data_8VDV
# 
_entry.id   8VDV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   8VDV         pdb_00008vdv 10.2210/pdb8vdv/pdb 
WWPDB D_1000279919 ?            ?                   
# 
_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       2025-03-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        8VDV 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-18 
_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              mei.xu@novartis.com 
_pdbx_contact_author.name_first         Mei 
_pdbx_contact_author.name_last          Xu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2118-6591 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, M.'     1 ?                   
'Chopra, R.' 2 0000-0003-1877-6619 
# 
_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                     'PCSK9 in complex with inhibitor' 
_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 'Xu, M.' 1 ? 
primary 'Xu, M.' 2 ? 
# 
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 'Proprotein convertase subtilisin/kexin type 9'         10490.109 1   3.4.21.- ? 'PRODOMAIN, UNP RESIDUES 1-152' ? 
2 polymer man 'Proprotein convertase subtilisin/kexin type 9'         56107.277 1   3.4.21.- ? 'UNP RESIDUES 153-692'          ? 
3 polymer syn 'Inhibitor YBX-PHE-VAL-GLY-THR-THR-PHA-MAA-BIF-EME-NEH' 1235.493  1   ?        ? ?                               ? 
4 water   nat water                                                   18.015    258 ?        ? ?                               ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Neural apoptosis-regulated convertase 1,NARC-1,Proprotein convertase 9,PC9,Subtilisin/kexin-like protease PC9' 
2 'Neural apoptosis-regulated convertase 1,NARC-1,Proprotein convertase 9,PC9,Subtilisin/kexin-like protease PC9' 
# 
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  
;TATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHV
DYIEEDSSVFAQ
;
;TATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHV
DYIEEDSSVFAQ
;
A ? 
2 'polypeptide(L)' no no  
;SIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAG
VVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLV
TAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHV
AGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMAT
AIARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAEASMGTRVHC
HQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVTVACEEGWTL
TGCSALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEGAVTAVAICCRS
;
;SIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAG
VVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLV
TAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHV
AGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMAT
AIARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAEASMGTRVHC
HQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVTVACEEGWTL
TGCSALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEGAVTAVAICCRS
;
B ? 
3 'polypeptide(L)' no yes '(YBX)FVGTT(PHA)(MAA)(BIF)(EME)(NEH)' XFVGTTFAFXX L ? 
# 
_pdbx_entity_nonpoly.entity_id   4 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   ALA n 
1 3   THR n 
1 4   PHE n 
1 5   HIS n 
1 6   ARG n 
1 7   CYS n 
1 8   ALA n 
1 9   LYS n 
1 10  ASP n 
1 11  PRO n 
1 12  TRP n 
1 13  ARG n 
1 14  LEU n 
1 15  PRO n 
1 16  GLY n 
1 17  THR n 
1 18  TYR n 
1 19  VAL n 
1 20  VAL n 
1 21  VAL n 
1 22  LEU n 
1 23  LYS n 
1 24  GLU n 
1 25  GLU n 
1 26  THR n 
1 27  HIS n 
1 28  LEU n 
1 29  SER n 
1 30  GLN n 
1 31  SER n 
1 32  GLU n 
1 33  ARG n 
1 34  THR n 
1 35  ALA n 
1 36  ARG n 
1 37  ARG n 
1 38  LEU n 
1 39  GLN n 
1 40  ALA n 
1 41  GLN n 
1 42  ALA n 
1 43  ALA n 
1 44  ARG n 
1 45  ARG n 
1 46  GLY n 
1 47  TYR n 
1 48  LEU n 
1 49  THR n 
1 50  LYS n 
1 51  ILE n 
1 52  LEU n 
1 53  HIS n 
1 54  VAL n 
1 55  PHE n 
1 56  HIS n 
1 57  GLY n 
1 58  LEU n 
1 59  LEU n 
1 60  PRO n 
1 61  GLY n 
1 62  PHE n 
1 63  LEU n 
1 64  VAL n 
1 65  LYS n 
1 66  MET n 
1 67  SER n 
1 68  GLY n 
1 69  ASP n 
1 70  LEU n 
1 71  LEU n 
1 72  GLU n 
1 73  LEU n 
1 74  ALA n 
1 75  LEU n 
1 76  LYS n 
1 77  LEU n 
1 78  PRO n 
1 79  HIS n 
1 80  VAL n 
1 81  ASP n 
1 82  TYR n 
1 83  ILE n 
1 84  GLU n 
1 85  GLU n 
1 86  ASP n 
1 87  SER n 
1 88  SER n 
1 89  VAL n 
1 90  PHE n 
1 91  ALA n 
1 92  GLN n 
2 1   SER n 
2 2   ILE n 
2 3   PRO n 
2 4   TRP n 
2 5   ASN n 
2 6   LEU n 
2 7   GLU n 
2 8   ARG n 
2 9   ILE n 
2 10  THR n 
2 11  PRO n 
2 12  PRO n 
2 13  ARG n 
2 14  TYR n 
2 15  ARG n 
2 16  ALA n 
2 17  ASP n 
2 18  GLU n 
2 19  TYR n 
2 20  GLN n 
2 21  PRO n 
2 22  PRO n 
2 23  ASP n 
2 24  GLY n 
2 25  GLY n 
2 26  SER n 
2 27  LEU n 
2 28  VAL n 
2 29  GLU n 
2 30  VAL n 
2 31  TYR n 
2 32  LEU n 
2 33  LEU n 
2 34  ASP n 
2 35  THR n 
2 36  SER n 
2 37  ILE n 
2 38  GLN n 
2 39  SER n 
2 40  ASP n 
2 41  HIS n 
2 42  ARG n 
2 43  GLU n 
2 44  ILE n 
2 45  GLU n 
2 46  GLY n 
2 47  ARG n 
2 48  VAL n 
2 49  MET n 
2 50  VAL n 
2 51  THR n 
2 52  ASP n 
2 53  PHE n 
2 54  GLU n 
2 55  ASN n 
2 56  VAL n 
2 57  PRO n 
2 58  GLU n 
2 59  GLU n 
2 60  ASP n 
2 61  GLY n 
2 62  THR n 
2 63  ARG n 
2 64  PHE n 
2 65  HIS n 
2 66  ARG n 
2 67  GLN n 
2 68  ALA n 
2 69  SER n 
2 70  LYS n 
2 71  CYS n 
2 72  ASP n 
2 73  SER n 
2 74  HIS n 
2 75  GLY n 
2 76  THR n 
2 77  HIS n 
2 78  LEU n 
2 79  ALA n 
2 80  GLY n 
2 81  VAL n 
2 82  VAL n 
2 83  SER n 
2 84  GLY n 
2 85  ARG n 
2 86  ASP n 
2 87  ALA n 
2 88  GLY n 
2 89  VAL n 
2 90  ALA n 
2 91  LYS n 
2 92  GLY n 
2 93  ALA n 
2 94  SER n 
2 95  MET n 
2 96  ARG n 
2 97  SER n 
2 98  LEU n 
2 99  ARG n 
2 100 VAL n 
2 101 LEU n 
2 102 ASN n 
2 103 CYS n 
2 104 GLN n 
2 105 GLY n 
2 106 LYS n 
2 107 GLY n 
2 108 THR n 
2 109 VAL n 
2 110 SER n 
2 111 GLY n 
2 112 THR n 
2 113 LEU n 
2 114 ILE n 
2 115 GLY n 
2 116 LEU n 
2 117 GLU n 
2 118 PHE n 
2 119 ILE n 
2 120 ARG n 
2 121 LYS n 
2 122 SER n 
2 123 GLN n 
2 124 LEU n 
2 125 VAL n 
2 126 GLN n 
2 127 PRO n 
2 128 VAL n 
2 129 GLY n 
2 130 PRO n 
2 131 LEU n 
2 132 VAL n 
2 133 VAL n 
2 134 LEU n 
2 135 LEU n 
2 136 PRO n 
2 137 LEU n 
2 138 ALA n 
2 139 GLY n 
2 140 GLY n 
2 141 TYR n 
2 142 SER n 
2 143 ARG n 
2 144 VAL n 
2 145 LEU n 
2 146 ASN n 
2 147 ALA n 
2 148 ALA n 
2 149 CYS n 
2 150 GLN n 
2 151 ARG n 
2 152 LEU n 
2 153 ALA n 
2 154 ARG n 
2 155 ALA n 
2 156 GLY n 
2 157 VAL n 
2 158 VAL n 
2 159 LEU n 
2 160 VAL n 
2 161 THR n 
2 162 ALA n 
2 163 ALA n 
2 164 GLY n 
2 165 ASN n 
2 166 PHE n 
2 167 ARG n 
2 168 ASP n 
2 169 ASP n 
2 170 ALA n 
2 171 CYS n 
2 172 LEU n 
2 173 TYR n 
2 174 SER n 
2 175 PRO n 
2 176 ALA n 
2 177 SER n 
2 178 ALA n 
2 179 PRO n 
2 180 GLU n 
2 181 VAL n 
2 182 ILE n 
2 183 THR n 
2 184 VAL n 
2 185 GLY n 
2 186 ALA n 
2 187 THR n 
2 188 ASN n 
2 189 ALA n 
2 190 GLN n 
2 191 ASP n 
2 192 GLN n 
2 193 PRO n 
2 194 VAL n 
2 195 THR n 
2 196 LEU n 
2 197 GLY n 
2 198 THR n 
2 199 LEU n 
2 200 GLY n 
2 201 THR n 
2 202 ASN n 
2 203 PHE n 
2 204 GLY n 
2 205 ARG n 
2 206 CYS n 
2 207 VAL n 
2 208 ASP n 
2 209 LEU n 
2 210 PHE n 
2 211 ALA n 
2 212 PRO n 
2 213 GLY n 
2 214 GLU n 
2 215 ASP n 
2 216 ILE n 
2 217 ILE n 
2 218 GLY n 
2 219 ALA n 
2 220 SER n 
2 221 SER n 
2 222 ASP n 
2 223 CYS n 
2 224 SER n 
2 225 THR n 
2 226 CYS n 
2 227 PHE n 
2 228 VAL n 
2 229 SER n 
2 230 GLN n 
2 231 SER n 
2 232 GLY n 
2 233 THR n 
2 234 SER n 
2 235 GLN n 
2 236 ALA n 
2 237 ALA n 
2 238 ALA n 
2 239 HIS n 
2 240 VAL n 
2 241 ALA n 
2 242 GLY n 
2 243 ILE n 
2 244 ALA n 
2 245 ALA n 
2 246 MET n 
2 247 MET n 
2 248 LEU n 
2 249 SER n 
2 250 ALA n 
2 251 GLU n 
2 252 PRO n 
2 253 GLU n 
2 254 LEU n 
2 255 THR n 
2 256 LEU n 
2 257 ALA n 
2 258 GLU n 
2 259 LEU n 
2 260 ARG n 
2 261 GLN n 
2 262 ARG n 
2 263 LEU n 
2 264 ILE n 
2 265 HIS n 
2 266 PHE n 
2 267 SER n 
2 268 ALA n 
2 269 LYS n 
2 270 ASP n 
2 271 VAL n 
2 272 ILE n 
2 273 ASN n 
2 274 GLU n 
2 275 ALA n 
2 276 TRP n 
2 277 PHE n 
2 278 PRO n 
2 279 GLU n 
2 280 ASP n 
2 281 GLN n 
2 282 ARG n 
2 283 VAL n 
2 284 LEU n 
2 285 THR n 
2 286 PRO n 
2 287 ASN n 
2 288 LEU n 
2 289 VAL n 
2 290 ALA n 
2 291 ALA n 
2 292 LEU n 
2 293 PRO n 
2 294 PRO n 
2 295 SER n 
2 296 THR n 
2 297 HIS n 
2 298 GLY n 
2 299 ALA n 
2 300 GLY n 
2 301 TRP n 
2 302 GLN n 
2 303 LEU n 
2 304 PHE n 
2 305 CYS n 
2 306 ARG n 
2 307 THR n 
2 308 VAL n 
2 309 TRP n 
2 310 SER n 
2 311 ALA n 
2 312 HIS n 
2 313 SER n 
2 314 GLY n 
2 315 PRO n 
2 316 THR n 
2 317 ARG n 
2 318 MET n 
2 319 ALA n 
2 320 THR n 
2 321 ALA n 
2 322 ILE n 
2 323 ALA n 
2 324 ARG n 
2 325 CYS n 
2 326 ALA n 
2 327 PRO n 
2 328 ASP n 
2 329 GLU n 
2 330 GLU n 
2 331 LEU n 
2 332 LEU n 
2 333 SER n 
2 334 CYS n 
2 335 SER n 
2 336 SER n 
2 337 PHE n 
2 338 SER n 
2 339 ARG n 
2 340 SER n 
2 341 GLY n 
2 342 LYS n 
2 343 ARG n 
2 344 ARG n 
2 345 GLY n 
2 346 GLU n 
2 347 ARG n 
2 348 MET n 
2 349 GLU n 
2 350 ALA n 
2 351 GLN n 
2 352 GLY n 
2 353 GLY n 
2 354 LYS n 
2 355 LEU n 
2 356 VAL n 
2 357 CYS n 
2 358 ARG n 
2 359 ALA n 
2 360 HIS n 
2 361 ASN n 
2 362 ALA n 
2 363 PHE n 
2 364 GLY n 
2 365 GLY n 
2 366 GLU n 
2 367 GLY n 
2 368 VAL n 
2 369 TYR n 
2 370 ALA n 
2 371 ILE n 
2 372 ALA n 
2 373 ARG n 
2 374 CYS n 
2 375 CYS n 
2 376 LEU n 
2 377 LEU n 
2 378 PRO n 
2 379 GLN n 
2 380 ALA n 
2 381 ASN n 
2 382 CYS n 
2 383 SER n 
2 384 VAL n 
2 385 HIS n 
2 386 THR n 
2 387 ALA n 
2 388 PRO n 
2 389 PRO n 
2 390 ALA n 
2 391 GLU n 
2 392 ALA n 
2 393 SER n 
2 394 MET n 
2 395 GLY n 
2 396 THR n 
2 397 ARG n 
2 398 VAL n 
2 399 HIS n 
2 400 CYS n 
2 401 HIS n 
2 402 GLN n 
2 403 GLN n 
2 404 GLY n 
2 405 HIS n 
2 406 VAL n 
2 407 LEU n 
2 408 THR n 
2 409 GLY n 
2 410 CYS n 
2 411 SER n 
2 412 SER n 
2 413 HIS n 
2 414 TRP n 
2 415 GLU n 
2 416 VAL n 
2 417 GLU n 
2 418 ASP n 
2 419 LEU n 
2 420 GLY n 
2 421 THR n 
2 422 HIS n 
2 423 LYS n 
2 424 PRO n 
2 425 PRO n 
2 426 VAL n 
2 427 LEU n 
2 428 ARG n 
2 429 PRO n 
2 430 ARG n 
2 431 GLY n 
2 432 GLN n 
2 433 PRO n 
2 434 ASN n 
2 435 GLN n 
2 436 CYS n 
2 437 VAL n 
2 438 GLY n 
2 439 HIS n 
2 440 ARG n 
2 441 GLU n 
2 442 ALA n 
2 443 SER n 
2 444 ILE n 
2 445 HIS n 
2 446 ALA n 
2 447 SER n 
2 448 CYS n 
2 449 CYS n 
2 450 HIS n 
2 451 ALA n 
2 452 PRO n 
2 453 GLY n 
2 454 LEU n 
2 455 GLU n 
2 456 CYS n 
2 457 LYS n 
2 458 VAL n 
2 459 LYS n 
2 460 GLU n 
2 461 HIS n 
2 462 GLY n 
2 463 ILE n 
2 464 PRO n 
2 465 ALA n 
2 466 PRO n 
2 467 GLN n 
2 468 GLU n 
2 469 GLN n 
2 470 VAL n 
2 471 THR n 
2 472 VAL n 
2 473 ALA n 
2 474 CYS n 
2 475 GLU n 
2 476 GLU n 
2 477 GLY n 
2 478 TRP n 
2 479 THR n 
2 480 LEU n 
2 481 THR n 
2 482 GLY n 
2 483 CYS n 
2 484 SER n 
2 485 ALA n 
2 486 LEU n 
2 487 PRO n 
2 488 GLY n 
2 489 THR n 
2 490 SER n 
2 491 HIS n 
2 492 VAL n 
2 493 LEU n 
2 494 GLY n 
2 495 ALA n 
2 496 TYR n 
2 497 ALA n 
2 498 VAL n 
2 499 ASP n 
2 500 ASN n 
2 501 THR n 
2 502 CYS n 
2 503 VAL n 
2 504 VAL n 
2 505 ARG n 
2 506 SER n 
2 507 ARG n 
2 508 ASP n 
2 509 VAL n 
2 510 SER n 
2 511 THR n 
2 512 THR n 
2 513 GLY n 
2 514 SER n 
2 515 THR n 
2 516 SER n 
2 517 GLU n 
2 518 GLY n 
2 519 ALA n 
2 520 VAL n 
2 521 THR n 
2 522 ALA n 
2 523 VAL n 
2 524 ALA n 
2 525 ILE n 
2 526 CYS n 
2 527 CYS n 
2 528 ARG n 
2 529 SER n 
3 1   YBX n 
3 2   PHE n 
3 3   VAL n 
3 4   GLY n 
3 5   THR n 
3 6   THR n 
3 7   PHA n 
3 8   MAA n 
3 9   BIF n 
3 10  EME n 
3 11  NEH 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 92  human ? 'PCSK9, NARC1, PSEC0052' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? human 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 529 human ? 'PCSK9, NARC1, PSEC0052' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? human 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_src_syn.entity_id              3 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       11 
_pdbx_entity_src_syn.organism_scientific    'synthetic construct' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       32630 
_pdbx_entity_src_syn.details                ? 
# 
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 
BIF 'L-peptide linking' n '(R)-2-AMINO-3-(4-PHENYLCYCLOHEXYL)PROPANOIC ACID' BIPHENYLALANINE 'C15 H15 N O2'   241.285 
CYS 'L-peptide linking' y CYSTEINE                                           ?               'C3 H7 N O2 S'   121.158 
EME 'L-peptide linking' n 'N-methyl-L-glutamic acid'                         ?               'C6 H11 N O4'    161.156 
GLN 'L-peptide linking' y GLUTAMINE                                          ?               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                    ?               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                            ?               'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                          ?               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                              ?               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                         ?               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                            ?               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                             ?               'C6 H15 N2 O2 1' 147.195 
MAA 'L-peptide linking' n N-methyl-L-alanine                                 ?               'C4 H9 N O2'     103.120 
MET 'L-peptide linking' y METHIONINE                                         ?               'C5 H11 N O2 S'  149.211 
NEH non-polymer         . ETHANAMINE                                         ?               'C2 H7 N'        45.084  
PHA 'L-peptide linking' n PHENYLALANINAL                                     ?               'C9 H11 N O'     149.190 
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 
YBX non-polymer         . '(ethylsulfanyl)acetic acid'                       ?               'C4 H8 O2 S'     120.170 
# 
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   THR 1   61  61  THR THR A . n 
A 1 2   ALA 2   62  62  ALA ALA A . n 
A 1 3   THR 3   63  63  THR THR A . n 
A 1 4   PHE 4   64  64  PHE PHE A . n 
A 1 5   HIS 5   65  65  HIS HIS A . n 
A 1 6   ARG 6   66  66  ARG ARG A . n 
A 1 7   CYS 7   67  67  CYS CYS A . n 
A 1 8   ALA 8   68  68  ALA ALA A . n 
A 1 9   LYS 9   69  69  LYS LYS A . n 
A 1 10  ASP 10  70  70  ASP ASP A . n 
A 1 11  PRO 11  71  71  PRO PRO A . n 
A 1 12  TRP 12  72  72  TRP TRP A . n 
A 1 13  ARG 13  73  73  ARG ARG A . n 
A 1 14  LEU 14  74  74  LEU LEU A . n 
A 1 15  PRO 15  75  75  PRO PRO A . n 
A 1 16  GLY 16  76  76  GLY GLY A . n 
A 1 17  THR 17  77  77  THR THR A . n 
A 1 18  TYR 18  78  78  TYR TYR A . n 
A 1 19  VAL 19  79  79  VAL VAL A . n 
A 1 20  VAL 20  80  80  VAL VAL A . n 
A 1 21  VAL 21  81  81  VAL VAL A . n 
A 1 22  LEU 22  82  82  LEU LEU A . n 
A 1 23  LYS 23  83  83  LYS LYS A . n 
A 1 24  GLU 24  84  84  GLU GLU A . n 
A 1 25  GLU 25  85  85  GLU GLU A . n 
A 1 26  THR 26  86  86  THR THR A . n 
A 1 27  HIS 27  87  87  HIS HIS A . n 
A 1 28  LEU 28  88  88  LEU LEU A . n 
A 1 29  SER 29  89  89  SER SER A . n 
A 1 30  GLN 30  90  90  GLN GLN A . n 
A 1 31  SER 31  91  91  SER SER A . n 
A 1 32  GLU 32  92  92  GLU GLU A . n 
A 1 33  ARG 33  93  93  ARG ARG A . n 
A 1 34  THR 34  94  94  THR THR A . n 
A 1 35  ALA 35  95  95  ALA ALA A . n 
A 1 36  ARG 36  96  96  ARG ARG A . n 
A 1 37  ARG 37  97  97  ARG ARG A . n 
A 1 38  LEU 38  98  98  LEU LEU A . n 
A 1 39  GLN 39  99  99  GLN GLN A . n 
A 1 40  ALA 40  100 100 ALA ALA A . n 
A 1 41  GLN 41  101 101 GLN GLN A . n 
A 1 42  ALA 42  102 102 ALA ALA A . n 
A 1 43  ALA 43  103 103 ALA ALA A . n 
A 1 44  ARG 44  104 104 ARG ARG A . n 
A 1 45  ARG 45  105 105 ARG ARG A . n 
A 1 46  GLY 46  106 106 GLY GLY A . n 
A 1 47  TYR 47  107 107 TYR TYR A . n 
A 1 48  LEU 48  108 108 LEU LEU A . n 
A 1 49  THR 49  109 109 THR THR A . n 
A 1 50  LYS 50  110 110 LYS LYS A . n 
A 1 51  ILE 51  111 111 ILE ILE A . n 
A 1 52  LEU 52  112 112 LEU LEU A . n 
A 1 53  HIS 53  113 113 HIS HIS A . n 
A 1 54  VAL 54  114 114 VAL VAL A . n 
A 1 55  PHE 55  115 115 PHE PHE A . n 
A 1 56  HIS 56  116 116 HIS HIS A . n 
A 1 57  GLY 57  117 117 GLY GLY A . n 
A 1 58  LEU 58  118 118 LEU LEU A . n 
A 1 59  LEU 59  119 119 LEU LEU A . n 
A 1 60  PRO 60  120 120 PRO PRO A . n 
A 1 61  GLY 61  121 121 GLY GLY A . n 
A 1 62  PHE 62  122 122 PHE PHE A . n 
A 1 63  LEU 63  123 123 LEU LEU A . n 
A 1 64  VAL 64  124 124 VAL VAL A . n 
A 1 65  LYS 65  125 125 LYS LYS A . n 
A 1 66  MET 66  126 126 MET MET A . n 
A 1 67  SER 67  127 127 SER SER A . n 
A 1 68  GLY 68  128 128 GLY GLY A . n 
A 1 69  ASP 69  129 129 ASP ASP A . n 
A 1 70  LEU 70  130 130 LEU LEU A . n 
A 1 71  LEU 71  131 131 LEU LEU A . n 
A 1 72  GLU 72  132 132 GLU GLU A . n 
A 1 73  LEU 73  133 133 LEU LEU A . n 
A 1 74  ALA 74  134 134 ALA ALA A . n 
A 1 75  LEU 75  135 135 LEU LEU A . n 
A 1 76  LYS 76  136 136 LYS LYS A . n 
A 1 77  LEU 77  137 137 LEU LEU A . n 
A 1 78  PRO 78  138 138 PRO PRO A . n 
A 1 79  HIS 79  139 139 HIS HIS A . n 
A 1 80  VAL 80  140 140 VAL VAL A . n 
A 1 81  ASP 81  141 141 ASP ASP A . n 
A 1 82  TYR 82  142 142 TYR TYR A . n 
A 1 83  ILE 83  143 143 ILE ILE A . n 
A 1 84  GLU 84  144 144 GLU GLU A . n 
A 1 85  GLU 85  145 145 GLU GLU A . n 
A 1 86  ASP 86  146 146 ASP ASP A . n 
A 1 87  SER 87  147 147 SER SER A . n 
A 1 88  SER 88  148 148 SER SER A . n 
A 1 89  VAL 89  149 149 VAL VAL A . n 
A 1 90  PHE 90  150 150 PHE PHE A . n 
A 1 91  ALA 91  151 151 ALA ALA A . n 
A 1 92  GLN 92  152 152 GLN GLN A . n 
B 2 1   SER 1   153 153 SER SER B . n 
B 2 2   ILE 2   154 154 ILE ILE B . n 
B 2 3   PRO 3   155 155 PRO PRO B . n 
B 2 4   TRP 4   156 156 TRP TRP B . n 
B 2 5   ASN 5   157 157 ASN ASN B . n 
B 2 6   LEU 6   158 158 LEU LEU B . n 
B 2 7   GLU 7   159 159 GLU GLU B . n 
B 2 8   ARG 8   160 160 ARG ARG B . n 
B 2 9   ILE 9   161 161 ILE ILE B . n 
B 2 10  THR 10  162 162 THR THR B . n 
B 2 11  PRO 11  163 163 PRO PRO B . n 
B 2 12  PRO 12  164 164 PRO PRO B . n 
B 2 13  ARG 13  165 165 ARG ARG B . n 
B 2 14  TYR 14  166 166 TYR TYR B . n 
B 2 15  ARG 15  167 167 ARG ARG B . n 
B 2 16  ALA 16  168 ?   ?   ?   B . n 
B 2 17  ASP 17  169 ?   ?   ?   B . n 
B 2 18  GLU 18  170 ?   ?   ?   B . n 
B 2 19  TYR 19  171 ?   ?   ?   B . n 
B 2 20  GLN 20  172 ?   ?   ?   B . n 
B 2 21  PRO 21  173 ?   ?   ?   B . n 
B 2 22  PRO 22  174 ?   ?   ?   B . n 
B 2 23  ASP 23  175 ?   ?   ?   B . n 
B 2 24  GLY 24  176 176 GLY GLY B . n 
B 2 25  GLY 25  177 177 GLY GLY B . n 
B 2 26  SER 26  178 178 SER SER B . n 
B 2 27  LEU 27  179 179 LEU LEU B . n 
B 2 28  VAL 28  180 180 VAL VAL B . n 
B 2 29  GLU 29  181 181 GLU GLU B . n 
B 2 30  VAL 30  182 182 VAL VAL B . n 
B 2 31  TYR 31  183 183 TYR TYR B . n 
B 2 32  LEU 32  184 184 LEU LEU B . n 
B 2 33  LEU 33  185 185 LEU LEU B . n 
B 2 34  ASP 34  186 186 ASP ASP B . n 
B 2 35  THR 35  187 187 THR THR B . n 
B 2 36  SER 36  188 188 SER SER B . n 
B 2 37  ILE 37  189 189 ILE ILE B . n 
B 2 38  GLN 38  190 190 GLN GLN B . n 
B 2 39  SER 39  191 191 SER SER B . n 
B 2 40  ASP 40  192 192 ASP ASP B . n 
B 2 41  HIS 41  193 193 HIS HIS B . n 
B 2 42  ARG 42  194 194 ARG ARG B . n 
B 2 43  GLU 43  195 195 GLU GLU B . n 
B 2 44  ILE 44  196 196 ILE ILE B . n 
B 2 45  GLU 45  197 197 GLU GLU B . n 
B 2 46  GLY 46  198 198 GLY GLY B . n 
B 2 47  ARG 47  199 199 ARG ARG B . n 
B 2 48  VAL 48  200 200 VAL VAL B . n 
B 2 49  MET 49  201 201 MET MET B . n 
B 2 50  VAL 50  202 202 VAL VAL B . n 
B 2 51  THR 51  203 203 THR THR B . n 
B 2 52  ASP 52  204 204 ASP ASP B . n 
B 2 53  PHE 53  205 205 PHE PHE B . n 
B 2 54  GLU 54  206 206 GLU GLU B . n 
B 2 55  ASN 55  207 207 ASN ASN B . n 
B 2 56  VAL 56  208 208 VAL VAL B . n 
B 2 57  PRO 57  209 209 PRO PRO B . n 
B 2 58  GLU 58  210 210 GLU GLU B . n 
B 2 59  GLU 59  211 211 GLU GLU B . n 
B 2 60  ASP 60  212 212 ASP ASP B . n 
B 2 61  GLY 61  213 ?   ?   ?   B . n 
B 2 62  THR 62  214 ?   ?   ?   B . n 
B 2 63  ARG 63  215 ?   ?   ?   B . n 
B 2 64  PHE 64  216 ?   ?   ?   B . n 
B 2 65  HIS 65  217 ?   ?   ?   B . n 
B 2 66  ARG 66  218 ?   ?   ?   B . n 
B 2 67  GLN 67  219 ?   ?   ?   B . n 
B 2 68  ALA 68  220 220 ALA ALA B . n 
B 2 69  SER 69  221 221 SER SER B . n 
B 2 70  LYS 70  222 222 LYS LYS B . n 
B 2 71  CYS 71  223 223 CYS CYS B . n 
B 2 72  ASP 72  224 224 ASP ASP B . n 
B 2 73  SER 73  225 225 SER SER B . n 
B 2 74  HIS 74  226 226 HIS HIS B . n 
B 2 75  GLY 75  227 227 GLY GLY B . n 
B 2 76  THR 76  228 228 THR THR B . n 
B 2 77  HIS 77  229 229 HIS HIS B . n 
B 2 78  LEU 78  230 230 LEU LEU B . n 
B 2 79  ALA 79  231 231 ALA ALA B . n 
B 2 80  GLY 80  232 232 GLY GLY B . n 
B 2 81  VAL 81  233 233 VAL VAL B . n 
B 2 82  VAL 82  234 234 VAL VAL B . n 
B 2 83  SER 83  235 235 SER SER B . n 
B 2 84  GLY 84  236 236 GLY GLY B . n 
B 2 85  ARG 85  237 237 ARG ARG B . n 
B 2 86  ASP 86  238 238 ASP ASP B . n 
B 2 87  ALA 87  239 239 ALA ALA B . n 
B 2 88  GLY 88  240 240 GLY GLY B . n 
B 2 89  VAL 89  241 241 VAL VAL B . n 
B 2 90  ALA 90  242 242 ALA ALA B . n 
B 2 91  LYS 91  243 243 LYS LYS B . n 
B 2 92  GLY 92  244 244 GLY GLY B . n 
B 2 93  ALA 93  245 245 ALA ALA B . n 
B 2 94  SER 94  246 246 SER SER B . n 
B 2 95  MET 95  247 247 MET MET B . n 
B 2 96  ARG 96  248 248 ARG ARG B . n 
B 2 97  SER 97  249 249 SER SER B . n 
B 2 98  LEU 98  250 250 LEU LEU B . n 
B 2 99  ARG 99  251 251 ARG ARG B . n 
B 2 100 VAL 100 252 252 VAL VAL B . n 
B 2 101 LEU 101 253 253 LEU LEU B . n 
B 2 102 ASN 102 254 254 ASN ASN B . n 
B 2 103 CYS 103 255 255 CYS CYS B . n 
B 2 104 GLN 104 256 256 GLN GLN B . n 
B 2 105 GLY 105 257 257 GLY GLY B . n 
B 2 106 LYS 106 258 258 LYS LYS B . n 
B 2 107 GLY 107 259 259 GLY GLY B . n 
B 2 108 THR 108 260 260 THR THR B . n 
B 2 109 VAL 109 261 261 VAL VAL B . n 
B 2 110 SER 110 262 262 SER SER B . n 
B 2 111 GLY 111 263 263 GLY GLY B . n 
B 2 112 THR 112 264 264 THR THR B . n 
B 2 113 LEU 113 265 265 LEU LEU B . n 
B 2 114 ILE 114 266 266 ILE ILE B . n 
B 2 115 GLY 115 267 267 GLY GLY B . n 
B 2 116 LEU 116 268 268 LEU LEU B . n 
B 2 117 GLU 117 269 269 GLU GLU B . n 
B 2 118 PHE 118 270 270 PHE PHE B . n 
B 2 119 ILE 119 271 271 ILE ILE B . n 
B 2 120 ARG 120 272 272 ARG ARG B . n 
B 2 121 LYS 121 273 273 LYS LYS B . n 
B 2 122 SER 122 274 274 SER SER B . n 
B 2 123 GLN 123 275 275 GLN GLN B . n 
B 2 124 LEU 124 276 276 LEU LEU B . n 
B 2 125 VAL 125 277 277 VAL VAL B . n 
B 2 126 GLN 126 278 278 GLN GLN B . n 
B 2 127 PRO 127 279 279 PRO PRO B . n 
B 2 128 VAL 128 280 280 VAL VAL B . n 
B 2 129 GLY 129 281 281 GLY GLY B . n 
B 2 130 PRO 130 282 282 PRO PRO B . n 
B 2 131 LEU 131 283 283 LEU LEU B . n 
B 2 132 VAL 132 284 284 VAL VAL B . n 
B 2 133 VAL 133 285 285 VAL VAL B . n 
B 2 134 LEU 134 286 286 LEU LEU B . n 
B 2 135 LEU 135 287 287 LEU LEU B . n 
B 2 136 PRO 136 288 288 PRO PRO B . n 
B 2 137 LEU 137 289 289 LEU LEU B . n 
B 2 138 ALA 138 290 290 ALA ALA B . n 
B 2 139 GLY 139 291 291 GLY GLY B . n 
B 2 140 GLY 140 292 292 GLY GLY B . n 
B 2 141 TYR 141 293 293 TYR TYR B . n 
B 2 142 SER 142 294 294 SER SER B . n 
B 2 143 ARG 143 295 295 ARG ARG B . n 
B 2 144 VAL 144 296 296 VAL VAL B . n 
B 2 145 LEU 145 297 297 LEU LEU B . n 
B 2 146 ASN 146 298 298 ASN ASN B . n 
B 2 147 ALA 147 299 299 ALA ALA B . n 
B 2 148 ALA 148 300 300 ALA ALA B . n 
B 2 149 CYS 149 301 301 CYS CYS B . n 
B 2 150 GLN 150 302 302 GLN GLN B . n 
B 2 151 ARG 151 303 303 ARG ARG B . n 
B 2 152 LEU 152 304 304 LEU LEU B . n 
B 2 153 ALA 153 305 305 ALA ALA B . n 
B 2 154 ARG 154 306 306 ARG ARG B . n 
B 2 155 ALA 155 307 307 ALA ALA B . n 
B 2 156 GLY 156 308 308 GLY GLY B . n 
B 2 157 VAL 157 309 309 VAL VAL B . n 
B 2 158 VAL 158 310 310 VAL VAL B . n 
B 2 159 LEU 159 311 311 LEU LEU B . n 
B 2 160 VAL 160 312 312 VAL VAL B . n 
B 2 161 THR 161 313 313 THR THR B . n 
B 2 162 ALA 162 314 314 ALA ALA B . n 
B 2 163 ALA 163 315 315 ALA ALA B . n 
B 2 164 GLY 164 316 316 GLY GLY B . n 
B 2 165 ASN 165 317 317 ASN ASN B . n 
B 2 166 PHE 166 318 318 PHE PHE B . n 
B 2 167 ARG 167 319 319 ARG ARG B . n 
B 2 168 ASP 168 320 320 ASP ASP B . n 
B 2 169 ASP 169 321 321 ASP ASP B . n 
B 2 170 ALA 170 322 322 ALA ALA B . n 
B 2 171 CYS 171 323 323 CYS CYS B . n 
B 2 172 LEU 172 324 324 LEU LEU B . n 
B 2 173 TYR 173 325 325 TYR TYR B . n 
B 2 174 SER 174 326 326 SER SER B . n 
B 2 175 PRO 175 327 327 PRO PRO B . n 
B 2 176 ALA 176 328 328 ALA ALA B . n 
B 2 177 SER 177 329 329 SER SER B . n 
B 2 178 ALA 178 330 330 ALA ALA B . n 
B 2 179 PRO 179 331 331 PRO PRO B . n 
B 2 180 GLU 180 332 332 GLU GLU B . n 
B 2 181 VAL 181 333 333 VAL VAL B . n 
B 2 182 ILE 182 334 334 ILE ILE B . n 
B 2 183 THR 183 335 335 THR THR B . n 
B 2 184 VAL 184 336 336 VAL VAL B . n 
B 2 185 GLY 185 337 337 GLY GLY B . n 
B 2 186 ALA 186 338 338 ALA ALA B . n 
B 2 187 THR 187 339 339 THR THR B . n 
B 2 188 ASN 188 340 340 ASN ASN B . n 
B 2 189 ALA 189 341 341 ALA ALA B . n 
B 2 190 GLN 190 342 342 GLN GLN B . n 
B 2 191 ASP 191 343 343 ASP ASP B . n 
B 2 192 GLN 192 344 344 GLN GLN B . n 
B 2 193 PRO 193 345 345 PRO PRO B . n 
B 2 194 VAL 194 346 346 VAL VAL B . n 
B 2 195 THR 195 347 347 THR THR B . n 
B 2 196 LEU 196 348 348 LEU LEU B . n 
B 2 197 GLY 197 349 349 GLY GLY B . n 
B 2 198 THR 198 350 350 THR THR B . n 
B 2 199 LEU 199 351 351 LEU LEU B . n 
B 2 200 GLY 200 352 352 GLY GLY B . n 
B 2 201 THR 201 353 353 THR THR B . n 
B 2 202 ASN 202 354 354 ASN ASN B . n 
B 2 203 PHE 203 355 355 PHE PHE B . n 
B 2 204 GLY 204 356 356 GLY GLY B . n 
B 2 205 ARG 205 357 357 ARG ARG B . n 
B 2 206 CYS 206 358 358 CYS CYS B . n 
B 2 207 VAL 207 359 359 VAL VAL B . n 
B 2 208 ASP 208 360 360 ASP ASP B . n 
B 2 209 LEU 209 361 361 LEU LEU B . n 
B 2 210 PHE 210 362 362 PHE PHE B . n 
B 2 211 ALA 211 363 363 ALA ALA B . n 
B 2 212 PRO 212 364 364 PRO PRO B . n 
B 2 213 GLY 213 365 365 GLY GLY B . n 
B 2 214 GLU 214 366 366 GLU GLU B . n 
B 2 215 ASP 215 367 367 ASP ASP B . n 
B 2 216 ILE 216 368 368 ILE ILE B . n 
B 2 217 ILE 217 369 369 ILE ILE B . n 
B 2 218 GLY 218 370 370 GLY GLY B . n 
B 2 219 ALA 219 371 371 ALA ALA B . n 
B 2 220 SER 220 372 372 SER SER B . n 
B 2 221 SER 221 373 373 SER SER B . n 
B 2 222 ASP 222 374 374 ASP ASP B . n 
B 2 223 CYS 223 375 375 CYS CYS B . n 
B 2 224 SER 224 376 376 SER SER B . n 
B 2 225 THR 225 377 377 THR THR B . n 
B 2 226 CYS 226 378 378 CYS CYS B . n 
B 2 227 PHE 227 379 379 PHE PHE B . n 
B 2 228 VAL 228 380 380 VAL VAL B . n 
B 2 229 SER 229 381 381 SER SER B . n 
B 2 230 GLN 230 382 382 GLN GLN B . n 
B 2 231 SER 231 383 383 SER SER B . n 
B 2 232 GLY 232 384 384 GLY GLY B . n 
B 2 233 THR 233 385 385 THR THR B . n 
B 2 234 SER 234 386 386 SER SER B . n 
B 2 235 GLN 235 387 387 GLN GLN B . n 
B 2 236 ALA 236 388 388 ALA ALA B . n 
B 2 237 ALA 237 389 389 ALA ALA B . n 
B 2 238 ALA 238 390 390 ALA ALA B . n 
B 2 239 HIS 239 391 391 HIS HIS B . n 
B 2 240 VAL 240 392 392 VAL VAL B . n 
B 2 241 ALA 241 393 393 ALA ALA B . n 
B 2 242 GLY 242 394 394 GLY GLY B . n 
B 2 243 ILE 243 395 395 ILE ILE B . n 
B 2 244 ALA 244 396 396 ALA ALA B . n 
B 2 245 ALA 245 397 397 ALA ALA B . n 
B 2 246 MET 246 398 398 MET MET B . n 
B 2 247 MET 247 399 399 MET MET B . n 
B 2 248 LEU 248 400 400 LEU LEU B . n 
B 2 249 SER 249 401 401 SER SER B . n 
B 2 250 ALA 250 402 402 ALA ALA B . n 
B 2 251 GLU 251 403 403 GLU GLU B . n 
B 2 252 PRO 252 404 404 PRO PRO B . n 
B 2 253 GLU 253 405 405 GLU GLU B . n 
B 2 254 LEU 254 406 406 LEU LEU B . n 
B 2 255 THR 255 407 407 THR THR B . n 
B 2 256 LEU 256 408 408 LEU LEU B . n 
B 2 257 ALA 257 409 409 ALA ALA B . n 
B 2 258 GLU 258 410 410 GLU GLU B . n 
B 2 259 LEU 259 411 411 LEU LEU B . n 
B 2 260 ARG 260 412 412 ARG ARG B . n 
B 2 261 GLN 261 413 413 GLN GLN B . n 
B 2 262 ARG 262 414 414 ARG ARG B . n 
B 2 263 LEU 263 415 415 LEU LEU B . n 
B 2 264 ILE 264 416 416 ILE ILE B . n 
B 2 265 HIS 265 417 417 HIS HIS B . n 
B 2 266 PHE 266 418 418 PHE PHE B . n 
B 2 267 SER 267 419 419 SER SER B . n 
B 2 268 ALA 268 420 420 ALA ALA B . n 
B 2 269 LYS 269 421 421 LYS LYS B . n 
B 2 270 ASP 270 422 422 ASP ASP B . n 
B 2 271 VAL 271 423 423 VAL VAL B . n 
B 2 272 ILE 272 424 424 ILE ILE B . n 
B 2 273 ASN 273 425 425 ASN ASN B . n 
B 2 274 GLU 274 426 426 GLU GLU B . n 
B 2 275 ALA 275 427 427 ALA ALA B . n 
B 2 276 TRP 276 428 428 TRP TRP B . n 
B 2 277 PHE 277 429 429 PHE PHE B . n 
B 2 278 PRO 278 430 430 PRO PRO B . n 
B 2 279 GLU 279 431 431 GLU GLU B . n 
B 2 280 ASP 280 432 432 ASP ASP B . n 
B 2 281 GLN 281 433 433 GLN GLN B . n 
B 2 282 ARG 282 434 434 ARG ARG B . n 
B 2 283 VAL 283 435 435 VAL VAL B . n 
B 2 284 LEU 284 436 436 LEU LEU B . n 
B 2 285 THR 285 437 437 THR THR B . n 
B 2 286 PRO 286 438 438 PRO PRO B . n 
B 2 287 ASN 287 439 439 ASN ASN B . n 
B 2 288 LEU 288 440 440 LEU LEU B . n 
B 2 289 VAL 289 441 441 VAL VAL B . n 
B 2 290 ALA 290 442 442 ALA ALA B . n 
B 2 291 ALA 291 443 443 ALA ALA B . n 
B 2 292 LEU 292 444 444 LEU LEU B . n 
B 2 293 PRO 293 445 445 PRO PRO B . n 
B 2 294 PRO 294 446 446 PRO PRO B . n 
B 2 295 SER 295 447 447 SER SER B . n 
B 2 296 THR 296 448 448 THR THR B . n 
B 2 297 HIS 297 449 449 HIS HIS B . n 
B 2 298 GLY 298 450 ?   ?   ?   B . n 
B 2 299 ALA 299 451 ?   ?   ?   B . n 
B 2 300 GLY 300 452 452 GLY GLY B . n 
B 2 301 TRP 301 453 453 TRP TRP B . n 
B 2 302 GLN 302 454 454 GLN GLN B . n 
B 2 303 LEU 303 455 455 LEU LEU B . n 
B 2 304 PHE 304 456 456 PHE PHE B . n 
B 2 305 CYS 305 457 457 CYS CYS B . n 
B 2 306 ARG 306 458 458 ARG ARG B . n 
B 2 307 THR 307 459 459 THR THR B . n 
B 2 308 VAL 308 460 460 VAL VAL B . n 
B 2 309 TRP 309 461 461 TRP TRP B . n 
B 2 310 SER 310 462 462 SER SER B . n 
B 2 311 ALA 311 463 463 ALA ALA B . n 
B 2 312 HIS 312 464 464 HIS HIS B . n 
B 2 313 SER 313 465 465 SER SER B . n 
B 2 314 GLY 314 466 466 GLY GLY B . n 
B 2 315 PRO 315 467 467 PRO PRO B . n 
B 2 316 THR 316 468 468 THR THR B . n 
B 2 317 ARG 317 469 469 ARG ARG B . n 
B 2 318 MET 318 470 470 MET MET B . n 
B 2 319 ALA 319 471 471 ALA ALA B . n 
B 2 320 THR 320 472 472 THR THR B . n 
B 2 321 ALA 321 473 473 ALA ALA B . n 
B 2 322 ILE 322 474 474 ILE ILE B . n 
B 2 323 ALA 323 475 475 ALA ALA B . n 
B 2 324 ARG 324 476 476 ARG ARG B . n 
B 2 325 CYS 325 477 477 CYS CYS B . n 
B 2 326 ALA 326 478 478 ALA ALA B . n 
B 2 327 PRO 327 479 479 PRO PRO B . n 
B 2 328 ASP 328 480 480 ASP ASP B . n 
B 2 329 GLU 329 481 481 GLU GLU B . n 
B 2 330 GLU 330 482 482 GLU GLU B . n 
B 2 331 LEU 331 483 483 LEU LEU B . n 
B 2 332 LEU 332 484 484 LEU LEU B . n 
B 2 333 SER 333 485 485 SER SER B . n 
B 2 334 CYS 334 486 486 CYS CYS B . n 
B 2 335 SER 335 487 487 SER SER B . n 
B 2 336 SER 336 488 488 SER SER B . n 
B 2 337 PHE 337 489 489 PHE PHE B . n 
B 2 338 SER 338 490 490 SER SER B . n 
B 2 339 ARG 339 491 491 ARG ARG B . n 
B 2 340 SER 340 492 492 SER SER B . n 
B 2 341 GLY 341 493 493 GLY GLY B . n 
B 2 342 LYS 342 494 494 LYS LYS B . n 
B 2 343 ARG 343 495 495 ARG ARG B . n 
B 2 344 ARG 344 496 496 ARG ARG B . n 
B 2 345 GLY 345 497 497 GLY GLY B . n 
B 2 346 GLU 346 498 498 GLU GLU B . n 
B 2 347 ARG 347 499 499 ARG ARG B . n 
B 2 348 MET 348 500 500 MET MET B . n 
B 2 349 GLU 349 501 501 GLU GLU B . n 
B 2 350 ALA 350 502 502 ALA ALA B . n 
B 2 351 GLN 351 503 503 GLN GLN B . n 
B 2 352 GLY 352 504 504 GLY GLY B . n 
B 2 353 GLY 353 505 505 GLY GLY B . n 
B 2 354 LYS 354 506 506 LYS LYS B . n 
B 2 355 LEU 355 507 507 LEU LEU B . n 
B 2 356 VAL 356 508 508 VAL VAL B . n 
B 2 357 CYS 357 509 509 CYS CYS B . n 
B 2 358 ARG 358 510 510 ARG ARG B . n 
B 2 359 ALA 359 511 511 ALA ALA B . n 
B 2 360 HIS 360 512 512 HIS HIS B . n 
B 2 361 ASN 361 513 513 ASN ASN B . n 
B 2 362 ALA 362 514 514 ALA ALA B . n 
B 2 363 PHE 363 515 515 PHE PHE B . n 
B 2 364 GLY 364 516 516 GLY GLY B . n 
B 2 365 GLY 365 517 517 GLY GLY B . n 
B 2 366 GLU 366 518 518 GLU GLU B . n 
B 2 367 GLY 367 519 519 GLY GLY B . n 
B 2 368 VAL 368 520 520 VAL VAL B . n 
B 2 369 TYR 369 521 521 TYR TYR B . n 
B 2 370 ALA 370 522 522 ALA ALA B . n 
B 2 371 ILE 371 523 523 ILE ILE B . n 
B 2 372 ALA 372 524 524 ALA ALA B . n 
B 2 373 ARG 373 525 525 ARG ARG B . n 
B 2 374 CYS 374 526 526 CYS CYS B . n 
B 2 375 CYS 375 527 527 CYS CYS B . n 
B 2 376 LEU 376 528 528 LEU LEU B . n 
B 2 377 LEU 377 529 529 LEU LEU B . n 
B 2 378 PRO 378 530 530 PRO PRO B . n 
B 2 379 GLN 379 531 531 GLN GLN B . n 
B 2 380 ALA 380 532 532 ALA ALA B . n 
B 2 381 ASN 381 533 533 ASN ASN B . n 
B 2 382 CYS 382 534 534 CYS CYS B . n 
B 2 383 SER 383 535 535 SER SER B . n 
B 2 384 VAL 384 536 536 VAL VAL B . n 
B 2 385 HIS 385 537 537 HIS HIS B . n 
B 2 386 THR 386 538 538 THR THR B . n 
B 2 387 ALA 387 539 539 ALA ALA B . n 
B 2 388 PRO 388 540 540 PRO PRO B . n 
B 2 389 PRO 389 541 541 PRO PRO B . n 
B 2 390 ALA 390 542 542 ALA ALA B . n 
B 2 391 GLU 391 543 543 GLU GLU B . n 
B 2 392 ALA 392 544 ?   ?   ?   B . n 
B 2 393 SER 393 545 ?   ?   ?   B . n 
B 2 394 MET 394 546 ?   ?   ?   B . n 
B 2 395 GLY 395 547 547 GLY GLY B . n 
B 2 396 THR 396 548 548 THR THR B . n 
B 2 397 ARG 397 549 549 ARG ARG B . n 
B 2 398 VAL 398 550 550 VAL VAL B . n 
B 2 399 HIS 399 551 551 HIS HIS B . n 
B 2 400 CYS 400 552 552 CYS CYS B . n 
B 2 401 HIS 401 553 553 HIS HIS B . n 
B 2 402 GLN 402 554 ?   ?   ?   B . n 
B 2 403 GLN 403 555 ?   ?   ?   B . n 
B 2 404 GLY 404 556 ?   ?   ?   B . n 
B 2 405 HIS 405 557 557 HIS HIS B . n 
B 2 406 VAL 406 558 558 VAL VAL B . n 
B 2 407 LEU 407 559 559 LEU LEU B . n 
B 2 408 THR 408 560 560 THR THR B . n 
B 2 409 GLY 409 561 561 GLY GLY B . n 
B 2 410 CYS 410 562 562 CYS CYS B . n 
B 2 411 SER 411 563 563 SER SER B . n 
B 2 412 SER 412 564 564 SER SER B . n 
B 2 413 HIS 413 565 565 HIS HIS B . n 
B 2 414 TRP 414 566 566 TRP TRP B . n 
B 2 415 GLU 415 567 567 GLU GLU B . n 
B 2 416 VAL 416 568 568 VAL VAL B . n 
B 2 417 GLU 417 569 569 GLU GLU B . n 
B 2 418 ASP 418 570 570 ASP ASP B . n 
B 2 419 LEU 419 571 571 LEU LEU B . n 
B 2 420 GLY 420 572 ?   ?   ?   B . n 
B 2 421 THR 421 573 ?   ?   ?   B . n 
B 2 422 HIS 422 574 ?   ?   ?   B . n 
B 2 423 LYS 423 575 ?   ?   ?   B . n 
B 2 424 PRO 424 576 ?   ?   ?   B . n 
B 2 425 PRO 425 577 ?   ?   ?   B . n 
B 2 426 VAL 426 578 ?   ?   ?   B . n 
B 2 427 LEU 427 579 ?   ?   ?   B . n 
B 2 428 ARG 428 580 ?   ?   ?   B . n 
B 2 429 PRO 429 581 ?   ?   ?   B . n 
B 2 430 ARG 430 582 ?   ?   ?   B . n 
B 2 431 GLY 431 583 ?   ?   ?   B . n 
B 2 432 GLN 432 584 ?   ?   ?   B . n 
B 2 433 PRO 433 585 585 PRO PRO B . n 
B 2 434 ASN 434 586 586 ASN ASN B . n 
B 2 435 GLN 435 587 587 GLN GLN B . n 
B 2 436 CYS 436 588 588 CYS CYS B . n 
B 2 437 VAL 437 589 589 VAL VAL B . n 
B 2 438 GLY 438 590 590 GLY GLY B . n 
B 2 439 HIS 439 591 591 HIS HIS B . n 
B 2 440 ARG 440 592 592 ARG ARG B . n 
B 2 441 GLU 441 593 593 GLU GLU B . n 
B 2 442 ALA 442 594 594 ALA ALA B . n 
B 2 443 SER 443 595 595 SER SER B . n 
B 2 444 ILE 444 596 596 ILE ILE B . n 
B 2 445 HIS 445 597 597 HIS HIS B . n 
B 2 446 ALA 446 598 598 ALA ALA B . n 
B 2 447 SER 447 599 599 SER SER B . n 
B 2 448 CYS 448 600 600 CYS CYS B . n 
B 2 449 CYS 449 601 601 CYS CYS B . n 
B 2 450 HIS 450 602 602 HIS HIS B . n 
B 2 451 ALA 451 603 603 ALA ALA B . n 
B 2 452 PRO 452 604 604 PRO PRO B . n 
B 2 453 GLY 453 605 605 GLY GLY B . n 
B 2 454 LEU 454 606 606 LEU LEU B . n 
B 2 455 GLU 455 607 607 GLU GLU B . n 
B 2 456 CYS 456 608 608 CYS CYS B . n 
B 2 457 LYS 457 609 609 LYS LYS B . n 
B 2 458 VAL 458 610 610 VAL VAL B . n 
B 2 459 LYS 459 611 611 LYS LYS B . n 
B 2 460 GLU 460 612 612 GLU GLU B . n 
B 2 461 HIS 461 613 613 HIS HIS B . n 
B 2 462 GLY 462 614 614 GLY GLY B . n 
B 2 463 ILE 463 615 615 ILE ILE B . n 
B 2 464 PRO 464 616 616 PRO PRO B . n 
B 2 465 ALA 465 617 ?   ?   ?   B . n 
B 2 466 PRO 466 618 ?   ?   ?   B . n 
B 2 467 GLN 467 619 619 GLN GLN B . n 
B 2 468 GLU 468 620 620 GLU GLU B . n 
B 2 469 GLN 469 621 621 GLN GLN B . n 
B 2 470 VAL 470 622 622 VAL VAL B . n 
B 2 471 THR 471 623 623 THR THR B . n 
B 2 472 VAL 472 624 624 VAL VAL B . n 
B 2 473 ALA 473 625 625 ALA ALA B . n 
B 2 474 CYS 474 626 626 CYS CYS B . n 
B 2 475 GLU 475 627 627 GLU GLU B . n 
B 2 476 GLU 476 628 628 GLU GLU B . n 
B 2 477 GLY 477 629 629 GLY GLY B . n 
B 2 478 TRP 478 630 630 TRP TRP B . n 
B 2 479 THR 479 631 631 THR THR B . n 
B 2 480 LEU 480 632 632 LEU LEU B . n 
B 2 481 THR 481 633 633 THR THR B . n 
B 2 482 GLY 482 634 634 GLY GLY B . n 
B 2 483 CYS 483 635 635 CYS CYS B . n 
B 2 484 SER 484 636 636 SER SER B . n 
B 2 485 ALA 485 637 637 ALA ALA B . n 
B 2 486 LEU 486 638 638 LEU LEU B . n 
B 2 487 PRO 487 639 639 PRO PRO B . n 
B 2 488 GLY 488 640 ?   ?   ?   B . n 
B 2 489 THR 489 641 ?   ?   ?   B . n 
B 2 490 SER 490 642 642 SER SER B . n 
B 2 491 HIS 491 643 643 HIS HIS B . n 
B 2 492 VAL 492 644 644 VAL VAL B . n 
B 2 493 LEU 493 645 645 LEU LEU B . n 
B 2 494 GLY 494 646 646 GLY GLY B . n 
B 2 495 ALA 495 647 647 ALA ALA B . n 
B 2 496 TYR 496 648 648 TYR TYR B . n 
B 2 497 ALA 497 649 649 ALA ALA B . n 
B 2 498 VAL 498 650 650 VAL VAL B . n 
B 2 499 ASP 499 651 651 ASP ASP B . n 
B 2 500 ASN 500 652 652 ASN ASN B . n 
B 2 501 THR 501 653 653 THR THR B . n 
B 2 502 CYS 502 654 654 CYS CYS B . n 
B 2 503 VAL 503 655 655 VAL VAL B . n 
B 2 504 VAL 504 656 656 VAL VAL B . n 
B 2 505 ARG 505 657 657 ARG ARG B . n 
B 2 506 SER 506 658 658 SER SER B . n 
B 2 507 ARG 507 659 659 ARG ARG B . n 
B 2 508 ASP 508 660 ?   ?   ?   B . n 
B 2 509 VAL 509 661 ?   ?   ?   B . n 
B 2 510 SER 510 662 ?   ?   ?   B . n 
B 2 511 THR 511 663 ?   ?   ?   B . n 
B 2 512 THR 512 664 ?   ?   ?   B . n 
B 2 513 GLY 513 665 ?   ?   ?   B . n 
B 2 514 SER 514 666 ?   ?   ?   B . n 
B 2 515 THR 515 667 ?   ?   ?   B . n 
B 2 516 SER 516 668 ?   ?   ?   B . n 
B 2 517 GLU 517 669 ?   ?   ?   B . n 
B 2 518 GLY 518 670 ?   ?   ?   B . n 
B 2 519 ALA 519 671 671 ALA ALA B . n 
B 2 520 VAL 520 672 672 VAL VAL B . n 
B 2 521 THR 521 673 673 THR THR B . n 
B 2 522 ALA 522 674 674 ALA ALA B . n 
B 2 523 VAL 523 675 675 VAL VAL B . n 
B 2 524 ALA 524 676 676 ALA ALA B . n 
B 2 525 ILE 525 677 677 ILE ILE B . n 
B 2 526 CYS 526 678 678 CYS CYS B . n 
B 2 527 CYS 527 679 679 CYS CYS B . n 
B 2 528 ARG 528 680 680 ARG ARG B . n 
B 2 529 SER 529 681 681 SER SER B . n 
C 3 1   YBX 1   1   1   YBX LI1 L . n 
C 3 2   PHE 2   2   1   PHE LI1 L . n 
C 3 3   VAL 3   3   1   VAL LI1 L . n 
C 3 4   GLY 4   4   1   GLY LI1 L . n 
C 3 5   THR 5   5   1   THR LI1 L . n 
C 3 6   THR 6   6   1   THR LI1 L . n 
C 3 7   PHA 7   7   1   PHA LI1 L . n 
C 3 8   MAA 8   8   1   MAA LI1 L . n 
C 3 9   BIF 9   9   1   BIF LI1 L . n 
C 3 10  EME 10  10  1   EME LI1 L . n 
C 3 11  NEH 11  11  1   NEH LI1 L . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 EME ? ? EME ? ? 'SUBJECT OF INVESTIGATION' ? 
2 PHA ? ? PHA ? ? 'SUBJECT OF INVESTIGATION' ? 
3 YBX ? ? YBX ? ? 'SUBJECT OF INVESTIGATION' ? 
4 MAA ? ? MAA ? ? 'SUBJECT OF INVESTIGATION' ? 
5 BIF ? ? BIF ? ? 'SUBJECT OF INVESTIGATION' ? 
6 NEH ? ? NEH ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 4 HOH 1   201 255 HOH HOH A . 
D 4 HOH 2   202 250 HOH HOH A . 
D 4 HOH 3   203 89  HOH HOH A . 
D 4 HOH 4   204 183 HOH HOH A . 
D 4 HOH 5   205 175 HOH HOH A . 
D 4 HOH 6   206 30  HOH HOH A . 
D 4 HOH 7   207 84  HOH HOH A . 
D 4 HOH 8   208 224 HOH HOH A . 
D 4 HOH 9   209 70  HOH HOH A . 
D 4 HOH 10  210 45  HOH HOH A . 
D 4 HOH 11  211 119 HOH HOH A . 
D 4 HOH 12  212 16  HOH HOH A . 
D 4 HOH 13  213 22  HOH HOH A . 
D 4 HOH 14  214 62  HOH HOH A . 
D 4 HOH 15  215 65  HOH HOH A . 
D 4 HOH 16  216 5   HOH HOH A . 
D 4 HOH 17  217 215 HOH HOH A . 
D 4 HOH 18  218 91  HOH HOH A . 
D 4 HOH 19  219 210 HOH HOH A . 
D 4 HOH 20  220 194 HOH HOH A . 
D 4 HOH 21  221 34  HOH HOH A . 
D 4 HOH 22  222 88  HOH HOH A . 
D 4 HOH 23  223 209 HOH HOH A . 
D 4 HOH 24  224 92  HOH HOH A . 
D 4 HOH 25  225 36  HOH HOH A . 
D 4 HOH 26  226 100 HOH HOH A . 
D 4 HOH 27  227 200 HOH HOH A . 
D 4 HOH 28  228 173 HOH HOH A . 
D 4 HOH 29  229 254 HOH HOH A . 
D 4 HOH 30  230 106 HOH HOH A . 
D 4 HOH 31  231 161 HOH HOH A . 
D 4 HOH 32  232 54  HOH HOH A . 
D 4 HOH 33  233 212 HOH HOH A . 
D 4 HOH 34  234 139 HOH HOH A . 
D 4 HOH 35  235 241 HOH HOH A . 
D 4 HOH 36  236 153 HOH HOH A . 
D 4 HOH 37  237 137 HOH HOH A . 
D 4 HOH 38  238 157 HOH HOH A . 
D 4 HOH 39  239 26  HOH HOH A . 
D 4 HOH 40  240 176 HOH HOH A . 
D 4 HOH 41  241 110 HOH HOH A . 
D 4 HOH 42  242 47  HOH HOH A . 
D 4 HOH 43  243 46  HOH HOH A . 
D 4 HOH 44  244 201 HOH HOH A . 
D 4 HOH 45  245 48  HOH HOH A . 
D 4 HOH 46  246 185 HOH HOH A . 
D 4 HOH 47  247 3   HOH HOH A . 
D 4 HOH 48  248 249 HOH HOH A . 
D 4 HOH 49  249 240 HOH HOH A . 
D 4 HOH 50  250 243 HOH HOH A . 
D 4 HOH 51  251 152 HOH HOH A . 
D 4 HOH 52  252 253 HOH HOH A . 
D 4 HOH 53  253 248 HOH HOH A . 
D 4 HOH 54  254 198 HOH HOH A . 
E 4 HOH 1   701 158 HOH HOH B . 
E 4 HOH 2   702 230 HOH HOH B . 
E 4 HOH 3   703 237 HOH HOH B . 
E 4 HOH 4   704 232 HOH HOH B . 
E 4 HOH 5   705 69  HOH HOH B . 
E 4 HOH 6   706 234 HOH HOH B . 
E 4 HOH 7   707 186 HOH HOH B . 
E 4 HOH 8   708 233 HOH HOH B . 
E 4 HOH 9   709 25  HOH HOH B . 
E 4 HOH 10  710 102 HOH HOH B . 
E 4 HOH 11  711 191 HOH HOH B . 
E 4 HOH 12  712 17  HOH HOH B . 
E 4 HOH 13  713 192 HOH HOH B . 
E 4 HOH 14  714 222 HOH HOH B . 
E 4 HOH 15  715 75  HOH HOH B . 
E 4 HOH 16  716 228 HOH HOH B . 
E 4 HOH 17  717 227 HOH HOH B . 
E 4 HOH 18  718 109 HOH HOH B . 
E 4 HOH 19  719 37  HOH HOH B . 
E 4 HOH 20  720 220 HOH HOH B . 
E 4 HOH 21  721 138 HOH HOH B . 
E 4 HOH 22  722 29  HOH HOH B . 
E 4 HOH 23  723 67  HOH HOH B . 
E 4 HOH 24  724 74  HOH HOH B . 
E 4 HOH 25  725 184 HOH HOH B . 
E 4 HOH 26  726 238 HOH HOH B . 
E 4 HOH 27  727 144 HOH HOH B . 
E 4 HOH 28  728 33  HOH HOH B . 
E 4 HOH 29  729 189 HOH HOH B . 
E 4 HOH 30  730 252 HOH HOH B . 
E 4 HOH 31  731 27  HOH HOH B . 
E 4 HOH 32  732 118 HOH HOH B . 
E 4 HOH 33  733 44  HOH HOH B . 
E 4 HOH 34  734 213 HOH HOH B . 
E 4 HOH 35  735 257 HOH HOH B . 
E 4 HOH 36  736 136 HOH HOH B . 
E 4 HOH 37  737 23  HOH HOH B . 
E 4 HOH 38  738 11  HOH HOH B . 
E 4 HOH 39  739 146 HOH HOH B . 
E 4 HOH 40  740 15  HOH HOH B . 
E 4 HOH 41  741 206 HOH HOH B . 
E 4 HOH 42  742 56  HOH HOH B . 
E 4 HOH 43  743 63  HOH HOH B . 
E 4 HOH 44  744 66  HOH HOH B . 
E 4 HOH 45  745 9   HOH HOH B . 
E 4 HOH 46  746 113 HOH HOH B . 
E 4 HOH 47  747 58  HOH HOH B . 
E 4 HOH 48  748 195 HOH HOH B . 
E 4 HOH 49  749 2   HOH HOH B . 
E 4 HOH 50  750 165 HOH HOH B . 
E 4 HOH 51  751 85  HOH HOH B . 
E 4 HOH 52  752 43  HOH HOH B . 
E 4 HOH 53  753 55  HOH HOH B . 
E 4 HOH 54  754 114 HOH HOH B . 
E 4 HOH 55  755 111 HOH HOH B . 
E 4 HOH 56  756 128 HOH HOH B . 
E 4 HOH 57  757 142 HOH HOH B . 
E 4 HOH 58  758 19  HOH HOH B . 
E 4 HOH 59  759 96  HOH HOH B . 
E 4 HOH 60  760 120 HOH HOH B . 
E 4 HOH 61  761 104 HOH HOH B . 
E 4 HOH 62  762 90  HOH HOH B . 
E 4 HOH 63  763 79  HOH HOH B . 
E 4 HOH 64  764 10  HOH HOH B . 
E 4 HOH 65  765 1   HOH HOH B . 
E 4 HOH 66  766 21  HOH HOH B . 
E 4 HOH 67  767 32  HOH HOH B . 
E 4 HOH 68  768 150 HOH HOH B . 
E 4 HOH 69  769 40  HOH HOH B . 
E 4 HOH 70  770 28  HOH HOH B . 
E 4 HOH 71  771 77  HOH HOH B . 
E 4 HOH 72  772 82  HOH HOH B . 
E 4 HOH 73  773 107 HOH HOH B . 
E 4 HOH 74  774 112 HOH HOH B . 
E 4 HOH 75  775 24  HOH HOH B . 
E 4 HOH 76  776 103 HOH HOH B . 
E 4 HOH 77  777 127 HOH HOH B . 
E 4 HOH 78  778 18  HOH HOH B . 
E 4 HOH 79  779 221 HOH HOH B . 
E 4 HOH 80  780 168 HOH HOH B . 
E 4 HOH 81  781 134 HOH HOH B . 
E 4 HOH 82  782 31  HOH HOH B . 
E 4 HOH 83  783 178 HOH HOH B . 
E 4 HOH 84  784 251 HOH HOH B . 
E 4 HOH 85  785 64  HOH HOH B . 
E 4 HOH 86  786 42  HOH HOH B . 
E 4 HOH 87  787 124 HOH HOH B . 
E 4 HOH 88  788 143 HOH HOH B . 
E 4 HOH 89  789 117 HOH HOH B . 
E 4 HOH 90  790 72  HOH HOH B . 
E 4 HOH 91  791 59  HOH HOH B . 
E 4 HOH 92  792 129 HOH HOH B . 
E 4 HOH 93  793 132 HOH HOH B . 
E 4 HOH 94  794 41  HOH HOH B . 
E 4 HOH 95  795 130 HOH HOH B . 
E 4 HOH 96  796 13  HOH HOH B . 
E 4 HOH 97  797 38  HOH HOH B . 
E 4 HOH 98  798 12  HOH HOH B . 
E 4 HOH 99  799 99  HOH HOH B . 
E 4 HOH 100 800 87  HOH HOH B . 
E 4 HOH 101 801 35  HOH HOH B . 
E 4 HOH 102 802 116 HOH HOH B . 
E 4 HOH 103 803 190 HOH HOH B . 
E 4 HOH 104 804 174 HOH HOH B . 
E 4 HOH 105 805 171 HOH HOH B . 
E 4 HOH 106 806 154 HOH HOH B . 
E 4 HOH 107 807 149 HOH HOH B . 
E 4 HOH 108 808 51  HOH HOH B . 
E 4 HOH 109 809 20  HOH HOH B . 
E 4 HOH 110 810 159 HOH HOH B . 
E 4 HOH 111 811 131 HOH HOH B . 
E 4 HOH 112 812 93  HOH HOH B . 
E 4 HOH 113 813 160 HOH HOH B . 
E 4 HOH 114 814 52  HOH HOH B . 
E 4 HOH 115 815 177 HOH HOH B . 
E 4 HOH 116 816 181 HOH HOH B . 
E 4 HOH 117 817 108 HOH HOH B . 
E 4 HOH 118 818 14  HOH HOH B . 
E 4 HOH 119 819 122 HOH HOH B . 
E 4 HOH 120 820 8   HOH HOH B . 
E 4 HOH 121 821 7   HOH HOH B . 
E 4 HOH 122 822 214 HOH HOH B . 
E 4 HOH 123 823 50  HOH HOH B . 
E 4 HOH 124 824 60  HOH HOH B . 
E 4 HOH 125 825 94  HOH HOH B . 
E 4 HOH 126 826 187 HOH HOH B . 
E 4 HOH 127 827 197 HOH HOH B . 
E 4 HOH 128 828 80  HOH HOH B . 
E 4 HOH 129 829 83  HOH HOH B . 
E 4 HOH 130 830 216 HOH HOH B . 
E 4 HOH 131 831 86  HOH HOH B . 
E 4 HOH 132 832 196 HOH HOH B . 
E 4 HOH 133 833 135 HOH HOH B . 
E 4 HOH 134 834 121 HOH HOH B . 
E 4 HOH 135 835 4   HOH HOH B . 
E 4 HOH 136 836 39  HOH HOH B . 
E 4 HOH 137 837 218 HOH HOH B . 
E 4 HOH 138 838 71  HOH HOH B . 
E 4 HOH 139 839 226 HOH HOH B . 
E 4 HOH 140 840 166 HOH HOH B . 
E 4 HOH 141 841 6   HOH HOH B . 
E 4 HOH 142 842 78  HOH HOH B . 
E 4 HOH 143 843 57  HOH HOH B . 
E 4 HOH 144 844 49  HOH HOH B . 
E 4 HOH 145 845 199 HOH HOH B . 
E 4 HOH 146 846 141 HOH HOH B . 
E 4 HOH 147 847 105 HOH HOH B . 
E 4 HOH 148 848 76  HOH HOH B . 
E 4 HOH 149 849 148 HOH HOH B . 
E 4 HOH 150 850 207 HOH HOH B . 
E 4 HOH 151 851 98  HOH HOH B . 
E 4 HOH 152 852 239 HOH HOH B . 
E 4 HOH 153 853 180 HOH HOH B . 
E 4 HOH 154 854 95  HOH HOH B . 
E 4 HOH 155 855 155 HOH HOH B . 
E 4 HOH 156 856 81  HOH HOH B . 
E 4 HOH 157 857 53  HOH HOH B . 
E 4 HOH 158 858 169 HOH HOH B . 
E 4 HOH 159 859 231 HOH HOH B . 
E 4 HOH 160 860 170 HOH HOH B . 
E 4 HOH 161 861 202 HOH HOH B . 
E 4 HOH 162 862 204 HOH HOH B . 
E 4 HOH 163 863 115 HOH HOH B . 
E 4 HOH 164 864 163 HOH HOH B . 
E 4 HOH 165 865 179 HOH HOH B . 
E 4 HOH 166 866 245 HOH HOH B . 
E 4 HOH 167 867 151 HOH HOH B . 
E 4 HOH 168 868 147 HOH HOH B . 
E 4 HOH 169 869 182 HOH HOH B . 
E 4 HOH 170 870 235 HOH HOH B . 
E 4 HOH 171 871 223 HOH HOH B . 
E 4 HOH 172 872 97  HOH HOH B . 
E 4 HOH 173 873 101 HOH HOH B . 
E 4 HOH 174 874 133 HOH HOH B . 
E 4 HOH 175 875 203 HOH HOH B . 
E 4 HOH 176 876 188 HOH HOH B . 
E 4 HOH 177 877 236 HOH HOH B . 
E 4 HOH 178 878 219 HOH HOH B . 
E 4 HOH 179 879 217 HOH HOH B . 
E 4 HOH 180 880 193 HOH HOH B . 
E 4 HOH 181 881 205 HOH HOH B . 
E 4 HOH 182 882 258 HOH HOH B . 
E 4 HOH 183 883 172 HOH HOH B . 
E 4 HOH 184 884 225 HOH HOH B . 
E 4 HOH 185 885 229 HOH HOH B . 
E 4 HOH 186 886 156 HOH HOH B . 
E 4 HOH 187 887 211 HOH HOH B . 
E 4 HOH 188 888 244 HOH HOH B . 
E 4 HOH 189 889 256 HOH HOH B . 
E 4 HOH 190 890 167 HOH HOH B . 
E 4 HOH 191 891 246 HOH HOH B . 
E 4 HOH 192 892 242 HOH HOH B . 
E 4 HOH 193 893 123 HOH HOH B . 
E 4 HOH 194 894 208 HOH HOH B . 
E 4 HOH 195 895 164 HOH HOH B . 
E 4 HOH 196 896 247 HOH HOH B . 
F 4 HOH 1   101 125 HOH HOH L . 
F 4 HOH 2   102 126 HOH HOH L . 
F 4 HOH 3   103 68  HOH HOH L . 
F 4 HOH 4   104 61  HOH HOH L . 
F 4 HOH 5   105 145 HOH HOH L . 
F 4 HOH 6   106 140 HOH HOH L . 
F 4 HOH 7   107 73  HOH HOH L . 
F 4 HOH 8   108 162 HOH HOH L . 
# 
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  ? ? ? 1.8_1069 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                     8VDV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     63.086 
_cell.length_a_esd                 ? 
_cell.length_b                     70.846 
_cell.length_b_esd                 ? 
_cell.length_c                     149.007 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8VDV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8VDV 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.89 
_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          EVAPORATION 
_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    '20.0% Peg-6000, 0.1M Tris pH8.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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 R 1M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-11-14 
_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   1 
_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                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8VDV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.972 
_reflns.d_resolution_low                               149.007 
_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                                     47937 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.094 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       307800 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.087 
_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                                    1.972 
_reflns_shell.d_res_low                                     1.978 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           3285 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             496 
_reflns_shell.percent_possible_obs                          100.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.6 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.8 
_reflns_shell.pdbx_Rrim_I_all                               0.685 
_reflns_shell.pdbx_Rpim_I_all                               0.264 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_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                                  0.631 
_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                                 8VDV 
_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                            1.972 
_refine.ls_d_res_low                             58.094 
_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                     47859 
_refine.ls_number_reflns_R_free                  2426 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1872 
_refine.ls_R_factor_R_free                       0.2168 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1857 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.38 
_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                            0.18 
_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                       1.972 
_refine_hist.d_res_low                        58.094 
_refine_hist.number_atoms_solvent             258 
_refine_hist.number_atoms_total               4633 
_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        4286 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         89 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  ? 4476 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.520  ? 6056 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.338 ? 1609 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.091  ? 695  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 787  ? 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' 1.972  2.0117 . . 171 2607 100.00 . . . . 0.2206 . . . . . . . . . . . 0.2912 
'X-RAY DIFFRACTION' 2.0117 2.0555 . . 144 2611 100.00 . . . . 0.2125 . . . . . . . . . . . 0.2499 
'X-RAY DIFFRACTION' 2.0555 2.1033 . . 155 2642 100.00 . . . . 0.2029 . . . . . . . . . . . 0.2266 
'X-RAY DIFFRACTION' 2.1033 2.1559 . . 141 2642 100.00 . . . . 0.1912 . . . . . . . . . . . 0.2289 
'X-RAY DIFFRACTION' 2.1559 2.2142 . . 141 2627 100.00 . . . . 0.1885 . . . . . . . . . . . 0.2499 
'X-RAY DIFFRACTION' 2.2142 2.2794 . . 135 2650 100.00 . . . . 0.1979 . . . . . . . . . . . 0.2372 
'X-RAY DIFFRACTION' 2.2794 2.3529 . . 146 2633 100.00 . . . . 0.1900 . . . . . . . . . . . 0.2506 
'X-RAY DIFFRACTION' 2.3529 2.4370 . . 145 2663 100.00 . . . . 0.1874 . . . . . . . . . . . 0.2374 
'X-RAY DIFFRACTION' 2.4370 2.5346 . . 131 2661 100.00 . . . . 0.1917 . . . . . . . . . . . 0.1989 
'X-RAY DIFFRACTION' 2.5346 2.6500 . . 136 2648 100.00 . . . . 0.2029 . . . . . . . . . . . 0.2251 
'X-RAY DIFFRACTION' 2.6500 2.7897 . . 143 2673 100.00 . . . . 0.1986 . . . . . . . . . . . 0.2481 
'X-RAY DIFFRACTION' 2.7897 2.9644 . . 134 2678 100.00 . . . . 0.1874 . . . . . . . . . . . 0.2124 
'X-RAY DIFFRACTION' 2.9644 3.1933 . . 140 2661 100.00 . . . . 0.1905 . . . . . . . . . . . 0.2036 
'X-RAY DIFFRACTION' 3.1933 3.5146 . . 134 2733 100.00 . . . . 0.1807 . . . . . . . . . . . 0.1844 
'X-RAY DIFFRACTION' 3.5146 4.0231 . . 149 2685 100.00 . . . . 0.1698 . . . . . . . . . . . 0.2113 
'X-RAY DIFFRACTION' 4.0231 5.0682 . . 139 2740 99.00  . . . . 0.1597 . . . . . . . . . . . 0.1772 
'X-RAY DIFFRACTION' 5.0682 58.094 . . 142 2879 100.00 . . . . 0.1941 . . . . . . . . . . . 0.2310 
# 
_struct.entry_id                     8VDV 
_struct.title                        'pcsk9 in complex with inhibitor' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8VDV 
_struct_keywords.text            'cyclic peptide, HYDROLASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   HYDROLASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
# 
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 PCSK9_HUMAN Q8NBP7 ? 1 
;TATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHV
DYIEEDSSVFAQ
;
61 
2 UNP PCSK9_HUMAN Q8NBP7 ? 2 
;SIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAG
VVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLV
TAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHV
AGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMAT
AVARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAEASMGTRVHC
HQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVTVACEEGWTL
TGCSALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEGAVTAVAICCRS
;
0  
3 PDB 8VDV        8VDV   ? 3 ? 1  
# 
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 8VDV A 1 ? 92  ? Q8NBP7 61  ? 152 ? 61  152 
2 2 8VDV B 1 ? 529 ? Q8NBP7 153 ? 681 ? 153 681 
3 3 8VDV L 1 ? 11  ? 8VDV   1   ? 11  ? 1   11  
# 
_struct_ref_seq_dif.align_id                     2 
_struct_ref_seq_dif.pdbx_pdb_id_code             8VDV 
_struct_ref_seq_dif.mon_id                       ILE 
_struct_ref_seq_dif.pdbx_pdb_strand_id           B 
_struct_ref_seq_dif.seq_num                      322 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   Q8NBP7 
_struct_ref_seq_dif.db_mon_id                    VAL 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          474 
_struct_ref_seq_dif.details                      conflict 
_struct_ref_seq_dif.pdbx_auth_seq_num            474 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_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   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
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)' 4590  ? 
1 MORE         -25   ? 
1 'SSA (A^2)'  23550 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 LYS A 9   ? PRO A 11  ? LYS A 69  PRO A 71  5 ? 3  
HELX_P HELX_P2  AA2 HIS A 27  ? ARG A 44  ? HIS A 87  ARG A 104 1 ? 18 
HELX_P HELX_P3  AA3 SER A 67  ? ASP A 69  ? SER A 127 ASP A 129 5 ? 3  
HELX_P HELX_P4  AA4 LEU A 70  ? LYS A 76  ? LEU A 130 LYS A 136 1 ? 7  
HELX_P HELX_P5  AA5 PRO B 3   ? ILE B 9   ? PRO B 155 ILE B 161 1 ? 7  
HELX_P HELX_P6  AA6 ASP B 72  ? GLY B 84  ? ASP B 224 GLY B 236 1 ? 13 
HELX_P HELX_P7  AA7 VAL B 109 ? GLN B 126 ? VAL B 261 GLN B 278 1 ? 18 
HELX_P HELX_P8  AA8 SER B 142 ? ALA B 155 ? SER B 294 ALA B 307 1 ? 14 
HELX_P HELX_P9  AA9 ASP B 169 ? CYS B 171 ? ASP B 321 CYS B 323 5 ? 3  
HELX_P HELX_P10 AB1 GLY B 232 ? GLU B 251 ? GLY B 384 GLU B 403 1 ? 20 
HELX_P HELX_P11 AB2 THR B 255 ? PHE B 266 ? THR B 407 PHE B 418 1 ? 12 
HELX_P HELX_P12 AB3 ASN B 273 ? PHE B 277 ? ASN B 425 PHE B 429 5 ? 5  
HELX_P HELX_P13 AB4 PRO B 278 ? ARG B 282 ? PRO B 430 ARG B 434 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? B CYS 71  SG ? ? ? 1_555 B CYS 103 SG ? ? B CYS 223 B CYS 255 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
disulf2  disulf ?    ? B CYS 171 SG ? ? ? 1_555 B CYS 206 SG ? ? B CYS 323 B CYS 358 1_555 ? ? ? ? ? ? ? 2.080 ? ? 
disulf3  disulf ?    ? B CYS 223 SG ? ? ? 1_555 B CYS 226 SG ? ? B CYS 375 B CYS 378 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf4  disulf ?    ? B CYS 305 SG ? ? ? 1_555 B CYS 375 SG ? ? B CYS 457 B CYS 527 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
disulf5  disulf ?    ? B CYS 325 SG ? ? ? 1_555 B CYS 374 SG ? ? B CYS 477 B CYS 526 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf6  disulf ?    ? B CYS 334 SG ? ? ? 1_555 B CYS 357 SG ? ? B CYS 486 B CYS 509 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
disulf7  disulf ?    ? B CYS 382 SG ? ? ? 1_555 B CYS 449 SG ? ? B CYS 534 B CYS 601 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
disulf8  disulf ?    ? B CYS 400 SG ? ? ? 1_555 B CYS 448 SG ? ? B CYS 552 B CYS 600 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf9  disulf ?    ? B CYS 410 SG ? ? ? 1_555 B CYS 436 SG ? ? B CYS 562 B CYS 588 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf10 disulf ?    ? B CYS 456 SG ? ? ? 1_555 B CYS 527 SG ? ? B CYS 608 B CYS 679 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf11 disulf ?    ? B CYS 474 SG ? ? ? 1_555 B CYS 526 SG ? ? B CYS 626 B CYS 678 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf12 disulf ?    ? B CYS 483 SG ? ? ? 1_555 B CYS 502 SG ? ? B CYS 635 B CYS 654 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
covale1  covale both ? C YBX 1   C5 ? ? ? 1_555 C PHE 2   N  ? ? L YBX 1   L PHE 2   1_555 ? ? ? ? ? ? ? 1.337 ? ? 
covale2  covale none ? C GLY 4   CA ? ? ? 1_555 C NEH 11  CB ? ? L GLY 4   L NEH 11  1_555 ? ? ? ? ? ? ? 1.537 ? ? 
covale3  covale both ? C THR 6   C  ? ? ? 1_555 C PHA 7   N  ? ? L THR 6   L PHA 7   1_555 ? ? ? ? ? ? ? 1.325 ? ? 
covale4  covale both ? C PHA 7   C  ? ? ? 1_555 C MAA 8   N  ? ? L PHA 7   L MAA 8   1_555 ? ? ? ? ? ? ? 1.353 ? ? 
covale5  covale both ? C MAA 8   C  ? ? ? 1_555 C BIF 9   N  ? ? L MAA 8   L BIF 9   1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale6  covale both ? C BIF 9   C  ? ? ? 1_555 C EME 10  N  ? ? L BIF 9   L EME 10  1_555 ? ? ? ? ? ? ? 1.348 ? ? 
covale7  covale both ? C EME 10  C  ? ? ? 1_555 C NEH 11  N  ? ? L EME 10  L NEH 11  1_555 ? ? ? ? ? ? ? 1.323 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  PHA C 7   ? .   . .   . PHA L 7   ? 1_555 .   . .   . .     .  .  PHE 1 PHA Dehydroxylation 'Named protein modification' 
2  MAA C 8   ? .   . .   . MAA L 8   ? 1_555 .   . .   . .     .  .  ALA 1 MAA Methylation     'Named protein modification' 
3  EME C 10  ? .   . .   . EME L 10  ? 1_555 .   . .   . .     .  .  GLU 1 EME Methylation     'Named protein modification' 
4  YBX C 1   ? .   . .   . YBX L 1   ? 1_555 .   . .   . .     .  .  ?   1 YBX None            'Non-standard residue'       
5  BIF C 9   ? .   . .   . BIF L 9   ? 1_555 .   . .   . .     .  .  ?   1 BIF None            'Non-standard residue'       
6  NEH C 11  ? .   . .   . NEH L 11  ? 1_555 .   . .   . .     .  .  ?   1 NEH None            'Non-standard residue'       
7  CYS B 71  ? CYS B 103 ? CYS B 223 ? 1_555 CYS B 255 ? 1_555 SG SG .   . .   None            'Disulfide bridge'           
8  CYS B 171 ? CYS B 206 ? CYS B 323 ? 1_555 CYS B 358 ? 1_555 SG SG .   . .   None            'Disulfide bridge'           
9  CYS B 223 ? CYS B 226 ? CYS B 375 ? 1_555 CYS B 378 ? 1_555 SG SG .   . .   None            'Disulfide bridge'           
10 CYS B 305 ? CYS B 375 ? CYS B 457 ? 1_555 CYS B 527 ? 1_555 SG SG .   . .   None            'Disulfide bridge'           
11 CYS B 325 ? CYS B 374 ? CYS B 477 ? 1_555 CYS B 526 ? 1_555 SG SG .   . .   None            'Disulfide bridge'           
12 CYS B 334 ? CYS B 357 ? CYS B 486 ? 1_555 CYS B 509 ? 1_555 SG SG .   . .   None            'Disulfide bridge'           
13 CYS B 382 ? CYS B 449 ? CYS B 534 ? 1_555 CYS B 601 ? 1_555 SG SG .   . .   None            'Disulfide bridge'           
14 CYS B 400 ? CYS B 448 ? CYS B 552 ? 1_555 CYS B 600 ? 1_555 SG SG .   . .   None            'Disulfide bridge'           
15 CYS B 410 ? CYS B 436 ? CYS B 562 ? 1_555 CYS B 588 ? 1_555 SG SG .   . .   None            'Disulfide bridge'           
16 CYS B 456 ? CYS B 527 ? CYS B 608 ? 1_555 CYS B 679 ? 1_555 SG SG .   . .   None            'Disulfide bridge'           
17 CYS B 474 ? CYS B 526 ? CYS B 626 ? 1_555 CYS B 678 ? 1_555 SG SG .   . .   None            'Disulfide bridge'           
18 CYS B 483 ? CYS B 502 ? CYS B 635 ? 1_555 CYS B 654 ? 1_555 SG SG .   . .   None            'Disulfide bridge'           
19 GLY C 4   ? NEH C 11  ? GLY L 4   ? 1_555 NEH L 11  ? 1_555 CA CB .   . .   None            'Non-standard linkage'       
# 
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 SER 174 B . ? SER 326 B PRO 175 B ? PRO 327 B 1 -0.58 
2 PHA 7   C . ? PHA 7   L MAA 8   C ? MAA 8   L 1 4.66  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 6 ? 
AA3 ? 7 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 3 ? 
AA8 ? 3 ? 
AA9 ? 3 ? 
AB1 ? 2 ? 
AB2 ? 3 ? 
AB3 ? 3 ? 
# 
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 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? 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 THR A 3   ? HIS A 5   ? THR A 63  HIS A 65  
AA1 2 VAL A 80  ? ALA A 91  ? VAL A 140 ALA A 151 
AA1 3 LYS B 106 ? THR B 108 ? LYS B 258 THR B 260 
AA2 1 LYS A 50  ? PHE A 55  ? LYS A 110 PHE A 115 
AA2 2 GLY A 61  ? LYS A 65  ? GLY A 121 LYS A 125 
AA2 3 ARG A 13  ? LEU A 22  ? ARG A 73  LEU A 82  
AA2 4 VAL A 80  ? ALA A 91  ? VAL A 140 ALA A 151 
AA2 5 LEU B 137 ? GLY B 140 ? LEU B 289 GLY B 292 
AA2 6 TYR B 173 ? SER B 174 ? TYR B 325 SER B 326 
AA3 1 VAL B 48  ? GLU B 54  ? VAL B 200 GLU B 206 
AA3 2 SER B 94  ? ARG B 99  ? SER B 246 ARG B 251 
AA3 3 GLU B 29  ? ASP B 34  ? GLU B 181 ASP B 186 
AA3 4 LEU B 131 ? LEU B 135 ? LEU B 283 LEU B 287 
AA3 5 VAL B 158 ? ALA B 162 ? VAL B 310 ALA B 314 
AA3 6 ILE B 182 ? THR B 187 ? ILE B 334 THR B 339 
AA3 7 LEU B 209 ? PRO B 212 ? LEU B 361 PRO B 364 
AA4 1 THR B 195 ? LEU B 196 ? THR B 347 LEU B 348 
AA4 2 LEU B 199 ? GLY B 200 ? LEU B 351 GLY B 352 
AA5 1 ILE B 216 ? ALA B 219 ? ILE B 368 ALA B 371 
AA5 2 PHE B 227 ? GLN B 230 ? PHE B 379 GLN B 382 
AA6 1 ALA B 268 ? LYS B 269 ? ALA B 420 LYS B 421 
AA6 2 LEU B 288 ? VAL B 289 ? LEU B 440 VAL B 441 
AA7 1 PHE B 304 ? TRP B 309 ? PHE B 456 TRP B 461 
AA7 2 TYR B 369 ? LEU B 376 ? TYR B 521 LEU B 528 
AA7 3 GLU B 330 ? PHE B 337 ? GLU B 482 PHE B 489 
AA8 1 THR B 320 ? ALA B 323 ? THR B 472 ALA B 475 
AA8 2 LYS B 354 ? ASN B 361 ? LYS B 506 ASN B 513 
AA8 3 ARG B 343 ? GLN B 351 ? ARG B 495 GLN B 503 
AA9 1 ASN B 381 ? ALA B 387 ? ASN B 533 ALA B 539 
AA9 2 SER B 443 ? HIS B 450 ? SER B 595 HIS B 602 
AA9 3 VAL B 406 ? HIS B 413 ? VAL B 558 HIS B 565 
AB1 1 THR B 396 ? HIS B 399 ? THR B 548 HIS B 551 
AB1 2 GLN B 435 ? GLY B 438 ? GLN B 587 GLY B 590 
AB2 1 GLU B 455 ? ILE B 463 ? GLU B 607 ILE B 615 
AB2 2 VAL B 520 ? ARG B 528 ? VAL B 672 ARG B 680 
AB2 3 THR B 479 ? ALA B 485 ? THR B 631 ALA B 637 
AB3 1 GLN B 469 ? ALA B 473 ? GLN B 621 ALA B 625 
AB3 2 THR B 501 ? SER B 506 ? THR B 653 SER B 658 
AB3 3 VAL B 492 ? VAL B 498 ? VAL B 644 VAL B 650 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N HIS A 5   ? N HIS A 65  O GLU A 85  ? O GLU A 145 
AA1 2 3 N VAL A 89  ? N VAL A 149 O GLY B 107 ? O GLY B 259 
AA2 1 2 N LYS A 50  ? N LYS A 110 O LYS A 65  ? O LYS A 125 
AA2 2 3 O PHE A 62  ? O PHE A 122 N VAL A 20  ? N VAL A 80  
AA2 3 4 N VAL A 21  ? N VAL A 81  O ASP A 81  ? O ASP A 141 
AA2 4 5 N PHE A 90  ? N PHE A 150 O ALA B 138 ? O ALA B 290 
AA2 5 6 N GLY B 139 ? N GLY B 291 O SER B 174 ? O SER B 326 
AA3 1 2 N MET B 49  ? N MET B 201 O MET B 95  ? O MET B 247 
AA3 2 3 O LEU B 98  ? O LEU B 250 N LEU B 32  ? N LEU B 184 
AA3 3 4 N TYR B 31  ? N TYR B 183 O VAL B 132 ? O VAL B 284 
AA3 4 5 N VAL B 133 ? N VAL B 285 O VAL B 158 ? O VAL B 310 
AA3 5 6 N LEU B 159 ? N LEU B 311 O ILE B 182 ? O ILE B 334 
AA3 6 7 N GLY B 185 ? N GLY B 337 O LEU B 209 ? O LEU B 361 
AA4 1 2 N LEU B 196 ? N LEU B 348 O LEU B 199 ? O LEU B 351 
AA5 1 2 N ILE B 216 ? N ILE B 368 O GLN B 230 ? O GLN B 382 
AA6 1 2 N ALA B 268 ? N ALA B 420 O VAL B 289 ? O VAL B 441 
AA7 1 2 N VAL B 308 ? N VAL B 460 O ALA B 372 ? O ALA B 524 
AA7 2 3 O CYS B 375 ? O CYS B 527 N GLU B 330 ? N GLU B 482 
AA8 1 2 N ALA B 323 ? N ALA B 475 O CYS B 357 ? O CYS B 509 
AA8 2 3 O ARG B 358 ? O ARG B 510 N ARG B 347 ? N ARG B 499 
AA9 1 2 N SER B 383 ? N SER B 535 O CYS B 448 ? O CYS B 600 
AA9 2 3 O SER B 443 ? O SER B 595 N HIS B 413 ? N HIS B 565 
AB1 1 2 N THR B 396 ? N THR B 548 O GLY B 438 ? O GLY B 590 
AB2 1 2 N LYS B 457 ? N LYS B 609 O CYS B 526 ? O CYS B 678 
AB2 2 3 O CYS B 527 ? O CYS B 679 N THR B 479 ? N THR B 631 
AB3 1 2 N VAL B 472 ? N VAL B 624 O CYS B 502 ? O CYS B 654 
AB3 2 3 O THR B 501 ? O THR B 653 N VAL B 498 ? N VAL B 650 
# 
_pdbx_entry_details.entry_id                   8VDV 
_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   Y 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              179 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              179 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              179 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                130.34 
_pdbx_validate_rmsd_angle.angle_target_value         115.30 
_pdbx_validate_rmsd_angle.angle_deviation            15.04 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.30 
_pdbx_validate_rmsd_angle.linker_flag                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 HIS A 139 ? ? 73.40   -4.87   
2  1 ASP B 186 ? ? -161.89 -158.45 
3  1 GLU B 197 ? ? -32.84  125.45  
4  1 ALA B 242 ? ? -113.34 71.67   
5  1 VAL B 280 ? ? -126.66 -146.96 
6  1 GLU B 332 ? ? 81.21   -5.18   
7  1 LEU B 348 ? ? -153.42 78.51   
8  1 GLN B 503 ? ? -168.92 112.22  
9  1 ALA B 542 ? ? -76.77  -154.14 
10 1 ASP B 651 ? ? 56.74   -114.92 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 GLY B 244 ? ? ALA B 245 ? ? -148.52 
2 1 ALA B 542 ? ? GLU B 543 ? ? 139.96  
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             ALA 
_pdbx_validate_main_chain_plane.auth_asym_id             B 
_pdbx_validate_main_chain_plane.auth_seq_id              330 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   10.16 
# 
_pdbx_molecule_features.prd_id    PRD_002534 
_pdbx_molecule_features.name      'Inhibitor YBX-PHE-VAL-GLY-THR-THR-PHA-MAA-BIF-EME-NEH' 
_pdbx_molecule_features.type      'Cyclic peptide' 
_pdbx_molecule_features.class     Inhibitor 
_pdbx_molecule_features.details   ? 
