data_9IIS
# 
_entry.id   9IIS 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9IIS         pdb_00009iis 10.2210/pdb9iis/pdb 
WWPDB D_1300048874 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.title'          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IIS 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        'different part of FKP' 
_pdbx_database_related.db_id          9iip 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              chunhung@gate.sinica.edu.tw 
_pdbx_contact_author.name_first         Chun-Hung 
_pdbx_contact_author.name_last          Lin 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6795-8825 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ko, T.P.'  1 0000-0003-1794-2638 
'Lin, S.W.' 2 0000-0001-7777-2090 
'Hsu, M.F.' 3 0000-0002-5473-5171 
'Lin, C.H.' 4 0000-0002-6795-8825 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            301 
_citation.language                  ? 
_citation.page_first                108344 
_citation.page_last                 108344 
_citation.title                     
'Structural insight into the catalytic mechanism of the bifunctional enzyme l-fucokinase/GDP-fucose pyrophosphorylase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2025.108344 
_citation.pdbx_database_id_PubMed   39993526 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lin, S.W.'    1 ? 
primary 'Ko, T.P.'     2 ? 
primary 'Chiang, H.Y.' 3 ? 
primary 'Wu, C.G.'     4 ? 
primary 'Hsu, M.F.'    5 ? 
primary 'Wang, A.H.'   6 ? 
primary 'Lin, C.H.'    7 ? 
# 
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 'Ubiquitin-like protein SMT3,L-fucokinase/L-fucose-1-P guanylyltransferase' 69781.258 1   ? ? ? 
'GDP-fucose pyrophosphorylase part of FKP with a SUMO tag' 
2 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'                       238.305   1   ? ? ? ? 
3 non-polymer syn 'ACETATE ION'                                                               59.044    1   ? ? ? ? 
4 water       nat water                                                                       18.015    220 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGSSHHHHHHGSGLVPRGSASMSDSEVNQEAKPEVKPEVKPETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKE
MDSLRFLYDGIRIQADQTPEDLDMEDNDIIEAHREQIGGEFMQKLLSLPSNLVQSFHELERVNRTDWFCTSDPVGKKLGS
GGGTSWLLEECYNEYSDGATFGEWLEKEKRILLHAGGQSRRLPGYAPSGKILTPVPVFRWERGQHLGQNLLSLQLPLYEK
