ? 1.721   37.666  69.414  1.00 90.47  ?  378 VAL A CA  1 
ATOM   1605 C C   . VAL A 1 397 ? 1.420   38.048  70.859  1.00 88.77  ?  378 VAL A C   1 
ATOM   1606 O O   . VAL A 1 397 ? 2.334   38.218  71.675  1.00 87.92  ?  378 VAL A O   1 
ATOM   1607 C CB  . VAL A 1 397 ? 1.351   38.804  68.452  1.00 83.36  ?  378 VAL A CB  1 
ATOM   1608 C CG1 . VAL A 1 397 ? 2.083   40.052  68.833  1.00 81.80  ?  378 VAL A CG1 1 
ATOM   1609 C CG2 . VAL A 1 397 ? 1.712   38.426  67.052  1.00 94.41  ?  378 VAL A CG2 1 
ATOM   1610 N N   . GLU A 1 398 ? 0.133   38.181  71.192  1.00 85.96  ?  379 GLU A N   1 
ATOM   1611 C CA  . GLU A 1 398 ? -0.258  38.532  72.552  1.00 82.85  ?  379 GLU A CA  1 
ATOM   1612 C C   . GLU A 1 398 ? 0.449   37.676  73.594  1.00 84.07  ?  379 GLU A C   1 
ATOM   1613 O O   . GLU A 1 398 ? 0.944   38.207  74.602  1.00 79.51  ?  379 GLU A O   1 
ATOM   1614 C CB  . GLU A 1 398 ? -1.775  38.428  72.709  1.00 86.31  ?  379 GLU A CB  1 
ATOM   1615 C CG  . GLU A 1 398 ? -2.285  39.181  73.940  1.00 95.16  ?  379 GLU A CG  1 
ATOM   1616 C CD  . GLU A 1 398 ? -3.807  39.252  74.038  1.00 105.80 ?  379 GLU A CD  1 
ATOM   1617 O OE1 . GLU A 1 398 ? -4.348  39.196  75.181  1.00 104.06 ?  379 GLU A OE1 1 
ATOM   1618 O OE2 . GLU A 1 398 ? -4.451  39.409  72.969  1.00 107.54 ?  379 GLU A OE2 1 
ATOM   1619 N N   . GLN A 1 399 ? 0.549   36.355  73.349  1.00 85.51  ?  380 GLN A N   1 
ATOM   1620 C CA  . GLN A 1 399 ? 1.095   35.475  74.374  1.00 84.19  ?  380 GLN A CA  1 
ATOM   1621 C C   . GLN A 1 399 ? 2.581   35.761  74.512  1.00 82.21  ?  380 GLN A C   1 
ATOM   1622 O O   . GLN A 1 399 ? 3.165   35.610  75.595  1.00 82.84  ?  380 GLN A O   1 
ATOM   1623 C CB  . GLN A 1 399 ? 1.018   34.011  73.979  1.00 100.20 ?  380 GLN A CB  1 
ATOM   1624 C CG  . GLN A 1 399 ? 0.773   32.983  75.113  1.00 112.83 ?  380 GLN A CG  1 
ATOM   1625 C CD  . GLN A 1 399 ? 1.394   31.606  74.822  1.00 116.89 ?  380 GLN A CD  1 
ATOM   1626 O OE1 . GLN A 1 399 ? 2.478   31.535  74.220  1.00 108.65 ?  380 GLN A OE1 1 
ATOM   1627 N NE2 . GLN A 1 399 ? 0.580   30.563  74.932  1.00 119.43 ?  380 GLN A NE2 1 
ATOM   1628 N N   . GLU A 1 400 ? 3.211   36.092  73.381  1.00 78.78  ?  381 GLU A N   1 
ATOM   1629 C CA  . GLU A 1 400 ? 4.616   36.461  73.377  1.00 80.03  ?  381 GLU A CA  1 
ATOM   1630 C C   . GLU A 1 400 ? 4.812   37.771  74.120  1.00 80.94  ?  381 GLU A C   1 
ATOM   1631 O O   . GLU A 1 400 ? 5.706   37.896  74.972  1.00 75.24  ?  381 GLU A O   1 
ATOM   1632 C CB  . GLU A 1 400 ? 5.114   36.544  71.931  1.00 76.45  ?  381 GLU A CB  1 
ATOM   1633 C CG  . GLU A 1 400 ? 6.629   36.384  71.788  1.00 83.65  ?  381 GLU A CG  1 
ATOM   1634 C CD  . GLU A 1 400 ? 7.172   35.030  72.330  1.00 94.71  ?  381 GLU A CD  1 
ATOM   1635 O OE1 . GLU A 1 400 ? 6.400   34.053  72.515  1.00 94.71  ?  381 GLU A OE1 1 
ATOM   1636 O OE2 . GLU A 1 400 ? 8.392   34.952  72.605  1.00 97.77  ?  381 GLU A OE2 1 
ATOM   1637 N N   . PHE A 1 401 ? 3.942   38.747  73.830  1.00 81.43  ?  382 PHE A N   1 
ATOM   1638 C CA  . PHE A 1 401 ? 3.887   39.985  74.589  1.00 71.94  ?  382 PHE A CA  1 
ATOM   1639 C C   . PHE A 1 401 ? 3.881   39.704  76.091  1.00 76.13  ?  382 PHE A C   1 
ATOM   1640 O O   . PHE A 1 401 ? 4.761   40.174  76.828  1.00 76.60  ?  382 PHE A O   1 
ATOM   1641 C CB  . PHE A 1 401 ? 2.656   40.795  74.170  1.00 76.90  ?  382 PHE A CB  1 
ATOM   1642 C CG  . PHE A 1 401 ? 2.376   41.978  75.072  1.00 82.59  ?  382 PHE A CG  1 
ATOM   1643 C CD1 . PHE A 1 401 ? 3.335   42.969  75.263  1.00 74.02  ?  382 PHE A CD1 1 
ATOM   1644 C CD2 . PHE A 1 401 ? 1.173   42.083  75.753  1.00 82.72  ?  382 PHE A CD2 1 
ATOM   1645 C CE1 . PHE A 1 401 ? 3.102   44.007  76.098  1.00 70.37  ?  382 PHE A CE1 1 
ATOM   1646 C CE2 . PHE A 1 401 ? 0.938   43.142  76.597  1.00 80.84  ?  382 PHE A CE2 1 
ATOM   1647 C CZ  . PHE A 1 401 ? 1.900   44.097  76.770  1.00 72.85  ?  382 PHE A CZ  1 
ATOM   1648 N N   . ASN A 1 402 ? 2.917   38.904  76.562  1.00 73.33  ?  383 ASN A N   1 
ATOM   1649 C CA  . ASN A 1 402 ? 2.873   38.638  77.997  1.00 74.36  ?  383 ASN A CA  1 
ATOM   1650 C C   . ASN A 1 402 ? 4.087   37.861  78.461  1.00 76.01  ?  383 ASN A C   1 
ATOM   1651 O O   . ASN A 1 402 ? 4.549   38.055  79.592  1.00 78.78  ?  383 ASN A O   1 
ATOM   1652 C CB  . ASN A 1 402 ? 1.596   37.904  78.382  1.00 67.51  ?  383 ASN A CB  1 
ATOM   1653 C CG  . ASN A 1 402 ? 0.360   38.610  77.875  1.00 82.88  ?  383 ASN A CG  1 
ATOM   1654 O OD1 . ASN A 1 402 ? -0.345  38.092  77.017  1.00 82.56  ?  383 ASN A OD1 1 
ATOM   1655 N ND2 . ASN A 1 402 ? 0.129   39.848  78.355  1.00 87.43  ?  383 ASN A ND2 1 
ATOM   1656 N N   . ARG A 1 403 ? 4.623   36.995  77.608  1.00 76.03  ?  384 ARG A N   1 
ATOM   1657 C CA  . ARG A 1 403 ? 5.810   36.250  77.990  1.00 79.51  ?  384 ARG A CA  1 
ATOM   1658 C C   . ARG A 1 403 ? 7.014   37.183  78.077  1.00 72.56  ?  384 ARG A C   1 
ATOM   1659 O O   . ARG A 1 403 ? 7.873   37.033  78.959  1.00 70.28  ?  384 ARG A O   1 
ATOM   1660 C CB  . ARG A 1 403 ? 6.023   35.106  76.991  1.00 89.02  ?  384 ARG A CB  1 
ATOM   1661 C CG  . ARG A 1 403 ? 5.166   33.848  77.224  1.00 92.92  ?  384 ARG A CG  1 
ATOM   1662 C CD  . ARG A 1 403 ? 5.133   32.891  75.999  1.00 97.07  ?  384 ARG A CD  1 
ATOM   1663 N NE  . ARG A 1 403 ? 6.443   32.321  75.655  1.00 109.22 ?  384 ARG A NE  1 
ATOM   1664 C CZ  . ARG A 1 403 ? 7.154   31.478  76.416  1.00 117.31 ?  384 ARG A CZ  1 
ATOM   1665 N NH1 . ARG A 1 403 ? 6.704   31.059  77.608  1.00 110.69 ?  384 ARG A NH1 1 
ATOM   1666 N NH2 . ARG A 1 403 ? 8.343   31.050  75.981  1.00 111.39 ?  384 ARG A NH2 1 
ATOM   1667 N N   . LEU A 1 404 ? 7.063   38.182  77.192  1.00 71.70  ?  385 LEU A N   1 
ATOM   1668 C CA  . LEU A 1 404 ? 8.118   39.187  77.258  1.00 72.27  ?  385 LEU A CA  1 
ATOM   1669 C C   . LEU A 1 404 ? 8.017   40.043  78.524  1.00 76.97  ?  385 LEU A C   1 
ATOM   1670 O O   . LEU A 1 404 ? 9.046   40.419  79.106  1.00 76.42  ?  385 LEU A O   1 
ATOM   1671 C CB  . LEU A 1 404 ? 8.073   40.065  76.017  1.00 67.18  ?  385 LEU A CB  1 
ATOM   1672 C CG  . LEU A 1 404 ? 8.540   39.479  74.692  1.00 69.05  ?  385 LEU A CG  1 
ATOM   1673 C CD1 . LEU A 1 404 ? 7.937   40.248  73.510  1.00 62.68  ?  385 LEU A CD1 1 
ATOM   1674 C CD2 . LEU A 1 404 ? 10.051  39.520  74.636  1.00 68.66  ?  385 LEU A CD2 1 
ATOM   1675 N N   . LEU A 1 405 ? 6.798   40.369  78.969  1.00 70.00  ?  386 LEU A N   1 
ATOM   1676 C CA  . LEU A 1 405 ? 6.653   41.072  80.244  1.00 72.33  ?  386 LEU A CA  1 
ATOM   1677 C C   . LEU A 1 405 ? 7.167   40.232  81.419  1.00 77.66  ?  386 LEU A C   1 
ATOM   1678 O O   . LEU A 1 405 ? 7.951   40.725  82.242  1.00 75.60  ?  386 LEU A O   1 
ATOM   1679 C CB  . LEU A 1 405 ? 5.197   41.473  80.459  1.00 75.18  ?  386 LEU A CB  1 
ATOM   1680 C CG  . LEU A 1 405 ? 4.788   42.676  79.615  1.00 76.30  ?  386 LEU A CG  1 
ATOM   1681 C CD1 . LEU A 1 405 ? 3.285   42.869  79.585  1.00 76.76  ?  386 LEU A CD1 1 
ATOM   1682 C CD2 . LEU A 1 405 ? 5.468   43.891  80.167  1.00 70.12  ?  386 LEU A CD2 1 
ATOM   1683 N N   . GLU A 1 406 ? 6.730   38.960  81.527  1.00 71.73  ?  387 GLU A N   1 
ATOM   1684 C CA  . GLU A 1 406 ? 7.268   38.112  82.588  1.00 72.01  ?  387 GLU A CA  1 
ATOM   1685 C C   . GLU A 1 406 ? 8.785   38.023  82.508  1.00 74.93  ?  387 GLU A C   1 
ATOM   1686 O O   . GLU A 1 406 ? 9.464   37.912  83.541  1.00 74.32  ?  387 GLU A O   1 
ATOM   1687 C CB  . GLU A 1 406 ? 6.720   36.695  82.529  1.00 80.76  ?  387 GLU A CB  1 
ATOM   1688 C CG  . GLU A 1 406 ? 5.246   36.467  82.332  1.00 89.84  ?  387 GLU A CG  1 
ATOM   1689 C CD  . GLU A 1 406 ? 4.937   34.942  82.224  1.00 107.48 ?  387 GLU A CD  1 
ATOM   1690 O OE1 . GLU A 1 406 ? 5.567   34.125  82.964  1.00 107.22 ?  387 GLU A OE1 1 
ATOM   1691 O OE2 . GLU A 1 406 ? 4.131   34.557  81.331  1.00 102.54 ?  387 GLU A OE2 1 
ATOM   1692 N N   . ALA A 1 407 ? 9.332   38.043  81.291  1.00 71.11  ?  388 ALA A N   1 
ATOM   1693 C CA  . ALA A 1 407 ? 10.774  37.945  81.137  1.00 71.70  ?  388 ALA A CA  1 
ATOM   1694 C C   . ALA A 1 407 ? 11.479  39.141  81.771  1.00 74.63  ?  388 ALA A C   1 
ATOM   1695 O O   . ALA A 1 407 ? 12.502  38.980  82.460  1.00 72.44  ?  388 ALA A O   1 
ATOM   1696 C CB  . ALA A 1 407 ? 11.109  37.821  79.656  1.00 77.34  ?  388 ALA A CB  1 
ATOM   1697 N N   . THR A 1 408 ? 10.944  40.349  81.539  1.00 73.85  ?  389 THR A N   1 
ATOM   1698 C CA  . THR A 1 408 ? 11.497  41.549  82.161  1.00 70.93  ?  389 THR A CA  1 
ATOM   1699 C C   . THR A 1 408 ? 11.398  41.461  83.667  1.00 71.36  ?  389 THR A C   1 
ATOM   1700 O O   . THR A 1 408 ? 12.315  41.879  84.386  1.00 70.31  ?  389 THR A O   1 
ATOM   1701 C CB  . THR A 1 408 ? 10.758  42.791  81.676  1.00 71.66  ?  389 THR A CB  1 
ATOM   1702 O OG1 . THR A 1 408 ? 9.351   42.610  81.888  1.00 76.08  ?  389 THR A OG1 1 
ATOM   1703 C CG2 . THR A 1 408 ? 11.007  43.026  80.199  1.00 72.69  ?  389 THR A CG2 1 
ATOM   1704 N N   . SER A 1 409 ? 10.290  40.909  84.165  1.00 70.66  ?  390 SER A N   1 
ATOM   1705 C CA  . SER A 1 409 ? 10.158  40.764  85.602  1.00 71.83  ?  390 SER A CA  1 
ATOM   1706 C C   . SER A 1 409 ? 11.243  39.847  86.145  1.00 75.60  ?  390 SER A C   1 
ATOM   1707 O O   . SER A 1 409 ? 11.849  40.138  87.186  1.00 77.88  ?  390 SER A O   1 
ATOM   1708 C CB  . SER A 1 409 ? 8.769   40.257  85.950  1.00 63.77  ?  390 SER A CB  1 
ATOM   1709 O OG  . SER A 1 409 ? 8.647   40.227  87.361  1.00 75.84  ?  390 SER A OG  1 
ATOM   1710 N N   . TYR A 1 410 ? 11.539  38.766  85.413  1.00 73.04  ?  391 TYR A N   1 
ATOM   1711 C CA  . TYR A 1 410 ? 12.599  37.849  85.811  1.00 78.79  ?  391 TYR A CA  1 
ATOM   1712 C C   . TYR A 1 410 ? 13.974  38.528  85.755  1.00 83.28  ?  391 TYR A C   1 
ATOM   1713 O O   . TYR A 1 410 ? 14.762  38.410  86.707  1.00 85.21  ?  391 TYR A O   1 
ATOM   1714 C CB  . TYR A 1 410 ? 12.523  36.586  84.936  1.00 88.03  ?  391 TYR A CB  1 
ATOM   1715 C CG  . TYR A 1 410 ? 13.638  35.566  85.127  1.00 91.42  ?  391 TYR A CG  1 
ATOM   1716 C CD1 . TYR A 1 410 ? 14.701  35.502  84.240  1.00 91.61  ?  391 TYR A CD1 1 
ATOM   1717 C CD2 . TYR A 1 410 ? 13.622  34.676  86.188  1.00 96.78  ?  391 TYR A CD2 1 
ATOM   1718 C CE1 . TYR A 1 410 ? 15.719  34.594  84.405  1.00 98.37  ?  391 TYR A CE1 1 
ATOM   1719 C CE2 . TYR A 1 410 ? 14.644  33.754  86.363  1.00 105.38 ?  391 TYR A CE2 1 
ATOM   1720 C CZ  . TYR A 1 410 ? 15.694  33.719  85.468  1.00 102.80 ?  391 TYR A CZ  1 
ATOM   1721 O OH  . TYR A 1 410 ? 16.720  32.808  85.635  1.00 102.86 ?  391 TYR A OH  1 
ATOM   1722 N N   . LEU A 1 411 ? 14.283  39.251  84.661  1.00 76.21  ?  392 LEU A N   1 
ATOM   1723 C CA  . LEU A 1 411 ? 15.466  40.116  84.673  1.00 81.60  ?  392 LEU A CA  1 
ATOM   1724 C C   . LEU A 1 411 ? 15.517  41.047  85.871  1.00 85.68  ?  392 LEU A C   1 
ATOM   1725 O O   . LEU A 1 411 ? 16.609  41.373  86.352  1.00 88.71  ?  392 LEU A O   1 
ATOM   1726 C CB  . LEU A 1 411 ? 15.563  40.977  83.421  1.00 78.22  ?  392 LEU A CB  1 
ATOM   1727 C CG  . LEU A 1 411 ? 16.111  40.506  82.109  1.00 79.97  ?  392 LEU A CG  1 
ATOM   1728 C CD1 . LEU A 1 411 ? 15.857  41.560  81.084  1.00 71.07  ?  392 LEU A CD1 1 
ATOM   1729 C CD2 . LEU A 1 411 ? 17.598  40.506  82.392  1.00 86.39  ?  392 LEU A CD2 1 
ATOM   1730 N N   . SER A 1 412 ? 14.372  41.545  86.327  1.00 81.97  ?  393 SER A N   1 
ATOM   1731 C CA  . SER A 1 412 ? 14.419  42.508  87.417  1.00 85.41  ?  393 SER A CA  1 
ATOM   1732 C C   . SER A 1 412 ? 14.683  41.811  88.755  1.00 88.01  ?  393 SER A C   1 
ATOM   1733 O O   . SER A 1 412 ? 15.701  42.064  89.412  1.00 85.89  ?  393 SER A O   1 
ATOM   1734 C CB  . SER A 1 412 ? 13.119  43.318  87.444  1.00 82.18  ?  393 SER A CB  1 
ATOM   1735 O OG  . SER A 1 412 ? 13.187  44.342  88.417  1.00 82.68  ?  393 SER A OG  1 
ATOM   1736 N N   . HIS A 1 413 ? 13.808  40.879  89.140  1.00 86.02  ?  394 HIS A N   1 
ATOM   1737 C CA  . HIS A 1 413 ? 13.782  40.385  90.510  1.00 92.40  ?  394 HIS A CA  1 
ATOM   1738 C C   . HIS A 1 413 ? 14.682  39.178  90.758  1.00 97.92  ?  394 HIS A C   1 
ATOM   1739 O O   . HIS A 1 413 ? 15.054  38.926  91.913  1.00 103.58 ?  394 HIS A O   1 
ATOM   1740 C CB  . HIS A 1 413 ? 12.334  40.066  90.901  1.00 90.48  ?  394 HIS A CB  1 
ATOM   1741 C CG  . HIS A 1 413 ? 11.415  41.245  90.787  1.00 95.82  ?  394 HIS A CG  1 
ATOM   1742 N ND1 . HIS A 1 413 ? 10.242  41.212  90.062  1.00 96.66  ?  394 HIS A ND1 1 
ATOM   1743 C CD2 . HIS A 1 413 ? 11.514  42.505  91.285  1.00 105.06 ?  394 HIS A CD2 1 
ATOM   1744 C CE1 . HIS A 1 413 ? 9.652   42.396  90.126  1.00 103.38 ?  394 HIS A CE1 1 
ATOM   1745 N NE2 . HIS A 1 413 ? 10.404  43.200  90.860  1.00 105.20 ?  394 HIS A NE2 1 
ATOM   1746 N N   . GLN A 1 414 ? 15.063  38.448  89.713  1.00 98.40  ?  395 GLN A N   1 
ATOM   1747 C CA  . GLN A 1 414 ? 15.896  37.257  89.839  1.00 102.17 ?  395 GLN A CA  1 
ATOM   1748 C C   . GLN A 1 414 ? 17.336  37.457  89.384  1.00 98.86  ?  395 GLN A C   1 
ATOM   1749 O O   . GLN A 1 414 ? 18.244  36.836  89.940  1.00 98.62  ?  395 GLN A O   1 
ATOM   1750 C CB  . GLN A 1 414 ? 15.266  36.110  89.047  1.00 99.94  ?  395 GLN A CB  1 
ATOM   1751 C CG  . GLN A 1 414 ? 14.012  35.566  89.699  1.00 106.82 ?  395 GLN A CG  1 
ATOM   1752 C CD  . GLN A 1 414 ? 14.289  34.940  91.054  1.00 121.78 ?  395 GLN A CD  1 
ATOM   1753 O OE1 . GLN A 1 414 ? 15.242  34.166  91.214  1.00 125.54 ?  395 GLN A OE1 1 
ATOM   1754 N NE2 . GLN A 1 414 ? 13.467  35.286  92.045  1.00 125.27 ?  395 GLN A NE2 1 
ATOM   1755 N N   . LEU A 1 415 ? 17.570  38.304  88.387  1.00 94.46  ?  396 LEU A N   1 
ATOM   1756 C CA  . LEU A 1 415 ? 18.903  38.583  87.871  1.00 94.74  ?  396 LEU A CA  1 
ATOM   1757 C C   . LEU A 1 415 ? 19.435  39.947  88.309  1.00 101.34 ?  396 LEU A C   1 
ATOM   1758 O O   . LEU A 1 415 ? 20.551  40.316  87.918  1.00 99.92  ?  396 LEU A O   1 
ATOM   1759 C CB  . LEU A 1 415 ? 18.886  38.482  86.341  1.00 96.30  ?  396 LEU A CB  1 
ATOM   1760 C CG  . LEU A 1 415 ? 19.110  37.093  85.723  1.00 97.25  ?  396 LEU A CG  1 
ATOM   1761 C CD1 . LEU A 1 415 ? 18.120  36.106  86.281  1.00 92.87  ?  396 LEU A CD1 1 
ATOM   1762 C CD2 . LEU A 1 415 ? 18.956  37.142  84.203  1.00 95.83  ?  396 LEU A CD2 1 
ATOM   1763 N N   . ASP A 1 416 ? 18.654  40.689  89.115  1.00 104.59 ?  397 ASP A N   1 
ATOM   1764 C CA  . ASP A 1 416 ? 18.976  42.037  89.618  1.00 100.97 ?  397 ASP A CA  1 
ATOM   1765 C C   . ASP A 1 416 ? 19.571  42.933  88.523  1.00 100.71 ?  397 ASP A C   1 
ATOM   1766 O O   . ASP A 1 416 ? 20.564  43.637  88.731  1.00 107.32 ?  397 ASP A O   1 
ATOM   1767 C CB  . ASP A 1 416 ? 19.898  41.957  90.842  1.00 100.91 ?  397 ASP A CB  1 
ATOM   1768 C CG  . ASP A 1 416 ? 19.758  43.175  91.781  1.00 118.79 ?  397 ASP A CG  1 
ATOM   1769 O OD1 . ASP A 1 416 ? 19.630  44.335  91.295  1.00 119.91 ?  397 ASP A OD1 1 
ATOM   1770 O OD2 . ASP A 1 416 ? 19.768  42.965  93.021  1.00 126.41 ?  397 ASP A OD2 1 
ATOM   1771 N N   . PHE A 1 417 ? 18.937  42.928  87.347  1.00 91.10  ?  398 PHE A N   1 
ATOM   1772 C CA  . PHE A 1 417 ? 19.408  43.700  86.191  1.00 92.13  ?  398 PHE A CA  1 
ATOM   1773 C C   . PHE A 1 417 ? 18.753  45.085  86.215  1.00 91.45  ?  398 PHE A C   1 
ATOM   1774 O O   . PHE A 1 417 ? 17.911  45.436  85.388  1.00 91.12  ?  398 PHE A O   1 
ATOM   1775 C CB  . PHE A 1 417 ? 19.110  42.938  84.898  1.00 87.82  ?  398 PHE A CB  1 
ATOM   1776 C CG  . PHE A 1 417 ? 19.475  43.681  83.627  1.00 82.30  ?  398 PHE A CG  1 
ATOM   1777 C CD1 . PHE A 1 417 ? 20.794  44.004  83.335  1.00 81.13  ?  398 PHE A CD1 1 
ATOM   1778 C CD2 . PHE A 1 417 ? 18.487  44.046  82.720  1.00 78.64  ?  398 PHE A CD2 1 
ATOM   1779 C CE1 . PHE A 1 417 ? 21.117  44.686  82.158  1.00 85.32  ?  398 PHE A CE1 1 
ATOM   1780 C CE2 . PHE A 1 417 ? 18.797  44.732  81.547  1.00 76.07  ?  398 PHE A CE2 1 
ATOM   1781 C CZ  . PHE A 1 417 ? 20.115  45.052  81.263  1.00 78.80  ?  398 PHE A CZ  1 
ATOM   1782 N N   . ASN A 1 418 ? 19.147  45.889  87.202  1.00 91.23  ?  399 ASN A N   1 
ATOM   1783 C CA  . ASN A 1 418 ? 18.437  47.136  87.435  1.00 89.51  ?  399 ASN A CA  1 
ATOM   1784 C C   . ASN A 1 418 ? 19.287  48.384  87.330  1.00 91.62  ?  399 ASN A C   1 
ATOM   1785 O O   . ASN A 1 418 ? 18.760  49.486  87.536  1.00 93.16  ?  399 ASN A O   1 
ATOM   1786 C CB  . ASN A 1 418 ? 17.765  47.097  88.798  1.00 91.91  ?  399 ASN A CB  1 
ATOM   1787 C CG  . ASN A 1 418 ? 16.747  46.019  88.875  1.00 90.45  ?  399 ASN A CG  1 
ATOM   1788 O OD1 . ASN A 1 418 ? 15.963  45.837  87.936  1.00 85.54  ?  399 ASN A OD1 1 
ATOM   1789 N ND2 . ASN A 1 418 ? 16.745  45.276  89.982  1.00 92.98  ?  399 ASN A ND2 1 
ATOM   1790 N N   . VAL A 1 419 ? 20.570  48.255  87.017  1.00 93.50  ?  400 VAL A N   1 
ATOM   1791 C CA  . VAL A 1 419 ? 21.425  49.397  86.722  1.00 94.48  ?  400 VAL A CA  1 
ATOM   1792 C C   . VAL A 1 419 ? 22.224  49.052  85.472  1.00 97.28  ?  400 VAL A C   1 
ATOM   1793 O O   . VAL A 1 419 ? 22.612  47.897  85.278  1.00 99.11  ?  400 VAL A O   1 
ATOM   1794 C CB  . VAL A 1 419 ? 22.342  49.735  87.915  1.00 93.01  ?  400 VAL A CB  1 
ATOM   1795 C CG1 . VAL A 1 419 ? 23.449  50.694  87.488  1.00 97.46  ?  400 VAL A CG1 1 
ATOM   1796 C CG2 . VAL A 1 419 ? 21.522  50.291  89.085  1.00 86.90  ?  400 VAL A CG2 1 
ATOM   1797 N N   . LEU A 1 420 ? 22.446  50.042  84.606  1.00 100.24 ?  401 LEU A N   1 
ATOM   1798 C CA  . LEU A 1 420 ? 23.163  49.803  83.353  1.00 102.22 ?  401 LEU A CA  1 
ATOM   1799 C C   . LEU A 1 420 ? 23.963  51.059  83.018  1.00 106.78 ?  401 LEU A C   1 
ATOM   1800 O O   . LEU A 1 420 ? 23.399  52.044  82.527  1.00 100.56 ?  401 LEU A O   1 
ATOM   1801 C CB  . LEU A 1 420 ? 22.197  49.435  82.239  1.00 101.45 ?  401 LEU A CB  1 
ATOM   1802 C CG  . LEU A 1 420 ? 22.828  48.750  81.036  1.00 100.37 ?  401 LEU A CG  1 
ATOM   1803 C CD1 . LEU A 1 420 ? 23.718  47.633  81.539  1.00 99.52  ?  401 LEU A CD1 1 
ATOM   1804 C CD2 . LEU A 1 420 ? 21.739  48.239  80.083  1.00 86.82  ?  401 LEU A CD2 1 
ATOM   1805 N N   . ASN A 1 421 ? 25.275  51.000  83.275  1.00 110.05 ?  402 ASN A N   1 
ATOM   1806 C CA  . ASN A 1 421 ? 26.194  52.126  83.073  1.00 115.93 ?  402 ASN A CA  1 
ATOM   1807 C C   . ASN A 1 421 ? 25.896  53.254  84.059  1.00 111.46 ?  402 ASN A C   1 
ATOM   1808 O O   . ASN A 1 421 ? 25.866  54.427  83.678  1.00 111.17 ?  402 ASN A O   1 
ATOM   1809 C CB  . ASN A 1 421 ? 26.166  52.669  81.632  1.00 120.11 ?  402 ASN A CB  1 
ATOM   1810 C CG  . ASN A 1 421 ? 26.352  51.587  80.566  1.00 121.72 ?  402 ASN A CG  1 
ATOM   1811 O OD1 . ASN A 1 421 ? 27.065  50.591  80.763  1.00 123.01 ?  402 ASN A OD1 1 
ATOM   1812 N ND2 . ASN A 1 421 ? 25.729  51.805  79.407  1.00 120.01 ?  402 ASN A ND2 1 
ATOM   1813 N N   . ASN A 1 422 ? 25.658  52.894  85.325  1.00 110.51 ?  403 ASN A N   1 
ATOM   1814 C CA  . ASN A 1 422 ? 25.352  53.811  86.426  1.00 112.97 ?  403 ASN A CA  1 
ATOM   1815 C C   . ASN A 1 422 ? 23.968  54.445  86.327  1.00 108.60 ?  403 ASN A C   1 
ATOM   1816 O O   . ASN A 1 422 ? 23.675  55.379  87.084  1.00 112.10 ?  403 ASN A O   1 
ATOM   1817 C CB  . ASN A 1 422 ? 26.394  54.933  86.551  1.00 117.64 ?  403 ASN A CB  1 
ATOM   1818 C CG  . ASN A 1 422 ? 27.691  54.460  87.167  1.00 123.91 ?  403 ASN A CG  1 
ATOM   1819 O OD1 . ASN A 1 422 ? 28.656  54.147  86.457  1.00 122.92 ?  403 ASN A OD1 1 
ATOM   1820 N ND2 . ASN A 1 422 ? 27.728  54.411  88.497  1.00 120.13 ?  403 ASN A ND2 1 
ATOM   1821 N N   . LYS A 1 423 ? 23.109  53.974  85.425  1.00 102.50 ?  404 LYS A N   1 
ATOM   1822 C CA  . LYS A 1 423 ? 21.788  54.541  85.225  1.00 90.92  ?  404 LYS A CA  1 
ATOM   1823 C C   . LYS A 1 423 ? 20.727  53.470  85.446  1.00 92.34  ?  404 LYS A C   1 
ATOM   1824 O O   . LYS A 1 423 ? 20.983  52.283  85.221  1.00 92.79  ?  404 LYS A O   1 
ATOM   1825 C CB  . LYS A 1 423 ? 21.665  55.121  83.811  1.00 96.23  ?  404 LYS A CB  1 
ATOM   1826 C CG  . LYS A 1 423 ? 22.885  55.953  83.390  1.00 101.15 ?  404 LYS A CG  1 
ATOM   1827 C CD  . LYS A 1 423 ? 22.967  56.170  81.874  1.00 99.57  ?  404 LYS A CD  1 
ATOM   1828 C CE  . LYS A 1 423 ? 21.620  56.594  81.283  1.00 102.08 ?  404 LYS A CE  1 
ATOM   1829 N NZ  . LYS A 1 423 ? 21.740  57.465  80.070  1.00 99.03  ?  404 LYS A NZ  1 
ATOM   1830 N N   . PRO A 1 424 ? 19.541  53.846  85.917  1.00 89.17  ?  405 PRO A N   1 
ATOM   1831 C CA  . PRO A 1 424 ? 18.494  52.843  86.141  1.00 82.14  ?  405 PRO A CA  1 
ATOM   1832 C C   . PRO A 1 424 ? 18.030  52.242  84.828  1.00 81.30  ?  405 PRO A C   1 
ATOM   1833 O O   . PRO A 1 424 ? 17.871  52.934  83.817  1.00 80.65  ?  405 PRO A O   1 
ATOM   1834 C CB  . PRO A 1 424 ? 17.371  53.642  86.809  1.00 74.28  ?  405 PRO A CB  1 
ATOM   1835 C CG  . PRO A 1 424 ? 18.075  54.769  87.431  1.00 85.24  ?  405 PRO A CG  1 
ATOM   1836 C CD  . PRO A 1 424 ? 19.132  55.155  86.435  1.00 86.07  ?  405 PRO A CD  1 
ATOM   1837 N N   . VAL A 1 425 ? 17.808  50.934  84.854  1.00 75.82  ?  406 VAL A N   1 
ATOM   1838 C CA  . VAL A 1 425 ? 17.278  50.271  83.681  1.00 74.00  ?  406 VAL A CA  1 
ATOM   1839 C C   . VAL A 1 425 ? 15.815  50.650  83.531  1.00 66.56  ?  406 VAL A C   1 
ATOM   1840 O O   . VAL A 1 425 ? 15.056  50.627  84.507  1.00 65.44  ?  406 VAL A O   1 
ATOM   1841 C CB  . VAL A 1 425 ? 17.458  48.755  83.804  1.00 73.59  ?  406 VAL A CB  1 
ATOM   1842 C CG1 . VAL A 1 425 ? 16.806  48.058  82.626  1.00 62.00  ?  406 VAL A CG1 1 
ATOM   1843 C CG2 . VAL A 1 425 ? 18.937  48.413  83.940  1.00 78.61  ?  406 VAL A CG2 1 
ATOM   1844 N N   . SER A 1 426 ? 15.412  51.015  82.315  1.00 64.67  ?  407 SER A N   1 
ATOM   1845 C CA  . SER A 1 426 ? 13.994  51.235  82.063  1.00 67.20  ?  407 SER A CA  1 
ATOM   1846 C C   . SER A 1 426 ? 13.306  49.955  81.589  1.00 67.96  ?  407 SER A C   1 
ATOM   1847 O O   . SER A 1 426 ? 13.947  48.971  81.216  1.00 69.16  ?  407 SER A O   1 
ATOM   1848 C CB  . SER A 1 426 ? 13.785  52.332  81.034  1.00 63.68  ?  407 SER A CB  1 
ATOM   1849 O OG  . SER A 1 426 ? 14.006  51.842  79.736  1.00 62.34  ?  407 SER A OG  1 
ATOM   1850 N N   . LEU A 1 427 ? 11.972  49.975  81.600  1.00 63.97  ?  408 LEU A N   1 
ATOM   1851 C CA  . LEU A 1 427 ? 11.242  48.829  81.077  1.00 60.99  ?  408 LEU A CA  1 
ATOM   1852 C C   . LEU A 1 427 ? 11.544  48.633  79.603  1.00 60.83  ?  408 LEU A C   1 
ATOM   1853 O O   . LEU A 1 427 ? 11.767  47.504  79.160  1.00 65.88  ?  408 LEU A O   1 
ATOM   1854 C CB  . LEU A 1 427 ? 9.736   48.990  81.298  1.00 64.52  ?  408 LEU A CB  1 
ATOM   1855 C CG  . LEU A 1 427 ? 8.879   47.801  80.841  1.00 54.41  ?  408 LEU A CG  1 
ATOM   1856 C CD1 . LEU A 1 427 ? 9.367   46.630  81.578  1.00 55.47  ?  408 LEU A CD1 1 
ATOM   1857 C CD2 . LEU A 1 427 ? 7.403   48.008  81.144  1.00 49.22  ?  408 LEU A CD2 1 
ATOM   1858 N N   . GLY A 1 428 ? 11.580  49.723  78.835  1.00 60.31  ?  409 GLY A N   1 
ATOM   1859 C CA  . GLY A 1 428 ? 11.852  49.611  77.410  1.00 60.32  ?  409 GLY A CA  1 
ATOM   1860 C C   . GLY A 1 428 ? 13.199  48.980  77.099  1.00 62.54  ?  409 GLY A C   1 
ATOM   1861 O O   . GLY A 1 428 ? 13.294  48.091  76.251  1.00 58.85  ?  409 GLY A O   1 
ATOM   1862 N N   . GLN A 1 429 ? 14.258  49.438  77.773  1.00 62.37  ?  410 GLN A N   1 
ATOM   1863 C CA  . GLN A 1 429 ? 15.565  48.806  77.622  1.00 63.72  ?  410 GLN A CA  1 
ATOM   1864 C C   . GLN A 1 429 ? 15.475  47.308  77.865  1.00 69.43  ?  410 GLN A C   1 
ATOM   1865 O O   . GLN A 1 429 ? 15.969  46.506  77.066  1.00 74.43  ?  410 GLN A O   1 
ATOM   1866 C CB  . GLN A 1 429 ? 16.569  49.415  78.593  1.00 63.57  ?  410 GLN A CB  1 
ATOM   1867 C CG  . GLN A 1 429 ? 16.990  50.812  78.291  1.00 74.51  ?  410 GLN A CG  1 
ATOM   1868 C CD  . GLN A 1 429 ? 17.794  51.377  79.427  1.00 81.04  ?  410 GLN A CD  1 
ATOM   1869 O OE1 . GLN A 1 429 ? 18.447  50.626  80.153  1.00 81.46  ?  410 GLN A OE1 1 
ATOM   1870 N NE2 . GLN A 1 429 ? 17.733  52.701  79.614  1.00 93.11  ?  410 GLN A NE2 1 
ATOM   1871 N N   . ALA A 1 430 ? 14.842  46.916  78.974  1.00 67.66  ?  411 ALA A N   1 
ATOM   1872 C CA  . ALA A 1 430 ? 14.762  45.507  79.340  1.00 63.92  ?  411 ALA A CA  1 
ATOM   1873 C C   . ALA A 1 430 ? 14.004  44.693  78.295  1.00 65.67  ?  411 ALA A C   1 
ATOM   1874 O O   . ALA A 1 430 ? 14.360  43.541  78.028  1.00 71.00  ?  411 ALA A O   1 
ATOM   1875 C CB  . ALA A 1 430 ? 14.107  45.366  80.714  1.00 63.67  ?  411 ALA A CB  1 
ATOM   1876 N N   . LEU A 1 431 ? 12.954  45.259  77.697  1.00 63.11  ?  412 LEU A N   1 
ATOM   1877 C CA  . LEU A 1 431 ? 12.270  44.552  76.615  1.00 67.61  ?  412 LEU A CA  1 
ATOM   1878 C C   . LEU A 1 431 ? 13.179  44.345  75.408  1.00 70.39  ?  412 LEU A C   1 
ATOM   1879 O O   . LEU A 1 431 ? 13.168  43.271  74.799  1.00 73.80  ?  412 LEU A O   1 
ATOM   1880 C CB  . LEU A 1 431 ? 11.013  45.297  76.187  1.00 65.99  ?  412 LEU A CB  1 
ATOM   1881 C CG  . LEU A 1 431 ? 9.816   45.187  77.118  1.00 64.25  ?  412 LEU A CG  1 
ATOM   1882 C CD1 . LEU A 1 431 ? 8.773   46.115  76.595  1.00 62.22  ?  412 LEU A CD1 1 
ATOM   1883 C CD2 . LEU A 1 431 ? 9.268   43.787  77.189  1.00 61.54  ?  412 LEU A CD2 1 
ATOM   1884 N N   . GLU A 1 432 ? 13.954  45.362  75.026  1.00 71.26  ?  413 GLU A N   1 
ATOM   1885 C CA  . GLU A 1 432 ? 14.968  45.154  74.000  1.00 71.35  ?  413 GLU A CA  1 
ATOM   1886 C C   . GLU A 1 432 ? 15.917  44.029  74.396  1.00 73.51  ?  413 GLU A C   1 
ATOM   1887 O O   . GLU A 1 432 ? 16.016  43.018  73.696  1.00 77.20  ?  413 GLU A O   1 
ATOM   1888 C CB  . GLU A 1 432 ? 15.728  46.446  73.727  1.00 74.14  ?  413 GLU A CB  1 
ATOM   1889 C CG  . GLU A 1 432 ? 15.112  47.291  72.615  1.00 85.98  ?  413 GLU A CG  1 
ATOM   1890 C CD  . GLU A 1 432 ? 15.825  48.639  72.434  1.00 105.81 ?  413 GLU A CD  1 
ATOM   1891 O OE1 . GLU A 1 432 ? 16.387  49.181  73.433  1.00 99.45  ?  413 GLU A OE1 1 
ATOM   1892 O OE2 . GLU A 1 432 ? 15.824  49.148  71.284  1.00 109.73 ?  413 GLU A OE2 1 
ATOM   1893 N N   . VAL A 1 433 ? 16.599  44.169  75.537  1.00 69.71  ?  414 VAL A N   1 
ATOM   1894 C CA  . VAL A 1 433 ? 17.486  43.104  76.012  1.00 70.07  ?  414 VAL A CA  1 
ATOM   1895 C C   . VAL A 1 433 ? 16.815  41.737  76.023  1.00 76.10  ?  414 VAL A C   1 
ATOM   1896 O O   . VAL A 1 433 ? 17.479  40.717  75.809  1.00 82.77  ?  414 VAL A O   1 
ATOM   1897 C CB  . VAL A 1 433 ? 18.063  43.447  77.395  1.00 71.82  ?  414 VAL A CB  1 
ATOM   1898 C CG1 . VAL A 1 433 ? 18.680  42.212  78.034  1.00 71.86  ?  414 VAL A CG1 1 
ATOM   1899 C CG2 . VAL A 1 433 ? 19.154  44.482  77.228  1.00 73.20  ?  414 VAL A CG2 1 
ATOM   1900 N N   . VAL A 1 434 ? 15.507  41.670  76.259  1.00 76.43  ?  415 VAL A N   1 
ATOM   1901 C CA  . VAL A 1 434 ? 14.875  40.356  76.213  1.00 74.54  ?  415 VAL A CA  1 
ATOM   1902 C C   . VAL A 1 434 ? 14.650  39.927  74.768  1.00 75.45  ?  415 VAL A C   1 
ATOM   1903 O O   . VAL A 1 434 ? 14.977  38.799  74.392  1.00 78.89  ?  415 VAL A O   1 
ATOM   1904 C CB  . VAL A 1 434 ? 13.576  40.330  77.036  1.00 72.01  ?  415 VAL A CB  1 
ATOM   1905 C CG1 . VAL A 1 434 ? 12.763  39.103  76.692  1.00 68.12  ?  415 VAL A CG1 1 
ATOM   1906 C CG2 . VAL A 1 434 ? 13.903  40.296  78.498  1.00 68.20  ?  415 VAL A CG2 1 
ATOM   1907 N N   . ILE A 1 435 ? 14.143  40.824  73.919  1.00 77.35  ?  416 ILE A N   1 
ATOM   1908 C CA  . ILE A 1 435 ? 13.928  40.466  72.513  1.00 77.94  ?  416 ILE A CA  1 
ATOM   1909 C C   . ILE A 1 435 ? 15.243  40.084  71.838  1.00 80.52  ?  416 ILE A C   1 
ATOM   1910 O O   . ILE A 1 435 ? 15.313  39.086  71.117  1.00 86.48  ?  416 ILE A O   1 
ATOM   1911 C CB  . ILE A 1 435 ? 13.228  41.603  71.751  1.00 69.42  ?  416 ILE A CB  1 
ATOM   1912 C CG1 . ILE A 1 435 ? 11.740  41.600  72.097  1.00 72.38  ?  416 ILE A CG1 1 
ATOM   1913 C CG2 . ILE A 1 435 ? 13.423  41.404  70.263  1.00 67.46  ?  416 ILE A CG2 1 
ATOM   1914 C CD1 . ILE A 1 435 ? 10.919  42.590  71.330  1.00 70.25  ?  416 ILE A CD1 1 
ATOM   1915 N N   . GLN A 1 436 ? 16.300  40.876  72.047  1.00 82.24  ?  417 GLN A N   1 
ATOM   1916 C CA  . GLN A 1 436 ? 17.618  40.500  71.539  1.00 81.47  ?  417 GLN A CA  1 
ATOM   1917 C C   . GLN A 1 436 ? 17.982  39.071  71.947  1.00 84.91  ?  417 GLN A C   1 
ATOM   1918 O O   . GLN A 1 436 ? 18.304  38.238  71.095  1.00 88.21  ?  417 GLN A O   1 
ATOM   1919 C CB  . GLN A 1 436 ? 18.683  41.496  72.016  1.00 79.63  ?  417 GLN A CB  1 
ATOM   1920 C CG  . GLN A 1 436 ? 18.883  42.685  71.076  1.00 82.76  ?  417 GLN A CG  1 
ATOM   1921 C CD  . GLN A 1 436 ? 19.132  44.012  71.809  1.00 94.80  ?  417 GLN A CD  1 
ATOM   1922 O OE1 . GLN A 1 436 ? 19.710  44.054  72.908  1.00 91.10  ?  417 GLN A OE1 1 
ATOM   1923 N NE2 . GLN A 1 436 ? 18.687  45.107  71.193  1.00 98.64  ?  417 GLN A NE2 1 
ATOM   1924 N N   . LEU A 1 437 ? 17.900  38.752  73.241  1.00 78.58  ?  418 LEU A N   1 
ATOM   1925 C CA  . LEU A 1 437 ? 18.300  37.421  73.678  1.00 76.23  ?  418 LEU A CA  1 
ATOM   1926 C C   . LEU A 1 437 ? 17.403  36.318  73.104  1.00 84.95  ?  418 LEU A C   1 
ATOM   1927 O O   . LEU A 1 437 ? 17.799  35.142  73.118  1.00 86.06  ?  418 LEU A O   1 
ATOM   1928 C CB  . LEU A 1 437 ? 18.336  37.368  75.212  1.00 75.18  ?  418 LEU A CB  1 
ATOM   1929 C CG  . LEU A 1 437 ? 19.555  38.084  75.808  1.00 84.02  ?  418 LEU A CG  1 
ATOM   1930 C CD1 . LEU A 1 437 ? 19.775  37.804  77.297  1.00 92.00  ?  418 LEU A CD1 1 
ATOM   1931 C CD2 . LEU A 1 437 ? 20.783  37.720  75.012  1.00 85.43  ?  418 LEU A CD2 1 
ATOM   1932 N N   . GLN A 1 438 ? 16.215  36.651  72.590  1.00 80.92  ?  419 GLN A N   1 
ATOM   1933 C CA  . GLN A 1 438 ? 15.407  35.620  71.945  1.00 80.52  ?  419 GLN A CA  1 
ATOM   1934 C C   . GLN A 1 438 ? 15.788  35.461  70.482  1.00 88.35  ?  419 GLN A C   1 
ATOM   1935 O O   . GLN A 1 438 ? 15.834  34.343  69.965  1.00 91.87  ?  419 GLN A O   1 
ATOM   1936 C CB  . GLN A 1 438 ? 13.908  35.922  72.059  1.00 77.71  ?  419 GLN A CB  1 
ATOM   1937 C CG  . GLN A 1 438 ? 13.331  35.910  73.478  1.00 76.88  ?  419 GLN A CG  1 
ATOM   1938 C CD  . GLN A 1 438 ? 13.870  34.805  74.366  1.00 90.38  ?  419 GLN A CD  1 
ATOM   1939 O OE1 . GLN A 1 438 ? 14.653  35.053  75.298  1.00 85.60  ?  419 GLN A OE1 1 
ATOM   1940 N NE2 . GLN A 1 438 ? 13.445  33.571  74.090  1.00 103.81 ?  419 GLN A NE2 1 
ATOM   1941 N N   . GLU A 1 439 ? 16.080  36.567  69.807  1.00 90.13  ?  420 GLU A N   1 
ATOM   1942 C CA  . GLU A 1 439 ? 16.707  36.484  68.496  1.00 90.63  ?  420 GLU A CA  1 
ATOM   1943 C C   . GLU A 1 439 ? 18.092  35.832  68.568  1.00 90.58  ?  420 GLU A C   1 
ATOM   1944 O O   . GLU A 1 439 ? 18.436  35.022  67.701  1.00 90.58  ?  420 GLU A O   1 
ATOM   1945 C CB  . GLU A 1 439 ? 16.724  37.882  67.866  1.00 89.80  ?  420 GLU A CB  1 
ATOM   1946 C CG  . GLU A 1 439 ? 15.343  38.240  67.299  1.00 99.34  ?  420 GLU A CG  1 
ATOM   1947 C CD  . GLU A 1 439 ? 15.171  39.651  66.768  1.00 106.72 ?  420 GLU A CD  1 
ATOM   1948 O OE1 . GLU A 1 439 ? 15.992  40.554  67.078  1.00 97.52  ?  420 GLU A OE1 1 
ATOM   1949 O OE2 . GLU A 1 439 ? 14.310  39.797  65.851  1.00 109.93 ?  420 GLU A OE2 1 
ATOM   1950 N N   . LYS A 1 440 ? 18.892  36.136  69.602  1.00 90.74  ?  421 LYS A N   1 
ATOM   1951 C CA  . LYS A 1 440 ? 20.133  35.381  69.807  1.00 86.40  ?  421 LYS A CA  1 
ATOM   1952 C C   . LYS A 1 440 ? 19.859  33.888  69.819  1.00 90.26  ?  421 LYS A C   1 
ATOM   1953 O O   . LYS A 1 440 ? 20.494  33.117  69.095  1.00 97.57  ?  421 LYS A O   1 
ATOM   1954 C CB  . LYS A 1 440 ? 20.821  35.762  71.113  1.00 79.44  ?  421 LYS A CB  1 
ATOM   1955 C CG  . LYS A 1 440 ? 22.160  35.086  71.319  1.00 74.30  ?  421 LYS A CG  1 
ATOM   1956 C CD  . LYS A 1 440 ? 22.334  34.765  72.777  1.00 91.23  ?  421 LYS A CD  1 
ATOM   1957 C CE  . LYS A 1 440 ? 23.766  34.857  73.272  1.00 96.44  ?  421 LYS A CE  1 
ATOM   1958 N NZ  . LYS A 1 440 ? 24.707  34.021  72.516  1.00 105.62 ?  421 LYS A NZ  1 
ATOM   1959 N N   . HIS A 1 441 ? 18.892  33.462  70.622  1.00 91.48  ?  422 HIS A N   1 
ATOM   1960 C CA  . HIS A 1 441 ? 18.707  32.031  70.822  1.00 93.73  ?  422 HIS A CA  1 
ATOM   1961 C C   . HIS A 1 441 ? 18.136  31.348  69.581  1.00 89.32  ?  422 HIS A C   1 
ATOM   1962 O O   . HIS A 1 441 ? 18.436  30.177  69.341  1.00 97.68  ?  422 HIS A O   1 
ATOM   1963 C CB  . HIS A 1 441 ? 17.830  31.793  72.047  1.00 98.33  ?  422 HIS A CB  1 
ATOM   1964 C CG  . HIS A 1 441 ? 17.275  30.411  72.139  1.00 97.46  ?  422 HIS A CG  1 
ATOM   1965 N ND1 . HIS A 1 441 ? 16.091  30.042  71.534  1.00 100.30 ?  422 HIS A ND1 1 
ATOM   1966 C CD2 . HIS A 1 441 ? 17.730  29.312  72.785  1.00 94.81  ?  422 HIS A CD2 1 
ATOM   1967 C CE1 . HIS A 1 441 ? 15.842  28.772  71.800  1.00 93.91  ?  422 HIS A CE1 1 
ATOM   1968 N NE2 . HIS A 1 441 ? 16.821  28.307  72.555  1.00 98.33  ?  422 HIS A NE2 1 
ATOM   1969 N N   . VAL A 1 442 ? 17.344  32.047  68.768  1.00 83.27  ?  423 VAL A N   1 
ATOM   1970 C CA  . VAL A 1 442 ? 16.967  31.490  67.469  1.00 88.42  ?  423 VAL A CA  1 
ATOM   1971 C C   . VAL A 1 442 ? 18.201  31.213  66.607  1.00 96.22  ?  423 VAL A C   1 
ATOM   1972 O O   . VAL A 1 442 ? 18.289  30.177  65.933  1.00 97.71  ?  423 VAL A O   1 
ATOM   1973 C CB  . VAL A 1 442 ? 15.975  32.422  66.751  1.00 88.64  ?  423 VAL A CB  1 
ATOM   1974 C CG1 . VAL A 1 442 ? 16.035  32.204  65.251  1.00 92.46  ?  423 VAL A CG1 1 
ATOM   1975 C CG2 . VAL A 1 442 ? 14.564  32.178  67.246  1.00 86.81  ?  423 VAL A CG2 1 
ATOM   1976 N N   . LYS A 1 443 ? 19.176  32.120  66.616  1.00 96.70  ?  424 LYS A N   1 
ATOM   1977 C CA  . LYS A 1 443 ? 20.387  31.872  65.844  1.00 91.88  ?  424 LYS A CA  1 
ATOM   1978 C C   . LYS A 1 443 ? 21.282  30.837  66.516  1.00 93.52  ?  424 LYS A C   1 
ATOM   1979 O O   . LYS A 1 443 ? 21.825  29.971  65.827  1.00 100.77 ?  424 LYS A O   1 
ATOM   1980 C CB  . LYS A 1 443 ? 21.152  33.172  65.615  1.00 88.66  ?  424 LYS A CB  1 
ATOM   1981 C CG  . LYS A 1 443 ? 20.401  34.150  64.762  1.00 86.90  ?  424 LYS A CG  1 
ATOM   1982 C CD  . LYS A 1 443 ? 21.166  35.444  64.638  1.00 95.54  ?  424 LYS A CD  1 
ATOM   1983 C CE  . LYS A 1 443 ? 20.222  36.587  64.347  1.00 94.79  ?  424 LYS A CE  1 
ATOM   1984 N NZ  . LYS A 1 443 ? 19.724  36.495  62.960  1.00 94.46  ?  424 LYS A NZ  1 
ATOM   1985 N N   . ASP A 1 444 ? 21.453  30.897  67.847  1.00 91.56  ?  425 ASP A N   1 
ATOM   1986 C CA  . ASP A 1 444 ? 22.253  29.881  68.533  1.00 99.13  ?  425 ASP A CA  1 
ATOM   1987 C C   . ASP A 1 444 ? 21.805  28.470  68.170  1.00 104.04 ?  425 ASP A C   1 
ATOM   1988 O O   . ASP A 1 444 ? 22.611  27.527  68.198  1.00 100.71 ?  425 ASP A O   1 
ATOM   1989 C CB  . ASP A 1 444 ? 22.186  30.044  70.062  1.00 97.12  ?  425 ASP A CB  1 
ATOM   1990 C CG  . ASP A 1 444 ? 23.350  30.860  70.633  1.00 107.97 ?  425 ASP A CG  1 
ATOM   1991 O OD1 . ASP A 1 444 ? 23.533  30.844  71.882  1.00 112.43 ?  425 ASP A OD1 1 
ATOM   1992 O OD2 . ASP A 1 444 ? 24.067  31.526  69.845  1.00 106.65 ?  425 ASP A OD2 1 
ATOM   1993 N N   . GLU A 1 445 ? 20.532  28.309  67.805  1.00 101.66 ?  426 GLU A N   1 
ATOM   1994 C CA  . GLU A 1 445 ? 19.967  26.984  67.640  1.00 103.91 ?  426 GLU A CA  1 
ATOM   1995 C C   . GLU A 1 445 ? 19.796  26.589  66.180  1.00 100.48 ?  426 GLU A C   1 
ATOM   1996 O O   . GLU A 1 445 ? 19.714  25.392  65.884  1.00 103.70 ?  426 GLU A O   1 
ATOM   1997 C CB  . GLU A 1 445 ? 18.622  26.891  68.380  1.00 101.21 ?  426 GLU A CB  1 
ATOM   1998 C CG  . GLU A 1 445 ? 18.383  25.517  68.968  1.00 108.39 ?  426 GLU A CG  1 
ATOM   1999 C CD  . GLU A 1 445 ? 17.064  25.391  69.685  1.00 108.43 ?  426 GLU A CD  1 
ATOM   2000 O OE1 . GLU A 1 445 ? 16.165  26.212  69.409  1.00 107.00 ?  426 GLU A OE1 1 
ATOM   2001 O OE2 . GLU A 1 445 ? 16.948  24.485  70.544  1.00 110.33 ?  426 GLU A OE2 1 
ATOM   2002 N N   . GLN A 1 446 ? 19.759  27.553  65.264  1.00 99.33  ?  427 GLN A N   1 
ATOM   2003 C CA  . GLN A 1 446 ? 20.009  27.237  63.862  1.00 99.45  ?  427 GLN A CA  1 
ATOM   2004 C C   . GLN A 1 446 ? 21.434  26.743  63.677  1.00 99.37  ?  427 GLN A C   1 
ATOM   2005 O O   . GLN A 1 446 ? 21.679  25.731  63.011  1.00 97.96  ?  427 GLN A O   1 
ATOM   2006 C CB  . GLN A 1 446 ? 19.775  28.466  62.999  1.00 97.91  ?  427 GLN A CB  1 
ATOM   2007 C CG  . GLN A 1 446 ? 18.351  28.873  62.920  1.00 99.68  ?  427 GLN A CG  1 
ATOM   2008 C CD  . GLN A 1 446 ? 18.031  29.497  61.599  1.00 105.10 ?  427 GLN A CD  1 
ATOM   2009 O OE1 . GLN A 1 446 ? 18.186  30.710  61.410  1.00 102.06 ?  427 GLN A OE1 1 
ATOM   2010 N NE2 . GLN A 1 446 ? 17.601  28.667  60.654  1.00 112.29 ?  427 GLN A NE2 1 
ATOM   2011 N N   . ILE A 1 447 ? 22.391  27.455  64.265  1.00 100.86 ?  428 ILE A N   1 
ATOM   2012 C CA  . ILE A 1 447 ? 23.782  27.038  64.192  1.00 97.69  ?  428 ILE A CA  1 
ATOM   2013 C C   . ILE A 1 447 ? 23.943  25.611  64.703  1.00 99.09  ?  428 ILE A C   1 
ATOM   2014 O O   . ILE A 1 447 ? 24.520  24.763  64.017  1.00 102.65 ?  428 ILE A O   1 
ATOM   2015 C CB  . ILE A 1 447 ? 24.679  28.032  64.947  1.00 98.19  ?  428 ILE A CB  1 
ATOM   2016 C CG1 . ILE A 1 447 ? 24.888  29.280  64.086  1.00 102.42 ?  428 ILE A CG1 1 
ATOM   2017 C CG2 . ILE A 1 447 ? 25.995  27.390  65.341  1.00 102.10 ?  428 ILE A CG2 1 
ATOM   2018 C CD1 . ILE A 1 447 ? 25.144  30.526  64.873  1.00 105.74 ?  428 ILE A CD1 1 
ATOM   2019 N N   . GLU A 1 448 ? 23.403  25.307  65.891  1.00 101.74 ?  429 GLU A N   1 
ATOM   2020 C CA  . GLU A 1 448 ? 23.611  23.971  66.452  1.00 100.83 ?  429 GLU A CA  1 
ATOM   2021 C C   . GLU A 1 448 ? 22.958  22.883  65.598  1.00 100.86 ?  429 GLU A C   1 
ATOM   2022 O O   . GLU A 1 448 ? 23.409  21.728  65.611  1.00 99.76  ?  429 GLU A O   1 
ATOM   2023 C CB  . GLU A 1 448 ? 23.090  23.889  67.889  1.00 98.76  ?  429 GLU A CB  1 
ATOM   2024 C CG  . GLU A 1 448 ? 23.679  22.702  68.662  1.00 109.54 ?  429 GLU A CG  1 
ATOM   2025 C CD  . GLU A 1 448 ? 22.842  22.269  69.871  1.00 124.38 ?  429 GLU A CD  1 
ATOM   2026 O OE1 . GLU A 1 448 ? 21.667  22.692  69.973  1.00 123.14 ?  429 GLU A OE1 1 
ATOM   2027 O OE2 . GLU A 1 448 ? 23.353  21.478  70.704  1.00 124.52 ?  429 GLU A OE2 1 
ATOM   2028 N N   . HIS A 1 449 ? 21.914  23.227  64.844  1.00 95.14  ?  430 HIS A N   1 
ATOM   2029 C CA  . HIS A 1 449 ? 21.226  22.236  64.019  1.00 92.80  ?  430 HIS A CA  1 
ATOM   2030 C C   . HIS A 1 449 ? 21.981  21.960  62.730  1.00 97.97  ?  430 HIS A C   1 
ATOM   2031 O O   . HIS A 1 449 ? 22.243  20.802  62.399  1.00 102.91 ?  430 HIS A O   1 
ATOM   2032 C CB  . HIS A 1 449 ? 19.809  22.709  63.719  1.00 97.73  ?  430 HIS A CB  1 
ATOM   2033 C CG  . HIS A 1 449 ? 19.208  22.145  62.464  1.00 96.02  ?  430 HIS A CG  1 
ATOM   2034 N ND1 . HIS A 1 449 ? 19.440  22.684  61.216  1.00 94.86  ?  430 HIS A ND1 1 
ATOM   2035 C CD2 . HIS A 1 449 ? 18.319  21.138  62.278  1.00 95.74  ?  430 HIS A CD2 1 
ATOM   2036 C CE1 . HIS A 1 449 ? 18.739  22.020  60.314  1.00 95.30  ?  430 HIS A CE1 1 
ATOM   2037 N NE2 . HIS A 1 449 ? 18.051  21.078  60.932  1.00 96.17  ?  430 HIS A NE2 1 
ATOM   2038 N N   . TRP A 1 450 ? 22.327  23.006  61.977  1.00 98.95  ?  431 TRP A N   1 
ATOM   2039 C CA  . TRP A 1 450 ? 23.192  22.805  60.822  1.00 91.54  ?  431 TRP A CA  1 
ATOM   2040 C C   . TRP A 1 450 ? 24.539  22.223  61.226  1.00 94.44  ?  431 TRP A C   1 
ATOM   2041 O O   . TRP A 1 450 ? 25.134  21.472  60.455  1.00 104.31 ?  431 TRP A O   1 
ATOM   2042 C CB  . TRP A 1 450 ? 23.399  24.112  60.075  1.00 93.93  ?  431 TRP A CB  1 
ATOM   2043 C CG  . TRP A 1 450 ? 22.144  24.688  59.515  1.00 103.39 ?  431 TRP A CG  1 
ATOM   2044 C CD1 . TRP A 1 450 ? 21.407  25.707  60.046  1.00 108.50 ?  431 TRP A CD1 1 
ATOM   2045 C CD2 . TRP A 1 450 ? 21.488  24.315  58.297  1.00 103.27 ?  431 TRP A CD2 1 
ATOM   2046 N NE1 . TRP A 1 450 ? 20.326  25.982  59.243  1.00 107.40 ?  431 TRP A NE1 1 
ATOM   2047 C CE2 . TRP A 1 450 ? 20.353  25.143  58.163  1.00 102.43 ?  431 TRP A CE2 1 
ATOM   2048 C CE3 . TRP A 1 450 ? 21.747  23.366  57.309  1.00 104.39 ?  431 TRP A CE3 1 
ATOM   2049 C CZ2 . TRP A 1 450 ? 19.480  25.047  57.086  1.00 104.21 ?  431 TRP A CZ2 1 
ATOM   2050 C CZ3 . TRP A 1 450 ? 20.876  23.274  56.234  1.00 109.42 ?  431 TRP A CZ3 1 
ATOM   2051 C CH2 . TRP A 1 450 ? 19.757  24.111  56.132  1.00 108.39 ?  431 TRP A CH2 1 
ATOM   2052 N N   . LYS A 1 451 ? 25.044  22.542  62.417  1.00 92.04  ?  432 LYS A N   1 
ATOM   2053 C CA  . LYS A 1 451 ? 26.272  21.889  62.857  1.00 96.74  ?  432 LYS A CA  1 
ATOM   2054 C C   . LYS A 1 451 ? 26.084  20.385  63.048  1.00 97.96  ?  432 LYS A C   1 
ATOM   2055 O O   . LYS A 1 451 ? 27.075  19.649  63.089  1.00 96.73  ?  432 LYS A O   1 
ATOM   2056 C CB  . LYS A 1 451 ? 26.804  22.536  64.146  1.00 94.74  ?  432 LYS A CB  1 
ATOM   2057 C CG  . LYS A 1 451 ? 27.719  23.747  63.910  1.00 99.27  ?  432 LYS A CG  1 
ATOM   2058 C CD  . LYS A 1 451 ? 28.912  23.765  64.871  1.00 107.06 ?  432 LYS A CD  1 
ATOM   2059 C CE  . LYS A 1 451 ? 29.388  25.201  65.156  1.00 116.48 ?  432 LYS A CE  1 
ATOM   2060 N NZ  . LYS A 1 451 ? 30.231  25.313  66.396  1.00 117.84 ?  432 LYS A NZ  1 
ATOM   2061 N N   . LYS A 1 452 ? 24.837  19.917  63.178  1.00 99.36  ?  433 LYS A N   1 
ATOM   2062 C CA  . LYS A 1 452 ? 24.563  18.485  63.222  1.00 97.51  ?  433 LYS A CA  1 
ATOM   2063 C C   . LYS A 1 452 ? 24.573  17.889  61.824  1.00 97.20  ?  433 LYS A C   1 
ATOM   2064 O O   . LYS A 1 452 ? 24.874  16.704  61.653  1.00 101.48 ?  433 LYS A O   1 
ATOM   2065 C CB  . LYS A 1 452 ? 23.209  18.211  63.896  1.00 96.05  ?  433 LYS A CB  1 
ATOM   2066 C CG  . LYS A 1 452 ? 23.236  18.175  65.427  1.00 109.61 ?  433 LYS A CG  1 
ATOM   2067 C CD  . LYS A 1 452 ? 21.819  18.189  66.029  1.00 114.87 ?  433 LYS A CD  1 
ATOM   2068 C CE  . LYS A 1 452 ? 21.856  18.192  67.562  1.00 119.80 ?  433 LYS A CE  1 
ATOM   2069 N NZ  . LYS A 1 452 ? 20.700  17.456  68.164  1.00 115.25 ?  433 LYS A NZ  1 
ATOM   2070 N N   . ILE A 1 453 ? 24.262  18.688  60.814  1.00 92.00  ?  434 ILE A N   1 
ATOM   2071 C CA  . ILE A 1 453 ? 24.298  18.162  59.464  1.00 93.27  ?  434 ILE A CA  1 
ATOM   2072 C C   . ILE A 1 453 ? 25.737  18.058  58.952  1.00 98.27  ?  434 ILE A C   1 
ATOM   2073 O O   . ILE A 1 453 ? 26.108  17.043  58.362  1.00 105.39 ?  434 ILE A O   1 
ATOM   2074 C CB  . ILE A 1 453 ? 23.401  19.002  58.545  1.00 91.47  ?  434 ILE A CB  1 
ATOM   2075 C CG1 . ILE A 1 453 ? 21.949  18.888  59.001  1.00 95.49  ?  434 ILE A CG1 1 
ATOM   2076 C CG2 . ILE A 1 453 ? 23.469  18.489  57.141  1.00 92.93  ?  434 ILE A CG2 1 
ATOM   2077 C CD1 . ILE A 1 453 ? 20.956  19.552  58.043  1.00 92.70  ?  434 ILE A CD1 1 
ATOM   2078 N N   . VAL A 1 454 ? 26.592  19.059  59.192  1.00 95.66  ?  435 VAL A N   1 
ATOM   2079 C CA  . VAL A 1 454 ? 28.005  18.880  58.844  1.00 95.50  ?  435 VAL A CA  1 
ATOM   2080 C C   . VAL A 1 454 ? 28.613  17.696  59.598  1.00 100.48 ?  435 VAL A C   1 
ATOM   2081 O O   . VAL A 1 454 ? 29.359  16.906  59.015  1.00 111.56 ?  435 VAL A O   1 
ATOM   2082 C CB  . VAL A 1 454 ? 28.835  20.160  59.076  1.00 96.33  ?  435 VAL A CB  1 
ATOM   2083 C CG1 . VAL A 1 454 ? 28.584  21.183  58.014  1.00 93.65  ?  435 VAL A CG1 1 
ATOM   2084 C CG2 . VAL A 1 454 ? 28.612  20.738  60.475  1.00 98.54  ?  435 VAL A CG2 1 
ATOM   2085 N N   . LYS A 1 455 ? 28.333  17.555  60.897  1.00 94.96  ?  436 LYS A N   1 
ATOM   2086 C CA  . LYS A 1 455 ? 28.957  16.461  61.639  1.00 100.41 ?  436 LYS A CA  1 
ATOM   2087 C C   . LYS A 1 455 ? 28.516  15.095  61.116  1.00 110.44 ?  436 LYS A C   1 
ATOM   2088 O O   . LYS A 1 455 ? 29.180  14.086  61.399  1.00 113.82 ?  436 LYS A O   1 
ATOM   2089 C CB  . LYS A 1 455 ? 28.654  16.604  63.141  1.00 101.17 ?  436 LYS A CB  1 
ATOM   2090 C CG  . LYS A 1 455 ? 29.533  15.791  64.106  1.00 98.50  ?  436 LYS A CG  1 
ATOM   2091 C CD  . LYS A 1 455 ? 28.748  14.661  64.780  1.00 110.78 ?  436 LYS A CD  1 
ATOM   2092 C CE  . LYS A 1 455 ? 29.414  14.212  66.098  1.00 121.25 ?  436 LYS A CE  1 
ATOM   2093 N NZ  . LYS A 1 455 ? 28.642  13.170  66.863  1.00 121.37 ?  436 LYS A NZ  1 
ATOM   2094 N N   . THR A 1 456 ? 27.437  15.044  60.333  1.00 106.92 ?  437 THR A N   1 
ATOM   2095 C CA  . THR A 1 456 ? 26.933  13.809  59.748  1.00 105.22 ?  437 THR A CA  1 
ATOM   2096 C C   . THR A 1 456 ? 27.235  13.682  58.260  1.00 102.57 ?  437 THR A C   1 
ATOM   2097 O O   . THR A 1 456 ? 27.633  12.609  57.814  1.00 108.24 ?  437 THR A O   1 
ATOM   2098 C CB  . THR A 1 456 ? 25.424  13.686  60.008  1.00 103.26 ?  437 THR A CB  1 
ATOM   2099 O OG1 . THR A 1 456 ? 25.219  13.293  61.375  1.00 105.76 ?  437 THR A OG1 1 
ATOM   2100 C CG2 . THR A 1 456 ? 24.803  12.639  59.124  1.00 106.24 ?  437 THR A CG2 1 
ATOM   2101 N N   . GLN A 1 457 ? 27.098  14.752  57.478  1.00 101.24 ?  438 GLN A N   1 
ATOM   2102 C CA  . GLN A 1 457 ? 27.657  14.764  56.128  1.00 96.46  ?  438 GLN A CA  1 
ATOM   2103 C C   . GLN A 1 457 ? 29.143  14.438  56.102  1.00 100.80 ?  438 GLN A C   1 
ATOM   2104 O O   . GLN A 1 457 ? 29.656  14.053  55.053  1.00 108.23 ?  438 GLN A O   1 
ATOM   2105 C CB  . GLN A 1 457 ? 27.498  16.134  55.485  1.00 98.46  ?  438 GLN A CB  1 
ATOM   2106 C CG  . GLN A 1 457 ? 26.084  16.587  55.246  1.00 103.40 ?  438 GLN A CG  1 
ATOM   2107 C CD  . GLN A 1 457 ? 25.504  16.138  53.938  1.00 101.89 ?  438 GLN A CD  1 
ATOM   2108 O OE1 . GLN A 1 457 ? 24.340  15.762  53.861  1.00 103.49 ?  438 GLN A OE1 1 
ATOM   2109 N NE2 . GLN A 1 457 ? 26.301  16.212  52.887  1.00 108.93 ?  438 GLN A NE2 1 
ATOM   2110 N N   . GLU A 1 458 ? 29.863  14.625  57.205  1.00 103.43 ?  439 GLU A N   1 
ATOM   2111 C CA  . GLU A 1 458 ? 31.291  14.329  57.219  1.00 106.32 ?  439 GLU A CA  1 
ATOM   2112 C C   . GLU A 1 458 ? 31.589  12.907  57.657  1.00 102.10 ?  439 GLU A C   1 
ATOM   2113 O O   . GLU A 1 458 ? 32.604  12.348  57.233  1.00 100.20 ?  439 GLU A O   1 
ATOM   2114 C CB  . GLU A 1 458 ? 32.042  15.305  58.131  1.00 111.40 ?  439 GLU A CB  1 
ATOM   2115 C CG  . GLU A 1 458 ? 32.381  16.634  57.474  1.00 111.51 ?  439 GLU A CG  1 
ATOM   2116 C CD  . GLU A 1 458 ? 33.377  17.472  58.289  1.00 128.56 ?  439 GLU A CD  1 
ATOM   2117 O OE1 . GLU A 1 458 ? 33.774  17.039  59.404  1.00 130.11 ?  439 GLU A OE1 1 
ATOM   2118 O OE2 . GLU A 1 458 ? 33.739  18.582  57.823  1.00 126.29 ?  439 GLU A OE2 1 
ATOM   2119 N N   . GLU A 1 459 ? 30.756  12.332  58.535  1.00 108.65 ?  440 GLU A N   1 
ATOM   2120 C CA  . GLU A 1 459 ? 30.788  10.889  58.761  1.00 107.25 ?  440 GLU A CA  1 
ATOM   2121 C C   . GLU A 1 459 ? 30.486  10.141  57.468  1.00 103.53 ?  440 GLU A C   1 
ATOM   2122 O O   . GLU A 1 459 ? 31.085  9.096   57.185  1.00 100.25 ?  440 GLU A O   1 
ATOM   2123 C CB  . GLU A 1 459 ? 29.780  10.492  59.841  1.00 104.03 ?  440 GLU A CB  1 
ATOM   2124 C CG  . GLU A 1 459 ? 30.312  10.465  61.263  1.00 122.80 ?  440 GLU A CG  1 
ATOM   2125 C CD  . GLU A 1 459 ? 29.272  9.947   62.270  1.00 136.14 ?  440 GLU A CD  1 
ATOM   2126 O OE1 . GLU A 1 459 ? 28.662  8.881   61.998  1.00 128.44 ?  440 GLU A OE1 1 
ATOM   2127 O OE2 . GLU A 1 459 ? 29.074  10.598  63.331  1.00 136.02 ?  440 GLU A OE2 1 
ATOM   2128 N N   . LEU A 1 460 ? 29.567  10.679  56.664  1.00 96.76  ?  441 LEU A N   1 
ATOM   2129 C CA  . LEU A 1 460 ? 29.232  10.074  55.383  1.00 96.15  ?  441 LEU A CA  1 
ATOM   2130 C C   . LEU A 1 460 ? 30.382  10.208  54.370  1.00 101.55 ?  441 LEU A C   1 
ATOM   2131 O O   . LEU A 1 460 ? 30.702  9.243   53.666  1.00 101.36 ?  441 LEU A O   1 
ATOM   2132 C CB  . LEU A 1 460 ? 27.940  10.699  54.859  1.00 94.18  ?  441 LEU A CB  1 
ATOM   2133 C CG  . LEU A 1 460 ? 27.563  10.499  53.392  1.00 96.62  ?  441 LEU A CG  1 
ATOM   2134 C CD1 . LEU A 1 460 ? 27.532  9.028   53.036  1.00 102.00 ?  441 LEU A CD1 1 
ATOM   2135 C CD2 . LEU A 1 460 ? 26.239  11.160  53.030  1.00 94.46  ?  441 LEU A CD2 1 
ATOM   2136 N N   . LYS A 1 461 ? 31.005  11.392  54.278  1.00 99.32  ?  442 LYS A N   1 
ATOM   2137 C CA  . LYS A 1 461 ? 32.194  11.596  53.441  1.00 97.42  ?  442 LYS A CA  1 
ATOM   2138 C C   . LYS A 1 461 ? 33.280  10.558  53.744  1.00 98.35  ?  442 LYS A C   1 
ATOM   2139 O O   . LYS A 1 461 ? 33.801  9.909   52.835  1.00 104.99 ?  442 LYS A O   1 
ATOM   2140 C CB  . LYS A 1 461 ? 32.718  13.021  53.672  1.00 95.83  ?  442 LYS A CB  1 
ATOM   2141 C CG  . LYS A 1 461 ? 33.877  13.553  52.813  1.00 90.05  ?  442 LYS A CG  1 
ATOM   2142 C CD  . LYS A 1 461 ? 34.177  15.014  53.211  1.00 108.40 ?  442 LYS A CD  1 
ATOM   2143 C CE  . LYS A 1 461 ? 35.188  15.746  52.363  1.00 114.40 ?  442 LYS A CE  1 
ATOM   2144 N NZ  . LYS A 1 461 ? 36.532  15.501  52.754  1.00 111.92 ?  442 LYS A NZ  1 
ATOM   2145 N N   . GLU A 1 462 ? 33.673  10.415  55.014  1.00 95.07  ?  443 GLU A N   1 
ATOM   2146 C CA  . GLU A 1 462 ? 34.697  9.429   55.338  1.00 99.23  ?  443 GLU A CA  1 
ATOM   2147 C C   . GLU A 1 462 ? 34.244  8.019   54.993  1.00 99.62  ?  443 GLU A C   1 
ATOM   2148 O O   . GLU A 1 462 ? 35.076  7.159   54.680  1.00 95.64  ?  443 GLU A O   1 
ATOM   2149 C CB  . GLU A 1 462 ? 35.109  9.504   56.811  1.00 100.63 ?  443 GLU A CB  1 
ATOM   2150 C CG  . GLU A 1 462 ? 36.153  10.584  57.107  1.00 111.95 ?  443 GLU A CG  1 
ATOM   2151 C CD  . GLU A 1 462 ? 36.848  10.389  58.452  1.00 126.15 ?  443 GLU A CD  1 
ATOM   2152 O OE1 . GLU A 1 462 ? 36.479  9.440   59.183  1.00 120.72 ?  443 GLU A OE1 1 
ATOM   2153 O OE2 . GLU A 1 462 ? 37.784  11.169  58.758  1.00 131.56 ?  443 GLU A OE2 1 
ATOM   2154 N N   . LEU A 1 463 ? 32.945  7.773   55.008  1.00 97.01  ?  444 LEU A N   1 
ATOM   2155 C CA  . LEU A 1 463 ? 32.458  6.449   54.675  1.00 93.65  ?  444 LEU A CA  1 
ATOM   2156 C C   . LEU A 1 463 ? 32.324  6.232   53.179  1.00 96.29  ?  444 LEU A C   1 
ATOM   2157 O O   . LEU A 1 463 ? 32.530  5.114   52.704  1.00 101.04 ?  444 LEU A O   1 
ATOM   2158 C CB  . LEU A 1 463 ? 31.155  6.199   55.413  1.00 92.22  ?  444 LEU A CB  1 
ATOM   2159 C CG  . LEU A 1 463 ? 30.516  4.866   55.141  1.00 90.71  ?  444 LEU A CG  1 
ATOM   2160 C CD1 . LEU A 1 463 ? 29.887  4.348   56.368  1.00 93.25  ?  444 LEU A CD1 1 
ATOM   2161 C CD2 . LEU A 1 463 ? 29.420  5.223   54.175  1.00 85.47  ?  444 LEU A CD2 1 
ATOM   2162 N N   . LEU A 1 464 ? 31.997  7.261   52.410  1.00 96.27  ?  445 LEU A N   1 
ATOM   2163 C CA  . LEU A 1 464 ? 32.121  7.089   50.970  1.00 95.47  ?  445 LEU A CA  1 
ATOM   2164 C C   . LEU A 1 464 ? 33.579  6.910   50.562  1.00 97.91  ?  445 LEU A C   1 
ATOM   2165 O O   . LEU A 1 464 ? 33.863  6.218   49.583  1.00 100.12 ?  445 LEU A O   1 
ATOM   2166 C CB  . LEU A 1 464 ? 31.481  8.262   50.233  1.00 96.06  ?  445 LEU A CB  1 
ATOM   2167 C CG  . LEU A 1 464 ? 29.980  8.399   50.478  1.00 92.46  ?  445 LEU A CG  1 
ATOM   2168 C CD1 . LEU A 1 464 ? 29.352  9.202   49.358  1.00 96.43  ?  445 LEU A CD1 1 
ATOM   2169 C CD2 . LEU A 1 464 ? 29.323  7.032   50.587  1.00 86.91  ?  445 LEU A CD2 1 
ATOM   2170 N N   . ASN A 1 465 ? 34.517  7.472   51.328  1.00 97.93  ?  446 ASN A N   1 
ATOM   2171 C CA  . ASN A 1 465 ? 35.929  7.266   51.027  1.00 97.60  ?  446 ASN A CA  1 
ATOM   2172 C C   . ASN A 1 465 ? 36.342  5.809   51.235  1.00 98.67  ?  446 ASN A C   1 
ATOM   2173 O O   . ASN A 1 465 ? 37.007  5.229   50.371  1.00 99.85  ?  446 ASN A O   1 
ATOM   2174 C CB  . ASN A 1 465 ? 36.800  8.210   51.856  1.00 96.90  ?  446 ASN A CB  1 
ATOM   2175 C CG  . ASN A 1 465 ? 37.075  9.525   51.139  1.00 105.70 ?  446 ASN A CG  1 
ATOM   2176 O OD1 . ASN A 1 465 ? 36.852  9.649   49.929  1.00 99.09  ?  446 ASN A OD1 1 
ATOM   2177 N ND2 . ASN A 1 465 ? 37.570  10.518  51.888  1.00 112.94 ?  446 ASN A ND2 1 
ATOM   2178 N N   . LYS A 1 466 ? 35.972  5.188   52.368  1.00 98.12  ?  447 LYS A N   1 
ATOM   2179 C CA  . LYS A 1 466 ? 36.261  3.759   52.490  1.00 97.56  ?  447 LYS A CA  1 
ATOM   2180 C C   . LYS A 1 466 ? 35.557  2.986   51.381  1.00 95.90  ?  447 LYS A C   1 
ATOM   2181 O O   . LYS A 1 466 ? 36.141  2.078   50.790  1.00 99.62  ?  447 LYS A O   1 
ATOM   2182 C CB  . LYS A 1 466 ? 35.867  3.175   53.864  1.00 91.67  ?  447 LYS A CB  1 
ATOM   2183 C CG  . LYS A 1 466 ? 36.678  3.641   55.084  1.00 95.86  ?  447 LYS A CG  1 
ATOM   2184 C CD  . LYS A 1 466 ? 36.205  2.962   56.378  1.00 103.11 ?  447 LYS A CD  1 
ATOM   2185 C CE  . LYS A 1 466 ? 36.691  1.507   56.516  1.00 106.02 ?  447 LYS A CE  1 
ATOM   2186 N NZ  . LYS A 1 466 ? 38.178  1.384   56.794  1.00 111.38 ?  447 LYS A NZ  1 
ATOM   2187 N N   . MET A 1 467 ? 34.314  3.337   51.064  1.00 89.98  ?  448 MET A N   1 
ATOM   2188 C CA  . MET A 1 467 ? 33.622  2.583   50.025  1.00 90.78  ?  448 MET A CA  1 
ATOM   2189 C C   . MET A 1 467 ? 34.165  2.816   48.615  1.00 94.15  ?  448 MET A C   1 
ATOM   2190 O O   . MET A 1 467 ? 33.996  1.949   47.754  1.00 96.25  ?  448 MET A O   1 
ATOM   2191 C CB  . MET A 1 467 ? 32.139  2.872   50.057  1.00 96.33  ?  448 MET A CB  1 
ATOM   2192 C CG  . MET A 1 467 ? 31.380  2.177   51.173  1.00 98.82  ?  448 MET A CG  1 
ATOM   2193 S SD  . MET A 1 467 ? 29.654  2.760   51.143  1.00 113.98 ?  448 MET A SD  1 
ATOM   2194 C CE  . MET A 1 467 ? 29.018  2.374   49.479  1.00 99.35  ?  448 MET A CE  1 
ATOM   2195 N N   . VAL A 1 468 ? 34.788  3.950   48.319  1.00 96.42  ?  449 VAL A N   1 
ATOM   2196 C CA  . VAL A 1 468 ? 35.338  4.035   46.970  1.00 93.00  ?  449 VAL A CA  1 
ATOM   2197 C C   . VAL A 1 468 ? 36.642  3.250   46.919  1.00 96.87  ?  449 VAL A C   1 
ATOM   2198 O O   . VAL A 1 468 ? 36.936  2.584   45.925  1.00 102.99 ?  449 VAL A O   1 