# 
_pdbx_molecule.instance_id   1 
_pdbx_molecule.prd_id        PRD_002534 
_pdbx_molecule.asym_id       C 
# 
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 B ALA 168 ? B ALA 16  
2  1 Y 1 B ASP 169 ? B ASP 17  
3  1 Y 1 B GLU 170 ? B GLU 18  
4  1 Y 1 B TYR 171 ? B TYR 19  
5  1 Y 1 B GLN 172 ? B GLN 20  
6  1 Y 1 B PRO 173 ? B PRO 21  
7  1 Y 1 B PRO 174 ? B PRO 22  
8  1 Y 1 B ASP 175 ? B ASP 23  
9  1 Y 1 B GLY 213 ? B GLY 61  
10 1 Y 1 B THR 214 ? B THR 62  
11 1 Y 1 B ARG 215 ? B ARG 63  
12 1 Y 1 B PHE 216 ? B PHE 64  
13 1 Y 1 B HIS 217 ? B HIS 65  
14 1 Y 1 B ARG 218 ? B ARG 66  
15 1 Y 1 B GLN 219 ? B GLN 67  
16 1 Y 1 B GLY 450 ? B GLY 298 
17 1 Y 1 B ALA 451 ? B ALA 299 
18 1 Y 1 B ALA 544 ? B ALA 392 
19 1 Y 1 B SER 545 ? B SER 393 
20 1 Y 1 B MET 546 ? B MET 394 
21 1 Y 1 B GLN 554 ? B GLN 402 
22 1 Y 1 B GLN 555 ? B GLN 403 
23 1 Y 1 B GLY 556 ? B GLY 404 
24 1 Y 1 B GLY 572 ? B GLY 420 
25 1 Y 1 B THR 573 ? B THR 421 
26 1 Y 1 B HIS 574 ? B HIS 422 
27 1 Y 1 B LYS 575 ? B LYS 423 
28 1 Y 1 B PRO 576 ? B PRO 424 
29 1 Y 1 B PRO 577 ? B PRO 425 
30 1 Y 1 B VAL 578 ? B VAL 426 
31 1 Y 1 B LEU 579 ? B LEU 427 
32 1 Y 1 B ARG 580 ? B ARG 428 
33 1 Y 1 B PRO 581 ? B PRO 429 
34 1 Y 1 B ARG 582 ? B ARG 430 
35 1 Y 1 B GLY 583 ? B GLY 431 
36 1 Y 1 B GLN 584 ? B GLN 432 
37 1 Y 1 B ALA 617 ? B ALA 465 
38 1 Y 1 B PRO 618 ? B PRO 466 
39 1 Y 1 B GLY 640 ? B GLY 488 
40 1 Y 1 B THR 641 ? B THR 489 
41 1 Y 1 B ASP 660 ? B ASP 508 
42 1 Y 1 B VAL 661 ? B VAL 509 
43 1 Y 1 B SER 662 ? B SER 510 
44 1 Y 1 B THR 663 ? B THR 511 
45 1 Y 1 B THR 664 ? B THR 512 
46 1 Y 1 B GLY 665 ? B GLY 513 
47 1 Y 1 B SER 666 ? B SER 514 
48 1 Y 1 B THR 667 ? B THR 515 
49 1 Y 1 B SER 668 ? B SER 516 
50 1 Y 1 B GLU 669 ? B GLU 517 
51 1 Y 1 B GLY 670 ? B GLY 518 
# 
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  
BIF N    N N N 74  
BIF CA   C N S 75  
BIF C    C N N 76  
BIF OXT  O N N 77  
BIF CB   C N N 78  
BIF CG   C Y N 79  
BIF CD2  C Y N 80  
BIF CE2  C Y N 81  
BIF CZ   C Y N 82  
BIF CE1  C Y N 83  
BIF CD1  C Y N 84  
BIF C8   C Y N 85  
BIF C9   C Y N 86  
BIF C10  C Y N 87  
BIF C11  C Y N 88  
BIF C12  C Y N 89  
BIF C13  C Y N 90  
BIF O    O N N 91  
BIF H    H N N 92  
BIF H2   H N N 93  
BIF HA   H N N 94  
BIF HXT  H N N 95  
BIF HB2  H N N 96  
BIF HB3  H N N 97  
BIF HD2  H N N 98  
BIF HE2  H N N 99  
BIF HE1  H N N 100 
BIF HD1  H N N 101 
BIF H8   H N N 102 
BIF H9   H N N 103 
BIF H10  H N N 104 
BIF H11  H N N 105 
BIF H13  H N N 106 
CYS N    N N N 107 
CYS CA   C N R 108 
CYS C    C N N 109 
CYS O    O N N 110 
CYS CB   C N N 111 
CYS SG   S N N 112 
CYS OXT  O N N 113 
CYS H    H N N 114 
CYS H2   H N N 115 
CYS HA   H N N 116 
CYS HB2  H N N 117 
CYS HB3  H N N 118 
CYS HG   H N N 119 
CYS HXT  H N N 120 
EME C7   C N N 121 
EME N    N N N 122 
EME CA   C N S 123 
EME C    C N N 124 
EME O    O N N 125 
EME CB   C N N 126 
EME CG   C N N 127 
EME CD   C N N 128 
EME OE2  O N N 129 
EME OE1  O N N 130 
EME OXT  O N N 131 
EME H1   H N N 132 
EME H4   H N N 133 
EME H3   H N N 134 
EME H    H N N 135 
EME HA   H N N 136 
EME H7   H N N 137 
EME H8   H N N 138 
EME H9   H N N 139 
EME H10  H N N 140 
EME H11  H N N 141 
EME HXT  H N N 142 
GLN N    N N N 143 
GLN CA   C N S 144 
GLN C    C N N 145 
GLN O    O N N 146 
GLN CB   C N N 147 
GLN CG   C N N 148 
GLN CD   C N N 149 
GLN OE1  O N N 150 
GLN NE2  N N N 151 
GLN OXT  O N N 152 
GLN H    H N N 153 
GLN H2   H N N 154 
GLN HA   H N N 155 
GLN HB2  H N N 156 
GLN HB3  H N N 157 
GLN HG2  H N N 158 
GLN HG3  H N N 159 
GLN HE21 H N N 160 
GLN HE22 H N N 161 
GLN HXT  H N N 162 
GLU N    N N N 163 
GLU CA   C N S 164 
GLU C    C N N 165 
GLU O    O N N 166 
GLU CB   C N N 167 
GLU CG   C N N 168 
GLU CD   C N N 169 
GLU OE1  O N N 170 
GLU OE2  O N N 171 
GLU OXT  O N N 172 
GLU H    H N N 173 
GLU H2   H N N 174 
GLU HA   H N N 175 
GLU HB2  H N N 176 
GLU HB3  H N N 177 
GLU HG2  H N N 178 
GLU HG3  H N N 179 
GLU HE2  H N N 180 
GLU HXT  H N N 181 
GLY N    N N N 182 
GLY CA   C N N 183 
GLY C    C N N 184 
GLY O    O N N 185 
GLY OXT  O N N 186 
GLY H    H N N 187 
GLY H2   H N N 188 
GLY HA2  H N N 189 
GLY HA3  H N N 190 
GLY HXT  H N N 191 
HIS N    N N N 192 
HIS CA   C N S 193 
HIS C    C N N 194 
HIS O    O N N 195 
HIS CB   C N N 196 
HIS CG   C Y N 197 
HIS ND1  N Y N 198 
HIS CD2  C Y N 199 
HIS CE1  C Y N 200 
HIS NE2  N Y N 201 
HIS OXT  O N N 202 
HIS H    H N N 203 
HIS H2   H N N 204 
HIS HA   H N N 205 
HIS HB2  H N N 206 
HIS HB3  H N N 207 
HIS HD1  H N N 208 
HIS HD2  H N N 209 
HIS HE1  H N N 210 
HIS HE2  H N N 211 
HIS HXT  H N N 212 
HOH O    O N N 213 
HOH H1   H N N 214 
HOH H2   H N N 215 
ILE N    N N N 216 
ILE CA   C N S 217 
ILE C    C N N 218 
ILE O    O N N 219 
ILE CB   C N S 220 
ILE CG1  C N N 221 
ILE CG2  C N N 222 
ILE CD1  C N N 223 
ILE OXT  O N N 224 
ILE H    H N N 225 
ILE H2   H N N 226 
ILE HA   H N N 227 
ILE HB   H N N 228 
ILE HG12 H N N 229 
ILE HG13 H N N 230 
ILE HG21 H N N 231 
ILE HG22 H N N 232 
ILE HG23 H N N 233 
ILE HD11 H N N 234 
ILE HD12 H N N 235 
ILE HD13 H N N 236 
ILE HXT  H N N 237 
LEU N    N N N 238 
LEU CA   C N S 239 
LEU C    C N N 240 
LEU O    O N N 241 
LEU CB   C N N 242 
LEU CG   C N N 243 
LEU CD1  C N N 244 
LEU CD2  C N N 245 
LEU OXT  O N N 246 
LEU H    H N N 247 
LEU H2   H N N 248 
LEU HA   H N N 249 
LEU HB2  H N N 250 
LEU HB3  H N N 251 
LEU HG   H N N 252 
LEU HD11 H N N 253 
LEU HD12 H N N 254 
LEU HD13 H N N 255 
LEU HD21 H N N 256 
LEU HD22 H N N 257 
LEU HD23 H N N 258 
LEU HXT  H N N 259 
LYS N    N N N 260 
LYS CA   C N S 261 
LYS C    C N N 262 
LYS O    O N N 263 
LYS CB   C N N 264 
LYS CG   C N N 265 
LYS CD   C N N 266 
LYS CE   C N N 267 
LYS NZ   N N N 268 
LYS OXT  O N N 269 
LYS H    H N N 270 
LYS H2   H N N 271 
LYS HA   H N N 272 
LYS HB2  H N N 273 
LYS HB3  H N N 274 
LYS HG2  H N N 275 
LYS HG3  H N N 276 
LYS HD2  H N N 277 
LYS HD3  H N N 278 
LYS HE2  H N N 279 
LYS HE3  H N N 280 
LYS HZ1  H N N 281 
LYS HZ2  H N N 282 
LYS HZ3  H N N 283 
LYS HXT  H N N 284 
MAA N    N N N 285 
MAA CM   C N N 286 
MAA CA   C N S 287 
MAA CB   C N N 288 
MAA C    C N N 289 
MAA O    O N N 290 
MAA OXT  O N N 291 
MAA H    H N N 292 
MAA HM1  H N N 293 
MAA HM2  H N N 294 
MAA HM3  H N N 295 
MAA HA   H N N 296 
MAA HB1  H N N 297 
MAA HB2  H N N 298 
MAA HB3  H N N 299 
MAA HXT  H N N 300 
MET N    N N N 301 
MET CA   C N S 302 
MET C    C N N 303 
MET O    O N N 304 
MET CB   C N N 305 
MET CG   C N N 306 
MET SD   S N N 307 
MET CE   C N N 308 
MET OXT  O N N 309 
MET H    H N N 310 
MET H2   H N N 311 
MET HA   H N N 312 
MET HB2  H N N 313 
MET HB3  H N N 314 
MET HG2  H N N 315 
MET HG3  H N N 316 
MET HE1  H N N 317 
MET HE2  H N N 318 
MET HE3  H N N 319 
MET HXT  H N N 320 
NEH N    N N N 321 
NEH CA   C N N 322 
NEH CB   C N N 323 
NEH H    H N N 324 
NEH HA2  H N N 325 
NEH HA3  H N N 326 
NEH HB1  H N N 327 
NEH HB2  H N N 328 
NEH HB3  H N N 329 
NEH H2   H N N 330 
PHA N    N N N 331 
PHA CA   C N S 332 
PHA C    C N N 333 
PHA O    O N N 334 
PHA CB   C N N 335 
PHA CG   C Y N 336 
PHA CD1  C Y N 337 
PHA CD2  C Y N 338 
PHA CE1  C Y N 339 
PHA CE2  C Y N 340 
PHA CZ   C Y N 341 
PHA H    H N N 342 
PHA H2   H N N 343 
PHA HA   H N N 344 
PHA HC   H N N 345 
PHA HB2  H N N 346 
PHA HB3  H N N 347 
PHA HD1  H N N 348 
PHA HD2  H N N 349 
PHA HE1  H N N 350 
PHA HE2  H N N 351 
PHA HZ   H N N 352 
PHE N    N N N 353 
PHE CA   C N S 354 
PHE C    C N N 355 
PHE O    O N N 356 
PHE CB   C N N 357 
PHE CG   C Y N 358 
PHE CD1  C Y N 359 
PHE CD2  C Y N 360 
PHE CE1  C Y N 361 
PHE CE2  C Y N 362 
PHE CZ   C Y N 363 
PHE OXT  O N N 364 
PHE H    H N N 365 
PHE H2   H N N 366 
PHE HA   H N N 367 
PHE HB2  H N N 368 
PHE HB3  H N N 369 
PHE HD1  H N N 370 
PHE HD2  H N N 371 
PHE HE1  H N N 372 
PHE HE2  H N N 373 
PHE HZ   H N N 374 
PHE HXT  H N N 375 
PRO N    N N N 376 
PRO CA   C N S 377 
PRO C    C N N 378 
PRO O    O N N 379 
PRO CB   C N N 380 
PRO CG   C N N 381 
PRO CD   C N N 382 
PRO OXT  O N N 383 
PRO H    H N N 384 
PRO HA   H N N 385 
PRO HB2  H N N 386 
PRO HB3  H N N 387 
PRO HG2  H N N 388 
PRO HG3  H N N 389 
PRO HD2  H N N 390 
PRO HD3  H N N 391 
PRO HXT  H N N 392 
SER N    N N N 393 
SER CA   C N S 394 
SER C    C N N 395 
SER O    O N N 396 
SER CB   C N N 397 
SER OG   O N N 398 
SER OXT  O N N 399 
SER H    H N N 400 
SER H2   H N N 401 
SER HA   H N N 402 
SER HB2  H N N 403 
SER HB3  H N N 404 
SER HG   H N N 405 
SER HXT  H N N 406 
THR N    N N N 407 
THR CA   C N S 408 
THR C    C N N 409 
THR O    O N N 410 
THR CB   C N R 411 
THR OG1  O N N 412 
THR CG2  C N N 413 
THR OXT  O N N 414 
THR H    H N N 415 
THR H2   H N N 416 
THR HA   H N N 417 
THR HB   H N N 418 
THR HG1  H N N 419 
THR HG21 H N N 420 
THR HG22 H N N 421 
THR HG23 H N N 422 
THR HXT  H N N 423 
TRP N    N N N 424 
TRP CA   C N S 425 
TRP C    C N N 426 
TRP O    O N N 427 
TRP CB   C N N 428 
TRP CG   C Y N 429 
TRP CD1  C Y N 430 
TRP CD2  C Y N 431 
TRP NE1  N Y N 432 
TRP CE2  C Y N 433 
TRP CE3  C Y N 434 
TRP CZ2  C Y N 435 
TRP CZ3  C Y N 436 
TRP CH2  C Y N 437 
TRP OXT  O N N 438 
TRP H    H N N 439 
TRP H2   H N N 440 
TRP HA   H N N 441 
TRP HB2  H N N 442 
TRP HB3  H N N 443 
TRP HD1  H N N 444 
TRP HE1  H N N 445 
TRP HE3  H N N 446 
TRP HZ2  H N N 447 
TRP HZ3  H N N 448 
TRP HH2  H N N 449 
TRP HXT  H N N 450 
TYR N    N N N 451 
TYR CA   C N S 452 
TYR C    C N N 453 
TYR O    O N N 454 
TYR CB   C N N 455 
TYR CG   C Y N 456 
TYR CD1  C Y N 457 
TYR CD2  C Y N 458 
TYR CE1  C Y N 459 
TYR CE2  C Y N 460 
TYR CZ   C Y N 461 
TYR OH   O N N 462 
TYR OXT  O N N 463 
TYR H    H N N 464 
TYR H2   H N N 465 
TYR HA   H N N 466 
TYR HB2  H N N 467 
TYR HB3  H N N 468 
TYR HD1  H N N 469 
TYR HD2  H N N 470 
TYR HE1  H N N 471 
TYR HE2  H N N 472 
TYR HH   H N N 473 
TYR HXT  H N N 474 
VAL N    N N N 475 
VAL CA   C N S 476 
VAL C    C N N 477 
VAL O    O N N 478 
VAL CB   C N N 479 
VAL CG1  C N N 480 
VAL CG2  C N N 481 
VAL OXT  O N N 482 
VAL H    H N N 483 
VAL H2   H N N 484 
VAL HA   H N N 485 
VAL HB   H N N 486 
VAL HG11 H N N 487 
VAL HG12 H N N 488 
VAL HG13 H N N 489 
VAL HG21 H N N 490 
VAL HG22 H N N 491 
VAL HG23 H N N 492 
VAL HXT  H N N 493 
YBX O1   O N N 494 
YBX C5   C N N 495 
YBX C6   C N N 496 
YBX S1   S N N 497 
YBX C7   C N N 498 
YBX C8   C N N 499 
YBX O2   O N N 500 
YBX H1   H N N 501 
YBX H2   H N N 502 
YBX H3   H N N 503 
YBX H4   H N N 504 
YBX H5   H N N 505 
YBX H6   H N N 506 
YBX H7   H N N 507 
YBX H8   H N N 508 
# 
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  
BIF N   CA   sing N N 70  
BIF N   H    sing N N 71  
BIF N   H2   sing N N 72  
BIF CA  C    sing N N 73  
BIF CA  CB   sing N N 74  
BIF CA  HA   sing N N 75  
BIF C   OXT  sing N N 76  
BIF C   O    doub N N 77  
BIF OXT HXT  sing N N 78  
BIF CB  CG   sing N N 79  
BIF CB  HB2  sing N N 80  
BIF CB  HB3  sing N N 81  
BIF CG  CD2  doub Y N 82  
BIF CG  CD1  sing Y N 83  
BIF CD2 CE2  sing Y N 84  
BIF CD2 HD2  sing N N 85  
BIF CE2 CZ   doub Y N 86  
BIF CE2 HE2  sing N N 87  
BIF CZ  CE1  sing Y N 88  
BIF CZ  C12  sing Y N 89  
BIF CE1 CD1  doub Y N 90  
BIF CE1 HE1  sing N N 91  
BIF CD1 HD1  sing N N 92  
BIF C8  C9   doub Y N 93  
BIF C8  C13  sing Y N 94  
BIF C8  H8   sing N N 95  
BIF C9  C10  sing Y N 96  
BIF C9  H9   sing N N 97  
BIF C10 C11  doub Y N 98  
BIF C10 H10  sing N N 99  
BIF C11 C12  sing Y N 100 
BIF C11 H11  sing N N 101 
BIF C12 C13  doub Y N 102 
BIF C13 H13  sing N N 103 
CYS N   CA   sing N N 104 
CYS N   H    sing N N 105 
CYS N   H2   sing N N 106 
CYS CA  C    sing N N 107 
CYS CA  CB   sing N N 108 
CYS CA  HA   sing N N 109 
CYS C   O    doub N N 110 
CYS C   OXT  sing N N 111 
CYS CB  SG   sing N N 112 
CYS CB  HB2  sing N N 113 
CYS CB  HB3  sing N N 114 
CYS SG  HG   sing N N 115 
CYS OXT HXT  sing N N 116 
EME C7  N    sing N N 117 
EME N   CA   sing N N 118 
EME CB  CA   sing N N 119 
EME CB  CG   sing N N 120 
EME CA  C    sing N N 121 
EME OE2 CD   doub N N 122 
EME O   C    doub N N 123 
EME CD  CG   sing N N 124 
EME CD  OE1  sing N N 125 
EME C   OXT  sing N N 126 
EME C7  H1   sing N N 127 
EME C7  H4   sing N N 128 
EME C7  H3   sing N N 129 
EME N   H    sing N N 130 
EME CA  HA   sing N N 131 
EME CB  H7   sing N N 132 
EME CB  H8   sing N N 133 
EME CG  H9   sing N N 134 
EME CG  H10  sing N N 135 
EME OE1 H11  sing N N 136 
EME OXT HXT  sing N N 137 
GLN N   CA   sing N N 138 
GLN N   H    sing N N 139 
GLN N   H2   sing N N 140 
GLN CA  C    sing N N 141 
GLN CA  CB   sing N N 142 
GLN CA  HA   sing N N 143 
GLN C   O    doub N N 144 
GLN C   OXT  sing N N 145 
GLN CB  CG   sing N N 146 
GLN CB  HB2  sing N N 147 
GLN CB  HB3  sing N N 148 
GLN CG  CD   sing N N 149 
GLN CG  HG2  sing N N 150 
GLN CG  HG3  sing N N 151 
GLN CD  OE1  doub N N 152 
GLN CD  NE2  sing N N 153 
GLN NE2 HE21 sing N N 154 
GLN NE2 HE22 sing N N 155 
GLN OXT HXT  sing N N 156 
GLU N   CA   sing N N 157 
GLU N   H    sing N N 158 
GLU N   H2   sing N N 159 
GLU CA  C    sing N N 160 
GLU CA  CB   sing N N 161 
GLU CA  HA   sing N N 162 
GLU C   O    doub N N 163 
GLU C   OXT  sing N N 164 
GLU CB  CG   sing N N 165 
GLU CB  HB2  sing N N 166 
GLU CB  HB3  sing N N 167 
GLU CG  CD   sing N N 168 
GLU CG  HG2  sing N N 169 
GLU CG  HG3  sing N N 170 
GLU CD  OE1  doub N N 171 
GLU CD  OE2  sing N N 172 
GLU OE2 HE2  sing N N 173 
GLU OXT HXT  sing N N 174 
GLY N   CA   sing N N 175 
GLY N   H    sing N N 176 
GLY N   H2   sing N N 177 
GLY CA  C    sing N N 178 
GLY CA  HA2  sing N N 179 
GLY CA  HA3  sing N N 180 
GLY C   O    doub N N 181 
GLY C   OXT  sing N N 182 
GLY OXT HXT  sing N N 183 
HIS N   CA   sing N N 184 
HIS N   H    sing N N 185 
HIS N   H2   sing N N 186 
HIS CA  C    sing N N 187 
HIS CA  CB   sing N N 188 
HIS CA  HA   sing N N 189 
HIS C   O    doub N N 190 
HIS C   OXT  sing N N 191 
HIS CB  CG   sing N N 192 
HIS CB  HB2  sing N N 193 
HIS CB  HB3  sing N N 194 
HIS CG  ND1  sing Y N 195 
HIS CG  CD2  doub Y N 196 
HIS ND1 CE1  doub Y N 197 
HIS ND1 HD1  sing N N 198 
HIS CD2 NE2  sing Y N 199 
HIS CD2 HD2  sing N N 200 
HIS CE1 NE2  sing Y N 201 
HIS CE1 HE1  sing N N 202 
HIS NE2 HE2  sing N N 203 
HIS OXT HXT  sing N N 204 
HOH O   H1   sing N N 205 
HOH O   H2   sing N N 206 
ILE N   CA   sing N N 207 
ILE N   H    sing N N 208 
ILE N   H2   sing N N 209 
ILE CA  C    sing N N 210 
ILE CA  CB   sing N N 211 
ILE CA  HA   sing N N 212 
ILE C   O    doub N N 213 
ILE C   OXT  sing N N 214 
ILE CB  CG1  sing N N 215 
ILE CB  CG2  sing N N 216 
ILE CB  HB   sing N N 217 
ILE CG1 CD1  sing N N 218 
ILE CG1 HG12 sing N N 219 
ILE CG1 HG13 sing N N 220 
ILE CG2 HG21 sing N N 221 
ILE CG2 HG22 sing N N 222 
ILE CG2 HG23 sing N N 223 
ILE CD1 HD11 sing N N 224 
ILE CD1 HD12 sing N N 225 
ILE CD1 HD13 sing N N 226 
ILE OXT HXT  sing N N 227 
LEU N   CA   sing N N 228 
LEU N   H    sing N N 229 
LEU N   H2   sing N N 230 
LEU CA  C    sing N N 231 
LEU CA  CB   sing N N 232 
LEU CA  HA   sing N N 233 
LEU C   O    doub N N 234 
LEU C   OXT  sing N N 235 
LEU CB  CG   sing N N 236 
LEU CB  HB2  sing N N 237 
LEU CB  HB3  sing N N 238 
LEU CG  CD1  sing N N 239 
LEU CG  CD2  sing N N 240 
LEU CG  HG   sing N N 241 
LEU CD1 HD11 sing N N 242 
LEU CD1 HD12 sing N N 243 
LEU CD1 HD13 sing N N 244 
LEU CD2 HD21 sing N N 245 
LEU CD2 HD22 sing N N 246 
LEU CD2 HD23 sing N N 247 
LEU OXT HXT  sing N N 248 
LYS N   CA   sing N N 249 
LYS N   H    sing N N 250 
LYS N   H2   sing N N 251 
LYS CA  C    sing N N 252 
LYS CA  CB   sing N N 253 
LYS CA  HA   sing N N 254 
LYS C   O    doub N N 255 
LYS C   OXT  sing N N 256 
LYS CB  CG   sing N N 257 
LYS CB  HB2  sing N N 258 
LYS CB  HB3  sing N N 259 
LYS CG  CD   sing N N 260 
LYS CG  HG2  sing N N 261 
LYS CG  HG3  sing N N 262 
LYS CD  CE   sing N N 263 
LYS CD  HD2  sing N N 264 
LYS CD  HD3  sing N N 265 
LYS CE  NZ   sing N N 266 
LYS CE  HE2  sing N N 267 
LYS CE  HE3  sing N N 268 
LYS NZ  HZ1  sing N N 269 
LYS NZ  HZ2  sing N N 270 
LYS NZ  HZ3  sing N N 271 
LYS OXT HXT  sing N N 272 
MAA N   CM   sing N N 273 
MAA N   CA   sing N N 274 
MAA N   H    sing N N 275 
MAA CM  HM1  sing N N 276 
MAA CM  HM2  sing N N 277 
MAA CM  HM3  sing N N 278 
MAA CA  CB   sing N N 279 
MAA CA  C    sing N N 280 
MAA CA  HA   sing N N 281 
MAA CB  HB1  sing N N 282 
MAA CB  HB2  sing N N 283 
MAA CB  HB3  sing N N 284 
MAA C   O    doub N N 285 
MAA C   OXT  sing N N 286 
MAA OXT HXT  sing N N 287 
MET N   CA   sing N N 288 
MET N   H    sing N N 289 
MET N   H2   sing N N 290 
MET CA  C    sing N N 291 
MET CA  CB   sing N N 292 
MET CA  HA   sing N N 293 
MET C   O    doub N N 294 
MET C   OXT  sing N N 295 
MET CB  CG   sing N N 296 
MET CB  HB2  sing N N 297 
MET CB  HB3  sing N N 298 
MET CG  SD   sing N N 299 
MET CG  HG2  sing N N 300 
MET CG  HG3  sing N N 301 
MET SD  CE   sing N N 302 
MET CE  HE1  sing N N 303 
MET CE  HE2  sing N N 304 
MET CE  HE3  sing N N 305 
MET OXT HXT  sing N N 306 
NEH N   CA   sing N N 307 
NEH N   H    sing N N 308 
NEH CA  CB   sing N N 309 
NEH CA  HA2  sing N N 310 
NEH CA  HA3  sing N N 311 
NEH CB  HB1  sing N N 312 
NEH CB  HB2  sing N N 313 
NEH CB  HB3  sing N N 314 
NEH H2  N    sing N N 315 
PHA N   CA   sing N N 316 
PHA N   H    sing N N 317 
PHA N   H2   sing N N 318 
PHA CA  C    sing N N 319 
PHA CA  CB   sing N N 320 
PHA CA  HA   sing N N 321 
PHA C   O    doub N N 322 
PHA C   HC   sing N N 323 
PHA CB  CG   sing N N 324 
PHA CB  HB2  sing N N 325 
PHA CB  HB3  sing N N 326 
PHA CG  CD1  doub Y N 327 
PHA CG  CD2  sing Y N 328 
PHA CD1 CE1  sing Y N 329 
PHA CD1 HD1  sing N N 330 
PHA CD2 CE2  doub Y N 331 
PHA CD2 HD2  sing N N 332 
PHA CE1 CZ   doub Y N 333 
PHA CE1 HE1  sing N N 334 
PHA CE2 CZ   sing Y N 335 
PHA CE2 HE2  sing N N 336 
PHA CZ  HZ   sing N N 337 
PHE N   CA   sing N N 338 
PHE N   H    sing N N 339 
PHE N   H2   sing N N 340 
PHE CA  C    sing N N 341 
PHE CA  CB   sing N N 342 
PHE CA  HA   sing N N 343 
PHE C   O    doub N N 344 
PHE C   OXT  sing N N 345 
PHE CB  CG   sing N N 346 
PHE CB  HB2  sing N N 347 
PHE CB  HB3  sing N N 348 
PHE CG  CD1  doub Y N 349 
PHE CG  CD2  sing Y N 350 
PHE CD1 CE1  sing Y N 351 
PHE CD1 HD1  sing N N 352 
PHE CD2 CE2  doub Y N 353 
PHE CD2 HD2  sing N N 354 
PHE CE1 CZ   doub Y N 355 
PHE CE1 HE1  sing N N 356 
PHE CE2 CZ   sing Y N 357 
PHE CE2 HE2  sing N N 358 
PHE CZ  HZ   sing N N 359 
PHE OXT HXT  sing N N 360 
PRO N   CA   sing N N 361 
PRO N   CD   sing N N 362 
PRO N   H    sing N N 363 
PRO CA  C    sing N N 364 
PRO CA  CB   sing N N 365 
PRO CA  HA   sing N N 366 
PRO C   O    doub N N 367 
PRO C   OXT  sing N N 368 
PRO CB  CG   sing N N 369 
PRO CB  HB2  sing N N 370 
PRO CB  HB3  sing N N 371 
PRO CG  CD   sing N N 372 
PRO CG  HG2  sing N N 373 
PRO CG  HG3  sing N N 374 
PRO CD  HD2  sing N N 375 
PRO CD  HD3  sing N N 376 
PRO OXT HXT  sing N N 377 
SER N   CA   sing N N 378 
SER N   H    sing N N 379 
SER N   H2   sing N N 380 
SER CA  C    sing N N 381 
SER CA  CB   sing N N 382 
SER CA  HA   sing N N 383 
SER C   O    doub N N 384 
SER C   OXT  sing N N 385 
SER CB  OG   sing N N 386 
SER CB  HB2  sing N N 387 
SER CB  HB3  sing N N 388 
SER OG  HG   sing N N 389 
SER OXT HXT  sing N N 390 
THR N   CA   sing N N 391 
THR N   H    sing N N 392 
THR N   H2   sing N N 393 
THR CA  C    sing N N 394 
THR CA  CB   sing N N 395 
THR CA  HA   sing N N 396 
THR C   O    doub N N 397 
THR C   OXT  sing N N 398 
THR CB  OG1  sing N N 399 
THR CB  CG2  sing N N 400 
THR CB  HB   sing N N 401 
THR OG1 HG1  sing N N 402 
THR CG2 HG21 sing N N 403 
THR CG2 HG22 sing N N 404 
THR CG2 HG23 sing N N 405 
THR OXT HXT  sing N N 406 
TRP N   CA   sing N N 407 
TRP N   H    sing N N 408 
TRP N   H2   sing N N 409 
TRP CA  C    sing N N 410 
TRP CA  CB   sing N N 411 
TRP CA  HA   sing N N 412 
TRP C   O    doub N N 413 
TRP C   OXT  sing N N 414 
TRP CB  CG   sing N N 415 
TRP CB  HB2  sing N N 416 
TRP CB  HB3  sing N N 417 
TRP CG  CD1  doub Y N 418 
TRP CG  CD2  sing Y N 419 
TRP CD1 NE1  sing Y N 420 
TRP CD1 HD1  sing N N 421 
TRP CD2 CE2  doub Y N 422 
TRP CD2 CE3  sing Y N 423 
TRP NE1 CE2  sing Y N 424 
TRP NE1 HE1  sing N N 425 
TRP CE2 CZ2  sing Y N 426 
TRP CE3 CZ3  doub Y N 427 
TRP CE3 HE3  sing N N 428 
TRP CZ2 CH2  doub Y N 429 
TRP CZ2 HZ2  sing N N 430 
TRP CZ3 CH2  sing Y N 431 
TRP CZ3 HZ3  sing N N 432 
TRP CH2 HH2  sing N N 433 
TRP OXT HXT  sing N N 434 
TYR N   CA   sing N N 435 
TYR N   H    sing N N 436 
TYR N   H2   sing N N 437 
TYR CA  C    sing N N 438 
TYR CA  CB   sing N N 439 
TYR CA  HA   sing N N 440 
TYR C   O    doub N N 441 
TYR C   OXT  sing N N 442 
TYR CB  CG   sing N N 443 
TYR CB  HB2  sing N N 444 
TYR CB  HB3  sing N N 445 
TYR CG  CD1  doub Y N 446 
TYR CG  CD2  sing Y N 447 
TYR CD1 CE1  sing Y N 448 
TYR CD1 HD1  sing N N 449 
TYR CD2 CE2  doub Y N 450 
TYR CD2 HD2  sing N N 451 
TYR CE1 CZ   doub Y N 452 
TYR CE1 HE1  sing N N 453 
TYR CE2 CZ   sing Y N 454 
TYR CE2 HE2  sing N N 455 
TYR CZ  OH   sing N N 456 
TYR OH  HH   sing N N 457 
TYR OXT HXT  sing N N 458 
VAL N   CA   sing N N 459 
VAL N   H    sing N N 460 
VAL N   H2   sing N N 461 
VAL CA  C    sing N N 462 
VAL CA  CB   sing N N 463 
VAL CA  HA   sing N N 464 
VAL C   O    doub N N 465 
VAL C   OXT  sing N N 466 
VAL CB  CG1  sing N N 467 
VAL CB  CG2  sing N N 468 
VAL CB  HB   sing N N 469 
VAL CG1 HG11 sing N N 470 
VAL CG1 HG12 sing N N 471 
VAL CG1 HG13 sing N N 472 
VAL CG2 HG21 sing N N 473 
VAL CG2 HG22 sing N N 474 
VAL CG2 HG23 sing N N 475 
VAL OXT HXT  sing N N 476 
YBX C8  C7   sing N N 477 
YBX C7  S1   sing N N 478 
YBX C6  C5   sing N N 479 
YBX C6  S1   sing N N 480 
YBX C5  O1   doub N N 481 
YBX C5  O2   sing N N 482 
YBX C6  H1   sing N N 483 
YBX C6  H2   sing N N 484 
YBX C7  H3   sing N N 485 
YBX C7  H4   sing N N 486 
YBX C8  H5   sing N N 487 
YBX C8  H6   sing N N 488 
YBX C8  H7   sing N N 489 
YBX O2  H8   sing N N 490 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7kfa 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8VDV 
_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]   0.015851 
_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]   0.014115 
_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]   0.006711 
_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 
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   . THR A 1 1   ? -14.543 -28.385 52.125 1.00 43.22 ? 61  THR A N   1 
ATOM   2    C CA  . THR A 1 1   ? -14.557 -28.372 50.666 1.00 41.08 ? 61  THR A CA  1 
ATOM   3    C C   . THR A 1 1   ? -13.143 -28.157 50.081 1.00 26.38 ? 61  THR A C   1 
ATOM   4    O O   . THR A 1 1   ? -12.944 -28.178 48.866 1.00 27.32 ? 61  THR A O   1 
ATOM   5    C CB  . THR A 1 1   ? -15.542 -27.318 50.106 1.00 41.41 ? 61  THR A CB  1 
ATOM   6    O OG1 . THR A 1 1   ? -15.380 -26.085 50.817 1.00 48.73 ? 61  THR A OG1 1 
ATOM   7    C CG2 . THR A 1 1   ? -16.981 -27.784 50.276 1.00 49.57 ? 61  THR A CG2 1 
ATOM   8    N N   . ALA A 1 2   ? -12.162 -28.012 50.962 1.00 22.99 ? 62  ALA A N   1 
ATOM   9    C CA  . ALA A 1 2   ? -10.777 -27.701 50.601 1.00 19.67 ? 62  ALA A CA  1 
ATOM   10   C C   . ALA A 1 2   ? -10.099 -29.013 50.190 1.00 19.32 ? 62  ALA A C   1 
ATOM   11   O O   . ALA A 1 2   ? -10.309 -30.042 50.846 1.00 19.99 ? 62  ALA A O   1 
ATOM   12   C CB  . ALA A 1 2   ? -10.018 -27.055 51.741 1.00 19.99 ? 62  ALA A CB  1 
ATOM   13   N N   . THR A 1 3   ? -9.347  -29.025 49.088 1.00 17.08 ? 63  THR A N   1 
ATOM   14   C CA  . THR A 1 3   ? -8.773  -30.285 48.589 1.00 17.93 ? 63  THR A CA  1 
ATOM   15   C C   . THR A 1 3   ? -7.240  -30.229 48.514 1.00 17.65 ? 63  THR A C   1 
ATOM   16   O O   . THR A 1 3   ? -6.627  -29.148 48.477 1.00 13.84 ? 63  THR A O   1 
ATOM   17   C CB  . THR A 1 3   ? -9.348  -30.632 47.191 1.00 15.45 ? 63  THR A CB  1 
ATOM   18   O OG1 . THR A 1 3   ? -9.141  -29.512 46.308 1.00 16.56 ? 63  THR A OG1 1 
ATOM   19   C CG2 . THR A 1 3   ? -10.855 -30.955 47.280 1.00 17.91 ? 63  THR A CG2 1 
ATOM   20   N N   . PHE A 1 4   ? -6.625  -31.409 48.468 1.00 14.17 ? 64  PHE A N   1 
ATOM   21   C CA  . PHE A 1 4   ? -5.176  -31.550 48.434 1.00 15.72 ? 64  PHE A CA  1 
ATOM   22   C C   . PHE A 1 4   ? -4.707  -32.146 47.111 1.00 17.58 ? 64  PHE A C   1 
ATOM   23   O O   . PHE A 1 4   ? -5.322  -33.060 46.551 1.00 17.35 ? 64  PHE A O   1 
ATOM   24   C CB  . PHE A 1 4   ? -4.761  -32.503 49.561 1.00 16.88 ? 64  PHE A CB  1 
ATOM   25   C CG  . PHE A 1 4   ? -3.286  -32.794 49.606 1.00 16.14 ? 64  PHE A CG  1 
ATOM   26   C CD1 . PHE A 1 4   ? -2.347  -31.772 49.578 1.00 14.58 ? 64  PHE A CD1 1 
ATOM   27   C CD2 . PHE A 1 4   ? -2.838  -34.102 49.640 1.00 14.77 ? 64  PHE A CD2 1 
ATOM   28   C CE1 . PHE A 1 4   ? -0.987  -32.058 49.616 1.00 13.88 ? 64  PHE A CE1 1 
ATOM   29   C CE2 . PHE A 1 4   ? -1.471  -34.396 49.676 1.00 13.79 ? 64  PHE A CE2 1 
ATOM   30   C CZ  . PHE A 1 4   ? -0.554  -33.387 49.650 1.00 16.49 ? 64  PHE A CZ  1 
ATOM   31   N N   . HIS A 1 5   ? -3.556  -31.678 46.653 1.00 11.54 ? 65  HIS A N   1 
ATOM   32   C CA  . HIS A 1 5   ? -3.030  -32.112 45.386 1.00 11.86 ? 65  HIS A CA  1 
ATOM   33   C C   . HIS A 1 5   ? -1.525  -32.248 45.457 1.00 13.72 ? 65  HIS A C   1 
ATOM   34   O O   . HIS A 1 5   ? -0.822  -31.437 46.063 1.00 12.29 ? 65  HIS A O   1 
ATOM   35   C CB  . HIS A 1 5   ? -3.390  -31.090 44.294 1.00 14.35 ? 65  HIS A CB  1 
ATOM   36   C CG  . HIS A 1 5   ? -4.850  -30.756 44.227 1.00 15.52 ? 65  HIS A CG  1 
ATOM   37   N ND1 . HIS A 1 5   ? -5.754  -31.497 43.498 1.00 16.66 ? 65  HIS A ND1 1 
ATOM   38   C CD2 . HIS A 1 5   ? -5.572  -29.787 44.843 1.00 15.44 ? 65  HIS A CD2 1 
ATOM   39   C CE1 . HIS A 1 5   ? -6.966  -30.980 43.638 1.00 17.27 ? 65  HIS A CE1 1 
ATOM   40   N NE2 . HIS A 1 5   ? -6.883  -29.941 44.450 1.00 16.90 ? 65  HIS A NE2 1 
ATOM   41   N N   . ARG A 1 6   ? -1.017  -33.294 44.833 1.00 15.67 ? 66  ARG A N   1 
ATOM   42   C CA  . ARG A 1 6   ? 0.416   -33.402 44.652 1.00 14.16 ? 66  ARG A CA  1 
ATOM   43   C C   . ARG A 1 6   ? 0.733   -34.020 43.304 1.00 15.00 ? 66  ARG A C   1 
ATOM   44   O O   . ARG A 1 6   ? -0.122  -34.625 42.663 1.00 12.49 ? 66  ARG A O   1 
ATOM   45   C CB  . ARG A 1 6   ? 1.068   -34.227 45.753 1.00 15.78 ? 66  ARG A CB  1 
ATOM   46   C CG  . ARG A 1 6   ? 0.722   -35.709 45.680 1.00 16.54 ? 66  ARG A CG  1 
ATOM   47   C CD  . ARG A 1 6   ? 1.134   -36.363 46.950 1.00 18.50 ? 66  ARG A CD  1 
ATOM   48   N NE  . ARG A 1 6   ? 1.081   -37.814 46.823 1.00 20.68 ? 66  ARG A NE  1 
ATOM   49   C CZ  . ARG A 1 6   ? 1.201   -38.654 47.843 1.00 21.19 ? 66  ARG A CZ  1 
ATOM   50   N NH1 . ARG A 1 6   ? 1.448   -38.183 49.060 1.00 24.66 ? 66  ARG A NH1 1 
ATOM   51   N NH2 . ARG A 1 6   ? 1.159   -39.950 47.622 1.00 24.15 ? 66  ARG A NH2 1 
ATOM   52   N N   . CYS A 1 7   ? 1.977   -33.860 42.893 1.00 13.03 ? 67  CYS A N   1 
ATOM   53   C CA  . CYS A 1 7   ? 2.408   -34.195 41.552 1.00 13.53 ? 67  CYS A CA  1 
ATOM   54   C C   . CYS A 1 7   ? 2.214   -35.701 41.327 1.00 13.59 ? 67  CYS A C   1 
ATOM   55   O O   . CYS A 1 7   ? 2.671   -36.513 42.133 1.00 13.44 ? 67  CYS A O   1 
ATOM   56   C CB  . CYS A 1 7   ? 3.875   -33.780 41.376 1.00 15.85 ? 67  CYS A CB  1 
ATOM   57   S SG  . CYS A 1 7   ? 4.568   -33.972 39.719 1.00 17.03 ? 67  CYS A SG  1 
ATOM   58   N N   . ALA A 1 8   ? 1.602   -36.050 40.198 1.00 14.34 ? 68  ALA A N   1 
ATOM   59   C CA  . ALA A 1 8   ? 1.371   -37.447 39.784 1.00 17.01 ? 68  ALA A CA  1 
ATOM   60   C C   . ALA A 1 8   ? 2.702   -38.126 39.428 1.00 17.47 ? 68  ALA A C   1 
ATOM   61   O O   . ALA A 1 8   ? 2.795   -39.351 39.434 1.00 15.54 ? 68  ALA A O   1 
ATOM   62   C CB  . ALA A 1 8   ? 0.429   -37.489 38.595 1.00 13.29 ? 68  ALA A CB  1 
ATOM   63   N N   . LYS A 1 9   ? 3.684   -37.348 38.989 1.00 16.80 ? 69  LYS A N   1 
ATOM   64   C CA  . LYS A 1 9   ? 5.016   -37.882 38.686 1.00 17.86 ? 69  LYS A CA  1 
ATOM   65   C C   . LYS A 1 9   ? 5.817   -37.963 39.974 1.00 19.02 ? 69  LYS A C   1 
ATOM   66   O O   . LYS A 1 9   ? 6.419   -36.974 40.403 1.00 17.20 ? 69  LYS A O   1 
ATOM   67   C CB  . LYS A 1 9   ? 5.753   -36.979 37.700 1.00 17.58 ? 69  LYS A CB  1 
ATOM   68   C CG  . LYS A 1 9   ? 4.994   -36.631 36.431 1.00 24.60 ? 69  LYS A CG  1 
ATOM   69   C CD  . LYS A 1 9   ? 5.456   -37.464 35.249 1.00 30.71 ? 69  LYS A CD  1 
ATOM   70   C CE  . LYS A 1 9   ? 4.581   -37.225 34.022 1.00 29.42 ? 69  LYS A CE  1 
ATOM   71   N NZ  . LYS A 1 9   ? 4.265   -38.513 33.344 1.00 31.74 ? 69  LYS A NZ  1 
ATOM   72   N N   . ASP A 1 10  ? 5.800   -39.125 40.615 1.00 18.33 ? 70  ASP A N   1 
ATOM   73   C CA  . ASP A 1 10  ? 6.328   -39.241 41.971 1.00 18.01 ? 70  ASP A CA  1 
ATOM   74   C C   . ASP A 1 10  ? 7.786   -38.762 42.182 1.00 16.33 ? 70  ASP A C   1 
ATOM   75   O O   . ASP A 1 10  ? 8.076   -38.092 43.180 1.00 16.99 ? 70  ASP A O   1 
ATOM   76   C CB  . ASP A 1 10  ? 6.149   -40.689 42.472 1.00 20.85 ? 70  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 10  ? 5.967   -40.767 43.966 1.00 21.97 ? 70  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 10  ? 4.896   -40.313 44.469 1.00 22.79 ? 70  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 10  ? 6.869   -41.280 44.637 1.00 28.35 ? 70  ASP A OD2 1 
ATOM   80   N N   . PRO A 1 11  ? 8.713   -39.083 41.253 1.00 18.18 ? 71  PRO A N   1 
ATOM   81   C CA  . PRO A 1 11  ? 10.086  -38.576 41.435 1.00 18.60 ? 71  PRO A CA  1 
ATOM   82   C C   . PRO A 1 11  ? 10.165  -37.036 41.438 1.00 18.75 ? 71  PRO A C   1 
ATOM   83   O O   . PRO A 1 11  ? 11.219  -36.503 41.785 1.00 17.77 ? 71  PRO A O   1 
ATOM   84   C CB  . PRO A 1 11  ? 10.847  -39.139 40.222 1.00 17.24 ? 71  PRO A CB  1 
ATOM   85   C CG  . PRO A 1 11  ? 10.017  -40.292 39.762 1.00 22.54 ? 71  PRO A CG  1 
ATOM   86   C CD  . PRO A 1 11  ? 8.603   -39.924 40.051 1.00 19.80 ? 71  PRO A CD  1 
ATOM   87   N N   . TRP A 1 12  ? 9.143   -36.332 40.939 1.00 17.13 ? 72  TRP A N   1 
ATOM   88   C CA  . TRP A 1 12  ? 9.240   -34.863 40.845 1.00 14.91 ? 72  TRP A CA  1 
ATOM   89   C C   . TRP A 1 12  ? 8.627   -34.115 42.042 1.00 17.18 ? 72  TRP A C   1 
ATOM   90   O O   . TRP A 1 12  ? 8.652   -32.872 42.090 1.00 13.15 ? 72  TRP A O   1 
ATOM   91   C CB  . TRP A 1 12  ? 8.559   -34.384 39.564 1.00 12.86 ? 72  TRP A CB  1 
ATOM   92   C CG  . TRP A 1 12  ? 9.274   -34.861 38.322 1.00 13.58 ? 72  TRP A CG  1 
ATOM   93   C CD1 . TRP A 1 12  ? 10.462  -35.542 38.263 1.00 17.80 ? 72  TRP A CD1 1 
ATOM   94   C CD2 . TRP A 1 12  ? 8.854   -34.670 36.970 1.00 13.31 ? 72  TRP A CD2 1 
ATOM   95   N NE1 . TRP A 1 12  ? 10.791  -35.805 36.953 1.00 17.17 ? 72  TRP A NE1 1 
ATOM   96   C CE2 . TRP A 1 12  ? 9.827   -35.265 36.141 1.00 16.85 ? 72  TRP A CE2 1 
ATOM   97   C CE3 . TRP A 1 12  ? 7.757   -34.032 36.374 1.00 16.03 ? 72  TRP A CE3 1 
ATOM   98   C CZ2 . TRP A 1 12  ? 9.730   -35.256 34.758 1.00 17.89 ? 72  TRP A CZ2 1 
ATOM   99   C CZ3 . TRP A 1 12  ? 7.660   -34.029 35.002 1.00 17.02 ? 72  TRP A CZ3 1 
ATOM   100  C CH2 . TRP A 1 12  ? 8.640   -34.645 34.207 1.00 17.04 ? 72  TRP A CH2 1 
ATOM   101  N N   . ARG A 1 13  ? 8.023   -34.865 42.962 1.00 12.97 ? 73  ARG A N   1 
ATOM   102  C CA  . ARG A 1 13  ? 7.420   -34.300 44.171 1.00 13.91 ? 73  ARG A CA  1 
ATOM   103  C C   . ARG A 1 13  ? 8.508   -33.783 45.098 1.00 16.32 ? 73  ARG A C   1 
ATOM   104  O O   . ARG A 1 13  ? 9.610   -34.297 45.106 1.00 14.61 ? 73  ARG A O   1 
ATOM   105  C CB  . ARG A 1 13  ? 6.600   -35.369 44.894 1.00 17.49 ? 73  ARG A CB  1 
ATOM   106  C CG  . ARG A 1 13  ? 5.397   -35.908 44.130 1.00 12.93 ? 73  ARG A CG  1 
ATOM   107  C CD  . ARG A 1 13  ? 4.819   -37.051 44.966 1.00 16.33 ? 73  ARG A CD  1 
ATOM   108  N NE  . ARG A 1 13  ? 4.684   -36.654 46.368 1.00 17.67 ? 73  ARG A NE  1 
ATOM   109  C CZ  . ARG A 1 13  ? 4.740   -37.499 47.385 1.00 19.38 ? 73  ARG A CZ  1 
ATOM   110  N NH1 . ARG A 1 13  ? 4.616   -37.046 48.623 1.00 16.23 ? 73  ARG A NH1 1 
ATOM   111  N NH2 . ARG A 1 13  ? 4.889   -38.799 47.149 1.00 18.65 ? 73  ARG A NH2 1 
ATOM   112  N N   . LEU A 1 14  ? 8.179   -32.771 45.892 1.00 15.63 ? 74  LEU A N   1 
ATOM   113  C CA  . LEU A 1 14  ? 9.094   -32.218 46.885 1.00 13.65 ? 74  LEU A CA  1 
ATOM   114  C C   . LEU A 1 14  ? 8.342   -32.107 48.210 1.00 14.40 ? 74  LEU A C   1 
ATOM   115  O O   . LEU A 1 14  ? 7.846   -31.026 48.569 1.00 18.05 ? 74  LEU A O   1 
ATOM   116  C CB  . LEU A 1 14  ? 9.595   -30.842 46.430 1.00 14.67 ? 74  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 14  ? 10.416  -30.860 45.133 1.00 17.16 ? 74  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 14  ? 10.667  -29.436 44.653 1.00 16.79 ? 74  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 14  ? 11.747  -31.597 45.325 1.00 19.16 ? 74  LEU A CD2 1 
ATOM   120  N N   . PRO A 1 15  ? 8.149   -33.250 48.886 1.00 17.93 ? 75  PRO A N   1 
ATOM   121  C CA  . PRO A 1 15  ? 7.411   -33.318 50.154 1.00 21.74 ? 75  PRO A CA  1 
ATOM   122  C C   . PRO A 1 15  ? 8.016   -32.395 51.198 1.00 19.75 ? 75  PRO A C   1 
ATOM   123  O O   . PRO A 1 15  ? 9.209   -32.086 51.153 1.00 18.29 ? 75  PRO A O   1 
ATOM   124  C CB  . PRO A 1 15  ? 7.605   -34.770 50.612 1.00 18.86 ? 75  PRO A CB  1 
ATOM   125  C CG  . PRO A 1 15  ? 8.094   -35.505 49.440 1.00 21.22 ? 75  PRO A CG  1 
ATOM   126  C CD  . PRO A 1 15  ? 8.662   -34.560 48.452 1.00 16.49 ? 75  PRO A CD  1 
ATOM   127  N N   . GLY A 1 16  ? 7.195   -31.950 52.141 1.00 14.10 ? 76  GLY A N   1 
ATOM   128  C CA  . GLY A 1 16  ? 7.686   -31.099 53.209 1.00 19.68 ? 76  GLY A CA  1 
ATOM   129  C C   . GLY A 1 16  ? 7.510   -29.608 52.971 1.00 16.75 ? 76  GLY A C   1 
ATOM   130  O O   . GLY A 1 16  ? 7.744   -28.826 53.884 1.00 18.86 ? 76  GLY A O   1 
ATOM   131  N N   . THR A 1 17  ? 7.111   -29.214 51.758 1.00 14.44 ? 77  THR A N   1 
ATOM   132  C CA  . THR A 1 17  ? 6.762   -27.814 51.466 1.00 13.70 ? 77  THR A CA  1 
ATOM   133  C C   . THR A 1 17  ? 5.464   -27.773 50.687 1.00 14.89 ? 77  THR A C   1 
ATOM   134  O O   . THR A 1 17  ? 5.274   -28.553 49.758 1.00 14.84 ? 77  THR A O   1 
ATOM   135  C CB  . THR A 1 17  ? 7.865   -27.147 50.628 1.00 19.23 ? 77  THR A CB  1 
ATOM   136  O OG1 . THR A 1 17  ? 9.102   -27.189 51.356 1.00 22.45 ? 77  THR A OG1 1 
ATOM   137  C CG2 . THR A 1 17  ? 7.529   -25.685 50.362 1.00 20.81 ? 77  THR A CG2 1 
ATOM   138  N N   . TYR A 1 18  ? 4.553   -26.885 51.092 1.00 12.32 ? 78  TYR A N   1 
ATOM   139  C CA  . TYR A 1 18  ? 3.178   -26.834 50.585 1.00 13.04 ? 78  TYR A CA  1 
ATOM   140  C C   . TYR A 1 18  ? 2.792   -25.407 50.243 1.00 15.23 ? 78  TYR A C   1 
ATOM   141  O O   . TYR A 1 18  ? 3.106   -24.461 50.989 1.00 14.51 ? 78  TYR A O   1 
ATOM   142  C CB  . TYR A 1 18  ? 2.195   -27.406 51.633 1.00 15.13 ? 78  TYR A CB  1 
ATOM   143  C CG  . TYR A 1 18  ? 2.514   -28.869 51.929 1.00 17.05 ? 78  TYR A CG  1 
ATOM   144  C CD1 . TYR A 1 18  ? 1.957   -29.875 51.149 1.00 15.40 ? 78  TYR A CD1 1 
ATOM   145  C CD2 . TYR A 1 18  ? 3.400   -29.239 52.942 1.00 16.61 ? 78  TYR A CD2 1 
ATOM   146  C CE1 . TYR A 1 18  ? 2.271   -31.216 51.359 1.00 16.20 ? 78  TYR A CE1 1 
ATOM   147  C CE2 . TYR A 1 18  ? 3.712   -30.590 53.176 1.00 18.41 ? 78  TYR A CE2 1 
ATOM   148  C CZ  . TYR A 1 18  ? 3.139   -31.569 52.372 1.00 21.16 ? 78  TYR A CZ  1 
ATOM   149  O OH  . TYR A 1 18  ? 3.426   -32.919 52.577 1.00 23.80 ? 78  TYR A OH  1 
ATOM   150  N N   . VAL A 1 19  ? 2.102   -25.269 49.117 1.00 12.48 ? 79  VAL A N   1 
ATOM   151  C CA  . VAL A 1 19  ? 1.487   -24.021 48.721 1.00 14.34 ? 79  VAL A CA  1 
ATOM   152  C C   . VAL A 1 19  ? 0.047   -24.029 49.183 1.00 12.97 ? 79  VAL A C   1 
ATOM   153  O O   . VAL A 1 19  ? -0.742  -24.846 48.741 1.00 13.54 ? 79  VAL A O   1 
ATOM   154  C CB  . VAL A 1 19  ? 1.559   -23.788 47.189 1.00 14.00 ? 79  VAL A CB  1 
ATOM   155  C CG1 . VAL A 1 19  ? 0.915   -22.464 46.842 1.00 13.24 ? 79  VAL A CG1 1 
ATOM   156  C CG2 . VAL A 1 19  ? 2.988   -23.812 46.706 1.00 17.57 ? 79  VAL A CG2 1 
ATOM   157  N N   . VAL A 1 20  ? -0.289  -23.107 50.076 1.00 12.33 ? 80  VAL A N   1 
ATOM   158  C CA  . VAL A 1 20  ? -1.625  -23.035 50.643 1.00 12.40 ? 80  VAL A CA  1 
ATOM   159  C C   . VAL A 1 20  ? -2.362  -21.958 49.865 1.00 16.06 ? 80  VAL A C   1 
ATOM   160  O O   . VAL A 1 20  ? -1.979  -20.790 49.935 1.00 14.87 ? 80  VAL A O   1 
ATOM   161  C CB  . VAL A 1 20  ? -1.629  -22.757 52.168 1.00 13.97 ? 80  VAL A CB  1 
ATOM   162  C CG1 . VAL A 1 20  ? -3.074  -22.591 52.666 1.00 14.35 ? 80  VAL A CG1 1 
ATOM   163  C CG2 . VAL A 1 20  ? -0.916  -23.874 52.923 1.00 14.08 ? 80  VAL A CG2 1 
ATOM   164  N N   . VAL A 1 21  ? -3.370  -22.342 49.084 1.00 13.58 ? 81  VAL A N   1 
ATOM   165  C CA  . VAL A 1 21  ? -4.107  -21.394 48.234 1.00 12.73 ? 81  VAL A CA  1 
ATOM   166  C C   . VAL A 1 21  ? -5.449  -21.032 48.834 1.00 16.83 ? 81  VAL A C   1 
ATOM   167  O O   . VAL A 1 21  ? -6.274  -21.888 49.140 1.00 13.59 ? 81  VAL A O   1 
ATOM   168  C CB  . VAL A 1 21  ? -4.310  -21.942 46.803 1.00 13.36 ? 81  VAL A CB  1 
ATOM   169  C CG1 . VAL A 1 21  ? -5.043  -20.938 45.928 1.00 16.78 ? 81  VAL A CG1 1 
ATOM   170  C CG2 . VAL A 1 21  ? -2.953  -22.371 46.191 1.00 16.22 ? 81  VAL A CG2 1 
ATOM   171  N N   . LEU A 1 22  ? -5.651  -19.735 49.027 1.00 16.56 ? 82  LEU A N   1 
ATOM   172  C CA  . LEU A 1 22  ? -6.853  -19.261 49.686 1.00 16.08 ? 82  LEU A CA  1 
ATOM   173  C C   . LEU A 1 22  ? -7.870  -18.827 48.640 1.00 16.78 ? 82  LEU A C   1 
ATOM   174  O O   . LEU A 1 22  ? -7.532  -18.706 47.462 1.00 16.15 ? 82  LEU A O   1 
ATOM   175  C CB  . LEU A 1 22  ? -6.512  -18.137 50.679 1.00 16.43 ? 82  LEU A CB  1 
ATOM   176  C CG  . LEU A 1 22  ? -5.433  -18.507 51.725 1.00 16.13 ? 82  LEU A CG  1 
ATOM   177  C CD1 . LEU A 1 22  ? -5.148  -17.373 52.707 1.00 17.60 ? 82  LEU A CD1 1 
ATOM   178  C CD2 . LEU A 1 22  ? -5.702  -19.805 52.474 1.00 18.78 ? 82  LEU A CD2 1 
ATOM   179  N N   . LYS A 1 23  ? -9.115  -18.600 49.057 1.00 17.43 ? 83  LYS A N   1 
ATOM   180  C CA  . LYS A 1 23  ? -10.188 -18.294 48.119 1.00 18.86 ? 83  LYS A CA  1 
ATOM   181  C C   . LYS A 1 23  ? -9.924  -16.955 47.456 1.00 21.99 ? 83  LYS A C   1 
ATOM   182  O O   . LYS A 1 23  ? -9.334  -16.089 48.073 1.00 20.92 ? 83  LYS A O   1 
ATOM   183  C CB  . LYS A 1 23  ? -11.548 -18.287 48.809 1.00 22.72 ? 83  LYS A CB  1 
ATOM   184  C CG  . LYS A 1 23  ? -12.008 -19.643 49.263 1.00 26.35 ? 83  LYS A CG  1 
ATOM   185  C CD  . LYS A 1 23  ? -13.063 -19.485 50.328 1.00 32.74 ? 83  LYS A CD  1 
ATOM   186  C CE  . LYS A 1 23  ? -13.565 -20.844 50.712 1.00 34.92 ? 83  LYS A CE  1 
ATOM   187  N NZ  . LYS A 1 23  ? -13.588 -21.636 49.450 1.00 35.71 ? 83  LYS A NZ  1 
ATOM   188  N N   . GLU A 1 24  ? -10.374 -16.810 46.210 1.00 25.61 ? 84  GLU A N   1 
ATOM   189  C CA  . GLU A 1 24  ? -10.018 -15.685 45.334 1.00 29.92 ? 84  GLU A CA  1 
ATOM   190  C C   . GLU A 1 24  ? -9.988  -14.284 45.966 1.00 26.43 ? 84  GLU A C   1 
ATOM   191  O O   . GLU A 1 24  ? -9.061  -13.527 45.706 1.00 32.94 ? 84  GLU A O   1 
ATOM   192  C CB  . GLU A 1 24  ? -11.006 -15.662 44.166 1.00 32.93 ? 84  GLU A CB  1 
ATOM   193  C CG  . GLU A 1 24  ? -10.786 -14.541 43.176 1.00 42.46 ? 84  GLU A CG  1 
ATOM   194  C CD  . GLU A 1 24  ? -11.284 -14.906 41.796 1.00 51.32 ? 84  GLU A CD  1 
ATOM   195  O OE1 . GLU A 1 24  ? -11.841 -14.023 41.101 1.00 59.31 ? 84  GLU A OE1 1 
ATOM   196  O OE2 . GLU A 1 24  ? -11.110 -16.078 41.400 1.00 54.35 ? 84  GLU A OE2 1 
ATOM   197  N N   . GLU A 1 25  ? -11.005 -13.898 46.729 1.00 31.64 ? 85  GLU A N   1 
ATOM   198  C CA  . GLU A 1 25  ? -11.036 -12.498 47.202 1.00 31.35 ? 85  GLU A CA  1 
ATOM   199  C C   . GLU A 1 25  ? -10.348 -12.321 48.538 1.00 30.79 ? 85  GLU A C   1 
ATOM   200  O O   . GLU A 1 25  ? -10.417 -11.253 49.131 1.00 33.21 ? 85  GLU A O   1 
ATOM   201  C CB  . GLU A 1 25  ? -12.447 -11.921 47.239 1.00 38.02 ? 85  GLU A CB  1 
ATOM   202  C CG  . GLU A 1 25  ? -13.110 -11.767 45.890 1.00 44.46 ? 85  GLU A CG  1 
ATOM   203  C CD  . GLU A 1 25  ? -14.586 -12.016 45.971 1.00 54.90 ? 85  GLU A CD  1 
ATOM   204  O OE1 . GLU A 1 25  ? -15.206 -11.438 46.894 1.00 57.09 ? 85  GLU A OE1 1 
ATOM   205  O OE2 . GLU A 1 25  ? -15.127 -12.762 45.125 1.00 62.96 ? 85  GLU A OE2 1 
ATOM   206  N N   . THR A 1 26  ? -9.699  -13.361 49.038 1.00 21.37 ? 86  THR A N   1 
ATOM   207  C CA  . THR A 1 26  ? -9.019  -13.230 50.312 1.00 22.17 ? 86  THR A CA  1 
ATOM   208  C C   . THR A 1 26  ? -7.972  -12.121 50.270 1.00 19.99 ? 86  THR A C   1 
ATOM   209  O O   . THR A 1 26  ? -7.181  -12.037 49.336 1.00 18.91 ? 86  THR A O   1 
ATOM   210  C CB  . THR A 1 26  ? -8.342  -14.555 50.731 1.00 22.35 ? 86  THR A CB  1 
ATOM   211  O OG1 . THR A 1 26  ? -9.305  -15.621 50.677 1.00 21.47 ? 86  THR A OG1 1 
ATOM   212  C CG2 . THR A 1 26  ? -7.765  -14.439 52.121 1.00 20.00 ? 86  THR A CG2 1 
ATOM   213  N N   . HIS A 1 27  ? -7.972  -11.284 51.306 1.00 20.84 ? 87  HIS A N   1 
ATOM   214  C CA  . HIS A 1 27  ? -7.080  -10.136 51.407 1.00 21.30 ? 87  HIS A CA  1 
ATOM   215  C C   . HIS A 1 27  ? -5.763  -10.523 52.052 1.00 20.38 ? 87  HIS A C   1 
ATOM   216  O O   . HIS A 1 27  ? -5.693  -11.471 52.825 1.00 16.27 ? 87  HIS A O   1 
ATOM   217  C CB  . HIS A 1 27  ? -7.742  -9.013  52.233 1.00 23.39 ? 87  HIS A CB  1 
ATOM   218  C CG  . HIS A 1 27  ? -6.988  -7.721  52.188 1.00 20.47 ? 87  HIS A CG  1 
ATOM   219  N ND1 . HIS A 1 27  ? -5.944  -7.458  53.050 1.00 21.95 ? 87  HIS A ND1 1 
ATOM   220  C CD2 . HIS A 1 27  ? -7.047  -6.664  51.339 1.00 21.58 ? 87  HIS A CD2 1 
ATOM   221  C CE1 . HIS A 1 27  ? -5.411  -6.282  52.765 1.00 16.66 ? 87  HIS A CE1 1 
ATOM   222  N NE2 . HIS A 1 27  ? -6.056  -5.782  51.723 1.00 19.72 ? 87  HIS A NE2 1 
ATOM   223  N N   . LEU A 1 28  ? -4.699  -9.832  51.642 1.00 14.15 ? 88  LEU A N   1 
ATOM   224  C CA  . LEU A 1 28  ? -3.358  -10.054 52.186 1.00 16.68 ? 88  LEU A CA  1 
ATOM   225  C C   . LEU A 1 28  ? -3.370  -10.119 53.717 1.00 19.50 ? 88  LEU A C   1 
ATOM   226  O O   . LEU A 1 28  ? -2.685  -10.956 54.304 1.00 13.27 ? 88  LEU A O   1 
ATOM   227  C CB  . LEU A 1 28  ? -2.393  -8.951  51.717 1.00 17.78 ? 88  LEU A CB  1 
ATOM   228  C CG  . LEU A 1 28  ? -0.973  -9.043  52.285 1.00 17.40 ? 88  LEU A CG  1 
ATOM   229  C CD1 . LEU A 1 28  ? -0.373  -10.435 52.030 1.00 14.84 ? 88  LEU A CD1 1 
ATOM   230  C CD2 . LEU A 1 28  ? -0.075  -7.982  51.684 1.00 18.12 ? 88  LEU A CD2 1 
ATOM   231  N N   . SER A 1 29  ? -4.107  -9.212  54.368 1.00 15.88 ? 89  SER A N   1 
ATOM   232  C CA  . SER A 1 29  ? -4.168  -9.226  55.832 1.00 19.76 ? 89  SER A CA  1 
ATOM   233  C C   . SER A 1 29  ? -4.726  -10.570 56.321 1.00 16.55 ? 89  SER A C   1 
ATOM   234  O O   . SER A 1 29  ? -4.271  -11.114 57.317 1.00 17.99 ? 89  SER A O   1 
ATOM   235  C CB  . SER A 1 29  ? -5.053  -8.088  56.365 1.00 19.97 ? 89  SER A CB  1 
ATOM   236  O OG  . SER A 1 29  ? -4.342  -6.850  56.286 1.00 21.13 ? 89  SER A OG  1 
ATOM   237  N N   . GLN A 1 30  ? -5.718  -11.087 55.618 1.00 16.23 ? 90  GLN A N   1 
ATOM   238  C CA  . GLN A 1 30  ? -6.295  -12.377 55.984 1.00 18.58 ? 90  GLN A CA  1 
ATOM   239  C C   . GLN A 1 30  ? -5.332  -13.542 55.720 1.00 20.13 ? 90  GLN A C   1 
ATOM   240  O O   . GLN A 1 30  ? -5.261  -14.490 56.513 1.00 22.18 ? 90  GLN A O   1 
ATOM   241  C CB  . GLN A 1 30  ? -7.613  -12.604 55.251 1.00 21.83 ? 90  GLN A CB  1 
ATOM   242  C CG  . GLN A 1 30  ? -8.697  -11.602 55.594 1.00 31.07 ? 90  GLN A CG  1 
ATOM   243  C CD  . GLN A 1 30  ? -9.910  -11.692 54.672 1.00 31.31 ? 90  GLN A CD  1 
ATOM   244  O OE1 . GLN A 1 30  ? -9.804  -11.566 53.447 1.00 27.11 ? 90  GLN A OE1 1 
ATOM   245  N NE2 . GLN A 1 30  ? -11.079 -11.937 55.268 1.00 39.06 ? 90  GLN A NE2 1 
ATOM   246  N N   . SER A 1 31  ? -4.584  -13.473 54.614 1.00 15.87 ? 91  SER A N   1 
ATOM   247  C CA  . SER A 1 31  ? -3.596  -14.511 54.312 1.00 17.87 ? 91  SER A CA  1 
ATOM   248  C C   . SER A 1 31  ? -2.544  -14.599 55.401 1.00 18.82 ? 91  SER A C   1 
ATOM   249  O O   . SER A 1 31  ? -2.183  -15.693 55.834 1.00 17.00 ? 91  SER A O   1 
ATOM   250  C CB  . SER A 1 31  ? -2.926  -14.303 52.949 1.00 16.22 ? 91  SER A CB  1 
ATOM   251  O OG  . SER A 1 31  ? -3.888  -14.247 51.915 1.00 17.59 ? 91  SER A OG  1 
ATOM   252  N N   . GLU A 1 32  ? -2.067  -13.444 55.860 1.00 14.48 ? 92  GLU A N   1 
ATOM   253  C CA  . GLU A 1 32  ? -1.063  -13.397 56.913 1.00 16.10 ? 92  GLU A CA  1 
ATOM   254  C C   . GLU A 1 32  ? -1.601  -13.989 58.228 1.00 17.84 ? 92  GLU A C   1 
ATOM   255  O O   . GLU A 1 32  ? -0.899  -14.707 58.921 1.00 21.95 ? 92  GLU A O   1 
ATOM   256  C CB  . GLU A 1 32  ? -0.612  -11.928 57.121 1.00 20.68 ? 92  GLU A CB  1 
ATOM   257  C CG  . GLU A 1 32  ? 0.217   -11.383 55.974 1.00 19.03 ? 92  GLU A CG  1 
ATOM   258  C CD  . GLU A 1 32  ? 0.521   -9.896  56.095 1.00 22.74 ? 92  GLU A CD  1 
ATOM   259  O OE1 . GLU A 1 32  ? -0.118  -9.193  56.921 1.00 21.33 ? 92  GLU A OE1 1 
ATOM   260  O OE2 . GLU A 1 32  ? 1.390   -9.415  55.329 1.00 23.98 ? 92  GLU A OE2 1 
ATOM   261  N N   . ARG A 1 33  ? -2.831  -13.634 58.589 1.00 17.43 ? 93  ARG A N   1 
ATOM   262  C CA  . ARG A 1 33  ? -3.473  -14.171 59.795 1.00 22.16 ? 93  ARG A CA  1 
ATOM   263  C C   . ARG A 1 33  ? -3.690  -15.687 59.720 1.00 20.23 ? 93  ARG A C   1 
ATOM   264  O O   . ARG A 1 33  ? -3.491  -16.406 60.700 1.00 19.30 ? 93  ARG A O   1 
ATOM   265  C CB  . ARG A 1 33  ? -4.805  -13.473 60.011 1.00 22.10 ? 93  ARG A CB  1 
ATOM   266  C CG  . ARG A 1 33  ? -4.594  -12.069 60.550 1.00 30.13 ? 93  ARG A CG  1 
ATOM   267  C CD  . ARG A 1 33  ? -5.884  -11.297 60.498 1.00 32.44 ? 93  ARG A CD  1 
ATOM   268  N NE  . ARG A 1 33  ? -5.550  -9.883  60.376 1.00 42.55 ? 93  ARG A NE  1 
ATOM   269  C CZ  . ARG A 1 33  ? -6.355  -8.985  59.822 1.00 42.23 ? 93  ARG A CZ  1 
ATOM   270  N NH1 . ARG A 1 33  ? -7.504  -9.387  59.266 1.00 38.68 ? 93  ARG A NH1 1 
ATOM   271  N NH2 . ARG A 1 33  ? -5.980  -7.708  59.753 1.00 40.70 ? 93  ARG A NH2 1 
ATOM   272  N N   . THR A 1 34  ? -4.062  -16.165 58.539 1.00 18.82 ? 94  THR A N   1 
ATOM   273  C CA  . THR A 1 34  ? -4.232  -17.605 58.343 1.00 18.65 ? 94  THR A CA  1 
ATOM   274  C C   . THR A 1 34  ? -2.893  -18.359 58.490 1.00 17.41 ? 94  THR A C   1 
ATOM   275  O O   . THR A 1 34  ? -2.812  -19.437 59.107 1.00 18.82 ? 94  THR A O   1 
ATOM   276  C CB  . THR A 1 34  ? -4.923  -17.923 56.991 1.00 19.39 ? 94  THR A CB  1 
ATOM   277  O OG1 . THR A 1 34  ? -6.163  -17.225 56.884 1.00 20.71 ? 94  THR A OG1 1 
ATOM   278  C CG2 . THR A 1 34  ? -5.111  -19.454 56.786 1.00 15.98 ? 94  THR A CG2 1 
ATOM   279  N N   . ALA A 1 35  ? -1.826  -17.780 57.943 1.00 15.48 ? 95  ALA A N   1 
ATOM   280  C CA  . ALA A 1 35  ? -0.493  -18.351 58.126 1.00 17.86 ? 95  ALA A CA  1 
ATOM   281  C C   . ALA A 1 35  ? -0.070  -18.427 59.597 1.00 20.39 ? 95  ALA A C   1 
ATOM   282  O O   . ALA A 1 35  ? 0.474   -19.441 60.032 1.00 18.36 ? 95  ALA A O   1 
ATOM   283  C CB  . ALA A 1 35  ? 0.537   -17.580 57.323 1.00 18.32 ? 95  ALA A CB  1 
ATOM   284  N N   . ARG A 1 36  ? -0.277  -17.346 60.353 1.00 20.52 ? 96  ARG A N   1 
ATOM   285  C CA  . ARG A 1 36  ? 0.074   -17.309 61.785 1.00 22.22 ? 96  ARG A CA  1 
ATOM   286  C C   . ARG A 1 36  ? -0.761  -18.341 62.532 1.00 18.68 ? 96  ARG A C   1 
ATOM   287  O O   . ARG A 1 36  ? -0.263  -19.004 63.437 1.00 22.84 ? 96  ARG A O   1 
ATOM   288  C CB  . ARG A 1 36  ? -0.176  -15.914 62.393 1.00 22.86 ? 96  ARG A CB  1 
ATOM   289  C CG  . ARG A 1 36  ? 0.598   -14.742 61.778 1.00 30.58 ? 96  ARG A CG  1 
ATOM   290  C CD  . ARG A 1 36  ? 1.953   -15.172 61.215 1.00 38.03 ? 96  ARG A CD  1 
ATOM   291  N NE  . ARG A 1 36  ? 2.337   -14.475 59.982 1.00 42.62 ? 96  ARG A NE  1 
ATOM   292  C CZ  . ARG A 1 36  ? 3.457   -14.721 59.303 1.00 45.78 ? 96  ARG A CZ  1 
ATOM   293  N NH1 . ARG A 1 36  ? 4.320   -15.636 59.743 1.00 42.56 ? 96  ARG A NH1 1 
ATOM   294  N NH2 . ARG A 1 36  ? 3.716   -14.052 58.187 1.00 46.43 ? 96  ARG A NH2 1 
ATOM   295  N N   . ARG A 1 37  ? -2.027  -18.456 62.153 1.00 19.22 ? 97  ARG A N   1 
ATOM   296  C CA  . ARG A 1 37  ? -2.933  -19.428 62.783 1.00 20.84 ? 97  ARG A CA  1 
ATOM   297  C C   . ARG A 1 37  ? -2.460  -20.881 62.606 1.00 22.10 ? 97  ARG A C   1 
ATOM   298  O O   . ARG A 1 37  ? -2.412  -21.654 63.569 1.00 22.22 ? 97  ARG A O   1 
ATOM   299  C CB  . ARG A 1 37  ? -4.321  -19.254 62.219 1.00 22.78 ? 97  ARG A CB  1 
ATOM   300  C CG  . ARG A 1 37  ? -5.358  -20.115 62.848 1.00 27.28 ? 97  ARG A CG  1 
ATOM   301  C CD  . ARG A 1 37  ? -6.682  -19.797 62.201 1.00 35.07 ? 97  ARG A CD  1 
ATOM   302  N NE  . ARG A 1 37  ? -7.729  -20.731 62.609 1.00 43.44 ? 97  ARG A NE  1 
ATOM   303  C CZ  . ARG A 1 37  ? -8.543  -20.539 63.639 1.00 45.66 ? 97  ARG A CZ  1 
ATOM   304  N NH1 . ARG A 1 37  ? -8.456  -19.423 64.353 1.00 42.98 ? 97  ARG A NH1 1 
ATOM   305  N NH2 . ARG A 1 37  ? -9.459  -21.455 63.938 1.00 42.73 ? 97  ARG A NH2 1 
ATOM   306  N N   . LEU A 1 38  ? -2.108  -21.242 61.373 1.00 18.88 ? 98  LEU A N   1 
ATOM   307  C CA  . LEU A 1 38  ? -1.503  -22.553 61.095 1.00 20.25 ? 98  LEU A CA  1 
ATOM   308  C C   . LEU A 1 38  ? -0.285  -22.790 61.986 1.00 22.31 ? 98  LEU A C   1 
ATOM   309  O O   . LEU A 1 38  ? -0.152  -23.838 62.604 1.00 22.07 ? 98  LEU A O   1 
ATOM   310  C CB  . LEU A 1 38  ? -1.093  -22.654 59.628 1.00 20.03 ? 98  LEU A CB  1 
ATOM   311  C CG  . LEU A 1 38  ? -0.394  -23.954 59.216 1.00 21.30 ? 98  LEU A CG  1 
ATOM   312  C CD1 . LEU A 1 38  ? -1.211  -25.172 59.656 1.00 19.61 ? 98  LEU A CD1 1 
ATOM   313  C CD2 . LEU A 1 38  ? -0.137  -23.985 57.716 1.00 18.45 ? 98  LEU A CD2 1 
ATOM   314  N N   . GLN A 1 39  ? 0.601   -21.805 62.069 1.00 20.12 ? 99  GLN A N   1 
ATOM   315  C CA  . GLN A 1 39  ? 1.824   -21.983 62.840 1.00 20.86 ? 99  GLN A CA  1 
ATOM   316  C C   . GLN A 1 39  ? 1.541   -22.187 64.328 1.00 23.03 ? 99  GLN A C   1 
ATOM   317  O O   . GLN A 1 39  ? 2.236   -22.956 65.000 1.00 22.58 ? 99  GLN A O   1 
ATOM   318  C CB  . GLN A 1 39  ? 2.723   -20.760 62.706 1.00 23.78 ? 99  GLN A CB  1 
ATOM   319  C CG  . GLN A 1 39  ? 3.314   -20.545 61.349 1.00 25.32 ? 99  GLN A CG  1 
ATOM   320  C CD  . GLN A 1 39  ? 4.568   -19.703 61.419 1.00 26.14 ? 99  GLN A CD  1 
ATOM   321  O OE1 . GLN A 1 39  ? 4.503   -18.487 61.580 1.00 26.13 ? 99  GLN A OE1 1 
ATOM   322  N NE2 . GLN A 1 39  ? 5.720   -20.352 61.348 1.00 28.08 ? 99  GLN A NE2 1 
ATOM   323  N N   . ALA A 1 40  ? 0.530   -21.483 64.832 1.00 23.02 ? 100 ALA A N   1 
ATOM   324  C CA  . ALA A 1 40  ? 0.116   -21.599 66.226 1.00 26.11 ? 100 ALA A CA  1 
ATOM   325  C C   . ALA A 1 40  ? -0.509  -22.978 66.493 1.00 27.01 ? 100 ALA A C   1 
ATOM   326  O O   . ALA A 1 40  ? -0.128  -23.667 67.436 1.00 25.87 ? 100 ALA A O   1 
ATOM   327  C CB  . ALA A 1 40  ? -0.887  -20.487 66.585 1.00 23.21 ? 100 ALA A CB  1 
ATOM   328  N N   . GLN A 1 41  ? -1.446  -23.384 65.636 1.00 22.33 ? 101 GLN A N   1 
ATOM   329  C CA  . GLN A 1 41  ? -2.091  -24.684 65.766 1.00 26.79 ? 101 GLN A CA  1 
ATOM   330  C C   . GLN A 1 41  ? -1.116  -25.847 65.634 1.00 26.23 ? 101 GLN A C   1 
ATOM   331  O O   . GLN A 1 41  ? -1.253  -26.863 66.322 1.00 29.53 ? 101 GLN A O   1 
ATOM   332  C CB  . GLN A 1 41  ? -3.203  -24.819 64.735 1.00 26.97 ? 101 GLN A CB  1 
ATOM   333  C CG  . GLN A 1 41  ? -4.422  -23.967 65.026 1.00 28.25 ? 101 GLN A CG  1 
ATOM   334  C CD  . GLN A 1 41  ? -5.489  -24.126 63.976 1.00 31.81 ? 101 GLN A CD  1 
ATOM   335  O OE1 . GLN A 1 41  ? -5.289  -24.818 62.980 1.00 36.44 ? 101 GLN A OE1 1 
ATOM   336  N NE2 . GLN A 1 41  ? -6.628  -23.471 64.174 1.00 34.65 ? 101 GLN A NE2 1 
ATOM   337  N N   . ALA A 1 42  ? -0.143  -25.695 64.739 1.00 19.64 ? 102 ALA A N   1 
ATOM   338  C CA  . ALA A 1 42  ? 0.932   -26.665 64.574 1.00 24.06 ? 102 ALA A CA  1 
ATOM   339  C C   . ALA A 1 42  ? 1.821   -26.758 65.814 1.00 27.81 ? 102 ALA A C   1 
ATOM   340  O O   . ALA A 1 42  ? 2.111   -27.858 66.289 1.00 26.80 ? 102 ALA A O   1 
ATOM   341  C CB  . ALA A 1 42  ? 1.767   -26.332 63.337 1.00 21.13 ? 102 ALA A CB  1 
ATOM   342  N N   . ALA A 1 43  ? 2.298   -25.607 66.299 1.00 25.82 ? 103 ALA A N   1 
ATOM   343  C CA  . ALA A 1 43  ? 3.162   -25.561 67.487 1.00 27.65 ? 103 ALA A CA  1 
ATOM   344  C C   . ALA A 1 43  ? 2.529   -26.224 68.711 1.00 26.70 ? 103 ALA A C   1 
ATOM   345  O O   . ALA A 1 43  ? 3.208   -26.900 69.463 1.00 34.03 ? 103 ALA A O   1 
ATOM   346  C CB  . ALA A 1 43  ? 3.523   -24.123 67.832 1.00 25.44 ? 103 ALA A CB  1 
ATOM   347  N N   . ARG A 1 44  ? 1.227   -26.064 68.885 1.00 26.79 ? 104 ARG A N   1 
ATOM   348  C CA  . ARG A 1 44  ? 0.519   -26.681 70.005 1.00 30.25 ? 104 ARG A CA  1 
ATOM   349  C C   . ARG A 1 44  ? 0.510   -28.214 69.869 1.00 35.37 ? 104 ARG A C   1 
ATOM   350  O O   . ARG A 1 44  ? 0.275   -28.947 70.836 1.00 27.89 ? 104 ARG A O   1 
ATOM   351  C CB  . ARG A 1 44  ? -0.916  -26.151 70.087 1.00 34.29 ? 104 ARG A CB  1 
ATOM   352  C CG  . ARG A 1 44  ? -0.949  -24.689 70.577 1.00 36.50 ? 104 ARG A CG  1 
ATOM   353  C CD  . ARG A 1 44  ? -2.335  -24.211 70.997 1.00 39.80 ? 104 ARG A CD  1 
ATOM   354  N NE  . ARG A 1 44  ? -3.266  -24.136 69.878 1.00 45.02 ? 104 ARG A NE  1 
ATOM   355  C CZ  . ARG A 1 44  ? -4.256  -25.000 69.668 1.00 50.29 ? 104 ARG A CZ  1 
ATOM   356  N NH1 . ARG A 1 44  ? -4.459  -26.001 70.522 1.00 47.98 ? 104 ARG A NH1 1 
ATOM   357  N NH2 . ARG A 1 44  ? -5.060  -24.848 68.618 1.00 45.19 ? 104 ARG A NH2 1 
ATOM   358  N N   . ARG A 1 45  ? 0.699   -28.683 68.643 1.00 28.30 ? 105 ARG A N   1 
ATOM   359  C CA  . ARG A 1 45  ? 0.756   -30.101 68.366 1.00 28.55 ? 105 ARG A CA  1 
ATOM   360  C C   . ARG A 1 45  ? 2.193   -30.616 68.335 1.00 26.82 ? 105 ARG A C   1 
ATOM   361  O O   . ARG A 1 45  ? 2.433   -31.781 68.070 1.00 29.41 ? 105 ARG A O   1 
ATOM   362  C CB  . ARG A 1 45  ? 0.056   -30.382 67.051 1.00 29.24 ? 105 ARG A CB  1 
ATOM   363  C CG  . ARG A 1 45  ? -1.420  -30.113 67.075 1.00 32.44 ? 105 ARG A CG  1 
ATOM   364  C CD  . ARG A 1 45  ? -1.975  -30.665 65.799 1.00 37.69 ? 105 ARG A CD  1 
ATOM   365  N NE  . ARG A 1 45  ? -3.409  -30.470 65.630 1.00 42.18 ? 105 ARG A NE  1 
ATOM   366  C CZ  . ARG A 1 45  ? -4.165  -31.309 64.930 1.00 45.33 ? 105 ARG A CZ  1 
ATOM   367  N NH1 . ARG A 1 45  ? -3.589  -32.340 64.319 1.00 46.99 ? 105 ARG A NH1 1 
ATOM   368  N NH2 . ARG A 1 45  ? -5.466  -31.099 64.789 1.00 46.13 ? 105 ARG A NH2 1 
ATOM   369  N N   . GLY A 1 46  ? 3.143   -29.742 68.654 1.00 25.69 ? 106 GLY A N   1 
ATOM   370  C CA  . GLY A 1 46  ? 4.547   -30.101 68.703 1.00 26.83 ? 106 GLY A CA  1 
ATOM   371  C C   . GLY A 1 46  ? 5.301   -29.995 67.385 1.00 29.43 ? 106 GLY A C   1 
ATOM   372  O O   . GLY A 1 46  ? 6.400   -30.524 67.268 1.00 28.07 ? 106 GLY A O   1 
ATOM   373  N N   . TYR A 1 47  ? 4.719   -29.325 66.393 1.00 28.15 ? 107 TYR A N   1 
ATOM   374  C CA  . TYR A 1 47  ? 5.344   -29.228 65.075 1.00 26.77 ? 107 TYR A CA  1 
ATOM   375  C C   . TYR A 1 47  ? 5.954   -27.845 64.809 1.00 22.69 ? 107 TYR A C   1 
ATOM   376  O O   . TYR A 1 47  ? 5.285   -26.834 64.994 1.00 27.46 ? 107 TYR A O   1 
ATOM   377  C CB  . TYR A 1 47  ? 4.286   -29.501 63.999 1.00 25.21 ? 107 TYR A CB  1 
ATOM   378  C CG  . TYR A 1 47  ? 3.867   -30.952 63.873 1.00 24.77 ? 107 TYR A CG  1 
ATOM   379  C CD1 . TYR A 1 47  ? 2.780   -31.441 64.588 1.00 24.92 ? 107 TYR A CD1 1 
ATOM   380  C CD2 . TYR A 1 47  ? 4.554   -31.830 63.041 1.00 21.55 ? 107 TYR A CD2 1 
ATOM   381  C CE1 . TYR A 1 47  ? 2.378   -32.774 64.476 1.00 25.17 ? 107 TYR A CE1 1 
ATOM   382  C CE2 . TYR A 1 47  ? 4.163   -33.160 62.919 1.00 24.74 ? 107 TYR A CE2 1 
ATOM   383  C CZ  . TYR A 1 47  ? 3.079   -33.621 63.639 1.00 26.92 ? 107 TYR A CZ  1 
ATOM   384  O OH  . TYR A 1 47  ? 2.680   -34.938 63.521 1.00 25.91 ? 107 TYR A OH  1 
ATOM   385  N N   . LEU A 1 48  ? 7.197   -27.801 64.348 1.00 25.41 ? 108 LEU A N   1 
ATOM   386  C CA  . LEU A 1 48  ? 7.793   -26.561 63.831 1.00 26.18 ? 108 LEU A CA  1 
ATOM   387  C C   . LEU A 1 48  ? 7.293   -26.307 62.408 1.00 25.98 ? 108 LEU A C   1 
ATOM   388  O O   . LEU A 1 48  ? 7.120   -27.229 61.611 1.00 27.06 ? 108 LEU A O   1 
ATOM   389  C CB  . LEU A 1 48  ? 9.311   -26.643 63.843 1.00 31.79 ? 108 LEU A CB  1 
ATOM   390  C CG  . LEU A 1 48  ? 9.842   -26.667 65.280 1.00 38.27 ? 108 LEU A CG  1 
ATOM   391  C CD1 . LEU A 1 48  ? 11.226  -27.304 65.366 1.00 42.35 ? 108 LEU A CD1 1 
ATOM   392  C CD2 . LEU A 1 48  ? 9.850   -25.248 65.848 1.00 38.70 ? 108 LEU A CD2 1 
ATOM   393  N N   . THR A 1 49  ? 7.008   -25.054 62.100 1.00 21.82 ? 109 THR A N   1 
ATOM   394  C CA  . THR A 1 49  ? 6.664   -24.686 60.738 1.00 20.04 ? 109 THR A CA  1 
ATOM   395  C C   . THR A 1 49  ? 7.442   -23.456 60.352 1.00 23.72 ? 109 THR A C   1 
ATOM   396  O O   . THR A 1 49  ? 7.851   -22.688 61.215 1.00 25.55 ? 109 THR A O   1 
ATOM   397  C CB  . THR A 1 49  ? 5.176   -24.419 60.575 1.00 22.36 ? 109 THR A CB  1 
ATOM   398  O OG1 . THR A 1 49  ? 4.784   -23.409 61.501 1.00 22.74 ? 109 THR A OG1 1 
ATOM   399  C CG2 . THR A 1 49  ? 4.357   -25.703 60.823 1.00 20.62 ? 109 THR A CG2 1 
ATOM   400  N N   . LYS A 1 50  ? 7.565   -23.218 59.056 1.00 19.78 ? 110 LYS A N   1 
ATOM   401  C CA  . LYS A 1 50  ? 8.192   -22.002 58.557 1.00 20.32 ? 110 LYS A CA  1 
ATOM   402  C C   . LYS A 1 50  ? 7.383   -21.470 57.399 1.00 20.38 ? 110 LYS A C   1 
ATOM   403  O O   . LYS A 1 50  ? 7.156   -22.167 56.411 1.00 19.15 ? 110 LYS A O   1 
ATOM   404  C CB  . LYS A 1 50  ? 9.631   -22.308 58.113 1.00 24.11 ? 110 LYS A CB  1 
ATOM   405  C CG  . LYS A 1 50  ? 10.593  -21.110 58.135 1.00 29.20 ? 110 LYS A CG  1 
ATOM   406  C CD  . LYS A 1 50  ? 12.024  -21.562 57.835 1.00 34.04 ? 110 LYS A CD  1 
ATOM   407  C CE  . LYS A 1 50  ? 12.751  -20.598 56.915 1.00 47.69 ? 110 LYS A CE  1 
ATOM   408  N NZ  . LYS A 1 50  ? 13.969  -21.211 56.289 1.00 46.26 ? 110 LYS A NZ  1 
ATOM   409  N N   . ILE A 1 51  ? 6.973   -20.210 57.518 1.00 18.10 ? 111 ILE A N   1 
ATOM   410  C CA  . ILE A 1 51  ? 6.277   -19.518 56.443 1.00 17.17 ? 111 ILE A CA  1 
ATOM   411  C C   . ILE A 1 51  ? 7.324   -18.897 55.556 1.00 20.18 ? 111 ILE A C   1 
ATOM   412  O O   . ILE A 1 51  ? 7.940   -17.893 55.917 1.00 18.66 ? 111 ILE A O   1 
ATOM   413  C CB  . ILE A 1 51  ? 5.281   -18.463 56.982 1.00 21.52 ? 111 ILE A CB  1 
ATOM   414  C CG1 . ILE A 1 51  ? 4.332   -19.138 57.974 1.00 21.80 ? 111 ILE A CG1 1 
ATOM   415  C CG2 . ILE A 1 51  ? 4.468   -17.815 55.857 1.00 19.42 ? 111 ILE A CG2 1 
ATOM   416  C CD1 . ILE A 1 51  ? 3.380   -20.179 57.359 1.00 19.95 ? 111 ILE A CD1 1 
ATOM   417  N N   . LEU A 1 52  ? 7.511   -19.499 54.382 1.00 16.26 ? 112 LEU A N   1 
ATOM   418  C CA  . LEU A 1 52  ? 8.546   -19.056 53.452 1.00 15.67 ? 112 LEU A CA  1 
ATOM   419  C C   . LEU A 1 52  ? 8.173   -17.815 52.634 1.00 17.10 ? 112 LEU A C   1 
ATOM   420  O O   . LEU A 1 52  ? 9.057   -17.066 52.228 1.00 18.18 ? 112 LEU A O   1 
ATOM   421  C CB  . LEU A 1 52  ? 8.912   -20.209 52.501 1.00 17.96 ? 112 LEU A CB  1 
ATOM   422  C CG  . LEU A 1 52  ? 9.332   -21.530 53.166 1.00 18.35 ? 112 LEU A CG  1 
ATOM   423  C CD1 . LEU A 1 52  ? 9.666   -22.571 52.114 1.00 18.13 ? 112 LEU A CD1 1 
ATOM   424  C CD2 . LEU A 1 52  ? 10.518  -21.286 54.073 1.00 22.21 ? 112 LEU A CD2 1 
ATOM   425  N N   . HIS A 1 53  ? 6.885   -17.591 52.413 1.00 16.51 ? 113 HIS A N   1 
ATOM   426  C CA  . HIS A 1 53  ? 6.404   -16.545 51.495 1.00 16.54 ? 113 HIS A CA  1 
ATOM   427  C C   . HIS A 1 53  ? 4.907   -16.369 51.668 1.00 18.84 ? 113 HIS A C   1 
ATOM   428  O O   . HIS A 1 53  ? 4.187   -17.354 51.829 1.00 16.45 ? 113 HIS A O   1 
ATOM   429  C CB  . HIS A 1 53  ? 6.675   -16.930 50.033 1.00 17.97 ? 113 HIS A CB  1 
ATOM   430  C CG  . HIS A 1 53  ? 6.388   -15.823 49.059 1.00 17.29 ? 113 HIS A CG  1 
ATOM   431  N ND1 . HIS A 1 53  ? 7.293   -14.826 48.779 1.00 18.58 ? 113 HIS A ND1 1 
ATOM   432  C CD2 . HIS A 1 53  ? 5.281   -15.539 48.324 1.00 15.76 ? 113 HIS A CD2 1 
ATOM   433  C CE1 . HIS A 1 53  ? 6.765   -13.981 47.905 1.00 17.01 ? 113 HIS A CE1 1 
ATOM   434  N NE2 . HIS A 1 53  ? 5.543   -14.389 47.614 1.00 17.17 ? 113 HIS A NE2 1 
ATOM   435  N N   . VAL A 1 54  ? 4.422   -15.132 51.578 1.00 14.77 ? 114 VAL A N   1 
ATOM   436  C CA  . VAL A 1 54  ? 2.986   -14.895 51.562 1.00 17.40 ? 114 VAL A CA  1 
ATOM   437  C C   . VAL A 1 54  ? 2.652   -14.339 50.195 1.00 18.16 ? 114 VAL A C   1 
ATOM   438  O O   . VAL A 1 54  ? 3.219   -13.327 49.776 1.00 15.28 ? 114 VAL A O   1 
ATOM   439  C CB  . VAL A 1 54  ? 2.509   -13.910 52.690 1.00 16.08 ? 114 VAL A CB  1 
ATOM   440  C CG1 . VAL A 1 54  ? 1.011   -13.683 52.601 1.00 17.33 ? 114 VAL A CG1 1 
ATOM   441  C CG2 . VAL A 1 54  ? 2.849   -14.437 54.076 1.00 15.73 ? 114 VAL A CG2 1 