IMSLAPDKLHTLIASGDVYIRSEKPLQSIPEADVVCYGLWVDPSLATHHGVFASDRKHPEQLDFMLQKPSLAELESLSKT
HLFLMDIGIWLLSDRAVEILMKRSHKESSEELKYYDLYSDFGLALGTHPRIEDEEVNTLSVAILPLPGGEFYHYGTSKEL
ISSTLSVQNKVYDQRRIMHRKVKPNPAMFVQNAVVRIPLCAENADLWIENSHIGPKWKIASRHIITGVPENDWSLAVPAG
VCVDVVPMGDKGFVARPYGLDDVFKGDLRDSKTTLTGIPFGEWMSKRGLSYTDLKGRTDDLQAVSVFPMVNSVEELGLVL
RWMLSEPELEEGKNIWLRSEHFSADEISAGANLKRLYAQREEFRKGNWKALAVNHEK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHGSGLVPRGSASMSDSEVNQEAKPEVKPEVKPETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKE
MDSLRFLYDGIRIQADQTPEDLDMEDNDIIEAHREQIGGEFMQKLLSLPSNLVQSFHELERVNRTDWFCTSDPVGKKLGS
GGGTSWLLEECYNEYSDGATFGEWLEKEKRILLHAGGQSRRLPGYAPSGKILTPVPVFRWERGQHLGQNLLSLQLPLYEK
IMSLAPDKLHTLIASGDVYIRSEKPLQSIPEADVVCYGLWVDPSLATHHGVFASDRKHPEQLDFMLQKPSLAELESLSKT
HLFLMDIGIWLLSDRAVEILMKRSHKESSEELKYYDLYSDFGLALGTHPRIEDEEVNTLSVAILPLPGGEFYHYGTSKEL
ISSTLSVQNKVYDQRRIMHRKVKPNPAMFVQNAVVRIPLCAENADLWIENSHIGPKWKIASRHIITGVPENDWSLAVPAG
VCVDVVPMGDKGFVARPYGLDDVFKGDLRDSKTTLTGIPFGEWMSKRGLSYTDLKGRTDDLQAVSVFPMVNSVEELGLVL
RWMLSEPELEEGKNIWLRSEHFSADEISAGANLKRLYAQREEFRKGNWKALAVNHEK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 
3 'ACETATE ION'                                         ACT 
4 water                                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  GLY n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  ALA n 
1 21  SER n 
1 22  MET n 
1 23  SER n 
1 24  ASP n 
1 25  SER n 
1 26  GLU n 
1 27  VAL n 
1 28  ASN n 
1 29  GLN n 
1 30  GLU n 
1 31  ALA n 
1 32  LYS n 
1 33  PRO n 
1 34  GLU n 
1 35  VAL n 
1 36  LYS n 
1 37  PRO n 
1 38  GLU n 
1 39  VAL n 
1 40  LYS n 
1 41  PRO n 
1 42  GLU n 
1 43  THR n 
1 44  HIS n 
1 45  ILE n 
1 46  ASN n 
1 47  LEU n 
1 48  LYS n 
1 49  VAL n 
1 50  SER n 
1 51  ASP n 
1 52  GLY n 
1 53  SER n 
1 54  SER n 
1 55  GLU n 
1 56  ILE n 
1 57  PHE n 
1 58  PHE n 
1 59  LYS n 
1 60  ILE n 
1 61  LYS n 
1 62  LYS n 
1 63  THR n 
1 64  THR n 
1 65  PRO n 
1 66  LEU n 
1 67  ARG n 
1 68  ARG n 
1 69  LEU n 
1 70  MET n 
1 71  GLU n 
1 72  ALA n 
1 73  PHE n 
1 74  ALA n 
1 75  LYS n 
1 76  ARG n 
1 77  GLN n 
1 78  GLY n 
1 79  LYS n 
1 80  GLU n 
1 81  MET n 
1 82  ASP n 
1 83  SER n 
1 84  LEU n 
1 85  ARG n 
1 86  PHE n 
1 87  LEU n 
1 88  TYR n 
1 89  ASP n 
1 90  GLY n 
1 91  ILE n 
1 92  ARG n 
1 93  ILE n 
1 94  GLN n 
1 95  ALA n 
1 96  ASP n 
1 97  GLN n 
1 98  THR n 
1 99  PRO n 