ATOM   2199 C CB  . VAL A 1 468 ? 35.531  5.501   46.507  1.00 91.92  ?  449 VAL A CB  1 
ATOM   2200 C CG1 . VAL A 1 468 ? 36.787  6.156   47.122  1.00 98.72  ?  449 VAL A CG1 1 
ATOM   2201 C CG2 . VAL A 1 468 ? 35.460  5.663   44.988  1.00 88.36  ?  449 VAL A CG2 1 
ATOM   2202 N N   . ASN A 1 469 ? 37.427  3.295   48.002  1.00 96.19  ?  450 ASN A N   1 
ATOM   2203 C CA  . ASN A 1 469 ? 38.672  2.540   48.076  1.00 96.99  ?  450 ASN A CA  1 
ATOM   2204 C C   . ASN A 1 469 ? 38.416  1.043   48.101  1.00 98.03  ?  450 ASN A C   1 
ATOM   2205 O O   . ASN A 1 469 ? 39.212  0.271   47.559  1.00 101.41 ?  450 ASN A O   1 
ATOM   2206 C CB  . ASN A 1 469 ? 39.471  2.935   49.321  1.00 98.05  ?  450 ASN A CB  1 
ATOM   2207 C CG  . ASN A 1 469 ? 40.157  4.281   49.188  1.00 97.71  ?  450 ASN A CG  1 
ATOM   2208 O OD1 . ASN A 1 469 ? 40.115  4.927   48.134  1.00 92.11  ?  450 ASN A OD1 1 
ATOM   2209 N ND2 . ASN A 1 469 ? 40.831  4.697   50.263  1.00 102.31 ?  450 ASN A ND2 1 
ATOM   2210 N N   . LEU A 1 470 ? 37.329  0.614   48.742  1.00 97.69  ?  451 LEU A N   1 
ATOM   2211 C CA  . LEU A 1 470 ? 37.038  -0.812  48.812  1.00 96.20  ?  451 LEU A CA  1 
ATOM   2212 C C   . LEU A 1 470 ? 36.584  -1.343  47.457  1.00 94.48  ?  451 LEU A C   1 
ATOM   2213 O O   . LEU A 1 470 ? 37.006  -2.425  47.038  1.00 97.29  ?  451 LEU A O   1 
ATOM   2214 C CB  . LEU A 1 470 ? 35.987  -1.083  49.883  1.00 90.00  ?  451 LEU A CB  1 
ATOM   2215 C CG  . LEU A 1 470 ? 36.172  -2.462  50.483  1.00 91.60  ?  451 LEU A CG  1 
ATOM   2216 C CD1 . LEU A 1 470 ? 37.557  -2.556  51.137  1.00 92.60  ?  451 LEU A CD1 1 
ATOM   2217 C CD2 . LEU A 1 470 ? 35.057  -2.748  51.460  1.00 95.90  ?  451 LEU A CD2 1 
ATOM   2218 N N   . LYS A 1 471 ? 35.745  -0.593  46.749  1.00 87.91  ?  452 LYS A N   1 
ATOM   2219 C CA  . LYS A 1 471 ? 35.394  -0.969  45.389  1.00 90.41  ?  452 LYS A CA  1 
ATOM   2220 C C   . LYS A 1 471 ? 36.590  -0.919  44.435  1.00 98.46  ?  452 LYS A C   1 
ATOM   2221 O O   . LYS A 1 471 ? 36.451  -1.270  43.262  1.00 101.87 ?  452 LYS A O   1 
ATOM   2222 C CB  . LYS A 1 471 ? 34.272  -0.064  44.880  1.00 91.00  ?  452 LYS A CB  1 
ATOM   2223 C CG  . LYS A 1 471 ? 33.652  -0.484  43.560  1.00 86.50  ?  452 LYS A CG  1 
ATOM   2224 C CD  . LYS A 1 471 ? 32.701  0.556   43.035  1.00 93.33  ?  452 LYS A CD  1 
ATOM   2225 C CE  . LYS A 1 471 ? 32.168  0.167   41.680  1.00 100.27 ?  452 LYS A CE  1 
ATOM   2226 N NZ  . LYS A 1 471 ? 32.167  1.310   40.728  1.00 103.85 ?  452 LYS A NZ  1 
ATOM   2227 N N   . GLU A 1 472 ? 37.766  -0.498  44.886  1.00 99.93  ?  453 GLU A N   1 
ATOM   2228 C CA  . GLU A 1 472 ? 38.961  -0.605  44.060  1.00 97.11  ?  453 GLU A CA  1 
ATOM   2229 C C   . GLU A 1 472 ? 39.818  -1.798  44.440  1.00 97.95  ?  453 GLU A C   1 
ATOM   2230 O O   . GLU A 1 472 ? 40.343  -2.477  43.552  1.00 98.66  ?  453 GLU A O   1 
ATOM   2231 C CB  . GLU A 1 472 ? 39.794  0.681   44.134  1.00 97.46  ?  453 GLU A CB  1 
ATOM   2232 C CG  . GLU A 1 472 ? 39.004  1.839   43.616  1.00 106.98 ?  453 GLU A CG  1 
ATOM   2233 C CD  . GLU A 1 472 ? 38.558  1.597   42.183  1.00 117.89 ?  453 GLU A CD  1 
ATOM   2234 O OE1 . GLU A 1 472 ? 39.422  1.257   41.349  1.00 119.61 ?  453 GLU A OE1 1 
ATOM   2235 O OE2 . GLU A 1 472 ? 37.338  1.688   41.904  1.00 118.90 ?  453 GLU A OE2 1 
ATOM   2236 N N   . LYS A 1 473 ? 39.961  -2.078  45.744  1.00 96.15  ?  454 LYS A N   1 
ATOM   2237 C CA  . LYS A 1 473 ? 40.590  -3.325  46.152  1.00 102.31 ?  454 LYS A CA  1 
ATOM   2238 C C   . LYS A 1 473 ? 39.754  -4.511  45.673  1.00 98.43  ?  454 LYS A C   1 
ATOM   2239 O O   . LYS A 1 473 ? 40.315  -5.558  45.337  1.00 96.40  ?  454 LYS A O   1 
ATOM   2240 C CB  . LYS A 1 473 ? 40.834  -3.338  47.682  1.00 98.52  ?  454 LYS A CB  1 
ATOM   2241 C CG  . LYS A 1 473 ? 41.627  -4.603  48.152  1.00 110.69 ?  454 LYS A CG  1 
ATOM   2242 C CD  . LYS A 1 473 ? 43.098  -4.649  47.586  1.00 115.59 ?  454 LYS A CD  1 
ATOM   2243 C CE  . LYS A 1 473 ? 44.018  -5.721  48.186  1.00 112.43 ?  454 LYS A CE  1 
ATOM   2244 N NZ  . LYS A 1 473 ? 43.738  -7.084  47.736  1.00 112.42 ?  454 LYS A NZ  1 
ATOM   2245 N N   . ILE A 1 474 ? 38.441  -4.323  45.521  1.00 94.72  ?  455 ILE A N   1 
ATOM   2246 C CA  . ILE A 1 474 ? 37.587  -5.385  45.006  1.00 90.32  ?  455 ILE A CA  1 
ATOM   2247 C C   . ILE A 1 474 ? 37.744  -5.523  43.499  1.00 93.45  ?  455 ILE A C   1 
ATOM   2248 O O   . ILE A 1 474 ? 37.795  -6.635  42.969  1.00 94.69  ?  455 ILE A O   1 
ATOM   2249 C CB  . ILE A 1 474 ? 36.121  -5.136  45.405  1.00 91.94  ?  455 ILE A CB  1 
ATOM   2250 C CG1 . ILE A 1 474 ? 35.864  -5.622  46.836  1.00 92.51  ?  455 ILE A CG1 1 
ATOM   2251 C CG2 . ILE A 1 474 ? 35.171  -5.801  44.417  1.00 93.65  ?  455 ILE A CG2 1 
ATOM   2252 C CD1 . ILE A 1 474 ? 34.636  -4.986  47.482  1.00 92.94  ?  455 ILE A CD1 1 
ATOM   2253 N N   . LYS A 1 475 ? 37.849  -4.406  42.787  1.00 97.83  ?  456 LYS A N   1 
ATOM   2254 C CA  . LYS A 1 475 ? 37.940  -4.465  41.334  1.00 93.20  ?  456 LYS A CA  1 
ATOM   2255 C C   . LYS A 1 475 ? 39.189  -5.232  40.879  1.00 92.56  ?  456 LYS A C   1 
ATOM   2256 O O   . LYS A 1 475 ? 39.114  -6.062  39.965  1.00 87.21  ?  456 LYS A O   1 
ATOM   2257 C CB  . LYS A 1 475 ? 37.882  -3.035  40.771  1.00 89.30  ?  456 LYS A CB  1 
ATOM   2258 C CG  . LYS A 1 475 ? 37.773  -2.914  39.232  1.00 99.38  ?  456 LYS A CG  1 
ATOM   2259 C CD  . LYS A 1 475 ? 37.681  -1.433  38.693  1.00 112.44 ?  456 LYS A CD  1 
ATOM   2260 C CE  . LYS A 1 475 ? 36.304  -0.693  38.857  1.00 114.20 ?  456 LYS A CE  1 
ATOM   2261 N NZ  . LYS A 1 475 ? 35.158  -1.177  37.976  1.00 116.70 ?  456 LYS A NZ  1 
ATOM   2262 N N   . GLU A 1 476 ? 40.335  -5.015  41.538  1.00 92.50  ?  457 GLU A N   1 
ATOM   2263 C CA  . GLU A 1 476 ? 41.553  -5.714  41.142  1.00 92.26  ?  457 GLU A CA  1 
ATOM   2264 C C   . GLU A 1 476 ? 41.615  -7.123  41.721  1.00 92.62  ?  457 GLU A C   1 
ATOM   2265 O O   . GLU A 1 476 ? 42.175  -8.021  41.085  1.00 93.44  ?  457 GLU A O   1 
ATOM   2266 C CB  . GLU A 1 476 ? 42.812  -4.938  41.563  1.00 90.89  ?  457 GLU A CB  1 
ATOM   2267 C CG  . GLU A 1 476 ? 43.083  -4.953  43.069  1.00 102.27 ?  457 GLU A CG  1 
ATOM   2268 C CD  . GLU A 1 476 ? 44.407  -4.303  43.465  1.00 115.55 ?  457 GLU A CD  1 
ATOM   2269 O OE1 . GLU A 1 476 ? 45.005  -3.598  42.620  1.00 115.66 ?  457 GLU A OE1 1 
ATOM   2270 O OE2 . GLU A 1 476 ? 44.832  -4.481  44.637  1.00 121.89 ?  457 GLU A OE2 1 
ATOM   2271 N N   . LEU A 1 477 ? 41.078  -7.340  42.922  1.00 93.26  ?  458 LEU A N   1 
ATOM   2272 C CA  . LEU A 1 477 ? 41.134  -8.674  43.508  1.00 88.40  ?  458 LEU A CA  1 
ATOM   2273 C C   . LEU A 1 477 ? 40.209  -9.627  42.776  1.00 88.04  ?  458 LEU A C   1 
ATOM   2274 O O   . LEU A 1 477 ? 40.425  -10.839 42.803  1.00 88.63  ?  458 LEU A O   1 
ATOM   2275 C CB  . LEU A 1 477 ? 40.768  -8.626  44.987  1.00 90.05  ?  458 LEU A CB  1 
ATOM   2276 C CG  . LEU A 1 477 ? 40.953  -9.885  45.826  1.00 93.94  ?  458 LEU A CG  1 
ATOM   2277 C CD1 . LEU A 1 477 ? 42.433  -10.191 45.986  1.00 95.88  ?  458 LEU A CD1 1 
ATOM   2278 C CD2 . LEU A 1 477 ? 40.266  -9.725  47.183  1.00 92.28  ?  458 LEU A CD2 1 
ATOM   2279 N N   . HIS A 1 478 ? 39.173  -9.099  42.131  1.00 87.78  ?  459 HIS A N   1 
ATOM   2280 C CA  . HIS A 1 478 ? 38.344  -9.917  41.257  1.00 86.05  ?  459 HIS A CA  1 
ATOM   2281 C C   . HIS A 1 478 ? 39.096  -10.274 39.987  1.00 86.73  ?  459 HIS A C   1 
ATOM   2282 O O   . HIS A 1 478 ? 39.150  -11.444 39.595  1.00 90.05  ?  459 HIS A O   1 
ATOM   2283 C CB  . HIS A 1 478 ? 37.063  -9.169  40.922  1.00 89.82  ?  459 HIS A CB  1 
ATOM   2284 C CG  . HIS A 1 478 ? 36.187  -9.858  39.923  1.00 89.09  ?  459 HIS A CG  1 
ATOM   2285 N ND1 . HIS A 1 478 ? 35.279  -10.836 40.275  1.00 84.93  ?  459 HIS A ND1 1 
ATOM   2286 C CD2 . HIS A 1 478 ? 36.060  -9.688  38.584  1.00 85.17  ?  459 HIS A CD2 1 
ATOM   2287 C CE1 . HIS A 1 478 ? 34.626  -11.234 39.197  1.00 84.38  ?  459 HIS A CE1 1 
ATOM   2288 N NE2 . HIS A 1 478 ? 35.083  -10.556 38.157  1.00 84.48  ?  459 HIS A NE2 1 
ATOM   2289 N N   . GLN A 1 479 ? 39.661  -9.266  39.319  1.00 91.27  ?  460 GLN A N   1 
ATOM   2290 C CA  . GLN A 1 479 ? 40.598  -9.483  38.220  1.00 91.36  ?  460 GLN A CA  1 
ATOM   2291 C C   . GLN A 1 479 ? 41.563  -10.616 38.539  1.00 87.73  ?  460 GLN A C   1 
ATOM   2292 O O   . GLN A 1 479 ? 41.685  -11.582 37.783  1.00 88.16  ?  460 GLN A O   1 
ATOM   2293 C CB  . GLN A 1 479 ? 41.379  -8.191  37.943  1.00 88.77  ?  460 GLN A CB  1 
ATOM   2294 C CG  . GLN A 1 479 ? 42.268  -8.263  36.739  1.00 93.08  ?  460 GLN A CG  1 
ATOM   2295 C CD  . GLN A 1 479 ? 41.510  -8.694  35.502  1.00 101.77 ?  460 GLN A CD  1 
ATOM   2296 O OE1 . GLN A 1 479 ? 41.484  -9.880  35.160  1.00 99.75  ?  460 GLN A OE1 1 
ATOM   2297 N NE2 . GLN A 1 479 ? 40.923  -7.725  34.794  1.00 106.12 ?  460 GLN A NE2 1 
ATOM   2298 N N   . GLN A 1 480 ? 42.233  -10.513 39.683  1.00 82.25  ?  461 GLN A N   1 
ATOM   2299 C CA  . GLN A 1 480 ? 43.176  -11.534 40.094  1.00 82.69  ?  461 GLN A CA  1 
ATOM   2300 C C   . GLN A 1 480 ? 42.507  -12.906 40.222  1.00 91.03  ?  461 GLN A C   1 
ATOM   2301 O O   . GLN A 1 480 ? 43.118  -13.931 39.888  1.00 85.96  ?  461 GLN A O   1 
ATOM   2302 C CB  . GLN A 1 480 ? 43.818  -11.107 41.410  1.00 85.51  ?  461 GLN A CB  1 
ATOM   2303 C CG  . GLN A 1 480 ? 45.013  -10.187 41.240  1.00 85.44  ?  461 GLN A CG  1 
ATOM   2304 C CD  . GLN A 1 480 ? 45.469  -9.565  42.554  1.00 91.27  ?  461 GLN A CD  1 
ATOM   2305 O OE1 . GLN A 1 480 ? 45.649  -10.263 43.565  1.00 96.01  ?  461 GLN A OE1 1 
ATOM   2306 N NE2 . GLN A 1 480 ? 45.714  -8.262  42.533  1.00 87.89  ?  461 GLN A NE2 1 
ATOM   2307 N N   . TYR A 1 481 ? 41.255  -12.951 40.682  1.00 87.96  ?  462 TYR A N   1 
ATOM   2308 C CA  . TYR A 1 481 ? 40.587  -14.237 40.822  1.00 77.50  ?  462 TYR A CA  1 
ATOM   2309 C C   . TYR A 1 481 ? 40.219  -14.824 39.468  1.00 81.92  ?  462 TYR A C   1 
ATOM   2310 O O   . TYR A 1 481 ? 40.266  -16.046 39.300  1.00 85.99  ?  462 TYR A O   1 
ATOM   2311 C CB  . TYR A 1 481 ? 39.347  -14.104 41.697  1.00 78.69  ?  462 TYR A CB  1 
ATOM   2312 C CG  . TYR A 1 481 ? 38.355  -15.256 41.578  1.00 81.80  ?  462 TYR A CG  1 
ATOM   2313 C CD1 . TYR A 1 481 ? 37.284  -15.199 40.681  1.00 82.41  ?  462 TYR A CD1 1 
ATOM   2314 C CD2 . TYR A 1 481 ? 38.480  -16.393 42.376  1.00 79.94  ?  462 TYR A CD2 1 
ATOM   2315 C CE1 . TYR A 1 481 ? 36.374  -16.239 40.580  1.00 83.28  ?  462 TYR A CE1 1 
ATOM   2316 C CE2 . TYR A 1 481 ? 37.573  -17.444 42.283  1.00 79.22  ?  462 TYR A CE2 1 
ATOM   2317 C CZ  . TYR A 1 481 ? 36.523  -17.364 41.384  1.00 84.12  ?  462 TYR A CZ  1 
ATOM   2318 O OH  . TYR A 1 481 ? 35.619  -18.406 41.290  1.00 80.08  ?  462 TYR A OH  1 
ATOM   2319 N N   . LYS A 1 482 ? 39.813  -13.993 38.498  1.00 84.50  ?  463 LYS A N   1 
ATOM   2320 C CA  . LYS A 1 482 ? 39.559  -14.528 37.161  1.00 86.89  ?  463 LYS A CA  1 
ATOM   2321 C C   . LYS A 1 482 ? 40.816  -15.182 36.608  1.00 86.67  ?  463 LYS A C   1 
ATOM   2322 O O   . LYS A 1 482 ? 40.816  -16.373 36.283  1.00 83.00  ?  463 LYS A O   1 
ATOM   2323 C CB  . LYS A 1 482 ? 39.060  -13.445 36.201  1.00 84.44  ?  463 LYS A CB  1 
ATOM   2324 C CG  . LYS A 1 482 ? 37.776  -12.812 36.626  1.00 89.89  ?  463 LYS A CG  1 
ATOM   2325 C CD  . LYS A 1 482 ? 36.646  -13.813 36.893  1.00 91.97  ?  463 LYS A CD  1 
ATOM   2326 C CE  . LYS A 1 482 ? 35.887  -14.233 35.639  1.00 99.98  ?  463 LYS A CE  1 
ATOM   2327 N NZ  . LYS A 1 482 ? 34.659  -15.004 36.053  1.00 101.31 ?  463 LYS A NZ  1 
ATOM   2328 N N   . GLU A 1 483 ? 41.913  -14.419 36.552  1.00 81.39  ?  464 GLU A N   1 
ATOM   2329 C CA  . GLU A 1 483 ? 43.181  -14.926 36.046  1.00 83.20  ?  464 GLU A CA  1 
ATOM   2330 C C   . GLU A 1 483 ? 43.561  -16.261 36.693  1.00 86.39  ?  464 GLU A C   1 
ATOM   2331 O O   . GLU A 1 483 ? 43.959  -17.208 36.007  1.00 83.88  ?  464 GLU A O   1 
ATOM   2332 C CB  . GLU A 1 483 ? 44.273  -13.880 36.268  1.00 81.86  ?  464 GLU A CB  1 
ATOM   2333 C CG  . GLU A 1 483 ? 44.133  -12.649 35.369  1.00 96.97  ?  464 GLU A CG  1 
ATOM   2334 C CD  . GLU A 1 483 ? 44.906  -11.422 35.887  1.00 108.87 ?  464 GLU A CD  1 
ATOM   2335 O OE1 . GLU A 1 483 ? 44.769  -10.326 35.277  1.00 105.10 ?  464 GLU A OE1 1 
ATOM   2336 O OE2 . GLU A 1 483 ? 45.657  -11.564 36.894  1.00 111.37 ?  464 GLU A OE2 1 
ATOM   2337 N N   . ALA A 1 484 ? 43.445  -16.353 38.018  1.00 85.34  ?  465 ALA A N   1 
ATOM   2338 C CA  . ALA A 1 484 ? 43.706  -17.614 38.704  1.00 79.26  ?  465 ALA A CA  1 
ATOM   2339 C C   . ALA A 1 484 ? 42.744  -18.707 38.277  1.00 83.92  ?  465 ALA A C   1 
ATOM   2340 O O   . ALA A 1 484 ? 43.111  -19.886 38.282  1.00 83.87  ?  465 ALA A O   1 
ATOM   2341 C CB  . ALA A 1 484 ? 43.586  -17.434 40.216  1.00 82.40  ?  465 ALA A CB  1 
ATOM   2342 N N   . SER A 1 485 ? 41.501  -18.347 37.963  1.00 85.77  ?  466 SER A N   1 
ATOM   2343 C CA  . SER A 1 485 ? 40.490  -19.331 37.609  1.00 90.15  ?  466 SER A CA  1 
ATOM   2344 C C   . SER A 1 485 ? 40.561  -19.712 36.129  1.00 89.98  ?  466 SER A C   1 
ATOM   2345 O O   . SER A 1 485 ? 40.000  -20.745 35.732  1.00 84.28  ?  466 SER A O   1 
ATOM   2346 C CB  . SER A 1 485 ? 39.108  -18.774 38.000  1.00 84.66  ?  466 SER A CB  1 
ATOM   2347 O OG  . SER A 1 485 ? 38.094  -19.764 37.941  1.00 97.55  ?  466 SER A OG  1 
ATOM   2348 N N   . GLU A 1 486 ? 41.271  -18.906 35.326  1.00 89.07  ?  467 GLU A N   1 
ATOM   2349 C CA  . GLU A 1 486 ? 41.482  -19.169 33.907  1.00 88.95  ?  467 GLU A CA  1 
ATOM   2350 C C   . GLU A 1 486 ? 42.450  -20.327 33.694  1.00 88.15  ?  467 GLU A C   1 
ATOM   2351 O O   . GLU A 1 486 ? 42.349  -21.029 32.680  1.00 91.95  ?  467 GLU A O   1 
ATOM   2352 C CB  . GLU A 1 486 ? 42.042  -17.922 33.200  1.00 93.58  ?  467 GLU A CB  1 
ATOM   2353 C CG  . GLU A 1 486 ? 41.266  -16.604 33.391  1.00 105.60 ?  467 GLU A CG  1 
ATOM   2354 C CD  . GLU A 1 486 ? 40.092  -16.406 32.451  1.00 113.02 ?  467 GLU A CD  1 
ATOM   2355 O OE1 . GLU A 1 486 ? 40.313  -16.376 31.219  1.00 121.21 ?  467 GLU A OE1 1 
ATOM   2356 O OE2 . GLU A 1 486 ? 38.947  -16.285 32.956  1.00 112.44 ?  467 GLU A OE2 1 
ATOM   2357 N N   . VAL A 1 487 ? 43.408  -20.512 34.612  1.00 80.44  ?  468 VAL A N   1 
ATOM   2358 C CA  . VAL A 1 487 ? 44.358  -21.621 34.577  1.00 77.49  ?  468 VAL A CA  1 
ATOM   2359 C C   . VAL A 1 487 ? 43.587  -22.932 34.531  1.00 81.53  ?  468 VAL A C   1 
ATOM   2360 O O   . VAL A 1 487 ? 42.833  -23.240 35.454  1.00 79.54  ?  468 VAL A O   1 
ATOM   2361 C CB  . VAL A 1 487 ? 45.312  -21.575 35.781  1.00 64.48  ?  468 VAL A CB  1 
ATOM   2362 C CG1 . VAL A 1 487 ? 46.024  -22.870 35.931  1.00 63.67  ?  468 VAL A CG1 1 
ATOM   2363 C CG2 . VAL A 1 487 ? 46.315  -20.518 35.569  1.00 68.02  ?  468 VAL A CG2 1 
ATOM   2364 N N   . LYS A 1 488 ? 43.755  -23.765 33.358  1.00 90.09  ?  469 LYS A N   1 
ATOM   2365 C CA  . LYS A 1 488 ? 42.705  -24.743 33.540  1.00 88.80  ?  469 LYS A CA  1 
ATOM   2366 C C   . LYS A 1 488 ? 43.227  -25.960 34.295  1.00 86.87  ?  469 LYS A C   1 
ATOM   2367 O O   . LYS A 1 488 ? 44.443  -26.188 34.367  1.00 84.11  ?  469 LYS A O   1 
ATOM   2368 C CB  . LYS A 1 488 ? 42.094  -25.157 32.192  1.00 89.32  ?  469 LYS A CB  1 
ATOM   2369 C CG  . LYS A 1 488 ? 41.358  -24.025 31.401  1.00 98.04  ?  469 LYS A CG  1 
ATOM   2370 C CD  . LYS A 1 488 ? 40.291  -23.276 32.266  1.00 103.21 ?  469 LYS A CD  1 
ATOM   2371 C CE  . LYS A 1 488 ? 39.024  -24.065 32.592  1.00 104.02 ?  469 LYS A CE  1 
ATOM   2372 N NZ  . LYS A 1 488 ? 38.051  -23.245 33.387  1.00 98.06  ?  469 LYS A NZ  1 
ATOM   2373 N N   . PRO A 1 489 ? 42.312  -26.692 34.917  1.00 86.58  ?  470 PRO A N   1 
ATOM   2374 C CA  . PRO A 1 489 ? 42.681  -27.890 35.645  1.00 81.11  ?  470 PRO A CA  1 
ATOM   2375 C C   . PRO A 1 489 ? 43.258  -28.945 34.716  1.00 88.87  ?  470 PRO A C   1 
ATOM   2376 O O   . PRO A 1 489 ? 43.104  -28.869 33.486  1.00 90.59  ?  470 PRO A O   1 
ATOM   2377 C CB  . PRO A 1 489 ? 41.340  -28.346 36.248  1.00 81.29  ?  470 PRO A CB  1 
ATOM   2378 C CG  . PRO A 1 489 ? 40.489  -27.156 36.243  1.00 85.47  ?  470 PRO A CG  1 
ATOM   2379 C CD  . PRO A 1 489 ? 40.864  -26.444 34.996  1.00 89.78  ?  470 PRO A CD  1 
ATOM   2380 N N   . PRO A 1 490 ? 43.912  -29.975 35.268  1.00 94.78  ?  471 PRO A N   1 
ATOM   2381 C CA  . PRO A 1 490 ? 44.101  -30.123 36.720  1.00 87.98  ?  471 PRO A CA  1 
ATOM   2382 C C   . PRO A 1 490 ? 45.316  -29.298 37.195  1.00 84.17  ?  471 PRO A C   1 
ATOM   2383 O O   . PRO A 1 490 ? 46.269  -29.082 36.438  1.00 81.70  ?  471 PRO A O   1 
ATOM   2384 C CB  . PRO A 1 490 ? 44.270  -31.637 36.885  1.00 78.91  ?  471 PRO A CB  1 
ATOM   2385 C CG  . PRO A 1 490 ? 44.971  -32.054 35.609  1.00 82.26  ?  471 PRO A CG  1 
ATOM   2386 C CD  . PRO A 1 490 ? 44.438  -31.130 34.511  1.00 85.96  ?  471 PRO A CD  1 
ATOM   2387 N N   . ARG A 1 491 ? 45.248  -28.803 38.430  1.00 82.48  ?  472 ARG A N   1 
ATOM   2388 C CA  . ARG A 1 491 ? 46.114  -27.739 38.920  1.00 79.07  ?  472 ARG A CA  1 
ATOM   2389 C C   . ARG A 1 491 ? 47.028  -28.304 40.002  1.00 71.30  ?  472 ARG A C   1 
ATOM   2390 O O   . ARG A 1 491 ? 46.671  -29.280 40.660  1.00 86.42  ?  472 ARG A O   1 
ATOM   2391 C CB  . ARG A 1 491 ? 45.252  -26.596 39.462  1.00 77.59  ?  472 ARG A CB  1 
ATOM   2392 C CG  . ARG A 1 491 ? 44.641  -25.710 38.398  1.00 82.84  ?  472 ARG A CG  1 
ATOM   2393 C CD  . ARG A 1 491 ? 44.065  -24.450 39.001  1.00 83.26  ?  472 ARG A CD  1 
ATOM   2394 N NE  . ARG A 1 491 ? 42.663  -24.489 39.447  1.00 77.90  ?  472 ARG A NE  1 
ATOM   2395 C CZ  . ARG A 1 491 ? 41.653  -23.956 38.756  1.00 80.11  ?  472 ARG A CZ  1 
ATOM   2396 N NH1 . ARG A 1 491 ? 40.412  -24.012 39.227  1.00 81.42  ?  472 ARG A NH1 1 
ATOM   2397 N NH2 . ARG A 1 491 ? 41.885  -23.321 37.611  1.00 80.29  ?  472 ARG A NH2 1 
ATOM   2398 N N   . ASP A 1 492 ? 48.208  -27.714 40.212  1.00 66.36  ?  473 ASP A N   1 
ATOM   2399 C CA  . ASP A 1 492 ? 48.878  -28.187 41.416  1.00 70.53  ?  473 ASP A CA  1 
ATOM   2400 C C   . ASP A 1 492 ? 48.256  -27.454 42.602  1.00 72.43  ?  473 ASP A C   1 
ATOM   2401 O O   . ASP A 1 492 ? 47.375  -26.615 42.434  1.00 69.02  ?  473 ASP A O   1 
ATOM   2402 C CB  . ASP A 1 492 ? 50.406  -28.042 41.348  1.00 69.99  ?  473 ASP A CB  1 
ATOM   2403 C CG  . ASP A 1 492 ? 50.925  -26.616 41.561  1.00 84.10  ?  473 ASP A CG  1 
ATOM   2404 O OD1 . ASP A 1 492 ? 50.166  -25.668 41.864  1.00 84.52  ?  473 ASP A OD1 1 
ATOM   2405 O OD2 . ASP A 1 492 ? 52.157  -26.447 41.380  1.00 90.27  ?  473 ASP A OD2 1 
ATOM   2406 N N   . ILE A 1 493 ? 48.689  -27.766 43.819  1.00 79.38  ?  474 ILE A N   1 
ATOM   2407 C CA  . ILE A 1 493 ? 47.867  -27.288 44.922  1.00 79.03  ?  474 ILE A CA  1 
ATOM   2408 C C   . ILE A 1 493 ? 48.139  -25.828 45.273  1.00 76.06  ?  474 ILE A C   1 
ATOM   2409 O O   . ILE A 1 493 ? 47.232  -25.168 45.788  1.00 79.46  ?  474 ILE A O   1 
ATOM   2410 C CB  . ILE A 1 493 ? 47.991  -28.170 46.173  1.00 76.91  ?  474 ILE A CB  1 
ATOM   2411 C CG1 . ILE A 1 493 ? 46.728  -28.009 47.020  1.00 77.50  ?  474 ILE A CG1 1 
ATOM   2412 C CG2 . ILE A 1 493 ? 49.223  -27.772 46.969  1.00 76.14  ?  474 ILE A CG2 1 
ATOM   2413 C CD1 . ILE A 1 493 ? 45.512  -28.699 46.427  1.00 87.25  ?  474 ILE A CD1 1 
ATOM   2414 N N   . THR A 1 494 ? 49.331  -25.278 44.992  1.00 75.63  ?  475 THR A N   1 
ATOM   2415 C CA  . THR A 1 494 ? 49.492  -23.829 45.165  1.00 74.66  ?  475 THR A CA  1 
ATOM   2416 C C   . THR A 1 494 ? 48.634  -23.051 44.164  1.00 73.50  ?  475 THR A C   1 
ATOM   2417 O O   . THR A 1 494 ? 48.029  -22.038 44.511  1.00 75.11  ?  475 THR A O   1 
ATOM   2418 C CB  . THR A 1 494 ? 50.959  -23.395 45.042  1.00 71.83  ?  475 THR A CB  1 
ATOM   2419 O OG1 . THR A 1 494 ? 51.366  -23.431 43.667  1.00 82.36  ?  475 THR A OG1 1 
ATOM   2420 C CG2 . THR A 1 494 ? 51.887  -24.248 45.883  1.00 70.36  ?  475 THR A CG2 1 
ATOM   2421 N N   . ALA A 1 495 ? 48.561  -23.507 42.918  1.00 77.14  ?  476 ALA A N   1 
ATOM   2422 C CA  . ALA A 1 495 ? 47.659  -22.877 41.962  1.00 74.85  ?  476 ALA A CA  1 
ATOM   2423 C C   . ALA A 1 495 ? 46.188  -23.050 42.347  1.00 74.50  ?  476 ALA A C   1 
ATOM   2424 O O   . ALA A 1 495 ? 45.357  -22.190 42.029  1.00 73.49  ?  476 ALA A O   1 
ATOM   2425 C CB  . ALA A 1 495 ? 47.918  -23.445 40.570  1.00 75.31  ?  476 ALA A CB  1 
ATOM   2426 N N   . GLU A 1 496 ? 45.837  -24.154 43.005  1.00 79.31  ?  477 GLU A N   1 
ATOM   2427 C CA  . GLU A 1 496 ? 44.462  -24.334 43.461  1.00 82.11  ?  477 GLU A CA  1 
ATOM   2428 C C   . GLU A 1 496 ? 44.210  -23.554 44.735  1.00 80.35  ?  477 GLU A C   1 
ATOM   2429 O O   . GLU A 1 496 ? 43.088  -23.093 44.970  1.00 81.37  ?  477 GLU A O   1 
ATOM   2430 C CB  . GLU A 1 496 ? 44.150  -25.825 43.679  1.00 83.14  ?  477 GLU A CB  1 
ATOM   2431 C CG  . GLU A 1 496 ? 42.672  -26.134 43.939  1.00 89.83  ?  477 GLU A CG  1 
ATOM   2432 C CD  . GLU A 1 496 ? 41.824  -26.163 42.655  1.00 93.41  ?  477 GLU A CD  1 
ATOM   2433 O OE1 . GLU A 1 496 ? 42.391  -26.222 41.544  1.00 87.90  ?  477 GLU A OE1 1 
ATOM   2434 O OE2 . GLU A 1 496 ? 40.578  -26.124 42.756  1.00 104.96 ?  477 GLU A OE2 1 
ATOM   2435 N N   . PHE A 1 497 ? 45.244  -23.392 45.559  1.00 79.26  ?  478 PHE A N   1 
ATOM   2436 C CA  . PHE A 1 497 ? 45.099  -22.580 46.758  1.00 78.78  ?  478 PHE A CA  1 
ATOM   2437 C C   . PHE A 1 497 ? 44.968  -21.112 46.405  1.00 80.11  ?  478 PHE A C   1 
ATOM   2438 O O   . PHE A 1 497 ? 44.314  -20.366 47.138  1.00 83.82  ?  478 PHE A O   1 
ATOM   2439 C CB  . PHE A 1 497 ? 46.287  -22.811 47.693  1.00 81.01  ?  478 PHE A CB  1 
ATOM   2440 C CG  . PHE A 1 497 ? 46.497  -21.718 48.708  1.00 83.37  ?  478 PHE A CG  1 
ATOM   2441 C CD1 . PHE A 1 497 ? 45.738  -21.676 49.873  1.00 84.71  ?  478 PHE A CD1 1 
ATOM   2442 C CD2 . PHE A 1 497 ? 47.478  -20.761 48.520  1.00 82.01  ?  478 PHE A CD2 1 
ATOM   2443 C CE1 . PHE A 1 497 ? 45.939  -20.681 50.817  1.00 88.32  ?  478 PHE A CE1 1 
ATOM   2444 C CE2 . PHE A 1 497 ? 47.685  -19.764 49.462  1.00 89.51  ?  478 PHE A CE2 1 
ATOM   2445 C CZ  . PHE A 1 497 ? 46.916  -19.721 50.611  1.00 87.73  ?  478 PHE A CZ  1 
ATOM   2446 N N   . LEU A 1 498 ? 45.517  -20.716 45.274  1.00 81.74  ?  479 LEU A N   1 
ATOM   2447 C CA  . LEU A 1 498 ? 45.399  -19.296 44.897  1.00 78.24  ?  479 LEU A CA  1 
ATOM   2448 C C   . LEU A 1 498 ? 43.940  -18.986 44.625  1.00 77.10  ?  479 LEU A C   1 
ATOM   2449 O O   . LEU A 1 498 ? 43.462  -17.998 45.098  1.00 82.25  ?  479 LEU A O   1 
ATOM   2450 C CB  . LEU A 1 498 ? 46.210  -19.048 43.635  1.00 75.04  ?  479 LEU A CB  1 
ATOM   2451 C CG  . LEU A 1 498 ? 46.572  -17.591 43.419  1.00 72.02  ?  479 LEU A CG  1 
ATOM   2452 C CD1 . LEU A 1 498 ? 47.926  -17.309 44.017  1.00 79.98  ?  479 LEU A CD1 1 
ATOM   2453 C CD2 . LEU A 1 498 ? 46.569  -17.252 41.954  1.00 68.27  ?  479 LEU A CD2 1 
ATOM   2454 N N   . VAL A 1 499 ? 43.270  -19.830 43.872  1.00 77.99  ?  480 VAL A N   1 
ATOM   2455 C CA  . VAL A 1 499 ? 41.860  -19.530 43.547  1.00 78.08  ?  480 VAL A CA  1 
ATOM   2456 C C   . VAL A 1 499 ? 41.073  -19.509 44.840  1.00 80.00  ?  480 VAL A C   1 
ATOM   2457 O O   . VAL A 1 499 ? 40.375  -18.562 45.075  1.00 83.10  ?  480 VAL A O   1 
ATOM   2458 C CB  . VAL A 1 499 ? 41.317  -20.633 42.636  1.00 73.54  ?  480 VAL A CB  1 
ATOM   2459 C CG1 . VAL A 1 499 ? 39.962  -20.288 42.077  1.00 71.25  ?  480 VAL A CG1 1 
ATOM   2460 C CG2 . VAL A 1 499 ? 42.279  -20.932 41.519  1.00 76.80  ?  480 VAL A CG2 1 
ATOM   2461 N N   . LYS A 1 500 ? 41.269  -20.499 45.684  1.00 81.55  ?  481 LYS A N   1 
ATOM   2462 C CA  . LYS A 1 500 ? 40.459  -20.537 46.915  1.00 86.06  ?  481 LYS A CA  1 
ATOM   2463 C C   . LYS A 1 500 ? 40.783  -19.329 47.774  1.00 83.61  ?  481 LYS A C   1 
ATOM   2464 O O   . LYS A 1 500 ? 39.867  -18.722 48.269  1.00 86.28  ?  481 LYS A O   1 
ATOM   2465 C CB  . LYS A 1 500 ? 40.753  -21.811 47.700  1.00 88.60  ?  481 LYS A CB  1 
ATOM   2466 C CG  . LYS A 1 500 ? 40.597  -23.104 46.923  1.00 91.45  ?  481 LYS A CG  1 
ATOM   2467 C CD  . LYS A 1 500 ? 39.206  -23.304 46.395  1.00 101.02 ?  481 LYS A CD  1 
ATOM   2468 C CE  . LYS A 1 500 ? 38.748  -24.739 46.491  1.00 95.25  ?  481 LYS A CE  1 
ATOM   2469 N NZ  . LYS A 1 500 ? 39.580  -25.480 47.459  1.00 99.56  ?  481 LYS A NZ  1 
ATOM   2470 N N   . SER A 1 501 ? 42.051  -18.987 47.915  1.00 82.52  ?  482 SER A N   1 
ATOM   2471 C CA  . SER A 1 501 ? 42.344  -17.846 48.804  1.00 80.94  ?  482 SER A CA  1 
ATOM   2472 C C   . SER A 1 501 ? 41.727  -16.579 48.236  1.00 86.71  ?  482 SER A C   1 
ATOM   2473 O O   . SER A 1 501 ? 41.022  -15.910 48.937  1.00 89.02  ?  482 SER A O   1 
ATOM   2474 C CB  . SER A 1 501 ? 43.805  -17.709 49.004  1.00 84.61  ?  482 SER A CB  1 
ATOM   2475 O OG  . SER A 1 501 ? 44.332  -16.631 48.259  1.00 99.74  ?  482 SER A OG  1 
ATOM   2476 N N   . LYS A 1 502 ? 41.894  -16.351 46.947  1.00 84.56  ?  483 LYS A N   1 
ATOM   2477 C CA  . LYS A 1 502 ? 41.355  -15.122 46.332  1.00 80.91  ?  483 LYS A CA  1 
ATOM   2478 C C   . LYS A 1 502 ? 39.841  -15.135 46.476  1.00 83.41  ?  483 LYS A C   1 
ATOM   2479 O O   . LYS A 1 502 ? 39.293  -14.099 46.745  1.00 90.52  ?  483 LYS A O   1 
ATOM   2480 C CB  . LYS A 1 502 ? 41.697  -15.102 44.845  1.00 80.99  ?  483 LYS A CB  1 
ATOM   2481 C CG  . LYS A 1 502 ? 42.728  -14.088 44.389  1.00 80.85  ?  483 LYS A CG  1 
ATOM   2482 C CD  . LYS A 1 502 ? 43.937  -14.036 45.253  1.00 93.28  ?  483 LYS A CD  1 
ATOM   2483 C CE  . LYS A 1 502 ? 44.880  -12.933 44.834  1.00 96.99  ?  483 LYS A CE  1 
ATOM   2484 N NZ  . LYS A 1 502 ? 45.932  -12.686 45.844  1.00 94.21  ?  483 LYS A NZ  1 
ATOM   2485 N N   . HIS A 1 503 ? 39.195  -16.275 46.274  1.00 84.68  ?  484 HIS A N   1 
ATOM   2486 C CA  . HIS A 1 503 ? 37.722  -16.324 46.383  1.00 86.07  ?  484 HIS A CA  1 
ATOM   2487 C C   . HIS A 1 503 ? 37.299  -15.987 47.795  1.00 86.16  ?  484 HIS A C   1 
ATOM   2488 O O   . HIS A 1 503 ? 36.324  -15.307 47.970  1.00 91.41  ?  484 HIS A O   1 
ATOM   2489 C CB  . HIS A 1 503 ? 37.231  -17.735 46.134  1.00 86.92  ?  484 HIS A CB  1 
ATOM   2490 C CG  . HIS A 1 503 ? 35.752  -17.811 46.113  1.00 91.60  ?  484 HIS A CG  1 
ATOM   2491 N ND1 . HIS A 1 503 ? 35.021  -17.920 47.252  1.00 90.66  ?  484 HIS A ND1 1 
ATOM   2492 C CD2 . HIS A 1 503 ? 34.876  -17.771 45.097  1.00 91.31  ?  484 HIS A CD2 1 
ATOM   2493 C CE1 . HIS A 1 503 ? 33.751  -17.961 46.939  1.00 99.45  ?  484 HIS A CE1 1 
ATOM   2494 N NE2 . HIS A 1 503 ? 33.638  -17.872 45.630  1.00 94.94  ?  484 HIS A NE2 1 
ATOM   2495 N N   . ARG A 1 504 ? 38.001  -16.519 48.768  1.00 89.03  ?  485 ARG A N   1 
ATOM   2496 C CA  . ARG A 1 504 ? 37.610  -16.222 50.152  1.00 89.93  ?  485 ARG A CA  1 
ATOM   2497 C C   . ARG A 1 504 ? 37.796  -14.731 50.395  1.00 93.57  ?  485 ARG A C   1 
ATOM   2498 O O   . ARG A 1 504 ? 36.870  -14.096 50.865  1.00 94.22  ?  485 ARG A O   1 
ATOM   2499 C CB  . ARG A 1 504 ? 38.518  -17.022 51.076  1.00 88.77  ?  485 ARG A CB  1 
ATOM   2500 C CG  . ARG A 1 504 ? 38.391  -16.636 52.533  1.00 100.06 ?  485 ARG A CG  1 
ATOM   2501 C CD  . ARG A 1 504 ? 39.396  -15.571 52.846  1.00 94.73  ?  485 ARG A CD  1 
ATOM   2502 N NE  . ARG A 1 504 ? 38.975  -14.930 54.065  1.00 101.16 ?  485 ARG A NE  1 
ATOM   2503 C CZ  . ARG A 1 504 ? 39.664  -13.975 54.639  1.00 101.07 ?  485 ARG A CZ  1 
ATOM   2504 N NH1 . ARG A 1 504 ? 39.231  -13.428 55.756  1.00 107.53 ?  485 ARG A NH1 1 
ATOM   2505 N NH2 . ARG A 1 504 ? 40.788  -13.572 54.092  1.00 96.78  ?  485 ARG A NH2 1 
ATOM   2506 N N   . ASP A 1 505 ? 38.921  -14.189 49.952  1.00 94.91  ?  486 ASP A N   1 
ATOM   2507 C CA  . ASP A 1 505 ? 39.256  -12.769 50.192  1.00 89.22  ?  486 ASP A CA  1 
ATOM   2508 C C   . ASP A 1 505 ? 38.229  -11.871 49.531  1.00 87.72  ?  486 ASP A C   1 
ATOM   2509 O O   . ASP A 1 505 ? 37.917  -10.857 50.087  1.00 94.54  ?  486 ASP A O   1 
ATOM   2510 C CB  . ASP A 1 505 ? 40.592  -12.415 49.567  1.00 87.98  ?  486 ASP A CB  1 
ATOM   2511 C CG  . ASP A 1 505 ? 41.757  -12.936 50.362  1.00 94.43  ?  486 ASP A CG  1 
ATOM   2512 O OD1 . ASP A 1 505 ? 42.875  -12.573 50.034  1.00 93.68  ?  486 ASP A OD1 1 
ATOM   2513 O OD2 . ASP A 1 505 ? 41.518  -13.687 51.295  1.00 100.02 ?  486 ASP A OD2 1 
ATOM   2514 N N   . LEU A 1 506 ? 37.777  -12.211 48.347  1.00 88.30  ?  487 LEU A N   1 
ATOM   2515 C CA  . LEU A 1 506 ? 36.804  -11.310 47.714  1.00 85.06  ?  487 LEU A CA  1 
ATOM   2516 C C   . LEU A 1 506 ? 35.474  -11.448 48.436  1.00 90.06  ?  487 LEU A C   1 
ATOM   2517 O O   . LEU A 1 506 ? 34.700  -10.512 48.401  1.00 97.06  ?  487 LEU A O   1 
ATOM   2518 C CB  . LEU A 1 506 ? 36.684  -11.697 46.249  1.00 82.85  ?  487 LEU A CB  1 
ATOM   2519 C CG  . LEU A 1 506 ? 36.170  -10.590 45.353  1.00 83.93  ?  487 LEU A CG  1 
ATOM   2520 C CD1 . LEU A 1 506 ? 37.111  -10.388 44.195  1.00 91.20  ?  487 LEU A CD1 1 
ATOM   2521 C CD2 . LEU A 1 506 ? 34.789  -10.936 44.852  1.00 93.81  ?  487 LEU A CD2 1 
ATOM   2522 N N   . THR A 1 507 ? 35.197  -12.596 49.035  1.00 90.81  ?  488 THR A N   1 
ATOM   2523 C CA  . THR A 1 507 ? 33.937  -12.685 49.758  1.00 92.57  ?  488 THR A CA  1 
ATOM   2524 C C   . THR A 1 507 ? 34.008  -11.891 51.049  1.00 96.81  ?  488 THR A C   1 
ATOM   2525 O O   . THR A 1 507 ? 33.077  -11.142 51.368  1.00 102.21 ?  488 THR A O   1 
ATOM   2526 C CB  . THR A 1 507 ? 33.582  -14.144 50.040  1.00 88.40  ?  488 THR A CB  1 
ATOM   2527 O OG1 . THR A 1 507 ? 33.790  -14.916 48.858  1.00 95.35  ?  488 THR A OG1 1 
ATOM   2528 C CG2 . THR A 1 507 ? 32.132  -14.264 50.398  1.00 97.29  ?  488 THR A CG2 1 
ATOM   2529 N N   . ALA A 1 508 ? 35.112  -12.039 51.797  1.00 95.44  ?  489 ALA A N   1 
ATOM   2530 C CA  . ALA A 1 508 ? 35.335  -11.240 53.003  1.00 91.35  ?  489 ALA A CA  1 
ATOM   2531 C C   . ALA A 1 508 ? 35.280  -9.746  52.695  1.00 97.22  ?  489 ALA A C   1 
ATOM   2532 O O   . ALA A 1 508 ? 34.655  -8.966  53.427  1.00 102.91 ?  489 ALA A O   1 
ATOM   2533 C CB  . ALA A 1 508 ? 36.678  -11.610 53.634  1.00 78.49  ?  489 ALA A CB  1 
ATOM   2534 N N   . LEU A 1 509 ? 35.924  -9.334  51.609  1.00 94.30  ?  490 LEU A N   1 
ATOM   2535 C CA  . LEU A 1 509 ? 35.924  -7.954  51.159  1.00 88.26  ?  490 LEU A CA  1 
ATOM   2536 C C   . LEU A 1 509 ? 34.565  -7.510  50.643  1.00 91.47  ?  490 LEU A C   1 
ATOM   2537 O O   . LEU A 1 509 ? 34.339  -6.312  50.490  1.00 95.35  ?  490 LEU A O   1 
ATOM   2538 C CB  . LEU A 1 509 ? 36.964  -7.806  50.057  1.00 88.75  ?  490 LEU A CB  1 
ATOM   2539 C CG  . LEU A 1 509 ? 37.809  -6.557  50.019  1.00 91.38  ?  490 LEU A CG  1 
ATOM   2540 C CD1 . LEU A 1 509 ? 38.418  -6.414  51.383  1.00 92.89  ?  490 LEU A CD1 1 
ATOM   2541 C CD2 . LEU A 1 509 ? 38.890  -6.713  48.967  1.00 90.34  ?  490 LEU A CD2 1 
ATOM   2542 N N   . CYS A 1 510 ? 33.674  -8.437  50.331  1.00 94.46  ?  491 CYS A N   1 
ATOM   2543 C CA  . CYS A 1 510 ? 32.334  -8.068  49.914  1.00 94.87  ?  491 CYS A CA  1 
ATOM   2544 C C   . CYS A 1 510 ? 31.385  -7.993  51.094  1.00 100.90 ?  491 CYS A C   1 
ATOM   2545 O O   . CYS A 1 510 ? 30.408  -7.243  51.039  1.00 103.17 ?  491 CYS A O   1 
ATOM   2546 C CB  . CYS A 1 510 ? 31.797  -9.070  48.887  1.00 101.44 ?  491 CYS A CB  1 
ATOM   2547 S SG  . CYS A 1 510 ? 32.377  -8.825  47.186  1.00 98.27  ?  491 CYS A SG  1 
ATOM   2548 N N   . LYS A 1 511 ? 31.637  -8.779  52.148  1.00 100.87 ?  492 LYS A N   1 
ATOM   2549 C CA  . LYS A 1 511 ? 30.930  -8.573  53.407  1.00 103.22 ?  492 LYS A CA  1 
ATOM   2550 C C   . LYS A 1 511 ? 31.149  -7.152  53.914  1.00 105.83 ?  492 LYS A C   1 
ATOM   2551 O O   . LYS A 1 511 ? 30.196  -6.454  54.279  1.00 106.45 ?  492 LYS A O   1 
ATOM   2552 C CB  . LYS A 1 511 ? 31.390  -9.589  54.453  1.00 95.27  ?  492 LYS A CB  1 
ATOM   2553 C CG  . LYS A 1 511 ? 30.712  -10.936 54.366  1.00 112.89 ?  492 LYS A CG  1 
ATOM   2554 C CD  . LYS A 1 511 ? 31.017  -11.777 55.616  1.00 128.31 ?  492 LYS A CD  1 
ATOM   2555 C CE  . LYS A 1 511 ? 30.262  -13.123 55.616  1.00 133.77 ?  492 LYS A CE  1 
ATOM   2556 N NZ  . LYS A 1 511 ? 30.236  -13.794 56.968  1.00 109.10 ?  492 LYS A NZ  1 
ATOM   2557 N N   . GLU A 1 512 ? 32.409  -6.706  53.923  1.00 104.01 ?  493 GLU A N   1 
ATOM   2558 C CA  . GLU A 1 512 ? 32.755  -5.361  54.378  1.00 104.77 ?  493 GLU A CA  1 
ATOM   2559 C C   . GLU A 1 512 ? 31.964  -4.286  53.635  1.00 101.51 ?  493 GLU A C   1 
ATOM   2560 O O   . GLU A 1 512 ? 31.308  -3.446  54.257  1.00 103.96 ?  493 GLU A O   1 
ATOM   2561 C CB  . GLU A 1 512 ? 34.257  -5.131  54.207  1.00 105.31 ?  493 GLU A CB  1 
ATOM   2562 C CG  . GLU A 1 512 ? 34.823  -4.022  55.065  1.00 114.06 ?  493 GLU A CG  1 
ATOM   2563 C CD  . GLU A 1 512 ? 36.318  -4.163  55.285  1.00 119.27 ?  493 GLU A CD  1 
ATOM   2564 O OE1 . GLU A 1 512 ? 36.915  -3.258  55.915  1.00 130.33 ?  493 GLU A OE1 1 
ATOM   2565 O OE2 . GLU A 1 512 ? 36.895  -5.175  54.830  1.00 122.55 ?  493 GLU A OE2 1 
ATOM   2566 N N   . TYR A 1 513 ? 32.033  -4.282  52.301  1.00 97.56  ?  494 TYR A N   1 
ATOM   2567 C CA  . TYR A 1 513 ? 31.301  -3.289  51.519  1.00 92.56  ?  494 TYR A CA  1 
ATOM   2568 C C   . TYR A 1 513 ? 29.797  -3.459  51.647  1.00 96.98  ?  494 TYR A C   1 
ATOM   2569 O O   . TYR A 1 513 ? 29.054  -2.520  51.367  1.00 102.04 ?  494 TYR A O   1 
ATOM   2570 C CB  . TYR A 1 513 ? 31.716  -3.367  50.050  1.00 83.62  ?  494 TYR A CB  1 
ATOM   2571 C CG  . TYR A 1 513 ? 31.071  -2.379  49.093  1.00 80.01  ?  494 TYR A CG  1 
ATOM   2572 C CD1 . TYR A 1 513 ? 31.788  -1.296  48.600  1.00 84.82  ?  494 TYR A CD1 1 
ATOM   2573 C CD2 . TYR A 1 513 ? 29.766  -2.562  48.632  1.00 77.55  ?  494 TYR A CD2 1 
ATOM   2574 C CE1 . TYR A 1 513 ? 31.211  -0.403  47.702  1.00 83.33  ?  494 TYR A CE1 1 
ATOM   2575 C CE2 . TYR A 1 513 ? 29.184  -1.678  47.741  1.00 77.73  ?  494 TYR A CE2 1 
ATOM   2576 C CZ  . TYR A 1 513 ? 29.909  -0.601  47.279  1.00 81.95  ?  494 TYR A CZ  1 
ATOM   2577 O OH  . TYR A 1 513 ? 29.331  0.283   46.394  1.00 84.86  ?  494 TYR A OH  1 
ATOM   2578 N N   . ASP A 1 514 ? 29.316  -4.621  52.061  1.00 98.49  ?  495 ASP A N   1 
ATOM   2579 C CA  . ASP A 1 514 ? 27.883  -4.706  52.299  1.00 105.77 ?  495 ASP A CA  1 
ATOM   2580 C C   . ASP A 1 514 ? 27.517  -4.022  53.619  1.00 107.09 ?  495 ASP A C   1 
ATOM   2581 O O   . ASP A 1 514 ? 26.593  -3.198  53.663  1.00 103.61 ?  495 ASP A O   1 
ATOM   2582 C CB  . ASP A 1 514 ? 27.437  -6.173  52.253  1.00 113.32 ?  495 ASP A CB  1 
ATOM   2583 C CG  . ASP A 1 514 ? 27.374  -6.719  50.817  1.00 114.85 ?  495 ASP A CG  1 
ATOM   2584 O OD1 . ASP A 1 514 ? 27.211  -5.889  49.890  1.00 110.45 ?  495 ASP A OD1 1 
ATOM   2585 O OD2 . ASP A 1 514 ? 27.495  -7.956  50.607  1.00 108.24 ?  495 ASP A OD2 1 
ATOM   2586 N N   . GLU A 1 515 ? 28.271  -4.320  54.687  1.00 104.89 ?  496 GLU A N   1 
ATOM   2587 C CA  . GLU A 1 515 ? 28.102  -3.624  55.961  1.00 103.05 ?  496 GLU A CA  1 
ATOM   2588 C C   . GLU A 1 515 ? 28.227  -2.110  55.795  1.00 106.95 ?  496 GLU A C   1 
ATOM   2589 O O   . GLU A 1 515 ? 27.502  -1.342  56.440  1.00 106.10 ?  496 GLU A O   1 
ATOM   2590 C CB  . GLU A 1 515 ? 29.131  -4.133  56.975  1.00 101.15 ?  496 GLU A CB  1 
ATOM   2591 C CG  . GLU A 1 515 ? 28.884  -5.566  57.455  1.00 115.17 ?  496 GLU A CG  1 
ATOM   2592 C CD  . GLU A 1 515 ? 30.082  -6.169  58.195  1.00 121.23 ?  496 GLU A CD  1 
ATOM   2593 O OE1 . GLU A 1 515 ? 31.080  -5.433  58.409  1.00 118.93 ?  496 GLU A OE1 1 
ATOM   2594 O OE2 . GLU A 1 515 ? 30.016  -7.371  58.571  1.00 113.59 ?  496 GLU A OE2 1 
ATOM   2595 N N   . LEU A 1 516 ? 29.141  -1.659  54.935  1.00 105.54 ?  497 LEU A N   1 
ATOM   2596 C CA  . LEU A 1 516 ? 29.353  -0.225  54.776  1.00 96.54  ?  497 LEU A CA  1 
ATOM   2597 C C   . LEU A 1 516 ? 28.228  0.427   53.994  1.00 101.82 ?  497 LEU A C   1 
ATOM   2598 O O   . LEU A 1 516 ? 27.871  1.569   54.278  1.00 109.96 ?  497 LEU A O   1 
ATOM   2599 C CB  . LEU A 1 516 ? 30.693  0.064   54.097  1.00 91.87  ?  497 LEU A CB  1 
ATOM   2600 C CG  . LEU A 1 516 ? 31.840  0.389   55.059  1.00 93.53  ?  497 LEU A CG  1 
ATOM   2601 C CD1 . LEU A 1 516 ? 32.056  -0.714  56.115  1.00 100.60 ?  497 LEU A CD1 1 
ATOM   2602 C CD2 . LEU A 1 516 ? 33.122  0.700   54.305  1.00 92.52  ?  497 LEU A CD2 1 
ATOM   2603 N N   . ALA A 1 517 ? 27.659  -0.252  53.002  1.00 107.31 ?  498 ALA A N   1 
ATOM   2604 C CA  . ALA A 1 517 ? 26.507  0.363   52.343  1.00 107.97 ?  498 ALA A CA  1 
ATOM   2605 C C   . ALA A 1 517 ? 25.248  0.247   53.175  1.00 108.27 ?  498 ALA A C   1 
ATOM   2606 O O   . ALA A 1 517 ? 24.187  0.708   52.734  1.00 105.98 ?  498 ALA A O   1 
ATOM   2607 C CB  . ALA A 1 517 ? 26.273  -0.243  50.960  1.00 106.01 ?  498 ALA A CB  1 
ATOM   2608 N N   . GLU A 1 518 ? 25.347  -0.358  54.360  1.00 104.35 ?  499 GLU A N   1 
ATOM   2609 C CA  . GLU A 1 518 ? 24.252  -0.409  55.313  1.00 109.40 ?  499 GLU A CA  1 
ATOM   2610 C C   . GLU A 1 518 ? 24.292  0.778   56.267  1.00 110.91 ?  499 GLU A C   1 
ATOM   2611 O O   . GLU A 1 518 ? 23.281  1.457   56.464  1.00 112.26 ?  499 GLU A O   1 
ATOM   2612 C CB  . GLU A 1 518 ? 24.304  -1.728  56.087  1.00 112.66 ?  499 GLU A CB  1 
ATOM   2613 C CG  . GLU A 1 518 ? 22.966  -2.180  56.636  1.00 120.05 ?  499 GLU A CG  1 
ATOM   2614 C CD  . GLU A 1 518 ? 21.927  -2.455  55.534  1.00 130.94 ?  499 GLU A CD  1 
ATOM   2615 O OE1 . GLU A 1 518 ? 20.792  -2.839  55.894  1.00 134.79 ?  499 GLU A OE1 1 
ATOM   2616 O OE2 . GLU A 1 518 ? 22.220  -2.284  54.321  1.00 129.07 ?  499 GLU A OE2 1 
ATOM   2617 N N   . THR A 1 519 ? 25.455  1.027   56.873  1.00 109.84 ?  500 THR A N   1 
ATOM   2618 C CA  . THR A 1 519 ? 25.714  2.314   57.505  1.00 102.48 ?  500 THR A CA  1 
ATOM   2619 C C   . THR A 1 519 ? 25.432  3.467   56.545  1.00 103.76 ?  500 THR A C   1 
ATOM   2620 O O   . THR A 1 519 ? 24.719  4.410   56.887  1.00 112.81 ?  500 THR A O   1 
ATOM   2621 C CB  . THR A 1 519 ? 27.158  2.363   57.997  1.00 100.64 ?  500 THR A CB  1 
ATOM   2622 O OG1 . THR A 1 519 ? 27.351  1.370   59.017  1.00 101.12 ?  500 THR A OG1 1 
ATOM   2623 C CG2 . THR A 1 519 ? 27.472  3.734   58.547  1.00 105.79 ?  500 THR A CG2 1 
ATOM   2624 N N   . GLN A 1 520 ? 25.971  3.404   55.331  1.00 100.78 ?  501 GLN A N   1 
ATOM   2625 C CA  . GLN A 1 520 ? 25.705  4.436   54.332  1.00 101.45 ?  501 GLN A CA  1 
ATOM   2626 C C   . GLN A 1 520 ? 24.217  4.639   54.075  1.00 107.80 ?  501 GLN A C   1 
ATOM   2627 O O   . GLN A 1 520 ? 23.826  5.683   53.539  1.00 111.29 ?  501 GLN A O   1 
ATOM   2628 C CB  . GLN A 1 520 ? 26.410  4.082   53.018  1.00 104.77 ?  501 GLN A CB  1 
ATOM   2629 C CG  . GLN A 1 520 ? 26.449  5.177   51.946  1.00 102.44 ?  501 GLN A CG  1 
ATOM   2630 C CD  . GLN A 1 520 ? 25.627  4.835   50.707  1.00 102.95 ?  501 GLN A CD  1 
ATOM   2631 O OE1 . GLN A 1 520 ? 25.276  3.672   50.482  1.00 114.42 ?  501 GLN A OE1 1 
ATOM   2632 N NE2 . GLN A 1 520 ? 25.357  5.837   49.879  1.00 92.44  ?  501 GLN A NE2 1 
ATOM   2633 N N   . GLY A 1 521 ? 23.375  3.675   54.424  1.00 107.27 ?  502 GLY A N   1 
ATOM   2634 C CA  . GLY A 1 521 ? 21.952  3.864   54.228  1.00 111.83 ?  502 GLY A CA  1 
ATOM   2635 C C   . GLY A 1 521 ? 21.289  4.489   55.436  1.00 111.31 ?  502 GLY A C   1 
ATOM   2636 O O   . GLY A 1 521 ? 20.244  5.133   55.315  1.00 111.38 ?  502 GLY A O   1 
ATOM   2637 N N   . LYS A 1 522 ? 21.901  4.300   56.608  1.00 109.92 ?  503 LYS A N   1 
ATOM   2638 C CA  . LYS A 1 522 ? 21.357  4.864   57.836  1.00 112.81 ?  503 LYS A CA  1 
ATOM   2639 C C   . LYS A 1 522 ? 21.680  6.349   57.945  1.00 117.15 ?  503 LYS A C   1 
ATOM   2640 O O   . LYS A 1 522 ? 20.851  7.138   58.414  1.00 117.62 ?  503 LYS A O   1 
ATOM   2641 C CB  . LYS A 1 522 ? 21.933  4.153   59.053  1.00 112.61 ?  503 LYS A CB  1 
ATOM   2642 C CG  . LYS A 1 522 ? 21.685  2.672   59.170  1.00 108.39 ?  503 LYS A CG  1 
ATOM   2643 C CD  . LYS A 1 522 ? 22.044  2.330   60.614  1.00 119.66 ?  503 LYS A CD  1 
ATOM   2644 C CE  . LYS A 1 522 ? 23.552  2.510   60.954  1.00 120.49 ?  503 LYS A CE  1 
ATOM   2645 N NZ  . LYS A 1 522 ? 23.800  2.187   62.404  1.00 115.12 ?  503 LYS A NZ  1 
ATOM   2646 N N   . LEU A 1 523 ? 22.905  6.735   57.555  1.00 116.35 ?  504 LEU A N   1 
ATOM   2647 C CA  . LEU A 1 523 ? 23.321  8.130   57.595  1.00 108.46 ?  504 LEU A CA  1 
ATOM   2648 C C   . LEU A 1 523 ? 22.712  8.935   56.464  1.00 108.42 ?  504 LEU A C   1 
ATOM   2649 O O   . LEU A 1 523 ? 22.561  10.148  56.605  1.00 111.89 ?  504 LEU A O   1 
ATOM   2650 C CB  . LEU A 1 523 ? 24.848  8.272   57.551  1.00 103.69 ?  504 LEU A CB  1 
ATOM   2651 C CG  . LEU A 1 523 ? 25.718  7.720   58.686  1.00 110.03 ?  504 LEU A CG  1 
ATOM   2652 C CD1 . LEU A 1 523 ? 27.190  8.139   58.519  1.00 108.80 ?  504 LEU A CD1 1 
ATOM   2653 C CD2 . LEU A 1 523 ? 25.174  8.111   60.050  1.00 115.62 ?  504 LEU A CD2 1 
ATOM   2654 N N   . GLU A 1 524 ? 22.369  8.315   55.334  1.00 106.43 ?  505 GLU A N   1 
ATOM   2655 C CA  . GLU A 1 524 ? 21.673  9.113   54.325  1.00 114.15 ?  505 GLU A CA  1 
ATOM   2656 C C   . GLU A 1 524 ? 20.219  9.380   54.679  1.00 114.50 ?  505 GLU A C   1 
ATOM   2657 O O   . GLU A 1 524 ? 19.591  10.222  54.022  1.00 109.54 ?  505 GLU A O   1 
ATOM   2658 C CB  . GLU A 1 524 ? 21.718  8.498   52.921  1.00 117.38 ?  505 GLU A CB  1 
ATOM   2659 C CG  . GLU A 1 524 ? 22.914  8.893   52.048  1.00 113.98 ?  505 GLU A CG  1 
ATOM   2660 C CD  . GLU A 1 524 ? 22.765  8.397   50.608  1.00 119.09 ?  505 GLU A CD  1 
ATOM   2661 O OE1 . GLU A 1 524 ? 21.899  7.525   50.368  1.00 120.73 ?  505 GLU A OE1 1 
ATOM   2662 O OE2 . GLU A 1 524 ? 23.469  8.909   49.707  1.00 118.54 ?  505 GLU A OE2 1 
ATOM   2663 N N   . GLU A 1 525 ? 19.665  8.688   55.676  1.00 114.66 ?  506 GLU A N   1 
ATOM   2664 C CA  . GLU A 1 525 ? 18.318  8.998   56.145  1.00 119.55 ?  506 GLU A CA  1 
ATOM   2665 C C   . GLU A 1 525 ? 18.306  9.911   57.368  1.00 121.15 ?  506 GLU A C   1 
ATOM   2666 O O   . GLU A 1 525 ? 17.438  10.786  57.460  1.00 124.49 ?  506 GLU A O   1 
ATOM   2667 C CB  . GLU A 1 525 ? 17.543  7.707   56.440  1.00 120.00 ?  506 GLU A CB  1 
ATOM   2668 C CG  . GLU A 1 525 ? 17.883  7.034   57.757  1.00 123.57 ?  506 GLU A CG  1 
ATOM   2669 C CD  . GLU A 1 525 ? 17.154  5.718   57.933  1.00 133.53 ?  506 GLU A CD  1 
ATOM   2670 O OE1 . GLU A 1 525 ? 16.544  5.247   56.942  1.00 132.59 ?  506 GLU A OE1 1 
ATOM   2671 O OE2 . GLU A 1 525 ? 17.189  5.161   59.056  1.00 130.95 ?  506 GLU A OE2 1 
ATOM   2672 N N   . LYS A 1 526 ? 19.273  9.755   58.278  1.00 116.46 ?  507 LYS A N   1 
ATOM   2673 C CA  . LYS A 1 526 ? 19.527  10.664  59.389  1.00 109.74 ?  507 LYS A CA  1 
ATOM   2674 C C   . LYS A 1 526 ? 19.874  12.072  58.903  1.00 110.50 ?  507 LYS A C   1 
ATOM   2675 O O   . LYS A 1 526 ? 19.995  12.987  59.714  1.00 117.04 ?  507 LYS A O   1 
ATOM   2676 C CB  . LYS A 1 526 ? 20.655  10.080  60.242  1.00 108.08 ?  507 LYS A CB  1 
ATOM   2677 C CG  . LYS A 1 526 ? 21.036  10.817  61.500  1.00 113.37 ?  507 LYS A CG  1 
ATOM   2678 C CD  . LYS A 1 526 ? 21.742  9.850   62.451  1.00 118.56 ?  507 LYS A CD  1 
ATOM   2679 C CE  . LYS A 1 526 ? 22.346  10.562  63.650  1.00 119.89 ?  507 LYS A CE  1 
ATOM   2680 N NZ  . LYS A 1 526 ? 23.721  11.060  63.354  1.00 116.89 ?  507 LYS A NZ  1 
ATOM   2681 N N   . LEU A 1 527 ? 20.020  12.269  57.593  1.00 108.09 ?  508 LEU A N   1 
ATOM   2682 C CA  . LEU A 1 527 ? 20.327  13.567  56.991  1.00 114.44 ?  508 LEU A CA  1 
ATOM   2683 C C   . LEU A 1 527 ? 19.130  14.209  56.314  1.00 122.74 ?  508 LEU A C   1 
ATOM   2684 O O   . LEU A 1 527 ? 18.980  15.446  56.327  1.00 128.80 ?  508 LEU A O   1 
ATOM   2685 C CB  . LEU A 1 527 ? 21.429  13.458  55.936  1.00 114.48 ?  508 LEU A CB  1 
ATOM   2686 C CG  . LEU A 1 527 ? 22.861  13.474  56.402  1.00 113.92 ?  508 LEU A CG  1 
ATOM   2687 C CD1 . LEU A 1 527 ? 23.676  13.120  55.191  1.00 117.58 ?  508 LEU A CD1 1 
ATOM   2688 C CD2 . LEU A 1 527 ? 23.263  14.832  56.930  1.00 107.23 ?  508 LEU A CD2 1 
ATOM   2689 N N   . GLN A 1 528 ? 18.204  13.352  55.907  1.00 121.52 ?  509 GLN A N   1 
ATOM   2690 C CA  . GLN A 1 528 ? 16.935  13.843  55.334  1.00 127.61 ?  509 GLN A CA  1 
ATOM   2691 C C   . GLN A 1 528 ? 16.006  14.123  56.517  1.00 127.98 ?  509 GLN A C   1 
ATOM   2692 O O   . GLN A 1 528 ? 15.200  15.050  56.440  1.00 129.06 ?  509 GLN A O   1 
ATOM   2693 C CB  . GLN A 1 528 ? 16.347  12.796  54.395  1.00 125.20 ?  509 GLN A CB  1 
ATOM   2694 C CG  . GLN A 1 528 ? 16.111  13.323  52.992  1.00 129.55 ?  509 GLN A CG  1 
ATOM   2695 C CD  . GLN A 1 528 ? 15.377  14.638  53.029  1.00 137.86 ?  509 GLN A CD  1 
ATOM   2696 O OE1 . GLN A 1 528 ? 14.630  14.921  53.959  1.00 137.73 ?  509 GLN A OE1 1 
ATOM   2697 N NE2 . GLN A 1 528 ? 15.584  15.455  52.012  1.00 134.53 ?  509 GLN A NE2 1 
ATOM   2698 N N   . GLU A 1 529 ? 16.125  13.349  57.590  1.00 121.46 ?  510 GLU A N   1 
ATOM   2699 C CA  . GLU A 1 529 ? 15.231  13.628  58.735  1.00 121.24 ?  510 GLU A CA  1 
ATOM   2700 C C   . GLU A 1 529 ? 15.559  15.024  59.254  1.00 125.05 ?  510 GLU A C   1 
ATOM   2701 O O   . GLU A 1 529 ? 14.660  15.849  59.334  1.00 122.45 ?  510 GLU A O   1 
ATOM   2702 C CB  . GLU A 1 529 ? 15.440  12.570  59.817  1.00 126.22 ?  510 GLU A CB  1 
ATOM   2703 C CG  . GLU A 1 529 ? 15.151  13.053  61.224  1.00 129.10 ?  510 GLU A CG  1 
ATOM   2704 C CD  . GLU A 1 529 ? 13.998  12.345  61.918  1.00 137.36 ?  510 GLU A CD  1 
ATOM   2705 O OE1 . GLU A 1 529 ? 13.216  11.670  61.222  1.00 129.97 ?  510 GLU A OE1 1 
ATOM   2706 O OE2 . GLU A 1 529 ? 13.878  12.480  63.153  1.00 137.02 ?  510 GLU A OE2 1 
ATOM   2707 N N   . LEU A 1 530 ? 16.840  15.315  59.442  1.00 122.31 ?  511 LEU A N   1 
ATOM   2708 C CA  . LEU A 1 530 ? 17.243  16.639  59.964  1.00 109.89 ?  511 LEU A CA  1 
ATOM   2709 C C   . LEU A 1 530 ? 16.869  17.702  58.946  1.00 113.42 ?  511 LEU A C   1 
ATOM   2710 O O   . LEU A 1 530 ? 16.305  18.698  59.330  1.00 122.48 ?  511 LEU A O   1 
ATOM   2711 C CB  . LEU A 1 530 ? 18.743  16.628  60.219  1.00 104.45 ?  511 LEU A CB  1 
ATOM   2712 C CG  . LEU A 1 530 ? 19.204  15.507  61.137  1.00 115.63 ?  511 LEU A CG  1 
ATOM   2713 C CD1 . LEU A 1 530 ? 20.213  16.014  62.143  1.00 112.21 ?  511 LEU A CD1 1 
ATOM   2714 C CD2 . LEU A 1 530 ? 18.024  14.884  61.853  1.00 117.03 ?  511 LEU A CD2 1 
ATOM   2715 N N   . GLU A 1 531 ? 17.054  17.420  57.667  1.00 113.99 ?  512 GLU A N   1 
ATOM   2716 C CA  . GLU A 1 531 ? 16.755  18.430  56.629  1.00 120.93 ?  512 GLU A CA  1 
ATOM   2717 C C   . GLU A 1 531 ? 15.281  18.817  56.686  1.00 123.08 ?  512 GLU A C   1 
ATOM   2718 O O   . GLU A 1 531 ? 14.990  19.983  56.471  1.00 122.14 ?  512 GLU A O   1 
ATOM   2719 C CB  . GLU A 1 531 ? 17.097  17.883  55.247  1.00 123.47 ?  512 GLU A CB  1 
ATOM   2720 C CG  . GLU A 1 531 ? 16.846  18.869  54.121  1.00 126.57 ?  512 GLU A CG  1 
ATOM   2721 C CD  . GLU A 1 531 ? 15.385  19.091  53.762  1.00 135.90 ?  512 GLU A CD  1 
ATOM   2722 O OE1 . GLU A 1 531 ? 15.089  20.086  53.074  1.00 135.71 ?  512 GLU A OE1 1 
ATOM   2723 O OE2 . GLU A 1 531 ? 14.547  18.268  54.156  1.00 136.73 ?  512 GLU A OE2 1 
ATOM   2724 N N   . ALA A 1 532 ? 14.382  17.865  56.915  1.00 126.13 ?  513 ALA A N   1 
ATOM   2725 C CA  . ALA A 1 532 ? 12.938  18.179  56.957  1.00 128.07 ?  513 ALA A CA  1 
ATOM   2726 C C   . ALA A 1 532 ? 12.496  18.572  58.369  1.00 126.21 ?  513 ALA A C   1 
ATOM   2727 O O   . ALA A 1 532 ? 11.315  18.836  58.553  1.00 123.89 ?  513 ALA A O   1 
ATOM   2728 C CB  . ALA A 1 532 ? 12.138  17.021  56.433  1.00 129.12 ?  513 ALA A CB  1 
ATOM   2729 N N   . ASN A 1 533 ? 13.408  18.650  59.330  1.00 125.63 ?  514 ASN A N   1 
ATOM   2730 C CA  . ASN A 1 533 ? 12.982  19.070  60.686  1.00 123.40 ?  514 ASN A CA  1 
ATOM   2731 C C   . ASN A 1 533 ? 13.861  20.246  61.090  1.00 119.29 ?  514 ASN A C   1 
ATOM   2732 O O   . ASN A 1 533 ? 14.553  20.143  62.095  1.00 117.38 ?  514 ASN A O   1 
ATOM   2733 C CB  . ASN A 1 533 ? 13.173  17.940  61.694  1.00 123.84 ?  514 ASN A CB  1 
ATOM   2734 C CG  . ASN A 1 533 ? 11.886  17.206  61.990  1.00 134.48 ?  514 ASN A CG  1 
ATOM   2735 O OD1 . ASN A 1 533 ? 11.755  16.561  63.029  1.00 138.50 ?  514 ASN A OD1 1 
ATOM   2736 N ND2 . ASN A 1 533 ? 10.931  17.309  61.081  1.00 129.35 ?  514 ASN A ND2 1 
ATOM   2737 N N   . PRO A 1 534 ? 13.762  21.400  60.409  1.00 112.49 ?  515 PRO A N   1 
ATOM   2738 C CA  . PRO A 1 534 ? 14.606  22.526  60.682  1.00 113.32 ?  515 PRO A CA  1 
ATOM   2739 C C   . PRO A 1 534 ? 13.869  23.383  61.700  1.00 120.11 ?  515 PRO A C   1 
ATOM   2740 O O   . PRO A 1 534 ? 12.675  23.444  61.652  1.00 124.01 ?  515 PRO A O   1 
ATOM   2741 C CB  . PRO A 1 534 ? 14.545  23.269  59.360  1.00 110.84 ?  515 PRO A CB  1 
ATOM   2742 C CG  . PRO A 1 534 ? 13.118  23.144  58.988  1.00 110.02 ?  515 PRO A CG  1 
ATOM   2743 C CD  . PRO A 1 534 ? 12.732  21.763  59.461  1.00 110.65 ?  515 PRO A CD  1 
ATOM   2744 N N   . PRO A 1 535 ? 14.588  24.112  62.564  1.00 114.78 ?  516 PRO A N   1 
ATOM   2745 C CA  . PRO A 1 535 ? 13.981  24.940  63.579  1.00 112.80 ?  516 PRO A CA  1 
ATOM   2746 C C   . PRO A 1 535 ? 13.528  26.280  62.992  1.00 115.10 ?  516 PRO A C   1 
ATOM   2747 O O   . PRO A 1 535 ? 13.850  26.574  61.877  1.00 106.60 ?  516 PRO A O   1 
ATOM   2748 C CB  . PRO A 1 535 ? 15.119  25.063  64.582  1.00 115.05 ?  516 PRO A CB  1 
ATOM   2749 C CG  . PRO A 1 535 ? 16.324  25.146  63.710  1.00 112.68 ?  516 PRO A CG  1 
ATOM   2750 C CD  . PRO A 1 535 ? 16.025  24.215  62.564  1.00 112.38 ?  516 PRO A CD  1 
ATOM   2751 N N   . SER A 1 536 ? 12.823  27.074  63.793  1.00 121.12 ?  517 SER A N   1 
ATOM   2752 C CA  . SER A 1 536 ? 12.236  28.341  63.299  1.00 108.62 ?  517 SER A CA  1 
ATOM   2753 C C   . SER A 1 536 ? 13.305  29.238  62.696  1.00 99.29  ?  517 SER A C   1 
ATOM   2754 O O   . SER A 1 536 ? 14.359  29.377  63.276  1.00 94.98  ?  517 SER A O   1 
ATOM   2755 C CB  . SER A 1 536 ? 11.505  29.035  64.392  1.00 110.60 ?  517 SER A CB  1 
ATOM   2756 O OG  . SER A 1 536 ? 10.764  28.099  65.154  1.00 119.57 ?  517 SER A OG  1 
ATOM   2757 N N   . ASP A 1 537 ? 12.986  29.770  61.528  1.00 95.37  ?  518 ASP A N   1 
ATOM   2758 C CA  . ASP A 1 537 ? 13.835  30.665  60.714  1.00 101.20 ?  518 ASP A CA  1 
ATOM   2759 C C   . ASP A 1 537 ? 14.042  32.011  61.406  1.00 112.33 ?  518 ASP A C   1 
ATOM   2760 O O   . ASP A 1 537 ? 15.152  32.535  61.369  1.00 109.62 ?  518 ASP A O   1 
ATOM   2761 C CB  . ASP A 1 537 ? 13.161  30.829  59.357  1.00 104.55 ?  518 ASP A CB  1 
ATOM   2762 C CG  . ASP A 1 537 ? 13.806  31.857  58.459  1.00 115.16 ?  518 ASP A CG  1 
ATOM   2763 O OD1 . ASP A 1 537 ? 14.826  32.417  58.856  1.00 118.46 ?  518 ASP A OD1 1 
ATOM   2764 O OD2 . ASP A 1 537 ? 13.279  32.075  57.365  1.00 113.95 ?  518 ASP A OD2 1 
ATOM   2765 N N   . VAL A 1 538 ? 12.995  32.553  62.020  1.00 114.19 ?  519 VAL A N   1 
ATOM   2766 C CA  . VAL A 1 538 ? 13.094  33.901  62.641  1.00 103.02 ?  519 VAL A CA  1 
ATOM   2767 C C   . VAL A 1 538 ? 12.429  33.892  64.008  1.00 100.06 ?  519 VAL A C   1 
ATOM   2768 O O   . VAL A 1 538 ? 11.631  33.002  64.263  1.00 96.67  ?  519 VAL A O   1 
ATOM   2769 C CB  . VAL A 1 538 ? 12.339  34.905  61.765  1.00 97.90  ?  519 VAL A CB  1 
ATOM   2770 C CG1 . VAL A 1 538 ? 13.041  35.114  60.444  1.00 108.01 ?  519 VAL A CG1 1 
ATOM   2771 C CG2 . VAL A 1 538 ? 10.922  34.427  61.537  1.00 89.23  ?  519 VAL A CG2 1 
ATOM   2772 N N   . TYR A 1 539 ? 12.762  34.884  64.831  1.00 104.41 ?  520 TYR A N   1 
ATOM   2773 C CA  . TYR A 1 539 ? 12.080  35.034  66.114  1.00 96.00  ?  520 TYR A CA  1 
ATOM   2774 C C   . TYR A 1 539 ? 10.713  35.681  65.928  1.00 88.76  ?  520 TYR A C   1 
ATOM   2775 O O   . TYR A 1 539 ? 9.692   35.141  66.369  1.00 80.83  ?  520 TYR A O   1 
ATOM   2776 C CB  . TYR A 1 539 ? 12.913  35.862  67.087  1.00 94.29  ?  520 TYR A CB  1 
ATOM   2777 C CG  . TYR A 1 539 ? 12.134  36.126  68.344  1.00 94.87  ?  520 TYR A CG  1 
ATOM   2778 C CD1 . TYR A 1 539 ? 11.683  35.073  69.119  1.00 97.05  ?  520 TYR A CD1 1 
ATOM   2779 C CD2 . TYR A 1 539 ? 11.776  37.412  68.719  1.00 94.86  ?  520 TYR A CD2 1 
ATOM   2780 C CE1 . TYR A 1 539 ? 10.943  35.288  70.265  1.00 92.66  ?  520 TYR A CE1 1 
ATOM   2781 C CE2 . TYR A 1 539 ? 11.029  37.634  69.866  1.00 89.46  ?  520 TYR A CE2 1 
ATOM   2782 C CZ  . TYR A 1 539 ? 10.618  36.562  70.630  1.00 89.01  ?  520 TYR A CZ  1 
ATOM   2783 O OH  . TYR A 1 539 ? 9.876   36.752  71.764  1.00 86.80  ?  520 TYR A OH  1 
ATOM   2784 N N   . LEU A 1 540 ? 10.687  36.855  65.297  1.00 90.22  ?  521 LEU A N   1 
ATOM   2785 C CA  . LEU A 1 540 ? 9.452   37.494  64.873  1.00 90.13  ?  521 LEU A CA  1 
ATOM   2786 C C   . LEU A 1 540 ? 9.680   38.173  63.534  1.00 89.96  ?  521 LEU A C   1 
ATOM   2787 O O   . LEU A 1 540 ? 10.716  38.812  63.314  1.00 87.21  ?  521 LEU A O   1 
ATOM   2788 C CB  . LEU A 1 540 ? 8.950   38.534  65.885  1.00 95.49  ?  521 LEU A CB  1 
ATOM   2789 C CG  . LEU A 1 540 ? 8.505   38.090  67.285  1.00 96.86  ?  521 LEU A CG  1 
ATOM   2790 C CD1 . LEU A 1 540 ? 8.497   39.293  68.208  1.00 86.83  ?  521 LEU A CD1 1 
ATOM   2791 C CD2 . LEU A 1 540 ? 7.146   37.361  67.289  1.00 95.41  ?  521 LEU A CD2 1 
ATOM   2792 N N   . SER A 1 541 ? 8.699   38.039  62.650  1.00 87.23  ?  522 SER A N   1 
ATOM   2793 C CA  . SER A 1 541 ? 8.780   38.657  61.341  1.00 88.02  ?  522 SER A CA  1 