ATOM   442  N N   . PHE A 1 55  ? 1.735   -15.006 49.503 1.00 16.08 ? 115 PHE A N   1 
ATOM   443  C CA  . PHE A 1 55  ? 1.365   -14.663 48.130 1.00 18.46 ? 115 PHE A CA  1 
ATOM   444  C C   . PHE A 1 55  ? 0.280   -13.591 48.112 1.00 21.46 ? 115 PHE A C   1 
ATOM   445  O O   . PHE A 1 55  ? -0.744  -13.706 48.794 1.00 19.34 ? 115 PHE A O   1 
ATOM   446  C CB  . PHE A 1 55  ? 0.818   -15.901 47.404 1.00 16.18 ? 115 PHE A CB  1 
ATOM   447  C CG  . PHE A 1 55  ? 1.874   -16.898 47.037 1.00 16.90 ? 115 PHE A CG  1 
ATOM   448  C CD1 . PHE A 1 55  ? 2.778   -16.652 46.016 1.00 16.68 ? 115 PHE A CD1 1 
ATOM   449  C CD2 . PHE A 1 55  ? 1.986   -18.067 47.752 1.00 15.35 ? 115 PHE A CD2 1 
ATOM   450  C CE1 . PHE A 1 55  ? 3.744   -17.589 45.706 1.00 14.91 ? 115 PHE A CE1 1 
ATOM   451  C CE2 . PHE A 1 55  ? 2.943   -18.991 47.447 1.00 15.38 ? 115 PHE A CE2 1 
ATOM   452  C CZ  . PHE A 1 55  ? 3.826   -18.750 46.422 1.00 17.08 ? 115 PHE A CZ  1 
ATOM   453  N N   . HIS A 1 56  ? 0.474   -12.567 47.305 1.00 22.01 ? 116 HIS A N   1 
ATOM   454  C CA  . HIS A 1 56  ? -0.646  -11.701 46.948 1.00 23.97 ? 116 HIS A CA  1 
ATOM   455  C C   . HIS A 1 56  ? -0.386  -11.026 45.617 1.00 21.74 ? 116 HIS A C   1 
ATOM   456  O O   . HIS A 1 56  ? 0.762   -10.774 45.260 1.00 24.88 ? 116 HIS A O   1 
ATOM   457  C CB  . HIS A 1 56  ? -0.917  -10.681 48.056 1.00 25.08 ? 116 HIS A CB  1 
ATOM   458  C CG  . HIS A 1 56  ? 0.126   -9.623  48.138 1.00 24.10 ? 116 HIS A CG  1 
ATOM   459  N ND1 . HIS A 1 56  ? 1.360   -9.841  48.713 1.00 27.38 ? 116 HIS A ND1 1 
ATOM   460  C CD2 . HIS A 1 56  ? 0.137   -8.348  47.691 1.00 27.95 ? 116 HIS A CD2 1 
ATOM   461  C CE1 . HIS A 1 56  ? 2.079   -8.734  48.641 1.00 23.15 ? 116 HIS A CE1 1 
ATOM   462  N NE2 . HIS A 1 56  ? 1.360   -7.813  48.025 1.00 26.28 ? 116 HIS A NE2 1 
ATOM   463  N N   . GLY A 1 57  ? -1.441  -10.775 44.860 1.00 24.69 ? 117 GLY A N   1 
ATOM   464  C CA  . GLY A 1 57  ? -1.269  -10.094 43.593 1.00 32.12 ? 117 GLY A CA  1 
ATOM   465  C C   . GLY A 1 57  ? -1.714  -10.931 42.423 1.00 29.68 ? 117 GLY A C   1 
ATOM   466  O O   . GLY A 1 57  ? -2.216  -10.387 41.438 1.00 30.64 ? 117 GLY A O   1 
ATOM   467  N N   . LEU A 1 58  ? -1.526  -12.246 42.523 1.00 21.68 ? 118 LEU A N   1 
ATOM   468  C CA  . LEU A 1 58  ? -2.128  -13.159 41.574 1.00 22.43 ? 118 LEU A CA  1 
ATOM   469  C C   . LEU A 1 58  ? -3.078  -14.115 42.302 1.00 26.07 ? 118 LEU A C   1 
ATOM   470  O O   . LEU A 1 58  ? -4.282  -14.155 42.044 1.00 26.64 ? 118 LEU A O   1 
ATOM   471  C CB  . LEU A 1 58  ? -1.040  -13.942 40.830 1.00 22.32 ? 118 LEU A CB  1 
ATOM   472  C CG  . LEU A 1 58  ? -0.266  -13.162 39.759 1.00 20.47 ? 118 LEU A CG  1 
ATOM   473  C CD1 . LEU A 1 58  ? 0.804   -14.050 39.139 1.00 19.21 ? 118 LEU A CD1 1 
ATOM   474  C CD2 . LEU A 1 58  ? -1.190  -12.554 38.694 1.00 18.14 ? 118 LEU A CD2 1 
ATOM   475  N N   . LEU A 1 59  ? -2.512  -14.912 43.198 1.00 22.65 ? 119 LEU A N   1 
ATOM   476  C CA  . LEU A 1 59  ? -3.281  -15.831 44.026 1.00 21.06 ? 119 LEU A CA  1 
ATOM   477  C C   . LEU A 1 59  ? -3.042  -15.392 45.467 1.00 19.91 ? 119 LEU A C   1 
ATOM   478  O O   . LEU A 1 59  ? -1.922  -15.088 45.815 1.00 21.52 ? 119 LEU A O   1 
ATOM   479  C CB  . LEU A 1 59  ? -2.736  -17.253 43.856 1.00 24.53 ? 119 LEU A CB  1 
ATOM   480  C CG  . LEU A 1 59  ? -3.042  -17.944 42.513 1.00 25.22 ? 119 LEU A CG  1 
ATOM   481  C CD1 . LEU A 1 59  ? -2.543  -19.355 42.532 1.00 20.59 ? 119 LEU A CD1 1 
ATOM   482  C CD2 . LEU A 1 59  ? -4.536  -17.898 42.124 1.00 28.47 ? 119 LEU A CD2 1 
ATOM   483  N N   . PRO A 1 60  ? -4.066  -15.428 46.327 1.00 17.35 ? 120 PRO A N   1 
ATOM   484  C CA  . PRO A 1 60  ? -3.739  -15.277 47.745 1.00 16.73 ? 120 PRO A CA  1 
ATOM   485  C C   . PRO A 1 60  ? -3.354  -16.607 48.391 1.00 16.71 ? 120 PRO A C   1 
ATOM   486  O O   . PRO A 1 60  ? -3.792  -17.674 47.982 1.00 14.32 ? 120 PRO A O   1 
ATOM   487  C CB  . PRO A 1 60  ? -5.056  -14.757 48.343 1.00 17.29 ? 120 PRO A CB  1 
ATOM   488  C CG  . PRO A 1 60  ? -6.098  -15.320 47.498 1.00 19.67 ? 120 PRO A CG  1 
ATOM   489  C CD  . PRO A 1 60  ? -5.507  -15.587 46.108 1.00 21.14 ? 120 PRO A CD  1 
ATOM   490  N N   . GLY A 1 61  ? -2.446  -16.563 49.350 1.00 13.70 ? 121 GLY A N   1 
ATOM   491  C CA  . GLY A 1 61  ? -2.058  -17.779 50.035 1.00 15.95 ? 121 GLY A CA  1 
ATOM   492  C C   . GLY A 1 61  ? -0.677  -17.622 50.614 1.00 17.53 ? 121 GLY A C   1 
ATOM   493  O O   . GLY A 1 61  ? -0.208  -16.503 50.806 1.00 16.37 ? 121 GLY A O   1 
ATOM   494  N N   . PHE A 1 62  ? -0.019  -18.746 50.884 1.00 11.69 ? 122 PHE A N   1 
ATOM   495  C CA  . PHE A 1 62  ? 1.324   -18.716 51.445 1.00 14.62 ? 122 PHE A CA  1 
ATOM   496  C C   . PHE A 1 62  ? 2.066   -20.012 51.157 1.00 15.16 ? 122 PHE A C   1 
ATOM   497  O O   . PHE A 1 62  ? 1.455   -21.015 50.809 1.00 15.16 ? 122 PHE A O   1 
ATOM   498  C CB  . PHE A 1 62  ? 1.323   -18.398 52.945 1.00 17.21 ? 122 PHE A CB  1 
ATOM   499  C CG  . PHE A 1 62  ? 0.419   -19.280 53.775 1.00 13.76 ? 122 PHE A CG  1 
ATOM   500  C CD1 . PHE A 1 62  ? -0.911  -18.948 53.984 1.00 16.54 ? 122 PHE A CD1 1 
ATOM   501  C CD2 . PHE A 1 62  ? 0.927   -20.413 54.383 1.00 16.97 ? 122 PHE A CD2 1 
ATOM   502  C CE1 . PHE A 1 62  ? -1.740  -19.760 54.779 1.00 16.73 ? 122 PHE A CE1 1 
ATOM   503  C CE2 . PHE A 1 62  ? 0.102   -21.232 55.170 1.00 12.80 ? 122 PHE A CE2 1 
ATOM   504  C CZ  . PHE A 1 62  ? -1.213  -20.895 55.370 1.00 13.69 ? 122 PHE A CZ  1 
ATOM   505  N N   . LEU A 1 63  ? 3.382   -19.967 51.270 1.00 13.83 ? 123 LEU A N   1 
ATOM   506  C CA  . LEU A 1 63  ? 4.212   -21.138 51.101 1.00 15.52 ? 123 LEU A CA  1 
ATOM   507  C C   . LEU A 1 63  ? 4.690   -21.525 52.499 1.00 15.92 ? 123 LEU A C   1 
ATOM   508  O O   . LEU A 1 63  ? 5.247   -20.689 53.225 1.00 15.24 ? 123 LEU A O   1 
ATOM   509  C CB  . LEU A 1 63  ? 5.432   -20.757 50.253 1.00 15.58 ? 123 LEU A CB  1 
ATOM   510  C CG  . LEU A 1 63  ? 6.479   -21.822 49.950 1.00 14.00 ? 123 LEU A CG  1 
ATOM   511  C CD1 . LEU A 1 63  ? 5.795   -22.910 49.157 1.00 15.51 ? 123 LEU A CD1 1 
ATOM   512  C CD2 . LEU A 1 63  ? 7.618   -21.217 49.143 1.00 13.17 ? 123 LEU A CD2 1 
ATOM   513  N N   . VAL A 1 64  ? 4.531   -22.792 52.870 1.00 12.88 ? 124 VAL A N   1 
ATOM   514  C CA  . VAL A 1 64  ? 4.874   -23.245 54.215 1.00 12.67 ? 124 VAL A CA  1 
ATOM   515  C C   . VAL A 1 64  ? 5.696   -24.521 54.195 1.00 16.82 ? 124 VAL A C   1 
ATOM   516  O O   . VAL A 1 64  ? 5.426   -25.455 53.446 1.00 14.07 ? 124 VAL A O   1 
ATOM   517  C CB  . VAL A 1 64  ? 3.595   -23.435 55.094 1.00 13.13 ? 124 VAL A CB  1 
ATOM   518  C CG1 . VAL A 1 64  ? 2.637   -24.477 54.486 1.00 13.49 ? 124 VAL A CG1 1 
ATOM   519  C CG2 . VAL A 1 64  ? 3.978   -23.834 56.538 1.00 13.74 ? 124 VAL A CG2 1 
ATOM   520  N N   . LYS A 1 65  ? 6.740   -24.524 55.005 1.00 14.84 ? 125 LYS A N   1 
ATOM   521  C CA  . LYS A 1 65  ? 7.552   -25.696 55.213 1.00 15.29 ? 125 LYS A CA  1 
ATOM   522  C C   . LYS A 1 65  ? 7.075   -26.368 56.479 1.00 16.57 ? 125 LYS A C   1 
ATOM   523  O O   . LYS A 1 65  ? 7.108   -25.770 57.549 1.00 16.28 ? 125 LYS A O   1 
ATOM   524  C CB  . LYS A 1 65  ? 9.030   -25.316 55.322 1.00 15.85 ? 125 LYS A CB  1 
ATOM   525  C CG  . LYS A 1 65  ? 9.956   -26.498 55.484 1.00 25.57 ? 125 LYS A CG  1 
ATOM   526  C CD  . LYS A 1 65  ? 11.376  -26.098 55.164 1.00 30.32 ? 125 LYS A CD  1 
ATOM   527  C CE  . LYS A 1 65  ? 12.346  -27.183 55.573 1.00 36.75 ? 125 LYS A CE  1 
ATOM   528  N NZ  . LYS A 1 65  ? 12.236  -27.385 57.047 1.00 43.72 ? 125 LYS A NZ  1 
ATOM   529  N N   . MET A 1 66  ? 6.529   -27.574 56.347 1.00 15.74 ? 126 MET A N   1 
ATOM   530  C CA  . MET A 1 66  ? 5.918   -28.283 57.469 1.00 13.27 ? 126 MET A CA  1 
ATOM   531  C C   . MET A 1 66  ? 5.810   -29.750 57.104 1.00 18.49 ? 126 MET A C   1 
ATOM   532  O O   . MET A 1 66  ? 5.835   -30.110 55.926 1.00 18.41 ? 126 MET A O   1 
ATOM   533  C CB  . MET A 1 66  ? 4.531   -27.743 57.798 1.00 15.38 ? 126 MET A CB  1 
ATOM   534  C CG  . MET A 1 66  ? 3.496   -27.961 56.701 1.00 14.70 ? 126 MET A CG  1 
ATOM   535  S SD  . MET A 1 66  ? 1.865   -27.328 57.097 1.00 19.71 ? 126 MET A SD  1 
ATOM   536  C CE  . MET A 1 66  ? 0.850   -28.201 55.904 1.00 19.16 ? 126 MET A CE  1 
ATOM   537  N N   . SER A 1 67  ? 5.580   -30.579 58.109 1.00 17.55 ? 127 SER A N   1 
ATOM   538  C CA  . SER A 1 67  ? 5.261   -31.989 57.888 1.00 19.52 ? 127 SER A CA  1 
ATOM   539  C C   . SER A 1 67  ? 3.907   -32.143 57.245 1.00 17.32 ? 127 SER A C   1 
ATOM   540  O O   . SER A 1 67  ? 2.973   -31.420 57.558 1.00 16.28 ? 127 SER A O   1 
ATOM   541  C CB  . SER A 1 67  ? 5.279   -32.744 59.208 1.00 21.96 ? 127 SER A CB  1 
ATOM   542  O OG  . SER A 1 67  ? 4.599   -33.985 59.073 1.00 17.46 ? 127 SER A OG  1 
ATOM   543  N N   . GLY A 1 68  ? 3.793   -33.105 56.337 1.00 18.02 ? 128 GLY A N   1 
ATOM   544  C CA  . GLY A 1 68  ? 2.516   -33.394 55.727 1.00 17.58 ? 128 GLY A CA  1 
ATOM   545  C C   . GLY A 1 68  ? 1.482   -33.885 56.719 1.00 15.81 ? 128 GLY A C   1 
ATOM   546  O O   . GLY A 1 68  ? 0.296   -33.865 56.421 1.00 14.24 ? 128 GLY A O   1 
ATOM   547  N N   . ASP A 1 69  ? 1.930   -34.326 57.895 1.00 17.43 ? 129 ASP A N   1 
ATOM   548  C CA  . ASP A 1 69  ? 1.029   -34.670 59.002 1.00 16.26 ? 129 ASP A CA  1 
ATOM   549  C C   . ASP A 1 69  ? -0.026  -33.588 59.270 1.00 18.55 ? 129 ASP A C   1 
ATOM   550  O O   . ASP A 1 69  ? -1.143  -33.883 59.680 1.00 17.59 ? 129 ASP A O   1 
ATOM   551  C CB  . ASP A 1 69  ? 1.837   -34.851 60.293 1.00 16.21 ? 129 ASP A CB  1 
ATOM   552  C CG  . ASP A 1 69  ? 2.709   -36.108 60.304 1.00 24.20 ? 129 ASP A CG  1 
ATOM   553  O OD1 . ASP A 1 69  ? 2.895   -36.776 59.252 1.00 21.42 ? 129 ASP A OD1 1 
ATOM   554  O OD2 . ASP A 1 69  ? 3.241   -36.425 61.401 1.00 23.66 ? 129 ASP A OD2 1 
ATOM   555  N N   . LEU A 1 70  ? 0.358   -32.330 59.083 1.00 18.90 ? 130 LEU A N   1 
ATOM   556  C CA  . LEU A 1 70  ? -0.526  -31.193 59.367 1.00 16.22 ? 130 LEU A CA  1 
ATOM   557  C C   . LEU A 1 70  ? -1.548  -30.880 58.275 1.00 17.98 ? 130 LEU A C   1 
ATOM   558  O O   . LEU A 1 70  ? -2.296  -29.896 58.379 1.00 18.53 ? 130 LEU A O   1 
ATOM   559  C CB  . LEU A 1 70  ? 0.343   -29.948 59.606 1.00 13.62 ? 130 LEU A CB  1 
ATOM   560  C CG  . LEU A 1 70  ? 1.314   -30.124 60.785 1.00 18.42 ? 130 LEU A CG  1 
ATOM   561  C CD1 . LEU A 1 70  ? 2.407   -29.058 60.836 1.00 19.12 ? 130 LEU A CD1 1 
ATOM   562  C CD2 . LEU A 1 70  ? 0.540   -30.125 62.092 1.00 18.53 ? 130 LEU A CD2 1 
ATOM   563  N N   . LEU A 1 71  ? -1.591  -31.677 57.211 1.00 14.11 ? 131 LEU A N   1 
ATOM   564  C CA  . LEU A 1 71  ? -2.463  -31.304 56.111 1.00 15.41 ? 131 LEU A CA  1 
ATOM   565  C C   . LEU A 1 71  ? -3.947  -31.345 56.433 1.00 17.67 ? 131 LEU A C   1 
ATOM   566  O O   . LEU A 1 71  ? -4.687  -30.441 56.030 1.00 14.83 ? 131 LEU A O   1 
ATOM   567  C CB  . LEU A 1 71  ? -2.203  -32.165 54.873 1.00 16.24 ? 131 LEU A CB  1 
ATOM   568  C CG  . LEU A 1 71  ? -0.916  -31.780 54.128 1.00 17.47 ? 131 LEU A CG  1 
ATOM   569  C CD1 . LEU A 1 71  ? -0.522  -32.872 53.137 1.00 15.95 ? 131 LEU A CD1 1 
ATOM   570  C CD2 . LEU A 1 71  ? -1.126  -30.447 53.397 1.00 16.19 ? 131 LEU A CD2 1 
ATOM   571  N N   . GLU A 1 72  ? -4.395  -32.350 57.180 1.00 15.62 ? 132 GLU A N   1 
ATOM   572  C CA  . GLU A 1 72  ? -5.792  -32.368 57.592 1.00 18.88 ? 132 GLU A CA  1 
ATOM   573  C C   . GLU A 1 72  ? -6.127  -31.114 58.392 1.00 17.71 ? 132 GLU A C   1 
ATOM   574  O O   . GLU A 1 72  ? -7.176  -30.505 58.196 1.00 19.60 ? 132 GLU A O   1 
ATOM   575  C CB  . GLU A 1 72  ? -6.091  -33.607 58.427 1.00 20.72 ? 132 GLU A CB  1 
ATOM   576  C CG  . GLU A 1 72  ? -6.462  -34.793 57.550 1.00 23.69 ? 132 GLU A CG  1 
ATOM   577  C CD  . GLU A 1 72  ? -6.827  -36.029 58.348 1.00 31.79 ? 132 GLU A CD  1 
ATOM   578  O OE1 . GLU A 1 72  ? -6.434  -36.137 59.534 1.00 35.44 ? 132 GLU A OE1 1 
ATOM   579  O OE2 . GLU A 1 72  ? -7.487  -36.915 57.770 1.00 38.21 ? 132 GLU A OE2 1 
ATOM   580  N N   . LEU A 1 73  ? -5.233  -30.728 59.292 1.00 17.44 ? 133 LEU A N   1 
ATOM   581  C CA  . LEU A 1 73  ? -5.434  -29.496 60.053 1.00 18.47 ? 133 LEU A CA  1 
ATOM   582  C C   . LEU A 1 73  ? -5.497  -28.243 59.141 1.00 19.97 ? 133 LEU A C   1 
ATOM   583  O O   . LEU A 1 73  ? -6.424  -27.431 59.238 1.00 20.20 ? 133 LEU A O   1 
ATOM   584  C CB  . LEU A 1 73  ? -4.297  -29.353 61.061 1.00 23.00 ? 133 LEU A CB  1 
ATOM   585  C CG  . LEU A 1 73  ? -4.209  -28.094 61.932 1.00 29.29 ? 133 LEU A CG  1 
ATOM   586  C CD1 . LEU A 1 73  ? -5.481  -27.933 62.691 1.00 29.83 ? 133 LEU A CD1 1 
ATOM   587  C CD2 . LEU A 1 73  ? -3.030  -28.147 62.873 1.00 28.75 ? 133 LEU A CD2 1 
ATOM   588  N N   . ALA A 1 74  ? -4.525  -28.125 58.235 1.00 17.75 ? 134 ALA A N   1 
ATOM   589  C CA  . ALA A 1 74  ? -4.425  -26.978 57.333 1.00 16.89 ? 134 ALA A CA  1 
ATOM   590  C C   . ALA A 1 74  ? -5.626  -26.845 56.393 1.00 20.84 ? 134 ALA A C   1 
ATOM   591  O O   . ALA A 1 74  ? -6.114  -25.736 56.140 1.00 16.40 ? 134 ALA A O   1 
ATOM   592  C CB  . ALA A 1 74  ? -3.118  -27.036 56.551 1.00 13.54 ? 134 ALA A CB  1 
ATOM   593  N N   . LEU A 1 75  ? -6.146  -27.974 55.910 1.00 15.09 ? 135 LEU A N   1 
ATOM   594  C CA  . LEU A 1 75  ? -7.318  -27.922 55.033 1.00 14.88 ? 135 LEU A CA  1 
ATOM   595  C C   . LEU A 1 75  ? -8.550  -27.389 55.739 1.00 16.71 ? 135 LEU A C   1 
ATOM   596  O O   . LEU A 1 75  ? -9.498  -26.961 55.094 1.00 18.17 ? 135 LEU A O   1 
ATOM   597  C CB  . LEU A 1 75  ? -7.635  -29.306 54.443 1.00 13.58 ? 135 LEU A CB  1 
ATOM   598  C CG  . LEU A 1 75  ? -6.609  -29.805 53.412 1.00 16.71 ? 135 LEU A CG  1 
ATOM   599  C CD1 . LEU A 1 75  ? -6.721  -31.313 53.195 1.00 20.36 ? 135 LEU A CD1 1 
ATOM   600  C CD2 . LEU A 1 75  ? -6.729  -29.050 52.102 1.00 14.49 ? 135 LEU A CD2 1 
ATOM   601  N N   . LYS A 1 76  ? -8.542  -27.396 57.063 1.00 16.98 ? 136 LYS A N   1 
ATOM   602  C CA  . LYS A 1 76  ? -9.704  -26.885 57.793 1.00 22.36 ? 136 LYS A CA  1 
ATOM   603  C C   . LYS A 1 76  ? -9.574  -25.419 58.169 1.00 23.74 ? 136 LYS A C   1 
ATOM   604  O O   . LYS A 1 76  ? -10.501 -24.854 58.753 1.00 26.16 ? 136 LYS A O   1 
ATOM   605  C CB  . LYS A 1 76  ? -9.919  -27.709 59.054 1.00 21.63 ? 136 LYS A CB  1 
ATOM   606  C CG  . LYS A 1 76  ? -10.490 -29.060 58.767 1.00 27.08 ? 136 LYS A CG  1 
ATOM   607  C CD  . LYS A 1 76  ? -10.482 -29.934 59.985 1.00 33.72 ? 136 LYS A CD  1 
ATOM   608  C CE  . LYS A 1 76  ? -11.373 -31.134 59.727 1.00 40.93 ? 136 LYS A CE  1 
ATOM   609  N NZ  . LYS A 1 76  ? -11.888 -31.689 60.999 1.00 51.12 ? 136 LYS A NZ  1 
ATOM   610  N N   . LEU A 1 77  ? -8.454  -24.789 57.821 1.00 20.61 ? 137 LEU A N   1 
ATOM   611  C CA  . LEU A 1 77  ? -8.314  -23.368 58.128 1.00 20.44 ? 137 LEU A CA  1 
ATOM   612  C C   . LEU A 1 77  ? -9.308  -22.530 57.355 1.00 22.36 ? 137 LEU A C   1 
ATOM   613  O O   . LEU A 1 77  ? -9.727  -22.903 56.265 1.00 19.71 ? 137 LEU A O   1 
ATOM   614  C CB  . LEU A 1 77  ? -6.905  -22.881 57.789 1.00 23.54 ? 137 LEU A CB  1 
ATOM   615  C CG  . LEU A 1 77  ? -5.802  -23.478 58.656 1.00 23.55 ? 137 LEU A CG  1 
ATOM   616  C CD1 . LEU A 1 77  ? -4.463  -23.307 57.990 1.00 22.26 ? 137 LEU A CD1 1 
ATOM   617  C CD2 . LEU A 1 77  ? -5.831  -22.792 59.992 1.00 26.89 ? 137 LEU A CD2 1 
ATOM   618  N N   . PRO A 1 78  ? -9.663  -21.353 57.908 1.00 31.28 ? 138 PRO A N   1 
ATOM   619  C CA  . PRO A 1 78  ? -10.580 -20.484 57.164 1.00 25.49 ? 138 PRO A CA  1 
ATOM   620  C C   . PRO A 1 78  ? -9.932  -20.006 55.871 1.00 20.89 ? 138 PRO A C   1 
ATOM   621  O O   . PRO A 1 78  ? -8.717  -19.800 55.846 1.00 23.40 ? 138 PRO A O   1 
ATOM   622  C CB  . PRO A 1 78  ? -10.794 -19.296 58.119 1.00 31.80 ? 138 PRO A CB  1 
ATOM   623  C CG  . PRO A 1 78  ? -9.574  -19.297 59.009 1.00 33.56 ? 138 PRO A CG  1 
ATOM   624  C CD  . PRO A 1 78  ? -9.226  -20.754 59.179 1.00 32.15 ? 138 PRO A CD  1 
ATOM   625  N N   . HIS A 1 79  ? -10.756 -19.758 54.862 1.00 22.18 ? 139 HIS A N   1 
ATOM   626  C CA  . HIS A 1 79  ? -10.362 -19.215 53.567 1.00 25.62 ? 139 HIS A CA  1 
ATOM   627  C C   . HIS A 1 79  ? -9.614  -20.187 52.638 1.00 19.39 ? 139 HIS A C   1 
ATOM   628  O O   . HIS A 1 79  ? -9.339  -19.818 51.506 1.00 20.32 ? 139 HIS A O   1 
ATOM   629  C CB  . HIS A 1 79  ? -9.542  -17.924 53.706 1.00 23.88 ? 139 HIS A CB  1 
ATOM   630  C CG  . HIS A 1 79  ? -10.118 -16.938 54.680 1.00 33.00 ? 139 HIS A CG  1 
ATOM   631  N ND1 . HIS A 1 79  ? -11.342 -16.329 54.492 1.00 35.28 ? 139 HIS A ND1 1 
ATOM   632  C CD2 . HIS A 1 79  ? -9.628  -16.440 55.842 1.00 29.56 ? 139 HIS A CD2 1 
ATOM   633  C CE1 . HIS A 1 79  ? -11.589 -15.512 55.504 1.00 35.89 ? 139 HIS A CE1 1 
ATOM   634  N NE2 . HIS A 1 79  ? -10.564 -15.559 56.336 1.00 34.70 ? 139 HIS A NE2 1 
ATOM   635  N N   . VAL A 1 80  ? -9.285  -21.403 53.085 1.00 20.13 ? 140 VAL A N   1 
ATOM   636  C CA  . VAL A 1 80  ? -8.491  -22.315 52.240 1.00 18.28 ? 140 VAL A CA  1 
ATOM   637  C C   . VAL A 1 80  ? -9.335  -22.788 51.067 1.00 17.12 ? 140 VAL A C   1 
ATOM   638  O O   . VAL A 1 80  ? -10.458 -23.225 51.245 1.00 19.51 ? 140 VAL A O   1 
ATOM   639  C CB  . VAL A 1 80  ? -7.868  -23.508 53.025 1.00 19.11 ? 140 VAL A CB  1 
ATOM   640  C CG1 . VAL A 1 80  ? -7.167  -24.510 52.075 1.00 12.93 ? 140 VAL A CG1 1 
ATOM   641  C CG2 . VAL A 1 80  ? -6.948  -23.006 54.110 1.00 16.41 ? 140 VAL A CG2 1 
ATOM   642  N N   . ASP A 1 81  ? -8.781  -22.659 49.864 1.00 14.54 ? 141 ASP A N   1 
ATOM   643  C CA  . ASP A 1 81  ? -9.355  -23.225 48.641 1.00 14.00 ? 141 ASP A CA  1 
ATOM   644  C C   . ASP A 1 81  ? -8.771  -24.633 48.375 1.00 15.69 ? 141 ASP A C   1 
ATOM   645  O O   . ASP A 1 81  ? -9.500  -25.623 48.307 1.00 16.38 ? 141 ASP A O   1 
ATOM   646  C CB  . ASP A 1 81  ? -9.091  -22.266 47.477 1.00 16.34 ? 141 ASP A CB  1 
ATOM   647  C CG  . ASP A 1 81  ? -9.947  -22.536 46.270 1.00 18.97 ? 141 ASP A CG  1 
ATOM   648  O OD1 . ASP A 1 81  ? -10.767 -23.464 46.289 1.00 22.39 ? 141 ASP A OD1 1 
ATOM   649  O OD2 . ASP A 1 81  ? -9.758  -21.833 45.253 1.00 20.62 ? 141 ASP A OD2 1 
ATOM   650  N N   . TYR A 1 82  ? -7.443  -24.722 48.293 1.00 13.07 ? 142 TYR A N   1 
ATOM   651  C CA  . TYR A 1 82  ? -6.785  -26.024 48.153 1.00 14.50 ? 142 TYR A CA  1 
ATOM   652  C C   . TYR A 1 82  ? -5.334  -25.883 48.592 1.00 14.40 ? 142 TYR A C   1 
ATOM   653  O O   . TYR A 1 82  ? -4.838  -24.747 48.818 1.00 14.72 ? 142 TYR A O   1 
ATOM   654  C CB  . TYR A 1 82  ? -6.874  -26.549 46.710 1.00 12.04 ? 142 TYR A CB  1 
ATOM   655  C CG  . TYR A 1 82  ? -6.333  -25.606 45.661 1.00 13.57 ? 142 TYR A CG  1 
ATOM   656  C CD1 . TYR A 1 82  ? -7.125  -24.585 45.127 1.00 13.56 ? 142 TYR A CD1 1 
ATOM   657  C CD2 . TYR A 1 82  ? -5.043  -25.765 45.175 1.00 11.88 ? 142 TYR A CD2 1 
ATOM   658  C CE1 . TYR A 1 82  ? -6.627  -23.732 44.163 1.00 14.70 ? 142 TYR A CE1 1 
ATOM   659  C CE2 . TYR A 1 82  ? -4.527  -24.911 44.209 1.00 15.47 ? 142 TYR A CE2 1 
ATOM   660  C CZ  . TYR A 1 82  ? -5.326  -23.904 43.709 1.00 15.43 ? 142 TYR A CZ  1 
ATOM   661  O OH  . TYR A 1 82  ? -4.825  -23.054 42.745 1.00 13.23 ? 142 TYR A OH  1 
ATOM   662  N N   . ILE A 1 83  ? -4.663  -27.017 48.792 1.00 11.57 ? 143 ILE A N   1 
ATOM   663  C CA  . ILE A 1 83  ? -3.257  -27.024 49.159 1.00 10.61 ? 143 ILE A CA  1 
ATOM   664  C C   . ILE A 1 83  ? -2.520  -27.929 48.170 1.00 14.09 ? 143 ILE A C   1 
ATOM   665  O O   . ILE A 1 83  ? -3.002  -29.010 47.826 1.00 11.97 ? 143 ILE A O   1 
ATOM   666  C CB  . ILE A 1 83  ? -3.064  -27.520 50.602 1.00 12.17 ? 143 ILE A CB  1 
ATOM   667  C CG1 . ILE A 1 83  ? -3.858  -26.625 51.560 1.00 12.38 ? 143 ILE A CG1 1 
ATOM   668  C CG2 . ILE A 1 83  ? -1.583  -27.565 50.964 1.00 13.75 ? 143 ILE A CG2 1 
ATOM   669  C CD1 . ILE A 1 83  ? -3.866  -27.070 53.006 1.00 11.97 ? 143 ILE A CD1 1 
ATOM   670  N N   . GLU A 1 84  ? -1.399  -27.470 47.642 1.00 12.54 ? 144 GLU A N   1 
ATOM   671  C CA  . GLU A 1 84  ? -0.592  -28.307 46.744 1.00 12.24 ? 144 GLU A CA  1 
ATOM   672  C C   . GLU A 1 84  ? 0.831   -28.517 47.255 1.00 12.69 ? 144 GLU A C   1 
ATOM   673  O O   . GLU A 1 84  ? 1.506   -27.568 47.666 1.00 14.37 ? 144 GLU A O   1 
ATOM   674  C CB  . GLU A 1 84  ? -0.646  -27.724 45.314 1.00 15.25 ? 144 GLU A CB  1 
ATOM   675  C CG  . GLU A 1 84  ? 0.137   -28.538 44.289 1.00 15.91 ? 144 GLU A CG  1 
ATOM   676  C CD  . GLU A 1 84  ? 0.020   -28.009 42.869 1.00 19.23 ? 144 GLU A CD  1 
ATOM   677  O OE1 . GLU A 1 84  ? -1.097  -27.572 42.483 1.00 17.55 ? 144 GLU A OE1 1 
ATOM   678  O OE2 . GLU A 1 84  ? 1.035   -28.047 42.121 1.00 17.39 ? 144 GLU A OE2 1 
ATOM   679  N N   . GLU A 1 85  ? 1.286   -29.767 47.261 1.00 12.05 ? 145 GLU A N   1 
ATOM   680  C CA  . GLU A 1 85  ? 2.653   -30.069 47.661 1.00 10.83 ? 145 GLU A CA  1 
ATOM   681  C C   . GLU A 1 85  ? 3.571   -29.487 46.585 1.00 12.33 ? 145 GLU A C   1 
ATOM   682  O O   . GLU A 1 85  ? 3.238   -29.571 45.399 1.00 12.53 ? 145 GLU A O   1 
ATOM   683  C CB  . GLU A 1 85  ? 2.839   -31.584 47.740 1.00 14.36 ? 145 GLU A CB  1 
ATOM   684  C CG  . GLU A 1 85  ? 4.239   -32.020 48.118 1.00 11.46 ? 145 GLU A CG  1 
ATOM   685  C CD  . GLU A 1 85  ? 4.398   -33.509 47.895 1.00 18.29 ? 145 GLU A CD  1 
ATOM   686  O OE1 . GLU A 1 85  ? 4.444   -33.941 46.718 1.00 16.78 ? 145 GLU A OE1 1 
ATOM   687  O OE2 . GLU A 1 85  ? 4.465   -34.258 48.889 1.00 17.55 ? 145 GLU A OE2 1 
ATOM   688  N N   . ASP A 1 86  ? 4.710   -28.896 46.974 1.00 11.89 ? 146 ASP A N   1 
ATOM   689  C CA  . ASP A 1 86  ? 5.640   -28.304 45.995 1.00 10.81 ? 146 ASP A CA  1 
ATOM   690  C C   . ASP A 1 86  ? 6.217   -29.400 45.118 1.00 14.44 ? 146 ASP A C   1 
ATOM   691  O O   . ASP A 1 86  ? 6.233   -30.573 45.497 1.00 12.68 ? 146 ASP A O   1 
ATOM   692  C CB  . ASP A 1 86  ? 6.768   -27.535 46.724 1.00 11.65 ? 146 ASP A CB  1 
ATOM   693  C CG  . ASP A 1 86  ? 7.377   -26.434 45.874 1.00 13.99 ? 146 ASP A CG  1 
ATOM   694  O OD1 . ASP A 1 86  ? 6.914   -26.232 44.725 1.00 13.76 ? 146 ASP A OD1 1 
ATOM   695  O OD2 . ASP A 1 86  ? 8.304   -25.720 46.356 1.00 16.85 ? 146 ASP A OD2 1 
ATOM   696  N N   . SER A 1 87  ? 6.689   -29.031 43.935 1.00 13.40 ? 147 SER A N   1 
ATOM   697  C CA  . SER A 1 87  ? 7.252   -30.023 43.018 1.00 13.50 ? 147 SER A CA  1 
ATOM   698  C C   . SER A 1 87  ? 8.236   -29.367 42.058 1.00 13.84 ? 147 SER A C   1 
ATOM   699  O O   . SER A 1 87  ? 8.313   -28.132 41.991 1.00 12.86 ? 147 SER A O   1 
ATOM   700  C CB  . SER A 1 87  ? 6.123   -30.739 42.280 1.00 16.79 ? 147 SER A CB  1 
ATOM   701  O OG  . SER A 1 87  ? 5.382   -29.884 41.432 1.00 18.13 ? 147 SER A OG  1 
ATOM   702  N N   . SER A 1 88  ? 8.937   -30.173 41.259 1.00 10.81 ? 148 SER A N   1 
ATOM   703  C CA  . SER A 1 88  ? 10.044  -29.713 40.417 1.00 14.28 ? 148 SER A CA  1 
ATOM   704  C C   . SER A 1 88  ? 9.599   -29.268 39.034 1.00 13.78 ? 148 SER A C   1 
ATOM   705  O O   . SER A 1 88  ? 8.603   -29.758 38.515 1.00 13.67 ? 148 SER A O   1 
ATOM   706  C CB  . SER A 1 88  ? 11.081  -30.834 40.236 1.00 13.74 ? 148 SER A CB  1 
ATOM   707  O OG  . SER A 1 88  ? 11.771  -31.136 41.432 1.00 14.24 ? 148 SER A OG  1 
ATOM   708  N N   . VAL A 1 89  ? 10.288  -28.256 38.500 1.00 12.41 ? 149 VAL A N   1 
ATOM   709  C CA  . VAL A 1 89  ? 10.138  -27.870 37.097 1.00 13.47 ? 149 VAL A CA  1 
ATOM   710  C C   . VAL A 1 89  ? 11.557  -27.944 36.546 1.00 11.87 ? 149 VAL A C   1 
ATOM   711  O O   . VAL A 1 89  ? 12.535  -27.865 37.302 1.00 12.53 ? 149 VAL A O   1 
ATOM   712  C CB  . VAL A 1 89  ? 9.529   -26.446 36.905 1.00 11.21 ? 149 VAL A CB  1 
ATOM   713  C CG1 . VAL A 1 89  ? 8.075   -26.389 37.415 1.00 12.01 ? 149 VAL A CG1 1 
ATOM   714  C CG2 . VAL A 1 89  ? 10.390  -25.357 37.571 1.00 11.48 ? 149 VAL A CG2 1 
ATOM   715  N N   . PHE A 1 90  ? 11.678  -28.039 35.227 1.00 10.86 ? 150 PHE A N   1 
ATOM   716  C CA  . PHE A 1 90  ? 12.961  -28.317 34.572 1.00 10.52 ? 150 PHE A CA  1 
ATOM   717  C C   . PHE A 1 90  ? 13.115  -27.515 33.308 1.00 11.92 ? 150 PHE A C   1 
ATOM   718  O O   . PHE A 1 90  ? 12.137  -27.287 32.599 1.00 10.24 ? 150 PHE A O   1 
ATOM   719  C CB  . PHE A 1 90  ? 13.032  -29.796 34.184 1.00 11.79 ? 150 PHE A CB  1 
ATOM   720  C CG  . PHE A 1 90  ? 12.840  -30.738 35.326 1.00 13.65 ? 150 PHE A CG  1 
ATOM   721  C CD1 . PHE A 1 90  ? 13.938  -31.151 36.070 1.00 16.14 ? 150 PHE A CD1 1 
ATOM   722  C CD2 . PHE A 1 90  ? 11.583  -31.213 35.667 1.00 12.92 ? 150 PHE A CD2 1 
ATOM   723  C CE1 . PHE A 1 90  ? 13.800  -32.047 37.111 1.00 14.99 ? 150 PHE A CE1 1 
ATOM   724  C CE2 . PHE A 1 90  ? 11.429  -32.092 36.721 1.00 15.84 ? 150 PHE A CE2 1 
ATOM   725  C CZ  . PHE A 1 90  ? 12.557  -32.504 37.449 1.00 17.34 ? 150 PHE A CZ  1 
ATOM   726  N N   . ALA A 1 91  ? 14.340  -27.066 33.037 1.00 11.37 ? 151 ALA A N   1 
ATOM   727  C CA  . ALA A 1 91  ? 14.605  -26.404 31.776 1.00 11.57 ? 151 ALA A CA  1 
ATOM   728  C C   . ALA A 1 91  ? 14.168  -27.294 30.620 1.00 12.72 ? 151 ALA A C   1 
ATOM   729  O O   . ALA A 1 91  ? 14.506  -28.475 30.580 1.00 15.28 ? 151 ALA A O   1 
ATOM   730  C CB  . ALA A 1 91  ? 16.117  -26.191 31.669 1.00 12.94 ? 151 ALA A CB  1 
ATOM   731  N N   . GLN A 1 92  ? 13.427  -26.712 29.675 1.00 11.31 ? 152 GLN A N   1 
ATOM   732  C CA  . GLN A 1 92  ? 12.936  -27.398 28.478 1.00 10.71 ? 152 GLN A CA  1 
ATOM   733  C C   . GLN A 1 92  ? 13.617  -26.893 27.215 1.00 14.86 ? 152 GLN A C   1 
ATOM   734  O O   . GLN A 1 92  ? 13.124  -27.157 26.118 1.00 15.15 ? 152 GLN A O   1 
ATOM   735  C CB  . GLN A 1 92  ? 11.388  -27.278 28.446 1.00 11.43 ? 152 GLN A CB  1 
ATOM   736  C CG  . GLN A 1 92  ? 10.747  -28.043 29.619 1.00 11.88 ? 152 GLN A CG  1 
ATOM   737  C CD  . GLN A 1 92  ? 10.980  -29.551 29.617 1.00 14.92 ? 152 GLN A CD  1 
ATOM   738  O OE1 . GLN A 1 92  ? 10.486  -30.217 28.704 1.00 15.21 ? 152 GLN A OE1 1 
ATOM   739  N NE2 . GLN A 1 92  ? 11.972  -30.022 30.374 1.00 12.87 ? 152 GLN A NE2 1 
ATOM   740  O OXT . GLN A 1 92  ? 14.772  -26.432 27.198 1.00 20.60 ? 152 GLN A OXT 1 
ATOM   741  N N   . SER B 2 1   ? 23.753  -18.320 4.895  1.00 40.59 ? 153 SER B N   1 
ATOM   742  C CA  . SER B 2 1   ? 24.254  -17.796 6.152  1.00 41.81 ? 153 SER B CA  1 
ATOM   743  C C   . SER B 2 1   ? 23.114  -17.563 7.150  1.00 41.19 ? 153 SER B C   1 
ATOM   744  O O   . SER B 2 1   ? 23.326  -17.760 8.348  1.00 44.85 ? 153 SER B O   1 
ATOM   745  C CB  . SER B 2 1   ? 25.014  -16.484 5.928  1.00 44.01 ? 153 SER B CB  1 
ATOM   746  O OG  . SER B 2 1   ? 24.175  -15.488 5.365  1.00 50.13 ? 153 SER B OG  1 
ATOM   747  N N   . ILE B 2 2   ? 21.926  -17.154 6.688  1.00 33.50 ? 154 ILE B N   1 
ATOM   748  C CA  . ILE B 2 2   ? 20.771  -17.013 7.589  1.00 27.10 ? 154 ILE B CA  1 
ATOM   749  C C   . ILE B 2 2   ? 20.504  -18.372 8.243  1.00 22.98 ? 154 ILE B C   1 
ATOM   750  O O   . ILE B 2 2   ? 20.307  -19.375 7.551  1.00 24.99 ? 154 ILE B O   1 
ATOM   751  C CB  . ILE B 2 2   ? 19.481  -16.545 6.848  1.00 33.55 ? 154 ILE B CB  1 
ATOM   752  C CG1 . ILE B 2 2   ? 19.664  -15.144 6.253  1.00 35.16 ? 154 ILE B CG1 1 
ATOM   753  C CG2 . ILE B 2 2   ? 18.295  -16.458 7.800  1.00 29.25 ? 154 ILE B CG2 1 
ATOM   754  C CD1 . ILE B 2 2   ? 19.839  -14.039 7.276  1.00 34.27 ? 154 ILE B CD1 1 
ATOM   755  N N   . PRO B 2 3   ? 20.469  -18.421 9.582  1.00 23.41 ? 155 PRO B N   1 
ATOM   756  C CA  . PRO B 2 3   ? 20.057  -19.661 10.269 1.00 22.41 ? 155 PRO B CA  1 
ATOM   757  C C   . PRO B 2 3   ? 18.732  -20.220 9.739  1.00 18.20 ? 155 PRO B C   1 
ATOM   758  O O   . PRO B 2 3   ? 17.809  -19.437 9.502  1.00 19.44 ? 155 PRO B O   1 
ATOM   759  C CB  . PRO B 2 3   ? 19.886  -19.201 11.709 1.00 21.50 ? 155 PRO B CB  1 
ATOM   760  C CG  . PRO B 2 3   ? 20.867  -18.095 11.853 1.00 23.96 ? 155 PRO B CG  1 
ATOM   761  C CD  . PRO B 2 3   ? 20.812  -17.357 10.536 1.00 23.10 ? 155 PRO B CD  1 
ATOM   762  N N   . TRP B 2 4   ? 18.634  -21.537 9.586  1.00 18.15 ? 156 TRP B N   1 
ATOM   763  C CA  . TRP B 2 4   ? 17.468  -22.157 8.950  1.00 19.41 ? 156 TRP B CA  1 
ATOM   764  C C   . TRP B 2 4   ? 16.150  -21.733 9.621  1.00 16.73 ? 156 TRP B C   1 
ATOM   765  O O   . TRP B 2 4   ? 15.147  -21.533 8.956  1.00 16.99 ? 156 TRP B O   1 
ATOM   766  C CB  . TRP B 2 4   ? 17.608  -23.698 8.984  1.00 16.58 ? 156 TRP B CB  1 
ATOM   767  C CG  . TRP B 2 4   ? 17.218  -24.368 10.301 1.00 18.31 ? 156 TRP B CG  1 
ATOM   768  C CD1 . TRP B 2 4   ? 18.063  -24.762 11.309 1.00 17.25 ? 156 TRP B CD1 1 
ATOM   769  C CD2 . TRP B 2 4   ? 15.897  -24.728 10.732 1.00 18.14 ? 156 TRP B CD2 1 
ATOM   770  N NE1 . TRP B 2 4   ? 17.347  -25.323 12.338 1.00 15.39 ? 156 TRP B NE1 1 
ATOM   771  C CE2 . TRP B 2 4   ? 16.020  -25.319 12.008 1.00 16.79 ? 156 TRP B CE2 1 
ATOM   772  C CE3 . TRP B 2 4   ? 14.627  -24.616 10.158 1.00 18.10 ? 156 TRP B CE3 1 
ATOM   773  C CZ2 . TRP B 2 4   ? 14.926  -25.784 12.721 1.00 16.67 ? 156 TRP B CZ2 1 
ATOM   774  C CZ3 . TRP B 2 4   ? 13.530  -25.081 10.874 1.00 17.81 ? 156 TRP B CZ3 1 
ATOM   775  C CH2 . TRP B 2 4   ? 13.694  -25.663 12.138 1.00 15.26 ? 156 TRP B CH2 1 
ATOM   776  N N   . ASN B 2 5   ? 16.184  -21.604 10.944 1.00 15.27 ? 157 ASN B N   1 
ATOM   777  C CA  . ASN B 2 5   ? 15.017  -21.289 11.764 1.00 15.44 ? 157 ASN B CA  1 
ATOM   778  C C   . ASN B 2 5   ? 14.491  -19.870 11.549 1.00 15.91 ? 157 ASN B C   1 
ATOM   779  O O   . ASN B 2 5   ? 13.278  -19.609 11.593 1.00 15.76 ? 157 ASN B O   1 
ATOM   780  C CB  . ASN B 2 5   ? 15.347  -21.512 13.237 1.00 14.86 ? 157 ASN B CB  1 
ATOM   781  C CG  . ASN B 2 5   ? 16.598  -20.820 13.654 1.00 15.48 ? 157 ASN B CG  1 
ATOM   782  O OD1 . ASN B 2 5   ? 17.687  -21.179 13.207 1.00 14.17 ? 157 ASN B OD1 1 
ATOM   783  N ND2 . ASN B 2 5   ? 16.471  -19.842 14.570 1.00 13.32 ? 157 ASN B ND2 1 
ATOM   784  N N   . LEU B 2 6   ? 15.418  -18.940 11.341 1.00 13.88 ? 158 LEU B N   1 
ATOM   785  C CA  . LEU B 2 6   ? 15.013  -17.572 11.089 1.00 14.73 ? 158 LEU B CA  1 
ATOM   786  C C   . LEU B 2 6   ? 14.463  -17.403 9.680  1.00 17.71 ? 158 LEU B C   1 
ATOM   787  O O   . LEU B 2 6   ? 13.554  -16.594 9.457  1.00 16.98 ? 158 LEU B O   1 
ATOM   788  C CB  . LEU B 2 6   ? 16.178  -16.607 11.356 1.00 18.19 ? 158 LEU B CB  1 
ATOM   789  C CG  . LEU B 2 6   ? 16.745  -16.615 12.787 1.00 17.68 ? 158 LEU B CG  1 
ATOM   790  C CD1 . LEU B 2 6   ? 17.910  -15.611 12.943 1.00 17.40 ? 158 LEU B CD1 1 
ATOM   791  C CD2 . LEU B 2 6   ? 15.659  -16.371 13.818 1.00 14.84 ? 158 LEU B CD2 1 
ATOM   792  N N   . GLU B 2 7   ? 14.991  -18.176 8.729  1.00 15.92 ? 159 GLU B N   1 
ATOM   793  C CA  . GLU B 2 7   ? 14.372  -18.243 7.402  1.00 18.89 ? 159 GLU B CA  1 
ATOM   794  C C   . GLU B 2 7   ? 12.983  -18.900 7.444  1.00 16.59 ? 159 GLU B C   1 
ATOM   795  O O   . GLU B 2 7   ? 12.077  -18.503 6.708  1.00 16.44 ? 159 GLU B O   1 
ATOM   796  C CB  . GLU B 2 7   ? 15.260  -18.991 6.410  1.00 18.42 ? 159 GLU B CB  1 
ATOM   797  C CG  . GLU B 2 7   ? 14.849  -18.795 4.954  1.00 26.24 ? 159 GLU B CG  1 
ATOM   798  C CD  . GLU B 2 7   ? 14.759  -17.328 4.564  1.00 33.43 ? 159 GLU B CD  1 
ATOM   799  O OE1 . GLU B 2 7   ? 15.727  -16.578 4.856  1.00 35.11 ? 159 GLU B OE1 1 
ATOM   800  O OE2 . GLU B 2 7   ? 13.717  -16.897 4.009  1.00 31.77 ? 159 GLU B OE2 1 
ATOM   801  N N   . ARG B 2 8   ? 12.836  -19.935 8.268  1.00 15.88 ? 160 ARG B N   1 
ATOM   802  C CA  . ARG B 2 8   ? 11.598  -20.706 8.325  1.00 16.47 ? 160 ARG B CA  1 
ATOM   803  C C   . ARG B 2 8   ? 10.407  -19.835 8.781  1.00 17.02 ? 160 ARG B C   1 
ATOM   804  O O   . ARG B 2 8   ? 9.269   -20.021 8.337  1.00 17.27 ? 160 ARG B O   1 
ATOM   805  C CB  . ARG B 2 8   ? 11.762  -21.900 9.273  1.00 18.27 ? 160 ARG B CB  1 
ATOM   806  C CG  . ARG B 2 8   ? 10.616  -22.895 9.202  1.00 17.06 ? 160 ARG B CG  1 
ATOM   807  C CD  . ARG B 2 8   ? 10.460  -23.451 7.782  1.00 22.17 ? 160 ARG B CD  1 
ATOM   808  N NE  . ARG B 2 8   ? 11.752  -23.842 7.216  1.00 27.72 ? 160 ARG B NE  1 
ATOM   809  C CZ  . ARG B 2 8   ? 12.217  -25.092 7.194  1.00 27.00 ? 160 ARG B CZ  1 
ATOM   810  N NH1 . ARG B 2 8   ? 11.496  -26.085 7.719  1.00 28.08 ? 160 ARG B NH1 1 
ATOM   811  N NH2 . ARG B 2 8   ? 13.413  -25.353 6.667  1.00 25.82 ? 160 ARG B NH2 1 
ATOM   812  N N   . ILE B 2 9   ? 10.673  -18.899 9.688  1.00 15.37 ? 161 ILE B N   1 
ATOM   813  C CA  . ILE B 2 9   ? 9.616   -18.057 10.230 1.00 14.77 ? 161 ILE B CA  1 
ATOM   814  C C   . ILE B 2 9   ? 9.419   -16.807 9.385  1.00 17.90 ? 161 ILE B C   1 
ATOM   815  O O   . ILE B 2 9   ? 8.591   -15.956 9.700  1.00 17.33 ? 161 ILE B O   1 
ATOM   816  C CB  . ILE B 2 9   ? 9.870   -17.680 11.715 1.00 16.26 ? 161 ILE B CB  1 
ATOM   817  C CG1 . ILE B 2 9   ? 11.136  -16.841 11.878 1.00 13.38 ? 161 ILE B CG1 1 
ATOM   818  C CG2 . ILE B 2 9   ? 9.922   -18.930 12.606 1.00 12.34 ? 161 ILE B CG2 1 
ATOM   819  C CD1 . ILE B 2 9   ? 11.084  -15.910 13.080 1.00 14.55 ? 161 ILE B CD1 1 
ATOM   820  N N   . THR B 2 10  ? 10.221  -16.672 8.336  1.00 18.41 ? 162 THR B N   1 
ATOM   821  C CA  . THR B 2 10  ? 10.066  -15.541 7.427  1.00 17.77 ? 162 THR B CA  1 
ATOM   822  C C   . THR B 2 10  ? 8.927   -15.822 6.462  1.00 18.22 ? 162 THR B C   1 
ATOM   823  O O   . THR B 2 10  ? 8.943   -16.834 5.771  1.00 20.13 ? 162 THR B O   1 
ATOM   824  C CB  . THR B 2 10  ? 11.360  -15.279 6.640  1.00 21.76 ? 162 THR B CB  1 
ATOM   825  O OG1 . THR B 2 10  ? 12.392  -14.886 7.556  1.00 20.16 ? 162 THR B OG1 1 
ATOM   826  C CG2 . THR B 2 10  ? 11.170  -14.157 5.650  1.00 28.17 ? 162 THR B CG2 1 
ATOM   827  N N   . PRO B 2 11  ? 7.962   -14.911 6.365  1.00 21.41 ? 163 PRO B N   1 
ATOM   828  C CA  . PRO B 2 11  ? 6.773   -15.157 5.553  1.00 22.65 ? 163 PRO B CA  1 
ATOM   829  C C   . PRO B 2 11  ? 7.110   -15.042 4.051  1.00 23.66 ? 163 PRO B C   1 
ATOM   830  O O   . PRO B 2 11  ? 8.193   -14.582 3.713  1.00 22.37 ? 163 PRO B O   1 
ATOM   831  C CB  . PRO B 2 11  ? 5.819   -14.052 6.011  1.00 24.42 ? 163 PRO B CB  1 
ATOM   832  C CG  . PRO B 2 11  ? 6.705   -12.941 6.424  1.00 26.17 ? 163 PRO B CG  1 
ATOM   833  C CD  . PRO B 2 11  ? 7.951   -13.573 6.985  1.00 22.96 ? 163 PRO B CD  1 
ATOM   834  N N   . PRO B 2 12  ? 6.203   -15.491 3.167  1.00 26.53 ? 164 PRO B N   1 
ATOM   835  C CA  . PRO B 2 12  ? 6.445   -15.518 1.716  1.00 27.78 ? 164 PRO B CA  1 
ATOM   836  C C   . PRO B 2 12  ? 6.546   -14.129 1.089  1.00 30.55 ? 164 PRO B C   1 
ATOM   837  O O   . PRO B 2 12  ? 6.994   -14.012 -0.058 1.00 32.00 ? 164 PRO B O   1 
ATOM   838  C CB  . PRO B 2 12  ? 5.211   -16.266 1.176  1.00 31.72 ? 164 PRO B CB  1 
ATOM   839  C CG  . PRO B 2 12  ? 4.678   -17.008 2.363  1.00 30.67 ? 164 PRO B CG  1 
ATOM   840  C CD  . PRO B 2 12  ? 4.903   -16.090 3.505  1.00 29.89 ? 164 PRO B CD  1 
ATOM   841  N N   . ARG B 2 13  ? 6.171   -13.102 1.844  1.00 26.82 ? 165 ARG B N   1 
ATOM   842  C CA  . ARG B 2 13  ? 6.307   -11.722 1.400  1.00 32.23 ? 165 ARG B CA  1 
ATOM   843  C C   . ARG B 2 13  ? 6.724   -10.922 2.627  1.00 32.42 ? 165 ARG B C   1 
ATOM   844  O O   . ARG B 2 13  ? 6.034   -10.928 3.640  1.00 37.84 ? 165 ARG B O   1 
ATOM   845  C CB  . ARG B 2 13  ? 4.991   -11.214 0.805  1.00 35.68 ? 165 ARG B CB  1 
ATOM   846  C CG  . ARG B 2 13  ? 4.856   -9.716  0.794  1.00 42.67 ? 165 ARG B CG  1 
ATOM   847  C CD  . ARG B 2 13  ? 5.853   -9.179  -0.199 1.00 42.12 ? 165 ARG B CD  1 
ATOM   848  N NE  . ARG B 2 13  ? 5.297   -9.109  -1.551 1.00 51.38 ? 165 ARG B NE  1 
ATOM   849  C CZ  . ARG B 2 13  ? 4.673   -8.051  -2.057 1.00 49.95 ? 165 ARG B CZ  1 
ATOM   850  N NH1 . ARG B 2 13  ? 4.540   -6.950  -1.327 1.00 49.45 ? 165 ARG B NH1 1 
ATOM   851  N NH2 . ARG B 2 13  ? 4.219   -8.083  -3.304 1.00 44.65 ? 165 ARG B NH2 1 
ATOM   852  N N   . TYR B 2 14  ? 7.827   -10.193 2.544  1.00 31.64 ? 166 TYR B N   1 
ATOM   853  C CA  . TYR B 2 14  ? 8.284   -9.461  3.719  1.00 38.24 ? 166 TYR B CA  1 
ATOM   854  C C   . TYR B 2 14  ? 9.130   -8.228  3.397  1.00 42.69 ? 166 TYR B C   1 
ATOM   855  O O   . TYR B 2 14  ? 9.646   -8.073  2.283  1.00 35.18 ? 166 TYR B O   1 
ATOM   856  C CB  . TYR B 2 14  ? 9.036   -10.402 4.669  1.00 36.82 ? 166 TYR B CB  1 
ATOM   857  C CG  . TYR B 2 14  ? 10.341  -10.924 4.118  1.00 34.54 ? 166 TYR B CG  1 
ATOM   858  C CD1 . TYR B 2 14  ? 10.366  -11.937 3.167  1.00 36.80 ? 166 TYR B CD1 1 
ATOM   859  C CD2 . TYR B 2 14  ? 11.553  -10.415 4.564  1.00 39.19 ? 166 TYR B CD2 1 
ATOM   860  C CE1 . TYR B 2 14  ? 11.569  -12.422 2.663  1.00 40.02 ? 166 TYR B CE1 1 
ATOM   861  C CE2 . TYR B 2 14  ? 12.757  -10.887 4.070  1.00 38.91 ? 166 TYR B CE2 1 
ATOM   862  C CZ  . TYR B 2 14  ? 12.758  -11.891 3.123  1.00 38.14 ? 166 TYR B CZ  1 
ATOM   863  O OH  . TYR B 2 14  ? 13.960  -12.350 2.632  1.00 42.63 ? 166 TYR B OH  1 
ATOM   864  N N   . ARG B 2 15  ? 9.298   -7.385  4.413  1.00 44.58 ? 167 ARG B N   1 
ATOM   865  C CA  . ARG B 2 15  ? 9.835   -6.049  4.246  1.00 43.96 ? 167 ARG B CA  1 
ATOM   866  C C   . ARG B 2 15  ? 11.101  -5.840  5.068  1.00 45.10 ? 167 ARG B C   1 
ATOM   867  O O   . ARG B 2 15  ? 12.091  -6.559  4.907  1.00 45.09 ? 167 ARG B O   1 
ATOM   868  C CB  . ARG B 2 15  ? 8.757   -5.075  4.719  1.00 49.16 ? 167 ARG B CB  1 
ATOM   869  C CG  . ARG B 2 15  ? 8.990   -3.608  4.521  1.00 51.46 ? 167 ARG B CG  1 
ATOM   870  C CD  . ARG B 2 15  ? 8.267   -3.265  3.233  1.00 50.41 ? 167 ARG B CD  1 
ATOM   871  N NE  . ARG B 2 15  ? 8.412   -1.887  2.774  1.00 55.24 ? 167 ARG B NE  1 
ATOM   872  C CZ  . ARG B 2 15  ? 7.671   -1.370  1.795  1.00 57.02 ? 167 ARG B CZ  1 
ATOM   873  N NH1 . ARG B 2 15  ? 7.839   -0.105  1.420  1.00 53.17 ? 167 ARG B NH1 1 
ATOM   874  N NH2 . ARG B 2 15  ? 6.750   -2.124  1.192  1.00 49.93 ? 167 ARG B NH2 1 
ATOM   875  N N   . GLY B 2 24  ? 13.096  -5.618  16.166 1.00 45.18 ? 176 GLY B N   1 
ATOM   876  C CA  . GLY B 2 24  ? 11.718  -5.221  16.397 1.00 43.85 ? 176 GLY B CA  1 
ATOM   877  C C   . GLY B 2 24  ? 11.330  -5.461  17.845 1.00 40.78 ? 176 GLY B C   1 
ATOM   878  O O   . GLY B 2 24  ? 12.170  -5.886  18.637 1.00 38.40 ? 176 GLY B O   1 
ATOM   879  N N   . GLY B 2 25  ? 10.073  -5.208  18.205 1.00 36.91 ? 177 GLY B N   1 
ATOM   880  C CA  . GLY B 2 25  ? 9.641   -5.485  19.572 1.00 33.04 ? 177 GLY B CA  1 
ATOM   881  C C   . GLY B 2 25  ? 9.893   -4.471  20.694 1.00 36.76 ? 177 GLY B C   1 
ATOM   882  O O   . GLY B 2 25  ? 9.777   -4.837  21.858 1.00 37.46 ? 177 GLY B O   1 
ATOM   883  N N   . SER B 2 26  ? 10.169  -3.202  20.381 1.00 37.26 ? 178 SER B N   1 
ATOM   884  C CA  . SER B 2 26  ? 10.796  -2.277  21.350 1.00 37.99 ? 178 SER B CA  1 
ATOM   885  C C   . SER B 2 26  ? 9.848   -1.622  22.370 1.00 30.82 ? 178 SER B C   1 
ATOM   886  O O   . SER B 2 26  ? 10.238  -1.255  23.480 1.00 34.08 ? 178 SER B O   1 
ATOM   887  C CB  . SER B 2 26  ? 11.517  -1.177  20.582 1.00 35.33 ? 178 SER B CB  1 
ATOM   888  O OG  . SER B 2 26  ? 10.620  -0.578  19.659 1.00 43.41 ? 178 SER B OG  1 
ATOM   889  N N   . LEU B 2 27  ? 8.619   -1.408  21.941 1.00 31.96 ? 179 LEU B N   1 
ATOM   890  C CA  . LEU B 2 27  ? 7.517   -0.983  22.781 1.00 24.99 ? 179 LEU B CA  1 
ATOM   891  C C   . LEU B 2 27  ? 7.122   -2.122  23.762 1.00 20.94 ? 179 LEU B C   1 
ATOM   892  O O   . LEU B 2 27  ? 6.405   -1.906  24.752 1.00 16.94 ? 179 LEU B O   1 
ATOM   893  C CB  . LEU B 2 27  ? 6.414   -0.642  21.797 1.00 27.59 ? 179 LEU B CB  1 
ATOM   894  C CG  . LEU B 2 27  ? 4.953   -0.363  22.029 1.00 27.59 ? 179 LEU B CG  1 
ATOM   895  C CD1 . LEU B 2 27  ? 4.526   0.525   20.865 1.00 24.68 ? 179 LEU B CD1 1 
ATOM   896  C CD2 . LEU B 2 27  ? 4.188   -1.656  22.016 1.00 27.08 ? 179 LEU B CD2 1 
ATOM   897  N N   . VAL B 2 28  ? 7.547   -3.342  23.455 1.00 20.23 ? 180 VAL B N   1 
ATOM   898  C CA  . VAL B 2 28  ? 7.182   -4.516  24.249 1.00 19.26 ? 180 VAL B CA  1 
ATOM   899  C C   . VAL B 2 28  ? 8.360   -4.917  25.147 1.00 21.83 ? 180 VAL B C   1 
ATOM   900  O O   . VAL B 2 28  ? 9.520   -4.764  24.767 1.00 24.05 ? 180 VAL B O   1 
ATOM   901  C CB  . VAL B 2 28  ? 6.865   -5.671  23.278 1.00 20.52 ? 180 VAL B CB  1 
ATOM   902  C CG1 . VAL B 2 28  ? 6.537   -6.961  24.016 1.00 17.00 ? 180 VAL B CG1 1 
ATOM   903  C CG2 . VAL B 2 28  ? 5.730   -5.271  22.388 1.00 20.69 ? 180 VAL B CG2 1 
ATOM   904  N N   . GLU B 2 29  ? 8.071   -5.479  26.318 1.00 15.34 ? 181 GLU B N   1 
ATOM   905  C CA  . GLU B 2 29  ? 9.120   -6.033  27.151 1.00 15.43 ? 181 GLU B CA  1 
ATOM   906  C C   . GLU B 2 29  ? 8.877   -7.546  27.292 1.00 19.75 ? 181 GLU B C   1 
ATOM   907  O O   . GLU B 2 29  ? 7.719   -7.986  27.436 1.00 15.32 ? 181 GLU B O   1 
ATOM   908  C CB  . GLU B 2 29  ? 9.085   -5.315  28.499 1.00 23.74 ? 181 GLU B CB  1 
ATOM   909  C CG  . GLU B 2 29  ? 10.366  -4.507  28.756 1.00 37.24 ? 181 GLU B CG  1 
ATOM   910  C CD  . GLU B 2 29  ? 10.286  -3.645  30.002 1.00 37.36 ? 181 GLU B CD  1 
ATOM   911  O OE1 . GLU B 2 29  ? 9.734   -4.102  31.031 1.00 39.06 ? 181 GLU B OE1 1 
ATOM   912  O OE2 . GLU B 2 29  ? 10.759  -2.488  29.940 1.00 41.36 ? 181 GLU B OE2 1 
ATOM   913  N N   . VAL B 2 30  ? 9.942   -8.337  27.175 1.00 15.45 ? 182 VAL B N   1 
ATOM   914  C CA  . VAL B 2 30  ? 9.866   -9.801  27.324 1.00 14.98 ? 182 VAL B CA  1 
ATOM   915  C C   . VAL B 2 30  ? 10.541  -10.225 28.605 1.00 15.30 ? 182 VAL B C   1 
ATOM   916  O O   . VAL B 2 30  ? 11.741  -9.987  28.790 1.00 19.39 ? 182 VAL B O   1 
ATOM   917  C CB  . VAL B 2 30  ? 10.556  -10.522 26.142 1.00 14.59 ? 182 VAL B CB  1 
ATOM   918  C CG1 . VAL B 2 30  ? 10.401  -12.037 26.275 1.00 15.67 ? 182 VAL B CG1 1 
ATOM   919  C CG2 . VAL B 2 30  ? 9.946   -10.054 24.826 1.00 16.00 ? 182 VAL B CG2 1 
ATOM   920  N N   . TYR B 2 31  ? 9.783   -10.821 29.520 1.00 10.82 ? 183 TYR B N   1 
ATOM   921  C CA  . TYR B 2 31  ? 10.376  -11.405 30.710 1.00 13.15 ? 183 TYR B CA  1 
ATOM   922  C C   . TYR B 2 31  ? 10.784  -12.853 30.458 1.00 14.63 ? 183 TYR B C   1 
ATOM   923  O O   . TYR B 2 31  ? 10.073  -13.594 29.772 1.00 14.12 ? 183 TYR B O   1 
ATOM   924  C CB  . TYR B 2 31  ? 9.372   -11.357 31.856 1.00 14.26 ? 183 TYR B CB  1 
ATOM   925  C CG  . TYR B 2 31  ? 9.367   -10.056 32.595 1.00 16.59 ? 183 TYR B CG  1 
ATOM   926  C CD1 . TYR B 2 31  ? 8.564   -9.002  32.172 1.00 14.21 ? 183 TYR B CD1 1 
ATOM   927  C CD2 . TYR B 2 31  ? 10.153  -9.876  33.720 1.00 15.67 ? 183 TYR B CD2 1 
ATOM   928  C CE1 . TYR B 2 31  ? 8.542   -7.795  32.852 1.00 18.21 ? 183 TYR B CE1 1 
ATOM   929  C CE2 . TYR B 2 31  ? 10.141  -8.670  34.416 1.00 14.57 ? 183 TYR B CE2 1 
ATOM   930  C CZ  . TYR B 2 31  ? 9.333   -7.645  33.974 1.00 21.60 ? 183 TYR B CZ  1 
ATOM   931  O OH  . TYR B 2 31  ? 9.318   -6.446  34.648 1.00 17.65 ? 183 TYR B OH  1 
ATOM   932  N N   . LEU B 2 32  ? 11.946  -13.234 30.976 1.00 12.75 ? 184 LEU B N   1 
ATOM   933  C CA  . LEU B 2 32  ? 12.465  -14.592 30.855 1.00 12.84 ? 184 LEU B CA  1 
ATOM   934  C C   . LEU B 2 32  ? 12.616  -15.188 32.253 1.00 15.29 ? 184 LEU B C   1 
ATOM   935  O O   . LEU B 2 32  ? 13.263  -14.581 33.114 1.00 13.59 ? 184 LEU B O   1 
ATOM   936  C CB  . LEU B 2 32  ? 13.821  -14.570 30.124 1.00 12.43 ? 184 LEU B CB  1 
ATOM   937  C CG  . LEU B 2 32  ? 14.505  -15.931 29.979 1.00 14.78 ? 184 LEU B CG  1 
ATOM   938  C CD1 . LEU B 2 32  ? 13.548  -16.953 29.356 1.00 13.42 ? 184 LEU B CD1 1 
ATOM   939  C CD2 . LEU B 2 32  ? 15.790  -15.848 29.152 1.00 17.76 ? 184 LEU B CD2 1 
ATOM   940  N N   . LEU B 2 33  ? 12.004  -16.344 32.503 1.00 12.83 ? 185 LEU B N   1 
ATOM   941  C CA  . LEU B 2 33  ? 12.205  -17.054 33.763 1.00 12.01 ? 185 LEU B CA  1 
ATOM   942  C C   . LEU B 2 33  ? 13.058  -18.284 33.518 1.00 15.26 ? 185 LEU B C   1 
ATOM   943  O O   . LEU B 2 33  ? 12.596  -19.190 32.843 1.00 12.33 ? 185 LEU B O   1 
ATOM   944  C CB  . LEU B 2 33  ? 10.867  -17.482 34.394 1.00 13.18 ? 185 LEU B CB  1 
ATOM   945  C CG  . LEU B 2 33  ? 10.068  -16.390 35.105 1.00 17.22 ? 185 LEU B CG  1 
ATOM   946  C CD1 . LEU B 2 33  ? 9.366   -15.561 34.056 1.00 20.76 ? 185 LEU B CD1 1 
ATOM   947  C CD2 . LEU B 2 33  ? 9.092   -16.959 36.088 1.00 19.53 ? 185 LEU B CD2 1 
ATOM   948  N N   . ASP B 2 34  ? 14.299  -18.327 34.002 1.00 13.25 ? 186 ASP B N   1 
ATOM   949  C CA  . ASP B 2 34  ? 15.231  -19.333 33.497 1.00 14.90 ? 186 ASP B CA  1 
ATOM   950  C C   . ASP B 2 34  ? 16.415  -19.535 34.431 1.00 14.08 ? 186 ASP B C   1 
ATOM   951  O O   . ASP B 2 34  ? 16.360  -19.142 35.590 1.00 13.22 ? 186 ASP B O   1 
ATOM   952  C CB  . ASP B 2 34  ? 15.730  -18.865 32.130 1.00 14.34 ? 186 ASP B CB  1 
ATOM   953  C CG  . ASP B 2 34  ? 16.087  -20.006 31.205 1.00 20.35 ? 186 ASP B CG  1 
ATOM   954  O OD1 . ASP B 2 34  ? 16.781  -20.945 31.640 1.00 20.76 ? 186 ASP B OD1 1 
ATOM   955  O OD2 . ASP B 2 34  ? 15.710  -19.954 30.012 1.00 26.17 ? 186 ASP B OD2 1 
ATOM   956  N N   . THR B 2 35  ? 17.515  -20.066 33.897 1.00 14.37 ? 187 THR B N   1 
ATOM   957  C CA  . THR B 2 35  ? 18.767  -20.184 34.647 1.00 14.41 ? 187 THR B CA  1 
ATOM   958  C C   . THR B 2 35  ? 19.327  -18.774 34.703 1.00 15.53 ? 187 THR B C   1 
ATOM   959  O O   . THR B 2 35  ? 18.738  -17.839 34.161 1.00 13.45 ? 187 THR B O   1 
ATOM   960  C CB  . THR B 2 35  ? 19.787  -21.072 33.922 1.00 16.22 ? 187 THR B CB  1 
ATOM   961  O OG1 . THR B 2 35  ? 20.107  -20.478 32.657 1.00 14.27 ? 187 THR B OG1 1 
ATOM   962  C CG2 . THR B 2 35  ? 19.250  -22.494 33.708 1.00 13.81 ? 187 THR B CG2 1 
ATOM   963  N N   . SER B 2 36  ? 20.460  -18.600 35.368 1.00 17.01 ? 188 SER B N   1 
ATOM   964  C CA  . SER B 2 36  ? 21.134  -17.323 35.301 1.00 16.57 ? 188 SER B CA  1 
ATOM   965  C C   . SER B 2 36  ? 21.587  -17.131 33.854 1.00 19.85 ? 188 SER B C   1 
ATOM   966  O O   . SER B 2 36  ? 21.630  -18.078 33.068 1.00 18.75 ? 188 SER B O   1 
ATOM   967  C CB  . SER B 2 36  ? 22.322  -17.330 36.271 1.00 18.59 ? 188 SER B CB  1 
ATOM   968  O OG  . SER B 2 36  ? 23.108  -18.481 36.070 1.00 28.68 ? 188 SER B OG  1 
ATOM   969  N N   . ILE B 2 37  ? 21.893  -15.901 33.477 1.00 17.41 ? 189 ILE B N   1 
ATOM   970  C CA  . ILE B 2 37  ? 22.304  -15.657 32.105 1.00 20.08 ? 189 ILE B CA  1 
ATOM   971  C C   . ILE B 2 37  ? 23.649  -14.900 32.076 1.00 20.83 ? 189 ILE B C   1 
ATOM   972  O O   . ILE B 2 37  ? 23.979  -14.177 33.014 1.00 19.21 ? 189 ILE B O   1 
ATOM   973  C CB  . ILE B 2 37  ? 21.220  -14.911 31.316 1.00 19.71 ? 189 ILE B CB  1 
ATOM   974  C CG1 . ILE B 2 37  ? 21.076  -13.524 31.859 1.00 25.16 ? 189 ILE B CG1 1 
ATOM   975  C CG2 . ILE B 2 37  ? 19.799  -15.661 31.401 1.00 18.69 ? 189 ILE B CG2 1 
ATOM   976  C CD1 . ILE B 2 37  ? 20.302  -12.667 30.957 1.00 32.80 ? 189 ILE B CD1 1 
ATOM   977  N N   . GLN B 2 38  ? 24.426  -15.072 31.017 1.00 18.81 ? 190 GLN B N   1 
ATOM   978  C CA  . GLN B 2 38  ? 25.636  -14.255 30.819 1.00 20.94 ? 190 GLN B CA  1 
ATOM   979  C C   . GLN B 2 38  ? 25.213  -12.986 30.096 1.00 19.79 ? 190 GLN B C   1 
ATOM   980  O O   . GLN B 2 38  ? 25.188  -12.931 28.875 1.00 20.69 ? 190 GLN B O   1 
ATOM   981  C CB  . GLN B 2 38  ? 26.655  -15.082 30.025 1.00 20.77 ? 190 GLN B CB  1 
ATOM   982  C CG  . GLN B 2 38  ? 28.091  -14.537 29.985 1.00 30.34 ? 190 GLN B CG  1 
ATOM   983  C CD  . GLN B 2 38  ? 28.893  -15.126 28.820 1.00 37.21 ? 190 GLN B CD  1 
ATOM   984  O OE1 . GLN B 2 38  ? 28.406  -15.182 27.685 1.00 44.55 ? 190 GLN B OE1 1 
ATOM   985  N NE2 . GLN B 2 38  ? 30.119  -15.573 29.095 1.00 40.63 ? 190 GLN B NE2 1 
ATOM   986  N N   . SER B 2 39  ? 24.843  -11.960 30.861 1.00 21.83 ? 191 SER B N   1 
ATOM   987  C CA  . SER B 2 39  ? 24.223  -10.757 30.297 1.00 25.12 ? 191 SER B CA  1 
ATOM   988  C C   . SER B 2 39  ? 25.186  -9.846  29.503 1.00 26.65 ? 191 SER B C   1 
ATOM   989  O O   . SER B 2 39  ? 24.749  -8.930  28.805 1.00 25.83 ? 191 SER B O   1 
ATOM   990  C CB  . SER B 2 39  ? 23.575  -9.932  31.413 1.00 22.80 ? 191 SER B CB  1 
ATOM   991  O OG  . SER B 2 39  ? 24.492  -9.737  32.482 1.00 26.99 ? 191 SER B OG  1 
ATOM   992  N N   . ASP B 2 40  ? 26.483  -10.089 29.632 1.00 29.62 ? 192 ASP B N   1 
ATOM   993  C CA  . ASP B 2 40  ? 27.492  -9.331  28.881 1.00 31.42 ? 192 ASP B CA  1 
ATOM   994  C C   . ASP B 2 40  ? 27.863  -9.981  27.552 1.00 32.04 ? 192 ASP B C   1 
ATOM   995  O O   . ASP B 2 40  ? 28.700  -9.451  26.823 1.00 28.42 ? 192 ASP B O   1 
ATOM   996  C CB  . ASP B 2 40  ? 28.745  -9.147  29.729 1.00 32.77 ? 192 ASP B CB  1 
ATOM   997  C CG  . ASP B 2 40  ? 28.480  -8.319  30.965 1.00 43.00 ? 192 ASP B CG  1 
ATOM   998  O OD1 . ASP B 2 40  ? 27.484  -7.560  30.954 1.00 45.03 ? 192 ASP B OD1 1 
ATOM   999  O OD2 . ASP B 2 40  ? 29.264  -8.409  31.935 1.00 54.79 ? 192 ASP B OD2 1 
ATOM   1000 N N   . HIS B 2 41  ? 27.256  -11.125 27.242 1.00 24.41 ? 193 HIS B N   1 
ATOM   1001 C CA  . HIS B 2 41  ? 27.455  -11.729 25.937 1.00 25.47 ? 193 HIS B CA  1 
ATOM   1002 C C   . HIS B 2 41  ? 27.071  -10.727 24.864 1.00 24.59 ? 193 HIS B C   1 
ATOM   1003 O O   . HIS B 2 41  ? 26.131  -9.964  25.043 1.00 23.95 ? 193 HIS B O   1 
ATOM   1004 C CB  . HIS B 2 41  ? 26.603  -12.998 25.800 1.00 24.16 ? 193 HIS B CB  1 
ATOM   1005 C CG  . HIS B 2 41  ? 26.987  -13.844 24.633 1.00 23.24 ? 193 HIS B CG  1 
ATOM   1006 N ND1 . HIS B 2 41  ? 26.727  -13.467 23.334 1.00 20.29 ? 193 HIS B ND1 1 
ATOM   1007 C CD2 . HIS B 2 41  ? 27.636  -15.027 24.558 1.00 20.93 ? 193 HIS B CD2 1 
ATOM   1008 C CE1 . HIS B 2 41  ? 27.190  -14.388 22.507 1.00 20.52 ? 193 HIS B CE1 1 
ATOM   1009 N NE2 . HIS B 2 41  ? 27.748  -15.345 23.224 1.00 20.52 ? 193 HIS B NE2 1 
ATOM   1010 N N   . ARG B 2 42  ? 27.781  -10.723 23.733 1.00 27.01 ? 194 ARG B N   1 
ATOM   1011 C CA  . ARG B 2 42  ? 27.589  -9.657  22.740 1.00 24.77 ? 194 ARG B CA  1 
ATOM   1012 C C   . ARG B 2 42  ? 26.292  -9.767  21.952 1.00 28.10 ? 194 ARG B C   1 
ATOM   1013 O O   . ARG B 2 42  ? 25.818  -8.772  21.408 1.00 23.49 ? 194 ARG B O   1 
ATOM   1014 C CB  . ARG B 2 42  ? 28.780  -9.581  21.772 1.00 29.70 ? 194 ARG B CB  1 
ATOM   1015 C CG  . ARG B 2 42  ? 30.116  -9.586  22.467 1.00 38.00 ? 194 ARG B CG  1 
ATOM   1016 C CD  . ARG B 2 42  ? 30.454  -8.212  23.025 1.00 41.72 ? 194 ARG B CD  1 
ATOM   1017 N NE  . ARG B 2 42  ? 31.242  -8.344  24.247 1.00 46.27 ? 194 ARG B NE  1 
ATOM   1018 C CZ  . ARG B 2 42  ? 30.823  -7.935  25.442 1.00 45.41 ? 194 ARG B CZ  1 
ATOM   1019 N NH1 . ARG B 2 42  ? 29.641  -7.342  25.559 1.00 44.64 ? 194 ARG B NH1 1 
ATOM   1020 N NH2 . ARG B 2 42  ? 31.583  -8.114  26.516 1.00 50.16 ? 194 ARG B NH2 1 
ATOM   1021 N N   . GLU B 2 43  ? 25.679  -10.949 21.935 1.00 26.11 ? 195 GLU B N   1 
ATOM   1022 C CA  . GLU B 2 43  ? 24.365  -11.051 21.318 1.00 24.41 ? 195 GLU B CA  1 
ATOM   1023 C C   . GLU B 2 43  ? 23.350  -10.230 22.058 1.00 22.19 ? 195 GLU B C   1 
ATOM   1024 O O   . GLU B 2 43  ? 22.423  -9.691  21.458 1.00 26.28 ? 195 GLU B O   1 
ATOM   1025 C CB  . GLU B 2 43  ? 23.868  -12.510 21.295 1.00 27.23 ? 195 GLU B CB  1 
ATOM   1026 C CG  . GLU B 2 43  ? 24.326  -13.306 20.117 1.00 22.78 ? 195 GLU B CG  1 
ATOM   1027 C CD  . GLU B 2 43  ? 23.570  -12.879 18.857 1.00 27.00 ? 195 GLU B CD  1 
ATOM   1028 O OE1 . GLU B 2 43  ? 24.047  -11.905 18.226 1.00 24.63 ? 195 GLU B OE1 1 
ATOM   1029 O OE2 . GLU B 2 43  ? 22.507  -13.473 18.507 1.00 22.86 ? 195 GLU B OE2 1 
ATOM   1030 N N   . ILE B 2 44  ? 23.540  -10.116 23.366 1.00 23.61 ? 196 ILE B N   1 
ATOM   1031 C CA  . ILE B 2 44  ? 22.486  -9.578  24.225 1.00 26.11 ? 196 ILE B CA  1 
ATOM   1032 C C   . ILE B 2 44  ? 22.856  -8.435  25.176 1.00 26.28 ? 196 ILE B C   1 
ATOM   1033 O O   . ILE B 2 44  ? 21.967  -7.794  25.730 1.00 24.16 ? 196 ILE B O   1 
ATOM   1034 C CB  . ILE B 2 44  ? 21.850  -10.721 25.048 1.00 23.01 ? 196 ILE B CB  1 
ATOM   1035 C CG1 . ILE B 2 44  ? 22.926  -11.387 25.907 1.00 23.22 ? 196 ILE B CG1 1 
ATOM   1036 C CG2 . ILE B 2 44  ? 21.231  -11.762 24.126 1.00 23.24 ? 196 ILE B CG2 1 
ATOM   1037 C CD1 . ILE B 2 44  ? 22.419  -12.410 26.882 1.00 20.22 ? 196 ILE B CD1 1 
ATOM   1038 N N   . GLU B 2 45  ? 24.153  -8.249  25.430 1.00 27.05 ? 197 GLU B N   1 
ATOM   1039 C CA  . GLU B 2 45  ? 24.672  -7.088  26.169 1.00 30.71 ? 197 GLU B CA  1 
ATOM   1040 C C   . GLU B 2 45  ? 23.847  -5.834  25.923 1.00 25.37 ? 197 GLU B C   1 
ATOM   1041 O O   . GLU B 2 45  ? 23.640  -5.444  24.773 1.00 27.09 ? 197 GLU B O   1 
ATOM   1042 C CB  . GLU B 2 45  ? 26.119  -6.821  25.777 1.00 34.06 ? 197 GLU B CB  1 
ATOM   1043 C CG  . GLU B 2 45  ? 26.565  -5.401  26.022 1.00 39.42 ? 197 GLU B CG  1 
ATOM   1044 C CD  . GLU B 2 45  ? 27.824  -5.103  25.263 1.00 51.27 ? 197 GLU B CD  1 
ATOM   1045 O OE1 . GLU B 2 45  ? 27.779  -5.107  24.010 1.00 52.45 ? 197 GLU B OE1 1 
ATOM   1046 O OE2 . GLU B 2 45  ? 28.880  -4.937  25.917 1.00 59.76 ? 197 GLU B OE2 1 
ATOM   1047 N N   . GLY B 2 46  ? 23.369  -5.207  26.999 1.00 25.45 ? 198 GLY B N   1 
ATOM   1048 C CA  . GLY B 2 46  ? 22.611  -3.977  26.861 1.00 28.38 ? 198 GLY B CA  1 
ATOM   1049 C C   . GLY B 2 46  ? 21.172  -4.212  26.437 1.00 34.49 ? 198 GLY B C   1 
ATOM   1050 O O   . GLY B 2 46  ? 20.389  -3.274  26.361 1.00 38.64 ? 198 GLY B O   1 
ATOM   1051 N N   . ARG B 2 47  ? 20.806  -5.462  26.175 1.00 30.09 ? 199 ARG B N   1 
ATOM   1052 C CA  . ARG B 2 47  ? 19.435  -5.718  25.773 1.00 34.17 ? 199 ARG B CA  1 
ATOM   1053 C C   . ARG B 2 47  ? 18.650  -6.505  26.826 1.00 27.45 ? 199 ARG B C   1 
ATOM   1054 O O   . ARG B 2 47  ? 17.434  -6.405  26.928 1.00 29.00 ? 199 ARG B O   1 
ATOM   1055 C CB  . ARG B 2 47  ? 19.410  -6.434  24.424 1.00 34.42 ? 199 ARG B CB  1 
ATOM   1056 C CG  . ARG B 2 47  ? 19.828  -5.532  23.299 1.00 43.95 ? 199 ARG B CG  1 
ATOM   1057 C CD  . ARG B 2 47  ? 19.104  -4.228  23.230 1.00 47.46 ? 199 ARG B CD  1 
ATOM   1058 N NE  . ARG B 2 47  ? 19.279  -3.667  21.896 1.00 58.12 ? 199 ARG B NE  1 
ATOM   1059 C CZ  . ARG B 2 47  ? 20.378  -3.010  21.523 1.00 60.18 ? 199 ARG B CZ  1 
ATOM   1060 N NH1 . ARG B 2 47  ? 21.375  -2.845  22.390 1.00 56.89 ? 199 ARG B NH1 1 
ATOM   1061 N NH2 . ARG B 2 47  ? 20.493  -2.525  20.292 1.00 60.53 ? 199 ARG B NH2 1 
ATOM   1062 N N   . VAL B 2 48  ? 19.377  -7.279  27.620 1.00 26.01 ? 200 VAL B N   1 
ATOM   1063 C CA  . VAL B 2 48  ? 18.792  -7.978  28.741 1.00 24.79 ? 200 VAL B CA  1 
ATOM   1064 C C   . VAL B 2 48  ? 19.115  -7.303  30.070 1.00 27.16 ? 200 VAL B C   1 
ATOM   1065 O O   . VAL B 2 48  ? 20.284  -7.120  30.404 1.00 29.82 ? 200 VAL B O   1 
ATOM   1066 C CB  . VAL B 2 48  ? 19.235  -9.439  28.800 1.00 27.11 ? 200 VAL B CB  1 
ATOM   1067 C CG1 . VAL B 2 48  ? 18.481  -10.105 29.914 1.00 24.39 ? 200 VAL B CG1 1 
ATOM   1068 C CG2 . VAL B 2 48  ? 18.937  -10.140 27.473 1.00 27.06 ? 200 VAL B CG2 1 
ATOM   1069 N N   . MET B 2 49  ? 18.092  -6.985  30.849 1.00 23.21 ? 201 MET B N   1 
ATOM   1070 C CA  . MET B 2 49  ? 18.306  -6.537  32.218 1.00 23.77 ? 201 MET B CA  1 
ATOM   1071 C C   . MET B 2 49  ? 18.134  -7.693  33.176 1.00 20.65 ? 201 MET B C   1 
ATOM   1072 O O   . MET B 2 49  ? 17.058  -8.288  33.250 1.00 21.06 ? 201 MET B O   1 
ATOM   1073 C CB  . MET B 2 49  ? 17.305  -5.465  32.604 1.00 21.04 ? 201 MET B CB  1 
ATOM   1074 C CG  . MET B 2 49  ? 17.647  -4.931  33.963 1.00 29.74 ? 201 MET B CG  1 
ATOM   1075 S SD  . MET B 2 49  ? 16.224  -5.143  35.062 1.00 41.14 ? 201 MET B SD  1 
ATOM   1076 C CE  . MET B 2 49  ? 16.887  -4.423  36.572 1.00 31.00 ? 201 MET B CE  1 
ATOM   1077 N N   . VAL B 2 50  ? 19.170  -7.983  33.952 1.00 16.77 ? 202 VAL B N   1 
ATOM   1078 C CA  . VAL B 2 50  ? 19.071  -9.000  34.995 1.00 19.43 ? 202 VAL B CA  1 
ATOM   1079 C C   . VAL B 2 50  ? 18.408  -8.431  36.245 1.00 21.63 ? 202 VAL B C   1 
ATOM   1080 O O   . VAL B 2 50  ? 18.898  -7.453  36.808 1.00 18.35 ? 202 VAL B O   1 
ATOM   1081 C CB  . VAL B 2 50  ? 20.460  -9.579  35.358 1.00 19.10 ? 202 VAL B CB  1 
ATOM   1082 C CG1 . VAL B 2 50  ? 20.346  -10.594 36.483 1.00 18.14 ? 202 VAL B CG1 1 
ATOM   1083 C CG2 . VAL B 2 50  ? 21.092  -10.235 34.128 1.00 19.57 ? 202 VAL B CG2 1 
ATOM   1084 N N   . THR B 2 51  ? 17.273  -9.001  36.664 1.00 16.96 ? 203 THR B N   1 
ATOM   1085 C CA  . THR B 2 51  ? 16.536  -8.404  37.769 1.00 14.53 ? 203 THR B CA  1 
ATOM   1086 C C   . THR B 2 51  ? 17.244  -8.729  39.079 1.00 19.43 ? 203 THR B C   1 
ATOM   1087 O O   . THR B 2 51  ? 17.102  -8.012  40.062 1.00 18.45 ? 203 THR B O   1 
ATOM   1088 C CB  . THR B 2 51  ? 15.081  -8.945  37.859 1.00 19.63 ? 203 THR B CB  1 
ATOM   1089 O OG1 . THR B 2 51  ? 15.098  -10.365 38.084 1.00 14.17 ? 203 THR B OG1 1 
ATOM   1090 C CG2 . THR B 2 51  ? 14.272  -8.577  36.625 1.00 17.25 ? 203 THR B CG2 1 
ATOM   1091 N N   . ASP B 2 52  ? 18.014  -9.818  39.063 1.00 17.18 ? 204 ASP B N   1 
ATOM   1092 C CA  . ASP B 2 52  ? 18.553  -10.476 40.264 1.00 19.91 ? 204 ASP B CA  1 
ATOM   1093 C C   . ASP B 2 52  ? 17.473  -11.018 41.209 1.00 20.58 ? 204 ASP B C   1 
ATOM   1094 O O   . ASP B 2 52  ? 17.767  -11.412 42.344 1.00 17.21 ? 204 ASP B O   1 
ATOM   1095 C CB  . ASP B 2 52  ? 19.577  -9.609  41.022 1.00 25.03 ? 204 ASP B CB  1 
ATOM   1096 C CG  . ASP B 2 52  ? 20.914  -9.506  40.302 1.00 28.39 ? 204 ASP B CG  1 
ATOM   1097 O OD1 . ASP B 2 52  ? 21.407  -10.556 39.848 1.00 26.72 ? 204 ASP B OD1 1 
ATOM   1098 O OD2 . ASP B 2 52  ? 21.524  -8.416  40.273 1.00 29.74 ? 204 ASP B OD2 1 
ATOM   1099 N N   . PHE B 2 53  ? 16.241  -11.118 40.719 1.00 19.35 ? 205 PHE B N   1 
ATOM   1100 C CA  . PHE B 2 53  ? 15.304  -12.012 41.377 1.00 15.34 ? 205 PHE B CA  1 
ATOM   1101 C C   . PHE B 2 53  ? 15.844  -13.415 41.255 1.00 16.80 ? 205 PHE B C   1 
ATOM   1102 O O   . PHE B 2 53  ? 16.246  -13.840 40.164 1.00 16.11 ? 205 PHE B O   1 
ATOM   1103 C CB  . PHE B 2 53  ? 13.916  -11.991 40.741 1.00 18.41 ? 205 PHE B CB  1 
ATOM   1104 C CG  . PHE B 2 53  ? 12.985  -13.016 41.345 1.00 18.27 ? 205 PHE B CG  1 
ATOM   1105 C CD1 . PHE B 2 53  ? 12.928  -14.310 40.843 1.00 15.75 ? 205 PHE B CD1 1 
ATOM   1106 C CD2 . PHE B 2 53  ? 12.217  -12.697 42.449 1.00 18.58 ? 205 PHE B CD2 1 
ATOM   1107 C CE1 . PHE B 2 53  ? 12.100  -15.262 41.427 1.00 15.81 ? 205 PHE B CE1 1 
ATOM   1108 C CE2 . PHE B 2 53  ? 11.398  -13.631 43.032 1.00 18.71 ? 205 PHE B CE2 1 
ATOM   1109 C CZ  . PHE B 2 53  ? 11.327  -14.913 42.518 1.00 16.51 ? 205 PHE B CZ  1 
ATOM   1110 N N   . GLU B 2 54  ? 15.850  -14.139 42.364 1.00 14.03 ? 206 GLU B N   1 
ATOM   1111 C CA  . GLU B 2 54  ? 16.312  -15.519 42.356 1.00 15.50 ? 206 GLU B CA  1 
ATOM   1112 C C   . GLU B 2 54  ? 15.499  -16.334 43.357 1.00 19.61 ? 206 GLU B C   1 
ATOM   1113 O O   . GLU B 2 54  ? 15.254  -15.884 44.475 1.00 18.30 ? 206 GLU B O   1 
ATOM   1114 C CB  . GLU B 2 54  ? 17.809  -15.541 42.740 1.00 18.43 ? 206 GLU B CB  1 
ATOM   1115 C CG  . GLU B 2 54  ? 18.355  -16.928 43.029 1.00 26.31 ? 206 GLU B CG  1 
ATOM   1116 C CD  . GLU B 2 54  ? 19.877  -16.966 43.214 1.00 31.38 ? 206 GLU B CD  1 
ATOM   1117 O OE1 . GLU B 2 54  ? 20.625  -16.411 42.371 1.00 26.24 ? 206 GLU B OE1 1 
ATOM   1118 O OE2 . GLU B 2 54  ? 20.316  -17.520 44.248 1.00 40.48 ? 206 GLU B OE2 1 
ATOM   1119 N N   . ASN B 2 55  ? 14.941  -17.456 42.899 1.00 14.69 ? 207 ASN B N   1 
ATOM   1120 C CA  . ASN B 2 55  ? 14.314  -18.448 43.782 1.00 16.03 ? 207 ASN B CA  1 
ATOM   1121 C C   . ASN B 2 55  ? 14.538  -19.823 43.185 1.00 16.00 ? 207 ASN B C   1 
ATOM   1122 O O   . ASN B 2 55  ? 13.878  -20.187 42.207 1.00 12.63 ? 207 ASN B O   1 
ATOM   1123 C CB  . ASN B 2 55  ? 12.809  -18.206 43.951 1.00 16.27 ? 207 ASN B CB  1 
ATOM   1124 C CG  . ASN B 2 55  ? 12.232  -18.972 45.146 1.00 15.96 ? 207 ASN B CG  1 
ATOM   1125 O OD1 . ASN B 2 55  ? 12.181  -20.207 45.127 1.00 16.48 ? 207 ASN B OD1 1 
ATOM   1126 N ND2 . ASN B 2 55  ? 11.827  -18.257 46.194 1.00 16.40 ? 207 ASN B ND2 1 
ATOM   1127 N N   . VAL B 2 56  ? 15.555  -20.525 43.672 1.00 17.63 ? 208 VAL B N   1 
ATOM   1128 C CA  . VAL B 2 56  ? 15.988  -21.790 43.083 1.00 17.19 ? 208 VAL B CA  1 
ATOM   1129 C C   . VAL B 2 56  ? 16.271  -22.794 44.190 1.00 18.29 ? 208 VAL B C   1 
ATOM   1130 O O   . VAL B 2 56  ? 16.653  -22.400 45.284 1.00 16.31 ? 208 VAL B O   1 
ATOM   1131 C CB  . VAL B 2 56  ? 17.263  -21.606 42.220 1.00 17.19 ? 208 VAL B CB  1 
ATOM   1132 C CG1 . VAL B 2 56  ? 16.999  -20.613 41.103 1.00 17.56 ? 208 VAL B CG1 1 
ATOM   1133 C CG2 . VAL B 2 56  ? 18.464  -21.153 43.073 1.00 19.75 ? 208 VAL B CG2 1 
ATOM   1134 N N   . PRO B 2 57  ? 16.047  -24.102 43.937 1.00 18.60 ? 209 PRO B N   1 
ATOM   1135 C CA  . PRO B 2 57  ? 16.393  -25.100 44.962 1.00 20.19 ? 209 PRO B CA  1 
ATOM   1136 C C   . PRO B 2 57  ? 17.910  -25.354 44.990 1.00 24.20 ? 209 PRO B C   1 
ATOM   1137 O O   . PRO B 2 57  ? 18.593  -25.045 44.020 1.00 23.60 ? 209 PRO B O   1 
ATOM   1138 C CB  . PRO B 2 57  ? 15.614  -26.345 44.497 1.00 19.10 ? 209 PRO B CB  1 
ATOM   1139 C CG  . PRO B 2 57  ? 15.578  -26.205 42.992 1.00 18.82 ? 209 PRO B CG  1 