1 100 GLU n 
1 101 ASP n 
1 102 LEU n 
1 103 ASP n 
1 104 MET n 
1 105 GLU n 
1 106 ASP n 
1 107 ASN n 
1 108 ASP n 
1 109 ILE n 
1 110 ILE n 
1 111 GLU n 
1 112 ALA n 
1 113 HIS n 
1 114 ARG n 
1 115 GLU n 
1 116 GLN n 
1 117 ILE n 
1 118 GLY n 
1 119 GLY n 
1 120 GLU n 
1 121 PHE n 
1 122 MET n 
1 123 GLN n 
1 124 LYS n 
1 125 LEU n 
1 126 LEU n 
1 127 SER n 
1 128 LEU n 
1 129 PRO n 
1 130 SER n 
1 131 ASN n 
1 132 LEU n 
1 133 VAL n 
1 134 GLN n 
1 135 SER n 
1 136 PHE n 
1 137 HIS n 
1 138 GLU n 
1 139 LEU n 
1 140 GLU n 
1 141 ARG n 
1 142 VAL n 
1 143 ASN n 
1 144 ARG n 
1 145 THR n 
1 146 ASP n 
1 147 TRP n 
1 148 PHE n 
1 149 CYS n 
1 150 THR n 
1 151 SER n 
1 152 ASP n 
1 153 PRO n 
1 154 VAL n 
1 155 GLY n 
1 156 LYS n 
1 157 LYS n 
1 158 LEU n 
1 159 GLY n 
1 160 SER n 
1 161 GLY n 
1 162 GLY n 
1 163 GLY n 
1 164 THR n 
1 165 SER n 
1 166 TRP n 
1 167 LEU n 
1 168 LEU n 
1 169 GLU n 
1 170 GLU n 
1 171 CYS n 
1 172 TYR n 
1 173 ASN n 
1 174 GLU n 
1 175 TYR n 
1 176 SER n 
1 177 ASP n 
1 178 GLY n 
1 179 ALA n 
1 180 THR n 
1 181 PHE n 
1 182 GLY n 
1 183 GLU n 
1 184 TRP n 
1 185 LEU n 
1 186 GLU n 
1 187 LYS n 
1 188 GLU n 
1 189 LYS n 
1 190 ARG n 
1 191 ILE n 
1 192 LEU n 
1 193 LEU n 
1 194 HIS n 
1 195 ALA n 
1 196 GLY n 
1 197 GLY n 
1 198 GLN n 
1 199 SER n 
1 200 ARG n 
1 201 ARG n 
1 202 LEU n 
1 203 PRO n 
1 204 GLY n 
1 205 TYR n 
1 206 ALA n 
1 207 PRO n 
1 208 SER n 
1 209 GLY n 
1 210 LYS n 
1 211 ILE n 
1 212 LEU n 
1 213 THR n 
1 214 PRO n 
1 215 VAL n 
1 216 PRO n 
1 217 VAL n 
1 218 PHE n 
1 219 ARG n 
1 220 TRP n 
1 221 GLU n 
1 222 ARG n 
1 223 GLY n 
1 224 GLN n 
1 225 HIS n 
1 226 LEU n 
1 227 GLY n 
1 228 GLN n 
1 229 ASN n 
1 230 LEU n 
1 231 LEU n 
1 232 SER n 
1 233 LEU n 
1 234 GLN n 
1 235 LEU n 
1 236 PRO n 
1 237 LEU n 
1 238 TYR n 
1 239 GLU n 
1 240 LYS n 
1 241 ILE n 
1 242 MET n 
1 243 SER n 
1 244 LEU n 
1 245 ALA n 
1 246 PRO n 
1 247 ASP n 
1 248 LYS n 
1 249 LEU n 
1 250 HIS n 
1 251 THR n 
1 252 LEU n 
1 253 ILE n 
1 254 ALA n 
1 255 SER n 
1 256 GLY n 
1 257 ASP n 
1 258 VAL n 
1 259 TYR n 
1 260 ILE n 
1 261 ARG n 
1 262 SER n 
1 263 GLU n 
1 264 LYS n 
1 265 PRO n 
1 266 LEU n 
1 267 GLN n 
1 268 SER n 
1 269 ILE n 
1 270 PRO n 
1 271 GLU n 
1 272 ALA n 
1 273 ASP n 
1 274 VAL n 
1 275 VAL n 
1 276 CYS n 
1 277 TYR n 
1 278 GLY n 
1 279 LEU n 
1 280 TRP n 
1 281 VAL n 
1 282 ASP n 