ATOM   2794 C C   . SER A 1 541 ? 8.458   40.145  61.411  1.00 92.32  ?  522 SER A C   1 
ATOM   2795 O O   . SER A 1 541 ? 7.964   40.656  62.414  1.00 93.92  ?  522 SER A O   1 
ATOM   2796 C CB  . SER A 1 541 ? 7.820   37.977  60.372  1.00 91.99  ?  522 SER A CB  1 
ATOM   2797 O OG  . SER A 1 541 ? 6.488   38.404  60.582  1.00 90.93  ?  522 SER A OG  1 
ATOM   2798 N N   . SER A 1 542 ? 8.738   40.838  60.301  1.00 98.75  ?  523 SER A N   1 
ATOM   2799 C CA  . SER A 1 542 ? 8.278   42.212  60.112  1.00 98.95  ?  523 SER A CA  1 
ATOM   2800 C C   . SER A 1 542 ? 6.817   42.390  60.480  1.00 100.13 ?  523 SER A C   1 
ATOM   2801 O O   . SER A 1 542 ? 6.430   43.432  61.019  1.00 100.66 ?  523 SER A O   1 
ATOM   2802 C CB  . SER A 1 542 ? 8.455   42.638  58.659  1.00 102.40 ?  523 SER A CB  1 
ATOM   2803 O OG  . SER A 1 542 ? 7.891   43.938  58.470  1.00 115.76 ?  523 SER A OG  1 
ATOM   2804 N N   . ARG A 1 543 ? 6.003   41.408  60.156  1.00 98.86  ?  524 ARG A N   1 
ATOM   2805 C CA  . ARG A 1 543 ? 4.566   41.587  60.425  1.00 95.39  ?  524 ARG A CA  1 
ATOM   2806 C C   . ARG A 1 543 ? 4.300   41.263  61.880  1.00 95.40  ?  524 ARG A C   1 
ATOM   2807 O O   . ARG A 1 543 ? 3.496   41.933  62.477  1.00 94.13  ?  524 ARG A O   1 
ATOM   2808 C CB  . ARG A 1 543 ? 3.763   40.643  59.539  1.00 98.92  ?  524 ARG A CB  1 
ATOM   2809 C CG  . ARG A 1 543 ? 2.360   41.130  59.244  1.00 103.03 ?  524 ARG A CG  1 
ATOM   2810 C CD  . ARG A 1 543 ? 2.034   40.946  57.789  1.00 100.90 ?  524 ARG A CD  1 
ATOM   2811 N NE  . ARG A 1 543 ? 1.079   39.868  57.660  1.00 110.42 ?  524 ARG A NE  1 
ATOM   2812 C CZ  . ARG A 1 543 ? -0.227  40.029  57.742  1.00 125.42 ?  524 ARG A CZ  1 
ATOM   2813 N NH1 . ARG A 1 543 ? -1.027  38.988  57.611  1.00 127.49 ?  524 ARG A NH1 1 
ATOM   2814 N NH2 . ARG A 1 543 ? -0.733  41.227  57.954  1.00 125.19 ?  524 ARG A NH2 1 
ATOM   2815 N N   . ASP A 1 544 ? 4.907   40.218  62.409  1.00 96.10  ?  525 ASP A N   1 
ATOM   2816 C CA  . ASP A 1 544 ? 4.597   39.950  63.827  1.00 94.29  ?  525 ASP A CA  1 
ATOM   2817 C C   . ASP A 1 544 ? 5.106   41.115  64.662  1.00 97.15  ?  525 ASP A C   1 
ATOM   2818 O O   . ASP A 1 544 ? 4.319   41.655  65.411  1.00 99.03  ?  525 ASP A O   1 
ATOM   2819 C CB  . ASP A 1 544 ? 5.214   38.638  64.289  1.00 100.26 ?  525 ASP A CB  1 
ATOM   2820 C CG  . ASP A 1 544 ? 5.017   37.516  63.295  1.00 110.90 ?  525 ASP A CG  1 
ATOM   2821 O OD1 . ASP A 1 544 ? 3.856   37.224  62.970  1.00 115.83 ?  525 ASP A OD1 1 
ATOM   2822 O OD2 . ASP A 1 544 ? 6.034   36.963  62.842  1.00 105.92 ?  525 ASP A OD2 1 
ATOM   2823 N N   . ARG A 1 545 ? 6.332   41.568  64.425  1.00 98.69  ?  526 ARG A N   1 
ATOM   2824 C CA  . ARG A 1 545 ? 6.877   42.666  65.259  1.00 90.54  ?  526 ARG A CA  1 
ATOM   2825 C C   . ARG A 1 545 ? 6.009   43.900  65.085  1.00 83.83  ?  526 ARG A C   1 
ATOM   2826 O O   . ARG A 1 545 ? 6.080   44.759  65.916  1.00 89.22  ?  526 ARG A O   1 
ATOM   2827 C CB  . ARG A 1 545 ? 8.351   42.941  64.982  1.00 85.85  ?  526 ARG A CB  1 
ATOM   2828 C CG  . ARG A 1 545 ? 8.955   43.949  65.945  1.00 97.04  ?  526 ARG A CG  1 
ATOM   2829 C CD  . ARG A 1 545 ? 10.304  43.496  66.464  1.00 101.33 ?  526 ARG A CD  1 
ATOM   2830 N NE  . ARG A 1 545 ? 10.943  44.228  67.556  1.00 104.62 ?  526 ARG A NE  1 
ATOM   2831 C CZ  . ARG A 1 545 ? 10.501  45.333  68.155  1.00 111.22 ?  526 ARG A CZ  1 
ATOM   2832 N NH1 . ARG A 1 545 ? 9.375   45.909  67.782  1.00 96.61  ?  526 ARG A NH1 1 
ATOM   2833 N NH2 . ARG A 1 545 ? 11.202  45.871  69.135  1.00 111.97 ?  526 ARG A NH2 1 
ATOM   2834 N N   . GLN A 1 546 ? 5.234   43.980  64.018  1.00 77.34  ?  527 GLN A N   1 
ATOM   2835 C CA  . GLN A 1 546 ? 4.347   45.156  63.963  1.00 80.40  ?  527 GLN A CA  1 
ATOM   2836 C C   . GLN A 1 546 ? 3.181   44.959  64.916  1.00 79.52  ?  527 GLN A C   1 
ATOM   2837 O O   . GLN A 1 546 ? 2.853   45.878  65.607  1.00 88.06  ?  527 GLN A O   1 
ATOM   2838 C CB  . GLN A 1 546 ? 3.855   45.409  62.548  1.00 80.64  ?  527 GLN A CB  1 
ATOM   2839 C CG  . GLN A 1 546 ? 4.759   46.346  61.778  1.00 94.04  ?  527 GLN A CG  1 
ATOM   2840 C CD  . GLN A 1 546 ? 4.441   46.378  60.307  1.00 97.96  ?  527 GLN A CD  1 
ATOM   2841 O OE1 . GLN A 1 546 ? 3.460   45.816  59.846  1.00 100.38 ?  527 GLN A OE1 1 
ATOM   2842 N NE2 . GLN A 1 546 ? 5.271   47.066  59.555  1.00 95.30  ?  527 GLN A NE2 1 
ATOM   2843 N N   . ILE A 1 547 ? 2.596   43.774  64.957  1.00 78.76  ?  528 ILE A N   1 
ATOM   2844 C CA  . ILE A 1 547 ? 1.432   43.540  65.853  1.00 79.50  ?  528 ILE A CA  1 
ATOM   2845 C C   . ILE A 1 547 ? 1.882   43.642  67.299  1.00 78.54  ?  528 ILE A C   1 
ATOM   2846 O O   . ILE A 1 547 ? 1.124   44.109  68.105  1.00 75.97  ?  528 ILE A O   1 
ATOM   2847 C CB  . ILE A 1 547 ? 0.727   42.216  65.569  1.00 85.80  ?  528 ILE A CB  1 
ATOM   2848 C CG1 . ILE A 1 547 ? -0.105  42.310  64.300  1.00 87.75  ?  528 ILE A CG1 1 
ATOM   2849 C CG2 . ILE A 1 547 ? -0.142  41.846  66.745  1.00 79.60  ?  528 ILE A CG2 1 
ATOM   2850 C CD1 . ILE A 1 547 ? 0.489   41.580  63.146  1.00 86.91  ?  528 ILE A CD1 1 
ATOM   2851 N N   . LEU A 1 548 ? 3.085   43.185  67.607  1.00 77.87  ?  529 LEU A N   1 
ATOM   2852 C CA  . LEU A 1 548 ? 3.633   43.301  68.973  1.00 73.31  ?  529 LEU A CA  1 
ATOM   2853 C C   . LEU A 1 548 ? 3.756   44.777  69.328  1.00 77.41  ?  529 LEU A C   1 
ATOM   2854 O O   . LEU A 1 548 ? 3.563   45.099  70.460  1.00 72.17  ?  529 LEU A O   1 
ATOM   2855 C CB  . LEU A 1 548 ? 5.007   42.649  68.968  1.00 70.20  ?  529 LEU A CB  1 
ATOM   2856 C CG  . LEU A 1 548 ? 5.734   42.635  70.299  1.00 64.46  ?  529 LEU A CG  1 
ATOM   2857 C CD1 . LEU A 1 548 ? 5.011   41.766  71.288  1.00 65.28  ?  529 LEU A CD1 1 
ATOM   2858 C CD2 . LEU A 1 548 ? 7.132   42.118  70.104  1.00 63.82  ?  529 LEU A CD2 1 
ATOM   2859 N N   . ASP A 1 549 ? 4.164   45.619  68.393  1.00 77.27  ?  530 ASP A N   1 
ATOM   2860 C CA  . ASP A 1 549 ? 4.251   47.066  68.658  1.00 68.62  ?  530 ASP A CA  1 
ATOM   2861 C C   . ASP A 1 549 ? 2.885   47.584  69.084  1.00 69.73  ?  530 ASP A C   1 
ATOM   2862 O O   . ASP A 1 549 ? 2.849   48.553  69.776  1.00 75.42  ?  530 ASP A O   1 
ATOM   2863 C CB  . ASP A 1 549 ? 4.748   47.798  67.424  1.00 69.96  ?  530 ASP A CB  1 
ATOM   2864 C CG  . ASP A 1 549 ? 6.237   48.009  67.466  1.00 77.92  ?  530 ASP A CG  1 
ATOM   2865 O OD1 . ASP A 1 549 ? 6.826   47.648  68.457  1.00 74.84  ?  530 ASP A OD1 1 
ATOM   2866 O OD2 . ASP A 1 549 ? 6.772   48.537  66.508  1.00 85.04  ?  530 ASP A OD2 1 
ATOM   2867 N N   . TRP A 1 550 ? 1.796   46.972  68.659  1.00 66.72  ?  531 TRP A N   1 
ATOM   2868 C CA  . TRP A 1 550 ? 0.512   47.484  69.109  1.00 66.55  ?  531 TRP A CA  1 
ATOM   2869 C C   . TRP A 1 550 ? 0.311   47.192  70.586  1.00 66.81  ?  531 TRP A C   1 
ATOM   2870 O O   . TRP A 1 550 ? -0.181  48.047  71.330  1.00 70.44  ?  531 TRP A O   1 
ATOM   2871 C CB  . TRP A 1 550 ? -0.613  46.898  68.277  1.00 65.03  ?  531 TRP A CB  1 
ATOM   2872 C CG  . TRP A 1 550 ? -1.976  47.343  68.677  1.00 63.52  ?  531 TRP A CG  1 
ATOM   2873 C CD1 . TRP A 1 550 ? -2.747  48.284  68.051  1.00 65.56  ?  531 TRP A CD1 1 
ATOM   2874 C CD2 . TRP A 1 550 ? -2.764  46.835  69.766  1.00 63.13  ?  531 TRP A CD2 1 
ATOM   2875 N NE1 . TRP A 1 550 ? -3.959  48.400  68.692  1.00 66.45  ?  531 TRP A NE1 1 
ATOM   2876 C CE2 . TRP A 1 550 ? -3.995  47.523  69.746  1.00 64.93  ?  531 TRP A CE2 1 
ATOM   2877 C CE3 . TRP A 1 550 ? -2.541  45.872  70.764  1.00 70.41  ?  531 TRP A CE3 1 
ATOM   2878 C CZ2 . TRP A 1 550 ? -5.005  47.285  70.688  1.00 66.19  ?  531 TRP A CZ2 1 
ATOM   2879 C CZ3 . TRP A 1 550 ? -3.545  45.634  71.706  1.00 68.77  ?  531 TRP A CZ3 1 
ATOM   2880 C CH2 . TRP A 1 550 ? -4.764  46.340  71.658  1.00 64.74  ?  531 TRP A CH2 1 
ATOM   2881 N N   . HIS A 1 551 ? 0.693   45.998  71.026  1.00 63.28  ?  532 HIS A N   1 
ATOM   2882 C CA  . HIS A 1 551 ? 0.624   45.672  72.442  1.00 68.61  ?  532 HIS A CA  1 
ATOM   2883 C C   . HIS A 1 551 ? 1.574   46.526  73.270  1.00 69.20  ?  532 HIS A C   1 
ATOM   2884 O O   . HIS A 1 551 ? 1.345   46.706  74.471  1.00 71.64  ?  532 HIS A O   1 
ATOM   2885 C CB  . HIS A 1 551 ? 0.942   44.194  72.655  1.00 75.39  ?  532 HIS A CB  1 
ATOM   2886 C CG  . HIS A 1 551 ? -0.138  43.288  72.177  1.00 77.86  ?  532 HIS A CG  1 
ATOM   2887 N ND1 . HIS A 1 551 ? -1.229  42.966  72.950  1.00 86.39  ?  532 HIS A ND1 1 
ATOM   2888 C CD2 . HIS A 1 551 ? -0.331  42.689  70.980  1.00 77.67  ?  532 HIS A CD2 1 
ATOM   2889 C CE1 . HIS A 1 551 ? -2.032  42.174  72.261  1.00 89.20  ?  532 HIS A CE1 1 
ATOM   2890 N NE2 . HIS A 1 551 ? -1.512  41.993  71.062  1.00 84.94  ?  532 HIS A NE2 1 
ATOM   2891 N N   . PHE A 1 552 ? 2.649   47.036  72.668  1.00 65.13  ?  533 PHE A N   1 
ATOM   2892 C CA  . PHE A 1 552 ? 3.497   47.960  73.405  1.00 66.40  ?  533 PHE A CA  1 
ATOM   2893 C C   . PHE A 1 552 ? 2.849   49.329  73.485  1.00 65.41  ?  533 PHE A C   1 
ATOM   2894 O O   . PHE A 1 552 ? 2.900   49.977  74.534  1.00 63.23  ?  533 PHE A O   1 
ATOM   2895 C CB  . PHE A 1 552 ? 4.881   48.055  72.772  1.00 66.38  ?  533 PHE A CB  1 
ATOM   2896 C CG  . PHE A 1 552 ? 5.717   46.825  72.966  1.00 66.24  ?  533 PHE A CG  1 
ATOM   2897 C CD1 . PHE A 1 552 ? 5.614   46.077  74.132  1.00 70.73  ?  533 PHE A CD1 1 
ATOM   2898 C CD2 . PHE A 1 552 ? 6.603   46.409  71.982  1.00 62.37  ?  533 PHE A CD2 1 
ATOM   2899 C CE1 . PHE A 1 552 ? 6.396   44.928  74.313  1.00 70.45  ?  533 PHE A CE1 1 
ATOM   2900 C CE2 . PHE A 1 552 ? 7.383   45.289  72.161  1.00 62.97  ?  533 PHE A CE2 1 
ATOM   2901 C CZ  . PHE A 1 552 ? 7.281   44.544  73.325  1.00 64.69  ?  533 PHE A CZ  1 
ATOM   2902 N N   . ALA A 1 553 ? 2.209   49.770  72.400  1.00 67.01  ?  534 ALA A N   1 
ATOM   2903 C CA  . ALA A 1 553 ? 1.380   50.967  72.488  1.00 66.86  ?  534 ALA A CA  1 
ATOM   2904 C C   . ALA A 1 553 ? 0.327   50.836  73.576  1.00 64.30  ?  534 ALA A C   1 
ATOM   2905 O O   . ALA A 1 553 ? -0.023  51.830  74.209  1.00 71.62  ?  534 ALA A O   1 
ATOM   2906 C CB  . ALA A 1 553 ? 0.703   51.264  71.151  1.00 64.78  ?  534 ALA A CB  1 
ATOM   2907 N N   . ASN A 1 554 ? -0.189  49.635  73.820  1.00 62.24  ?  535 ASN A N   1 
ATOM   2908 C CA  . ASN A 1 554 ? -1.176  49.507  74.881  1.00 64.41  ?  535 ASN A CA  1 
ATOM   2909 C C   . ASN A 1 554 ? -0.562  49.772  76.253  1.00 62.07  ?  535 ASN A C   1 
ATOM   2910 O O   . ASN A 1 554 ? -1.145  50.508  77.046  1.00 64.18  ?  535 ASN A O   1 
ATOM   2911 C CB  . ASN A 1 554 ? -1.871  48.141  74.852  1.00 64.78  ?  535 ASN A CB  1 
ATOM   2912 C CG  . ASN A 1 554 ? -3.359  48.277  75.111  1.00 64.32  ?  535 ASN A CG  1 
ATOM   2913 O OD1 . ASN A 1 554 ? -3.977  49.240  74.668  1.00 69.89  ?  535 ASN A OD1 1 
ATOM   2914 N ND2 . ASN A 1 554 ? -3.916  47.387  75.898  1.00 64.41  ?  535 ASN A ND2 1 
ATOM   2915 N N   . LEU A 1 555 ? 0.585   49.149  76.579  1.00 60.46  ?  536 LEU A N   1 
ATOM   2916 C CA  . LEU A 1 555 ? 1.350   49.617  77.734  1.00 64.19  ?  536 LEU A CA  1 
ATOM   2917 C C   . LEU A 1 555 ? 1.645   51.108  77.714  1.00 64.63  ?  536 LEU A C   1 
ATOM   2918 O O   . LEU A 1 555 ? 1.578   51.759  78.759  1.00 65.45  ?  536 LEU A O   1 
ATOM   2919 C CB  . LEU A 1 555 ? 2.649   48.849  77.916  1.00 61.07  ?  536 LEU A CB  1 
ATOM   2920 C CG  . LEU A 1 555 ? 2.494   47.891  79.068  1.00 63.45  ?  536 LEU A CG  1 
ATOM   2921 C CD1 . LEU A 1 555 ? 1.529   46.811  78.767  1.00 81.85  ?  536 LEU A CD1 1 
ATOM   2922 C CD2 . LEU A 1 555 ? 3.900   47.386  79.402  1.00 63.71  ?  536 LEU A CD2 1 
ATOM   2923 N N   . GLU A 1 556 ? 2.015   51.665  76.565  1.00 61.52  ?  537 GLU A N   1 
ATOM   2924 C CA  . GLU A 1 556 ? 2.315   53.088  76.554  1.00 63.04  ?  537 GLU A CA  1 
ATOM   2925 C C   . GLU A 1 556 ? 1.081   53.902  76.953  1.00 66.46  ?  537 GLU A C   1 
ATOM   2926 O O   . GLU A 1 556 ? 1.182   54.856  77.740  1.00 62.65  ?  537 GLU A O   1 
ATOM   2927 C CB  . GLU A 1 556 ? 2.895   53.478  75.189  1.00 61.53  ?  537 GLU A CB  1 
ATOM   2928 C CG  . GLU A 1 556 ? 4.172   52.637  74.947  1.00 68.05  ?  537 GLU A CG  1 
ATOM   2929 C CD  . GLU A 1 556 ? 5.219   53.224  74.003  1.00 71.12  ?  537 GLU A CD  1 
ATOM   2930 O OE1 . GLU A 1 556 ? 4.862   53.644  72.866  1.00 71.92  ?  537 GLU A OE1 1 
ATOM   2931 O OE2 . GLU A 1 556 ? 6.416   53.232  74.414  1.00 67.62  ?  537 GLU A OE2 1 
ATOM   2932 N N   . PHE A 1 557 ? -0.100  53.486  76.489  1.00 64.55  ?  538 PHE A N   1 
ATOM   2933 C CA  . PHE A 1 557 ? -1.354  54.105  76.918  1.00 60.30  ?  538 PHE A CA  1 
ATOM   2934 C C   . PHE A 1 557 ? -1.632  53.887  78.405  1.00 59.75  ?  538 PHE A C   1 
ATOM   2935 O O   . PHE A 1 557 ? -1.973  54.830  79.115  1.00 68.39  ?  538 PHE A O   1 
ATOM   2936 C CB  . PHE A 1 557 ? -2.498  53.586  76.054  1.00 62.77  ?  538 PHE A CB  1 
ATOM   2937 C CG  . PHE A 1 557 ? -3.822  53.582  76.744  1.00 70.25  ?  538 PHE A CG  1 
ATOM   2938 C CD1 . PHE A 1 557 ? -4.418  54.754  77.138  1.00 70.97  ?  538 PHE A CD1 1 
ATOM   2939 C CD2 . PHE A 1 557 ? -4.482  52.376  76.987  1.00 73.87  ?  538 PHE A CD2 1 
ATOM   2940 C CE1 . PHE A 1 557 ? -5.645  54.740  77.785  1.00 74.00  ?  538 PHE A CE1 1 
ATOM   2941 C CE2 . PHE A 1 557 ? -5.716  52.351  77.617  1.00 73.31  ?  538 PHE A CE2 1 
ATOM   2942 C CZ  . PHE A 1 557 ? -6.299  53.546  78.014  1.00 77.90  ?  538 PHE A CZ  1 
ATOM   2943 N N   . ALA A 1 558 ? -1.498  52.657  78.899  1.00 60.06  ?  539 ALA A N   1 
ATOM   2944 C CA  . ALA A 1 558 ? -1.759  52.388  80.316  1.00 64.42  ?  539 ALA A CA  1 
ATOM   2945 C C   . ALA A 1 558 ? -0.975  53.318  81.255  1.00 68.51  ?  539 ALA A C   1 
ATOM   2946 O O   . ALA A 1 558 ? -1.518  53.824  82.250  1.00 67.89  ?  539 ALA A O   1 
ATOM   2947 C CB  . ALA A 1 558 ? -1.417  50.940  80.635  1.00 57.16  ?  539 ALA A CB  1 
ATOM   2948 N N   . ASN A 1 559 ? 0.300   53.538  80.967  1.00 59.95  ?  540 ASN A N   1 
ATOM   2949 C CA  . ASN A 1 559 ? 1.163   54.323  81.816  1.00 58.17  ?  540 ASN A CA  1 
ATOM   2950 C C   . ASN A 1 559 ? 1.422   55.703  81.244  1.00 60.37  ?  540 ASN A C   1 
ATOM   2951 O O   . ASN A 1 559 ? 2.268   56.439  81.768  1.00 60.64  ?  540 ASN A O   1 
ATOM   2952 C CB  . ASN A 1 559 ? 2.458   53.559  82.044  1.00 58.37  ?  540 ASN A CB  1 
ATOM   2953 C CG  . ASN A 1 559 ? 2.201   52.186  82.559  1.00 59.27  ?  540 ASN A CG  1 
ATOM   2954 O OD1 . ASN A 1 559 ? 1.916   51.958  83.747  1.00 62.31  ?  540 ASN A OD1 1 
ATOM   2955 N ND2 . ASN A 1 559 ? 2.184   51.256  81.639  1.00 68.16  ?  540 ASN A ND2 1 
ATOM   2956 N N   . ALA A 1 560 ? 0.688   56.074  80.205  1.00 59.77  ?  541 ALA A N   1 
ATOM   2957 C CA  . ALA A 1 560 ? 0.785   57.391  79.561  1.00 64.78  ?  541 ALA A CA  1 
ATOM   2958 C C   . ALA A 1 560 ? 2.229   57.888  79.382  1.00 57.77  ?  541 ALA A C   1 
ATOM   2959 O O   . ALA A 1 560 ? 2.544   59.031  79.696  1.00 56.60  ?  541 ALA A O   1 
ATOM   2960 C CB  . ALA A 1 560 ? -0.041  58.417  80.330  1.00 61.57  ?  541 ALA A CB  1 
ATOM   2961 N N   . THR A 1 561 ? 3.113   57.025  78.827  1.00 59.42  ?  542 THR A N   1 
ATOM   2962 C CA  . THR A 1 561 ? 4.530   57.350  78.658  1.00 52.31  ?  542 THR A CA  1 
ATOM   2963 C C   . THR A 1 561 ? 5.266   56.315  77.806  1.00 62.44  ?  542 THR A C   1 
ATOM   2964 O O   . THR A 1 561 ? 4.897   55.130  77.797  1.00 61.98  ?  542 THR A O   1 
ATOM   2965 C CB  . THR A 1 561 ? 5.216   57.478  80.022  1.00 52.61  ?  542 THR A CB  1 
ATOM   2966 O OG1 . THR A 1 561 ? 6.497   58.089  79.863  1.00 57.20  ?  542 THR A OG1 1 
ATOM   2967 C CG2 . THR A 1 561 ? 5.399   56.119  80.698  1.00 55.15  ?  542 THR A CG2 1 
ATOM   2968 N N   . PRO A 1 562 ? 6.267   56.733  77.030  1.00 62.56  ?  543 PRO A N   1 
ATOM   2969 C CA  . PRO A 1 562 ? 7.161   55.769  76.392  1.00 63.40  ?  543 PRO A CA  1 
ATOM   2970 C C   . PRO A 1 562 ? 7.729   54.772  77.385  1.00 60.87  ?  543 PRO A C   1 
ATOM   2971 O O   . PRO A 1 562 ? 8.180   55.144  78.472  1.00 61.42  ?  543 PRO A O   1 
ATOM   2972 C CB  . PRO A 1 562 ? 8.263   56.658  75.810  1.00 64.05  ?  543 PRO A CB  1 
ATOM   2973 C CG  . PRO A 1 562 ? 7.677   58.017  75.723  1.00 61.80  ?  543 PRO A CG  1 
ATOM   2974 C CD  . PRO A 1 562 ? 6.318   58.022  76.330  1.00 65.08  ?  543 PRO A CD  1 
ATOM   2975 N N   . LEU A 1 563 ? 7.744   53.494  76.987  1.00 59.57  ?  544 LEU A N   1 
ATOM   2976 C CA  . LEU A 1 563 ? 8.321   52.485  77.867  1.00 60.31  ?  544 LEU A CA  1 
ATOM   2977 C C   . LEU A 1 563 ? 9.786   52.761  78.173  1.00 56.24  ?  544 LEU A C   1 
ATOM   2978 O O   . LEU A 1 563 ? 10.320  52.203  79.134  1.00 61.71  ?  544 LEU A O   1 
ATOM   2979 C CB  . LEU A 1 563 ? 8.142   51.082  77.263  1.00 58.15  ?  544 LEU A CB  1 
ATOM   2980 C CG  . LEU A 1 563 ? 6.738   50.840  76.679  1.00 59.68  ?  544 LEU A CG  1 
ATOM   2981 C CD1 . LEU A 1 563 ? 6.623   49.486  76.025  1.00 63.92  ?  544 LEU A CD1 1 
ATOM   2982 C CD2 . LEU A 1 563 ? 5.622   51.012  77.713  1.00 63.28  ?  544 LEU A CD2 1 
ATOM   2983 N N   . SER A 1 564 ? 10.444  53.622  77.407  1.00 56.11  ?  545 SER A N   1 
ATOM   2984 C CA  . SER A 1 564 ? 11.842  53.920  77.672  1.00 57.60  ?  545 SER A CA  1 
ATOM   2985 C C   . SER A 1 564 ? 12.043  54.735  78.937  1.00 62.86  ?  545 SER A C   1 
ATOM   2986 O O   . SER A 1 564 ? 13.189  54.861  79.382  1.00 63.45  ?  545 SER A O   1 
ATOM   2987 C CB  . SER A 1 564 ? 12.442  54.660  76.479  1.00 65.31  ?  545 SER A CB  1 
ATOM   2988 O OG  . SER A 1 564 ? 11.555  55.670  76.024  1.00 73.30  ?  545 SER A OG  1 
ATOM   2989 N N   . THR A 1 565 ? 10.962  55.293  79.509  1.00 63.18  ?  546 THR A N   1 
ATOM   2990 C CA  . THR A 1 565 ? 10.995  56.112  80.716  1.00 60.68  ?  546 THR A CA  1 
ATOM   2991 C C   . THR A 1 565 ? 10.518  55.395  81.981  1.00 65.22  ?  546 THR A C   1 
ATOM   2992 O O   . THR A 1 565 ? 10.862  55.850  83.083  1.00 59.31  ?  546 THR A O   1 
ATOM   2993 C CB  . THR A 1 565 ? 10.114  57.358  80.548  1.00 61.26  ?  546 THR A CB  1 
ATOM   2994 O OG1 . THR A 1 565 ? 8.748   56.951  80.390  1.00 57.98  ?  546 THR A OG1 1 
ATOM   2995 C CG2 . THR A 1 565 ? 10.528  58.208  79.350  1.00 60.65  ?  546 THR A CG2 1 
ATOM   2996 N N   . LEU A 1 566 ? 9.713   54.323  81.859  1.00 62.99  ?  547 LEU A N   1 
ATOM   2997 C CA  . LEU A 1 566 ? 9.200   53.621  83.034  1.00 57.48  ?  547 LEU A CA  1 
ATOM   2998 C C   . LEU A 1 566 ? 10.338  52.908  83.750  1.00 62.60  ?  547 LEU A C   1 
ATOM   2999 O O   . LEU A 1 566 ? 11.270  52.403  83.114  1.00 63.61  ?  547 LEU A O   1 
ATOM   3000 C CB  . LEU A 1 566 ? 8.125   52.608  82.647  1.00 56.35  ?  547 LEU A CB  1 
ATOM   3001 C CG  . LEU A 1 566 ? 6.754   53.140  82.231  1.00 58.33  ?  547 LEU A CG  1 
ATOM   3002 C CD1 . LEU A 1 566 ? 6.034   52.183  81.303  1.00 58.53  ?  547 LEU A CD1 1 
ATOM   3003 C CD2 . LEU A 1 566 ? 5.911   53.342  83.435  1.00 61.77  ?  547 LEU A CD2 1 
ATOM   3004 N N   . SER A 1 567 ? 10.273  52.897  85.079  1.00 58.76  ?  548 SER A N   1 
ATOM   3005 C CA  . SER A 1 567 ? 11.222  52.135  85.872  1.00 59.29  ?  548 SER A CA  1 
ATOM   3006 C C   . SER A 1 567 ? 10.989  50.656  85.651  1.00 66.03  ?  548 SER A C   1 
ATOM   3007 O O   . SER A 1 567 ? 9.864   50.176  85.808  1.00 68.37  ?  548 SER A O   1 
ATOM   3008 C CB  . SER A 1 567 ? 11.051  52.460  87.352  1.00 60.55  ?  548 SER A CB  1 
ATOM   3009 O OG  . SER A 1 567 ? 11.716  51.512  88.171  1.00 59.06  ?  548 SER A OG  1 
ATOM   3010 N N   . LEU A 1 568 ? 12.041  49.918  85.293  1.00 66.74  ?  549 LEU A N   1 
ATOM   3011 C CA  . LEU A 1 568 ? 11.867  48.472  85.192  1.00 69.18  ?  549 LEU A CA  1 
ATOM   3012 C C   . LEU A 1 568 ? 11.479  47.886  86.553  1.00 64.32  ?  549 LEU A C   1 
ATOM   3013 O O   . LEU A 1 568 ? 10.485  47.161  86.662  1.00 59.19  ?  549 LEU A O   1 
ATOM   3014 C CB  . LEU A 1 568 ? 13.128  47.802  84.628  1.00 70.00  ?  549 LEU A CB  1 
ATOM   3015 C CG  . LEU A 1 568 ? 13.172  46.258  84.739  1.00 65.06  ?  549 LEU A CG  1 
ATOM   3016 C CD1 . LEU A 1 568 ? 12.160  45.608  83.804  1.00 56.04  ?  549 LEU A CD1 1 
ATOM   3017 C CD2 . LEU A 1 568 ? 14.573  45.719  84.498  1.00 61.55  ?  549 LEU A CD2 1 
ATOM   3018 N N   . LYS A 1 569 ? 12.207  48.252  87.617  1.00 60.22  ?  550 LYS A N   1 
ATOM   3019 C CA  . LYS A 1 569 ? 11.929  47.657  88.923  1.00 62.28  ?  550 LYS A CA  1 
ATOM   3020 C C   . LYS A 1 569 ? 10.512  47.962  89.407  1.00 65.36  ?  550 LYS A C   1 
ATOM   3021 O O   . LYS A 1 569 ? 9.810   47.062  89.888  1.00 65.74  ?  550 LYS A O   1 
ATOM   3022 C CB  . LYS A 1 569 ? 12.951  48.111  89.964  1.00 60.29  ?  550 LYS A CB  1 
ATOM   3023 C CG  . LYS A 1 569 ? 13.109  47.046  91.068  1.00 74.76  ?  550 LYS A CG  1 
ATOM   3024 C CD  . LYS A 1 569 ? 13.962  47.500  92.272  1.00 86.33  ?  550 LYS A CD  1 
ATOM   3025 C CE  . LYS A 1 569 ? 15.462  47.612  91.928  1.00 90.19  ?  550 LYS A CE  1 
ATOM   3026 N NZ  . LYS A 1 569 ? 16.383  47.495  93.117  1.00 84.60  ?  550 LYS A NZ  1 
ATOM   3027 N N   . HIS A 1 570 ? 10.054  49.214  89.256  1.00 68.90  ?  551 HIS A N   1 
ATOM   3028 C CA  . HIS A 1 570 ? 8.894   49.687  90.003  1.00 63.97  ?  551 HIS A CA  1 
ATOM   3029 C C   . HIS A 1 570 ? 7.661   50.070  89.185  1.00 62.74  ?  551 HIS A C   1 
ATOM   3030 O O   . HIS A 1 570 ? 6.633   50.382  89.793  1.00 61.32  ?  551 HIS A O   1 
ATOM   3031 C CB  . HIS A 1 570 ? 9.283   50.898  90.854  1.00 55.33  ?  551 HIS A CB  1 
ATOM   3032 C CG  . HIS A 1 570 ? 10.446  50.659  91.757  1.00 61.47  ?  551 HIS A CG  1 
ATOM   3033 N ND1 . HIS A 1 570 ? 10.394  49.780  92.817  1.00 67.02  ?  551 HIS A ND1 1 
ATOM   3034 C CD2 . HIS A 1 570 ? 11.680  51.220  91.793  1.00 64.90  ?  551 HIS A CD2 1 
ATOM   3035 C CE1 . HIS A 1 570 ? 11.552  49.796  93.458  1.00 68.42  ?  551 HIS A CE1 1 
ATOM   3036 N NE2 . HIS A 1 570 ? 12.351  50.663  92.860  1.00 62.22  ?  551 HIS A NE2 1 
ATOM   3037 N N   . TRP A 1 571 ? 7.711   50.053  87.851  1.00 59.27  ?  552 TRP A N   1 
ATOM   3038 C CA  . TRP A 1 571 ? 6.605   50.607  87.068  1.00 59.91  ?  552 TRP A CA  1 
ATOM   3039 C C   . TRP A 1 571 ? 5.254   49.979  87.385  1.00 61.53  ?  552 TRP A C   1 
ATOM   3040 O O   . TRP A 1 571 ? 4.212   50.566  87.080  1.00 64.68  ?  552 TRP A O   1 
ATOM   3041 C CB  . TRP A 1 571 ? 6.867   50.444  85.573  1.00 60.72  ?  552 TRP A CB  1 
ATOM   3042 C CG  . TRP A 1 571 ? 6.717   49.016  85.122  1.00 70.77  ?  552 TRP A CG  1 
ATOM   3043 C CD1 . TRP A 1 571 ? 7.651   48.003  85.230  1.00 64.04  ?  552 TRP A CD1 1 
ATOM   3044 C CD2 . TRP A 1 571 ? 5.562   48.431  84.501  1.00 67.47  ?  552 TRP A CD2 1 
ATOM   3045 N NE1 . TRP A 1 571 ? 7.137   46.841  84.713  1.00 60.46  ?  552 TRP A NE1 1 
ATOM   3046 C CE2 . TRP A 1 571 ? 5.868   47.072  84.252  1.00 58.69  ?  552 TRP A CE2 1 
ATOM   3047 C CE3 . TRP A 1 571 ? 4.304   48.924  84.131  1.00 62.72  ?  552 TRP A CE3 1 
ATOM   3048 C CZ2 . TRP A 1 571 ? 4.976   46.210  83.647  1.00 56.13  ?  552 TRP A CZ2 1 
ATOM   3049 C CZ3 . TRP A 1 571 ? 3.414   48.056  83.526  1.00 67.03  ?  552 TRP A CZ3 1 
ATOM   3050 C CH2 . TRP A 1 571 ? 3.761   46.709  83.287  1.00 62.80  ?  552 TRP A CH2 1 
ATOM   3051 N N   . ASP A 1 572 ? 5.229   48.797  87.963  1.00 68.28  ?  553 ASP A N   1 
ATOM   3052 C CA  . ASP A 1 572 ? 3.958   48.160  88.278  1.00 75.23  ?  553 ASP A CA  1 
ATOM   3053 C C   . ASP A 1 572 ? 3.820   47.941  89.780  1.00 73.95  ?  553 ASP A C   1 
ATOM   3054 O O   . ASP A 1 572 ? 3.130   47.027  90.216  1.00 80.74  ?  553 ASP A O   1 
ATOM   3055 C CB  . ASP A 1 572 ? 3.794   46.853  87.488  1.00 75.18  ?  553 ASP A CB  1 
ATOM   3056 C CG  . ASP A 1 572 ? 4.896   45.803  87.802  1.00 80.04  ?  553 ASP A CG  1 
ATOM   3057 O OD1 . ASP A 1 572 ? 6.001   46.163  88.321  1.00 72.97  ?  553 ASP A OD1 1 
ATOM   3058 O OD2 . ASP A 1 572 ? 4.636   44.601  87.531  1.00 81.84  ?  553 ASP A OD2 1 
ATOM   3059 N N   . GLN A 1 573 ? 4.464   48.794  90.586  1.00 74.68  ?  554 GLN A N   1 
ATOM   3060 C CA  . GLN A 1 573 ? 4.476   48.601  92.037  1.00 76.73  ?  554 GLN A CA  1 
ATOM   3061 C C   . GLN A 1 573 ? 3.087   48.685  92.669  1.00 76.75  ?  554 GLN A C   1 
ATOM   3062 O O   . GLN A 1 573 ? 2.910   48.223  93.803  1.00 79.05  ?  554 GLN A O   1 
ATOM   3063 C CB  . GLN A 1 573 ? 5.409   49.612  92.698  1.00 73.65  ?  554 GLN A CB  1 
ATOM   3064 C CG  . GLN A 1 573 ? 5.135   51.060  92.348  1.00 72.69  ?  554 GLN A CG  1 
ATOM   3065 C CD  . GLN A 1 573 ? 4.205   51.734  93.334  1.00 74.60  ?  554 GLN A CD  1 
ATOM   3066 O OE1 . GLN A 1 573 ? 4.411   51.680  94.562  1.00 74.21  ?  554 GLN A OE1 1 
ATOM   3067 N NE2 . GLN A 1 573 ? 3.166   52.370  92.804  1.00 71.64  ?  554 GLN A NE2 1 
ATOM   3068 N N   . ASP A 1 574 ? 2.097   49.215  91.951  1.00 73.02  ?  555 ASP A N   1 
ATOM   3069 C CA  . ASP A 1 574 ? 0.731   49.342  92.434  1.00 75.80  ?  555 ASP A CA  1 
ATOM   3070 C C   . ASP A 1 574 ? -0.194  48.222  91.932  1.00 84.78  ?  555 ASP A C   1 
ATOM   3071 O O   . ASP A 1 574 ? -1.421  48.354  92.022  1.00 82.80  ?  555 ASP A O   1 
ATOM   3072 C CB  . ASP A 1 574 ? 0.193   50.736  92.055  1.00 79.08  ?  555 ASP A CB  1 
ATOM   3073 C CG  . ASP A 1 574 ? 0.007   50.930  90.536  1.00 85.95  ?  555 ASP A CG  1 
ATOM   3074 O OD1 . ASP A 1 574 ? -1.147  51.116  90.084  1.00 85.26  ?  555 ASP A OD1 1 
ATOM   3075 O OD2 . ASP A 1 574 ? 1.015   50.893  89.790  1.00 89.40  ?  555 ASP A OD2 1 
ATOM   3076 N N   . ASP A 1 575 ? 0.363   47.110  91.427  1.00 94.73  ?  556 ASP A N   1 
ATOM   3077 C CA  . ASP A 1 575 ? -0.491  46.051  90.879  1.00 94.34  ?  556 ASP A CA  1 
ATOM   3078 C C   . ASP A 1 575 ? -1.248  45.307  91.971  1.00 91.64  ?  556 ASP A C   1 
ATOM   3079 O O   . ASP A 1 575 ? -2.381  44.864  91.741  1.00 88.56  ?  556 ASP A O   1 
ATOM   3080 C CB  . ASP A 1 575 ? 0.315   45.044  90.047  1.00 92.33  ?  556 ASP A CB  1 
ATOM   3081 C CG  . ASP A 1 575 ? 0.354   45.393  88.549  1.00 107.76 ?  556 ASP A CG  1 
ATOM   3082 O OD1 . ASP A 1 575 ? -0.001  46.543  88.153  1.00 110.48 ?  556 ASP A OD1 1 
ATOM   3083 O OD2 . ASP A 1 575 ? 0.726   44.488  87.762  1.00 114.87 ?  556 ASP A OD2 1 
ATOM   3084 N N   . ASP A 1 576 ? -0.652  45.180  93.162  1.00 85.12  ?  557 ASP A N   1 
ATOM   3085 C CA  . ASP A 1 576 ? -1.272  44.445  94.260  1.00 83.04  ?  557 ASP A CA  1 
ATOM   3086 C C   . ASP A 1 576 ? -2.622  45.013  94.689  1.00 82.84  ?  557 ASP A C   1 
ATOM   3087 O O   . ASP A 1 576 ? -3.403  44.311  95.340  1.00 86.68  ?  557 ASP A O   1 
ATOM   3088 C CB  . ASP A 1 576 ? -0.321  44.429  95.450  1.00 86.80  ?  557 ASP A CB  1 
ATOM   3089 C CG  . ASP A 1 576 ? 0.777   43.401  95.295  1.00 108.52 ?  557 ASP A CG  1 
ATOM   3090 O OD1 . ASP A 1 576 ? 1.079   43.009  94.139  1.00 107.43 ?  557 ASP A OD1 1 
ATOM   3091 O OD2 . ASP A 1 576 ? 1.325   42.975  96.336  1.00 119.83 ?  557 ASP A OD2 1 
ATOM   3092 N N   . PHE A 1 577 ? -2.921  46.260  94.347  1.00 82.83  ?  558 PHE A N   1 
ATOM   3093 C CA  . PHE A 1 577 ? -4.126  46.920  94.814  1.00 70.77  ?  558 PHE A CA  1 
ATOM   3094 C C   . PHE A 1 577 ? -5.142  47.099  93.701  1.00 75.82  ?  558 PHE A C   1 
ATOM   3095 O O   . PHE A 1 577 ? -6.016  47.960  93.813  1.00 80.14  ?  558 PHE A O   1 
ATOM   3096 C CB  . PHE A 1 577 ? -3.752  48.258  95.441  1.00 67.78  ?  558 PHE A CB  1 
ATOM   3097 C CG  . PHE A 1 577 ? -2.652  48.149  96.472  1.00 69.92  ?  558 PHE A CG  1 
ATOM   3098 C CD1 . PHE A 1 577 ? -2.947  47.888  97.803  1.00 70.74  ?  558 PHE A CD1 1 
ATOM   3099 C CD2 . PHE A 1 577 ? -1.317  48.291  96.115  1.00 69.05  ?  558 PHE A CD2 1 
ATOM   3100 C CE1 . PHE A 1 577 ? -1.928  47.789  98.768  1.00 64.22  ?  558 PHE A CE1 1 
ATOM   3101 C CE2 . PHE A 1 577 ? -0.299  48.180  97.083  1.00 62.31  ?  558 PHE A CE2 1 
ATOM   3102 C CZ  . PHE A 1 577 ? -0.614  47.928  98.403  1.00 54.27  ?  558 PHE A CZ  1 
ATOM   3103 N N   . GLU A 1 578 ? -5.022  46.319  92.619  1.00 77.27  ?  559 GLU A N   1 
ATOM   3104 C CA  . GLU A 1 578 ? -6.027  46.294  91.560  1.00 72.84  ?  559 GLU A CA  1 
ATOM   3105 C C   . GLU A 1 578 ? -7.401  46.037  92.176  1.00 71.81  ?  559 GLU A C   1 
ATOM   3106 O O   . GLU A 1 578 ? -7.539  45.282  93.144  1.00 70.85  ?  559 GLU A O   1 
ATOM   3107 C CB  . GLU A 1 578 ? -5.647  45.202  90.542  1.00 92.23  ?  559 GLU A CB  1 
ATOM   3108 C CG  . GLU A 1 578 ? -6.262  45.221  89.095  1.00 106.58 ?  559 GLU A CG  1 
ATOM   3109 C CD  . GLU A 1 578 ? -5.905  43.930  88.240  1.00 117.18 ?  559 GLU A CD  1 
ATOM   3110 O OE1 . GLU A 1 578 ? -5.348  42.931  88.789  1.00 99.96  ?  559 GLU A OE1 1 
ATOM   3111 O OE2 . GLU A 1 578 ? -6.199  43.914  87.016  1.00 112.51 ?  559 GLU A OE2 1 
ATOM   3112 N N   . PHE A 1 579 ? -8.415  46.720  91.669  1.00 72.74  ?  560 PHE A N   1 
ATOM   3113 C CA  . PHE A 1 579 ? -9.751  46.355  92.109  1.00 76.08  ?  560 PHE A CA  1 
ATOM   3114 C C   . PHE A 1 579 ? -10.204 45.078  91.380  1.00 79.53  ?  560 PHE A C   1 
ATOM   3115 O O   . PHE A 1 579 ? -9.585  44.634  90.404  1.00 85.39  ?  560 PHE A O   1 
ATOM   3116 C CB  . PHE A 1 579 ? -10.722 47.512  91.866  1.00 73.34  ?  560 PHE A CB  1 
ATOM   3117 C CG  . PHE A 1 579 ? -10.373 48.772  92.611  1.00 75.02  ?  560 PHE A CG  1 
ATOM   3118 C CD1 . PHE A 1 579 ? -9.891  48.721  93.916  1.00 78.83  ?  560 PHE A CD1 1 
ATOM   3119 C CD2 . PHE A 1 579 ? -10.531 50.022  92.010  1.00 75.01  ?  560 PHE A CD2 1 
ATOM   3120 C CE1 . PHE A 1 579 ? -9.562  49.900  94.616  1.00 71.60  ?  560 PHE A CE1 1 
ATOM   3121 C CE2 . PHE A 1 579 ? -10.207 51.212  92.703  1.00 69.03  ?  560 PHE A CE2 1 
ATOM   3122 C CZ  . PHE A 1 579 ? -9.719  51.146  94.001  1.00 65.61  ?  560 PHE A CZ  1 
ATOM   3123 N N   . THR A 1 580 ? -11.292 44.476  91.857  1.00 70.56  ?  561 THR A N   1 
ATOM   3124 C CA  . THR A 1 580 ? -11.865 43.304  91.207  1.00 73.94  ?  561 THR A CA  1 
ATOM   3125 C C   . THR A 1 580 ? -13.136 43.668  90.445  1.00 81.09  ?  561 THR A C   1 
ATOM   3126 O O   . THR A 1 580 ? -13.903 44.545  90.859  1.00 83.01  ?  561 THR A O   1 
ATOM   3127 C CB  . THR A 1 580 ? -12.188 42.214  92.216  1.00 70.17  ?  561 THR A CB  1 
ATOM   3128 O OG1 . THR A 1 580 ? -13.331 42.621  92.972  1.00 77.11  ?  561 THR A OG1 1 
ATOM   3129 C CG2 . THR A 1 580 ? -10.992 41.944  93.148  1.00 66.44  ?  561 THR A CG2 1 
ATOM   3130 N N   . GLY A 1 581 ? -13.350 42.986  89.326  1.00 80.32  ?  562 GLY A N   1 
ATOM   3131 C CA  . GLY A 1 581 ? -14.496 43.222  88.469  1.00 80.94  ?  562 GLY A CA  1 
ATOM   3132 C C   . GLY A 1 581 ? -14.092 43.816  87.131  1.00 80.94  ?  562 GLY A C   1 
ATOM   3133 O O   . GLY A 1 581 ? -12.931 44.163  86.885  1.00 74.39  ?  562 GLY A O   1 
ATOM   3134 N N   . SER A 1 582 ? -15.084 43.902  86.241  1.00 80.09  ?  563 SER A N   1 
ATOM   3135 C CA  . SER A 1 582 ? -14.820 44.525  84.951  1.00 86.59  ?  563 SER A CA  1 
ATOM   3136 C C   . SER A 1 582 ? -14.697 46.025  85.104  1.00 82.08  ?  563 SER A C   1 
ATOM   3137 O O   . SER A 1 582 ? -15.291 46.632  85.992  1.00 85.43  ?  563 SER A O   1 
ATOM   3138 C CB  . SER A 1 582 ? -15.904 44.224  83.910  1.00 92.75  ?  563 SER A CB  1 
ATOM   3139 O OG  . SER A 1 582 ? -15.801 42.907  83.394  1.00 110.32 ?  563 SER A OG  1 
ATOM   3140 N N   . HIS A 1 583 ? -13.889 46.603  84.232  1.00 77.23  ?  564 HIS A N   1 
ATOM   3141 C CA  . HIS A 1 583 ? -13.836 48.035  84.029  1.00 70.60  ?  564 HIS A CA  1 
ATOM   3142 C C   . HIS A 1 583 ? -15.179 48.512  83.500  1.00 76.69  ?  564 HIS A C   1 
ATOM   3143 O O   . HIS A 1 583 ? -15.960 47.727  82.957  1.00 88.66  ?  564 HIS A O   1 
ATOM   3144 C CB  . HIS A 1 583 ? -12.675 48.269  83.079  1.00 66.96  ?  564 HIS A CB  1 
ATOM   3145 C CG  . HIS A 1 583 ? -11.354 48.011  83.736  1.00 71.15  ?  564 HIS A CG  1 
ATOM   3146 N ND1 . HIS A 1 583 ? -11.158 46.911  84.545  1.00 71.87  ?  564 HIS A ND1 1 
ATOM   3147 C CD2 . HIS A 1 583 ? -10.126 48.553  83.546  1.00 70.72  ?  564 HIS A CD2 1 
ATOM   3148 C CE1 . HIS A 1 583 ? -9.902  46.877  84.949  1.00 68.92  ?  564 HIS A CE1 1 
ATOM   3149 N NE2 . HIS A 1 583 ? -9.248  47.850  84.341  1.00 70.83  ?  564 HIS A NE2 1 
ATOM   3150 N N   . LEU A 1 584 ? -15.489 49.788  83.705  1.00 74.81  ?  565 LEU A N   1 
ATOM   3151 C CA  . LEU A 1 584 ? -16.770 50.322  83.276  1.00 75.39  ?  565 LEU A CA  1 
ATOM   3152 C C   . LEU A 1 584 ? -16.512 51.670  82.643  1.00 79.30  ?  565 LEU A C   1 
ATOM   3153 O O   . LEU A 1 584 ? -15.433 52.249  82.788  1.00 77.92  ?  565 LEU A O   1 
ATOM   3154 C CB  . LEU A 1 584 ? -17.752 50.472  84.434  1.00 77.21  ?  565 LEU A CB  1 
ATOM   3155 C CG  . LEU A 1 584 ? -18.089 49.197  85.216  1.00 86.13  ?  565 LEU A CG  1 
ATOM   3156 C CD1 . LEU A 1 584 ? -17.036 48.930  86.256  1.00 80.15  ?  565 LEU A CD1 1 
ATOM   3157 C CD2 . LEU A 1 584 ? -19.414 49.307  85.922  1.00 92.99  ?  565 LEU A CD2 1 
ATOM   3158 N N   . THR A 1 585 ? -17.497 52.174  81.921  1.00 82.03  ?  566 THR A N   1 
ATOM   3159 C CA  . THR A 1 585 ? -17.390 53.537  81.440  1.00 80.94  ?  566 THR A CA  1 
ATOM   3160 C C   . THR A 1 585 ? -18.520 54.331  82.052  1.00 85.47  ?  566 THR A C   1 
ATOM   3161 O O   . THR A 1 585 ? -19.464 53.778  82.625  1.00 87.13  ?  566 THR A O   1 
ATOM   3162 C CB  . THR A 1 585 ? -17.418 53.642  79.899  1.00 86.24  ?  566 THR A CB  1 
ATOM   3163 O OG1 . THR A 1 585 ? -18.731 53.371  79.378  1.00 89.31  ?  566 THR A OG1 1 
ATOM   3164 C CG2 . THR A 1 585 ? -16.390 52.680  79.288  1.00 79.58  ?  566 THR A CG2 1 
ATOM   3165 N N   . VAL A 1 586 ? -18.396 55.643  81.960  1.00 86.85  ?  567 VAL A N   1 
ATOM   3166 C CA  . VAL A 1 586 ? -19.411 56.533  82.483  1.00 90.20  ?  567 VAL A CA  1 
ATOM   3167 C C   . VAL A 1 586 ? -20.102 57.085  81.254  1.00 94.39  ?  567 VAL A C   1 
ATOM   3168 O O   . VAL A 1 586 ? -19.496 57.815  80.459  1.00 95.93  ?  567 VAL A O   1 
ATOM   3169 C CB  . VAL A 1 586 ? -18.817 57.627  83.378  1.00 82.79  ?  567 VAL A CB  1 
ATOM   3170 C CG1 . VAL A 1 586 ? -19.839 58.731  83.603  1.00 94.54  ?  567 VAL A CG1 1 
ATOM   3171 C CG2 . VAL A 1 586 ? -18.340 57.028  84.684  1.00 70.96  ?  567 VAL A CG2 1 
ATOM   3172 N N   . ARG A 1 587 ? -21.351 56.680  81.067  1.00 98.86  ?  568 ARG A N   1 
ATOM   3173 C CA  . ARG A 1 587 ? -21.993 56.796  79.774  1.00 103.15 ?  568 ARG A CA  1 
ATOM   3174 C C   . ARG A 1 587 ? -22.807 58.080  79.652  1.00 106.10 ?  568 ARG A C   1 
ATOM   3175 O O   . ARG A 1 587 ? -23.171 58.457  78.534  1.00 107.33 ?  568 ARG A O   1 
ATOM   3176 C CB  . ARG A 1 587 ? -22.840 55.525  79.534  1.00 105.98 ?  568 ARG A CB  1 
ATOM   3177 C CG  . ARG A 1 587 ? -23.240 55.198  78.093  1.00 109.38 ?  568 ARG A CG  1 
ATOM   3178 C CD  . ARG A 1 587 ? -23.318 53.656  77.923  1.00 115.74 ?  568 ARG A CD  1 
ATOM   3179 N NE  . ARG A 1 587 ? -23.643 53.201  76.576  1.00 116.77 ?  568 ARG A NE  1 
ATOM   3180 C CZ  . ARG A 1 587 ? -24.871 53.166  76.068  1.00 117.62 ?  568 ARG A CZ  1 
ATOM   3181 N NH1 . ARG A 1 587 ? -25.897 53.543  76.827  1.00 120.53 ?  568 ARG A NH1 1 
ATOM   3182 N NH2 . ARG A 1 587 ? -25.081 52.745  74.824  1.00 115.22 ?  568 ARG A NH2 1 
ATOM   3183 N N   . ASN A 1 588 ? -22.812 58.860  80.728  1.00 104.86 ?  569 ASN A N   1 
ATOM   3184 C CA  . ASN A 1 588 ? -23.460 60.194  80.710  1.00 104.86 ?  569 ASN A CA  1 
ATOM   3185 C C   . ASN A 1 588 ? -22.384 61.241  80.967  1.00 100.58 ?  569 ASN A C   1 
ATOM   3186 O O   . ASN A 1 588 ? -22.743 62.360  81.304  1.00 99.15  ?  569 ASN A O   1 
ATOM   3187 C CB  . ASN A 1 588 ? -24.427 60.337  81.870  1.00 110.38 ?  569 ASN A CB  1 
ATOM   3188 C CG  . ASN A 1 588 ? -23.889 59.580  83.053  1.00 115.45 ?  569 ASN A CG  1 
ATOM   3189 O OD1 . ASN A 1 588 ? -22.892 58.884  82.918  1.00 111.33 ?  569 ASN A OD1 1 
ATOM   3190 N ND2 . ASN A 1 588 ? -24.540 59.698  84.194  1.00 117.81 ?  569 ASN A ND2 1 
ATOM   3191 N N   . GLY A 1 589 ? -21.115 60.868  80.829  1.00 96.23  ?  570 GLY A N   1 
ATOM   3192 C CA  . GLY A 1 589 ? -19.996 61.799  81.047  1.00 91.48  ?  570 GLY A CA  1 
ATOM   3193 C C   . GLY A 1 589 ? -19.478 61.682  82.457  1.00 92.32  ?  570 GLY A C   1 
ATOM   3194 O O   . GLY A 1 589 ? -20.279 61.702  83.359  1.00 96.39  ?  570 GLY A O   1 
ATOM   3195 N N   . TYR A 1 590 ? -18.165 61.640  82.647  1.00 85.17  ?  571 TYR A N   1 
ATOM   3196 C CA  . TYR A 1 590 ? -17.606 61.483  84.011  1.00 80.19  ?  571 TYR A CA  1 
ATOM   3197 C C   . TYR A 1 590 ? -17.706 62.800  84.767  1.00 79.94  ?  571 TYR A C   1 
ATOM   3198 O O   . TYR A 1 590 ? -17.680 62.780  85.965  1.00 77.47  ?  571 TYR A O   1 
ATOM   3199 C CB  . TYR A 1 590 ? -16.147 61.061  83.913  1.00 71.58  ?  571 TYR A CB  1 
ATOM   3200 C CG  . TYR A 1 590 ? -15.629 60.154  84.993  1.00 72.71  ?  571 TYR A CG  1 
ATOM   3201 C CD1 . TYR A 1 590 ? -16.242 60.047  86.216  1.00 77.09  ?  571 TYR A CD1 1 
ATOM   3202 C CD2 . TYR A 1 590 ? -14.492 59.417  84.788  1.00 69.42  ?  571 TYR A CD2 1 
ATOM   3203 C CE1 . TYR A 1 590 ? -15.745 59.215  87.197  1.00 74.20  ?  571 TYR A CE1 1 
ATOM   3204 C CE2 . TYR A 1 590 ? -13.981 58.581  85.751  1.00 64.10  ?  571 TYR A CE2 1 
ATOM   3205 C CZ  . TYR A 1 590 ? -14.611 58.479  86.961  1.00 74.14  ?  571 TYR A CZ  1 
ATOM   3206 O OH  . TYR A 1 590 ? -14.094 57.656  87.903  1.00 69.72  ?  571 TYR A OH  1 
ATOM   3207 N N   . SER A 1 591 ? -17.779 63.912  84.054  1.00 79.39  ?  572 SER A N   1 
ATOM   3208 C CA  . SER A 1 591 ? -17.871 65.239  84.690  1.00 75.11  ?  572 SER A CA  1 
ATOM   3209 C C   . SER A 1 591 ? -19.023 65.258  85.687  1.00 79.49  ?  572 SER A C   1 
ATOM   3210 O O   . SER A 1 591 ? -18.966 66.017  86.615  1.00 80.95  ?  572 SER A O   1 
ATOM   3211 C CB  . SER A 1 591 ? -18.037 66.277  83.652  1.00 71.77  ?  572 SER A CB  1 
ATOM   3212 O OG  . SER A 1 591 ? -19.400 66.429  83.353  1.00 72.88  ?  572 SER A OG  1 
ATOM   3213 N N   . CYS A 1 592 ? -20.013 64.404  85.523  1.00 82.30  ?  573 CYS A N   1 
ATOM   3214 C CA  . CYS A 1 592 ? -21.148 64.434  86.442  1.00 84.62  ?  573 CYS A CA  1 
ATOM   3215 C C   . CYS A 1 592 ? -20.729 64.218  87.897  1.00 84.59  ?  573 CYS A C   1 
ATOM   3216 O O   . CYS A 1 592 ? -21.507 64.546  88.804  1.00 87.69  ?  573 CYS A O   1 
ATOM   3217 C CB  . CYS A 1 592 ? -22.191 63.377  86.052  1.00 92.73  ?  573 CYS A CB  1 
ATOM   3218 S SG  . CYS A 1 592 ? -21.659 61.652  86.350  1.00 106.14 ?  573 CYS A SG  1 
ATOM   3219 N N   . VAL A 1 593 ? -19.533 63.677  88.145  1.00 81.66  ?  574 VAL A N   1 
ATOM   3220 C CA  . VAL A 1 593 ? -19.072 63.394  89.508  1.00 81.27  ?  574 VAL A CA  1 
ATOM   3221 C C   . VAL A 1 593 ? -18.450 64.633  90.145  1.00 76.87  ?  574 VAL A C   1 
ATOM   3222 O O   . VAL A 1 593 ? -18.891 65.032  91.232  1.00 75.28  ?  574 VAL A O   1 
ATOM   3223 C CB  . VAL A 1 593 ? -18.108 62.194  89.538  1.00 79.77  ?  574 VAL A CB  1 
ATOM   3224 C CG1 . VAL A 1 593 ? -17.170 62.253  90.759  1.00 67.29  ?  574 VAL A CG1 1 
ATOM   3225 C CG2 . VAL A 1 593 ? -18.909 60.899  89.564  1.00 81.07  ?  574 VAL A CG2 1 
ATOM   3226 N N   . PRO A 1 594 ? -17.438 65.266  89.540  1.00 74.90  ?  575 PRO A N   1 
ATOM   3227 C CA  . PRO A 1 594 ? -16.991 66.561  90.070  1.00 73.39  ?  575 PRO A CA  1 
ATOM   3228 C C   . PRO A 1 594 ? -18.139 67.523  90.298  1.00 80.40  ?  575 PRO A C   1 
ATOM   3229 O O   . PRO A 1 594 ? -18.323 68.037  91.417  1.00 81.33  ?  575 PRO A O   1 
ATOM   3230 C CB  . PRO A 1 594 ? -16.039 67.064  88.975  1.00 72.43  ?  575 PRO A CB  1 
ATOM   3231 C CG  . PRO A 1 594 ? -15.499 65.856  88.386  1.00 72.51  ?  575 PRO A CG  1 
ATOM   3232 C CD  . PRO A 1 594 ? -16.634 64.872  88.370  1.00 76.26  ?  575 PRO A CD  1 
ATOM   3233 N N   . VAL A 1 595 ? -18.932 67.762  89.249  1.00 78.04  ?  576 VAL A N   1 
ATOM   3234 C CA  . VAL A 1 595 ? -20.033 68.715  89.331  1.00 77.23  ?  576 VAL A CA  1 
ATOM   3235 C C   . VAL A 1 595 ? -20.931 68.397  90.526  1.00 78.35  ?  576 VAL A C   1 
ATOM   3236 O O   . VAL A 1 595 ? -21.391 69.299  91.238  1.00 79.88  ?  576 VAL A O   1 
ATOM   3237 C CB  . VAL A 1 595 ? -20.802 68.725  87.998  1.00 68.19  ?  576 VAL A CB  1 
ATOM   3238 C CG1 . VAL A 1 595 ? -22.057 69.561  88.105  1.00 67.08  ?  576 VAL A CG1 1 
ATOM   3239 C CG2 . VAL A 1 595 ? -19.882 69.231  86.885  1.00 59.46  ?  576 VAL A CG2 1 
ATOM   3240 N N   . ALA A 1 596 ? -21.153 67.111  90.796  1.00 72.61  ?  577 ALA A N   1 
ATOM   3241 C CA  . ALA A 1 596 ? -21.955 66.742  91.956  1.00 76.58  ?  577 ALA A CA  1 
ATOM   3242 C C   . ALA A 1 596 ? -21.228 67.081  93.249  1.00 82.39  ?  577 ALA A C   1 
ATOM   3243 O O   . ALA A 1 596 ? -21.799 67.706  94.152  1.00 84.68  ?  577 ALA A O   1 
ATOM   3244 C CB  . ALA A 1 596 ? -22.294 65.254  91.913  1.00 76.79  ?  577 ALA A CB  1 
ATOM   3245 N N   . LEU A 1 597 ? -19.973 66.643  93.366  1.00 81.97  ?  578 LEU A N   1 
ATOM   3246 C CA  . LEU A 1 597 ? -19.184 66.936  94.557  1.00 77.17  ?  578 LEU A CA  1 
ATOM   3247 C C   . LEU A 1 597 ? -19.082 68.439  94.784  1.00 82.12  ?  578 LEU A C   1 
ATOM   3248 O O   . LEU A 1 597 ? -19.114 68.911  95.934  1.00 84.36  ?  578 LEU A O   1 
ATOM   3249 C CB  . LEU A 1 597 ? -17.796 66.323  94.408  1.00 72.24  ?  578 LEU A CB  1 
ATOM   3250 C CG  . LEU A 1 597 ? -17.651 64.809  94.494  1.00 66.60  ?  578 LEU A CG  1 
ATOM   3251 C CD1 . LEU A 1 597 ? -16.187 64.509  94.492  1.00 63.89  ?  578 LEU A CD1 1 
ATOM   3252 C CD2 . LEU A 1 597 ? -18.318 64.220  95.745  1.00 67.03  ?  578 LEU A CD2 1 
ATOM   3253 N N   . ALA A 1 598 ? -18.997 69.205  93.689  1.00 76.02  ?  579 ALA A N   1 
ATOM   3254 C CA  . ALA A 1 598 ? -18.860 70.654  93.767  1.00 75.52  ?  579 ALA A CA  1 
ATOM   3255 C C   . ALA A 1 598 ? -20.030 71.335  94.469  1.00 77.87  ?  579 ALA A C   1 
ATOM   3256 O O   . ALA A 1 598 ? -19.860 72.451  94.968  1.00 82.67  ?  579 ALA A O   1 
ATOM   3257 C CB  . ALA A 1 598 ? -18.695 71.244  92.360  1.00 74.61  ?  579 ALA A CB  1 
ATOM   3258 N N   . GLU A 1 599 ? -21.205 70.710  94.532  1.00 80.70  ?  580 GLU A N   1 
ATOM   3259 C CA  . GLU A 1 599 ? -22.391 71.450  94.943  1.00 82.73  ?  580 GLU A CA  1 
ATOM   3260 C C   . GLU A 1 599 ? -22.307 71.701  96.449  1.00 86.38  ?  580 GLU A C   1 
ATOM   3261 O O   . GLU A 1 599 ? -21.988 70.794  97.233  1.00 80.96  ?  580 GLU A O   1 
ATOM   3262 C CB  . GLU A 1 599 ? -23.671 70.690  94.561  1.00 87.28  ?  580 GLU A CB  1 
ATOM   3263 C CG  . GLU A 1 599 ? -24.021 69.487  95.423  1.00 94.31  ?  580 GLU A CG  1 
ATOM   3264 C CD  . GLU A 1 599 ? -25.052 69.866  96.481  1.00 103.85 ?  580 GLU A CD  1 
ATOM   3265 O OE1 . GLU A 1 599 ? -25.867 70.774  96.175  1.00 105.23 ?  580 GLU A OE1 1 
ATOM   3266 O OE2 . GLU A 1 599 ? -25.006 69.330  97.621  1.00 107.40 ?  580 GLU A OE2 1 
ATOM   3267 N N   . GLY A 1 600 ? -22.513 72.961  96.843  1.00 87.90  ?  581 GLY A N   1 
ATOM   3268 C CA  . GLY A 1 600 ? -22.443 73.355  98.233  1.00 81.03  ?  581 GLY A CA  1 
ATOM   3269 C C   . GLY A 1 600 ? -21.138 73.984  98.674  1.00 74.78  ?  581 GLY A C   1 
ATOM   3270 O O   . GLY A 1 600 ? -20.997 74.286  99.866  1.00 79.45  ?  581 GLY A O   1 
ATOM   3271 N N   . LEU A 1 601 ? -20.197 74.220  97.765  1.00 67.73  ?  582 LEU A N   1 
ATOM   3272 C CA  . LEU A 1 601 ? -18.837 74.578  98.134  1.00 65.23  ?  582 LEU A CA  1 
ATOM   3273 C C   . LEU A 1 601 ? -18.455 75.936  97.574  1.00 66.73  ?  582 LEU A C   1 
ATOM   3274 O O   . LEU A 1 601 ? -18.911 76.332  96.498  1.00 70.00  ?  582 LEU A O   1 
ATOM   3275 C CB  . LEU A 1 601 ? -17.815 73.561  97.622  1.00 67.16  ?  582 LEU A CB  1 
ATOM   3276 C CG  . LEU A 1 601 ? -17.957 72.086  97.940  1.00 76.67  ?  582 LEU A CG  1 
ATOM   3277 C CD1 . LEU A 1 601 ? -16.619 71.414  97.669  1.00 77.67  ?  582 LEU A CD1 1 
ATOM   3278 C CD2 . LEU A 1 601 ? -18.394 71.880  99.383  1.00 78.11  ?  582 LEU A CD2 1 
ATOM   3279 N N   . ASP A 1 602 ? -17.551 76.615  98.283  1.00 70.35  ?  583 ASP A N   1 
ATOM   3280 C CA  . ASP A 1 602 ? -17.126 77.970  97.919  1.00 74.60  ?  583 ASP A CA  1 
ATOM   3281 C C   . ASP A 1 602 ? -15.961 77.873  96.941  1.00 74.35  ?  583 ASP A C   1 
ATOM   3282 O O   . ASP A 1 602 ? -14.804 77.687  97.343  1.00 74.60  ?  583 ASP A O   1 
ATOM   3283 C CB  . ASP A 1 602 ? -16.738 78.776  99.153  1.00 72.20  ?  583 ASP A CB  1 
ATOM   3284 C CG  . ASP A 1 602 ? -16.452 80.237  98.823  1.00 91.47  ?  583 ASP A CG  1 
ATOM   3285 O OD1 . ASP A 1 602 ? -15.776 80.913  99.641  1.00 95.73  ?  583 ASP A OD1 1 
ATOM   3286 O OD2 . ASP A 1 602 ? -16.907 80.715  97.741  1.00 91.54  ?  583 ASP A OD2 1 
ATOM   3287 N N   . ILE A 1 603 ? -16.260 78.031  95.652  1.00 62.88  ?  584 ILE A N   1 
ATOM   3288 C CA  . ILE A 1 603 ? -15.303 77.745  94.593  1.00 66.79  ?  584 ILE A CA  1 
ATOM   3289 C C   . ILE A 1 603 ? -15.089 79.022  93.796  1.00 66.19  ?  584 ILE A C   1 
ATOM   3290 O O   . ILE A 1 603 ? -16.032 79.549  93.192  1.00 69.96  ?  584 ILE A O   1 
ATOM   3291 C CB  . ILE A 1 603 ? -15.797 76.600  93.684  1.00 73.12  ?  584 ILE A CB  1 
ATOM   3292 C CG1 . ILE A 1 603 ? -16.002 75.315  94.476  1.00 62.77  ?  584 ILE A CG1 1 
ATOM   3293 C CG2 . ILE A 1 603 ? -14.829 76.322  92.539  1.00 64.13  ?  584 ILE A CG2 1 
ATOM   3294 C CD1 . ILE A 1 603 ? -16.752 74.280  93.714  1.00 68.01  ?  584 ILE A CD1 1 
ATOM   3295 N N   . LYS A 1 604 ? -13.861 79.523  93.785  1.00 67.20  ?  585 LYS A N   1 
ATOM   3296 C CA  . LYS A 1 604 ? -13.522 80.705  92.986  1.00 71.01  ?  585 LYS A CA  1 
ATOM   3297 C C   . LYS A 1 604 ? -12.972 80.212  91.649  1.00 65.62  ?  585 LYS A C   1 
ATOM   3298 O O   . LYS A 1 604 ? -11.821 79.776  91.579  1.00 66.18  ?  585 LYS A O   1 
ATOM   3299 C CB  . LYS A 1 604 ? -12.505 81.591  93.711  1.00 66.09  ?  585 LYS A CB  1 
ATOM   3300 C CG  . LYS A 1 604 ? -12.916 82.061  95.123  1.00 71.13  ?  585 LYS A CG  1 
ATOM   3301 C CD  . LYS A 1 604 ? -14.254 82.815  95.152  1.00 77.49  ?  585 LYS A CD  1 
ATOM   3302 C CE  . LYS A 1 604 ? -14.773 82.973  96.586  1.00 84.88  ?  585 LYS A CE  1 
ATOM   3303 N NZ  . LYS A 1 604 ? -16.172 82.437  96.710  1.00 83.90  ?  585 LYS A NZ  1 
ATOM   3304 N N   . LEU A 1 605 ? -13.783 80.273  90.587  1.00 60.30  ?  586 LEU A N   1 
ATOM   3305 C CA  . LEU A 1 605 ? -13.273 79.851  89.281  1.00 63.96  ?  586 LEU A CA  1 
ATOM   3306 C C   . LEU A 1 605 ? -12.501 80.982  88.610  1.00 66.00  ?  586 LEU A C   1 
ATOM   3307 O O   . LEU A 1 605 ? -12.585 82.153  88.998  1.00 76.23  ?  586 LEU A O   1 
ATOM   3308 C CB  . LEU A 1 605 ? -14.394 79.369  88.346  1.00 62.75  ?  586 LEU A CB  1 
ATOM   3309 C CG  . LEU A 1 605 ? -15.162 78.112  88.800  1.00 64.96  ?  586 LEU A CG  1 
ATOM   3310 C CD1 . LEU A 1 605 ? -16.398 77.788  87.962  1.00 58.92  ?  586 LEU A CD1 1 
ATOM   3311 C CD2 . LEU A 1 605 ? -14.236 76.905  88.851  1.00 69.45  ?  586 LEU A CD2 1 
ATOM   3312 N N   . ASN A 1 606 ? -11.733 80.616  87.598  1.00 61.63  ?  587 ASN A N   1 
ATOM   3313 C CA  . ASN A 1 606 ? -10.930 81.580  86.844  1.00 67.58  ?  587 ASN A CA  1 
ATOM   3314 C C   . ASN A 1 606 ? -9.949  82.322  87.740  1.00 66.67  ?  587 ASN A C   1 
ATOM   3315 O O   . ASN A 1 606 ? -9.697  83.514  87.565  1.00 70.56  ?  587 ASN A O   1 
ATOM   3316 C CB  . ASN A 1 606 ? -11.815 82.567  86.095  1.00 71.20  ?  587 ASN A CB  1 
ATOM   3317 C CG  . ASN A 1 606 ? -12.670 81.885  85.088  1.00 75.33  ?  587 ASN A CG  1 
ATOM   3318 O OD1 . ASN A 1 606 ? -12.168 81.385  84.069  1.00 82.24  ?  587 ASN A OD1 1 
ATOM   3319 N ND2 . ASN A 1 606 ? -13.969 81.804  85.374  1.00 73.79  ?  587 ASN A ND2 1 
ATOM   3320 N N   . THR A 1 607 ? -9.512  81.630  88.769  1.00 67.28  ?  588 THR A N   1 
ATOM   3321 C CA  . THR A 1 607 ? -8.576  82.201  89.750  1.00 61.12  ?  588 THR A CA  1 
ATOM   3322 C C   . THR A 1 607 ? -7.295  81.390  89.696  1.00 56.69  ?  588 THR A C   1 
ATOM   3323 O O   . THR A 1 607 ? -7.301  80.302  90.161  1.00 51.45  ?  588 THR A O   1 
ATOM   3324 C CB  . THR A 1 607 ? -9.158  82.086  91.154  1.00 64.40  ?  588 THR A CB  1 
ATOM   3325 O OG1 . THR A 1 607 ? -10.578 82.113  91.113  1.00 56.53  ?  588 THR A OG1 1 
ATOM   3326 C CG2 . THR A 1 607 ? -8.702  83.206  92.050  1.00 68.52  ?  588 THR A CG2 1 
ATOM   3327 N N   . ALA A 1 608 ? -6.230  81.948  89.163  1.00 53.39  ?  589 ALA A N   1 
ATOM   3328 C CA  . ALA A 1 608 ? -4.996  81.162  89.064  1.00 48.22  ?  589 ALA A CA  1 
ATOM   3329 C C   . ALA A 1 608 ? -4.060  81.518  90.200  1.00 53.61  ?  589 ALA A C   1 
ATOM   3330 O O   . ALA A 1 608 ? -3.667  82.633  90.285  1.00 57.38  ?  589 ALA A O   1 
ATOM   3331 C CB  . ALA A 1 608 ? -4.342  81.458  87.762  1.00 51.24  ?  589 ALA A CB  1 
ATOM   3332 N N   . VAL A 1 609 ? -3.688  80.548  91.010  1.00 50.24  ?  590 VAL A N   1 
ATOM   3333 C CA  . VAL A 1 609 ? -2.760  80.833  92.122  1.00 50.04  ?  590 VAL A CA  1 
ATOM   3334 C C   . VAL A 1 609 ? -1.401  81.145  91.526  1.00 57.71  ?  590 VAL A C   1 
ATOM   3335 O O   . VAL A 1 609 ? -1.029  80.517  90.579  1.00 51.60  ?  590 VAL A O   1 
ATOM   3336 C CB  . VAL A 1 609 ? -2.731  79.648  93.079  1.00 52.69  ?  590 VAL A CB  1 
ATOM   3337 C CG1 . VAL A 1 609 ? -1.550  79.695  94.012  1.00 47.18  ?  590 VAL A CG1 1 
ATOM   3338 C CG2 . VAL A 1 609 ? -4.016  79.607  93.858  1.00 53.89  ?  590 VAL A CG2 1 
ATOM   3339 N N   . ARG A 1 610 ? -0.714  82.135  92.059  1.00 61.12  ?  591 ARG A N   1 
ATOM   3340 C CA  . ARG A 1 610 ? 0.585   82.466  91.465  1.00 59.27  ?  591 ARG A CA  1 
ATOM   3341 C C   . ARG A 1 610 ? 1.669   82.341  92.522  1.00 58.35  ?  591 ARG A C   1 
ATOM   3342 O O   . ARG A 1 610 ? 2.790   82.104  92.169  1.00 51.76  ?  591 ARG A O   1 
ATOM   3343 C CB  . ARG A 1 610 ? 0.470   83.878  90.903  1.00 71.99  ?  591 ARG A CB  1 
ATOM   3344 C CG  . ARG A 1 610 ? 1.395   84.147  89.735  1.00 71.73  ?  591 ARG A CG  1 
ATOM   3345 C CD  . ARG A 1 610 ? 0.723   85.122  88.817  1.00 87.11  ?  591 ARG A CD  1 
ATOM   3346 N NE  . ARG A 1 610 ? 0.045   84.391  87.776  1.00 113.74 ?  591 ARG A NE  1 
ATOM   3347 C CZ  . ARG A 1 610 ? -0.164  84.878  86.570  1.00 104.48 ?  591 ARG A CZ  1 
ATOM   3348 N NH1 . ARG A 1 610 ? -0.787  84.147  85.661  1.00 110.46 ?  591 ARG A NH1 1 
ATOM   3349 N NH2 . ARG A 1 610 ? 0.265   86.091  86.283  1.00 97.61  ?  591 ARG A NH2 1 
ATOM   3350 N N   . GLN A 1 611 ? 1.315   82.532  93.779  1.00 58.54  ?  592 GLN A N   1 
ATOM   3351 C CA  . GLN A 1 611 ? 2.325   82.431  94.845  1.00 52.88  ?  592 GLN A CA  1 
ATOM   3352 C C   . GLN A 1 611 ? 1.689   81.862  96.091  1.00 54.87  ?  592 GLN A C   1 
ATOM   3353 O O   . GLN A 1 611 ? 0.603   82.252  96.404  1.00 52.69  ?  592 GLN A O   1 
ATOM   3354 C CB  . GLN A 1 611 ? 2.772   83.826  95.233  1.00 59.21  ?  592 GLN A CB  1 
ATOM   3355 C CG  . GLN A 1 611 ? 4.249   84.073  95.034  1.00 65.74  ?  592 GLN A CG  1 
ATOM   3356 C CD  . GLN A 1 611 ? 4.716   85.133  95.980  1.00 67.31  ?  592 GLN A CD  1 
ATOM   3357 O OE1 . GLN A 1 611 ? 4.295   85.192  97.115  1.00 65.14  ?  592 GLN A OE1 1 
ATOM   3358 N NE2 . GLN A 1 611 ? 5.590   85.985  95.505  1.00 68.39  ?  592 GLN A NE2 1 
ATOM   3359 N N   . VAL A 1 612 ? 2.397   80.980  96.776  1.00 52.99  ?  593 VAL A N   1 
ATOM   3360 C CA  . VAL A 1 612 ? 1.876   80.446  98.057  1.00 56.78  ?  593 VAL A CA  1 
ATOM   3361 C C   . VAL A 1 612 ? 2.876   80.855  99.122  1.00 61.39  ?  593 VAL A C   1 
ATOM   3362 O O   . VAL A 1 612 ? 4.027   80.538  98.976  1.00 59.88  ?  593 VAL A O   1 
ATOM   3363 C CB  . VAL A 1 612 ? 1.682   78.929  98.036  1.00 53.85  ?  593 VAL A CB  1 
ATOM   3364 C CG1 . VAL A 1 612 ? 1.211   78.435  99.371  1.00 51.60  ?  593 VAL A CG1 1 
ATOM   3365 C CG2 . VAL A 1 612 ? 0.689   78.518  96.992  1.00 50.24  ?  593 VAL A CG2 1 
ATOM   3366 N N   . ARG A 1 613 ? 2.399   81.544  100.144 1.00 55.49  ?  594 ARG A N   1 
ATOM   3367 C CA  . ARG A 1 613 ? 3.243   82.024  101.243 1.00 51.37  ?  594 ARG A CA  1 
ATOM   3368 C C   . ARG A 1 613 ? 2.756   81.322  102.494 1.00 57.51  ?  594 ARG A C   1 
ATOM   3369 O O   . ARG A 1 613 ? 1.577   81.378  102.741 1.00 57.02  ?  594 ARG A O   1 
ATOM   3370 C CB  . ARG A 1 613 ? 2.985   83.515  101.415 1.00 64.47  ?  594 ARG A CB  1 
ATOM   3371 C CG  . ARG A 1 613 ? 3.777   84.412  100.481 1.00 71.34  ?  594 ARG A CG  1 
ATOM   3372 C CD  . ARG A 1 613 ? 3.624   85.872  100.819 1.00 66.03  ?  594 ARG A CD  1 
ATOM   3373 N NE  . ARG A 1 613 ? 4.824   86.384  101.428 1.00 67.84  ?  594 ARG A NE  1 
ATOM   3374 C CZ  . ARG A 1 613 ? 5.867   86.797  100.753 1.00 70.53  ?  594 ARG A CZ  1 
ATOM   3375 N NH1 . ARG A 1 613 ? 5.846   86.783  99.440  1.00 64.52  ?  594 ARG A NH1 1 
ATOM   3376 N NH2 . ARG A 1 613 ? 6.923   87.248  101.386 1.00 72.11  ?  594 ARG A NH2 1 
ATOM   3377 N N   . TYR A 1 614 ? 3.650   80.668  103.220 1.00 55.05  ?  595 TYR A N   1 
ATOM   3378 C CA  . TYR A 1 614 ? 3.279   79.968  104.452 1.00 63.19  ?  595 TYR A CA  1 
ATOM   3379 C C   . TYR A 1 614 ? 4.320   80.309  105.514 1.00 65.16  ?  595 TYR A C   1 
ATOM   3380 O O   . TYR A 1 614 ? 5.531   80.215  105.264 1.00 63.12  ?  595 TYR A O   1 
ATOM   3381 C CB  . TYR A 1 614 ? 3.171   78.427  104.251 1.00 62.69  ?  595 TYR A CB  1 
ATOM   3382 C CG  . TYR A 1 614 ? 4.423   77.809  103.638 1.00 58.37  ?  595 TYR A CG  1 
ATOM   3383 C CD1 . TYR A 1 614 ? 4.680   77.931  102.276 1.00 53.83  ?  595 TYR A CD1 1 
ATOM   3384 C CD2 . TYR A 1 614 ? 5.366   77.156  104.427 1.00 53.93  ?  595 TYR A CD2 1 
ATOM   3385 C CE1 . TYR A 1 614 ? 5.817   77.419  101.712 1.00 55.05  ?  595 TYR A CE1 1 
ATOM   3386 C CE2 . TYR A 1 614 ? 6.522   76.631  103.864 1.00 57.61  ?  595 TYR A CE2 1 
ATOM   3387 C CZ  . TYR A 1 614 ? 6.736   76.765  102.498 1.00 55.75  ?  595 TYR A CZ  1 