ATOM   1140 C CD  . PRO B 2 57  ? 15.534  -24.715 42.698 1.00 18.80 ? 209 PRO B CD  1 
ATOM   1141 N N   . GLU B 2 58  ? 18.437  -25.888 46.083 1.00 26.45 ? 210 GLU B N   1 
ATOM   1142 C CA  . GLU B 2 58  ? 19.873  -26.173 46.161 1.00 36.76 ? 210 GLU B CA  1 
ATOM   1143 C C   . GLU B 2 58  ? 20.257  -27.294 45.206 1.00 36.07 ? 210 GLU B C   1 
ATOM   1144 O O   . GLU B 2 58  ? 19.440  -28.161 44.898 1.00 34.51 ? 210 GLU B O   1 
ATOM   1145 C CB  . GLU B 2 58  ? 20.287  -26.536 47.591 1.00 41.77 ? 210 GLU B CB  1 
ATOM   1146 C CG  . GLU B 2 58  ? 19.599  -27.723 48.208 1.00 49.30 ? 210 GLU B CG  1 
ATOM   1147 C CD  . GLU B 2 58  ? 20.143  -28.036 49.598 1.00 63.40 ? 210 GLU B CD  1 
ATOM   1148 O OE1 . GLU B 2 58  ? 21.227  -28.662 49.686 1.00 63.37 ? 210 GLU B OE1 1 
ATOM   1149 O OE2 . GLU B 2 58  ? 19.503  -27.630 50.596 1.00 66.47 ? 210 GLU B OE2 1 
ATOM   1150 N N   . GLU B 2 59  ? 21.499  -27.284 44.739 1.00 37.70 ? 211 GLU B N   1 
ATOM   1151 C CA  . GLU B 2 59  ? 21.981  -28.331 43.837 1.00 43.16 ? 211 GLU B CA  1 
ATOM   1152 C C   . GLU B 2 59  ? 21.993  -29.692 44.546 1.00 46.13 ? 211 GLU B C   1 
ATOM   1153 O O   . GLU B 2 59  ? 22.055  -29.771 45.775 1.00 45.97 ? 211 GLU B O   1 
ATOM   1154 C CB  . GLU B 2 59  ? 23.370  -27.990 43.286 1.00 40.19 ? 211 GLU B CB  1 
ATOM   1155 C CG  . GLU B 2 59  ? 23.364  -27.013 42.098 1.00 35.64 ? 211 GLU B CG  1 
ATOM   1156 C CD  . GLU B 2 59  ? 23.039  -25.582 42.489 1.00 40.38 ? 211 GLU B CD  1 
ATOM   1157 O OE1 . GLU B 2 59  ? 23.007  -25.293 43.710 1.00 47.86 ? 211 GLU B OE1 1 
ATOM   1158 O OE2 . GLU B 2 59  ? 22.793  -24.740 41.577 1.00 32.73 ? 211 GLU B OE2 1 
ATOM   1159 N N   . ASP B 2 60  ? 21.929  -30.756 43.749 1.00 47.83 ? 212 ASP B N   1 
ATOM   1160 C CA  . ASP B 2 60  ? 21.783  -32.122 44.259 1.00 51.35 ? 212 ASP B CA  1 
ATOM   1161 C C   . ASP B 2 60  ? 22.017  -33.166 43.175 1.00 51.70 ? 212 ASP B C   1 
ATOM   1162 O O   . ASP B 2 60  ? 23.085  -33.193 42.562 1.00 49.12 ? 212 ASP B O   1 
ATOM   1163 C CB  . ASP B 2 60  ? 20.391  -32.326 44.850 1.00 55.25 ? 212 ASP B CB  1 
ATOM   1164 C CG  . ASP B 2 60  ? 19.318  -32.399 43.769 1.00 57.56 ? 212 ASP B CG  1 
ATOM   1165 O OD1 . ASP B 2 60  ? 19.316  -31.523 42.870 1.00 58.71 ? 212 ASP B OD1 1 
ATOM   1166 O OD2 . ASP B 2 60  ? 18.475  -33.318 43.818 1.00 55.90 ? 212 ASP B OD2 1 
ATOM   1167 N N   . ALA B 2 68  ? 30.168  -23.500 35.797 1.00 46.09 ? 220 ALA B N   1 
ATOM   1168 C CA  . ALA B 2 68  ? 29.788  -22.091 35.818 1.00 47.85 ? 220 ALA B CA  1 
ATOM   1169 C C   . ALA B 2 68  ? 29.252  -21.653 34.449 1.00 49.31 ? 220 ALA B C   1 
ATOM   1170 O O   . ALA B 2 68  ? 28.199  -21.019 34.360 1.00 48.64 ? 220 ALA B O   1 
ATOM   1171 C CB  . ALA B 2 68  ? 30.973  -21.231 36.224 1.00 48.09 ? 220 ALA B CB  1 
ATOM   1172 N N   . SER B 2 69  ? 29.998  -22.016 33.405 1.00 50.74 ? 221 SER B N   1 
ATOM   1173 C CA  . SER B 2 69  ? 29.609  -22.011 31.982 1.00 42.59 ? 221 SER B CA  1 
ATOM   1174 C C   . SER B 2 69  ? 28.275  -22.749 31.780 1.00 41.52 ? 221 SER B C   1 
ATOM   1175 O O   . SER B 2 69  ? 27.367  -22.317 31.050 1.00 40.79 ? 221 SER B O   1 
ATOM   1176 C CB  . SER B 2 69  ? 30.708  -22.670 31.145 1.00 44.91 ? 221 SER B CB  1 
ATOM   1177 O OG  . SER B 2 69  ? 30.245  -22.989 29.845 1.00 48.72 ? 221 SER B OG  1 
ATOM   1178 N N   . LYS B 2 70  ? 28.178  -23.866 32.476 1.00 39.46 ? 222 LYS B N   1 
ATOM   1179 C CA  . LYS B 2 70  ? 27.027  -24.749 32.501 1.00 31.97 ? 222 LYS B CA  1 
ATOM   1180 C C   . LYS B 2 70  ? 25.866  -24.071 33.236 1.00 36.61 ? 222 LYS B C   1 
ATOM   1181 O O   . LYS B 2 70  ? 24.709  -24.213 32.802 1.00 31.72 ? 222 LYS B O   1 
ATOM   1182 C CB  . LYS B 2 70  ? 27.419  -26.070 33.152 1.00 40.41 ? 222 LYS B CB  1 
ATOM   1183 C CG  . LYS B 2 70  ? 26.324  -27.048 33.484 1.00 41.22 ? 222 LYS B CG  1 
ATOM   1184 C CD  . LYS B 2 70  ? 26.818  -27.784 34.717 1.00 42.04 ? 222 LYS B CD  1 
ATOM   1185 C CE  . LYS B 2 70  ? 25.762  -28.031 35.763 1.00 44.15 ? 222 LYS B CE  1 
ATOM   1186 N NZ  . LYS B 2 70  ? 26.445  -28.272 37.080 1.00 47.60 ? 222 LYS B NZ  1 
ATOM   1187 N N   . CYS B 2 71  ? 26.126  -23.387 34.351 1.00 30.88 ? 223 CYS B N   1 
ATOM   1188 C CA  . CYS B 2 71  ? 25.047  -22.709 35.068 1.00 26.53 ? 223 CYS B CA  1 
ATOM   1189 C C   . CYS B 2 71  ? 24.207  -21.770 34.175 1.00 25.77 ? 223 CYS B C   1 
ATOM   1190 O O   . CYS B 2 71  ? 23.002  -21.645 34.405 1.00 27.42 ? 223 CYS B O   1 
ATOM   1191 C CB  . CYS B 2 71  ? 25.582  -21.878 36.248 1.00 30.98 ? 223 CYS B CB  1 
ATOM   1192 S SG  . CYS B 2 71  ? 26.237  -22.836 37.655 1.00 40.65 ? 223 CYS B SG  1 
ATOM   1193 N N   . ASP B 2 72  ? 24.823  -21.017 33.265 1.00 23.18 ? 224 ASP B N   1 
ATOM   1194 C CA  . ASP B 2 72  ? 24.044  -20.050 32.482 1.00 22.21 ? 224 ASP B CA  1 
ATOM   1195 C C   . ASP B 2 72  ? 23.834  -20.344 30.987 1.00 19.57 ? 224 ASP B C   1 
ATOM   1196 O O   . ASP B 2 72  ? 23.395  -19.468 30.231 1.00 18.06 ? 224 ASP B O   1 
ATOM   1197 C CB  . ASP B 2 72  ? 24.578  -18.617 32.646 1.00 23.93 ? 224 ASP B CB  1 
ATOM   1198 C CG  . ASP B 2 72  ? 26.093  -18.542 32.556 1.00 33.86 ? 224 ASP B CG  1 
ATOM   1199 O OD1 . ASP B 2 72  ? 26.680  -19.395 31.850 1.00 32.70 ? 224 ASP B OD1 1 
ATOM   1200 O OD2 . ASP B 2 72  ? 26.683  -17.556 33.072 1.00 31.71 ? 224 ASP B OD2 1 
ATOM   1201 N N   . SER B 2 73  ? 24.066  -21.580 30.582 1.00 16.61 ? 225 SER B N   1 
ATOM   1202 C CA  . SER B 2 73  ? 23.974  -21.976 29.178 1.00 17.54 ? 225 SER B CA  1 
ATOM   1203 C C   . SER B 2 73  ? 22.529  -21.863 28.638 1.00 15.81 ? 225 SER B C   1 
ATOM   1204 O O   . SER B 2 73  ? 22.286  -21.310 27.573 1.00 13.96 ? 225 SER B O   1 
ATOM   1205 C CB  . SER B 2 73  ? 24.495  -23.399 29.043 1.00 19.51 ? 225 SER B CB  1 
ATOM   1206 O OG  . SER B 2 73  ? 24.136  -23.927 27.783 1.00 22.76 ? 225 SER B OG  1 
ATOM   1207 N N   . HIS B 2 74  ? 21.580  -22.448 29.367 1.00 13.70 ? 226 HIS B N   1 
ATOM   1208 C CA  . HIS B 2 74  ? 20.191  -22.545 28.891 1.00 12.91 ? 226 HIS B CA  1 
ATOM   1209 C C   . HIS B 2 74  ? 19.588  -21.155 28.739 1.00 11.80 ? 226 HIS B C   1 
ATOM   1210 O O   . HIS B 2 74  ? 19.109  -20.796 27.668 1.00 12.64 ? 226 HIS B O   1 
ATOM   1211 C CB  . HIS B 2 74  ? 19.387  -23.384 29.889 1.00 10.87 ? 226 HIS B CB  1 
ATOM   1212 C CG  . HIS B 2 74  ? 17.959  -23.627 29.493 1.00 15.29 ? 226 HIS B CG  1 
ATOM   1213 N ND1 . HIS B 2 74  ? 16.909  -22.988 30.115 1.00 13.75 ? 226 HIS B ND1 1 
ATOM   1214 C CD2 . HIS B 2 74  ? 17.401  -24.527 28.646 1.00 14.38 ? 226 HIS B CD2 1 
ATOM   1215 C CE1 . HIS B 2 74  ? 15.763  -23.421 29.606 1.00 14.38 ? 226 HIS B CE1 1 
ATOM   1216 N NE2 . HIS B 2 74  ? 16.035  -24.358 28.716 1.00 17.37 ? 226 HIS B NE2 1 
ATOM   1217 N N   . GLY B 2 75  ? 19.651  -20.358 29.796 1.00 12.16 ? 227 GLY B N   1 
ATOM   1218 C CA  . GLY B 2 75  ? 19.093  -19.008 29.803 1.00 10.88 ? 227 GLY B CA  1 
ATOM   1219 C C   . GLY B 2 75  ? 19.733  -18.089 28.775 1.00 15.57 ? 227 GLY B C   1 
ATOM   1220 O O   . GLY B 2 75  ? 19.057  -17.260 28.143 1.00 11.54 ? 227 GLY B O   1 
ATOM   1221 N N   . THR B 2 76  ? 21.066  -18.150 28.691 1.00 12.97 ? 228 THR B N   1 
ATOM   1222 C CA  . THR B 2 76  ? 21.786  -17.295 27.743 1.00 14.36 ? 228 THR B CA  1 
ATOM   1223 C C   . THR B 2 76  ? 21.372  -17.596 26.305 1.00 12.91 ? 228 THR B C   1 
ATOM   1224 O O   . THR B 2 76  ? 21.136  -16.690 25.508 1.00 12.52 ? 228 THR B O   1 
ATOM   1225 C CB  . THR B 2 76  ? 23.337  -17.441 27.888 1.00 15.52 ? 228 THR B CB  1 
ATOM   1226 O OG1 . THR B 2 76  ? 23.722  -17.185 29.244 1.00 15.59 ? 228 THR B OG1 1 
ATOM   1227 C CG2 . THR B 2 76  ? 24.089  -16.473 26.970 1.00 18.01 ? 228 THR B CG2 1 
ATOM   1228 N N   . HIS B 2 77  ? 21.263  -18.883 25.982 1.00 12.69 ? 229 HIS B N   1 
ATOM   1229 C CA  . HIS B 2 77  ? 20.877  -19.276 24.620 1.00 11.63 ? 229 HIS B CA  1 
ATOM   1230 C C   . HIS B 2 77  ? 19.488  -18.737 24.280 1.00 10.86 ? 229 HIS B C   1 
ATOM   1231 O O   . HIS B 2 77  ? 19.277  -18.146 23.213 1.00 11.27 ? 229 HIS B O   1 
ATOM   1232 C CB  . HIS B 2 77  ? 20.920  -20.800 24.462 1.00 12.49 ? 229 HIS B CB  1 
ATOM   1233 C CG  . HIS B 2 77  ? 20.772  -21.255 23.044 1.00 14.02 ? 229 HIS B CG  1 
ATOM   1234 N ND1 . HIS B 2 77  ? 19.557  -21.573 22.475 1.00 10.75 ? 229 HIS B ND1 1 
ATOM   1235 C CD2 . HIS B 2 77  ? 21.704  -21.471 22.082 1.00 11.41 ? 229 HIS B CD2 1 
ATOM   1236 C CE1 . HIS B 2 77  ? 19.742  -21.950 21.221 1.00 12.85 ? 229 HIS B CE1 1 
ATOM   1237 N NE2 . HIS B 2 77  ? 21.036  -21.887 20.951 1.00 13.20 ? 229 HIS B NE2 1 
ATOM   1238 N N   . LEU B 2 78  ? 18.548  -18.872 25.218 1.00 11.03 ? 230 LEU B N   1 
ATOM   1239 C CA  . LEU B 2 78  ? 17.152  -18.477 24.955 1.00 10.61 ? 230 LEU B CA  1 
ATOM   1240 C C   . LEU B 2 78  ? 17.005  -16.961 24.891 1.00 11.99 ? 230 LEU B C   1 
ATOM   1241 O O   . LEU B 2 78  ? 16.243  -16.468 24.069 1.00 11.75 ? 230 LEU B O   1 
ATOM   1242 C CB  . LEU B 2 78  ? 16.232  -19.041 26.038 1.00 8.25  ? 230 LEU B CB  1 
ATOM   1243 C CG  . LEU B 2 78  ? 16.183  -20.580 26.003 1.00 12.07 ? 230 LEU B CG  1 
ATOM   1244 C CD1 . LEU B 2 78  ? 15.335  -21.088 27.129 1.00 14.55 ? 230 LEU B CD1 1 
ATOM   1245 C CD2 . LEU B 2 78  ? 15.522  -21.013 24.674 1.00 13.15 ? 230 LEU B CD2 1 
ATOM   1246 N N   . ALA B 2 79  ? 17.715  -16.213 25.741 1.00 12.43 ? 231 ALA B N   1 
ATOM   1247 C CA  . ALA B 2 79  ? 17.743  -14.746 25.601 1.00 14.24 ? 231 ALA B CA  1 
ATOM   1248 C C   . ALA B 2 79  ? 18.225  -14.338 24.207 1.00 15.57 ? 231 ALA B C   1 
ATOM   1249 O O   . ALA B 2 79  ? 17.688  -13.415 23.585 1.00 15.67 ? 231 ALA B O   1 
ATOM   1250 C CB  . ALA B 2 79  ? 18.620  -14.131 26.682 1.00 16.72 ? 231 ALA B CB  1 
ATOM   1251 N N   . GLY B 2 80  ? 19.180  -15.094 23.692 1.00 15.11 ? 232 GLY B N   1 
ATOM   1252 C CA  . GLY B 2 80  ? 19.702  -14.884 22.351 1.00 15.66 ? 232 GLY B CA  1 
ATOM   1253 C C   . GLY B 2 80  ? 18.722  -15.260 21.241 1.00 13.62 ? 232 GLY B C   1 
ATOM   1254 O O   . GLY B 2 80  ? 18.567  -14.520 20.270 1.00 15.21 ? 232 GLY B O   1 
ATOM   1255 N N   . VAL B 2 81  ? 17.995  -16.361 21.404 1.00 10.22 ? 233 VAL B N   1 
ATOM   1256 C CA  . VAL B 2 81  ? 16.933  -16.670 20.431 1.00 10.50 ? 233 VAL B CA  1 
ATOM   1257 C C   . VAL B 2 81  ? 15.876  -15.564 20.343 1.00 13.20 ? 233 VAL B C   1 
ATOM   1258 O O   . VAL B 2 81  ? 15.459  -15.159 19.247 1.00 12.13 ? 233 VAL B O   1 
ATOM   1259 C CB  . VAL B 2 81  ? 16.274  -18.035 20.698 1.00 12.06 ? 233 VAL B CB  1 
ATOM   1260 C CG1 . VAL B 2 81  ? 15.181  -18.296 19.637 1.00 11.61 ? 233 VAL B CG1 1 
ATOM   1261 C CG2 . VAL B 2 81  ? 17.332  -19.140 20.674 1.00 10.80 ? 233 VAL B CG2 1 
ATOM   1262 N N   . VAL B 2 82  ? 15.496  -15.017 21.487 1.00 12.68 ? 234 VAL B N   1 
ATOM   1263 C CA  . VAL B 2 82  ? 14.475  -13.986 21.504 1.00 13.36 ? 234 VAL B CA  1 
ATOM   1264 C C   . VAL B 2 82  ? 14.985  -12.671 20.920 1.00 18.07 ? 234 VAL B C   1 
ATOM   1265 O O   . VAL B 2 82  ? 14.320  -12.060 20.076 1.00 20.56 ? 234 VAL B O   1 
ATOM   1266 C CB  . VAL B 2 82  ? 13.892  -13.744 22.919 1.00 15.61 ? 234 VAL B CB  1 
ATOM   1267 C CG1 . VAL B 2 82  ? 12.966  -12.504 22.923 1.00 15.84 ? 234 VAL B CG1 1 
ATOM   1268 C CG2 . VAL B 2 82  ? 13.183  -14.996 23.455 1.00 12.95 ? 234 VAL B CG2 1 
ATOM   1269 N N   . SER B 2 83  ? 16.143  -12.228 21.405 1.00 14.21 ? 235 SER B N   1 
ATOM   1270 C CA  . SER B 2 83  ? 16.570  -10.846 21.178 1.00 20.53 ? 235 SER B CA  1 
ATOM   1271 C C   . SER B 2 83  ? 17.979  -10.613 20.628 1.00 20.08 ? 235 SER B C   1 
ATOM   1272 O O   . SER B 2 83  ? 18.406  -9.459  20.499 1.00 19.79 ? 235 SER B O   1 
ATOM   1273 C CB  . SER B 2 83  ? 16.431  -10.087 22.500 1.00 21.96 ? 235 SER B CB  1 
ATOM   1274 O OG  . SER B 2 83  ? 17.366  -10.631 23.444 1.00 23.76 ? 235 SER B OG  1 
ATOM   1275 N N   . GLY B 2 84  ? 18.694  -11.691 20.315 1.00 21.28 ? 236 GLY B N   1 
ATOM   1276 C CA  . GLY B 2 84  ? 20.111  -11.608 19.943 1.00 18.16 ? 236 GLY B CA  1 
ATOM   1277 C C   . GLY B 2 84  ? 20.371  -10.764 18.702 1.00 22.22 ? 236 GLY B C   1 
ATOM   1278 O O   . GLY B 2 84  ? 19.644  -10.863 17.704 1.00 20.39 ? 236 GLY B O   1 
ATOM   1279 N N   . ARG B 2 85  ? 21.390  -9.917  18.745 1.00 23.45 ? 237 ARG B N   1 
ATOM   1280 C CA  . ARG B 2 85  ? 21.584  -8.985  17.641 1.00 22.13 ? 237 ARG B CA  1 
ATOM   1281 C C   . ARG B 2 85  ? 21.885  -9.670  16.305 1.00 25.54 ? 237 ARG B C   1 
ATOM   1282 O O   . ARG B 2 85  ? 21.409  -9.202  15.271 1.00 27.35 ? 237 ARG B O   1 
ATOM   1283 C CB  . ARG B 2 85  ? 22.594  -7.880  17.993 1.00 28.73 ? 237 ARG B CB  1 
ATOM   1284 C CG  . ARG B 2 85  ? 23.976  -8.296  18.380 1.00 33.40 ? 237 ARG B CG  1 
ATOM   1285 C CD  . ARG B 2 85  ? 24.784  -7.023  18.696 1.00 36.41 ? 237 ARG B CD  1 
ATOM   1286 N NE  . ARG B 2 85  ? 24.033  -6.175  19.630 1.00 40.28 ? 237 ARG B NE  1 
ATOM   1287 C CZ  . ARG B 2 85  ? 24.459  -5.782  20.829 1.00 44.61 ? 237 ARG B CZ  1 
ATOM   1288 N NH1 . ARG B 2 85  ? 25.666  -6.143  21.265 1.00 46.33 ? 237 ARG B NH1 1 
ATOM   1289 N NH2 . ARG B 2 85  ? 23.671  -5.035  21.596 1.00 40.45 ? 237 ARG B NH2 1 
ATOM   1290 N N   . ASP B 2 86  ? 22.571  -10.816 16.307 1.00 23.02 ? 238 ASP B N   1 
ATOM   1291 C CA  . ASP B 2 86  ? 22.832  -11.502 15.038 1.00 25.04 ? 238 ASP B CA  1 
ATOM   1292 C C   . ASP B 2 86  ? 21.822  -12.623 14.724 1.00 26.70 ? 238 ASP B C   1 
ATOM   1293 O O   . ASP B 2 86  ? 21.368  -12.756 13.583 1.00 30.12 ? 238 ASP B O   1 
ATOM   1294 C CB  . ASP B 2 86  ? 24.236  -12.103 15.025 1.00 23.21 ? 238 ASP B CB  1 
ATOM   1295 C CG  . ASP B 2 86  ? 25.325  -11.052 14.873 1.00 30.40 ? 238 ASP B CG  1 
ATOM   1296 O OD1 . ASP B 2 86  ? 25.015  -9.912  14.447 1.00 32.70 ? 238 ASP B OD1 1 
ATOM   1297 O OD2 . ASP B 2 86  ? 26.495  -11.362 15.196 1.00 35.64 ? 238 ASP B OD2 1 
ATOM   1298 N N   . ALA B 2 87  ? 21.456  -13.407 15.738 1.00 20.55 ? 239 ALA B N   1 
ATOM   1299 C CA  . ALA B 2 87  ? 20.664  -14.622 15.524 1.00 20.14 ? 239 ALA B CA  1 
ATOM   1300 C C   . ALA B 2 87  ? 19.311  -14.620 16.236 1.00 22.81 ? 239 ALA B C   1 
ATOM   1301 O O   . ALA B 2 87  ? 18.662  -15.667 16.370 1.00 16.17 ? 239 ALA B O   1 
ATOM   1302 C CB  . ALA B 2 87  ? 21.465  -15.836 15.918 1.00 20.44 ? 239 ALA B CB  1 
ATOM   1303 N N   . GLY B 2 88  ? 18.871  -13.448 16.684 1.00 17.56 ? 240 GLY B N   1 
ATOM   1304 C CA  . GLY B 2 88  ? 17.612  -13.383 17.412 1.00 18.36 ? 240 GLY B CA  1 
ATOM   1305 C C   . GLY B 2 88  ? 16.432  -13.210 16.493 1.00 20.10 ? 240 GLY B C   1 
ATOM   1306 O O   . GLY B 2 88  ? 16.591  -12.838 15.328 1.00 19.54 ? 240 GLY B O   1 
ATOM   1307 N N   . VAL B 2 89  ? 15.238  -13.458 17.035 1.00 18.36 ? 241 VAL B N   1 
ATOM   1308 C CA  . VAL B 2 89  ? 13.989  -13.309 16.306 1.00 15.14 ? 241 VAL B CA  1 
ATOM   1309 C C   . VAL B 2 89  ? 13.520  -11.875 16.324 1.00 18.62 ? 241 VAL B C   1 
ATOM   1310 O O   . VAL B 2 89  ? 13.046  -11.363 15.301 1.00 18.69 ? 241 VAL B O   1 
ATOM   1311 C CB  . VAL B 2 89  ? 12.893  -14.263 16.884 1.00 16.46 ? 241 VAL B CB  1 
ATOM   1312 C CG1 . VAL B 2 89  ? 11.506  -13.924 16.340 1.00 16.85 ? 241 VAL B CG1 1 
ATOM   1313 C CG2 . VAL B 2 89  ? 13.280  -15.730 16.599 1.00 10.86 ? 241 VAL B CG2 1 
ATOM   1314 N N   . ALA B 2 90  ? 13.547  -11.268 17.508 1.00 18.86 ? 242 ALA B N   1 
ATOM   1315 C CA  . ALA B 2 90  ? 13.074  -9.895  17.700 1.00 23.55 ? 242 ALA B CA  1 
ATOM   1316 C C   . ALA B 2 90  ? 14.320  -9.065  18.057 1.00 27.89 ? 242 ALA B C   1 
ATOM   1317 O O   . ALA B 2 90  ? 14.498  -8.681  19.223 1.00 23.92 ? 242 ALA B O   1 
ATOM   1318 C CB  . ALA B 2 90  ? 12.049  -9.848  18.841 1.00 21.82 ? 242 ALA B CB  1 
ATOM   1319 N N   . LYS B 2 91  ? 15.198  -8.830  17.079 1.00 25.28 ? 243 LYS B N   1 
ATOM   1320 C CA  . LYS B 2 91  ? 16.553  -8.309  17.339 1.00 31.81 ? 243 LYS B CA  1 
ATOM   1321 C C   . LYS B 2 91  ? 16.569  -7.079  18.237 1.00 31.30 ? 243 LYS B C   1 
ATOM   1322 O O   . LYS B 2 91  ? 17.446  -6.942  19.096 1.00 40.26 ? 243 LYS B O   1 
ATOM   1323 C CB  . LYS B 2 91  ? 17.312  -8.045  16.031 1.00 27.29 ? 243 LYS B CB  1 
ATOM   1324 C CG  . LYS B 2 91  ? 17.529  -9.298  15.218 1.00 29.80 ? 243 LYS B CG  1 
ATOM   1325 C CD  . LYS B 2 91  ? 18.469  -9.087  14.054 1.00 29.89 ? 243 LYS B CD  1 
ATOM   1326 C CE  . LYS B 2 91  ? 19.018  -10.424 13.566 1.00 30.15 ? 243 LYS B CE  1 
ATOM   1327 N NZ  . LYS B 2 91  ? 17.966  -11.357 13.063 1.00 38.02 ? 243 LYS B NZ  1 
ATOM   1328 N N   . GLY B 2 92  ? 15.613  -6.181  18.047 1.00 37.59 ? 244 GLY B N   1 
ATOM   1329 C CA  . GLY B 2 92  ? 15.443  -5.086  18.987 1.00 43.91 ? 244 GLY B CA  1 
ATOM   1330 C C   . GLY B 2 92  ? 15.322  -5.502  20.457 1.00 48.38 ? 244 GLY B C   1 
ATOM   1331 O O   . GLY B 2 92  ? 16.135  -5.077  21.293 1.00 45.86 ? 244 GLY B O   1 
ATOM   1332 N N   . ALA B 2 93  ? 14.349  -6.373  20.749 1.00 38.93 ? 245 ALA B N   1 
ATOM   1333 C CA  . ALA B 2 93  ? 13.620  -6.420  22.029 1.00 33.13 ? 245 ALA B CA  1 
ATOM   1334 C C   . ALA B 2 93  ? 14.369  -6.241  23.363 1.00 29.17 ? 245 ALA B C   1 
ATOM   1335 O O   . ALA B 2 93  ? 15.454  -6.783  23.560 1.00 28.96 ? 245 ALA B O   1 
ATOM   1336 C CB  . ALA B 2 93  ? 12.834  -7.727  22.088 1.00 32.72 ? 245 ALA B CB  1 
ATOM   1337 N N   . SER B 2 94  ? 13.720  -5.543  24.304 1.00 21.89 ? 246 SER B N   1 
ATOM   1338 C CA  . SER B 2 94  ? 14.206  -5.420  25.680 1.00 22.09 ? 246 SER B CA  1 
ATOM   1339 C C   . SER B 2 94  ? 13.784  -6.667  26.441 1.00 24.33 ? 246 SER B C   1 
ATOM   1340 O O   . SER B 2 94  ? 12.628  -7.083  26.342 1.00 22.99 ? 246 SER B O   1 
ATOM   1341 C CB  . SER B 2 94  ? 13.599  -4.186  26.359 1.00 24.76 ? 246 SER B CB  1 
ATOM   1342 O OG  . SER B 2 94  ? 13.876  -3.007  25.633 1.00 34.27 ? 246 SER B OG  1 
ATOM   1343 N N   . MET B 2 95  ? 14.673  -7.214  27.258 1.00 19.45 ? 247 MET B N   1 
ATOM   1344 C CA  . MET B 2 95  ? 14.316  -8.355  28.081 1.00 18.56 ? 247 MET B CA  1 
ATOM   1345 C C   . MET B 2 95  ? 14.649  -8.091  29.534 1.00 19.63 ? 247 MET B C   1 
ATOM   1346 O O   . MET B 2 95  ? 15.506  -7.251  29.837 1.00 19.08 ? 247 MET B O   1 
ATOM   1347 C CB  . MET B 2 95  ? 15.051  -9.611  27.601 1.00 17.67 ? 247 MET B CB  1 
ATOM   1348 C CG  . MET B 2 95  ? 14.840  -9.938  26.128 1.00 20.24 ? 247 MET B CG  1 
ATOM   1349 S SD  . MET B 2 95  ? 15.515  -11.575 25.755 1.00 22.53 ? 247 MET B SD  1 
ATOM   1350 C CE  . MET B 2 95  ? 14.304  -12.630 26.577 1.00 20.41 ? 247 MET B CE  1 
ATOM   1351 N N   . ARG B 2 96  ? 13.922  -8.752  30.432 1.00 12.03 ? 248 ARG B N   1 
ATOM   1352 C CA  . ARG B 2 96  ? 14.256  -8.773  31.845 1.00 13.84 ? 248 ARG B CA  1 
ATOM   1353 C C   . ARG B 2 96  ? 14.275  -10.229 32.305 1.00 16.96 ? 248 ARG B C   1 
ATOM   1354 O O   . ARG B 2 96  ? 13.336  -10.978 31.992 1.00 14.89 ? 248 ARG B O   1 
ATOM   1355 C CB  . ARG B 2 96  ? 13.229  -7.955  32.641 1.00 15.34 ? 248 ARG B CB  1 
ATOM   1356 C CG  . ARG B 2 96  ? 13.037  -6.516  32.112 1.00 20.02 ? 248 ARG B CG  1 
ATOM   1357 C CD  . ARG B 2 96  ? 12.246  -5.677  33.108 1.00 28.84 ? 248 ARG B CD  1 
ATOM   1358 N NE  . ARG B 2 96  ? 12.034  -4.299  32.661 1.00 33.31 ? 248 ARG B NE  1 
ATOM   1359 C CZ  . ARG B 2 96  ? 12.954  -3.339  32.665 1.00 39.58 ? 248 ARG B CZ  1 
ATOM   1360 N NH1 . ARG B 2 96  ? 12.642  -2.127  32.220 1.00 44.98 ? 248 ARG B NH1 1 
ATOM   1361 N NH2 . ARG B 2 96  ? 14.181  -3.585  33.102 1.00 39.10 ? 248 ARG B NH2 1 
ATOM   1362 N N   . SER B 2 97  ? 15.296  -10.631 33.068 1.00 14.59 ? 249 SER B N   1 
ATOM   1363 C CA  . SER B 2 97  ? 15.447  -12.043 33.426 1.00 13.47 ? 249 SER B CA  1 
ATOM   1364 C C   . SER B 2 97  ? 15.295  -12.239 34.916 1.00 15.90 ? 249 SER B C   1 
ATOM   1365 O O   . SER B 2 97  ? 15.781  -11.429 35.717 1.00 14.89 ? 249 SER B O   1 
ATOM   1366 C CB  . SER B 2 97  ? 16.813  -12.603 33.019 1.00 16.57 ? 249 SER B CB  1 
ATOM   1367 O OG  . SER B 2 97  ? 17.861  -11.710 33.270 1.00 18.03 ? 249 SER B OG  1 
ATOM   1368 N N   . LEU B 2 98  ? 14.610  -13.321 35.271 1.00 13.37 ? 250 LEU B N   1 
ATOM   1369 C CA  . LEU B 2 98  ? 14.442  -13.791 36.645 1.00 13.54 ? 250 LEU B CA  1 
ATOM   1370 C C   . LEU B 2 98  ? 15.068  -15.154 36.729 1.00 14.80 ? 250 LEU B C   1 
ATOM   1371 O O   . LEU B 2 98  ? 14.960  -15.957 35.792 1.00 12.88 ? 250 LEU B O   1 
ATOM   1372 C CB  . LEU B 2 98  ? 12.948  -13.929 37.013 1.00 15.26 ? 250 LEU B CB  1 
ATOM   1373 C CG  . LEU B 2 98  ? 12.160  -12.634 37.239 1.00 17.72 ? 250 LEU B CG  1 
ATOM   1374 C CD1 . LEU B 2 98  ? 11.990  -11.818 35.980 1.00 18.80 ? 250 LEU B CD1 1 
ATOM   1375 C CD2 . LEU B 2 98  ? 10.759  -13.014 37.807 1.00 14.20 ? 250 LEU B CD2 1 
ATOM   1376 N N   . ARG B 2 99  ? 15.729  -15.446 37.845 1.00 11.02 ? 251 ARG B N   1 
ATOM   1377 C CA  . ARG B 2 99  ? 16.375  -16.745 37.955 1.00 14.26 ? 251 ARG B CA  1 
ATOM   1378 C C   . ARG B 2 99  ? 15.490  -17.699 38.759 1.00 15.28 ? 251 ARG B C   1 
ATOM   1379 O O   . ARG B 2 99  ? 15.324  -17.554 39.965 1.00 13.95 ? 251 ARG B O   1 
ATOM   1380 C CB  . ARG B 2 99  ? 17.780  -16.633 38.579 1.00 14.57 ? 251 ARG B CB  1 
ATOM   1381 C CG  . ARG B 2 99  ? 18.523  -17.970 38.578 1.00 13.80 ? 251 ARG B CG  1 
ATOM   1382 C CD  . ARG B 2 99  ? 19.805  -17.950 39.399 1.00 17.31 ? 251 ARG B CD  1 
ATOM   1383 N NE  . ARG B 2 99  ? 20.520  -19.220 39.222 1.00 17.55 ? 251 ARG B NE  1 
ATOM   1384 C CZ  . ARG B 2 99  ? 21.374  -19.725 40.102 1.00 21.93 ? 251 ARG B CZ  1 
ATOM   1385 N NH1 . ARG B 2 99  ? 21.971  -20.888 39.869 1.00 17.08 ? 251 ARG B NH1 1 
ATOM   1386 N NH2 . ARG B 2 99  ? 21.602  -19.069 41.225 1.00 20.93 ? 251 ARG B NH2 1 
ATOM   1387 N N   . VAL B 2 100 ? 14.905  -18.679 38.082 1.00 14.51 ? 252 VAL B N   1 
ATOM   1388 C CA  . VAL B 2 100 ? 14.120  -19.701 38.772 1.00 11.40 ? 252 VAL B CA  1 
ATOM   1389 C C   . VAL B 2 100 ? 14.611  -21.109 38.524 1.00 14.50 ? 252 VAL B C   1 
ATOM   1390 O O   . VAL B 2 100 ? 14.062  -22.058 39.082 1.00 13.48 ? 252 VAL B O   1 
ATOM   1391 C CB  . VAL B 2 100 ? 12.576  -19.577 38.447 1.00 13.72 ? 252 VAL B CB  1 
ATOM   1392 C CG1 . VAL B 2 100 ? 12.044  -18.208 38.748 1.00 13.48 ? 252 VAL B CG1 1 
ATOM   1393 C CG2 . VAL B 2 100 ? 12.282  -19.970 37.007 1.00 12.97 ? 252 VAL B CG2 1 
ATOM   1394 N N   . LEU B 2 101 ? 15.696  -21.237 37.762 1.00 14.07 ? 253 LEU B N   1 
ATOM   1395 C CA  . LEU B 2 101 ? 16.301  -22.542 37.530 1.00 14.76 ? 253 LEU B CA  1 
ATOM   1396 C C   . LEU B 2 101 ? 17.744  -22.476 38.041 1.00 14.08 ? 253 LEU B C   1 
ATOM   1397 O O   . LEU B 2 101 ? 18.494  -21.541 37.720 1.00 16.66 ? 253 LEU B O   1 
ATOM   1398 C CB  . LEU B 2 101 ? 16.260  -22.884 36.036 1.00 10.96 ? 253 LEU B CB  1 
ATOM   1399 C CG  . LEU B 2 101 ? 14.876  -23.030 35.378 1.00 10.49 ? 253 LEU B CG  1 
ATOM   1400 C CD1 . LEU B 2 101 ? 15.020  -23.404 33.934 1.00 12.34 ? 253 LEU B CD1 1 
ATOM   1401 C CD2 . LEU B 2 101 ? 14.045  -24.077 36.079 1.00 12.11 ? 253 LEU B CD2 1 
ATOM   1402 N N   . ASN B 2 102 ? 18.131  -23.478 38.814 1.00 15.21 ? 254 ASN B N   1 
ATOM   1403 C CA  . ASN B 2 102 ? 19.504  -23.619 39.327 1.00 16.63 ? 254 ASN B CA  1 
ATOM   1404 C C   . ASN B 2 102 ? 20.512  -24.110 38.286 1.00 18.38 ? 254 ASN B C   1 
ATOM   1405 O O   . ASN B 2 102 ? 20.196  -24.217 37.099 1.00 14.18 ? 254 ASN B O   1 
ATOM   1406 C CB  . ASN B 2 102 ? 19.525  -24.431 40.637 1.00 17.48 ? 254 ASN B CB  1 
ATOM   1407 C CG  . ASN B 2 102 ? 19.311  -25.924 40.430 1.00 17.85 ? 254 ASN B CG  1 
ATOM   1408 O OD1 . ASN B 2 102 ? 19.401  -26.447 39.314 1.00 16.69 ? 254 ASN B OD1 1 
ATOM   1409 N ND2 . ASN B 2 102 ? 19.104  -26.637 41.535 1.00 17.88 ? 254 ASN B ND2 1 
ATOM   1410 N N   . CYS B 2 103 ? 21.749  -24.333 38.722 1.00 19.17 ? 255 CYS B N   1 
ATOM   1411 C CA  . CYS B 2 103 ? 22.829  -24.708 37.813 1.00 21.67 ? 255 CYS B CA  1 
ATOM   1412 C C   . CYS B 2 103 ? 22.581  -26.045 37.143 1.00 23.42 ? 255 CYS B C   1 
ATOM   1413 O O   . CYS B 2 103 ? 23.209  -26.354 36.133 1.00 24.65 ? 255 CYS B O   1 
ATOM   1414 C CB  . CYS B 2 103 ? 24.165  -24.763 38.562 1.00 27.20 ? 255 CYS B CB  1 
ATOM   1415 S SG  . CYS B 2 103 ? 24.719  -23.115 39.027 1.00 29.72 ? 255 CYS B SG  1 
ATOM   1416 N N   . GLN B 2 104 ? 21.675  -26.836 37.705 1.00 17.28 ? 256 GLN B N   1 
ATOM   1417 C CA  . GLN B 2 104 ? 21.341  -28.104 37.089 1.00 21.87 ? 256 GLN B CA  1 
ATOM   1418 C C   . GLN B 2 104 ? 20.084  -27.960 36.216 1.00 19.80 ? 256 GLN B C   1 
ATOM   1419 O O   . GLN B 2 104 ? 19.536  -28.950 35.738 1.00 20.57 ? 256 GLN B O   1 
ATOM   1420 C CB  . GLN B 2 104 ? 21.141  -29.173 38.163 1.00 22.79 ? 256 GLN B CB  1 
ATOM   1421 C CG  . GLN B 2 104 ? 22.469  -29.552 38.851 1.00 32.08 ? 256 GLN B CG  1 
ATOM   1422 C CD  . GLN B 2 104 ? 22.288  -30.320 40.152 1.00 43.42 ? 256 GLN B CD  1 
ATOM   1423 O OE1 . GLN B 2 104 ? 21.386  -30.030 40.942 1.00 44.87 ? 256 GLN B OE1 1 
ATOM   1424 N NE2 . GLN B 2 104 ? 23.162  -31.298 40.388 1.00 47.16 ? 256 GLN B NE2 1 
ATOM   1425 N N   . GLY B 2 105 ? 19.597  -26.736 36.030 1.00 16.69 ? 257 GLY B N   1 
ATOM   1426 C CA  . GLY B 2 105 ? 18.373  -26.533 35.251 1.00 15.48 ? 257 GLY B CA  1 
ATOM   1427 C C   . GLY B 2 105 ? 17.096  -26.938 35.981 1.00 15.69 ? 257 GLY B C   1 
ATOM   1428 O O   . GLY B 2 105 ? 16.075  -27.228 35.355 1.00 15.35 ? 257 GLY B O   1 
ATOM   1429 N N   . LYS B 2 106 ? 17.162  -26.963 37.307 1.00 13.46 ? 258 LYS B N   1 
ATOM   1430 C CA  . LYS B 2 106 ? 16.030  -27.371 38.140 1.00 15.98 ? 258 LYS B CA  1 
ATOM   1431 C C   . LYS B 2 106 ? 15.437  -26.247 38.966 1.00 12.75 ? 258 LYS B C   1 
ATOM   1432 O O   . LYS B 2 106 ? 16.169  -25.458 39.550 1.00 12.84 ? 258 LYS B O   1 
ATOM   1433 C CB  . LYS B 2 106 ? 16.419  -28.520 39.061 1.00 17.46 ? 258 LYS B CB  1 
ATOM   1434 C CG  . LYS B 2 106 ? 16.532  -29.852 38.392 1.00 21.64 ? 258 LYS B CG  1 
ATOM   1435 C CD  . LYS B 2 106 ? 17.058  -30.857 39.403 1.00 24.59 ? 258 LYS B CD  1 
ATOM   1436 C CE  . LYS B 2 106 ? 15.918  -31.478 40.184 1.00 32.97 ? 258 LYS B CE  1 
ATOM   1437 N NZ  . LYS B 2 106 ? 16.328  -32.778 40.808 1.00 38.23 ? 258 LYS B NZ  1 
ATOM   1438 N N   . GLY B 2 107 ? 14.111  -26.183 38.997 1.00 11.81 ? 259 GLY B N   1 
ATOM   1439 C CA  . GLY B 2 107 ? 13.397  -25.181 39.775 1.00 10.47 ? 259 GLY B CA  1 
ATOM   1440 C C   . GLY B 2 107 ? 12.269  -25.830 40.548 1.00 12.49 ? 259 GLY B C   1 
ATOM   1441 O O   . GLY B 2 107 ? 12.145  -27.056 40.603 1.00 10.97 ? 259 GLY B O   1 
ATOM   1442 N N   . THR B 2 108 ? 11.436  -24.998 41.150 1.00 10.91 ? 260 THR B N   1 
ATOM   1443 C CA  . THR B 2 108 ? 10.265  -25.454 41.870 1.00 11.64 ? 260 THR B CA  1 
ATOM   1444 C C   . THR B 2 108 ? 9.027   -24.745 41.363 1.00 12.69 ? 260 THR B C   1 
ATOM   1445 O O   . THR B 2 108 ? 9.092   -23.647 40.785 1.00 11.48 ? 260 THR B O   1 
ATOM   1446 C CB  . THR B 2 108 ? 10.393  -25.265 43.398 1.00 12.26 ? 260 THR B CB  1 
ATOM   1447 O OG1 . THR B 2 108 ? 10.390  -23.858 43.701 1.00 12.16 ? 260 THR B OG1 1 
ATOM   1448 C CG2 . THR B 2 108 ? 11.681  -25.919 43.945 1.00 13.26 ? 260 THR B CG2 1 
ATOM   1449 N N   . VAL B 2 109 ? 7.882   -25.379 41.578 1.00 10.41 ? 261 VAL B N   1 
ATOM   1450 C CA  . VAL B 2 109 ? 6.615   -24.727 41.292 1.00 10.56 ? 261 VAL B CA  1 
ATOM   1451 C C   . VAL B 2 109 ? 6.487   -23.452 42.140 1.00 12.54 ? 261 VAL B C   1 
ATOM   1452 O O   . VAL B 2 109 ? 6.127   -22.386 41.641 1.00 12.37 ? 261 VAL B O   1 
ATOM   1453 C CB  . VAL B 2 109 ? 5.411   -25.677 41.514 1.00 12.18 ? 261 VAL B CB  1 
ATOM   1454 C CG1 . VAL B 2 109 ? 4.096   -24.881 41.522 1.00 10.12 ? 261 VAL B CG1 1 
ATOM   1455 C CG2 . VAL B 2 109 ? 5.383   -26.748 40.411 1.00 11.87 ? 261 VAL B CG2 1 
ATOM   1456 N N   . SER B 2 110 ? 6.824   -23.554 43.422 1.00 12.37 ? 262 SER B N   1 
ATOM   1457 C CA  . SER B 2 110 ? 6.735   -22.393 44.306 1.00 12.51 ? 262 SER B CA  1 
ATOM   1458 C C   . SER B 2 110 ? 7.628   -21.271 43.819 1.00 11.71 ? 262 SER B C   1 
ATOM   1459 O O   . SER B 2 110 ? 7.221   -20.120 43.854 1.00 13.17 ? 262 SER B O   1 
ATOM   1460 C CB  . SER B 2 110 ? 7.050   -22.761 45.757 1.00 13.15 ? 262 SER B CB  1 
ATOM   1461 O OG  . SER B 2 110 ? 8.400   -23.192 45.912 1.00 13.48 ? 262 SER B OG  1 
ATOM   1462 N N   . GLY B 2 111 ? 8.859   -21.588 43.417 1.00 13.99 ? 263 GLY B N   1 
ATOM   1463 C CA  . GLY B 2 111 ? 9.752   -20.562 42.899 1.00 12.04 ? 263 GLY B CA  1 
ATOM   1464 C C   . GLY B 2 111 ? 9.219   -19.884 41.639 1.00 15.26 ? 263 GLY B C   1 
ATOM   1465 O O   . GLY B 2 111 ? 9.316   -18.674 41.485 1.00 12.54 ? 263 GLY B O   1 
ATOM   1466 N N   . THR B 2 112 ? 8.593   -20.666 40.763 1.00 11.19 ? 264 THR B N   1 
ATOM   1467 C CA  . THR B 2 112 ? 8.041   -20.124 39.523 1.00 10.23 ? 264 THR B CA  1 
ATOM   1468 C C   . THR B 2 112 ? 6.877   -19.193 39.873 1.00 12.18 ? 264 THR B C   1 
ATOM   1469 O O   . THR B 2 112 ? 6.778   -18.103 39.317 1.00 13.21 ? 264 THR B O   1 
ATOM   1470 C CB  . THR B 2 112 ? 7.629   -21.244 38.555 1.00 13.64 ? 264 THR B CB  1 
ATOM   1471 O OG1 . THR B 2 112 ? 8.762   -22.108 38.365 1.00 13.11 ? 264 THR B OG1 1 
ATOM   1472 C CG2 . THR B 2 112 ? 7.230   -20.663 37.177 1.00 13.21 ? 264 THR B CG2 1 
ATOM   1473 N N   . LEU B 2 113 ? 6.022   -19.607 40.808 1.00 11.62 ? 265 LEU B N   1 
ATOM   1474 C CA  . LEU B 2 113 ? 4.921   -18.724 41.296 1.00 12.23 ? 265 LEU B CA  1 
ATOM   1475 C C   . LEU B 2 113 ? 5.410   -17.399 41.845 1.00 11.28 ? 265 LEU B C   1 
ATOM   1476 O O   . LEU B 2 113 ? 4.796   -16.343 41.601 1.00 12.16 ? 265 LEU B O   1 
ATOM   1477 C CB  . LEU B 2 113 ? 4.127   -19.411 42.426 1.00 14.51 ? 265 LEU B CB  1 
ATOM   1478 C CG  . LEU B 2 113 ? 3.395   -20.719 42.134 1.00 12.21 ? 265 LEU B CG  1 
ATOM   1479 C CD1 . LEU B 2 113 ? 2.789   -21.304 43.390 1.00 16.30 ? 265 LEU B CD1 1 
ATOM   1480 C CD2 . LEU B 2 113 ? 2.267   -20.383 41.203 1.00 12.93 ? 265 LEU B CD2 1 
ATOM   1481 N N   . ILE B 2 114 ? 6.453   -17.453 42.675 1.00 11.46 ? 266 ILE B N   1 
ATOM   1482 C CA  . ILE B 2 114 ? 7.017   -16.231 43.251 1.00 13.47 ? 266 ILE B CA  1 
ATOM   1483 C C   . ILE B 2 114 ? 7.573   -15.332 42.137 1.00 13.50 ? 266 ILE B C   1 
ATOM   1484 O O   . ILE B 2 114 ? 7.423   -14.111 42.149 1.00 11.85 ? 266 ILE B O   1 
ATOM   1485 C CB  . ILE B 2 114 ? 8.025   -16.557 44.363 1.00 13.33 ? 266 ILE B CB  1 
ATOM   1486 C CG1 . ILE B 2 114 ? 7.300   -17.297 45.503 1.00 11.97 ? 266 ILE B CG1 1 
ATOM   1487 C CG2 . ILE B 2 114 ? 8.734   -15.275 44.837 1.00 15.97 ? 266 ILE B CG2 1 
ATOM   1488 C CD1 . ILE B 2 114 ? 8.224   -17.933 46.552 1.00 13.47 ? 266 ILE B CD1 1 
ATOM   1489 N N   . GLY B 2 115 ? 8.171   -15.951 41.128 1.00 11.82 ? 267 GLY B N   1 
ATOM   1490 C CA  . GLY B 2 115 ? 8.650   -15.213 39.970 1.00 12.75 ? 267 GLY B CA  1 
ATOM   1491 C C   . GLY B 2 115 ? 7.526   -14.524 39.203 1.00 16.22 ? 267 GLY B C   1 
ATOM   1492 O O   . GLY B 2 115 ? 7.642   -13.349 38.838 1.00 11.86 ? 267 GLY B O   1 
ATOM   1493 N N   . LEU B 2 116 ? 6.465   -15.280 38.899 1.00 11.69 ? 268 LEU B N   1 
ATOM   1494 C CA  . LEU B 2 116 ? 5.327   -14.697 38.214 1.00 13.03 ? 268 LEU B CA  1 
ATOM   1495 C C   . LEU B 2 116 ? 4.727   -13.557 39.004 1.00 13.05 ? 268 LEU B C   1 
ATOM   1496 O O   . LEU B 2 116 ? 4.379   -12.504 38.454 1.00 12.79 ? 268 LEU B O   1 
ATOM   1497 C CB  . LEU B 2 116 ? 4.246   -15.751 37.941 1.00 12.53 ? 268 LEU B CB  1 
ATOM   1498 C CG  . LEU B 2 116 ? 4.718   -16.840 36.983 1.00 13.50 ? 268 LEU B CG  1 
ATOM   1499 C CD1 . LEU B 2 116 ? 3.749   -18.052 37.035 1.00 18.14 ? 268 LEU B CD1 1 
ATOM   1500 C CD2 . LEU B 2 116 ? 4.916   -16.289 35.573 1.00 13.04 ? 268 LEU B CD2 1 
ATOM   1501 N N   . GLU B 2 117 ? 4.643   -13.752 40.312 1.00 13.65 ? 269 GLU B N   1 
ATOM   1502 C CA  . GLU B 2 117 ? 4.122   -12.706 41.188 1.00 16.32 ? 269 GLU B CA  1 
ATOM   1503 C C   . GLU B 2 117 ? 5.018   -11.454 41.156 1.00 14.60 ? 269 GLU B C   1 
ATOM   1504 O O   . GLU B 2 117 ? 4.516   -10.327 41.200 1.00 13.87 ? 269 GLU B O   1 
ATOM   1505 C CB  . GLU B 2 117 ? 4.013   -13.259 42.597 1.00 15.17 ? 269 GLU B CB  1 
ATOM   1506 C CG  . GLU B 2 117 ? 3.418   -12.308 43.593 1.00 21.81 ? 269 GLU B CG  1 
ATOM   1507 C CD  . GLU B 2 117 ? 3.530   -12.852 45.009 1.00 23.58 ? 269 GLU B CD  1 
ATOM   1508 O OE1 . GLU B 2 117 ? 4.620   -12.769 45.621 1.00 22.52 ? 269 GLU B OE1 1 
ATOM   1509 O OE2 . GLU B 2 117 ? 2.503   -13.395 45.489 1.00 20.66 ? 269 GLU B OE2 1 
ATOM   1510 N N   . PHE B 2 118 ? 6.331   -11.659 41.133 1.00 13.08 ? 270 PHE B N   1 
ATOM   1511 C CA  . PHE B 2 118 ? 7.298   -10.556 41.036 1.00 14.62 ? 270 PHE B CA  1 
ATOM   1512 C C   . PHE B 2 118 ? 7.102   -9.730  39.770 1.00 14.02 ? 270 PHE B C   1 
ATOM   1513 O O   . PHE B 2 118 ? 7.234   -8.506  39.786 1.00 13.77 ? 270 PHE B O   1 
ATOM   1514 C CB  . PHE B 2 118 ? 8.733   -11.136 41.058 1.00 14.70 ? 270 PHE B CB  1 
ATOM   1515 C CG  . PHE B 2 118 ? 9.848   -10.082 40.925 1.00 15.03 ? 270 PHE B CG  1 
ATOM   1516 C CD1 . PHE B 2 118 ? 10.403  -9.470  42.038 1.00 18.58 ? 270 PHE B CD1 1 
ATOM   1517 C CD2 . PHE B 2 118 ? 10.348  -9.747  39.683 1.00 15.76 ? 270 PHE B CD2 1 
ATOM   1518 C CE1 . PHE B 2 118 ? 11.435  -8.543  41.905 1.00 18.06 ? 270 PHE B CE1 1 
ATOM   1519 C CE2 . PHE B 2 118 ? 11.364  -8.806  39.543 1.00 19.66 ? 270 PHE B CE2 1 
ATOM   1520 C CZ  . PHE B 2 118 ? 11.905  -8.207  40.654 1.00 16.87 ? 270 PHE B CZ  1 
ATOM   1521 N N   . ILE B 2 119 ? 6.855   -10.400 38.646 1.00 13.67 ? 271 ILE B N   1 
ATOM   1522 C CA  . ILE B 2 119 ? 6.568   -9.692  37.390 1.00 13.77 ? 271 ILE B CA  1 
ATOM   1523 C C   . ILE B 2 119 ? 5.322   -8.807  37.492 1.00 14.09 ? 271 ILE B C   1 
ATOM   1524 O O   . ILE B 2 119 ? 5.316   -7.636  37.071 1.00 10.82 ? 271 ILE B O   1 
ATOM   1525 C CB  . ILE B 2 119 ? 6.381   -10.700 36.253 1.00 16.62 ? 271 ILE B CB  1 
ATOM   1526 C CG1 . ILE B 2 119 ? 7.708   -11.431 36.016 1.00 14.40 ? 271 ILE B CG1 1 
ATOM   1527 C CG2 . ILE B 2 119 ? 5.883   -9.988  34.980 1.00 15.69 ? 271 ILE B CG2 1 
ATOM   1528 C CD1 . ILE B 2 119 ? 7.577   -12.602 35.033 1.00 15.16 ? 271 ILE B CD1 1 
ATOM   1529 N N   . ARG B 2 120 ? 4.264   -9.364  38.074 1.00 12.80 ? 272 ARG B N   1 
ATOM   1530 C CA  . ARG B 2 120 ? 3.016   -8.616  38.214 1.00 13.21 ? 272 ARG B CA  1 
ATOM   1531 C C   . ARG B 2 120 ? 3.200   -7.406  39.129 1.00 13.05 ? 272 ARG B C   1 
ATOM   1532 O O   . ARG B 2 120 ? 2.732   -6.290  38.828 1.00 11.56 ? 272 ARG B O   1 
ATOM   1533 C CB  . ARG B 2 120 ? 1.883   -9.520  38.730 1.00 13.59 ? 272 ARG B CB  1 
ATOM   1534 C CG  . ARG B 2 120 ? 0.567   -8.783  38.977 1.00 14.34 ? 272 ARG B CG  1 
ATOM   1535 C CD  . ARG B 2 120 ? 0.095   -7.998  37.765 1.00 15.39 ? 272 ARG B CD  1 
ATOM   1536 N NE  . ARG B 2 120 ? -1.242  -7.440  38.007 1.00 14.35 ? 272 ARG B NE  1 
ATOM   1537 C CZ  . ARG B 2 120 ? -1.862  -6.570  37.221 1.00 14.35 ? 272 ARG B CZ  1 
ATOM   1538 N NH1 . ARG B 2 120 ? -1.302  -6.178  36.088 1.00 15.30 ? 272 ARG B NH1 1 
ATOM   1539 N NH2 . ARG B 2 120 ? -3.069  -6.149  37.546 1.00 13.74 ? 272 ARG B NH2 1 
ATOM   1540 N N   . LYS B 2 121 ? 3.915   -7.605  40.229 1.00 14.57 ? 273 LYS B N   1 
ATOM   1541 C CA  . LYS B 2 121 ? 4.211   -6.488  41.142 1.00 15.72 ? 273 LYS B CA  1 
ATOM   1542 C C   . LYS B 2 121 ? 5.039   -5.388  40.500 1.00 13.77 ? 273 LYS B C   1 
ATOM   1543 O O   . LYS B 2 121 ? 4.782   -4.202  40.722 1.00 14.45 ? 273 LYS B O   1 
ATOM   1544 C CB  . LYS B 2 121 ? 4.937   -6.998  42.379 1.00 16.03 ? 273 LYS B CB  1 
ATOM   1545 C CG  . LYS B 2 121 ? 4.092   -7.922  43.214 1.00 23.74 ? 273 LYS B CG  1 
ATOM   1546 C CD  . LYS B 2 121 ? 4.852   -8.386  44.445 1.00 29.34 ? 273 LYS B CD  1 
ATOM   1547 C CE  . LYS B 2 121 ? 3.917   -8.647  45.590 1.00 29.99 ? 273 LYS B CE  1 
ATOM   1548 N NZ  . LYS B 2 121 ? 4.507   -9.693  46.448 1.00 32.30 ? 273 LYS B NZ  1 
ATOM   1549 N N   . SER B 2 122 ? 6.041   -5.786  39.729 1.00 12.58 ? 274 SER B N   1 
ATOM   1550 C CA  . SER B 2 122 ? 6.866   -4.847  38.984 1.00 16.50 ? 274 SER B CA  1 
ATOM   1551 C C   . SER B 2 122 ? 6.020   -4.003  38.047 1.00 16.64 ? 274 SER B C   1 
ATOM   1552 O O   . SER B 2 122 ? 6.234   -2.810  37.910 1.00 16.94 ? 274 SER B O   1 
ATOM   1553 C CB  . SER B 2 122 ? 7.937   -5.587  38.179 1.00 15.29 ? 274 SER B CB  1 
ATOM   1554 O OG  . SER B 2 122 ? 8.812   -6.296  39.035 1.00 20.76 ? 274 SER B OG  1 
ATOM   1555 N N   . GLN B 2 123 ? 5.091   -4.654  37.358 1.00 15.40 ? 275 GLN B N   1 
ATOM   1556 C CA  . GLN B 2 123 ? 4.219   -3.961  36.423 1.00 14.14 ? 275 GLN B CA  1 
ATOM   1557 C C   . GLN B 2 123 ? 3.335   -2.913  37.111 1.00 15.62 ? 275 GLN B C   1 
ATOM   1558 O O   . GLN B 2 123 ? 3.152   -1.802  36.614 1.00 15.05 ? 275 GLN B O   1 
ATOM   1559 C CB  . GLN B 2 123 ? 3.339   -4.988  35.713 1.00 17.06 ? 275 GLN B CB  1 
ATOM   1560 C CG  . GLN B 2 123 ? 2.582   -4.468  34.530 1.00 19.34 ? 275 GLN B CG  1 
ATOM   1561 C CD  . GLN B 2 123 ? 1.525   -5.455  34.056 1.00 20.48 ? 275 GLN B CD  1 
ATOM   1562 O OE1 . GLN B 2 123 ? 1.169   -6.398  34.767 1.00 18.26 ? 275 GLN B OE1 1 
ATOM   1563 N NE2 . GLN B 2 123 ? 1.047   -5.266  32.841 1.00 22.02 ? 275 GLN B NE2 1 
ATOM   1564 N N   . LEU B 2 124 ? 2.765   -3.294  38.251 1.00 13.54 ? 276 LEU B N   1 
ATOM   1565 C CA  . LEU B 2 124 ? 1.880   -2.412  39.028 1.00 14.31 ? 276 LEU B CA  1 
ATOM   1566 C C   . LEU B 2 124 ? 2.623   -1.167  39.530 1.00 16.25 ? 276 LEU B C   1 
ATOM   1567 O O   . LEU B 2 124 ? 2.052   -0.068  39.608 1.00 15.99 ? 276 LEU B O   1 
ATOM   1568 C CB  . LEU B 2 124 ? 1.283   -3.174  40.222 1.00 11.49 ? 276 LEU B CB  1 
ATOM   1569 C CG  . LEU B 2 124 ? 0.199   -4.184  39.779 1.00 12.62 ? 276 LEU B CG  1 
ATOM   1570 C CD1 . LEU B 2 124 ? -0.150  -5.143  40.916 1.00 12.50 ? 276 LEU B CD1 1 
ATOM   1571 C CD2 . LEU B 2 124 ? -1.044  -3.449  39.296 1.00 15.86 ? 276 LEU B CD2 1 
ATOM   1572 N N   . VAL B 2 125 ? 3.897   -1.340  39.873 1.00 15.12 ? 277 VAL B N   1 
ATOM   1573 C CA  . VAL B 2 125 ? 4.724   -0.253  40.433 1.00 16.62 ? 277 VAL B CA  1 
ATOM   1574 C C   . VAL B 2 125 ? 5.236   0.665   39.333 1.00 17.65 ? 277 VAL B C   1 
ATOM   1575 O O   . VAL B 2 125 ? 5.374   1.878   39.523 1.00 17.08 ? 277 VAL B O   1 
ATOM   1576 C CB  . VAL B 2 125 ? 5.951   -0.833  41.224 1.00 20.03 ? 277 VAL B CB  1 
ATOM   1577 C CG1 . VAL B 2 125 ? 6.969   0.247   41.606 1.00 20.87 ? 277 VAL B CG1 1 
ATOM   1578 C CG2 . VAL B 2 125 ? 5.499   -1.652  42.442 1.00 18.76 ? 277 VAL B CG2 1 
ATOM   1579 N N   . GLN B 2 126 ? 5.547   0.097   38.176 1.00 15.79 ? 278 GLN B N   1 
ATOM   1580 C CA  . GLN B 2 126 ? 6.055   0.925   37.086 1.00 18.78 ? 278 GLN B CA  1 
ATOM   1581 C C   . GLN B 2 126 ? 5.523   0.443   35.733 1.00 17.95 ? 278 GLN B C   1 
ATOM   1582 O O   . GLN B 2 126 ? 6.213   -0.268  35.007 1.00 19.10 ? 278 GLN B O   1 
ATOM   1583 C CB  . GLN B 2 126 ? 7.610   0.995   37.118 1.00 26.41 ? 278 GLN B CB  1 
ATOM   1584 C CG  . GLN B 2 126 ? 8.335   -0.390  37.160 1.00 33.74 ? 278 GLN B CG  1 
ATOM   1585 C CD  . GLN B 2 126 ? 9.014   -0.790  38.503 1.00 37.82 ? 278 GLN B CD  1 
ATOM   1586 O OE1 . GLN B 2 126 ? 8.827   -1.924  38.983 1.00 23.65 ? 278 GLN B OE1 1 
ATOM   1587 N NE2 . GLN B 2 126 ? 9.838   0.123   39.082 1.00 32.91 ? 278 GLN B NE2 1 
ATOM   1588 N N   . PRO B 2 127 ? 4.280   0.818   35.390 1.00 18.60 ? 279 PRO B N   1 
ATOM   1589 C CA  . PRO B 2 127 ? 3.618   0.322   34.172 1.00 15.64 ? 279 PRO B CA  1 
ATOM   1590 C C   . PRO B 2 127 ? 4.383   0.752   32.907 1.00 18.79 ? 279 PRO B C   1 
ATOM   1591 O O   . PRO B 2 127 ? 4.893   1.873   32.842 1.00 16.50 ? 279 PRO B O   1 
ATOM   1592 C CB  . PRO B 2 127 ? 2.239   0.977   34.220 1.00 15.27 ? 279 PRO B CB  1 
ATOM   1593 C CG  . PRO B 2 127 ? 2.074   1.482   35.604 1.00 19.81 ? 279 PRO B CG  1 
ATOM   1594 C CD  . PRO B 2 127 ? 3.418   1.707   36.178 1.00 15.16 ? 279 PRO B CD  1 
ATOM   1595 N N   . VAL B 2 128 ? 4.512   -0.172  31.956 1.00 16.76 ? 280 VAL B N   1 
ATOM   1596 C CA  . VAL B 2 128 ? 5.145   0.054   30.655 1.00 17.98 ? 280 VAL B CA  1 
ATOM   1597 C C   . VAL B 2 128 ? 4.143   -0.389  29.604 1.00 15.92 ? 280 VAL B C   1 
ATOM   1598 O O   . VAL B 2 128 ? 2.945   -0.183  29.777 1.00 16.23 ? 280 VAL B O   1 
ATOM   1599 C CB  . VAL B 2 128 ? 6.528   -0.626  30.532 1.00 20.62 ? 280 VAL B CB  1 
ATOM   1600 C CG1 . VAL B 2 128 ? 7.554   0.084   31.406 1.00 20.98 ? 280 VAL B CG1 1 
ATOM   1601 C CG2 . VAL B 2 128 ? 6.451   -2.108  30.853 1.00 19.88 ? 280 VAL B CG2 1 
ATOM   1602 N N   . GLY B 2 129 ? 4.594   -0.920  28.474 1.00 17.82 ? 281 GLY B N   1 
ATOM   1603 C CA  . GLY B 2 129 ? 3.624   -1.340  27.476 1.00 17.36 ? 281 GLY B CA  1 
ATOM   1604 C C   . GLY B 2 129 ? 3.274   -2.819  27.640 1.00 21.12 ? 281 GLY B C   1 
ATOM   1605 O O   . GLY B 2 129 ? 3.284   -3.349  28.754 1.00 17.59 ? 281 GLY B O   1 
ATOM   1606 N N   . PRO B 2 130 ? 2.918   -3.473  26.532 1.00 17.94 ? 282 PRO B N   1 
ATOM   1607 C CA  . PRO B 2 130 ? 2.590   -4.906  26.490 1.00 17.40 ? 282 PRO B CA  1 
ATOM   1608 C C   . PRO B 2 130 ? 3.735   -5.717  27.087 1.00 15.63 ? 282 PRO B C   1 
ATOM   1609 O O   . PRO B 2 130 ? 4.894   -5.352  26.875 1.00 12.97 ? 282 PRO B O   1 
ATOM   1610 C CB  . PRO B 2 130 ? 2.490   -5.203  25.000 1.00 16.28 ? 282 PRO B CB  1 
ATOM   1611 C CG  . PRO B 2 130 ? 2.218   -3.881  24.350 1.00 18.79 ? 282 PRO B CG  1 
ATOM   1612 C CD  . PRO B 2 130 ? 2.801   -2.820  25.218 1.00 15.48 ? 282 PRO B CD  1 
ATOM   1613 N N   . LEU B 2 131 ? 3.418   -6.775  27.834 1.00 14.00 ? 283 LEU B N   1 
ATOM   1614 C CA  . LEU B 2 131 ? 4.433   -7.666  28.402 1.00 13.55 ? 283 LEU B CA  1 
ATOM   1615 C C   . LEU B 2 131 ? 4.256   -9.079  27.856 1.00 13.49 ? 283 LEU B C   1 
ATOM   1616 O O   . LEU B 2 131 ? 3.121   -9.586  27.774 1.00 13.18 ? 283 LEU B O   1 
ATOM   1617 C CB  . LEU B 2 131 ? 4.294   -7.710  29.927 1.00 17.14 ? 283 LEU B CB  1 
ATOM   1618 C CG  . LEU B 2 131 ? 5.170   -6.832  30.821 1.00 24.70 ? 283 LEU B CG  1 
ATOM   1619 C CD1 . LEU B 2 131 ? 5.290   -5.458  30.266 1.00 27.60 ? 283 LEU B CD1 1 
ATOM   1620 C CD2 . LEU B 2 131 ? 4.566   -6.763  32.238 1.00 21.08 ? 283 LEU B CD2 1 
ATOM   1621 N N   . VAL B 2 132 ? 5.368   -9.706  27.478 1.00 10.41 ? 284 VAL B N   1 
ATOM   1622 C CA  . VAL B 2 132 ? 5.401   -11.121 27.106 1.00 12.20 ? 284 VAL B CA  1 
ATOM   1623 C C   . VAL B 2 132 ? 6.280   -11.855 28.107 1.00 13.69 ? 284 VAL B C   1 
ATOM   1624 O O   . VAL B 2 132 ? 7.398   -11.419 28.414 1.00 16.69 ? 284 VAL B O   1 
ATOM   1625 C CB  . VAL B 2 132 ? 5.964   -11.362 25.669 1.00 15.20 ? 284 VAL B CB  1 
ATOM   1626 C CG1 . VAL B 2 132 ? 6.012   -12.880 25.357 1.00 13.93 ? 284 VAL B CG1 1 
ATOM   1627 C CG2 . VAL B 2 132 ? 5.129   -10.628 24.610 1.00 13.85 ? 284 VAL B CG2 1 
ATOM   1628 N N   . VAL B 2 133 ? 5.787   -12.967 28.630 1.00 12.34 ? 285 VAL B N   1 
ATOM   1629 C CA  . VAL B 2 133 ? 6.532   -13.746 29.596 1.00 11.03 ? 285 VAL B CA  1 
ATOM   1630 C C   . VAL B 2 133 ? 6.817   -15.102 28.991 1.00 10.97 ? 285 VAL B C   1 
ATOM   1631 O O   . VAL B 2 133 ? 5.897   -15.827 28.643 1.00 10.60 ? 285 VAL B O   1 
ATOM   1632 C CB  . VAL B 2 133 ? 5.738   -13.910 30.927 1.00 15.02 ? 285 VAL B CB  1 
ATOM   1633 C CG1 . VAL B 2 133 ? 6.470   -14.864 31.897 1.00 13.37 ? 285 VAL B CG1 1 
ATOM   1634 C CG2 . VAL B 2 133 ? 5.430   -12.571 31.557 1.00 12.88 ? 285 VAL B CG2 1 
ATOM   1635 N N   . LEU B 2 134 ? 8.092   -15.442 28.894 1.00 11.81 ? 286 LEU B N   1 
ATOM   1636 C CA  . LEU B 2 134 ? 8.539   -16.729 28.361 1.00 10.75 ? 286 LEU B CA  1 
ATOM   1637 C C   . LEU B 2 134 ? 8.846   -17.643 29.518 1.00 11.18 ? 286 LEU B C   1 
ATOM   1638 O O   . LEU B 2 134 ? 9.614   -17.309 30.422 1.00 13.13 ? 286 LEU B O   1 
ATOM   1639 C CB  . LEU B 2 134 ? 9.803   -16.543 27.516 1.00 11.66 ? 286 LEU B CB  1 
ATOM   1640 C CG  . LEU B 2 134 ? 10.443  -17.773 26.847 1.00 13.22 ? 286 LEU B CG  1 
ATOM   1641 C CD1 . LEU B 2 134 ? 9.534   -18.614 25.952 1.00 10.53 ? 286 LEU B CD1 1 
ATOM   1642 C CD2 . LEU B 2 134 ? 11.616  -17.292 26.039 1.00 15.54 ? 286 LEU B CD2 1 
ATOM   1643 N N   . LEU B 2 135 ? 8.211   -18.808 29.496 1.00 12.69 ? 287 LEU B N   1 
ATOM   1644 C CA  . LEU B 2 135 ? 8.380   -19.811 30.524 1.00 10.12 ? 287 LEU B CA  1 
ATOM   1645 C C   . LEU B 2 135 ? 8.969   -21.071 29.860 1.00 13.48 ? 287 LEU B C   1 
ATOM   1646 O O   . LEU B 2 135 ? 8.244   -21.956 29.440 1.00 11.99 ? 287 LEU B O   1 
ATOM   1647 C CB  . LEU B 2 135 ? 7.008   -20.114 31.117 1.00 11.28 ? 287 LEU B CB  1 
ATOM   1648 C CG  . LEU B 2 135 ? 6.488   -19.000 32.021 1.00 14.74 ? 287 LEU B CG  1 
ATOM   1649 C CD1 . LEU B 2 135 ? 4.969   -19.116 32.120 1.00 14.65 ? 287 LEU B CD1 1 
ATOM   1650 C CD2 . LEU B 2 135 ? 7.144   -19.101 33.376 1.00 21.52 ? 287 LEU B CD2 1 
ATOM   1651 N N   . PRO B 2 136 ? 10.298  -21.127 29.731 1.00 13.44 ? 288 PRO B N   1 
ATOM   1652 C CA  . PRO B 2 136 ? 10.998  -22.216 29.044 1.00 10.83 ? 288 PRO B CA  1 
ATOM   1653 C C   . PRO B 2 136 ? 11.248  -23.400 29.942 1.00 12.03 ? 288 PRO B C   1 
ATOM   1654 O O   . PRO B 2 136 ? 12.397  -23.859 30.046 1.00 11.97 ? 288 PRO B O   1 
ATOM   1655 C CB  . PRO B 2 136 ? 12.344  -21.581 28.691 1.00 13.61 ? 288 PRO B CB  1 
ATOM   1656 C CG  . PRO B 2 136 ? 12.582  -20.663 29.841 1.00 11.92 ? 288 PRO B CG  1 
ATOM   1657 C CD  . PRO B 2 136 ? 11.226  -20.120 30.259 1.00 12.08 ? 288 PRO B CD  1 
ATOM   1658 N N   . LEU B 2 137 ? 10.193  -23.885 30.573 1.00 11.58 ? 289 LEU B N   1 
ATOM   1659 C CA  . LEU B 2 137 ? 10.290  -24.856 31.651 1.00 11.67 ? 289 LEU B CA  1 
ATOM   1660 C C   . LEU B 2 137 ? 8.987   -25.666 31.779 1.00 12.97 ? 289 LEU B C   1 
ATOM   1661 O O   . LEU B 2 137 ? 7.936   -25.251 31.280 1.00 10.86 ? 289 LEU B O   1 
ATOM   1662 C CB  . LEU B 2 137 ? 10.620  -24.115 32.965 1.00 10.46 ? 289 LEU B CB  1 
ATOM   1663 C CG  . LEU B 2 137 ? 9.684   -23.010 33.514 1.00 12.77 ? 289 LEU B CG  1 
ATOM   1664 C CD1 . LEU B 2 137 ? 8.400   -23.529 34.161 1.00 12.84 ? 289 LEU B CD1 1 
ATOM   1665 C CD2 . LEU B 2 137 ? 10.441  -22.140 34.505 1.00 13.25 ? 289 LEU B CD2 1 
ATOM   1666 N N   . ALA B 2 138 ? 9.077   -26.825 32.426 1.00 10.84 ? 290 ALA B N   1 
ATOM   1667 C CA  . ALA B 2 138 ? 7.915   -27.675 32.627 1.00 12.96 ? 290 ALA B CA  1 
ATOM   1668 C C   . ALA B 2 138 ? 8.101   -28.578 33.838 1.00 13.09 ? 290 ALA B C   1 
ATOM   1669 O O   . ALA B 2 138 ? 9.217   -29.026 34.131 1.00 13.28 ? 290 ALA B O   1 
ATOM   1670 C CB  . ALA B 2 138 ? 7.609   -28.533 31.374 1.00 9.96  ? 290 ALA B CB  1 
ATOM   1671 N N   . GLY B 2 139 ? 6.989   -28.883 34.503 1.00 12.66 ? 291 GLY B N   1 
ATOM   1672 C CA  . GLY B 2 139 ? 6.924   -29.934 35.498 1.00 13.07 ? 291 GLY B CA  1 
ATOM   1673 C C   . GLY B 2 139 ? 5.642   -30.692 35.179 1.00 12.78 ? 291 GLY B C   1 
ATOM   1674 O O   . GLY B 2 139 ? 5.050   -30.487 34.120 1.00 9.68  ? 291 GLY B O   1 
ATOM   1675 N N   . GLY B 2 140 ? 5.210   -31.582 36.059 1.00 13.96 ? 292 GLY B N   1 
ATOM   1676 C CA  . GLY B 2 140 ? 3.938   -32.229 35.829 1.00 12.33 ? 292 GLY B CA  1 
ATOM   1677 C C   . GLY B 2 140 ? 2.762   -31.277 35.973 1.00 15.31 ? 292 GLY B C   1 
ATOM   1678 O O   . GLY B 2 140 ? 2.913   -30.175 36.486 1.00 13.67 ? 292 GLY B O   1 
ATOM   1679 N N   . TYR B 2 141 ? 1.563   -31.757 35.657 1.00 14.02 ? 293 TYR B N   1 
ATOM   1680 C CA  . TYR B 2 141 ? 0.370   -30.932 35.778 1.00 11.96 ? 293 TYR B CA  1 
ATOM   1681 C C   . TYR B 2 141 ? 0.311   -30.357 37.181 1.00 12.60 ? 293 TYR B C   1 
ATOM   1682 O O   . TYR B 2 141 ? 0.397   -31.080 38.164 1.00 11.66 ? 293 TYR B O   1 
ATOM   1683 C CB  . TYR B 2 141 ? -0.895  -31.774 35.514 1.00 12.57 ? 293 TYR B CB  1 
ATOM   1684 C CG  . TYR B 2 141 ? -2.181  -30.959 35.558 1.00 12.75 ? 293 TYR B CG  1 
ATOM   1685 C CD1 . TYR B 2 141 ? -2.860  -30.771 36.763 1.00 14.02 ? 293 TYR B CD1 1 
ATOM   1686 C CD2 . TYR B 2 141 ? -2.721  -30.383 34.409 1.00 15.83 ? 293 TYR B CD2 1 
ATOM   1687 C CE1 . TYR B 2 141 ? -4.027  -30.008 36.831 1.00 16.43 ? 293 TYR B CE1 1 
ATOM   1688 C CE2 . TYR B 2 141 ? -3.892  -29.627 34.467 1.00 16.43 ? 293 TYR B CE2 1 
ATOM   1689 C CZ  . TYR B 2 141 ? -4.532  -29.448 35.683 1.00 16.31 ? 293 TYR B CZ  1 
ATOM   1690 O OH  . TYR B 2 141 ? -5.691  -28.716 35.742 1.00 20.51 ? 293 TYR B OH  1 
ATOM   1691 N N   . SER B 2 142 ? 0.143   -29.043 37.267 1.00 13.00 ? 294 SER B N   1 
ATOM   1692 C CA  . SER B 2 142 ? 0.028   -28.370 38.554 1.00 13.50 ? 294 SER B CA  1 
ATOM   1693 C C   . SER B 2 142 ? -1.177  -27.456 38.607 1.00 14.70 ? 294 SER B C   1 
ATOM   1694 O O   . SER B 2 142 ? -1.269  -26.504 37.837 1.00 12.61 ? 294 SER B O   1 
ATOM   1695 C CB  . SER B 2 142 ? 1.304   -27.579 38.860 1.00 13.29 ? 294 SER B CB  1 
ATOM   1696 O OG  . SER B 2 142 ? 1.057   -26.623 39.890 1.00 14.02 ? 294 SER B OG  1 
ATOM   1697 N N   . ARG B 2 143 ? -2.102  -27.725 39.528 1.00 12.70 ? 295 ARG B N   1 
ATOM   1698 C CA  . ARG B 2 143 ? -3.287  -26.876 39.642 1.00 14.47 ? 295 ARG B CA  1 
ATOM   1699 C C   . ARG B 2 143 ? -2.840  -25.448 39.967 1.00 13.12 ? 295 ARG B C   1 
ATOM   1700 O O   . ARG B 2 143 ? -3.352  -24.491 39.368 1.00 11.54 ? 295 ARG B O   1 
ATOM   1701 C CB  . ARG B 2 143 ? -4.194  -27.401 40.764 1.00 14.43 ? 295 ARG B CB  1 
ATOM   1702 C CG  . ARG B 2 143 ? -5.475  -26.566 40.883 1.00 16.66 ? 295 ARG B CG  1 
ATOM   1703 C CD  . ARG B 2 143 ? -6.464  -27.106 41.915 1.00 15.51 ? 295 ARG B CD  1 
ATOM   1704 N NE  . ARG B 2 143 ? -7.672  -26.273 41.992 1.00 13.80 ? 295 ARG B NE  1 
ATOM   1705 C CZ  . ARG B 2 143 ? -8.702  -26.541 42.790 1.00 17.81 ? 295 ARG B CZ  1 
ATOM   1706 N NH1 . ARG B 2 143 ? -8.630  -27.580 43.604 1.00 15.97 ? 295 ARG B NH1 1 
ATOM   1707 N NH2 . ARG B 2 143 ? -9.771  -25.755 42.807 1.00 15.14 ? 295 ARG B NH2 1 
ATOM   1708 N N   . VAL B 2 144 ? -1.949  -25.276 40.946 1.00 11.88 ? 296 VAL B N   1 
ATOM   1709 C CA  . VAL B 2 144 ? -1.619  -23.905 41.392 1.00 10.53 ? 296 VAL B CA  1 
ATOM   1710 C C   . VAL B 2 144 ? -0.837  -23.162 40.304 1.00 10.36 ? 296 VAL B C   1 
ATOM   1711 O O   . VAL B 2 144 ? -1.130  -22.005 40.006 1.00 10.71 ? 296 VAL B O   1 
ATOM   1712 C CB  . VAL B 2 144 ? -0.887  -23.857 42.800 1.00 11.24 ? 296 VAL B CB  1 
ATOM   1713 C CG1 . VAL B 2 144 ? 0.500   -24.418 42.720 1.00 10.69 ? 296 VAL B CG1 1 
ATOM   1714 C CG2 . VAL B 2 144 ? -0.792  -22.441 43.330 1.00 12.91 ? 296 VAL B CG2 1 
ATOM   1715 N N   . LEU B 2 145 ? 0.068   -23.844 39.596 1.00 12.33 ? 297 LEU B N   1 
ATOM   1716 C CA  . LEU B 2 145 ? 0.832   -23.134 38.558 1.00 11.37 ? 297 LEU B CA  1 
ATOM   1717 C C   . LEU B 2 145 ? -0.101  -22.717 37.421 1.00 12.58 ? 297 LEU B C   1 
ATOM   1718 O O   . LEU B 2 145 ? -0.003  -21.602 36.914 1.00 11.61 ? 297 LEU B O   1 
ATOM   1719 C CB  . LEU B 2 145 ? 2.014   -23.976 38.044 1.00 11.68 ? 297 LEU B CB  1 
ATOM   1720 C CG  . LEU B 2 145 ? 2.964   -23.304 37.039 1.00 15.04 ? 297 LEU B CG  1 
ATOM   1721 C CD1 . LEU B 2 145 ? 3.502   -21.983 37.624 1.00 16.86 ? 297 LEU B CD1 1 
ATOM   1722 C CD2 . LEU B 2 145 ? 4.156   -24.187 36.696 1.00 13.12 ? 297 LEU B CD2 1 
ATOM   1723 N N   . ASN B 2 146 ? -0.978  -23.611 36.991 1.00 11.30 ? 298 ASN B N   1 
ATOM   1724 C CA  . ASN B 2 146 ? -1.957  -23.251 35.964 1.00 11.16 ? 298 ASN B CA  1 
ATOM   1725 C C   . ASN B 2 146 ? -2.851  -22.081 36.380 1.00 12.66 ? 298 ASN B C   1 
ATOM   1726 O O   . ASN B 2 146 ? -3.126  -21.183 35.578 1.00 12.93 ? 298 ASN B O   1 
ATOM   1727 C CB  . ASN B 2 146 ? -2.832  -24.464 35.619 1.00 10.58 ? 298 ASN B CB  1 
ATOM   1728 C CG  . ASN B 2 146 ? -2.104  -25.480 34.747 1.00 15.50 ? 298 ASN B CG  1 
ATOM   1729 O OD1 . ASN B 2 146 ? -0.900  -25.349 34.491 1.00 12.64 ? 298 ASN B OD1 1 
ATOM   1730 N ND2 . ASN B 2 146 ? -2.832  -26.500 34.278 1.00 12.44 ? 298 ASN B ND2 1 
ATOM   1731 N N   . ALA B 2 147 ? -3.253  -22.049 37.652 1.00 12.57 ? 299 ALA B N   1 
ATOM   1732 C CA  . ALA B 2 147 ? -4.144  -20.973 38.109 1.00 13.42 ? 299 ALA B CA  1 
ATOM   1733 C C   . ALA B 2 147 ? -3.407  -19.648 38.120 1.00 15.21 ? 299 ALA B C   1 
ATOM   1734 O O   . ALA B 2 147 ? -3.986  -18.615 37.788 1.00 15.57 ? 299 ALA B O   1 
ATOM   1735 C CB  . ALA B 2 147 ? -4.751  -21.288 39.500 1.00 13.14 ? 299 ALA B CB  1 
ATOM   1736 N N   . ALA B 2 148 ? -2.127  -19.672 38.499 1.00 12.88 ? 300 ALA B N   1 
ATOM   1737 C CA  . ALA B 2 148 ? -1.357  -18.431 38.563 1.00 15.15 ? 300 ALA B CA  1 
ATOM   1738 C C   . ALA B 2 148 ? -1.137  -17.875 37.162 1.00 14.47 ? 300 ALA B C   1 
ATOM   1739 O O   . ALA B 2 148 ? -1.266  -16.646 36.940 1.00 14.74 ? 300 ALA B O   1 
ATOM   1740 C CB  . ALA B 2 148 ? -0.030  -18.672 39.234 1.00 13.14 ? 300 ALA B CB  1 
ATOM   1741 N N   . CYS B 2 149 ? -0.820  -18.768 36.217 1.00 12.84 ? 301 CYS B N   1 
ATOM   1742 C CA  . CYS B 2 149 ? -0.688  -18.405 34.795 1.00 13.36 ? 301 CYS B CA  1 
ATOM   1743 C C   . CYS B 2 149 ? -1.974  -17.814 34.246 1.00 14.51 ? 301 CYS B C   1 
ATOM   1744 O O   . CYS B 2 149 ? -1.970  -16.768 33.576 1.00 13.49 ? 301 CYS B O   1 
ATOM   1745 C CB  . CYS B 2 149 ? -0.228  -19.630 33.971 1.00 12.30 ? 301 CYS B CB  1 
ATOM   1746 S SG  . CYS B 2 149 ? 1.499   -20.071 34.264 1.00 14.90 ? 301 CYS B SG  1 
ATOM   1747 N N   . GLN B 2 150 ? -3.083  -18.486 34.533 1.00 12.90 ? 302 GLN B N   1 
ATOM   1748 C CA  . GLN B 2 150 ? -4.381  -17.998 34.086 1.00 13.35 ? 302 GLN B CA  1 
ATOM   1749 C C   . GLN B 2 150 ? -4.674  -16.603 34.629 1.00 14.51 ? 302 GLN B C   1 
ATOM   1750 O O   . GLN B 2 150 ? -5.167  -15.723 33.914 1.00 15.89 ? 302 GLN B O   1 
ATOM   1751 C CB  . GLN B 2 150 ? -5.481  -18.947 34.569 1.00 17.64 ? 302 GLN B CB  1 
ATOM   1752 C CG  . GLN B 2 150 ? -6.852  -18.613 33.993 1.00 22.93 ? 302 GLN B CG  1 
ATOM   1753 C CD  . GLN B 2 150 ? -7.915  -19.610 34.457 1.00 33.79 ? 302 GLN B CD  1 
ATOM   1754 O OE1 . GLN B 2 150 ? -7.758  -20.270 35.495 1.00 40.20 ? 302 GLN B OE1 1 
ATOM   1755 N NE2 . GLN B 2 150 ? -8.972  -19.758 33.669 1.00 34.62 ? 302 GLN B NE2 1 
ATOM   1756 N N   . ARG B 2 151 ? -4.393  -16.422 35.914 1.00 12.33 ? 303 ARG B N   1 
ATOM   1757 C CA  . ARG B 2 151 ? -4.649  -15.155 36.575 1.00 16.81 ? 303 ARG B CA  1 
ATOM   1758 C C   . ARG B 2 151 ? -3.778  -14.054 35.948 1.00 16.47 ? 303 ARG B C   1 
ATOM   1759 O O   . ARG B 2 151 ? -4.230  -12.914 35.756 1.00 14.03 ? 303 ARG B O   1 
ATOM   1760 C CB  . ARG B 2 151 ? -4.383  -15.321 38.071 1.00 20.88 ? 303 ARG B CB  1 
ATOM   1761 C CG  . ARG B 2 151 ? -4.646  -14.103 38.877 1.00 29.54 ? 303 ARG B CG  1 
ATOM   1762 C CD  . ARG B 2 151 ? -6.106  -14.270 39.321 1.00 40.41 ? 303 ARG B CD  1 
ATOM   1763 N NE  . ARG B 2 151 ? -6.554  -13.331 40.346 1.00 50.91 ? 303 ARG B NE  1 
ATOM   1764 C CZ  . ARG B 2 151 ? -7.810  -13.275 40.780 1.00 54.33 ? 303 ARG B CZ  1 
ATOM   1765 N NH1 . ARG B 2 151 ? -8.707  -14.123 40.291 1.00 52.85 ? 303 ARG B NH1 1 
ATOM   1766 N NH2 . ARG B 2 151 ? -8.164  -12.399 41.711 1.00 51.34 ? 303 ARG B NH2 1 
ATOM   1767 N N   . LEU B 2 152 ? -2.531  -14.389 35.619 1.00 13.98 ? 304 LEU B N   1 
ATOM   1768 C CA  . LEU B 2 152 ? -1.622  -13.393 35.047 1.00 12.86 ? 304 LEU B CA  1 
ATOM   1769 C C   . LEU B 2 152 ? -2.029  -13.068 33.603 1.00 13.47 ? 304 LEU B C   1 
ATOM   1770 O O   . LEU B 2 152 ? -1.940  -11.929 33.168 1.00 17.78 ? 304 LEU B O   1 
ATOM   1771 C CB  . LEU B 2 152 ? -0.154  -13.845 35.176 1.00 15.08 ? 304 LEU B CB  1 
ATOM   1772 C CG  . LEU B 2 152 ? 0.907   -12.850 34.702 1.00 18.08 ? 304 LEU B CG  1 
ATOM   1773 C CD1 . LEU B 2 152 ? 0.795   -11.513 35.431 1.00 15.71 ? 304 LEU B CD1 1 
ATOM   1774 C CD2 . LEU B 2 152 ? 2.318   -13.414 34.899 1.00 14.90 ? 304 LEU B CD2 1 
ATOM   1775 N N   . ALA B 2 153 ? -2.514  -14.066 32.874 1.00 13.40 ? 305 ALA B N   1 
ATOM   1776 C CA  . ALA B 2 153 ? -3.036  -13.838 31.529 1.00 16.16 ? 305 ALA B CA  1 
ATOM   1777 C C   . ALA B 2 153 ? -4.275  -12.931 31.606 1.00 16.81 ? 305 ALA B C   1 
ATOM   1778 O O   . ALA B 2 153 ? -4.391  -11.982 30.839 1.00 20.67 ? 305 ALA B O   1 
ATOM   1779 C CB  . ALA B 2 153 ? -3.388  -15.165 30.851 1.00 17.35 ? 305 ALA B CB  1 
ATOM   1780 N N   . ARG B 2 154 ? -5.175  -13.191 32.556 1.00 15.68 ? 306 ARG B N   1 
ATOM   1781 C CA  . ARG B 2 154 ? -6.399  -12.380 32.681 1.00 19.33 ? 306 ARG B CA  1 
ATOM   1782 C C   . ARG B 2 154 ? -6.112  -10.950 33.091 1.00 18.35 ? 306 ARG B C   1 
ATOM   1783 O O   . ARG B 2 154 ? -6.922  -10.056 32.857 1.00 17.07 ? 306 ARG B O   1 
ATOM   1784 C CB  . ARG B 2 154 ? -7.403  -13.007 33.648 1.00 20.30 ? 306 ARG B CB  1 
ATOM   1785 C CG  . ARG B 2 154 ? -7.987  -14.307 33.174 1.00 32.13 ? 306 ARG B CG  1 
ATOM   1786 C CD  . ARG B 2 154 ? -9.158  -14.720 34.051 1.00 39.72 ? 306 ARG B CD  1 
ATOM   1787 N NE  . ARG B 2 154 ? -9.612  -16.057 33.698 1.00 45.65 ? 306 ARG B NE  1 
ATOM   1788 C CZ  . ARG B 2 154 ? -10.262 -16.342 32.575 1.00 49.97 ? 306 ARG B CZ  1 
ATOM   1789 N NH1 . ARG B 2 154 ? -10.551 -15.381 31.697 1.00 48.97 ? 306 ARG B NH1 1 
ATOM   1790 N NH2 . ARG B 2 154 ? -10.611 -17.596 32.323 1.00 51.83 ? 306 ARG B NH2 1 
ATOM   1791 N N   . ALA B 2 155 ? -4.978  -10.745 33.743 1.00 15.47 ? 307 ALA B N   1 
ATOM   1792 C CA  . ALA B 2 155 ? -4.522  -9.418  34.132 1.00 20.38 ? 307 ALA B CA  1 
ATOM   1793 C C   . ALA B 2 155 ? -3.945  -8.649  32.939 1.00 18.56 ? 307 ALA B C   1 
ATOM   1794 O O   . ALA B 2 155 ? -3.602  -7.469  33.062 1.00 19.20 ? 307 ALA B O   1 
ATOM   1795 C CB  . ALA B 2 155 ? -3.495  -9.534  35.256 1.00 17.90 ? 307 ALA B CB  1 
ATOM   1796 N N   . GLY B 2 156 ? -3.914  -9.305  31.780 1.00 16.37 ? 308 GLY B N   1 
ATOM   1797 C CA  . GLY B 2 156 ? -3.484  -8.716  30.512 1.00 16.65 ? 308 GLY B CA  1 
ATOM   1798 C C   . GLY B 2 156 ? -2.031  -8.935  30.100 1.00 18.39 ? 308 GLY B C   1 
ATOM   1799 O O   . GLY B 2 156 ? -1.502  -8.225  29.245 1.00 19.88 ? 308 GLY B O   1 
ATOM   1800 N N   . VAL B 2 157 ? -1.394  -9.957  30.663 1.00 16.24 ? 309 VAL B N   1 
ATOM   1801 C CA  . VAL B 2 157 ? -0.012  -10.273 30.297 1.00 15.43 ? 309 VAL B CA  1 
ATOM   1802 C C   . VAL B 2 157 ? 0.001   -11.513 29.370 1.00 16.82 ? 309 VAL B C   1 
ATOM   1803 O O   . VAL B 2 157 ? -0.774  -12.463 29.565 1.00 16.71 ? 309 VAL B O   1 
ATOM   1804 C CB  . VAL B 2 157 ? 0.810   -10.546 31.592 1.00 16.21 ? 309 VAL B CB  1 
ATOM   1805 C CG1 . VAL B 2 157 ? 2.206   -11.070 31.267 1.00 15.74 ? 309 VAL B CG1 1 
ATOM   1806 C CG2 . VAL B 2 157 ? 0.940   -9.249  32.423 1.00 14.60 ? 309 VAL B CG2 1 
ATOM   1807 N N   . VAL B 2 158 ? 0.842   -11.508 28.338 1.00 12.14 ? 310 VAL B N   1 
ATOM   1808 C CA  . VAL B 2 158 ? 0.901   -12.657 27.422 1.00 14.99 ? 310 VAL B CA  1 
ATOM   1809 C C   . VAL B 2 158 ? 1.945   -13.673 27.913 1.00 14.54 ? 310 VAL B C   1 
ATOM   1810 O O   . VAL B 2 158 ? 3.106   -13.339 28.147 1.00 13.04 ? 310 VAL B O   1 
ATOM   1811 C CB  . VAL B 2 158 ? 1.282   -12.204 25.984 1.00 14.77 ? 310 VAL B CB  1 
ATOM   1812 C CG1 . VAL B 2 158 ? 1.569   -13.411 25.093 1.00 12.37 ? 310 VAL B CG1 1 
ATOM   1813 C CG2 . VAL B 2 158 ? 0.163   -11.373 25.362 1.00 11.68 ? 310 VAL B CG2 1 
ATOM   1814 N N   . LEU B 2 159 ? 1.542   -14.935 28.001 1.00 13.65 ? 311 LEU B N   1 
ATOM   1815 C CA  . LEU B 2 159 ? 2.443   -15.993 28.450 1.00 14.46 ? 311 LEU B CA  1 
ATOM   1816 C C   . LEU B 2 159 ? 2.703   -16.991 27.337 1.00 14.71 ? 311 LEU B C   1 
ATOM   1817 O O   . LEU B 2 159 ? 1.778   -17.419 26.657 1.00 9.69  ? 311 LEU B O   1 
ATOM   1818 C CB  . LEU B 2 159 ? 1.868   -16.698 29.696 1.00 12.90 ? 311 LEU B CB  1 
ATOM   1819 C CG  . LEU B 2 159 ? 2.151   -15.988 31.031 1.00 16.82 ? 311 LEU B CG  1 
ATOM   1820 C CD1 . LEU B 2 159 ? 1.339   -14.727 31.203 1.00 17.08 ? 311 LEU B CD1 1 
ATOM   1821 C CD2 . LEU B 2 159 ? 1.781   -16.942 32.164 1.00 17.22 ? 311 LEU B CD2 1 
ATOM   1822 N N   . VAL B 2 160 ? 3.977   -17.342 27.145 1.00 10.86 ? 312 VAL B N   1 
ATOM   1823 C CA  . VAL B 2 160 ? 4.356   -18.305 26.130 1.00 10.39 ? 312 VAL B CA  1 
ATOM   1824 C C   . VAL B 2 160 ? 5.134   -19.387 26.846 1.00 11.34 ? 312 VAL B C   1 
ATOM   1825 O O   . VAL B 2 160 ? 6.091   -19.090 27.551 1.00 11.23 ? 312 VAL B O   1 
ATOM   1826 C CB  . VAL B 2 160 ? 5.220   -17.662 25.023 1.00 12.94 ? 312 VAL B CB  1 
ATOM   1827 C CG1 . VAL B 2 160 ? 5.573   -18.690 23.954 1.00 10.72 ? 312 VAL B CG1 1 
ATOM   1828 C CG2 . VAL B 2 160 ? 4.484   -16.484 24.383 1.00 12.27 ? 312 VAL B CG2 1 
ATOM   1829 N N   . THR B 2 161 ? 4.787   -20.650 26.648 1.00 11.73 ? 313 THR B N   1 
ATOM   1830 C CA  . THR B 2 161 ? 5.513   -21.685 27.364 1.00 9.47  ? 313 THR B CA  1 
ATOM   1831 C C   . THR B 2 161 ? 5.931   -22.826 26.455 1.00 10.04 ? 313 THR B C   1 
ATOM   1832 O O   . THR B 2 161 ? 5.364   -23.048 25.366 1.00 8.61  ? 313 THR B O   1 
ATOM   1833 C CB  . THR B 2 161 ? 4.666   -22.250 28.519 1.00 13.68 ? 313 THR B CB  1 
ATOM   1834 O OG1 . THR B 2 161 ? 5.517   -23.058 29.359 1.00 19.66 ? 313 THR B OG1 1 
ATOM   1835 C CG2 . THR B 2 161 ? 3.544   -23.101 27.988 1.00 9.63  ? 313 THR B CG2 1 
ATOM   1836 N N   . ALA B 2 162 ? 6.892   -23.599 26.940 1.00 9.26  ? 314 ALA B N   1 
ATOM   1837 C CA  . ALA B 2 162 ? 7.331   -24.786 26.238 1.00 7.72  ? 314 ALA B CA  1 
ATOM   1838 C C   . ALA B 2 162 ? 6.279   -25.892 26.342 1.00 8.31  ? 314 ALA B C   1 