1 283 PRO n 
1 284 SER n 
1 285 LEU n 
1 286 ALA n 
1 287 THR n 
1 288 HIS n 
1 289 HIS n 
1 290 GLY n 
1 291 VAL n 
1 292 PHE n 
1 293 ALA n 
1 294 SER n 
1 295 ASP n 
1 296 ARG n 
1 297 LYS n 
1 298 HIS n 
1 299 PRO n 
1 300 GLU n 
1 301 GLN n 
1 302 LEU n 
1 303 ASP n 
1 304 PHE n 
1 305 MET n 
1 306 LEU n 
1 307 GLN n 
1 308 LYS n 
1 309 PRO n 
1 310 SER n 
1 311 LEU n 
1 312 ALA n 
1 313 GLU n 
1 314 LEU n 
1 315 GLU n 
1 316 SER n 
1 317 LEU n 
1 318 SER n 
1 319 LYS n 
1 320 THR n 
1 321 HIS n 
1 322 LEU n 
1 323 PHE n 
1 324 LEU n 
1 325 MET n 
1 326 ASP n 
1 327 ILE n 
1 328 GLY n 
1 329 ILE n 
1 330 TRP n 
1 331 LEU n 
1 332 LEU n 
1 333 SER n 
1 334 ASP n 
1 335 ARG n 
1 336 ALA n 
1 337 VAL n 
1 338 GLU n 
1 339 ILE n 
1 340 LEU n 
1 341 MET n 
1 342 LYS n 
1 343 ARG n 
1 344 SER n 
1 345 HIS n 
1 346 LYS n 
1 347 GLU n 
1 348 SER n 
1 349 SER n 
1 350 GLU n 
1 351 GLU n 
1 352 LEU n 
1 353 LYS n 
1 354 TYR n 
1 355 TYR n 
1 356 ASP n 
1 357 LEU n 
1 358 TYR n 
1 359 SER n 
1 360 ASP n 
1 361 PHE n 
1 362 GLY n 
1 363 LEU n 
1 364 ALA n 
1 365 LEU n 
1 366 GLY n 
1 367 THR n 
1 368 HIS n 
1 369 PRO n 
1 370 ARG n 
1 371 ILE n 
1 372 GLU n 
1 373 ASP n 
1 374 GLU n 
1 375 GLU n 
1 376 VAL n 
1 377 ASN n 
1 378 THR n 
1 379 LEU n 
1 380 SER n 
1 381 VAL n 
1 382 ALA n 
1 383 ILE n 
1 384 LEU n 
1 385 PRO n 
1 386 LEU n 
1 387 PRO n 
1 388 GLY n 
1 389 GLY n 
1 390 GLU n 
1 391 PHE n 
1 392 TYR n 
1 393 HIS n 
1 394 TYR n 
1 395 GLY n 
1 396 THR n 
1 397 SER n 
1 398 LYS n 
1 399 GLU n 
1 400 LEU n 
1 401 ILE n 
1 402 SER n 
1 403 SER n 
1 404 THR n 
1 405 LEU n 
1 406 SER n 
1 407 VAL n 
1 408 GLN n 
1 409 ASN n 
1 410 LYS n 
1 411 VAL n 
1 412 TYR n 
1 413 ASP n 
1 414 GLN n 
1 415 ARG n 
1 416 ARG n 
1 417 ILE n 
1 418 MET n 
1 419 HIS n 
1 420 ARG n 
1 421 LYS n 
1 422 VAL n 
1 423 LYS n 
1 424 PRO n 
1 425 ASN n 
1 426 PRO n 
1 427 ALA n 
1 428 MET n 
1 429 PHE n 
1 430 VAL n 
1 431 GLN n 
1 432 ASN n 
1 433 ALA n 
1 434 VAL n 
1 435 VAL n 
1 436 ARG n 
1 437 ILE n 
1 438 PRO n 
1 439 LEU n 
1 440 CYS n 
1 441 ALA n 
1 442 GLU n 
1 443 ASN n 
1 444 ALA n 
1 445 ASP n 
1 446 LEU n 
1 447 TRP n 
1 448 ILE n 
1 449 GLU n 
1 450 ASN n 
1 451 SER n 
1 452 HIS n 
1 453 ILE n 
1 454 GLY n 
1 455 PRO n 
1 456 LYS n 
1 457 TRP n 
1 458 LYS n 
1 459 ILE n 
1 460 ALA n 
1 461 SER n 
1 462 ARG n 
1 463 HIS n 
1 464 ILE n 
1 465 ILE n 
1 466 THR n 