ATOM   3388 O OH  . TYR A 1 614 ? 7.876   76.263  101.904 1.00 53.35  ?  595 TYR A OH  1 
ATOM   3389 N N   . THR A 1 615 ? 3.843   80.723  106.688 1.00 64.08  ?  596 THR A N   1 
ATOM   3390 C CA  . THR A 1 615 ? 4.679   81.188  107.787 1.00 67.82  ?  596 THR A CA  1 
ATOM   3391 C C   . THR A 1 615 ? 4.195   80.520  109.057 1.00 67.93  ?  596 THR A C   1 
ATOM   3392 O O   . THR A 1 615 ? 3.092   79.965  109.098 1.00 68.29  ?  596 THR A O   1 
ATOM   3393 C CB  . THR A 1 615 ? 4.605   82.715  107.976 1.00 65.85  ?  596 THR A CB  1 
ATOM   3394 O OG1 . THR A 1 615 ? 3.251   83.090  108.298 1.00 66.34  ?  596 THR A OG1 1 
ATOM   3395 C CG2 . THR A 1 615 ? 5.104   83.469  106.733 1.00 58.08  ?  596 THR A CG2 1 
ATOM   3396 N N   . ALA A 1 616 ? 5.004   80.627  110.117 1.00 66.49  ?  597 ALA A N   1 
ATOM   3397 C CA  . ALA A 1 616 ? 4.672   79.942  111.362 1.00 64.51  ?  597 ALA A CA  1 
ATOM   3398 C C   . ALA A 1 616 ? 3.324   80.367  111.925 1.00 64.62  ?  597 ALA A C   1 
ATOM   3399 O O   . ALA A 1 616 ? 2.816   79.721  112.844 1.00 70.25  ?  597 ALA A O   1 
ATOM   3400 C CB  . ALA A 1 616 ? 5.765   80.169  112.400 1.00 62.44  ?  597 ALA A CB  1 
ATOM   3401 N N   . SER A 1 617 ? 2.713   81.406  111.381 1.00 72.75  ?  598 SER A N   1 
ATOM   3402 C CA  . SER A 1 617 ? 1.503   81.963  111.960 1.00 78.94  ?  598 SER A CA  1 
ATOM   3403 C C   . SER A 1 617 ? 0.327   81.937  111.000 1.00 74.73  ?  598 SER A C   1 
ATOM   3404 O O   . SER A 1 617 ? -0.767  82.393  111.363 1.00 76.93  ?  598 SER A O   1 
ATOM   3405 C CB  . SER A 1 617 ? 1.806   83.383  112.466 1.00 74.79  ?  598 SER A CB  1 
ATOM   3406 O OG  . SER A 1 617 ? 2.322   84.169  111.409 1.00 74.55  ?  598 SER A OG  1 
ATOM   3407 N N   . GLY A 1 618 ? 0.516   81.379  109.812 1.00 71.18  ?  599 GLY A N   1 
ATOM   3408 C CA  . GLY A 1 618 ? -0.549  81.216  108.846 1.00 71.70  ?  599 GLY A CA  1 
ATOM   3409 C C   . GLY A 1 618 ? -0.015  81.298  107.420 1.00 70.32  ?  599 GLY A C   1 
ATOM   3410 O O   . GLY A 1 618 ? 1.194   81.338  107.173 1.00 66.38  ?  599 GLY A O   1 
ATOM   3411 N N   . CYS A 1 619 ? -0.959  81.339  106.478 1.00 66.90  ?  600 CYS A N   1 
ATOM   3412 C CA  . CYS A 1 619 ? -0.653  81.259  105.058 1.00 66.86  ?  600 CYS A CA  1 
ATOM   3413 C C   . CYS A 1 619 ? -1.367  82.375  104.337 1.00 63.87  ?  600 CYS A C   1 
ATOM   3414 O O   . CYS A 1 619 ? -2.474  82.768  104.716 1.00 63.08  ?  600 CYS A O   1 
ATOM   3415 C CB  . CYS A 1 619 ? -1.119  79.946  104.443 1.00 65.84  ?  600 CYS A CB  1 
ATOM   3416 S SG  . CYS A 1 619 ? -0.415  78.522  105.225 1.00 72.60  ?  600 CYS A SG  1 
ATOM   3417 N N   . GLU A 1 620 ? -0.748  82.848  103.263 1.00 65.11  ?  601 GLU A N   1 
ATOM   3418 C CA  . GLU A 1 620 ? -1.474  83.662  102.302 1.00 71.99  ?  601 GLU A CA  1 
ATOM   3419 C C   . GLU A 1 620 ? -1.203  83.146  100.898 1.00 65.31  ?  601 GLU A C   1 
ATOM   3420 O O   . GLU A 1 620 ? -0.061  82.800  100.563 1.00 62.88  ?  601 GLU A O   1 
ATOM   3421 C CB  . GLU A 1 620 ? -1.132  85.169  102.429 1.00 78.85  ?  601 GLU A CB  1 
ATOM   3422 C CG  . GLU A 1 620 ? 0.350   85.523  102.494 1.00 83.06  ?  601 GLU A CG  1 
ATOM   3423 C CD  . GLU A 1 620 ? 0.589   87.041  102.653 1.00 95.92  ?  601 GLU A CD  1 
ATOM   3424 O OE1 . GLU A 1 620 ? 1.380   87.430  103.549 1.00 104.30 ?  601 GLU A OE1 1 
ATOM   3425 O OE2 . GLU A 1 620 ? -0.013  87.843  101.897 1.00 93.90  ?  601 GLU A OE2 1 
ATOM   3426 N N   . VAL A 1 621 ? -2.271  83.074  100.096 1.00 61.83  ?  602 VAL A N   1 
ATOM   3427 C CA  . VAL A 1 621 ? -2.214  82.621  98.706  1.00 66.51  ?  602 VAL A CA  1 
ATOM   3428 C C   . VAL A 1 621 ? -2.525  83.815  97.810  1.00 64.97  ?  602 VAL A C   1 
ATOM   3429 O O   . VAL A 1 621 ? -3.597  84.424  97.937  1.00 67.68  ?  602 VAL A O   1 
ATOM   3430 C CB  . VAL A 1 621 ? -3.209  81.475  98.432  1.00 67.88  ?  602 VAL A CB  1 
ATOM   3431 C CG1 . VAL A 1 621 ? -3.054  80.989  96.997  1.00 60.99  ?  602 VAL A CG1 1 
ATOM   3432 C CG2 . VAL A 1 621 ? -3.068  80.291  99.443  1.00 58.89  ?  602 VAL A CG2 1 
ATOM   3433 N N   . ILE A 1 622 ? -1.609  84.136  96.893  1.00 64.37  ?  603 ILE A N   1 
ATOM   3434 C CA  . ILE A 1 622 ? -1.805  85.201  95.907  1.00 63.96  ?  603 ILE A CA  1 
ATOM   3435 C C   . ILE A 1 622 ? -2.283  84.568  94.604  1.00 66.68  ?  603 ILE A C   1 
ATOM   3436 O O   . ILE A 1 622 ? -1.539  83.801  93.969  1.00 66.18  ?  603 ILE A O   1 
ATOM   3437 C CB  . ILE A 1 622 ? -0.510  85.987  95.644  1.00 64.43  ?  603 ILE A CB  1 
ATOM   3438 C CG1 . ILE A 1 622 ? 0.012   86.657  96.911  1.00 65.45  ?  603 ILE A CG1 1 
ATOM   3439 C CG2 . ILE A 1 622 ? -0.747  87.027  94.563  1.00 65.66  ?  603 ILE A CG2 1 
ATOM   3440 C CD1 . ILE A 1 622 ? 0.982   85.797  97.702  1.00 67.97  ?  603 ILE A CD1 1 
ATOM   3441 N N   . ALA A 1 623 ? -3.468  84.959  94.164  1.00 65.52  ?  604 ALA A N   1 
ATOM   3442 C CA  . ALA A 1 623 ? -4.052  84.454  92.909  1.00 65.26  ?  604 ALA A CA  1 
ATOM   3443 C C   . ALA A 1 623 ? -4.399  85.636  92.010  1.00 71.30  ?  604 ALA A C   1 
ATOM   3444 O O   . ALA A 1 623 ? -4.486  86.730  92.504  1.00 72.60  ?  604 ALA A O   1 
ATOM   3445 C CB  . ALA A 1 623 ? -5.275  83.658  93.237  1.00 57.45  ?  604 ALA A CB  1 
ATOM   3446 N N   . VAL A 1 624 ? -4.584  85.394  90.722  1.00 72.30  ?  605 VAL A N   1 
ATOM   3447 C CA  . VAL A 1 624 ? -4.965  86.450  89.743  1.00 69.54  ?  605 VAL A CA  1 
ATOM   3448 C C   . VAL A 1 624 ? -6.155  85.966  88.930  1.00 70.02  ?  605 VAL A C   1 
ATOM   3449 O O   . VAL A 1 624 ? -6.529  84.837  89.063  1.00 71.64  ?  605 VAL A O   1 
ATOM   3450 C CB  . VAL A 1 624 ? -3.824  86.808  88.790  1.00 70.34  ?  605 VAL A CB  1 
ATOM   3451 C CG1 . VAL A 1 624 ? -2.500  86.905  89.497  1.00 66.56  ?  605 VAL A CG1 1 
ATOM   3452 C CG2 . VAL A 1 624 ? -3.752  85.825  87.655  1.00 72.26  ?  605 VAL A CG2 1 
ATOM   3453 N N   . ASN A 1 625 ? -6.783  86.864  88.191  1.00 75.29  ?  606 ASN A N   1 
ATOM   3454 C CA  . ASN A 1 625 ? -7.931  86.497  87.332  1.00 83.23  ?  606 ASN A CA  1 
ATOM   3455 C C   . ASN A 1 625 ? -7.384  85.962  86.018  1.00 78.32  ?  606 ASN A C   1 
ATOM   3456 O O   . ASN A 1 625 ? -6.524  86.575  85.456  1.00 75.14  ?  606 ASN A O   1 
ATOM   3457 C CB  . ASN A 1 625 ? -8.800  87.706  87.041  1.00 88.06  ?  606 ASN A CB  1 
ATOM   3458 C CG  . ASN A 1 625 ? -10.151 87.322  86.505  1.00 88.64  ?  606 ASN A CG  1 
ATOM   3459 O OD1 . ASN A 1 625 ? -10.964 86.774  87.224  1.00 94.82  ?  606 ASN A OD1 1 
ATOM   3460 N ND2 . ASN A 1 625 ? -10.398 87.615  85.251  1.00 87.23  ?  606 ASN A ND2 1 
ATOM   3461 N N   . THR A 1 626 ? -7.855  84.814  85.579  1.00 78.67  ?  607 THR A N   1 
ATOM   3462 C CA  . THR A 1 626 ? -7.298  84.259  84.331  1.00 84.87  ?  607 THR A CA  1 
ATOM   3463 C C   . THR A 1 626 ? -7.641  85.155  83.153  1.00 86.95  ?  607 THR A C   1 
ATOM   3464 O O   . THR A 1 626 ? -6.819  85.272  82.260  1.00 86.91  ?  607 THR A O   1 
ATOM   3465 C CB  . THR A 1 626 ? -7.795  82.839  84.124  1.00 74.77  ?  607 THR A CB  1 
ATOM   3466 O OG1 . THR A 1 626 ? -9.187  82.887  84.396  1.00 73.84  ?  607 THR A OG1 1 
ATOM   3467 C CG2 . THR A 1 626 ? -7.150  81.889  85.095  1.00 67.58  ?  607 THR A CG2 1 
ATOM   3468 N N   . ARG A 1 627 ? -8.858  85.679  83.129  1.00 89.96  ?  608 ARG A N   1 
ATOM   3469 C CA  . ARG A 1 627 ? -9.302  86.542  82.014  1.00 86.58  ?  608 ARG A CA  1 
ATOM   3470 C C   . ARG A 1 627 ? -8.512  87.846  81.981  1.00 93.43  ?  608 ARG A C   1 
ATOM   3471 O O   . ARG A 1 627 ? -8.029  88.189  80.914  1.00 98.83  ?  608 ARG A O   1 
ATOM   3472 C CB  . ARG A 1 627 ? -10.805 86.725  82.153  1.00 82.84  ?  608 ARG A CB  1 
ATOM   3473 C CG  . ARG A 1 627 ? -11.516 85.390  82.272  1.00 82.52  ?  608 ARG A CG  1 
ATOM   3474 C CD  . ARG A 1 627 ? -12.860 85.558  82.916  1.00 83.35  ?  608 ARG A CD  1 
ATOM   3475 N NE  . ARG A 1 627 ? -12.725 85.634  84.351  1.00 92.49  ?  608 ARG A NE  1 
ATOM   3476 C CZ  . ARG A 1 627 ? -13.754 85.693  85.173  1.00 95.80  ?  608 ARG A CZ  1 
ATOM   3477 N NH1 . ARG A 1 627 ? -14.975 85.692  84.685  1.00 96.82  ?  608 ARG A NH1 1 
ATOM   3478 N NH2 . ARG A 1 627 ? -13.571 85.762  86.475  1.00 94.49  ?  608 ARG A NH2 1 
ATOM   3479 N N   . SER A 1 628 ? -8.342  88.511  83.119  1.00 93.78  ?  609 SER A N   1 
ATOM   3480 C CA  . SER A 1 628 ? -7.519  89.746  83.170  1.00 98.78  ?  609 SER A CA  1 
ATOM   3481 C C   . SER A 1 628 ? -6.464  89.538  84.244  1.00 94.61  ?  609 SER A C   1 
ATOM   3482 O O   . SER A 1 628 ? -6.825  89.632  85.388  1.00 87.48  ?  609 SER A O   1 
ATOM   3483 C CB  . SER A 1 628 ? -8.362  90.915  83.530  1.00 102.54 ?  609 SER A CB  1 
ATOM   3484 O OG  . SER A 1 628 ? -8.572  90.945  84.927  1.00 97.05  ?  609 SER A OG  1 
ATOM   3485 N N   . THR A 1 629 ? -5.198  89.398  83.883  1.00 94.51  ?  610 THR A N   1 
ATOM   3486 C CA  . THR A 1 629 ? -4.163  89.079  84.893  1.00 92.76  ?  610 THR A CA  1 
ATOM   3487 C C   . THR A 1 629 ? -3.923  90.215  85.885  1.00 93.59  ?  610 THR A C   1 
ATOM   3488 O O   . THR A 1 629 ? -3.434  89.935  86.954  1.00 88.17  ?  610 THR A O   1 
ATOM   3489 C CB  . THR A 1 629 ? -2.874  88.600  84.238  1.00 89.91  ?  610 THR A CB  1 
ATOM   3490 O OG1 . THR A 1 629 ? -2.095  89.771  84.038  1.00 102.49 ?  610 THR A OG1 1 
ATOM   3491 C CG2 . THR A 1 629 ? -3.118  87.928  82.913  1.00 81.58  ?  610 THR A CG2 1 
ATOM   3492 N N   . SER A 1 630 ? -4.198  91.455  85.522  1.00 101.59 ?  611 SER A N   1 
ATOM   3493 C CA  . SER A 1 630 ? -3.917  92.571  86.449  1.00 90.18  ?  611 SER A CA  1 
ATOM   3494 C C   . SER A 1 630 ? -4.711  92.427  87.744  1.00 85.14  ?  611 SER A C   1 
ATOM   3495 O O   . SER A 1 630 ? -4.149  92.715  88.760  1.00 83.28  ?  611 SER A O   1 
ATOM   3496 C CB  . SER A 1 630 ? -4.223  93.853  85.786  1.00 93.96  ?  611 SER A CB  1 
ATOM   3497 O OG  . SER A 1 630 ? -5.435  93.739  85.069  1.00 106.11 ?  611 SER A OG  1 
ATOM   3498 N N   . GLN A 1 631 ? -5.964  91.995  87.714  1.00 83.13  ?  612 GLN A N   1 
ATOM   3499 C CA  . GLN A 1 631 ? -6.739  91.888  88.976  1.00 78.24  ?  612 GLN A CA  1 
ATOM   3500 C C   . GLN A 1 631 ? -6.022  90.916  89.904  1.00 79.34  ?  612 GLN A C   1 
ATOM   3501 O O   . GLN A 1 631 ? -5.820  89.826  89.481  1.00 87.42  ?  612 GLN A O   1 
ATOM   3502 C CB  . GLN A 1 631 ? -8.081  91.270  88.629  1.00 87.86  ?  612 GLN A CB  1 
ATOM   3503 C CG  . GLN A 1 631 ? -9.198  91.623  89.584  1.00 95.52  ?  612 GLN A CG  1 
ATOM   3504 C CD  . GLN A 1 631 ? -10.464 91.735  88.783  1.00 103.66 ?  612 GLN A CD  1 
ATOM   3505 O OE1 . GLN A 1 631 ? -10.446 92.209  87.660  1.00 100.04 ?  612 GLN A OE1 1 
ATOM   3506 N NE2 . GLN A 1 631 ? -11.566 91.275  89.342  1.00 104.48 ?  612 GLN A NE2 1 
ATOM   3507 N N   . THR A 1 632 ? -5.791  91.261  91.166  1.00 78.91  ?  613 THR A N   1 
ATOM   3508 C CA  . THR A 1 632 ? -4.997  90.391  92.067  1.00 70.66  ?  613 THR A CA  1 
ATOM   3509 C C   . THR A 1 632 ? -5.773  90.073  93.338  1.00 67.38  ?  613 THR A C   1 
ATOM   3510 O O   . THR A 1 632 ? -6.419  90.952  93.845  1.00 71.93  ?  613 THR A O   1 
ATOM   3511 C CB  . THR A 1 632 ? -3.685  91.092  92.385  1.00 65.85  ?  613 THR A CB  1 
ATOM   3512 O OG1 . THR A 1 632 ? -2.924  91.013  91.191  1.00 69.38  ?  613 THR A OG1 1 
ATOM   3513 C CG2 . THR A 1 632 ? -2.913  90.431  93.492  1.00 64.91  ?  613 THR A CG2 1 
ATOM   3514 N N   . PHE A 1 633 ? -5.704  88.831  93.806  1.00 68.81  ?  614 PHE A N   1 
ATOM   3515 C CA  . PHE A 1 633 ? -6.449  88.400  94.980  1.00 69.75  ?  614 PHE A CA  1 
ATOM   3516 C C   . PHE A 1 633 ? -5.533  87.866  96.084  1.00 66.66  ?  614 PHE A C   1 
ATOM   3517 O O   . PHE A 1 633 ? -4.479  87.270  95.828  1.00 66.55  ?  614 PHE A O   1 
ATOM   3518 C CB  . PHE A 1 633 ? -7.476  87.348  94.595  1.00 69.06  ?  614 PHE A CB  1 
ATOM   3519 C CG  . PHE A 1 633 ? -8.578  87.877  93.736  1.00 77.77  ?  614 PHE A CG  1 
ATOM   3520 C CD1 . PHE A 1 633 ? -9.833  88.173  94.280  1.00 75.21  ?  614 PHE A CD1 1 
ATOM   3521 C CD2 . PHE A 1 633 ? -8.351  88.110  92.375  1.00 80.49  ?  614 PHE A CD2 1 
ATOM   3522 C CE1 . PHE A 1 633 ? -10.859 88.665  93.467  1.00 84.44  ?  614 PHE A CE1 1 
ATOM   3523 C CE2 . PHE A 1 633 ? -9.358  88.621  91.550  1.00 83.24  ?  614 PHE A CE2 1 
ATOM   3524 C CZ  . PHE A 1 633 ? -10.619 88.896  92.091  1.00 86.28  ?  614 PHE A CZ  1 
ATOM   3525 N N   . ILE A 1 634 ? -5.937  88.089  97.327  1.00 54.30  ?  615 ILE A N   1 
ATOM   3526 C CA  . ILE A 1 634 ? -5.160  87.650  98.473  1.00 59.49  ?  615 ILE A CA  1 
ATOM   3527 C C   . ILE A 1 634 ? -6.073  86.851  99.389  1.00 65.48  ?  615 ILE A C   1 
ATOM   3528 O O   . ILE A 1 634 ? -7.152  87.327  99.769  1.00 66.12  ?  615 ILE A O   1 
ATOM   3529 C CB  . ILE A 1 634 ? -4.543  88.829  99.243  1.00 65.16  ?  615 ILE A CB  1 
ATOM   3530 C CG1 . ILE A 1 634 ? -3.595  89.635  98.365  1.00 63.74  ?  615 ILE A CG1 1 
ATOM   3531 C CG2 . ILE A 1 634 ? -3.802  88.317  100.457 1.00 74.32  ?  615 ILE A CG2 1 
ATOM   3532 C CD1 . ILE A 1 634 ? -2.290  89.009  98.143  1.00 66.99  ?  615 ILE A CD1 1 
ATOM   3533 N N   . TYR A 1 635 ? -5.640  85.642  99.747  1.00 62.07  ?  616 TYR A N   1 
ATOM   3534 C CA  . TYR A 1 635 ? -6.394  84.786  100.651 1.00 66.83  ?  616 TYR A CA  1 
ATOM   3535 C C   . TYR A 1 635 ? -5.507  84.398  101.825 1.00 67.81  ?  616 TYR A C   1 
ATOM   3536 O O   . TYR A 1 635 ? -4.394  83.902  101.625 1.00 66.72  ?  616 TYR A O   1 
ATOM   3537 C CB  . TYR A 1 635 ? -6.915  83.557  99.914  1.00 67.52  ?  616 TYR A CB  1 
ATOM   3538 C CG  . TYR A 1 635 ? -7.872  83.871  98.764  1.00 65.45  ?  616 TYR A CG  1 
ATOM   3539 C CD1 . TYR A 1 635 ? -7.393  84.145  97.460  1.00 57.52  ?  616 TYR A CD1 1 
ATOM   3540 C CD2 . TYR A 1 635 ? -9.259  83.870  98.977  1.00 59.87  ?  616 TYR A CD2 1 
ATOM   3541 C CE1 . TYR A 1 635 ? -8.273  84.413  96.417  1.00 51.73  ?  616 TYR A CE1 1 
ATOM   3542 C CE2 . TYR A 1 635 ? -10.146 84.145  97.945  1.00 58.17  ?  616 TYR A CE2 1 
ATOM   3543 C CZ  . TYR A 1 635 ? -9.654  84.410  96.676  1.00 60.32  ?  616 TYR A CZ  1 
ATOM   3544 O OH  . TYR A 1 635 ? -10.578 84.677  95.688  1.00 72.24  ?  616 TYR A OH  1 
ATOM   3545 N N   . LYS A 1 636 ? -5.985  84.666  103.042 1.00 70.08  ?  617 LYS A N   1 
ATOM   3546 C CA  . LYS A 1 636 ? -5.268  84.368  104.277 1.00 66.88  ?  617 LYS A CA  1 
ATOM   3547 C C   . LYS A 1 636 ? -5.913  83.135  104.892 1.00 66.82  ?  617 LYS A C   1 
ATOM   3548 O O   . LYS A 1 636 ? -7.136  82.969  104.802 1.00 71.83  ?  617 LYS A O   1 
ATOM   3549 C CB  . LYS A 1 636 ? -5.327  85.541  105.268 1.00 71.06  ?  617 LYS A CB  1 
ATOM   3550 C CG  . LYS A 1 636 ? -5.046  86.932  104.688 1.00 81.00  ?  617 LYS A CG  1 
ATOM   3551 C CD  . LYS A 1 636 ? -3.582  87.406  104.803 1.00 88.61  ?  617 LYS A CD  1 
ATOM   3552 C CE  . LYS A 1 636 ? -3.398  88.809  104.139 1.00 89.91  ?  617 LYS A CE  1 
ATOM   3553 N NZ  . LYS A 1 636 ? -2.171  89.555  104.571 1.00 79.33  ?  617 LYS A NZ  1 
ATOM   3554 N N   . CYS A 1 637 ? -5.109  82.262  105.494 1.00 59.42  ?  618 CYS A N   1 
ATOM   3555 C CA  . CYS A 1 637 ? -5.689  81.011  105.962 1.00 62.90  ?  618 CYS A CA  1 
ATOM   3556 C C   . CYS A 1 637 ? -4.734  80.323  106.917 1.00 63.76  ?  618 CYS A C   1 
ATOM   3557 O O   . CYS A 1 637 ? -3.535  80.635  106.965 1.00 55.27  ?  618 CYS A O   1 
ATOM   3558 C CB  . CYS A 1 637 ? -6.007  80.091  104.789 1.00 68.88  ?  618 CYS A CB  1 
ATOM   3559 S SG  . CYS A 1 637 ? -4.502  79.748  103.820 1.00 71.19  ?  618 CYS A SG  1 
ATOM   3560 N N   . ASP A 1 638 ? -5.295  79.361  107.667 1.00 65.72  ?  619 ASP A N   1 
ATOM   3561 C CA  . ASP A 1 638 ? -4.478  78.547  108.568 1.00 69.18  ?  619 ASP A CA  1 
ATOM   3562 C C   . ASP A 1 638 ? -3.672  77.485  107.818 1.00 72.33  ?  619 ASP A C   1 
ATOM   3563 O O   . ASP A 1 638 ? -2.622  77.043  108.314 1.00 66.10  ?  619 ASP A O   1 
ATOM   3564 C CB  . ASP A 1 638 ? -5.354  77.876  109.623 1.00 65.81  ?  619 ASP A CB  1 
ATOM   3565 C CG  . ASP A 1 638 ? -6.174  78.871  110.429 1.00 77.42  ?  619 ASP A CG  1 
ATOM   3566 O OD1 . ASP A 1 638 ? -5.576  79.597  111.264 1.00 80.88  ?  619 ASP A OD1 1 
ATOM   3567 O OD2 . ASP A 1 638 ? -7.414  78.914  110.239 1.00 75.40  ?  619 ASP A OD2 1 
ATOM   3568 N N   . ALA A 1 639 ? -4.129  77.083  106.625 1.00 73.95  ?  620 ALA A N   1 
ATOM   3569 C CA  . ALA A 1 639 ? -3.568  75.943  105.907 1.00 68.80  ?  620 ALA A CA  1 
ATOM   3570 C C   . ALA A 1 639 ? -3.880  76.047  104.417 1.00 68.06  ?  620 ALA A C   1 
ATOM   3571 O O   . ALA A 1 639 ? -4.992  76.432  104.025 1.00 67.51  ?  620 ALA A O   1 
ATOM   3572 C CB  . ALA A 1 639 ? -4.121  74.624  106.452 1.00 60.21  ?  620 ALA A CB  1 
ATOM   3573 N N   . VAL A 1 640 ? -2.903  75.685  103.588 1.00 58.46  ?  621 VAL A N   1 
ATOM   3574 C CA  . VAL A 1 640 ? -3.130  75.518  102.159 1.00 62.35  ?  621 VAL A CA  1 
ATOM   3575 C C   . VAL A 1 640 ? -3.059  74.033  101.819 1.00 65.68  ?  621 VAL A C   1 
ATOM   3576 O O   . VAL A 1 640 ? -2.087  73.346  102.170 1.00 58.67  ?  621 VAL A O   1 
ATOM   3577 C CB  . VAL A 1 640 ? -2.116  76.298  101.314 1.00 61.84  ?  621 VAL A CB  1 
ATOM   3578 C CG1 . VAL A 1 640 ? -2.483  76.165  99.844  1.00 56.29  ?  621 VAL A CG1 1 
ATOM   3579 C CG2 . VAL A 1 640 ? -2.062  77.732  101.733 1.00 60.61  ?  621 VAL A CG2 1 
ATOM   3580 N N   . LEU A 1 641 ? -4.088  73.541  101.134 1.00 62.60  ?  622 LEU A N   1 
ATOM   3581 C CA  . LEU A 1 641 ? -4.082  72.209  100.551 1.00 56.66  ?  622 LEU A CA  1 
ATOM   3582 C C   . LEU A 1 641 ? -3.790  72.359  99.065  1.00 55.06  ?  622 LEU A C   1 
ATOM   3583 O O   . LEU A 1 641 ? -4.646  72.824  98.299  1.00 57.41  ?  622 LEU A O   1 
ATOM   3584 C CB  . LEU A 1 641 ? -5.413  71.506  100.786 1.00 58.21  ?  622 LEU A CB  1 
ATOM   3585 C CG  . LEU A 1 641 ? -5.523  70.143  100.110 1.00 58.92  ?  622 LEU A CG  1 
ATOM   3586 C CD1 . LEU A 1 641 ? -4.327  69.235  100.400 1.00 52.93  ?  622 LEU A CD1 1 
ATOM   3587 C CD2 . LEU A 1 641 ? -6.786  69.494  100.574 1.00 61.36  ?  622 LEU A CD2 1 
ATOM   3588 N N   . CYS A 1 642 ? -2.581  71.977  98.663  1.00 53.11  ?  623 CYS A N   1 
ATOM   3589 C CA  . CYS A 1 642 ? -2.176  72.021  97.263  1.00 55.16  ?  623 CYS A CA  1 
ATOM   3590 C C   . CYS A 1 642 ? -2.621  70.738  96.538  1.00 58.73  ?  623 CYS A C   1 
ATOM   3591 O O   . CYS A 1 642 ? -2.253  69.630  96.953  1.00 56.93  ?  623 CYS A O   1 
ATOM   3592 C CB  . CYS A 1 642 ? -0.661  72.185  97.200  1.00 48.95  ?  623 CYS A CB  1 
ATOM   3593 S SG  . CYS A 1 642 ? -0.076  72.220  95.501  1.00 62.98  ?  623 CYS A SG  1 
ATOM   3594 N N   . THR A 1 643 ? -3.418  70.866  95.459  1.00 55.52  ?  624 THR A N   1 
ATOM   3595 C CA  . THR A 1 643 ? -3.647  69.718  94.579  1.00 54.07  ?  624 THR A CA  1 
ATOM   3596 C C   . THR A 1 643 ? -3.229  70.062  93.148  1.00 53.46  ?  624 THR A C   1 
ATOM   3597 O O   . THR A 1 643 ? -3.810  69.599  92.170  1.00 59.70  ?  624 THR A O   1 
ATOM   3598 C CB  . THR A 1 643 ? -5.098  69.213  94.644  1.00 54.79  ?  624 THR A CB  1 
ATOM   3599 O OG1 . THR A 1 643 ? -5.964  69.879  93.711  1.00 53.48  ?  624 THR A OG1 1 
ATOM   3600 C CG2 . THR A 1 643 ? -5.641  69.478  96.019  1.00 51.77  ?  624 THR A CG2 1 
ATOM   3601 N N   . LEU A 1 644 ? -2.224  70.896  93.017  1.00 56.12  ?  625 LEU A N   1 
ATOM   3602 C CA  . LEU A 1 644 ? -1.678  71.215  91.712  1.00 55.31  ?  625 LEU A CA  1 
ATOM   3603 C C   . LEU A 1 644 ? -1.194  69.940  91.018  1.00 51.80  ?  625 LEU A C   1 
ATOM   3604 O O   . LEU A 1 644 ? -0.471  69.149  91.627  1.00 52.13  ?  625 LEU A O   1 
ATOM   3605 C CB  . LEU A 1 644 ? -0.526  72.211  91.881  1.00 51.40  ?  625 LEU A CB  1 
ATOM   3606 C CG  . LEU A 1 644 ? -0.995  73.600  92.312  1.00 56.53  ?  625 LEU A CG  1 
ATOM   3607 C CD1 . LEU A 1 644 ? 0.178   74.478  92.827  1.00 55.72  ?  625 LEU A CD1 1 
ATOM   3608 C CD2 . LEU A 1 644 ? -1.790  74.309  91.180  1.00 48.47  ?  625 LEU A CD2 1 
ATOM   3609 N N   . PRO A 1 645 ? -1.568  69.706  89.764  1.00 53.56  ?  626 PRO A N   1 
ATOM   3610 C CA  . PRO A 1 645 ? -0.971  68.596  89.002  1.00 54.99  ?  626 PRO A CA  1 
ATOM   3611 C C   . PRO A 1 645 ? 0.551   68.561  89.074  1.00 55.72  ?  626 PRO A C   1 
ATOM   3612 O O   . PRO A 1 645 ? 1.221   69.596  89.155  1.00 54.79  ?  626 PRO A O   1 
ATOM   3613 C CB  . PRO A 1 645 ? -1.461  68.849  87.567  1.00 45.38  ?  626 PRO A CB  1 
ATOM   3614 C CG  . PRO A 1 645 ? -2.789  69.506  87.777  1.00 50.26  ?  626 PRO A CG  1 
ATOM   3615 C CD  . PRO A 1 645 ? -2.601  70.407  88.989  1.00 52.33  ?  626 PRO A CD  1 
ATOM   3616 N N   . LEU A 1 646 ? 1.093   67.334  89.053  1.00 54.88  ?  627 LEU A N   1 
ATOM   3617 C CA  . LEU A 1 646 ? 2.541   67.157  89.105  1.00 52.84  ?  627 LEU A CA  1 
ATOM   3618 C C   . LEU A 1 646 ? 3.246   67.836  87.935  1.00 55.16  ?  627 LEU A C   1 
ATOM   3619 O O   . LEU A 1 646 ? 4.395   68.280  88.070  1.00 54.99  ?  627 LEU A O   1 
ATOM   3620 C CB  . LEU A 1 646 ? 2.874   65.682  89.105  1.00 53.15  ?  627 LEU A CB  1 
ATOM   3621 C CG  . LEU A 1 646 ? 4.355   65.368  88.920  1.00 55.81  ?  627 LEU A CG  1 
ATOM   3622 C CD1 . LEU A 1 646 ? 5.173   65.831  90.113  1.00 53.08  ?  627 LEU A CD1 1 
ATOM   3623 C CD2 . LEU A 1 646 ? 4.535   63.873  88.684  1.00 58.89  ?  627 LEU A CD2 1 
ATOM   3624 N N   . GLY A 1 647 ? 2.586   67.915  86.776  1.00 53.68  ?  628 GLY A N   1 
ATOM   3625 C CA  . GLY A 1 647 ? 3.172   68.628  85.654  1.00 52.19  ?  628 GLY A CA  1 
ATOM   3626 C C   . GLY A 1 647 ? 3.255   70.113  85.898  1.00 58.20  ?  628 GLY A C   1 
ATOM   3627 O O   . GLY A 1 647 ? 4.194   70.773  85.433  1.00 59.12  ?  628 GLY A O   1 
ATOM   3628 N N   . VAL A 1 648 ? 2.279   70.659  86.628  1.00 56.90  ?  629 VAL A N   1 
ATOM   3629 C CA  . VAL A 1 648 ? 2.349   72.053  87.034  1.00 54.39  ?  629 VAL A CA  1 
ATOM   3630 C C   . VAL A 1 648 ? 3.494   72.251  88.022  1.00 54.96  ?  629 VAL A C   1 
ATOM   3631 O O   . VAL A 1 648 ? 4.386   73.069  87.795  1.00 59.90  ?  629 VAL A O   1 
ATOM   3632 C CB  . VAL A 1 648 ? 0.996   72.496  87.615  1.00 53.64  ?  629 VAL A CB  1 
ATOM   3633 C CG1 . VAL A 1 648 ? 1.164   73.794  88.408  1.00 51.06  ?  629 VAL A CG1 1 
ATOM   3634 C CG2 . VAL A 1 648 ? -0.088  72.597  86.491  1.00 43.34  ?  629 VAL A CG2 1 
ATOM   3635 N N   . LEU A 1 649 ? 3.508   71.471  89.114  1.00 55.79  ?  630 LEU A N   1 
ATOM   3636 C CA  . LEU A 1 649 ? 4.569   71.530  90.128  1.00 52.30  ?  630 LEU A CA  1 
ATOM   3637 C C   . LEU A 1 649 ? 5.965   71.380  89.541  1.00 56.73  ?  630 LEU A C   1 
ATOM   3638 O O   . LEU A 1 649 ? 6.945   71.730  90.217  1.00 50.96  ?  630 LEU A O   1 
ATOM   3639 C CB  . LEU A 1 649 ? 4.397   70.408  91.172  1.00 54.21  ?  630 LEU A CB  1 
ATOM   3640 C CG  . LEU A 1 649 ? 3.221   70.447  92.148  1.00 57.65  ?  630 LEU A CG  1 
ATOM   3641 C CD1 . LEU A 1 649 ? 3.226   69.217  93.072  1.00 51.08  ?  630 LEU A CD1 1 
ATOM   3642 C CD2 . LEU A 1 649 ? 3.251   71.741  92.958  1.00 50.67  ?  630 LEU A CD2 1 
ATOM   3643 N N   . LYS A 1 650 ? 6.078   70.806  88.325  1.00 58.45  ?  631 LYS A N   1 
ATOM   3644 C CA  . LYS A 1 650 ? 7.348   70.470  87.688  1.00 54.01  ?  631 LYS A CA  1 
ATOM   3645 C C   . LYS A 1 650 ? 7.887   71.595  86.841  1.00 60.12  ?  631 LYS A C   1 
ATOM   3646 O O   . LYS A 1 650 ? 9.054   71.536  86.426  1.00 61.68  ?  631 LYS A O   1 
ATOM   3647 C CB  . LYS A 1 650 ? 7.194   69.271  86.767  1.00 53.44  ?  631 LYS A CB  1 
ATOM   3648 C CG  . LYS A 1 650 ? 7.486   67.932  87.356  1.00 59.44  ?  631 LYS A CG  1 
ATOM   3649 C CD  . LYS A 1 650 ? 7.100   66.833  86.360  1.00 50.40  ?  631 LYS A CD  1 
ATOM   3650 C CE  . LYS A 1 650 ? 7.743   65.505  86.737  1.00 55.61  ?  631 LYS A CE  1 
ATOM   3651 N NZ  . LYS A 1 650 ? 9.242   65.491  86.676  1.00 54.60  ?  631 LYS A NZ  1 
ATOM   3652 N N   . GLN A 1 651 ? 7.043   72.594  86.585  1.00 66.12  ?  632 GLN A N   1 
ATOM   3653 C CA  . GLN A 1 651 ? 7.211   73.552  85.499  1.00 62.42  ?  632 GLN A CA  1 
ATOM   3654 C C   . GLN A 1 651 ? 8.390   74.479  85.753  1.00 69.77  ?  632 GLN A C   1 
ATOM   3655 O O   . GLN A 1 651 ? 8.528   75.042  86.844  1.00 72.34  ?  632 GLN A O   1 
ATOM   3656 C CB  . GLN A 1 651 ? 5.895   74.310  85.353  1.00 54.66  ?  632 GLN A CB  1 
ATOM   3657 C CG  . GLN A 1 651 ? 5.804   75.471  84.449  1.00 71.38  ?  632 GLN A CG  1 
ATOM   3658 C CD  . GLN A 1 651 ? 4.347   75.847  84.156  1.00 77.89  ?  632 GLN A CD  1 
ATOM   3659 O OE1 . GLN A 1 651 ? 3.433   75.556  84.918  1.00 76.58  ?  632 GLN A OE1 1 
ATOM   3660 N NE2 . GLN A 1 651 ? 4.171   76.660  83.133  1.00 79.05  ?  632 GLN A NE2 1 
ATOM   3661 N N   . GLN A 1 652 ? 9.247   74.624  84.738  1.00 76.75  ?  633 GLN A N   1 
ATOM   3662 C CA  . GLN A 1 652 ? 10.430  75.492  84.796  1.00 80.84  ?  633 GLN A CA  1 
ATOM   3663 C C   . GLN A 1 652 ? 10.411  76.536  83.682  1.00 90.86  ?  633 GLN A C   1 
ATOM   3664 O O   . GLN A 1 652 ? 10.471  76.164  82.494  1.00 95.69  ?  633 GLN A O   1 
ATOM   3665 C CB  . GLN A 1 652 ? 11.717  74.674  84.685  1.00 83.02  ?  633 GLN A CB  1 
ATOM   3666 C CG  . GLN A 1 652 ? 12.119  73.947  85.964  1.00 77.93  ?  633 GLN A CG  1 
ATOM   3667 C CD  . GLN A 1 652 ? 11.798  74.770  87.184  1.00 84.20  ?  633 GLN A CD  1 
ATOM   3668 O OE1 . GLN A 1 652 ? 10.910  74.421  87.964  1.00 88.52  ?  633 GLN A OE1 1 
ATOM   3669 N NE2 . GLN A 1 652 ? 12.496  75.897  87.343  1.00 86.14  ?  633 GLN A NE2 1 
ATOM   3670 N N   . PRO A 1 653 ? 10.360  77.847  83.981  1.00 90.20  ?  634 PRO A N   1 
ATOM   3671 C CA  . PRO A 1 653 ? 10.221  78.498  85.295  1.00 81.98  ?  634 PRO A CA  1 
ATOM   3672 C C   . PRO A 1 653 ? 8.842   78.310  85.906  1.00 77.05  ?  634 PRO A C   1 
ATOM   3673 O O   . PRO A 1 653 ? 7.860   78.117  85.147  1.00 69.68  ?  634 PRO A O   1 
ATOM   3674 C CB  . PRO A 1 653 ? 10.487  80.003  84.995  1.00 77.62  ?  634 PRO A CB  1 
ATOM   3675 C CG  . PRO A 1 653 ? 11.271  79.987  83.722  1.00 89.90  ?  634 PRO A CG  1 
ATOM   3676 C CD  . PRO A 1 653 ? 10.756  78.814  82.939  1.00 92.94  ?  634 PRO A CD  1 
ATOM   3677 N N   . PRO A 1 654 ? 8.782   78.386  87.241  1.00 68.22  ?  635 PRO A N   1 
ATOM   3678 C CA  . PRO A 1 654 ? 7.541   78.103  87.975  1.00 66.14  ?  635 PRO A CA  1 
ATOM   3679 C C   . PRO A 1 654 ? 6.318   78.798  87.399  1.00 62.97  ?  635 PRO A C   1 
ATOM   3680 O O   . PRO A 1 654 ? 6.396   79.918  86.910  1.00 64.76  ?  635 PRO A O   1 
ATOM   3681 C CB  . PRO A 1 654 ? 7.853   78.623  89.382  1.00 58.00  ?  635 PRO A CB  1 
ATOM   3682 C CG  . PRO A 1 654 ? 9.315   78.358  89.521  1.00 67.81  ?  635 PRO A CG  1 
ATOM   3683 C CD  . PRO A 1 654 ? 9.935   78.504  88.143  1.00 70.01  ?  635 PRO A CD  1 
ATOM   3684 N N   . ALA A 1 655 ? 5.186   78.102  87.447  1.00 62.94  ?  636 ALA A N   1 
ATOM   3685 C CA  . ALA A 1 655 ? 3.890   78.753  87.375  1.00 57.62  ?  636 ALA A CA  1 
ATOM   3686 C C   . ALA A 1 655 ? 3.386   79.154  88.750  1.00 63.79  ?  636 ALA A C   1 
ATOM   3687 O O   . ALA A 1 655 ? 2.526   80.051  88.853  1.00 65.27  ?  636 ALA A O   1 
ATOM   3688 C CB  . ALA A 1 655 ? 2.846   77.838  86.736  1.00 56.33  ?  636 ALA A CB  1 
ATOM   3689 N N   . VAL A 1 656 ? 3.863   78.482  89.803  1.00 52.90  ?  637 VAL A N   1 
ATOM   3690 C CA  . VAL A 1 656 ? 3.494   78.820  91.168  1.00 55.59  ?  637 VAL A CA  1 
ATOM   3691 C C   . VAL A 1 656 ? 4.758   78.879  92.000  1.00 61.25  ?  637 VAL A C   1 
ATOM   3692 O O   . VAL A 1 656 ? 5.541   77.919  92.035  1.00 59.58  ?  637 VAL A O   1 
ATOM   3693 C CB  . VAL A 1 656 ? 2.491   77.841  91.808  1.00 50.20  ?  637 VAL A CB  1 
ATOM   3694 C CG1 . VAL A 1 656 ? 2.229   78.273  93.267  1.00 48.53  ?  637 VAL A CG1 1 
ATOM   3695 C CG2 . VAL A 1 656 ? 1.206   77.841  91.068  1.00 43.60  ?  637 VAL A CG2 1 
ATOM   3696 N N   . GLN A 1 657 ? 4.945   80.000  92.681  1.00 62.33  ?  638 GLN A N   1 
ATOM   3697 C CA  . GLN A 1 657 ? 6.125   80.212  93.487  1.00 57.28  ?  638 GLN A CA  1 
ATOM   3698 C C   . GLN A 1 657 ? 5.797   79.950  94.956  1.00 63.58  ?  638 GLN A C   1 
ATOM   3699 O O   . GLN A 1 657 ? 4.794   80.466  95.490  1.00 58.68  ?  638 GLN A O   1 
ATOM   3700 C CB  . GLN A 1 657 ? 6.646   81.619  93.264  1.00 56.18  ?  638 GLN A CB  1 
ATOM   3701 C CG  . GLN A 1 657 ? 7.854   81.939  94.083  1.00 69.59  ?  638 GLN A CG  1 
ATOM   3702 C CD  . GLN A 1 657 ? 8.236   83.399  94.044  1.00 76.59  ?  638 GLN A CD  1 
ATOM   3703 O OE1 . GLN A 1 657 ? 7.509   84.272  93.500  1.00 84.24  ?  638 GLN A OE1 1 
ATOM   3704 N NE2 . GLN A 1 657 ? 9.388   83.686  94.627  1.00 75.44  ?  638 GLN A NE2 1 
ATOM   3705 N N   . PHE A 1 658 ? 6.634   79.136  95.609  1.00 57.66  ?  639 PHE A N   1 
ATOM   3706 C CA  . PHE A 1 658 ? 6.451   78.879  97.029  1.00 58.39  ?  639 PHE A CA  1 
ATOM   3707 C C   . PHE A 1 658 ? 7.388   79.772  97.850  1.00 57.16  ?  639 PHE A C   1 
ATOM   3708 O O   . PHE A 1 658 ? 8.560   79.994  97.488  1.00 52.22  ?  639 PHE A O   1 
ATOM   3709 C CB  . PHE A 1 658 ? 6.648   77.385  97.326  1.00 61.94  ?  639 PHE A CB  1 
ATOM   3710 C CG  . PHE A 1 658 ? 5.500   76.503  96.821  1.00 53.95  ?  639 PHE A CG  1 
ATOM   3711 C CD1 . PHE A 1 658 ? 4.399   76.231  97.628  1.00 55.27  ?  639 PHE A CD1 1 
ATOM   3712 C CD2 . PHE A 1 658 ? 5.516   75.978  95.539  1.00 52.89  ?  639 PHE A CD2 1 
ATOM   3713 C CE1 . PHE A 1 658 ? 3.338   75.441  97.172  1.00 50.21  ?  639 PHE A CE1 1 
ATOM   3714 C CE2 . PHE A 1 658 ? 4.459   75.190  95.071  1.00 52.70  ?  639 PHE A CE2 1 
ATOM   3715 C CZ  . PHE A 1 658 ? 3.364   74.930  95.890  1.00 47.76  ?  639 PHE A CZ  1 
ATOM   3716 N N   . VAL A 1 659 ? 6.831   80.347  98.914  1.00 52.71  ?  640 VAL A N   1 
ATOM   3717 C CA  . VAL A 1 659 ? 7.552   81.290  99.767  1.00 55.01  ?  640 VAL A CA  1 
ATOM   3718 C C   . VAL A 1 659 ? 7.338   80.836  101.206 1.00 56.72  ?  640 VAL A C   1 
ATOM   3719 O O   . VAL A 1 659 ? 6.225   80.980  101.749 1.00 58.59  ?  640 VAL A O   1 
ATOM   3720 C CB  . VAL A 1 659 ? 7.085   82.749  99.540  1.00 63.92  ?  640 VAL A CB  1 
ATOM   3721 C CG1 . VAL A 1 659 ? 7.554   83.675  100.649 1.00 56.86  ?  640 VAL A CG1 1 
ATOM   3722 C CG2 . VAL A 1 659 ? 7.583   83.309  98.193  1.00 59.47  ?  640 VAL A CG2 1 
ATOM   3723 N N   . PRO A 1 660 ? 8.360   80.244  101.858 1.00 56.15  ?  641 PRO A N   1 
ATOM   3724 C CA  . PRO A 1 660 ? 9.687   79.947  101.288 1.00 49.50  ?  641 PRO A CA  1 
ATOM   3725 C C   . PRO A 1 660 ? 9.662   78.740  100.353 1.00 57.59  ?  641 PRO A C   1 
ATOM   3726 O O   . PRO A 1 660 ? 8.680   77.952  100.340 1.00 53.10  ?  641 PRO A O   1 
ATOM   3727 C CB  . PRO A 1 660 ? 10.537  79.662  102.524 1.00 48.22  ?  641 PRO A CB  1 
ATOM   3728 C CG  . PRO A 1 660 ? 9.548   79.180  103.566 1.00 45.79  ?  641 PRO A CG  1 
ATOM   3729 C CD  . PRO A 1 660 ? 8.224   79.790  103.263 1.00 52.90  ?  641 PRO A CD  1 
ATOM   3730 N N   . PRO A 1 661 ? 10.720  78.579  99.561  1.00 59.41  ?  642 PRO A N   1 
ATOM   3731 C CA  . PRO A 1 661 ? 10.712  77.508  98.551  1.00 55.72  ?  642 PRO A CA  1 
ATOM   3732 C C   . PRO A 1 661 ? 10.539  76.148  99.207  1.00 60.64  ?  642 PRO A C   1 
ATOM   3733 O O   . PRO A 1 661 ? 10.853  75.946  100.393 1.00 57.39  ?  642 PRO A O   1 
ATOM   3734 C CB  . PRO A 1 661 ? 12.087  77.626  97.882  1.00 51.08  ?  642 PRO A CB  1 
ATOM   3735 C CG  . PRO A 1 661 ? 12.525  79.027  98.176  1.00 51.84  ?  642 PRO A CG  1 
ATOM   3736 C CD  . PRO A 1 661 ? 12.009  79.284  99.585  1.00 51.23  ?  642 PRO A CD  1 
ATOM   3737 N N   . LEU A 1 662 ? 10.026  75.220  98.420  1.00 61.79  ?  643 LEU A N   1 
ATOM   3738 C CA  . LEU A 1 662 ? 9.861   73.859  98.893  1.00 55.32  ?  643 LEU A CA  1 
ATOM   3739 C C   . LEU A 1 662 ? 11.232  73.271  99.221  1.00 50.95  ?  643 LEU A C   1 
ATOM   3740 O O   . LEU A 1 662 ? 12.182  73.456  98.446  1.00 52.37  ?  643 LEU A O   1 
ATOM   3741 C CB  . LEU A 1 662 ? 9.121   73.047  97.826  1.00 51.17  ?  643 LEU A CB  1 
ATOM   3742 C CG  . LEU A 1 662 ? 7.698   73.626  97.732  1.00 51.89  ?  643 LEU A CG  1 
ATOM   3743 C CD1 . LEU A 1 662 ? 6.801   72.917  96.757  1.00 46.16  ?  643 LEU A CD1 1 
ATOM   3744 C CD2 . LEU A 1 662 ? 7.060   73.592  99.100  1.00 56.29  ?  643 LEU A CD2 1 
ATOM   3745 N N   . PRO A 1 663 ? 11.393  72.607  100.367 1.00 53.76  ?  644 PRO A N   1 
ATOM   3746 C CA  . PRO A 1 663 ? 12.690  71.971  100.674 1.00 52.79  ?  644 PRO A CA  1 
ATOM   3747 C C   . PRO A 1 663 ? 13.156  71.052  99.551  1.00 58.52  ?  644 PRO A C   1 
ATOM   3748 O O   . PRO A 1 663 ? 12.327  70.547  98.763  1.00 56.05  ?  644 PRO A O   1 
ATOM   3749 C CB  . PRO A 1 663 ? 12.413  71.176  101.959 1.00 42.84  ?  644 PRO A CB  1 
ATOM   3750 C CG  . PRO A 1 663 ? 10.922  71.033  102.017 1.00 46.50  ?  644 PRO A CG  1 
ATOM   3751 C CD  . PRO A 1 663 ? 10.352  72.267  101.353 1.00 52.76  ?  644 PRO A CD  1 
ATOM   3752 N N   . GLU A 1 664 ? 14.481  70.843  99.476  1.00 59.41  ?  645 GLU A N   1 
ATOM   3753 C CA  . GLU A 1 664 ? 15.045  69.988  98.434  1.00 58.49  ?  645 GLU A CA  1 
ATOM   3754 C C   . GLU A 1 664 ? 14.403  68.590  98.427  1.00 62.65  ?  645 GLU A C   1 
ATOM   3755 O O   . GLU A 1 664 ? 14.186  67.996  97.355  1.00 62.82  ?  645 GLU A O   1 
ATOM   3756 C CB  . GLU A 1 664 ? 16.569  69.892  98.625  1.00 61.14  ?  645 GLU A CB  1 
ATOM   3757 C CG  . GLU A 1 664 ? 17.371  69.427  97.394  1.00 80.08  ?  645 GLU A CG  1 
ATOM   3758 C CD  . GLU A 1 664 ? 17.390  67.928  97.162  1.00 96.09  ?  645 GLU A CD  1 
ATOM   3759 O OE1 . GLU A 1 664 ? 17.124  67.145  98.110  1.00 103.71 ?  645 GLU A OE1 1 
ATOM   3760 O OE2 . GLU A 1 664 ? 17.606  67.525  95.980  1.00 104.67 ?  645 GLU A OE2 1 
ATOM   3761 N N   . TRP A 1 665 ? 14.082  68.044  99.602  1.00 58.47  ?  646 TRP A N   1 
ATOM   3762 C CA  . TRP A 1 665 ? 13.567  66.687  99.596  1.00 52.70  ?  646 TRP A CA  1 
ATOM   3763 C C   . TRP A 1 665 ? 12.222  66.597  98.888  1.00 54.11  ?  646 TRP A C   1 
ATOM   3764 O O   . TRP A 1 665 ? 11.858  65.531  98.386  1.00 65.01  ?  646 TRP A O   1 
ATOM   3765 C CB  . TRP A 1 665 ? 13.453  66.130  101.009 1.00 48.51  ?  646 TRP A CB  1 
ATOM   3766 C CG  . TRP A 1 665 ? 12.539  66.833  101.902 1.00 47.71  ?  646 TRP A CG  1 
ATOM   3767 C CD1 . TRP A 1 665 ? 12.888  67.733  102.857 1.00 50.52  ?  646 TRP A CD1 1 
ATOM   3768 C CD2 . TRP A 1 665 ? 11.107  66.689  101.986 1.00 47.32  ?  646 TRP A CD2 1 
ATOM   3769 N NE1 . TRP A 1 665 ? 11.766  68.173  103.533 1.00 45.67  ?  646 TRP A NE1 1 
ATOM   3770 C CE2 . TRP A 1 665 ? 10.661  67.561  103.009 1.00 44.21  ?  646 TRP A CE2 1 
ATOM   3771 C CE3 . TRP A 1 665 ? 10.160  65.923  101.293 1.00 50.26  ?  646 TRP A CE3 1 
ATOM   3772 C CZ2 . TRP A 1 665 ? 9.313   67.689  103.360 1.00 44.34  ?  646 TRP A CZ2 1 
ATOM   3773 C CZ3 . TRP A 1 665 ? 8.802   66.062  101.639 1.00 51.54  ?  646 TRP A CZ3 1 
ATOM   3774 C CH2 . TRP A 1 665 ? 8.400   66.938  102.666 1.00 49.63  ?  646 TRP A CH2 1 
ATOM   3775 N N   . LYS A 1 666 ? 11.466  67.682  98.839  1.00 55.53  ?  647 LYS A N   1 
ATOM   3776 C CA  . LYS A 1 666 ? 10.237  67.687  98.057  1.00 52.73  ?  647 LYS A CA  1 
ATOM   3777 C C   . LYS A 1 666 ? 10.497  68.020  96.586  1.00 56.53  ?  647 LYS A C   1 
ATOM   3778 O O   . LYS A 1 666 ? 9.925   67.382  95.693  1.00 60.80  ?  647 LYS A O   1 
ATOM   3779 C CB  . LYS A 1 666 ? 9.253   68.675  98.668  1.00 49.14  ?  647 LYS A CB  1 
ATOM   3780 C CG  . LYS A 1 666 ? 8.016   68.954  97.850  1.00 50.96  ?  647 LYS A CG  1 
ATOM   3781 C CD  . LYS A 1 666 ? 6.983   67.887  98.067  1.00 54.93  ?  647 LYS A CD  1 
ATOM   3782 C CE  . LYS A 1 666 ? 6.440   67.917  99.488  1.00 55.31  ?  647 LYS A CE  1 
ATOM   3783 N NZ  . LYS A 1 666 ? 5.136   67.178  99.623  1.00 57.10  ?  647 LYS A NZ  1 
ATOM   3784 N N   . THR A 1 667 ? 11.357  68.996  96.297  1.00 53.12  ?  648 THR A N   1 
ATOM   3785 C CA  . THR A 1 667 ? 11.573  69.344  94.895  1.00 59.87  ?  648 THR A CA  1 
ATOM   3786 C C   . THR A 1 667 ? 12.263  68.214  94.140  1.00 63.14  ?  648 THR A C   1 
ATOM   3787 O O   . THR A 1 667 ? 12.041  68.059  92.933  1.00 58.78  ?  648 THR A O   1 
ATOM   3788 C CB  . THR A 1 667 ? 12.407  70.623  94.749  1.00 58.90  ?  648 THR A CB  1 
ATOM   3789 O OG1 . THR A 1 667 ? 13.747  70.358  95.188  1.00 66.67  ?  648 THR A OG1 1 
ATOM   3790 C CG2 . THR A 1 667 ? 11.821  71.765  95.574  1.00 45.55  ?  648 THR A CG2 1 
ATOM   3791 N N   . SER A 1 668 ? 13.097  67.417  94.830  1.00 67.46  ?  649 SER A N   1 
ATOM   3792 C CA  . SER A 1 668 ? 13.743  66.279  94.174  1.00 61.06  ?  649 SER A CA  1 
ATOM   3793 C C   . SER A 1 668 ? 12.758  65.167  93.886  1.00 57.69  ?  649 SER A C   1 
ATOM   3794 O O   . SER A 1 668 ? 12.813  64.561  92.809  1.00 57.90  ?  649 SER A O   1 
ATOM   3795 C CB  . SER A 1 668 ? 14.900  65.749  95.000  1.00 57.98  ?  649 SER A CB  1 
ATOM   3796 O OG  . SER A 1 668 ? 16.033  66.562  94.786  1.00 72.07  ?  649 SER A OG  1 
ATOM   3797 N N   . ALA A 1 669 ? 11.847  64.888  94.819  1.00 54.93  ?  650 ALA A N   1 
ATOM   3798 C CA  . ALA A 1 669 ? 10.733  64.012  94.475  1.00 56.04  ?  650 ALA A CA  1 
ATOM   3799 C C   . ALA A 1 669 ? 9.980   64.543  93.251  1.00 59.60  ?  650 ALA A C   1 
ATOM   3800 O O   . ALA A 1 669 ? 9.600   63.773  92.368  1.00 60.94  ?  650 ALA A O   1 
ATOM   3801 C CB  . ALA A 1 669 ? 9.798   63.846  95.672  1.00 52.36  ?  650 ALA A CB  1 
ATOM   3802 N N   . VAL A 1 670 ? 9.792   65.856  93.151  1.00 59.07  ?  651 VAL A N   1 
ATOM   3803 C CA  . VAL A 1 670 ? 9.041   66.382  92.016  1.00 58.52  ?  651 VAL A CA  1 
ATOM   3804 C C   . VAL A 1 670 ? 9.801   66.159  90.710  1.00 59.28  ?  651 VAL A C   1 
ATOM   3805 O O   . VAL A 1 670 ? 9.203   65.819  89.675  1.00 56.96  ?  651 VAL A O   1 
ATOM   3806 C CB  . VAL A 1 670 ? 8.704   67.867  92.235  1.00 57.00  ?  651 VAL A CB  1 
ATOM   3807 C CG1 . VAL A 1 670 ? 8.060   68.446  90.991  1.00 54.98  ?  651 VAL A CG1 1 
ATOM   3808 C CG2 . VAL A 1 670 ? 7.767   68.036  93.429  1.00 54.03  ?  651 VAL A CG2 1 
ATOM   3809 N N   . GLN A 1 671 ? 11.125  66.341  90.729  1.00 57.59  ?  652 GLN A N   1 
ATOM   3810 C CA  . GLN A 1 671 ? 11.912  66.098  89.525  1.00 56.53  ?  652 GLN A CA  1 
ATOM   3811 C C   . GLN A 1 671 ? 11.978  64.609  89.187  1.00 61.38  ?  652 GLN A C   1 
ATOM   3812 O O   . GLN A 1 671 ? 11.871  64.233  88.017  1.00 61.83  ?  652 GLN A O   1 
ATOM   3813 C CB  . GLN A 1 671 ? 13.314  66.653  89.698  1.00 59.44  ?  652 GLN A CB  1 
ATOM   3814 C CG  . GLN A 1 671 ? 13.425  68.160  89.497  1.00 74.99  ?  652 GLN A CG  1 
ATOM   3815 C CD  . GLN A 1 671 ? 14.689  68.739  90.159  1.00 92.69  ?  652 GLN A CD  1 
ATOM   3816 O OE1 . GLN A 1 671 ? 15.762  68.110  90.159  1.00 93.93  ?  652 GLN A OE1 1 
ATOM   3817 N NE2 . GLN A 1 671 ? 14.557  69.929  90.748  1.00 90.29  ?  652 GLN A NE2 1 
ATOM   3818 N N   . ARG A 1 672 ? 12.160  63.745  90.191  1.00 62.75  ?  653 ARG A N   1 
ATOM   3819 C CA  . ARG A 1 672 ? 12.367  62.330  89.906  1.00 53.33  ?  653 ARG A CA  1 
ATOM   3820 C C   . ARG A 1 672 ? 11.127  61.715  89.292  1.00 58.08  ?  653 ARG A C   1 
ATOM   3821 O O   . ARG A 1 672 ? 11.221  60.936  88.327  1.00 62.34  ?  653 ARG A O   1 
ATOM   3822 C CB  . ARG A 1 672 ? 12.759  61.569  91.176  1.00 53.85  ?  653 ARG A CB  1 
ATOM   3823 C CG  . ARG A 1 672 ? 14.198  61.807  91.587  1.00 60.38  ?  653 ARG A CG  1 
ATOM   3824 C CD  . ARG A 1 672 ? 14.662  60.849  92.643  1.00 55.30  ?  653 ARG A CD  1 
ATOM   3825 N NE  . ARG A 1 672 ? 13.745  60.787  93.765  1.00 50.81  ?  653 ARG A NE  1 
ATOM   3826 C CZ  . ARG A 1 672 ? 13.838  61.576  94.821  1.00 54.20  ?  653 ARG A CZ  1 
ATOM   3827 N NH1 . ARG A 1 672 ? 14.818  62.478  94.863  1.00 61.64  ?  653 ARG A NH1 1 
ATOM   3828 N NH2 . ARG A 1 672 ? 12.957  61.479  95.819  1.00 54.62  ?  653 ARG A NH2 1 
ATOM   3829 N N   . MET A 1 673 ? 9.955   62.053  89.829  1.00 51.44  ?  654 MET A N   1 
ATOM   3830 C CA  . MET A 1 673 ? 8.735   61.440  89.334  1.00 54.07  ?  654 MET A CA  1 
ATOM   3831 C C   . MET A 1 673 ? 8.527   61.750  87.854  1.00 60.56  ?  654 MET A C   1 
ATOM   3832 O O   . MET A 1 673 ? 9.091   62.695  87.285  1.00 61.75  ?  654 MET A O   1 
ATOM   3833 C CB  . MET A 1 673 ? 7.523   61.902  90.125  1.00 50.65  ?  654 MET A CB  1 
ATOM   3834 C CG  . MET A 1 673 ? 7.584   61.577  91.620  1.00 65.85  ?  654 MET A CG  1 
ATOM   3835 S SD  . MET A 1 673 ? 5.924   61.630  92.382  1.00 80.48  ?  654 MET A SD  1 
ATOM   3836 C CE  . MET A 1 673 ? 4.980   60.939  90.990  1.00 68.40  ?  654 MET A CE  1 
ATOM   3837 N N   . GLY A 1 674 ? 7.713   60.923  87.225  1.00 58.93  ?  655 GLY A N   1 
ATOM   3838 C CA  . GLY A 1 674 ? 7.388   61.073  85.820  1.00 54.72  ?  655 GLY A CA  1 
ATOM   3839 C C   . GLY A 1 674 ? 5.989   61.587  85.693  1.00 52.13  ?  655 GLY A C   1 
ATOM   3840 O O   . GLY A 1 674 ? 5.090   61.192  86.455  1.00 52.67  ?  655 GLY A O   1 
ATOM   3841 N N   . PHE A 1 675 ? 5.779   62.487  84.733  1.00 53.25  ?  656 PHE A N   1 
ATOM   3842 C CA  . PHE A 1 675 ? 4.444   62.987  84.451  1.00 57.12  ?  656 PHE A CA  1 
ATOM   3843 C C   . PHE A 1 675 ? 4.207   62.778  82.966  1.00 53.13  ?  656 PHE A C   1 
ATOM   3844 O O   . PHE A 1 675 ? 4.761   63.499  82.127  1.00 51.21  ?  656 PHE A O   1 
ATOM   3845 C CB  . PHE A 1 675 ? 4.251   64.459  84.874  1.00 47.75  ?  656 PHE A CB  1 
ATOM   3846 C CG  . PHE A 1 675 ? 2.805   64.841  85.007  1.00 46.61  ?  656 PHE A CG  1 
ATOM   3847 C CD1 . PHE A 1 675 ? 1.998   64.204  85.933  1.00 50.45  ?  656 PHE A CD1 1 
ATOM   3848 C CD2 . PHE A 1 675 ? 2.225   65.771  84.154  1.00 46.30  ?  656 PHE A CD2 1 
ATOM   3849 C CE1 . PHE A 1 675 ? 0.629   64.520  86.029  1.00 54.57  ?  656 PHE A CE1 1 
ATOM   3850 C CE2 . PHE A 1 675 ? 0.886   66.096  84.255  1.00 46.04  ?  656 PHE A CE2 1 
ATOM   3851 C CZ  . PHE A 1 675 ? 0.080   65.472  85.191  1.00 45.48  ?  656 PHE A CZ  1 
ATOM   3852 N N   . GLY A 1 676 ? 3.414   61.775  82.642  1.00 55.43  ?  657 GLY A N   1 
ATOM   3853 C CA  . GLY A 1 676 ? 3.211   61.377  81.264  1.00 59.29  ?  657 GLY A CA  1 
ATOM   3854 C C   . GLY A 1 676 ? 2.148   62.164  80.529  1.00 53.65  ?  657 GLY A C   1 
ATOM   3855 O O   . GLY A 1 676 ? 1.711   63.241  80.946  1.00 48.89  ?  657 GLY A O   1 
ATOM   3856 N N   . ASN A 1 677 ? 1.705   61.580  79.426  1.00 55.44  ?  658 ASN A N   1 
ATOM   3857 C CA  . ASN A 1 677 ? 0.897   62.281  78.433  1.00 59.87  ?  658 ASN A CA  1 
ATOM   3858 C C   . ASN A 1 677 ? 0.210   61.247  77.559  1.00 56.65  ?  658 ASN A C   1 
ATOM   3859 O O   . ASN A 1 677 ? 0.895   60.385  77.007  1.00 65.38  ?  658 ASN A O   1 
ATOM   3860 C CB  . ASN A 1 677 ? 1.780   63.176  77.581  1.00 55.19  ?  658 ASN A CB  1 
ATOM   3861 C CG  . ASN A 1 677 ? 0.987   63.999  76.607  1.00 61.40  ?  658 ASN A CG  1 
ATOM   3862 O OD1 . ASN A 1 677 ? -0.257  64.054  76.683  1.00 58.45  ?  658 ASN A OD1 1 
ATOM   3863 N ND2 . ASN A 1 677 ? 1.694   64.639  75.660  1.00 59.16  ?  658 ASN A ND2 1 
ATOM   3864 N N   . LEU A 1 678 ? -1.119  61.312  77.442  1.00 54.74  ?  659 LEU A N   1 
ATOM   3865 C CA  . LEU A 1 678 ? -1.809  60.639  76.354  1.00 61.21  ?  659 LEU A CA  1 
ATOM   3866 C C   . LEU A 1 678 ? -2.924  61.559  75.891  1.00 61.56  ?  659 LEU A C   1 
ATOM   3867 O O   . LEU A 1 678 ? -3.451  62.338  76.684  1.00 66.81  ?  659 LEU A O   1 
ATOM   3868 C CB  . LEU A 1 678 ? -2.395  59.279  76.759  1.00 66.70  ?  659 LEU A CB  1 
ATOM   3869 C CG  . LEU A 1 678 ? -3.669  59.129  77.570  1.00 66.68  ?  659 LEU A CG  1 
ATOM   3870 C CD1 . LEU A 1 678 ? -4.799  59.030  76.565  1.00 73.75  ?  659 LEU A CD1 1 
ATOM   3871 C CD2 . LEU A 1 678 ? -3.678  57.896  78.420  1.00 70.66  ?  659 LEU A CD2 1 
ATOM   3872 N N   . ASN A 1 679 ? -3.303  61.476  74.615  1.00 59.83  ?  660 ASN A N   1 
ATOM   3873 C CA  . ASN A 1 679 ? -4.350  62.367  74.127  1.00 65.69  ?  660 ASN A CA  1 
ATOM   3874 C C   . ASN A 1 679 ? -5.487  61.597  73.473  1.00 64.18  ?  660 ASN A C   1 
ATOM   3875 O O   . ASN A 1 679 ? -5.374  60.400  73.214  1.00 68.26  ?  660 ASN A O   1 
ATOM   3876 C CB  . ASN A 1 679 ? -3.776  63.411  73.189  1.00 61.71  ?  660 ASN A CB  1 
ATOM   3877 C CG  . ASN A 1 679 ? -3.121  64.542  73.959  1.00 70.15  ?  660 ASN A CG  1 
ATOM   3878 O OD1 . ASN A 1 679 ? -3.783  65.228  74.761  1.00 64.56  ?  660 ASN A OD1 1 
ATOM   3879 N ND2 . ASN A 1 679 ? -1.812  64.720  73.759  1.00 70.32  ?  660 ASN A ND2 1 
ATOM   3880 N N   . LYS A 1 680 ? -6.611  62.291  73.260  1.00 59.57  ?  661 LYS A N   1 
ATOM   3881 C CA  . LYS A 1 680 ? -7.811  61.696  72.684  1.00 63.24  ?  661 LYS A CA  1 
ATOM   3882 C C   . LYS A 1 680 ? -8.315  62.517  71.506  1.00 67.83  ?  661 LYS A C   1 
ATOM   3883 O O   . LYS A 1 680 ? -8.222  63.747  71.502  1.00 71.18  ?  661 LYS A O   1 
ATOM   3884 C CB  . LYS A 1 680 ? -8.948  61.567  73.697  1.00 59.39  ?  661 LYS A CB  1 
ATOM   3885 C CG  . LYS A 1 680 ? -8.661  60.610  74.789  1.00 63.49  ?  661 LYS A CG  1 
ATOM   3886 C CD  . LYS A 1 680 ? -9.836  60.432  75.729  1.00 61.05  ?  661 LYS A CD  1 
ATOM   3887 C CE  . LYS A 1 680 ? -9.292  60.075  77.097  1.00 61.98  ?  661 LYS A CE  1 
ATOM   3888 N NZ  . LYS A 1 680 ? -9.984  58.952  77.782  1.00 75.14  ?  661 LYS A NZ  1 
ATOM   3889 N N   . VAL A 1 681 ? -8.856  61.823  70.502  1.00 74.03  ?  662 VAL A N   1 
ATOM   3890 C CA  . VAL A 1 681 ? -9.565  62.447  69.388  1.00 75.67  ?  662 VAL A CA  1 
ATOM   3891 C C   . VAL A 1 681 ? -11.002 61.980  69.432  1.00 75.10  ?  662 VAL A C   1 
ATOM   3892 O O   . VAL A 1 681 ? -11.262 60.773  69.384  1.00 79.09  ?  662 VAL A O   1 
ATOM   3893 C CB  . VAL A 1 681 ? -8.964  62.094  68.028  1.00 66.41  ?  662 VAL A CB  1 
ATOM   3894 C CG1 . VAL A 1 681 ? -9.746  62.823  66.986  1.00 67.60  ?  662 VAL A CG1 1 
ATOM   3895 C CG2 . VAL A 1 681 ? -7.502  62.459  67.981  1.00 68.53  ?  662 VAL A CG2 1 
ATOM   3896 N N   . VAL A 1 682 ? -11.936 62.919  69.486  1.00 74.82  ?  663 VAL A N   1 
ATOM   3897 C CA  . VAL A 1 682 ? -13.342 62.577  69.633  1.00 80.71  ?  663 VAL A CA  1 
ATOM   3898 C C   . VAL A 1 682 ? -14.008 62.803  68.288  1.00 84.28  ?  663 VAL A C   1 
ATOM   3899 O O   . VAL A 1 682 ? -14.007 63.928  67.776  1.00 80.15  ?  663 VAL A O   1 
ATOM   3900 C CB  . VAL A 1 682 ? -14.020 63.414  70.719  1.00 85.06  ?  663 VAL A CB  1 
ATOM   3901 C CG1 . VAL A 1 682 ? -15.452 62.922  70.935  1.00 84.60  ?  663 VAL A CG1 1 
ATOM   3902 C CG2 . VAL A 1 682 ? -13.193 63.417  71.970  1.00 85.66  ?  663 VAL A CG2 1 
ATOM   3903 N N   . LEU A 1 683 ? -14.576 61.737  67.721  1.00 92.11  ?  664 LEU A N   1 
ATOM   3904 C CA  . LEU A 1 683 ? -15.198 61.750  66.401  1.00 85.80  ?  664 LEU A CA  1 
ATOM   3905 C C   . LEU A 1 683 ? -16.695 61.530  66.559  1.00 86.32  ?  664 LEU A C   1 
ATOM   3906 O O   . LEU A 1 683 ? -17.131 60.469  67.033  1.00 82.69  ?  664 LEU A O   1 
ATOM   3907 C CB  . LEU A 1 683 ? -14.570 60.683  65.508  1.00 81.85  ?  664 LEU A CB  1 
ATOM   3908 C CG  . LEU A 1 683 ? -13.081 60.988  65.333  1.00 79.12  ?  664 LEU A CG  1 
ATOM   3909 C CD1 . LEU A 1 683 ? -12.291 59.796  64.808  1.00 79.41  ?  664 LEU A CD1 1 
ATOM   3910 C CD2 . LEU A 1 683 ? -12.912 62.183  64.436  1.00 71.61  ?  664 LEU A CD2 1 
ATOM   3911 N N   . CYS A 1 684 ? -17.470 62.546  66.188  1.00 90.34  ?  665 CYS A N   1 
ATOM   3912 C CA  . CYS A 1 684 ? -18.925 62.512  66.277  1.00 96.95  ?  665 CYS A CA  1 
ATOM   3913 C C   . CYS A 1 684 ? -19.502 62.338  64.881  1.00 96.26  ?  665 CYS A C   1 
ATOM   3914 O O   . CYS A 1 684 ? -19.160 63.096  63.967  1.00 93.02  ?  665 CYS A O   1 
ATOM   3915 C CB  . CYS A 1 684 ? -19.464 63.791  66.911  1.00 99.91  ?  665 CYS A CB  1 
ATOM   3916 S SG  . CYS A 1 684 ? -18.661 64.182  68.460  1.00 97.22  ?  665 CYS A SG  1 
ATOM   3917 N N   . PHE A 1 685 ? -20.371 61.353  64.717  1.00 97.39  ?  666 PHE A N   1 
ATOM   3918 C CA  . PHE A 1 685 ? -20.806 60.973  63.395  1.00 100.96 ?  666 PHE A CA  1 
ATOM   3919 C C   . PHE A 1 685 ? -22.311 61.067  63.265  1.00 105.23 ?  666 PHE A C   1 
ATOM   3920 O O   . PHE A 1 685 ? -23.051 61.162  64.240  1.00 99.35  ?  666 PHE A O   1 
ATOM   3921 C CB  . PHE A 1 685 ? -20.344 59.561  63.052  1.00 96.65  ?  666 PHE A CB  1 
ATOM   3922 C CG  . PHE A 1 685 ? -18.893 59.474  62.836  1.00 88.88  ?  666 PHE A CG  1 
ATOM   3923 C CD1 . PHE A 1 685 ? -18.303 60.251  61.857  1.00 92.04  ?  666 PHE A CD1 1 
ATOM   3924 C CD2 . PHE A 1 685 ? -18.119 58.627  63.598  1.00 85.94  ?  666 PHE A CD2 1 
ATOM   3925 C CE1 . PHE A 1 685 ? -16.966 60.190  61.633  1.00 92.93  ?  666 PHE A CE1 1 
ATOM   3926 C CE2 . PHE A 1 685 ? -16.765 58.555  63.383  1.00 86.48  ?  666 PHE A CE2 1 
ATOM   3927 C CZ  . PHE A 1 685 ? -16.186 59.340  62.396  1.00 90.77  ?  666 PHE A CZ  1 
ATOM   3928 N N   . ASP A 1 686 ? -22.763 61.032  62.017  1.00 110.49 ?  667 ASP A N   1 
ATOM   3929 C CA  . ASP A 1 686 ? -24.188 60.890  61.749  1.00 110.71 ?  667 ASP A CA  1 
ATOM   3930 C C   . ASP A 1 686 ? -24.625 59.458  61.472  1.00 115.32 ?  667 ASP A C   1 
ATOM   3931 O O   . ASP A 1 686 ? -25.712 59.296  60.913  1.00 122.14 ?  667 ASP A O   1 
ATOM   3932 C CB  . ASP A 1 686 ? -24.624 61.795  60.587  1.00 111.86 ?  667 ASP A CB  1 
ATOM   3933 C CG  . ASP A 1 686 ? -23.915 61.441  59.286  1.00 123.79 ?  667 ASP A CG  1 
ATOM   3934 O OD1 . ASP A 1 686 ? -22.792 60.906  59.308  1.00 120.17 ?  667 ASP A OD1 1 
ATOM   3935 O OD2 . ASP A 1 686 ? -24.531 61.682  58.224  1.00 127.39 ?  667 ASP A OD2 1 
ATOM   3936 N N   . ARG A 1 687 ? -23.851 58.439  61.874  1.00 110.19 ?  668 ARG A N   1 
ATOM   3937 C CA  . ARG A 1 687 ? -24.361 57.068  61.896  1.00 101.85 ?  668 ARG A CA  1 
ATOM   3938 C C   . ARG A 1 687 ? -23.329 56.125  62.471  1.00 98.00  ?  668 ARG A C   1 
ATOM   3939 O O   . ARG A 1 687 ? -22.125 56.311  62.279  1.00 98.64  ?  668 ARG A O   1 
ATOM   3940 C CB  . ARG A 1 687 ? -24.785 56.567  60.491  1.00 111.27 ?  668 ARG A CB  1 
ATOM   3941 C CG  . ARG A 1 687 ? -23.808 56.840  59.345  1.00 112.41 ?  668 ARG A CG  1 
ATOM   3942 C CD  . ARG A 1 687 ? -24.493 56.461  58.021  1.00 122.77 ?  668 ARG A CD  1 
ATOM   3943 N NE  . ARG A 1 687 ? -23.761 56.905  56.833  1.00 130.03 ?  668 ARG A NE  1 
ATOM   3944 C CZ  . ARG A 1 687 ? -24.046 58.012  56.142  1.00 129.51 ?  668 ARG A CZ  1 
ATOM   3945 N NH1 . ARG A 1 687 ? -25.052 58.797  56.533  1.00 121.21 ?  668 ARG A NH1 1 
ATOM   3946 N NH2 . ARG A 1 687 ? -23.325 58.338  55.064  1.00 117.11 ?  668 ARG A NH2 1 
ATOM   3947 N N   . VAL A 1 688 ? -23.827 55.093  63.150  1.00 94.87  ?  669 VAL A N   1 
ATOM   3948 C CA  . VAL A 1 688 ? -22.979 53.965  63.494  1.00 93.54  ?  669 VAL A CA  1 
ATOM   3949 C C   . VAL A 1 688 ? -22.601 53.220  62.217  1.00 99.91  ?  669 VAL A C   1 
ATOM   3950 O O   . VAL A 1 688 ? -23.469 52.834  61.418  1.00 100.64 ?  669 VAL A O   1 
ATOM   3951 C CB  . VAL A 1 688 ? -23.690 53.043  64.488  1.00 85.99  ?  669 VAL A CB  1 
ATOM   3952 C CG1 . VAL A 1 688 ? -22.763 51.904  64.885  1.00 90.83  ?  669 VAL A CG1 1 
ATOM   3953 C CG2 . VAL A 1 688 ? -24.162 53.826  65.698  1.00 85.64  ?  669 VAL A CG2 1 
ATOM   3954 N N   . PHE A 1 689 ? -21.296 53.040  62.000  1.00 96.03  ?  670 PHE A N   1 
ATOM   3955 C CA  . PHE A 1 689 ? -20.801 52.281  60.859  1.00 92.63  ?  670 PHE A CA  1 
ATOM   3956 C C   . PHE A 1 689 ? -19.768 51.248  61.281  1.00 89.71  ?  670 PHE A C   1 
ATOM   3957 O O   . PHE A 1 689 ? -19.001 50.775  60.439  1.00 94.42  ?  670 PHE A O   1 
ATOM   3958 C CB  . PHE A 1 689 ? -20.205 53.206  59.801  1.00 91.64  ?  670 PHE A CB  1 
ATOM   3959 C CG  . PHE A 1 689 ? -19.025 53.988  60.281  1.00 97.36  ?  670 PHE A CG  1 
ATOM   3960 C CD1 . PHE A 1 689 ? -17.769 53.399  60.382  1.00 100.43 ?  670 PHE A CD1 1 
ATOM   3961 C CD2 . PHE A 1 689 ? -19.164 55.321  60.626  1.00 94.22  ?  670 PHE A CD2 1 
ATOM   3962 C CE1 . PHE A 1 689 ? -16.682 54.114  60.830  1.00 98.39  ?  670 PHE A CE1 1 
ATOM   3963 C CE2 . PHE A 1 689 ? -18.079 56.045  61.060  1.00 93.85  ?  670 PHE A CE2 1 
ATOM   3964 C CZ  . PHE A 1 689 ? -16.836 55.440  61.168  1.00 94.10  ?  670 PHE A CZ  1 
ATOM   3965 N N   . TRP A 1 690 ? -19.724 50.911  62.559  1.00 85.58  ?  671 TRP A N   1 
ATOM   3966 C CA  . TRP A 1 690 ? -18.774 49.972  63.136  1.00 89.32  ?  671 TRP A CA  1 
ATOM   3967 C C   . TRP A 1 690 ? -19.566 48.868  63.819  1.00 84.59  ?  671 TRP A C   1 
ATOM   3968 O O   . TRP A 1 690 ? -20.790 48.929  63.903  1.00 82.78  ?  671 TRP A O   1 
ATOM   3969 C CB  . TRP A 1 690 ? -17.841 50.684  64.130  1.00 97.98  ?  671 TRP A CB  1 
ATOM   3970 C CG  . TRP A 1 690 ? -18.581 51.626  65.094  1.00 90.61  ?  671 TRP A CG  1 
ATOM   3971 C CD1 . TRP A 1 690 ? -19.242 51.273  66.237  1.00 84.52  ?  671 TRP A CD1 1 
ATOM   3972 C CD2 . TRP A 1 690 ? -18.746 53.048  64.962  1.00 88.26  ?  671 TRP A CD2 1 
ATOM   3973 N NE1 . TRP A 1 690 ? -19.800 52.379  66.822  1.00 86.06  ?  671 TRP A NE1 1 
ATOM   3974 C CE2 . TRP A 1 690 ? -19.512 53.482  66.062  1.00 86.22  ?  671 TRP A CE2 1 
ATOM   3975 C CE3 . TRP A 1 690 ? -18.323 53.994  64.020  1.00 90.32  ?  671 TRP A CE3 1 
ATOM   3976 C CZ2 . TRP A 1 690 ? -19.862 54.820  66.250  1.00 85.39  ?  671 TRP A CZ2 1 
ATOM   3977 C CZ3 . TRP A 1 690 ? -18.669 55.325  64.211  1.00 86.68  ?  671 TRP A CZ3 1 
ATOM   3978 C CH2 . TRP A 1 690 ? -19.430 55.723  65.314  1.00 86.20  ?  671 TRP A CH2 1 
ATOM   3979 N N   . ASP A 1 691 ? -18.865 47.875  64.329  1.00 85.01  ?  672 ASP A N   1 
ATOM   3980 C CA  . ASP A 1 691 ? -19.530 46.792  65.044  1.00 92.95  ?  672 ASP A CA  1 
ATOM   3981 C C   . ASP A 1 691 ? -20.113 47.300  66.360  1.00 99.38  ?  672 ASP A C   1 
ATOM   3982 O O   . ASP A 1 691 ? -19.349 47.547  67.306  1.00 100.24 ?  672 ASP A O   1 