ATOM   1839 O O   . ALA B 2 162 ? 5.673   -26.075 27.387 1.00 9.06  ? 314 ALA B O   1 
ATOM   1840 C CB  . ALA B 2 162 ? 8.670   -25.248 26.834 1.00 10.19 ? 314 ALA B CB  1 
ATOM   1841 N N   . ALA B 2 163 ? 6.015   -26.602 25.246 1.00 8.84  ? 315 ALA B N   1 
ATOM   1842 C CA  . ALA B 2 163 ? 5.122   -27.785 25.304 1.00 10.99 ? 315 ALA B CA  1 
ATOM   1843 C C   . ALA B 2 163 ? 5.645   -28.892 26.227 1.00 8.42  ? 315 ALA B C   1 
ATOM   1844 O O   . ALA B 2 163 ? 4.870   -29.677 26.823 1.00 9.60  ? 315 ALA B O   1 
ATOM   1845 C CB  . ALA B 2 163 ? 4.877   -28.347 23.899 1.00 10.05 ? 315 ALA B CB  1 
ATOM   1846 N N   . GLY B 2 164 ? 6.969   -28.977 26.359 1.00 9.08  ? 316 GLY B N   1 
ATOM   1847 C CA  . GLY B 2 164 ? 7.583   -30.098 27.084 1.00 8.44  ? 316 GLY B CA  1 
ATOM   1848 C C   . GLY B 2 164 ? 8.298   -31.033 26.126 1.00 10.87 ? 316 GLY B C   1 
ATOM   1849 O O   . GLY B 2 164 ? 7.902   -31.151 24.960 1.00 9.74  ? 316 GLY B O   1 
ATOM   1850 N N   . ASN B 2 165 ? 9.347   -31.693 26.629 1.00 11.36 ? 317 ASN B N   1 
ATOM   1851 C CA  . ASN B 2 165 ? 10.219  -32.505 25.792 1.00 11.15 ? 317 ASN B CA  1 
ATOM   1852 C C   . ASN B 2 165 ? 10.140  -34.021 25.937 1.00 11.42 ? 317 ASN B C   1 
ATOM   1853 O O   . ASN B 2 165 ? 11.116  -34.726 25.639 1.00 10.62 ? 317 ASN B O   1 
ATOM   1854 C CB  . ASN B 2 165 ? 11.657  -32.120 26.132 1.00 11.57 ? 317 ASN B CB  1 
ATOM   1855 C CG  . ASN B 2 165 ? 11.990  -30.662 25.825 1.00 11.16 ? 317 ASN B CG  1 
ATOM   1856 O OD1 . ASN B 2 165 ? 11.333  -29.993 25.023 1.00 11.79 ? 317 ASN B OD1 1 
ATOM   1857 N ND2 . ASN B 2 165 ? 13.043  -30.169 26.478 1.00 11.56 ? 317 ASN B ND2 1 
ATOM   1858 N N   . PHE B 2 166 ? 8.969   -34.528 26.277 1.00 13.27 ? 318 PHE B N   1 
ATOM   1859 C CA  . PHE B 2 166 ? 8.825   -35.928 26.688 1.00 12.86 ? 318 PHE B CA  1 
ATOM   1860 C C   . PHE B 2 166 ? 8.094   -36.791 25.692 1.00 12.31 ? 318 PHE B C   1 
ATOM   1861 O O   . PHE B 2 166 ? 7.679   -37.904 26.046 1.00 11.58 ? 318 PHE B O   1 
ATOM   1862 C CB  . PHE B 2 166 ? 8.170   -35.969 28.057 1.00 12.49 ? 318 PHE B CB  1 
ATOM   1863 C CG  . PHE B 2 166 ? 8.934   -35.131 29.074 1.00 15.84 ? 318 PHE B CG  1 
ATOM   1864 C CD1 . PHE B 2 166 ? 10.155  -35.555 29.562 1.00 20.96 ? 318 PHE B CD1 1 
ATOM   1865 C CD2 . PHE B 2 166 ? 8.447   -33.918 29.494 1.00 15.10 ? 318 PHE B CD2 1 
ATOM   1866 C CE1 . PHE B 2 166 ? 10.868  -34.776 30.462 1.00 20.29 ? 318 PHE B CE1 1 
ATOM   1867 C CE2 . PHE B 2 166 ? 9.164   -33.138 30.389 1.00 16.32 ? 318 PHE B CE2 1 
ATOM   1868 C CZ  . PHE B 2 166 ? 10.370  -33.584 30.865 1.00 14.97 ? 318 PHE B CZ  1 
ATOM   1869 N N   . ARG B 2 167 ? 7.888   -36.281 24.481 1.00 9.68  ? 319 ARG B N   1 
ATOM   1870 C CA  . ARG B 2 167 ? 7.082   -37.036 23.518 1.00 12.24 ? 319 ARG B CA  1 
ATOM   1871 C C   . ARG B 2 167 ? 5.800   -37.616 24.101 1.00 13.91 ? 319 ARG B C   1 
ATOM   1872 O O   . ARG B 2 167 ? 5.489   -38.816 23.986 1.00 10.46 ? 319 ARG B O   1 
ATOM   1873 C CB  . ARG B 2 167 ? 7.947   -38.146 22.891 1.00 13.89 ? 319 ARG B CB  1 
ATOM   1874 C CG  . ARG B 2 167 ? 7.424   -38.631 21.568 1.00 17.74 ? 319 ARG B CG  1 
ATOM   1875 C CD  . ARG B 2 167 ? 8.245   -39.831 21.049 1.00 20.78 ? 319 ARG B CD  1 
ATOM   1876 N NE  . ARG B 2 167 ? 8.129   -39.899 19.599 1.00 21.37 ? 319 ARG B NE  1 
ATOM   1877 C CZ  . ARG B 2 167 ? 8.490   -40.935 18.859 1.00 24.91 ? 319 ARG B CZ  1 
ATOM   1878 N NH1 . ARG B 2 167 ? 9.178   -41.927 19.405 1.00 32.55 ? 319 ARG B NH1 1 
ATOM   1879 N NH2 . ARG B 2 167 ? 8.344   -40.877 17.547 1.00 29.43 ? 319 ARG B NH2 1 
ATOM   1880 N N   . ASP B 2 168 ? 5.039   -36.709 24.706 1.00 9.13  ? 320 ASP B N   1 
ATOM   1881 C CA  . ASP B 2 168 ? 3.876   -37.046 25.525 1.00 11.39 ? 320 ASP B CA  1 
ATOM   1882 C C   . ASP B 2 168 ? 2.842   -35.968 25.335 1.00 11.55 ? 320 ASP B C   1 
ATOM   1883 O O   . ASP B 2 168 ? 3.074   -34.986 24.620 1.00 9.25  ? 320 ASP B O   1 
ATOM   1884 C CB  . ASP B 2 168 ? 4.324   -37.105 26.988 1.00 12.39 ? 320 ASP B CB  1 
ATOM   1885 C CG  . ASP B 2 168 ? 3.376   -37.892 27.887 1.00 17.31 ? 320 ASP B CG  1 
ATOM   1886 O OD1 . ASP B 2 168 ? 2.376   -38.474 27.393 1.00 14.76 ? 320 ASP B OD1 1 
ATOM   1887 O OD2 . ASP B 2 168 ? 3.657   -37.947 29.118 1.00 17.51 ? 320 ASP B OD2 1 
ATOM   1888 N N   . ASP B 2 169 ? 1.673   -36.179 25.923 1.00 10.64 ? 321 ASP B N   1 
ATOM   1889 C CA  . ASP B 2 169 ? 0.559   -35.264 25.795 1.00 11.63 ? 321 ASP B CA  1 
ATOM   1890 C C   . ASP B 2 169 ? 0.886   -34.028 26.650 1.00 10.62 ? 321 ASP B C   1 
ATOM   1891 O O   . ASP B 2 169 ? 1.027   -34.143 27.860 1.00 10.03 ? 321 ASP B O   1 
ATOM   1892 C CB  . ASP B 2 169 ? -0.686  -35.964 26.343 1.00 11.87 ? 321 ASP B CB  1 
ATOM   1893 C CG  . ASP B 2 169 ? -1.951  -35.186 26.125 1.00 15.80 ? 321 ASP B CG  1 
ATOM   1894 O OD1 . ASP B 2 169 ? -1.911  -33.944 25.953 1.00 14.00 ? 321 ASP B OD1 1 
ATOM   1895 O OD2 . ASP B 2 169 ? -3.020  -35.834 26.126 1.00 21.26 ? 321 ASP B OD2 1 
ATOM   1896 N N   . ALA B 2 170 ? 0.956   -32.851 26.045 1.00 9.45  ? 322 ALA B N   1 
ATOM   1897 C CA  . ALA B 2 170 ? 1.308   -31.652 26.803 1.00 11.84 ? 322 ALA B CA  1 
ATOM   1898 C C   . ALA B 2 170 ? 0.294   -31.328 27.906 1.00 10.77 ? 322 ALA B C   1 
ATOM   1899 O O   . ALA B 2 170 ? 0.611   -30.590 28.825 1.00 10.93 ? 322 ALA B O   1 
ATOM   1900 C CB  . ALA B 2 170 ? 1.490   -30.460 25.865 1.00 10.64 ? 322 ALA B CB  1 
ATOM   1901 N N   . CYS B 2 171 ? -0.937  -31.840 27.812 1.00 11.23 ? 323 CYS B N   1 
ATOM   1902 C CA  . CYS B 2 171 ? -1.920  -31.576 28.875 1.00 9.80  ? 323 CYS B CA  1 
ATOM   1903 C C   . CYS B 2 171 ? -1.568  -32.166 30.229 1.00 11.53 ? 323 CYS B C   1 
ATOM   1904 O O   . CYS B 2 171 ? -2.198  -31.819 31.251 1.00 12.34 ? 323 CYS B O   1 
ATOM   1905 C CB  . CYS B 2 171 ? -3.340  -32.054 28.474 1.00 16.64 ? 323 CYS B CB  1 
ATOM   1906 S SG  . CYS B 2 171 ? -4.006  -31.337 26.920 1.00 20.21 ? 323 CYS B SG  1 
ATOM   1907 N N   . LEU B 2 172 ? -0.574  -33.047 30.246 1.00 10.42 ? 324 LEU B N   1 
ATOM   1908 C CA  . LEU B 2 172 ? -0.109  -33.674 31.485 1.00 10.76 ? 324 LEU B CA  1 
ATOM   1909 C C   . LEU B 2 172 ? 1.010   -32.879 32.162 1.00 11.24 ? 324 LEU B C   1 
ATOM   1910 O O   . LEU B 2 172 ? 1.574   -33.340 33.159 1.00 9.21  ? 324 LEU B O   1 
ATOM   1911 C CB  . LEU B 2 172 ? 0.342   -35.122 31.191 1.00 11.49 ? 324 LEU B CB  1 
ATOM   1912 C CG  . LEU B 2 172 ? -0.704  -36.001 30.476 1.00 13.71 ? 324 LEU B CG  1 
ATOM   1913 C CD1 . LEU B 2 172 ? -0.235  -37.449 30.353 1.00 11.39 ? 324 LEU B CD1 1 
ATOM   1914 C CD2 . LEU B 2 172 ? -2.032  -35.931 31.197 1.00 12.37 ? 324 LEU B CD2 1 
ATOM   1915 N N   . TYR B 2 173 ? 1.300   -31.678 31.644 1.00 10.34 ? 325 TYR B N   1 
ATOM   1916 C CA  . TYR B 2 173 ? 2.449   -30.877 32.099 1.00 9.06  ? 325 TYR B CA  1 
ATOM   1917 C C   . TYR B 2 173 ? 2.001   -29.456 32.352 1.00 9.75  ? 325 TYR B C   1 
ATOM   1918 O O   . TYR B 2 173 ? 1.010   -29.008 31.761 1.00 9.63  ? 325 TYR B O   1 
ATOM   1919 C CB  . TYR B 2 173 ? 3.607   -30.907 31.079 1.00 9.98  ? 325 TYR B CB  1 
ATOM   1920 C CG  . TYR B 2 173 ? 4.099   -32.319 30.870 1.00 9.10  ? 325 TYR B CG  1 
ATOM   1921 C CD1 . TYR B 2 173 ? 3.469   -33.167 29.975 1.00 8.85  ? 325 TYR B CD1 1 
ATOM   1922 C CD2 . TYR B 2 173 ? 5.160   -32.821 31.626 1.00 12.04 ? 325 TYR B CD2 1 
ATOM   1923 C CE1 . TYR B 2 173 ? 3.887   -34.464 29.807 1.00 10.62 ? 325 TYR B CE1 1 
ATOM   1924 C CE2 . TYR B 2 173 ? 5.585   -34.133 31.485 1.00 12.16 ? 325 TYR B CE2 1 
ATOM   1925 C CZ  . TYR B 2 173 ? 4.936   -34.943 30.577 1.00 14.29 ? 325 TYR B CZ  1 
ATOM   1926 O OH  . TYR B 2 173 ? 5.347   -36.248 30.406 1.00 16.27 ? 325 TYR B OH  1 
ATOM   1927 N N   . SER B 2 174 ? 2.714   -28.754 33.227 1.00 10.53 ? 326 SER B N   1 
ATOM   1928 C CA  . SER B 2 174 ? 2.490   -27.326 33.459 1.00 12.48 ? 326 SER B CA  1 
ATOM   1929 C C   . SER B 2 174 ? 3.800   -26.557 33.375 1.00 10.79 ? 326 SER B C   1 
ATOM   1930 O O   . SER B 2 174 ? 4.847   -27.080 33.745 1.00 10.52 ? 326 SER B O   1 
ATOM   1931 C CB  . SER B 2 174 ? 1.875   -27.113 34.862 1.00 10.53 ? 326 SER B CB  1 
ATOM   1932 O OG  . SER B 2 174 ? 0.519   -27.571 34.946 1.00 10.91 ? 326 SER B OG  1 
ATOM   1933 N N   . PRO B 2 175 ? 3.756   -25.284 32.956 1.00 9.90  ? 327 PRO B N   1 
ATOM   1934 C CA  . PRO B 2 175 ? 2.570   -24.522 32.546 1.00 11.78 ? 327 PRO B CA  1 
ATOM   1935 C C   . PRO B 2 175 ? 1.987   -24.880 31.177 1.00 11.89 ? 327 PRO B C   1 
ATOM   1936 O O   . PRO B 2 175 ? 1.024   -24.215 30.802 1.00 12.10 ? 327 PRO B O   1 
ATOM   1937 C CB  . PRO B 2 175 ? 3.054   -23.044 32.544 1.00 10.30 ? 327 PRO B CB  1 
ATOM   1938 C CG  . PRO B 2 175 ? 4.538   -23.077 32.688 1.00 10.68 ? 327 PRO B CG  1 
ATOM   1939 C CD  . PRO B 2 175 ? 4.989   -24.474 33.017 1.00 11.31 ? 327 PRO B CD  1 
ATOM   1940 N N   . ALA B 2 176 ? 2.540   -25.846 30.440 1.00 10.02 ? 328 ALA B N   1 
ATOM   1941 C CA  . ALA B 2 176 ? 2.016   -26.189 29.105 1.00 10.17 ? 328 ALA B CA  1 
ATOM   1942 C C   . ALA B 2 176 ? 0.481   -26.280 29.032 1.00 10.08 ? 328 ALA B C   1 
ATOM   1943 O O   . ALA B 2 176 ? -0.129  -25.833 28.058 1.00 10.63 ? 328 ALA B O   1 
ATOM   1944 C CB  . ALA B 2 176 ? 2.624   -27.525 28.640 1.00 9.48  ? 328 ALA B CB  1 
ATOM   1945 N N   . SER B 2 177 ? -0.099  -26.978 30.006 1.00 11.28 ? 329 SER B N   1 
ATOM   1946 C CA  . SER B 2 177 ? -1.549  -27.291 30.078 1.00 11.26 ? 329 SER B CA  1 
ATOM   1947 C C   . SER B 2 177 ? -2.448  -26.136 30.524 1.00 12.51 ? 329 SER B C   1 
ATOM   1948 O O   . SER B 2 177 ? -3.669  -26.213 30.433 1.00 14.38 ? 329 SER B O   1 
ATOM   1949 C CB  . SER B 2 177 ? -1.828  -28.478 30.974 1.00 9.97  ? 329 SER B CB  1 
ATOM   1950 O OG  . SER B 2 177 ? -1.451  -28.150 32.300 1.00 13.94 ? 329 SER B OG  1 
ATOM   1951 N N   . ALA B 2 178 ? -1.829  -25.052 30.939 1.00 13.82 ? 330 ALA B N   1 
ATOM   1952 C CA  . ALA B 2 178 ? -2.483  -23.853 31.510 1.00 14.94 ? 330 ALA B CA  1 
ATOM   1953 C C   . ALA B 2 178 ? -3.296  -23.003 30.605 1.00 17.90 ? 330 ALA B C   1 
ATOM   1954 O O   . ALA B 2 178 ? -2.937  -22.828 29.442 1.00 17.44 ? 330 ALA B O   1 
ATOM   1955 C CB  . ALA B 2 178 ? -1.395  -22.980 32.096 1.00 15.50 ? 330 ALA B CB  1 
ATOM   1956 N N   . PRO B 2 179 ? -4.557  -22.810 31.001 1.00 23.65 ? 331 PRO B N   1 
ATOM   1957 C CA  . PRO B 2 179 ? -5.510  -22.124 30.138 1.00 26.19 ? 331 PRO B CA  1 
ATOM   1958 C C   . PRO B 2 179 ? -5.051  -20.686 29.872 1.00 22.86 ? 331 PRO B C   1 
ATOM   1959 O O   . PRO B 2 179 ? -4.531  -20.079 30.818 1.00 24.64 ? 331 PRO B O   1 
ATOM   1960 C CB  . PRO B 2 179 ? -6.818  -22.140 30.933 1.00 25.96 ? 331 PRO B CB  1 
ATOM   1961 C CG  . PRO B 2 179 ? -6.364  -22.196 32.368 1.00 29.03 ? 331 PRO B CG  1 
ATOM   1962 C CD  . PRO B 2 179 ? -5.052  -22.961 32.385 1.00 18.77 ? 331 PRO B CD  1 
ATOM   1963 N N   . GLU B 2 180 ? -5.178  -20.202 28.632 1.00 20.55 ? 332 GLU B N   1 
ATOM   1964 C CA  . GLU B 2 180 ? -4.804  -18.835 28.233 1.00 20.73 ? 332 GLU B CA  1 
ATOM   1965 C C   . GLU B 2 180 ? -3.309  -18.595 27.949 1.00 20.86 ? 332 GLU B C   1 
ATOM   1966 O O   . GLU B 2 180 ? -2.916  -17.480 27.634 1.00 31.59 ? 332 GLU B O   1 
ATOM   1967 C CB  . GLU B 2 180 ? -5.306  -17.853 29.286 1.00 24.11 ? 332 GLU B CB  1 
ATOM   1968 C CG  . GLU B 2 180 ? -6.842  -18.023 29.316 1.00 30.24 ? 332 GLU B CG  1 
ATOM   1969 C CD  . GLU B 2 180 ? -7.614  -17.017 30.118 1.00 40.94 ? 332 GLU B CD  1 
ATOM   1970 O OE1 . GLU B 2 180 ? -8.624  -17.448 30.722 1.00 42.62 ? 332 GLU B OE1 1 
ATOM   1971 O OE2 . GLU B 2 180 ? -7.258  -15.817 30.122 1.00 41.61 ? 332 GLU B OE2 1 
ATOM   1972 N N   . VAL B 2 181 ? -2.467  -19.585 28.181 1.00 15.98 ? 333 VAL B N   1 
ATOM   1973 C CA  . VAL B 2 181 ? -1.024  -19.476 27.902 1.00 17.61 ? 333 VAL B CA  1 
ATOM   1974 C C   . VAL B 2 181 ? -0.794  -20.066 26.494 1.00 19.61 ? 333 VAL B C   1 
ATOM   1975 O O   . VAL B 2 181 ? -1.469  -21.029 26.100 1.00 24.40 ? 333 VAL B O   1 
ATOM   1976 C CB  . VAL B 2 181 ? -0.215  -20.247 28.948 1.00 19.92 ? 333 VAL B CB  1 
ATOM   1977 C CG1 . VAL B 2 181 ? 1.280   -20.209 28.623 1.00 25.62 ? 333 VAL B CG1 1 
ATOM   1978 C CG2 . VAL B 2 181 ? -0.468  -19.679 30.311 1.00 16.07 ? 333 VAL B CG2 1 
ATOM   1979 N N   . ILE B 2 182 ? 0.058   -19.434 25.690 1.00 15.42 ? 334 ILE B N   1 
ATOM   1980 C CA  . ILE B 2 182 ? 0.418   -19.953 24.359 1.00 11.82 ? 334 ILE B CA  1 
ATOM   1981 C C   . ILE B 2 182 ? 1.473   -21.066 24.471 1.00 13.25 ? 334 ILE B C   1 
ATOM   1982 O O   . ILE B 2 182 ? 2.611   -20.829 24.856 1.00 11.78 ? 334 ILE B O   1 
ATOM   1983 C CB  . ILE B 2 182 ? 0.930   -18.820 23.446 1.00 14.12 ? 334 ILE B CB  1 
ATOM   1984 C CG1 . ILE B 2 182 ? -0.181  -17.770 23.284 1.00 14.02 ? 334 ILE B CG1 1 
ATOM   1985 C CG2 . ILE B 2 182 ? 1.323   -19.356 22.065 1.00 11.66 ? 334 ILE B CG2 1 
ATOM   1986 C CD1 . ILE B 2 182 ? 0.330   -16.371 23.034 1.00 17.66 ? 334 ILE B CD1 1 
ATOM   1987 N N   . THR B 2 183 ? 1.077   -22.288 24.145 1.00 9.12  ? 335 THR B N   1 
ATOM   1988 C CA  . THR B 2 183 ? 1.969   -23.444 24.328 1.00 11.73 ? 335 THR B CA  1 
ATOM   1989 C C   . THR B 2 183 ? 2.603   -23.924 23.019 1.00 9.80  ? 335 THR B C   1 
ATOM   1990 O O   . THR B 2 183 ? 1.898   -24.201 22.050 1.00 7.37  ? 335 THR B O   1 
ATOM   1991 C CB  . THR B 2 183 ? 1.163   -24.573 24.928 1.00 9.10  ? 335 THR B CB  1 
ATOM   1992 O OG1 . THR B 2 183 ? 0.587   -24.113 26.154 1.00 9.12  ? 335 THR B OG1 1 
ATOM   1993 C CG2 . THR B 2 183 ? 2.071   -25.802 25.206 1.00 8.48  ? 335 THR B CG2 1 
ATOM   1994 N N   . VAL B 2 184 ? 3.927   -24.076 23.008 1.00 10.69 ? 336 VAL B N   1 
ATOM   1995 C CA  . VAL B 2 184 ? 4.657   -24.213 21.752 1.00 9.22  ? 336 VAL B CA  1 
ATOM   1996 C C   . VAL B 2 184 ? 5.458   -25.512 21.647 1.00 9.00  ? 336 VAL B C   1 
ATOM   1997 O O   . VAL B 2 184 ? 6.304   -25.781 22.506 1.00 7.33  ? 336 VAL B O   1 
ATOM   1998 C CB  . VAL B 2 184 ? 5.622   -23.018 21.525 1.00 8.64  ? 336 VAL B CB  1 
ATOM   1999 C CG1 . VAL B 2 184 ? 6.148   -23.076 20.108 1.00 7.25  ? 336 VAL B CG1 1 
ATOM   2000 C CG2 . VAL B 2 184 ? 4.914   -21.641 21.784 1.00 9.71  ? 336 VAL B CG2 1 
ATOM   2001 N N   . GLY B 2 185 ? 5.180   -26.322 20.619 1.00 9.71  ? 337 GLY B N   1 
ATOM   2002 C CA  . GLY B 2 185 ? 5.936   -27.541 20.367 1.00 7.56  ? 337 GLY B CA  1 
ATOM   2003 C C   . GLY B 2 185 ? 7.096   -27.260 19.425 1.00 11.07 ? 337 GLY B C   1 
ATOM   2004 O O   . GLY B 2 185 ? 7.191   -26.170 18.858 1.00 9.12  ? 337 GLY B O   1 
ATOM   2005 N N   . ALA B 2 186 ? 7.952   -28.249 19.198 1.00 10.08 ? 338 ALA B N   1 
ATOM   2006 C CA  . ALA B 2 186 ? 9.199   -28.010 18.442 1.00 9.79  ? 338 ALA B CA  1 
ATOM   2007 C C   . ALA B 2 186 ? 9.197   -28.827 17.160 1.00 10.07 ? 338 ALA B C   1 
ATOM   2008 O O   . ALA B 2 186 ? 8.911   -30.028 17.190 1.00 10.32 ? 338 ALA B O   1 
ATOM   2009 C CB  . ALA B 2 186 ? 10.402  -28.394 19.285 1.00 9.97  ? 338 ALA B CB  1 
ATOM   2010 N N   . THR B 2 187 ? 9.532   -28.195 16.034 1.00 10.77 ? 339 THR B N   1 
ATOM   2011 C CA  . THR B 2 187 ? 9.742   -28.899 14.764 1.00 11.53 ? 339 THR B CA  1 
ATOM   2012 C C   . THR B 2 187 ? 11.165  -28.678 14.278 1.00 15.07 ? 339 THR B C   1 
ATOM   2013 O O   . THR B 2 187 ? 11.873  -27.781 14.754 1.00 11.69 ? 339 THR B O   1 
ATOM   2014 C CB  . THR B 2 187 ? 8.746   -28.450 13.671 1.00 15.43 ? 339 THR B CB  1 
ATOM   2015 O OG1 . THR B 2 187 ? 8.684   -27.017 13.686 1.00 12.12 ? 339 THR B OG1 1 
ATOM   2016 C CG2 . THR B 2 187 ? 7.339   -28.967 13.968 1.00 13.13 ? 339 THR B CG2 1 
ATOM   2017 N N   . ASN B 2 188 ? 11.625  -29.563 13.399 1.00 12.03 ? 340 ASN B N   1 
ATOM   2018 C CA  . ASN B 2 188 ? 12.990  -29.494 12.885 1.00 16.14 ? 340 ASN B CA  1 
ATOM   2019 C C   . ASN B 2 188 ? 13.040  -28.856 11.493 1.00 15.63 ? 340 ASN B C   1 
ATOM   2020 O O   . ASN B 2 188 ? 12.017  -28.390 10.978 1.00 15.30 ? 340 ASN B O   1 
ATOM   2021 C CB  . ASN B 2 188 ? 13.608  -30.904 12.912 1.00 13.90 ? 340 ASN B CB  1 
ATOM   2022 C CG  . ASN B 2 188 ? 12.937  -31.863 11.957 1.00 18.57 ? 340 ASN B CG  1 
ATOM   2023 O OD1 . ASN B 2 188 ? 12.224  -31.461 11.047 1.00 19.05 ? 340 ASN B OD1 1 
ATOM   2024 N ND2 . ASN B 2 188 ? 13.091  -33.152 12.217 1.00 20.95 ? 340 ASN B ND2 1 
ATOM   2025 N N   . ALA B 2 189 ? 14.222  -28.839 10.882 1.00 15.97 ? 341 ALA B N   1 
ATOM   2026 C CA  . ALA B 2 189 ? 14.409  -28.231 9.558  1.00 16.66 ? 341 ALA B CA  1 
ATOM   2027 C C   . ALA B 2 189 ? 13.555  -28.861 8.457  1.00 20.12 ? 341 ALA B C   1 
ATOM   2028 O O   . ALA B 2 189 ? 13.306  -28.233 7.435  1.00 22.17 ? 341 ALA B O   1 
ATOM   2029 C CB  . ALA B 2 189 ? 15.895  -28.290 9.163  1.00 18.99 ? 341 ALA B CB  1 
ATOM   2030 N N   . GLN B 2 190 ? 13.103  -30.095 8.666  1.00 17.64 ? 342 GLN B N   1 
ATOM   2031 C CA  . GLN B 2 190 ? 12.187  -30.744 7.714  1.00 24.70 ? 342 GLN B CA  1 
ATOM   2032 C C   . GLN B 2 190 ? 10.719  -30.552 8.120  1.00 23.62 ? 342 GLN B C   1 
ATOM   2033 O O   . GLN B 2 190 ? 9.826   -31.249 7.642  1.00 24.95 ? 342 GLN B O   1 
ATOM   2034 C CB  . GLN B 2 190 ? 12.561  -32.224 7.523  1.00 25.40 ? 342 GLN B CB  1 
ATOM   2035 C CG  . GLN B 2 190 ? 13.894  -32.470 6.790  1.00 27.14 ? 342 GLN B CG  1 
ATOM   2036 C CD  . GLN B 2 190 ? 15.089  -32.233 7.681  1.00 34.34 ? 342 GLN B CD  1 
ATOM   2037 O OE1 . GLN B 2 190 ? 15.133  -32.700 8.826  1.00 39.70 ? 342 GLN B OE1 1 
ATOM   2038 N NE2 . GLN B 2 190 ? 16.078  -31.498 7.163  1.00 38.73 ? 342 GLN B NE2 1 
ATOM   2039 N N   . ASP B 2 191 ? 10.496  -29.600 9.020  1.00 19.95 ? 343 ASP B N   1 
ATOM   2040 C CA  . ASP B 2 191 ? 9.171   -29.319 9.571  1.00 21.14 ? 343 ASP B CA  1 
ATOM   2041 C C   . ASP B 2 191 ? 8.554   -30.542 10.239 1.00 22.47 ? 343 ASP B C   1 
ATOM   2042 O O   . ASP B 2 191 ? 7.335   -30.655 10.322 1.00 22.37 ? 343 ASP B O   1 
ATOM   2043 C CB  . ASP B 2 191 ? 8.205   -28.763 8.507  1.00 21.61 ? 343 ASP B CB  1 
ATOM   2044 C CG  . ASP B 2 191 ? 8.501   -27.325 8.093  1.00 25.37 ? 343 ASP B CG  1 
ATOM   2045 O OD1 . ASP B 2 191 ? 8.902   -26.467 8.925  1.00 25.11 ? 343 ASP B OD1 1 
ATOM   2046 O OD2 . ASP B 2 191 ? 8.355   -27.052 6.882  1.00 31.87 ? 343 ASP B OD2 1 
ATOM   2047 N N   . GLN B 2 192 ? 9.377   -31.469 10.718 1.00 19.28 ? 344 GLN B N   1 
ATOM   2048 C CA  . GLN B 2 192 ? 8.802   -32.602 11.418 1.00 19.22 ? 344 GLN B CA  1 
ATOM   2049 C C   . GLN B 2 192 ? 8.974   -32.426 12.919 1.00 14.95 ? 344 GLN B C   1 
ATOM   2050 O O   . GLN B 2 192 ? 9.872   -31.702 13.363 1.00 14.63 ? 344 GLN B O   1 
ATOM   2051 C CB  . GLN B 2 192 ? 9.434   -33.904 10.899 1.00 24.07 ? 344 GLN B CB  1 
ATOM   2052 C CG  . GLN B 2 192 ? 9.182   -34.089 9.380  1.00 25.02 ? 344 GLN B CG  1 
ATOM   2053 C CD  . GLN B 2 192 ? 7.707   -33.793 8.988  1.00 27.25 ? 344 GLN B CD  1 
ATOM   2054 O OE1 . GLN B 2 192 ? 6.782   -34.429 9.498  1.00 26.56 ? 344 GLN B OE1 1 
ATOM   2055 N NE2 . GLN B 2 192 ? 7.498   -32.819 8.093  1.00 25.99 ? 344 GLN B NE2 1 
ATOM   2056 N N   . PRO B 2 193 ? 8.082   -33.039 13.702 1.00 14.97 ? 345 PRO B N   1 
ATOM   2057 C CA  . PRO B 2 193 ? 8.162   -32.932 15.158 1.00 14.47 ? 345 PRO B CA  1 
ATOM   2058 C C   . PRO B 2 193 ? 9.475   -33.489 15.662 1.00 17.07 ? 345 PRO B C   1 
ATOM   2059 O O   . PRO B 2 193 ? 9.853   -34.559 15.165 1.00 16.04 ? 345 PRO B O   1 
ATOM   2060 C CB  . PRO B 2 193 ? 6.934   -33.679 15.686 1.00 14.74 ? 345 PRO B CB  1 
ATOM   2061 C CG  . PRO B 2 193 ? 6.086   -33.968 14.481 1.00 21.47 ? 345 PRO B CG  1 
ATOM   2062 C CD  . PRO B 2 193 ? 6.945   -33.863 13.256 1.00 18.14 ? 345 PRO B CD  1 
ATOM   2063 N N   . VAL B 2 194 ? 10.111  -32.865 16.650 1.00 13.85 ? 346 VAL B N   1 
ATOM   2064 C CA  . VAL B 2 194 ? 11.442  -33.295 17.054 1.00 17.13 ? 346 VAL B CA  1 
ATOM   2065 C C   . VAL B 2 194 ? 11.223  -34.580 17.818 1.00 20.47 ? 346 VAL B C   1 
ATOM   2066 O O   . VAL B 2 194 ? 10.324  -34.665 18.653 1.00 16.15 ? 346 VAL B O   1 
ATOM   2067 C CB  . VAL B 2 194 ? 12.187  -32.259 17.933 1.00 14.04 ? 346 VAL B CB  1 
ATOM   2068 C CG1 . VAL B 2 194 ? 13.506  -32.841 18.441 1.00 18.11 ? 346 VAL B CG1 1 
ATOM   2069 C CG2 . VAL B 2 194 ? 12.425  -30.947 17.191 1.00 12.63 ? 346 VAL B CG2 1 
ATOM   2070 N N   . THR B 2 195 ? 11.964  -35.619 17.432 1.00 20.29 ? 347 THR B N   1 
ATOM   2071 C CA  . THR B 2 195 ? 12.035  -36.846 18.211 1.00 25.82 ? 347 THR B CA  1 
ATOM   2072 C C   . THR B 2 195 ? 13.483  -37.286 18.465 1.00 30.69 ? 347 THR B C   1 
ATOM   2073 O O   . THR B 2 195 ? 14.381  -37.020 17.671 1.00 28.63 ? 347 THR B O   1 
ATOM   2074 C CB  . THR B 2 195 ? 11.353  -37.992 17.441 1.00 31.32 ? 347 THR B CB  1 
ATOM   2075 O OG1 . THR B 2 195 ? 12.107  -38.298 16.261 1.00 33.95 ? 347 THR B OG1 1 
ATOM   2076 C CG2 . THR B 2 195 ? 9.941   -37.598 17.017 1.00 27.92 ? 347 THR B CG2 1 
ATOM   2077 N N   . LEU B 2 196 ? 13.696  -37.934 19.607 1.00 27.71 ? 348 LEU B N   1 
ATOM   2078 C CA  . LEU B 2 196 ? 14.994  -38.453 20.016 1.00 25.44 ? 348 LEU B CA  1 
ATOM   2079 C C   . LEU B 2 196 ? 14.670  -39.620 20.939 1.00 28.11 ? 348 LEU B C   1 
ATOM   2080 O O   . LEU B 2 196 ? 14.676  -39.479 22.161 1.00 24.89 ? 348 LEU B O   1 
ATOM   2081 C CB  . LEU B 2 196 ? 15.809  -37.386 20.753 1.00 26.60 ? 348 LEU B CB  1 
ATOM   2082 C CG  . LEU B 2 196 ? 17.287  -37.741 21.017 1.00 31.75 ? 348 LEU B CG  1 
ATOM   2083 C CD1 . LEU B 2 196 ? 18.091  -37.804 19.709 1.00 29.46 ? 348 LEU B CD1 1 
ATOM   2084 C CD2 . LEU B 2 196 ? 17.958  -36.804 22.025 1.00 25.47 ? 348 LEU B CD2 1 
ATOM   2085 N N   . GLY B 2 197 ? 14.312  -40.754 20.337 1.00 34.93 ? 349 GLY B N   1 
ATOM   2086 C CA  . GLY B 2 197 ? 13.999  -41.967 21.078 1.00 27.07 ? 349 GLY B CA  1 
ATOM   2087 C C   . GLY B 2 197 ? 12.657  -41.879 21.760 1.00 26.53 ? 349 GLY B C   1 
ATOM   2088 O O   . GLY B 2 197 ? 11.630  -41.591 21.132 1.00 33.59 ? 349 GLY B O   1 
ATOM   2089 N N   . THR B 2 198 ? 12.655  -42.125 23.064 1.00 22.33 ? 350 THR B N   1 
ATOM   2090 C CA  . THR B 2 198 ? 11.454  -41.959 23.864 1.00 21.42 ? 350 THR B CA  1 
ATOM   2091 C C   . THR B 2 198 ? 11.218  -40.474 24.169 1.00 21.39 ? 350 THR B C   1 
ATOM   2092 O O   . THR B 2 198 ? 10.247  -40.113 24.805 1.00 23.37 ? 350 THR B O   1 
ATOM   2093 C CB  . THR B 2 198 ? 11.593  -42.722 25.182 1.00 29.06 ? 350 THR B CB  1 
ATOM   2094 O OG1 . THR B 2 198 ? 12.545  -42.058 26.018 1.00 28.24 ? 350 THR B OG1 1 
ATOM   2095 C CG2 . THR B 2 198 ? 12.092  -44.140 24.920 1.00 31.13 ? 350 THR B CG2 1 
ATOM   2096 N N   . LEU B 2 199 ? 12.142  -39.629 23.720 1.00 19.25 ? 351 LEU B N   1 
ATOM   2097 C CA  . LEU B 2 199 ? 12.078  -38.191 23.956 1.00 16.11 ? 351 LEU B CA  1 
ATOM   2098 C C   . LEU B 2 199 ? 11.774  -37.421 22.681 1.00 15.58 ? 351 LEU B C   1 
ATOM   2099 O O   . LEU B 2 199 ? 11.813  -37.999 21.605 1.00 17.67 ? 351 LEU B O   1 
ATOM   2100 C CB  . LEU B 2 199 ? 13.372  -37.703 24.634 1.00 19.94 ? 351 LEU B CB  1 
ATOM   2101 C CG  . LEU B 2 199 ? 13.811  -38.250 26.000 1.00 19.52 ? 351 LEU B CG  1 
ATOM   2102 C CD1 . LEU B 2 199 ? 15.138  -37.609 26.380 1.00 21.89 ? 351 LEU B CD1 1 
ATOM   2103 C CD2 . LEU B 2 199 ? 12.751  -37.974 27.064 1.00 15.91 ? 351 LEU B CD2 1 
ATOM   2104 N N   . GLY B 2 200 ? 11.312  -36.179 22.807 1.00 14.28 ? 352 GLY B N   1 
ATOM   2105 C CA  . GLY B 2 200 ? 10.860  -35.383 21.670 1.00 10.04 ? 352 GLY B CA  1 
ATOM   2106 C C   . GLY B 2 200 ? 9.814   -34.355 22.024 1.00 10.48 ? 352 GLY B C   1 
ATOM   2107 O O   . GLY B 2 200 ? 9.385   -34.318 23.164 1.00 10.81 ? 352 GLY B O   1 
ATOM   2108 N N   . THR B 2 201 ? 9.342   -33.582 21.049 1.00 11.20 ? 353 THR B N   1 
ATOM   2109 C CA  . THR B 2 201 ? 8.308   -32.578 21.340 1.00 10.56 ? 353 THR B CA  1 
ATOM   2110 C C   . THR B 2 201 ? 7.045   -33.218 21.921 1.00 10.08 ? 353 THR B C   1 
ATOM   2111 O O   . THR B 2 201 ? 6.615   -34.282 21.433 1.00 11.93 ? 353 THR B O   1 
ATOM   2112 C CB  . THR B 2 201 ? 7.932   -31.711 20.120 1.00 9.96  ? 353 THR B CB  1 
ATOM   2113 O OG1 . THR B 2 201 ? 7.067   -30.649 20.569 1.00 9.80  ? 353 THR B OG1 1 
ATOM   2114 C CG2 . THR B 2 201 ? 7.266   -32.522 19.016 1.00 9.54  ? 353 THR B CG2 1 
ATOM   2115 N N   . ASN B 2 202 ? 6.445   -32.605 22.947 1.00 10.23 ? 354 ASN B N   1 
ATOM   2116 C CA  . ASN B 2 202 ? 5.091   -32.990 23.341 1.00 8.72  ? 354 ASN B CA  1 
ATOM   2117 C C   . ASN B 2 202 ? 4.091   -32.579 22.257 1.00 11.11 ? 354 ASN B C   1 
ATOM   2118 O O   . ASN B 2 202 ? 4.436   -31.839 21.319 1.00 10.08 ? 354 ASN B O   1 
ATOM   2119 C CB  . ASN B 2 202 ? 4.698   -32.361 24.693 1.00 8.92  ? 354 ASN B CB  1 
ATOM   2120 C CG  . ASN B 2 202 ? 5.303   -33.080 25.878 1.00 11.16 ? 354 ASN B CG  1 
ATOM   2121 O OD1 . ASN B 2 202 ? 5.932   -34.134 25.729 1.00 12.47 ? 354 ASN B OD1 1 
ATOM   2122 N ND2 . ASN B 2 202 ? 5.108   -32.526 27.069 1.00 10.88 ? 354 ASN B ND2 1 
ATOM   2123 N N   . PHE B 2 203 ? 2.851   -33.044 22.392 1.00 9.86  ? 355 PHE B N   1 
ATOM   2124 C CA  . PHE B 2 203 ? 1.828   -32.832 21.365 1.00 13.20 ? 355 PHE B CA  1 
ATOM   2125 C C   . PHE B 2 203 ? 0.443   -32.839 21.999 1.00 10.27 ? 355 PHE B C   1 
ATOM   2126 O O   . PHE B 2 203 ? 0.304   -32.820 23.228 1.00 10.70 ? 355 PHE B O   1 
ATOM   2127 C CB  . PHE B 2 203 ? 1.940   -33.981 20.343 1.00 14.47 ? 355 PHE B CB  1 
ATOM   2128 C CG  . PHE B 2 203 ? 2.155   -35.342 20.983 1.00 11.30 ? 355 PHE B CG  1 
ATOM   2129 C CD1 . PHE B 2 203 ? 1.152   -35.949 21.716 1.00 13.00 ? 355 PHE B CD1 1 
ATOM   2130 C CD2 . PHE B 2 203 ? 3.369   -36.004 20.850 1.00 13.06 ? 355 PHE B CD2 1 
ATOM   2131 C CE1 . PHE B 2 203 ? 1.344   -37.188 22.317 1.00 11.38 ? 355 PHE B CE1 1 
ATOM   2132 C CE2 . PHE B 2 203 ? 3.579   -37.248 21.441 1.00 13.65 ? 355 PHE B CE2 1 
ATOM   2133 C CZ  . PHE B 2 203 ? 2.576   -37.841 22.171 1.00 12.11 ? 355 PHE B CZ  1 
ATOM   2134 N N   . GLY B 2 204 ? -0.597  -32.871 21.168 1.00 9.20  ? 356 GLY B N   1 
ATOM   2135 C CA  . GLY B 2 204 ? -1.950  -32.955 21.698 1.00 10.36 ? 356 GLY B CA  1 
ATOM   2136 C C   . GLY B 2 204 ? -2.615  -31.603 21.755 1.00 13.56 ? 356 GLY B C   1 
ATOM   2137 O O   . GLY B 2 204 ? -2.084  -30.640 21.205 1.00 9.72  ? 356 GLY B O   1 
ATOM   2138 N N   . ARG B 2 205 ? -3.797  -31.549 22.365 1.00 11.91 ? 357 ARG B N   1 
ATOM   2139 C CA  . ARG B 2 205 ? -4.687  -30.389 22.231 1.00 15.21 ? 357 ARG B CA  1 
ATOM   2140 C C   . ARG B 2 205 ? -4.296  -29.173 23.071 1.00 9.35  ? 357 ARG B C   1 
ATOM   2141 O O   . ARG B 2 205 ? -4.822  -28.086 22.878 1.00 13.19 ? 357 ARG B O   1 
ATOM   2142 C CB  . ARG B 2 205 ? -6.133  -30.769 22.549 1.00 15.69 ? 357 ARG B CB  1 
ATOM   2143 C CG  . ARG B 2 205 ? -6.260  -31.415 23.906 1.00 15.98 ? 357 ARG B CG  1 
ATOM   2144 C CD  . ARG B 2 205 ? -7.687  -31.432 24.448 1.00 19.30 ? 357 ARG B CD  1 
ATOM   2145 N NE  . ARG B 2 205 ? -7.634  -31.753 25.874 1.00 22.37 ? 357 ARG B NE  1 
ATOM   2146 C CZ  . ARG B 2 205 ? -7.622  -30.850 26.846 1.00 20.34 ? 357 ARG B CZ  1 
ATOM   2147 N NH1 . ARG B 2 205 ? -7.728  -29.561 26.555 1.00 18.80 ? 357 ARG B NH1 1 
ATOM   2148 N NH2 . ARG B 2 205 ? -7.531  -31.245 28.112 1.00 26.46 ? 357 ARG B NH2 1 
ATOM   2149 N N   . CYS B 2 206 ? -3.419  -29.354 24.042 1.00 9.94  ? 358 CYS B N   1 
ATOM   2150 C CA  . CYS B 2 206 ? -2.885  -28.216 24.776 1.00 12.80 ? 358 CYS B CA  1 
ATOM   2151 C C   . CYS B 2 206 ? -1.739  -27.483 24.071 1.00 13.00 ? 358 CYS B C   1 
ATOM   2152 O O   . CYS B 2 206 ? -1.284  -26.448 24.558 1.00 14.05 ? 358 CYS B O   1 
ATOM   2153 C CB  . CYS B 2 206 ? -2.483  -28.670 26.193 1.00 12.01 ? 358 CYS B CB  1 
ATOM   2154 S SG  . CYS B 2 206 ? -3.912  -29.275 27.180 1.00 15.86 ? 358 CYS B SG  1 
ATOM   2155 N N   . VAL B 2 207 ? -1.275  -27.998 22.936 1.00 13.00 ? 359 VAL B N   1 
ATOM   2156 C CA  . VAL B 2 207 ? -0.246  -27.290 22.152 1.00 10.97 ? 359 VAL B CA  1 
ATOM   2157 C C   . VAL B 2 207 ? -0.920  -26.345 21.183 1.00 12.18 ? 359 VAL B C   1 
ATOM   2158 O O   . VAL B 2 207 ? -1.760  -26.777 20.419 1.00 10.12 ? 359 VAL B O   1 
ATOM   2159 C CB  . VAL B 2 207 ? 0.661   -28.276 21.353 1.00 12.44 ? 359 VAL B CB  1 
ATOM   2160 C CG1 . VAL B 2 207 ? 1.634   -27.496 20.450 1.00 10.16 ? 359 VAL B CG1 1 
ATOM   2161 C CG2 . VAL B 2 207 ? 1.446   -29.160 22.284 1.00 9.05  ? 359 VAL B CG2 1 
ATOM   2162 N N   . ASP B 2 208 ? -0.523  -25.072 21.148 1.00 9.12  ? 360 ASP B N   1 
ATOM   2163 C CA  . ASP B 2 208 ? -1.177  -24.140 20.233 1.00 10.89 ? 360 ASP B CA  1 
ATOM   2164 C C   . ASP B 2 208 ? -0.594  -24.195 18.831 1.00 11.27 ? 360 ASP B C   1 
ATOM   2165 O O   . ASP B 2 208 ? -1.327  -24.089 17.842 1.00 13.88 ? 360 ASP B O   1 
ATOM   2166 C CB  . ASP B 2 208 ? -1.084  -22.726 20.815 1.00 11.99 ? 360 ASP B CB  1 
ATOM   2167 C CG  . ASP B 2 208 ? -1.970  -22.582 22.019 1.00 14.18 ? 360 ASP B CG  1 
ATOM   2168 O OD1 . ASP B 2 208 ? -3.202  -22.619 21.819 1.00 14.24 ? 360 ASP B OD1 1 
ATOM   2169 O OD2 . ASP B 2 208 ? -1.464  -22.508 23.172 1.00 14.20 ? 360 ASP B OD2 1 
ATOM   2170 N N   . LEU B 2 209 ? 0.727   -24.308 18.742 1.00 8.44  ? 361 LEU B N   1 
ATOM   2171 C CA  . LEU B 2 209 ? 1.397   -24.365 17.458 1.00 9.61  ? 361 LEU B CA  1 
ATOM   2172 C C   . LEU B 2 209 ? 2.812   -24.869 17.675 1.00 8.67  ? 361 LEU B C   1 
ATOM   2173 O O   . LEU B 2 209 ? 3.255   -25.043 18.812 1.00 8.75  ? 361 LEU B O   1 
ATOM   2174 C CB  . LEU B 2 209 ? 1.417   -22.989 16.764 1.00 10.36 ? 361 LEU B CB  1 
ATOM   2175 C CG  . LEU B 2 209 ? 2.345   -21.880 17.291 1.00 12.37 ? 361 LEU B CG  1 
ATOM   2176 C CD1 . LEU B 2 209 ? 2.163   -20.629 16.423 1.00 14.19 ? 361 LEU B CD1 1 
ATOM   2177 C CD2 . LEU B 2 209 ? 2.077   -21.502 18.750 1.00 11.83 ? 361 LEU B CD2 1 
ATOM   2178 N N   . PHE B 2 210 ? 3.503   -25.159 16.582 1.00 10.60 ? 362 PHE B N   1 
ATOM   2179 C CA  . PHE B 2 210 ? 4.913   -25.541 16.644 1.00 11.41 ? 362 PHE B CA  1 
ATOM   2180 C C   . PHE B 2 210 ? 5.783   -24.417 16.119 1.00 12.51 ? 362 PHE B C   1 
ATOM   2181 O O   . PHE B 2 210 ? 5.287   -23.477 15.500 1.00 10.67 ? 362 PHE B O   1 
ATOM   2182 C CB  . PHE B 2 210 ? 5.149   -26.838 15.849 1.00 11.51 ? 362 PHE B CB  1 
ATOM   2183 C CG  . PHE B 2 210 ? 4.460   -28.025 16.442 1.00 12.18 ? 362 PHE B CG  1 
ATOM   2184 C CD1 . PHE B 2 210 ? 3.098   -28.213 16.229 1.00 11.54 ? 362 PHE B CD1 1 
ATOM   2185 C CD2 . PHE B 2 210 ? 5.141   -28.933 17.226 1.00 11.20 ? 362 PHE B CD2 1 
ATOM   2186 C CE1 . PHE B 2 210 ? 2.432   -29.305 16.789 1.00 10.51 ? 362 PHE B CE1 1 
ATOM   2187 C CE2 . PHE B 2 210 ? 4.496   -30.014 17.782 1.00 11.44 ? 362 PHE B CE2 1 
ATOM   2188 C CZ  . PHE B 2 210 ? 3.125   -30.195 17.575 1.00 12.25 ? 362 PHE B CZ  1 
ATOM   2189 N N   . ALA B 2 211 ? 7.068   -24.474 16.432 1.00 11.81 ? 363 ALA B N   1 
ATOM   2190 C CA  . ALA B 2 211 ? 8.030   -23.508 15.913 1.00 11.48 ? 363 ALA B CA  1 
ATOM   2191 C C   . ALA B 2 211 ? 9.387   -24.190 15.866 1.00 10.51 ? 363 ALA B C   1 
ATOM   2192 O O   . ALA B 2 211 ? 9.586   -25.225 16.516 1.00 11.50 ? 363 ALA B O   1 
ATOM   2193 C CB  . ALA B 2 211 ? 8.037   -22.214 16.773 1.00 11.81 ? 363 ALA B CB  1 
ATOM   2194 N N   . PRO B 2 212 ? 10.336  -23.641 15.092 1.00 11.53 ? 364 PRO B N   1 
ATOM   2195 C CA  . PRO B 2 212 ? 11.673  -24.259 15.044 1.00 13.81 ? 364 PRO B CA  1 
ATOM   2196 C C   . PRO B 2 212 ? 12.286  -24.519 16.420 1.00 12.58 ? 364 PRO B C   1 
ATOM   2197 O O   . PRO B 2 212 ? 12.329  -23.594 17.214 1.00 12.99 ? 364 PRO B O   1 
ATOM   2198 C CB  . PRO B 2 212 ? 12.481  -23.244 14.254 1.00 11.52 ? 364 PRO B CB  1 
ATOM   2199 C CG  . PRO B 2 212 ? 11.457  -22.704 13.273 1.00 15.07 ? 364 PRO B CG  1 
ATOM   2200 C CD  . PRO B 2 212 ? 10.239  -22.509 14.157 1.00 10.47 ? 364 PRO B CD  1 
ATOM   2201 N N   . GLY B 2 213 ? 12.647  -25.761 16.736 1.00 10.15 ? 365 GLY B N   1 
ATOM   2202 C CA  . GLY B 2 213 ? 13.226  -26.060 18.040 1.00 11.74 ? 365 GLY B CA  1 
ATOM   2203 C C   . GLY B 2 213 ? 14.240  -27.203 18.016 1.00 10.10 ? 365 GLY B C   1 
ATOM   2204 O O   . GLY B 2 213 ? 14.492  -27.852 19.033 1.00 11.59 ? 365 GLY B O   1 
ATOM   2205 N N   . GLU B 2 214 ? 14.862  -27.399 16.865 1.00 11.57 ? 366 GLU B N   1 
ATOM   2206 C CA  . GLU B 2 214 ? 16.003  -28.310 16.714 1.00 13.13 ? 366 GLU B CA  1 
ATOM   2207 C C   . GLU B 2 214 ? 17.127  -27.599 15.999 1.00 13.71 ? 366 GLU B C   1 
ATOM   2208 O O   . GLU B 2 214 ? 16.882  -26.952 14.986 1.00 16.18 ? 366 GLU B O   1 
ATOM   2209 C CB  . GLU B 2 214 ? 15.601  -29.528 15.881 1.00 15.55 ? 366 GLU B CB  1 
ATOM   2210 C CG  . GLU B 2 214 ? 16.747  -30.565 15.799 1.00 16.36 ? 366 GLU B CG  1 
ATOM   2211 C CD  . GLU B 2 214 ? 16.320  -31.956 15.316 1.00 21.41 ? 366 GLU B CD  1 
ATOM   2212 O OE1 . GLU B 2 214 ? 15.240  -32.453 15.698 1.00 21.95 ? 366 GLU B OE1 1 
ATOM   2213 O OE2 . GLU B 2 214 ? 17.105  -32.578 14.563 1.00 25.21 ? 366 GLU B OE2 1 
ATOM   2214 N N   . ASP B 2 215 ? 18.360  -27.762 16.478 1.00 15.84 ? 367 ASP B N   1 
ATOM   2215 C CA  . ASP B 2 215 ? 19.536  -27.215 15.799 1.00 14.62 ? 367 ASP B CA  1 
ATOM   2216 C C   . ASP B 2 215 ? 19.400  -25.692 15.644 1.00 14.51 ? 367 ASP B C   1 
ATOM   2217 O O   . ASP B 2 215 ? 19.495  -25.141 14.540 1.00 13.86 ? 367 ASP B O   1 
ATOM   2218 C CB  . ASP B 2 215 ? 19.698  -27.866 14.425 1.00 15.11 ? 367 ASP B CB  1 
ATOM   2219 C CG  . ASP B 2 215 ? 20.971  -27.443 13.708 1.00 20.05 ? 367 ASP B CG  1 
ATOM   2220 O OD1 . ASP B 2 215 ? 21.915  -26.969 14.378 1.00 19.91 ? 367 ASP B OD1 1 
ATOM   2221 O OD2 . ASP B 2 215 ? 21.015  -27.560 12.456 1.00 21.20 ? 367 ASP B OD2 1 
ATOM   2222 N N   . ILE B 2 216 ? 19.112  -25.025 16.754 1.00 12.19 ? 368 ILE B N   1 
ATOM   2223 C CA  . ILE B 2 216 ? 18.825  -23.588 16.745 1.00 12.66 ? 368 ILE B CA  1 
ATOM   2224 C C   . ILE B 2 216 ? 20.073  -22.835 17.207 1.00 13.36 ? 368 ILE B C   1 
ATOM   2225 O O   . ILE B 2 216 ? 20.506  -22.967 18.361 1.00 13.47 ? 368 ILE B O   1 
ATOM   2226 C CB  . ILE B 2 216 ? 17.682  -23.245 17.712 1.00 12.39 ? 368 ILE B CB  1 
ATOM   2227 C CG1 . ILE B 2 216 ? 16.385  -23.957 17.310 1.00 10.68 ? 368 ILE B CG1 1 
ATOM   2228 C CG2 . ILE B 2 216 ? 17.492  -21.705 17.826 1.00 10.07 ? 368 ILE B CG2 1 
ATOM   2229 C CD1 . ILE B 2 216 ? 15.901  -23.674 15.892 1.00 9.64  ? 368 ILE B CD1 1 
ATOM   2230 N N   . ILE B 2 217 ? 20.666  -22.040 16.340 1.00 13.78 ? 369 ILE B N   1 
ATOM   2231 C CA  . ILE B 2 217 ? 21.896  -21.369 16.742 1.00 16.82 ? 369 ILE B CA  1 
ATOM   2232 C C   . ILE B 2 217 ? 21.578  -20.155 17.614 1.00 16.79 ? 369 ILE B C   1 
ATOM   2233 O O   . ILE B 2 217 ? 20.580  -19.440 17.401 1.00 15.87 ? 369 ILE B O   1 
ATOM   2234 C CB  . ILE B 2 217 ? 22.770  -20.993 15.513 1.00 21.11 ? 369 ILE B CB  1 
ATOM   2235 C CG1 . ILE B 2 217 ? 24.148  -20.489 15.969 1.00 25.01 ? 369 ILE B CG1 1 
ATOM   2236 C CG2 . ILE B 2 217 ? 22.175  -19.825 14.801 1.00 23.80 ? 369 ILE B CG2 1 
ATOM   2237 C CD1 . ILE B 2 217 ? 25.182  -21.607 16.372 1.00 27.75 ? 369 ILE B CD1 1 
ATOM   2238 N N   . GLY B 2 218 ? 22.365  -20.000 18.677 1.00 15.11 ? 370 GLY B N   1 
ATOM   2239 C CA  . GLY B 2 218 ? 22.239  -18.837 19.544 1.00 14.37 ? 370 GLY B CA  1 
ATOM   2240 C C   . GLY B 2 218 ? 23.410  -18.642 20.485 1.00 17.76 ? 370 GLY B C   1 
ATOM   2241 O O   . GLY B 2 218 ? 24.331  -19.459 20.505 1.00 16.03 ? 370 GLY B O   1 
ATOM   2242 N N   . ALA B 2 219 ? 23.377  -17.548 21.252 1.00 15.52 ? 371 ALA B N   1 
ATOM   2243 C CA  . ALA B 2 219 ? 24.445  -17.218 22.203 1.00 20.43 ? 371 ALA B CA  1 
ATOM   2244 C C   . ALA B 2 219 ? 24.895  -18.391 23.062 1.00 21.82 ? 371 ALA B C   1 
ATOM   2245 O O   . ALA B 2 219 ? 24.060  -19.042 23.718 1.00 15.27 ? 371 ALA B O   1 
ATOM   2246 C CB  . ALA B 2 219 ? 23.994  -16.072 23.114 1.00 17.09 ? 371 ALA B CB  1 
ATOM   2247 N N   . SER B 2 220 ? 26.217  -18.604 23.141 1.00 17.07 ? 372 SER B N   1 
ATOM   2248 C CA  . SER B 2 220 ? 26.768  -19.631 24.018 1.00 17.50 ? 372 SER B CA  1 
ATOM   2249 C C   . SER B 2 220 ? 27.486  -18.965 25.183 1.00 22.79 ? 372 SER B C   1 
ATOM   2250 O O   . SER B 2 220 ? 28.290  -18.049 24.986 1.00 22.40 ? 372 SER B O   1 
ATOM   2251 C CB  . SER B 2 220 ? 27.793  -20.484 23.258 1.00 19.45 ? 372 SER B CB  1 
ATOM   2252 O OG  . SER B 2 220 ? 28.357  -21.470 24.113 1.00 20.22 ? 372 SER B OG  1 
ATOM   2253 N N   . SER B 2 221 ? 27.164  -19.367 26.407 1.00 20.37 ? 373 SER B N   1 
ATOM   2254 C CA  . SER B 2 221 ? 27.841  -18.788 27.556 1.00 25.92 ? 373 SER B CA  1 
ATOM   2255 C C   . SER B 2 221 ? 29.258  -19.342 27.752 1.00 26.51 ? 373 SER B C   1 
ATOM   2256 O O   . SER B 2 221 ? 29.933  -18.957 28.698 1.00 26.03 ? 373 SER B O   1 
ATOM   2257 C CB  . SER B 2 221 ? 27.035  -19.045 28.818 1.00 25.35 ? 373 SER B CB  1 
ATOM   2258 O OG  . SER B 2 221 ? 26.954  -20.444 29.058 1.00 26.46 ? 373 SER B OG  1 
ATOM   2259 N N   . ASP B 2 222 ? 29.735  -20.177 26.834 1.00 29.02 ? 374 ASP B N   1 
ATOM   2260 C CA  . ASP B 2 222 ? 31.139  -20.606 26.859 1.00 32.76 ? 374 ASP B CA  1 
ATOM   2261 C C   . ASP B 2 222 ? 32.036  -19.375 26.737 1.00 29.26 ? 374 ASP B C   1 
ATOM   2262 O O   . ASP B 2 222 ? 33.045  -19.294 27.432 1.00 35.53 ? 374 ASP B O   1 
ATOM   2263 C CB  . ASP B 2 222 ? 31.432  -21.629 25.755 1.00 24.62 ? 374 ASP B CB  1 
ATOM   2264 C CG  . ASP B 2 222 ? 30.835  -23.004 26.064 1.00 35.84 ? 374 ASP B CG  1 
ATOM   2265 O OD1 . ASP B 2 222 ? 30.469  -23.256 27.234 1.00 38.86 ? 374 ASP B OD1 1 
ATOM   2266 O OD2 . ASP B 2 222 ? 30.771  -23.861 25.160 1.00 36.46 ? 374 ASP B OD2 1 
ATOM   2267 N N   . CYS B 2 223 ? 31.709  -18.431 25.859 1.00 29.10 ? 375 CYS B N   1 
ATOM   2268 C CA  . CYS B 2 223 ? 32.542  -17.227 25.734 1.00 26.94 ? 375 CYS B CA  1 
ATOM   2269 C C   . CYS B 2 223 ? 31.674  -16.101 25.189 1.00 29.39 ? 375 CYS B C   1 
ATOM   2270 O O   . CYS B 2 223 ? 30.643  -16.353 24.586 1.00 27.15 ? 375 CYS B O   1 
ATOM   2271 C CB  . CYS B 2 223 ? 33.759  -17.501 24.838 1.00 27.33 ? 375 CYS B CB  1 
ATOM   2272 S SG  . CYS B 2 223 ? 33.552  -17.080 23.087 1.00 31.82 ? 375 CYS B SG  1 
ATOM   2273 N N   . SER B 2 224 ? 32.082  -14.855 25.415 1.00 23.88 ? 376 SER B N   1 
ATOM   2274 C CA  . SER B 2 224 ? 31.205  -13.714 25.191 1.00 25.22 ? 376 SER B CA  1 
ATOM   2275 C C   . SER B 2 224 ? 30.850  -13.474 23.731 1.00 25.14 ? 376 SER B C   1 
ATOM   2276 O O   . SER B 2 224 ? 29.974  -12.659 23.428 1.00 26.97 ? 376 SER B O   1 
ATOM   2277 C CB  . SER B 2 224 ? 31.857  -12.455 25.765 1.00 33.36 ? 376 SER B CB  1 
ATOM   2278 O OG  . SER B 2 224 ? 32.954  -12.045 24.968 1.00 39.25 ? 376 SER B OG  1 
ATOM   2279 N N   . THR B 2 225 ? 31.513  -14.178 22.821 1.00 23.78 ? 377 THR B N   1 
ATOM   2280 C CA  . THR B 2 225 ? 31.184  -14.053 21.409 1.00 24.74 ? 377 THR B CA  1 
ATOM   2281 C C   . THR B 2 225 ? 30.876  -15.412 20.796 1.00 25.21 ? 377 THR B C   1 
ATOM   2282 O O   . THR B 2 225 ? 30.721  -15.526 19.582 1.00 27.16 ? 377 THR B O   1 
ATOM   2283 C CB  . THR B 2 225 ? 32.318  -13.376 20.623 1.00 30.41 ? 377 THR B CB  1 
ATOM   2284 O OG1 . THR B 2 225 ? 33.506  -14.164 20.758 1.00 26.72 ? 377 THR B OG1 1 
ATOM   2285 C CG2 . THR B 2 225 ? 32.566  -11.966 21.132 1.00 29.58 ? 377 THR B CG2 1 
ATOM   2286 N N   . CYS B 2 226 ? 30.791  -16.443 21.623 1.00 21.06 ? 378 CYS B N   1 
ATOM   2287 C CA  . CYS B 2 226 ? 30.583  -17.783 21.095 1.00 22.59 ? 378 CYS B CA  1 
ATOM   2288 C C   . CYS B 2 226 ? 29.109  -18.085 20.799 1.00 22.57 ? 378 CYS B C   1 
ATOM   2289 O O   . CYS B 2 226 ? 28.205  -17.423 21.343 1.00 21.10 ? 378 CYS B O   1 
ATOM   2290 C CB  . CYS B 2 226 ? 31.099  -18.796 22.119 1.00 22.30 ? 378 CYS B CB  1 
ATOM   2291 S SG  . CYS B 2 226 ? 32.925  -18.835 22.271 1.00 33.04 ? 378 CYS B SG  1 
ATOM   2292 N N   . PHE B 2 227 ? 28.879  -19.072 19.916 1.00 17.75 ? 379 PHE B N   1 
ATOM   2293 C CA  . PHE B 2 227 ? 27.532  -19.514 19.547 1.00 17.42 ? 379 PHE B CA  1 
ATOM   2294 C C   . PHE B 2 227 ? 27.473  -21.025 19.639 1.00 19.26 ? 379 PHE B C   1 
ATOM   2295 O O   . PHE B 2 227 ? 28.498  -21.691 19.453 1.00 18.11 ? 379 PHE B O   1 
ATOM   2296 C CB  . PHE B 2 227 ? 27.179  -19.077 18.129 1.00 16.05 ? 379 PHE B CB  1 
ATOM   2297 C CG  . PHE B 2 227 ? 26.817  -17.630 18.014 1.00 22.60 ? 379 PHE B CG  1 
ATOM   2298 C CD1 . PHE B 2 227 ? 27.803  -16.651 17.961 1.00 24.11 ? 379 PHE B CD1 1 
ATOM   2299 C CD2 . PHE B 2 227 ? 25.490  -17.245 17.963 1.00 22.11 ? 379 PHE B CD2 1 
ATOM   2300 C CE1 . PHE B 2 227 ? 27.466  -15.309 17.875 1.00 26.77 ? 379 PHE B CE1 1 
ATOM   2301 C CE2 . PHE B 2 227 ? 25.149  -15.912 17.870 1.00 22.73 ? 379 PHE B CE2 1 
ATOM   2302 C CZ  . PHE B 2 227 ? 26.134  -14.944 17.823 1.00 25.28 ? 379 PHE B CZ  1 
ATOM   2303 N N   . VAL B 2 228 ? 26.285  -21.569 19.888 1.00 17.77 ? 380 VAL B N   1 
ATOM   2304 C CA  . VAL B 2 228 ? 26.097  -23.019 19.997 1.00 15.93 ? 380 VAL B CA  1 
ATOM   2305 C C   . VAL B 2 228 ? 24.697  -23.350 19.463 1.00 18.32 ? 380 VAL B C   1 
ATOM   2306 O O   . VAL B 2 228 ? 23.784  -22.543 19.618 1.00 15.83 ? 380 VAL B O   1 
ATOM   2307 C CB  . VAL B 2 228 ? 26.266  -23.509 21.442 1.00 17.30 ? 380 VAL B CB  1 
ATOM   2308 C CG1 . VAL B 2 228 ? 25.157  -22.972 22.353 1.00 17.97 ? 380 VAL B CG1 1 
ATOM   2309 C CG2 . VAL B 2 228 ? 26.301  -25.021 21.487 1.00 16.21 ? 380 VAL B CG2 1 
ATOM   2310 N N   . SER B 2 229 ? 24.527  -24.499 18.801 1.00 19.19 ? 381 SER B N   1 
ATOM   2311 C CA  . SER B 2 229 ? 23.186  -24.928 18.426 1.00 17.03 ? 381 SER B CA  1 
ATOM   2312 C C   . SER B 2 229 ? 22.594  -25.763 19.549 1.00 14.91 ? 381 SER B C   1 
ATOM   2313 O O   . SER B 2 229 ? 23.239  -26.684 20.035 1.00 14.05 ? 381 SER B O   1 
ATOM   2314 C CB  . SER B 2 229 ? 23.173  -25.729 17.120 1.00 16.32 ? 381 SER B CB  1 
ATOM   2315 O OG  . SER B 2 229 ? 23.507  -24.892 16.037 1.00 26.96 ? 381 SER B OG  1 
ATOM   2316 N N   . GLN B 2 230 ? 21.351  -25.460 19.923 1.00 14.19 ? 382 GLN B N   1 
ATOM   2317 C CA  . GLN B 2 230 ? 20.618  -26.180 20.962 1.00 14.88 ? 382 GLN B CA  1 
ATOM   2318 C C   . GLN B 2 230 ? 19.225  -26.519 20.453 1.00 12.93 ? 382 GLN B C   1 
ATOM   2319 O O   . GLN B 2 230 ? 18.732  -25.902 19.516 1.00 12.30 ? 382 GLN B O   1 
ATOM   2320 C CB  . GLN B 2 230 ? 20.531  -25.324 22.227 1.00 15.00 ? 382 GLN B CB  1 
ATOM   2321 C CG  . GLN B 2 230 ? 21.875  -25.192 22.953 1.00 14.31 ? 382 GLN B CG  1 
ATOM   2322 C CD  . GLN B 2 230 ? 21.735  -24.655 24.361 1.00 16.56 ? 382 GLN B CD  1 
ATOM   2323 O OE1 . GLN B 2 230 ? 20.620  -24.523 24.888 1.00 14.64 ? 382 GLN B OE1 1 
ATOM   2324 N NE2 . GLN B 2 230 ? 22.873  -24.302 24.974 1.00 17.27 ? 382 GLN B NE2 1 
ATOM   2325 N N   . SER B 2 231 ? 18.614  -27.514 21.083 1.00 11.27 ? 383 SER B N   1 
ATOM   2326 C CA  . SER B 2 231 ? 17.292  -28.023 20.722 1.00 12.33 ? 383 SER B CA  1 
ATOM   2327 C C   . SER B 2 231 ? 16.369  -28.099 21.931 1.00 14.20 ? 383 SER B C   1 
ATOM   2328 O O   . SER B 2 231 ? 16.819  -28.479 23.007 1.00 9.35  ? 383 SER B O   1 
ATOM   2329 C CB  . SER B 2 231 ? 17.430  -29.406 20.089 1.00 14.48 ? 383 SER B CB  1 
ATOM   2330 O OG  . SER B 2 231 ? 18.267  -29.320 18.946 1.00 13.56 ? 383 SER B OG  1 
ATOM   2331 N N   . GLY B 2 232 ? 15.063  -27.887 21.729 1.00 11.53 ? 384 GLY B N   1 
ATOM   2332 C CA  . GLY B 2 232 ? 14.082  -28.042 22.804 1.00 11.38 ? 384 GLY B CA  1 
ATOM   2333 C C   . GLY B 2 232 ? 12.795  -27.281 22.555 1.00 11.32 ? 384 GLY B C   1 
ATOM   2334 O O   . GLY B 2 232 ? 12.744  -26.415 21.691 1.00 10.56 ? 384 GLY B O   1 
ATOM   2335 N N   . THR B 2 233 ? 11.732  -27.624 23.277 1.00 8.85  ? 385 THR B N   1 
ATOM   2336 C CA  . THR B 2 233 ? 10.515  -26.852 23.073 1.00 10.27 ? 385 THR B CA  1 
ATOM   2337 C C   . THR B 2 233 ? 10.652  -25.423 23.638 1.00 11.70 ? 385 THR B C   1 
ATOM   2338 O O   . THR B 2 233 ? 9.890   -24.552 23.253 1.00 9.99  ? 385 THR B O   1 
ATOM   2339 C CB  . THR B 2 233 ? 9.266   -27.569 23.671 1.00 9.59  ? 385 THR B CB  1 
ATOM   2340 O OG1 . THR B 2 233 ? 9.531   -27.935 25.035 1.00 10.17 ? 385 THR B OG1 1 
ATOM   2341 C CG2 . THR B 2 233 ? 8.968   -28.847 22.892 1.00 9.23  ? 385 THR B CG2 1 
ATOM   2342 N N   . SER B 2 234 ? 11.567  -25.187 24.582 1.00 11.65 ? 386 SER B N   1 
ATOM   2343 C CA  . SER B 2 234 ? 11.882  -23.798 24.971 1.00 11.09 ? 386 SER B CA  1 
ATOM   2344 C C   . SER B 2 234 ? 12.412  -22.985 23.796 1.00 12.04 ? 386 SER B C   1 
ATOM   2345 O O   . SER B 2 234 ? 12.091  -21.807 23.691 1.00 9.66  ? 386 SER B O   1 
ATOM   2346 C CB  . SER B 2 234 ? 12.948  -23.759 26.038 1.00 15.70 ? 386 SER B CB  1 
ATOM   2347 O OG  . SER B 2 234 ? 12.363  -24.441 27.145 1.00 20.47 ? 386 SER B OG  1 
ATOM   2348 N N   . GLN B 2 235 ? 13.315  -23.548 22.987 1.00 9.42  ? 387 GLN B N   1 
ATOM   2349 C CA  . GLN B 2 235 ? 13.825  -22.793 21.818 1.00 11.03 ? 387 GLN B CA  1 
ATOM   2350 C C   . GLN B 2 235 ? 12.644  -22.475 20.901 1.00 10.02 ? 387 GLN B C   1 
ATOM   2351 O O   . GLN B 2 235 ? 12.530  -21.357 20.383 1.00 10.58 ? 387 GLN B O   1 
ATOM   2352 C CB  . GLN B 2 235 ? 14.929  -23.537 21.050 1.00 11.74 ? 387 GLN B CB  1 
ATOM   2353 C CG  . GLN B 2 235 ? 16.372  -23.388 21.581 1.00 11.68 ? 387 GLN B CG  1 
ATOM   2354 C CD  . GLN B 2 235 ? 16.619  -24.150 22.853 1.00 14.39 ? 387 GLN B CD  1 
ATOM   2355 O OE1 . GLN B 2 235 ? 15.924  -25.127 23.166 1.00 12.25 ? 387 GLN B OE1 1 
ATOM   2356 N NE2 . GLN B 2 235 ? 17.660  -23.746 23.584 1.00 14.06 ? 387 GLN B NE2 1 
ATOM   2357 N N   . ALA B 2 236 ? 11.774  -23.458 20.685 1.00 10.67 ? 388 ALA B N   1 
ATOM   2358 C CA  . ALA B 2 236 ? 10.557  -23.220 19.901 1.00 9.16  ? 388 ALA B CA  1 
ATOM   2359 C C   . ALA B 2 236 ? 9.712   -22.091 20.509 1.00 10.68 ? 388 ALA B C   1 
ATOM   2360 O O   . ALA B 2 236 ? 9.265   -21.192 19.813 1.00 8.93  ? 388 ALA B O   1 
ATOM   2361 C CB  . ALA B 2 236 ? 9.740   -24.515 19.809 1.00 7.72  ? 388 ALA B CB  1 
ATOM   2362 N N   . ALA B 2 237 ? 9.486   -22.162 21.819 1.00 11.39 ? 389 ALA B N   1 
ATOM   2363 C CA  . ALA B 2 237 ? 8.688   -21.153 22.517 1.00 9.87  ? 389 ALA B CA  1 
ATOM   2364 C C   . ALA B 2 237 ? 9.331   -19.762 22.399 1.00 12.98 ? 389 ALA B C   1 
ATOM   2365 O O   . ALA B 2 237 ? 8.640   -18.744 22.362 1.00 12.56 ? 389 ALA B O   1 
ATOM   2366 C CB  . ALA B 2 237 ? 8.516   -21.540 23.955 1.00 7.58  ? 389 ALA B CB  1 
ATOM   2367 N N   . ALA B 2 238 ? 10.663  -19.726 22.409 1.00 10.65 ? 390 ALA B N   1 
ATOM   2368 C CA  . ALA B 2 238 ? 11.392  -18.453 22.275 1.00 12.41 ? 390 ALA B CA  1 
ATOM   2369 C C   . ALA B 2 238 ? 11.120  -17.796 20.910 1.00 11.25 ? 390 ALA B C   1 
ATOM   2370 O O   . ALA B 2 238 ? 11.029  -16.569 20.814 1.00 11.46 ? 390 ALA B O   1 
ATOM   2371 C CB  . ALA B 2 238 ? 12.909  -18.679 22.455 1.00 10.31 ? 390 ALA B CB  1 
ATOM   2372 N N   . HIS B 2 239 ? 11.005  -18.597 19.851 1.00 10.21 ? 391 HIS B N   1 
ATOM   2373 C CA  . HIS B 2 239 ? 10.639  -18.045 18.534 1.00 13.44 ? 391 HIS B CA  1 
ATOM   2374 C C   . HIS B 2 239 ? 9.261   -17.377 18.605 1.00 11.87 ? 391 HIS B C   1 
ATOM   2375 O O   . HIS B 2 239 ? 9.070   -16.285 18.089 1.00 12.19 ? 391 HIS B O   1 
ATOM   2376 C CB  . HIS B 2 239 ? 10.585  -19.154 17.483 1.00 12.82 ? 391 HIS B CB  1 
ATOM   2377 C CG  . HIS B 2 239 ? 11.939  -19.562 16.990 1.00 14.44 ? 391 HIS B CG  1 
ATOM   2378 N ND1 . HIS B 2 239 ? 12.774  -20.369 17.726 1.00 12.70 ? 391 HIS B ND1 1 
ATOM   2379 C CD2 . HIS B 2 239 ? 12.605  -19.276 15.847 1.00 12.03 ? 391 HIS B CD2 1 
ATOM   2380 C CE1 . HIS B 2 239 ? 13.902  -20.569 17.058 1.00 14.97 ? 391 HIS B CE1 1 
ATOM   2381 N NE2 . HIS B 2 239 ? 13.828  -19.908 15.917 1.00 13.17 ? 391 HIS B NE2 1 
ATOM   2382 N N   . VAL B 2 240 ? 8.312   -18.024 19.285 1.00 12.03 ? 392 VAL B N   1 
ATOM   2383 C CA  . VAL B 2 240 ? 6.950   -17.487 19.341 1.00 10.87 ? 392 VAL B CA  1 
ATOM   2384 C C   . VAL B 2 240 ? 6.912   -16.269 20.250 1.00 11.06 ? 392 VAL B C   1 
ATOM   2385 O O   . VAL B 2 240 ? 6.248   -15.290 19.925 1.00 12.97 ? 392 VAL B O   1 
ATOM   2386 C CB  . VAL B 2 240 ? 5.906   -18.598 19.768 1.00 12.06 ? 392 VAL B CB  1 
ATOM   2387 C CG1 . VAL B 2 240 ? 4.532   -17.988 20.078 1.00 11.18 ? 392 VAL B CG1 1 
ATOM   2388 C CG2 . VAL B 2 240 ? 5.771   -19.650 18.679 1.00 8.79  ? 392 VAL B CG2 1 
ATOM   2389 N N   . ALA B 2 241 ? 7.680   -16.286 21.341 1.00 10.15 ? 393 ALA B N   1 
ATOM   2390 C CA  . ALA B 2 241 ? 7.820   -15.096 22.180 1.00 10.69 ? 393 ALA B CA  1 
ATOM   2391 C C   . ALA B 2 241 ? 8.357   -13.908 21.377 1.00 13.69 ? 393 ALA B C   1 
ATOM   2392 O O   . ALA B 2 241 ? 7.839   -12.798 21.474 1.00 12.83 ? 393 ALA B O   1 
ATOM   2393 C CB  . ALA B 2 241 ? 8.721   -15.375 23.382 1.00 12.21 ? 393 ALA B CB  1 
ATOM   2394 N N   . GLY B 2 242 ? 9.403   -14.145 20.595 1.00 14.14 ? 394 GLY B N   1 
ATOM   2395 C CA  . GLY B 2 242 ? 9.924   -13.146 19.664 1.00 14.20 ? 394 GLY B CA  1 
ATOM   2396 C C   . GLY B 2 242 ? 8.908   -12.657 18.633 1.00 14.11 ? 394 GLY B C   1 
ATOM   2397 O O   . GLY B 2 242 ? 8.774   -11.454 18.403 1.00 14.58 ? 394 GLY B O   1 
ATOM   2398 N N   . ILE B 2 243 ? 8.202   -13.591 17.994 1.00 11.81 ? 395 ILE B N   1 
ATOM   2399 C CA  . ILE B 2 243 ? 7.169   -13.227 17.027 1.00 10.60 ? 395 ILE B CA  1 
ATOM   2400 C C   . ILE B 2 243 ? 6.040   -12.419 17.681 1.00 15.72 ? 395 ILE B C   1 
ATOM   2401 O O   . ILE B 2 243 ? 5.623   -11.378 17.156 1.00 12.85 ? 395 ILE B O   1 
ATOM   2402 C CB  . ILE B 2 243 ? 6.562   -14.500 16.329 1.00 13.75 ? 395 ILE B CB  1 
ATOM   2403 C CG1 . ILE B 2 243 ? 7.619   -15.222 15.467 1.00 12.36 ? 395 ILE B CG1 1 
ATOM   2404 C CG2 . ILE B 2 243 ? 5.302   -14.139 15.504 1.00 14.67 ? 395 ILE B CG2 1 
ATOM   2405 C CD1 . ILE B 2 243 ? 7.161   -16.589 14.912 1.00 13.68 ? 395 ILE B CD1 1 
ATOM   2406 N N   . ALA B 2 244 ? 5.638   -12.825 18.888 1.00 14.43 ? 396 ALA B N   1 
ATOM   2407 C CA  . ALA B 2 244 ? 4.566   -12.126 19.616 1.00 13.36 ? 396 ALA B CA  1 
ATOM   2408 C C   . ALA B 2 244 ? 4.995   -10.690 19.965 1.00 12.94 ? 396 ALA B C   1 
ATOM   2409 O O   . ALA B 2 244 ? 4.193   -9.750  19.862 1.00 15.57 ? 396 ALA B O   1 
ATOM   2410 C CB  . ALA B 2 244 ? 4.200   -12.878 20.897 1.00 10.86 ? 396 ALA B CB  1 
ATOM   2411 N N   . ALA B 2 245 ? 6.239   -10.518 20.396 1.00 13.84 ? 397 ALA B N   1 
ATOM   2412 C CA  . ALA B 2 245 ? 6.756   -9.183  20.768 1.00 15.18 ? 397 ALA B CA  1 
ATOM   2413 C C   . ALA B 2 245 ? 6.706   -8.221  19.567 1.00 16.81 ? 397 ALA B C   1 
ATOM   2414 O O   . ALA B 2 245 ? 6.416   -7.019  19.698 1.00 18.13 ? 397 ALA B O   1 
ATOM   2415 C CB  . ALA B 2 245 ? 8.163   -9.300  21.319 1.00 15.39 ? 397 ALA B CB  1 
ATOM   2416 N N   . MET B 2 246 ? 7.031   -8.760  18.399 1.00 14.27 ? 398 MET B N   1 
ATOM   2417 C CA  . MET B 2 246 ? 6.997   -8.041  17.121 1.00 17.58 ? 398 MET B CA  1 
ATOM   2418 C C   . MET B 2 246 ? 5.553   -7.717  16.756 1.00 17.60 ? 398 MET B C   1 
ATOM   2419 O O   . MET B 2 246 ? 5.246   -6.655  16.241 1.00 15.81 ? 398 MET B O   1 
ATOM   2420 C CB  . MET B 2 246 ? 7.625   -8.903  16.025 1.00 15.85 ? 398 MET B CB  1 
ATOM   2421 C CG  . MET B 2 246 ? 9.055   -9.296  16.246 1.00 25.58 ? 398 MET B CG  1 
ATOM   2422 S SD  . MET B 2 246 ? 10.288  -8.240  15.553 1.00 39.39 ? 398 MET B SD  1 
ATOM   2423 C CE  . MET B 2 246 ? 10.295  -8.944  13.940 1.00 23.88 ? 398 MET B CE  1 
ATOM   2424 N N   . MET B 2 247 ? 4.672   -8.691  16.937 1.00 15.19 ? 399 MET B N   1 
ATOM   2425 C CA  . MET B 2 247 ? 3.261   -8.464  16.597 1.00 14.05 ? 399 MET B CA  1 
ATOM   2426 C C   . MET B 2 247 ? 2.637   -7.406  17.506 1.00 15.07 ? 399 MET B C   1 
ATOM   2427 O O   . MET B 2 247 ? 1.847   -6.581  17.058 1.00 16.36 ? 399 MET B O   1 
ATOM   2428 C CB  . MET B 2 247 ? 2.456   -9.772  16.688 1.00 14.01 ? 399 MET B CB  1 
ATOM   2429 C CG  . MET B 2 247 ? 2.707   -10.744 15.529 1.00 16.97 ? 399 MET B CG  1 
ATOM   2430 S SD  . MET B 2 247 ? 1.823   -12.310 15.752 1.00 22.00 ? 399 MET B SD  1 
ATOM   2431 C CE  . MET B 2 247 ? 2.098   -13.191 14.186 1.00 25.08 ? 399 MET B CE  1 
ATOM   2432 N N   . LEU B 2 248 ? 3.007   -7.431  18.783 1.00 13.87 ? 400 LEU B N   1 
ATOM   2433 C CA  . LEU B 2 248 ? 2.451   -6.484  19.754 1.00 15.97 ? 400 LEU B CA  1 
ATOM   2434 C C   . LEU B 2 248 ? 3.085   -5.093  19.592 1.00 16.90 ? 400 LEU B C   1 
ATOM   2435 O O   . LEU B 2 248 ? 2.512   -4.109  20.013 1.00 19.25 ? 400 LEU B O   1 
ATOM   2436 C CB  . LEU B 2 248 ? 2.653   -6.991  21.185 1.00 15.17 ? 400 LEU B CB  1 
ATOM   2437 C CG  . LEU B 2 248 ? 1.759   -8.181  21.557 1.00 16.83 ? 400 LEU B CG  1 
ATOM   2438 C CD1 . LEU B 2 248 ? 2.233   -8.803  22.866 1.00 17.67 ? 400 LEU B CD1 1 
ATOM   2439 C CD2 . LEU B 2 248 ? 0.290   -7.791  21.646 1.00 19.16 ? 400 LEU B CD2 1 
ATOM   2440 N N   . SER B 2 249 ? 4.307   -5.008  19.070 1.00 16.47 ? 401 SER B N   1 
ATOM   2441 C CA  . SER B 2 249 ? 4.863   -3.685  18.754 1.00 19.67 ? 401 SER B CA  1 
ATOM   2442 C C   . SER B 2 249 ? 4.142   -2.983  17.618 1.00 18.65 ? 401 SER B C   1 
ATOM   2443 O O   . SER B 2 249 ? 3.949   -1.764  17.660 1.00 17.57 ? 401 SER B O   1 
ATOM   2444 C CB  . SER B 2 249 ? 6.333   -3.807  18.404 1.00 20.53 ? 401 SER B CB  1 
ATOM   2445 O OG  . SER B 2 249 ? 6.996   -4.461  19.450 1.00 26.46 ? 401 SER B OG  1 
ATOM   2446 N N   . ALA B 2 250 ? 3.714   -3.769  16.637 1.00 15.43 ? 402 ALA B N   1 
ATOM   2447 C CA  . ALA B 2 250 ? 3.014   -3.264  15.453 1.00 18.84 ? 402 ALA B CA  1 
ATOM   2448 C C   . ALA B 2 250 ? 1.564   -2.946  15.783 1.00 19.43 ? 402 ALA B C   1 
ATOM   2449 O O   . ALA B 2 250 ? 0.991   -1.959  15.260 1.00 17.96 ? 402 ALA B O   1 
ATOM   2450 C CB  . ALA B 2 250 ? 3.101   -4.277  14.304 1.00 15.41 ? 402 ALA B CB  1 
ATOM   2451 N N   . GLU B 2 251 ? 0.961   -3.772  16.636 1.00 14.96 ? 403 GLU B N   1 
ATOM   2452 C CA  . GLU B 2 251 ? -0.453  -3.612  16.992 1.00 16.21 ? 403 GLU B CA  1 
ATOM   2453 C C   . GLU B 2 251 ? -0.571  -3.752  18.503 1.00 16.94 ? 403 GLU B C   1 
ATOM   2454 O O   . GLU B 2 251 ? -0.952  -4.804  19.019 1.00 17.03 ? 403 GLU B O   1 
ATOM   2455 C CB  . GLU B 2 251 ? -1.328  -4.671  16.315 1.00 19.23 ? 403 GLU B CB  1 
ATOM   2456 C CG  . GLU B 2 251 ? -1.338  -4.662  14.789 1.00 20.02 ? 403 GLU B CG  1 
ATOM   2457 C CD  . GLU B 2 251 ? -2.288  -5.723  14.217 1.00 23.58 ? 403 GLU B CD  1 
ATOM   2458 O OE1 . GLU B 2 251 ? -1.916  -6.921  14.177 1.00 25.29 ? 403 GLU B OE1 1 
ATOM   2459 O OE2 . GLU B 2 251 ? -3.418  -5.375  13.814 1.00 27.50 ? 403 GLU B OE2 1 
ATOM   2460 N N   . PRO B 2 252 ? -0.183  -2.698  19.237 1.00 17.80 ? 404 PRO B N   1 
ATOM   2461 C CA  . PRO B 2 252 ? -0.082  -2.773  20.702 1.00 18.05 ? 404 PRO B CA  1 
ATOM   2462 C C   . PRO B 2 252 ? -1.417  -3.055  21.416 1.00 14.98 ? 404 PRO B C   1 
ATOM   2463 O O   . PRO B 2 252 ? -1.372  -3.467  22.577 1.00 16.63 ? 404 PRO B O   1 
ATOM   2464 C CB  . PRO B 2 252 ? 0.481   -1.389  21.089 1.00 20.27 ? 404 PRO B CB  1 
ATOM   2465 C CG  . PRO B 2 252 ? 1.126   -0.890  19.812 1.00 17.72 ? 404 PRO B CG  1 
ATOM   2466 C CD  . PRO B 2 252 ? 0.256   -1.393  18.721 1.00 17.36 ? 404 PRO B CD  1 
ATOM   2467 N N   . GLU B 2 253 ? -2.555  -2.779  20.789 1.00 15.17 ? 405 GLU B N   1 
ATOM   2468 C CA  . GLU B 2 253 ? -3.833  -2.993  21.466 1.00 17.46 ? 405 GLU B CA  1 
ATOM   2469 C C   . GLU B 2 253 ? -4.359  -4.433  21.353 1.00 17.65 ? 405 GLU B C   1 
ATOM   2470 O O   . GLU B 2 253 ? -5.438  -4.730  21.860 1.00 17.57 ? 405 GLU B O   1 
ATOM   2471 C CB  . GLU B 2 253 ? -4.884  -1.989  20.974 1.00 16.99 ? 405 GLU B CB  1 
ATOM   2472 C CG  . GLU B 2 253 ? -4.505  -0.525  21.286 1.00 20.35 ? 405 GLU B CG  1 
ATOM   2473 C CD  . GLU B 2 253 ? -5.500  0.507   20.741 1.00 29.75 ? 405 GLU B CD  1 
ATOM   2474 O OE1 . GLU B 2 253 ? -6.587  0.101   20.277 1.00 25.05 ? 405 GLU B OE1 1 
ATOM   2475 O OE2 . GLU B 2 253 ? -5.195  1.731   20.778 1.00 25.10 ? 405 GLU B OE2 1 
ATOM   2476 N N   . LEU B 2 254 ? -3.633  -5.335  20.698 1.00 18.55 ? 406 LEU B N   1 
ATOM   2477 C CA  . LEU B 2 254 ? -4.153  -6.709  20.578 1.00 17.33 ? 406 LEU B CA  1 
ATOM   2478 C C   . LEU B 2 254 ? -4.472  -7.330  21.937 1.00 17.83 ? 406 LEU B C   1 
ATOM   2479 O O   . LEU B 2 254 ? -3.663  -7.240  22.870 1.00 15.11 ? 406 LEU B O   1 
ATOM   2480 C CB  . LEU B 2 254 ? -3.161  -7.644  19.876 1.00 16.10 ? 406 LEU B CB  1 
ATOM   2481 C CG  . LEU B 2 254 ? -2.918  -7.348  18.399 1.00 17.36 ? 406 LEU B CG  1 
ATOM   2482 C CD1 . LEU B 2 254 ? -1.817  -8.273  17.832 1.00 14.43 ? 406 LEU B CD1 1 
ATOM   2483 C CD2 . LEU B 2 254 ? -4.199  -7.320  17.572 1.00 17.09 ? 406 LEU B CD2 1 
ATOM   2484 N N   . THR B 2 255 ? -5.667  -7.911  22.059 1.00 16.66 ? 407 THR B N   1 
ATOM   2485 C CA  . THR B 2 255 ? -6.012  -8.786  23.186 1.00 19.37 ? 407 THR B CA  1 
ATOM   2486 C C   . THR B 2 255 ? -5.304  -10.152 22.994 1.00 16.83 ? 407 THR B C   1 
ATOM   2487 O O   . THR B 2 255 ? -4.799  -10.458 21.914 1.00 16.25 ? 407 THR B O   1 
ATOM   2488 C CB  . THR B 2 255 ? -7.527  -9.031  23.266 1.00 19.00 ? 407 THR B CB  1 
ATOM   2489 O OG1 . THR B 2 255 ? -7.953  -9.809  22.149 1.00 20.26 ? 407 THR B OG1 1 
ATOM   2490 C CG2 . THR B 2 255 ? -8.294  -7.721  23.321 1.00 20.65 ? 407 THR B CG2 1 
ATOM   2491 N N   . LEU B 2 256 ? -5.196  -10.941 24.058 1.00 15.53 ? 408 LEU B N   1 
ATOM   2492 C CA  . LEU B 2 256 ? -4.656  -12.288 23.930 1.00 16.21 ? 408 LEU B CA  1 
ATOM   2493 C C   . LEU B 2 256 ? -5.356  -13.107 22.829 1.00 17.05 ? 408 LEU B C   1 
ATOM   2494 O O   . LEU B 2 256 ? -4.696  -13.843 22.095 1.00 16.21 ? 408 LEU B O   1 
ATOM   2495 C CB  . LEU B 2 256 ? -4.751  -13.024 25.270 1.00 18.43 ? 408 LEU B CB  1 
ATOM   2496 C CG  . LEU B 2 256 ? -4.216  -14.443 25.159 1.00 22.58 ? 408 LEU B CG  1 
ATOM   2497 C CD1 . LEU B 2 256 ? -2.726  -14.387 24.763 1.00 22.72 ? 408 LEU B CD1 1 
ATOM   2498 C CD2 . LEU B 2 256 ? -4.475  -15.206 26.426 1.00 21.90 ? 408 LEU B CD2 1 
ATOM   2499 N N   . ALA B 2 257 ? -6.685  -12.980 22.696 1.00 16.99 ? 409 ALA B N   1 
ATOM   2500 C CA  . ALA B 2 257 ? -7.406  -13.805 21.718 1.00 15.53 ? 409 ALA B CA  1 
ATOM   2501 C C   . ALA B 2 257 ? -7.091  -13.354 20.289 1.00 17.99 ? 409 ALA B C   1 
ATOM   2502 O O   . ALA B 2 257 ? -6.977  -14.177 19.376 1.00 16.53 ? 409 ALA B O   1 
ATOM   2503 C CB  . ALA B 2 257 ? -8.908  -13.815 21.985 1.00 19.45 ? 409 ALA B CB  1 
ATOM   2504 N N   . GLU B 2 258 ? -6.929  -12.043 20.115 1.00 15.13 ? 410 GLU B N   1 
ATOM   2505 C CA  . GLU B 2 258 ? -6.544  -11.492 18.819 1.00 17.08 ? 410 GLU B CA  1 
ATOM   2506 C C   . GLU B 2 258 ? -5.124  -11.887 18.444 1.00 16.23 ? 410 GLU B C   1 
ATOM   2507 O O   . GLU B 2 258 ? -4.826  -12.154 17.274 1.00 14.50 ? 410 GLU B O   1 
ATOM   2508 C CB  . GLU B 2 258 ? -6.701  -9.967  18.830 1.00 14.59 ? 410 GLU B CB  1 
ATOM   2509 C CG  . GLU B 2 258 ? -8.157  -9.512  18.829 1.00 18.78 ? 410 GLU B CG  1 
ATOM   2510 C CD  . GLU B 2 258 ? -8.301  -8.019  19.075 1.00 21.74 ? 410 GLU B CD  1 
ATOM   2511 O OE1 . GLU B 2 258 ? -7.353  -7.375  19.598 1.00 16.92 ? 410 GLU B OE1 1 
ATOM   2512 O OE2 . GLU B 2 258 ? -9.336  -7.468  18.665 1.00 25.76 ? 410 GLU B OE2 1 
ATOM   2513 N N   . LEU B 2 259 ? -4.245  -11.937 19.436 1.00 14.65 ? 411 LEU B N   1 
ATOM   2514 C CA  . LEU B 2 259 ? -2.860  -12.323 19.183 1.00 13.75 ? 411 LEU B CA  1 
ATOM   2515 C C   . LEU B 2 259 ? -2.791  -13.824 18.849 1.00 14.82 ? 411 LEU B C   1 
ATOM   2516 O O   . LEU B 2 259 ? -2.117  -14.258 17.911 1.00 13.03 ? 411 LEU B O   1 
ATOM   2517 C CB  . LEU B 2 259 ? -2.001  -12.013 20.399 1.00 13.73 ? 411 LEU B CB  1 
ATOM   2518 C CG  . LEU B 2 259 ? -0.548  -12.476 20.357 1.00 17.49 ? 411 LEU B CG  1 
ATOM   2519 C CD1 . LEU B 2 259 ? 0.216   -11.727 19.284 1.00 15.37 ? 411 LEU B CD1 1 
ATOM   2520 C CD2 . LEU B 2 259 ? 0.093   -12.311 21.740 1.00 18.15 ? 411 LEU B CD2 1 
ATOM   2521 N N   . ARG B 2 260 ? -3.539  -14.635 19.584 1.00 16.22 ? 412 ARG B N   1 
ATOM   2522 C CA  . ARG B 2 260 ? -3.526  -16.064 19.291 1.00 13.98 ? 412 ARG B CA  1 
ATOM   2523 C C   . ARG B 2 260 ? -4.082  -16.334 17.898 1.00 13.73 ? 412 ARG B C   1 
ATOM   2524 O O   . ARG B 2 260 ? -3.542  -17.185 17.166 1.00 14.02 ? 412 ARG B O   1 
ATOM   2525 C CB  . ARG B 2 260 ? -4.340  -16.831 20.346 1.00 15.98 ? 412 ARG B CB  1 
ATOM   2526 C CG  . ARG B 2 260 ? -4.256  -18.331 20.143 1.00 15.89 ? 412 ARG B CG  1 
ATOM   2527 C CD  . ARG B 2 260 ? -5.209  -19.075 21.054 1.00 21.79 ? 412 ARG B CD  1 
ATOM   2528 N NE  . ARG B 2 260 ? -4.802  -18.923 22.447 1.00 22.19 ? 412 ARG B NE  1 
ATOM   2529 C CZ  . ARG B 2 260 ? -5.447  -18.252 23.378 1.00 24.69 ? 412 ARG B CZ  1 
ATOM   2530 N NH1 . ARG B 2 260 ? -6.576  -17.593 23.090 1.00 32.12 ? 412 ARG B NH1 1 
ATOM   2531 N NH2 . ARG B 2 260 ? -4.951  -18.240 24.605 1.00 26.47 ? 412 ARG B NH2 1 
ATOM   2532 N N   . GLN B 2 261 ? -5.143  -15.624 17.513 1.00 12.53 ? 413 GLN B N   1 
ATOM   2533 C CA  . GLN B 2 261 ? -5.733  -15.857 16.204 1.00 11.48 ? 413 GLN B CA  1 
ATOM   2534 C C   . GLN B 2 261 ? -4.772  -15.456 15.071 1.00 11.84 ? 413 GLN B C   1 
ATOM   2535 O O   . GLN B 2 261 ? -4.747  -16.073 14.014 1.00 13.97 ? 413 GLN B O   1 
ATOM   2536 C CB  . GLN B 2 261 ? -7.054  -15.080 16.065 1.00 12.69 ? 413 GLN B CB  1 
ATOM   2537 C CG  . GLN B 2 261 ? -8.190  -15.627 16.964 1.00 13.99 ? 413 GLN B CG  1 