1 467 GLY n 
1 468 VAL n 
1 469 PRO n 
1 470 GLU n 
1 471 ASN n 
1 472 ASP n 
1 473 TRP n 
1 474 SER n 
1 475 LEU n 
1 476 ALA n 
1 477 VAL n 
1 478 PRO n 
1 479 ALA n 
1 480 GLY n 
1 481 VAL n 
1 482 CYS n 
1 483 VAL n 
1 484 ASP n 
1 485 VAL n 
1 486 VAL n 
1 487 PRO n 
1 488 MET n 
1 489 GLY n 
1 490 ASP n 
1 491 LYS n 
1 492 GLY n 
1 493 PHE n 
1 494 VAL n 
1 495 ALA n 
1 496 ARG n 
1 497 PRO n 
1 498 TYR n 
1 499 GLY n 
1 500 LEU n 
1 501 ASP n 
1 502 ASP n 
1 503 VAL n 
1 504 PHE n 
1 505 LYS n 
1 506 GLY n 
1 507 ASP n 
1 508 LEU n 
1 509 ARG n 
1 510 ASP n 
1 511 SER n 
1 512 LYS n 
1 513 THR n 
1 514 THR n 
1 515 LEU n 
1 516 THR n 
1 517 GLY n 
1 518 ILE n 
1 519 PRO n 
1 520 PHE n 
1 521 GLY n 
1 522 GLU n 
1 523 TRP n 
1 524 MET n 
1 525 SER n 
1 526 LYS n 
1 527 ARG n 
1 528 GLY n 
1 529 LEU n 
1 530 SER n 
1 531 TYR n 
1 532 THR n 
1 533 ASP n 
1 534 LEU n 
1 535 LYS n 
1 536 GLY n 
1 537 ARG n 
1 538 THR n 
1 539 ASP n 
1 540 ASP n 
1 541 LEU n 
1 542 GLN n 
1 543 ALA n 
1 544 VAL n 
1 545 SER n 
1 546 VAL n 
1 547 PHE n 
1 548 PRO n 
1 549 MET n 
1 550 VAL n 
1 551 ASN n 
1 552 SER n 
1 553 VAL n 
1 554 GLU n 
1 555 GLU n 
1 556 LEU n 
1 557 GLY n 
1 558 LEU n 
1 559 VAL n 
1 560 LEU n 
1 561 ARG n 
1 562 TRP n 
1 563 MET n 
1 564 LEU n 
1 565 SER n 
1 566 GLU n 
1 567 PRO n 
1 568 GLU n 
1 569 LEU n 
1 570 GLU n 
1 571 GLU n 
1 572 GLY n 
1 573 LYS n 
1 574 ASN n 
1 575 ILE n 
1 576 TRP n 
1 577 LEU n 
1 578 ARG n 
1 579 SER n 
1 580 GLU n 
1 581 HIS n 
1 582 PHE n 
1 583 SER n 
1 584 ALA n 
1 585 ASP n 
1 586 GLU n 
1 587 ILE n 
1 588 SER n 
1 589 ALA n 
1 590 GLY n 
1 591 ALA n 
1 592 ASN n 
1 593 LEU n 
1 594 LYS n 
1 595 ARG n 
1 596 LEU n 
1 597 TYR n 
1 598 ALA n 
1 599 GLN n 
1 600 ARG n 
1 601 GLU n 
1 602 GLU n 
1 603 PHE n 
1 604 ARG n 
1 605 LYS n 
1 606 GLY n 
1 607 ASN n 
1 608 TRP n 
1 609 LYS n 
1 610 ALA n 
1 611 LEU n 
1 612 ALA n 
1 613 VAL n 
1 614 ASN n 
1 615 HIS n 
1 616 GLU n 
1 617 LYS 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   121 ? ? SMT3 ? ? ? ? ? ? 'Saccharomyces cerevisiae S288C' 559292 ? ? ? ? ? ? ? ? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? plasmid ? ? ? pET-SUMO ? ? 
1 2 sample 'Biological sequence' 122 617 ? ? fkp  ? ? ? ? ? ? 'Bacteroides fragilis'           817    ? ? ? ? ? ? ? ? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? plasmid ? ? ? pET-SUMO ? ? 