ATOM   3983 C CB  . ASP A 1 691 ? -18.536 45.655  65.299  1.00 100.95 ?  672 ASP A CB  1 
ATOM   3984 C CG  . ASP A 1 691 ? -19.216 44.355  65.710  1.00 107.02 ?  672 ASP A CG  1 
ATOM   3985 O OD1 . ASP A 1 691 ? -20.397 44.413  66.122  1.00 104.72 ?  672 ASP A OD1 1 
ATOM   3986 O OD2 . ASP A 1 691 ? -18.559 43.281  65.642  1.00 108.59 ?  672 ASP A OD2 1 
ATOM   3987 N N   . PRO A 1 692 ? -21.436 47.454  66.481  1.00 97.22  ?  673 PRO A N   1 
ATOM   3988 C CA  . PRO A 1 692 ? -22.004 47.983  67.733  1.00 95.97  ?  673 PRO A CA  1 
ATOM   3989 C C   . PRO A 1 692 ? -21.804 47.081  68.944  1.00 96.35  ?  673 PRO A C   1 
ATOM   3990 O O   . PRO A 1 692 ? -21.840 47.574  70.077  1.00 100.01 ?  673 PRO A O   1 
ATOM   3991 C CB  . PRO A 1 692 ? -23.493 48.149  67.392  1.00 90.06  ?  673 PRO A CB  1 
ATOM   3992 C CG  . PRO A 1 692 ? -23.521 48.242  65.891  1.00 90.60  ?  673 PRO A CG  1 
ATOM   3993 C CD  . PRO A 1 692 ? -22.482 47.249  65.471  1.00 96.90  ?  673 PRO A CD  1 
ATOM   3994 N N   . SER A 1 693 ? -21.605 45.782  68.750  1.00 101.83 ?  674 SER A N   1 
ATOM   3995 C CA  . SER A 1 693 ? -21.369 44.848  69.845  1.00 109.65 ?  674 SER A CA  1 
ATOM   3996 C C   . SER A 1 693 ? -19.898 44.793  70.253  1.00 109.01 ?  674 SER A C   1 
ATOM   3997 O O   . SER A 1 693 ? -19.510 43.948  71.078  1.00 105.54 ?  674 SER A O   1 
ATOM   3998 C CB  . SER A 1 693 ? -21.873 43.453  69.454  1.00 112.65 ?  674 SER A CB  1 
ATOM   3999 O OG  . SER A 1 693 ? -21.314 43.044  68.214  1.00 105.09 ?  674 SER A OG  1 
ATOM   4000 N N   . VAL A 1 694 ? -19.088 45.679  69.682  1.00 103.68 ?  675 VAL A N   1 
ATOM   4001 C CA  . VAL A 1 694 ? -17.666 45.816  69.967  1.00 100.88 ?  675 VAL A CA  1 
ATOM   4002 C C   . VAL A 1 694 ? -17.433 47.198  70.555  1.00 98.12  ?  675 VAL A C   1 
ATOM   4003 O O   . VAL A 1 694 ? -17.758 48.215  69.922  1.00 99.40  ?  675 VAL A O   1 
ATOM   4004 C CB  . VAL A 1 694 ? -16.823 45.585  68.704  1.00 99.79  ?  675 VAL A CB  1 
ATOM   4005 C CG1 . VAL A 1 694 ? -15.420 46.111  68.877  1.00 95.15  ?  675 VAL A CG1 1 
ATOM   4006 C CG2 . VAL A 1 694 ? -16.739 44.087  68.467  1.00 101.98 ?  675 VAL A CG2 1 
ATOM   4007 N N   . ASN A 1 695 ? -16.872 47.236  71.768  1.00 93.14  ?  676 ASN A N   1 
ATOM   4008 C CA  . ASN A 1 695 ? -16.611 48.522  72.403  1.00 90.27  ?  676 ASN A CA  1 
ATOM   4009 C C   . ASN A 1 695 ? -15.319 49.154  71.913  1.00 90.88  ?  676 ASN A C   1 
ATOM   4010 O O   . ASN A 1 695 ? -15.240 50.383  71.801  1.00 94.41  ?  676 ASN A O   1 
ATOM   4011 C CB  . ASN A 1 695 ? -16.566 48.378  73.918  1.00 83.98  ?  676 ASN A CB  1 
ATOM   4012 C CG  . ASN A 1 695 ? -17.927 48.148  74.507  1.00 94.69  ?  676 ASN A CG  1 
ATOM   4013 O OD1 . ASN A 1 695 ? -18.121 47.251  75.335  1.00 96.61  ?  676 ASN A OD1 1 
ATOM   4014 N ND2 . ASN A 1 695 ? -18.898 48.945  74.066  1.00 92.41  ?  676 ASN A ND2 1 
ATOM   4015 N N   . LEU A 1 696 ? -14.310 48.350  71.595  1.00 88.37  ?  677 LEU A N   1 
ATOM   4016 C CA  . LEU A 1 696 ? -12.999 48.889  71.271  1.00 86.95  ?  677 LEU A CA  1 
ATOM   4017 C C   . LEU A 1 696 ? -12.340 48.052  70.187  1.00 82.64  ?  677 LEU A C   1 
ATOM   4018 O O   . LEU A 1 696 ? -12.562 46.847  70.106  1.00 92.57  ?  677 LEU A O   1 
ATOM   4019 C CB  . LEU A 1 696 ? -12.149 48.984  72.552  1.00 86.09  ?  677 LEU A CB  1 
ATOM   4020 C CG  . LEU A 1 696 ? -11.658 47.744  73.284  1.00 81.86  ?  677 LEU A CG  1 
ATOM   4021 C CD1 . LEU A 1 696 ? -10.584 48.132  74.278  1.00 75.98  ?  677 LEU A CD1 1 
ATOM   4022 C CD2 . LEU A 1 696 ? -12.805 47.064  74.008  1.00 92.90  ?  677 LEU A CD2 1 
ATOM   4023 N N   . PHE A 1 697 ? -11.556 48.697  69.324  1.00 80.30  ?  678 PHE A N   1 
ATOM   4024 C CA  . PHE A 1 697 ? -10.864 47.950  68.279  1.00 78.10  ?  678 PHE A CA  1 
ATOM   4025 C C   . PHE A 1 697 ? -9.569  48.648  67.879  1.00 75.97  ?  678 PHE A C   1 
ATOM   4026 O O   . PHE A 1 697 ? -9.483  49.878  67.852  1.00 74.44  ?  678 PHE A O   1 
ATOM   4027 C CB  . PHE A 1 697 ? -11.752 47.734  67.055  1.00 69.63  ?  678 PHE A CB  1 
ATOM   4028 C CG  . PHE A 1 697 ? -12.151 48.989  66.353  1.00 68.90  ?  678 PHE A CG  1 
ATOM   4029 C CD1 . PHE A 1 697 ? -13.426 49.514  66.527  1.00 75.76  ?  678 PHE A CD1 1 
ATOM   4030 C CD2 . PHE A 1 697 ? -11.275 49.635  65.481  1.00 69.23  ?  678 PHE A CD2 1 
ATOM   4031 C CE1 . PHE A 1 697 ? -13.827 50.692  65.854  1.00 75.13  ?  678 PHE A CE1 1 
ATOM   4032 C CE2 . PHE A 1 697 ? -11.655 50.816  64.813  1.00 71.19  ?  678 PHE A CE2 1 
ATOM   4033 C CZ  . PHE A 1 697 ? -12.932 51.344  64.999  1.00 71.98  ?  678 PHE A CZ  1 
ATOM   4034 N N   . GLY A 1 698 ? -8.562  47.842  67.547  1.00 76.14  ?  679 GLY A N   1 
ATOM   4035 C CA  . GLY A 1 698 ? -7.218  48.351  67.365  1.00 76.72  ?  679 GLY A CA  1 
ATOM   4036 C C   . GLY A 1 698 ? -6.906  48.736  65.938  1.00 70.67  ?  679 GLY A C   1 
ATOM   4037 O O   . GLY A 1 698 ? -7.683  48.478  65.034  1.00 74.90  ?  679 GLY A O   1 
ATOM   4038 N N   . HIS A 1 699 ? -5.753  49.383  65.765  1.00 70.06  ?  680 HIS A N   1 
ATOM   4039 C CA  . HIS A 1 699 ? -5.212  49.702  64.447  1.00 68.29  ?  680 HIS A CA  1 
ATOM   4040 C C   . HIS A 1 699 ? -3.706  49.604  64.542  1.00 73.75  ?  680 HIS A C   1 
ATOM   4041 O O   . HIS A 1 699 ? -3.098  50.328  65.335  1.00 69.69  ?  680 HIS A O   1 
ATOM   4042 C CB  . HIS A 1 699 ? -5.599  51.083  63.966  1.00 64.57  ?  680 HIS A CB  1 
ATOM   4043 C CG  . HIS A 1 699 ? -4.588  51.684  63.039  1.00 77.69  ?  680 HIS A CG  1 
ATOM   4044 N ND1 . HIS A 1 699 ? -4.480  51.311  61.717  1.00 87.71  ?  680 HIS A ND1 1 
ATOM   4045 C CD2 . HIS A 1 699 ? -3.640  52.632  63.239  1.00 79.99  ?  680 HIS A CD2 1 
ATOM   4046 C CE1 . HIS A 1 699 ? -3.517  52.011  61.141  1.00 86.26  ?  680 HIS A CE1 1 
ATOM   4047 N NE2 . HIS A 1 699 ? -2.992  52.823  62.042  1.00 80.02  ?  680 HIS A NE2 1 
ATOM   4048 N N   . VAL A 1 700 ? -3.107  48.726  63.737  1.00 80.50  ?  681 VAL A N   1 
ATOM   4049 C CA  . VAL A 1 700 ? -1.701  48.405  63.910  1.00 77.47  ?  681 VAL A CA  1 
ATOM   4050 C C   . VAL A 1 700 ? -0.860  49.421  63.170  1.00 79.87  ?  681 VAL A C   1 
ATOM   4051 O O   . VAL A 1 700 ? -1.211  49.882  62.081  1.00 72.32  ?  681 VAL A O   1 
ATOM   4052 C CB  . VAL A 1 700 ? -1.397  46.975  63.467  1.00 75.92  ?  681 VAL A CB  1 
ATOM   4053 C CG1 . VAL A 1 700 ? 0.083   46.652  63.699  1.00 77.45  ?  681 VAL A CG1 1 
ATOM   4054 C CG2 . VAL A 1 700 ? -2.281  46.046  64.254  1.00 79.14  ?  681 VAL A CG2 1 
ATOM   4055 N N   . GLY A 1 701 ? 0.229   49.821  63.818  1.00 88.21  ?  682 GLY A N   1 
ATOM   4056 C CA  . GLY A 1 701 ? 1.044   50.882  63.297  1.00 88.90  ?  682 GLY A CA  1 
ATOM   4057 C C   . GLY A 1 701 ? 1.870   50.428  62.116  1.00 92.51  ?  682 GLY A C   1 
ATOM   4058 O O   . GLY A 1 701 ? 2.113   49.243  61.897  1.00 93.09  ?  682 GLY A O   1 
ATOM   4059 N N   . SER A 1 702 ? 2.290   51.423  61.340  1.00 99.41  ?  683 SER A N   1 
ATOM   4060 C CA  . SER A 1 702 ? 3.253   51.204  60.266  1.00 99.73  ?  683 SER A CA  1 
ATOM   4061 C C   . SER A 1 702 ? 4.619   50.828  60.826  1.00 96.20  ?  683 SER A C   1 
ATOM   4062 O O   . SER A 1 702 ? 5.261   49.876  60.372  1.00 96.28  ?  683 SER A O   1 
ATOM   4063 C CB  . SER A 1 702 ? 3.373   52.488  59.450  1.00 110.00 ?  683 SER A CB  1 
ATOM   4064 O OG  . SER A 1 702 ? 2.118   52.863  58.909  1.00 114.33 ?  683 SER A OG  1 
ATOM   4065 N N   . THR A 1 703 ? 5.060   51.569  61.828  1.00 95.54  ?  684 THR A N   1 
ATOM   4066 C CA  . THR A 1 703 ? 6.416   51.572  62.330  1.00 95.10  ?  684 THR A CA  1 
ATOM   4067 C C   . THR A 1 703 ? 6.369   51.494  63.848  1.00 89.48  ?  684 THR A C   1 
ATOM   4068 O O   . THR A 1 703 ? 5.322   51.703  64.469  1.00 80.31  ?  684 THR A O   1 
ATOM   4069 C CB  . THR A 1 703 ? 7.131   52.852  61.892  1.00 93.86  ?  684 THR A CB  1 
ATOM   4070 O OG1 . THR A 1 703 ? 6.276   53.965  62.184  1.00 95.42  ?  684 THR A OG1 1 
ATOM   4071 C CG2 . THR A 1 703 ? 7.387   52.830  60.417  1.00 98.26  ?  684 THR A CG2 1 
ATOM   4072 N N   . THR A 1 704 ? 7.522   51.183  64.440  1.00 85.21  ?  685 THR A N   1 
ATOM   4073 C CA  . THR A 1 704 ? 7.636   51.277  65.884  1.00 76.95  ?  685 THR A CA  1 
ATOM   4074 C C   . THR A 1 704 ? 7.382   52.707  66.348  1.00 82.44  ?  685 THR A C   1 
ATOM   4075 O O   . THR A 1 704 ? 6.620   52.932  67.301  1.00 76.69  ?  685 THR A O   1 
ATOM   4076 C CB  . THR A 1 704 ? 9.014   50.779  66.316  1.00 84.17  ?  685 THR A CB  1 
ATOM   4077 O OG1 . THR A 1 704 ? 9.133   49.383  66.006  1.00 82.98  ?  685 THR A OG1 1 
ATOM   4078 C CG2 . THR A 1 704 ? 9.237   50.988  67.804  1.00 81.54  ?  685 THR A CG2 1 
ATOM   4079 N N   . ALA A 1 705 ? 7.949   53.692  65.633  1.00 86.51  ?  686 ALA A N   1 
ATOM   4080 C CA  . ALA A 1 705 ? 7.888   55.079  66.084  1.00 75.07  ?  686 ALA A CA  1 
ATOM   4081 C C   . ALA A 1 705 ? 6.470   55.621  66.129  1.00 74.99  ?  686 ALA A C   1 
ATOM   4082 O O   . ALA A 1 705 ? 6.200   56.543  66.904  1.00 89.69  ?  686 ALA A O   1 
ATOM   4083 C CB  . ALA A 1 705 ? 8.743   55.980  65.204  1.00 75.24  ?  686 ALA A CB  1 
ATOM   4084 N N   . SER A 1 706 ? 5.554   55.098  65.321  1.00 70.16  ?  687 SER A N   1 
ATOM   4085 C CA  . SER A 1 706 ? 4.176   55.566  65.378  1.00 71.42  ?  687 SER A CA  1 
ATOM   4086 C C   . SER A 1 706 ? 3.245   54.532  66.006  1.00 72.00  ?  687 SER A C   1 
ATOM   4087 O O   . SER A 1 706 ? 2.026   54.563  65.762  1.00 65.80  ?  687 SER A O   1 
ATOM   4088 C CB  . SER A 1 706 ? 3.675   55.958  63.988  1.00 72.45  ?  687 SER A CB  1 
ATOM   4089 O OG  . SER A 1 706 ? 3.323   54.805  63.234  1.00 91.42  ?  687 SER A OG  1 
ATOM   4090 N N   . ARG A 1 707 ? 3.789   53.617  66.821  1.00 67.95  ?  688 ARG A N   1 
ATOM   4091 C CA  . ARG A 1 707 ? 2.926   52.580  67.374  1.00 64.34  ?  688 ARG A CA  1 
ATOM   4092 C C   . ARG A 1 707 ? 1.791   53.185  68.188  1.00 69.13  ?  688 ARG A C   1 
ATOM   4093 O O   . ARG A 1 707 ? 0.710   52.595  68.263  1.00 70.13  ?  688 ARG A O   1 
ATOM   4094 C CB  . ARG A 1 707 ? 3.735   51.562  68.181  1.00 57.72  ?  688 ARG A CB  1 
ATOM   4095 C CG  . ARG A 1 707 ? 4.477   52.054  69.361  1.00 60.03  ?  688 ARG A CG  1 
ATOM   4096 C CD  . ARG A 1 707 ? 5.433   50.987  69.845  1.00 64.00  ?  688 ARG A CD  1 
ATOM   4097 N NE  . ARG A 1 707 ? 6.003   51.309  71.147  1.00 64.54  ?  688 ARG A NE  1 
ATOM   4098 C CZ  . ARG A 1 707 ? 6.962   50.612  71.746  1.00 69.91  ?  688 ARG A CZ  1 
ATOM   4099 N NH1 . ARG A 1 707 ? 7.484   49.538  71.161  1.00 77.60  ?  688 ARG A NH1 1 
ATOM   4100 N NH2 . ARG A 1 707 ? 7.412   50.990  72.931  1.00 70.21  ?  688 ARG A NH2 1 
ATOM   4101 N N   . GLY A 1 708 ? 1.982   54.396  68.724  1.00 74.75  ?  689 GLY A N   1 
ATOM   4102 C CA  . GLY A 1 708 ? 0.971   55.036  69.544  1.00 66.19  ?  689 GLY A CA  1 
ATOM   4103 C C   . GLY A 1 708 ? -0.023  55.907  68.798  1.00 70.35  ?  689 GLY A C   1 
ATOM   4104 O O   . GLY A 1 708 ? -1.088  56.229  69.336  1.00 65.54  ?  689 GLY A O   1 
ATOM   4105 N N   . GLU A 1 709 ? 0.311   56.286  67.560  1.00 71.57  ?  690 GLU A N   1 
ATOM   4106 C CA  . GLU A 1 709 ? -0.463  57.242  66.763  1.00 66.66  ?  690 GLU A CA  1 
ATOM   4107 C C   . GLU A 1 709 ? -1.789  56.633  66.295  1.00 73.44  ?  690 GLU A C   1 
ATOM   4108 O O   . GLU A 1 709 ? -1.846  55.872  65.324  1.00 78.31  ?  690 GLU A O   1 
ATOM   4109 C CB  . GLU A 1 709 ? 0.374   57.697  65.580  1.00 67.51  ?  690 GLU A CB  1 
ATOM   4110 C CG  . GLU A 1 709 ? -0.240  58.816  64.809  1.00 83.29  ?  690 GLU A CG  1 
ATOM   4111 C CD  . GLU A 1 709 ? 0.666   59.289  63.684  1.00 97.61  ?  690 GLU A CD  1 
ATOM   4112 O OE1 . GLU A 1 709 ? 0.165   59.422  62.534  1.00 97.71  ?  690 GLU A OE1 1 
ATOM   4113 O OE2 . GLU A 1 709 ? 1.881   59.509  63.959  1.00 94.95  ?  690 GLU A OE2 1 
ATOM   4114 N N   . LEU A 1 710 ? -2.870  56.964  66.994  1.00 70.63  ?  691 LEU A N   1 
ATOM   4115 C CA  . LEU A 1 710 ? -4.216  56.521  66.631  1.00 71.69  ?  691 LEU A CA  1 
ATOM   4116 C C   . LEU A 1 710 ? -4.363  54.999  66.674  1.00 71.49  ?  691 LEU A C   1 
ATOM   4117 O O   . LEU A 1 710 ? -5.022  54.398  65.827  1.00 71.19  ?  691 LEU A O   1 
ATOM   4118 C CB  . LEU A 1 710 ? -4.609  57.082  65.269  1.00 75.02  ?  691 LEU A CB  1 
ATOM   4119 C CG  . LEU A 1 710 ? -4.682  58.607  65.429  1.00 75.94  ?  691 LEU A CG  1 
ATOM   4120 C CD1 . LEU A 1 710 ? -4.613  59.379  64.101  1.00 71.27  ?  691 LEU A CD1 1 
ATOM   4121 C CD2 . LEU A 1 710 ? -5.936  58.968  66.240  1.00 69.82  ?  691 LEU A CD2 1 
ATOM   4122 N N   . PHE A 1 711 ? -3.814  54.379  67.715  1.00 68.91  ?  692 PHE A N   1 
ATOM   4123 C CA  . PHE A 1 711 ? -3.723  52.933  67.762  1.00 63.81  ?  692 PHE A CA  1 
ATOM   4124 C C   . PHE A 1 711 ? -4.994  52.248  68.254  1.00 69.01  ?  692 PHE A C   1 
ATOM   4125 O O   . PHE A 1 711 ? -5.104  51.029  68.095  1.00 73.34  ?  692 PHE A O   1 
ATOM   4126 C CB  . PHE A 1 711 ? -2.526  52.525  68.633  1.00 63.62  ?  692 PHE A CB  1 
ATOM   4127 C CG  . PHE A 1 711 ? -2.835  52.426  70.100  1.00 67.86  ?  692 PHE A CG  1 
ATOM   4128 C CD1 . PHE A 1 711 ? -3.031  53.562  70.858  1.00 71.85  ?  692 PHE A CD1 1 
ATOM   4129 C CD2 . PHE A 1 711 ? -2.922  51.188  70.732  1.00 71.48  ?  692 PHE A CD2 1 
ATOM   4130 C CE1 . PHE A 1 711 ? -3.325  53.462  72.232  1.00 77.11  ?  692 PHE A CE1 1 
ATOM   4131 C CE2 . PHE A 1 711 ? -3.211  51.077  72.107  1.00 71.06  ?  692 PHE A CE2 1 
ATOM   4132 C CZ  . PHE A 1 711 ? -3.414  52.205  72.854  1.00 70.60  ?  692 PHE A CZ  1 
ATOM   4133 N N   . LEU A 1 712 ? -5.959  52.954  68.845  1.00 72.27  ?  693 LEU A N   1 
ATOM   4134 C CA  . LEU A 1 712 ? -7.095  52.252  69.442  1.00 72.68  ?  693 LEU A CA  1 
ATOM   4135 C C   . LEU A 1 712 ? -8.336  53.125  69.269  1.00 71.74  ?  693 LEU A C   1 
ATOM   4136 O O   . LEU A 1 712 ? -8.233  54.352  69.223  1.00 72.50  ?  693 LEU A O   1 
ATOM   4137 C CB  . LEU A 1 712 ? -6.881  51.997  70.942  1.00 66.60  ?  693 LEU A CB  1 
ATOM   4138 C CG  . LEU A 1 712 ? -7.620  50.849  71.655  1.00 76.77  ?  693 LEU A CG  1 
ATOM   4139 C CD1 . LEU A 1 712 ? -7.022  50.641  73.059  1.00 74.71  ?  693 LEU A CD1 1 
ATOM   4140 C CD2 . LEU A 1 712 ? -9.146  50.778  71.653  1.00 80.36  ?  693 LEU A CD2 1 
ATOM   4141 N N   . PHE A 1 713 ? -9.512  52.503  69.183  1.00 69.78  ?  694 PHE A N   1 
ATOM   4142 C CA  . PHE A 1 713 ? -10.767 53.239  69.063  1.00 73.43  ?  694 PHE A CA  1 
ATOM   4143 C C   . PHE A 1 713 ? -11.794 52.691  70.050  1.00 82.85  ?  694 PHE A C   1 
ATOM   4144 O O   . PHE A 1 713 ? -11.884 51.474  70.237  1.00 79.40  ?  694 PHE A O   1 
ATOM   4145 C CB  . PHE A 1 713 ? -11.333 53.162  67.638  1.00 68.99  ?  694 PHE A CB  1 
ATOM   4146 C CG  . PHE A 1 713 ? -10.521 53.902  66.621  1.00 68.31  ?  694 PHE A CG  1 
ATOM   4147 C CD1 . PHE A 1 713 ? -9.244  53.474  66.279  1.00 68.50  ?  694 PHE A CD1 1 
ATOM   4148 C CD2 . PHE A 1 713 ? -11.032 55.034  65.999  1.00 70.01  ?  694 PHE A CD2 1 
ATOM   4149 C CE1 . PHE A 1 713 ? -8.473  54.169  65.337  1.00 70.41  ?  694 PHE A CE1 1 
ATOM   4150 C CE2 . PHE A 1 713 ? -10.271 55.737  65.044  1.00 73.54  ?  694 PHE A CE2 1 
ATOM   4151 C CZ  . PHE A 1 713 ? -8.989  55.305  64.715  1.00 70.77  ?  694 PHE A CZ  1 
ATOM   4152 N N   . TRP A 1 714 ? -12.578 53.586  70.674  1.00 84.41  ?  695 TRP A N   1 
ATOM   4153 C CA  . TRP A 1 714 ? -13.588 53.192  71.657  1.00 81.75  ?  695 TRP A CA  1 
ATOM   4154 C C   . TRP A 1 714 ? -14.976 53.577  71.173  1.00 83.97  ?  695 TRP A C   1 
ATOM   4155 O O   . TRP A 1 714 ? -15.187 54.699  70.694  1.00 81.90  ?  695 TRP A O   1 
ATOM   4156 C CB  . TRP A 1 714 ? -13.355 53.819  73.033  1.00 84.40  ?  695 TRP A CB  1 
ATOM   4157 C CG  . TRP A 1 714 ? -12.007 53.568  73.635  1.00 86.05  ?  695 TRP A CG  1 
ATOM   4158 C CD1 . TRP A 1 714 ? -10.795 53.969  73.142  1.00 84.65  ?  695 TRP A CD1 1 
ATOM   4159 C CD2 . TRP A 1 714 ? -11.727 52.847  74.841  1.00 79.33  ?  695 TRP A CD2 1 
ATOM   4160 N NE1 . TRP A 1 714 ? -9.782  53.543  73.969  1.00 82.17  ?  695 TRP A NE1 1 
ATOM   4161 C CE2 . TRP A 1 714 ? -10.327 52.848  75.015  1.00 78.60  ?  695 TRP A CE2 1 
ATOM   4162 C CE3 . TRP A 1 714 ? -12.521 52.207  75.790  1.00 78.57  ?  695 TRP A CE3 1 
ATOM   4163 C CZ2 . TRP A 1 714 ? -9.709  52.237  76.096  1.00 78.28  ?  695 TRP A CZ2 1 
ATOM   4164 C CZ3 . TRP A 1 714 ? -11.904 51.592  76.861  1.00 78.90  ?  695 TRP A CZ3 1 
ATOM   4165 C CH2 . TRP A 1 714 ? -10.511 51.612  77.007  1.00 75.58  ?  695 TRP A CH2 1 
ATOM   4166 N N   . ASN A 1 715 ? -15.901 52.626  71.294  1.00 84.34  ?  696 ASN A N   1 
ATOM   4167 C CA  . ASN A 1 715 ? -17.329 52.775  71.028  1.00 90.04  ?  696 ASN A CA  1 
ATOM   4168 C C   . ASN A 1 715 ? -17.966 52.624  72.402  1.00 92.00  ?  696 ASN A C   1 
ATOM   4169 O O   . ASN A 1 715 ? -18.251 51.513  72.854  1.00 94.54  ?  696 ASN A O   1 
ATOM   4170 C CB  . ASN A 1 715 ? -17.840 51.719  70.009  1.00 86.20  ?  696 ASN A CB  1 
ATOM   4171 C CG  . ASN A 1 715 ? -19.371 51.599  69.977  1.00 92.01  ?  696 ASN A CG  1 
ATOM   4172 O OD1 . ASN A 1 715 ? -20.067 52.464  69.439  1.00 95.35  ?  696 ASN A OD1 1 
ATOM   4173 N ND2 . ASN A 1 715 ? -19.892 50.500  70.524  1.00 88.50  ?  696 ASN A ND2 1 
ATOM   4174 N N   . LEU A 1 716 ? -18.154 53.749  73.087  1.00 98.00  ?  697 LEU A N   1 
ATOM   4175 C CA  . LEU A 1 716 ? -18.508 53.711  74.499  1.00 101.37 ?  697 LEU A CA  1 
ATOM   4176 C C   . LEU A 1 716 ? -19.867 54.288  74.806  1.00 100.28 ?  697 LEU A C   1 
ATOM   4177 O O   . LEU A 1 716 ? -20.436 53.961  75.856  1.00 96.42  ?  697 LEU A O   1 
ATOM   4178 C CB  . LEU A 1 716 ? -17.471 54.471  75.342  1.00 94.68  ?  697 LEU A CB  1 
ATOM   4179 C CG  . LEU A 1 716 ? -16.106 53.786  75.403  1.00 93.96  ?  697 LEU A CG  1 
ATOM   4180 C CD1 . LEU A 1 716 ? -15.167 54.556  76.321  1.00 88.27  ?  697 LEU A CD1 1 
ATOM   4181 C CD2 . LEU A 1 716 ? -16.238 52.295  75.797  1.00 86.59  ?  697 LEU A CD2 1 
ATOM   4182 N N   . TYR A 1 717 ? -20.404 55.117  73.924  1.00 106.13 ?  698 TYR A N   1 
ATOM   4183 C CA  . TYR A 1 717 ? -21.520 55.979  74.251  1.00 106.11 ?  698 TYR A CA  1 
ATOM   4184 C C   . TYR A 1 717 ? -22.775 55.537  73.515  1.00 112.21 ?  698 TYR A C   1 
ATOM   4185 O O   . TYR A 1 717 ? -22.735 54.718  72.584  1.00 114.39 ?  698 TYR A O   1 
ATOM   4186 C CB  . TYR A 1 717 ? -21.162 57.435  73.927  1.00 101.13 ?  698 TYR A CB  1 
ATOM   4187 C CG  . TYR A 1 717 ? -19.960 57.895  74.733  1.00 97.96  ?  698 TYR A CG  1 
ATOM   4188 C CD1 . TYR A 1 717 ? -18.709 58.050  74.138  1.00 94.95  ?  698 TYR A CD1 1 
ATOM   4189 C CD2 . TYR A 1 717 ? -20.072 58.133  76.105  1.00 97.98  ?  698 TYR A CD2 1 
ATOM   4190 C CE1 . TYR A 1 717 ? -17.605 58.452  74.889  1.00 95.32  ?  698 TYR A CE1 1 
ATOM   4191 C CE2 . TYR A 1 717 ? -18.979 58.532  76.862  1.00 92.89  ?  698 TYR A CE2 1 
ATOM   4192 C CZ  . TYR A 1 717 ? -17.749 58.689  76.252  1.00 92.92  ?  698 TYR A CZ  1 
ATOM   4193 O OH  . TYR A 1 717 ? -16.661 59.074  77.010  1.00 90.73  ?  698 TYR A OH  1 
ATOM   4194 N N   . LYS A 1 718 ? -23.903 56.068  73.993  1.00 111.85 ?  699 LYS A N   1 
ATOM   4195 C CA  . LYS A 1 718 ? -25.188 55.838  73.344  1.00 118.27 ?  699 LYS A CA  1 
ATOM   4196 C C   . LYS A 1 718 ? -25.162 56.358  71.906  1.00 115.75 ?  699 LYS A C   1 
ATOM   4197 O O   . LYS A 1 718 ? -25.416 55.608  70.951  1.00 117.17 ?  699 LYS A O   1 
ATOM   4198 C CB  . LYS A 1 718 ? -26.301 56.501  74.173  1.00 116.25 ?  699 LYS A CB  1 
ATOM   4199 C CG  . LYS A 1 718 ? -27.723 56.403  73.595  1.00 122.58 ?  699 LYS A CG  1 
ATOM   4200 C CD  . LYS A 1 718 ? -28.214 54.952  73.456  1.00 122.10 ?  699 LYS A CD  1 
ATOM   4201 C CE  . LYS A 1 718 ? -29.530 54.878  72.677  1.00 119.95 ?  699 LYS A CE  1 
ATOM   4202 N NZ  . LYS A 1 718 ? -29.402 55.330  71.252  1.00 117.33 ?  699 LYS A NZ  1 
ATOM   4203 N N   . ALA A 1 719 ? -24.807 57.640  71.733  1.00 103.33 ?  700 ALA A N   1 
ATOM   4204 C CA  . ALA A 1 719 ? -24.706 58.318  70.442  1.00 103.17 ?  700 ALA A CA  1 
ATOM   4205 C C   . ALA A 1 719 ? -23.628 57.696  69.544  1.00 100.96 ?  700 ALA A C   1 
ATOM   4206 O O   . ALA A 1 719 ? -22.901 56.788  69.972  1.00 99.85  ?  700 ALA A O   1 
ATOM   4207 C CB  . ALA A 1 719 ? -24.432 59.812  70.670  1.00 90.54  ?  700 ALA A CB  1 
ATOM   4208 N N   . PRO A 1 720 ? -23.512 58.129  68.282  1.00 95.17  ?  701 PRO A N   1 
ATOM   4209 C CA  . PRO A 1 720 ? -22.412 57.650  67.417  1.00 94.82  ?  701 PRO A CA  1 
ATOM   4210 C C   . PRO A 1 720 ? -21.103 58.421  67.584  1.00 92.49  ?  701 PRO A C   1 
ATOM   4211 O O   . PRO A 1 720 ? -20.763 59.356  66.839  1.00 91.59  ?  701 PRO A O   1 
ATOM   4212 C CB  . PRO A 1 720 ? -22.980 57.849  66.012  1.00 97.75  ?  701 PRO A CB  1 
ATOM   4213 C CG  . PRO A 1 720 ? -23.878 59.012  66.161  1.00 99.09  ?  701 PRO A CG  1 
ATOM   4214 C CD  . PRO A 1 720 ? -24.517 58.875  67.503  1.00 98.27  ?  701 PRO A CD  1 
ATOM   4215 N N   . ILE A 1 721 ? -20.332 58.014  68.582  1.00 88.02  ?  702 ILE A N   1 
ATOM   4216 C CA  . ILE A 1 721 ? -19.051 58.636  68.870  1.00 86.69  ?  702 ILE A CA  1 
ATOM   4217 C C   . ILE A 1 721 ? -18.007 57.538  68.913  1.00 82.31  ?  702 ILE A C   1 
ATOM   4218 O O   . ILE A 1 721 ? -18.113 56.587  69.709  1.00 82.72  ?  702 ILE A O   1 
ATOM   4219 C CB  . ILE A 1 721 ? -19.072 59.433  70.186  1.00 90.40  ?  702 ILE A CB  1 
ATOM   4220 C CG1 . ILE A 1 721 ? -20.043 60.617  70.069  1.00 94.09  ?  702 ILE A CG1 1 
ATOM   4221 C CG2 . ILE A 1 721 ? -17.679 59.906  70.552  1.00 84.23  ?  702 ILE A CG2 1 
ATOM   4222 C CD1 . ILE A 1 721 ? -20.356 61.304  71.365  1.00 89.07  ?  702 ILE A CD1 1 
ATOM   4223 N N   . LEU A 1 722 ? -17.036 57.642  68.020  1.00 79.71  ?  703 LEU A N   1 
ATOM   4224 C CA  . LEU A 1 722 ? -15.791 56.909  68.143  1.00 86.59  ?  703 LEU A CA  1 
ATOM   4225 C C   . LEU A 1 722 ? -14.772 57.807  68.826  1.00 87.77  ?  703 LEU A C   1 
ATOM   4226 O O   . LEU A 1 722 ? -14.816 59.036  68.700  1.00 89.82  ?  703 LEU A O   1 
ATOM   4227 C CB  . LEU A 1 722 ? -15.276 56.461  66.773  1.00 84.60  ?  703 LEU A CB  1 
ATOM   4228 C CG  . LEU A 1 722 ? -15.841 55.146  66.232  1.00 82.74  ?  703 LEU A CG  1 
ATOM   4229 C CD1 . LEU A 1 722 ? -15.065 54.751  64.988  1.00 87.26  ?  703 LEU A CD1 1 
ATOM   4230 C CD2 . LEU A 1 722 ? -15.837 54.019  67.275  1.00 77.29  ?  703 LEU A CD2 1 
ATOM   4231 N N   . LEU A 1 723 ? -13.844 57.189  69.547  1.00 83.43  ?  704 LEU A N   1 
ATOM   4232 C CA  . LEU A 1 723 ? -12.904 57.957  70.347  1.00 81.20  ?  704 LEU A CA  1 
ATOM   4233 C C   . LEU A 1 723 ? -11.551 57.263  70.298  1.00 78.37  ?  704 LEU A C   1 
ATOM   4234 O O   . LEU A 1 723 ? -11.441 56.093  70.670  1.00 83.98  ?  704 LEU A O   1 
ATOM   4235 C CB  . LEU A 1 723 ? -13.485 58.104  71.754  1.00 82.07  ?  704 LEU A CB  1 
ATOM   4236 C CG  . LEU A 1 723 ? -13.025 58.908  72.956  1.00 87.31  ?  704 LEU A CG  1 
ATOM   4237 C CD1 . LEU A 1 723 ? -14.289 59.426  73.662  1.00 84.16  ?  704 LEU A CD1 1 
ATOM   4238 C CD2 . LEU A 1 723 ? -12.330 57.953  73.880  1.00 85.62  ?  704 LEU A CD2 1 
ATOM   4239 N N   . ALA A 1 724 ? -10.541 57.978  69.792  1.00 72.51  ?  705 ALA A N   1 
ATOM   4240 C CA  . ALA A 1 724 ? -9.286  57.410  69.299  1.00 69.92  ?  705 ALA A CA  1 
ATOM   4241 C C   . ALA A 1 724 ? -8.099  57.887  70.131  1.00 75.79  ?  705 ALA A C   1 
ATOM   4242 O O   . ALA A 1 724 ? -7.842  59.097  70.212  1.00 74.02  ?  705 ALA A O   1 
ATOM   4243 C CB  . ALA A 1 724 ? -9.060  57.803  67.835  1.00 68.95  ?  705 ALA A CB  1 
ATOM   4244 N N   . LEU A 1 725 ? -7.334  56.940  70.676  1.00 70.86  ?  706 LEU A N   1 
ATOM   4245 C CA  . LEU A 1 725 ? -6.222  57.246  71.569  1.00 66.78  ?  706 LEU A CA  1 
ATOM   4246 C C   . LEU A 1 725 ? -4.951  57.582  70.792  1.00 65.13  ?  706 LEU A C   1 
ATOM   4247 O O   . LEU A 1 725 ? -4.778  57.177  69.646  1.00 71.66  ?  706 LEU A O   1 
ATOM   4248 C CB  . LEU A 1 725 ? -5.981  56.054  72.493  1.00 71.79  ?  706 LEU A CB  1 
ATOM   4249 C CG  . LEU A 1 725 ? -6.556  56.098  73.917  1.00 79.84  ?  706 LEU A CG  1 
ATOM   4250 C CD1 . LEU A 1 725 ? -7.997  56.578  73.910  1.00 73.20  ?  706 LEU A CD1 1 
ATOM   4251 C CD2 . LEU A 1 725 ? -6.494  54.690  74.548  1.00 71.96  ?  706 LEU A CD2 1 
ATOM   4252 N N   . VAL A 1 726 ? -4.065  58.347  71.426  1.00 67.42  ?  707 VAL A N   1 
ATOM   4253 C CA  . VAL A 1 726 ? -2.729  58.662  70.907  1.00 64.70  ?  707 VAL A CA  1 
ATOM   4254 C C   . VAL A 1 726 ? -1.746  58.522  72.069  1.00 66.41  ?  707 VAL A C   1 
ATOM   4255 O O   . VAL A 1 726 ? -1.624  59.427  72.899  1.00 70.43  ?  707 VAL A O   1 
ATOM   4256 C CB  . VAL A 1 726 ? -2.659  60.064  70.307  1.00 62.07  ?  707 VAL A CB  1 
ATOM   4257 C CG1 . VAL A 1 726 ? -1.221  60.392  69.878  1.00 62.18  ?  707 VAL A CG1 1 
ATOM   4258 C CG2 . VAL A 1 726 ? -3.613  60.178  69.153  1.00 66.55  ?  707 VAL A CG2 1 
ATOM   4259 N N   . ALA A 1 727 ? -1.040  57.406  72.131  1.00 63.16  ?  708 ALA A N   1 
ATOM   4260 C CA  . ALA A 1 727 ? -0.217  57.055  73.275  1.00 62.37  ?  708 ALA A CA  1 
ATOM   4261 C C   . ALA A 1 727 ? 1.255   57.232  72.936  1.00 56.55  ?  708 ALA A C   1 
ATOM   4262 O O   . ALA A 1 727 ? 1.608   57.665  71.850  1.00 62.66  ?  708 ALA A O   1 
ATOM   4263 C CB  . ALA A 1 727 ? -0.498  55.610  73.699  1.00 67.72  ?  708 ALA A CB  1 
ATOM   4264 N N   . GLY A 1 728 ? 2.116   56.867  73.880  1.00 59.34  ?  709 GLY A N   1 
ATOM   4265 C CA  . GLY A 1 728 ? 3.554   56.750  73.694  1.00 62.27  ?  709 GLY A CA  1 
ATOM   4266 C C   . GLY A 1 728 ? 4.197   58.017  73.167  1.00 63.15  ?  709 GLY A C   1 
ATOM   4267 O O   . GLY A 1 728 ? 3.741   59.131  73.428  1.00 68.83  ?  709 GLY A O   1 
ATOM   4268 N N   . GLU A 1 729 ? 5.272   57.842  72.390  1.00 70.20  ?  710 GLU A N   1 
ATOM   4269 C CA  . GLU A 1 729 ? 5.959   58.994  71.802  1.00 67.30  ?  710 GLU A CA  1 
ATOM   4270 C C   . GLU A 1 729 ? 5.059   59.766  70.844  1.00 65.73  ?  710 GLU A C   1 
ATOM   4271 O O   . GLU A 1 729 ? 5.259   60.968  70.637  1.00 69.57  ?  710 GLU A O   1 
ATOM   4272 C CB  . GLU A 1 729 ? 7.236   58.559  71.080  1.00 62.57  ?  710 GLU A CB  1 
ATOM   4273 C CG  . GLU A 1 729 ? 8.237   57.762  71.952  1.00 69.63  ?  710 GLU A CG  1 
ATOM   4274 C CD  . GLU A 1 729 ? 9.135   58.663  72.788  1.00 78.73  ?  710 GLU A CD  1 
ATOM   4275 O OE1 . GLU A 1 729 ? 8.860   59.882  72.818  1.00 86.55  ?  710 GLU A OE1 1 
ATOM   4276 O OE2 . GLU A 1 729 ? 10.125  58.179  73.383  1.00 84.24  ?  710 GLU A OE2 1 
ATOM   4277 N N   . ALA A 1 730 ? 4.051   59.112  70.275  1.00 65.58  ?  711 ALA A N   1 
ATOM   4278 C CA  . ALA A 1 730 ? 3.114   59.818  69.411  1.00 65.70  ?  711 ALA A CA  1 
ATOM   4279 C C   . ALA A 1 730 ? 2.408   60.958  70.139  1.00 70.37  ?  711 ALA A C   1 
ATOM   4280 O O   . ALA A 1 730 ? 2.156   62.011  69.539  1.00 73.76  ?  711 ALA A O   1 
ATOM   4281 C CB  . ALA A 1 730 ? 2.092   58.834  68.846  1.00 67.61  ?  711 ALA A CB  1 
ATOM   4282 N N   . ALA A 1 731 ? 2.093   60.775  71.425  1.00 71.47  ?  712 ALA A N   1 
ATOM   4283 C CA  . ALA A 1 731 ? 1.251   61.735  72.138  1.00 71.76  ?  712 ALA A CA  1 
ATOM   4284 C C   . ALA A 1 731 ? 1.868   63.123  72.127  1.00 73.65  ?  712 ALA A C   1 
ATOM   4285 O O   . ALA A 1 731 ? 1.184   64.121  71.871  1.00 73.11  ?  712 ALA A O   1 
ATOM   4286 C CB  . ALA A 1 731 ? 1.011   61.269  73.577  1.00 61.99  ?  712 ALA A CB  1 
ATOM   4287 N N   . GLY A 1 732 ? 3.173   63.204  72.390  1.00 76.43  ?  713 GLY A N   1 
ATOM   4288 C CA  . GLY A 1 732 ? 3.820   64.499  72.469  1.00 79.77  ?  713 GLY A CA  1 
ATOM   4289 C C   . GLY A 1 732 ? 4.013   65.176  71.134  1.00 75.59  ?  713 GLY A C   1 
ATOM   4290 O O   . GLY A 1 732 ? 4.170   66.396  71.095  1.00 85.40  ?  713 GLY A O   1 
ATOM   4291 N N   . ILE A 1 733 ? 3.993   64.415  70.043  1.00 78.22  ?  714 ILE A N   1 
ATOM   4292 C CA  . ILE A 1 733 ? 4.229   64.960  68.709  1.00 76.87  ?  714 ILE A CA  1 
ATOM   4293 C C   . ILE A 1 733 ? 2.924   65.342  68.019  1.00 81.38  ?  714 ILE A C   1 
ATOM   4294 O O   . ILE A 1 733 ? 2.856   66.368  67.343  1.00 85.71  ?  714 ILE A O   1 
ATOM   4295 C CB  . ILE A 1 733 ? 5.028   63.945  67.874  1.00 73.40  ?  714 ILE A CB  1 
ATOM   4296 C CG1 . ILE A 1 733 ? 6.317   63.575  68.614  1.00 72.44  ?  714 ILE A CG1 1 
ATOM   4297 C CG2 . ILE A 1 733 ? 5.317   64.529  66.515  1.00 71.31  ?  714 ILE A CG2 1 
ATOM   4298 C CD1 . ILE A 1 733 ? 7.342   62.809  67.820  1.00 65.58  ?  714 ILE A CD1 1 
ATOM   4299 N N   . MET A 1 734 ? 1.858   64.553  68.172  1.00 79.85  ?  715 MET A N   1 
ATOM   4300 C CA  . MET A 1 734 ? 0.585   64.942  67.574  1.00 80.38  ?  715 MET A CA  1 
ATOM   4301 C C   . MET A 1 734 ? 0.050   66.249  68.136  1.00 85.47  ?  715 MET A C   1 
ATOM   4302 O O   . MET A 1 734 ? -0.939  66.778  67.613  1.00 91.52  ?  715 MET A O   1 
ATOM   4303 C CB  . MET A 1 734 ? -0.448  63.831  67.759  1.00 84.26  ?  715 MET A CB  1 
ATOM   4304 C CG  . MET A 1 734 ? -0.103  62.598  66.906  1.00 92.45  ?  715 MET A CG  1 
ATOM   4305 S SD  . MET A 1 734 ? -0.053  63.001  65.129  1.00 106.95 ?  715 MET A SD  1 
ATOM   4306 C CE  . MET A 1 734 ? 1.576   62.393  64.677  1.00 94.25  ?  715 MET A CE  1 
ATOM   4307 N N   . GLU A 1 735 ? 0.687   66.800  69.166  1.00 84.91  ?  716 GLU A N   1 
ATOM   4308 C CA  . GLU A 1 735 ? 0.178   68.038  69.721  1.00 83.84  ?  716 GLU A CA  1 
ATOM   4309 C C   . GLU A 1 735 ? 0.591   69.238  68.885  1.00 81.43  ?  716 GLU A C   1 
ATOM   4310 O O   . GLU A 1 735 ? -0.031  70.298  68.997  1.00 80.33  ?  716 GLU A O   1 
ATOM   4311 C CB  . GLU A 1 735 ? 0.638   68.188  71.172  1.00 78.87  ?  716 GLU A CB  1 
ATOM   4312 C CG  . GLU A 1 735 ? -0.408  67.628  72.131  1.00 77.94  ?  716 GLU A CG  1 
ATOM   4313 C CD  . GLU A 1 735 ? -0.048  67.766  73.605  1.00 78.29  ?  716 GLU A CD  1 
ATOM   4314 O OE1 . GLU A 1 735 ? -0.467  66.881  74.408  1.00 70.27  ?  716 GLU A OE1 1 
ATOM   4315 O OE2 . GLU A 1 735 ? 0.582   68.801  73.965  1.00 79.16  ?  716 GLU A OE2 1 
ATOM   4316 N N   . ASN A 1 736 ? 1.603   69.072  68.037  1.00 82.80  ?  717 ASN A N   1 
ATOM   4317 C CA  . ASN A 1 736 ? 2.089   70.080  67.105  1.00 83.26  ?  717 ASN A CA  1 
ATOM   4318 C C   . ASN A 1 736 ? 1.414   70.019  65.742  1.00 87.42  ?  717 ASN A C   1 
ATOM   4319 O O   . ASN A 1 736 ? 1.892   70.658  64.802  1.00 95.35  ?  717 ASN A O   1 
ATOM   4320 C CB  . ASN A 1 736 ? 3.587   69.908  66.903  1.00 87.74  ?  717 ASN A CB  1 
ATOM   4321 C CG  . ASN A 1 736 ? 4.387   70.557  67.988  1.00 97.59  ?  717 ASN A CG  1 
ATOM   4322 O OD1 . ASN A 1 736 ? 3.851   71.296  68.826  1.00 88.53  ?  717 ASN A OD1 1 
ATOM   4323 N ND2 . ASN A 1 736 ? 5.682   70.256  68.014  1.00 110.93 ?  717 ASN A ND2 1 
ATOM   4324 N N   . ILE A 1 737 ? 0.334   69.261  65.603  1.00 88.12  ?  718 ILE A N   1 
ATOM   4325 C CA  . ILE A 1 737 ? -0.321  69.045  64.322  1.00 93.59  ?  718 ILE A CA  1 
ATOM   4326 C C   . ILE A 1 737 ? -1.765  69.513  64.442  1.00 93.11  ?  718 ILE A C   1 
ATOM   4327 O O   . ILE A 1 737 ? -2.396  69.323  65.488  1.00 87.64  ?  718 ILE A O   1 
ATOM   4328 C CB  . ILE A 1 737 ? -0.209  67.560  63.912  1.00 89.48  ?  718 ILE A CB  1 
ATOM   4329 C CG1 . ILE A 1 737 ? 1.168   67.309  63.300  1.00 83.65  ?  718 ILE A CG1 1 
ATOM   4330 C CG2 . ILE A 1 737 ? -1.316  67.134  62.961  1.00 88.24  ?  718 ILE A CG2 1 
ATOM   4331 C CD1 . ILE A 1 737 ? 1.540   65.867  63.268  1.00 95.15  ?  718 ILE A CD1 1 
ATOM   4332 N N   . SER A 1 738 ? -2.274  70.147  63.381  1.00 91.83  ?  719 SER A N   1 
ATOM   4333 C CA  . SER A 1 738 ? -3.611  70.729  63.400  1.00 94.55  ?  719 SER A CA  1 
ATOM   4334 C C   . SER A 1 738 ? -4.687  69.667  63.636  1.00 92.97  ?  719 SER A C   1 
ATOM   4335 O O   . SER A 1 738 ? -4.476  68.467  63.444  1.00 91.48  ?  719 SER A O   1 
ATOM   4336 C CB  . SER A 1 738 ? -3.899  71.462  62.086  1.00 100.17 ?  719 SER A CB  1 
ATOM   4337 O OG  . SER A 1 738 ? -4.476  70.588  61.121  1.00 102.07 ?  719 SER A OG  1 
ATOM   4338 N N   . ASP A 1 739 ? -5.867  70.138  64.050  1.00 92.55  ?  720 ASP A N   1 
ATOM   4339 C CA  . ASP A 1 739 ? -7.004  69.245  64.256  1.00 89.15  ?  720 ASP A CA  1 
ATOM   4340 C C   . ASP A 1 739 ? -7.392  68.537  62.962  1.00 95.42  ?  720 ASP A C   1 
ATOM   4341 O O   . ASP A 1 739 ? -7.731  67.346  62.973  1.00 92.83  ?  720 ASP A O   1 
ATOM   4342 C CB  . ASP A 1 739 ? -8.197  70.038  64.807  1.00 101.32 ?  720 ASP A CB  1 
ATOM   4343 C CG  . ASP A 1 739 ? -7.909  70.700  66.172  1.00 107.56 ?  720 ASP A CG  1 
ATOM   4344 O OD1 . ASP A 1 739 ? -7.349  70.024  67.075  1.00 98.29  ?  720 ASP A OD1 1 
ATOM   4345 O OD2 . ASP A 1 739 ? -8.228  71.912  66.327  1.00 109.00 ?  720 ASP A OD2 1 
ATOM   4346 N N   . ASP A 1 740 ? -7.331  69.250  61.830  1.00 99.17  ?  721 ASP A N   1 
ATOM   4347 C CA  . ASP A 1 740 ? -7.801  68.686  60.569  1.00 95.61  ?  721 ASP A CA  1 
ATOM   4348 C C   . ASP A 1 740 ? -6.826  67.667  60.003  1.00 95.28  ?  721 ASP A C   1 
ATOM   4349 O O   . ASP A 1 740 ? -7.249  66.610  59.516  1.00 98.21  ?  721 ASP A O   1 
ATOM   4350 C CB  . ASP A 1 740 ? -8.074  69.793  59.560  1.00 98.51  ?  721 ASP A CB  1 
ATOM   4351 C CG  . ASP A 1 740 ? -9.224  70.683  59.983  1.00 108.74 ?  721 ASP A CG  1 
ATOM   4352 O OD1 . ASP A 1 740 ? -9.547  70.698  61.197  1.00 117.77 ?  721 ASP A OD1 1 
ATOM   4353 O OD2 . ASP A 1 740 ? -9.829  71.336  59.102  1.00 108.50 ?  721 ASP A OD2 1 
ATOM   4354 N N   . VAL A 1 741 ? -5.524  67.951  60.064  1.00 86.65  ?  722 VAL A N   1 
ATOM   4355 C CA  . VAL A 1 741 ? -4.562  66.906  59.744  1.00 86.31  ?  722 VAL A CA  1 
ATOM   4356 C C   . VAL A 1 741 ? -4.767  65.675  60.627  1.00 87.94  ?  722 VAL A C   1 
ATOM   4357 O O   . VAL A 1 741 ? -4.600  64.541  60.164  1.00 89.07  ?  722 VAL A O   1 
ATOM   4358 C CB  . VAL A 1 741 ? -3.141  67.471  59.849  1.00 87.34  ?  722 VAL A CB  1 
ATOM   4359 C CG1 . VAL A 1 741 ? -2.125  66.431  59.434  1.00 85.87  ?  722 VAL A CG1 1 
ATOM   4360 C CG2 . VAL A 1 741 ? -3.048  68.664  58.965  1.00 87.20  ?  722 VAL A CG2 1 
ATOM   4361 N N   . ILE A 1 742 ? -5.168  65.860  61.888  1.00 88.17  ?  723 ILE A N   1 
ATOM   4362 C CA  . ILE A 1 742 ? -5.349  64.709  62.770  1.00 88.89  ?  723 ILE A CA  1 
ATOM   4363 C C   . ILE A 1 742 ? -6.637  63.974  62.439  1.00 88.28  ?  723 ILE A C   1 
ATOM   4364 O O   . ILE A 1 742 ? -6.662  62.739  62.373  1.00 90.94  ?  723 ILE A O   1 
ATOM   4365 C CB  . ILE A 1 742 ? -5.312  65.123  64.256  1.00 91.88  ?  723 ILE A CB  1 
ATOM   4366 C CG1 . ILE A 1 742 ? -3.876  65.330  64.736  1.00 90.43  ?  723 ILE A CG1 1 
ATOM   4367 C CG2 . ILE A 1 742 ? -5.968  64.056  65.140  1.00 79.67  ?  723 ILE A CG2 1 
ATOM   4368 C CD1 . ILE A 1 742 ? -3.791  65.955  66.122  1.00 89.39  ?  723 ILE A CD1 1 
ATOM   4369 N N   . VAL A 1 743 ? -7.735  64.706  62.243  1.00 89.88  ?  724 VAL A N   1 
ATOM   4370 C CA  . VAL A 1 743 ? -8.971  64.004  61.905  1.00 97.70  ?  724 VAL A CA  1 
ATOM   4371 C C   . VAL A 1 743 ? -8.841  63.335  60.525  1.00 94.13  ?  724 VAL A C   1 
ATOM   4372 O O   . VAL A 1 743 ? -9.451  62.286  60.278  1.00 89.72  ?  724 VAL A O   1 
ATOM   4373 C CB  . VAL A 1 743 ? -10.181 64.963  62.018  1.00 92.62  ?  724 VAL A CB  1 
ATOM   4374 C CG1 . VAL A 1 743 ? -11.500 64.234  61.766  1.00 89.87  ?  724 VAL A CG1 1 
ATOM   4375 C CG2 . VAL A 1 743 ? -10.227 65.585  63.404  1.00 78.03  ?  724 VAL A CG2 1 
ATOM   4376 N N   . GLY A 1 744 ? -7.993  63.884  59.643  1.00 92.06  ?  725 GLY A N   1 
ATOM   4377 C CA  . GLY A 1 744 ? -7.737  63.239  58.361  1.00 90.40  ?  725 GLY A CA  1 
ATOM   4378 C C   . GLY A 1 744 ? -7.154  61.844  58.505  1.00 89.10  ?  725 GLY A C   1 
ATOM   4379 O O   . GLY A 1 744 ? -7.644  60.885  57.896  1.00 87.57  ?  725 GLY A O   1 
ATOM   4380 N N   . ARG A 1 745 ? -6.096  61.711  59.313  1.00 82.87  ?  726 ARG A N   1 
ATOM   4381 C CA  . ARG A 1 745 ? -5.508  60.395  59.535  1.00 80.27  ?  726 ARG A CA  1 
ATOM   4382 C C   . ARG A 1 745 ? -6.508  59.446  60.181  1.00 87.86  ?  726 ARG A C   1 
ATOM   4383 O O   . ARG A 1 745 ? -6.508  58.242  59.891  1.00 90.47  ?  726 ARG A O   1 
ATOM   4384 C CB  . ARG A 1 745 ? -4.261  60.510  60.400  1.00 76.30  ?  726 ARG A CB  1 
ATOM   4385 C CG  . ARG A 1 745 ? -3.459  61.742  60.170  1.00 79.96  ?  726 ARG A CG  1 
ATOM   4386 C CD  . ARG A 1 745 ? -2.033  61.495  60.571  1.00 82.20  ?  726 ARG A CD  1 
ATOM   4387 N NE  . ARG A 1 745 ? -1.168  62.632  60.284  1.00 81.94  ?  726 ARG A NE  1 
ATOM   4388 C CZ  . ARG A 1 745 ? 0.067   62.752  60.758  1.00 89.97  ?  726 ARG A CZ  1 
ATOM   4389 N NH1 . ARG A 1 745 ? 0.565   61.799  61.535  1.00 96.69  ?  726 ARG A NH1 1 
ATOM   4390 N NH2 . ARG A 1 745 ? 0.805   63.816  60.464  1.00 84.64  ?  726 ARG A NH2 1 
ATOM   4391 N N   . CYS A 1 746 ? -7.355  59.968  61.075  1.00 84.70  ?  727 CYS A N   1 
ATOM   4392 C CA  . CYS A 1 746 ? -8.424  59.165  61.664  1.00 84.56  ?  727 CYS A CA  1 
ATOM   4393 C C   . CYS A 1 746 ? -9.371  58.633  60.606  1.00 87.26  ?  727 CYS A C   1 
ATOM   4394 O O   . CYS A 1 746 ? -9.788  57.471  60.656  1.00 85.16  ?  727 CYS A O   1 
ATOM   4395 C CB  . CYS A 1 746 ? -9.214  59.995  62.669  1.00 92.22  ?  727 CYS A CB  1 
ATOM   4396 S SG  . CYS A 1 746 ? -8.493  60.058  64.280  1.00 95.98  ?  727 CYS A SG  1 
ATOM   4397 N N   . LEU A 1 747 ? -9.756  59.496  59.662  1.00 94.85  ?  728 LEU A N   1 
ATOM   4398 C CA  . LEU A 1 747 ? -10.698 59.118  58.614  1.00 93.38  ?  728 LEU A CA  1 
ATOM   4399 C C   . LEU A 1 747 ? -10.069 58.111  57.664  1.00 90.40  ?  728 LEU A C   1 
ATOM   4400 O O   . LEU A 1 747 ? -10.679 57.079  57.343  1.00 85.65  ?  728 LEU A O   1 
ATOM   4401 C CB  . LEU A 1 747 ? -11.155 60.372  57.874  1.00 90.47  ?  728 LEU A CB  1 
ATOM   4402 C CG  . LEU A 1 747 ? -11.973 61.272  58.812  1.00 95.42  ?  728 LEU A CG  1 
ATOM   4403 C CD1 . LEU A 1 747 ? -12.298 62.643  58.194  1.00 93.20  ?  728 LEU A CD1 1 
ATOM   4404 C CD2 . LEU A 1 747 ? -13.232 60.549  59.324  1.00 94.82  ?  728 LEU A CD2 1 
ATOM   4405 N N   . ALA A 1 748 ? -8.839  58.398  57.217  1.00 86.10  ?  729 ALA A N   1 
ATOM   4406 C CA  . ALA A 1 748 ? -8.031  57.418  56.501  1.00 84.75  ?  729 ALA A CA  1 
ATOM   4407 C C   . ALA A 1 748 ? -8.108  56.045  57.168  1.00 87.48  ?  729 ALA A C   1 
ATOM   4408 O O   . ALA A 1 748 ? -8.638  55.088  56.592  1.00 89.29  ?  729 ALA A O   1 
ATOM   4409 C CB  . ALA A 1 748 ? -6.584  57.904  56.424  1.00 73.63  ?  729 ALA A CB  1 
ATOM   4410 N N   . ILE A 1 749 ? -7.601  55.941  58.397  1.00 81.40  ?  730 ILE A N   1 
ATOM   4411 C CA  . ILE A 1 749 ? -7.576  54.653  59.086  1.00 86.92  ?  730 ILE A CA  1 
ATOM   4412 C C   . ILE A 1 749 ? -8.957  54.006  59.064  1.00 90.11  ?  730 ILE A C   1 
ATOM   4413 O O   . ILE A 1 749 ? -9.102  52.824  58.729  1.00 92.34  ?  730 ILE A O   1 
ATOM   4414 C CB  . ILE A 1 749 ? -7.032  54.821  60.520  1.00 85.88  ?  730 ILE A CB  1 
ATOM   4415 C CG1 . ILE A 1 749 ? -5.542  55.176  60.474  1.00 87.10  ?  730 ILE A CG1 1 
ATOM   4416 C CG2 . ILE A 1 749 ? -7.253  53.565  61.363  1.00 71.79  ?  730 ILE A CG2 1 
ATOM   4417 C CD1 . ILE A 1 749 ? -4.958  55.641  61.787  1.00 81.53  ?  730 ILE A CD1 1 
ATOM   4418 N N   . LEU A 1 750 ? -9.998  54.783  59.363  1.00 86.97  ?  731 LEU A N   1 
ATOM   4419 C CA  . LEU A 1 750 ? -11.328 54.192  59.453  1.00 88.89  ?  731 LEU A CA  1 
ATOM   4420 C C   . LEU A 1 750 ? -11.841 53.757  58.078  1.00 99.64  ?  731 LEU A C   1 
ATOM   4421 O O   . LEU A 1 750 ? -12.558 52.748  57.972  1.00 97.28  ?  731 LEU A O   1 
ATOM   4422 C CB  . LEU A 1 750 ? -12.291 55.174  60.119  1.00 90.36  ?  731 LEU A CB  1 
ATOM   4423 C CG  . LEU A 1 750 ? -12.061 55.503  61.599  1.00 86.42  ?  731 LEU A CG  1 
ATOM   4424 C CD1 . LEU A 1 750 ? -12.848 56.746  61.966  1.00 88.17  ?  731 LEU A CD1 1 
ATOM   4425 C CD2 . LEU A 1 750 ? -12.435 54.354  62.517  1.00 80.77  ?  731 LEU A CD2 1 
ATOM   4426 N N   . LYS A 1 751 ? -11.486 54.505  57.018  1.00 98.45  ?  732 LYS A N   1 
ATOM   4427 C CA  . LYS A 1 751 ? -11.755 54.072  55.644  1.00 95.26  ?  732 LYS A CA  1 
ATOM   4428 C C   . LYS A 1 751 ? -11.194 52.675  55.387  1.00 96.50  ?  732 LYS A C   1 
ATOM   4429 O O   . LYS A 1 751 ? -11.928 51.749  55.020  1.00 98.32  ?  732 LYS A O   1 
ATOM   4430 C CB  . LYS A 1 751 ? -11.154 55.068  54.639  1.00 98.06  ?  732 LYS A CB  1 
ATOM   4431 C CG  . LYS A 1 751 ? -11.930 56.376  54.446  1.00 96.73  ?  732 LYS A CG  1 
ATOM   4432 C CD  . LYS A 1 751 ? -11.187 57.420  53.599  1.00 92.37  ?  732 LYS A CD  1 
ATOM   4433 C CE  . LYS A 1 751 ? -11.985 58.732  53.537  1.00 91.97  ?  732 LYS A CE  1 
ATOM   4434 N NZ  . LYS A 1 751 ? -13.463 58.525  53.769  1.00 91.70  ?  732 LYS A NZ  1 
ATOM   4435 N N   . GLY A 1 752 ? -9.880  52.509  55.593  1.00 93.25  ?  733 GLY A N   1 
ATOM   4436 C CA  . GLY A 1 752 ? -9.244  51.221  55.376  1.00 89.16  ?  733 GLY A CA  1 
ATOM   4437 C C   . GLY A 1 752 ? -9.912  50.059  56.089  1.00 94.46  ?  733 GLY A C   1 
ATOM   4438 O O   . GLY A 1 752 ? -9.869  48.925  55.604  1.00 103.29 ?  733 GLY A O   1 
ATOM   4439 N N   . ILE A 1 753 ? -10.538 50.332  57.224  1.00 91.57  ?  734 ILE A N   1 
ATOM   4440 C CA  . ILE A 1 753 ? -11.139 49.196  57.970  1.00 97.77  ?  734 ILE A CA  1 
ATOM   4441 C C   . ILE A 1 753 ? -12.593 49.033  57.566  1.00 96.61  ?  734 ILE A C   1 
ATOM   4442 O O   . ILE A 1 753 ? -13.098 47.948  57.737  1.00 101.90 ?  734 ILE A O   1 
ATOM   4443 C CB  . ILE A 1 753 ? -11.017 49.353  59.491  1.00 94.17  ?  734 ILE A CB  1 
ATOM   4444 C CG1 . ILE A 1 753 ? -9.617  49.015  59.991  1.00 95.60  ?  734 ILE A CG1 1 
ATOM   4445 C CG2 . ILE A 1 753 ? -12.041 48.478  60.167  1.00 87.14  ?  734 ILE A CG2 1 
ATOM   4446 C CD1 . ILE A 1 753 ? -8.554  49.945  59.480  1.00 94.31  ?  734 ILE A CD1 1 
ATOM   4447 N N   . PHE A 1 754 ? -13.258 50.084  57.118  1.00 95.55  ?  735 PHE A N   1 
ATOM   4448 C CA  . PHE A 1 754 ? -14.679 49.857  56.768  1.00 98.45  ?  735 PHE A CA  1 
ATOM   4449 C C   . PHE A 1 754 ? -14.976 50.263  55.331  1.00 95.98  ?  735 PHE A C   1 
ATOM   4450 O O   . PHE A 1 754 ? -16.109 50.100  54.916  1.00 95.50  ?  735 PHE A O   1 
ATOM   4451 C CB  . PHE A 1 754 ? -15.591 50.607  57.729  1.00 94.45  ?  735 PHE A CB  1 
ATOM   4452 C CG  . PHE A 1 754 ? -15.283 50.374  59.179  1.00 93.42  ?  735 PHE A CG  1 
ATOM   4453 C CD1 . PHE A 1 754 ? -14.393 51.183  59.846  1.00 92.67  ?  735 PHE A CD1 1 
ATOM   4454 C CD2 . PHE A 1 754 ? -15.899 49.358  59.874  1.00 92.03  ?  735 PHE A CD2 1 
ATOM   4455 C CE1 . PHE A 1 754 ? -14.119 50.971  61.181  1.00 92.32  ?  735 PHE A CE1 1 
ATOM   4456 C CE2 . PHE A 1 754 ? -15.624 49.149  61.209  1.00 92.72  ?  735 PHE A CE2 1 
ATOM   4457 C CZ  . PHE A 1 754 ? -14.734 49.956  61.858  1.00 92.42  ?  735 PHE A CZ  1 
ATOM   4458 N N   . GLY A 1 755 ? -14.002 50.826  54.631  1.00 90.72  ?  736 GLY A N   1 
ATOM   4459 C CA  . GLY A 1 755 ? -14.212 51.233  53.233  1.00 91.79  ?  736 GLY A CA  1 
ATOM   4460 C C   . GLY A 1 755 ? -14.638 52.677  53.123  1.00 98.99  ?  736 GLY A C   1 
ATOM   4461 O O   . GLY A 1 755 ? -15.475 53.096  53.899  1.00 96.69  ?  736 GLY A O   1 
ATOM   4462 N N   . SER A 1 756 ? -14.240 53.334  52.045  1.00 100.18 ?  737 SER A N   1 
ATOM   4463 C CA  . SER A 1 756 ? -14.485 54.782  51.872  1.00 95.69  ?  737 SER A CA  1 
ATOM   4464 C C   . SER A 1 756 ? -15.969 55.129  51.866  1.00 99.37  ?  737 SER A C   1 
ATOM   4465 O O   . SER A 1 756 ? -16.313 56.231  52.264  1.00 102.13 ?  737 SER A O   1 
ATOM   4466 C CB  . SER A 1 756 ? -13.789 55.271  50.666  1.00 92.63  ?  737 SER A CB  1 
ATOM   4467 O OG  . SER A 1 756 ? -12.474 54.757  50.660  1.00 98.25  ?  737 SER A OG  1 
ATOM   4468 N N   . SER A 1 757 ? -16.812 54.276  51.321  1.00 104.95 ?  738 SER A N   1 
ATOM   4469 C CA  . SER A 1 757 ? -18.242 54.648  51.300  1.00 110.16 ?  738 SER A CA  1 
ATOM   4470 C C   . SER A 1 757 ? -18.851 54.739  52.698  1.00 107.84 ?  738 SER A C   1 
ATOM   4471 O O   . SER A 1 757 ? -19.611 55.669  52.928  1.00 106.65 ?  738 SER A O   1 
ATOM   4472 C CB  . SER A 1 757 ? -19.025 53.696  50.467  1.00 109.90 ?  738 SER A CB  1 
ATOM   4473 O OG  . SER A 1 757 ? -20.399 53.777  50.806  1.00 114.52 ?  738 SER A OG  1 
ATOM   4474 N N   . ALA A 1 758 ? -18.519 53.817  53.594  1.00 105.13 ?  739 ALA A N   1 
ATOM   4475 C CA  . ALA A 1 758 ? -19.255 53.748  54.878  1.00 108.13 ?  739 ALA A CA  1 
ATOM   4476 C C   . ALA A 1 758 ? -18.785 54.726  55.956  1.00 109.76 ?  739 ALA A C   1 
ATOM   4477 O O   . ALA A 1 758 ? -19.367 54.703  57.024  1.00 107.77 ?  739 ALA A O   1 
ATOM   4478 C CB  . ALA A 1 758 ? -19.218 52.337  55.392  1.00 98.24  ?  739 ALA A CB  1 
ATOM   4479 N N   . VAL A 1 759 ? -17.807 55.572  55.687  1.00 110.39 ?  740 VAL A N   1 
ATOM   4480 C CA  . VAL A 1 759 ? -17.292 56.469  56.720  1.00 104.80 ?  740 VAL A CA  1 
ATOM   4481 C C   . VAL A 1 759 ? -17.496 57.917  56.266  1.00 103.06 ?  740 VAL A C   1 
ATOM   4482 O O   . VAL A 1 759 ? -16.786 58.418  55.376  1.00 100.51 ?  740 VAL A O   1 
ATOM   4483 C CB  . VAL A 1 759 ? -15.831 56.137  57.073  1.00 105.99 ?  740 VAL A CB  1 
ATOM   4484 C CG1 . VAL A 1 759 ? -14.897 56.301  55.877  1.00 102.72 ?  740 VAL A CG1 1 
ATOM   4485 C CG2 . VAL A 1 759 ? -15.345 56.928  58.272  1.00 106.70 ?  740 VAL A CG2 1 
ATOM   4486 N N   . PRO A 1 760 ? -18.462 58.622  56.861  1.00 103.85 ?  741 PRO A N   1 
ATOM   4487 C CA  . PRO A 1 760 ? -18.790 60.006  56.479  1.00 101.40 ?  741 PRO A CA  1 
ATOM   4488 C C   . PRO A 1 760 ? -17.874 61.030  57.140  1.00 103.78 ?  741 PRO A C   1 
ATOM   4489 O O   . PRO A 1 760 ? -17.027 60.668  57.983  1.00 107.40 ?  741 PRO A O   1 
ATOM   4490 C CB  . PRO A 1 760 ? -20.249 60.143  56.939  1.00 97.81  ?  741 PRO A CB  1 
ATOM   4491 C CG  . PRO A 1 760 ? -20.408 59.143  58.062  1.00 101.56 ?  741 PRO A CG  1 
ATOM   4492 C CD  . PRO A 1 760 ? -19.310 58.107  57.956  1.00 100.87 ?  741 PRO A CD  1 
ATOM   4493 N N   . GLN A 1 761 ? -18.066 62.315  56.785  1.00 101.29 ?  742 GLN A N   1 
ATOM   4494 C CA  . GLN A 1 761 ? -17.371 63.288  57.608  1.00 104.94 ?  742 GLN A CA  1 
ATOM   4495 C C   . GLN A 1 761 ? -17.960 63.302  59.023  1.00 110.65 ?  742 GLN A C   1 
ATOM   4496 O O   . GLN A 1 761 ? -19.157 63.000  59.243  1.00 109.44 ?  742 GLN A O   1 
ATOM   4497 C CB  . GLN A 1 761 ? -17.394 64.697  56.977  1.00 99.80  ?  742 GLN A CB  1 
ATOM   4498 C CG  . GLN A 1 761 ? -16.650 64.687  55.633  1.00 113.49 ?  742 GLN A CG  1 
ATOM   4499 C CD  . GLN A 1 761 ? -15.125 64.388  55.870  1.00 112.39 ?  742 GLN A CD  1 
ATOM   4500 O OE1 . GLN A 1 761 ? -14.629 63.356  55.383  1.00 109.60 ?  742 GLN A OE1 1 
ATOM   4501 N NE2 . GLN A 1 761 ? -14.370 65.318  56.324  1.00 110.84 ?  742 GLN A NE2 1 
ATOM   4502 N N   . PRO A 1 762 ? -17.123 63.626  60.008  1.00 105.40 ?  743 PRO A N   1 
ATOM   4503 C CA  . PRO A 1 762 ? -17.647 63.802  61.358  1.00 96.90  ?  743 PRO A CA  1 
ATOM   4504 C C   . PRO A 1 762 ? -18.351 65.140  61.524  1.00 96.00  ?  743 PRO A C   1 
ATOM   4505 O O   . PRO A 1 762 ? -17.873 66.179  61.061  1.00 93.01  ?  743 PRO A O   1 
ATOM   4506 C CB  . PRO A 1 762 ? -16.402 63.732  62.250  1.00 95.04  ?  743 PRO A CB  1 
ATOM   4507 C CG  . PRO A 1 762 ? -15.251 64.128  61.359  1.00 97.56  ?  743 PRO A CG  1 
ATOM   4508 C CD  . PRO A 1 762 ? -15.644 63.629  59.987  1.00 99.21  ?  743 PRO A CD  1 
ATOM   4509 N N   . LYS A 1 763 ? -19.517 65.108  62.179  1.00 93.85  ?  744 LYS A N   1 
ATOM   4510 C CA  . LYS A 1 763 ? -20.245 66.346  62.456  1.00 94.49  ?  744 LYS A CA  1 
ATOM   4511 C C   . LYS A 1 763 ? -19.453 67.256  63.392  1.00 98.15  ?  744 LYS A C   1 
ATOM   4512 O O   . LYS A 1 763 ? -19.253 68.441  63.099  1.00 98.26  ?  744 LYS A O   1 
ATOM   4513 C CB  . LYS A 1 763 ? -21.621 66.001  63.028  1.00 95.26  ?  744 LYS A CB  1 
ATOM   4514 C CG  . LYS A 1 763 ? -22.388 65.061  62.119  1.00 105.60 ?  744 LYS A CG  1 
ATOM   4515 C CD  . LYS A 1 763 ? -23.046 65.854  60.963  1.00 115.16 ?  744 LYS A CD  1 
ATOM   4516 C CE  . LYS A 1 763 ? -23.279 64.995  59.712  1.00 111.71 ?  744 LYS A CE  1 
ATOM   4517 N NZ  . LYS A 1 763 ? -23.673 65.801  58.533  1.00 108.69 ?  744 LYS A NZ  1 
ATOM   4518 N N   . GLU A 1 764 ? -18.985 66.710  64.523  1.00 102.31 ?  745 GLU A N   1 
ATOM   4519 C CA  . GLU A 1 764 ? -18.195 67.417  65.530  1.00 97.06  ?  745 GLU A CA  1 
ATOM   4520 C C   . GLU A 1 764 ? -16.894 66.666  65.819  1.00 91.84  ?  745 GLU A C   1 
ATOM   4521 O O   . GLU A 1 764 ? -16.898 65.438  65.968  1.00 87.82  ?  745 GLU A O   1 
ATOM   4522 C CB  . GLU A 1 764 ? -19.001 67.587  66.839  1.00 98.19  ?  745 GLU A CB  1 
ATOM   4523 C CG  . GLU A 1 764 ? -20.150 68.601  66.768  1.00 101.93 ?  745 GLU A CG  1 
ATOM   4524 C CD  . GLU A 1 764 ? -19.666 70.027  66.467  1.00 106.29 ?  745 GLU A CD  1 
ATOM   4525 O OE1 . GLU A 1 764 ? -18.711 70.488  67.136  1.00 105.59 ?  745 GLU A OE1 1 
ATOM   4526 O OE2 . GLU A 1 764 ? -20.248 70.695  65.574  1.00 110.46 ?  745 GLU A OE2 1 
ATOM   4527 N N   . THR A 1 765 ? -15.778 67.407  65.907  1.00 88.29  ?  746 THR A N   1 
ATOM   4528 C CA  . THR A 1 765 ? -14.486 66.836  66.285  1.00 87.36  ?  746 THR A CA  1 
ATOM   4529 C C   . THR A 1 765 ? -13.811 67.659  67.377  1.00 86.88  ?  746 THR A C   1 
ATOM   4530 O O   . THR A 1 765 ? -13.799 68.894  67.316  1.00 96.25  ?  746 THR A O   1 
ATOM   4531 C CB  . THR A 1 765 ? -13.517 66.753  65.106  1.00 83.73  ?  746 THR A CB  1 
ATOM   4532 O OG1 . THR A 1 765 ? -13.150 68.079  64.716  1.00 87.38  ?  746 THR A OG1 1 
ATOM   4533 C CG2 . THR A 1 765 ? -14.135 66.032  63.943  1.00 84.62  ?  746 THR A CG2 1 
ATOM   4534 N N   . VAL A 1 766 ? -13.210 66.956  68.347  1.00 83.05  ?  747 VAL A N   1 
ATOM   4535 C CA  . VAL A 1 766 ? -12.431 67.526  69.449  1.00 81.62  ?  747 VAL A CA  1 
ATOM   4536 C C   . VAL A 1 766 ? -11.121 66.756  69.573  1.00 77.15  ?  747 VAL A C   1 
ATOM   4537 O O   . VAL A 1 766 ? -11.129 65.520  69.584  1.00 81.86  ?  747 VAL A O   1 
ATOM   4538 C CB  . VAL A 1 766 ? -13.185 67.443  70.791  1.00 82.71  ?  747 VAL A CB  1 
ATOM   4539 C CG1 . VAL A 1 766 ? -12.438 68.190  71.842  1.00 79.19  ?  747 VAL A CG1 1 
ATOM   4540 C CG2 . VAL A 1 766 ? -14.584 67.970  70.658  1.00 88.71  ?  747 VAL A CG2 1 
ATOM   4541 N N   . VAL A 1 767 ? -10.010 67.472  69.723  1.00 69.56  ?  748 VAL A N   1 
ATOM   4542 C CA  . VAL A 1 767 ? -8.694  66.861  69.913  1.00 72.19  ?  748 VAL A CA  1 
ATOM   4543 C C   . VAL A 1 767 ? -8.062  67.432  71.177  1.00 75.43  ?  748 VAL A C   1 
ATOM   4544 O O   . VAL A 1 767 ? -7.829  68.643  71.251  1.00 83.11  ?  748 VAL A O   1 
ATOM   4545 C CB  . VAL A 1 767 ? -7.777  67.119  68.710  1.00 74.47  ?  748 VAL A CB  1 
ATOM   4546 C CG1 . VAL A 1 767 ? -6.407  66.530  68.949  1.00 74.33  ?  748 VAL A CG1 1 
ATOM   4547 C CG2 . VAL A 1 767 ? -8.387  66.551  67.453  1.00 78.31  ?  748 VAL A CG2 1 
ATOM   4548 N N   . SER A 1 768 ? -7.728  66.572  72.149  1.00 67.81  ?  749 SER A N   1 
ATOM   4549 C CA  . SER A 1 768 ? -7.125  67.068  73.390  1.00 66.77  ?  749 SER A CA  1 
ATOM   4550 C C   . SER A 1 768 ? -5.623  67.331  73.233  1.00 68.71  ?  749 SER A C   1 
ATOM   4551 O O   . SER A 1 768 ? -4.946  66.697  72.419  1.00 70.62  ?  749 SER A O   1 
ATOM   4552 C CB  . SER A 1 768 ? -7.291  66.074  74.532  1.00 56.75  ?  749 SER A CB  1 
ATOM   4553 O OG  . SER A 1 768 ? -6.348  65.043  74.372  1.00 56.23  ?  749 SER A OG  1 
ATOM   4554 N N   . ARG A 1 769 ? -5.084  68.264  74.070  1.00 60.93  ?  750 ARG A N   1 
ATOM   4555 C CA  . ARG A 1 769 ? -3.616  68.493  74.171  1.00 65.86  ?  750 ARG A CA  1 
ATOM   4556 C C   . ARG A 1 769 ? -3.200  68.701  75.633  1.00 68.54  ?  750 ARG A C   1 
ATOM   4557 O O   . ARG A 1 769 ? -2.895  69.812  76.080  1.00 72.10  ?  750 ARG A O   1 
ATOM   4558 C CB  . ARG A 1 769 ? -3.164  69.693  73.356  1.00 64.71  ?  750 ARG A CB  1 
ATOM   4559 C CG  . ARG A 1 769 ? -3.241  69.503  71.929  1.00 70.33  ?  750 ARG A CG  1 
ATOM   4560 C CD  . ARG A 1 769 ? -2.840  70.752  71.253  1.00 81.01  ?  750 ARG A CD  1 
ATOM   4561 N NE  . ARG A 1 769 ? -2.863  70.533  69.811  1.00 93.58  ?  750 ARG A NE  1 
ATOM   4562 C CZ  . ARG A 1 769 ? -3.976  70.540  69.085  1.00 96.06  ?  750 ARG A CZ  1 
ATOM   4563 N NH1 . ARG A 1 769 ? -5.168  70.685  69.688  1.00 93.30  ?  750 ARG A NH1 1 
ATOM   4564 N NH2 . ARG A 1 769 ? -3.904  70.350  67.791  1.00 88.45  ?  750 ARG A NH2 1 
ATOM   4565 N N   . TRP A 1 770 ? -3.126  67.607  76.384  1.00 65.11  ?  751 TRP A N   1 
ATOM   4566 C CA  . TRP A 1 770 ? -2.940  67.717  77.819  1.00 57.27  ?  751 TRP A CA  1 
ATOM   4567 C C   . TRP A 1 770 ? -1.567  68.262  78.166  1.00 61.97  ?  751 TRP A C   1 
ATOM   4568 O O   . TRP A 1 770 ? -1.424  69.012  79.141  1.00 64.28  ?  751 TRP A O   1 
ATOM   4569 C CB  . TRP A 1 770 ? -3.177  66.362  78.459  1.00 56.22  ?  751 TRP A CB  1 
ATOM   4570 C CG  . TRP A 1 770 ? -4.614  66.072  78.510  1.00 55.25  ?  751 TRP A CG  1 
ATOM   4571 C CD1 . TRP A 1 770 ? -5.321  65.248  77.687  1.00 56.95  ?  751 TRP A CD1 1 
ATOM   4572 C CD2 . TRP A 1 770 ? -5.553  66.651  79.410  1.00 58.45  ?  751 TRP A CD2 1 
ATOM   4573 N NE1 . TRP A 1 770 ? -6.653  65.257  78.042  1.00 56.71  ?  751 TRP A NE1 1 
ATOM   4574 C CE2 . TRP A 1 770 ? -6.822  66.117  79.094  1.00 57.44  ?  751 TRP A CE2 1 
ATOM   4575 C CE3 . TRP A 1 770 ? -5.441  67.556  80.474  1.00 52.01  ?  751 TRP A CE3 1 
ATOM   4576 C CZ2 . TRP A 1 770 ? -7.975  66.467  79.794  1.00 57.43  ?  751 TRP A CZ2 1 