ATOM   2538 C CD  . GLN B 2 261 ? -9.165  -16.513 16.229 1.00 13.91 ? 413 GLN B CD  1 
ATOM   2539 O OE1 . GLN B 2 261 ? -8.899  -16.940 15.105 1.00 12.12 ? 413 GLN B OE1 1 
ATOM   2540 N NE2 . GLN B 2 261 ? -10.326 -16.768 16.840 1.00 13.65 ? 413 GLN B NE2 1 
ATOM   2541 N N   . ARG B 2 262 ? -4.003  -14.395 15.284 1.00 10.95 ? 414 ARG B N   1 
ATOM   2542 C CA  . ARG B 2 262 ? -2.982  -14.002 14.308 1.00 14.21 ? 414 ARG B CA  1 
ATOM   2543 C C   . ARG B 2 262 ? -1.840  -14.996 14.204 1.00 12.77 ? 414 ARG B C   1 
ATOM   2544 O O   . ARG B 2 262 ? -1.397  -15.306 13.102 1.00 15.14 ? 414 ARG B O   1 
ATOM   2545 C CB  . ARG B 2 262 ? -2.456  -12.615 14.643 1.00 12.59 ? 414 ARG B CB  1 
ATOM   2546 C CG  . ARG B 2 262 ? -3.429  -11.526 14.140 1.00 14.25 ? 414 ARG B CG  1 
ATOM   2547 C CD  . ARG B 2 262 ? -3.245  -10.262 14.922 1.00 17.23 ? 414 ARG B CD  1 
ATOM   2548 N NE  . ARG B 2 262 ? -4.042  -9.157  14.389 1.00 19.91 ? 414 ARG B NE  1 
ATOM   2549 C CZ  . ARG B 2 262 ? -5.349  -9.003  14.579 1.00 22.13 ? 414 ARG B CZ  1 
ATOM   2550 N NH1 . ARG B 2 262 ? -5.968  -7.945  14.059 1.00 24.25 ? 414 ARG B NH1 1 
ATOM   2551 N NH2 . ARG B 2 262 ? -6.051  -9.916  15.257 1.00 20.53 ? 414 ARG B NH2 1 
ATOM   2552 N N   . LEU B 2 263 ? -1.356  -15.483 15.345 1.00 14.51 ? 415 LEU B N   1 
ATOM   2553 C CA  . LEU B 2 263 ? -0.303  -16.496 15.331 1.00 14.61 ? 415 LEU B CA  1 
ATOM   2554 C C   . LEU B 2 263 ? -0.738  -17.741 14.547 1.00 14.77 ? 415 LEU B C   1 
ATOM   2555 O O   . LEU B 2 263 ? 0.042   -18.300 13.767 1.00 13.15 ? 415 LEU B O   1 
ATOM   2556 C CB  . LEU B 2 263 ? 0.070   -16.908 16.757 1.00 16.25 ? 415 LEU B CB  1 
ATOM   2557 C CG  . LEU B 2 263 ? 0.882   -15.873 17.510 1.00 16.37 ? 415 LEU B CG  1 
ATOM   2558 C CD1 . LEU B 2 263 ? 0.858   -16.234 18.995 1.00 17.36 ? 415 LEU B CD1 1 
ATOM   2559 C CD2 . LEU B 2 263 ? 2.309   -15.892 16.971 1.00 18.46 ? 415 LEU B CD2 1 
ATOM   2560 N N   . ILE B 2 264 ? -2.000  -18.143 14.715 1.00 14.70 ? 416 ILE B N   1 
ATOM   2561 C CA  . ILE B 2 264 ? -2.518  -19.328 14.013 1.00 13.21 ? 416 ILE B CA  1 
ATOM   2562 C C   . ILE B 2 264 ? -2.630  -18.990 12.540 1.00 15.74 ? 416 ILE B C   1 
ATOM   2563 O O   . ILE B 2 264 ? -2.217  -19.765 11.676 1.00 13.79 ? 416 ILE B O   1 
ATOM   2564 C CB  . ILE B 2 264 ? -3.920  -19.747 14.560 1.00 14.78 ? 416 ILE B CB  1 
ATOM   2565 C CG1 . ILE B 2 264 ? -3.799  -20.296 15.994 1.00 13.15 ? 416 ILE B CG1 1 
ATOM   2566 C CG2 . ILE B 2 264 ? -4.591  -20.727 13.606 1.00 14.38 ? 416 ILE B CG2 1 
ATOM   2567 C CD1 . ILE B 2 264 ? -5.153  -20.430 16.764 1.00 16.77 ? 416 ILE B CD1 1 
ATOM   2568 N N   . HIS B 2 265 ? -3.191  -17.816 12.260 1.00 13.38 ? 417 HIS B N   1 
ATOM   2569 C CA  . HIS B 2 265 ? -3.507  -17.436 10.892 1.00 16.58 ? 417 HIS B CA  1 
ATOM   2570 C C   . HIS B 2 265 ? -2.223  -17.295 10.060 1.00 16.25 ? 417 HIS B C   1 
ATOM   2571 O O   . HIS B 2 265 ? -2.189  -17.678 8.886  1.00 15.85 ? 417 HIS B O   1 
ATOM   2572 C CB  . HIS B 2 265 ? -4.341  -16.146 10.845 1.00 18.08 ? 417 HIS B CB  1 
ATOM   2573 C CG  . HIS B 2 265 ? -4.613  -15.664 9.456  1.00 24.45 ? 417 HIS B CG  1 
ATOM   2574 N ND1 . HIS B 2 265 ? -4.022  -14.544 8.909  1.00 29.40 ? 417 HIS B ND1 1 
ATOM   2575 C CD2 . HIS B 2 265 ? -5.430  -16.163 8.495  1.00 26.51 ? 417 HIS B CD2 1 
ATOM   2576 C CE1 . HIS B 2 265 ? -4.464  -14.372 7.675  1.00 24.77 ? 417 HIS B CE1 1 
ATOM   2577 N NE2 . HIS B 2 265 ? -5.314  -15.344 7.397  1.00 26.76 ? 417 HIS B NE2 1 
ATOM   2578 N N   . PHE B 2 266 ? -1.181  -16.688 10.642 1.00 14.36 ? 418 PHE B N   1 
ATOM   2579 C CA  . PHE B 2 266 ? 0.087   -16.507 9.924  1.00 17.23 ? 418 PHE B CA  1 
ATOM   2580 C C   . PHE B 2 266 ? 1.053   -17.714 9.944  1.00 17.19 ? 418 PHE B C   1 
ATOM   2581 O O   . PHE B 2 266 ? 2.135   -17.673 9.364  1.00 16.69 ? 418 PHE B O   1 
ATOM   2582 C CB  . PHE B 2 266 ? 0.779   -15.238 10.423 1.00 20.40 ? 418 PHE B CB  1 
ATOM   2583 C CG  . PHE B 2 266 ? -0.004  -13.990 10.137 1.00 20.91 ? 418 PHE B CG  1 
ATOM   2584 C CD1 . PHE B 2 266 ? -0.380  -13.682 8.847  1.00 23.53 ? 418 PHE B CD1 1 
ATOM   2585 C CD2 . PHE B 2 266 ? -0.357  -13.128 11.158 1.00 21.66 ? 418 PHE B CD2 1 
ATOM   2586 C CE1 . PHE B 2 266 ? -1.101  -12.523 8.576  1.00 33.56 ? 418 PHE B CE1 1 
ATOM   2587 C CE2 . PHE B 2 266 ? -1.071  -11.978 10.894 1.00 27.50 ? 418 PHE B CE2 1 
ATOM   2588 C CZ  . PHE B 2 266 ? -1.447  -11.675 9.606  1.00 34.41 ? 418 PHE B CZ  1 
ATOM   2589 N N   . SER B 2 267 ? 0.632   -18.798 10.563 1.00 14.20 ? 419 SER B N   1 
ATOM   2590 C CA  . SER B 2 267 ? 1.449   -19.999 10.592 1.00 14.73 ? 419 SER B CA  1 
ATOM   2591 C C   . SER B 2 267 ? 1.414   -20.681 9.236  1.00 14.24 ? 419 SER B C   1 
ATOM   2592 O O   . SER B 2 267 ? 0.398   -20.606 8.543  1.00 15.10 ? 419 SER B O   1 
ATOM   2593 C CB  . SER B 2 267 ? 0.930   -20.991 11.649 1.00 14.23 ? 419 SER B CB  1 
ATOM   2594 O OG  . SER B 2 267 ? 1.319   -20.644 12.956 1.00 14.20 ? 419 SER B OG  1 
ATOM   2595 N N   . ALA B 2 268 ? 2.467   -21.434 8.916  1.00 13.13 ? 420 ALA B N   1 
ATOM   2596 C CA  . ALA B 2 268 ? 2.479   -22.398 7.813  1.00 13.32 ? 420 ALA B CA  1 
ATOM   2597 C C   . ALA B 2 268 ? 1.580   -23.570 8.192  1.00 17.38 ? 420 ALA B C   1 
ATOM   2598 O O   . ALA B 2 268 ? 1.631   -24.055 9.329  1.00 17.43 ? 420 ALA B O   1 
ATOM   2599 C CB  . ALA B 2 268 ? 3.909   -22.892 7.534  1.00 13.65 ? 420 ALA B CB  1 
ATOM   2600 N N   . LYS B 2 269 ? 0.712   -24.007 7.281  1.00 16.86 ? 421 LYS B N   1 
ATOM   2601 C CA  . LYS B 2 269 ? -0.296  -25.007 7.627  1.00 19.27 ? 421 LYS B CA  1 
ATOM   2602 C C   . LYS B 2 269 ? -0.040  -26.334 6.910  1.00 16.95 ? 421 LYS B C   1 
ATOM   2603 O O   . LYS B 2 269 ? 0.461   -26.353 5.799  1.00 17.50 ? 421 LYS B O   1 
ATOM   2604 C CB  . LYS B 2 269 ? -1.684  -24.457 7.284  1.00 23.18 ? 421 LYS B CB  1 
ATOM   2605 C CG  . LYS B 2 269 ? -1.867  -23.099 7.987  1.00 22.91 ? 421 LYS B CG  1 
ATOM   2606 C CD  . LYS B 2 269 ? -3.267  -22.696 8.302  1.00 27.63 ? 421 LYS B CD  1 
ATOM   2607 C CE  . LYS B 2 269 ? -3.257  -21.329 8.996  1.00 20.56 ? 421 LYS B CE  1 
ATOM   2608 N NZ  . LYS B 2 269 ? -2.441  -20.297 8.249  1.00 21.70 ? 421 LYS B NZ  1 
ATOM   2609 N N   . ASP B 2 270 ? -0.348  -27.432 7.588  1.00 18.21 ? 422 ASP B N   1 
ATOM   2610 C CA  . ASP B 2 270 ? -0.320  -28.772 6.995  1.00 22.32 ? 422 ASP B CA  1 
ATOM   2611 C C   . ASP B 2 270 ? 1.055   -29.145 6.464  1.00 25.57 ? 422 ASP B C   1 
ATOM   2612 O O   . ASP B 2 270 ? 1.184   -29.879 5.486  1.00 26.78 ? 422 ASP B O   1 
ATOM   2613 C CB  . ASP B 2 270 ? -1.374  -28.917 5.900  1.00 22.04 ? 422 ASP B CB  1 
ATOM   2614 C CG  . ASP B 2 270 ? -1.613  -30.375 5.501  1.00 36.13 ? 422 ASP B CG  1 
ATOM   2615 O OD1 . ASP B 2 270 ? -1.944  -31.198 6.381  1.00 39.04 ? 422 ASP B OD1 1 
ATOM   2616 O OD2 . ASP B 2 270 ? -1.451  -30.704 4.298  1.00 42.63 ? 422 ASP B OD2 1 
ATOM   2617 N N   . VAL B 2 271 ? 2.088   -28.725 7.172  1.00 20.24 ? 423 VAL B N   1 
ATOM   2618 C CA  . VAL B 2 271 ? 3.428   -29.012 6.713  1.00 22.35 ? 423 VAL B CA  1 
ATOM   2619 C C   . VAL B 2 271 ? 4.026   -30.119 7.615  1.00 22.37 ? 423 VAL B C   1 
ATOM   2620 O O   . VAL B 2 271 ? 5.002   -30.781 7.260  1.00 19.67 ? 423 VAL B O   1 
ATOM   2621 C CB  . VAL B 2 271 ? 4.267   -27.718 6.767  1.00 24.14 ? 423 VAL B CB  1 
ATOM   2622 C CG1 . VAL B 2 271 ? 5.628   -28.021 6.518  1.00 33.74 ? 423 VAL B CG1 1 
ATOM   2623 C CG2 . VAL B 2 271 ? 3.856   -26.789 5.646  1.00 24.80 ? 423 VAL B CG2 1 
ATOM   2624 N N   . ILE B 2 272 ? 3.407   -30.370 8.763  1.00 20.61 ? 424 ILE B N   1 
ATOM   2625 C CA  . ILE B 2 272 ? 3.873   -31.475 9.625  1.00 23.19 ? 424 ILE B CA  1 
ATOM   2626 C C   . ILE B 2 272 ? 3.266   -32.814 9.165  1.00 23.35 ? 424 ILE B C   1 
ATOM   2627 O O   . ILE B 2 272 ? 2.069   -32.901 8.905  1.00 26.44 ? 424 ILE B O   1 
ATOM   2628 C CB  . ILE B 2 272 ? 3.524   -31.175 11.109 1.00 23.19 ? 424 ILE B CB  1 
ATOM   2629 C CG1 . ILE B 2 272 ? 4.046   -29.779 11.478 1.00 21.59 ? 424 ILE B CG1 1 
ATOM   2630 C CG2 . ILE B 2 272 ? 4.162   -32.170 12.038 1.00 26.89 ? 424 ILE B CG2 1 
ATOM   2631 C CD1 . ILE B 2 272 ? 3.635   -29.275 12.863 1.00 19.23 ? 424 ILE B CD1 1 
ATOM   2632 N N   . ASN B 2 273 ? 4.091   -33.859 9.046  1.00 26.68 ? 425 ASN B N   1 
ATOM   2633 C CA  . ASN B 2 273 ? 3.584   -35.221 8.795  1.00 29.36 ? 425 ASN B CA  1 
ATOM   2634 C C   . ASN B 2 273 ? 3.024   -35.790 10.087 1.00 23.57 ? 425 ASN B C   1 
ATOM   2635 O O   . ASN B 2 273 ? 3.754   -36.044 11.034 1.00 24.60 ? 425 ASN B O   1 
ATOM   2636 C CB  . ASN B 2 273 ? 4.679   -36.159 8.284  1.00 31.42 ? 425 ASN B CB  1 
ATOM   2637 C CG  . ASN B 2 273 ? 4.154   -37.540 7.941  1.00 32.14 ? 425 ASN B CG  1 
ATOM   2638 O OD1 . ASN B 2 273 ? 2.999   -37.883 8.235  1.00 34.40 ? 425 ASN B OD1 1 
ATOM   2639 N ND2 . ASN B 2 273 ? 5.001   -38.347 7.311  1.00 33.55 ? 425 ASN B ND2 1 
ATOM   2640 N N   . GLU B 2 274 ? 1.729   -36.023 10.131 1.00 28.79 ? 426 GLU B N   1 
ATOM   2641 C CA  . GLU B 2 274 ? 1.123   -36.344 11.412 1.00 28.55 ? 426 GLU B CA  1 
ATOM   2642 C C   . GLU B 2 274 ? 1.352   -37.789 11.837 1.00 27.56 ? 426 GLU B C   1 
ATOM   2643 O O   . GLU B 2 274 ? 1.007   -38.161 12.955 1.00 26.88 ? 426 GLU B O   1 
ATOM   2644 C CB  . GLU B 2 274 ? -0.369  -36.064 11.335 1.00 28.85 ? 426 GLU B CB  1 
ATOM   2645 C CG  . GLU B 2 274 ? -0.636  -34.622 11.046 1.00 35.62 ? 426 GLU B CG  1 
ATOM   2646 C CD  . GLU B 2 274 ? -2.099  -34.313 10.955 1.00 40.62 ? 426 GLU B CD  1 
ATOM   2647 O OE1 . GLU B 2 274 ? -2.904  -35.273 10.783 1.00 45.16 ? 426 GLU B OE1 1 
ATOM   2648 O OE2 . GLU B 2 274 ? -2.426  -33.099 11.008 1.00 32.47 ? 426 GLU B OE2 1 
ATOM   2649 N N   . ALA B 2 275 ? 1.943   -38.591 10.947 1.00 28.92 ? 427 ALA B N   1 
ATOM   2650 C CA  . ALA B 2 275 ? 2.385   -39.959 11.267 1.00 29.04 ? 427 ALA B CA  1 
ATOM   2651 C C   . ALA B 2 275 ? 3.329   -40.049 12.470 1.00 29.68 ? 427 ALA B C   1 
ATOM   2652 O O   . ALA B 2 275 ? 3.412   -41.096 13.121 1.00 28.83 ? 427 ALA B O   1 
ATOM   2653 C CB  . ALA B 2 275 ? 3.082   -40.591 10.055 1.00 30.49 ? 427 ALA B CB  1 
ATOM   2654 N N   . TRP B 2 276 ? 4.072   -38.977 12.740 1.00 25.55 ? 428 TRP B N   1 
ATOM   2655 C CA  . TRP B 2 276 ? 4.987   -38.965 13.882 1.00 23.47 ? 428 TRP B CA  1 
ATOM   2656 C C   . TRP B 2 276 ? 4.279   -39.047 15.229 1.00 21.89 ? 428 TRP B C   1 
ATOM   2657 O O   . TRP B 2 276 ? 4.837   -39.548 16.219 1.00 26.04 ? 428 TRP B O   1 
ATOM   2658 C CB  . TRP B 2 276 ? 5.773   -37.663 13.831 1.00 24.19 ? 428 TRP B CB  1 
ATOM   2659 C CG  . TRP B 2 276 ? 6.708   -37.676 12.699 1.00 26.52 ? 428 TRP B CG  1 
ATOM   2660 C CD1 . TRP B 2 276 ? 6.504   -37.155 11.458 1.00 26.70 ? 428 TRP B CD1 1 
ATOM   2661 C CD2 . TRP B 2 276 ? 7.948   -38.389 12.638 1.00 31.77 ? 428 TRP B CD2 1 
ATOM   2662 N NE1 . TRP B 2 276 ? 7.578   -37.426 10.651 1.00 29.42 ? 428 TRP B NE1 1 
ATOM   2663 C CE2 . TRP B 2 276 ? 8.477   -38.189 11.349 1.00 31.32 ? 428 TRP B CE2 1 
ATOM   2664 C CE3 . TRP B 2 276 ? 8.677   -39.148 13.561 1.00 31.92 ? 428 TRP B CE3 1 
ATOM   2665 C CZ2 . TRP B 2 276 ? 9.698   -38.720 10.954 1.00 33.32 ? 428 TRP B CZ2 1 
ATOM   2666 C CZ3 . TRP B 2 276 ? 9.890   -39.674 13.172 1.00 35.93 ? 428 TRP B CZ3 1 
ATOM   2667 C CH2 . TRP B 2 276 ? 10.391  -39.458 11.876 1.00 37.20 ? 428 TRP B CH2 1 
ATOM   2668 N N   . PHE B 2 277 ? 3.061   -38.526 15.280 1.00 19.54 ? 429 PHE B N   1 
ATOM   2669 C CA  . PHE B 2 277 ? 2.337   -38.499 16.530 1.00 15.80 ? 429 PHE B CA  1 
ATOM   2670 C C   . PHE B 2 277 ? 1.586   -39.809 16.720 1.00 17.47 ? 429 PHE B C   1 
ATOM   2671 O O   . PHE B 2 277 ? 1.177   -40.443 15.739 1.00 14.76 ? 429 PHE B O   1 
ATOM   2672 C CB  . PHE B 2 277 ? 1.307   -37.379 16.523 1.00 18.70 ? 429 PHE B CB  1 
ATOM   2673 C CG  . PHE B 2 277 ? 1.892   -36.003 16.310 1.00 18.25 ? 429 PHE B CG  1 
ATOM   2674 C CD1 . PHE B 2 277 ? 2.899   -35.535 17.128 1.00 15.08 ? 429 PHE B CD1 1 
ATOM   2675 C CD2 . PHE B 2 277 ? 1.386   -35.167 15.335 1.00 19.22 ? 429 PHE B CD2 1 
ATOM   2676 C CE1 . PHE B 2 277 ? 3.409   -34.260 16.948 1.00 17.26 ? 429 PHE B CE1 1 
ATOM   2677 C CE2 . PHE B 2 277 ? 1.907   -33.891 15.145 1.00 16.40 ? 429 PHE B CE2 1 
ATOM   2678 C CZ  . PHE B 2 277 ? 2.903   -33.444 15.962 1.00 13.04 ? 429 PHE B CZ  1 
ATOM   2679 N N   . PRO B 2 278 ? 1.391   -40.203 17.985 1.00 12.52 ? 430 PRO B N   1 
ATOM   2680 C CA  . PRO B 2 278 ? 0.520   -41.342 18.270 1.00 16.03 ? 430 PRO B CA  1 
ATOM   2681 C C   . PRO B 2 278 ? -0.832  -41.127 17.607 1.00 16.38 ? 430 PRO B C   1 
ATOM   2682 O O   . PRO B 2 278 ? -1.283  -39.987 17.463 1.00 15.78 ? 430 PRO B O   1 
ATOM   2683 C CB  . PRO B 2 278 ? 0.436   -41.369 19.795 1.00 15.04 ? 430 PRO B CB  1 
ATOM   2684 C CG  . PRO B 2 278 ? 1.646   -40.610 20.250 1.00 15.93 ? 430 PRO B CG  1 
ATOM   2685 C CD  . PRO B 2 278 ? 1.939   -39.596 19.205 1.00 16.37 ? 430 PRO B CD  1 
ATOM   2686 N N   . GLU B 2 279 ? -1.476  -42.221 17.223 1.00 15.45 ? 431 GLU B N   1 
ATOM   2687 C CA  . GLU B 2 279 ? -2.658  -42.164 16.380 1.00 20.15 ? 431 GLU B CA  1 
ATOM   2688 C C   . GLU B 2 279 ? -3.775  -41.276 16.914 1.00 18.63 ? 431 GLU B C   1 
ATOM   2689 O O   . GLU B 2 279 ? -4.353  -40.488 16.159 1.00 20.16 ? 431 GLU B O   1 
ATOM   2690 C CB  . GLU B 2 279 ? -3.192  -43.593 16.166 1.00 21.85 ? 431 GLU B CB  1 
ATOM   2691 C CG  . GLU B 2 279 ? -2.260  -44.476 15.363 1.00 27.48 ? 431 GLU B CG  1 
ATOM   2692 C CD  . GLU B 2 279 ? -2.869  -45.823 15.042 1.00 31.31 ? 431 GLU B CD  1 
ATOM   2693 O OE1 . GLU B 2 279 ? -4.043  -46.057 15.416 1.00 34.93 ? 431 GLU B OE1 1 
ATOM   2694 O OE2 . GLU B 2 279 ? -2.148  -46.676 14.473 1.00 38.92 ? 431 GLU B OE2 1 
ATOM   2695 N N   . ASP B 2 280 ? -4.065  -41.381 18.213 1.00 19.40 ? 432 ASP B N   1 
ATOM   2696 C CA  . ASP B 2 280 ? -5.200  -40.643 18.786 1.00 24.50 ? 432 ASP B CA  1 
ATOM   2697 C C   . ASP B 2 280 ? -4.909  -39.142 18.955 1.00 23.25 ? 432 ASP B C   1 
ATOM   2698 O O   . ASP B 2 280 ? -5.814  -38.342 19.189 1.00 19.97 ? 432 ASP B O   1 
ATOM   2699 C CB  . ASP B 2 280 ? -5.623  -41.226 20.135 1.00 26.19 ? 432 ASP B CB  1 
ATOM   2700 C CG  . ASP B 2 280 ? -6.255  -42.597 20.012 1.00 31.99 ? 432 ASP B CG  1 
ATOM   2701 O OD1 . ASP B 2 280 ? -6.905  -42.892 18.985 1.00 30.45 ? 432 ASP B OD1 1 
ATOM   2702 O OD2 . ASP B 2 280 ? -6.160  -43.366 20.988 1.00 42.15 ? 432 ASP B OD2 1 
ATOM   2703 N N   . GLN B 2 281 ? -3.639  -38.770 18.850 1.00 17.34 ? 433 GLN B N   1 
ATOM   2704 C CA  . GLN B 2 281 ? -3.256  -37.378 19.081 1.00 17.44 ? 433 GLN B CA  1 
ATOM   2705 C C   . GLN B 2 281 ? -3.230  -36.569 17.795 1.00 17.48 ? 433 GLN B C   1 
ATOM   2706 O O   . GLN B 2 281 ? -3.151  -35.338 17.830 1.00 15.44 ? 433 GLN B O   1 
ATOM   2707 C CB  . GLN B 2 281 ? -1.915  -37.316 19.817 1.00 17.98 ? 433 GLN B CB  1 
ATOM   2708 C CG  . GLN B 2 281 ? -1.945  -38.013 21.168 1.00 16.50 ? 433 GLN B CG  1 
ATOM   2709 C CD  . GLN B 2 281 ? -2.530  -37.126 22.254 1.00 18.38 ? 433 GLN B CD  1 
ATOM   2710 O OE1 . GLN B 2 281 ? -2.870  -35.960 22.008 1.00 16.05 ? 433 GLN B OE1 1 
ATOM   2711 N NE2 . GLN B 2 281 ? -2.635  -37.658 23.460 1.00 20.33 ? 433 GLN B NE2 1 
ATOM   2712 N N   . ARG B 2 282 ? -3.307  -37.262 16.665 1.00 18.12 ? 434 ARG B N   1 
ATOM   2713 C CA  . ARG B 2 282 ? -3.256  -36.630 15.347 1.00 19.95 ? 434 ARG B CA  1 
ATOM   2714 C C   . ARG B 2 282 ? -4.390  -35.627 15.132 1.00 20.19 ? 434 ARG B C   1 
ATOM   2715 O O   . ARG B 2 282 ? -4.180  -34.526 14.641 1.00 22.13 ? 434 ARG B O   1 
ATOM   2716 C CB  . ARG B 2 282 ? -3.244  -37.700 14.253 1.00 21.73 ? 434 ARG B CB  1 
ATOM   2717 C CG  . ARG B 2 282 ? -1.910  -38.444 14.211 1.00 22.85 ? 434 ARG B CG  1 
ATOM   2718 C CD  . ARG B 2 282 ? -1.973  -39.690 13.347 1.00 20.65 ? 434 ARG B CD  1 
ATOM   2719 N NE  . ARG B 2 282 ? -0.796  -40.530 13.599 1.00 21.89 ? 434 ARG B NE  1 
ATOM   2720 C CZ  . ARG B 2 282 ? -0.645  -41.764 13.127 1.00 21.69 ? 434 ARG B CZ  1 
ATOM   2721 N NH1 . ARG B 2 282 ? -1.601  -42.300 12.381 1.00 18.86 ? 434 ARG B NH1 1 
ATOM   2722 N NH2 . ARG B 2 282 ? 0.441   -42.462 13.421 1.00 23.13 ? 434 ARG B NH2 1 
ATOM   2723 N N   . VAL B 2 283 ? -5.612  -36.059 15.376 1.00 19.11 ? 435 VAL B N   1 
ATOM   2724 C CA  . VAL B 2 283 ? -6.737  -35.148 15.274 1.00 19.40 ? 435 VAL B CA  1 
ATOM   2725 C C   . VAL B 2 283 ? -6.653  -33.965 16.281 1.00 19.33 ? 435 VAL B C   1 
ATOM   2726 O O   . VAL B 2 283 ? -7.134  -32.863 16.009 1.00 21.62 ? 435 VAL B O   1 
ATOM   2727 C CB  . VAL B 2 283 ? -8.054  -35.891 15.499 1.00 22.46 ? 435 VAL B CB  1 
ATOM   2728 C CG1 . VAL B 2 283 ? -9.155  -34.990 15.187 1.00 32.92 ? 435 VAL B CG1 1 
ATOM   2729 C CG2 . VAL B 2 283 ? -8.189  -37.019 14.502 1.00 28.93 ? 435 VAL B CG2 1 
ATOM   2730 N N   . LEU B 2 284 ? -6.041  -34.188 17.441 1.00 15.25 ? 436 LEU B N   1 
ATOM   2731 C CA  . LEU B 2 284 ? -5.984  -33.145 18.475 1.00 18.22 ? 436 LEU B CA  1 
ATOM   2732 C C   . LEU B 2 284 ? -4.859  -32.102 18.312 1.00 16.82 ? 436 LEU B C   1 
ATOM   2733 O O   . LEU B 2 284 ? -4.919  -31.018 18.902 1.00 14.47 ? 436 LEU B O   1 
ATOM   2734 C CB  . LEU B 2 284 ? -5.787  -33.857 19.831 1.00 15.96 ? 436 LEU B CB  1 
ATOM   2735 C CG  . LEU B 2 284 ? -6.904  -34.795 20.318 1.00 17.52 ? 436 LEU B CG  1 
ATOM   2736 C CD1 . LEU B 2 284 ? -6.592  -35.441 21.658 1.00 23.85 ? 436 LEU B CD1 1 
ATOM   2737 C CD2 . LEU B 2 284 ? -8.194  -34.097 20.429 1.00 18.77 ? 436 LEU B CD2 1 
ATOM   2738 N N   . THR B 2 285 ? -3.834  -32.436 17.537 1.00 14.49 ? 437 THR B N   1 
ATOM   2739 C CA  . THR B 2 285 ? -2.621  -31.629 17.490 1.00 14.72 ? 437 THR B CA  1 
ATOM   2740 C C   . THR B 2 285 ? -2.648  -30.634 16.328 1.00 13.80 ? 437 THR B C   1 
ATOM   2741 O O   . THR B 2 285 ? -2.752  -31.052 15.167 1.00 13.02 ? 437 THR B O   1 
ATOM   2742 C CB  . THR B 2 285 ? -1.385  -32.571 17.404 1.00 14.32 ? 437 THR B CB  1 
ATOM   2743 O OG1 . THR B 2 285 ? -1.367  -33.447 18.525 1.00 11.56 ? 437 THR B OG1 1 
ATOM   2744 C CG2 . THR B 2 285 ? -0.064  -31.767 17.281 1.00 13.04 ? 437 THR B CG2 1 
ATOM   2745 N N   . PRO B 2 286 ? -2.490  -29.328 16.592 1.00 13.93 ? 438 PRO B N   1 
ATOM   2746 C CA  . PRO B 2 286 ? -2.587  -28.400 15.460 1.00 14.55 ? 438 PRO B CA  1 
ATOM   2747 C C   . PRO B 2 286 ? -1.395  -28.548 14.506 1.00 14.28 ? 438 PRO B C   1 
ATOM   2748 O O   . PRO B 2 286 ? -0.247  -28.695 14.930 1.00 12.49 ? 438 PRO B O   1 
ATOM   2749 C CB  . PRO B 2 286 ? -2.536  -27.001 16.124 1.00 12.93 ? 438 PRO B CB  1 
ATOM   2750 C CG  . PRO B 2 286 ? -2.756  -27.260 17.567 1.00 20.13 ? 438 PRO B CG  1 
ATOM   2751 C CD  . PRO B 2 286 ? -2.213  -28.633 17.853 1.00 13.38 ? 438 PRO B CD  1 
ATOM   2752 N N   . ASN B 2 287 ? -1.674  -28.570 13.209 1.00 13.34 ? 439 ASN B N   1 
ATOM   2753 C CA  . ASN B 2 287 ? -0.618  -28.716 12.216 1.00 13.82 ? 439 ASN B CA  1 
ATOM   2754 C C   . ASN B 2 287 ? -0.271  -27.310 11.713 1.00 14.62 ? 439 ASN B C   1 
ATOM   2755 O O   . ASN B 2 287 ? -0.748  -26.856 10.669 1.00 14.57 ? 439 ASN B O   1 
ATOM   2756 C CB  . ASN B 2 287 ? -1.105  -29.613 11.076 1.00 16.93 ? 439 ASN B CB  1 
ATOM   2757 C CG  . ASN B 2 287 ? 0.032   -30.165 10.250 1.00 21.28 ? 439 ASN B CG  1 
ATOM   2758 O OD1 . ASN B 2 287 ? 0.975   -29.437 9.924  1.00 17.72 ? 439 ASN B OD1 1 
ATOM   2759 N ND2 . ASN B 2 287 ? -0.016  -31.457 9.941  1.00 17.99 ? 439 ASN B ND2 1 
ATOM   2760 N N   . LEU B 2 288 ? 0.546   -26.626 12.520 1.00 11.93 ? 440 LEU B N   1 
ATOM   2761 C CA  . LEU B 2 288 ? 0.918   -25.211 12.349 1.00 12.86 ? 440 LEU B CA  1 
ATOM   2762 C C   . LEU B 2 288 ? 2.378   -24.995 12.731 1.00 12.29 ? 440 LEU B C   1 
ATOM   2763 O O   . LEU B 2 288 ? 2.813   -25.452 13.784 1.00 10.49 ? 440 LEU B O   1 
ATOM   2764 C CB  . LEU B 2 288 ? 0.094   -24.348 13.308 1.00 14.47 ? 440 LEU B CB  1 
ATOM   2765 C CG  . LEU B 2 288 ? -1.437  -24.369 13.198 1.00 13.10 ? 440 LEU B CG  1 
ATOM   2766 C CD1 . LEU B 2 288 ? -2.063  -23.632 14.373 1.00 14.79 ? 440 LEU B CD1 1 
ATOM   2767 C CD2 . LEU B 2 288 ? -1.859  -23.736 11.902 1.00 16.68 ? 440 LEU B CD2 1 
ATOM   2768 N N   . VAL B 2 289 ? 3.124   -24.268 11.903 1.00 12.81 ? 441 VAL B N   1 
ATOM   2769 C CA  . VAL B 2 289 ? 4.507   -23.887 12.234 1.00 11.66 ? 441 VAL B CA  1 
ATOM   2770 C C   . VAL B 2 289 ? 4.530   -22.369 12.168 1.00 13.83 ? 441 VAL B C   1 
ATOM   2771 O O   . VAL B 2 289 ? 4.187   -21.800 11.138 1.00 13.86 ? 441 VAL B O   1 
ATOM   2772 C CB  . VAL B 2 289 ? 5.564   -24.514 11.320 1.00 8.84  ? 441 VAL B CB  1 
ATOM   2773 C CG1 . VAL B 2 289 ? 7.004   -24.076 11.743 1.00 10.87 ? 441 VAL B CG1 1 
ATOM   2774 C CG2 . VAL B 2 289 ? 5.454   -26.053 11.382 1.00 11.58 ? 441 VAL B CG2 1 
ATOM   2775 N N   . ALA B 2 290 ? 4.895   -21.738 13.286 1.00 13.28 ? 442 ALA B N   1 
ATOM   2776 C CA  . ALA B 2 290 ? 4.839   -20.294 13.471 1.00 14.84 ? 442 ALA B CA  1 
ATOM   2777 C C   . ALA B 2 290 ? 5.587   -19.547 12.386 1.00 17.53 ? 442 ALA B C   1 
ATOM   2778 O O   . ALA B 2 290 ? 6.583   -20.034 11.849 1.00 9.59  ? 442 ALA B O   1 
ATOM   2779 C CB  . ALA B 2 290 ? 5.429   -19.938 14.833 1.00 11.52 ? 442 ALA B CB  1 
ATOM   2780 N N   . ALA B 2 291 ? 5.086   -18.356 12.053 1.00 13.37 ? 443 ALA B N   1 
ATOM   2781 C CA  . ALA B 2 291 ? 5.793   -17.486 11.142 1.00 13.30 ? 443 ALA B CA  1 
ATOM   2782 C C   . ALA B 2 291 ? 5.449   -16.039 11.467 1.00 16.31 ? 443 ALA B C   1 
ATOM   2783 O O   . ALA B 2 291 ? 4.390   -15.742 12.029 1.00 17.46 ? 443 ALA B O   1 
ATOM   2784 C CB  . ALA B 2 291 ? 5.389   -17.799 9.721  1.00 12.40 ? 443 ALA B CB  1 
ATOM   2785 N N   . LEU B 2 292 ? 6.348   -15.141 11.114 1.00 17.58 ? 444 LEU B N   1 
ATOM   2786 C CA  . LEU B 2 292 ? 6.084   -13.700 11.161 1.00 19.68 ? 444 LEU B CA  1 
ATOM   2787 C C   . LEU B 2 292 ? 4.985   -13.264 10.195 1.00 17.28 ? 444 LEU B C   1 
ATOM   2788 O O   . LEU B 2 292 ? 4.796   -13.878 9.160  1.00 16.34 ? 444 LEU B O   1 
ATOM   2789 C CB  . LEU B 2 292 ? 7.365   -12.947 10.819 1.00 17.44 ? 444 LEU B CB  1 
ATOM   2790 C CG  . LEU B 2 292 ? 8.428   -12.916 11.921 1.00 21.37 ? 444 LEU B CG  1 
ATOM   2791 C CD1 . LEU B 2 292 ? 9.784   -12.609 11.311 1.00 21.99 ? 444 LEU B CD1 1 
ATOM   2792 C CD2 . LEU B 2 292 ? 8.093   -11.967 13.038 1.00 20.36 ? 444 LEU B CD2 1 
ATOM   2793 N N   . PRO B 2 293 ? 4.223   -12.219 10.548 1.00 21.44 ? 445 PRO B N   1 
ATOM   2794 C CA  . PRO B 2 293 ? 3.196   -11.721 9.621  1.00 27.29 ? 445 PRO B CA  1 
ATOM   2795 C C   . PRO B 2 293 ? 3.892   -11.140 8.377  1.00 24.20 ? 445 PRO B C   1 
ATOM   2796 O O   . PRO B 2 293 ? 4.935   -10.539 8.529  1.00 24.14 ? 445 PRO B O   1 
ATOM   2797 C CB  . PRO B 2 293 ? 2.446   -10.665 10.429 1.00 24.02 ? 445 PRO B CB  1 
ATOM   2798 C CG  . PRO B 2 293 ? 3.407   -10.248 11.476 1.00 28.82 ? 445 PRO B CG  1 
ATOM   2799 C CD  . PRO B 2 293 ? 4.298   -11.419 11.777 1.00 20.38 ? 445 PRO B CD  1 
ATOM   2800 N N   . PRO B 2 294 ? 3.291   -11.275 7.190  1.00 26.18 ? 446 PRO B N   1 
ATOM   2801 C CA  . PRO B 2 294 ? 3.719   -10.741 5.890  1.00 32.65 ? 446 PRO B CA  1 
ATOM   2802 C C   . PRO B 2 294 ? 3.597   -9.230  5.854  1.00 39.66 ? 446 PRO B C   1 
ATOM   2803 O O   . PRO B 2 294 ? 2.928   -8.653  6.707  1.00 36.23 ? 446 PRO B O   1 
ATOM   2804 C CB  . PRO B 2 294 ? 2.748   -11.375 4.895  1.00 34.35 ? 446 PRO B CB  1 
ATOM   2805 C CG  . PRO B 2 294 ? 1.583   -11.751 5.693  1.00 31.84 ? 446 PRO B CG  1 
ATOM   2806 C CD  . PRO B 2 294 ? 2.027   -12.018 7.082  1.00 28.70 ? 446 PRO B CD  1 
ATOM   2807 N N   . SER B 2 295 ? 4.280   -8.592  4.911  1.00 44.42 ? 447 SER B N   1 
ATOM   2808 C CA  . SER B 2 295 ? 4.055   -7.170  4.682  1.00 51.06 ? 447 SER B CA  1 
ATOM   2809 C C   . SER B 2 295 ? 2.619   -6.863  4.241  1.00 52.34 ? 447 SER B C   1 
ATOM   2810 O O   . SER B 2 295 ? 2.165   -5.735  4.445  1.00 60.33 ? 447 SER B O   1 
ATOM   2811 C CB  . SER B 2 295 ? 5.028   -6.658  3.604  1.00 48.97 ? 447 SER B CB  1 
ATOM   2812 O OG  . SER B 2 295 ? 6.383   -6.901  3.949  1.00 51.39 ? 447 SER B OG  1 
ATOM   2813 N N   . THR B 2 296 ? 1.890   -7.820  3.656  1.00 52.70 ? 448 THR B N   1 
ATOM   2814 C CA  . THR B 2 296 ? 0.476   -7.536  3.320  1.00 59.76 ? 448 THR B CA  1 
ATOM   2815 C C   . THR B 2 296 ? -0.476  -7.134  4.485  1.00 63.02 ? 448 THR B C   1 
ATOM   2816 O O   . THR B 2 296 ? -1.463  -6.439  4.227  1.00 70.35 ? 448 THR B O   1 
ATOM   2817 C CB  . THR B 2 296 ? -0.168  -8.692  2.478  1.00 59.20 ? 448 THR B CB  1 
ATOM   2818 O OG1 . THR B 2 296 ? -1.569  -8.441  2.303  1.00 63.02 ? 448 THR B OG1 1 
ATOM   2819 C CG2 . THR B 2 296 ? 0.008   -10.036 3.141  1.00 54.56 ? 448 THR B CG2 1 
ATOM   2820 N N   . HIS B 2 297 ? -0.189  -7.524  5.733  1.00 59.95 ? 449 HIS B N   1 
ATOM   2821 C CA  . HIS B 2 297 ? -0.858  -6.923  6.909  1.00 64.00 ? 449 HIS B CA  1 
ATOM   2822 C C   . HIS B 2 297 ? -0.163  -7.367  8.201  1.00 62.42 ? 449 HIS B C   1 
ATOM   2823 O O   . HIS B 2 297 ? -0.801  -7.901  9.118  1.00 55.30 ? 449 HIS B O   1 
ATOM   2824 C CB  . HIS B 2 297 ? -2.385  -7.184  6.999  1.00 67.46 ? 449 HIS B CB  1 
ATOM   2825 C CG  . HIS B 2 297 ? -2.806  -8.619  6.884  1.00 62.56 ? 449 HIS B CG  1 
ATOM   2826 N ND1 . HIS B 2 297 ? -2.264  -9.509  5.979  1.00 63.21 ? 449 HIS B ND1 1 
ATOM   2827 C CD2 . HIS B 2 297 ? -3.739  -9.313  7.580  1.00 57.57 ? 449 HIS B CD2 1 
ATOM   2828 C CE1 . HIS B 2 297 ? -2.843  -10.690 6.128  1.00 58.00 ? 449 HIS B CE1 1 
ATOM   2829 N NE2 . HIS B 2 297 ? -3.742  -10.598 7.093  1.00 54.14 ? 449 HIS B NE2 1 
ATOM   2830 N N   . GLY B 2 300 ? -7.711  -3.240  7.207  1.00 54.24 ? 452 GLY B N   1 
ATOM   2831 C CA  . GLY B 2 300 ? -8.525  -4.084  6.349  1.00 52.90 ? 452 GLY B CA  1 
ATOM   2832 C C   . GLY B 2 300 ? -9.018  -5.316  7.089  1.00 54.60 ? 452 GLY B C   1 
ATOM   2833 O O   . GLY B 2 300 ? -8.281  -6.302  7.243  1.00 47.26 ? 452 GLY B O   1 
ATOM   2834 N N   . TRP B 2 301 ? -10.268 -5.269  7.550  1.00 47.44 ? 453 TRP B N   1 
ATOM   2835 C CA  . TRP B 2 301 ? -10.758 -6.303  8.452  1.00 44.90 ? 453 TRP B CA  1 
ATOM   2836 C C   . TRP B 2 301 ? -11.006 -7.641  7.758  1.00 45.44 ? 453 TRP B C   1 
ATOM   2837 O O   . TRP B 2 301 ? -11.474 -7.697  6.621  1.00 47.62 ? 453 TRP B O   1 
ATOM   2838 C CB  . TRP B 2 301 ? -12.026 -5.824  9.176  1.00 48.13 ? 453 TRP B CB  1 
ATOM   2839 C CG  . TRP B 2 301 ? -12.503 -6.782  10.243 1.00 48.95 ? 453 TRP B CG  1 
ATOM   2840 C CD1 . TRP B 2 301 ? -12.091 -6.843  11.550 1.00 44.97 ? 453 TRP B CD1 1 
ATOM   2841 C CD2 . TRP B 2 301 ? -13.518 -7.784  10.099 1.00 43.83 ? 453 TRP B CD2 1 
ATOM   2842 N NE1 . TRP B 2 301 ? -12.765 -7.843  12.212 1.00 46.36 ? 453 TRP B NE1 1 
ATOM   2843 C CE2 . TRP B 2 301 ? -13.650 -8.431  11.346 1.00 42.75 ? 453 TRP B CE2 1 
ATOM   2844 C CE3 . TRP B 2 301 ? -14.318 -8.201  9.035  1.00 45.22 ? 453 TRP B CE3 1 
ATOM   2845 C CZ2 . TRP B 2 301 ? -14.552 -9.475  11.553 1.00 37.66 ? 453 TRP B CZ2 1 
ATOM   2846 C CZ3 . TRP B 2 301 ? -15.213 -9.241  9.238  1.00 44.71 ? 453 TRP B CZ3 1 
ATOM   2847 C CH2 . TRP B 2 301 ? -15.319 -9.867  10.488 1.00 37.21 ? 453 TRP B CH2 1 
ATOM   2848 N N   . GLN B 2 302 ? -10.709 -8.710  8.496  1.00 45.83 ? 454 GLN B N   1 
ATOM   2849 C CA  . GLN B 2 302 ? -10.785 -10.101 8.051  1.00 37.12 ? 454 GLN B CA  1 
ATOM   2850 C C   . GLN B 2 302 ? -11.384 -10.974 9.139  1.00 31.32 ? 454 GLN B C   1 
ATOM   2851 O O   . GLN B 2 302 ? -11.251 -10.685 10.326 1.00 30.34 ? 454 GLN B O   1 
ATOM   2852 C CB  . GLN B 2 302 ? -9.387  -10.644 7.722  1.00 36.12 ? 454 GLN B CB  1 
ATOM   2853 C CG  . GLN B 2 302 ? -9.434  -12.175 7.489  1.00 40.02 ? 454 GLN B CG  1 
ATOM   2854 C CD  . GLN B 2 302 ? -8.375  -12.750 6.580  1.00 45.85 ? 454 GLN B CD  1 
ATOM   2855 O OE1 . GLN B 2 302 ? -7.271  -12.210 6.459  1.00 49.34 ? 454 GLN B OE1 1 
ATOM   2856 N NE2 . GLN B 2 302 ? -8.692  -13.901 5.971  1.00 45.29 ? 454 GLN B NE2 1 
ATOM   2857 N N   . LEU B 2 303 ? -12.066 -12.031 8.730  1.00 29.03 ? 455 LEU B N   1 
ATOM   2858 C CA  . LEU B 2 303 ? -12.670 -12.947 9.664  1.00 23.32 ? 455 LEU B CA  1 
ATOM   2859 C C   . LEU B 2 303 ? -11.693 -14.040 10.104 1.00 17.71 ? 455 LEU B C   1 
ATOM   2860 O O   . LEU B 2 303 ? -11.346 -14.947 9.346  1.00 20.15 ? 455 LEU B O   1 
ATOM   2861 C CB  . LEU B 2 303 ? -13.915 -13.585 9.037  1.00 22.82 ? 455 LEU B CB  1 
ATOM   2862 C CG  . LEU B 2 303 ? -14.689 -14.594 9.887  1.00 21.29 ? 455 LEU B CG  1 
ATOM   2863 C CD1 . LEU B 2 303 ? -14.967 -14.070 11.287 1.00 21.47 ? 455 LEU B CD1 1 
ATOM   2864 C CD2 . LEU B 2 303 ? -15.968 -15.050 9.179  1.00 24.44 ? 455 LEU B CD2 1 
ATOM   2865 N N   . PHE B 2 304 ? -11.309 -13.991 11.369 1.00 18.14 ? 456 PHE B N   1 
ATOM   2866 C CA  . PHE B 2 304 ? -10.387 -14.970 11.920 1.00 17.83 ? 456 PHE B CA  1 
ATOM   2867 C C   . PHE B 2 304 ? -11.178 -15.953 12.766 1.00 14.50 ? 456 PHE B C   1 
ATOM   2868 O O   . PHE B 2 304 ? -11.939 -15.536 13.629 1.00 14.61 ? 456 PHE B O   1 
ATOM   2869 C CB  . PHE B 2 304 ? -9.399  -14.315 12.883 1.00 16.78 ? 456 PHE B CB  1 
ATOM   2870 C CG  . PHE B 2 304 ? -8.403  -13.378 12.232 1.00 21.10 ? 456 PHE B CG  1 
ATOM   2871 C CD1 . PHE B 2 304 ? -7.370  -13.879 11.459 1.00 23.36 ? 456 PHE B CD1 1 
ATOM   2872 C CD2 . PHE B 2 304 ? -8.446  -12.020 12.468 1.00 24.31 ? 456 PHE B CD2 1 
ATOM   2873 C CE1 . PHE B 2 304 ? -6.426  -13.041 10.882 1.00 25.63 ? 456 PHE B CE1 1 
ATOM   2874 C CE2 . PHE B 2 304 ? -7.503  -11.181 11.896 1.00 27.29 ? 456 PHE B CE2 1 
ATOM   2875 C CZ  . PHE B 2 304 ? -6.488  -11.703 11.107 1.00 24.59 ? 456 PHE B CZ  1 
ATOM   2876 N N   . CYS B 2 305 ? -10.975 -17.247 12.535 1.00 13.15 ? 457 CYS B N   1 
ATOM   2877 C CA  . CYS B 2 305 ? -11.595 -18.301 13.343 1.00 14.23 ? 457 CYS B CA  1 
ATOM   2878 C C   . CYS B 2 305 ? -10.539 -19.325 13.723 1.00 13.93 ? 457 CYS B C   1 
ATOM   2879 O O   . CYS B 2 305 ? -9.545  -19.527 13.006 1.00 13.91 ? 457 CYS B O   1 
ATOM   2880 C CB  . CYS B 2 305 ? -12.692 -19.038 12.574 1.00 15.44 ? 457 CYS B CB  1 
ATOM   2881 S SG  . CYS B 2 305 ? -14.183 -18.099 12.202 1.00 17.50 ? 457 CYS B SG  1 
ATOM   2882 N N   . ARG B 2 306 ? -10.777 -19.996 14.845 1.00 13.61 ? 458 ARG B N   1 
ATOM   2883 C CA  . ARG B 2 306 ? -9.908  -21.055 15.351 1.00 16.10 ? 458 ARG B CA  1 
ATOM   2884 C C   . ARG B 2 306 ? -10.728 -22.197 15.933 1.00 15.98 ? 458 ARG B C   1 
ATOM   2885 O O   . ARG B 2 306 ? -11.881 -22.011 16.309 1.00 16.03 ? 458 ARG B O   1 
ATOM   2886 C CB  . ARG B 2 306 ? -8.969  -20.508 16.423 1.00 14.37 ? 458 ARG B CB  1 
ATOM   2887 C CG  . ARG B 2 306 ? -9.656  -20.085 17.712 1.00 15.09 ? 458 ARG B CG  1 
ATOM   2888 C CD  . ARG B 2 306 ? -8.668  -19.507 18.728 1.00 17.78 ? 458 ARG B CD  1 
ATOM   2889 N NE  . ARG B 2 306 ? -9.331  -19.058 19.961 1.00 20.27 ? 458 ARG B NE  1 
ATOM   2890 C CZ  . ARG B 2 306 ? -9.181  -19.616 21.165 1.00 20.35 ? 458 ARG B CZ  1 
ATOM   2891 N NH1 . ARG B 2 306 ? -8.399  -20.677 21.330 1.00 17.13 ? 458 ARG B NH1 1 
ATOM   2892 N NH2 . ARG B 2 306 ? -9.832  -19.110 22.208 1.00 20.83 ? 458 ARG B NH2 1 
ATOM   2893 N N   . THR B 2 307 ? -10.155 -23.390 15.929 1.00 13.16 ? 459 THR B N   1 
ATOM   2894 C CA  . THR B 2 307 ? -10.832 -24.594 16.417 1.00 17.10 ? 459 THR B CA  1 
ATOM   2895 C C   . THR B 2 307 ? -10.362 -24.910 17.818 1.00 18.97 ? 459 THR B C   1 
ATOM   2896 O O   . THR B 2 307 ? -9.157  -24.973 18.063 1.00 15.21 ? 459 THR B O   1 
ATOM   2897 C CB  . THR B 2 307 ? -10.547 -25.776 15.504 1.00 16.21 ? 459 THR B CB  1 
ATOM   2898 O OG1 . THR B 2 307 ? -11.027 -25.452 14.198 1.00 18.03 ? 459 THR B OG1 1 
ATOM   2899 C CG2 . THR B 2 307 ? -11.282 -27.020 16.008 1.00 15.87 ? 459 THR B CG2 1 
ATOM   2900 N N   . VAL B 2 308 ? -11.301 -25.057 18.741 1.00 15.26 ? 460 VAL B N   1 
ATOM   2901 C CA  . VAL B 2 308 ? -10.987 -25.260 20.152 1.00 14.77 ? 460 VAL B CA  1 
ATOM   2902 C C   . VAL B 2 308 ? -11.535 -26.627 20.563 1.00 16.68 ? 460 VAL B C   1 
ATOM   2903 O O   . VAL B 2 308 ? -12.756 -26.830 20.579 1.00 15.18 ? 460 VAL B O   1 
ATOM   2904 C CB  . VAL B 2 308 ? -11.647 -24.211 21.026 1.00 16.66 ? 460 VAL B CB  1 
ATOM   2905 C CG1 . VAL B 2 308 ? -11.365 -24.532 22.491 1.00 18.14 ? 460 VAL B CG1 1 
ATOM   2906 C CG2 . VAL B 2 308 ? -11.113 -22.815 20.651 1.00 14.44 ? 460 VAL B CG2 1 
ATOM   2907 N N   . TRP B 2 309 ? -10.644 -27.580 20.836 1.00 14.09 ? 461 TRP B N   1 
ATOM   2908 C CA  . TRP B 2 309 ? -11.050 -28.904 21.323 1.00 15.36 ? 461 TRP B CA  1 
ATOM   2909 C C   . TRP B 2 309 ? -11.190 -28.891 22.842 1.00 15.04 ? 461 TRP B C   1 
ATOM   2910 O O   . TRP B 2 309 ? -10.323 -28.364 23.543 1.00 15.94 ? 461 TRP B O   1 
ATOM   2911 C CB  . TRP B 2 309 ? -9.980  -29.937 20.957 1.00 16.98 ? 461 TRP B CB  1 
ATOM   2912 C CG  . TRP B 2 309 ? -10.008 -30.319 19.526 1.00 18.55 ? 461 TRP B CG  1 
ATOM   2913 C CD1 . TRP B 2 309 ? -9.621  -29.540 18.452 1.00 15.93 ? 461 TRP B CD1 1 
ATOM   2914 C CD2 . TRP B 2 309 ? -10.449 -31.554 18.986 1.00 14.75 ? 461 TRP B CD2 1 
ATOM   2915 N NE1 . TRP B 2 309 ? -9.795  -30.240 17.281 1.00 17.05 ? 461 TRP B NE1 1 
ATOM   2916 C CE2 . TRP B 2 309 ? -10.312 -31.472 17.581 1.00 15.10 ? 461 TRP B CE2 1 
ATOM   2917 C CE3 . TRP B 2 309 ? -10.970 -32.725 19.551 1.00 16.53 ? 461 TRP B CE3 1 
ATOM   2918 C CZ2 . TRP B 2 309 ? -10.659 -32.511 16.746 1.00 16.41 ? 461 TRP B CZ2 1 
ATOM   2919 C CZ3 . TRP B 2 309 ? -11.311 -33.756 18.722 1.00 14.76 ? 461 TRP B CZ3 1 
ATOM   2920 C CH2 . TRP B 2 309 ? -11.160 -33.645 17.332 1.00 18.30 ? 461 TRP B CH2 1 
ATOM   2921 N N   . SER B 2 310 ? -12.256 -29.499 23.370 1.00 17.88 ? 462 SER B N   1 
ATOM   2922 C CA  . SER B 2 310 ? -12.390 -29.632 24.814 1.00 16.24 ? 462 SER B CA  1 
ATOM   2923 C C   . SER B 2 310 ? -11.459 -30.721 25.327 1.00 16.93 ? 462 SER B C   1 
ATOM   2924 O O   . SER B 2 310 ? -10.942 -31.542 24.568 1.00 16.02 ? 462 SER B O   1 
ATOM   2925 C CB  . SER B 2 310 ? -13.807 -30.077 25.201 1.00 15.62 ? 462 SER B CB  1 
ATOM   2926 O OG  . SER B 2 310 ? -14.077 -31.379 24.710 1.00 18.20 ? 462 SER B OG  1 
ATOM   2927 N N   . ALA B 2 311 ? -11.273 -30.734 26.637 1.00 18.11 ? 463 ALA B N   1 
ATOM   2928 C CA  . ALA B 2 311 ? -10.892 -31.962 27.344 1.00 20.91 ? 463 ALA B CA  1 
ATOM   2929 C C   . ALA B 2 311 ? -11.882 -33.093 27.026 1.00 21.55 ? 463 ALA B C   1 
ATOM   2930 O O   . ALA B 2 311 ? -13.062 -32.838 26.799 1.00 22.74 ? 463 ALA B O   1 
ATOM   2931 C CB  . ALA B 2 311 ? -10.843 -31.708 28.846 1.00 20.77 ? 463 ALA B CB  1 
ATOM   2932 N N   . HIS B 2 312 ? -11.397 -34.335 26.989 1.00 21.83 ? 464 HIS B N   1 
ATOM   2933 C CA  . HIS B 2 312 ? -12.249 -35.521 26.800 1.00 24.11 ? 464 HIS B CA  1 
ATOM   2934 C C   . HIS B 2 312 ? -13.239 -35.619 27.976 1.00 24.62 ? 464 HIS B C   1 
ATOM   2935 O O   . HIS B 2 312 ? -12.873 -35.340 29.113 1.00 24.21 ? 464 HIS B O   1 
ATOM   2936 C CB  . HIS B 2 312 ? -11.316 -36.727 26.791 1.00 24.62 ? 464 HIS B CB  1 
ATOM   2937 C CG  . HIS B 2 312 ? -11.957 -38.024 26.404 1.00 23.25 ? 464 HIS B CG  1 
ATOM   2938 N ND1 . HIS B 2 312 ? -12.134 -38.425 25.096 1.00 31.08 ? 464 HIS B ND1 1 
ATOM   2939 C CD2 . HIS B 2 312 ? -12.408 -39.045 27.169 1.00 23.29 ? 464 HIS B CD2 1 
ATOM   2940 C CE1 . HIS B 2 312 ? -12.691 -39.627 25.074 1.00 26.83 ? 464 HIS B CE1 1 
ATOM   2941 N NE2 . HIS B 2 312 ? -12.870 -40.025 26.320 1.00 25.33 ? 464 HIS B NE2 1 
ATOM   2942 N N   . SER B 2 313 ? -14.513 -35.894 27.683 1.00 18.94 ? 465 SER B N   1 
ATOM   2943 C CA  . SER B 2 313 ? -15.573 -35.944 28.713 1.00 21.25 ? 465 SER B CA  1 
ATOM   2944 C C   . SER B 2 313 ? -15.431 -37.082 29.738 1.00 24.91 ? 465 SER B C   1 
ATOM   2945 O O   . SER B 2 313 ? -16.008 -37.010 30.832 1.00 23.21 ? 465 SER B O   1 
ATOM   2946 C CB  . SER B 2 313 ? -16.934 -36.153 28.035 1.00 20.14 ? 465 SER B CB  1 
ATOM   2947 O OG  . SER B 2 313 ? -17.047 -37.466 27.498 1.00 22.25 ? 465 SER B OG  1 
ATOM   2948 N N   . GLY B 2 314 ? -14.682 -38.125 29.395 1.00 21.10 ? 466 GLY B N   1 
ATOM   2949 C CA  . GLY B 2 314 ? -14.633 -39.346 30.197 1.00 21.83 ? 466 GLY B CA  1 
ATOM   2950 C C   . GLY B 2 314 ? -15.876 -40.198 29.923 1.00 25.64 ? 466 GLY B C   1 
ATOM   2951 O O   . GLY B 2 314 ? -16.792 -39.753 29.207 1.00 23.58 ? 466 GLY B O   1 
ATOM   2952 N N   . PRO B 2 315 ? -15.914 -41.432 30.466 1.00 22.32 ? 467 PRO B N   1 
ATOM   2953 C CA  . PRO B 2 315 ? -16.905 -42.434 30.064 1.00 23.64 ? 467 PRO B CA  1 
ATOM   2954 C C   . PRO B 2 315 ? -18.270 -42.397 30.789 1.00 23.48 ? 467 PRO B C   1 
ATOM   2955 O O   . PRO B 2 315 ? -19.103 -43.250 30.487 1.00 22.27 ? 467 PRO B O   1 
ATOM   2956 C CB  . PRO B 2 315 ? -16.188 -43.752 30.371 1.00 22.59 ? 467 PRO B CB  1 
ATOM   2957 C CG  . PRO B 2 315 ? -15.324 -43.427 31.552 1.00 21.08 ? 467 PRO B CG  1 
ATOM   2958 C CD  . PRO B 2 315 ? -15.000 -41.950 31.502 1.00 21.05 ? 467 PRO B CD  1 
ATOM   2959 N N   . THR B 2 316 ? -18.499 -41.490 31.738 1.00 24.86 ? 468 THR B N   1 
ATOM   2960 C CA  . THR B 2 316 ? -19.803 -41.485 32.452 1.00 26.03 ? 468 THR B CA  1 
ATOM   2961 C C   . THR B 2 316 ? -20.990 -41.319 31.509 1.00 30.08 ? 468 THR B C   1 
ATOM   2962 O O   . THR B 2 316 ? -20.920 -40.617 30.498 1.00 29.60 ? 468 THR B O   1 
ATOM   2963 C CB  . THR B 2 316 ? -19.883 -40.458 33.577 1.00 27.25 ? 468 THR B CB  1 
ATOM   2964 O OG1 . THR B 2 316 ? -19.861 -39.138 33.025 1.00 31.76 ? 468 THR B OG1 1 
ATOM   2965 C CG2 . THR B 2 316 ? -18.738 -40.642 34.559 1.00 27.13 ? 468 THR B CG2 1 
ATOM   2966 N N   . ARG B 2 317 ? -22.073 -42.016 31.829 1.00 33.01 ? 469 ARG B N   1 
ATOM   2967 C CA  . ARG B 2 317 ? -23.217 -42.154 30.935 1.00 35.22 ? 469 ARG B CA  1 
ATOM   2968 C C   . ARG B 2 317 ? -23.779 -40.793 30.522 1.00 34.67 ? 469 ARG B C   1 
ATOM   2969 O O   . ARG B 2 317 ? -24.195 -40.608 29.378 1.00 37.38 ? 469 ARG B O   1 
ATOM   2970 C CB  . ARG B 2 317 ? -24.308 -43.010 31.587 1.00 38.30 ? 469 ARG B CB  1 
ATOM   2971 C CG  . ARG B 2 317 ? -23.781 -44.398 31.836 1.00 43.91 ? 469 ARG B CG  1 
ATOM   2972 C CD  . ARG B 2 317 ? -23.426 -45.097 30.541 1.00 49.77 ? 469 ARG B CD  1 
ATOM   2973 N NE  . ARG B 2 317 ? -22.468 -46.180 30.758 1.00 46.96 ? 469 ARG B NE  1 
ATOM   2974 C CZ  . ARG B 2 317 ? -21.173 -46.080 30.462 1.00 43.28 ? 469 ARG B CZ  1 
ATOM   2975 N NH1 . ARG B 2 317 ? -20.700 -44.941 29.948 1.00 36.92 ? 469 ARG B NH1 1 
ATOM   2976 N NH2 . ARG B 2 317 ? -20.348 -47.107 30.682 1.00 35.60 ? 469 ARG B NH2 1 
ATOM   2977 N N   . MET B 2 318 ? -23.814 -39.867 31.480 1.00 32.93 ? 470 MET B N   1 
ATOM   2978 C CA  . MET B 2 318 ? -24.277 -38.492 31.281 1.00 37.25 ? 470 MET B CA  1 
ATOM   2979 C C   . MET B 2 318 ? -23.128 -37.503 31.109 1.00 30.19 ? 470 MET B C   1 
ATOM   2980 O O   . MET B 2 318 ? -23.306 -36.316 31.376 1.00 30.54 ? 470 MET B O   1 
ATOM   2981 C CB  . MET B 2 318 ? -25.089 -38.046 32.508 1.00 37.06 ? 470 MET B CB  1 
ATOM   2982 C CG  . MET B 2 318 ? -26.332 -38.873 32.846 1.00 45.32 ? 470 MET B CG  1 
ATOM   2983 S SD  . MET B 2 318 ? -27.616 -38.830 31.568 1.00 63.05 ? 470 MET B SD  1 
ATOM   2984 C CE  . MET B 2 318 ? -27.234 -40.274 30.580 1.00 46.30 ? 470 MET B CE  1 
ATOM   2985 N N   . ALA B 2 319 ? -21.972 -37.967 30.638 1.00 31.56 ? 471 ALA B N   1 
ATOM   2986 C CA  . ALA B 2 319 ? -20.796 -37.099 30.549 1.00 28.10 ? 471 ALA B CA  1 
ATOM   2987 C C   . ALA B 2 319 ? -20.997 -36.050 29.480 1.00 26.59 ? 471 ALA B C   1 
ATOM   2988 O O   . ALA B 2 319 ? -21.608 -36.327 28.433 1.00 28.88 ? 471 ALA B O   1 
ATOM   2989 C CB  . ALA B 2 319 ? -19.549 -37.925 30.205 1.00 29.69 ? 471 ALA B CB  1 
ATOM   2990 N N   . THR B 2 320 ? -20.541 -34.835 29.773 1.00 24.25 ? 472 THR B N   1 
ATOM   2991 C CA  . THR B 2 320 ? -20.468 -33.781 28.770 1.00 25.75 ? 472 THR B CA  1 
ATOM   2992 C C   . THR B 2 320 ? -19.073 -33.149 28.724 1.00 25.03 ? 472 THR B C   1 
ATOM   2993 O O   . THR B 2 320 ? -18.420 -32.981 29.759 1.00 24.42 ? 472 THR B O   1 
ATOM   2994 C CB  . THR B 2 320 ? -21.565 -32.697 28.944 1.00 28.59 ? 472 THR B CB  1 
ATOM   2995 O OG1 . THR B 2 320 ? -21.245 -31.887 30.083 1.00 31.00 ? 472 THR B OG1 1 
ATOM   2996 C CG2 . THR B 2 320 ? -22.959 -33.322 29.122 1.00 30.14 ? 472 THR B CG2 1 
ATOM   2997 N N   . ALA B 2 321 ? -18.620 -32.825 27.520 1.00 22.60 ? 473 ALA B N   1 
ATOM   2998 C CA  . ALA B 2 321 ? -17.385 -32.079 27.303 1.00 22.95 ? 473 ALA B CA  1 
ATOM   2999 C C   . ALA B 2 321 ? -17.784 -30.654 26.926 1.00 22.43 ? 473 ALA B C   1 
ATOM   3000 O O   . ALA B 2 321 ? -18.815 -30.467 26.281 1.00 17.75 ? 473 ALA B O   1 
ATOM   3001 C CB  . ALA B 2 321 ? -16.570 -32.721 26.202 1.00 21.91 ? 473 ALA B CB  1 
ATOM   3002 N N   . ILE B 2 322 ? -17.057 -29.648 27.397 1.00 16.51 ? 474 ILE B N   1 
ATOM   3003 C CA  . ILE B 2 322 ? -17.386 -28.258 27.059 1.00 17.86 ? 474 ILE B CA  1 
ATOM   3004 C C   . ILE B 2 322 ? -16.197 -27.556 26.407 1.00 21.55 ? 474 ILE B C   1 
ATOM   3005 O O   . ILE B 2 322 ? -15.078 -27.591 26.939 1.00 18.62 ? 474 ILE B O   1 
ATOM   3006 C CB  . ILE B 2 322 ? -17.856 -27.459 28.272 1.00 21.27 ? 474 ILE B CB  1 
ATOM   3007 C CG1 . ILE B 2 322 ? -19.152 -28.093 28.800 1.00 26.43 ? 474 ILE B CG1 1 
ATOM   3008 C CG2 . ILE B 2 322 ? -18.119 -25.983 27.878 1.00 22.19 ? 474 ILE B CG2 1 
ATOM   3009 C CD1 . ILE B 2 322 ? -19.948 -27.220 29.742 1.00 38.50 ? 474 ILE B CD1 1 
ATOM   3010 N N   . ALA B 2 323 ? -16.417 -26.987 25.223 1.00 19.22 ? 475 ALA B N   1 
ATOM   3011 C CA  . ALA B 2 323 ? -15.403 -26.139 24.572 1.00 16.12 ? 475 ALA B CA  1 
ATOM   3012 C C   . ALA B 2 323 ? -15.856 -24.679 24.611 1.00 17.61 ? 475 ALA B C   1 
ATOM   3013 O O   . ALA B 2 323 ? -16.978 -24.351 24.207 1.00 20.18 ? 475 ALA B O   1 
ATOM   3014 C CB  . ALA B 2 323 ? -15.205 -26.590 23.129 1.00 13.41 ? 475 ALA B CB  1 
ATOM   3015 N N   . ARG B 2 324 ? -15.021 -23.807 25.172 1.00 18.98 ? 476 ARG B N   1 
ATOM   3016 C CA  . ARG B 2 324 ? -15.336 -22.379 25.256 1.00 17.97 ? 476 ARG B CA  1 
ATOM   3017 C C   . ARG B 2 324 ? -14.435 -21.491 24.415 1.00 17.83 ? 476 ARG B C   1 
ATOM   3018 O O   . ARG B 2 324 ? -13.256 -21.790 24.216 1.00 17.95 ? 476 ARG B O   1 
ATOM   3019 C CB  . ARG B 2 324 ? -15.137 -21.905 26.698 1.00 19.29 ? 476 ARG B CB  1 
ATOM   3020 C CG  . ARG B 2 324 ? -15.987 -22.614 27.735 1.00 28.25 ? 476 ARG B CG  1 
ATOM   3021 C CD  . ARG B 2 324 ? -15.734 -22.006 29.122 1.00 33.66 ? 476 ARG B CD  1 
ATOM   3022 N NE  . ARG B 2 324 ? -16.741 -22.449 30.089 1.00 37.65 ? 476 ARG B NE  1 
ATOM   3023 C CZ  . ARG B 2 324 ? -16.780 -23.658 30.644 1.00 41.87 ? 476 ARG B CZ  1 
ATOM   3024 N NH1 . ARG B 2 324 ? -15.861 -24.570 30.336 1.00 37.48 ? 476 ARG B NH1 1 
ATOM   3025 N NH2 . ARG B 2 324 ? -17.755 -23.960 31.496 1.00 43.38 ? 476 ARG B NH2 1 
ATOM   3026 N N   . CYS B 2 325 ? -14.965 -20.325 24.065 1.00 16.92 ? 477 CYS B N   1 
ATOM   3027 C CA  . CYS B 2 325 ? -14.216 -19.297 23.354 1.00 20.49 ? 477 CYS B CA  1 
ATOM   3028 C C   . CYS B 2 325 ? -13.754 -18.260 24.349 1.00 25.39 ? 477 CYS B C   1 
ATOM   3029 O O   . CYS B 2 325 ? -14.224 -18.251 25.488 1.00 20.54 ? 477 CYS B O   1 
ATOM   3030 C CB  . CYS B 2 325 ? -15.101 -18.642 22.282 1.00 20.87 ? 477 CYS B CB  1 
ATOM   3031 S SG  . CYS B 2 325 ? -15.772 -19.789 21.062 1.00 21.07 ? 477 CYS B SG  1 
ATOM   3032 N N   . ALA B 2 326 ? -12.864 -17.365 23.917 1.00 21.11 ? 478 ALA B N   1 
ATOM   3033 C CA  . ALA B 2 326 ? -12.420 -16.273 24.762 1.00 20.88 ? 478 ALA B CA  1 
ATOM   3034 C C   . ALA B 2 326 ? -13.561 -15.271 24.867 1.00 24.15 ? 478 ALA B C   1 
ATOM   3035 O O   . ALA B 2 326 ? -14.434 -15.235 23.997 1.00 20.98 ? 478 ALA B O   1 
ATOM   3036 C CB  . ALA B 2 326 ? -11.171 -15.602 24.156 1.00 20.62 ? 478 ALA B CB  1 
ATOM   3037 N N   . PRO B 2 327 ? -13.530 -14.410 25.897 1.00 25.29 ? 479 PRO B N   1 
ATOM   3038 C CA  . PRO B 2 327 ? -14.600 -13.424 26.108 1.00 27.93 ? 479 PRO B CA  1 
ATOM   3039 C C   . PRO B 2 327 ? -14.854 -12.558 24.885 1.00 26.45 ? 479 PRO B C   1 
ATOM   3040 O O   . PRO B 2 327 ? -15.998 -12.156 24.677 1.00 27.80 ? 479 PRO B O   1 
ATOM   3041 C CB  . PRO B 2 327 ? -14.066 -12.566 27.257 1.00 28.90 ? 479 PRO B CB  1 
ATOM   3042 C CG  . PRO B 2 327 ? -13.141 -13.470 27.993 1.00 30.79 ? 479 PRO B CG  1 
ATOM   3043 C CD  . PRO B 2 327 ? -12.511 -14.358 26.961 1.00 27.11 ? 479 PRO B CD  1 
ATOM   3044 N N   . ASP B 2 328 ? -13.810 -12.194 24.145 1.00 25.53 ? 480 ASP B N   1 
ATOM   3045 C CA  . ASP B 2 328 ? -14.000 -11.313 22.982 1.00 26.89 ? 480 ASP B CA  1 
ATOM   3046 C C   . ASP B 2 328 ? -14.240 -12.047 21.652 1.00 23.22 ? 480 ASP B C   1 
ATOM   3047 O O   . ASP B 2 328 ? -14.257 -11.417 20.584 1.00 24.53 ? 480 ASP B O   1 
ATOM   3048 C CB  . ASP B 2 328 ? -12.864 -10.291 22.845 1.00 25.42 ? 480 ASP B CB  1 
ATOM   3049 C CG  . ASP B 2 328 ? -11.495 -10.935 22.881 1.00 27.24 ? 480 ASP B CG  1 
ATOM   3050 O OD1 . ASP B 2 328 ? -11.313 -11.961 23.590 1.00 27.05 ? 480 ASP B OD1 1 
ATOM   3051 O OD2 . ASP B 2 328 ? -10.594 -10.412 22.184 1.00 24.42 ? 480 ASP B OD2 1 
ATOM   3052 N N   . GLU B 2 329 ? -14.396 -13.368 21.715 1.00 19.62 ? 481 GLU B N   1 
ATOM   3053 C CA  . GLU B 2 329 ? -14.708 -14.176 20.530 1.00 19.07 ? 481 GLU B CA  1 
ATOM   3054 C C   . GLU B 2 329 ? -16.179 -14.593 20.541 1.00 22.01 ? 481 GLU B C   1 
ATOM   3055 O O   . GLU B 2 329 ? -16.819 -14.592 21.589 1.00 20.92 ? 481 GLU B O   1 
ATOM   3056 C CB  . GLU B 2 329 ? -13.844 -15.446 20.510 1.00 18.97 ? 481 GLU B CB  1 
ATOM   3057 C CG  . GLU B 2 329 ? -12.338 -15.230 20.223 1.00 17.13 ? 481 GLU B CG  1 
ATOM   3058 C CD  . GLU B 2 329 ? -11.527 -16.513 20.360 1.00 19.50 ? 481 GLU B CD  1 
ATOM   3059 O OE1 . GLU B 2 329 ? -11.886 -17.384 21.197 1.00 19.40 ? 481 GLU B OE1 1 
ATOM   3060 O OE2 . GLU B 2 329 ? -10.530 -16.677 19.612 1.00 20.31 ? 481 GLU B OE2 1 
ATOM   3061 N N   . GLU B 2 330 ? -16.719 -14.909 19.367 1.00 19.34 ? 482 GLU B N   1 
ATOM   3062 C CA  . GLU B 2 330 ? -18.054 -15.503 19.235 1.00 23.67 ? 482 GLU B CA  1 
ATOM   3063 C C   . GLU B 2 330 ? -17.925 -16.961 18.861 1.00 17.70 ? 482 GLU B C   1 
ATOM   3064 O O   . GLU B 2 330 ? -17.107 -17.311 18.014 1.00 18.03 ? 482 GLU B O   1 
ATOM   3065 C CB  . GLU B 2 330 ? -18.858 -14.787 18.160 1.00 22.53 ? 482 GLU B CB  1 
ATOM   3066 C CG  . GLU B 2 330 ? -18.847 -13.303 18.358 1.00 28.63 ? 482 GLU B CG  1 
ATOM   3067 C CD  . GLU B 2 330 ? -19.923 -12.885 19.340 1.00 31.24 ? 482 GLU B CD  1 
ATOM   3068 O OE1 . GLU B 2 330 ? -20.881 -13.664 19.529 1.00 29.54 ? 482 GLU B OE1 1 
ATOM   3069 O OE2 . GLU B 2 330 ? -19.794 -11.796 19.933 1.00 37.99 ? 482 GLU B OE2 1 
ATOM   3070 N N   . LEU B 2 331 ? -18.722 -17.814 19.497 1.00 17.09 ? 483 LEU B N   1 
ATOM   3071 C CA  . LEU B 2 331 ? -18.877 -19.197 19.064 1.00 17.72 ? 483 LEU B CA  1 
ATOM   3072 C C   . LEU B 2 331 ? -19.759 -19.277 17.822 1.00 20.29 ? 483 LEU B C   1 
ATOM   3073 O O   . LEU B 2 331 ? -20.979 -19.196 17.929 1.00 21.05 ? 483 LEU B O   1 
ATOM   3074 C CB  . LEU B 2 331 ? -19.554 -19.961 20.196 1.00 18.84 ? 483 LEU B CB  1 
ATOM   3075 C CG  . LEU B 2 331 ? -19.792 -21.447 19.889 1.00 17.59 ? 483 LEU B CG  1 
ATOM   3076 C CD1 . LEU B 2 331 ? -18.464 -22.155 19.925 1.00 14.16 ? 483 LEU B CD1 1 
ATOM   3077 C CD2 . LEU B 2 331 ? -20.770 -22.137 20.856 1.00 20.04 ? 483 LEU B CD2 1 
ATOM   3078 N N   . LEU B 2 332 ? -19.170 -19.505 16.648 1.00 16.14 ? 484 LEU B N   1 
ATOM   3079 C CA  . LEU B 2 332 ? -19.963 -19.610 15.409 1.00 15.48 ? 484 LEU B CA  1 
ATOM   3080 C C   . LEU B 2 332 ? -20.429 -21.013 15.051 1.00 16.78 ? 484 LEU B C   1 
ATOM   3081 O O   . LEU B 2 332 ? -21.356 -21.185 14.251 1.00 15.07 ? 484 LEU B O   1 
ATOM   3082 C CB  . LEU B 2 332 ? -19.226 -18.983 14.218 1.00 19.03 ? 484 LEU B CB  1 
ATOM   3083 C CG  . LEU B 2 332 ? -18.950 -17.477 14.311 1.00 20.82 ? 484 LEU B CG  1 
ATOM   3084 C CD1 . LEU B 2 332 ? -18.658 -16.874 12.930 1.00 22.13 ? 484 LEU B CD1 1 
ATOM   3085 C CD2 . LEU B 2 332 ? -20.086 -16.750 14.963 1.00 21.07 ? 484 LEU B CD2 1 
ATOM   3086 N N   . SER B 2 333 ? -19.788 -22.034 15.605 1.00 13.30 ? 485 SER B N   1 
ATOM   3087 C CA  . SER B 2 333 ? -20.318 -23.386 15.421 1.00 14.32 ? 485 SER B CA  1 
ATOM   3088 C C   . SER B 2 333 ? -19.796 -24.330 16.487 1.00 15.14 ? 485 SER B C   1 
ATOM   3089 O O   . SER B 2 333 ? -18.877 -23.991 17.233 1.00 15.07 ? 485 SER B O   1 
ATOM   3090 C CB  . SER B 2 333 ? -19.964 -23.942 14.044 1.00 13.20 ? 485 SER B CB  1 
ATOM   3091 O OG  . SER B 2 333 ? -18.572 -24.255 13.952 1.00 16.59 ? 485 SER B OG  1 
ATOM   3092 N N   . CYS B 2 334 ? -20.320 -25.551 16.490 1.00 18.58 ? 486 CYS B N   1 
ATOM   3093 C CA  . CYS B 2 334 ? -20.027 -26.515 17.544 1.00 18.87 ? 486 CYS B CA  1 
ATOM   3094 C C   . CYS B 2 334 ? -20.174 -27.899 16.949 1.00 17.44 ? 486 CYS B C   1 
ATOM   3095 O O   . CYS B 2 334 ? -21.222 -28.234 16.394 1.00 14.70 ? 486 CYS B O   1 
ATOM   3096 C CB  . CYS B 2 334 ? -21.028 -26.265 18.686 1.00 19.85 ? 486 CYS B CB  1 
ATOM   3097 S SG  . CYS B 2 334 ? -21.056 -27.504 20.031 1.00 22.25 ? 486 CYS B SG  1 
ATOM   3098 N N   . SER B 2 335 ? -19.120 -28.705 17.055 1.00 15.25 ? 487 SER B N   1 
ATOM   3099 C CA  . SER B 2 335 ? -19.145 -30.094 16.583 1.00 15.43 ? 487 SER B CA  1 
ATOM   3100 C C   . SER B 2 335 ? -18.617 -31.000 17.677 1.00 16.28 ? 487 SER B C   1 
ATOM   3101 O O   . SER B 2 335 ? -18.343 -30.519 18.784 1.00 13.50 ? 487 SER B O   1 
ATOM   3102 C CB  . SER B 2 335 ? -18.386 -30.286 15.263 1.00 17.82 ? 487 SER B CB  1 
ATOM   3103 O OG  . SER B 2 335 ? -16.985 -30.051 15.407 1.00 22.83 ? 487 SER B OG  1 
ATOM   3104 N N   . SER B 2 336 ? -18.522 -32.304 17.400 1.00 16.53 ? 488 SER B N   1 
ATOM   3105 C CA  . SER B 2 336 ? -18.045 -33.257 18.406 1.00 18.92 ? 488 SER B CA  1 
ATOM   3106 C C   . SER B 2 336 ? -17.423 -34.460 17.721 1.00 18.74 ? 488 SER B C   1 
ATOM   3107 O O   . SER B 2 336 ? -17.561 -34.645 16.510 1.00 18.64 ? 488 SER B O   1 
ATOM   3108 C CB  . SER B 2 336 ? -19.176 -33.740 19.326 1.00 17.40 ? 488 SER B CB  1 
ATOM   3109 O OG  . SER B 2 336 ? -20.249 -34.319 18.595 1.00 18.65 ? 488 SER B OG  1 
ATOM   3110 N N   . PHE B 2 337 ? -16.751 -35.296 18.502 1.00 16.67 ? 489 PHE B N   1 
ATOM   3111 C CA  . PHE B 2 337 ? -16.003 -36.401 17.927 1.00 19.20 ? 489 PHE B CA  1 
ATOM   3112 C C   . PHE B 2 337 ? -15.791 -37.418 19.050 1.00 19.93 ? 489 PHE B C   1 
ATOM   3113 O O   . PHE B 2 337 ? -15.473 -37.047 20.182 1.00 17.66 ? 489 PHE B O   1 
ATOM   3114 C CB  . PHE B 2 337 ? -14.638 -35.904 17.425 1.00 20.65 ? 489 PHE B CB  1 
ATOM   3115 C CG  . PHE B 2 337 ? -13.743 -37.011 16.898 1.00 20.78 ? 489 PHE B CG  1 
ATOM   3116 C CD1 . PHE B 2 337 ? -13.947 -37.555 15.640 1.00 23.93 ? 489 PHE B CD1 1 
ATOM   3117 C CD2 . PHE B 2 337 ? -12.705 -37.506 17.663 1.00 22.57 ? 489 PHE B CD2 1 
ATOM   3118 C CE1 . PHE B 2 337 ? -13.137 -38.589 15.166 1.00 26.76 ? 489 PHE B CE1 1 
ATOM   3119 C CE2 . PHE B 2 337 ? -11.889 -38.534 17.183 1.00 25.21 ? 489 PHE B CE2 1 
ATOM   3120 C CZ  . PHE B 2 337 ? -12.103 -39.065 15.939 1.00 24.79 ? 489 PHE B CZ  1 
ATOM   3121 N N   . SER B 2 338 ? -16.018 -38.694 18.736 1.00 22.29 ? 490 SER B N   1 
ATOM   3122 C CA  . SER B 2 338 ? -15.526 -39.812 19.540 1.00 29.98 ? 490 SER B CA  1 
ATOM   3123 C C   . SER B 2 338 ? -14.885 -40.884 18.653 1.00 26.40 ? 490 SER B C   1 
ATOM   3124 O O   . SER B 2 338 ? -15.374 -41.190 17.559 1.00 22.53 ? 490 SER B O   1 
ATOM   3125 C CB  . SER B 2 338 ? -16.650 -40.433 20.366 1.00 30.92 ? 490 SER B CB  1 
ATOM   3126 O OG  . SER B 2 338 ? -17.187 -41.578 19.733 1.00 36.86 ? 490 SER B OG  1 
ATOM   3127 N N   . ARG B 2 339 ? -13.853 -41.535 19.165 1.00 31.28 ? 491 ARG B N   1 
ATOM   3128 C CA  . ARG B 2 339 ? -13.129 -42.510 18.358 1.00 32.84 ? 491 ARG B CA  1 
ATOM   3129 C C   . ARG B 2 339 ? -13.917 -43.773 18.074 1.00 31.20 ? 491 ARG B C   1 
ATOM   3130 O O   . ARG B 2 339 ? -13.771 -44.375 17.015 1.00 29.52 ? 491 ARG B O   1 
ATOM   3131 C CB  . ARG B 2 339 ? -11.819 -42.853 19.053 1.00 37.31 ? 491 ARG B CB  1 
ATOM   3132 C CG  . ARG B 2 339 ? -10.980 -41.645 19.214 1.00 40.86 ? 491 ARG B CG  1 
ATOM   3133 C CD  . ARG B 2 339 ? -9.889  -41.910 20.210 1.00 41.76 ? 491 ARG B CD  1 
ATOM   3134 N NE  . ARG B 2 339 ? -9.342  -40.653 20.717 1.00 38.86 ? 491 ARG B NE  1 
ATOM   3135 C CZ  . ARG B 2 339 ? -8.682  -39.750 20.001 1.00 37.65 ? 491 ARG B CZ  1 
ATOM   3136 N NH1 . ARG B 2 339 ? -8.493  -39.908 18.687 1.00 37.35 ? 491 ARG B NH1 1 
ATOM   3137 N NH2 . ARG B 2 339 ? -8.247  -38.650 20.605 1.00 35.73 ? 491 ARG B NH2 1 
ATOM   3138 N N   . SER B 2 340 ? -14.793 -44.120 19.014 1.00 31.54 ? 492 SER B N   1 
ATOM   3139 C CA  . SER B 2 340 ? -15.726 -45.241 18.872 1.00 35.42 ? 492 SER B CA  1 
ATOM   3140 C C   . SER B 2 340 ? -16.949 -44.927 18.038 1.00 38.88 ? 492 SER B C   1 
ATOM   3141 O O   . SER B 2 340 ? -17.529 -45.821 17.431 1.00 37.21 ? 492 SER B O   1 
ATOM   3142 C CB  . SER B 2 340 ? -16.175 -45.730 20.243 1.00 35.53 ? 492 SER B CB  1 
ATOM   3143 O OG  . SER B 2 340 ? -16.854 -44.714 20.958 1.00 39.38 ? 492 SER B OG  1 
ATOM   3144 N N   . GLY B 2 341 ? -17.345 -43.660 18.011 1.00 33.95 ? 493 GLY B N   1 
ATOM   3145 C CA  . GLY B 2 341 ? -18.600 -43.296 17.386 1.00 35.96 ? 493 GLY B CA  1 
ATOM   3146 C C   . GLY B 2 341 ? -19.783 -43.430 18.323 1.00 38.00 ? 493 GLY B C   1 
ATOM   3147 O O   . GLY B 2 341 ? -20.931 -43.302 17.897 1.00 36.12 ? 493 GLY B O   1 
ATOM   3148 N N   . LYS B 2 342 ? -19.509 -43.693 19.598 1.00 34.64 ? 494 LYS B N   1 
ATOM   3149 C CA  . LYS B 2 342 ? -20.574 -43.800 20.588 1.00 28.23 ? 494 LYS B CA  1 
ATOM   3150 C C   . LYS B 2 342 ? -20.843 -42.440 21.247 1.00 32.52 ? 494 LYS B C   1 
ATOM   3151 O O   . LYS B 2 342 ? -20.184 -42.051 22.223 1.00 27.89 ? 494 LYS B O   1 
ATOM   3152 C CB  . LYS B 2 342 ? -20.251 -44.869 21.630 1.00 35.57 ? 494 LYS B CB  1 
ATOM   3153 C CG  . LYS B 2 342 ? -20.364 -46.292 21.100 1.00 34.54 ? 494 LYS B CG  1 
ATOM   3154 C CD  . LYS B 2 342 ? -19.726 -47.278 22.057 1.00 43.60 ? 494 LYS B CD  1 
ATOM   3155 C CE  . LYS B 2 342 ? -19.840 -48.708 21.545 1.00 42.29 ? 494 LYS B CE  1 
ATOM   3156 N NZ  . LYS B 2 342 ? -19.350 -49.667 22.580 1.00 53.14 ? 494 LYS B NZ  1 
ATOM   3157 N N   . ARG B 2 343 ? -21.846 -41.744 20.712 1.00 28.34 ? 495 ARG B N   1 
ATOM   3158 C CA  . ARG B 2 343 ? -21.894 -40.286 20.712 1.00 29.80 ? 495 ARG B CA  1 
ATOM   3159 C C   . ARG B 2 343 ? -23.366 -39.913 20.742 1.00 23.61 ? 495 ARG B C   1 
ATOM   3160 O O   . ARG B 2 343 ? -24.158 -40.566 20.072 1.00 21.16 ? 495 ARG B O   1 
ATOM   3161 C CB  . ARG B 2 343 ? -21.309 -39.834 19.369 1.00 27.41 ? 495 ARG B CB  1 
ATOM   3162 C CG  . ARG B 2 343 ? -20.682 -38.491 19.341 1.00 33.17 ? 495 ARG B CG  1 
ATOM   3163 C CD  . ARG B 2 343 ? -19.729 -38.399 18.149 1.00 32.83 ? 495 ARG B CD  1 
ATOM   3164 N NE  . ARG B 2 343 ? -20.424 -38.504 16.862 1.00 32.28 ? 495 ARG B NE  1 
ATOM   3165 C CZ  . ARG B 2 343 ? -21.038 -37.490 16.257 1.00 27.01 ? 495 ARG B CZ  1 
ATOM   3166 N NH1 . ARG B 2 343 ? -21.633 -37.673 15.089 1.00 26.62 ? 495 ARG B NH1 1 
ATOM   3167 N NH2 . ARG B 2 343 ? -21.066 -36.292 16.827 1.00 27.46 ? 495 ARG B NH2 1 
ATOM   3168 N N   . ARG B 2 344 ? -23.743 -38.917 21.537 1.00 22.33 ? 496 ARG B N   1 
ATOM   3169 C CA  . ARG B 2 344 ? -25.067 -38.317 21.430 1.00 21.52 ? 496 ARG B CA  1 
ATOM   3170 C C   . ARG B 2 344 ? -25.058 -36.873 20.858 1.00 23.91 ? 496 ARG B C   1 
ATOM   3171 O O   . ARG B 2 344 ? -25.983 -36.096 21.102 1.00 19.28 ? 496 ARG B O   1 
ATOM   3172 C CB  . ARG B 2 344 ? -25.790 -38.396 22.778 1.00 22.78 ? 496 ARG B CB  1 
ATOM   3173 C CG  . ARG B 2 344 ? -26.395 -39.809 22.959 1.00 22.05 ? 496 ARG B CG  1 
ATOM   3174 C CD  . ARG B 2 344 ? -27.308 -39.967 24.158 1.00 25.63 ? 496 ARG B CD  1 
ATOM   3175 N NE  . ARG B 2 344 ? -26.739 -39.461 25.399 1.00 33.13 ? 496 ARG B NE  1 
ATOM   3176 C CZ  . ARG B 2 344 ? -27.176 -38.395 26.063 1.00 38.75 ? 496 ARG B CZ  1 
ATOM   3177 N NH1 . ARG B 2 344 ? -28.195 -37.678 25.598 1.00 41.49 ? 496 ARG B NH1 1 
ATOM   3178 N NH2 . ARG B 2 344 ? -26.576 -38.038 27.194 1.00 44.80 ? 496 ARG B NH2 1 
ATOM   3179 N N   . GLY B 2 345 ? -24.000 -36.523 20.118 1.00 20.42 ? 497 GLY B N   1 
ATOM   3180 C CA  . GLY B 2 345 ? -23.863 -35.223 19.456 1.00 15.21 ? 497 GLY B CA  1 
ATOM   3181 C C   . GLY B 2 345 ? -23.552 -34.026 20.326 1.00 17.84 ? 497 GLY B C   1 
ATOM   3182 O O   . GLY B 2 345 ? -22.911 -34.137 21.367 1.00 16.55 ? 497 GLY B O   1 
ATOM   3183 N N   . GLU B 2 346 ? -23.986 -32.848 19.893 1.00 15.06 ? 498 GLU B N   1 
ATOM   3184 C CA  . GLU B 2 346 ? -23.601 -31.632 20.603 1.00 17.41 ? 498 GLU B CA  1 
ATOM   3185 C C   . GLU B 2 346 ? -24.628 -30.520 20.455 1.00 15.41 ? 498 GLU B C   1 
ATOM   3186 O O   . GLU B 2 346 ? -25.473 -30.578 19.577 1.00 16.36 ? 498 GLU B O   1 
ATOM   3187 C CB  . GLU B 2 346 ? -22.241 -31.132 20.066 1.00 17.35 ? 498 GLU B CB  1 
ATOM   3188 C CG  . GLU B 2 346 ? -22.260 -30.509 18.657 1.00 16.75 ? 498 GLU B CG  1 
ATOM   3189 C CD  . GLU B 2 346 ? -22.540 -31.503 17.549 1.00 18.50 ? 498 GLU B CD  1 
ATOM   3190 O OE1 . GLU B 2 346 ? -21.931 -32.607 17.579 1.00 20.53 ? 498 GLU B OE1 1 
ATOM   3191 O OE2 . GLU B 2 346 ? -23.333 -31.182 16.622 1.00 16.82 ? 498 GLU B OE2 1 
ATOM   3192 N N   . ARG B 2 347 ? -24.563 -29.522 21.327 1.00 17.06 ? 499 ARG B N   1 
ATOM   3193 C CA  . ARG B 2 347 ? -25.467 -28.365 21.280 1.00 22.27 ? 499 ARG B CA  1 
ATOM   3194 C C   . ARG B 2 347 ? -24.706 -27.166 21.829 1.00 20.81 ? 499 ARG B C   1 
ATOM   3195 O O   . ARG B 2 347 ? -23.777 -27.309 22.618 1.00 17.47 ? 499 ARG B O   1 
ATOM   3196 C CB  . ARG B 2 347 ? -26.723 -28.586 22.114 1.00 21.46 ? 499 ARG B CB  1 
ATOM   3197 C CG  . ARG B 2 347 ? -26.542 -28.717 23.591 1.00 31.85 ? 499 ARG B CG  1 
ATOM   3198 C CD  . ARG B 2 347 ? -27.615 -29.636 24.146 1.00 34.02 ? 499 ARG B CD  1 
ATOM   3199 N NE  . ARG B 2 347 ? -27.356 -30.021 25.532 1.00 38.43 ? 499 ARG B NE  1 
ATOM   3200 C CZ  . ARG B 2 347 ? -27.341 -29.190 26.572 1.00 46.95 ? 499 ARG B CZ  1 
ATOM   3201 N NH1 . ARG B 2 347 ? -27.562 -27.886 26.409 1.00 51.49 ? 499 ARG B NH1 1 
ATOM   3202 N NH2 . ARG B 2 347 ? -27.091 -29.667 27.785 1.00 49.51 ? 499 ARG B NH2 1 
ATOM   3203 N N   . MET B 2 348 ? -25.112 -25.983 21.404 1.00 24.91 ? 500 MET B N   1 
ATOM   3204 C CA  . MET B 2 348 ? -24.597 -24.727 21.934 1.00 26.34 ? 500 MET B CA  1 
ATOM   3205 C C   . MET B 2 348 ? -25.479 -24.227 23.067 1.00 28.97 ? 500 MET B C   1 
ATOM   3206 O O   . MET B 2 348 ? -26.686 -24.111 22.904 1.00 33.81 ? 500 MET B O   1 
ATOM   3207 C CB  . MET B 2 348 ? -24.597 -23.700 20.797 1.00 29.29 ? 500 MET B CB  1 
ATOM   3208 C CG  . MET B 2 348 ? -23.716 -24.163 19.635 1.00 26.70 ? 500 MET B CG  1 
ATOM   3209 S SD  . MET B 2 348 ? -23.782 -23.196 18.105 1.00 39.73 ? 500 MET B SD  1 
ATOM   3210 C CE  . MET B 2 348 ? -25.126 -24.012 17.213 1.00 31.48 ? 500 MET B CE  1 
ATOM   3211 N N   . GLU B 2 349 ? -24.910 -24.018 24.255 1.00 29.93 ? 501 GLU B N   1 
ATOM   3212 C CA  . GLU B 2 349 ? -25.726 -23.614 25.396 1.00 35.84 ? 501 GLU B CA  1 
ATOM   3213 C C   . GLU B 2 349 ? -25.113 -22.360 25.994 1.00 36.84 ? 501 GLU B C   1 
ATOM   3214 O O   . GLU B 2 349 ? -23.888 -22.165 25.994 1.00 31.64 ? 501 GLU B O   1 
ATOM   3215 C CB  . GLU B 2 349 ? -25.800 -24.730 26.449 1.00 40.56 ? 501 GLU B CB  1 
ATOM   3216 C CG  . GLU B 2 349 ? -24.626 -24.831 27.407 1.00 45.74 ? 501 GLU B CG  1 
ATOM   3217 C CD  . GLU B 2 349 ? -25.001 -25.487 28.734 1.00 48.24 ? 501 GLU B CD  1 
ATOM   3218 O OE1 . GLU B 2 349 ? -25.643 -26.562 28.699 1.00 50.41 ? 501 GLU B OE1 1 
ATOM   3219 O OE2 . GLU B 2 349 ? -24.643 -24.937 29.804 1.00 49.68 ? 501 GLU B OE2 1 
ATOM   3220 N N   . ALA B 2 350 ? -25.987 -21.480 26.472 1.00 30.00 ? 502 ALA B N   1 
ATOM   3221 C CA  . ALA B 2 350 ? -25.536 -20.258 27.098 1.00 32.33 ? 502 ALA B CA  1 
ATOM   3222 C C   . ALA B 2 350 ? -25.091 -20.507 28.515 1.00 39.25 ? 502 ALA B C   1 
ATOM   3223 O O   . ALA B 2 350 ? -25.537 -21.451 29.166 1.00 41.77 ? 502 ALA B O   1 
ATOM   3224 C CB  . ALA B 2 350 ? -26.605 -19.195 27.043 1.00 31.66 ? 502 ALA B CB  1 
ATOM   3225 N N   . GLN B 2 351 ? -24.199 -19.649 28.989 1.00 39.08 ? 503 GLN B N   1 
ATOM   3226 C CA  . GLN B 2 351 ? -23.486 -19.905 30.228 1.00 40.28 ? 503 GLN B CA  1 
ATOM   3227 C C   . GLN B 2 351 ? -22.781 -18.625 30.595 1.00 43.75 ? 503 GLN B C   1 
ATOM   3228 O O   . GLN B 2 351 ? -21.824 -18.216 29.937 1.00 46.78 ? 503 GLN B O   1 
ATOM   3229 C CB  . GLN B 2 351 ? -22.503 -21.059 30.040 1.00 42.91 ? 503 GLN B CB  1 
ATOM   3230 C CG  . GLN B 2 351 ? -21.939 -21.664 31.285 1.00 45.31 ? 503 GLN B CG  1 
ATOM   3231 C CD  . GLN B 2 351 ? -21.489 -23.089 31.038 1.00 46.60 ? 503 GLN B CD  1 
ATOM   3232 O OE1 . GLN B 2 351 ? -20.347 -23.452 31.327 1.00 47.27 ? 503 GLN B OE1 1 
ATOM   3233 N NE2 . GLN B 2 351 ? -22.385 -23.904 30.485 1.00 46.39 ? 503 GLN B NE2 1 
ATOM   3234 N N   . GLY B 2 352 ? -23.230 -18.012 31.681 1.00 43.91 ? 504 GLY B N   1 
ATOM   3235 C CA  . GLY B 2 352 ? -22.783 -16.674 32.010 1.00 43.59 ? 504 GLY B CA  1 
ATOM   3236 C C   . GLY B 2 352 ? -23.064 -15.716 30.867 1.00 44.45 ? 504 GLY B C   1 