ATOM   4577 C CZ3 . TRP A 1 770 ? -6.573  67.888  81.170  1.00 49.83  ?  751 TRP A CZ3 1 
ATOM   4578 C CH2 . TRP A 1 770 ? -7.830  67.345  80.831  1.00 56.21  ?  751 TRP A CH2 1 
ATOM   4579 N N   . ARG A 1 771 ? -0.540  67.906  77.397  1.00 61.06  ?  752 ARG A N   1 
ATOM   4580 C CA  . ARG A 1 771 ? 0.768   68.478  77.694  1.00 61.05  ?  752 ARG A CA  1 
ATOM   4581 C C   . ARG A 1 771 ? 0.773   69.981  77.423  1.00 64.58  ?  752 ARG A C   1 
ATOM   4582 O O   . ARG A 1 771 ? 1.425   70.748  78.145  1.00 62.42  ?  752 ARG A O   1 
ATOM   4583 C CB  . ARG A 1 771 ? 1.845   67.751  76.895  1.00 56.45  ?  752 ARG A CB  1 
ATOM   4584 C CG  . ARG A 1 771 ? 3.274   68.025  77.314  1.00 49.97  ?  752 ARG A CG  1 
ATOM   4585 C CD  . ARG A 1 771 ? 3.573   67.411  78.657  1.00 59.79  ?  752 ARG A CD  1 
ATOM   4586 N NE  . ARG A 1 771 ? 4.183   66.077  78.592  1.00 60.10  ?  752 ARG A NE  1 
ATOM   4587 C CZ  . ARG A 1 771 ? 4.217   65.237  79.626  1.00 56.30  ?  752 ARG A CZ  1 
ATOM   4588 N NH1 . ARG A 1 771 ? 3.684   65.598  80.773  1.00 59.37  ?  752 ARG A NH1 1 
ATOM   4589 N NH2 . ARG A 1 771 ? 4.775   64.039  79.529  1.00 64.18  ?  752 ARG A NH2 1 
ATOM   4590 N N   . ALA A 1 772 ? 0.010   70.426  76.423  1.00 71.79  ?  753 ALA A N   1 
ATOM   4591 C CA  . ALA A 1 772 ? -0.081  71.856  76.143  1.00 66.52  ?  753 ALA A CA  1 
ATOM   4592 C C   . ALA A 1 772 ? -0.869  72.596  77.223  1.00 66.49  ?  753 ALA A C   1 
ATOM   4593 O O   . ALA A 1 772 ? -0.531  73.737  77.560  1.00 70.14  ?  753 ALA A O   1 
ATOM   4594 C CB  . ALA A 1 772 ? -0.716  72.075  74.769  1.00 66.08  ?  753 ALA A CB  1 
ATOM   4595 N N   . ASP A 1 773 ? -1.935  71.981  77.754  1.00 63.76  ?  754 ASP A N   1 
ATOM   4596 C CA  . ASP A 1 773 ? -2.768  72.580  78.794  1.00 63.71  ?  754 ASP A CA  1 
ATOM   4597 C C   . ASP A 1 773 ? -1.907  73.148  79.927  1.00 64.62  ?  754 ASP A C   1 
ATOM   4598 O O   . ASP A 1 773 ? -1.113  72.409  80.530  1.00 66.53  ?  754 ASP A O   1 
ATOM   4599 C CB  . ASP A 1 773 ? -3.746  71.552  79.366  1.00 60.90  ?  754 ASP A CB  1 
ATOM   4600 C CG  . ASP A 1 773 ? -4.821  72.189  80.264  1.00 62.06  ?  754 ASP A CG  1 
ATOM   4601 O OD1 . ASP A 1 773 ? -4.735  73.416  80.546  1.00 64.54  ?  754 ASP A OD1 1 
ATOM   4602 O OD2 . ASP A 1 773 ? -5.761  71.460  80.676  1.00 56.90  ?  754 ASP A OD2 1 
ATOM   4603 N N   . PRO A 1 774 ? -2.032  74.433  80.249  1.00 62.75  ?  755 PRO A N   1 
ATOM   4604 C CA  . PRO A 1 774 ? -1.226  74.996  81.338  1.00 67.14  ?  755 PRO A CA  1 
ATOM   4605 C C   . PRO A 1 774 ? -1.660  74.592  82.755  1.00 61.83  ?  755 PRO A C   1 
ATOM   4606 O O   . PRO A 1 774 ? -0.901  74.862  83.701  1.00 61.20  ?  755 PRO A O   1 
ATOM   4607 C CB  . PRO A 1 774 ? -1.388  76.497  81.120  1.00 57.66  ?  755 PRO A CB  1 
ATOM   4608 C CG  . PRO A 1 774 ? -2.744  76.596  80.559  1.00 59.35  ?  755 PRO A CG  1 
ATOM   4609 C CD  . PRO A 1 774 ? -2.763  75.485  79.543  1.00 61.02  ?  755 PRO A CD  1 
ATOM   4610 N N   . TRP A 1 775 ? -2.840  73.998  82.937  1.00 54.69  ?  756 TRP A N   1 
ATOM   4611 C CA  . TRP A 1 775 ? -3.337  73.598  84.248  1.00 57.43  ?  756 TRP A CA  1 
ATOM   4612 C C   . TRP A 1 775 ? -3.162  72.100  84.491  1.00 63.09  ?  756 TRP A C   1 
ATOM   4613 O O   . TRP A 1 775 ? -3.727  71.549  85.446  1.00 62.03  ?  756 TRP A O   1 
ATOM   4614 C CB  . TRP A 1 775 ? -4.800  74.018  84.368  1.00 55.57  ?  756 TRP A CB  1 
ATOM   4615 C CG  . TRP A 1 775 ? -4.978  75.441  83.837  1.00 68.04  ?  756 TRP A CG  1 
ATOM   4616 C CD1 . TRP A 1 775 ? -5.780  75.851  82.798  1.00 65.29  ?  756 TRP A CD1 1 
ATOM   4617 C CD2 . TRP A 1 775 ? -4.329  76.636  84.328  1.00 67.32  ?  756 TRP A CD2 1 
ATOM   4618 N NE1 . TRP A 1 775 ? -5.669  77.211  82.627  1.00 66.87  ?  756 TRP A NE1 1 
ATOM   4619 C CE2 . TRP A 1 775 ? -4.797  77.715  83.554  1.00 63.81  ?  756 TRP A CE2 1 
ATOM   4620 C CE3 . TRP A 1 775 ? -3.411  76.890  85.352  1.00 62.51  ?  756 TRP A CE3 1 
ATOM   4621 C CZ2 . TRP A 1 775 ? -4.374  79.017  83.765  1.00 62.98  ?  756 TRP A CZ2 1 
ATOM   4622 C CZ3 . TRP A 1 775 ? -2.995  78.184  85.554  1.00 64.51  ?  756 TRP A CZ3 1 
ATOM   4623 C CH2 . TRP A 1 775 ? -3.466  79.232  84.757  1.00 62.36  ?  756 TRP A CH2 1 
ATOM   4624 N N   . ALA A 1 776 ? -2.411  71.429  83.619  1.00 65.01  ?  757 ALA A N   1 
ATOM   4625 C CA  . ALA A 1 776 ? -2.147  70.000  83.696  1.00 55.36  ?  757 ALA A CA  1 
ATOM   4626 C C   . ALA A 1 776 ? -0.678  69.779  83.395  1.00 51.57  ?  757 ALA A C   1 
ATOM   4627 O O   . ALA A 1 776 ? 0.052   69.227  84.224  1.00 50.33  ?  757 ALA A O   1 
ATOM   4628 C CB  . ALA A 1 776 ? -3.013  69.225  82.705  1.00 54.60  ?  757 ALA A CB  1 
ATOM   4629 N N   . ARG A 1 777 ? -0.240  70.257  82.224  1.00 54.58  ?  758 ARG A N   1 
ATOM   4630 C CA  . ARG A 1 777 ? 1.116   70.056  81.716  1.00 54.71  ?  758 ARG A CA  1 
ATOM   4631 C C   . ARG A 1 777 ? 1.394   68.578  81.448  1.00 58.48  ?  758 ARG A C   1 
ATOM   4632 O O   . ARG A 1 777 ? 2.545   68.119  81.535  1.00 57.24  ?  758 ARG A O   1 
ATOM   4633 C CB  . ARG A 1 777 ? 2.177   70.641  82.650  1.00 52.94  ?  758 ARG A CB  1 
ATOM   4634 C CG  . ARG A 1 777 ? 2.150   72.168  82.845  1.00 63.80  ?  758 ARG A CG  1 
ATOM   4635 C CD  . ARG A 1 777 ? 2.185   72.886  81.507  1.00 70.37  ?  758 ARG A CD  1 
ATOM   4636 N NE  . ARG A 1 777 ? 2.871   74.176  81.492  1.00 78.64  ?  758 ARG A NE  1 
ATOM   4637 C CZ  . ARG A 1 777 ? 2.495   75.192  80.703  1.00 83.80  ?  758 ARG A CZ  1 
ATOM   4638 N NH1 . ARG A 1 777 ? 1.425   75.064  79.928  1.00 84.58  ?  758 ARG A NH1 1 
ATOM   4639 N NH2 . ARG A 1 777 ? 3.150   76.348  80.678  1.00 78.20  ?  758 ARG A NH2 1 
ATOM   4640 N N   . GLY A 1 778 ? 0.342   67.834  81.126  1.00 54.29  ?  759 GLY A N   1 
ATOM   4641 C CA  . GLY A 1 778 ? 0.426   66.395  80.994  1.00 54.37  ?  759 GLY A CA  1 
ATOM   4642 C C   . GLY A 1 778 ? -0.878  65.754  81.437  1.00 55.14  ?  759 GLY A C   1 
ATOM   4643 O O   . GLY A 1 778 ? -1.851  66.436  81.750  1.00 56.96  ?  759 GLY A O   1 
ATOM   4644 N N   . SER A 1 779 ? -0.881  64.420  81.467  1.00 55.83  ?  760 SER A N   1 
ATOM   4645 C CA  . SER A 1 779 ? -2.108  63.658  81.673  1.00 56.33  ?  760 SER A CA  1 
ATOM   4646 C C   . SER A 1 779 ? -2.173  62.959  83.030  1.00 55.80  ?  760 SER A C   1 
ATOM   4647 O O   . SER A 1 779 ? -3.092  63.231  83.793  1.00 57.18  ?  760 SER A O   1 
ATOM   4648 C CB  . SER A 1 779 ? -2.249  62.655  80.540  1.00 56.35  ?  760 SER A CB  1 
ATOM   4649 O OG  . SER A 1 779 ? -1.218  61.702  80.681  1.00 64.33  ?  760 SER A OG  1 
ATOM   4650 N N   . TYR A 1 780 ? -1.270  62.022  83.352  1.00 56.27  ?  761 TYR A N   1 
ATOM   4651 C CA  . TYR A 1 780 ? -1.108  61.565  84.731  1.00 57.56  ?  761 TYR A CA  1 
ATOM   4652 C C   . TYR A 1 780 ? 0.335   61.117  84.956  1.00 58.46  ?  761 TYR A C   1 
ATOM   4653 O O   . TYR A 1 780 ? 1.202   61.308  84.103  1.00 59.12  ?  761 TYR A O   1 
ATOM   4654 C CB  . TYR A 1 780 ? -2.104  60.469  85.110  1.00 55.23  ?  761 TYR A CB  1 
ATOM   4655 C CG  . TYR A 1 780 ? -2.357  59.445  84.065  1.00 65.98  ?  761 TYR A CG  1 
ATOM   4656 C CD1 . TYR A 1 780 ? -1.573  58.302  83.982  1.00 66.22  ?  761 TYR A CD1 1 
ATOM   4657 C CD2 . TYR A 1 780 ? -3.392  59.611  83.143  1.00 66.83  ?  761 TYR A CD2 1 
ATOM   4658 C CE1 . TYR A 1 780 ? -1.813  57.339  83.037  1.00 61.93  ?  761 TYR A CE1 1 
ATOM   4659 C CE2 . TYR A 1 780 ? -3.631  58.654  82.173  1.00 70.32  ?  761 TYR A CE2 1 
ATOM   4660 C CZ  . TYR A 1 780 ? -2.832  57.521  82.132  1.00 69.52  ?  761 TYR A CZ  1 
ATOM   4661 O OH  . TYR A 1 780 ? -3.051  56.560  81.192  1.00 68.07  ?  761 TYR A OH  1 
ATOM   4662 N N   . SER A 1 781 ? 0.606   60.565  86.133  1.00 58.72  ?  762 SER A N   1 
ATOM   4663 C CA  . SER A 1 781 ? 1.973   60.356  86.574  1.00 54.22  ?  762 SER A CA  1 
ATOM   4664 C C   . SER A 1 781 ? 2.316   58.893  86.403  1.00 56.04  ?  762 SER A C   1 
ATOM   4665 O O   . SER A 1 781 ? 1.438   58.051  86.239  1.00 60.08  ?  762 SER A O   1 
ATOM   4666 C CB  . SER A 1 781 ? 2.158   60.788  88.031  1.00 57.35  ?  762 SER A CB  1 
ATOM   4667 O OG  . SER A 1 781 ? 1.373   59.982  88.915  1.00 59.39  ?  762 SER A OG  1 
ATOM   4668 N N   . TYR A 1 782 ? 3.610   58.602  86.440  1.00 55.45  ?  763 TYR A N   1 
ATOM   4669 C CA  . TYR A 1 782 ? 4.102   57.267  86.158  1.00 55.40  ?  763 TYR A CA  1 
ATOM   4670 C C   . TYR A 1 782 ? 5.414   57.110  86.897  1.00 59.25  ?  763 TYR A C   1 
ATOM   4671 O O   . TYR A 1 782 ? 6.073   58.106  87.208  1.00 63.18  ?  763 TYR A O   1 
ATOM   4672 C CB  . TYR A 1 782 ? 4.300   57.053  84.667  1.00 50.62  ?  763 TYR A CB  1 
ATOM   4673 C CG  . TYR A 1 782 ? 5.469   57.802  84.073  1.00 51.71  ?  763 TYR A CG  1 
ATOM   4674 C CD1 . TYR A 1 782 ? 6.786   57.351  84.242  1.00 52.40  ?  763 TYR A CD1 1 
ATOM   4675 C CD2 . TYR A 1 782 ? 5.262   58.917  83.275  1.00 49.80  ?  763 TYR A CD2 1 
ATOM   4676 C CE1 . TYR A 1 782 ? 7.853   58.010  83.656  1.00 50.81  ?  763 TYR A CE1 1 
ATOM   4677 C CE2 . TYR A 1 782 ? 6.318   59.573  82.695  1.00 51.42  ?  763 TYR A CE2 1 
ATOM   4678 C CZ  . TYR A 1 782 ? 7.618   59.123  82.887  1.00 52.18  ?  763 TYR A CZ  1 
ATOM   4679 O OH  . TYR A 1 782 ? 8.682   59.828  82.316  1.00 55.91  ?  763 TYR A OH  1 
ATOM   4680 N N   . VAL A 1 783 ? 5.816   55.867  87.174  1.00 62.57  ?  764 VAL A N   1 
ATOM   4681 C CA  . VAL A 1 783 ? 7.000   55.658  88.007  1.00 60.31  ?  764 VAL A CA  1 
ATOM   4682 C C   . VAL A 1 783 ? 8.187   55.669  87.054  1.00 56.70  ?  764 VAL A C   1 
ATOM   4683 O O   . VAL A 1 783 ? 8.517   54.657  86.434  1.00 59.49  ?  764 VAL A O   1 
ATOM   4684 C CB  . VAL A 1 783 ? 6.947   54.370  88.831  1.00 56.87  ?  764 VAL A CB  1 
ATOM   4685 C CG1 . VAL A 1 783 ? 8.177   54.333  89.816  1.00 50.78  ?  764 VAL A CG1 1 
ATOM   4686 C CG2 . VAL A 1 783 ? 5.616   54.212  89.535  1.00 55.80  ?  764 VAL A CG2 1 
ATOM   4687 N N   . ALA A 1 784 ? 8.804   56.837  86.919  1.00 56.71  ?  765 ALA A N   1 
ATOM   4688 C CA  . ALA A 1 784 ? 9.951   56.996  86.051  1.00 51.30  ?  765 ALA A CA  1 
ATOM   4689 C C   . ALA A 1 784 ? 11.100  56.128  86.519  1.00 52.86  ?  765 ALA A C   1 
ATOM   4690 O O   . ALA A 1 784 ? 11.202  55.766  87.696  1.00 54.93  ?  765 ALA A O   1 
ATOM   4691 C CB  . ALA A 1 784 ? 10.389  58.445  86.032  1.00 58.44  ?  765 ALA A CB  1 
ATOM   4692 N N   . ALA A 1 785 ? 11.950  55.763  85.570  1.00 55.13  ?  766 ALA A N   1 
ATOM   4693 C CA  . ALA A 1 785 ? 13.197  55.106  85.925  1.00 65.49  ?  766 ALA A CA  1 
ATOM   4694 C C   . ALA A 1 785 ? 14.000  56.021  86.849  1.00 65.75  ?  766 ALA A C   1 
ATOM   4695 O O   . ALA A 1 785 ? 14.091  57.231  86.628  1.00 68.02  ?  766 ALA A O   1 
ATOM   4696 C CB  . ALA A 1 785 ? 13.982  54.748  84.655  1.00 64.24  ?  766 ALA A CB  1 
ATOM   4697 N N   . GLY A 1 786 ? 14.556  55.449  87.911  1.00 68.23  ?  767 GLY A N   1 
ATOM   4698 C CA  . GLY A 1 786 ? 15.227  56.252  88.914  1.00 67.72  ?  767 GLY A CA  1 
ATOM   4699 C C   . GLY A 1 786 ? 14.317  56.806  89.987  1.00 63.32  ?  767 GLY A C   1 
ATOM   4700 O O   . GLY A 1 786 ? 14.812  57.392  90.958  1.00 66.06  ?  767 GLY A O   1 
ATOM   4701 N N   . SER A 1 787 ? 13.008  56.659  89.836  1.00 58.19  ?  768 SER A N   1 
ATOM   4702 C CA  . SER A 1 787 ? 12.042  56.992  90.865  1.00 61.15  ?  768 SER A CA  1 
ATOM   4703 C C   . SER A 1 787 ? 11.590  55.689  91.533  1.00 63.66  ?  768 SER A C   1 
ATOM   4704 O O   . SER A 1 787 ? 12.136  54.606  91.280  1.00 62.75  ?  768 SER A O   1 
ATOM   4705 C CB  . SER A 1 787 ? 10.874  57.786  90.246  1.00 59.74  ?  768 SER A CB  1 
ATOM   4706 O OG  . SER A 1 787 ? 9.924   58.276  91.196  1.00 55.14  ?  768 SER A OG  1 
ATOM   4707 N N   . SER A 1 788 ? 10.584  55.791  92.393  1.00 56.12  ?  769 SER A N   1 
ATOM   4708 C CA  . SER A 1 788 ? 10.008  54.617  93.028  1.00 58.74  ?  769 SER A CA  1 
ATOM   4709 C C   . SER A 1 788 ? 8.683   55.029  93.642  1.00 60.09  ?  769 SER A C   1 
ATOM   4710 O O   . SER A 1 788 ? 8.311   56.201  93.629  1.00 61.63  ?  769 SER A O   1 
ATOM   4711 C CB  . SER A 1 788 ? 10.911  54.045  94.114  1.00 55.67  ?  769 SER A CB  1 
ATOM   4712 O OG  . SER A 1 788 ? 10.761  54.822  95.267  1.00 57.55  ?  769 SER A OG  1 
ATOM   4713 N N   . GLY A 1 789 ? 7.970   54.056  94.199  1.00 66.41  ?  770 GLY A N   1 
ATOM   4714 C CA  . GLY A 1 789 ? 6.752   54.405  94.888  1.00 59.12  ?  770 GLY A CA  1 
ATOM   4715 C C   . GLY A 1 789 ? 6.991   55.184  96.148  1.00 59.56  ?  770 GLY A C   1 
ATOM   4716 O O   . GLY A 1 789 ? 6.052   55.785  96.685  1.00 61.93  ?  770 GLY A O   1 
ATOM   4717 N N   . ASN A 1 790 ? 8.224   55.192  96.643  1.00 62.35  ?  771 ASN A N   1 
ATOM   4718 C CA  . ASN A 1 790 ? 8.484   55.984  97.835  1.00 66.82  ?  771 ASN A CA  1 
ATOM   4719 C C   . ASN A 1 790 ? 8.422   57.486  97.539  1.00 61.01  ?  771 ASN A C   1 
ATOM   4720 O O   . ASN A 1 790 ? 8.092   58.276  98.426  1.00 61.38  ?  771 ASN A O   1 
ATOM   4721 C CB  . ASN A 1 790 ? 9.835   55.605  98.445  1.00 69.12  ?  771 ASN A CB  1 
ATOM   4722 C CG  . ASN A 1 790 ? 10.049  56.276  99.787  1.00 92.60  ?  771 ASN A CG  1 
ATOM   4723 O OD1 . ASN A 1 790 ? 10.957  57.120  99.944  1.00 83.27  ?  771 ASN A OD1 1 
ATOM   4724 N ND2 . ASN A 1 790 ? 9.206   55.914  100.777 1.00 91.40  ?  771 ASN A ND2 1 
ATOM   4725 N N   . ASP A 1 791 ? 8.743   57.899  96.310  1.00 59.20  ?  772 ASP A N   1 
ATOM   4726 C CA  . ASP A 1 791 ? 8.571   59.291  95.924  1.00 49.86  ?  772 ASP A CA  1 
ATOM   4727 C C   . ASP A 1 791 ? 7.132   59.744  96.057  1.00 54.28  ?  772 ASP A C   1 
ATOM   4728 O O   . ASP A 1 791 ? 6.871   60.917  96.345  1.00 54.54  ?  772 ASP A O   1 
ATOM   4729 C CB  . ASP A 1 791 ? 9.038   59.494  94.498  1.00 50.11  ?  772 ASP A CB  1 
ATOM   4730 C CG  . ASP A 1 791 ? 10.504  59.713  94.435  1.00 55.54  ?  772 ASP A CG  1 
ATOM   4731 O OD1 . ASP A 1 791 ? 11.087  59.859  95.544  1.00 57.15  ?  772 ASP A OD1 1 
ATOM   4732 O OD2 . ASP A 1 791 ? 11.066  59.735  93.310  1.00 56.04  ?  772 ASP A OD2 1 
ATOM   4733 N N   . TYR A 1 792 ? 6.183   58.845  95.842  1.00 56.53  ?  773 TYR A N   1 
ATOM   4734 C CA  . TYR A 1 792 ? 4.799   59.222  96.066  1.00 59.45  ?  773 TYR A CA  1 
ATOM   4735 C C   . TYR A 1 792 ? 4.554   59.533  97.544  1.00 58.14  ?  773 TYR A C   1 
ATOM   4736 O O   . TYR A 1 792 ? 3.699   60.355  97.876  1.00 62.20  ?  773 TYR A O   1 
ATOM   4737 C CB  . TYR A 1 792 ? 3.879   58.108  95.575  1.00 55.09  ?  773 TYR A CB  1 
ATOM   4738 C CG  . TYR A 1 792 ? 3.742   58.005  94.064  1.00 63.19  ?  773 TYR A CG  1 
ATOM   4739 C CD1 . TYR A 1 792 ? 4.607   57.202  93.308  1.00 63.10  ?  773 TYR A CD1 1 
ATOM   4740 C CD2 . TYR A 1 792 ? 2.737   58.690  93.388  1.00 63.13  ?  773 TYR A CD2 1 
ATOM   4741 C CE1 . TYR A 1 792 ? 4.454   57.077  91.914  1.00 63.77  ?  773 TYR A CE1 1 
ATOM   4742 C CE2 . TYR A 1 792 ? 2.581   58.580  92.005  1.00 64.16  ?  773 TYR A CE2 1 
ATOM   4743 C CZ  . TYR A 1 792 ? 3.435   57.775  91.262  1.00 68.72  ?  773 TYR A CZ  1 
ATOM   4744 O OH  . TYR A 1 792 ? 3.262   57.685  89.861  1.00 67.89  ?  773 TYR A OH  1 
ATOM   4745 N N   . ASP A 1 793 ? 5.306   58.916  98.446  1.00 58.68  ?  774 ASP A N   1 
ATOM   4746 C CA  . ASP A 1 793 ? 5.095   59.211  99.854  1.00 57.75  ?  774 ASP A CA  1 
ATOM   4747 C C   . ASP A 1 793 ? 5.698   60.550  100.213 1.00 59.07  ?  774 ASP A C   1 
ATOM   4748 O O   . ASP A 1 793 ? 5.130   61.291  101.023 1.00 62.74  ?  774 ASP A O   1 
ATOM   4749 C CB  . ASP A 1 793 ? 5.687   58.106  100.728 1.00 63.85  ?  774 ASP A CB  1 
ATOM   4750 C CG  . ASP A 1 793 ? 4.746   56.923  100.879 1.00 67.33  ?  774 ASP A CG  1 
ATOM   4751 O OD1 . ASP A 1 793 ? 5.210   55.813  101.268 1.00 68.34  ?  774 ASP A OD1 1 
ATOM   4752 O OD2 . ASP A 1 793 ? 3.537   57.130  100.574 1.00 69.02  ?  774 ASP A OD2 1 
ATOM   4753 N N   . LEU A 1 794 ? 6.845   60.867  99.613  1.00 55.78  ?  775 LEU A N   1 
ATOM   4754 C CA  . LEU A 1 794 ? 7.408   62.203  99.742  1.00 56.35  ?  775 LEU A CA  1 
ATOM   4755 C C   . LEU A 1 794 ? 6.431   63.273  99.256  1.00 59.03  ?  775 LEU A C   1 
ATOM   4756 O O   . LEU A 1 794 ? 6.202   64.269  99.948  1.00 62.97  ?  775 LEU A O   1 
ATOM   4757 C CB  . LEU A 1 794 ? 8.734   62.285  98.995  1.00 54.35  ?  775 LEU A CB  1 
ATOM   4758 C CG  . LEU A 1 794 ? 9.851   61.485  99.654  1.00 46.95  ?  775 LEU A CG  1 
ATOM   4759 C CD1 . LEU A 1 794 ? 11.177  61.864  99.030  1.00 57.01  ?  775 LEU A CD1 1 
ATOM   4760 C CD2 . LEU A 1 794 ? 9.862   61.804  101.107 1.00 45.10  ?  775 LEU A CD2 1 
ATOM   4761 N N   . MET A 1 795 ? 5.826   63.088  98.079  1.00 54.54  ?  776 MET A N   1 
ATOM   4762 C CA  . MET A 1 795 ? 4.863   64.085  97.626  1.00 52.67  ?  776 MET A CA  1 
ATOM   4763 C C   . MET A 1 795 ? 3.734   64.283  98.614  1.00 57.42  ?  776 MET A C   1 
ATOM   4764 O O   . MET A 1 795 ? 3.110   65.346  98.623  1.00 61.80  ?  776 MET A O   1 
ATOM   4765 C CB  . MET A 1 795 ? 4.250   63.715  96.275  1.00 58.06  ?  776 MET A CB  1 
ATOM   4766 C CG  . MET A 1 795 ? 5.258   63.597  95.161  1.00 62.71  ?  776 MET A CG  1 
ATOM   4767 S SD  . MET A 1 795 ? 6.026   65.173  94.811  1.00 72.48  ?  776 MET A SD  1 
ATOM   4768 C CE  . MET A 1 795 ? 4.585   66.260  94.761  1.00 61.40  ?  776 MET A CE  1 
ATOM   4769 N N   . ALA A 1 796 ? 3.449   63.299  99.452  1.00 62.42  ?  777 ALA A N   1 
ATOM   4770 C CA  . ALA A 1 796 ? 2.317   63.464  100.351 1.00 65.76  ?  777 ALA A CA  1 
ATOM   4771 C C   . ALA A 1 796 ? 2.679   64.108  101.698 1.00 62.37  ?  777 ALA A C   1 
ATOM   4772 O O   . ALA A 1 796 ? 1.759   64.516  102.414 1.00 62.91  ?  777 ALA A O   1 
ATOM   4773 C CB  . ALA A 1 796 ? 1.617   62.113  100.570 1.00 54.20  ?  777 ALA A CB  1 
ATOM   4774 N N   . GLN A 1 797 ? 3.973   64.235  102.063 1.00 54.83  ?  778 GLN A N   1 
ATOM   4775 C CA  . GLN A 1 797 ? 4.303   64.798  103.373 1.00 60.62  ?  778 GLN A CA  1 
ATOM   4776 C C   . GLN A 1 797 ? 4.036   66.298  103.376 1.00 67.35  ?  778 GLN A C   1 
ATOM   4777 O O   . GLN A 1 797 ? 4.447   67.002  102.433 1.00 57.48  ?  778 GLN A O   1 
ATOM   4778 C CB  . GLN A 1 797 ? 5.754   64.531  103.799 1.00 60.56  ?  778 GLN A CB  1 
ATOM   4779 C CG  . GLN A 1 797 ? 6.001   63.066  104.121 1.00 78.07  ?  778 GLN A CG  1 
ATOM   4780 C CD  . GLN A 1 797 ? 4.902   62.435  105.018 1.00 94.04  ?  778 GLN A CD  1 
ATOM   4781 O OE1 . GLN A 1 797 ? 4.175   61.512  104.569 1.00 85.70  ?  778 GLN A OE1 1 
ATOM   4782 N NE2 . GLN A 1 797 ? 4.816   62.884  106.294 1.00 87.93  ?  778 GLN A NE2 1 
ATOM   4783 N N   . PRO A 1 798 ? 3.341   66.817  104.396 1.00 63.00  ?  779 PRO A N   1 
ATOM   4784 C CA  . PRO A 1 798 ? 3.100   68.261  104.488 1.00 62.31  ?  779 PRO A CA  1 
ATOM   4785 C C   . PRO A 1 798 ? 4.370   69.024  104.825 1.00 58.38  ?  779 PRO A C   1 
ATOM   4786 O O   . PRO A 1 798 ? 5.390   68.454  105.249 1.00 51.93  ?  779 PRO A O   1 
ATOM   4787 C CB  . PRO A 1 798 ? 2.075   68.376  105.615 1.00 63.44  ?  779 PRO A CB  1 
ATOM   4788 C CG  . PRO A 1 798 ? 2.296   67.185  106.423 1.00 61.24  ?  779 PRO A CG  1 
ATOM   4789 C CD  . PRO A 1 798 ? 2.665   66.088  105.475 1.00 55.96  ?  779 PRO A CD  1 
ATOM   4790 N N   . ILE A 1 799 ? 4.284   70.346  104.642 1.00 52.54  ?  780 ILE A N   1 
ATOM   4791 C CA  . ILE A 1 799 ? 5.397   71.248  104.917 1.00 59.54  ?  780 ILE A CA  1 
ATOM   4792 C C   . ILE A 1 799 ? 5.145   72.037  106.198 1.00 58.22  ?  780 ILE A C   1 
ATOM   4793 O O   . ILE A 1 799 ? 4.033   72.525  106.452 1.00 56.62  ?  780 ILE A O   1 
ATOM   4794 C CB  . ILE A 1 799 ? 5.654   72.191  103.736 1.00 60.72  ?  780 ILE A CB  1 
ATOM   4795 C CG1 . ILE A 1 799 ? 5.794   71.356  102.467 1.00 52.61  ?  780 ILE A CG1 1 
ATOM   4796 C CG2 . ILE A 1 799 ? 6.915   73.022  104.007 1.00 59.04  ?  780 ILE A CG2 1 
ATOM   4797 C CD1 . ILE A 1 799 ? 7.062   70.576  102.465 1.00 50.49  ?  780 ILE A CD1 1 
ATOM   4798 N N   . THR A 1 800 ? 6.183   72.130  107.022 1.00 63.59  ?  781 THR A N   1 
ATOM   4799 C CA  . THR A 1 800 ? 6.133   72.873  108.270 1.00 64.26  ?  781 THR A CA  1 
ATOM   4800 C C   . THR A 1 800 ? 7.122   74.018  108.160 1.00 64.07  ?  781 THR A C   1 
ATOM   4801 O O   . THR A 1 800 ? 8.336   73.771  108.033 1.00 63.06  ?  781 THR A O   1 
ATOM   4802 C CB  . THR A 1 800 ? 6.465   71.992  109.478 1.00 61.77  ?  781 THR A CB  1 
ATOM   4803 O OG1 . THR A 1 800 ? 5.331   71.171  109.811 1.00 62.75  ?  781 THR A OG1 1 
ATOM   4804 C CG2 . THR A 1 800 ? 6.823   72.852  110.658 1.00 68.64  ?  781 THR A CG2 1 
ATOM   4805 N N   . PRO A 1 801 ? 6.650   75.264  108.192 1.00 66.36  ?  782 PRO A N   1 
ATOM   4806 C CA  . PRO A 1 801 ? 7.555   76.417  108.089 1.00 62.83  ?  782 PRO A CA  1 
ATOM   4807 C C   . PRO A 1 801 ? 8.450   76.514  109.312 1.00 68.77  ?  782 PRO A C   1 
ATOM   4808 O O   . PRO A 1 801 ? 8.140   75.989  110.385 1.00 70.84  ?  782 PRO A O   1 
ATOM   4809 C CB  . PRO A 1 801 ? 6.593   77.599  108.038 1.00 61.85  ?  782 PRO A CB  1 
ATOM   4810 C CG  . PRO A 1 801 ? 5.398   77.107  108.841 1.00 61.30  ?  782 PRO A CG  1 
ATOM   4811 C CD  . PRO A 1 801 ? 5.269   75.657  108.528 1.00 59.61  ?  782 PRO A CD  1 
ATOM   4812 N N   . GLY A 1 802 ? 9.571   77.212  109.153 1.00 71.09  ?  783 GLY A N   1 
ATOM   4813 C CA  . GLY A 1 802 ? 10.395  77.542  110.299 1.00 75.39  ?  783 GLY A CA  1 
ATOM   4814 C C   . GLY A 1 802 ? 9.671   78.456  111.281 1.00 79.07  ?  783 GLY A C   1 
ATOM   4815 O O   . GLY A 1 802 ? 8.602   79.006  110.985 1.00 79.40  ?  783 GLY A O   1 
ATOM   4816 N N   . PRO A 1 803 ? 10.244  78.655  112.465 1.00 81.36  ?  784 PRO A N   1 
ATOM   4817 C CA  . PRO A 1 803 ? 9.617   79.572  113.426 1.00 83.67  ?  784 PRO A CA  1 
ATOM   4818 C C   . PRO A 1 803 ? 9.789   81.026  112.999 1.00 87.74  ?  784 PRO A C   1 
ATOM   4819 O O   . PRO A 1 803 ? 10.806  81.409  112.411 1.00 81.28  ?  784 PRO A O   1 
ATOM   4820 C CB  . PRO A 1 803 ? 10.358  79.283  114.737 1.00 81.58  ?  784 PRO A CB  1 
ATOM   4821 C CG  . PRO A 1 803 ? 11.677  78.679  114.315 1.00 84.59  ?  784 PRO A CG  1 
ATOM   4822 C CD  . PRO A 1 803 ? 11.595  78.236  112.878 1.00 75.80  ?  784 PRO A CD  1 
ATOM   4823 N N   . SER A 1 804 ? 8.760   81.836  113.285 1.00 95.47  ?  785 SER A N   1 
ATOM   4824 C CA  . SER A 1 804 ? 8.832   83.288  113.099 1.00 96.02  ?  785 SER A CA  1 
ATOM   4825 C C   . SER A 1 804 ? 9.933   83.844  113.990 1.00 99.07  ?  785 SER A C   1 
ATOM   4826 O O   . SER A 1 804 ? 10.978  84.306  113.506 1.00 87.31  ?  785 SER A O   1 
ATOM   4827 C CB  . SER A 1 804 ? 7.504   83.981  113.451 1.00 90.73  ?  785 SER A CB  1 
ATOM   4828 O OG  . SER A 1 804 ? 6.454   83.734  112.526 1.00 81.11  ?  785 SER A OG  1 
ATOM   4829 N N   . ILE A 1 805 ? 9.689   83.771  115.301 1.00 103.76 ?  786 ILE A N   1 
ATOM   4830 C CA  . ILE A 1 805 ? 10.596  84.263  116.334 1.00 103.04 ?  786 ILE A CA  1 
ATOM   4831 C C   . ILE A 1 805 ? 11.621  83.151  116.512 1.00 103.48 ?  786 ILE A C   1 
ATOM   4832 O O   . ILE A 1 805 ? 11.220  82.004  116.764 1.00 101.17 ?  786 ILE A O   1 
ATOM   4833 C CB  . ILE A 1 805 ? 9.885   84.520  117.674 1.00 101.57 ?  786 ILE A CB  1 
ATOM   4834 C CG1 . ILE A 1 805 ? 8.616   85.358  117.511 1.00 102.09 ?  786 ILE A CG1 1 
ATOM   4835 C CG2 . ILE A 1 805 ? 10.814  85.277  118.585 1.00 100.79 ?  786 ILE A CG2 1 
ATOM   4836 C CD1 . ILE A 1 805 ? 7.345   84.489  117.331 1.00 100.91 ?  786 ILE A CD1 1 
ATOM   4837 N N   . PRO A 1 806 ? 12.925  83.402  116.394 1.00 109.33 ?  787 PRO A N   1 
ATOM   4838 C CA  . PRO A 1 806 ? 13.884  82.325  116.684 1.00 109.33 ?  787 PRO A CA  1 
ATOM   4839 C C   . PRO A 1 806 ? 13.843  81.951  118.168 1.00 106.45 ?  787 PRO A C   1 
ATOM   4840 O O   . PRO A 1 806 ? 13.647  82.804  119.048 1.00 89.28  ?  787 PRO A O   1 
ATOM   4841 C CB  . PRO A 1 806 ? 15.241  82.908  116.252 1.00 98.81  ?  787 PRO A CB  1 
ATOM   4842 C CG  . PRO A 1 806 ? 15.057  84.380  116.320 1.00 106.46 ?  787 PRO A CG  1 
ATOM   4843 C CD  . PRO A 1 806 ? 13.591  84.673  116.062 1.00 104.63 ?  787 PRO A CD  1 
ATOM   4844 N N   . GLY A 1 807 ? 13.974  80.641  118.425 1.00 103.50 ?  788 GLY A N   1 
ATOM   4845 C CA  . GLY A 1 807 ? 13.752  80.063  119.736 1.00 99.12  ?  788 GLY A CA  1 
ATOM   4846 C C   . GLY A 1 807 ? 12.297  79.930  120.147 1.00 99.04  ?  788 GLY A C   1 
ATOM   4847 O O   . GLY A 1 807 ? 12.023  79.622  121.314 1.00 97.91  ?  788 GLY A O   1 
ATOM   4848 N N   . ALA A 1 808 ? 11.356  80.180  119.242 1.00 95.49  ?  789 ALA A N   1 
ATOM   4849 C CA  . ALA A 1 808 ? 9.957   79.963  119.525 1.00 86.91  ?  789 ALA A CA  1 
ATOM   4850 C C   . ALA A 1 808 ? 9.633   78.488  119.326 1.00 96.84  ?  789 ALA A C   1 
ATOM   4851 O O   . ALA A 1 808 ? 10.380  77.769  118.652 1.00 95.13  ?  789 ALA A O   1 
ATOM   4852 C CB  . ALA A 1 808 ? 9.097   80.832  118.617 1.00 92.26  ?  789 ALA A CB  1 
ATOM   4853 N N   . PRO A 1 809 ? 8.531   78.005  119.909 1.00 97.30  ?  790 PRO A N   1 
ATOM   4854 C CA  . PRO A 1 809 ? 8.217   76.577  119.801 1.00 87.58  ?  790 PRO A CA  1 
ATOM   4855 C C   . PRO A 1 809 ? 7.947   76.182  118.358 1.00 93.95  ?  790 PRO A C   1 
ATOM   4856 O O   . PRO A 1 809 ? 7.304   76.921  117.594 1.00 85.77  ?  790 PRO A O   1 
ATOM   4857 C CB  . PRO A 1 809 ? 6.970   76.424  120.679 1.00 85.73  ?  790 PRO A CB  1 
ATOM   4858 C CG  . PRO A 1 809 ? 6.295   77.758  120.580 1.00 91.23  ?  790 PRO A CG  1 
ATOM   4859 C CD  . PRO A 1 809 ? 7.457   78.730  120.626 1.00 98.09  ?  790 PRO A CD  1 
ATOM   4860 N N   . GLN A 1 810 ? 8.483   75.006  118.000 1.00 95.57  ?  791 GLN A N   1 
ATOM   4861 C CA  . GLN A 1 810 ? 8.319   74.257  116.756 1.00 91.97  ?  791 GLN A CA  1 
ATOM   4862 C C   . GLN A 1 810 ? 6.874   74.296  116.254 1.00 88.71  ?  791 GLN A C   1 
ATOM   4863 O O   . GLN A 1 810 ? 5.960   73.791  116.926 1.00 82.54  ?  791 GLN A O   1 
ATOM   4864 C CB  . GLN A 1 810 ? 8.831   72.835  117.008 1.00 81.79  ?  791 GLN A CB  1 
ATOM   4865 C CG  . GLN A 1 810 ? 8.365   71.741  116.058 1.00 88.61  ?  791 GLN A CG  1 
ATOM   4866 C CD  . GLN A 1 810 ? 8.771   71.937  114.612 1.00 91.28  ?  791 GLN A CD  1 
ATOM   4867 O OE1 . GLN A 1 810 ? 7.907   72.133  113.756 1.00 95.95  ?  791 GLN A OE1 1 
ATOM   4868 N NE2 . GLN A 1 810 ? 10.082  71.884  114.326 1.00 89.83  ?  791 GLN A NE2 1 
ATOM   4869 N N   . PRO A 1 811 ? 6.622   74.911  115.099 1.00 89.15  ?  792 PRO A N   1 
ATOM   4870 C CA  . PRO A 1 811 ? 5.237   75.147  114.674 1.00 90.77  ?  792 PRO A CA  1 
ATOM   4871 C C   . PRO A 1 811 ? 4.560   73.939  114.014 1.00 84.22  ?  792 PRO A C   1 
ATOM   4872 O O   . PRO A 1 811 ? 5.133   72.876  113.775 1.00 77.18  ?  792 PRO A O   1 
ATOM   4873 C CB  . PRO A 1 811 ? 5.358   76.330  113.691 1.00 79.78  ?  792 PRO A CB  1 
ATOM   4874 C CG  . PRO A 1 811 ? 6.752   76.224  113.160 1.00 77.07  ?  792 PRO A CG  1 
ATOM   4875 C CD  . PRO A 1 811 ? 7.587   75.707  114.308 1.00 79.42  ?  792 PRO A CD  1 
ATOM   4876 N N   . ILE A 1 812 ? 3.286   74.170  113.725 1.00 86.48  ?  793 ILE A N   1 
ATOM   4877 C CA  . ILE A 1 812 ? 2.257   73.325  113.138 1.00 72.54  ?  793 ILE A CA  1 
ATOM   4878 C C   . ILE A 1 812 ? 2.644   73.123  111.671 1.00 71.55  ?  793 ILE A C   1 
ATOM   4879 O O   . ILE A 1 812 ? 3.373   73.952  111.114 1.00 66.54  ?  793 ILE A O   1 
ATOM   4880 C CB  . ILE A 1 812 ? 0.905   74.060  113.263 1.00 76.39  ?  793 ILE A CB  1 
ATOM   4881 C CG1 . ILE A 1 812 ? 0.639   74.523  114.700 1.00 80.70  ?  793 ILE A CG1 1 
ATOM   4882 C CG2 . ILE A 1 812 ? -0.247  73.261  112.784 1.00 81.17  ?  793 ILE A CG2 1 
ATOM   4883 C CD1 . ILE A 1 812 ? 1.151   76.014  114.976 1.00 77.36  ?  793 ILE A CD1 1 
ATOM   4884 N N   . PRO A 1 813 ? 2.204   72.059  110.996 1.00 79.83  ?  794 PRO A N   1 
ATOM   4885 C CA  . PRO A 1 813 ? 2.336   72.025  109.533 1.00 69.70  ?  794 PRO A CA  1 
ATOM   4886 C C   . PRO A 1 813 ? 1.255   72.870  108.866 1.00 65.48  ?  794 PRO A C   1 
ATOM   4887 O O   . PRO A 1 813 ? 0.099   72.893  109.308 1.00 63.46  ?  794 PRO A O   1 
ATOM   4888 C CB  . PRO A 1 813 ? 2.162   70.534  109.214 1.00 61.39  ?  794 PRO A CB  1 
ATOM   4889 C CG  . PRO A 1 813 ? 2.496   69.866  110.509 1.00 58.61  ?  794 PRO A CG  1 
ATOM   4890 C CD  . PRO A 1 813 ? 1.874   70.718  111.507 1.00 68.01  ?  794 PRO A CD  1 
ATOM   4891 N N   . ARG A 1 814 ? 1.635   73.553  107.776 1.00 59.04  ?  795 ARG A N   1 
ATOM   4892 C CA  . ARG A 1 814 ? 0.765   74.550  107.158 1.00 59.62  ?  795 ARG A CA  1 
ATOM   4893 C C   . ARG A 1 814 ? 0.425   74.286  105.696 1.00 57.39  ?  795 ARG A C   1 
ATOM   4894 O O   . ARG A 1 814 ? -0.607  74.784  105.217 1.00 55.06  ?  795 ARG A O   1 
ATOM   4895 C CB  . ARG A 1 814 ? 1.406   75.947  107.252 1.00 60.83  ?  795 ARG A CB  1 
ATOM   4896 C CG  . ARG A 1 814 ? 1.629   76.493  108.677 1.00 60.94  ?  795 ARG A CG  1 
ATOM   4897 C CD  . ARG A 1 814 ? 0.415   77.240  109.158 1.00 58.00  ?  795 ARG A CD  1 
ATOM   4898 N NE  . ARG A 1 814 ? 0.606   77.706  110.523 1.00 67.41  ?  795 ARG A NE  1 
ATOM   4899 C CZ  . ARG A 1 814 ? -0.376  78.088  111.338 1.00 69.88  ?  795 ARG A CZ  1 
ATOM   4900 N NH1 . ARG A 1 814 ? -1.649  78.029  110.942 1.00 66.78  ?  795 ARG A NH1 1 
ATOM   4901 N NH2 . ARG A 1 814 ? -0.079  78.521  112.559 1.00 65.36  ?  795 ARG A NH2 1 
ATOM   4902 N N   . LEU A 1 815 ? 1.264   73.545  104.969 1.00 56.19  ?  796 LEU A N   1 
ATOM   4903 C CA  . LEU A 1 815 ? 1.112   73.308  103.531 1.00 57.82  ?  796 LEU A CA  1 
ATOM   4904 C C   . LEU A 1 815 ? 1.001   71.806  103.272 1.00 57.91  ?  796 LEU A C   1 
ATOM   4905 O O   . LEU A 1 815 ? 1.947   71.053  103.543 1.00 54.45  ?  796 LEU A O   1 
ATOM   4906 C CB  . LEU A 1 815 ? 2.293   73.905  102.763 1.00 53.12  ?  796 LEU A CB  1 
ATOM   4907 C CG  . LEU A 1 815 ? 2.294   73.737  101.252 1.00 52.59  ?  796 LEU A CG  1 
ATOM   4908 C CD1 . LEU A 1 815 ? 0.973   74.260  100.656 1.00 52.23  ?  796 LEU A CD1 1 
ATOM   4909 C CD2 . LEU A 1 815 ? 3.529   74.413  100.605 1.00 44.24  ?  796 LEU A CD2 1 
ATOM   4910 N N   . PHE A 1 816 ? -0.154  71.379  102.755 1.00 57.15  ?  797 PHE A N   1 
ATOM   4911 C CA  . PHE A 1 816 ? -0.511  69.977  102.568 1.00 60.29  ?  797 PHE A CA  1 
ATOM   4912 C C   . PHE A 1 816 ? -0.737  69.664  101.084 1.00 56.50  ?  797 PHE A C   1 
ATOM   4913 O O   . PHE A 1 816 ? -1.222  70.513  100.330 1.00 59.10  ?  797 PHE A O   1 
ATOM   4914 C CB  . PHE A 1 816 ? -1.779  69.644  103.371 1.00 59.68  ?  797 PHE A CB  1 
ATOM   4915 C CG  . PHE A 1 816 ? -1.674  69.945  104.844 1.00 62.49  ?  797 PHE A CG  1 
ATOM   4916 C CD1 . PHE A 1 816 ? -1.757  71.243  105.322 1.00 63.61  ?  797 PHE A CD1 1 
ATOM   4917 C CD2 . PHE A 1 816 ? -1.525  68.912  105.766 1.00 68.26  ?  797 PHE A CD2 1 
ATOM   4918 C CE1 . PHE A 1 816 ? -1.675  71.507  106.695 1.00 60.34  ?  797 PHE A CE1 1 
ATOM   4919 C CE2 . PHE A 1 816 ? -1.430  69.172  107.135 1.00 62.36  ?  797 PHE A CE2 1 
ATOM   4920 C CZ  . PHE A 1 816 ? -1.508  70.463  107.597 1.00 61.96  ?  797 PHE A CZ  1 
ATOM   4921 N N   . PHE A 1 817 ? -0.425  68.434  100.651 1.00 60.56  ?  798 PHE A N   1 
ATOM   4922 C CA  . PHE A 1 817 ? -0.545  68.076  99.233  1.00 57.10  ?  798 PHE A CA  1 
ATOM   4923 C C   . PHE A 1 817 ? -1.486  66.900  98.997  1.00 54.66  ?  798 PHE A C   1 
ATOM   4924 O O   . PHE A 1 817 ? -1.337  65.849  99.623  1.00 57.16  ?  798 PHE A O   1 
ATOM   4925 C CB  . PHE A 1 817 ? 0.813   67.734  98.632  1.00 53.49  ?  798 PHE A CB  1 
ATOM   4926 C CG  . PHE A 1 817 ? 1.822   68.795  98.806  1.00 60.96  ?  798 PHE A CG  1 
ATOM   4927 C CD1 . PHE A 1 817 ? 2.057   69.707  97.787  1.00 60.80  ?  798 PHE A CD1 1 
ATOM   4928 C CD2 . PHE A 1 817 ? 2.542   68.895  99.985  1.00 60.41  ?  798 PHE A CD2 1 
ATOM   4929 C CE1 . PHE A 1 817 ? 2.986   70.713  97.929  1.00 51.90  ?  798 PHE A CE1 1 
ATOM   4930 C CE2 . PHE A 1 817 ? 3.490   69.897  100.137 1.00 61.93  ?  798 PHE A CE2 1 
ATOM   4931 C CZ  . PHE A 1 817 ? 3.723   70.799  99.098  1.00 53.69  ?  798 PHE A CZ  1 
ATOM   4932 N N   . ALA A 1 818 ? -2.320  67.022  97.984  1.00 55.07  ?  799 ALA A N   1 
ATOM   4933 C CA  . ALA A 1 818 ? -3.188  65.903  97.587  1.00 54.78  ?  799 ALA A CA  1 
ATOM   4934 C C   . ALA A 1 818 ? -3.166  65.770  96.072  1.00 51.76  ?  799 ALA A C   1 
ATOM   4935 O O   . ALA A 1 818 ? -2.476  66.505  95.420  1.00 55.56  ?  799 ALA A O   1 
ATOM   4936 C CB  . ALA A 1 818 ? -4.576  66.116  98.075  1.00 54.17  ?  799 ALA A CB  1 
ATOM   4937 N N   . GLY A 1 819 ? -3.924  64.828  95.545  1.00 61.10  ?  800 GLY A N   1 
ATOM   4938 C CA  . GLY A 1 819 ? -3.948  64.636  94.092  1.00 61.60  ?  800 GLY A CA  1 
ATOM   4939 C C   . GLY A 1 819 ? -3.465  63.266  93.710  1.00 58.36  ?  800 GLY A C   1 
ATOM   4940 O O   . GLY A 1 819 ? -2.900  62.613  94.526  1.00 51.89  ?  800 GLY A O   1 
ATOM   4941 N N   . GLU A 1 820 ? -3.543  62.953  92.436  1.00 58.02  ?  801 GLU A N   1 
ATOM   4942 C CA  . GLU A 1 820 ? -3.177  61.640  91.880  1.00 54.55  ?  801 GLU A CA  1 
ATOM   4943 C C   . GLU A 1 820 ? -1.727  61.279  92.180  1.00 57.03  ?  801 GLU A C   1 
ATOM   4944 O O   . GLU A 1 820 ? -1.479  60.151  92.418  1.00 55.75  ?  801 GLU A O   1 
ATOM   4945 C CB  . GLU A 1 820 ? -3.330  61.729  90.372  1.00 57.62  ?  801 GLU A CB  1 
ATOM   4946 C CG  . GLU A 1 820 ? -2.316  60.913  89.638  1.00 62.35  ?  801 GLU A CG  1 
ATOM   4947 C CD  . GLU A 1 820 ? -1.434  61.704  88.722  1.00 62.15  ?  801 GLU A CD  1 
ATOM   4948 O OE1 . GLU A 1 820 ? -0.397  61.195  88.352  1.00 75.07  ?  801 GLU A OE1 1 
ATOM   4949 O OE2 . GLU A 1 820 ? -1.786  62.803  88.415  1.00 62.19  ?  801 GLU A OE2 1 
ATOM   4950 N N   . HIS A 1 821 ? -0.801  62.217  92.199  1.00 54.32  ?  802 HIS A N   1 
ATOM   4951 C CA  . HIS A 1 821 ? 0.621   61.861  92.389  1.00 48.78  ?  802 HIS A CA  1 
ATOM   4952 C C   . HIS A 1 821 ? 1.005   61.720  93.852  1.00 53.83  ?  802 HIS A C   1 
ATOM   4953 O O   . HIS A 1 821 ? 2.172   61.590  94.105  1.00 55.70  ?  802 HIS A O   1 
ATOM   4954 C CB  . HIS A 1 821 ? 1.495   62.938  91.780  1.00 49.33  ?  802 HIS A CB  1 
ATOM   4955 C CG  . HIS A 1 821 ? 1.071   64.289  92.213  1.00 63.86  ?  802 HIS A CG  1 
ATOM   4956 N ND1 . HIS A 1 821 ? -0.184  64.738  92.008  1.00 60.57  ?  802 HIS A ND1 1 
ATOM   4957 C CD2 . HIS A 1 821 ? 1.714   65.261  92.878  1.00 55.95  ?  802 HIS A CD2 1 
ATOM   4958 C CE1 . HIS A 1 821 ? -0.301  65.928  92.517  1.00 52.95  ?  802 HIS A CE1 1 
ATOM   4959 N NE2 . HIS A 1 821 ? 0.834   66.264  93.055  1.00 54.96  ?  802 HIS A NE2 1 
ATOM   4960 N N   . THR A 1 822 ? 0.080   61.869  94.783  1.00 54.23  ?  803 THR A N   1 
ATOM   4961 C CA  . THR A 1 822 ? 0.462   61.765  96.202  1.00 59.32  ?  803 THR A CA  1 
ATOM   4962 C C   . THR A 1 822 ? 0.012   60.448  96.814  1.00 59.36  ?  803 THR A C   1 
ATOM   4963 O O   . THR A 1 822 ? 0.294   60.225  97.959  1.00 66.23  ?  803 THR A O   1 
ATOM   4964 C CB  . THR A 1 822 ? -0.214  62.883  96.974  1.00 61.34  ?  803 THR A CB  1 
ATOM   4965 O OG1 . THR A 1 822 ? -1.578  62.671  96.667  1.00 53.60  ?  803 THR A OG1 1 
ATOM   4966 C CG2 . THR A 1 822 ? 0.196   64.240  96.471  1.00 58.04  ?  803 THR A CG2 1 
ATOM   4967 N N   . ILE A 1 823 ? -0.637  59.589  96.062  1.00 59.42  ?  804 ILE A N   1 
ATOM   4968 C CA  . ILE A 1 823 ? -1.118  58.346  96.702  1.00 52.30  ?  804 ILE A CA  1 
ATOM   4969 C C   . ILE A 1 823 ? -0.384  57.153  96.111  1.00 58.47  ?  804 ILE A C   1 
ATOM   4970 O O   . ILE A 1 823 ? -0.694  56.763  95.028  1.00 57.22  ?  804 ILE A O   1 
ATOM   4971 C CB  . ILE A 1 823 ? -2.630  58.277  96.539  1.00 47.02  ?  804 ILE A CB  1 
ATOM   4972 C CG1 . ILE A 1 823 ? -3.232  57.150  97.354  1.00 55.25  ?  804 ILE A CG1 1 
ATOM   4973 C CG2 . ILE A 1 823 ? -2.997  58.187  95.091  1.00 47.16  ?  804 ILE A CG2 1 
ATOM   4974 C CD1 . ILE A 1 823 ? -4.688  57.320  97.553  1.00 54.93  ?  804 ILE A CD1 1 
ATOM   4975 N N   . ARG A 1 824 ? 0.551   56.608  96.875  1.00 65.02  ?  805 ARG A N   1 
ATOM   4976 C CA  . ARG A 1 824 ? 1.412   55.479  96.492  1.00 60.55  ?  805 ARG A CA  1 
ATOM   4977 C C   . ARG A 1 824 ? 0.645   54.311  95.892  1.00 57.95  ?  805 ARG A C   1 
ATOM   4978 O O   . ARG A 1 824 ? 0.981   53.825  94.810  1.00 61.40  ?  805 ARG A O   1 
ATOM   4979 C CB  . ARG A 1 824 ? 2.168   54.984  97.725  1.00 58.83  ?  805 ARG A CB  1 
ATOM   4980 C CG  . ARG A 1 824 ? 3.424   54.294  97.440  1.00 55.62  ?  805 ARG A CG  1 
ATOM   4981 C CD  . ARG A 1 824 ? 3.920   53.567  98.647  1.00 59.40  ?  805 ARG A CD  1 
ATOM   4982 N NE  . ARG A 1 824 ? 5.033   52.694  98.279  1.00 66.36  ?  805 ARG A NE  1 
ATOM   4983 C CZ  . ARG A 1 824 ? 6.282   52.829  98.722  1.00 65.50  ?  805 ARG A CZ  1 
ATOM   4984 N NH1 . ARG A 1 824 ? 6.601   53.796  99.587  1.00 65.90  ?  805 ARG A NH1 1 
ATOM   4985 N NH2 . ARG A 1 824 ? 7.213   51.988  98.293  1.00 61.89  ?  805 ARG A NH2 1 
ATOM   4986 N N   . ASN A 1 825 ? -0.355  53.806  96.604  1.00 61.64  ?  806 ASN A N   1 
ATOM   4987 C CA  . ASN A 1 825 ? -1.010  52.577  96.164  1.00 62.07  ?  806 ASN A CA  1 
ATOM   4988 C C   . ASN A 1 825 ? -2.098  52.777  95.112  1.00 61.72  ?  806 ASN A C   1 
ATOM   4989 O O   . ASN A 1 825 ? -2.669  51.772  94.662  1.00 64.49  ?  806 ASN A O   1 
ATOM   4990 C CB  . ASN A 1 825 ? -1.579  51.835  97.371  1.00 50.70  ?  806 ASN A CB  1 
ATOM   4991 C CG  . ASN A 1 825 ? -0.486  51.406  98.320  1.00 58.67  ?  806 ASN A CG  1 
ATOM   4992 O OD1 . ASN A 1 825 ? -0.753  50.907  99.408  1.00 59.59  ?  806 ASN A OD1 1 
ATOM   4993 N ND2 . ASN A 1 825 ? 0.778   51.585  97.897  1.00 60.19  ?  806 ASN A ND2 1 
ATOM   4994 N N   . TYR A 1 826 ? -2.426  54.027  94.720  1.00 50.38  ?  807 TYR A N   1 
ATOM   4995 C CA  . TYR A 1 826 ? -3.440  54.170  93.679  1.00 52.36  ?  807 TYR A CA  1 
ATOM   4996 C C   . TYR A 1 826 ? -3.176  55.348  92.757  1.00 50.35  ?  807 TYR A C   1 
ATOM   4997 O O   . TYR A 1 826 ? -4.114  56.102  92.457  1.00 49.53  ?  807 TYR A O   1 
ATOM   4998 C CB  . TYR A 1 826 ? -4.849  54.315  94.275  1.00 55.39  ?  807 TYR A CB  1 
ATOM   4999 C CG  . TYR A 1 826 ? -5.209  53.237  95.265  1.00 56.81  ?  807 TYR A CG  1 
ATOM   5000 C CD1 . TYR A 1 826 ? -5.994  52.147  94.902  1.00 62.47  ?  807 TYR A CD1 1 
ATOM   5001 C CD2 . TYR A 1 826 ? -4.741  53.297  96.562  1.00 60.44  ?  807 TYR A CD2 1 
ATOM   5002 C CE1 . TYR A 1 826 ? -6.301  51.151  95.829  1.00 68.46  ?  807 TYR A CE1 1 
ATOM   5003 C CE2 . TYR A 1 826 ? -5.020  52.300  97.478  1.00 66.94  ?  807 TYR A CE2 1 
ATOM   5004 C CZ  . TYR A 1 826 ? -5.804  51.245  97.121  1.00 65.87  ?  807 TYR A CZ  1 
ATOM   5005 O OH  . TYR A 1 826 ? -6.070  50.300  98.077  1.00 68.26  ?  807 TYR A OH  1 
ATOM   5006 N N   . PRO A 1 827 ? -1.955  55.514  92.245  1.00 53.38  ?  808 PRO A N   1 
ATOM   5007 C CA  . PRO A 1 827 ? -1.643  56.716  91.467  1.00 54.78  ?  808 PRO A CA  1 
ATOM   5008 C C   . PRO A 1 827 ? -2.386  56.751  90.148  1.00 51.76  ?  808 PRO A C   1 
ATOM   5009 O O   . PRO A 1 827 ? -3.056  55.807  89.752  1.00 57.05  ?  808 PRO A O   1 
ATOM   5010 C CB  . PRO A 1 827 ? -0.131  56.647  91.262  1.00 52.19  ?  808 PRO A CB  1 
ATOM   5011 C CG  . PRO A 1 827 ? 0.237   55.294  91.511  1.00 54.35  ?  808 PRO A CG  1 
ATOM   5012 C CD  . PRO A 1 827 ? -0.770  54.665  92.408  1.00 57.03  ?  808 PRO A CD  1 
ATOM   5013 N N   . ALA A 1 828 ? -2.343  57.934  89.539  1.00 59.33  ?  809 ALA A N   1 
ATOM   5014 C CA  . ALA A 1 828 ? -2.799  58.179  88.167  1.00 55.42  ?  809 ALA A CA  1 
ATOM   5015 C C   . ALA A 1 828 ? -4.216  57.678  87.915  1.00 56.98  ?  809 ALA A C   1 
ATOM   5016 O O   . ALA A 1 828 ? -4.525  57.131  86.856  1.00 68.84  ?  809 ALA A O   1 
ATOM   5017 C CB  . ALA A 1 828 ? -1.837  57.544  87.172  1.00 63.02  ?  809 ALA A CB  1 
ATOM   5018 N N   . THR A 1 829 ? -5.091  57.858  88.886  1.00 56.84  ?  810 THR A N   1 
ATOM   5019 C CA  . THR A 1 829 ? -6.476  57.444  88.744  1.00 59.36  ?  810 THR A CA  1 
ATOM   5020 C C   . THR A 1 829 ? -7.370  58.513  89.344  1.00 57.48  ?  810 THR A C   1 
ATOM   5021 O O   . THR A 1 829 ? -6.903  59.421  90.028  1.00 59.85  ?  810 THR A O   1 
ATOM   5022 C CB  . THR A 1 829 ? -6.731  56.114  89.445  1.00 60.12  ?  810 THR A CB  1 
ATOM   5023 O OG1 . THR A 1 829 ? -6.412  56.263  90.839  1.00 61.37  ?  810 THR A OG1 1 
ATOM   5024 C CG2 . THR A 1 829 ? -5.904  55.010  88.827  1.00 60.23  ?  810 THR A CG2 1 
ATOM   5025 N N   . VAL A 1 830 ? -8.669  58.400  89.089  1.00 54.81  ?  811 VAL A N   1 
ATOM   5026 C CA  . VAL A 1 830 ? -9.619  59.238  89.802  1.00 52.57  ?  811 VAL A CA  1 
ATOM   5027 C C   . VAL A 1 830 ? -9.777  58.751  91.232  1.00 58.27  ?  811 VAL A C   1 
ATOM   5028 O O   . VAL A 1 830 ? -9.672  59.532  92.183  1.00 60.22  ?  811 VAL A O   1 
ATOM   5029 C CB  . VAL A 1 830 ? -10.964 59.275  89.072  1.00 51.73  ?  811 VAL A CB  1 
ATOM   5030 C CG1 . VAL A 1 830 ? -12.044 59.687  90.034  1.00 52.36  ?  811 VAL A CG1 1 
ATOM   5031 C CG2 . VAL A 1 830 ? -10.890 60.232  87.909  1.00 58.01  ?  811 VAL A CG2 1 
ATOM   5032 N N   . HIS A 1 831 ? -10.011 57.453  91.413  1.00 54.29  ?  812 HIS A N   1 
ATOM   5033 C CA  . HIS A 1 831 ? -10.171 56.971  92.768  1.00 56.78  ?  812 HIS A CA  1 
ATOM   5034 C C   . HIS A 1 831 ? -8.938  57.279  93.617  1.00 59.58  ?  812 HIS A C   1 
ATOM   5035 O O   . HIS A 1 831 ? -9.050  57.354  94.841  1.00 62.41  ?  812 HIS A O   1 
ATOM   5036 C CB  . HIS A 1 831 ? -10.483 55.466  92.793  1.00 57.31  ?  812 HIS A CB  1 
ATOM   5037 C CG  . HIS A 1 831 ? -9.498  54.625  92.039  1.00 61.97  ?  812 HIS A CG  1 
ATOM   5038 N ND1 . HIS A 1 831 ? -8.427  54.003  92.653  1.00 55.97  ?  812 HIS A ND1 1 
ATOM   5039 C CD2 . HIS A 1 831 ? -9.443  54.265  90.732  1.00 60.40  ?  812 HIS A CD2 1 
ATOM   5040 C CE1 . HIS A 1 831 ? -7.723  53.345  91.750  1.00 53.07  ?  812 HIS A CE1 1 
ATOM   5041 N NE2 . HIS A 1 831 ? -8.324  53.478  90.580  1.00 57.16  ?  812 HIS A NE2 1 
ATOM   5042 N N   . GLY A 1 832 ? -7.768  57.477  93.016  1.00 55.56  ?  813 GLY A N   1 
ATOM   5043 C CA  . GLY A 1 832 ? -6.615  57.762  93.855  1.00 57.42  ?  813 GLY A CA  1 
ATOM   5044 C C   . GLY A 1 832 ? -6.574  59.238  94.219  1.00 57.96  ?  813 GLY A C   1 
ATOM   5045 O O   . GLY A 1 832 ? -6.268  59.614  95.361  1.00 54.70  ?  813 GLY A O   1 
ATOM   5046 N N   . ALA A 1 833 ? -6.854  60.087  93.227  1.00 52.39  ?  814 ALA A N   1 
ATOM   5047 C CA  . ALA A 1 833 ? -7.130  61.485  93.506  1.00 52.32  ?  814 ALA A CA  1 
ATOM   5048 C C   . ALA A 1 833 ? -8.095  61.604  94.679  1.00 56.83  ?  814 ALA A C   1 
ATOM   5049 O O   . ALA A 1 833 ? -7.773  62.183  95.725  1.00 56.28  ?  814 ALA A O   1 
ATOM   5050 C CB  . ALA A 1 833 ? -7.703  62.161  92.260  1.00 51.19  ?  814 ALA A CB  1 
ATOM   5051 N N   . LEU A 1 834 ? -9.282  61.019  94.524  1.00 60.96  ?  815 LEU A N   1 
ATOM   5052 C CA  . LEU A 1 834 ? -10.311 61.128  95.546  1.00 58.15  ?  815 LEU A CA  1 
ATOM   5053 C C   . LEU A 1 834 ? -9.820  60.610  96.885  1.00 53.43  ?  815 LEU A C   1 
ATOM   5054 O O   . LEU A 1 834 ? -10.025 61.246  97.919  1.00 58.96  ?  815 LEU A O   1 
ATOM   5055 C CB  . LEU A 1 834 ? -11.575 60.397  95.096  1.00 59.73  ?  815 LEU A CB  1 
ATOM   5056 C CG  . LEU A 1 834 ? -12.766 60.405  96.050  1.00 64.19  ?  815 LEU A CG  1 
ATOM   5057 C CD1 . LEU A 1 834 ? -14.073 60.346  95.263  1.00 63.93  ?  815 LEU A CD1 1 
ATOM   5058 C CD2 . LEU A 1 834 ? -12.664 59.214  97.004  1.00 62.79  ?  815 LEU A CD2 1 
ATOM   5059 N N   . LEU A 1 835 ? -9.155  59.473  96.898  1.00 51.92  ?  816 LEU A N   1 
ATOM   5060 C CA  . LEU A 1 835 ? -8.715  58.980  98.197  1.00 59.88  ?  816 LEU A CA  1 
ATOM   5061 C C   . LEU A 1 835 ? -7.696  59.922  98.821  1.00 55.88  ?  816 LEU A C   1 
ATOM   5062 O O   . LEU A 1 835 ? -7.617  60.014  100.053 1.00 54.96  ?  816 LEU A O   1 
ATOM   5063 C CB  . LEU A 1 835 ? -8.131  57.566  98.081  1.00 57.98  ?  816 LEU A CB  1 
ATOM   5064 C CG  . LEU A 1 835 ? -9.083  56.421  97.743  1.00 57.84  ?  816 LEU A CG  1 
ATOM   5065 C CD1 . LEU A 1 835 ? -8.344  55.116  97.798  1.00 67.83  ?  816 LEU A CD1 1 
ATOM   5066 C CD2 . LEU A 1 835 ? -10.236 56.397  98.701  1.00 59.53  ?  816 LEU A CD2 1 
ATOM   5067 N N   . SER A 1 836 ? -6.897  60.611  98.002  1.00 54.86  ?  817 SER A N   1 
ATOM   5068 C CA  . SER A 1 836 ? -5.861  61.449  98.593  1.00 54.79  ?  817 SER A CA  1 
ATOM   5069 C C   . SER A 1 836 ? -6.475  62.702  99.204  1.00 58.74  ?  817 SER A C   1 
ATOM   5070 O O   . SER A 1 836 ? -6.003  63.188  100.243 1.00 57.73  ?  817 SER A O   1 
ATOM   5071 C CB  . SER A 1 836 ? -4.779  61.788  97.555  1.00 52.10  ?  817 SER A CB  1 
ATOM   5072 O OG  . SER A 1 836 ? -5.251  62.618  96.503  1.00 47.95  ?  817 SER A OG  1 
ATOM   5073 N N   . GLY A 1 837 ? -7.538  63.223  98.584  1.00 58.35  ?  818 GLY A N   1 
ATOM   5074 C CA  . GLY A 1 837 ? -8.305  64.280  99.218  1.00 58.28  ?  818 GLY A CA  1 
ATOM   5075 C C   . GLY A 1 837 ? -8.841  63.849  100.568 1.00 55.76  ?  818 GLY A C   1 
ATOM   5076 O O   . GLY A 1 837 ? -8.658  64.535  101.571 1.00 61.85  ?  818 GLY A O   1 
ATOM   5077 N N   . LEU A 1 838 ? -9.490  62.690  100.617 1.00 56.63  ?  819 LEU A N   1 
ATOM   5078 C CA  . LEU A 1 838 ? -9.977  62.196  101.895 1.00 54.19  ?  819 LEU A CA  1 
ATOM   5079 C C   . LEU A 1 838 ? -8.844  62.151  102.905 1.00 54.58  ?  819 LEU A C   1 
ATOM   5080 O O   . LEU A 1 838 ? -8.998  62.576  104.055 1.00 61.45  ?  819 LEU A O   1 
ATOM   5081 C CB  . LEU A 1 838 ? -10.616 60.818  101.728 1.00 53.05  ?  819 LEU A CB  1 
ATOM   5082 C CG  . LEU A 1 838 ? -11.818 60.778  100.788 1.00 59.82  ?  819 LEU A CG  1 
ATOM   5083 C CD1 . LEU A 1 838 ? -12.574 59.460  100.892 1.00 63.05  ?  819 LEU A CD1 1 
ATOM   5084 C CD2 . LEU A 1 838 ? -12.732 61.962  101.048 1.00 58.78  ?  819 LEU A CD2 1 
ATOM   5085 N N   . ARG A 1 839 ? -7.685  61.668  102.477 1.00 52.35  ?  820 ARG A N   1 
ATOM   5086 C CA  . ARG A 1 839 ? -6.549  61.561  103.373 1.00 51.12  ?  820 ARG A CA  1 
ATOM   5087 C C   . ARG A 1 839 ? -6.145  62.914  103.920 1.00 57.49  ?  820 ARG A C   1 
ATOM   5088 O O   . ARG A 1 839 ? -6.011  63.079  105.137 1.00 58.89  ?  820 ARG A O   1 
ATOM   5089 C CB  . ARG A 1 839 ? -5.379  60.872  102.678 1.00 45.33  ?  820 ARG A CB  1 
ATOM   5090 C CG  . ARG A 1 839 ? -4.129  61.012  103.475 1.00 47.28  ?  820 ARG A CG  1 
ATOM   5091 C CD  . ARG A 1 839 ? -2.965  60.319  102.877 1.00 55.02  ?  820 ARG A CD  1 
ATOM   5092 N NE  . ARG A 1 839 ? -2.817  60.525  101.416 1.00 70.38  ?  820 ARG A NE  1 
ATOM   5093 C CZ  . ARG A 1 839 ? -2.305  61.599  100.797 1.00 62.05  ?  820 ARG A CZ  1 
ATOM   5094 N NH1 . ARG A 1 839 ? -1.965  62.699  101.482 1.00 61.93  ?  820 ARG A NH1 1 
ATOM   5095 N NH2 . ARG A 1 839 ? -2.198  61.606  99.455  1.00 60.86  ?  820 ARG A NH2 1 
ATOM   5096 N N   . GLU A 1 840 ? -5.950  63.907  103.056 1.00 58.88  ?  821 GLU A N   1 
ATOM   5097 C CA  . GLU A 1 840 ? -5.524  65.172  103.626 1.00 60.87  ?  821 GLU A CA  1 
ATOM   5098 C C   . GLU A 1 840 ? -6.586  65.759  104.535 1.00 61.89  ?  821 GLU A C   1 
ATOM   5099 O O   . GLU A 1 840 ? -6.275  66.181  105.655 1.00 67.35  ?  821 GLU A O   1 
ATOM   5100 C CB  . GLU A 1 840 ? -5.096  66.213  102.599 1.00 55.70  ?  821 GLU A CB  1 
ATOM   5101 C CG  . GLU A 1 840 ? -3.829  65.979  101.787 1.00 63.75  ?  821 GLU A CG  1 
ATOM   5102 C CD  . GLU A 1 840 ? -2.627  65.444  102.601 1.00 71.49  ?  821 GLU A CD  1 
ATOM   5103 O OE1 . GLU A 1 840 ? -2.725  65.217  103.787 1.00 71.49  ?  821 GLU A OE1 1 
ATOM   5104 O OE2 . GLU A 1 840 ? -1.470  65.576  102.151 1.00 81.67  ?  821 GLU A OE2 1 
ATOM   5105 N N   . ALA A 1 841 ? -7.843  65.763  104.100 1.00 55.74  ?  822 ALA A N   1 
ATOM   5106 C CA  . ALA A 1 841 ? -8.889  66.294  104.962 1.00 58.12  ?  822 ALA A CA  1 
ATOM   5107 C C   . ALA A 1 841 ? -8.854  65.625  106.332 1.00 58.44  ?  822 ALA A C   1 
ATOM   5108 O O   . ALA A 1 841 ? -9.045  66.271  107.360 1.00 66.17  ?  822 ALA A O   1 
ATOM   5109 C CB  . ALA A 1 841 ? -10.254 66.130  104.298 1.00 57.79  ?  822 ALA A CB  1 
ATOM   5110 N N   . GLY A 1 842 ? -8.551  64.348  106.380 1.00 60.99  ?  823 GLY A N   1 
ATOM   5111 C CA  . GLY A 1 842 ? -8.395  63.724  107.673 1.00 65.44  ?  823 GLY A CA  1 
ATOM   5112 C C   . GLY A 1 842 ? -7.275  64.344  108.483 1.00 63.68  ?  823 GLY A C   1 
ATOM   5113 O O   . GLY A 1 842 ? -7.437  64.598  109.672 1.00 69.94  ?  823 GLY A O   1 
ATOM   5114 N N   . ARG A 1 843 ? -6.116  64.580  107.869 1.00 61.03  ?  824 ARG A N   1 
ATOM   5115 C CA  . ARG A 1 843 ? -4.998  64.947  108.729 1.00 68.40  ?  824 ARG A CA  1 
ATOM   5116 C C   . ARG A 1 843 ? -4.956  66.437  108.995 1.00 65.05  ?  824 ARG A C   1 
ATOM   5117 O O   . ARG A 1 843 ? -4.375  66.858  110.002 1.00 64.44  ?  824 ARG A O   1 
ATOM   5118 C CB  . ARG A 1 843 ? -3.652  64.494  108.159 1.00 57.50  ?  824 ARG A CB  1 
ATOM   5119 C CG  . ARG A 1 843 ? -3.141  65.338  107.127 1.00 56.97  ?  824 ARG A CG  1 
ATOM   5120 C CD  . ARG A 1 843 ? -2.075  64.653  106.335 1.00 74.05  ?  824 ARG A CD  1 
ATOM   5121 N NE  . ARG A 1 843 ? -0.827  64.281  106.978 1.00 84.12  ?  824 ARG A NE  1 
ATOM   5122 C CZ  . ARG A 1 843 ? 0.104   63.559  106.353 1.00 79.87  ?  824 ARG A CZ  1 
ATOM   5123 N NH1 . ARG A 1 843 ? -0.114  63.165  105.092 1.00 73.44  ?  824 ARG A NH1 1 
ATOM   5124 N NH2 . ARG A 1 843 ? 1.239   63.242  106.975 1.00 79.67  ?  824 ARG A NH2 1 
ATOM   5125 N N   . ILE A 1 844 ? -5.558  67.232  108.114 1.00 65.76  ?  825 ILE A N   1 
ATOM   5126 C CA  . ILE A 1 844 ? -5.740  68.646  108.398 1.00 69.49  ?  825 ILE A CA  1 
ATOM   5127 C C   . ILE A 1 844 ? -6.709  68.808  109.559 1.00 66.57  ?  825 ILE A C   1 
ATOM   5128 O O   . ILE A 1 844 ? -6.442  69.546  110.510 1.00 68.82  ?  825 ILE A O   1 
ATOM   5129 C CB  . ILE A 1 844 ? -6.208  69.393  107.129 1.00 66.78  ?  825 ILE A CB  1 
ATOM   5130 C CG1 . ILE A 1 844 ? -5.044  69.585  106.156 1.00 58.16  ?  825 ILE A CG1 1 
ATOM   5131 C CG2 . ILE A 1 844 ? -6.889  70.738  107.456 1.00 59.84  ?  825 ILE A CG2 1 
ATOM   5132 C CD1 . ILE A 1 844 ? -5.521  70.081  104.797 1.00 63.86  ?  825 ILE A CD1 1 
ATOM   5133 N N   . ALA A 1 845 ? -7.820  68.076  109.521 1.00 59.72  ?  826 ALA A N   1 
ATOM   5134 C CA  . ALA A 1 845 ? -8.758  68.104  110.635 1.00 67.30  ?  826 ALA A CA  1 
ATOM   5135 C C   . ALA A 1 845 ? -8.096  67.634  111.927 1.00 71.10  ?  826 ALA A C   1 
ATOM   5136 O O   . ALA A 1 845 ? -8.235  68.268  112.977 1.00 69.02  ?  826 ALA A O   1 
ATOM   5137 C CB  . ALA A 1 845 ? -9.975  67.242  110.313 1.00 66.34  ?  826 ALA A CB  1 
ATOM   5138 N N   . ASP A 1 846 ? -7.369  66.518  111.867 1.00 74.45  ?  827 ASP A N   1 
ATOM   5139 C CA  . ASP A 1 846 ? -6.632  66.028  113.029 1.00 77.68  ?  827 ASP A CA  1 
ATOM   5140 C C   . ASP A 1 846 ? -5.725  67.107  113.602 1.00 77.46  ?  827 ASP A C   1 
ATOM   5141 O O   . ASP A 1 846 ? -5.442  67.125  114.807 1.00 80.83  ?  827 ASP A O   1 
ATOM   5142 C CB  . ASP A 1 846 ? -5.805  64.803  112.621 1.00 74.99  ?  827 ASP A CB  1 
ATOM   5143 C CG  . ASP A 1 846 ? -6.565  63.499  112.816 1.00 88.13  ?  827 ASP A CG  1 
ATOM   5144 O OD1 . ASP A 1 846 ? -5.918  62.414  112.875 1.00 93.69  ?  827 ASP A OD1 1 
ATOM   5145 O OD2 . ASP A 1 846 ? -7.820  63.571  112.935 1.00 84.16  ?  827 ASP A OD2 1 
ATOM   5146 N N   . GLN A 1 847 ? -5.273  68.019  112.757 1.00 73.35  ?  828 GLN A N   1 
ATOM   5147 C CA  . GLN A 1 847 ? -4.247  68.971  113.127 1.00 72.70  ?  828 GLN A CA  1 
ATOM   5148 C C   . GLN A 1 847 ? -4.840  70.239  113.708 1.00 76.29  ?  828 GLN A C   1 
ATOM   5149 O O   . GLN A 1 847 ? -4.298  70.795  114.661 1.00 78.83  ?  828 GLN A O   1 
ATOM   5150 C CB  . GLN A 1 847 ? -3.407  69.300  111.895 1.00 73.90  ?  828 GLN A CB  1 
ATOM   5151 C CG  . GLN A 1 847 ? -2.457  70.450  112.061 1.00 76.79  ?  828 GLN A CG  1 
ATOM   5152 C CD  . GLN A 1 847 ? -1.371  70.123  113.026 1.00 85.76  ?  828 GLN A CD  1 
ATOM   5153 O OE1 . GLN A 1 847 ? -1.307  70.699  114.116 1.00 84.77  ?  828 GLN A OE1 1 
ATOM   5154 N NE2 . GLN A 1 847 ? -0.514  69.160  112.655 1.00 92.01  ?  828 GLN A NE2 1 
ATOM   5155 N N   . PHE A 1 848 ? -5.958  70.695  113.154 1.00 77.16  ?  829 PHE A N   1 
ATOM   5156 C CA  . PHE A 1 848 ? -6.513  71.993  113.479 1.00 72.37  ?  829 PHE A CA  1 
ATOM   5157 C C   . PHE A 1 848 ? -7.802  71.906  114.272 1.00 73.87  ?  829 PHE A C   1 
ATOM   5158 O O   . PHE A 1 848 ? -8.294  72.936  114.740 1.00 81.65  ?  829 PHE A O   1 
ATOM   5159 C CB  . PHE A 1 848 ? -6.713  72.806  112.187 1.00 68.20  ?  829 PHE A CB  1 
ATOM   5160 C CG  . PHE A 1 848 ? -5.414  73.242  111.571 1.00 70.55  ?  829 PHE A CG  1 
ATOM   5161 C CD1 . PHE A 1 848 ? -4.805  74.420  111.972 1.00 74.35  ?  829 PHE A CD1 1 
ATOM   5162 C CD2 . PHE A 1 848 ? -4.768  72.461  110.641 1.00 72.44  ?  829 PHE A CD2 1 
ATOM   5163 C CE1 . PHE A 1 848 ? -3.584  74.823  111.442 1.00 65.95  ?  829 PHE A CE1 1 
ATOM   5164 C CE2 . PHE A 1 848 ? -3.550  72.866  110.102 1.00 70.52  ?  829 PHE A CE2 1 
ATOM   5165 C CZ  . PHE A 1 848 ? -2.967  74.049  110.509 1.00 70.61  ?  829 PHE A CZ  1 
ATOM   5166 N N   . LEU A 1 849 ? -8.342  70.713  114.459 1.00 74.23  ?  830 LEU A N   1 
ATOM   5167 C CA  . LEU A 1 849 ? -9.492  70.508  115.320 1.00 74.81  ?  830 LEU A CA  1 
ATOM   5168 C C   . LEU A 1 849 ? -9.206  69.496  116.416 1.00 76.13  ?  830 LEU A C   1 
ATOM   5169 O O   . LEU A 1 849 ? -10.102 69.215  117.217 1.00 80.54  ?  830 LEU A O   1 
ATOM   5170 C CB  . LEU A 1 849 ? -10.703 70.025  114.506 1.00 68.92  ?  830 LEU A CB  1 
ATOM   5171 C CG  . LEU A 1 849 ? -11.118 70.783  113.238 1.00 77.05  ?  830 LEU A CG  1 
ATOM   5172 C CD1 . LEU A 1 849 ? -12.411 70.170  112.680 1.00 76.77  ?  830 LEU A CD1 1 
ATOM   5173 C CD2 . LEU A 1 849 ? -11.228 72.329  113.389 1.00 67.78  ?  830 LEU A CD2 1 
ATOM   5174 N N   . GLY A 1 850 ? -7.997  68.923  116.459 1.00 75.95  ?  831 GLY A N   1 
ATOM   5175 C CA  . GLY A 1 850 ? -7.652  67.867  117.391 1.00 77.55  ?  831 GLY A CA  1 
ATOM   5176 C C   . GLY A 1 850 ? -8.490  66.622  117.184 1.00 86.35  ?  831 GLY A C   1 
ATOM   5177 O O   . GLY A 1 850 ? -9.489  66.647  116.457 1.00 80.40  ?  831 GLY A O   1 
ATOM   5178 N N   . ALA A 1 851 ? -8.120  65.523  117.834 1.00 93.34  ?  832 ALA A N   1 
ATOM   5179 C CA  . ALA A 1 851 ? -8.800  64.248  117.607 1.00 99.75  ?  832 ALA A CA  1 
ATOM   5180 C C   . ALA A 1 851 ? -9.027  63.536  118.943 1.00 108.57 ?  832 ALA A C   1 
ATOM   5181 O O   . ALA A 1 851 ? -8.093  62.926  119.478 1.00 111.34 ?  832 ALA A O   1 
ATOM   5182 C CB  . ALA A 1 851 ? -7.975  63.397  116.650 1.00 94.64  ?  832 ALA A CB  1 
ATOM   5183 N N   . MET A 1 852 ? -10.262 63.571  119.476 1.00 109.26 ?  833 MET A N   1 
ATOM   5184 C CA  . MET A 1 852 ? -10.446 62.955  120.792 1.00 116.10 ?  833 MET A CA  1 
ATOM   5185 C C   . MET A 1 852 ? -10.381 61.439  120.727 1.00 114.40 ?  833 MET A C   1 
ATOM   5186 O O   . MET A 1 852 ? -10.216 60.804  121.775 1.00 111.43 ?  833 MET A O   1 
ATOM   5187 C CB  . MET A 1 852 ? -11.788 63.319  121.451 1.00 115.65 ?  833 MET A CB  1 
ATOM   5188 C CG  . MET A 1 852 ? -12.088 64.806  121.636 1.00 128.41 ?  833 MET A CG  1 
ATOM   5189 S SD  . MET A 1 852 ? -10.892 65.892  122.434 1.00 147.38 ?  833 MET A SD  1 
ATOM   5190 C CE  . MET A 1 852 ? -10.288 66.749  120.964 1.00 110.74 ?  833 MET A CE  1 
ATOM   5191 N N   . TYR A 1 853 ? -10.514 60.841  119.514 1.00 108.63 ?  834 TYR A N   1 
ATOM   5192 C CA  . TYR A 1 853 ? -10.586 59.380  119.360 1.00 105.19 ?  834 TYR A CA  1 
ATOM   5193 C C   . TYR A 1 853 ? -9.224  58.654  119.647 1.00 103.33 ?  834 TYR A C   1 
ATOM   5194 O O   . TYR A 1 853 ? -9.128  57.433  119.415 1.00 96.81  ?  834 TYR A O   1 
ATOM   5195 C CB  . TYR A 1 853 ? -11.113 59.001  117.959 1.00 104.09 ?  834 TYR A CB  1 
ATOM   5196 C CG  . TYR A 1 853 ? -10.369 59.611  116.772 1.00 105.08 ?  834 TYR A CG  1 
ATOM   5197 C CD1 . TYR A 1 853 ? -10.851 60.758  116.130 1.00 99.96  ?  834 TYR A CD1 1 
ATOM   5198 C CD2 . TYR A 1 853 ? -9.189  59.026  116.289 1.00 98.51  ?  834 TYR A CD2 1 
ATOM   5199 C CE1 . TYR A 1 853 ? -10.175 61.312  115.048 1.00 94.04  ?  834 TYR A CE1 1 
ATOM   5200 C CE2 . TYR A 1 853 ? -8.500  59.575  115.217 1.00 97.90  ?  834 TYR A CE2 1 
ATOM   5201 C CZ  . TYR A 1 853 ? -8.994  60.716  114.599 1.00 98.44  ?  834 TYR A CZ  1 
ATOM   5202 O OH  . TYR A 1 853 ? -8.301  61.247  113.531 1.00 93.21  ?  834 TYR A OH  1 
ATOM   5203 N N   . THR A 1 854 ? -8.189  59.341  120.141 1.00 107.29 ?  835 THR A N   1 
ATOM   5204 C CA  . THR A 1 854 ? -6.904  58.709  120.431 1.00 109.22 ?  835 THR A CA  1 
ATOM   5205 C C   . THR A 1 854 ? -6.739  58.375  121.919 1.00 109.54 ?  835 THR A C   1 
ATOM   5206 O O   . THR A 1 854 ? -5.829  57.613  122.274 1.00 106.26 ?  835 THR A O   1 
ATOM   5207 C CB  . THR A 1 854 ? -5.757  59.622  119.930 1.00 111.89 ?  835 THR A CB  1 
ATOM   5208 O OG1 . THR A 1 854 ? -5.891  59.808  118.509 1.00 102.12 ?  835 THR A OG1 1 
ATOM   5209 C CG2 . THR A 1 854 ? -4.351  59.009  120.219 1.00 102.44 ?  835 THR A CG2 1 
ATOM   5210 N N   . LEU A 1 855 ? -7.625  58.886  122.780 1.00 111.56 ?  836 LEU A N   1 
ATOM   5211 C CA  . LEU A 1 855 ? -7.612  58.654  124.229 1.00 107.50 ?  836 LEU A CA  1 
ATOM   5212 C C   . LEU A 1 855 ? -8.224  57.277  124.596 1.00 102.08 ?  836 LEU A C   1 
ATOM   5213 O O   . LEU A 1 855 ? -7.884  56.625  125.609 1.00 90.20  ?  836 LEU A O   1 
ATOM   5214 C CB  . LEU A 1 855 ? -8.388  59.786  124.927 1.00 113.22 ?  836 LEU A CB  1 
ATOM   5215 C CG  . LEU A 1 855 ? -7.667  61.057  125.390 1.00 111.91 ?  836 LEU A CG  1 
ATOM   5216 C CD1 . LEU A 1 855 ? -7.073  61.796  124.192 1.00 110.52 ?  836 LEU A CD1 1 
ATOM   5217 C CD2 . LEU A 1 855 ? -8.609  61.959  126.200 1.00 103.76 ?  836 LEU A CD2 1 
ATOM   5218 N N   . ARG B 2 12  ? 12.006  31.439  90.676  1.00 127.27 ?  308 ARG B N   1 
ATOM   5219 C CA  . ARG B 2 12  ? 13.257  30.705  90.529  1.00 133.66 ?  308 ARG B CA  1 
ATOM   5220 C C   . ARG B 2 12  ? 13.722  30.702  89.056  1.00 131.92 ?  308 ARG B C   1 
ATOM   5221 O O   . ARG B 2 12  ? 14.917  30.849  88.777  1.00 129.10 ?  308 ARG B O   1 
ATOM   5222 C CB  . ARG B 2 12  ? 13.117  29.249  91.044  1.00 137.06 ?  308 ARG B CB  1 
ATOM   5223 C CG  . ARG B 2 12  ? 13.026  29.051  92.577  1.00 135.19 ?  308 ARG B CG  1 
ATOM   5224 C CD  . ARG B 2 12  ? 14.269  29.553  93.338  1.00 145.57 ?  308 ARG B CD  1 
ATOM   5225 N NE  . ARG B 2 12  ? 14.012  30.832  94.011  1.00 150.22 ?  308 ARG B NE  1 
ATOM   5226 C CZ  . ARG B 2 12  ? 14.947  31.725  94.343  1.00 149.34 ?  308 ARG B CZ  1 
ATOM   5227 N NH1 . ARG B 2 12  ? 16.227  31.487  94.074  1.00 148.19 ?  308 ARG B NH1 1 
ATOM   5228 N NH2 . ARG B 2 12  ? 14.601  32.863  94.944  1.00 143.97 ?  308 ARG B NH2 1 
ATOM   5229 N N   . LYS B 2 13  ? 12.785  30.550  88.118  1.00 127.95 ?  309 LYS B N   1 
ATOM   5230 C CA  . LYS B 2 13  ? 13.108  30.222  86.730  1.00 119.24 ?  309 LYS B CA  1 
ATOM   5231 C C   . LYS B 2 13  ? 12.281  31.060  85.763  1.00 115.59 ?  309 LYS B C   1 
ATOM   5232 O O   . LYS B 2 13  ? 11.153  31.454  86.090  1.00 114.65 ?  309 LYS B O   1 
ATOM   5233 C CB  . LYS B 2 13  ? 12.864  28.726  86.453  1.00 121.00 ?  309 LYS B CB  1 
ATOM   5234 C CG  . LYS B 2 13  ? 13.799  27.778  87.214  1.00 129.53 ?  309 LYS B CG  1 
ATOM   5235 C CD  . LYS B 2 13  ? 13.798  26.368  86.610  1.00 129.32 ?  309 LYS B CD  1 
ATOM   5236 C CE  . LYS B 2 13  ? 14.952  25.514  87.147  1.00 127.97 ?  309 LYS B CE  1 
ATOM   5237 N NZ  . LYS B 2 13  ? 15.145  24.243  86.388  1.00 108.37 ?  309 LYS B NZ  1 
ATOM   5238 N N   . PRO B 2 14  ? 12.800  31.325  84.556  1.00 111.04 ?  310 PRO B N   1 
ATOM   5239 C CA  . PRO B 2 14  ? 12.082  32.192  83.592  1.00 103.08 ?  310 PRO B CA  1 
ATOM   5240 C C   . PRO B 2 14  ? 10.806  31.534  83.107  1.00 103.73 ?  310 PRO B C   1 
ATOM   5241 O O   . PRO B 2 14  ? 10.560  30.360  83.414  1.00 114.35 ?  310 PRO B O   1 
ATOM   5242 C CB  . PRO B 2 14  ? 13.083  32.362  82.434  1.00 95.16  ?  310 PRO B CB  1 
ATOM   5243 C CG  . PRO B 2 14  ? 14.192  31.444  82.673  1.00 95.79  ?  310 PRO B CG  1 
ATOM   5244 C CD  . PRO B 2 14  ? 14.018  30.729  83.973  1.00 107.90 ?  310 PRO B CD  1 
ATOM   5245 N N   . PRO B 2 15  ? 9.968   32.241  82.348  1.00 102.33 ?  311 PRO B N   1 
ATOM   5246 C CA  . PRO B 2 15  ? 8.979   31.534  81.536  1.00 103.45 ?  311 PRO B CA  1 
ATOM   5247 C C   . PRO B 2 15  ? 9.724   30.582  80.623  1.00 111.79 ?  311 PRO B C   1 
ATOM   5248 O O   . PRO B 2 15  ? 10.921  30.743  80.376  1.00 115.78 ?  311 PRO B O   1 
ATOM   5249 C CB  . PRO B 2 15  ? 8.281   32.644  80.737  1.00 102.56 ?  311 PRO B CB  1 
ATOM   5250 C CG  . PRO B 2 15  ? 8.626   33.886  81.401  1.00 93.36  ?  311 PRO B CG  1 
ATOM   5251 C CD  . PRO B 2 15  ? 9.960   33.684  82.063  1.00 102.42 ?  311 PRO B CD  1 
ATOM   5252 N N   . LYS B 2 16  ? 9.017   29.572  80.131  1.00 116.13 ?  312 LYS B N   1 
ATOM   5253 C CA  . LYS B 2 16  ? 9.688   28.505  79.402  1.00 121.50 ?  312 LYS B CA  1 
ATOM   5254 C C   . LYS B 2 16  ? 9.937   28.935  77.960  1.00 122.87 ?  312 LYS B C   1 
ATOM   5255 O O   . LYS B 2 16  ? 9.121   29.641  77.363  1.00 116.54 ?  312 LYS B O   1 
ATOM   5256 C CB  . LYS B 2 16  ? 8.865   27.219  79.462  1.00 120.63 ?  312 LYS B CB  1 
ATOM   5257 C CG  . LYS B 2 16  ? 8.649   26.671  80.883  1.00 123.68 ?  312 LYS B CG  1 
ATOM   5258 C CD  . LYS B 2 16  ? 9.911   26.039  81.487  1.00 125.63 ?  312 LYS B CD  1 
ATOM   5259 C CE  . LYS B 2 16  ? 9.673   25.571  82.925  1.00 121.75 ?  312 LYS B CE  1 
ATOM   5260 N NZ  . LYS B 2 16  ? 10.879  24.923  83.518  1.00 124.71 ?  312 LYS B NZ  1 
ATOM   5261 N N   . GLY B 2 17  ? 11.090  28.535  77.412  1.00 123.72 ?  313 GLY B N   1 
ATOM   5262 C CA  . GLY B 2 17  ? 11.512  28.947  76.082  1.00 125.07 ?  313 GLY B CA  1 
ATOM   5263 C C   . GLY B 2 17  ? 12.281  30.259  76.025  1.00 126.02 ?  313 GLY B C   1 
ATOM   5264 O O   . GLY B 2 17  ? 13.174  30.407  75.175  1.00 123.05 ?  313 GLY B O   1 
ATOM   5265 N N   . MET B 2 18  ? 11.922  31.225  76.878  1.00 107.50 ?  314 MET B N   1 
ATOM   5266 C CA  . MET B 2 18  ? 12.759  32.392  77.135  1.00 103.35 ?  314 MET B CA  1 
ATOM   5267 C C   . MET B 2 18  ? 14.149  31.955  77.583  1.00 105.62 ?  314 MET B C   1 
ATOM   5268 O O   . MET B 2 18  ? 14.284  31.120  78.484  1.00 106.26 ?  314 MET B O   1 
ATOM   5269 C CB  . MET B 2 18  ? 12.098  33.240  78.225  1.00 108.67 ?  314 MET B CB  1 
ATOM   5270 C CG  . MET B 2 18  ? 10.709  33.747  77.849  1.00 102.59 ?  314 MET B CG  1 
ATOM   5271 S SD  . MET B 2 18  ? 10.777  35.049  76.618  1.00 96.57  ?  314 MET B SD  1 
ATOM   5272 C CE  . MET B 2 18  ? 9.149   35.014  75.927  1.00 87.60  ?  314 MET B CE  1 
ATOM   5273 N N   . PHE B 2 19  ? 15.189  32.516  76.970  1.00 97.36  ?  315 PHE B N   1 
ATOM   5274 C CA  . PHE B 2 19  ? 16.554  32.147  77.327  1.00 109.61 ?  315 PHE B CA  1 
ATOM   5275 C C   . PHE B 2 19  ? 17.275  33.342  77.936  1.00 105.57 ?  315 PHE B C   1 
ATOM   5276 O O   . PHE B 2 19  ? 17.482  34.357  77.265  1.00 105.10 ?  315 PHE B O   1 
ATOM   5277 C CB  . PHE B 2 19  ? 17.306  31.578  76.122  1.00 110.51 ?  315 PHE B CB  1 
ATOM   5278 C CG  . PHE B 2 19  ? 17.183  30.079  76.000  1.00 117.30 ?  315 PHE B CG  1 
ATOM   5279 C CD1 . PHE B 2 19  ? 15.963  29.497  75.649  1.00 113.94 ?  315 PHE B CD1 1 
ATOM   5280 C CD2 . PHE B 2 19  ? 18.271  29.245  76.278  1.00 121.14 ?  315 PHE B CD2 1 
ATOM   5281 C CE1 . PHE B 2 19  ? 15.821  28.112  75.552  1.00 109.79 ?  315 PHE B CE1 1 
ATOM   5282 C CE2 . PHE B 2 19  ? 18.145  27.848  76.182  1.00 124.21 ?  315 PHE B CE2 1 
ATOM   5283 C CZ  . PHE B 2 19  ? 16.917  27.282  75.817  1.00 114.27 ?  315 PHE B CZ  1 
ATOM   5284 N N   . LEU B 2 20  ? 17.655  33.212  79.209  1.00 103.33 ?  316 LEU B N   1 
ATOM   5285 C CA  . LEU B 2 20  ? 18.132  34.347  79.996  1.00 103.67 ?  316 LEU B CA  1 
ATOM   5286 C C   . LEU B 2 20  ? 19.075  33.800  81.069  1.00 108.79 ?  316 LEU B C   1 
ATOM   5287 O O   . LEU B 2 20  ? 18.632  33.398  82.149  1.00 108.90 ?  316 LEU B O   1 
ATOM   5288 C CB  . LEU B 2 20  ? 16.958  35.089  80.623  1.00 108.22 ?  316 LEU B CB  1 
ATOM   5289 C CG  . LEU B 2 20  ? 15.777  35.541  79.750  1.00 98.10  ?  316 LEU B CG  1 
ATOM   5290 C CD1 . LEU B 2 20  ? 14.557  35.848  80.567  1.00 92.19  ?  316 LEU B CD1 1 
ATOM   5291 C CD2 . LEU B 2 20  ? 16.166  36.763  78.960  1.00 98.71  ?  316 LEU B CD2 1 
ATOM   5292 N N   . SER B 2 21  ? 20.368  33.781  80.772  1.00 113.14 ?  317 SER B N   1 
ATOM   5293 C CA  . SER B 2 21  ? 21.311  33.480  81.838  1.00 122.36 ?  317 SER B CA  1 
ATOM   5294 C C   . SER B 2 21  ? 22.176  34.701  82.100  1.00 123.83 ?  317 SER B C   1 
ATOM   5295 O O   . SER B 2 21  ? 22.262  35.625  81.278  1.00 119.47 ?  317 SER B O   1 
ATOM   5296 C CB  . SER B 2 21  ? 22.179  32.250  81.533  1.00 125.93 ?  317 SER B CB  1 
ATOM   5297 O OG  . SER B 2 21  ? 23.172  32.508  80.567  1.00 126.40 ?  317 SER B OG  1 
ATOM   5298 N N   . GLN B 2 22  ? 22.780  34.705  83.290  1.00 121.56 ?  318 GLN B N   1 
ATOM   5299 C CA  . GLN B 2 22  ? 23.593  35.843  83.688  1.00 124.55 ?  318 GLN B CA  1 
ATOM   5300 C C   . GLN B 2 22  ? 24.691  36.114  82.671  1.00 129.27 ?  318 GLN B C   1 
ATOM   5301 O O   . GLN B 2 22  ? 24.980  37.280  82.373  1.00 127.17 ?  318 GLN B O   1 
ATOM   5302 C CB  . GLN B 2 22  ? 24.168  35.617  85.089  1.00 124.78 ?  318 GLN B CB  1 
ATOM   5303 C CG  . GLN B 2 22  ? 24.783  36.858  85.713  1.00 131.38 ?  318 GLN B CG  1 
ATOM   5304 C CD  . GLN B 2 22  ? 23.781  37.991  85.851  1.00 134.01 ?  318 GLN B CD  1 
ATOM   5305 O OE1 . GLN B 2 22  ? 23.895  39.034  85.191  1.00 134.01 ?  318 GLN B OE1 1 
ATOM   5306 N NE2 . GLN B 2 22  ? 22.769  37.777  86.692  1.00 124.40 ?  318 GLN B NE2 1 
ATOM   5307 N N   . GLU B 2 23  ? 25.276  35.057  82.093  1.00 130.09 ?  319 GLU B N   1 
ATOM   5308 C CA  . GLU B 2 23  ? 26.303  35.270  81.092  1.00 129.65 ?  319 GLU B CA  1 
ATOM   5309 C C   . GLU B 2 23  ? 25.761  35.965  79.851  1.00 127.52 ?  319 GLU B C   1 
ATOM   5310 O O   . GLU B 2 23  ? 26.530  36.686  79.193  1.00 126.56 ?  319 GLU B O   1 
ATOM   5311 C CB  . GLU B 2 23  ? 27.023  33.948  80.746  1.00 130.37 ?  319 GLU B CB  1 
ATOM   5312 C CG  . GLU B 2 23  ? 26.227  33.018  79.831  1.00 137.17 ?  319 GLU B CG  1 
ATOM   5313 C CD  . GLU B 2 23  ? 26.992  31.782  79.348  1.00 139.37 ?  319 GLU B CD  1 
ATOM   5314 O OE1 . GLU B 2 23  ? 28.217  31.673  79.617  1.00 140.07 ?  319 GLU B OE1 1 
ATOM   5315 O OE2 . GLU B 2 23  ? 26.362  30.923  78.684  1.00 131.67 ?  319 GLU B OE2 1 
ATOM   5316 N N   . ASP B 2 24  ? 24.487  35.780  79.478  1.00 125.65 ?  320 ASP B N   1 
ATOM   5317 C CA  . ASP B 2 24  ? 24.291  36.242  78.114  1.00 122.70 ?  320 ASP B CA  1 
ATOM   5318 C C   . ASP B 2 24  ? 23.888  37.702  78.170  1.00 120.70 ?  320 ASP B C   1 
ATOM   5319 O O   . ASP B 2 24  ? 24.057  38.440  77.189  1.00 119.15 ?  320 ASP B O   1 
ATOM   5320 C CB  . ASP B 2 24  ? 23.200  35.482  77.339  1.00 120.71 ?  320 ASP B CB  1 
ATOM   5321 C CG  . ASP B 2 24  ? 23.294  34.016  77.487  1.00 130.24 ?  320 ASP B CG  1 
ATOM   5322 O OD1 . ASP B 2 24  ? 24.263  33.550  78.092  1.00 141.75 ?  320 ASP B OD1 1 
ATOM   5323 O OD2 . ASP B 2 24  ? 22.472  33.328  76.762  1.00 123.90 ?  320 ASP B OD2 1 
ATOM   5324 N N   . VAL B 2 25  ? 23.277  38.107  79.303  1.00 124.92 ?  321 VAL B N   1 
ATOM   5325 C CA  . VAL B 2 25  ? 22.781  39.476  79.436  1.00 122.25 ?  321 VAL B CA  1 
ATOM   5326 C C   . VAL B 2 25  ? 23.947  40.455  79.410  1.00 123.38 ?  321 VAL B C   1 
ATOM   5327 O O   . VAL B 2 25  ? 23.892  41.488  78.727  1.00 120.06 ?  321 VAL B O   1 
ATOM   5328 C CB  . VAL B 2 25  ? 21.923  39.619  80.714  1.00 115.93 ?  321 VAL B CB  1 
ATOM   5329 C CG1 . VAL B 2 25  ? 20.770  38.619  80.722  1.00 115.73 ?  321 VAL B CG1 1 
ATOM   5330 C CG2 . VAL B 2 25  ? 22.764  39.520  82.002  1.00 121.77 ?  321 VAL B CG2 1 
ATOM   5331 N N   . GLU B 2 26  ? 25.035  40.124  80.114  1.00 123.65 ?  322 GLU B N   1 
ATOM   5332 C CA  . GLU B 2 26  ? 26.175  41.027  80.179  1.00 125.99 ?  322 GLU B CA  1 
ATOM   5333 C C   . GLU B 2 26  ? 26.789  41.220  78.802  1.00 123.92 ?  322 GLU B C   1 
ATOM   5334 O O   . GLU B 2 26  ? 27.156  42.342  78.429  1.00 125.14 ?  322 GLU B O   1 
ATOM   5335 C CB  . GLU B 2 26  ? 27.222  40.498  81.163  1.00 125.24 ?  322 GLU B CB  1 
ATOM   5336 C CG  . GLU B 2 26  ? 26.653  39.887  82.443  1.00 128.07 ?  322 GLU B CG  1 
ATOM   5337 C CD  . GLU B 2 26  ? 27.717  39.184  83.287  1.00 139.73 ?  322 GLU B CD  1 
ATOM   5338 O OE1 . GLU B 2 26  ? 28.650  38.595  82.691  1.00 143.41 ?  322 GLU B OE1 1 
ATOM   5339 O OE2 . GLU B 2 26  ? 27.616  39.210  84.540  1.00 134.63 ?  322 GLU B OE2 1 
ATOM   5340 N N   . ALA B 2 27  ? 26.887  40.139  78.026  1.00 122.35 ?  323 ALA B N   1 
ATOM   5341 C CA  . ALA B 2 27  ? 27.498  40.183  76.704  1.00 126.00 ?  323 ALA B CA  1 
ATOM   5342 C C   . ALA B 2 27  ? 26.683  40.986  75.696  1.00 124.06 ?  323 ALA B C   1 
ATOM   5343 O O   . ALA B 2 27  ? 27.217  41.359  74.642  1.00 122.71 ?  323 ALA B O   1 
ATOM   5344 C CB  . ALA B 2 27  ? 27.715  38.756  76.194  1.00 122.38 ?  323 ALA B CB  1 
ATOM   5345 N N   . VAL B 2 28  ? 25.412  41.268  75.989  1.00 120.82 ?  324 VAL B N   1 
ATOM   5346 C CA  . VAL B 2 28  ? 24.588  42.085  75.105  1.00 122.55 ?  324 VAL B CA  1 
ATOM   5347 C C   . VAL B 2 28  ? 24.429  43.508  75.632  1.00 123.07 ?  324 VAL B C   1 
ATOM   5348 O O   . VAL B 2 28  ? 24.011  44.402  74.873  1.00 116.74 ?  324 VAL B O   1 
ATOM   5349 C CB  . VAL B 2 28  ? 23.223  41.399  74.879  1.00 119.83 ?  324 VAL B CB  1 
ATOM   5350 C CG1 . VAL B 2 28  ? 22.416  42.097  73.802  1.00 117.58 ?  324 VAL B CG1 1 
ATOM   5351 C CG2 . VAL B 2 28  ? 23.454  39.957  74.489  1.00 109.79 ?  324 VAL B CG2 1 
ATOM   5352 N N   . SER B 2 29  ? 24.795  43.754  76.893  1.00 122.52 ?  325 SER B N   1 
ATOM   5353 C CA  . SER B 2 29  ? 24.770  45.086  77.474  1.00 120.57 ?  325 SER B CA  1 
ATOM   5354 C C   . SER B 2 29  ? 26.124  45.790  77.448  1.00 124.95 ?  325 SER B C   1 
ATOM   5355 O O   . SER B 2 29  ? 26.155  47.026  77.496  1.00 128.31 ?  325 SER B O   1 
ATOM   5356 C CB  . SER B 2 29  ? 24.271  45.013  78.922  1.00 115.30 ?  325 SER B CB  1 
ATOM   5357 O OG  . SER B 2 29  ? 25.039  44.100  79.689  1.00 115.54 ?  325 SER B OG  1 
ATOM   5358 N N   . ALA B 2 30  ? 27.229  45.038  77.349  1.00 121.33 ?  326 ALA B N   1 
ATOM   5359 C CA  . ALA B 2 30  ? 28.591  45.551  77.507  1.00 123.32 ?  326 ALA B CA  1 
ATOM   5360 C C   . ALA B 2 30  ? 28.837  46.891  76.818  1.00 126.48 ?  326 ALA B C   1 
ATOM   5361 O O   . ALA B 2 30  ? 29.622  47.708  77.314  1.00 129.14 ?  326 ALA B O   1 
ATOM   5362 C CB  . ALA B 2 30  ? 29.601  44.521  77.000  1.00 122.81 ?  326 ALA B CB  1 
ATOM   5363 N N   . ASN B 2 31  ? 28.178  47.141  75.689  1.00 119.89 ?  327 ASN B N   1 
ATOM   5364 C CA  . ASN B 2 31  ? 28.238  48.465  75.078  1.00 124.74 ?  327 ASN B CA  1 
ATOM   5365 C C   . ASN B 2 31  ? 26.986  48.685  74.232  1.00 122.13 ?  327 ASN B C   1 
ATOM   5366 O O   . ASN B 2 31  ? 26.037  47.896  74.276  1.00 120.02 ?  327 ASN B O   1 
ATOM   5367 C CB  . ASN B 2 31  ? 29.535  48.644  74.276  1.00 127.62 ?  327 ASN B CB  1 
ATOM   5368 C CG  . ASN B 2 31  ? 29.626  47.710  73.102  1.00 126.21 ?  327 ASN B CG  1 
ATOM   5369 O OD1 . ASN B 2 31  ? 29.091  47.990  72.020  1.00 122.34 ?  327 ASN B OD1 1 
ATOM   5370 N ND2 . ASN B 2 31  ? 30.314  46.586  73.301  1.00 124.77 ?  327 ASN B ND2 1 
ATOM   5371 N N   . ALA B 2 32  ? 26.994  49.777  73.459  1.00 122.81 ?  328 ALA B N   1 
ATOM   5372 C CA  . ALA B 2 32  ? 25.778  50.254  72.805  1.00 123.62 ?  328 ALA B CA  1 
ATOM   5373 C C   . ALA B 2 32  ? 25.319  49.293  71.718  1.00 129.19 ?  328 ALA B C   1 
ATOM   5374 O O   . ALA B 2 32  ? 24.160  48.861  71.710  1.00 133.52 ?  328 ALA B O   1 
ATOM   5375 C CB  . ALA B 2 32  ? 26.005  51.653  72.228  1.00 120.50 ?  328 ALA B CB  1 
ATOM   5376 N N   . THR B 2 33  ? 26.210  48.951  70.785  1.00 131.20 ?  329 THR B N   1 
ATOM   5377 C CA  . THR B 2 33  ? 25.899  47.988  69.734  1.00 130.02 ?  329 THR B CA  1 
ATOM   5378 C C   . THR B 2 33  ? 26.426  46.589  70.036  1.00 126.90 ?  329 THR B C   1 
ATOM   5379 O O   . THR B 2 33  ? 26.399  45.734  69.146  1.00 125.67 ?  329 THR B O   1 
ATOM   5380 C CB  . THR B 2 33  ? 26.436  48.462  68.374  1.00 129.26 ?  329 THR B CB  1 
ATOM   5381 O OG1 . THR B 2 33  ? 27.774  48.963  68.523  1.00 127.77 ?  329 THR B OG1 1 
ATOM   5382 C CG2 . THR B 2 33  ? 25.524  49.538  67.756  1.00 120.21 ?  329 THR B CG2 1 
ATOM   5383 N N   . ALA B 2 34  ? 26.885  46.329  71.271  1.00 126.06 ?  330 ALA B N   1 
ATOM   5384 C CA  . ALA B 2 34  ? 27.241  44.968  71.677  1.00 119.83 ?  330 ALA B CA  1 
ATOM   5385 C C   . ALA B 2 34  ? 26.121  43.983  71.398  1.00 118.17 ?  330 ALA B C   1 
ATOM   5386 O O   . ALA B 2 34  ? 26.361  42.772  71.371  1.00 117.89 ?  330 ALA B O   1 
ATOM   5387 C CB  . ALA B 2 34  ? 27.586  44.910  73.168  1.00 121.28 ?  330 ALA B CB  1 
ATOM   5388 N N   . ALA B 2 35  ? 24.897  44.479  71.220  1.00 124.81 ?  331 ALA B N   1 
ATOM   5389 C CA  . ALA B 2 35  ? 23.797  43.648  70.749  1.00 119.25 ?  331 ALA B CA  1 
ATOM   5390 C C   . ALA B 2 35  ? 23.984  43.280  69.285  1.00 114.50 ?  331 ALA B C   1 
ATOM   5391 O O   . ALA B 2 35  ? 24.114  42.102  68.938  1.00 116.56 ?  331 ALA B O   1 
ATOM   5392 C CB  . ALA B 2 35  ? 22.472  44.385  70.953  1.00 118.60 ?  331 ALA B CB  1 
ATOM   5393 N N   . THR B 2 36  ? 23.994  44.284  68.409  1.00 115.20 ?  332 THR B N   1 
ATOM   5394 C CA  . THR B 2 36  ? 24.175  44.043  66.981  1.00 116.43 ?  332 THR B CA  1 
ATOM   5395 C C   . THR B 2 36  ? 25.450  43.268  66.667  1.00 117.71 ?  332 THR B C   1 
ATOM   5396 O O   . THR B 2 36  ? 25.453  42.436  65.750  1.00 114.76 ?  332 THR B O   1 
ATOM   5397 C CB  . THR B 2 36  ? 24.145  45.371  66.220  1.00 120.91 ?  332 THR B CB  1 
ATOM   5398 O OG1 . THR B 2 36  ? 22.804  45.890  66.217  1.00 119.54 ?  332 THR B OG1 1 
ATOM   5399 C CG2 . THR B 2 36  ? 24.667  45.229  64.804  1.00 123.36 ?  332 THR B CG2 1 
ATOM   5400 N N   . THR B 2 37  ? 26.545  43.509  67.399  1.00 120.11 ?  333 THR B N   1 
ATOM   5401 C CA  . THR B 2 37  ? 27.777  42.797  67.064  1.00 115.58 ?  333 THR B CA  1 
ATOM   5402 C C   . THR B 2 37  ? 27.566  41.293  67.173  1.00 116.47 ?  333 THR B C   1 
ATOM   5403 O O   . THR B 2 37  ? 27.806  40.552  66.217  1.00 120.53 ?  333 THR B O   1 
ATOM   5404 C CB  . THR B 2 37  ? 28.950  43.209  67.960  1.00 118.15 ?  333 THR B CB  1 
ATOM   5405 O OG1 . THR B 2 37  ? 28.732  42.729  69.299  1.00 122.76 ?  333 THR B OG1 1 
ATOM   5406 C CG2 . THR B 2 37  ? 29.119  44.731  67.970  1.00 121.21 ?  333 THR B CG2 1 
ATOM   5407 N N   . VAL B 2 38  ? 27.075  40.827  68.325  1.00 117.49 ?  334 VAL B N   1 
ATOM   5408 C CA  . VAL B 2 38  ? 27.077  39.395  68.590  1.00 116.86 ?  334 VAL B CA  1 
ATOM   5409 C C   . VAL B 2 38  ? 25.989  38.685  67.785  1.00 110.65 ?  334 VAL B C   1 
ATOM   5410 O O   . VAL B 2 38  ? 26.088  37.477  67.558  1.00 111.76 ?  334 VAL B O   1 
ATOM   5411 C CB  . VAL B 2 38  ? 26.934  39.116  70.104  1.00 110.46 ?  334 VAL B CB  1 
ATOM   5412 C CG1 . VAL B 2 38  ? 25.520  39.360  70.584  1.00 100.49 ?  334 VAL B CG1 1 
ATOM   5413 C CG2 . VAL B 2 38  ? 27.475  37.724  70.475  1.00 113.41 ?  334 VAL B CG2 1 
ATOM   5414 N N   . LEU B 2 39  ? 24.960  39.399  67.332  1.00 106.55 ?  335 LEU B N   1 
ATOM   5415 C CA  . LEU B 2 39  ? 24.035  38.866  66.337  1.00 106.55 ?  335 LEU B CA  1 
ATOM   5416 C C   . LEU B 2 39  ? 24.513  39.037  64.900  1.00 114.46 ?  335 LEU B C   1 
ATOM   5417 O O   . LEU B 2 39  ? 23.795  38.633  63.977  1.00 113.65 ?  335 LEU B O   1 
ATOM   5418 C CB  . LEU B 2 39  ? 22.663  39.525  66.440  1.00 112.75 ?  335 LEU B CB  1 
ATOM   5419 C CG  . LEU B 2 39  ? 21.575  39.026  67.380  1.00 107.02 ?  335 LEU B CG  1 
ATOM   5420 C CD1 . LEU B 2 39  ? 22.015  39.113  68.825  1.00 103.17 ?  335 LEU B CD1 1 
ATOM   5421 C CD2 . LEU B 2 39  ? 20.295  39.811  67.103  1.00 100.99 ?  335 LEU B CD2 1 
ATOM   5422 N N   . ARG B 2 40  ? 25.645  39.692  64.670  1.00 117.36 ?  336 ARG B N   1 
ATOM   5423 C CA  . ARG B 2 40  ? 26.273  39.633  63.362  1.00 114.30 ?  336 ARG B CA  1 
ATOM   5424 C C   . ARG B 2 40  ? 27.378  38.593  63.320  1.00 112.86 ?  336 ARG B C   1 
ATOM   5425 O O   . ARG B 2 40  ? 27.571  37.958  62.281  1.00 117.24 ?  336 ARG B O   1 
ATOM   5426 C CB  . ARG B 2 40  ? 26.821  41.009  62.964  1.00 117.93 ?  336 ARG B CB  1 
ATOM   5427 C CG  . ARG B 2 40  ? 26.804  41.256  61.463  1.00 121.41 ?  336 ARG B CG  1 
ATOM   5428 C CD  . ARG B 2 40  ? 27.544  42.539  61.063  1.00 127.57 ?  336 ARG B CD  1 
ATOM   5429 N NE  . ARG B 2 40  ? 26.913  43.776  61.541  1.00 135.82 ?  336 ARG B NE  1 
ATOM   5430 C CZ  . ARG B 2 40  ? 27.507  44.679  62.321  1.00 132.36 ?  336 ARG B CZ  1 
ATOM   5431 N NH1 . ARG B 2 40  ? 28.755  44.487  62.736  1.00 133.48 ?  336 ARG B NH1 1 
ATOM   5432 N NH2 . ARG B 2 40  ? 26.855  45.776  62.685  1.00 123.43 ?  336 ARG B NH2 1 
ATOM   5433 N N   . GLN B 2 41  ? 28.087  38.404  64.440  1.00 110.77 ?  337 GLN B N   1 
ATOM   5434 C CA  . GLN B 2 41  ? 28.934  37.242  64.704  1.00 117.91 ?  337 GLN B CA  1 
ATOM   5435 C C   . GLN B 2 41  ? 28.222  35.934  64.355  1.00 116.23 ?  337 GLN B C   1 
ATOM   5436 O O   . GLN B 2 41  ? 28.848  34.990  63.857  1.00 111.63 ?  337 GLN B O   1 
ATOM   5437 C CB  . GLN B 2 41  ? 29.353  37.234  66.187  1.00 121.11 ?  337 GLN B CB  1 
ATOM   5438 C CG  . GLN B 2 41  ? 30.532  36.316  66.587  1.00 129.70 ?  337 GLN B CG  1 
ATOM   5439 C CD  . GLN B 2 41  ? 31.907  36.871  66.222  1.00 133.22 ?  337 GLN B CD  1 
ATOM   5440 O OE1 . GLN B 2 41  ? 32.024  37.805  65.424  1.00 128.81 ?  337 GLN B OE1 1 
ATOM   5441 N NE2 . GLN B 2 41  ? 32.954  36.305  66.829  1.00 127.30 ?  337 GLN B NE2 1 
ATOM   5442 N N   . LEU B 2 42  ? 26.912  35.870  64.615  1.00 115.27 ?  338 LEU B N   1 
ATOM   5443 C CA  . LEU B 2 42  ? 26.156  34.636  64.441  1.00 110.40 ?  338 LEU B CA  1 
ATOM   5444 C C   . LEU B 2 42  ? 25.548  34.505  63.052  1.00 109.74 ?  338 LEU B C   1 
ATOM   5445 O O   . LEU B 2 42  ? 25.448  33.390  62.534  1.00 113.50 ?  338 LEU B O   1 
ATOM   5446 C CB  . LEU B 2 42  ? 25.046  34.520  65.491  1.00 102.21 ?  338 LEU B CB  1 
ATOM   5447 C CG  . LEU B 2 42  ? 25.507  34.246  66.923  1.00 103.95 ?  338 LEU B CG  1 
ATOM   5448 C CD1 . LEU B 2 42  ? 24.312  34.181  67.860  1.00 100.56 ?  338 LEU B CD1 1 
ATOM   5449 C CD2 . LEU B 2 42  ? 26.365  32.998  67.037  1.00 100.28 ?  338 LEU B CD2 1 
ATOM   5450 N N   . ASP B 2 43  ? 25.112  35.603  62.434  1.00 107.38 ?  339 ASP B N   1 
ATOM   5451 C CA  . ASP B 2 43  ? 24.683  35.505  61.043  1.00 110.02 ?  339 ASP B CA  1 
ATOM   5452 C C   . ASP B 2 43  ? 25.835  35.069  60.151  1.00 111.42 ?  339 ASP B C   1 
ATOM   5453 O O   . ASP B 2 43  ? 25.633  34.342  59.173  1.00 111.87 ?  339 ASP B O   1 
ATOM   5454 C CB  . ASP B 2 43  ? 24.108  36.836  60.557  1.00 119.15 ?  339 ASP B CB  1 
ATOM   5455 C CG  . ASP B 2 43  ? 22.611  36.952  60.791  1.00 119.85 ?  339 ASP B CG  1 
ATOM   5456 O OD1 . ASP B 2 43  ? 22.096  36.212  61.657  1.00 114.00 ?  339 ASP B OD1 1 
ATOM   5457 O OD2 . ASP B 2 43  ? 21.948  37.763  60.097  1.00 121.23 ?  339 ASP B OD2 1 
ATOM   5458 N N   . MET B 2 44  ? 27.053  35.494  60.478  1.00 113.67 ?  340 MET B N   1 
ATOM   5459 C CA  . MET B 2 44  ? 28.195  35.092  59.676  1.00 111.95 ?  340 MET B CA  1 
ATOM   5460 C C   . MET B 2 44  ? 28.660  33.684  60.038  1.00 111.98 ?  340 MET B C   1 
ATOM   5461 O O   . MET B 2 44  ? 29.076  32.932  59.155  1.00 115.84 ?  340 MET B O   1 
ATOM   5462 C CB  . MET B 2 44  ? 29.321  36.122  59.820  1.00 112.27 ?  340 MET B CB  1 
ATOM   5463 C CG  . MET B 2 44  ? 29.198  37.286  58.814  1.00 117.97 ?  340 MET B CG  1 
ATOM   5464 S SD  . MET B 2 44  ? 30.591  38.452  58.795  1.00 138.44 ?  340 MET B SD  1 
ATOM   5465 C CE  . MET B 2 44  ? 30.482  39.121  57.125  1.00 113.21 ?  340 MET B CE  1 
ATOM   5466 N N   . GLU B 2 45  ? 28.565  33.287  61.312  1.00 111.90 ?  341 GLU B N   1 
ATOM   5467 C CA  . GLU B 2 45  ? 28.895  31.909  61.679  1.00 108.39 ?  341 GLU B CA  1 
ATOM   5468 C C   . GLU B 2 45  ? 27.914  30.904  61.087  1.00 105.62 ?  341 GLU B C   1 
ATOM   5469 O O   . GLU B 2 45  ? 28.190  29.702  61.100  1.00 109.33 ?  341 GLU B O   1 
ATOM   5470 C CB  . GLU B 2 45  ? 28.949  31.757  63.211  1.00 116.45 ?  341 GLU B CB  1 
ATOM   5471 C CG  . GLU B 2 45  ? 29.476  30.393  63.754  1.00 118.19 ?  341 GLU B CG  1 
ATOM   5472 C CD  . GLU B 2 45  ? 30.983  30.154  63.561  1.00 126.59 ?  341 GLU B CD  1 
ATOM   5473 O OE1 . GLU B 2 45  ? 31.624  30.831  62.720  1.00 128.86 ?  341 GLU B OE1 1 
ATOM   5474 O OE2 . GLU B 2 45  ? 31.528  29.265  64.255  1.00 124.30 ?  341 GLU B OE2 1 
ATOM   5475 N N   . LEU B 2 46  ? 26.786  31.364  60.558  1.00 104.05 ?  342 LEU B N   1 
ATOM   5476 C CA  . LEU B 2 46  ? 25.796  30.498  59.933  1.00 100.46 ?  342 LEU B CA  1 
ATOM   5477 C C   . LEU B 2 46  ? 25.818  30.508  58.415  1.00 101.14 ?  342 LEU B C   1 
ATOM   5478 O O   . LEU B 2 46  ? 25.611  29.451  57.818  1.00 103.90 ?  342 LEU B O   1 
ATOM   5479 C CB  . LEU B 2 46  ? 24.406  30.830  60.473  1.00 102.53 ?  342 LEU B CB  1 
ATOM   5480 C CG  . LEU B 2 46  ? 23.087  30.344  59.873  1.00 103.31 ?  342 LEU B CG  1 
ATOM   5481 C CD1 . LEU B 2 46  ? 22.983  28.903  59.505  1.00 106.77 ?  342 LEU B CD1 1 
ATOM   5482 C CD2 . LEU B 2 46  ? 22.231  30.440  61.107  1.00 109.71 ?  342 LEU B CD2 1 
ATOM   5483 N N   . VAL B 2 47  ? 26.072  31.641  57.757  1.00 103.31 ?  343 VAL B N   1 
ATOM   5484 C CA  . VAL B 2 47  ? 26.450  31.568  56.346  1.00 103.07 ?  343 VAL B CA  1 
ATOM   5485 C C   . VAL B 2 47  ? 27.660  30.663  56.175  1.00 98.32  ?  343 VAL B C   1 
ATOM   5486 O O   . VAL B 2 47  ? 27.662  29.763  55.331  1.00 94.65  ?  343 VAL B O   1 
ATOM   5487 C CB  . VAL B 2 47  ? 26.703  32.966  55.762  1.00 101.45 ?  343 VAL B CB  1 
ATOM   5488 C CG1 . VAL B 2 47  ? 27.390  32.823  54.420  1.00 107.65 ?  343 VAL B CG1 1 
ATOM   5489 C CG2 . VAL B 2 47  ? 25.381  33.645  55.530  1.00 94.48  ?  343 VAL B CG2 1 
ATOM   5490 N N   . SER B 2 48  ? 28.698  30.894  56.984  1.00 99.76  ?  344 SER B N   1 
ATOM   5491 C CA  . SER B 2 48  ? 29.859  30.017  57.091  1.00 98.83  ?  344 SER B CA  1 
ATOM   5492 C C   . SER B 2 48  ? 29.510  28.531  57.046  1.00 102.07 ?  344 SER B C   1 
ATOM   5493 O O   . SER B 2 48  ? 30.125  27.758  56.308  1.00 102.98 ?  344 SER B O   1 
ATOM   5494 C CB  . SER B 2 48  ? 30.594  30.355  58.394  1.00 108.86 ?  344 SER B CB  1 
ATOM   5495 O OG  . SER B 2 48  ? 31.676  29.483  58.668  1.00 119.62 ?  344 SER B OG  1 
ATOM   5496 N N   . VAL B 2 49  ? 28.539  28.101  57.845  1.00 104.45 ?  345 VAL B N   1 
ATOM   5497 C CA  . VAL B 2 49  ? 28.287  26.668  57.947  1.00 99.39  ?  345 VAL B CA  1 
ATOM   5498 C C   . VAL B 2 49  ? 27.401  26.200  56.816  1.00 94.68  ?  345 VAL B C   1 
ATOM   5499 O O   . VAL B 2 49  ? 27.598  25.120  56.270  1.00 102.66 ?  345 VAL B O   1 
ATOM   5500 C CB  . VAL B 2 49  ? 27.675  26.314  59.306  1.00 103.53 ?  345 VAL B CB  1 
ATOM   5501 C CG1 . VAL B 2 49  ? 27.002  24.941  59.239  1.00 97.08  ?  345 VAL B CG1 1 
ATOM   5502 C CG2 . VAL B 2 49  ? 28.758  26.331  60.364  1.00 112.39 ?  345 VAL B CG2 1 
ATOM   5503 N N   . LYS B 2 50  ? 26.426  26.999  56.421  1.00 94.52  ?  346 LYS B N   1 
ATOM   5504 C CA  . LYS B 2 50  ? 25.571  26.565  55.334  1.00 94.14  ?  346 LYS B CA  1 
ATOM   5505 C C   . LYS B 2 50  ? 26.288  26.426  53.993  1.00 99.42  ?  346 LYS B C   1 
ATOM   5506 O O   . LYS B 2 50  ? 25.811  25.673  53.138  1.00 95.94  ?  346 LYS B O   1 
ATOM   5507 C CB  . LYS B 2 50  ? 24.404  27.492  55.146  1.00 93.20  ?  346 LYS B CB  1 
ATOM   5508 C CG  . LYS B 2 50  ? 23.287  27.162  56.130  1.00 99.84  ?  346 LYS B CG  1 
ATOM   5509 C CD  . LYS B 2 50  ? 22.126  28.151  56.124  1.00 102.83 ?  346 LYS B CD  1 
ATOM   5510 C CE  . LYS B 2 50  ? 21.197  28.023  54.934  1.00 100.67 ?  346 LYS B CE  1 
ATOM   5511 N NZ  . LYS B 2 50  ? 19.900  28.674  55.288  1.00 101.21 ?  346 LYS B NZ  1 
ATOM   5512 N N   . ARG B 2 51  ? 27.468  26.992  53.764  1.00 101.98 ?  347 ARG B N   1 
ATOM   5513 C CA  . ARG B 2 51  ? 28.086  26.538  52.513  1.00 104.31 ?  347 ARG B CA  1 
ATOM   5514 C C   . ARG B 2 51  ? 29.229  25.518  52.687  1.00 104.74 ?  347 ARG B C   1 
ATOM   5515 O O   . ARG B 2 51  ? 29.717  24.961  51.686  1.00 112.82 ?  347 ARG B O   1 
ATOM   5516 C CB  . ARG B 2 51  ? 28.632  27.725  51.717  1.00 105.29 ?  347 ARG B CB  1 
ATOM   5517 C CG  . ARG B 2 51  ? 29.944  28.270  52.219  1.00 99.74  ?  347 ARG B CG  1 
ATOM   5518 C CD  . ARG B 2 51  ? 29.902  28.988  53.451  1.00 113.25 ?  347 ARG B CD  1 
ATOM   5519 N NE  . ARG B 2 51  ? 30.980  29.905  53.618  1.00 124.82 ?  347 ARG B NE  1 
ATOM   5520 C CZ  . ARG B 2 51  ? 32.223  29.614  53.864  1.00 118.01 ?  347 ARG B CZ  1 
ATOM   5521 N NH1 . ARG B 2 51  ? 32.591  28.316  53.952  1.00 116.42 ?  347 ARG B NH1 1 
ATOM   5522 N NH2 . ARG B 2 51  ? 33.023  30.614  54.062  1.00 115.11 ?  347 ARG B NH2 1 
ATOM   5523 N N   . GLN B 2 52  ? 29.817  25.370  53.874  1.00 97.50  ?  348 GLN B N   1 
ATOM   5524 C CA  . GLN B 2 52  ? 30.550  24.114  53.998  1.00 101.91 ?  348 GLN B CA  1 
ATOM   5525 C C   . GLN B 2 52  ? 29.579  22.933  54.001  1.00 100.72 ?  348 GLN B C   1 
ATOM   5526 O O   . GLN B 2 52  ? 29.982  21.814  53.660  1.00 102.63 ?  348 GLN B O   1 
ATOM   5527 C CB  . GLN B 2 52  ? 31.453  24.048  55.242  1.00 100.07 ?  348 GLN B CB  1 
ATOM   5528 C CG  . GLN B 2 52  ? 30.839  24.382  56.603  1.00 112.69 ?  348 GLN B CG  1 
ATOM   5529 C CD  . GLN B 2 52  ? 31.610  23.741  57.798  1.00 116.73 ?  348 GLN B CD  1 
ATOM   5530 O OE1 . GLN B 2 52  ? 32.197  22.654  57.668  1.00 115.13 ?  348 GLN B OE1 1 
ATOM   5531 N NE2 . GLN B 2 52  ? 31.640  24.442  58.942  1.00 113.05 ?  348 GLN B NE2 1 
ATOM   5532 N N   . ILE B 2 53  ? 28.297  23.160  54.339  1.00 101.03 ?  349 ILE B N   1 
ATOM   5533 C CA  . ILE B 2 53  ? 27.280  22.134  54.098  1.00 97.46  ?  349 ILE B CA  1 
ATOM   5534 C C   . ILE B 2 53  ? 27.193  21.827  52.622  1.00 97.11  ?  349 ILE B C   1 
ATOM   5535 O O   . ILE B 2 53  ? 27.078  20.671  52.224  1.00 103.21 ?  349 ILE B O   1 
ATOM   5536 C CB  . ILE B 2 53  ? 25.899  22.567  54.625  1.00 99.82  ?  349 ILE B CB  1 
ATOM   5537 C CG1 . ILE B 2 53  ? 25.756  22.394  56.132  1.00 96.71  ?  349 ILE B CG1 1 
ATOM   5538 C CG2 . ILE B 2 53  ? 24.787  21.761  53.933  1.00 94.84  ?  349 ILE B CG2 1 
ATOM   5539 C CD1 . ILE B 2 53  ? 25.670  20.986  56.525  1.00 99.06  ?  349 ILE B CD1 1 
ATOM   5540 N N   . GLN B 2 54  ? 27.207  22.854  51.791  1.00 98.28  ?  350 GLN B N   1 
ATOM   5541 C CA  . GLN B 2 54  ? 26.807  22.637  50.417  1.00 101.09 ?  350 GLN B CA  1 
ATOM   5542 C C   . GLN B 2 54  ? 27.979  22.088  49.617  1.00 104.93 ?  350 GLN B C   1 
ATOM   5543 O O   . GLN B 2 54  ? 27.793  21.532  48.528  1.00 103.97 ?  350 GLN B O   1 
ATOM   5544 C CB  . GLN B 2 54  ? 26.341  23.952  49.813  1.00 98.06  ?  350 GLN B CB  1 
ATOM   5545 C CG  . GLN B 2 54  ? 25.394  23.835  48.661  1.00 105.68 ?  350 GLN B CG  1 
ATOM   5546 C CD  . GLN B 2 54  ? 25.082  25.183  48.059  1.00 127.21 ?  350 GLN B CD  1 
ATOM   5547 O OE1 . GLN B 2 54  ? 25.797  26.154  48.325  1.00 130.94 ?  350 GLN B OE1 1 
ATOM   5548 N NE2 . GLN B 2 54  ? 23.880  25.306  47.483  1.00 126.85 ?  350 GLN B NE2 1 
ATOM   5549 N N   . ASN B 2 55  ? 29.181  22.239  50.166  1.00 102.94 ?  351 ASN B N   1 
ATOM   5550 C CA  . ASN B 2 55  ? 30.468  21.881  49.599  1.00 100.28 ?  351 ASN B CA  1 
ATOM   5551 C C   . ASN B 2 55  ? 30.806  20.424  49.907  1.00 99.62  ?  351 ASN B C   1 
ATOM   5552 O O   . ASN B 2 55  ? 31.294  19.703  49.032  1.00 103.18 ?  351 ASN B O   1 
ATOM   5553 C CB  . ASN B 2 55  ? 31.494  22.881  50.149  1.00 99.37  ?  351 ASN B CB  1 
ATOM   5554 C CG  . ASN B 2 55  ? 32.837  22.836  49.463  1.00 101.30 ?  351 ASN B CG  1 
ATOM   5555 O OD1 . ASN B 2 55  ? 33.354  21.782  49.116  1.00 107.73 ?  351 ASN B OD1 1 
ATOM   5556 N ND2 . ASN B 2 55  ? 33.372  24.015  49.183  1.00 101.69 ?  351 ASN B ND2 1 
ATOM   5557 N N   . ILE B 2 56  ? 30.520  19.965  51.125  1.00 101.42 ?  352 ILE B N   1 
ATOM   5558 C CA  . ILE B 2 56  ? 30.598  18.541  51.431  1.00 93.41  ?  352 ILE B CA  1 
ATOM   5559 C C   . ILE B 2 56  ? 29.410  17.793  50.846  1.00 95.73  ?  352 ILE B C   1 
ATOM   5560 O O   . ILE B 2 56  ? 29.535  16.630  50.467  1.00 102.14 ?  352 ILE B O   1 
ATOM   5561 C CB  . ILE B 2 56  ? 30.713  18.350  52.948  1.00 92.44  ?  352 ILE B CB  1 
ATOM   5562 C CG1 . ILE B 2 56  ? 32.079  18.871  53.404  1.00 102.61 ?  352 ILE B CG1 1 
ATOM   5563 C CG2 . ILE B 2 56  ? 30.478  16.900  53.341  1.00 94.50  ?  352 ILE B CG2 1 
ATOM   5564 C CD1 . ILE B 2 56  ? 32.277  18.934  54.904  1.00 110.76 ?  352 ILE B CD1 1 
ATOM   5565 N N   . LYS B 2 57  ? 28.251  18.437  50.730  1.00 99.41  ?  353 LYS B N   1 
ATOM   5566 C CA  . LYS B 2 57  ? 27.134  17.836  50.008  1.00 97.41  ?  353 LYS B CA  1 
ATOM   5567 C C   . LYS B 2 57  ? 27.437  17.679  48.521  1.00 96.22  ?  353 LYS B C   1 
ATOM   5568 O O   . LYS B 2 57  ? 26.770  16.893  47.843  1.00 98.44  ?  353 LYS B O   1 
ATOM   5569 C CB  . LYS B 2 57  ? 25.868  18.678  50.255  1.00 99.76  ?  353 LYS B CB  1 
ATOM   5570 C CG  . LYS B 2 57  ? 24.603  18.313  49.489  1.00 99.63  ?  353 LYS B CG  1 
ATOM   5571 C CD  . LYS B 2 57  ? 23.361  19.073  50.009  1.00 101.16 ?  353 LYS B CD  1 
ATOM   5572 C CE  . LYS B 2 57  ? 23.075  18.781  51.494  1.00 108.98 ?  353 LYS B CE  1 
ATOM   5573 N NZ  . LYS B 2 57  ? 21.621  18.885  51.858  1.00 110.45 ?  353 LYS B NZ  1 
ATOM   5574 N N   . GLN B 2 58  ? 28.450  18.370  48.009  1.00 99.65  ?  354 GLN B N   1 
ATOM   5575 C CA  . GLN B 2 58  ? 28.855  18.274  46.610  1.00 101.38 ?  354 GLN B CA  1 
ATOM   5576 C C   . GLN B 2 58  ? 30.053  17.352  46.404  1.00 100.74 ?  354 GLN B C   1 
ATOM   5577 O O   . GLN B 2 58  ? 30.084  16.582  45.437  1.00 94.84  ?  354 GLN B O   1 
ATOM   5578 C CB  . GLN B 2 58  ? 29.186  19.668  46.085  1.00 100.00 ?  354 GLN B CB  1 
ATOM   5579 C CG  . GLN B 2 58  ? 29.013  19.848  44.603  1.00 102.41 ?  354 GLN B CG  1 
ATOM   5580 C CD  . GLN B 2 58  ? 28.744  21.305  44.255  1.00 115.85 ?  354 GLN B CD  1 
ATOM   5581 O OE1 . GLN B 2 58  ? 27.615  21.682  43.929  1.00 117.06 ?  354 GLN B OE1 1 
ATOM   5582 N NE2 . GLN B 2 58  ? 29.778  22.138  44.351  1.00 117.14 ?  354 GLN B NE2 1 
ATOM   5583 N N   . THR B 2 59  ? 31.055  17.454  47.283  1.00 98.09  ?  355 THR B N   1 
ATOM   5584 C CA  . THR B 2 59  ? 32.094  16.436  47.384  1.00 94.11  ?  355 THR B CA  1 
ATOM   5585 C C   . THR B 2 59  ? 31.491  15.039  47.488  1.00 97.18  ?  355 THR B C   1 
ATOM   5586 O O   . THR B 2 59  ? 31.942  14.102  46.817  1.00 98.84  ?  355 THR B O   1 
ATOM   5587 C CB  . THR B 2 59  ? 32.984  16.738  48.598  1.00 96.54  ?  355 THR B CB  1 
ATOM   5588 O OG1 . THR B 2 59  ? 33.845  17.847  48.298  1.00 100.83 ?  355 THR B OG1 1 
ATOM   5589 C CG2 . THR B 2 59  ? 33.820  15.522  49.018  1.00 95.02  ?  355 THR B CG2 1 
ATOM   5590 N N   . ASN B 2 60  ? 30.459  14.884  48.316  1.00 97.22  ?  356 ASN B N   1 
ATOM   5591 C CA  . ASN B 2 60  ? 29.848  13.582  48.535  1.00 90.98  ?  356 ASN B CA  1 
ATOM   5592 C C   . ASN B 2 60  ? 28.930  13.180  47.391  1.00 95.31  ?  356 ASN B C   1 
ATOM   5593 O O   . ASN B 2 60  ? 28.603  11.998  47.258  1.00 98.36  ?  356 ASN B O   1 
ATOM   5594 C CB  . ASN B 2 60  ? 29.072  13.590  49.853  1.00 83.70  ?  356 ASN B CB  1 
ATOM   5595 C CG  . ASN B 2 60  ? 29.933  13.201  51.032  1.00 93.93  ?  356 ASN B CG  1 
ATOM   5596 O OD1 . ASN B 2 60  ? 31.151  13.383  51.015  1.00 95.37  ?  356 ASN B OD1 1 
ATOM   5597 N ND2 . ASN B 2 60  ? 29.306  12.687  52.074  1.00 98.10  ?  356 ASN B ND2 1 
ATOM   5598 N N   . SER B 2 61  ? 28.485  14.135  46.577  1.00 96.22  ?  357 SER B N   1 
ATOM   5599 C CA  . SER B 2 61  ? 27.740  13.781  45.374  1.00 98.63  ?  357 SER B CA  1 
ATOM   5600 C C   . SER B 2 61  ? 28.656  13.175  44.318  1.00 101.98 ?  357 SER B C   1 
ATOM   5601 O O   . SER B 2 61  ? 28.214  12.372  43.489  1.00 99.22  ?  357 SER B O   1 
ATOM   5602 C CB  . SER B 2 61  ? 27.036  15.018  44.821  1.00 93.88  ?  357 SER B CB  1 
ATOM   5603 O OG  . SER B 2 61  ? 26.320  14.698  43.651  1.00 92.34  ?  357 SER B OG  1 
ATOM   5604 N N   . ALA B 2 62  ? 29.934  13.553  44.343  1.00 103.74 ?  358 ALA B N   1 
ATOM   5605 C CA  . ALA B 2 62  ? 30.916  13.052  43.394  1.00 96.82  ?  358 ALA B CA  1 
ATOM   5606 C C   . ALA B 2 62  ? 31.418  11.669  43.794  1.00 101.27 ?  358 ALA B C   1 
ATOM   5607 O O   . ALA B 2 62  ? 31.495  10.770  42.951  1.00 104.37 ?  358 ALA B O   1 
ATOM   5608 C CB  . ALA B 2 62  ? 32.073  14.046  43.286  1.00 96.07  ?  358 ALA B CB  1 
ATOM   5609 N N   . LEU B 2 63  ? 31.778  11.485  45.076  1.00 102.43 ?  359 LEU B N   1 
ATOM   5610 C CA  . LEU B 2 63  ? 32.115  10.153  45.585  1.00 99.36  ?  359 LEU B CA  1 
ATOM   5611 C C   . LEU B 2 63  ? 30.976  9.166   45.368  1.00 103.63 ?  359 LEU B C   1 
ATOM   5612 O O   . LEU B 2 63  ? 31.213  7.967   45.205  1.00 107.79 ?  359 LEU B O   1 
ATOM   5613 C CB  . LEU B 2 63  ? 32.448  10.189  47.082  1.00 94.50  ?  359 LEU B CB  1 
ATOM   5614 C CG  . LEU B 2 63  ? 33.626  10.964  47.677  1.00 102.15 ?  359 LEU B CG  1 
ATOM   5615 C CD1 . LEU B 2 63  ? 34.006  10.363  49.035  1.00 98.89  ?  359 LEU B CD1 1 
ATOM   5616 C CD2 . LEU B 2 63  ? 34.829  11.021  46.734  1.00 104.43 ?  359 LEU B CD2 1 
ATOM   5617 N N   . LYS B 2 64  ? 29.738  9.645   45.379  1.00 107.56 ?  360 LYS B N   1 
ATOM   5618 C CA  . LYS B 2 64  ? 28.587  8.774   45.190  1.00 109.27 ?  360 LYS B CA  1 
ATOM   5619 C C   . LYS B 2 64  ? 28.405  8.388   43.725  1.00 111.44 ?  360 LYS B C   1 
ATOM   5620 O O   . LYS B 2 64  ? 27.819  7.336   43.436  1.00 114.06 ?  360 LYS B O   1 
ATOM   5621 C CB  . LYS B 2 64  ? 27.345  9.479   45.750  1.00 112.45 ?  360 LYS B CB  1 
ATOM   5622 C CG  . LYS B 2 64  ? 26.063  8.674   45.867  1.00 111.14 ?  360 LYS B CG  1 
ATOM   5623 C CD  . LYS B 2 64  ? 25.002  9.521   46.581  1.00 121.25 ?  360 LYS B CD  1 
ATOM   5624 C CE  . LYS B 2 64  ? 24.596  10.725  45.720  1.00 124.61 ?  360 LYS B CE  1 
ATOM   5625 N NZ  . LYS B 2 64  ? 23.453  11.514  46.260  1.00 125.27 ?  360 LYS B NZ  1 
ATOM   5626 N N   . GLU B 2 65  ? 28.986  9.176   42.830  1.00 108.63 ?  361 GLU B N   1 
ATOM   5627 C CA  . GLU B 2 65  ? 28.882  8.900   41.379  1.00 112.01 ?  361 GLU B CA  1 
ATOM   5628 C C   . GLU B 2 65  ? 29.799  7.732   41.041  1.00 114.88 ?  361 GLU B C   1 
ATOM   5629 O O   . GLU B 2 65  ? 29.453  6.934   40.190  1.00 118.06 ?  361 GLU B O   1 
ATOM   5630 C CB  . GLU B 2 65  ? 29.355  10.126  40.609  1.00 112.84 ?  361 GLU B CB  1 
ATOM   5631 C CG  . GLU B 2 65  ? 29.072  10.062  39.127  1.00 124.11 ?  361 GLU B CG  1 
ATOM   5632 C CD  . GLU B 2 65  ? 27.729  9.470   38.754  1.00 136.45 ?  361 GLU B CD  1 
ATOM   5633 O OE1 . GLU B 2 65  ? 26.868  9.362   39.641  1.00 138.64 ?  361 GLU B OE1 1 
ATOM   5634 O OE2 . GLU B 2 65  ? 27.550  9.115   37.575  1.00 131.44 ?  361 GLU B OE2 1 
ATOM   5635 N N   . LYS B 2 66  ? 30.931  7.647   41.723  1.00 110.81 ?  362 LYS B N   1 
ATOM   5636 C CA  . LYS B 2 66  ? 31.928  6.576   41.504  1.00 106.65 ?  362 LYS B CA  1 
ATOM   5637 C C   . LYS B 2 66  ? 31.397  5.211   41.931  1.00 107.80 ?  362 LYS B C   1 
ATOM   5638 O O   . LYS B 2 66  ? 31.844  4.233   41.367  1.00 112.68 ?  362 LYS B O   1 
ATOM   5639 C CB  . LYS B 2 66  ? 33.221  6.908   42.238  1.00 97.93  ?  362 LYS B CB  1 
ATOM   5640 C CG  . LYS B 2 66  ? 33.980  8.087   41.668  1.00 99.26  ?  362 LYS B CG  1 
ATOM   5641 C CD  . LYS B 2 66  ? 35.239  8.343   42.430  1.00 99.43  ?  362 LYS B CD  1 
ATOM   5642 C CE  . LYS B 2 66  ? 35.888  9.650   42.048  1.00 108.49 ?  362 LYS B CE  1 
ATOM   5643 N NZ  . LYS B 2 66  ? 35.360  10.146  40.758  1.00 116.21 ?  362 LYS B NZ  1 
ATOM   5644 N N   . LEU B 2 67  ? 30.456  5.143   42.866  1.00 105.12 ?  363 LEU B N   1 
ATOM   5645 C CA  . LEU B 2 67  ? 29.940  3.842   43.361  1.00 108.06 ?  363 LEU B CA  1 
ATOM   5646 C C   . LEU B 2 67  ? 28.743  3.372   42.541  1.00 116.77 ?  363 LEU B C   1 
ATOM   5647 O O   . LEU B 2 67  ? 28.076  2.424   42.976  1.00 110.37 ?  363 LEU B O   1 
ATOM   5648 C CB  . LEU B 2 67  ? 29.519  4.001   44.817  1.00 100.43 ?  363 LEU B CB  1 
ATOM   5649 C CG  . LEU B 2 67  ? 30.653  4.343   45.765  1.00 99.90  ?  363 LEU B CG  1 
ATOM   5650 C CD1 . LEU B 2 67  ? 30.477  3.635   47.089  1.00 97.03  ?  363 LEU B CD1 1 
ATOM   5651 C CD2 . LEU B 2 67  ? 31.974  3.975   45.134  1.00 103.23 ?  363 LEU B CD2 1 
ATOM   5652 N N   . ASP B 2 68  ? 28.444  4.031   41.428  1.00 117.30 ?  364 ASP B N   1 
ATOM   5653 C CA  . ASP B 2 68  ? 27.287  3.602   40.615  1.00 119.74 ?  364 ASP B CA  1 
ATOM   5654 C C   . ASP B 2 68  ? 27.515  2.148   40.217  1.00 124.02 ?  364 ASP B C   1 
ATOM   5655 O O   . ASP B 2 68  ? 28.598  1.827   39.732  1.00 123.24 ?  364 ASP B O   1 
ATOM   5656 C CB  . ASP B 2 68  ? 27.180  4.463   39.362  1.00 124.47 ?  364 ASP B CB  1 
ATOM   5657 C CG  . ASP B 2 68  ? 27.553  3.708   38.102  1.00 130.89 ?  364 ASP B CG  1 
ATOM   5658 O OD1 . ASP B 2 68  ? 26.628  3.271   37.406  1.00 131.37 ?  364 ASP B OD1 1 
ATOM   5659 O OD2 . ASP B 2 68  ? 28.762  3.534   37.852  1.00 126.43 ?  364 ASP B OD2 1 
ATOM   5660 N N   . GLY B 2 69  ? 26.494  1.318   40.400  1.00 125.97 ?  365 GLY B N   1 
ATOM   5661 C CA  . GLY B 2 69  ? 26.563  -0.113  40.060  1.00 120.17 ?  365 GLY B CA  1 
ATOM   5662 C C   . GLY B 2 69  ? 27.024  -0.946  41.233  1.00 115.59 ?  365 GLY B C   1 
ATOM   5663 O O   . GLY B 2 69  ? 26.979  -2.166  41.135  1.00 116.66 ?  365 GLY B O   1 
ATOM   5664 N N   . GLY B 2 70  ? 27.416  -0.304  42.324  1.00 116.25 ?  366 GLY B N   1 
ATOM   5665 C CA  . GLY B 2 70  ? 27.876  -1.067  43.490  1.00 111.77 ?  366 GLY B CA  1 
ATOM   5666 C C   . GLY B 2 70  ? 29.009  -1.978  43.099  1.00 104.05 ?  366 GLY B C   1 
ATOM   5667 O O   . GLY B 2 70  ? 29.941  -1.519  42.455  1.00 95.88  ?  366 GLY B O   1 
ATOM   5668 N N   . ILE B 2 71  ? 28.899  -3.239  43.478  1.00 105.09 ?  367 ILE B N   1 
ATOM   5669 C CA  . ILE B 2 71  ? 29.937  -4.245  43.148  1.00 106.28 ?  367 ILE B CA  1 
ATOM   5670 C C   . ILE B 2 71  ? 29.198  -5.452  42.598  1.00 105.00 ?  367 ILE B C   1 
ATOM   5671 O O   . ILE B 2 71  ? 29.617  -6.551  42.858  1.00 108.03 ?  367 ILE B O   1 
ATOM   5672 C CB  . ILE B 2 71  ? 30.669  -4.629  44.433  1.00 98.12  ?  367 ILE B CB  1 
ATOM   5673 C CG1 . ILE B 2 71  ? 29.702  -5.193  45.466  1.00 92.41  ?  367 ILE B CG1 1 
ATOM   5674 C CG2 . ILE B 2 71  ? 31.416  -3.449  44.991  1.00 88.33  ?  367 ILE B CG2 1 
ATOM   5675 C CD1 . ILE B 2 71  ? 30.348  -5.437  46.788  1.00 87.05  ?  367 ILE B CD1 1 
ATOM   5676 N N   . GLU B 2 72  ? 28.148  -5.235  41.830  1.00 108.75 ?  368 GLU B N   1 
ATOM   5677 C CA  . GLU B 2 72  ? 27.374  -6.393  41.416  1.00 113.94 ?  368 GLU B CA  1 
ATOM   5678 C C   . GLU B 2 72  ? 28.071  -7.202  40.324  1.00 112.04 ?  368 GLU B C   1 
ATOM   5679 O O   . GLU B 2 72  ? 27.984  -8.437  40.357  1.00 110.01 ?  368 GLU B O   1 
ATOM   5680 C CB  . GLU B 2 72  ? 25.988  -5.907  41.032  1.00 115.42 ?  368 GLU B CB  1 
ATOM   5681 C CG  . GLU B 2 72  ? 25.439  -5.212  42.292  1.00 122.13 ?  368 GLU B CG  1 
ATOM   5682 C CD  . GLU B 2 72  ? 25.254  -6.173  43.441  1.00 124.00 ?  368 GLU B CD  1 
ATOM   5683 O OE1 . GLU B 2 72  ? 24.688  -7.270  43.250  1.00 126.54 ?  368 GLU B OE1 1 
ATOM   5684 O OE2 . GLU B 2 72  ? 25.848  -5.897  44.515  1.00 118.03 ?  368 GLU B OE2 1 
ATOM   5685 N N   . PRO B 2 73  ? 28.800  -6.588  39.379  1.00 110.17 ?  369 PRO B N   1 
ATOM   5686 C CA  . PRO B 2 73  ? 29.642  -7.404  38.483  1.00 108.13 ?  369 PRO B CA  1 
ATOM   5687 C C   . PRO B 2 73  ? 30.696  -8.196  39.224  1.00 106.07 ?  369 PRO B C   1 
ATOM   5688 O O   . PRO B 2 73  ? 31.260  -9.141  38.665  1.00 112.56 ?  369 PRO B O   1 
ATOM   5689 C CB  . PRO B 2 73  ? 30.295  -6.381  37.549  1.00 112.76 ?  369 PRO B CB  1 
ATOM   5690 C CG  . PRO B 2 73  ? 29.681  -5.081  37.835  1.00 111.03 ?  369 PRO B CG  1 
ATOM   5691 C CD  . PRO B 2 73  ? 28.906  -5.145  39.089  1.00 110.82 ?  369 PRO B CD  1 
ATOM   5692 N N   . TYR B 2 74  ? 30.962  -7.851  40.473  1.00 104.14 ?  370 TYR B N   1 
ATOM   5693 C CA  . TYR B 2 74  ? 32.156  -8.255  41.195  1.00 99.99  ?  370 TYR B CA  1 
ATOM   5694 C C   . TYR B 2 74  ? 31.867  -9.350  42.196  1.00 99.20  ?  370 TYR B C   1 
ATOM   5695 O O   . TYR B 2 74  ? 32.782  -9.793  42.898  1.00 94.93  ?  370 TYR B O   1 
ATOM   5696 C CB  . TYR B 2 74  ? 32.725  -7.033  41.918  1.00 106.78 ?  370 TYR B CB  1 
ATOM   5697 C CG  . TYR B 2 74  ? 33.287  -6.026  40.963  1.00 106.60 ?  370 TYR B CG  1 
ATOM   5698 C CD1 . TYR B 2 74  ? 34.626  -5.728  40.935  1.00 106.31 ?  370 TYR B CD1 1 
ATOM   5699 C CD2 . TYR B 2 74  ? 32.469  -5.454  39.986  1.00 108.13 ?  370 TYR B CD2 1 
ATOM   5700 C CE1 . TYR B 2 74  ? 35.111  -4.829  40.031  1.00 107.21 ?  370 TYR B CE1 1 
ATOM   5701 C CE2 . TYR B 2 74  ? 32.957  -4.579  39.070  1.00 106.57 ?  370 TYR B CE2 1 
ATOM   5702 C CZ  . TYR B 2 74  ? 34.276  -4.261  39.099  1.00 107.05 ?  370 TYR B CZ  1 
ATOM   5703 O OH  . TYR B 2 74  ? 34.780  -3.379  38.184  1.00 109.20 ?  370 TYR B OH  1 
ATOM   5704 N N   . ARG B 2 75  ? 30.609  -9.771  42.284  1.00 106.02 ?  371 ARG B N   1 
ATOM   5705 C CA  . ARG B 2 75  ? 30.225  -10.866 43.149  1.00 111.19 ?  371 ARG B CA  1 
ATOM   5706 C C   . ARG B 2 75  ? 30.663  -12.207 42.603  1.00 111.29 ?  371 ARG B C   1 
ATOM   5707 O O   . ARG B 2 75  ? 30.942  -12.388 41.411  1.00 111.77 ?  371 ARG B O   1 
ATOM   5708 C CB  . ARG B 2 75  ? 28.718  -10.936 43.360  1.00 114.27 ?  371 ARG B CB  1 
ATOM   5709 C CG  . ARG B 2 75  ? 28.277  -10.575 44.742  1.00 112.94 ?  371 ARG B CG  1 
ATOM   5710 C CD  . ARG B 2 75  ? 28.025  -9.131  44.964  1.00 118.06 ?  371 ARG B CD  1 
ATOM   5711 N NE  . ARG B 2 75  ? 27.627  -8.981  46.361  1.00 122.80 ?  371 ARG B NE  1 
ATOM   5712 C CZ  . ARG B 2 75  ? 27.115  -7.876  46.888  1.00 122.10 ?  371 ARG B CZ  1 
ATOM   5713 N NH1 . ARG B 2 75  ? 26.897  -6.816  46.122  1.00 119.97 ?  371 ARG B NH1 1 
ATOM   5714 N NH2 . ARG B 2 75  ? 26.796  -7.840  48.172  1.00 116.44 ?  371 ARG B NH2 1 
ATOM   5715 N N   . LEU B 2 76  ? 30.675  -13.165 43.513  1.00 110.66 ?  372 LEU B N   1 
ATOM   5716 C CA  . LEU B 2 76  ? 30.828  -14.564 43.219  1.00 114.86 ?  372 LEU B CA  1 
ATOM   5717 C C   . LEU B 2 76  ? 29.653  -15.289 43.849  1.00 121.82 ?  372 LEU B C   1 
ATOM   5718 O O   . LEU B 2 76  ? 29.242  -14.954 44.971  1.00 122.03 ?  372 LEU B O   1 
ATOM   5719 C CB  . LEU B 2 76  ? 32.145  -15.103 43.781  1.00 109.78 ?  372 LEU B CB  1 
ATOM   5720 C CG  . LEU B 2 76  ? 33.336  -14.452 43.091  1.00 100.86 ?  372 LEU B CG  1 
ATOM   5721 C CD1 . LEU B 2 76  ? 34.642  -14.941 43.676  1.00 97.64  ?  372 LEU B CD1 1 
ATOM   5722 C CD2 . LEU B 2 76  ? 33.281  -14.690 41.579  1.00 99.90  ?  372 LEU B CD2 1 
ATOM   5723 N N   . PRO B 2 77  ? 29.075  -16.258 43.152  1.00 121.90 ?  373 PRO B N   1 
ATOM   5724 C CA  . PRO B 2 77  ? 27.997  -17.031 43.763  1.00 123.84 ?  373 PRO B CA  1 
ATOM   5725 C C   . PRO B 2 77  ? 28.465  -17.755 45.015  1.00 127.87 ?  373 PRO B C   1 
ATOM   5726 O O   . PRO B 2 77  ? 29.651  -18.003 45.229  1.00 122.70 ?  373 PRO B O   1 
ATOM   5727 C CB  . PRO B 2 77  ? 27.592  -18.025 42.676  1.00 121.72 ?  373 PRO B CB  1 
ATOM   5728 C CG  . PRO B 2 77  ? 28.291  -17.663 41.476  1.00 121.30 ?  373 PRO B CG  1 
ATOM   5729 C CD  . PRO B 2 77  ? 29.211  -16.512 41.710  1.00 113.78 ?  373 PRO B CD  1 
ATOM   5730 N N   . GLU B 2 78  ? 27.486  -18.090 45.840  1.00 135.00 ?  374 GLU B N   1 
ATOM   5731 C CA  . GLU B 2 78  ? 27.658  -18.839 47.071  1.00 140.32 ?  374 GLU B CA  1 
ATOM   5732 C C   . GLU B 2 78  ? 27.732  -20.308 46.812  1.00 143.58 ?  374 GLU B C   1 
ATOM   5733 O O   . GLU B 2 78  ? 26.748  -20.870 46.343  1.00 139.63 ?  374 GLU B O   1 
ATOM   5734 C CB  . GLU B 2 78  ? 26.508  -18.524 48.010  1.00 141.88 ?  374 GLU B CB  1 
ATOM   5735 C CG  . GLU B 2 78  ? 26.972  -17.218 48.833  1.00 148.45 ?  374 GLU B CG  1 
ATOM   5736 C CD  . GLU B 2 78  ? 25.898  -16.526 49.685  1.00 152.20 ?  374 GLU B CD  1 
ATOM   5737 O OE1 . GLU B 2 78  ? 24.704  -16.656 49.227  1.00 152.94 ?  374 GLU B OE1 1 
ATOM   5738 O OE2 . GLU B 2 78  ? 26.226  -16.154 50.896  1.00 147.54 ?  374 GLU B OE2 1 
ATOM   5739 N N   . VAL B 2 79  ? 28.877  -20.915 47.154  1.00 146.67 ?  375 VAL B N   1 
ATOM   5740 C CA  . VAL B 2 79  ? 29.050  -22.366 47.103  1.00 143.05 ?  375 VAL B CA  1 
ATOM   5741 C C   . VAL B 2 79  ? 28.495  -23.002 48.373  1.00 144.89 ?  375 VAL B C   1 
ATOM   5742 O O   . VAL B 2 79  ? 28.924  -22.703 49.495  1.00 144.28 ?  375 VAL B O   1 
ATOM   5743 C CB  . VAL B 2 79  ? 30.516  -22.769 46.859  1.00 142.75 ?  375 VAL B CB  1 
ATOM   5744 C CG1 . VAL B 2 79  ? 30.912  -22.452 45.431  1.00 136.77 ?  375 VAL B CG1 1 
ATOM   5745 C CG2 . VAL B 2 79  ? 31.489  -22.020 47.824  1.00 141.49 ?  375 VAL B CG2 1 
ATOM   5746 N N   . ILE B 2 80  ? 27.501  -23.852 48.180  1.00 145.98 ?  376 ILE B N   1 
ATOM   5747 C CA  . ILE B 2 80  ? 26.829  -24.601 49.225  1.00 147.62 ?  376 ILE B CA  1 
ATOM   5748 C C   . ILE B 2 80  ? 27.403  -26.011 49.164  1.00 150.28 ?  376 ILE B C   1 
ATOM   5749 O O   . ILE B 2 80  ? 27.183  -26.736 48.184  1.00 149.49 ?  376 ILE B O   1 
ATOM   5750 C CB  . ILE B 2 80  ? 25.309  -24.580 49.004  1.00 145.90 ?  376 ILE B CB  1 
ATOM   5751 C CG1 . ILE B 2 80  ? 24.979  -24.782 47.505  1.00 142.80 ?  376 ILE B CG1 1 
ATOM   5752 C CG2 . ILE B 2 80  ? 24.730  -23.256 49.497  1.00 135.26 ?  376 ILE B CG2 1 
ATOM   5753 C CD1 . ILE B 2 80  ? 23.501  -25.050 47.199  1.00 131.00 ?  376 ILE B CD1 1 
ATOM   5754 N N   . GLN B 2 81  ? 28.180  -26.402 50.177  1.00 149.60 ?  377 GLN B N   1 
ATOM   5755 C CA  . GLN B 2 81  ? 28.747  -27.748 50.179  1.00 151.07 ?  377 GLN B CA  1 
ATOM   5756 C C   . GLN B 2 81  ? 28.741  -28.335 51.584  1.00 146.07 ?  377 GLN B C   1 
ATOM   5757 O O   . GLN B 2 81  ? 29.153  -27.680 52.550  1.00 138.37 ?  377 GLN B O   1 
ATOM   5758 C CB  . GLN B 2 81  ? 30.164  -27.768 49.575  1.00 149.14 ?  377 GLN B CB  1 
ATOM   5759 C CG  . GLN B 2 81  ? 31.289  -27.165 50.410  1.00 142.47 ?  377 GLN B CG  1 
ATOM   5760 C CD  . GLN B 2 81  ? 32.665  -27.583 49.896  1.00 137.54 ?  377 GLN B CD  1 
ATOM   5761 O OE1 . GLN B 2 81  ? 32.941  -28.776 49.711  1.00 138.04 ?  377 GLN B OE1 1 
ATOM   5762 N NE2 . GLN B 2 81  ? 33.529  -26.599 49.650  1.00 128.18 ?  377 GLN B NE2 1 
ATOM   5763 N N   . LYS B 2 82  ? 28.267  -29.578 51.673  1.00 146.11 ?  378 LYS B N   1 
ATOM   5764 C CA  . LYS B 2 82  ? 28.080  -30.248 52.952  1.00 146.04 ?  378 LYS B CA  1 
ATOM   5765 C C   . LYS B 2 82  ? 29.435  -30.528 53.607  1.00 143.47 ?  378 LYS B C   1 