ATOM   3237 O O   . GLY B 2 352 ? -22.269 -14.815 30.602 1.00 46.77 ? 504 GLY B O   1 
ATOM   3238 N N   . GLY B 2 353 ? -24.199 -15.888 30.194 1.00 44.92 ? 505 GLY B N   1 
ATOM   3239 C CA  . GLY B 2 353 ? -24.562 -14.987 29.111 1.00 46.36 ? 505 GLY B CA  1 
ATOM   3240 C C   . GLY B 2 353 ? -23.721 -15.121 27.851 1.00 46.77 ? 505 GLY B C   1 
ATOM   3241 O O   . GLY B 2 353 ? -23.681 -14.214 27.017 1.00 48.41 ? 505 GLY B O   1 
ATOM   3242 N N   . LYS B 2 354 ? -23.081 -16.271 27.685 1.00 39.65 ? 506 LYS B N   1 
ATOM   3243 C CA  . LYS B 2 354 ? -22.183 -16.481 26.559 1.00 35.60 ? 506 LYS B CA  1 
ATOM   3244 C C   . LYS B 2 354 ? -22.301 -17.928 26.094 1.00 28.88 ? 506 LYS B C   1 
ATOM   3245 O O   . LYS B 2 354 ? -22.390 -18.852 26.899 1.00 29.74 ? 506 LYS B O   1 
ATOM   3246 C CB  . LYS B 2 354 ? -20.752 -16.173 27.000 1.00 42.81 ? 506 LYS B CB  1 
ATOM   3247 C CG  . LYS B 2 354 ? -19.698 -16.465 25.958 1.00 33.60 ? 506 LYS B CG  1 
ATOM   3248 C CD  . LYS B 2 354 ? -18.397 -15.731 26.266 1.00 40.86 ? 506 LYS B CD  1 
ATOM   3249 C CE  . LYS B 2 354 ? -17.304 -16.137 25.273 1.00 27.34 ? 506 LYS B CE  1 
ATOM   3250 N NZ  . LYS B 2 354 ? -17.704 -15.724 23.898 1.00 29.25 ? 506 LYS B NZ  1 
ATOM   3251 N N   . LEU B 2 355 ? -22.295 -18.126 24.783 1.00 24.91 ? 507 LEU B N   1 
ATOM   3252 C CA  . LEU B 2 355 ? -22.519 -19.455 24.237 1.00 25.99 ? 507 LEU B CA  1 
ATOM   3253 C C   . LEU B 2 355 ? -21.261 -20.307 24.284 1.00 25.84 ? 507 LEU B C   1 
ATOM   3254 O O   . LEU B 2 355 ? -20.168 -19.817 23.990 1.00 22.73 ? 507 LEU B O   1 
ATOM   3255 C CB  . LEU B 2 355 ? -23.043 -19.353 22.805 1.00 27.77 ? 507 LEU B CB  1 
ATOM   3256 C CG  . LEU B 2 355 ? -24.445 -18.762 22.606 1.00 31.32 ? 507 LEU B CG  1 
ATOM   3257 C CD1 . LEU B 2 355 ? -24.657 -18.414 21.121 1.00 28.98 ? 507 LEU B CD1 1 
ATOM   3258 C CD2 . LEU B 2 355 ? -25.528 -19.704 23.108 1.00 22.01 ? 507 LEU B CD2 1 
ATOM   3259 N N   . VAL B 2 356 ? -21.429 -21.556 24.722 1.00 25.06 ? 508 VAL B N   1 
ATOM   3260 C CA  . VAL B 2 356 ? -20.364 -22.560 24.796 1.00 21.63 ? 508 VAL B CA  1 
ATOM   3261 C C   . VAL B 2 356 ? -20.819 -23.751 23.966 1.00 23.31 ? 508 VAL B C   1 
ATOM   3262 O O   . VAL B 2 356 ? -22.015 -23.890 23.676 1.00 22.79 ? 508 VAL B O   1 
ATOM   3263 C CB  . VAL B 2 356 ? -20.038 -22.992 26.250 1.00 22.64 ? 508 VAL B CB  1 
ATOM   3264 C CG1 . VAL B 2 356 ? -19.792 -21.772 27.132 1.00 25.28 ? 508 VAL B CG1 1 
ATOM   3265 C CG2 . VAL B 2 356 ? -21.157 -23.868 26.820 1.00 29.93 ? 508 VAL B CG2 1 
ATOM   3266 N N   . CYS B 2 357 ? -19.874 -24.606 23.586 1.00 18.48 ? 509 CYS B N   1 
ATOM   3267 C CA  . CYS B 2 357 ? -20.147 -25.813 22.811 1.00 17.06 ? 509 CYS B CA  1 
ATOM   3268 C C   . CYS B 2 357 ? -20.131 -27.020 23.750 1.00 19.14 ? 509 CYS B C   1 
ATOM   3269 O O   . CYS B 2 357 ? -19.131 -27.302 24.398 1.00 19.50 ? 509 CYS B O   1 
ATOM   3270 C CB  . CYS B 2 357 ? -19.057 -25.973 21.739 1.00 17.20 ? 509 CYS B CB  1 
ATOM   3271 S SG  . CYS B 2 357 ? -19.158 -27.478 20.789 1.00 18.30 ? 509 CYS B SG  1 
ATOM   3272 N N   . ARG B 2 358 ? -21.257 -27.711 23.862 1.00 19.81 ? 510 ARG B N   1 
ATOM   3273 C CA  . ARG B 2 358 ? -21.337 -28.875 24.742 1.00 19.31 ? 510 ARG B CA  1 
ATOM   3274 C C   . ARG B 2 358 ? -21.616 -30.161 23.985 1.00 21.00 ? 510 ARG B C   1 
ATOM   3275 O O   . ARG B 2 358 ? -22.544 -30.214 23.172 1.00 20.31 ? 510 ARG B O   1 
ATOM   3276 C CB  . ARG B 2 358 ? -22.438 -28.609 25.768 1.00 22.00 ? 510 ARG B CB  1 
ATOM   3277 C CG  . ARG B 2 358 ? -22.568 -29.677 26.838 1.00 28.51 ? 510 ARG B CG  1 
ATOM   3278 C CD  . ARG B 2 358 ? -23.842 -29.475 27.632 1.00 39.52 ? 510 ARG B CD  1 
ATOM   3279 N NE  . ARG B 2 358 ? -23.659 -28.370 28.568 1.00 45.10 ? 510 ARG B NE  1 
ATOM   3280 C CZ  . ARG B 2 358 ? -23.330 -28.532 29.846 1.00 47.19 ? 510 ARG B CZ  1 
ATOM   3281 N NH1 . ARG B 2 358 ? -23.179 -29.760 30.333 1.00 48.36 ? 510 ARG B NH1 1 
ATOM   3282 N NH2 . ARG B 2 358 ? -23.170 -27.477 30.635 1.00 46.84 ? 510 ARG B NH2 1 
ATOM   3283 N N   . ALA B 2 359 ? -20.828 -31.206 24.258 1.00 17.89 ? 511 ALA B N   1 
ATOM   3284 C CA  . ALA B 2 359 ? -20.985 -32.490 23.577 1.00 17.56 ? 511 ALA B CA  1 
ATOM   3285 C C   . ALA B 2 359 ? -21.365 -33.550 24.582 1.00 20.82 ? 511 ALA B C   1 
ATOM   3286 O O   . ALA B 2 359 ? -21.006 -33.445 25.744 1.00 22.84 ? 511 ALA B O   1 
ATOM   3287 C CB  . ALA B 2 359 ? -19.699 -32.901 22.870 1.00 17.34 ? 511 ALA B CB  1 
ATOM   3288 N N   . HIS B 2 360 ? -22.095 -34.560 24.123 1.00 19.87 ? 512 HIS B N   1 
ATOM   3289 C CA  . HIS B 2 360 ? -22.703 -35.568 25.000 1.00 24.84 ? 512 HIS B CA  1 
ATOM   3290 C C   . HIS B 2 360 ? -22.209 -36.943 24.683 1.00 21.17 ? 512 HIS B C   1 
ATOM   3291 O O   . HIS B 2 360 ? -22.206 -37.351 23.520 1.00 22.41 ? 512 HIS B O   1 
ATOM   3292 C CB  . HIS B 2 360 ? -24.227 -35.585 24.808 1.00 25.69 ? 512 HIS B CB  1 
ATOM   3293 C CG  . HIS B 2 360 ? -24.903 -34.337 25.267 1.00 27.96 ? 512 HIS B CG  1 
ATOM   3294 N ND1 . HIS B 2 360 ? -25.160 -34.071 26.593 1.00 35.58 ? 512 HIS B ND1 1 
ATOM   3295 C CD2 . HIS B 2 360 ? -25.390 -33.285 24.572 1.00 29.69 ? 512 HIS B CD2 1 
ATOM   3296 C CE1 . HIS B 2 360 ? -25.762 -32.901 26.699 1.00 34.66 ? 512 HIS B CE1 1 
ATOM   3297 N NE2 . HIS B 2 360 ? -25.916 -32.405 25.485 1.00 35.69 ? 512 HIS B NE2 1 
ATOM   3298 N N   . ASN B 2 361 ? -21.808 -37.670 25.722 1.00 22.51 ? 513 ASN B N   1 
ATOM   3299 C CA  . ASN B 2 361 ? -21.356 -39.045 25.564 1.00 24.10 ? 513 ASN B CA  1 
ATOM   3300 C C   . ASN B 2 361 ? -22.569 -39.950 25.433 1.00 26.98 ? 513 ASN B C   1 
ATOM   3301 O O   . ASN B 2 361 ? -23.645 -39.607 25.920 1.00 24.58 ? 513 ASN B O   1 
ATOM   3302 C CB  . ASN B 2 361 ? -20.528 -39.459 26.780 1.00 24.02 ? 513 ASN B CB  1 
ATOM   3303 C CG  . ASN B 2 361 ? -19.870 -40.798 26.589 1.00 24.84 ? 513 ASN B CG  1 
ATOM   3304 O OD1 . ASN B 2 361 ? -19.633 -41.216 25.455 1.00 25.35 ? 513 ASN B OD1 1 
ATOM   3305 N ND2 . ASN B 2 361 ? -19.639 -41.521 27.691 1.00 24.68 ? 513 ASN B ND2 1 
ATOM   3306 N N   . ALA B 2 362 ? -22.414 -41.084 24.757 1.00 26.34 ? 514 ALA B N   1 
ATOM   3307 C CA  . ALA B 2 362 ? -23.468 -42.087 24.701 1.00 27.55 ? 514 ALA B CA  1 
ATOM   3308 C C   . ALA B 2 362 ? -23.283 -43.085 25.832 1.00 35.59 ? 514 ALA B C   1 
ATOM   3309 O O   . ALA B 2 362 ? -22.174 -43.278 26.342 1.00 34.57 ? 514 ALA B O   1 
ATOM   3310 C CB  . ALA B 2 362 ? -23.436 -42.808 23.383 1.00 29.55 ? 514 ALA B CB  1 
ATOM   3311 N N   . PHE B 2 363 ? -24.366 -43.760 26.188 1.00 40.28 ? 515 PHE B N   1 
ATOM   3312 C CA  . PHE B 2 363 ? -24.296 -44.877 27.121 1.00 42.48 ? 515 PHE B CA  1 
ATOM   3313 C C   . PHE B 2 363 ? -23.338 -45.959 26.627 1.00 39.03 ? 515 PHE B C   1 
ATOM   3314 O O   . PHE B 2 363 ? -23.486 -46.483 25.526 1.00 38.22 ? 515 PHE B O   1 
ATOM   3315 C CB  . PHE B 2 363 ? -25.688 -45.483 27.302 1.00 51.05 ? 515 PHE B CB  1 
ATOM   3316 C CG  . PHE B 2 363 ? -25.848 -46.215 28.597 1.00 55.93 ? 515 PHE B CG  1 
ATOM   3317 C CD1 . PHE B 2 363 ? -25.303 -47.486 28.744 1.00 53.32 ? 515 PHE B CD1 1 
ATOM   3318 C CD2 . PHE B 2 363 ? -26.518 -45.642 29.670 1.00 57.99 ? 515 PHE B CD2 1 
ATOM   3319 C CE1 . PHE B 2 363 ? -25.422 -48.183 29.929 1.00 55.10 ? 515 PHE B CE1 1 
ATOM   3320 C CE2 . PHE B 2 363 ? -26.637 -46.338 30.873 1.00 61.51 ? 515 PHE B CE2 1 
ATOM   3321 C CZ  . PHE B 2 363 ? -26.087 -47.611 30.997 1.00 58.85 ? 515 PHE B CZ  1 
ATOM   3322 N N   . GLY B 2 364 ? -22.326 -46.253 27.434 1.00 42.31 ? 516 GLY B N   1 
ATOM   3323 C CA  . GLY B 2 364 ? -21.299 -47.212 27.070 1.00 37.99 ? 516 GLY B CA  1 
ATOM   3324 C C   . GLY B 2 364 ? -20.156 -46.655 26.248 1.00 37.01 ? 516 GLY B C   1 
ATOM   3325 O O   . GLY B 2 364 ? -19.241 -47.391 25.891 1.00 43.05 ? 516 GLY B O   1 
ATOM   3326 N N   . GLY B 2 365 ? -20.217 -45.368 25.921 1.00 35.39 ? 517 GLY B N   1 
ATOM   3327 C CA  . GLY B 2 365 ? -19.131 -44.699 25.223 1.00 29.82 ? 517 GLY B CA  1 
ATOM   3328 C C   . GLY B 2 365 ? -17.962 -44.429 26.155 1.00 29.14 ? 517 GLY B C   1 
ATOM   3329 O O   . GLY B 2 365 ? -18.149 -44.108 27.333 1.00 26.32 ? 517 GLY B O   1 
ATOM   3330 N N   . GLU B 2 366 ? -16.750 -44.477 25.618 1.00 27.53 ? 518 GLU B N   1 
ATOM   3331 C CA  . GLU B 2 366 ? -15.563 -44.077 26.376 1.00 26.57 ? 518 GLU B CA  1 
ATOM   3332 C C   . GLU B 2 366 ? -15.456 -42.578 26.617 1.00 24.94 ? 518 GLU B C   1 
ATOM   3333 O O   . GLU B 2 366 ? -14.643 -42.125 27.428 1.00 22.64 ? 518 GLU B O   1 
ATOM   3334 C CB  . GLU B 2 366 ? -14.293 -44.600 25.704 1.00 33.39 ? 518 GLU B CB  1 
ATOM   3335 C CG  . GLU B 2 366 ? -13.945 -43.942 24.395 1.00 35.43 ? 518 GLU B CG  1 
ATOM   3336 C CD  . GLU B 2 366 ? -14.896 -44.351 23.290 1.00 39.22 ? 518 GLU B CD  1 
ATOM   3337 O OE1 . GLU B 2 366 ? -15.729 -45.264 23.522 1.00 41.87 ? 518 GLU B OE1 1 
ATOM   3338 O OE2 . GLU B 2 366 ? -14.817 -43.759 22.189 1.00 42.91 ? 518 GLU B OE2 1 
ATOM   3339 N N   . GLY B 2 367 ? -16.276 -41.806 25.908 1.00 26.73 ? 519 GLY B N   1 
ATOM   3340 C CA  . GLY B 2 367 ? -16.243 -40.352 26.006 1.00 24.84 ? 519 GLY B CA  1 
ATOM   3341 C C   . GLY B 2 367 ? -16.167 -39.606 24.684 1.00 23.49 ? 519 GLY B C   1 
ATOM   3342 O O   . GLY B 2 367 ? -16.031 -40.207 23.612 1.00 23.38 ? 519 GLY B O   1 
ATOM   3343 N N   . VAL B 2 368 ? -16.331 -38.286 24.756 1.00 21.05 ? 520 VAL B N   1 
ATOM   3344 C CA  . VAL B 2 368 ? -16.387 -37.473 23.544 1.00 19.99 ? 520 VAL B CA  1 
ATOM   3345 C C   . VAL B 2 368 ? -15.668 -36.160 23.739 1.00 18.46 ? 520 VAL B C   1 
ATOM   3346 O O   . VAL B 2 368 ? -15.407 -35.750 24.870 1.00 17.26 ? 520 VAL B O   1 
ATOM   3347 C CB  . VAL B 2 368 ? -17.857 -37.136 23.174 1.00 17.74 ? 520 VAL B CB  1 
ATOM   3348 C CG1 . VAL B 2 368 ? -18.638 -38.395 22.897 1.00 21.57 ? 520 VAL B CG1 1 
ATOM   3349 C CG2 . VAL B 2 368 ? -18.529 -36.295 24.286 1.00 19.60 ? 520 VAL B CG2 1 
ATOM   3350 N N   . TYR B 2 369 ? -15.338 -35.510 22.620 1.00 17.64 ? 521 TYR B N   1 
ATOM   3351 C CA  . TYR B 2 369 ? -14.808 -34.154 22.617 1.00 15.04 ? 521 TYR B CA  1 
ATOM   3352 C C   . TYR B 2 369 ? -15.843 -33.193 22.073 1.00 14.18 ? 521 TYR B C   1 
ATOM   3353 O O   . TYR B 2 369 ? -16.532 -33.495 21.118 1.00 15.92 ? 521 TYR B O   1 
ATOM   3354 C CB  . TYR B 2 369 ? -13.582 -34.062 21.702 1.00 18.07 ? 521 TYR B CB  1 
ATOM   3355 C CG  . TYR B 2 369 ? -12.392 -34.914 22.135 1.00 16.97 ? 521 TYR B CG  1 
ATOM   3356 C CD1 . TYR B 2 369 ? -11.505 -34.461 23.108 1.00 20.77 ? 521 TYR B CD1 1 
ATOM   3357 C CD2 . TYR B 2 369 ? -12.162 -36.170 21.575 1.00 19.37 ? 521 TYR B CD2 1 
ATOM   3358 C CE1 . TYR B 2 369 ? -10.401 -35.236 23.505 1.00 19.25 ? 521 TYR B CE1 1 
ATOM   3359 C CE2 . TYR B 2 369 ? -11.067 -36.953 21.973 1.00 23.29 ? 521 TYR B CE2 1 
ATOM   3360 C CZ  . TYR B 2 369 ? -10.201 -36.471 22.939 1.00 21.82 ? 521 TYR B CZ  1 
ATOM   3361 O OH  . TYR B 2 369 ? -9.115  -37.230 23.328 1.00 28.24 ? 521 TYR B OH  1 
ATOM   3362 N N   . ALA B 2 370 ? -15.908 -32.016 22.677 1.00 15.13 ? 522 ALA B N   1 
ATOM   3363 C CA  . ALA B 2 370 ? -16.659 -30.891 22.133 1.00 17.74 ? 522 ALA B CA  1 
ATOM   3364 C C   . ALA B 2 370 ? -15.641 -30.048 21.378 1.00 17.24 ? 522 ALA B C   1 
ATOM   3365 O O   . ALA B 2 370 ? -14.471 -29.976 21.778 1.00 13.19 ? 522 ALA B O   1 
ATOM   3366 C CB  . ALA B 2 370 ? -17.289 -30.074 23.250 1.00 14.95 ? 522 ALA B CB  1 
ATOM   3367 N N   . ILE B 2 371 ? -16.043 -29.524 20.220 1.00 15.27 ? 523 ILE B N   1 
ATOM   3368 C CA  . ILE B 2 371 ? -15.114 -28.874 19.303 1.00 14.95 ? 523 ILE B CA  1 
ATOM   3369 C C   . ILE B 2 371 ? -15.752 -27.557 18.879 1.00 16.56 ? 523 ILE B C   1 
ATOM   3370 O O   . ILE B 2 371 ? -16.700 -27.546 18.092 1.00 15.43 ? 523 ILE B O   1 
ATOM   3371 C CB  . ILE B 2 371 ? -14.847 -29.730 18.075 1.00 19.00 ? 523 ILE B CB  1 
ATOM   3372 C CG1 . ILE B 2 371 ? -14.251 -31.074 18.493 1.00 15.20 ? 523 ILE B CG1 1 
ATOM   3373 C CG2 . ILE B 2 371 ? -13.877 -29.008 17.154 1.00 15.58 ? 523 ILE B CG2 1 
ATOM   3374 C CD1 . ILE B 2 371 ? -14.496 -32.192 17.532 1.00 17.91 ? 523 ILE B CD1 1 
ATOM   3375 N N   . ALA B 2 372 ? -15.307 -26.460 19.487 1.00 14.38 ? 524 ALA B N   1 
ATOM   3376 C CA  . ALA B 2 372 ? -15.803 -25.128 19.158 1.00 16.20 ? 524 ALA B CA  1 
ATOM   3377 C C   . ALA B 2 372 ? -15.064 -24.464 18.000 1.00 17.33 ? 524 ALA B C   1 
ATOM   3378 O O   . ALA B 2 372 ? -13.848 -24.652 17.802 1.00 15.61 ? 524 ALA B O   1 
ATOM   3379 C CB  . ALA B 2 372 ? -15.717 -24.220 20.407 1.00 13.27 ? 524 ALA B CB  1 
ATOM   3380 N N   . ARG B 2 373 ? -15.801 -23.692 17.220 1.00 12.45 ? 525 ARG B N   1 
ATOM   3381 C CA  . ARG B 2 373 ? -15.224 -22.750 16.275 1.00 11.82 ? 525 ARG B CA  1 
ATOM   3382 C C   . ARG B 2 373 ? -15.435 -21.336 16.785 1.00 15.02 ? 525 ARG B C   1 
ATOM   3383 O O   . ARG B 2 373 ? -16.562 -20.849 16.824 1.00 11.23 ? 525 ARG B O   1 
ATOM   3384 C CB  . ARG B 2 373 ? -15.823 -22.970 14.883 1.00 14.98 ? 525 ARG B CB  1 
ATOM   3385 C CG  . ARG B 2 373 ? -15.005 -22.322 13.775 1.00 16.09 ? 525 ARG B CG  1 
ATOM   3386 C CD  . ARG B 2 373 ? -13.794 -23.153 13.335 1.00 16.35 ? 525 ARG B CD  1 
ATOM   3387 N NE  . ARG B 2 373 ? -13.232 -22.520 12.141 1.00 18.60 ? 525 ARG B NE  1 
ATOM   3388 C CZ  . ARG B 2 373 ? -11.978 -22.629 11.721 1.00 18.23 ? 525 ARG B CZ  1 
ATOM   3389 N NH1 . ARG B 2 373 ? -11.080 -23.325 12.418 1.00 16.38 ? 525 ARG B NH1 1 
ATOM   3390 N NH2 . ARG B 2 373 ? -11.617 -21.977 10.628 1.00 16.85 ? 525 ARG B NH2 1 
ATOM   3391 N N   . CYS B 2 374 ? -14.341 -20.702 17.209 1.00 10.96 ? 526 CYS B N   1 
ATOM   3392 C CA  . CYS B 2 374 ? -14.377 -19.450 17.941 1.00 14.20 ? 526 CYS B CA  1 
ATOM   3393 C C   . CYS B 2 374 ? -13.777 -18.387 17.023 1.00 17.25 ? 526 CYS B C   1 
ATOM   3394 O O   . CYS B 2 374 ? -12.668 -18.568 16.501 1.00 14.69 ? 526 CYS B O   1 
ATOM   3395 C CB  . CYS B 2 374 ? -13.509 -19.577 19.194 1.00 17.14 ? 526 CYS B CB  1 
ATOM   3396 S SG  . CYS B 2 374 ? -14.148 -20.826 20.386 1.00 18.48 ? 526 CYS B SG  1 
ATOM   3397 N N   . CYS B 2 375 ? -14.481 -17.281 16.836 1.00 15.28 ? 527 CYS B N   1 
ATOM   3398 C CA  . CYS B 2 375 ? -14.144 -16.330 15.775 1.00 16.88 ? 527 CYS B CA  1 
ATOM   3399 C C   . CYS B 2 375 ? -14.173 -14.911 16.289 1.00 18.75 ? 527 CYS B C   1 
ATOM   3400 O O   . CYS B 2 375 ? -14.828 -14.636 17.290 1.00 19.64 ? 527 CYS B O   1 
ATOM   3401 C CB  . CYS B 2 375 ? -15.140 -16.455 14.618 1.00 16.37 ? 527 CYS B CB  1 
ATOM   3402 S SG  . CYS B 2 375 ? -15.286 -18.116 13.932 1.00 17.62 ? 527 CYS B SG  1 
ATOM   3403 N N   . LEU B 2 376 ? -13.402 -14.022 15.660 1.00 17.57 ? 528 LEU B N   1 
ATOM   3404 C CA  . LEU B 2 376 ? -13.413 -12.623 16.050 1.00 20.32 ? 528 LEU B CA  1 
ATOM   3405 C C   . LEU B 2 376 ? -14.389 -11.904 15.116 1.00 24.61 ? 528 LEU B C   1 
ATOM   3406 O O   . LEU B 2 376 ? -14.107 -11.713 13.929 1.00 24.77 ? 528 LEU B O   1 
ATOM   3407 C CB  . LEU B 2 376 ? -11.999 -12.026 15.959 1.00 20.71 ? 528 LEU B CB  1 
ATOM   3408 C CG  . LEU B 2 376 ? -11.001 -12.564 16.986 1.00 19.27 ? 528 LEU B CG  1 
ATOM   3409 C CD1 . LEU B 2 376 ? -9.597  -12.150 16.648 1.00 18.97 ? 528 LEU B CD1 1 
ATOM   3410 C CD2 . LEU B 2 376 ? -11.379 -12.043 18.361 1.00 18.64 ? 528 LEU B CD2 1 
ATOM   3411 N N   . LEU B 2 377 ? -15.556 -11.567 15.648 1.00 27.39 ? 529 LEU B N   1 
ATOM   3412 C CA  . LEU B 2 377 ? -16.643 -11.015 14.856 1.00 28.55 ? 529 LEU B CA  1 
ATOM   3413 C C   . LEU B 2 377 ? -17.232 -9.935  15.753 1.00 37.01 ? 529 LEU B C   1 
ATOM   3414 O O   . LEU B 2 377 ? -18.146 -10.193 16.532 1.00 36.51 ? 529 LEU B O   1 
ATOM   3415 C CB  . LEU B 2 377 ? -17.664 -12.089 14.491 1.00 31.26 ? 529 LEU B CB  1 
ATOM   3416 C CG  . LEU B 2 377 ? -18.659 -11.682 13.400 1.00 33.51 ? 529 LEU B CG  1 
ATOM   3417 C CD1 . LEU B 2 377 ? -17.940 -11.281 12.139 1.00 33.50 ? 529 LEU B CD1 1 
ATOM   3418 C CD2 . LEU B 2 377 ? -19.641 -12.784 13.084 1.00 28.09 ? 529 LEU B CD2 1 
ATOM   3419 N N   . PRO B 2 378 ? -16.704 -8.718  15.666 1.00 39.73 ? 530 PRO B N   1 
ATOM   3420 C CA  . PRO B 2 378 ? -17.313 -7.627  16.425 1.00 47.25 ? 530 PRO B CA  1 
ATOM   3421 C C   . PRO B 2 378 ? -18.604 -7.127  15.801 1.00 50.04 ? 530 PRO B C   1 
ATOM   3422 O O   . PRO B 2 378 ? -18.782 -7.261  14.583 1.00 44.85 ? 530 PRO B O   1 
ATOM   3423 C CB  . PRO B 2 378 ? -16.246 -6.538  16.346 1.00 49.80 ? 530 PRO B CB  1 
ATOM   3424 C CG  . PRO B 2 378 ? -15.632 -6.753  15.001 1.00 45.47 ? 530 PRO B CG  1 
ATOM   3425 C CD  . PRO B 2 378 ? -15.568 -8.259  14.848 1.00 44.00 ? 530 PRO B CD  1 
ATOM   3426 N N   . GLN B 2 379 ? -19.531 -6.672  16.645 1.00 52.28 ? 531 GLN B N   1 
ATOM   3427 C CA  . GLN B 2 379 ? -20.816 -6.162  16.175 1.00 56.71 ? 531 GLN B CA  1 
ATOM   3428 C C   . GLN B 2 379 ? -21.731 -7.299  15.753 1.00 53.76 ? 531 GLN B C   1 
ATOM   3429 O O   . GLN B 2 379 ? -22.822 -7.066  15.225 1.00 55.52 ? 531 GLN B O   1 
ATOM   3430 C CB  . GLN B 2 379 ? -20.659 -5.106  15.079 1.00 58.88 ? 531 GLN B CB  1 
ATOM   3431 C CG  . GLN B 2 379 ? -19.667 -4.008  15.492 1.00 59.79 ? 531 GLN B CG  1 
ATOM   3432 C CD  . GLN B 2 379 ? -20.018 -3.369  16.846 1.00 67.56 ? 531 GLN B CD  1 
ATOM   3433 O OE1 . GLN B 2 379 ? -19.766 -3.953  17.909 1.00 67.97 ? 531 GLN B OE1 1 
ATOM   3434 N NE2 . GLN B 2 379 ? -20.601 -2.174  16.810 1.00 71.49 ? 531 GLN B NE2 1 
ATOM   3435 N N   . ALA B 2 380 ? -21.279 -8.532  15.956 1.00 48.64 ? 532 ALA B N   1 
ATOM   3436 C CA  . ALA B 2 380 ? -22.135 -9.653  15.639 1.00 46.94 ? 532 ALA B CA  1 
ATOM   3437 C C   . ALA B 2 380 ? -23.155 -9.772  16.744 1.00 45.51 ? 532 ALA B C   1 
ATOM   3438 O O   . ALA B 2 380 ? -22.857 -9.622  17.928 1.00 45.27 ? 532 ALA B O   1 
ATOM   3439 C CB  . ALA B 2 380 ? -21.351 -10.920 15.518 1.00 40.44 ? 532 ALA B CB  1 
ATOM   3440 N N   . ASN B 2 381 ? -24.383 -10.017 16.323 1.00 45.48 ? 533 ASN B N   1 
ATOM   3441 C CA  . ASN B 2 381 ? -25.443 -10.427 17.205 1.00 43.25 ? 533 ASN B CA  1 
ATOM   3442 C C   . ASN B 2 381 ? -25.866 -11.832 16.804 1.00 37.59 ? 533 ASN B C   1 
ATOM   3443 O O   . ASN B 2 381 ? -26.562 -12.007 15.805 1.00 32.66 ? 533 ASN B O   1 
ATOM   3444 C CB  . ASN B 2 381 ? -26.606 -9.453  17.049 1.00 43.65 ? 533 ASN B CB  1 
ATOM   3445 C CG  . ASN B 2 381 ? -26.343 -8.117  17.746 1.00 50.89 ? 533 ASN B CG  1 
ATOM   3446 O OD1 . ASN B 2 381 ? -25.465 -8.020  18.612 1.00 53.00 ? 533 ASN B OD1 1 
ATOM   3447 N ND2 . ASN B 2 381 ? -27.073 -7.081  17.347 1.00 53.10 ? 533 ASN B ND2 1 
ATOM   3448 N N   . CYS B 2 382 ? -25.451 -12.823 17.589 1.00 31.17 ? 534 CYS B N   1 
ATOM   3449 C CA  . CYS B 2 382 ? -25.688 -14.233 17.265 1.00 31.26 ? 534 CYS B CA  1 
ATOM   3450 C C   . CYS B 2 382 ? -26.656 -14.894 18.222 1.00 34.26 ? 534 CYS B C   1 
ATOM   3451 O O   . CYS B 2 382 ? -26.709 -14.591 19.421 1.00 36.52 ? 534 CYS B O   1 
ATOM   3452 C CB  . CYS B 2 382 ? -24.385 -15.043 17.258 1.00 32.33 ? 534 CYS B CB  1 
ATOM   3453 S SG  . CYS B 2 382 ? -23.139 -14.508 16.047 1.00 34.72 ? 534 CYS B SG  1 
ATOM   3454 N N   . SER B 2 383 ? -27.433 -15.813 17.673 1.00 28.24 ? 535 SER B N   1 
ATOM   3455 C CA  . SER B 2 383 ? -28.418 -16.504 18.464 1.00 30.70 ? 535 SER B CA  1 
ATOM   3456 C C   . SER B 2 383 ? -28.430 -17.970 18.072 1.00 29.57 ? 535 SER B C   1 
ATOM   3457 O O   . SER B 2 383 ? -27.821 -18.349 17.071 1.00 24.32 ? 535 SER B O   1 
ATOM   3458 C CB  . SER B 2 383 ? -29.766 -15.884 18.127 1.00 26.08 ? 535 SER B CB  1 
ATOM   3459 O OG  . SER B 2 383 ? -30.019 -15.968 16.735 1.00 30.52 ? 535 SER B OG  1 
ATOM   3460 N N   . VAL B 2 384 ? -29.185 -18.786 18.802 1.00 24.42 ? 536 VAL B N   1 
ATOM   3461 C CA  . VAL B 2 384 ? -29.355 -20.187 18.430 1.00 20.65 ? 536 VAL B CA  1 
ATOM   3462 C C   . VAL B 2 384 ? -30.821 -20.479 18.177 1.00 23.30 ? 536 VAL B C   1 
ATOM   3463 O O   . VAL B 2 384 ? -31.675 -19.999 18.922 1.00 20.38 ? 536 VAL B O   1 
ATOM   3464 C CB  . VAL B 2 384 ? -28.785 -21.137 19.543 1.00 20.09 ? 536 VAL B CB  1 
ATOM   3465 C CG1 . VAL B 2 384 ? -28.973 -22.595 19.183 1.00 20.26 ? 536 VAL B CG1 1 
ATOM   3466 C CG2 . VAL B 2 384 ? -27.295 -20.871 19.768 1.00 23.42 ? 536 VAL B CG2 1 
ATOM   3467 N N   . HIS B 2 385 ? -31.107 -21.226 17.113 1.00 17.61 ? 537 HIS B N   1 
ATOM   3468 C CA  . HIS B 2 385 ? -32.475 -21.638 16.784 1.00 20.34 ? 537 HIS B CA  1 
ATOM   3469 C C   . HIS B 2 385 ? -32.460 -23.141 16.878 1.00 19.51 ? 537 HIS B C   1 
ATOM   3470 O O   . HIS B 2 385 ? -31.650 -23.810 16.234 1.00 19.65 ? 537 HIS B O   1 
ATOM   3471 C CB  . HIS B 2 385 ? -32.839 -21.234 15.357 1.00 18.11 ? 537 HIS B CB  1 
ATOM   3472 C CG  . HIS B 2 385 ? -32.976 -19.756 15.163 1.00 24.83 ? 537 HIS B CG  1 
ATOM   3473 N ND1 . HIS B 2 385 ? -32.118 -18.841 15.733 1.00 28.03 ? 537 HIS B ND1 1 
ATOM   3474 C CD2 . HIS B 2 385 ? -33.895 -19.030 14.480 1.00 27.34 ? 537 HIS B CD2 1 
ATOM   3475 C CE1 . HIS B 2 385 ? -32.491 -17.617 15.396 1.00 27.97 ? 537 HIS B CE1 1 
ATOM   3476 N NE2 . HIS B 2 385 ? -33.566 -17.704 14.635 1.00 30.55 ? 537 HIS B NE2 1 
ATOM   3477 N N   . THR B 2 386 ? -33.356 -23.683 17.683 1.00 16.72 ? 538 THR B N   1 
ATOM   3478 C CA  . THR B 2 386 ? -33.366 -25.106 17.934 1.00 15.36 ? 538 THR B CA  1 
ATOM   3479 C C   . THR B 2 386 ? -34.673 -25.731 17.532 1.00 19.66 ? 538 THR B C   1 
ATOM   3480 O O   . THR B 2 386 ? -35.752 -25.135 17.747 1.00 19.25 ? 538 THR B O   1 
ATOM   3481 C CB  . THR B 2 386 ? -33.118 -25.396 19.449 1.00 18.30 ? 538 THR B CB  1 
ATOM   3482 O OG1 . THR B 2 386 ? -31.786 -25.002 19.791 1.00 20.96 ? 538 THR B OG1 1 
ATOM   3483 C CG2 . THR B 2 386 ? -33.306 -26.873 19.819 1.00 17.66 ? 538 THR B CG2 1 
ATOM   3484 N N   . ALA B 2 387 ? -34.616 -26.950 16.998 1.00 18.46 ? 539 ALA B N   1 
ATOM   3485 C CA  . ALA B 2 387 ? -35.880 -27.644 16.871 1.00 20.19 ? 539 ALA B CA  1 
ATOM   3486 C C   . ALA B 2 387 ? -35.646 -29.001 17.487 1.00 20.72 ? 539 ALA B C   1 
ATOM   3487 O O   . ALA B 2 387 ? -34.723 -29.712 17.093 1.00 19.20 ? 539 ALA B O   1 
ATOM   3488 C CB  . ALA B 2 387 ? -36.300 -27.768 15.419 1.00 20.26 ? 539 ALA B CB  1 
ATOM   3489 N N   . PRO B 2 388 ? -36.587 -29.434 18.339 1.00 19.16 ? 540 PRO B N   1 
ATOM   3490 C CA  . PRO B 2 388 ? -36.500 -30.750 18.971 1.00 16.88 ? 540 PRO B CA  1 
ATOM   3491 C C   . PRO B 2 388 ? -36.883 -31.813 17.961 1.00 17.51 ? 540 PRO B C   1 
ATOM   3492 O O   . PRO B 2 388 ? -37.354 -31.435 16.901 1.00 21.33 ? 540 PRO B O   1 
ATOM   3493 C CB  . PRO B 2 388 ? -37.497 -30.641 20.131 1.00 19.98 ? 540 PRO B CB  1 
ATOM   3494 C CG  . PRO B 2 388 ? -37.440 -29.137 20.473 1.00 19.17 ? 540 PRO B CG  1 
ATOM   3495 C CD  . PRO B 2 388 ? -37.414 -28.495 19.119 1.00 18.61 ? 540 PRO B CD  1 
ATOM   3496 N N   . PRO B 2 389 ? -36.690 -33.102 18.272 1.00 20.55 ? 541 PRO B N   1 
ATOM   3497 C CA  . PRO B 2 389 ? -36.983 -34.092 17.218 1.00 23.75 ? 541 PRO B CA  1 
ATOM   3498 C C   . PRO B 2 389 ? -38.406 -34.090 16.597 1.00 30.15 ? 541 PRO B C   1 
ATOM   3499 O O   . PRO B 2 389 ? -39.404 -33.973 17.304 1.00 24.98 ? 541 PRO B O   1 
ATOM   3500 C CB  . PRO B 2 389 ? -36.774 -35.424 17.971 1.00 21.05 ? 541 PRO B CB  1 
ATOM   3501 C CG  . PRO B 2 389 ? -35.824 -35.080 19.093 1.00 21.80 ? 541 PRO B CG  1 
ATOM   3502 C CD  . PRO B 2 389 ? -36.187 -33.705 19.518 1.00 20.99 ? 541 PRO B CD  1 
ATOM   3503 N N   . ALA B 2 390 ? -38.421 -34.054 15.259 1.00 32.55 ? 542 ALA B N   1 
ATOM   3504 C CA  . ALA B 2 390 ? -39.585 -34.091 14.357 1.00 32.85 ? 542 ALA B CA  1 
ATOM   3505 C C   . ALA B 2 390 ? -40.170 -35.497 14.218 1.00 43.70 ? 542 ALA B C   1 
ATOM   3506 O O   . ALA B 2 390 ? -39.980 -36.380 15.057 1.00 38.00 ? 542 ALA B O   1 
ATOM   3507 C CB  . ALA B 2 390 ? -39.171 -33.595 12.990 1.00 35.99 ? 542 ALA B CB  1 
ATOM   3508 N N   . GLU B 2 391 ? -40.820 -35.699 13.067 1.00 53.89 ? 543 GLU B N   1 
ATOM   3509 C CA  . GLU B 2 391 ? -40.691 -36.967 12.351 1.00 54.83 ? 543 GLU B CA  1 
ATOM   3510 C C   . GLU B 2 391 ? -40.338 -36.746 10.862 1.00 55.17 ? 543 GLU B C   1 
ATOM   3511 O O   . GLU B 2 391 ? -41.079 -36.108 10.114 1.00 52.95 ? 543 GLU B O   1 
ATOM   3512 C CB  . GLU B 2 391 ? -41.979 -37.784 12.484 1.00 51.75 ? 543 GLU B CB  1 
ATOM   3513 C CG  . GLU B 2 391 ? -41.979 -38.597 13.749 1.00 51.77 ? 543 GLU B CG  1 
ATOM   3514 C CD  . GLU B 2 391 ? -40.646 -39.296 13.941 1.00 55.08 ? 543 GLU B CD  1 
ATOM   3515 O OE1 . GLU B 2 391 ? -40.196 -39.973 12.986 1.00 49.53 ? 543 GLU B OE1 1 
ATOM   3516 O OE2 . GLU B 2 391 ? -40.037 -39.150 15.027 1.00 55.48 ? 543 GLU B OE2 1 
ATOM   3517 N N   . GLY B 2 395 ? -37.718 -35.662 8.241  1.00 52.47 ? 547 GLY B N   1 
ATOM   3518 C CA  . GLY B 2 395 ? -36.599 -35.559 9.184  1.00 44.54 ? 547 GLY B CA  1 
ATOM   3519 C C   . GLY B 2 395 ? -36.669 -34.209 9.922  1.00 43.30 ? 547 GLY B C   1 
ATOM   3520 O O   . GLY B 2 395 ? -37.587 -33.441 9.653  1.00 49.81 ? 547 GLY B O   1 
ATOM   3521 N N   . THR B 2 396 ? -35.721 -33.876 10.811 1.00 38.20 ? 548 THR B N   1 
ATOM   3522 C CA  . THR B 2 396 ? -35.785 -32.579 11.549 1.00 31.80 ? 548 THR B CA  1 
ATOM   3523 C C   . THR B 2 396 ? -34.996 -31.392 10.951 1.00 31.64 ? 548 THR B C   1 
ATOM   3524 O O   . THR B 2 396 ? -33.848 -31.548 10.534 1.00 34.69 ? 548 THR B O   1 
ATOM   3525 C CB  . THR B 2 396 ? -35.255 -32.785 13.013 1.00 27.67 ? 548 THR B CB  1 
ATOM   3526 O OG1 . THR B 2 396 ? -35.884 -33.909 13.646 1.00 29.21 ? 548 THR B OG1 1 
ATOM   3527 C CG2 . THR B 2 396 ? -35.441 -31.533 13.856 1.00 27.24 ? 548 THR B CG2 1 
ATOM   3528 N N   . ARG B 2 397 ? -35.622 -30.207 10.945 1.00 28.03 ? 549 ARG B N   1 
ATOM   3529 C CA  . ARG B 2 397 ? -35.128 -29.013 10.235 1.00 33.61 ? 549 ARG B CA  1 
ATOM   3530 C C   . ARG B 2 397 ? -35.327 -27.726 11.037 1.00 29.58 ? 549 ARG B C   1 
ATOM   3531 O O   . ARG B 2 397 ? -36.300 -27.592 11.768 1.00 27.97 ? 549 ARG B O   1 
ATOM   3532 C CB  . ARG B 2 397 ? -35.871 -28.863 8.907  1.00 38.36 ? 549 ARG B CB  1 
ATOM   3533 C CG  . ARG B 2 397 ? -35.557 -29.979 7.954  1.00 41.45 ? 549 ARG B CG  1 
ATOM   3534 C CD  . ARG B 2 397 ? -36.091 -29.728 6.571  1.00 42.84 ? 549 ARG B CD  1 
ATOM   3535 N NE  . ARG B 2 397 ? -35.805 -30.896 5.745  1.00 52.13 ? 549 ARG B NE  1 
ATOM   3536 C CZ  . ARG B 2 397 ? -35.283 -30.834 4.525  1.00 51.43 ? 549 ARG B CZ  1 
ATOM   3537 N NH1 . ARG B 2 397 ? -35.003 -29.649 3.985  1.00 49.30 ? 549 ARG B NH1 1 
ATOM   3538 N NH2 . ARG B 2 397 ? -35.035 -31.954 3.851  1.00 46.60 ? 549 ARG B NH2 1 
ATOM   3539 N N   . VAL B 2 398 ? -34.409 -26.767 10.878 1.00 26.99 ? 550 VAL B N   1 
ATOM   3540 C CA  . VAL B 2 398 ? -34.518 -25.455 11.516 1.00 21.30 ? 550 VAL B CA  1 
ATOM   3541 C C   . VAL B 2 398 ? -33.740 -24.431 10.677 1.00 27.81 ? 550 VAL B C   1 
ATOM   3542 O O   . VAL B 2 398 ? -32.725 -24.764 10.070 1.00 26.81 ? 550 VAL B O   1 
ATOM   3543 C CB  . VAL B 2 398 ? -33.980 -25.489 12.977 1.00 22.75 ? 550 VAL B CB  1 
ATOM   3544 C CG1 . VAL B 2 398 ? -32.445 -25.420 13.026 1.00 27.44 ? 550 VAL B CG1 1 
ATOM   3545 C CG2 . VAL B 2 398 ? -34.547 -24.347 13.768 1.00 26.25 ? 550 VAL B CG2 1 
ATOM   3546 N N   . HIS B 2 399 ? -34.208 -23.187 10.632 1.00 30.54 ? 551 HIS B N   1 
ATOM   3547 C CA  . HIS B 2 399 ? -33.523 -22.177 9.819  1.00 33.22 ? 551 HIS B CA  1 
ATOM   3548 C C   . HIS B 2 399 ? -33.396 -20.814 10.478 1.00 32.38 ? 551 HIS B C   1 
ATOM   3549 O O   . HIS B 2 399 ? -34.084 -20.511 11.449 1.00 35.04 ? 551 HIS B O   1 
ATOM   3550 C CB  . HIS B 2 399 ? -34.198 -22.041 8.456  1.00 39.01 ? 551 HIS B CB  1 
ATOM   3551 C CG  . HIS B 2 399 ? -35.541 -21.391 8.531  1.00 39.70 ? 551 HIS B CG  1 
ATOM   3552 N ND1 . HIS B 2 399 ? -36.694 -22.087 8.821  1.00 43.00 ? 551 HIS B ND1 1 
ATOM   3553 C CD2 . HIS B 2 399 ? -35.909 -20.096 8.387  1.00 41.15 ? 551 HIS B CD2 1 
ATOM   3554 C CE1 . HIS B 2 399 ? -37.719 -21.252 8.833  1.00 45.91 ? 551 HIS B CE1 1 
ATOM   3555 N NE2 . HIS B 2 399 ? -37.269 -20.036 8.575  1.00 45.16 ? 551 HIS B NE2 1 
ATOM   3556 N N   . CYS B 2 400 ? -32.464 -20.010 9.987  1.00 31.06 ? 552 CYS B N   1 
ATOM   3557 C CA  . CYS B 2 400 ? -32.346 -18.643 10.470 1.00 33.90 ? 552 CYS B CA  1 
ATOM   3558 C C   . CYS B 2 400 ? -33.387 -17.760 9.789  1.00 40.50 ? 552 CYS B C   1 
ATOM   3559 O O   . CYS B 2 400 ? -33.171 -17.292 8.673  1.00 49.63 ? 552 CYS B O   1 
ATOM   3560 C CB  . CYS B 2 400 ? -30.956 -18.087 10.147 1.00 35.80 ? 552 CYS B CB  1 
ATOM   3561 S SG  . CYS B 2 400 ? -29.568 -19.082 10.751 1.00 31.42 ? 552 CYS B SG  1 
ATOM   3562 N N   . HIS B 2 401 ? -34.525 -17.571 10.448 1.00 38.69 ? 553 HIS B N   1 
ATOM   3563 C CA  . HIS B 2 401 ? -35.709 -16.945 9.846  1.00 44.54 ? 553 HIS B CA  1 
ATOM   3564 C C   . HIS B 2 401 ? -35.704 -15.409 9.856  1.00 41.50 ? 553 HIS B C   1 
ATOM   3565 O O   . HIS B 2 401 ? -34.912 -14.766 10.548 1.00 44.37 ? 553 HIS B O   1 
ATOM   3566 C CB  . HIS B 2 401 ? -36.974 -17.477 10.545 1.00 44.23 ? 553 HIS B CB  1 
ATOM   3567 C CG  . HIS B 2 401 ? -37.093 -17.084 11.981 1.00 45.41 ? 553 HIS B CG  1 
ATOM   3568 N ND1 . HIS B 2 401 ? -37.529 -15.845 12.392 1.00 51.97 ? 553 HIS B ND1 1 
ATOM   3569 C CD2 . HIS B 2 401 ? -36.825 -17.784 13.111 1.00 42.14 ? 553 HIS B CD2 1 
ATOM   3570 C CE1 . HIS B 2 401 ? -37.525 -15.797 13.713 1.00 43.76 ? 553 HIS B CE1 1 
ATOM   3571 N NE2 . HIS B 2 401 ? -37.099 -16.959 14.174 1.00 42.60 ? 553 HIS B NE2 1 
ATOM   3572 N N   . HIS B 2 405 ? -30.081 -12.303 8.860  1.00 40.07 ? 557 HIS B N   1 
ATOM   3573 C CA  . HIS B 2 405 ? -29.237 -13.265 9.561  1.00 37.37 ? 557 HIS B CA  1 
ATOM   3574 C C   . HIS B 2 405 ? -28.586 -14.276 8.606  1.00 35.41 ? 557 HIS B C   1 
ATOM   3575 O O   . HIS B 2 405 ? -29.212 -14.739 7.650  1.00 39.46 ? 557 HIS B O   1 
ATOM   3576 C CB  . HIS B 2 405 ? -30.015 -13.966 10.693 1.00 37.33 ? 557 HIS B CB  1 
ATOM   3577 C CG  . HIS B 2 405 ? -30.079 -13.180 11.970 1.00 37.76 ? 557 HIS B CG  1 
ATOM   3578 N ND1 . HIS B 2 405 ? -29.740 -13.721 13.192 1.00 41.08 ? 557 HIS B ND1 1 
ATOM   3579 C CD2 . HIS B 2 405 ? -30.440 -11.897 12.217 1.00 41.85 ? 557 HIS B CD2 1 
ATOM   3580 C CE1 . HIS B 2 405 ? -29.884 -12.807 14.136 1.00 42.04 ? 557 HIS B CE1 1 
ATOM   3581 N NE2 . HIS B 2 405 ? -30.307 -11.690 13.571 1.00 40.92 ? 557 HIS B NE2 1 
ATOM   3582 N N   . VAL B 2 406 ? -27.330 -14.623 8.888  1.00 31.53 ? 558 VAL B N   1 
ATOM   3583 C CA  . VAL B 2 406 ? -26.580 -15.651 8.149  1.00 27.03 ? 558 VAL B CA  1 
ATOM   3584 C C   . VAL B 2 406 ? -26.380 -16.864 9.045  1.00 24.32 ? 558 VAL B C   1 
ATOM   3585 O O   . VAL B 2 406 ? -26.098 -16.718 10.231 1.00 20.30 ? 558 VAL B O   1 
ATOM   3586 C CB  . VAL B 2 406 ? -25.206 -15.123 7.628  1.00 26.75 ? 558 VAL B CB  1 
ATOM   3587 C CG1 . VAL B 2 406 ? -25.403 -13.899 6.774  1.00 31.99 ? 558 VAL B CG1 1 
ATOM   3588 C CG2 . VAL B 2 406 ? -24.246 -14.822 8.768  1.00 25.89 ? 558 VAL B CG2 1 
ATOM   3589 N N   . LEU B 2 407 ? -26.505 -18.058 8.473  1.00 23.66 ? 559 LEU B N   1 
ATOM   3590 C CA  . LEU B 2 407 ? -26.187 -19.284 9.193  1.00 22.91 ? 559 LEU B CA  1 
ATOM   3591 C C   . LEU B 2 407 ? -24.685 -19.545 9.194  1.00 20.65 ? 559 LEU B C   1 
ATOM   3592 O O   . LEU B 2 407 ? -24.051 -19.602 8.132  1.00 21.94 ? 559 LEU B O   1 
ATOM   3593 C CB  . LEU B 2 407 ? -26.875 -20.455 8.519  1.00 20.42 ? 559 LEU B CB  1 
ATOM   3594 C CG  . LEU B 2 407 ? -26.542 -21.875 9.002  1.00 21.60 ? 559 LEU B CG  1 
ATOM   3595 C CD1 . LEU B 2 407 ? -27.207 -22.164 10.341 1.00 20.69 ? 559 LEU B CD1 1 
ATOM   3596 C CD2 . LEU B 2 407 ? -26.897 -22.922 7.958  1.00 21.39 ? 559 LEU B CD2 1 
ATOM   3597 N N   . THR B 2 408 ? -24.119 -19.730 10.384 1.00 18.60 ? 560 THR B N   1 
ATOM   3598 C CA  . THR B 2 408 ? -22.672 -19.939 10.515 1.00 19.00 ? 560 THR B CA  1 
ATOM   3599 C C   . THR B 2 408 ? -22.332 -21.368 10.974 1.00 16.41 ? 560 THR B C   1 
ATOM   3600 O O   . THR B 2 408 ? -21.180 -21.778 10.888 1.00 13.92 ? 560 THR B O   1 
ATOM   3601 C CB  . THR B 2 408 ? -22.064 -18.953 11.533 1.00 17.10 ? 560 THR B CB  1 
ATOM   3602 O OG1 . THR B 2 408 ? -22.581 -19.207 12.846 1.00 13.92 ? 560 THR B OG1 1 
ATOM   3603 C CG2 . THR B 2 408 ? -22.383 -17.494 11.144 1.00 17.65 ? 560 THR B CG2 1 
ATOM   3604 N N   . GLY B 2 409 ? -23.321 -22.145 11.408 1.00 15.19 ? 561 GLY B N   1 
ATOM   3605 C CA  . GLY B 2 409 ? -23.049 -23.436 12.045 1.00 14.58 ? 561 GLY B CA  1 
ATOM   3606 C C   . GLY B 2 409 ? -24.292 -24.269 12.292 1.00 17.99 ? 561 GLY B C   1 
ATOM   3607 O O   . GLY B 2 409 ? -25.338 -23.728 12.618 1.00 14.77 ? 561 GLY B O   1 
ATOM   3608 N N   . CYS B 2 410 ? -24.200 -25.578 12.034 1.00 19.36 ? 562 CYS B N   1 
ATOM   3609 C CA  . CYS B 2 410 ? -25.238 -26.545 12.436 1.00 17.93 ? 562 CYS B CA  1 
ATOM   3610 C C   . CYS B 2 410 ? -24.725 -27.524 13.470 1.00 20.34 ? 562 CYS B C   1 
ATOM   3611 O O   . CYS B 2 410 ? -23.620 -28.044 13.335 1.00 17.78 ? 562 CYS B O   1 
ATOM   3612 C CB  . CYS B 2 410 ? -25.717 -27.361 11.234 1.00 17.67 ? 562 CYS B CB  1 
ATOM   3613 S SG  . CYS B 2 410 ? -26.437 -26.358 9.916  1.00 25.46 ? 562 CYS B SG  1 
ATOM   3614 N N   . SER B 2 411 ? -25.538 -27.783 14.493 1.00 16.40 ? 563 SER B N   1 
ATOM   3615 C CA  . SER B 2 411 ? -25.266 -28.823 15.467 1.00 16.09 ? 563 SER B CA  1 
ATOM   3616 C C   . SER B 2 411 ? -26.481 -29.712 15.659 1.00 17.00 ? 563 SER B C   1 
ATOM   3617 O O   . SER B 2 411 ? -27.595 -29.337 15.284 1.00 14.39 ? 563 SER B O   1 
ATOM   3618 C CB  . SER B 2 411 ? -24.924 -28.193 16.826 1.00 14.71 ? 563 SER B CB  1 
ATOM   3619 O OG  . SER B 2 411 ? -23.782 -27.351 16.733 1.00 21.69 ? 563 SER B OG  1 
ATOM   3620 N N   . SER B 2 412 ? -26.279 -30.892 16.226 1.00 13.96 ? 564 SER B N   1 
ATOM   3621 C CA  . SER B 2 412 ? -27.398 -31.811 16.473 1.00 18.92 ? 564 SER B CA  1 
ATOM   3622 C C   . SER B 2 412 ? -27.060 -32.655 17.692 1.00 17.97 ? 564 SER B C   1 
ATOM   3623 O O   . SER B 2 412 ? -25.924 -33.149 17.794 1.00 15.33 ? 564 SER B O   1 
ATOM   3624 C CB  . SER B 2 412 ? -27.627 -32.715 15.270 1.00 18.06 ? 564 SER B CB  1 
ATOM   3625 O OG  . SER B 2 412 ? -28.797 -33.492 15.454 1.00 24.71 ? 564 SER B OG  1 
ATOM   3626 N N   . HIS B 2 413 ? -28.000 -32.812 18.622 1.00 14.63 ? 565 HIS B N   1 
ATOM   3627 C CA  . HIS B 2 413 ? -27.833 -33.826 19.659 1.00 17.43 ? 565 HIS B CA  1 
ATOM   3628 C C   . HIS B 2 413 ? -29.097 -34.698 19.758 1.00 19.88 ? 565 HIS B C   1 
ATOM   3629 O O   . HIS B 2 413 ? -30.187 -34.293 19.336 1.00 17.08 ? 565 HIS B O   1 
ATOM   3630 C CB  . HIS B 2 413 ? -27.476 -33.209 21.025 1.00 16.53 ? 565 HIS B CB  1 
ATOM   3631 C CG  . HIS B 2 413 ? -28.649 -32.671 21.780 1.00 18.79 ? 565 HIS B CG  1 
ATOM   3632 N ND1 . HIS B 2 413 ? -29.318 -31.515 21.426 1.00 21.90 ? 565 HIS B ND1 1 
ATOM   3633 C CD2 . HIS B 2 413 ? -29.304 -33.165 22.859 1.00 22.20 ? 565 HIS B CD2 1 
ATOM   3634 C CE1 . HIS B 2 413 ? -30.321 -31.310 22.268 1.00 21.22 ? 565 HIS B CE1 1 
ATOM   3635 N NE2 . HIS B 2 413 ? -30.338 -32.300 23.143 1.00 21.81 ? 565 HIS B NE2 1 
ATOM   3636 N N   . TRP B 2 414 ? -28.944 -35.900 20.301 1.00 20.58 ? 566 TRP B N   1 
ATOM   3637 C CA  . TRP B 2 414 ? -30.068 -36.802 20.500 1.00 23.16 ? 566 TRP B CA  1 
ATOM   3638 C C   . TRP B 2 414 ? -30.038 -37.395 21.898 1.00 28.59 ? 566 TRP B C   1 
ATOM   3639 O O   . TRP B 2 414 ? -28.995 -37.399 22.557 1.00 26.28 ? 566 TRP B O   1 
ATOM   3640 C CB  . TRP B 2 414 ? -30.107 -37.883 19.415 1.00 22.77 ? 566 TRP B CB  1 
ATOM   3641 C CG  . TRP B 2 414 ? -28.757 -38.540 19.147 1.00 25.96 ? 566 TRP B CG  1 
ATOM   3642 C CD1 . TRP B 2 414 ? -28.319 -39.732 19.659 1.00 27.11 ? 566 TRP B CD1 1 
ATOM   3643 C CD2 . TRP B 2 414 ? -27.712 -38.075 18.274 1.00 24.71 ? 566 TRP B CD2 1 
ATOM   3644 N NE1 . TRP B 2 414 ? -27.050 -40.015 19.201 1.00 22.26 ? 566 TRP B NE1 1 
ATOM   3645 C CE2 . TRP B 2 414 ? -26.662 -39.027 18.335 1.00 22.95 ? 566 TRP B CE2 1 
ATOM   3646 C CE3 . TRP B 2 414 ? -27.551 -36.943 17.464 1.00 24.97 ? 566 TRP B CE3 1 
ATOM   3647 C CZ2 . TRP B 2 414 ? -25.470 -38.878 17.622 1.00 25.12 ? 566 TRP B CZ2 1 
ATOM   3648 C CZ3 . TRP B 2 414 ? -26.362 -36.793 16.745 1.00 23.20 ? 566 TRP B CZ3 1 
ATOM   3649 C CH2 . TRP B 2 414 ? -25.339 -37.762 16.828 1.00 22.62 ? 566 TRP B CH2 1 
ATOM   3650 N N   . GLU B 2 415 ? -31.165 -37.904 22.363 1.00 30.38 ? 567 GLU B N   1 
ATOM   3651 C CA  . GLU B 2 415 ? -31.164 -38.522 23.675 1.00 33.64 ? 567 GLU B CA  1 
ATOM   3652 C C   . GLU B 2 415 ? -31.391 -40.026 23.521 1.00 36.58 ? 567 GLU B C   1 
ATOM   3653 O O   . GLU B 2 415 ? -31.352 -40.766 24.493 1.00 43.91 ? 567 GLU B O   1 
ATOM   3654 C CB  . GLU B 2 415 ? -32.171 -37.836 24.615 1.00 40.16 ? 567 GLU B CB  1 
ATOM   3655 C CG  . GLU B 2 415 ? -31.565 -36.647 25.355 1.00 38.94 ? 567 GLU B CG  1 
ATOM   3656 C CD  . GLU B 2 415 ? -32.526 -35.509 25.585 1.00 49.44 ? 567 GLU B CD  1 
ATOM   3657 O OE1 . GLU B 2 415 ? -32.908 -35.309 26.761 1.00 57.54 ? 567 GLU B OE1 1 
ATOM   3658 O OE2 . GLU B 2 415 ? -32.838 -34.767 24.623 1.00 50.48 ? 567 GLU B OE2 1 
ATOM   3659 N N   . VAL B 2 416 ? -31.637 -40.468 22.290 1.00 38.36 ? 568 VAL B N   1 
ATOM   3660 C CA  . VAL B 2 416 ? -31.865 -41.884 22.006 1.00 45.93 ? 568 VAL B CA  1 
ATOM   3661 C C   . VAL B 2 416 ? -30.532 -42.637 21.892 1.00 49.99 ? 568 VAL B C   1 
ATOM   3662 O O   . VAL B 2 416 ? -29.493 -42.045 21.594 1.00 43.76 ? 568 VAL B O   1 
ATOM   3663 C CB  . VAL B 2 416 ? -32.684 -42.070 20.697 1.00 49.18 ? 568 VAL B CB  1 
ATOM   3664 C CG1 . VAL B 2 416 ? -31.889 -41.624 19.476 1.00 43.40 ? 568 VAL B CG1 1 
ATOM   3665 C CG2 . VAL B 2 416 ? -33.179 -43.510 20.541 1.00 52.62 ? 568 VAL B CG2 1 
ATOM   3666 N N   . GLU B 2 417 ? -30.579 -43.939 22.160 1.00 56.73 ? 569 GLU B N   1 
ATOM   3667 C CA  . GLU B 2 417 ? -29.437 -44.857 22.085 1.00 56.92 ? 569 GLU B CA  1 
ATOM   3668 C C   . GLU B 2 417 ? -28.907 -45.153 20.659 1.00 57.66 ? 569 GLU B C   1 
ATOM   3669 O O   . GLU B 2 417 ? -27.699 -45.289 20.453 1.00 57.73 ? 569 GLU B O   1 
ATOM   3670 C CB  . GLU B 2 417 ? -29.816 -46.170 22.775 1.00 62.56 ? 569 GLU B CB  1 
ATOM   3671 C CG  . GLU B 2 417 ? -30.461 -45.941 24.151 1.00 67.29 ? 569 GLU B CG  1 
ATOM   3672 C CD  . GLU B 2 417 ? -29.739 -46.603 25.324 1.00 72.13 ? 569 GLU B CD  1 
ATOM   3673 O OE1 . GLU B 2 417 ? -28.986 -47.581 25.119 1.00 72.35 ? 569 GLU B OE1 1 
ATOM   3674 O OE2 . GLU B 2 417 ? -29.946 -46.140 26.470 1.00 70.73 ? 569 GLU B OE2 1 
ATOM   3675 N N   . ASP B 2 418 ? -29.818 -45.230 19.686 1.00 61.07 ? 570 ASP B N   1 
ATOM   3676 C CA  . ASP B 2 418 ? -29.487 -45.360 18.255 1.00 62.82 ? 570 ASP B CA  1 
ATOM   3677 C C   . ASP B 2 418 ? -30.680 -44.937 17.377 1.00 64.80 ? 570 ASP B C   1 
ATOM   3678 O O   . ASP B 2 418 ? -31.775 -44.723 17.901 1.00 66.44 ? 570 ASP B O   1 
ATOM   3679 C CB  . ASP B 2 418 ? -29.041 -46.794 17.929 1.00 64.65 ? 570 ASP B CB  1 
ATOM   3680 C CG  . ASP B 2 418 ? -27.916 -46.852 16.901 1.00 69.28 ? 570 ASP B CG  1 
ATOM   3681 O OD1 . ASP B 2 418 ? -27.889 -46.001 15.985 1.00 68.80 ? 570 ASP B OD1 1 
ATOM   3682 O OD2 . ASP B 2 418 ? -27.055 -47.759 17.012 1.00 66.91 ? 570 ASP B OD2 1 
ATOM   3683 N N   . LEU B 2 419 ? -30.488 -44.800 16.061 1.00 65.11 ? 571 LEU B N   1 
ATOM   3684 C CA  . LEU B 2 419 ? -31.596 -44.373 15.189 1.00 62.75 ? 571 LEU B CA  1 
ATOM   3685 C C   . LEU B 2 419 ? -32.725 -45.395 15.090 1.00 64.31 ? 571 LEU B C   1 
ATOM   3686 O O   . LEU B 2 419 ? -33.403 -45.476 14.060 1.00 64.61 ? 571 LEU B O   1 
ATOM   3687 C CB  . LEU B 2 419 ? -31.103 -44.040 13.769 1.00 63.57 ? 571 LEU B CB  1 
ATOM   3688 C CG  . LEU B 2 419 ? -30.326 -44.958 12.808 1.00 69.49 ? 571 LEU B CG  1 
ATOM   3689 C CD1 . LEU B 2 419 ? -30.541 -46.458 13.036 1.00 63.66 ? 571 LEU B CD1 1 
ATOM   3690 C CD2 . LEU B 2 419 ? -30.714 -44.592 11.371 1.00 66.86 ? 571 LEU B CD2 1 
ATOM   3691 N N   . PRO B 2 433 ? -29.998 -23.829 2.925  1.00 44.63 ? 585 PRO B N   1 
ATOM   3692 C CA  . PRO B 2 433 ? -30.660 -22.526 2.728  1.00 40.01 ? 585 PRO B CA  1 
ATOM   3693 C C   . PRO B 2 433 ? -30.737 -21.579 3.959  1.00 41.76 ? 585 PRO B C   1 
ATOM   3694 O O   . PRO B 2 433 ? -31.830 -21.088 4.285  1.00 38.66 ? 585 PRO B O   1 
ATOM   3695 C CB  . PRO B 2 433 ? -32.065 -22.875 2.192  1.00 43.45 ? 585 PRO B CB  1 
ATOM   3696 C CG  . PRO B 2 433 ? -32.208 -24.393 2.398  1.00 38.91 ? 585 PRO B CG  1 
ATOM   3697 C CD  . PRO B 2 433 ? -30.799 -24.945 2.377  1.00 45.15 ? 585 PRO B CD  1 
ATOM   3698 N N   . ASN B 2 434 ? -29.600 -21.317 4.617  1.00 35.07 ? 586 ASN B N   1 
ATOM   3699 C CA  . ASN B 2 434 ? -29.627 -20.888 6.024  1.00 32.70 ? 586 ASN B CA  1 
ATOM   3700 C C   . ASN B 2 434 ? -30.409 -21.882 6.871  1.00 31.05 ? 586 ASN B C   1 
ATOM   3701 O O   . ASN B 2 434 ? -30.965 -21.518 7.903  1.00 27.43 ? 586 ASN B O   1 
ATOM   3702 C CB  . ASN B 2 434 ? -30.141 -19.451 6.195  1.00 35.69 ? 586 ASN B CB  1 
ATOM   3703 C CG  . ASN B 2 434 ? -29.200 -18.420 5.605  1.00 44.84 ? 586 ASN B CG  1 
ATOM   3704 O OD1 . ASN B 2 434 ? -28.036 -18.725 5.299  1.00 45.80 ? 586 ASN B OD1 1 
ATOM   3705 N ND2 . ASN B 2 434 ? -29.676 -17.182 5.480  1.00 46.41 ? 586 ASN B ND2 1 
ATOM   3706 N N   . GLN B 2 435 ? -30.461 -23.125 6.391  1.00 33.02 ? 587 GLN B N   1 
ATOM   3707 C CA  . GLN B 2 435 ? -31.160 -24.233 7.033  1.00 30.62 ? 587 GLN B CA  1 
ATOM   3708 C C   . GLN B 2 435 ? -30.263 -25.373 7.508  1.00 31.21 ? 587 GLN B C   1 
ATOM   3709 O O   . GLN B 2 435 ? -29.362 -25.806 6.784  1.00 31.60 ? 587 GLN B O   1 
ATOM   3710 C CB  . GLN B 2 435 ? -32.167 -24.811 6.061  1.00 31.66 ? 587 GLN B CB  1 
ATOM   3711 C CG  . GLN B 2 435 ? -33.140 -25.732 6.679  1.00 30.51 ? 587 GLN B CG  1 
ATOM   3712 C CD  . GLN B 2 435 ? -34.257 -26.062 5.729  1.00 33.50 ? 587 GLN B CD  1 
ATOM   3713 O OE1 . GLN B 2 435 ? -35.379 -25.585 5.890  1.00 35.68 ? 587 GLN B OE1 1 
ATOM   3714 N NE2 . GLN B 2 435 ? -33.958 -26.890 4.732  1.00 37.65 ? 587 GLN B NE2 1 
ATOM   3715 N N   . CYS B 2 436 ? -30.505 -25.868 8.718  1.00 26.63 ? 588 CYS B N   1 
ATOM   3716 C CA  . CYS B 2 436 ? -29.843 -27.086 9.165  1.00 25.47 ? 588 CYS B CA  1 
ATOM   3717 C C   . CYS B 2 436 ? -30.831 -28.228 9.140  1.00 27.11 ? 588 CYS B C   1 
ATOM   3718 O O   . CYS B 2 436 ? -31.994 -28.060 9.475  1.00 27.74 ? 588 CYS B O   1 
ATOM   3719 C CB  . CYS B 2 436 ? -29.349 -26.911 10.598 1.00 20.23 ? 588 CYS B CB  1 
ATOM   3720 S SG  . CYS B 2 436 ? -28.130 -25.591 10.750 1.00 22.26 ? 588 CYS B SG  1 
ATOM   3721 N N   . VAL B 2 437 ? -30.350 -29.410 8.791  1.00 28.66 ? 589 VAL B N   1 
ATOM   3722 C CA  . VAL B 2 437 ? -31.203 -30.580 8.769  1.00 30.33 ? 589 VAL B CA  1 
ATOM   3723 C C   . VAL B 2 437 ? -30.569 -31.700 9.556  1.00 29.09 ? 589 VAL B C   1 
ATOM   3724 O O   . VAL B 2 437 ? -29.386 -31.974 9.402  1.00 28.70 ? 589 VAL B O   1 
ATOM   3725 C CB  . VAL B 2 437 ? -31.426 -31.048 7.324  1.00 35.34 ? 589 VAL B CB  1 
ATOM   3726 C CG1 . VAL B 2 437 ? -32.232 -32.323 7.319  1.00 38.04 ? 589 VAL B CG1 1 
ATOM   3727 C CG2 . VAL B 2 437 ? -32.148 -29.970 6.526  1.00 35.99 ? 589 VAL B CG2 1 
ATOM   3728 N N   . GLY B 2 438 ? -31.338 -32.278 10.472 1.00 28.95 ? 590 GLY B N   1 
ATOM   3729 C CA  . GLY B 2 438 ? -30.911 -33.435 11.249 1.00 32.84 ? 590 GLY B CA  1 
ATOM   3730 C C   . GLY B 2 438 ? -31.738 -34.709 11.120 1.00 32.81 ? 590 GLY B C   1 
ATOM   3731 O O   . GLY B 2 438 ? -32.729 -34.774 10.381 1.00 33.63 ? 590 GLY B O   1 
ATOM   3732 N N   . HIS B 2 439 ? -31.306 -35.736 11.848 1.00 30.95 ? 591 HIS B N   1 
ATOM   3733 C CA  . HIS B 2 439 ? -32.083 -36.959 12.004 1.00 34.23 ? 591 HIS B CA  1 
ATOM   3734 C C   . HIS B 2 439 ? -33.440 -36.716 12.672 1.00 31.03 ? 591 HIS B C   1 
ATOM   3735 O O   . HIS B 2 439 ? -33.612 -35.817 13.509 1.00 28.38 ? 591 HIS B O   1 
ATOM   3736 C CB  . HIS B 2 439 ? -31.296 -37.961 12.848 1.00 32.09 ? 591 HIS B CB  1 
ATOM   3737 C CG  . HIS B 2 439 ? -31.845 -39.348 12.794 1.00 34.85 ? 591 HIS B CG  1 
ATOM   3738 N ND1 . HIS B 2 439 ? -32.937 -39.740 13.539 1.00 42.52 ? 591 HIS B ND1 1 
ATOM   3739 C CD2 . HIS B 2 439 ? -31.461 -40.440 12.091 1.00 46.88 ? 591 HIS B CD2 1 
ATOM   3740 C CE1 . HIS B 2 439 ? -33.203 -41.013 13.298 1.00 40.71 ? 591 HIS B CE1 1 
ATOM   3741 N NE2 . HIS B 2 439 ? -32.323 -41.461 12.421 1.00 47.30 ? 591 HIS B NE2 1 
ATOM   3742 N N   . ARG B 2 440 ? -34.410 -37.540 12.301 1.00 33.71 ? 592 ARG B N   1 
ATOM   3743 C CA  . ARG B 2 440 ? -35.779 -37.352 12.752 1.00 32.10 ? 592 ARG B CA  1 
ATOM   3744 C C   . ARG B 2 440 ? -35.912 -37.504 14.272 1.00 26.92 ? 592 ARG B C   1 
ATOM   3745 O O   . ARG B 2 440 ? -36.792 -36.911 14.887 1.00 30.29 ? 592 ARG B O   1 
ATOM   3746 C CB  . ARG B 2 440 ? -36.689 -38.345 12.004 1.00 40.63 ? 592 ARG B CB  1 
ATOM   3747 C CG  . ARG B 2 440 ? -36.513 -39.817 12.343 1.00 43.36 ? 592 ARG B CG  1 
ATOM   3748 C CD  . ARG B 2 440 ? -36.943 -40.721 11.160 1.00 50.17 ? 592 ARG B CD  1 
ATOM   3749 N NE  . ARG B 2 440 ? -38.382 -40.966 11.067 1.00 60.46 ? 592 ARG B NE  1 
ATOM   3750 C CZ  . ARG B 2 440 ? -38.985 -41.492 10.000 1.00 60.51 ? 592 ARG B CZ  1 
ATOM   3751 N NH1 . ARG B 2 440 ? -38.271 -41.833 8.930  1.00 60.62 ? 592 ARG B NH1 1 
ATOM   3752 N NH2 . ARG B 2 440 ? -40.299 -41.677 9.999  1.00 50.39 ? 592 ARG B NH2 1 
ATOM   3753 N N   . GLU B 2 441 ? -35.000 -38.249 14.882 1.00 26.29 ? 593 GLU B N   1 
ATOM   3754 C CA  . GLU B 2 441 ? -34.995 -38.467 16.328 1.00 24.40 ? 593 GLU B CA  1 
ATOM   3755 C C   . GLU B 2 441 ? -34.030 -37.529 17.068 1.00 25.32 ? 593 GLU B C   1 
ATOM   3756 O O   . GLU B 2 441 ? -33.846 -37.654 18.291 1.00 19.82 ? 593 GLU B O   1 
ATOM   3757 C CB  . GLU B 2 441 ? -34.580 -39.902 16.609 1.00 33.24 ? 593 GLU B CB  1 
ATOM   3758 C CG  . GLU B 2 441 ? -35.426 -40.935 15.893 1.00 37.69 ? 593 GLU B CG  1 
ATOM   3759 C CD  . GLU B 2 441 ? -35.067 -42.345 16.320 1.00 46.88 ? 593 GLU B CD  1 
ATOM   3760 O OE1 . GLU B 2 441 ? -34.463 -43.071 15.507 1.00 49.78 ? 593 GLU B OE1 1 
ATOM   3761 O OE2 . GLU B 2 441 ? -35.353 -42.714 17.481 1.00 51.48 ? 593 GLU B OE2 1 
ATOM   3762 N N   . ALA B 2 442 ? -33.420 -36.587 16.349 1.00 20.95 ? 594 ALA B N   1 
ATOM   3763 C CA  . ALA B 2 442 ? -32.421 -35.706 16.959 1.00 20.57 ? 594 ALA B CA  1 
ATOM   3764 C C   . ALA B 2 442 ? -32.909 -34.265 17.021 1.00 20.14 ? 594 ALA B C   1 
ATOM   3765 O O   . ALA B 2 442 ? -33.700 -33.842 16.175 1.00 17.44 ? 594 ALA B O   1 
ATOM   3766 C CB  . ALA B 2 442 ? -31.155 -35.749 16.121 1.00 22.15 ? 594 ALA B CB  1 
ATOM   3767 N N   . SER B 2 443 ? -32.423 -33.505 18.002 1.00 15.67 ? 595 SER B N   1 
ATOM   3768 C CA  . SER B 2 443 ? -32.636 -32.064 17.984 1.00 16.28 ? 595 SER B CA  1 
ATOM   3769 C C   . SER B 2 443 ? -31.617 -31.423 17.061 1.00 18.64 ? 595 SER B C   1 
ATOM   3770 O O   . SER B 2 443 ? -30.526 -31.964 16.877 1.00 17.56 ? 595 SER B O   1 
ATOM   3771 C CB  . SER B 2 443 ? -32.461 -31.455 19.386 1.00 17.70 ? 595 SER B CB  1 
ATOM   3772 O OG  . SER B 2 443 ? -33.369 -31.987 20.331 1.00 18.11 ? 595 SER B OG  1 
ATOM   3773 N N   . ILE B 2 444 ? -31.956 -30.291 16.455 1.00 18.56 ? 596 ILE B N   1 
ATOM   3774 C CA  . ILE B 2 444 ? -31.050 -29.669 15.485 1.00 17.78 ? 596 ILE B CA  1 
ATOM   3775 C C   . ILE B 2 444 ? -30.948 -28.208 15.903 1.00 19.91 ? 596 ILE B C   1 
ATOM   3776 O O   . ILE B 2 444 ? -31.949 -27.600 16.293 1.00 15.93 ? 596 ILE B O   1 
ATOM   3777 C CB  . ILE B 2 444 ? -31.518 -29.871 14.061 1.00 20.63 ? 596 ILE B CB  1 
ATOM   3778 C CG1 . ILE B 2 444 ? -32.765 -29.114 13.747 1.00 31.00 ? 596 ILE B CG1 1 
ATOM   3779 C CG2 . ILE B 2 444 ? -31.749 -31.365 13.772 1.00 29.37 ? 596 ILE B CG2 1 
ATOM   3780 C CD1 . ILE B 2 444 ? -32.688 -28.829 12.375 1.00 35.41 ? 596 ILE B CD1 1 
ATOM   3781 N N   . HIS B 2 445 ? -29.748 -27.643 15.816 1.00 15.68 ? 597 HIS B N   1 
ATOM   3782 C CA  . HIS B 2 445 ? -29.474 -26.299 16.311 1.00 15.66 ? 597 HIS B CA  1 
ATOM   3783 C C   . HIS B 2 445 ? -28.748 -25.493 15.257 1.00 20.56 ? 597 HIS B C   1 
ATOM   3784 O O   . HIS B 2 445 ? -27.804 -25.986 14.629 1.00 18.69 ? 597 HIS B O   1 
ATOM   3785 C CB  . HIS B 2 445 ? -28.594 -26.360 17.576 1.00 17.89 ? 597 HIS B CB  1 
ATOM   3786 C CG  . HIS B 2 445 ? -29.030 -27.391 18.570 1.00 18.68 ? 597 HIS B CG  1 
ATOM   3787 N ND1 . HIS B 2 445 ? -30.086 -27.204 19.433 1.00 19.50 ? 597 HIS B ND1 1 
ATOM   3788 C CD2 . HIS B 2 445 ? -28.559 -28.635 18.820 1.00 18.48 ? 597 HIS B CD2 1 
ATOM   3789 C CE1 . HIS B 2 445 ? -30.244 -28.287 20.178 1.00 19.22 ? 597 HIS B CE1 1 
ATOM   3790 N NE2 . HIS B 2 445 ? -29.338 -29.176 19.818 1.00 19.80 ? 597 HIS B NE2 1 
ATOM   3791 N N   . ALA B 2 446 ? -29.227 -24.283 15.002 1.00 20.58 ? 598 ALA B N   1 
ATOM   3792 C CA  . ALA B 2 446 ? -28.585 -23.432 14.002 1.00 19.89 ? 598 ALA B CA  1 
ATOM   3793 C C   . ALA B 2 446 ? -28.013 -22.240 14.711 1.00 21.10 ? 598 ALA B C   1 
ATOM   3794 O O   . ALA B 2 446 ? -28.696 -21.622 15.526 1.00 21.53 ? 598 ALA B O   1 
ATOM   3795 C CB  . ALA B 2 446 ? -29.590 -23.001 12.940 1.00 19.02 ? 598 ALA B CB  1 
ATOM   3796 N N   . SER B 2 447 ? -26.753 -21.910 14.411 1.00 19.10 ? 599 SER B N   1 
ATOM   3797 C CA  . SER B 2 447 ? -26.166 -20.652 14.868 1.00 17.55 ? 599 SER B CA  1 
ATOM   3798 C C   . SER B 2 447 ? -26.400 -19.624 13.796 1.00 21.26 ? 599 SER B C   1 
ATOM   3799 O O   . SER B 2 447 ? -25.963 -19.791 12.659 1.00 18.91 ? 599 SER B O   1 
ATOM   3800 C CB  . SER B 2 447 ? -24.663 -20.783 15.091 1.00 24.64 ? 599 SER B CB  1 
ATOM   3801 O OG  . SER B 2 447 ? -24.086 -19.480 15.207 1.00 27.13 ? 599 SER B OG  1 
ATOM   3802 N N   . CYS B 2 448 ? -27.126 -18.574 14.159 1.00 21.49 ? 600 CYS B N   1 
ATOM   3803 C CA  . CYS B 2 448 ? -27.544 -17.535 13.237 1.00 26.78 ? 600 CYS B CA  1 
ATOM   3804 C C   . CYS B 2 448 ? -26.992 -16.204 13.716 1.00 28.03 ? 600 CYS B C   1 
ATOM   3805 O O   . CYS B 2 448 ? -27.148 -15.846 14.883 1.00 27.76 ? 600 CYS B O   1 
ATOM   3806 C CB  . CYS B 2 448 ? -29.065 -17.447 13.261 1.00 26.97 ? 600 CYS B CB  1 
ATOM   3807 S SG  . CYS B 2 448 ? -29.861 -18.980 12.757 1.00 32.84 ? 600 CYS B SG  1 
ATOM   3808 N N   . CYS B 2 449 ? -26.273 -15.507 12.856 1.00 27.07 ? 601 CYS B N   1 
ATOM   3809 C CA  . CYS B 2 449 ? -25.732 -14.210 13.239 1.00 30.86 ? 601 CYS B CA  1 
ATOM   3810 C C   . CYS B 2 449 ? -26.218 -13.111 12.317 1.00 32.74 ? 601 CYS B C   1 
ATOM   3811 O O   . CYS B 2 449 ? -26.303 -13.251 11.098 1.00 29.99 ? 601 CYS B O   1 
ATOM   3812 C CB  . CYS B 2 449 ? -24.203 -14.216 13.176 1.00 32.30 ? 601 CYS B CB  1 
ATOM   3813 S SG  . CYS B 2 449 ? -23.450 -15.451 14.262 1.00 32.04 ? 601 CYS B SG  1 
ATOM   3814 N N   . HIS B 2 450 ? -26.470 -11.983 12.960 1.00 31.92 ? 602 HIS B N   1 
ATOM   3815 C CA  . HIS B 2 450 ? -26.618 -10.734 12.272 1.00 40.90 ? 602 HIS B CA  1 
ATOM   3816 C C   . HIS B 2 450 ? -25.270 -10.108 12.193 1.00 36.98 ? 602 HIS B C   1 
ATOM   3817 O O   . HIS B 2 450 ? -24.711 -9.612  13.169 1.00 36.60 ? 602 HIS B O   1 
ATOM   3818 C CB  . HIS B 2 450 ? -27.615 -9.812  12.980 1.00 46.26 ? 602 HIS B CB  1 
ATOM   3819 C CG  . HIS B 2 450 ? -28.107 -8.680  12.142 1.00 48.46 ? 602 HIS B CG  1 
ATOM   3820 N ND1 . HIS B 2 450 ? -28.545 -8.827  10.845 1.00 53.47 ? 602 HIS B ND1 1 
ATOM   3821 C CD2 . HIS B 2 450 ? -28.165 -7.353  12.412 1.00 52.33 ? 602 HIS B CD2 1 
ATOM   3822 C CE1 . HIS B 2 450 ? -28.884 -7.644  10.362 1.00 54.41 ? 602 HIS B CE1 1 
ATOM   3823 N NE2 . HIS B 2 450 ? -28.660 -6.731  11.292 1.00 51.72 ? 602 HIS B NE2 1 
ATOM   3824 N N   . ALA B 2 451 ? -24.758 -10.123 10.980 1.00 38.84 ? 603 ALA B N   1 
ATOM   3825 C CA  . ALA B 2 451 ? -23.424 -9.652  10.794 1.00 41.35 ? 603 ALA B CA  1 
ATOM   3826 C C   . ALA B 2 451 ? -23.320 -8.957  9.473  1.00 45.23 ? 603 ALA B C   1 
ATOM   3827 O O   . ALA B 2 451 ? -23.016 -9.585  8.457  1.00 39.62 ? 603 ALA B O   1 
ATOM   3828 C CB  . ALA B 2 451 ? -22.461 -10.850 10.832 1.00 41.36 ? 603 ALA B CB  1 
ATOM   3829 N N   . PRO B 2 452 ? -23.681 -7.674  9.460  1.00 50.95 ? 604 PRO B N   1 
ATOM   3830 C CA  . PRO B 2 452 ? -23.866 -7.057  8.155  1.00 51.88 ? 604 PRO B CA  1 
ATOM   3831 C C   . PRO B 2 452 ? -22.442 -6.994  7.617  1.00 48.28 ? 604 PRO B C   1 
ATOM   3832 O O   . PRO B 2 452 ? -21.539 -6.662  8.385  1.00 49.59 ? 604 PRO B O   1 
ATOM   3833 C CB  . PRO B 2 452 ? -24.540 -5.703  8.420  1.00 53.34 ? 604 PRO B CB  1 
ATOM   3834 C CG  . PRO B 2 452 ? -24.908 -5.750  9.916  1.00 53.44 ? 604 PRO B CG  1 
ATOM   3835 C CD  . PRO B 2 452 ? -23.957 -6.736  10.560 1.00 55.40 ? 604 PRO B CD  1 
ATOM   3836 N N   . GLY B 2 453 ? -22.219 -7.369  6.376  1.00 42.76 ? 605 GLY B N   1 
ATOM   3837 C CA  . GLY B 2 453 ? -20.923 -7.196  5.754  1.00 43.29 ? 605 GLY B CA  1 
ATOM   3838 C C   . GLY B 2 453 ? -20.278 -8.571  5.698  1.00 40.50 ? 605 GLY B C   1 
ATOM   3839 O O   . GLY B 2 453 ? -19.099 -8.707  5.373  1.00 42.59 ? 605 GLY B O   1 
ATOM   3840 N N   . LEU B 2 454 ? -21.063 -9.595  6.037  1.00 39.45 ? 606 LEU B N   1 
ATOM   3841 C CA  . LEU B 2 454 ? -20.536 -10.936 6.219  1.00 37.13 ? 606 LEU B CA  1 
ATOM   3842 C C   . LEU B 2 454 ? -21.234 -11.629 5.089  1.00 36.70 ? 606 LEU B C   1 
ATOM   3843 O O   . LEU B 2 454 ? -22.456 -11.572 4.999  1.00 34.35 ? 606 LEU B O   1 
ATOM   3844 C CB  . LEU B 2 454 ? -20.886 -11.560 7.567  1.00 38.46 ? 606 LEU B CB  1 
ATOM   3845 C CG  . LEU B 2 454 ? -19.765 -12.493 8.044  1.00 38.22 ? 606 LEU B CG  1 
ATOM   3846 C CD1 . LEU B 2 454 ? -18.477 -11.721 8.315  1.00 39.07 ? 606 LEU B CD1 1 
ATOM   3847 C CD2 . LEU B 2 454 ? -20.170 -13.306 9.263  1.00 37.80 ? 606 LEU B CD2 1 
ATOM   3848 N N   . GLU B 2 455 ? -20.493 -12.296 4.232  1.00 35.01 ? 607 GLU B N   1 
ATOM   3849 C CA  . GLU B 2 455 ? -21.119 -13.166 3.276  1.00 34.16 ? 607 GLU B CA  1 
ATOM   3850 C C   . GLU B 2 455 ? -20.790 -14.591 3.669  1.00 32.80 ? 607 GLU B C   1 
ATOM   3851 O O   . GLU B 2 455 ? -19.641 -14.870 4.011  1.00 26.66 ? 607 GLU B O   1 
ATOM   3852 C CB  . GLU B 2 455 ? -20.598 -12.817 1.879  1.00 33.73 ? 607 GLU B CB  1 
ATOM   3853 C CG  . GLU B 2 455 ? -20.964 -13.734 0.758  1.00 37.55 ? 607 GLU B CG  1 
ATOM   3854 C CD  . GLU B 2 455 ? -20.357 -13.270 -0.565 1.00 41.92 ? 607 GLU B CD  1 
ATOM   3855 O OE1 . GLU B 2 455 ? -19.455 -12.397 -0.535 1.00 43.99 ? 607 GLU B OE1 1 
ATOM   3856 O OE2 . GLU B 2 455 ? -20.780 -13.776 -1.632 1.00 42.08 ? 607 GLU B OE2 1 
ATOM   3857 N N   . CYS B 2 456 ? -21.769 -15.492 3.622  1.00 27.16 ? 608 CYS B N   1 
ATOM   3858 C CA  . CYS B 2 456 ? -21.485 -16.903 3.864  1.00 25.26 ? 608 CYS B CA  1 
ATOM   3859 C C   . CYS B 2 456 ? -22.077 -17.771 2.775  1.00 28.29 ? 608 CYS B C   1 
ATOM   3860 O O   . CYS B 2 456 ? -23.152 -17.473 2.230  1.00 26.73 ? 608 CYS B O   1 
ATOM   3861 C CB  . CYS B 2 456 ? -22.020 -17.381 5.222  1.00 27.56 ? 608 CYS B CB  1 
ATOM   3862 S SG  . CYS B 2 456 ? -21.461 -16.414 6.659  1.00 27.23 ? 608 CYS B SG  1 
ATOM   3863 N N   . LYS B 2 457 ? -21.366 -18.851 2.462  1.00 20.77 ? 609 LYS B N   1 
ATOM   3864 C CA  . LYS B 2 457 ? -21.860 -19.882 1.563  1.00 25.32 ? 609 LYS B CA  1 
ATOM   3865 C C   . LYS B 2 457 ? -21.638 -21.267 2.137  1.00 26.66 ? 609 LYS B C   1 
ATOM   3866 O O   . LYS B 2 457 ? -20.765 -21.463 2.986  1.00 25.59 ? 609 LYS B O   1 
ATOM   3867 C CB  . LYS B 2 457 ? -21.178 -19.782 0.206  1.00 27.29 ? 609 LYS B CB  1 
ATOM   3868 C CG  . LYS B 2 457 ? -21.436 -18.468 -0.515 1.00 30.32 ? 609 LYS B CG  1 
ATOM   3869 C CD  . LYS B 2 457 ? -20.834 -18.532 -1.891 1.00 28.73 ? 609 LYS B CD  1 
ATOM   3870 C CE  . LYS B 2 457 ? -21.334 -17.426 -2.783 1.00 28.28 ? 609 LYS B CE  1 
ATOM   3871 N NZ  . LYS B 2 457 ? -20.431 -17.371 -3.979 1.00 26.51 ? 609 LYS B NZ  1 
ATOM   3872 N N   . VAL B 2 458 ? -22.352 -22.240 1.588  1.00 23.38 ? 610 VAL B N   1 
ATOM   3873 C CA  . VAL B 2 458 ? -22.244 -23.619 2.021  1.00 24.65 ? 610 VAL B CA  1 
ATOM   3874 C C   . VAL B 2 458 ? -21.724 -24.517 0.898  1.00 27.70 ? 610 VAL B C   1 
ATOM   3875 O O   . VAL B 2 458 ? -22.254 -24.523 -0.208 1.00 30.72 ? 610 VAL B O   1 
ATOM   3876 C CB  . VAL B 2 458 ? -23.618 -24.148 2.477  1.00 26.77 ? 610 VAL B CB  1 
ATOM   3877 C CG1 . VAL B 2 458 ? -23.483 -25.568 2.966  1.00 30.02 ? 610 VAL B CG1 1 
ATOM   3878 C CG2 . VAL B 2 458 ? -24.181 -23.264 3.586  1.00 28.94 ? 610 VAL B CG2 1 
ATOM   3879 N N   . LYS B 2 459 ? -20.682 -25.282 1.195  1.00 25.04 ? 611 LYS B N   1 
ATOM   3880 C CA  . LYS B 2 459 ? -20.061 -26.180 0.233  1.00 28.38 ? 611 LYS B CA  1 
ATOM   3881 C C   . LYS B 2 459 ? -20.154 -27.606 0.743  1.00 30.46 ? 611 LYS B C   1 
ATOM   3882 O O   . LYS B 2 459 ? -19.842 -27.875 1.901  1.00 26.55 ? 611 LYS B O   1 
ATOM   3883 C CB  . LYS B 2 459 ? -18.598 -25.771 0.052  1.00 29.92 ? 611 LYS B CB  1 
ATOM   3884 C CG  . LYS B 2 459 ? -17.843 -26.510 -1.056 1.00 35.22 ? 611 LYS B CG  1 
ATOM   3885 C CD  . LYS B 2 459 ? -16.418 -25.952 -1.200 1.00 32.38 ? 611 LYS B CD  1 
ATOM   3886 C CE  . LYS B 2 459 ? -15.535 -26.830 -2.083 1.00 37.83 ? 611 LYS B CE  1 
ATOM   3887 N NZ  . LYS B 2 459 ? -14.174 -26.208 -2.280 1.00 26.81 ? 611 LYS B NZ  1 
ATOM   3888 N N   . GLU B 2 460 ? -20.609 -28.510 -0.115 1.00 30.53 ? 612 GLU B N   1 
ATOM   3889 C CA  . GLU B 2 460 ? -20.869 -29.882 0.274  1.00 31.74 ? 612 GLU B CA  1 
ATOM   3890 C C   . GLU B 2 460 ? -19.967 -30.812 -0.530 1.00 37.04 ? 612 GLU B C   1 
ATOM   3891 O O   . GLU B 2 460 ? -19.637 -30.513 -1.678 1.00 38.90 ? 612 GLU B O   1 
ATOM   3892 C CB  . GLU B 2 460 ? -22.307 -30.236 -0.073 1.00 38.75 ? 612 GLU B CB  1 
ATOM   3893 C CG  . GLU B 2 460 ? -23.299 -29.824 0.980  1.00 38.59 ? 612 GLU B CG  1 
ATOM   3894 C CD  . GLU B 2 460 ? -24.682 -30.396 0.720  1.00 47.80 ? 612 GLU B CD  1 
ATOM   3895 O OE1 . GLU B 2 460 ? -24.878 -31.033 -0.338 1.00 49.73 ? 612 GLU B OE1 1 
ATOM   3896 O OE2 . GLU B 2 460 ? -25.592 -30.159 1.544  1.00 50.66 ? 612 GLU B OE2 1 
ATOM   3897 N N   . HIS B 2 461 ? -19.589 -31.947 0.049  1.00 37.29 ? 613 HIS B N   1 
ATOM   3898 C CA  . HIS B 2 461 ? -18.945 -33.004 -0.717 1.00 39.88 ? 613 HIS B CA  1 
ATOM   3899 C C   . HIS B 2 461 ? -19.180 -34.379 -0.103 1.00 41.75 ? 613 HIS B C   1 
ATOM   3900 O O   . HIS B 2 461 ? -18.990 -34.584 1.097  1.00 35.64 ? 613 HIS B O   1 
ATOM   3901 C CB  . HIS B 2 461 ? -17.440 -32.749 -0.819 1.00 38.05 ? 613 HIS B CB  1 
ATOM   3902 C CG  . HIS B 2 461 ? -16.708 -33.781 -1.617 1.00 43.12 ? 613 HIS B CG  1 
ATOM   3903 N ND1 . HIS B 2 461 ? -15.519 -34.341 -1.199 1.00 44.40 ? 613 HIS B ND1 1 
ATOM   3904 C CD2 . HIS B 2 461 ? -17.004 -34.369 -2.800 1.00 41.75 ? 613 HIS B CD2 1 
ATOM   3905 C CE1 . HIS B 2 461 ? -15.110 -35.222 -2.096 1.00 44.23 ? 613 HIS B CE1 1 
ATOM   3906 N NE2 . HIS B 2 461 ? -15.996 -35.259 -3.076 1.00 39.12 ? 613 HIS B NE2 1 
ATOM   3907 N N   . GLY B 2 462 ? -19.583 -35.330 -0.938 1.00 46.89 ? 614 GLY B N   1 
ATOM   3908 C CA  . GLY B 2 462 ? -19.797 -36.682 -0.467 1.00 43.15 ? 614 GLY B CA  1 
ATOM   3909 C C   . GLY B 2 462 ? -19.258 -37.768 -1.369 1.00 52.37 ? 614 GLY B C   1 
ATOM   3910 O O   . GLY B 2 462 ? -19.114 -37.566 -2.575 1.00 51.85 ? 614 GLY B O   1 
ATOM   3911 N N   . ILE B 2 463 ? -18.936 -38.913 -0.769 1.00 55.03 ? 615 ILE B N   1 
ATOM   3912 C CA  . ILE B 2 463 ? -18.380 -40.055 -1.493 1.00 58.06 ? 615 ILE B CA  1 
ATOM   3913 C C   . ILE B 2 463 ? -18.904 -41.326 -0.812 1.00 60.41 ? 615 ILE B C   1 
ATOM   3914 O O   . ILE B 2 463 ? -19.419 -41.248 0.307  1.00 61.26 ? 615 ILE B O   1 
ATOM   3915 C CB  . ILE B 2 463 ? -16.816 -40.053 -1.549 1.00 60.74 ? 615 ILE B CB  1 
ATOM   3916 C CG1 . ILE B 2 463 ? -16.195 -39.764 -0.181 1.00 57.62 ? 615 ILE B CG1 1 
ATOM   3917 C CG2 . ILE B 2 463 ? -16.307 -39.118 -2.655 1.00 57.49 ? 615 ILE B CG2 1 
ATOM   3918 C CD1 . ILE B 2 463 ? -14.694 -39.501 -0.231 1.00 53.96 ? 615 ILE B CD1 1 
ATOM   3919 N N   . PRO B 2 464 ? -18.794 -42.490 -1.487 1.00 64.67 ? 616 PRO B N   1 
ATOM   3920 C CA  . PRO B 2 464 ? -18.986 -43.838 -0.928 1.00 62.03 ? 616 PRO B CA  1 
ATOM   3921 C C   . PRO B 2 464 ? -18.488 -44.027 0.506  1.00 60.82 ? 616 PRO B C   1 
ATOM   3922 O O   . PRO B 2 464 ? -18.596 -45.140 1.028  1.00 63.04 ? 616 PRO B O   1 
ATOM   3923 C CB  . PRO B 2 464 ? -18.184 -44.709 -1.892 1.00 59.46 ? 616 PRO B CB  1 
ATOM   3924 C CG  . PRO B 2 464 ? -18.422 -44.044 -3.210 1.00 59.07 ? 616 PRO B CG  1 
ATOM   3925 C CD  . PRO B 2 464 ? -18.539 -42.556 -2.939 1.00 61.95 ? 616 PRO B CD  1 
ATOM   3926 N N   . GLN B 2 467 ? -15.756 -45.266 3.216  1.00 57.86 ? 619 GLN B N   1 
ATOM   3927 C CA  . GLN B 2 467 ? -14.891 -44.091 3.311  1.00 56.88 ? 619 GLN B CA  1 
ATOM   3928 C C   . GLN B 2 467 ? -14.624 -43.650 4.755  1.00 54.99 ? 619 GLN B C   1 
ATOM   3929 O O   . GLN B 2 467 ? -15.537 -43.255 5.487  1.00 55.84 ? 619 GLN B O   1 
ATOM   3930 C CB  . GLN B 2 467 ? -15.504 -42.934 2.523  1.00 59.80 ? 619 GLN B CB  1 
ATOM   3931 C CG  . GLN B 2 467 ? -15.261 -43.016 1.018  1.00 62.74 ? 619 GLN B CG  1 
ATOM   3932 C CD  . GLN B 2 467 ? -13.816 -42.733 0.632  1.00 61.95 ? 619 GLN B CD  1 
ATOM   3933 O OE1 . GLN B 2 467 ? -12.937 -42.609 1.493  1.00 58.32 ? 619 GLN B OE1 1 
ATOM   3934 N NE2 . GLN B 2 467 ? -13.566 -42.615 -0.669 1.00 60.57 ? 619 GLN B NE2 1 
ATOM   3935 N N   . GLU B 2 468 ? -13.348 -43.647 5.130  1.00 50.21 ? 620 GLU B N   1 