ATOM   5766 O O   . LYS B 2 82  ? 30.345  -31.074 52.971  1.00 140.65 ?  378 LYS B O   1 
ATOM   5767 C CB  . LYS B 2 82  ? 27.286  -31.547 52.742  1.00 143.29 ?  378 LYS B CB  1 
ATOM   5768 C CG  . LYS B 2 82  ? 25.815  -31.360 52.288  1.00 137.09 ?  378 LYS B CG  1 
ATOM   5769 C CD  . LYS B 2 82  ? 24.940  -32.570 52.680  1.00 142.16 ?  378 LYS B CD  1 
ATOM   5770 C CE  . LYS B 2 82  ? 23.488  -32.456 52.179  1.00 139.71 ?  378 LYS B CE  1 
ATOM   5771 N NZ  . LYS B 2 82  ? 22.655  -33.675 52.489  1.00 122.05 ?  378 LYS B NZ  1 
ATOM   5772 N N   . CYS B 2 83  ? 29.568  -30.139 54.878  1.00 135.12 ?  379 CYS B N   1 
ATOM   5773 C CA  . CYS B 2 83  ? 30.820  -30.305 55.612  1.00 132.81 ?  379 CYS B CA  1 
ATOM   5774 C C   . CYS B 2 83  ? 31.158  -31.777 55.852  1.00 137.60 ?  379 CYS B C   1 
ATOM   5775 O O   . CYS B 2 83  ? 30.295  -32.579 56.218  1.00 140.14 ?  379 CYS B O   1 
ATOM   5776 C CB  . CYS B 2 83  ? 30.741  -29.577 56.950  1.00 130.56 ?  379 CYS B CB  1 
ATOM   5777 S SG  . CYS B 2 83  ? 32.327  -29.397 57.799  1.00 131.19 ?  379 CYS B SG  1 
ATOM   5778 N N   . ASN B 2 84  ? 32.438  -32.118 55.679  1.00 136.65 ?  380 ASN B N   1 
ATOM   5779 C CA  . ASN B 2 84  ? 32.929  -33.489 55.730  1.00 136.80 ?  380 ASN B CA  1 
ATOM   5780 C C   . ASN B 2 84  ? 33.947  -33.647 56.859  1.00 133.37 ?  380 ASN B C   1 
ATOM   5781 O O   . ASN B 2 84  ? 34.503  -32.673 57.373  1.00 129.36 ?  380 ASN B O   1 
ATOM   5782 C CB  . ASN B 2 84  ? 33.553  -33.899 54.378  1.00 135.26 ?  380 ASN B CB  1 
ATOM   5783 C CG  . ASN B 2 84  ? 33.561  -35.410 54.161  1.00 135.70 ?  380 ASN B CG  1 
ATOM   5784 O OD1 . ASN B 2 84  ? 34.449  -36.114 54.646  1.00 130.95 ?  380 ASN B OD1 1 
ATOM   5785 N ND2 . ASN B 2 84  ? 32.570  -35.910 53.422  1.00 131.34 ?  380 ASN B ND2 1 
ATOM   5786 N N   . ALA B 2 85  ? 34.191  -34.898 57.240  1.00 131.25 ?  381 ALA B N   1 
ATOM   5787 C CA  . ALA B 2 85  ? 35.041  -35.207 58.380  1.00 127.46 ?  381 ALA B CA  1 
ATOM   5788 C C   . ALA B 2 85  ? 36.474  -35.537 57.986  1.00 130.66 ?  381 ALA B C   1 
ATOM   5789 O O   . ALA B 2 85  ? 37.414  -35.069 58.636  1.00 120.42 ?  381 ALA B O   1 
ATOM   5790 C CB  . ALA B 2 85  ? 34.442  -36.379 59.162  1.00 133.71 ?  381 ALA B CB  1 
ATOM   5791 N N   . ARG B 2 86  ? 36.634  -36.438 57.027  1.00 137.30 ?  382 ARG B N   1 
ATOM   5792 C CA  . ARG B 2 86  ? 38.003  -36.903 56.701  1.00 137.57 ?  382 ARG B CA  1 
ATOM   5793 C C   . ARG B 2 86  ? 38.820  -35.778 56.083  1.00 137.28 ?  382 ARG B C   1 
ATOM   5794 O O   . ARG B 2 86  ? 38.266  -34.933 55.385  1.00 132.15 ?  382 ARG B O   1 
ATOM   5795 C CB  . ARG B 2 86  ? 37.988  -38.158 55.828  1.00 137.14 ?  382 ARG B CB  1 
ATOM   5796 C CG  . ARG B 2 86  ? 37.805  -37.878 54.347  1.00 144.90 ?  382 ARG B CG  1 
ATOM   5797 C CD  . ARG B 2 86  ? 37.235  -39.090 53.646  1.00 144.68 ?  382 ARG B CD  1 
ATOM   5798 N NE  . ARG B 2 86  ? 38.259  -39.705 52.824  1.00 151.61 ?  382 ARG B NE  1 
ATOM   5799 C CZ  . ARG B 2 86  ? 39.479  -39.987 53.250  1.00 159.20 ?  382 ARG B CZ  1 
ATOM   5800 N NH1 . ARG B 2 86  ? 40.349  -40.547 52.430  1.00 154.99 ?  382 ARG B NH1 1 
ATOM   5801 N NH2 . ARG B 2 86  ? 39.820  -39.712 54.494  1.00 159.29 ?  382 ARG B NH2 1 
ATOM   5802 N N   . TRP B 2 87  ? 40.115  -35.803 56.350  1.00 139.15 ?  383 TRP B N   1 
ATOM   5803 C CA  . TRP B 2 87  ? 41.030  -34.783 55.798  1.00 128.03 ?  383 TRP B CA  1 
ATOM   5804 C C   . TRP B 2 87  ? 41.690  -35.407 54.579  1.00 133.44 ?  383 TRP B C   1 
ATOM   5805 O O   . TRP B 2 87  ? 42.535  -36.263 54.773  1.00 139.28 ?  383 TRP B O   1 
ATOM   5806 C CB  . TRP B 2 87  ? 42.118  -34.478 56.819  1.00 119.97 ?  383 TRP B CB  1 
ATOM   5807 C CG  . TRP B 2 87  ? 41.726  -33.468 57.840  1.00 124.26 ?  383 TRP B CG  1 
ATOM   5808 C CD1 . TRP B 2 87  ? 41.054  -33.695 58.997  1.00 128.12 ?  383 TRP B CD1 1 
ATOM   5809 C CD2 . TRP B 2 87  ? 42.001  -32.066 57.805  1.00 122.61 ?  383 TRP B CD2 1 
ATOM   5810 N NE1 . TRP B 2 87  ? 40.886  -32.525 59.680  1.00 129.43 ?  383 TRP B NE1 1 
ATOM   5811 C CE2 . TRP B 2 87  ? 41.453  -31.510 58.969  1.00 119.24 ?  383 TRP B CE2 1 
ATOM   5812 C CE3 . TRP B 2 87  ? 42.646  -31.227 56.906  1.00 119.27 ?  383 TRP B CE3 1 
ATOM   5813 C CZ2 . TRP B 2 87  ? 41.537  -30.158 59.257  1.00 112.74 ?  383 TRP B CZ2 1 
ATOM   5814 C CZ3 . TRP B 2 87  ? 42.729  -29.889 57.191  1.00 109.98 ?  383 TRP B CZ3 1 
ATOM   5815 C CH2 . TRP B 2 87  ? 42.183  -29.362 58.350  1.00 110.14 ?  383 TRP B CH2 1 
ATOM   5816 N N   . THR B 2 88  ? 41.343  -34.991 53.370  1.00 126.35 ?  384 THR B N   1 
ATOM   5817 C CA  . THR B 2 88  ? 42.063  -35.585 52.224  1.00 130.80 ?  384 THR B CA  1 
ATOM   5818 C C   . THR B 2 88  ? 43.415  -34.889 52.115  1.00 117.63 ?  384 THR B C   1 
ATOM   5819 O O   . THR B 2 88  ? 43.512  -33.744 52.531  1.00 112.02 ?  384 THR B O   1 
ATOM   5820 C CB  . THR B 2 88  ? 41.227  -35.539 50.949  1.00 131.14 ?  384 THR B CB  1 
ATOM   5821 O OG1 . THR B 2 88  ? 41.738  -34.510 50.113  1.00 114.73 ?  384 THR B OG1 1 
ATOM   5822 C CG2 . THR B 2 88  ? 39.769  -35.288 51.230  1.00 130.33 ?  384 THR B CG2 1 
ATOM   5823 N N   . THR B 2 89  ? 44.377  -35.489 51.426  1.00 116.11 ?  385 THR B N   1 
ATOM   5824 C CA  . THR B 2 89  ? 45.722  -34.876 51.309  1.00 102.47 ?  385 THR B CA  1 
ATOM   5825 C C   . THR B 2 89  ? 45.614  -33.506 50.649  1.00 103.55 ?  385 THR B C   1 
ATOM   5826 O O   . THR B 2 89  ? 46.297  -32.609 51.066  1.00 86.59  ?  385 THR B O   1 
ATOM   5827 C CB  . THR B 2 89  ? 46.660  -35.756 50.489  1.00 95.58  ?  385 THR B CB  1 
ATOM   5828 O OG1 . THR B 2 89  ? 46.450  -37.098 50.903  1.00 91.11  ?  385 THR B OG1 1 
ATOM   5829 C CG2 . THR B 2 89  ? 48.109  -35.426 50.727  1.00 87.89  ?  385 THR B CG2 1 
ATOM   5830 N N   . GLU B 2 90  ? 44.764  -33.350 49.649  1.00 113.83 ?  386 GLU B N   1 
ATOM   5831 C CA  . GLU B 2 90  ? 44.607  -32.023 49.034  1.00 105.79 ?  386 GLU B CA  1 
ATOM   5832 C C   . GLU B 2 90  ? 44.114  -31.059 50.106  1.00 102.62 ?  386 GLU B C   1 
ATOM   5833 O O   . GLU B 2 90  ? 44.716  -30.018 50.244  1.00 94.66  ?  386 GLU B O   1 
ATOM   5834 C CB  . GLU B 2 90  ? 43.629  -32.161 47.874  1.00 114.32 ?  386 GLU B CB  1 
ATOM   5835 C CG  . GLU B 2 90  ? 42.633  -31.032 47.747  1.00 122.55 ?  386 GLU B CG  1 
ATOM   5836 C CD  . GLU B 2 90  ? 41.615  -31.268 46.645  1.00 136.54 ?  386 GLU B CD  1 
ATOM   5837 O OE1 . GLU B 2 90  ? 41.007  -30.289 46.175  1.00 135.51 ?  386 GLU B OE1 1 
ATOM   5838 O OE2 . GLU B 2 90  ? 41.439  -32.435 46.256  1.00 133.87 ?  386 GLU B OE2 1 
ATOM   5839 N N   . GLU B 2 91  ? 43.141  -31.445 50.926  1.00 109.62 ?  387 GLU B N   1 
ATOM   5840 C CA  . GLU B 2 91  ? 42.646  -30.503 51.958  1.00 106.70 ?  387 GLU B CA  1 
ATOM   5841 C C   . GLU B 2 91  ? 43.755  -30.196 52.943  1.00 93.17  ?  387 GLU B C   1 
ATOM   5842 O O   . GLU B 2 91  ? 43.884  -29.059 53.319  1.00 92.10  ?  387 GLU B O   1 
ATOM   5843 C CB  . GLU B 2 91  ? 41.424  -31.019 52.703  1.00 107.61 ?  387 GLU B CB  1 
ATOM   5844 C CG  . GLU B 2 91  ? 40.709  -32.124 51.983  1.00 111.36 ?  387 GLU B CG  1 
ATOM   5845 C CD  . GLU B 2 91  ? 39.202  -32.001 51.895  1.00 124.64 ?  387 GLU B CD  1 
ATOM   5846 O OE1 . GLU B 2 91  ? 38.708  -31.687 50.802  1.00 124.48 ?  387 GLU B OE1 1 
ATOM   5847 O OE2 . GLU B 2 91  ? 38.528  -32.234 52.911  1.00 124.23 ?  387 GLU B OE2 1 
ATOM   5848 N N   . GLN B 2 92  ? 44.555  -31.182 53.301  1.00 94.11  ?  388 GLN B N   1 
ATOM   5849 C CA  . GLN B 2 92  ? 45.647  -30.923 54.256  1.00 93.09  ?  388 GLN B CA  1 
ATOM   5850 C C   . GLN B 2 92  ? 46.574  -29.864 53.681  1.00 87.50  ?  388 GLN B C   1 
ATOM   5851 O O   . GLN B 2 92  ? 46.898  -28.946 54.384  1.00 77.94  ?  388 GLN B O   1 
ATOM   5852 C CB  . GLN B 2 92  ? 46.522  -32.164 54.270  1.00 100.89 ?  388 GLN B CB  1 
ATOM   5853 C CG  . GLN B 2 92  ? 46.685  -32.819 55.620  1.00 93.87  ?  388 GLN B CG  1 
ATOM   5854 C CD  . GLN B 2 92  ? 46.588  -34.301 55.426  1.00 93.62  ?  388 GLN B CD  1 
ATOM   5855 O OE1 . GLN B 2 92  ? 45.583  -34.801 54.966  1.00 102.40 ?  388 GLN B OE1 1 
ATOM   5856 N NE2 . GLN B 2 92  ? 47.645  -35.008 55.753  1.00 96.32  ?  388 GLN B NE2 1 
ATOM   5857 N N   . LEU B 2 93  ? 46.927  -29.999 52.410  1.00 99.91  ?  389 LEU B N   1 
ATOM   5858 C CA  . LEU B 2 93  ? 47.860  -29.085 51.721  1.00 84.25  ?  389 LEU B CA  1 
ATOM   5859 C C   . LEU B 2 93  ? 47.269  -27.695 51.651  1.00 85.92  ?  389 LEU B C   1 
ATOM   5860 O O   . LEU B 2 93  ? 47.998  -26.758 51.850  1.00 86.45  ?  389 LEU B O   1 
ATOM   5861 C CB  . LEU B 2 93  ? 48.140  -29.651 50.340  1.00 75.63  ?  389 LEU B CB  1 
ATOM   5862 C CG  . LEU B 2 93  ? 49.246  -30.684 50.352  1.00 72.70  ?  389 LEU B CG  1 
ATOM   5863 C CD1 . LEU B 2 93  ? 49.345  -31.362 49.016  1.00 72.27  ?  389 LEU B CD1 1 
ATOM   5864 C CD2 . LEU B 2 93  ? 50.551  -30.035 50.720  1.00 66.80  ?  389 LEU B CD2 1 
ATOM   5865 N N   . LEU B 2 94  ? 45.973  -27.582 51.420  1.00 89.40  ?  390 LEU B N   1 
ATOM   5866 C CA  . LEU B 2 94  ? 45.384  -26.227 51.373  1.00 86.22  ?  390 LEU B CA  1 
ATOM   5867 C C   . LEU B 2 94  ? 45.559  -25.575 52.736  1.00 84.22  ?  390 LEU B C   1 
ATOM   5868 O O   . LEU B 2 94  ? 46.008  -24.450 52.790  1.00 81.65  ?  390 LEU B O   1 
ATOM   5869 C CB  . LEU B 2 94  ? 43.901  -26.370 51.058  1.00 81.25  ?  390 LEU B CB  1 
ATOM   5870 C CG  . LEU B 2 94  ? 43.584  -26.550 49.586  1.00 84.40  ?  390 LEU B CG  1 
ATOM   5871 C CD1 . LEU B 2 94  ? 42.123  -26.860 49.388  1.00 88.95  ?  390 LEU B CD1 1 
ATOM   5872 C CD2 . LEU B 2 94  ? 43.940  -25.303 48.829  1.00 81.58  ?  390 LEU B CD2 1 
ATOM   5873 N N   . ALA B 2 95  ? 45.307  -26.322 53.798  1.00 86.29  ?  391 ALA B N   1 
ATOM   5874 C CA  . ALA B 2 95  ? 45.388  -25.765 55.155  1.00 80.78  ?  391 ALA B CA  1 
ATOM   5875 C C   . ALA B 2 95  ? 46.786  -25.243 55.437  1.00 81.85  ?  391 ALA B C   1 
ATOM   5876 O O   . ALA B 2 95  ? 46.889  -24.134 55.908  1.00 84.85  ?  391 ALA B O   1 
ATOM   5877 C CB  . ALA B 2 95  ? 45.053  -26.859 56.117  1.00 82.95  ?  391 ALA B CB  1 
ATOM   5878 N N   . VAL B 2 96  ? 47.815  -25.995 55.100  1.00 79.71  ?  392 VAL B N   1 
ATOM   5879 C CA  . VAL B 2 96  ? 49.177  -25.513 55.428  1.00 80.75  ?  392 VAL B CA  1 
ATOM   5880 C C   . VAL B 2 96  ? 49.429  -24.212 54.691  1.00 87.95  ?  392 VAL B C   1 
ATOM   5881 O O   . VAL B 2 96  ? 50.126  -23.377 55.203  1.00 88.29  ?  392 VAL B O   1 
ATOM   5882 C CB  . VAL B 2 96  ? 50.229  -26.534 55.011  1.00 83.38  ?  392 VAL B CB  1 
ATOM   5883 C CG1 . VAL B 2 96  ? 51.510  -25.825 54.643  1.00 81.30  ?  392 VAL B CG1 1 
ATOM   5884 C CG2 . VAL B 2 96  ? 50.469  -27.524 56.120  1.00 87.10  ?  392 VAL B CG2 1 
ATOM   5885 N N   . GLN B 2 97  ? 48.905  -24.091 53.492  1.00 87.75  ?  393 GLN B N   1 
ATOM   5886 C CA  . GLN B 2 97  ? 49.108  -22.835 52.784  1.00 87.33  ?  393 GLN B CA  1 
ATOM   5887 C C   . GLN B 2 97  ? 48.250  -21.721 53.364  1.00 88.82  ?  393 GLN B C   1 
ATOM   5888 O O   . GLN B 2 97  ? 48.690  -20.566 53.435  1.00 91.25  ?  393 GLN B O   1 
ATOM   5889 C CB  . GLN B 2 97  ? 48.824  -23.029 51.310  1.00 85.44  ?  393 GLN B CB  1 
ATOM   5890 C CG  . GLN B 2 97  ? 49.947  -23.712 50.599  1.00 80.49  ?  393 GLN B CG  1 
ATOM   5891 C CD  . GLN B 2 97  ? 49.656  -23.813 49.137  1.00 81.97  ?  393 GLN B CD  1 
ATOM   5892 O OE1 . GLN B 2 97  ? 48.800  -24.610 48.723  1.00 78.00  ?  393 GLN B OE1 1 
ATOM   5893 N NE2 . GLN B 2 97  ? 50.294  -22.946 48.341  1.00 81.52  ?  393 GLN B NE2 1 
ATOM   5894 N N   . ALA B 2 98  ? 47.022  -22.049 53.772  1.00 87.66  ?  394 ALA B N   1 
ATOM   5895 C CA  . ALA B 2 98  ? 46.166  -21.068 54.428  1.00 87.64  ?  394 ALA B CA  1 
ATOM   5896 C C   . ALA B 2 98  ? 46.798  -20.576 55.723  1.00 89.48  ?  394 ALA B C   1 
ATOM   5897 O O   . ALA B 2 98  ? 46.805  -19.373 56.010  1.00 86.70  ?  394 ALA B O   1 
ATOM   5898 C CB  . ALA B 2 98  ? 44.791  -21.680 54.688  1.00 83.69  ?  394 ALA B CB  1 
ATOM   5899 N N   . ILE B 2 99  ? 47.346  -21.497 56.512  1.00 90.17  ?  395 ILE B N   1 
ATOM   5900 C CA  . ILE B 2 99  ? 48.062  -21.116 57.725  1.00 90.73  ?  395 ILE B CA  1 
ATOM   5901 C C   . ILE B 2 99  ? 49.156  -20.114 57.401  1.00 92.45  ?  395 ILE B C   1 
ATOM   5902 O O   . ILE B 2 99  ? 49.293  -19.087 58.069  1.00 102.43 ?  395 ILE B O   1 
ATOM   5903 C CB  . ILE B 2 99  ? 48.629  -22.359 58.433  1.00 94.26  ?  395 ILE B CB  1 
ATOM   5904 C CG1 . ILE B 2 99  ? 47.517  -23.323 58.845  1.00 93.62  ?  395 ILE B CG1 1 
ATOM   5905 C CG2 . ILE B 2 99  ? 49.421  -21.978 59.632  1.00 96.33  ?  395 ILE B CG2 1 
ATOM   5906 C CD1 . ILE B 2 99  ? 48.046  -24.589 59.502  1.00 96.03  ?  395 ILE B CD1 1 
ATOM   5907 N N   . ARG B 2 100 ? 49.911  -20.364 56.352  1.00 95.15  ?  396 ARG B N   1 
ATOM   5908 C CA  . ARG B 2 100 ? 51.024  -19.434 56.073  1.00 95.95  ?  396 ARG B CA  1 
ATOM   5909 C C   . ARG B 2 100 ? 50.475  -18.101 55.599  1.00 91.68  ?  396 ARG B C   1 
ATOM   5910 O O   . ARG B 2 100 ? 51.065  -17.091 55.903  1.00 90.86  ?  396 ARG B O   1 
ATOM   5911 C CB  . ARG B 2 100 ? 51.927  -20.003 54.989  1.00 92.81  ?  396 ARG B CB  1 
ATOM   5912 C CG  . ARG B 2 100 ? 52.969  -19.008 54.524  1.00 90.82  ?  396 ARG B CG  1 
ATOM   5913 C CD  . ARG B 2 100 ? 54.183  -19.103 55.400  1.00 95.37  ?  396 ARG B CD  1 
ATOM   5914 N NE  . ARG B 2 100 ? 55.161  -18.144 54.944  1.00 101.63 ?  396 ARG B NE  1 
ATOM   5915 C CZ  . ARG B 2 100 ? 54.899  -16.875 54.743  1.00 98.19  ?  396 ARG B CZ  1 
ATOM   5916 N NH1 . ARG B 2 100 ? 53.688  -16.417 54.972  1.00 99.82  ?  396 ARG B NH1 1 
ATOM   5917 N NH2 . ARG B 2 100 ? 55.845  -16.067 54.322  1.00 97.56  ?  396 ARG B NH2 1 
ATOM   5918 N N   . LYS B 2 101 ? 49.392  -18.121 54.846  1.00 88.93  ?  397 LYS B N   1 
ATOM   5919 C CA  . LYS B 2 101 ? 48.895  -16.845 54.297  1.00 92.62  ?  397 LYS B CA  1 
ATOM   5920 C C   . LYS B 2 101 ? 48.162  -16.082 55.381  1.00 99.02  ?  397 LYS B C   1 
ATOM   5921 O O   . LYS B 2 101 ? 47.922  -14.900 55.201  1.00 97.14  ?  397 LYS B O   1 
ATOM   5922 C CB  . LYS B 2 101 ? 47.897  -17.091 53.174  1.00 90.36  ?  397 LYS B CB  1 
ATOM   5923 C CG  . LYS B 2 101 ? 47.747  -15.929 52.214  1.00 88.70  ?  397 LYS B CG  1 
ATOM   5924 C CD  . LYS B 2 101 ? 46.327  -15.610 51.907  1.00 90.80  ?  397 LYS B CD  1 
ATOM   5925 C CE  . LYS B 2 101 ? 46.205  -14.498 50.893  1.00 95.15  ?  397 LYS B CE  1 
ATOM   5926 N NZ  . LYS B 2 101 ? 44.842  -13.916 50.883  1.00 105.64 ?  397 LYS B NZ  1 
ATOM   5927 N N   . TYR B 2 102 ? 47.798  -16.753 56.458  1.00 101.47 ?  398 TYR B N   1 
ATOM   5928 C CA  . TYR B 2 102 ? 47.046  -16.036 57.508  1.00 105.73 ?  398 TYR B CA  1 
ATOM   5929 C C   . TYR B 2 102 ? 47.688  -16.293 58.864  1.00 107.38 ?  398 TYR B C   1 
ATOM   5930 O O   . TYR B 2 102 ? 48.498  -15.490 59.353  1.00 109.80 ?  398 TYR B O   1 
ATOM   5931 C CB  . TYR B 2 102 ? 45.612  -16.554 57.516  1.00 100.40 ?  398 TYR B CB  1 
ATOM   5932 C CG  . TYR B 2 102 ? 44.885  -16.348 56.217  1.00 98.77  ?  398 TYR B CG  1 
ATOM   5933 C CD1 . TYR B 2 102 ? 44.373  -15.116 55.888  1.00 94.99  ?  398 TYR B CD1 1 
ATOM   5934 C CD2 . TYR B 2 102 ? 44.721  -17.369 55.307  1.00 102.90 ?  398 TYR B CD2 1 
ATOM   5935 C CE1 . TYR B 2 102 ? 43.698  -14.905 54.704  1.00 95.90  ?  398 TYR B CE1 1 
ATOM   5936 C CE2 . TYR B 2 102 ? 44.045  -17.178 54.117  1.00 95.92  ?  398 TYR B CE2 1 
ATOM   5937 C CZ  . TYR B 2 102 ? 43.534  -15.938 53.813  1.00 96.97  ?  398 TYR B CZ  1 
ATOM   5938 O OH  . TYR B 2 102 ? 42.872  -15.708 52.654  1.00 91.50  ?  398 TYR B OH  1 
ATOM   5939 N N   . GLY B 2 103 ? 47.310  -17.422 59.444  1.00 106.17 ?  399 GLY B N   1 
ATOM   5940 C CA  . GLY B 2 103 ? 47.801  -17.827 60.765  1.00 108.92 ?  399 GLY B CA  1 
ATOM   5941 C C   . GLY B 2 103 ? 46.800  -17.388 61.801  1.00 115.10 ?  399 GLY B C   1 
ATOM   5942 O O   . GLY B 2 103 ? 46.525  -16.191 61.856  1.00 116.41 ?  399 GLY B O   1 
ATOM   5943 N N   . ARG B 2 104 ? 46.161  -18.347 62.463  1.00 116.40 ?  400 ARG B N   1 
ATOM   5944 C CA  . ARG B 2 104 ? 45.171  -18.127 63.551  1.00 114.80 ?  400 ARG B CA  1 
ATOM   5945 C C   . ARG B 2 104 ? 43.781  -17.674 63.083  1.00 114.34 ?  400 ARG B C   1 
ATOM   5946 O O   . ARG B 2 104 ? 42.875  -17.781 63.886  1.00 120.65 ?  400 ARG B O   1 
ATOM   5947 C CB  . ARG B 2 104 ? 45.740  -17.343 64.735  1.00 115.59 ?  400 ARG B CB  1 
ATOM   5948 C CG  . ARG B 2 104 ? 46.750  -18.123 65.561  1.00 115.48 ?  400 ARG B CG  1 
ATOM   5949 C CD  . ARG B 2 104 ? 47.863  -17.221 66.039  1.00 113.33 ?  400 ARG B CD  1 
ATOM   5950 N NE  . ARG B 2 104 ? 48.929  -17.973 66.666  1.00 116.31 ?  400 ARG B NE  1 
ATOM   5951 C CZ  . ARG B 2 104 ? 50.178  -17.551 66.732  1.00 116.83 ?  400 ARG B CZ  1 
ATOM   5952 N NH1 . ARG B 2 104 ? 51.099  -18.291 67.321  1.00 107.79 ?  400 ARG B NH1 1 
ATOM   5953 N NH2 . ARG B 2 104 ? 50.502  -16.386 66.209  1.00 108.65 ?  400 ARG B NH2 1 
ATOM   5954 N N   . ASP B 2 105 ? 43.580  -17.216 61.853  1.00 107.59 ?  401 ASP B N   1 
ATOM   5955 C CA  . ASP B 2 105 ? 42.208  -16.781 61.496  1.00 105.75 ?  401 ASP B CA  1 
ATOM   5956 C C   . ASP B 2 105 ? 41.391  -17.988 61.036  1.00 105.32 ?  401 ASP B C   1 
ATOM   5957 O O   . ASP B 2 105 ? 41.016  -18.019 59.877  1.00 106.89 ?  401 ASP B O   1 
ATOM   5958 C CB  . ASP B 2 105 ? 42.246  -15.642 60.488  1.00 102.75 ?  401 ASP B CB  1 
ATOM   5959 C CG  . ASP B 2 105 ? 40.868  -15.132 60.136  1.00 110.52 ?  401 ASP B CG  1 
ATOM   5960 O OD1 . ASP B 2 105 ? 40.786  -14.056 59.541  1.00 107.13 ?  401 ASP B OD1 1 
ATOM   5961 O OD2 . ASP B 2 105 ? 39.896  -15.817 60.459  1.00 110.91 ?  401 ASP B OD2 1 
ATOM   5962 N N   . PHE B 2 106 ? 41.078  -18.892 61.958  1.00 104.48 ?  402 PHE B N   1 
ATOM   5963 C CA  . PHE B 2 106 ? 40.368  -20.155 61.660  1.00 107.47 ?  402 PHE B CA  1 
ATOM   5964 C C   . PHE B 2 106 ? 39.145  -19.918 60.785  1.00 107.39 ?  402 PHE B C   1 
ATOM   5965 O O   . PHE B 2 106 ? 38.836  -20.776 59.977  1.00 107.63 ?  402 PHE B O   1 
ATOM   5966 C CB  . PHE B 2 106 ? 40.014  -20.851 62.969  1.00 112.55 ?  402 PHE B CB  1 
ATOM   5967 C CG  . PHE B 2 106 ? 41.162  -20.880 63.939  1.00 117.56 ?  402 PHE B CG  1 
ATOM   5968 C CD1 . PHE B 2 106 ? 40.952  -20.859 65.301  1.00 123.49 ?  402 PHE B CD1 1 
ATOM   5969 C CD2 . PHE B 2 106 ? 42.460  -20.937 63.483  1.00 117.73 ?  402 PHE B CD2 1 
ATOM   5970 C CE1 . PHE B 2 106 ? 42.020  -20.884 66.179  1.00 125.92 ?  402 PHE B CE1 1 
ATOM   5971 C CE2 . PHE B 2 106 ? 43.526  -20.951 64.364  1.00 116.18 ?  402 PHE B CE2 1 
ATOM   5972 C CZ  . PHE B 2 106 ? 43.305  -20.931 65.712  1.00 119.14 ?  402 PHE B CZ  1 
ATOM   5973 N N   . GLN B 2 107 ? 38.462  -18.796 60.938  1.00 104.53 ?  403 GLN B N   1 
ATOM   5974 C CA  . GLN B 2 107 ? 37.289  -18.644 60.055  1.00 105.76 ?  403 GLN B CA  1 
ATOM   5975 C C   . GLN B 2 107 ? 37.746  -18.546 58.602  1.00 108.96 ?  403 GLN B C   1 
ATOM   5976 O O   . GLN B 2 107 ? 37.104  -19.142 57.744  1.00 109.20 ?  403 GLN B O   1 
ATOM   5977 C CB  . GLN B 2 107 ? 36.531  -17.380 60.427  1.00 105.18 ?  403 GLN B CB  1 
ATOM   5978 C CG  . GLN B 2 107 ? 35.317  -17.151 59.553  1.00 106.57 ?  403 GLN B CG  1 
ATOM   5979 C CD  . GLN B 2 107 ? 34.378  -18.314 59.704  1.00 108.78 ?  403 GLN B CD  1 
ATOM   5980 O OE1 . GLN B 2 107 ? 34.687  -19.285 60.370  1.00 113.58 ?  403 GLN B OE1 1 
ATOM   5981 N NE2 . GLN B 2 107 ? 33.216  -18.218 59.091  1.00 110.74 ?  403 GLN B NE2 1 
ATOM   5982 N N   . ALA B 2 108 ? 38.808  -17.800 58.323  1.00 109.29 ?  404 ALA B N   1 
ATOM   5983 C CA  . ALA B 2 108 ? 39.215  -17.690 56.912  1.00 105.89 ?  404 ALA B CA  1 
ATOM   5984 C C   . ALA B 2 108 ? 39.619  -19.066 56.407  1.00 106.97 ?  404 ALA B C   1 
ATOM   5985 O O   . ALA B 2 108 ? 39.080  -19.492 55.382  1.00 107.98 ?  404 ALA B O   1 
ATOM   5986 C CB  . ALA B 2 108 ? 40.373  -16.749 56.811  1.00 98.34  ?  404 ALA B CB  1 
ATOM   5987 N N   . ILE B 2 109 ? 40.436  -19.764 57.186  1.00 99.95  ?  405 ILE B N   1 
ATOM   5988 C CA  . ILE B 2 109 ? 40.933  -21.100 56.777  1.00 94.47  ?  405 ILE B CA  1 
ATOM   5989 C C   . ILE B 2 109 ? 39.737  -21.992 56.509  1.00 98.04  ?  405 ILE B C   1 
ATOM   5990 O O   . ILE B 2 109 ? 39.706  -22.610 55.474  1.00 95.82  ?  405 ILE B O   1 
ATOM   5991 C CB  . ILE B 2 109 ? 41.835  -21.658 57.867  1.00 89.89  ?  405 ILE B CB  1 
ATOM   5992 C CG1 . ILE B 2 109 ? 42.945  -20.666 58.176  1.00 89.98  ?  405 ILE B CG1 1 
ATOM   5993 C CG2 . ILE B 2 109 ? 42.398  -22.985 57.438  1.00 93.59  ?  405 ILE B CG2 1 
ATOM   5994 C CD1 . ILE B 2 109 ? 44.127  -21.298 58.819  1.00 92.58  ?  405 ILE B CD1 1 
ATOM   5995 N N   . SER B 2 110 ? 38.788  -22.015 57.425  1.00 104.75 ?  406 SER B N   1 
ATOM   5996 C CA  . SER B 2 110 ? 37.560  -22.770 57.189  1.00 107.22 ?  406 SER B CA  1 
ATOM   5997 C C   . SER B 2 110 ? 36.923  -22.418 55.843  1.00 107.56 ?  406 SER B C   1 
ATOM   5998 O O   . SER B 2 110 ? 36.311  -23.285 55.202  1.00 108.08 ?  406 SER B O   1 
ATOM   5999 C CB  . SER B 2 110 ? 36.571  -22.518 58.336  1.00 106.86 ?  406 SER B CB  1 
ATOM   6000 O OG  . SER B 2 110 ? 35.344  -23.203 58.144  1.00 110.44 ?  406 SER B OG  1 
ATOM   6001 N N   . ASP B 2 111 ? 37.062  -21.157 55.393  1.00 104.13 ?  407 ASP B N   1 
ATOM   6002 C CA  . ASP B 2 111 ? 36.449  -20.726 54.134  1.00 106.76 ?  407 ASP B CA  1 
ATOM   6003 C C   . ASP B 2 111 ? 37.293  -21.075 52.917  1.00 103.29 ?  407 ASP B C   1 
ATOM   6004 O O   . ASP B 2 111 ? 36.740  -21.254 51.823  1.00 106.03 ?  407 ASP B O   1 
ATOM   6005 C CB  . ASP B 2 111 ? 36.184  -19.214 54.121  1.00 112.72 ?  407 ASP B CB  1 
ATOM   6006 C CG  . ASP B 2 111 ? 35.304  -18.751 55.271  1.00 117.40 ?  407 ASP B CG  1 
ATOM   6007 O OD1 . ASP B 2 111 ? 34.428  -19.542 55.704  1.00 116.44 ?  407 ASP B OD1 1 
ATOM   6008 O OD2 . ASP B 2 111 ? 35.470  -17.579 55.709  1.00 114.58 ?  407 ASP B OD2 1 
ATOM   6009 N N   . VAL B 2 112 ? 38.619  -21.120 53.071  1.00 99.47  ?  408 VAL B N   1 
ATOM   6010 C CA  . VAL B 2 112 ? 39.483  -21.642 52.015  1.00 95.61  ?  408 VAL B CA  1 
ATOM   6011 C C   . VAL B 2 112 ? 39.190  -23.117 51.760  1.00 95.98  ?  408 VAL B C   1 
ATOM   6012 O O   . VAL B 2 112 ? 38.915  -23.526 50.625  1.00 97.56  ?  408 VAL B O   1 
ATOM   6013 C CB  . VAL B 2 112 ? 40.961  -21.408 52.372  1.00 87.26  ?  408 VAL B CB  1 
ATOM   6014 C CG1 . VAL B 2 112 ? 41.852  -22.186 51.453  1.00 88.97  ?  408 VAL B CG1 1 
ATOM   6015 C CG2 . VAL B 2 112 ? 41.279  -19.950 52.216  1.00 84.80  ?  408 VAL B CG2 1 
ATOM   6016 N N   . ILE B 2 113 ? 39.233  -23.937 52.810  1.00 92.93  ?  409 ILE B N   1 
ATOM   6017 C CA  . ILE B 2 113 ? 39.083  -25.369 52.611  1.00 90.69  ?  409 ILE B CA  1 
ATOM   6018 C C   . ILE B 2 113 ? 37.649  -25.726 52.254  1.00 99.66  ?  409 ILE B C   1 
ATOM   6019 O O   . ILE B 2 113 ? 37.408  -26.722 51.561  1.00 108.70 ?  409 ILE B O   1 
ATOM   6020 C CB  . ILE B 2 113 ? 39.591  -26.105 53.854  1.00 88.67  ?  409 ILE B CB  1 
ATOM   6021 C CG1 . ILE B 2 113 ? 40.961  -25.536 54.217  1.00 83.62  ?  409 ILE B CG1 1 
ATOM   6022 C CG2 . ILE B 2 113 ? 39.687  -27.584 53.579  1.00 94.98  ?  409 ILE B CG2 1 
ATOM   6023 C CD1 . ILE B 2 113 ? 41.531  -26.046 55.502  1.00 85.18  ?  409 ILE B CD1 1 
ATOM   6024 N N   . GLY B 2 114 ? 36.681  -24.925 52.687  1.00 100.87 ?  410 GLY B N   1 
ATOM   6025 C CA  . GLY B 2 114 ? 35.335  -25.028 52.158  1.00 109.01 ?  410 GLY B CA  1 
ATOM   6026 C C   . GLY B 2 114 ? 34.445  -26.100 52.755  1.00 116.73 ?  410 GLY B C   1 
ATOM   6027 O O   . GLY B 2 114 ? 33.251  -25.854 52.957  1.00 120.50 ?  410 GLY B O   1 
ATOM   6028 N N   . ASN B 2 115 ? 34.988  -27.292 53.024  1.00 115.33 ?  411 ASN B N   1 
ATOM   6029 C CA  . ASN B 2 115 ? 34.173  -28.371 53.574  1.00 117.84 ?  411 ASN B CA  1 
ATOM   6030 C C   . ASN B 2 115 ? 34.714  -28.799 54.935  1.00 115.43 ?  411 ASN B C   1 
ATOM   6031 O O   . ASN B 2 115 ? 34.736  -29.986 55.274  1.00 124.67 ?  411 ASN B O   1 
ATOM   6032 C CB  . ASN B 2 115 ? 34.077  -29.544 52.574  1.00 123.98 ?  411 ASN B CB  1 
ATOM   6033 C CG  . ASN B 2 115 ? 35.280  -30.493 52.613  1.00 121.82 ?  411 ASN B CG  1 
ATOM   6034 O OD1 . ASN B 2 115 ? 36.391  -30.123 52.985  1.00 114.13 ?  411 ASN B OD1 1 
ATOM   6035 N ND2 . ASN B 2 115 ? 35.033  -31.747 52.246  1.00 127.72 ?  411 ASN B ND2 1 
ATOM   6036 N N   . LYS B 2 116 ? 35.120  -27.814 55.735  1.00 112.45 ?  412 LYS B N   1 
ATOM   6037 C CA  . LYS B 2 116 ? 35.800  -28.017 57.010  1.00 112.71 ?  412 LYS B CA  1 
ATOM   6038 C C   . LYS B 2 116 ? 35.455  -26.867 57.945  1.00 117.95 ?  412 LYS B C   1 
ATOM   6039 O O   . LYS B 2 116 ? 35.704  -25.702 57.622  1.00 117.08 ?  412 LYS B O   1 
ATOM   6040 C CB  . LYS B 2 116 ? 37.315  -28.131 56.800  1.00 107.74 ?  412 LYS B CB  1 
ATOM   6041 C CG  . LYS B 2 116 ? 37.626  -29.378 55.976  1.00 117.27 ?  412 LYS B CG  1 
ATOM   6042 C CD  . LYS B 2 116 ? 37.404  -30.686 56.738  1.00 119.49 ?  412 LYS B CD  1 
ATOM   6043 C CE  . LYS B 2 116 ? 38.575  -30.940 57.597  1.00 118.10 ?  412 LYS B CE  1 
ATOM   6044 N NZ  . LYS B 2 116 ? 39.533  -31.218 56.544  1.00 118.57 ?  412 LYS B NZ  1 
ATOM   6045 N N   . SER B 2 117 ? 34.893  -27.207 59.103  1.00 123.26 ?  413 SER B N   1 
ATOM   6046 C CA  . SER B 2 117 ? 34.456  -26.248 60.106  1.00 119.18 ?  413 SER B CA  1 
ATOM   6047 C C   . SER B 2 117 ? 35.624  -25.775 60.967  1.00 117.24 ?  413 SER B C   1 
ATOM   6048 O O   . SER B 2 117 ? 36.722  -26.342 60.959  1.00 115.70 ?  413 SER B O   1 
ATOM   6049 C CB  . SER B 2 117 ? 33.395  -26.865 61.008  1.00 122.18 ?  413 SER B CB  1 
ATOM   6050 O OG  . SER B 2 117 ? 34.015  -27.555 62.085  1.00 122.21 ?  413 SER B OG  1 
ATOM   6051 N N   . VAL B 2 118 ? 35.328  -24.765 61.788  1.00 117.09 ?  414 VAL B N   1 
ATOM   6052 C CA  . VAL B 2 118 ? 36.350  -23.995 62.490  1.00 115.64 ?  414 VAL B CA  1 
ATOM   6053 C C   . VAL B 2 118 ? 36.947  -24.801 63.641  1.00 118.96 ?  414 VAL B C   1 
ATOM   6054 O O   . VAL B 2 118 ? 38.104  -24.587 64.039  1.00 114.57 ?  414 VAL B O   1 
ATOM   6055 C CB  . VAL B 2 118 ? 35.714  -22.692 62.995  1.00 104.77 ?  414 VAL B CB  1 
ATOM   6056 C CG1 . VAL B 2 118 ? 36.771  -21.752 63.584  1.00 97.40  ?  414 VAL B CG1 1 
ATOM   6057 C CG2 . VAL B 2 118 ? 34.802  -22.077 61.934  1.00 103.74 ?  414 VAL B CG2 1 
ATOM   6058 N N   . VAL B 2 119 ? 36.155  -25.714 64.210  1.00 121.12 ?  415 VAL B N   1 
ATOM   6059 C CA  . VAL B 2 119 ? 36.638  -26.607 65.252  1.00 122.21 ?  415 VAL B CA  1 
ATOM   6060 C C   . VAL B 2 119 ? 37.608  -27.632 64.673  1.00 125.53 ?  415 VAL B C   1 
ATOM   6061 O O   . VAL B 2 119 ? 38.670  -27.892 65.256  1.00 125.68 ?  415 VAL B O   1 
ATOM   6062 C CB  . VAL B 2 119 ? 35.442  -27.265 65.976  1.00 123.39 ?  415 VAL B CB  1 
ATOM   6063 C CG1 . VAL B 2 119 ? 34.540  -28.029 65.006  1.00 121.28 ?  415 VAL B CG1 1 
ATOM   6064 C CG2 . VAL B 2 119 ? 35.943  -28.226 67.053  1.00 119.63 ?  415 VAL B CG2 1 
ATOM   6065 N N   . GLN B 2 120 ? 37.277  -28.222 63.510  1.00 121.83 ?  416 GLN B N   1 
ATOM   6066 C CA  . GLN B 2 120 ? 38.207  -29.170 62.904  1.00 121.07 ?  416 GLN B CA  1 
ATOM   6067 C C   . GLN B 2 120 ? 39.526  -28.490 62.572  1.00 118.45 ?  416 GLN B C   1 
ATOM   6068 O O   . GLN B 2 120 ? 40.593  -29.103 62.689  1.00 114.88 ?  416 GLN B O   1 
ATOM   6069 C CB  . GLN B 2 120 ? 37.606  -29.812 61.656  1.00 114.21 ?  416 GLN B CB  1 
ATOM   6070 C CG  . GLN B 2 120 ? 36.280  -30.487 61.876  1.00 113.73 ?  416 GLN B CG  1 
ATOM   6071 C CD  . GLN B 2 120 ? 35.371  -30.366 60.682  1.00 119.73 ?  416 GLN B CD  1 
ATOM   6072 O OE1 . GLN B 2 120 ? 34.975  -29.273 60.322  1.00 125.85 ?  416 GLN B OE1 1 
ATOM   6073 N NE2 . GLN B 2 120 ? 35.017  -31.490 60.074  1.00 121.44 ?  416 GLN B NE2 1 
ATOM   6074 N N   . VAL B 2 121 ? 39.471  -27.212 62.183  1.00 116.57 ?  417 VAL B N   1 
ATOM   6075 C CA  . VAL B 2 121 ? 40.692  -26.476 61.864  1.00 115.39 ?  417 VAL B CA  1 
ATOM   6076 C C   . VAL B 2 121 ? 41.579  -26.371 63.098  1.00 121.95 ?  417 VAL B C   1 
ATOM   6077 O O   . VAL B 2 121 ? 42.786  -26.632 63.041  1.00 119.92 ?  417 VAL B O   1 
ATOM   6078 C CB  . VAL B 2 121 ? 40.359  -25.081 61.304  1.00 110.75 ?  417 VAL B CB  1 
ATOM   6079 C CG1 . VAL B 2 121 ? 41.644  -24.312 60.990  1.00 105.90 ?  417 VAL B CG1 1 
ATOM   6080 C CG2 . VAL B 2 121 ? 39.423  -25.161 60.109  1.00 105.69 ?  417 VAL B CG2 1 
ATOM   6081 N N   . LYS B 2 122 ? 40.989  -25.984 64.234  1.00 126.02 ?  418 LYS B N   1 
ATOM   6082 C CA  . LYS B 2 122 ? 41.760  -25.893 65.468  1.00 123.47 ?  418 LYS B CA  1 
ATOM   6083 C C   . LYS B 2 122 ? 42.263  -27.264 65.895  1.00 120.67 ?  418 LYS B C   1 
ATOM   6084 O O   . LYS B 2 122 ? 43.396  -27.403 66.371  1.00 117.66 ?  418 LYS B O   1 
ATOM   6085 C CB  . LYS B 2 122 ? 40.919  -25.252 66.573  1.00 121.88 ?  418 LYS B CB  1 
ATOM   6086 C CG  . LYS B 2 122 ? 41.666  -25.108 67.904  1.00 125.46 ?  418 LYS B CG  1 
ATOM   6087 C CD  . LYS B 2 122 ? 42.961  -24.335 67.682  1.00 124.70 ?  418 LYS B CD  1 
ATOM   6088 C CE  . LYS B 2 122 ? 43.812  -24.086 68.912  1.00 124.92 ?  418 LYS B CE  1 
ATOM   6089 N NZ  . LYS B 2 122 ? 45.071  -23.356 68.515  1.00 117.63 ?  418 LYS B NZ  1 
ATOM   6090 N N   . ASN B 2 123 ? 41.440  -28.293 65.716  1.00 119.61 ?  419 ASN B N   1 
ATOM   6091 C CA  . ASN B 2 123 ? 41.903  -29.637 66.021  1.00 129.49 ?  419 ASN B CA  1 
ATOM   6092 C C   . ASN B 2 123 ? 43.031  -30.054 65.081  1.00 130.20 ?  419 ASN B C   1 
ATOM   6093 O O   . ASN B 2 123 ? 44.009  -30.675 65.518  1.00 127.20 ?  419 ASN B O   1 
ATOM   6094 C CB  . ASN B 2 123 ? 40.733  -30.621 65.966  1.00 132.40 ?  419 ASN B CB  1 
ATOM   6095 C CG  . ASN B 2 123 ? 40.148  -30.895 67.335  1.00 133.68 ?  419 ASN B CG  1 
ATOM   6096 O OD1 . ASN B 2 123 ? 40.187  -30.037 68.222  1.00 134.63 ?  419 ASN B OD1 1 
ATOM   6097 N ND2 . ASN B 2 123 ? 39.628  -32.104 67.528  1.00 136.55 ?  419 ASN B ND2 1 
ATOM   6098 N N   . PHE B 2 124 ? 42.913  -29.717 63.788  1.00 128.39 ?  420 PHE B N   1 
ATOM   6099 C CA  . PHE B 2 124 ? 44.020  -29.884 62.847  1.00 124.02 ?  420 PHE B CA  1 
ATOM   6100 C C   . PHE B 2 124 ? 45.323  -29.335 63.405  1.00 124.43 ?  420 PHE B C   1 
ATOM   6101 O O   . PHE B 2 124 ? 46.381  -29.967 63.290  1.00 124.29 ?  420 PHE B O   1 
ATOM   6102 C CB  . PHE B 2 124 ? 43.698  -29.193 61.519  1.00 118.18 ?  420 PHE B CB  1 
ATOM   6103 C CG  . PHE B 2 124 ? 44.775  -29.358 60.473  1.00 116.80 ?  420 PHE B CG  1 
ATOM   6104 C CD1 . PHE B 2 124 ? 44.681  -30.362 59.535  1.00 116.06 ?  420 PHE B CD1 1 
ATOM   6105 C CD2 . PHE B 2 124 ? 45.866  -28.501 60.421  1.00 115.14 ?  420 PHE B CD2 1 
ATOM   6106 C CE1 . PHE B 2 124 ? 45.646  -30.515 58.570  1.00 112.11 ?  420 PHE B CE1 1 
ATOM   6107 C CE2 . PHE B 2 124 ? 46.845  -28.658 59.456  1.00 110.71 ?  420 PHE B CE2 1 
ATOM   6108 C CZ  . PHE B 2 124 ? 46.729  -29.671 58.533  1.00 106.31 ?  420 PHE B CZ  1 
ATOM   6109 N N   . PHE B 2 125 ? 45.249  -28.144 64.005  1.00 122.25 ?  421 PHE B N   1 
ATOM   6110 C CA  . PHE B 2 125 ? 46.446  -27.440 64.446  1.00 119.07 ?  421 PHE B CA  1 
ATOM   6111 C C   . PHE B 2 125 ? 47.311  -28.289 65.360  1.00 124.82 ?  421 PHE B C   1 
ATOM   6112 O O   . PHE B 2 125 ? 48.532  -28.107 65.393  1.00 121.41 ?  421 PHE B O   1 
ATOM   6113 C CB  . PHE B 2 125 ? 46.065  -26.156 65.166  1.00 120.32 ?  421 PHE B CB  1 
ATOM   6114 C CG  . PHE B 2 125 ? 46.071  -24.942 64.287  1.00 119.90 ?  421 PHE B CG  1 
ATOM   6115 C CD1 . PHE B 2 125 ? 47.215  -24.163 64.170  1.00 112.57 ?  421 PHE B CD1 1 
ATOM   6116 C CD2 . PHE B 2 125 ? 44.926  -24.555 63.602  1.00 120.16 ?  421 PHE B CD2 1 
ATOM   6117 C CE1 . PHE B 2 125 ? 47.221  -23.033 63.375  1.00 106.86 ?  421 PHE B CE1 1 
ATOM   6118 C CE2 . PHE B 2 125 ? 44.924  -23.425 62.800  1.00 114.24 ?  421 PHE B CE2 1 
ATOM   6119 C CZ  . PHE B 2 125 ? 46.073  -22.664 62.688  1.00 110.47 ?  421 PHE B CZ  1 
ATOM   6120 N N   . VAL B 2 126 ? 46.715  -29.207 66.118  1.00 125.87 ?  422 VAL B N   1 
ATOM   6121 C CA  . VAL B 2 126 ? 47.484  -30.008 67.049  1.00 127.48 ?  422 VAL B CA  1 
ATOM   6122 C C   . VAL B 2 126 ? 47.579  -31.471 66.611  1.00 128.26 ?  422 VAL B C   1 
ATOM   6123 O O   . VAL B 2 126 ? 48.588  -32.126 66.900  1.00 129.54 ?  422 VAL B O   1 
ATOM   6124 C CB  . VAL B 2 126 ? 46.916  -29.891 68.483  1.00 126.07 ?  422 VAL B CB  1 
ATOM   6125 C CG1 . VAL B 2 126 ? 45.597  -30.663 68.645  1.00 130.36 ?  422 VAL B CG1 1 
ATOM   6126 C CG2 . VAL B 2 126 ? 47.987  -30.220 69.536  1.00 124.05 ?  422 VAL B CG2 1 
ATOM   6127 N N   . ASN B 2 127 ? 46.581  -31.997 65.898  1.00 125.12 ?  423 ASN B N   1 
ATOM   6128 C CA  . ASN B 2 127 ? 46.686  -33.363 65.400  1.00 126.63 ?  423 ASN B CA  1 
ATOM   6129 C C   . ASN B 2 127 ? 47.840  -33.485 64.410  1.00 128.20 ?  423 ASN B C   1 
ATOM   6130 O O   . ASN B 2 127 ? 48.776  -34.268 64.613  1.00 129.33 ?  423 ASN B O   1 
ATOM   6131 C CB  . ASN B 2 127 ? 45.365  -33.798 64.760  1.00 129.08 ?  423 ASN B CB  1 
ATOM   6132 C CG  . ASN B 2 127 ? 44.205  -33.760 65.733  1.00 131.54 ?  423 ASN B CG  1 
ATOM   6133 O OD1 . ASN B 2 127 ? 44.358  -34.106 66.904  1.00 136.57 ?  423 ASN B OD1 1 
ATOM   6134 N ND2 . ASN B 2 127 ? 43.035  -33.342 65.253  1.00 129.51 ?  423 ASN B ND2 1 
ATOM   6135 N N   . TYR B 2 128 ? 47.798  -32.692 63.333  1.00 128.39 ?  424 TYR B N   1 
ATOM   6136 C CA  . TYR B 2 128 ? 48.824  -32.710 62.296  1.00 128.12 ?  424 TYR B CA  1 
ATOM   6137 C C   . TYR B 2 128 ? 49.928  -31.684 62.562  1.00 121.93 ?  424 TYR B C   1 
ATOM   6138 O O   . TYR B 2 128 ? 50.539  -31.157 61.626  1.00 120.50 ?  424 TYR B O   1 
ATOM   6139 C CB  . TYR B 2 128 ? 48.173  -32.503 60.925  1.00 117.20 ?  424 TYR B CB  1 
ATOM   6140 C CG  . TYR B 2 128 ? 47.307  -33.679 60.488  1.00 117.35 ?  424 TYR B CG  1 
ATOM   6141 C CD1 . TYR B 2 128 ? 47.877  -34.880 60.084  1.00 113.90 ?  424 TYR B CD1 1 
ATOM   6142 C CD2 . TYR B 2 128 ? 45.915  -33.593 60.505  1.00 118.18 ?  424 TYR B CD2 1 
ATOM   6143 C CE1 . TYR B 2 128 ? 47.082  -35.957 59.683  1.00 119.00 ?  424 TYR B CE1 1 
ATOM   6144 C CE2 . TYR B 2 128 ? 45.113  -34.667 60.112  1.00 117.29 ?  424 TYR B CE2 1 
ATOM   6145 C CZ  . TYR B 2 128 ? 45.702  -35.846 59.705  1.00 119.43 ?  424 TYR B CZ  1 
ATOM   6146 O OH  . TYR B 2 128 ? 44.909  -36.911 59.318  1.00 119.94 ?  424 TYR B OH  1 
ATOM   6147 N N   . ARG B 2 129 ? 50.225  -31.438 63.833  1.00 122.50 ?  425 ARG B N   1 
ATOM   6148 C CA  . ARG B 2 129 ? 51.152  -30.401 64.273  1.00 120.65 ?  425 ARG B CA  1 
ATOM   6149 C C   . ARG B 2 129 ? 52.607  -30.769 64.021  1.00 117.58 ?  425 ARG B C   1 
ATOM   6150 O O   . ARG B 2 129 ? 53.397  -29.933 63.576  1.00 106.00 ?  425 ARG B O   1 
ATOM   6151 C CB  . ARG B 2 129 ? 50.919  -30.179 65.758  1.00 128.30 ?  425 ARG B CB  1 
ATOM   6152 C CG  . ARG B 2 129 ? 51.654  -29.060 66.420  1.00 128.85 ?  425 ARG B CG  1 
ATOM   6153 C CD  . ARG B 2 129 ? 51.395  -29.232 67.916  1.00 137.90 ?  425 ARG B CD  1 
ATOM   6154 N NE  . ARG B 2 129 ? 52.544  -28.907 68.752  1.00 143.68 ?  425 ARG B NE  1 
ATOM   6155 C CZ  . ARG B 2 129 ? 52.913  -27.665 69.040  1.00 146.55 ?  425 ARG B CZ  1 
ATOM   6156 N NH1 . ARG B 2 129 ? 52.208  -26.645 68.561  1.00 146.26 ?  425 ARG B NH1 1 
ATOM   6157 N NH2 . ARG B 2 129 ? 53.971  -27.443 69.811  1.00 138.12 ?  425 ARG B NH2 1 
ATOM   6158 N N   . ARG B 2 130 ? 52.989  -31.995 64.380  1.00 127.95 ?  426 ARG B N   1 
ATOM   6159 C CA  . ARG B 2 130 ? 54.331  -32.498 64.097  1.00 128.98 ?  426 ARG B CA  1 
ATOM   6160 C C   . ARG B 2 130 ? 54.541  -32.663 62.599  1.00 123.61 ?  426 ARG B C   1 
ATOM   6161 O O   . ARG B 2 130 ? 55.412  -32.024 61.992  1.00 110.75 ?  426 ARG B O   1 
ATOM   6162 C CB  . ARG B 2 130 ? 54.522  -33.863 64.770  1.00 140.92 ?  426 ARG B CB  1 
ATOM   6163 C CG  . ARG B 2 130 ? 54.407  -33.900 66.271  1.00 146.68 ?  426 ARG B CG  1 
ATOM   6164 C CD  . ARG B 2 130 ? 55.400  -34.898 66.846  1.00 150.00 ?  426 ARG B CD  1 
ATOM   6165 N NE  . ARG B 2 130 ? 55.904  -34.436 68.134  1.00 159.92 ?  426 ARG B NE  1 
ATOM   6166 C CZ  . ARG B 2 130 ? 56.811  -35.080 68.861  1.00 161.76 ?  426 ARG B CZ  1 
ATOM   6167 N NH1 . ARG B 2 130 ? 57.323  -36.222 68.416  1.00 161.80 ?  426 ARG B NH1 1 
ATOM   6168 N NH2 . ARG B 2 130 ? 57.211  -34.577 70.026  1.00 154.47 ?  426 ARG B NH2 1 
ATOM   6169 N N   . ARG B 2 131 ? 53.734  -33.545 62.003  1.00 122.62 ?  427 ARG B N   1 
ATOM   6170 C CA  . ARG B 2 131 ? 53.978  -34.040 60.661  1.00 118.40 ?  427 ARG B CA  1 
ATOM   6171 C C   . ARG B 2 131 ? 53.991  -32.899 59.649  1.00 119.32 ?  427 ARG B C   1 
ATOM   6172 O O   . ARG B 2 131 ? 54.732  -32.941 58.657  1.00 121.08 ?  427 ARG B O   1 
ATOM   6173 C CB  . ARG B 2 131 ? 52.912  -35.089 60.332  1.00 118.19 ?  427 ARG B CB  1 
ATOM   6174 C CG  . ARG B 2 131 ? 53.005  -36.347 61.200  1.00 116.00 ?  427 ARG B CG  1 
ATOM   6175 C CD  . ARG B 2 131 ? 51.926  -37.370 60.870  1.00 117.06 ?  427 ARG B CD  1 
ATOM   6176 N NE  . ARG B 2 131 ? 50.651  -37.083 61.518  1.00 117.19 ?  427 ARG B NE  1 
ATOM   6177 C CZ  . ARG B 2 131 ? 49.523  -37.741 61.259  1.00 127.42 ?  427 ARG B CZ  1 
ATOM   6178 N NH1 . ARG B 2 131 ? 49.498  -38.719 60.350  1.00 120.68 ?  427 ARG B NH1 1 
ATOM   6179 N NH2 . ARG B 2 131 ? 48.415  -37.421 61.915  1.00 130.78 ?  427 ARG B NH2 1 
ATOM   6180 N N   . PHE B 2 132 ? 53.194  -31.859 59.894  1.00 111.50 ?  428 PHE B N   1 
ATOM   6181 C CA  . PHE B 2 132 ? 53.121  -30.706 59.009  1.00 106.11 ?  428 PHE B CA  1 
ATOM   6182 C C   . PHE B 2 132 ? 53.853  -29.506 59.541  1.00 110.44 ?  428 PHE B C   1 
ATOM   6183 O O   . PHE B 2 132 ? 53.745  -28.424 58.958  1.00 106.95 ?  428 PHE B O   1 
ATOM   6184 C CB  . PHE B 2 132 ? 51.684  -30.309 58.738  1.00 99.19  ?  428 PHE B CB  1 
ATOM   6185 C CG  . PHE B 2 132 ? 51.079  -31.096 57.679  1.00 94.37  ?  428 PHE B CG  1 
ATOM   6186 C CD1 . PHE B 2 132 ? 51.869  -31.928 56.909  1.00 93.33  ?  428 PHE B CD1 1 
ATOM   6187 C CD2 . PHE B 2 132 ? 49.742  -31.005 57.427  1.00 97.61  ?  428 PHE B CD2 1 
ATOM   6188 C CE1 . PHE B 2 132 ? 51.329  -32.676 55.919  1.00 95.82  ?  428 PHE B CE1 1 
ATOM   6189 C CE2 . PHE B 2 132 ? 49.193  -31.737 56.436  1.00 101.49 ?  428 PHE B CE2 1 
ATOM   6190 C CZ  . PHE B 2 132 ? 49.979  -32.582 55.674  1.00 101.55 ?  428 PHE B CZ  1 
ATOM   6191 N N   . ASN B 2 133 ? 54.548  -29.657 60.657  1.00 116.95 ?  429 ASN B N   1 
ATOM   6192 C CA  . ASN B 2 133 ? 55.515  -28.672 61.096  1.00 111.04 ?  429 ASN B CA  1 
ATOM   6193 C C   . ASN B 2 133 ? 54.856  -27.294 61.194  1.00 110.87 ?  429 ASN B C   1 
ATOM   6194 O O   . ASN B 2 133 ? 55.407  -26.267 60.792  1.00 111.12 ?  429 ASN B O   1 
ATOM   6195 C CB  . ASN B 2 133 ? 56.704  -28.691 60.145  1.00 100.26 ?  429 ASN B CB  1 
ATOM   6196 C CG  . ASN B 2 133 ? 57.878  -27.961 60.684  1.00 108.18 ?  429 ASN B CG  1 
ATOM   6197 O OD1 . ASN B 2 133 ? 57.757  -27.087 61.548  1.00 114.83 ?  429 ASN B OD1 1 
ATOM   6198 N ND2 . ASN B 2 133 ? 59.058  -28.368 60.234  1.00 101.47 ?  429 ASN B ND2 1 
ATOM   6199 N N   . ILE B 2 134 ? 53.631  -27.292 61.724  1.00 114.14 ?  430 ILE B N   1 
ATOM   6200 C CA  . ILE B 2 134 ? 52.817  -26.089 61.839  1.00 109.74 ?  430 ILE B CA  1 
ATOM   6201 C C   . ILE B 2 134 ? 53.512  -25.039 62.689  1.00 112.32 ?  430 ILE B C   1 
ATOM   6202 O O   . ILE B 2 134 ? 53.182  -23.848 62.611  1.00 107.89 ?  430 ILE B O   1 
ATOM   6203 C CB  . ILE B 2 134 ? 51.428  -26.480 62.391  1.00 106.77 ?  430 ILE B CB  1 
ATOM   6204 C CG1 . ILE B 2 134 ? 50.745  -27.440 61.409  1.00 114.92 ?  430 ILE B CG1 1 
ATOM   6205 C CG2 . ILE B 2 134 ? 50.552  -25.285 62.618  1.00 101.82 ?  430 ILE B CG2 1 
ATOM   6206 C CD1 . ILE B 2 134 ? 49.473  -28.067 61.904  1.00 120.42 ?  430 ILE B CD1 1 
ATOM   6207 N N   . ASP B 2 135 ? 54.500  -25.458 63.481  1.00 123.24 ?  431 ASP B N   1 
ATOM   6208 C CA  . ASP B 2 135 ? 55.227  -24.543 64.354  1.00 123.82 ?  431 ASP B CA  1 
ATOM   6209 C C   . ASP B 2 135 ? 55.982  -23.495 63.540  1.00 119.17 ?  431 ASP B C   1 
ATOM   6210 O O   . ASP B 2 135 ? 55.701  -22.294 63.640  1.00 113.78 ?  431 ASP B O   1 
ATOM   6211 C CB  . ASP B 2 135 ? 56.187  -25.337 65.254  1.00 131.72 ?  431 ASP B CB  1 
ATOM   6212 C CG  . ASP B 2 135 ? 55.464  -26.141 66.350  1.00 144.04 ?  431 ASP B CG  1 
ATOM   6213 O OD1 . ASP B 2 135 ? 54.228  -26.319 66.263  1.00 144.42 ?  431 ASP B OD1 1 
ATOM   6214 O OD2 . ASP B 2 135 ? 56.144  -26.598 67.303  1.00 144.23 ?  431 ASP B OD2 1 
ATOM   6215 N N   . GLU B 2 136 ? 56.953  -23.937 62.721  1.00 120.12 ?  432 GLU B N   1 
ATOM   6216 C CA  . GLU B 2 136 ? 57.721  -22.993 61.908  1.00 114.46 ?  432 GLU B CA  1 
ATOM   6217 C C   . GLU B 2 136 ? 56.815  -22.178 61.009  1.00 112.04 ?  432 GLU B C   1 
ATOM   6218 O O   . GLU B 2 136 ? 57.075  -20.998 60.767  1.00 114.52 ?  432 GLU B O   1 
ATOM   6219 C CB  . GLU B 2 136 ? 58.768  -23.701 61.043  1.00 105.57 ?  432 GLU B CB  1 
ATOM   6220 C CG  . GLU B 2 136 ? 59.902  -24.374 61.779  1.00 111.14 ?  432 GLU B CG  1 
ATOM   6221 C CD  . GLU B 2 136 ? 60.759  -25.248 60.861  1.00 108.68 ?  432 GLU B CD  1 
ATOM   6222 O OE1 . GLU B 2 136 ? 60.193  -26.131 60.180  1.00 112.94 ?  432 GLU B OE1 1 
ATOM   6223 O OE2 . GLU B 2 136 ? 61.999  -25.071 60.828  1.00 108.10 ?  432 GLU B OE2 1 
ATOM   6224 N N   . VAL B 2 137 ? 55.752  -22.795 60.493  1.00 111.83 ?  433 VAL B N   1 
ATOM   6225 C CA  . VAL B 2 137 ? 54.864  -22.086 59.577  1.00 111.44 ?  433 VAL B CA  1 
ATOM   6226 C C   . VAL B 2 137 ? 54.406  -20.765 60.184  1.00 110.83 ?  433 VAL B C   1 
ATOM   6227 O O   . VAL B 2 137 ? 54.467  -19.718 59.533  1.00 110.85 ?  433 VAL B O   1 
ATOM   6228 C CB  . VAL B 2 137 ? 53.664  -22.964 59.186  1.00 110.54 ?  433 VAL B CB  1 
ATOM   6229 C CG1 . VAL B 2 137 ? 52.637  -22.124 58.440  1.00 100.19 ?  433 VAL B CG1 1 
ATOM   6230 C CG2 . VAL B 2 137 ? 54.133  -24.146 58.351  1.00 110.39 ?  433 VAL B CG2 1 
ATOM   6231 N N   . LEU B 2 138 ? 53.958  -20.782 61.446  1.00 113.66 ?  434 LEU B N   1 
ATOM   6232 C CA  . LEU B 2 138 ? 53.457  -19.540 62.027  1.00 110.16 ?  434 LEU B CA  1 
ATOM   6233 C C   . LEU B 2 138 ? 54.577  -18.542 62.267  1.00 113.48 ?  434 LEU B C   1 
ATOM   6234 O O   . LEU B 2 138 ? 54.382  -17.335 62.091  1.00 112.48 ?  434 LEU B O   1 
ATOM   6235 C CB  . LEU B 2 138 ? 52.678  -19.800 63.311  1.00 104.33 ?  434 LEU B CB  1 
ATOM   6236 C CG  . LEU B 2 138 ? 51.376  -20.501 62.949  1.00 109.80 ?  434 LEU B CG  1 
ATOM   6237 C CD1 . LEU B 2 138 ? 50.468  -20.780 64.138  1.00 105.60 ?  434 LEU B CD1 1 
ATOM   6238 C CD2 . LEU B 2 138 ? 50.688  -19.683 61.875  1.00 115.81 ?  434 LEU B CD2 1 
ATOM   6239 N N   . GLN B 2 139 ? 55.762  -19.022 62.647  1.00 116.65 ?  435 GLN B N   1 
ATOM   6240 C CA  . GLN B 2 139 ? 56.912  -18.130 62.716  1.00 117.79 ?  435 GLN B CA  1 
ATOM   6241 C C   . GLN B 2 139 ? 57.094  -17.378 61.404  1.00 115.66 ?  435 GLN B C   1 
ATOM   6242 O O   . GLN B 2 139 ? 57.220  -16.147 61.400  1.00 119.06 ?  435 GLN B O   1 
ATOM   6243 C CB  . GLN B 2 139 ? 58.167  -18.915 63.068  1.00 117.57 ?  435 GLN B CB  1 
ATOM   6244 C CG  . GLN B 2 139 ? 58.491  -18.900 64.537  1.00 123.00 ?  435 GLN B CG  1 
ATOM   6245 C CD  . GLN B 2 139 ? 59.629  -19.823 64.862  1.00 126.18 ?  435 GLN B CD  1 
ATOM   6246 O OE1 . GLN B 2 139 ? 60.792  -19.486 64.635  1.00 127.39 ?  435 GLN B OE1 1 
ATOM   6247 N NE2 . GLN B 2 139 ? 59.307  -21.013 65.361  1.00 120.91 ?  435 GLN B NE2 1 
ATOM   6248 N N   . GLU B 2 140 ? 57.065  -18.098 60.272  1.00 116.66 ?  436 GLU B N   1 
ATOM   6249 C CA  . GLU B 2 140 ? 57.210  -17.431 58.983  1.00 116.34 ?  436 GLU B CA  1 
ATOM   6250 C C   . GLU B 2 140 ? 56.113  -16.413 58.733  1.00 117.90 ?  436 GLU B C   1 
ATOM   6251 O O   . GLU B 2 140 ? 56.354  -15.396 58.071  1.00 116.69 ?  436 GLU B O   1 
ATOM   6252 C CB  . GLU B 2 140 ? 57.227  -18.421 57.821  1.00 116.22 ?  436 GLU B CB  1 
ATOM   6253 C CG  . GLU B 2 140 ? 58.492  -19.213 57.582  1.00 110.22 ?  436 GLU B CG  1 
ATOM   6254 C CD  . GLU B 2 140 ? 59.684  -18.309 57.269  1.00 120.81 ?  436 GLU B CD  1 
ATOM   6255 O OE1 . GLU B 2 140 ? 59.519  -17.099 56.931  1.00 119.96 ?  436 GLU B OE1 1 
ATOM   6256 O OE2 . GLU B 2 140 ? 60.794  -18.858 57.215  1.00 113.91 ?  436 GLU B OE2 1 
ATOM   6257 N N   . TRP B 2 141 ? 54.883  -16.694 59.178  1.00 117.51 ?  437 TRP B N   1 
ATOM   6258 C CA  . TRP B 2 141 ? 53.826  -15.717 58.950  1.00 114.70 ?  437 TRP B CA  1 
ATOM   6259 C C   . TRP B 2 141 ? 54.079  -14.447 59.753  1.00 120.21 ?  437 TRP B C   1 
ATOM   6260 O O   . TRP B 2 141 ? 53.890  -13.333 59.245  1.00 123.88 ?  437 TRP B O   1 
ATOM   6261 C CB  . TRP B 2 141 ? 52.455  -16.283 59.301  1.00 109.34 ?  437 TRP B CB  1 
ATOM   6262 C CG  . TRP B 2 141 ? 51.483  -15.165 59.423  1.00 115.66 ?  437 TRP B CG  1 
ATOM   6263 C CD1 . TRP B 2 141 ? 51.118  -14.284 58.441  1.00 120.10 ?  437 TRP B CD1 1 
ATOM   6264 C CD2 . TRP B 2 141 ? 50.830  -14.722 60.618  1.00 120.76 ?  437 TRP B CD2 1 
ATOM   6265 N NE1 . TRP B 2 141 ? 50.241  -13.347 58.941  1.00 124.32 ?  437 TRP B NE1 1 
ATOM   6266 C CE2 . TRP B 2 141 ? 50.056  -13.586 60.279  1.00 123.00 ?  437 TRP B CE2 1 
ATOM   6267 C CE3 . TRP B 2 141 ? 50.806  -15.183 61.936  1.00 122.74 ?  437 TRP B CE3 1 
ATOM   6268 C CZ2 . TRP B 2 141 ? 49.245  -12.927 61.207  1.00 118.16 ?  437 TRP B CZ2 1 
ATOM   6269 C CZ3 . TRP B 2 141 ? 50.012  -14.516 62.860  1.00 126.02 ?  437 TRP B CZ3 1 
ATOM   6270 C CH2 . TRP B 2 141 ? 49.242  -13.401 62.489  1.00 118.12 ?  437 TRP B CH2 1 
ATOM   6271 N N   . GLU B 2 142 ? 54.534  -14.593 60.999  1.00 119.13 ?  438 GLU B N   1 
ATOM   6272 C CA  . GLU B 2 142 ? 54.670  -13.430 61.870  1.00 123.23 ?  438 GLU B CA  1 
ATOM   6273 C C   . GLU B 2 142 ? 55.720  -12.452 61.349  1.00 124.07 ?  438 GLU B C   1 
ATOM   6274 O O   . GLU B 2 142 ? 55.580  -11.236 61.540  1.00 123.75 ?  438 GLU B O   1 
ATOM   6275 C CB  . GLU B 2 142 ? 54.979  -13.890 63.299  1.00 122.78 ?  438 GLU B CB  1 
ATOM   6276 C CG  . GLU B 2 142 ? 53.726  -13.947 64.192  1.00 124.12 ?  438 GLU B CG  1 
ATOM   6277 C CD  . GLU B 2 142 ? 53.815  -14.970 65.327  1.00 124.90 ?  438 GLU B CD  1 
ATOM   6278 O OE1 . GLU B 2 142 ? 52.753  -15.318 65.892  1.00 120.99 ?  438 GLU B OE1 1 
ATOM   6279 O OE2 . GLU B 2 142 ? 54.934  -15.433 65.646  1.00 123.84 ?  438 GLU B OE2 1 
ATOM   6280 N N   . ALA B 2 143 ? 56.751  -12.951 60.658  1.00 118.89 ?  439 ALA B N   1 
ATOM   6281 C CA  . ALA B 2 143 ? 57.743  -12.058 60.063  1.00 122.00 ?  439 ALA B CA  1 
ATOM   6282 C C   . ALA B 2 143 ? 57.104  -11.088 59.068  1.00 128.97 ?  439 ALA B C   1 
ATOM   6283 O O   . ALA B 2 143 ? 57.490  -9.914  58.998  1.00 134.56 ?  439 ALA B O   1 
ATOM   6284 C CB  . ALA B 2 143 ? 58.848  -12.874 59.395  1.00 117.77 ?  439 ALA B CB  1 
ATOM   6285 N N   . GLU B 2 144 ? 56.120  -11.552 58.300  1.00 127.41 ?  440 GLU B N   1 
ATOM   6286 C CA  . GLU B 2 144 ? 55.380  -10.700 57.365  1.00 121.35 ?  440 GLU B CA  1 
ATOM   6287 C C   . GLU B 2 144 ? 54.343  -9.828  58.084  1.00 122.69 ?  440 GLU B C   1 
ATOM   6288 O O   . GLU B 2 144 ? 53.195  -10.244 58.297  1.00 116.78 ?  440 GLU B O   1 
ATOM   6289 C CB  . GLU B 2 144 ? 54.680  -11.558 56.308  1.00 126.30 ?  440 GLU B CB  1 
ATOM   6290 C CG  . GLU B 2 144 ? 55.527  -11.875 55.073  1.00 127.52 ?  440 GLU B CG  1 
ATOM   6291 C CD  . GLU B 2 144 ? 54.727  -12.560 53.967  1.00 123.96 ?  440 GLU B CD  1 
ATOM   6292 O OE1 . GLU B 2 144 ? 55.119  -13.668 53.529  1.00 118.39 ?  440 GLU B OE1 1 
ATOM   6293 O OE2 . GLU B 2 144 ? 53.701  -11.984 53.538  1.00 124.74 ?  440 GLU B OE2 1 
HETATM 6294 C C4  . XRK C 3 .   ? -5.567  53.124  85.389  1.00 90.86  ?  901 XRK A C4  1 
HETATM 6295 C C14 . XRK C 3 .   ? -6.559  61.875  79.128  1.00 61.58  ?  901 XRK A C14 1 
HETATM 6296 C C5  . XRK C 3 .   ? -6.882  53.141  84.985  1.00 84.79  ?  901 XRK A C5  1 
HETATM 6297 C C6  . XRK C 3 .   ? -7.333  54.150  84.161  1.00 82.41  ?  901 XRK A C6  1 
HETATM 6298 C C11 . XRK C 3 .   ? -7.303  59.469  81.913  1.00 66.14  ?  901 XRK A C11 1 
HETATM 6299 C C7  . XRK C 3 .   ? -6.480  55.153  83.739  1.00 82.70  ?  901 XRK A C7  1 
HETATM 6300 C C8  . XRK C 3 .   ? -7.032  56.233  82.839  1.00 77.66  ?  901 XRK A C8  1 
HETATM 6301 C C9  . XRK C 3 .   ? -6.429  56.486  81.470  1.00 69.14  ?  901 XRK A C9  1 
HETATM 6302 C C10 . XRK C 3 .   ? -7.510  57.379  80.894  1.00 78.09  ?  901 XRK A C10 1 
HETATM 6303 C C12 . XRK C 3 .   ? -7.218  60.027  80.658  1.00 65.67  ?  901 XRK A C12 1 
HETATM 6304 C C13 . XRK C 3 .   ? -6.657  61.260  80.488  1.00 68.68  ?  901 XRK A C13 1 
HETATM 6305 N N1  . XRK C 3 .   ? -7.876  58.239  81.992  1.00 72.76  ?  901 XRK A N1  1 
HETATM 6306 N N2  . XRK C 3 .   ? -6.946  59.521  84.278  1.00 69.34  ?  901 XRK A N2  1 
HETATM 6307 C C3  . XRK C 3 .   ? -4.706  54.121  84.984  1.00 87.04  ?  901 XRK A C3  1 
HETATM 6308 N N3  . XRK C 3 .   ? -4.907  74.089  88.693  1.00 52.94  ?  901 XRK A N3  1 
HETATM 6309 C C1  . XRK C 3 .   ? -1.843  52.809  86.720  1.00 92.98  ?  901 XRK A C1  1 
HETATM 6310 C C15 . XRK C 3 .   ? -6.164  61.957  81.628  1.00 70.87  ?  901 XRK A C15 1 
HETATM 6311 C C16 . XRK C 3 .   ? -5.550  63.310  81.456  1.00 57.43  ?  901 XRK A C16 1 
HETATM 6312 C C17 . XRK C 3 .   ? -6.263  61.386  82.866  1.00 66.92  ?  901 XRK A C17 1 
HETATM 6313 C C18 . XRK C 3 .   ? -6.831  60.130  83.017  1.00 68.46  ?  901 XRK A C18 1 
HETATM 6314 C C19 . XRK C 3 .   ? -6.338  60.180  85.456  1.00 66.67  ?  901 XRK A C19 1 
HETATM 6315 C C2  . XRK C 3 .   ? -3.313  54.066  85.410  1.00 86.61  ?  901 XRK A C2  1 
HETATM 6316 C C20 . XRK C 3 .   ? -7.270  61.053  86.231  1.00 59.40  ?  901 XRK A C20 1 
HETATM 6317 C C21 . XRK C 3 .   ? -6.499  62.022  87.120  1.00 59.98  ?  901 XRK A C21 1 
HETATM 6318 C C22 . XRK C 3 .   ? -7.299  62.666  88.237  1.00 57.88  ?  901 XRK A C22 1 
HETATM 6319 C C23 . XRK C 3 .   ? -6.430  63.534  89.109  1.00 57.92  ?  901 XRK A C23 1 
HETATM 6320 C C24 . XRK C 3 .   ? -6.104  69.799  89.813  1.00 56.13  ?  901 XRK A C24 1 
HETATM 6321 C C25 . XRK C 3 .   ? -6.692  71.131  89.464  1.00 54.80  ?  901 XRK A C25 1 
HETATM 6322 C C26 . XRK C 3 .   ? -6.022  73.175  88.771  1.00 59.87  ?  901 XRK A C26 1 
HETATM 6323 C C27 . XRK C 3 .   ? -3.752  73.947  87.992  1.00 53.88  ?  901 XRK A C27 1 
HETATM 6324 C C28 . XRK C 3 .   ? -3.620  75.810  88.962  1.00 51.80  ?  901 XRK A C28 1 
HETATM 6325 C C29 . XRK C 3 .   ? -3.303  77.066  89.480  1.00 48.89  ?  901 XRK A C29 1 
HETATM 6326 C C30 . XRK C 3 .   ? -5.340  77.025  90.535  1.00 50.66  ?  901 XRK A C30 1 
HETATM 6327 C C31 . XRK C 3 .   ? -4.835  75.293  89.309  1.00 48.25  ?  901 XRK A C31 1 
HETATM 6328 C C32 . XRK C 3 .   ? -6.333  72.465  87.476  1.00 58.80  ?  901 XRK A C32 1 
HETATM 6329 C C33 . XRK C 3 .   ? -7.090  71.253  88.000  1.00 57.56  ?  901 XRK A C33 1 
HETATM 6330 C C34 . XRK C 3 .   ? -7.561  58.334  84.420  1.00 67.19  ?  901 XRK A C34 1 
HETATM 6331 C C35 . XRK C 3 .   ? -8.891  57.138  85.699  1.00 68.24  ?  901 XRK A C35 1 
HETATM 6332 C C36 . XRK C 3 .   ? -9.274  56.980  83.427  1.00 70.75  ?  901 XRK A C36 1 
HETATM 6333 C C37 . XRK C 3 .   ? -7.878  57.477  83.228  1.00 74.52  ?  901 XRK A C37 1 
HETATM 6334 C C38 . XRK C 3 .   ? -5.156  55.128  84.150  1.00 80.67  ?  901 XRK A C38 1 
HETATM 6335 N N4  . XRK C 3 .   ? -2.946  74.953  88.124  1.00 51.56  ?  901 XRK A N4  1 
HETATM 6336 N N5  . XRK C 3 .   ? -2.174  77.697  89.230  1.00 43.13  ?  901 XRK A N5  1 
HETATM 6337 N N6  . XRK C 3 .   ? -4.200  77.656  90.281  1.00 43.86  ?  901 XRK A N6  1 
HETATM 6338 N N7  . XRK C 3 .   ? -5.756  75.858  90.088  1.00 58.99  ?  901 XRK A N7  1 
HETATM 6339 N N8  . XRK C 3 .   ? -7.919  57.978  85.593  1.00 63.82  ?  901 XRK A N8  1 
HETATM 6340 N N9  . XRK C 3 .   ? -9.664  56.761  84.667  1.00 71.85  ?  901 XRK A N9  1 
HETATM 6341 O O1  . XRK C 3 .   ? -3.151  53.397  86.534  1.00 94.09  ?  901 XRK A O1  1 
HETATM 6342 O O10 . XRK C 3 .   ? -5.984  66.708  89.670  1.00 55.70  ?  901 XRK A O10 1 
HETATM 6343 O O11 . XRK C 3 .   ? -7.848  66.957  88.088  1.00 53.35  ?  901 XRK A O11 1 
HETATM 6344 O O12 . XRK C 3 .   ? -5.632  68.038  87.628  1.00 52.33  -1 901 XRK A O12 1 
HETATM 6345 O O13 . XRK C 3 .   ? -7.070  68.818  89.443  1.00 65.75  ?  901 XRK A O13 1 
HETATM 6346 O O14 . XRK C 3 .   ? -5.704  72.149  89.656  1.00 57.32  ?  901 XRK A O14 1 
HETATM 6347 O O15 . XRK C 3 .   ? -7.197  73.282  86.735  1.00 53.60  ?  901 XRK A O15 1 
HETATM 6348 O O16 . XRK C 3 .   ? -8.495  71.331  87.922  1.00 67.06  ?  901 XRK A O16 1 
HETATM 6349 O O17 . XRK C 3 .   ? -9.125  56.667  86.771  1.00 63.02  ?  901 XRK A O17 1 
HETATM 6350 O O18 . XRK C 3 .   ? -10.005 56.769  82.496  1.00 70.54  ?  901 XRK A O18 1 
HETATM 6351 O O2  . XRK C 3 .   ? -2.396  54.510  84.786  1.00 86.48  ?  901 XRK A O2  1 
HETATM 6352 O O3  . XRK C 3 .   ? -8.621  56.626  80.547  1.00 76.53  ?  901 XRK A O3  1 
HETATM 6353 O O4  . XRK C 3 .   ? -7.919  61.812  85.303  1.00 63.36  ?  901 XRK A O4  1 
HETATM 6354 O O5  . XRK C 3 .   ? -5.503  61.339  87.763  1.00 56.71  ?  901 XRK A O5  1 
HETATM 6355 O O6  . XRK C 3 .   ? -8.339  63.447  87.672  1.00 61.38  ?  901 XRK A O6  1 
HETATM 6356 O O7  . XRK C 3 .   ? -7.181  64.576  89.754  1.00 62.65  ?  901 XRK A O7  1 
HETATM 6357 O O8  . XRK C 3 .   ? -7.494  66.086  91.558  1.00 62.12  ?  901 XRK A O8  1 
HETATM 6358 O O9  . XRK C 3 .   ? -5.262  64.976  91.251  1.00 53.13  -1 901 XRK A O9  1 
HETATM 6359 P P1  . XRK C 3 .   ? -6.446  65.597  90.677  1.00 56.81  ?  901 XRK A P1  1 
HETATM 6360 P P2  . XRK C 3 .   ? -6.644  67.608  88.573  1.00 55.31  ?  901 XRK A P2  1 
# 