ATOM   3936 C CA  . GLU B 2 468 ? -12.935 -43.449 6.516  1.00 49.61 ? 620 GLU B CA  1 
ATOM   3937 C C   . GLU B 2 468 ? -13.019 -41.975 6.859  1.00 48.07 ? 620 GLU B C   1 
ATOM   3938 O O   . GLU B 2 468 ? -13.228 -41.591 8.013  1.00 44.44 ? 620 GLU B O   1 
ATOM   3939 C CB  . GLU B 2 468 ? -11.515 -43.959 6.749  1.00 51.37 ? 620 GLU B CB  1 
ATOM   3940 C CG  . GLU B 2 468 ? -11.080 -43.982 8.199  1.00 61.02 ? 620 GLU B CG  1 
ATOM   3941 C CD  . GLU B 2 468 ? -9.877  -44.877 8.422  1.00 71.40 ? 620 GLU B CD  1 
ATOM   3942 O OE1 . GLU B 2 468 ? -9.131  -45.112 7.444  1.00 72.61 ? 620 GLU B OE1 1 
ATOM   3943 O OE2 . GLU B 2 468 ? -9.671  -45.344 9.567  1.00 71.89 ? 620 GLU B OE2 1 
ATOM   3944 N N   . GLN B 2 469 ? -12.891 -41.155 5.824  1.00 45.68 ? 621 GLN B N   1 
ATOM   3945 C CA  . GLN B 2 469 ? -12.778 -39.727 5.994  1.00 38.15 ? 621 GLN B CA  1 
ATOM   3946 C C   . GLN B 2 469 ? -13.150 -39.042 4.698  1.00 39.55 ? 621 GLN B C   1 
ATOM   3947 O O   . GLN B 2 469 ? -12.646 -39.391 3.630  1.00 40.01 ? 621 GLN B O   1 
ATOM   3948 C CB  . GLN B 2 469 ? -11.341 -39.386 6.355  1.00 38.50 ? 621 GLN B CB  1 
ATOM   3949 C CG  . GLN B 2 469 ? -11.067 -37.910 6.271  1.00 33.98 ? 621 GLN B CG  1 
ATOM   3950 C CD  . GLN B 2 469 ? -9.686  -37.546 6.739  1.00 37.42 ? 621 GLN B CD  1 
ATOM   3951 O OE1 . GLN B 2 469 ? -9.302  -37.848 7.872  1.00 39.57 ? 621 GLN B OE1 1 
ATOM   3952 N NE2 . GLN B 2 469 ? -8.929  -36.873 5.877  1.00 36.63 ? 621 GLN B NE2 1 
ATOM   3953 N N   . VAL B 2 470 ? -14.069 -38.089 4.793  1.00 32.61 ? 622 VAL B N   1 
ATOM   3954 C CA  . VAL B 2 470 ? -14.393 -37.223 3.673  1.00 30.80 ? 622 VAL B CA  1 
ATOM   3955 C C   . VAL B 2 470 ? -14.110 -35.773 4.059  1.00 30.76 ? 622 VAL B C   1 
ATOM   3956 O O   . VAL B 2 470 ? -14.250 -35.406 5.228  1.00 29.16 ? 622 VAL B O   1 
ATOM   3957 C CB  . VAL B 2 470 ? -15.847 -37.461 3.136  1.00 38.06 ? 622 VAL B CB  1 
ATOM   3958 C CG1 . VAL B 2 470 ? -16.854 -37.485 4.278  1.00 36.43 ? 622 VAL B CG1 1 
ATOM   3959 C CG2 . VAL B 2 470 ? -16.253 -36.425 2.082  1.00 37.29 ? 622 VAL B CG2 1 
ATOM   3960 N N   . THR B 2 471 ? -13.782 -34.942 3.078  1.00 28.74 ? 623 THR B N   1 
ATOM   3961 C CA  . THR B 2 471 ? -13.098 -33.678 3.316  1.00 28.98 ? 623 THR B CA  1 
ATOM   3962 C C   . THR B 2 471 ? -13.624 -32.662 2.305  1.00 28.78 ? 623 THR B C   1 
ATOM   3963 O O   . THR B 2 471 ? -13.861 -33.005 1.149  1.00 32.41 ? 623 THR B O   1 
ATOM   3964 C CB  . THR B 2 471 ? -11.573 -33.926 3.156  1.00 34.09 ? 623 THR B CB  1 
ATOM   3965 O OG1 . THR B 2 471 ? -10.956 -33.971 4.453  1.00 32.93 ? 623 THR B OG1 1 
ATOM   3966 C CG2 . THR B 2 471 ? -10.923 -32.855 2.335  1.00 27.10 ? 623 THR B CG2 1 
ATOM   3967 N N   . VAL B 2 472 ? -13.877 -31.435 2.757  1.00 24.94 ? 624 VAL B N   1 
ATOM   3968 C CA  . VAL B 2 472 ? -14.300 -30.352 1.877  1.00 22.87 ? 624 VAL B CA  1 
ATOM   3969 C C   . VAL B 2 472 ? -13.750 -29.043 2.443  1.00 25.98 ? 624 VAL B C   1 
ATOM   3970 O O   . VAL B 2 472 ? -13.850 -28.783 3.649  1.00 24.05 ? 624 VAL B O   1 
ATOM   3971 C CB  . VAL B 2 472 ? -15.839 -30.310 1.669  1.00 29.78 ? 624 VAL B CB  1 
ATOM   3972 C CG1 . VAL B 2 472 ? -16.579 -29.938 2.960  1.00 23.00 ? 624 VAL B CG1 1 
ATOM   3973 C CG2 . VAL B 2 472 ? -16.184 -29.340 0.564  1.00 29.59 ? 624 VAL B CG2 1 
ATOM   3974 N N   . ALA B 2 473 ? -13.105 -28.263 1.575  1.00 25.32 ? 625 ALA B N   1 
ATOM   3975 C CA  . ALA B 2 473 ? -12.417 -27.031 1.953  1.00 24.82 ? 625 ALA B CA  1 
ATOM   3976 C C   . ALA B 2 473 ? -13.083 -25.760 1.440  1.00 22.89 ? 625 ALA B C   1 
ATOM   3977 O O   . ALA B 2 473 ? -13.549 -25.707 0.304  1.00 27.49 ? 625 ALA B O   1 
ATOM   3978 C CB  . ALA B 2 473 ? -10.968 -27.085 1.452  1.00 22.11 ? 625 ALA B CB  1 
ATOM   3979 N N   . CYS B 2 474 ? -13.099 -24.714 2.258  1.00 20.72 ? 626 CYS B N   1 
ATOM   3980 C CA  . CYS B 2 474 ? -13.480 -23.393 1.774  1.00 20.67 ? 626 CYS B CA  1 
ATOM   3981 C C   . CYS B 2 474 ? -12.445 -22.890 0.763  1.00 29.89 ? 626 CYS B C   1 
ATOM   3982 O O   . CYS B 2 474 ? -11.323 -23.394 0.702  1.00 21.41 ? 626 CYS B O   1 
ATOM   3983 C CB  . CYS B 2 474 ? -13.551 -22.384 2.931  1.00 24.78 ? 626 CYS B CB  1 
ATOM   3984 S SG  . CYS B 2 474 ? -14.757 -22.805 4.231  1.00 30.82 ? 626 CYS B SG  1 
ATOM   3985 N N   . GLU B 2 475 ? -12.866 -21.943 -0.071 1.00 29.04 ? 627 GLU B N   1 
ATOM   3986 C CA  . GLU B 2 475 ? -12.017 -21.332 -1.093 1.00 31.18 ? 627 GLU B CA  1 
ATOM   3987 C C   . GLU B 2 475 ? -11.074 -20.328 -0.439 1.00 31.34 ? 627 GLU B C   1 
ATOM   3988 O O   . GLU B 2 475 ? -11.375 -19.806 0.639  1.00 27.72 ? 627 GLU B O   1 
ATOM   3989 C CB  . GLU B 2 475 ? -12.880 -20.640 -2.167 1.00 33.36 ? 627 GLU B CB  1 
ATOM   3990 C CG  . GLU B 2 475 ? -13.966 -21.508 -2.846 1.00 35.79 ? 627 GLU B CG  1 
ATOM   3991 C CD  . GLU B 2 475 ? -13.424 -22.748 -3.552 1.00 40.76 ? 627 GLU B CD  1 
ATOM   3992 O OE1 . GLU B 2 475 ? -12.200 -22.815 -3.811 1.00 48.75 ? 627 GLU B OE1 1 
ATOM   3993 O OE2 . GLU B 2 475 ? -14.224 -23.672 -3.840 1.00 42.14 ? 627 GLU B OE2 1 
ATOM   3994 N N   . GLU B 2 476 ? -9.924  -20.077 -1.059 1.00 30.56 ? 628 GLU B N   1 
ATOM   3995 C CA  . GLU B 2 476 ? -8.965  -19.105 -0.524 1.00 29.75 ? 628 GLU B CA  1 
ATOM   3996 C C   . GLU B 2 476 ? -9.641  -17.748 -0.289 1.00 29.72 ? 628 GLU B C   1 
ATOM   3997 O O   . GLU B 2 476 ? -10.422 -17.279 -1.122 1.00 28.66 ? 628 GLU B O   1 
ATOM   3998 C CB  . GLU B 2 476 ? -7.782  -18.955 -1.493 1.00 35.74 ? 628 GLU B CB  1 
ATOM   3999 C CG  . GLU B 2 476 ? -6.518  -18.378 -0.864 1.00 41.38 ? 628 GLU B CG  1 
ATOM   4000 C CD  . GLU B 2 476 ? -6.633  -16.872 -0.578 1.00 48.46 ? 628 GLU B CD  1 
ATOM   4001 O OE1 . GLU B 2 476 ? -6.024  -16.380 0.406  1.00 49.02 ? 628 GLU B OE1 1 
ATOM   4002 O OE2 . GLU B 2 476 ? -7.339  -16.177 -1.343 1.00 52.60 ? 628 GLU B OE2 1 
ATOM   4003 N N   . GLY B 2 477 ? -9.358  -17.140 0.865  1.00 26.84 ? 629 GLY B N   1 
ATOM   4004 C CA  . GLY B 2 477 ? -9.939  -15.867 1.256  1.00 26.76 ? 629 GLY B CA  1 
ATOM   4005 C C   . GLY B 2 477 ? -11.268 -15.988 1.999  1.00 29.36 ? 629 GLY B C   1 
ATOM   4006 O O   . GLY B 2 477 ? -11.830 -14.992 2.455  1.00 31.41 ? 629 GLY B O   1 
ATOM   4007 N N   . TRP B 2 478 ? -11.750 -17.220 2.146  1.00 27.39 ? 630 TRP B N   1 
ATOM   4008 C CA  . TRP B 2 478 ? -12.958 -17.516 2.925  1.00 26.93 ? 630 TRP B CA  1 
ATOM   4009 C C   . TRP B 2 478 ? -12.556 -18.227 4.206  1.00 28.20 ? 630 TRP B C   1 
ATOM   4010 O O   . TRP B 2 478 ? -11.521 -18.894 4.261  1.00 24.08 ? 630 TRP B O   1 
ATOM   4011 C CB  . TRP B 2 478 ? -13.918 -18.402 2.122  1.00 24.56 ? 630 TRP B CB  1 
ATOM   4012 C CG  . TRP B 2 478 ? -14.518 -17.701 0.941  1.00 27.40 ? 630 TRP B CG  1 
ATOM   4013 C CD1 . TRP B 2 478 ? -13.908 -17.445 -0.254 1.00 29.07 ? 630 TRP B CD1 1 
ATOM   4014 C CD2 . TRP B 2 478 ? -15.863 -17.226 0.811  1.00 28.58 ? 630 TRP B CD2 1 
ATOM   4015 N NE1 . TRP B 2 478 ? -14.772 -16.801 -1.103 1.00 30.67 ? 630 TRP B NE1 1 
ATOM   4016 C CE2 . TRP B 2 478 ? -15.984 -16.664 -0.480 1.00 29.77 ? 630 TRP B CE2 1 
ATOM   4017 C CE3 . TRP B 2 478 ? -16.977 -17.221 1.659  1.00 29.23 ? 630 TRP B CE3 1 
ATOM   4018 C CZ2 . TRP B 2 478 ? -17.161 -16.096 -0.938 1.00 30.55 ? 630 TRP B CZ2 1 
ATOM   4019 C CZ3 . TRP B 2 478 ? -18.148 -16.648 1.206  1.00 29.62 ? 630 TRP B CZ3 1 
ATOM   4020 C CH2 . TRP B 2 478 ? -18.231 -16.093 -0.083 1.00 33.68 ? 630 TRP B CH2 1 
ATOM   4021 N N   . THR B 2 479 ? -13.331 -18.025 5.264  1.00 21.22 ? 631 THR B N   1 
ATOM   4022 C CA  . THR B 2 479 ? -13.010 -18.623 6.553  1.00 22.87 ? 631 THR B CA  1 
ATOM   4023 C C   . THR B 2 479 ? -14.060 -19.675 6.932  1.00 21.20 ? 631 THR B C   1 
ATOM   4024 O O   . THR B 2 479 ? -15.248 -19.377 6.929  1.00 19.49 ? 631 THR B O   1 
ATOM   4025 C CB  . THR B 2 479 ? -12.973 -17.537 7.637  1.00 20.05 ? 631 THR B CB  1 
ATOM   4026 O OG1 . THR B 2 479 ? -11.912 -16.605 7.347  1.00 18.11 ? 631 THR B OG1 1 
ATOM   4027 C CG2 . THR B 2 479 ? -12.731 -18.167 8.996  1.00 18.27 ? 631 THR B CG2 1 
ATOM   4028 N N   . LEU B 2 480 ? -13.646 -20.916 7.166  1.00 18.26 ? 632 LEU B N   1 
ATOM   4029 C CA  . LEU B 2 480 ? -14.585 -21.950 7.621  1.00 20.67 ? 632 LEU B CA  1 
ATOM   4030 C C   . LEU B 2 480 ? -15.140 -21.559 8.996  1.00 17.52 ? 632 LEU B C   1 
ATOM   4031 O O   . LEU B 2 480 ? -14.382 -21.397 9.965  1.00 16.88 ? 632 LEU B O   1 
ATOM   4032 C CB  . LEU B 2 480 ? -13.877 -23.293 7.704  1.00 18.33 ? 632 LEU B CB  1 
ATOM   4033 C CG  . LEU B 2 480 ? -14.655 -24.560 8.058  1.00 18.69 ? 632 LEU B CG  1 
ATOM   4034 C CD1 . LEU B 2 480 ? -15.755 -24.799 7.062  1.00 19.20 ? 632 LEU B CD1 1 
ATOM   4035 C CD2 . LEU B 2 480 ? -13.720 -25.732 8.034  1.00 18.89 ? 632 LEU B CD2 1 
ATOM   4036 N N   . THR B 2 481 ? -16.459 -21.430 9.095  1.00 19.06 ? 633 THR B N   1 
ATOM   4037 C CA  . THR B 2 481 ? -17.116 -21.151 10.379 1.00 15.43 ? 633 THR B CA  1 
ATOM   4038 C C   . THR B 2 481 ? -17.784 -22.399 10.959 1.00 15.89 ? 633 THR B C   1 
ATOM   4039 O O   . THR B 2 481 ? -17.929 -22.523 12.182 1.00 15.91 ? 633 THR B O   1 
ATOM   4040 C CB  . THR B 2 481 ? -18.164 -20.029 10.267 1.00 16.73 ? 633 THR B CB  1 
ATOM   4041 O OG1 . THR B 2 481 ? -19.219 -20.417 9.376  1.00 17.46 ? 633 THR B OG1 1 
ATOM   4042 C CG2 . THR B 2 481 ? -17.521 -18.746 9.789  1.00 17.61 ? 633 THR B CG2 1 
ATOM   4043 N N   . GLY B 2 482 ? -18.243 -23.288 10.083 1.00 14.08 ? 634 GLY B N   1 
ATOM   4044 C CA  . GLY B 2 482 ? -18.918 -24.501 10.526 1.00 17.04 ? 634 GLY B CA  1 
ATOM   4045 C C   . GLY B 2 482 ? -18.633 -25.749 9.715  1.00 18.18 ? 634 GLY B C   1 
ATOM   4046 O O   . GLY B 2 482 ? -18.456 -25.701 8.504  1.00 19.32 ? 634 GLY B O   1 
ATOM   4047 N N   . CYS B 2 483 ? -18.622 -26.890 10.386 1.00 16.39 ? 635 CYS B N   1 
ATOM   4048 C CA  . CYS B 2 483 ? -18.297 -28.158 9.742  1.00 16.35 ? 635 CYS B CA  1 
ATOM   4049 C C   . CYS B 2 483 ? -19.184 -29.224 10.339 1.00 17.53 ? 635 CYS B C   1 
ATOM   4050 O O   . CYS B 2 483 ? -19.226 -29.376 11.550 1.00 15.97 ? 635 CYS B O   1 
ATOM   4051 C CB  . CYS B 2 483 ? -16.822 -28.509 9.982  1.00 18.17 ? 635 CYS B CB  1 
ATOM   4052 S SG  . CYS B 2 483 ? -16.323 -30.195 9.508  1.00 20.66 ? 635 CYS B SG  1 
ATOM   4053 N N   . SER B 2 484 ? -19.907 -29.956 9.504  1.00 19.90 ? 636 SER B N   1 
ATOM   4054 C CA  . SER B 2 484 ? -20.820 -30.976 10.016 1.00 21.01 ? 636 SER B CA  1 
ATOM   4055 C C   . SER B 2 484 ? -21.025 -32.046 8.956  1.00 22.04 ? 636 SER B C   1 
ATOM   4056 O O   . SER B 2 484 ? -20.646 -31.858 7.793  1.00 22.98 ? 636 SER B O   1 
ATOM   4057 C CB  . SER B 2 484 ? -22.169 -30.352 10.406 1.00 24.13 ? 636 SER B CB  1 
ATOM   4058 O OG  . SER B 2 484 ? -22.867 -29.865 9.266  1.00 22.85 ? 636 SER B OG  1 
ATOM   4059 N N   . ALA B 2 485 ? -21.577 -33.188 9.356  1.00 25.15 ? 637 ALA B N   1 
ATOM   4060 C CA  . ALA B 2 485 ? -21.903 -34.246 8.406  1.00 26.28 ? 637 ALA B CA  1 
ATOM   4061 C C   . ALA B 2 485 ? -23.407 -34.258 8.144  1.00 35.19 ? 637 ALA B C   1 
ATOM   4062 O O   . ALA B 2 485 ? -24.200 -34.121 9.079  1.00 31.71 ? 637 ALA B O   1 
ATOM   4063 C CB  . ALA B 2 485 ? -21.464 -35.581 8.964  1.00 29.01 ? 637 ALA B CB  1 
ATOM   4064 N N   . LEU B 2 486 ? -23.794 -34.346 6.874  1.00 32.67 ? 638 LEU B N   1 
ATOM   4065 C CA  . LEU B 2 486 ? -25.180 -34.587 6.489  1.00 41.26 ? 638 LEU B CA  1 
ATOM   4066 C C   . LEU B 2 486 ? -25.629 -35.875 7.205  1.00 39.97 ? 638 LEU B C   1 
ATOM   4067 O O   . LEU B 2 486 ? -24.880 -36.853 7.248  1.00 40.80 ? 638 LEU B O   1 
ATOM   4068 C CB  . LEU B 2 486 ? -25.267 -34.733 4.964  1.00 40.87 ? 638 LEU B CB  1 
ATOM   4069 C CG  . LEU B 2 486 ? -26.216 -33.718 4.287  1.00 42.12 ? 638 LEU B CG  1 
ATOM   4070 C CD1 . LEU B 2 486 ? -25.963 -33.646 2.789  1.00 37.37 ? 638 LEU B CD1 1 
ATOM   4071 C CD2 . LEU B 2 486 ? -27.688 -33.932 4.538  1.00 48.79 ? 638 LEU B CD2 1 
ATOM   4072 N N   . PRO B 2 487 ? -26.860 -35.913 7.735  1.00 41.50 ? 639 PRO B N   1 
ATOM   4073 C CA  . PRO B 2 487 ? -27.287 -37.158 8.397  1.00 42.84 ? 639 PRO B CA  1 
ATOM   4074 C C   . PRO B 2 487 ? -27.681 -38.293 7.452  1.00 43.66 ? 639 PRO B C   1 
ATOM   4075 O O   . PRO B 2 487 ? -27.889 -38.069 6.263  1.00 46.56 ? 639 PRO B O   1 
ATOM   4076 C CB  . PRO B 2 487 ? -28.507 -36.713 9.213  1.00 44.51 ? 639 PRO B CB  1 
ATOM   4077 C CG  . PRO B 2 487 ? -29.026 -35.498 8.526  1.00 41.85 ? 639 PRO B CG  1 
ATOM   4078 C CD  . PRO B 2 487 ? -27.895 -34.864 7.767  1.00 39.99 ? 639 PRO B CD  1 
ATOM   4079 N N   . SER B 2 490 ? -21.500 -44.442 6.725  1.00 53.66 ? 642 SER B N   1 
ATOM   4080 C CA  . SER B 2 490 ? -22.887 -44.248 7.136  1.00 54.92 ? 642 SER B CA  1 
ATOM   4081 C C   . SER B 2 490 ? -23.023 -44.009 8.641  1.00 56.53 ? 642 SER B C   1 
ATOM   4082 O O   . SER B 2 490 ? -23.920 -43.282 9.076  1.00 54.37 ? 642 SER B O   1 
ATOM   4083 C CB  . SER B 2 490 ? -23.734 -45.467 6.744  1.00 58.54 ? 642 SER B CB  1 
ATOM   4084 O OG  . SER B 2 490 ? -23.624 -45.774 5.364  1.00 65.85 ? 642 SER B OG  1 
ATOM   4085 N N   . HIS B 2 491 ? -22.126 -44.602 9.427  1.00 49.30 ? 643 HIS B N   1 
ATOM   4086 C CA  . HIS B 2 491 ? -21.998 -44.274 10.849 1.00 48.85 ? 643 HIS B CA  1 
ATOM   4087 C C   . HIS B 2 491 ? -20.832 -43.329 11.173 1.00 49.06 ? 643 HIS B C   1 
ATOM   4088 O O   . HIS B 2 491 ? -19.660 -43.729 11.117 1.00 46.85 ? 643 HIS B O   1 
ATOM   4089 C CB  . HIS B 2 491 ? -21.810 -45.535 11.682 1.00 48.27 ? 643 HIS B CB  1 
ATOM   4090 C CG  . HIS B 2 491 ? -21.565 -45.241 13.124 1.00 53.18 ? 643 HIS B CG  1 
ATOM   4091 N ND1 . HIS B 2 491 ? -22.460 -44.518 13.885 1.00 55.28 ? 643 HIS B ND1 1 
ATOM   4092 C CD2 . HIS B 2 491 ? -20.522 -45.525 13.939 1.00 52.92 ? 643 HIS B CD2 1 
ATOM   4093 C CE1 . HIS B 2 491 ? -21.986 -44.384 15.111 1.00 53.02 ? 643 HIS B CE1 1 
ATOM   4094 N NE2 . HIS B 2 491 ? -20.810 -44.984 15.171 1.00 50.21 ? 643 HIS B NE2 1 
ATOM   4095 N N   . VAL B 2 492 ? -21.144 -42.078 11.513 1.00 44.01 ? 644 VAL B N   1 
ATOM   4096 C CA  . VAL B 2 492 ? -20.090 -41.081 11.673 1.00 41.62 ? 644 VAL B CA  1 
ATOM   4097 C C   . VAL B 2 492 ? -19.526 -40.974 13.099 1.00 37.22 ? 644 VAL B C   1 
ATOM   4098 O O   . VAL B 2 492 ? -20.261 -40.958 14.093 1.00 36.81 ? 644 VAL B O   1 
ATOM   4099 C CB  . VAL B 2 492 ? -20.578 -39.692 11.179 1.00 40.92 ? 644 VAL B CB  1 
ATOM   4100 C CG1 . VAL B 2 492 ? -21.215 -39.815 9.794  1.00 41.04 ? 644 VAL B CG1 1 
ATOM   4101 C CG2 . VAL B 2 492 ? -21.594 -39.104 12.144 1.00 40.59 ? 644 VAL B CG2 1 
ATOM   4102 N N   . LEU B 2 493 ? -18.193 -40.899 13.173 1.00 32.97 ? 645 LEU B N   1 
ATOM   4103 C CA  . LEU B 2 493 ? -17.465 -40.641 14.412 1.00 27.61 ? 645 LEU B CA  1 
ATOM   4104 C C   . LEU B 2 493 ? -17.520 -39.198 14.866 1.00 25.81 ? 645 LEU B C   1 
ATOM   4105 O O   . LEU B 2 493 ? -17.516 -38.913 16.063 1.00 23.50 ? 645 LEU B O   1 
ATOM   4106 C CB  . LEU B 2 493 ? -15.992 -41.012 14.210 1.00 26.62 ? 645 LEU B CB  1 
ATOM   4107 C CG  . LEU B 2 493 ? -15.586 -42.492 14.300 1.00 38.67 ? 645 LEU B CG  1 
ATOM   4108 C CD1 . LEU B 2 493 ? -16.679 -43.458 13.846 1.00 36.16 ? 645 LEU B CD1 1 
ATOM   4109 C CD2 . LEU B 2 493 ? -14.296 -42.725 13.512 1.00 36.13 ? 645 LEU B CD2 1 
ATOM   4110 N N   . GLY B 2 494 ? -17.515 -38.280 13.911 1.00 26.52 ? 646 GLY B N   1 
ATOM   4111 C CA  . GLY B 2 494 ? -17.607 -36.868 14.245 1.00 22.10 ? 646 GLY B CA  1 
ATOM   4112 C C   . GLY B 2 494 ? -17.159 -35.998 13.103 1.00 19.83 ? 646 GLY B C   1 
ATOM   4113 O O   . GLY B 2 494 ? -16.853 -36.476 12.016 1.00 22.99 ? 646 GLY B O   1 
ATOM   4114 N N   . ALA B 2 495 ? -17.122 -34.701 13.351 1.00 24.14 ? 647 ALA B N   1 
ATOM   4115 C CA  . ALA B 2 495 ? -16.716 -33.755 12.333 1.00 21.47 ? 647 ALA B CA  1 
ATOM   4116 C C   . ALA B 2 495 ? -15.913 -32.661 13.038 1.00 19.52 ? 647 ALA B C   1 
ATOM   4117 O O   . ALA B 2 495 ? -16.157 -32.387 14.214 1.00 21.78 ? 647 ALA B O   1 
ATOM   4118 C CB  . ALA B 2 495 ? -17.955 -33.174 11.648 1.00 18.86 ? 647 ALA B CB  1 
ATOM   4119 N N   . TYR B 2 496 ? -14.959 -32.046 12.342 1.00 23.48 ? 648 TYR B N   1 
ATOM   4120 C CA  . TYR B 2 496 ? -14.144 -30.970 12.923 1.00 17.47 ? 648 TYR B CA  1 
ATOM   4121 C C   . TYR B 2 496 ? -13.511 -30.163 11.805 1.00 19.51 ? 648 TYR B C   1 
ATOM   4122 O O   . TYR B 2 496 ? -13.156 -30.699 10.756 1.00 19.18 ? 648 TYR B O   1 
ATOM   4123 C CB  . TYR B 2 496 ? -13.074 -31.542 13.883 1.00 19.31 ? 648 TYR B CB  1 
ATOM   4124 C CG  . TYR B 2 496 ? -12.343 -32.777 13.352 1.00 23.33 ? 648 TYR B CG  1 
ATOM   4125 C CD1 . TYR B 2 496 ? -12.808 -34.047 13.650 1.00 21.49 ? 648 TYR B CD1 1 
ATOM   4126 C CD2 . TYR B 2 496 ? -11.169 -32.671 12.601 1.00 22.44 ? 648 TYR B CD2 1 
ATOM   4127 C CE1 . TYR B 2 496 ? -12.152 -35.179 13.201 1.00 24.18 ? 648 TYR B CE1 1 
ATOM   4128 C CE2 . TYR B 2 496 ? -10.506 -33.813 12.132 1.00 23.94 ? 648 TYR B CE2 1 
ATOM   4129 C CZ  . TYR B 2 496 ? -11.017 -35.056 12.440 1.00 25.71 ? 648 TYR B CZ  1 
ATOM   4130 O OH  . TYR B 2 496 ? -10.413 -36.198 11.976 1.00 31.91 ? 648 TYR B OH  1 
ATOM   4131 N N   . ALA B 2 497 ? -13.362 -28.864 12.041 1.00 18.26 ? 649 ALA B N   1 
ATOM   4132 C CA  . ALA B 2 497 ? -12.648 -27.976 11.151 1.00 18.16 ? 649 ALA B CA  1 
ATOM   4133 C C   . ALA B 2 497 ? -11.149 -28.149 11.389 1.00 22.19 ? 649 ALA B C   1 
ATOM   4134 O O   . ALA B 2 497 ? -10.708 -28.165 12.532 1.00 26.69 ? 649 ALA B O   1 
ATOM   4135 C CB  . ALA B 2 497 ? -13.040 -26.539 11.460 1.00 20.31 ? 649 ALA B CB  1 
ATOM   4136 N N   . VAL B 2 498 ? -10.374 -28.317 10.319 1.00 19.74 ? 650 VAL B N   1 
ATOM   4137 C CA  . VAL B 2 498 ? -8.905  -28.265 10.382 1.00 21.54 ? 650 VAL B CA  1 
ATOM   4138 C C   . VAL B 2 498 ? -8.539  -27.091 9.496  1.00 21.67 ? 650 VAL B C   1 
ATOM   4139 O O   . VAL B 2 498 ? -8.630  -27.194 8.271  1.00 21.67 ? 650 VAL B O   1 
ATOM   4140 C CB  . VAL B 2 498 ? -8.262  -29.558 9.825  1.00 21.47 ? 650 VAL B CB  1 
ATOM   4141 C CG1 . VAL B 2 498 ? -6.749  -29.470 9.911  1.00 27.75 ? 650 VAL B CG1 1 
ATOM   4142 C CG2 . VAL B 2 498 ? -8.705  -30.776 10.631 1.00 20.93 ? 650 VAL B CG2 1 
ATOM   4143 N N   . ASP B 2 499 ? -8.138  -25.983 10.110 1.00 19.57 ? 651 ASP B N   1 
ATOM   4144 C CA  . ASP B 2 499 ? -7.913  -24.729 9.384  1.00 24.76 ? 651 ASP B CA  1 
ATOM   4145 C C   . ASP B 2 499 ? -9.195  -24.329 8.635  1.00 22.94 ? 651 ASP B C   1 
ATOM   4146 O O   . ASP B 2 499 ? -10.211 -24.082 9.275  1.00 21.91 ? 651 ASP B O   1 
ATOM   4147 C CB  . ASP B 2 499 ? -6.713  -24.857 8.446  1.00 24.11 ? 651 ASP B CB  1 
ATOM   4148 C CG  . ASP B 2 499 ? -6.346  -23.555 7.779  1.00 29.24 ? 651 ASP B CG  1 
ATOM   4149 O OD1 . ASP B 2 499 ? -6.642  -22.471 8.341  1.00 35.10 ? 651 ASP B OD1 1 
ATOM   4150 O OD2 . ASP B 2 499 ? -5.780  -23.613 6.662  1.00 38.80 ? 651 ASP B OD2 1 
ATOM   4151 N N   . ASN B 2 500 ? -9.177  -24.310 7.302  1.00 21.31 ? 652 ASN B N   1 
ATOM   4152 C CA  . ASN B 2 500 ? -10.384 -23.974 6.515  1.00 20.19 ? 652 ASN B CA  1 
ATOM   4153 C C   . ASN B 2 500 ? -10.926 -25.171 5.768  1.00 19.81 ? 652 ASN B C   1 
ATOM   4154 O O   . ASN B 2 500 ? -11.644 -25.022 4.776  1.00 22.09 ? 652 ASN B O   1 
ATOM   4155 C CB  . ASN B 2 500 ? -10.140 -22.790 5.567  1.00 22.60 ? 652 ASN B CB  1 
ATOM   4156 C CG  . ASN B 2 500 ? -9.943  -21.462 6.306  1.00 28.68 ? 652 ASN B CG  1 
ATOM   4157 O OD1 . ASN B 2 500 ? -10.741 -21.111 7.188  1.00 21.31 ? 652 ASN B OD1 1 
ATOM   4158 N ND2 . ASN B 2 500 ? -8.877  -20.724 5.964  1.00 32.39 ? 652 ASN B ND2 1 
ATOM   4159 N N   . THR B 2 501 ? -10.616 -26.358 6.283  1.00 18.43 ? 653 THR B N   1 
ATOM   4160 C CA  . THR B 2 501 ? -11.091 -27.620 5.737  1.00 20.86 ? 653 THR B CA  1 
ATOM   4161 C C   . THR B 2 501 ? -11.987 -28.308 6.752  1.00 20.51 ? 653 THR B C   1 
ATOM   4162 O O   . THR B 2 501 ? -11.612 -28.439 7.920  1.00 20.70 ? 653 THR B O   1 
ATOM   4163 C CB  . THR B 2 501 ? -9.909  -28.569 5.413  1.00 21.54 ? 653 THR B CB  1 
ATOM   4164 O OG1 . THR B 2 501 ? -9.045  -27.947 4.453  1.00 25.34 ? 653 THR B OG1 1 
ATOM   4165 C CG2 . THR B 2 501 ? -10.410 -29.888 4.871  1.00 21.24 ? 653 THR B CG2 1 
ATOM   4166 N N   . CYS B 2 502 ? -13.182 -28.717 6.324  1.00 18.46 ? 654 CYS B N   1 
ATOM   4167 C CA  . CYS B 2 502 ? -14.111 -29.438 7.180  1.00 18.80 ? 654 CYS B CA  1 
ATOM   4168 C C   . CYS B 2 502 ? -13.820 -30.932 7.019  1.00 21.54 ? 654 CYS B C   1 
ATOM   4169 O O   . CYS B 2 502 ? -13.806 -31.464 5.900  1.00 21.88 ? 654 CYS B O   1 
ATOM   4170 C CB  . CYS B 2 502 ? -15.557 -29.141 6.777  1.00 21.70 ? 654 CYS B CB  1 
ATOM   4171 S SG  . CYS B 2 502 ? -16.760 -30.268 7.522  1.00 22.50 ? 654 CYS B SG  1 
ATOM   4172 N N   . VAL B 2 503 ? -13.570 -31.618 8.126  1.00 19.69 ? 655 VAL B N   1 
ATOM   4173 C CA  . VAL B 2 503 ? -13.285 -33.042 8.051  1.00 20.09 ? 655 VAL B CA  1 
ATOM   4174 C C   . VAL B 2 503 ? -14.390 -33.863 8.692  1.00 20.75 ? 655 VAL B C   1 
ATOM   4175 O O   . VAL B 2 503 ? -14.769 -33.614 9.829  1.00 21.15 ? 655 VAL B O   1 
ATOM   4176 C CB  . VAL B 2 503 ? -11.942 -33.388 8.781  1.00 21.53 ? 655 VAL B CB  1 
ATOM   4177 C CG1 . VAL B 2 503 ? -11.685 -34.888 8.771  1.00 24.22 ? 655 VAL B CG1 1 
ATOM   4178 C CG2 . VAL B 2 503 ? -10.783 -32.624 8.145  1.00 19.20 ? 655 VAL B CG2 1 
ATOM   4179 N N   . VAL B 2 504 ? -14.906 -34.854 7.963  1.00 21.30 ? 656 VAL B N   1 
ATOM   4180 C CA  . VAL B 2 504 ? -15.865 -35.788 8.531  1.00 22.06 ? 656 VAL B CA  1 
ATOM   4181 C C   . VAL B 2 504 ? -15.275 -37.189 8.620  1.00 30.02 ? 656 VAL B C   1 
ATOM   4182 O O   . VAL B 2 504 ? -14.755 -37.732 7.637  1.00 25.51 ? 656 VAL B O   1 
ATOM   4183 C CB  . VAL B 2 504 ? -17.157 -35.814 7.687  1.00 26.70 ? 656 VAL B CB  1 
ATOM   4184 C CG1 . VAL B 2 504 ? -18.020 -36.999 8.074  1.00 26.59 ? 656 VAL B CG1 1 
ATOM   4185 C CG2 . VAL B 2 504 ? -17.951 -34.512 7.894  1.00 25.91 ? 656 VAL B CG2 1 
ATOM   4186 N N   . ARG B 2 505 ? -15.387 -37.797 9.793  1.00 26.77 ? 657 ARG B N   1 
ATOM   4187 C CA  . ARG B 2 505 ? -14.801 -39.107 10.008 1.00 30.88 ? 657 ARG B CA  1 
ATOM   4188 C C   . ARG B 2 505 ? -15.924 -40.119 10.176 1.00 35.81 ? 657 ARG B C   1 
ATOM   4189 O O   . ARG B 2 505 ? -16.871 -39.879 10.930 1.00 33.67 ? 657 ARG B O   1 
ATOM   4190 C CB  . ARG B 2 505 ? -13.899 -39.075 11.239 1.00 31.79 ? 657 ARG B CB  1 
ATOM   4191 C CG  . ARG B 2 505 ? -12.610 -38.333 11.000 1.00 31.60 ? 657 ARG B CG  1 
ATOM   4192 C CD  . ARG B 2 505 ? -11.643 -39.227 10.280 1.00 30.61 ? 657 ARG B CD  1 
ATOM   4193 N NE  . ARG B 2 505 ? -11.306 -40.362 11.128 1.00 39.94 ? 657 ARG B NE  1 
ATOM   4194 C CZ  . ARG B 2 505 ? -10.401 -40.315 12.100 1.00 38.16 ? 657 ARG B CZ  1 
ATOM   4195 N NH1 . ARG B 2 505 ? -9.728  -39.189 12.315 1.00 34.78 ? 657 ARG B NH1 1 
ATOM   4196 N NH2 . ARG B 2 505 ? -10.165 -41.385 12.850 1.00 37.48 ? 657 ARG B NH2 1 
ATOM   4197 N N   . SER B 2 506 ? -15.867 -41.234 9.451  1.00 36.13 ? 658 SER B N   1 
ATOM   4198 C CA  . SER B 2 506 ? -16.868 -42.261 9.692  1.00 42.08 ? 658 SER B CA  1 
ATOM   4199 C C   . SER B 2 506 ? -16.236 -43.634 9.839  1.00 44.82 ? 658 SER B C   1 
ATOM   4200 O O   . SER B 2 506 ? -15.059 -43.830 9.544  1.00 44.23 ? 658 SER B O   1 
ATOM   4201 C CB  . SER B 2 506 ? -17.882 -42.272 8.545  1.00 42.10 ? 658 SER B CB  1 
ATOM   4202 O OG  . SER B 2 506 ? -17.272 -42.646 7.321  1.00 52.54 ? 658 SER B OG  1 
ATOM   4203 N N   . ARG B 2 507 ? -17.057 -44.592 10.256 1.00 52.27 ? 659 ARG B N   1 
ATOM   4204 C CA  . ARG B 2 507 ? -16.603 -45.960 10.481 1.00 54.62 ? 659 ARG B CA  1 
ATOM   4205 C C   . ARG B 2 507 ? -16.682 -46.801 9.212  1.00 54.52 ? 659 ARG B C   1 
ATOM   4206 O O   . ARG B 2 507 ? -17.779 -47.129 8.744  1.00 58.16 ? 659 ARG B O   1 
ATOM   4207 C CB  . ARG B 2 507 ? -17.408 -46.597 11.613 1.00 54.90 ? 659 ARG B CB  1 
ATOM   4208 C CG  . ARG B 2 507 ? -16.580 -47.495 12.518 1.00 59.67 ? 659 ARG B CG  1 
ATOM   4209 C CD  . ARG B 2 507 ? -17.098 -47.352 13.954 1.00 58.14 ? 659 ARG B CD  1 
ATOM   4210 N NE  . ARG B 2 507 ? -16.167 -47.843 14.971 1.00 59.56 ? 659 ARG B NE  1 
ATOM   4211 C CZ  . ARG B 2 507 ? -15.066 -47.189 15.350 1.00 54.99 ? 659 ARG B CZ  1 
ATOM   4212 N NH1 . ARG B 2 507 ? -14.758 -46.020 14.798 1.00 51.34 ? 659 ARG B NH1 1 
ATOM   4213 N NH2 . ARG B 2 507 ? -14.270 -47.697 16.286 1.00 54.66 ? 659 ARG B NH2 1 
ATOM   4214 N N   . ALA B 2 519 ? -21.898 -43.199 1.718  1.00 53.82 ? 671 ALA B N   1 
ATOM   4215 C CA  . ALA B 2 519 ? -22.671 -42.048 1.271  1.00 58.02 ? 671 ALA B CA  1 
ATOM   4216 C C   . ALA B 2 519 ? -22.619 -40.952 2.329  1.00 56.88 ? 671 ALA B C   1 
ATOM   4217 O O   . ALA B 2 519 ? -23.650 -40.377 2.690  1.00 59.90 ? 671 ALA B O   1 
ATOM   4218 C CB  . ALA B 2 519 ? -24.112 -42.451 1.010  1.00 48.81 ? 671 ALA B CB  1 
ATOM   4219 N N   . VAL B 2 520 ? -21.407 -40.633 2.778  1.00 52.01 ? 672 VAL B N   1 
ATOM   4220 C CA  . VAL B 2 520 ? -21.186 -39.568 3.754  1.00 46.86 ? 672 VAL B CA  1 
ATOM   4221 C C   . VAL B 2 520 ? -20.933 -38.251 3.082  1.00 44.53 ? 672 VAL B C   1 
ATOM   4222 O O   . VAL B 2 520 ? -20.301 -38.206 2.037  1.00 47.36 ? 672 VAL B O   1 
ATOM   4223 C CB  . VAL B 2 520 ? -19.971 -39.869 4.672  1.00 49.78 ? 672 VAL B CB  1 
ATOM   4224 C CG1 . VAL B 2 520 ? -20.423 -40.177 6.097  1.00 50.84 ? 672 VAL B CG1 1 
ATOM   4225 C CG2 . VAL B 2 520 ? -19.088 -40.972 4.086  1.00 49.56 ? 672 VAL B CG2 1 
ATOM   4226 N N   . THR B 2 521 ? -21.418 -37.174 3.682  1.00 43.32 ? 673 THR B N   1 
ATOM   4227 C CA  . THR B 2 521 ? -21.375 -35.887 3.024  1.00 41.54 ? 673 THR B CA  1 
ATOM   4228 C C   . THR B 2 521 ? -20.913 -34.906 4.082  1.00 37.41 ? 673 THR B C   1 
ATOM   4229 O O   . THR B 2 521 ? -21.538 -34.752 5.133  1.00 36.76 ? 673 THR B O   1 
ATOM   4230 C CB  . THR B 2 521 ? -22.727 -35.459 2.394  1.00 45.13 ? 673 THR B CB  1 
ATOM   4231 O OG1 . THR B 2 521 ? -23.083 -36.341 1.323  1.00 51.24 ? 673 THR B OG1 1 
ATOM   4232 C CG2 . THR B 2 521 ? -22.644 -34.014 1.887  1.00 40.99 ? 673 THR B CG2 1 
ATOM   4233 N N   . ALA B 2 522 ? -19.800 -34.256 3.780  1.00 32.40 ? 674 ALA B N   1 
ATOM   4234 C CA  . ALA B 2 522 ? -19.227 -33.199 4.588  1.00 29.51 ? 674 ALA B CA  1 
ATOM   4235 C C   . ALA B 2 522 ? -19.878 -31.895 4.178  1.00 29.70 ? 674 ALA B C   1 
ATOM   4236 O O   . ALA B 2 522 ? -20.125 -31.674 2.994  1.00 29.63 ? 674 ALA B O   1 
ATOM   4237 C CB  . ALA B 2 522 ? -17.721 -33.130 4.399  1.00 30.37 ? 674 ALA B CB  1 
ATOM   4238 N N   . VAL B 2 523 ? -20.181 -31.037 5.142  1.00 27.04 ? 675 VAL B N   1 
ATOM   4239 C CA  . VAL B 2 523 ? -20.801 -29.763 4.837  1.00 23.78 ? 675 VAL B CA  1 
ATOM   4240 C C   . VAL B 2 523 ? -20.008 -28.683 5.529  1.00 22.19 ? 675 VAL B C   1 
ATOM   4241 O O   . VAL B 2 523 ? -19.914 -28.672 6.756  1.00 20.35 ? 675 VAL B O   1 
ATOM   4242 C CB  . VAL B 2 523 ? -22.273 -29.722 5.330  1.00 24.49 ? 675 VAL B CB  1 
ATOM   4243 C CG1 . VAL B 2 523 ? -22.903 -28.408 5.004  1.00 22.50 ? 675 VAL B CG1 1 
ATOM   4244 C CG2 . VAL B 2 523 ? -23.088 -30.857 4.715  1.00 29.67 ? 675 VAL B CG2 1 
ATOM   4245 N N   . ALA B 2 524 ? -19.448 -27.769 4.735  1.00 20.55 ? 676 ALA B N   1 
ATOM   4246 C CA  . ALA B 2 524 ? -18.660 -26.658 5.256  1.00 21.76 ? 676 ALA B CA  1 
ATOM   4247 C C   . ALA B 2 524 ? -19.448 -25.386 5.046  1.00 21.83 ? 676 ALA B C   1 
ATOM   4248 O O   . ALA B 2 524 ? -19.960 -25.140 3.950  1.00 23.22 ? 676 ALA B O   1 
ATOM   4249 C CB  . ALA B 2 524 ? -17.333 -26.550 4.507  1.00 19.84 ? 676 ALA B CB  1 
ATOM   4250 N N   . ILE B 2 525 ? -19.525 -24.566 6.089  1.00 22.00 ? 677 ILE B N   1 
ATOM   4251 C CA  . ILE B 2 525 ? -20.068 -23.224 5.995  1.00 18.31 ? 677 ILE B CA  1 
ATOM   4252 C C   . ILE B 2 525 ? -18.885 -22.280 5.992  1.00 22.52 ? 677 ILE B C   1 
ATOM   4253 O O   . ILE B 2 525 ? -18.055 -22.325 6.911  1.00 18.76 ? 677 ILE B O   1 
ATOM   4254 C CB  . ILE B 2 525 ? -20.999 -22.926 7.189  1.00 19.04 ? 677 ILE B CB  1 
ATOM   4255 C CG1 . ILE B 2 525 ? -22.185 -23.908 7.173  1.00 20.59 ? 677 ILE B CG1 1 
ATOM   4256 C CG2 . ILE B 2 525 ? -21.493 -21.481 7.127  1.00 16.98 ? 677 ILE B CG2 1 
ATOM   4257 C CD1 . ILE B 2 525 ? -23.123 -23.813 8.372  1.00 20.01 ? 677 ILE B CD1 1 
ATOM   4258 N N   . CYS B 2 526 ? -18.792 -21.454 4.948  1.00 21.31 ? 678 CYS B N   1 
ATOM   4259 C CA  . CYS B 2 526 ? -17.642 -20.581 4.742  1.00 22.90 ? 678 CYS B CA  1 
ATOM   4260 C C   . CYS B 2 526 ? -18.066 -19.124 4.661  1.00 23.23 ? 678 CYS B C   1 
ATOM   4261 O O   . CYS B 2 526 ? -19.009 -18.797 3.923  1.00 23.15 ? 678 CYS B O   1 
ATOM   4262 C CB  . CYS B 2 526 ? -16.971 -20.961 3.411  1.00 22.37 ? 678 CYS B CB  1 
ATOM   4263 S SG  . CYS B 2 526 ? -16.549 -22.724 3.263  1.00 26.12 ? 678 CYS B SG  1 
ATOM   4264 N N   . CYS B 2 527 ? -17.383 -18.237 5.381  1.00 19.29 ? 679 CYS B N   1 
ATOM   4265 C CA  . CYS B 2 527 ? -17.788 -16.827 5.383  1.00 22.38 ? 679 CYS B CA  1 
ATOM   4266 C C   . CYS B 2 527 ? -16.590 -15.922 5.109  1.00 26.13 ? 679 CYS B C   1 
ATOM   4267 O O   . CYS B 2 527 ? -15.443 -16.303 5.342  1.00 21.56 ? 679 CYS B O   1 
ATOM   4268 C CB  . CYS B 2 527 ? -18.407 -16.429 6.733  1.00 21.69 ? 679 CYS B CB  1 
ATOM   4269 S SG  . CYS B 2 527 ? -19.814 -17.439 7.283  1.00 22.52 ? 679 CYS B SG  1 
ATOM   4270 N N   . ARG B 2 528 ? -16.877 -14.701 4.670  1.00 25.41 ? 680 ARG B N   1 
ATOM   4271 C CA  . ARG B 2 528 ? -15.867 -13.654 4.514  1.00 28.40 ? 680 ARG B CA  1 
ATOM   4272 C C   . ARG B 2 528 ? -16.486 -12.259 4.649  1.00 31.66 ? 680 ARG B C   1 
ATOM   4273 O O   . ARG B 2 528 ? -17.709 -12.114 4.628  1.00 30.33 ? 680 ARG B O   1 
ATOM   4274 C CB  . ARG B 2 528 ? -15.145 -13.776 3.178  1.00 27.35 ? 680 ARG B CB  1 
ATOM   4275 C CG  . ARG B 2 528 ? -15.957 -13.248 2.003  1.00 34.29 ? 680 ARG B CG  1 
ATOM   4276 C CD  . ARG B 2 528 ? -15.154 -13.346 0.710  1.00 39.20 ? 680 ARG B CD  1 
ATOM   4277 N NE  . ARG B 2 528 ? -15.972 -13.240 -0.502 1.00 43.76 ? 680 ARG B NE  1 
ATOM   4278 C CZ  . ARG B 2 528 ? -15.483 -13.284 -1.739 1.00 36.50 ? 680 ARG B CZ  1 
ATOM   4279 N NH1 . ARG B 2 528 ? -14.182 -13.431 -1.931 1.00 34.79 ? 680 ARG B NH1 1 
ATOM   4280 N NH2 . ARG B 2 528 ? -16.296 -13.189 -2.779 1.00 38.39 ? 680 ARG B NH2 1 
ATOM   4281 N N   . SER B 2 529 ? -15.648 -11.241 4.833  1.00 32.26 ? 681 SER B N   1 
ATOM   4282 C CA  . SER B 2 529 ? -16.101 -9.847  4.730  1.00 37.93 ? 681 SER B CA  1 
ATOM   4283 C C   . SER B 2 529 ? -16.643 -9.567  3.329  1.00 38.34 ? 681 SER B C   1 
ATOM   4284 O O   . SER B 2 529 ? -17.448 -8.647  3.125  1.00 40.54 ? 681 SER B O   1 
ATOM   4285 C CB  . SER B 2 529 ? -14.914 -8.924  4.966  1.00 40.93 ? 681 SER B CB  1 
ATOM   4286 O OG  . SER B 2 529 ? -14.437 -9.049  6.283  1.00 47.54 ? 681 SER B OG  1 
HETATM 4287 O O1  . YBX C 3 1   ? 20.395  -29.572 20.665 1.00 18.04 ? 1   YBX L O1  1 
HETATM 4288 C C5  . YBX C 3 1   ? 21.304  -30.346 20.360 1.00 18.27 ? 1   YBX L C5  1 
HETATM 4289 C C6  . YBX C 3 1   ? 22.281  -29.965 19.263 1.00 17.59 ? 1   YBX L C6  1 
HETATM 4290 S S1  . YBX C 3 1   ? 21.494  -29.568 17.683 1.00 19.91 ? 1   YBX L S1  1 
HETATM 4291 C C7  . YBX C 3 1   ? 20.651  -31.144 17.395 1.00 20.27 ? 1   YBX L C7  1 
HETATM 4292 C C8  . YBX C 3 1   ? 20.484  -31.530 15.931 1.00 28.54 ? 1   YBX L C8  1 
ATOM   4293 N N   . PHE C 3 2   ? 21.474  -31.526 20.965 1.00 13.37 ? 2   PHE L N   1 
ATOM   4294 C CA  . PHE C 3 2   ? 20.656  -32.010 22.071 1.00 16.55 ? 2   PHE L CA  1 
ATOM   4295 C C   . PHE C 3 2   ? 21.658  -31.976 23.229 1.00 18.51 ? 2   PHE L C   1 
ATOM   4296 O O   . PHE C 3 2   ? 22.454  -32.904 23.373 1.00 21.57 ? 2   PHE L O   1 
ATOM   4297 C CB  . PHE C 3 2   ? 20.180  -33.447 21.812 1.00 14.77 ? 2   PHE L CB  1 
ATOM   4298 C CG  . PHE C 3 2   ? 19.240  -33.541 20.636 1.00 16.40 ? 2   PHE L CG  1 
ATOM   4299 C CD1 . PHE C 3 2   ? 19.684  -34.065 19.401 1.00 16.97 ? 2   PHE L CD1 1 
ATOM   4300 C CD2 . PHE C 3 2   ? 17.915  -33.089 20.787 1.00 15.92 ? 2   PHE L CD2 1 
ATOM   4301 C CE1 . PHE C 3 2   ? 18.786  -34.133 18.317 1.00 16.89 ? 2   PHE L CE1 1 
ATOM   4302 C CE2 . PHE C 3 2   ? 17.025  -33.151 19.692 1.00 15.55 ? 2   PHE L CE2 1 
ATOM   4303 C CZ  . PHE C 3 2   ? 17.457  -33.679 18.459 1.00 18.68 ? 2   PHE L CZ  1 
ATOM   4304 N N   . VAL C 3 3   ? 21.670  -30.900 24.035 1.00 17.83 ? 3   VAL L N   1 
ATOM   4305 C CA  . VAL C 3 3   ? 22.602  -30.685 25.160 1.00 17.83 ? 3   VAL L CA  1 
ATOM   4306 C C   . VAL C 3 3   ? 22.044  -31.116 26.523 1.00 19.06 ? 3   VAL L C   1 
ATOM   4307 O O   . VAL C 3 3   ? 20.828  -31.103 26.723 1.00 16.56 ? 3   VAL L O   1 
ATOM   4308 C CB  . VAL C 3 3   ? 23.221  -29.265 25.066 1.00 17.17 ? 3   VAL L CB  1 
ATOM   4309 C CG1 . VAL C 3 3   ? 24.033  -28.995 23.783 1.00 16.30 ? 3   VAL L CG1 1 
ATOM   4310 C CG2 . VAL C 3 3   ? 22.192  -28.140 25.351 1.00 12.57 ? 3   VAL L CG2 1 
ATOM   4311 N N   . GLY C 3 4   ? 22.944  -31.479 27.435 1.00 18.70 ? 4   GLY L N   1 
ATOM   4312 C CA  . GLY C 3 4   ? 22.666  -31.938 28.791 1.00 20.05 ? 4   GLY L CA  1 
ATOM   4313 C C   . GLY C 3 4   ? 22.003  -30.863 29.634 1.00 17.00 ? 4   GLY L C   1 
ATOM   4314 O O   . GLY C 3 4   ? 21.454  -31.203 30.681 1.00 17.88 ? 4   GLY L O   1 
ATOM   4315 N N   . THR C 3 5   ? 22.057  -29.582 29.254 1.00 14.59 ? 5   THR L N   1 
ATOM   4316 C CA  . THR C 3 5   ? 21.461  -28.478 30.003 1.00 13.97 ? 5   THR L CA  1 
ATOM   4317 C C   . THR C 3 5   ? 19.966  -28.375 29.732 1.00 14.58 ? 5   THR L C   1 
ATOM   4318 O O   . THR C 3 5   ? 19.264  -27.562 30.346 1.00 16.07 ? 5   THR L O   1 
ATOM   4319 C CB  . THR C 3 5   ? 22.204  -27.149 29.808 1.00 13.93 ? 5   THR L CB  1 
ATOM   4320 O OG1 . THR C 3 5   ? 22.419  -26.971 28.420 1.00 14.59 ? 5   THR L OG1 1 
ATOM   4321 C CG2 . THR C 3 5   ? 23.521  -27.051 30.596 1.00 16.89 ? 5   THR L CG2 1 
ATOM   4322 N N   . THR C 3 6   ? 19.496  -29.159 28.765 1.00 13.50 ? 6   THR L N   1 
ATOM   4323 C CA  . THR C 3 6   ? 18.118  -29.240 28.313 1.00 14.14 ? 6   THR L CA  1 
ATOM   4324 C C   . THR C 3 6   ? 17.568  -30.546 28.878 1.00 13.98 ? 6   THR L C   1 
ATOM   4325 O O   . THR C 3 6   ? 18.037  -31.611 28.485 1.00 15.46 ? 6   THR L O   1 
ATOM   4326 C CB  . THR C 3 6   ? 17.900  -29.016 26.798 1.00 12.58 ? 6   THR L CB  1 
ATOM   4327 O OG1 . THR C 3 6   ? 18.458  -27.787 26.350 1.00 13.83 ? 6   THR L OG1 1 
ATOM   4328 C CG2 . THR C 3 6   ? 16.408  -29.146 26.398 1.00 13.65 ? 6   THR L CG2 1 
HETATM 4329 N N   . PHA C 3 7   ? 16.600  -30.513 29.782 1.00 14.79 ? 7   PHA L N   1 
HETATM 4330 C CA  . PHA C 3 7   ? 15.990  -31.724 30.348 1.00 16.42 ? 7   PHA L CA  1 
HETATM 4331 C C   . PHA C 3 7   ? 15.068  -32.364 29.275 1.00 18.22 ? 7   PHA L C   1 
HETATM 4332 O O   . PHA C 3 7   ? 14.324  -31.625 28.611 1.00 14.12 ? 7   PHA L O   1 
HETATM 4333 C CB  . PHA C 3 7   ? 15.416  -31.392 31.748 1.00 16.80 ? 7   PHA L CB  1 
HETATM 4334 C CG  . PHA C 3 7   ? 14.937  -32.574 32.575 1.00 21.39 ? 7   PHA L CG  1 
HETATM 4335 C CD1 . PHA C 3 7   ? 15.874  -33.358 33.293 1.00 19.89 ? 7   PHA L CD1 1 
HETATM 4336 C CD2 . PHA C 3 7   ? 13.556  -32.883 32.659 1.00 19.86 ? 7   PHA L CD2 1 
HETATM 4337 C CE1 . PHA C 3 7   ? 15.438  -34.466 34.060 1.00 22.44 ? 7   PHA L CE1 1 
HETATM 4338 C CE2 . PHA C 3 7   ? 13.127  -33.994 33.442 1.00 20.63 ? 7   PHA L CE2 1 
HETATM 4339 C CZ  . PHA C 3 7   ? 14.066  -34.788 34.141 1.00 22.41 ? 7   PHA L CZ  1 
HETATM 4340 N N   . MAA C 3 8   ? 15.089  -33.683 28.975 1.00 18.24 ? 8   MAA L N   1 
HETATM 4341 C CM  . MAA C 3 8   ? 14.188  -34.200 27.925 1.00 15.80 ? 8   MAA L CM  1 
HETATM 4342 C CA  . MAA C 3 8   ? 15.904  -34.683 29.684 1.00 17.83 ? 8   MAA L CA  1 
HETATM 4343 C CB  . MAA C 3 8   ? 15.035  -35.683 30.487 1.00 18.75 ? 8   MAA L CB  1 
HETATM 4344 C C   . MAA C 3 8   ? 16.995  -35.318 28.828 1.00 17.84 ? 8   MAA L C   1 
HETATM 4345 O O   . MAA C 3 8   ? 17.221  -36.524 28.874 1.00 16.55 ? 8   MAA L O   1 
HETATM 4346 N N   . BIF C 3 9   ? 17.686  -34.529 28.015 1.00 15.21 ? 9   BIF L N   1 
HETATM 4347 C CA  . BIF C 3 9   ? 18.740  -35.032 27.146 1.00 20.17 ? 9   BIF L CA  1 
HETATM 4348 C C   . BIF C 3 9   ? 19.989  -35.365 27.957 1.00 20.00 ? 9   BIF L C   1 
HETATM 4349 C CB  . BIF C 3 9   ? 19.056  -34.042 26.001 1.00 17.01 ? 9   BIF L CB  1 
HETATM 4350 C CG  . BIF C 3 9   ? 17.860  -33.569 25.201 1.00 17.88 ? 9   BIF L CG  1 
HETATM 4351 C CD2 . BIF C 3 9   ? 17.723  -32.203 24.890 1.00 15.55 ? 9   BIF L CD2 1 
HETATM 4352 C CE2 . BIF C 3 9   ? 16.611  -31.786 24.145 1.00 14.21 ? 9   BIF L CE2 1 
HETATM 4353 C CZ  . BIF C 3 9   ? 15.635  -32.706 23.708 1.00 16.80 ? 9   BIF L CZ  1 
HETATM 4354 C CE1 . BIF C 3 9   ? 15.784  -34.068 24.031 1.00 17.17 ? 9   BIF L CE1 1 
HETATM 4355 C CD1 . BIF C 3 9   ? 16.898  -34.496 24.774 1.00 15.87 ? 9   BIF L CD1 1 
HETATM 4356 C C8  . BIF C 3 9   ? 13.509  -30.790 21.209 1.00 12.16 ? 9   BIF L C8  1 
HETATM 4357 C C9  . BIF C 3 9   ? 12.220  -31.260 21.518 1.00 15.51 ? 9   BIF L C9  1 
HETATM 4358 C C10 . BIF C 3 9   ? 12.069  -32.215 22.539 1.00 11.81 ? 9   BIF L C10 1 
HETATM 4359 C C11 . BIF C 3 9   ? 13.183  -32.704 23.249 1.00 15.00 ? 9   BIF L C11 1 
HETATM 4360 C C12 . BIF C 3 9   ? 14.475  -32.232 22.944 1.00 12.78 ? 9   BIF L C12 1 
HETATM 4361 C C13 . BIF C 3 9   ? 14.622  -31.269 21.927 1.00 14.23 ? 9   BIF L C13 1 
HETATM 4362 O O   . BIF C 3 9   ? 20.275  -34.695 28.956 1.00 18.07 ? 9   BIF L O   1 
HETATM 4363 C C7  . EME C 3 10  ? 20.491  -37.164 26.375 1.00 16.74 ? 10  EME L C7  1 
HETATM 4364 N N   . EME C 3 10  ? 20.806  -36.369 27.581 1.00 21.39 ? 10  EME L N   1 
HETATM 4365 C CA  . EME C 3 10  ? 22.036  -36.641 28.328 1.00 25.16 ? 10  EME L CA  1 
HETATM 4366 C C   . EME C 3 10  ? 22.974  -35.445 28.082 1.00 22.54 ? 10  EME L C   1 
HETATM 4367 O O   . EME C 3 10  ? 23.169  -35.038 26.928 1.00 26.99 ? 10  EME L O   1 
HETATM 4368 C CB  . EME C 3 10  ? 22.569  -38.069 28.071 1.00 28.26 ? 10  EME L CB  1 
HETATM 4369 C CG  . EME C 3 10  ? 23.238  -38.679 29.319 1.00 35.01 ? 10  EME L CG  1 
HETATM 4370 C CD  . EME C 3 10  ? 22.255  -38.866 30.477 1.00 43.68 ? 10  EME L CD  1 
HETATM 4371 O OE2 . EME C 3 10  ? 21.074  -39.206 30.355 1.00 49.21 ? 10  EME L OE2 1 
HETATM 4372 O OE1 . EME C 3 10  ? 22.827  -38.605 31.685 1.00 54.91 ? 10  EME L OE1 1 
HETATM 4373 N N   . NEH C 3 11  ? 23.578  -34.828 29.085 1.00 20.25 ? 11  NEH L N   1 
HETATM 4374 C CA  . NEH C 3 11  ? 24.494  -33.715 28.880 1.00 23.40 ? 11  NEH L CA  1 
HETATM 4375 C CB  . NEH C 3 11  ? 23.938  -32.426 29.502 1.00 19.19 ? 11  NEH L CB  1 
HETATM 4376 O O   . HOH D 4 .   ? -1.567  -33.222 63.483 1.00 34.94 ? 201 HOH A O   1 
HETATM 4377 O O   . HOH D 4 .   ? 16.635  -26.109 25.633 1.00 14.60 ? 202 HOH A O   1 
HETATM 4378 O O   . HOH D 4 .   ? 3.342   -28.589 42.930 1.00 21.26 ? 203 HOH A O   1 
HETATM 4379 O O   . HOH D 4 .   ? 2.933   -39.262 31.338 1.00 30.10 ? 204 HOH A O   1 
HETATM 4380 O O   . HOH D 4 .   ? 11.395  -26.322 52.089 1.00 38.11 ? 205 HOH A O   1 
HETATM 4381 O O   . HOH D 4 .   ? 4.038   -32.637 44.532 1.00 14.51 ? 206 HOH A O   1 
HETATM 4382 O O   . HOH D 4 .   ? 10.384  -26.446 47.742 1.00 19.46 ? 207 HOH A O   1 
HETATM 4383 O O   . HOH D 4 .   ? -12.699 -34.050 61.798 1.00 50.80 ? 208 HOH A O   1 
HETATM 4384 O O   . HOH D 4 .   ? 13.445  -29.125 41.663 1.00 19.20 ? 209 HOH A O   1 
HETATM 4385 O O   . HOH D 4 .   ? -3.401  -32.794 60.505 1.00 19.76 ? 210 HOH A O   1 
HETATM 4386 O O   . HOH D 4 .   ? -1.781  -9.277  58.972 1.00 30.21 ? 211 HOH A O   1 
HETATM 4387 O O   . HOH D 4 .   ? 6.337   -31.117 38.626 1.00 20.63 ? 212 HOH A O   1 
HETATM 4388 O O   . HOH D 4 .   ? 2.503   -34.959 50.518 1.00 20.17 ? 213 HOH A O   1 
HETATM 4389 O O   . HOH D 4 .   ? 2.855   -7.460  54.304 1.00 20.63 ? 214 HOH A O   1 
HETATM 4390 O O   . HOH D 4 .   ? 4.444   -24.161 64.157 1.00 23.24 ? 215 HOH A O   1 
HETATM 4391 O O   . HOH D 4 .   ? -3.016  -12.605 50.022 1.00 18.63 ? 216 HOH A O   1 
HETATM 4392 O O   . HOH D 4 .   ? 3.639   -30.574 39.528 1.00 31.30 ? 217 HOH A O   1 
HETATM 4393 O O   . HOH D 4 .   ? -9.243  -31.793 56.986 1.00 22.36 ? 218 HOH A O   1 
HETATM 4394 O O   . HOH D 4 .   ? -10.250 -32.720 51.335 1.00 29.35 ? 219 HOH A O   1 
HETATM 4395 O O   . HOH D 4 .   ? 9.275   -29.802 55.920 1.00 24.92 ? 220 HOH A O   1 
HETATM 4396 O O   . HOH D 4 .   ? -7.223  -25.745 61.265 1.00 26.20 ? 221 HOH A O   1 
HETATM 4397 O O   . HOH D 4 .   ? -11.799 -15.506 51.830 1.00 32.56 ? 222 HOH A O   1 
HETATM 4398 O O   . HOH D 4 .   ? -12.281 -23.678 53.254 1.00 29.64 ? 223 HOH A O   1 
HETATM 4399 O O   . HOH D 4 .   ? -0.892  -37.263 42.457 1.00 17.21 ? 224 HOH A O   1 
HETATM 4400 O O   . HOH D 4 .   ? 6.523   -29.741 60.647 1.00 21.37 ? 225 HOH A O   1 
HETATM 4401 O O   . HOH D 4 .   ? 2.699   -39.136 43.055 1.00 19.35 ? 226 HOH A O   1 
HETATM 4402 O O   . HOH D 4 .   ? 10.215  -29.346 49.979 1.00 29.65 ? 227 HOH A O   1 
HETATM 4403 O O   . HOH D 4 .   ? 0.707   -38.911 44.270 1.00 29.92 ? 228 HOH A O   1 
HETATM 4404 O O   . HOH D 4 .   ? -4.611  -11.252 48.474 1.00 26.75 ? 229 HOH A O   1 
HETATM 4405 O O   . HOH D 4 .   ? -8.252  -19.496 44.733 1.00 26.45 ? 230 HOH A O   1 
HETATM 4406 O O   . HOH D 4 .   ? 1.770   -17.895 65.063 1.00 34.21 ? 231 HOH A O   1 
HETATM 4407 O O   . HOH D 4 .   ? 3.195   -37.064 56.449 1.00 19.46 ? 232 HOH A O   1 
HETATM 4408 O O   . HOH D 4 .   ? -12.205 -24.961 44.351 1.00 37.27 ? 233 HOH A O   1 
HETATM 4409 O O   . HOH D 4 .   ? 6.403   -13.117 51.867 1.00 20.83 ? 234 HOH A O   1 
HETATM 4410 O O   . HOH D 4 .   ? -8.898  -23.414 61.931 1.00 32.50 ? 235 HOH A O   1 
HETATM 4411 O O   . HOH D 4 .   ? 8.685   -30.230 64.014 1.00 33.25 ? 236 HOH A O   1 
HETATM 4412 O O   . HOH D 4 .   ? -10.075 -22.675 42.519 1.00 27.66 ? 237 HOH A O   1 
HETATM 4413 O O   . HOH D 4 .   ? -11.627 -19.070 44.890 1.00 33.63 ? 238 HOH A O   1 
HETATM 4414 O O   . HOH D 4 .   ? 10.171  -14.570 49.167 1.00 37.08 ? 239 HOH A O   1 
HETATM 4415 O O   . HOH D 4 .   ? 3.048   -38.900 62.939 1.00 36.42 ? 240 HOH A O   1 
HETATM 4416 O O   . HOH D 4 .   ? 7.842   -18.467 59.731 1.00 26.76 ? 241 HOH A O   1 
HETATM 4417 O O   . HOH D 4 .   ? -4.837  -8.236  49.165 1.00 17.20 ? 242 HOH A O   1 
HETATM 4418 O O   . HOH D 4 .   ? 12.036  -33.828 42.785 1.00 30.70 ? 243 HOH A O   1 
HETATM 4419 O O   . HOH D 4 .   ? 11.311  -32.822 49.173 1.00 27.18 ? 244 HOH A O   1 
HETATM 4420 O O   . HOH D 4 .   ? -4.055  -27.876 66.957 1.00 36.70 ? 245 HOH A O   1 
HETATM 4421 O O   . HOH D 4 .   ? 3.899   -11.182 54.934 1.00 35.06 ? 246 HOH A O   1 
HETATM 4422 O O   . HOH D 4 .   ? -8.013  -34.646 47.335 1.00 28.29 ? 247 HOH A O   1 
HETATM 4423 O O   . HOH D 4 .   ? 9.745   -26.537 59.345 1.00 33.00 ? 248 HOH A O   1 
HETATM 4424 O O   . HOH D 4 .   ? 13.059  -38.717 43.500 1.00 43.84 ? 249 HOH A O   1 
HETATM 4425 O O   . HOH D 4 .   ? -8.282  -13.907 58.157 1.00 39.04 ? 250 HOH A O   1 
HETATM 4426 O O   . HOH D 4 .   ? 1.179   -21.985 70.063 1.00 37.65 ? 251 HOH A O   1 
HETATM 4427 O O   . HOH D 4 .   ? 0.418   -42.973 49.162 1.00 23.18 ? 252 HOH A O   1 
HETATM 4428 O O   . HOH D 4 .   ? 9.369   -29.110 58.631 1.00 34.11 ? 253 HOH A O   1 
HETATM 4429 O O   . HOH D 4 .   ? -8.118  -19.222 40.164 1.00 36.75 ? 254 HOH A O   1 
HETATM 4430 O O   . HOH E 4 .   ? -3.032  -38.003 26.619 1.00 30.21 ? 701 HOH B O   1 
HETATM 4431 O O   . HOH E 4 .   ? 13.901  -5.596  4.028  1.00 48.75 ? 702 HOH B O   1 
HETATM 4432 O O   . HOH E 4 .   ? 25.731  -6.848  32.264 1.00 39.03 ? 703 HOH B O   1 
HETATM 4433 O O   . HOH E 4 .   ? 10.452  -6.540  23.567 1.00 35.05 ? 704 HOH B O   1 
HETATM 4434 O O   . HOH E 4 .   ? -11.776 -11.434 12.527 1.00 25.24 ? 705 HOH B O   1 
HETATM 4435 O O   . HOH E 4 .   ? -24.605 -18.665 17.425 1.00 33.72 ? 706 HOH B O   1 
HETATM 4436 O O   . HOH E 4 .   ? -6.210  -38.987 15.738 1.00 28.03 ? 707 HOH B O   1 
HETATM 4437 O O   . HOH E 4 .   ? -24.306 -37.440 27.878 1.00 38.94 ? 708 HOH B O   1 
HETATM 4438 O O   . HOH E 4 .   ? -18.283 -26.622 13.333 1.00 19.61 ? 709 HOH B O   1 
HETATM 4439 O O   . HOH E 4 .   ? -15.778 -11.315 18.638 1.00 27.07 ? 710 HOH B O   1 
HETATM 4440 O O   . HOH E 4 .   ? 10.864  -36.448 13.928 1.00 31.76 ? 711 HOH B O   1 
HETATM 4441 O O   . HOH E 4 .   ? -33.884 -12.462 10.630 1.00 51.16 ? 712 HOH B O   1 
HETATM 4442 O O   . HOH E 4 .   ? -2.355  -20.155 5.725  1.00 28.03 ? 713 HOH B O   1 
HETATM 4443 O O   . HOH E 4 .   ? 29.573  -23.392 22.980 1.00 28.58 ? 714 HOH B O   1 
HETATM 4444 O O   . HOH E 4 .   ? 0.526   -7.503  14.558 1.00 22.05 ? 715 HOH B O   1 
HETATM 4445 O O   . HOH E 4 .   ? -19.298 -18.517 29.648 1.00 39.14 ? 716 HOH B O   1 
HETATM 4446 O O   . HOH E 4 .   ? -2.205  -33.617 7.206  1.00 43.83 ? 717 HOH B O   1 
HETATM 4447 O O   . HOH E 4 .   ? -1.573  -6.109  32.253 1.00 24.61 ? 718 HOH B O   1 
HETATM 4448 O O   . HOH E 4 .   ? -17.732 -19.574 24.803 1.00 23.77 ? 719 HOH B O   1 
HETATM 4449 O O   . HOH E 4 .   ? -25.541 -18.805 4.637  1.00 41.22 ? 720 HOH B O   1 
HETATM 4450 O O   . HOH E 4 .   ? 0.534   -40.030 28.349 1.00 28.54 ? 721 HOH B O   1 
HETATM 4451 O O   . HOH E 4 .   ? -33.056 -34.303 21.466 1.00 22.56 ? 722 HOH B O   1 
HETATM 4452 O O   . HOH E 4 .   ? 12.453  -22.304 41.109 1.00 12.65 ? 723 HOH B O   1 
HETATM 4453 O O   . HOH E 4 .   ? 17.304  -15.686 34.423 1.00 16.95 ? 724 HOH B O   1 
HETATM 4454 O O   . HOH E 4 .   ? -23.097 -37.996 5.737  1.00 45.48 ? 725 HOH B O   1 
HETATM 4455 O O   . HOH E 4 .   ? -6.767  -27.768 37.913 1.00 30.39 ? 726 HOH B O   1 
HETATM 4456 O O   . HOH E 4 .   ? -2.947  -12.041 28.192 1.00 26.57 ? 727 HOH B O   1 
HETATM 4457 O O   . HOH E 4 .   ? -22.953 -25.391 15.230 1.00 21.64 ? 728 HOH B O   1 
HETATM 4458 O O   . HOH E 4 .   ? -43.092 -35.231 14.256 1.00 49.33 ? 729 HOH B O   1 
HETATM 4459 O O   . HOH E 4 .   ? -33.424 -36.931 20.767 1.00 23.00 ? 730 HOH B O   1 
HETATM 4460 O O   . HOH E 4 .   ? -17.763 -42.278 23.191 1.00 28.17 ? 731 HOH B O   1 
HETATM 4461 O O   . HOH E 4 .   ? 14.009  -34.706 15.185 1.00 22.29 ? 732 HOH B O   1 
HETATM 4462 O O   . HOH E 4 .   ? 19.939  -22.462 13.585 1.00 15.52 ? 733 HOH B O   1 
HETATM 4463 O O   . HOH E 4 .   ? -6.044  -11.621 37.136 1.00 32.70 ? 734 HOH B O   1 
HETATM 4464 O O   . HOH E 4 .   ? -19.320 -17.412 22.693 1.00 28.39 ? 735 HOH B O   1 
HETATM 4465 O O   . HOH E 4 .   ? -4.855  -25.752 5.430  1.00 38.34 ? 736 HOH B O   1 
HETATM 4466 O O   . HOH E 4 .   ? -4.694  -3.485  15.137 1.00 25.21 ? 737 HOH B O   1 
HETATM 4467 O O   . HOH E 4 .   ? 2.988   0.554   16.841 1.00 16.92 ? 738 HOH B O   1 
HETATM 4468 O O   . HOH E 4 .   ? 21.107  -6.030  37.063 1.00 31.77 ? 739 HOH B O   1 
HETATM 4469 O O   . HOH E 4 .   ? 24.347  -20.600 26.071 1.00 15.71 ? 740 HOH B O   1 
HETATM 4470 O O   . HOH E 4 .   ? -10.910 -20.645 24.674 1.00 24.95 ? 741 HOH B O   1 
HETATM 4471 O O   . HOH E 4 .   ? -0.485  0.396   38.997 1.00 13.64 ? 742 HOH B O   1 
HETATM 4472 O O   . HOH E 4 .   ? -17.006 -38.795 32.524 1.00 26.55 ? 743 HOH B O   1 
HETATM 4473 O O   . HOH E 4 .   ? -7.785  -28.000 24.404 1.00 24.65 ? 744 HOH B O   1 
HETATM 4474 O O   . HOH E 4 .   ? 19.304  -29.078 23.771 1.00 14.80 ? 745 HOH B O   1 
HETATM 4475 O O   . HOH E 4 .   ? -7.918  -25.573 4.926  1.00 31.86 ? 746 HOH B O   1 
HETATM 4476 O O   . HOH E 4 .   ? 5.509   -26.075 30.055 1.00 15.90 ? 747 HOH B O   1 
HETATM 4477 O O   . HOH E 4 .   ? 18.724  -20.296 5.601  1.00 32.07 ? 748 HOH B O   1 
HETATM 4478 O O   . HOH E 4 .   ? -1.582  -31.497 24.588 1.00 14.00 ? 749 HOH B O   1 
HETATM 4479 O O   . HOH E 4 .   ? 6.422   -2.815  27.270 1.00 25.36 ? 750 HOH B O   1 
HETATM 4480 O O   . HOH E 4 .   ? -1.815  -33.147 13.781 1.00 26.18 ? 751 HOH B O   1 
HETATM 4481 O O   . HOH E 4 .   ? -3.982  -23.760 17.650 1.00 17.23 ? 752 HOH B O   1 
HETATM 4482 O O   . HOH E 4 .   ? -1.290  -15.362 27.956 1.00 16.09 ? 753 HOH B O   1 
HETATM 4483 O O   . HOH E 4 .   ? 16.453  -29.052 12.375 1.00 21.36 ? 754 HOH B O   1 
HETATM 4484 O O   . HOH E 4 .   ? -1.731  -5.752  24.014 1.00 22.36 ? 755 HOH B O   1 
HETATM 4485 O O   . HOH E 4 .   ? -8.471  -8.730  15.303 1.00 28.72 ? 756 HOH B O   1 
HETATM 4486 O O   . HOH E 4 .   ? -7.097  -26.454 17.152 1.00 25.32 ? 757 HOH B O   1 
HETATM 4487 O O   . HOH E 4 .   ? -20.920 -35.920 21.000 1.00 21.45 ? 758 HOH B O   1 
HETATM 4488 O O   . HOH E 4 .   ? -4.596  -32.525 32.267 1.00 16.46 ? 759 HOH B O   1 
HETATM 4489 O O   . HOH E 4 .   ? -12.659 -43.146 28.946 1.00 26.71 ? 760 HOH B O   1 
HETATM 4490 O O   . HOH E 4 .   ? 2.919   -15.614 7.804  1.00 18.92 ? 761 HOH B O   1 
HETATM 4491 O O   . HOH E 4 .   ? 1.706   -0.968  12.850 1.00 25.98 ? 762 HOH B O   1 
HETATM 4492 O O   . HOH E 4 .   ? 19.588  -17.230 18.600 1.00 21.64 ? 763 HOH B O   1 
HETATM 4493 O O   . HOH E 4 .   ? -11.992 -14.717 5.407  1.00 23.94 ? 764 HOH B O   1 
HETATM 4494 O O   . HOH E 4 .   ? 20.212  -25.834 27.223 1.00 14.35 ? 765 HOH B O   1 
HETATM 4495 O O   . HOH E 4 .   ? 21.570  -15.635 19.844 1.00 18.03 ? 766 HOH B O   1 
HETATM 4496 O O   . HOH E 4 .   ? 0.198   -13.897 44.149 1.00 21.36 ? 767 HOH B O   1 
HETATM 4497 O O   . HOH E 4 .   ? 18.926  -28.488 10.987 1.00 27.81 ? 768 HOH B O   1 
HETATM 4498 O O   . HOH E 4 .   ? 6.952   -12.409 44.273 1.00 19.17 ? 769 HOH B O   1 
HETATM 4499 O O   . HOH E 4 .   ? 4.457   4.211   34.183 1.00 15.80 ? 770 HOH B O   1 
HETATM 4500 O O   . HOH E 4 .   ? -22.115 -33.457 12.025 1.00 31.80 ? 771 HOH B O   1 
HETATM 4501 O O   . HOH E 4 .   ? 22.770  -6.903  29.278 1.00 29.41 ? 772 HOH B O   1 
HETATM 4502 O O   . HOH E 4 .   ? -7.974  -25.956 12.850 1.00 21.58 ? 773 HOH B O   1 
HETATM 4503 O O   . HOH E 4 .   ? -15.682 -27.912 14.282 1.00 25.84 ? 774 HOH B O   1 
HETATM 4504 O O   . HOH E 4 .   ? 10.249  -21.460 46.973 1.00 16.64 ? 775 HOH B O   1 
HETATM 4505 O O   . HOH E 4 .   ? -8.235  -21.820 12.247 1.00 20.49 ? 776 HOH B O   1 
HETATM 4506 O O   . HOH E 4 .   ? 6.863   -21.123 9.337  1.00 19.11 ? 777 HOH B O   1 
HETATM 4507 O O   . HOH E 4 .   ? -39.711 -33.379 19.976 1.00 20.14 ? 778 HOH B O   1 
HETATM 4508 O O   . HOH E 4 .   ? 15.597  -4.546  29.325 1.00 32.64 ? 779 HOH B O   1 
HETATM 4509 O O   . HOH E 4 .   ? -23.107 -31.163 13.870 1.00 29.52 ? 780 HOH B O   1 
HETATM 4510 O O   . HOH E 4 .   ? -20.728 -27.924 13.364 1.00 22.09 ? 781 HOH B O   1 
HETATM 4511 O O   . HOH E 4 .   ? -4.255  -28.240 12.248 1.00 21.63 ? 782 HOH B O   1 
HETATM 4512 O O   . HOH E 4 .   ? 21.014  -22.937 9.882  1.00 25.34 ? 783 HOH B O   1 
HETATM 4513 O O   . HOH E 4 .   ? 12.865  -22.812 44.440 1.00 17.08 ? 784 HOH B O   1 
HETATM 4514 O O   . HOH E 4 .   ? 18.754  -18.424 15.568 1.00 18.76 ? 785 HOH B O   1 
HETATM 4515 O O   . HOH E 4 .   ? -6.988  -17.603 13.190 1.00 14.43 ? 786 HOH B O   1 
HETATM 4516 O O   . HOH E 4 .   ? -2.193  -30.083 41.008 1.00 18.39 ? 787 HOH B O   1 
HETATM 4517 O O   . HOH E 4 .   ? 26.752  -11.241 18.375 1.00 26.95 ? 788 HOH B O   1 
HETATM 4518 O O   . HOH E 4 .   ? -5.733  -27.987 31.045 1.00 25.88 ? 789 HOH B O   1 
HETATM 4519 O O   . HOH E 4 .   ? -4.966  -6.133  35.098 1.00 18.48 ? 790 HOH B O   1 
HETATM 4520 O O   . HOH E 4 .   ? -5.813  -24.675 38.053 1.00 15.59 ? 791 HOH B O   1 
HETATM 4521 O O   . HOH E 4 .   ? -28.885 -35.232 13.262 1.00 26.94 ? 792 HOH B O   1 
HETATM 4522 O O   . HOH E 4 .   ? 22.094  -27.399 33.785 1.00 25.05 ? 793 HOH B O   1 
HETATM 4523 O O   . HOH E 4 .   ? 3.262   -2.785  31.500 1.00 24.24 ? 794 HOH B O   1 
HETATM 4524 O O   . HOH E 4 .   ? -7.710  -16.763 20.184 1.00 21.24 ? 795 HOH B O   1 
HETATM 4525 O O   . HOH E 4 .   ? -4.192  -34.027 23.661 1.00 14.82 ? 796 HOH B O   1 
HETATM 4526 O O   . HOH E 4 .   ? -21.601 -26.440 11.324 1.00 18.49 ? 797 HOH B O   1 
HETATM 4527 O O   . HOH E 4 .   ? 10.172  -26.099 11.426 1.00 15.92 ? 798 HOH B O   1 
HETATM 4528 O O   . HOH E 4 .   ? 21.263  -23.127 44.231 1.00 37.99 ? 799 HOH B O   1 
HETATM 4529 O O   . HOH E 4 .   ? -12.528 -24.605 26.248 1.00 24.71 ? 800 HOH B O   1 
HETATM 4530 O O   . HOH E 4 .   ? 2.744   -17.436 13.680 1.00 14.21 ? 801 HOH B O   1 
HETATM 4531 O O   . HOH E 4 .   ? -5.790  -26.191 34.443 1.00 30.78 ? 802 HOH B O   1 
HETATM 4532 O O   . HOH E 4 .   ? -32.162 -22.468 21.026 1.00 27.38 ? 803 HOH B O   1 
HETATM 4533 O O   . HOH E 4 .   ? -6.829  -18.465 37.874 1.00 30.68 ? 804 HOH B O   1 
HETATM 4534 O O   . HOH E 4 .   ? -11.294 -7.852  20.704 1.00 33.40 ? 805 HOH B O   1 
HETATM 4535 O O   . HOH E 4 .   ? -8.576  -34.597 27.339 1.00 25.95 ? 806 HOH B O   1 
HETATM 4536 O O   . HOH E 4 .   ? -12.860 -28.574 28.448 1.00 26.37 ? 807 HOH B O   1 
HETATM 4537 O O   . HOH E 4 .   ? -9.135  -29.515 14.499 1.00 22.68 ? 808 HOH B O   1 
HETATM 4538 O O   . HOH E 4 .   ? 17.998  -12.759 38.179 1.00 14.73 ? 809 HOH B O   1 
HETATM 4539 O O   . HOH E 4 .   ? -11.106 -44.097 15.997 1.00 36.21 ? 810 HOH B O   1 
HETATM 4540 O O   . HOH E 4 .   ? -23.404 -12.412 20.074 1.00 39.42 ? 811 HOH B O   1 
HETATM 4541 O O   . HOH E 4 .   ? -8.595  -12.165 24.682 1.00 23.75 ? 812 HOH B O   1 
HETATM 4542 O O   . HOH E 4 .   ? -14.859 -30.577 29.001 1.00 25.17 ? 813 HOH B O   1 
HETATM 4543 O O   . HOH E 4 .   ? -6.226  -28.450 18.930 1.00 14.10 ? 814 HOH B O   1 
HETATM 4544 O O   . HOH E 4 .   ? 3.301   -43.826 12.169 1.00 37.00 ? 815 HOH B O   1 
HETATM 4545 O O   . HOH E 4 .   ? -34.099 -29.893 22.191 1.00 26.37 ? 816 HOH B O   1 
HETATM 4546 O O   . HOH E 4 .   ? -6.117  -9.841  26.576 1.00 33.16 ? 817 HOH B O   1 
HETATM 4547 O O   . HOH E 4 .   ? 0.663   -7.647  27.407 1.00 19.80 ? 818 HOH B O   1 
HETATM 4548 O O   . HOH E 4 .   ? -3.628  -26.739 10.364 1.00 21.92 ? 819 HOH B O   1 
HETATM 4549 O O   . HOH E 4 .   ? 21.354  -21.152 37.049 1.00 17.96 ? 820 HOH B O   1 
HETATM 4550 O O   . HOH E 4 .   ? 21.304  -13.949 35.544 1.00 16.88 ? 821 HOH B O   1 
HETATM 4551 O O   . HOH E 4 .   ? 7.283   4.003   39.002 1.00 28.20 ? 822 HOH B O   1 
HETATM 4552 O O   . HOH E 4 .   ? 21.961  -24.109 31.723 1.00 16.09 ? 823 HOH B O   1 
HETATM 4553 O O   . HOH E 4 .   ? 7.473   -35.948 19.206 1.00 19.10 ? 824 HOH B O   1 
HETATM 4554 O O   . HOH E 4 .   ? 0.720   -22.501 4.790  1.00 21.21 ? 825 HOH B O   1 
HETATM 4555 O O   . HOH E 4 .   ? -36.600 -22.088 11.879 1.00 41.92 ? 826 HOH B O   1 
HETATM 4556 O O   . HOH E 4 .   ? 24.676  -18.799 38.505 1.00 32.95 ? 827 HOH B O   1 
HETATM 4557 O O   . HOH E 4 .   ? -7.736  -24.114 40.034 1.00 19.69 ? 828 HOH B O   1 
HETATM 4558 O O   . HOH E 4 .   ? 17.853  -18.318 3.873  1.00 34.77 ? 829 HOH B O   1 
HETATM 4559 O O   . HOH E 4 .   ? -7.678  -21.169 27.478 1.00 33.38 ? 830 HOH B O   1 
HETATM 4560 O O   . HOH E 4 .   ? -7.734  -27.220 20.975 1.00 21.38 ? 831 HOH B O   1 
HETATM 4561 O O   . HOH E 4 .   ? -21.723 -27.235 8.634  1.00 25.18 ? 832 HOH B O   1 
HETATM 4562 O O   . HOH E 4 .   ? -12.911 -29.111 -1.233 1.00 32.65 ? 833 HOH B O   1 
HETATM 4563 O O   . HOH E 4 .   ? -21.198 -16.297 20.802 1.00 26.48 ? 834 HOH B O   1 
HETATM 4564 O O   . HOH E 4 .   ? 5.757   -38.179 18.656 1.00 26.33 ? 835 HOH B O   1 
HETATM 4565 O O   . HOH E 4 .   ? -7.609  -23.424 14.432 1.00 17.80 ? 836 HOH B O   1 
HETATM 4566 O O   . HOH E 4 .   ? -22.387 -15.786 22.980 1.00 30.13 ? 837 HOH B O   1 
HETATM 4567 O O   . HOH E 4 .   ? 1.289   -33.898 38.153 1.00 18.78 ? 838 HOH B O   1 
HETATM 4568 O O   . HOH E 4 .   ? 0.777   -31.187 41.096 1.00 28.71 ? 839 HOH B O   1 
HETATM 4569 O O   . HOH E 4 .   ? 1.821   -40.196 25.043 1.00 23.10 ? 840 HOH B O   1 
HETATM 4570 O O   . HOH E 4 .   ? 16.842  -19.144 45.970 1.00 23.39 ? 841 HOH B O   1 
HETATM 4571 O O   . HOH E 4 .   ? -7.372  -22.919 19.280 1.00 26.24 ? 842 HOH B O   1 
HETATM 4572 O O   . HOH E 4 .   ? 15.491  -42.622 23.848 1.00 31.05 ? 843 HOH B O   1 
HETATM 4573 O O   . HOH E 4 .   ? 13.603  -3.481  21.399 1.00 39.06 ? 844 HOH B O   1 
HETATM 4574 O O   . HOH E 4 .   ? -38.360 -29.700 12.318 1.00 33.63 ? 845 HOH B O   1 
HETATM 4575 O O   . HOH E 4 .   ? 26.305  -23.217 25.838 1.00 25.17 ? 846 HOH B O   1 
HETATM 4576 O O   . HOH E 4 .   ? 8.945   -3.987  15.700 1.00 43.49 ? 847 HOH B O   1 
HETATM 4577 O O   . HOH E 4 .   ? -21.523 -43.182 -2.572 1.00 52.70 ? 848 HOH B O   1 
HETATM 4578 O O   . HOH E 4 .   ? 10.838  -19.532 48.744 1.00 24.25 ? 849 HOH B O   1 
HETATM 4579 O O   . HOH E 4 .   ? 25.574  -25.657 25.129 1.00 23.91 ? 850 HOH B O   1 
HETATM 4580 O O   . HOH E 4 .   ? 18.584  -13.586 35.533 1.00 20.81 ? 851 HOH B O   1 
HETATM 4581 O O   . HOH E 4 .   ? -19.551 -34.652 32.639 1.00 36.25 ? 852 HOH B O   1 
HETATM 4582 O O   . HOH E 4 .   ? -9.091  -17.508 6.640  1.00 34.61 ? 853 HOH B O   1 
HETATM 4583 O O   . HOH E 4 .   ? -13.346 -40.929 22.339 1.00 36.23 ? 854 HOH B O   1 
HETATM 4584 O O   . HOH E 4 .   ? 12.700  -15.319 46.260 1.00 24.45 ? 855 HOH B O   1 
HETATM 4585 O O   . HOH E 4 .   ? -10.930 -27.092 45.584 1.00 30.95 ? 856 HOH B O   1 
HETATM 4586 O O   . HOH E 4 .   ? -15.734 -20.841 0.169  1.00 32.48 ? 857 HOH B O   1 
HETATM 4587 O O   . HOH E 4 .   ? 14.127  -15.184 1.429  1.00 40.44 ? 858 HOH B O   1 
HETATM 4588 O O   . HOH E 4 .   ? 23.474  -12.430 35.504 1.00 25.32 ? 859 HOH B O   1 
HETATM 4589 O O   . HOH E 4 .   ? 14.425  -8.775  14.092 1.00 35.47 ? 860 HOH B O   1 
HETATM 4590 O O   . HOH E 4 .   ? 21.306  -31.391 35.047 1.00 39.51 ? 861 HOH B O   1 
HETATM 4591 O O   . HOH E 4 .   ? -7.160  -21.538 3.523  1.00 36.37 ? 862 HOH B O   1 
HETATM 4592 O O   . HOH E 4 .   ? 21.829  -6.402  33.819 1.00 31.62 ? 863 HOH B O   1 
HETATM 4593 O O   . HOH E 4 .   ? 20.580  -13.519 39.483 1.00 31.83 ? 864 HOH B O   1 
HETATM 4594 O O   . HOH E 4 .   ? 12.198  -35.392 10.263 1.00 30.25 ? 865 HOH B O   1 
HETATM 4595 O O   . HOH E 4 .   ? -0.106  -35.131 7.784  1.00 35.95 ? 866 HOH B O   1 
HETATM 4596 O O   . HOH E 4 .   ? 7.666   -37.690 31.895 1.00 29.01 ? 867 HOH B O   1 
HETATM 4597 O O   . HOH E 4 .   ? -23.840 -34.314 15.759 1.00 24.40 ? 868 HOH B O   1 
HETATM 4598 O O   . HOH E 4 .   ? 16.069  -1.128  33.611 1.00 46.22 ? 869 HOH B O   1 
HETATM 4599 O O   . HOH E 4 .   ? -0.254  -3.535  4.327  1.00 61.29 ? 870 HOH B O   1 
HETATM 4600 O O   . HOH E 4 .   ? -6.842  -39.900 13.381 1.00 40.37 ? 871 HOH B O   1 
HETATM 4601 O O   . HOH E 4 .   ? -32.404 -15.847 12.200 1.00 40.29 ? 872 HOH B O   1 
HETATM 4602 O O   . HOH E 4 .   ? -6.451  -23.123 36.119 1.00 24.53 ? 873 HOH B O   1 
HETATM 4603 O O   . HOH E 4 .   ? -20.278 -33.210 14.876 1.00 25.66 ? 874 HOH B O   1 
HETATM 4604 O O   . HOH E 4 .   ? 3.131   -6.029  8.583  1.00 50.81 ? 875 HOH B O   1 
HETATM 4605 O O   . HOH E 4 .   ? 16.639  -2.415  23.313 1.00 46.81 ? 876 HOH B O   1 
HETATM 4606 O O   . HOH E 4 .   ? -5.265  -19.811 6.668  1.00 42.35 ? 877 HOH B O   1 
HETATM 4607 O O   . HOH E 4 .   ? 5.099   -7.026  12.899 1.00 36.57 ? 878 HOH B O   1 
HETATM 4608 O O   . HOH E 4 .   ? 0.977   -44.798 11.041 1.00 36.00 ? 879 HOH B O   1 
HETATM 4609 O O   . HOH E 4 .   ? -12.077 -35.789 0.223  1.00 45.96 ? 880 HOH B O   1 
HETATM 4610 O O   . HOH E 4 .   ? 9.027   -3.677  41.960 1.00 35.53 ? 881 HOH B O   1 
HETATM 4611 O O   . HOH E 4 .   ? -2.517  -41.144 22.566 1.00 25.43 ? 882 HOH B O   1 
HETATM 4612 O O   . HOH E 4 .   ? -10.298 -9.823  26.349 1.00 38.14 ? 883 HOH B O   1 
HETATM 4613 O O   . HOH E 4 .   ? 27.168  -25.700 28.774 1.00 35.15 ? 884 HOH B O   1 
HETATM 4614 O O   . HOH E 4 .   ? -5.820  -38.487 25.120 1.00 38.52 ? 885 HOH B O   1 
HETATM 4615 O O   . HOH E 4 .   ? -27.005 -18.057 31.248 1.00 51.39 ? 886 HOH B O   1 
HETATM 4616 O O   . HOH E 4 .   ? 5.940   -19.851 6.648  1.00 31.74 ? 887 HOH B O   1 
HETATM 4617 O O   . HOH E 4 .   ? -25.531 -31.694 12.508 1.00 32.22 ? 888 HOH B O   1 
HETATM 4618 O O   . HOH E 4 .   ? 11.591  -23.669 48.144 1.00 27.53 ? 889 HOH B O   1 
HETATM 4619 O O   . HOH E 4 .   ? -29.740 -40.482 15.916 1.00 42.47 ? 890 HOH B O   1 
HETATM 4620 O O   . HOH E 4 .   ? -6.721  -29.748 39.548 1.00 24.99 ? 891 HOH B O   1 
HETATM 4621 O O   . HOH E 4 .   ? -7.216  -7.466  36.038 1.00 25.36 ? 892 HOH B O   1 
HETATM 4622 O O   . HOH E 4 .   ? -5.623  -24.629 15.751 1.00 18.17 ? 893 HOH B O   1 
HETATM 4623 O O   . HOH E 4 .   ? 2.173   -7.072  12.623 1.00 31.34 ? 894 HOH B O   1 
HETATM 4624 O O   . HOH E 4 .   ? 1.834   -15.214 5.531  1.00 29.98 ? 895 HOH B O   1 
HETATM 4625 O O   . HOH E 4 .   ? 27.654  -27.558 24.396 1.00 34.29 ? 896 HOH B O   1 
HETATM 4626 O O   . HOH F 4 .   ? 22.357  -35.285 24.145 1.00 31.72 ? 101 HOH L O   1 
HETATM 4627 O O   . HOH F 4 .   ? 18.903  -34.020 31.183 1.00 24.56 ? 102 HOH L O   1 
HETATM 4628 O O   . HOH F 4 .   ? 24.902  -26.623 27.311 1.00 18.92 ? 103 HOH L O   1 
HETATM 4629 O O   . HOH F 4 .   ? 20.199  -26.067 32.468 1.00 17.08 ? 104 HOH L O   1 
HETATM 4630 O O   . HOH F 4 .   ? 16.571  -39.124 29.856 1.00 34.95 ? 105 HOH L O   1 
HETATM 4631 O O   . HOH F 4 .   ? 23.042  -35.463 31.837 1.00 34.96 ? 106 HOH L O   1 
HETATM 4632 O O   . HOH F 4 .   ? 25.831  -31.581 26.418 1.00 17.90 ? 107 HOH L O   1 
HETATM 4633 O O   . HOH F 4 .   ? 18.722  -36.618 32.778 1.00 37.61 ? 108 HOH L O   1 
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