# 
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 
ACT non-polymer         . 'ACETATE ION'                                         ?     'C2 H3 O2 -1'    59.044  
ALA 'L-peptide linking' y ALANINE                                               ?     'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                              ?     'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                            ?     'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                       ?     'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                              ?     'C3 H7 N O2 S'   121.158 
EPE non-polymer         . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S' 238.305 
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 
MET 'L-peptide linking' y METHIONINE                                            ?     'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                         ?     'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                               ?     'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                ?     'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                             ?     'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                            ?     'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                              ?     'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                ?     'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -120 ?   ?   ?   A . n 
A 1 2   GLY 2   -119 ?   ?   ?   A . n 
A 1 3   SER 3   -118 ?   ?   ?   A . n 
A 1 4   SER 4   -117 ?   ?   ?   A . n 
A 1 5   HIS 5   -116 ?   ?   ?   A . n 
A 1 6   HIS 6   -115 ?   ?   ?   A . n 
A 1 7   HIS 7   -114 ?   ?   ?   A . n 
A 1 8   HIS 8   -113 ?   ?   ?   A . n 
A 1 9   HIS 9   -112 ?   ?   ?   A . n 
A 1 10  HIS 10  -111 ?   ?   ?   A . n 
A 1 11  GLY 11  -110 ?   ?   ?   A . n 
A 1 12  SER 12  -109 ?   ?   ?   A . n 
A 1 13  GLY 13  -108 ?   ?   ?   A . n 
A 1 14  LEU 14  -107 ?   ?   ?   A . n 
A 1 15  VAL 15  -106 ?   ?   ?   A . n 
A 1 16  PRO 16  -105 ?   ?   ?   A . n 
A 1 17  ARG 17  -104 ?   ?   ?   A . n 
A 1 18  GLY 18  -103 ?   ?   ?   A . n 
A 1 19  SER 19  -102 ?   ?   ?   A . n 
A 1 20  ALA 20  -101 ?   ?   ?   A . n 
A 1 21  SER 21  -100 ?   ?   ?   A . n 
A 1 22  MET 22  -99  ?   ?   ?   A . n 
A 1 23  SER 23  -98  ?   ?   ?   A . n 
A 1 24  ASP 24  -97  ?   ?   ?   A . n 
A 1 25  SER 25  -96  ?   ?   ?   A . n 
A 1 26  GLU 26  -95  ?   ?   ?   A . n 
A 1 27  VAL 27  -94  ?   ?   ?   A . n 
A 1 28  ASN 28  -93  ?   ?   ?   A . n 
A 1 29  GLN 29  -92  ?   ?   ?   A . n 
A 1 30  GLU 30  -91  ?   ?   ?   A . n 
A 1 31  ALA 31  -90  ?   ?   ?   A . n 
A 1 32  LYS 32  -89  ?   ?   ?   A . n 
A 1 33  PRO 33  -88  ?   ?   ?   A . n 
A 1 34  GLU 34  -87  ?   ?   ?   A . n 
A 1 35  VAL 35  -86  ?   ?   ?   A . n 
A 1 36  LYS 36  -85  ?   ?   ?   A . n 
A 1 37  PRO 37  -84  ?   ?   ?   A . n 
A 1 38  GLU 38  -83  ?   ?   ?   A . n 
A 1 39  VAL 39  -82  ?   ?   ?   A . n 
A 1 40  LYS 40  -81  ?   ?   ?   A . n 
A 1 41  PRO 41  -80  ?   ?   ?   A . n 
A 1 42  GLU 42  -79  ?   ?   ?   A . n 
A 1 43  THR 43  -78  -78 THR THR A . n 
A 1 44  HIS 44  -77  -77 HIS HIS A . n 
A 1 45  ILE 45  -76  -76 ILE ILE A . n 
A 1 46  ASN 46  -75  -75 ASN ASN A . n 
A 1 47  LEU 47  -74  -74 LEU LEU A . n 
A 1 48  LYS 48  -73  -73 LYS LYS A . n 
A 1 49  VAL 49  -72  -72 VAL VAL A . n 
A 1 50  SER 50  -71  -71 SER SER A . n 
A 1 51  ASP 51  -70  -70 ASP ASP A . n 
A 1 52  GLY 52  -69  -69 GLY GLY A . n 
A 1 53  SER 53  -68  -68 SER SER A . n 
A 1 54  SER 54  -67  -67 SER SER A . n 
A 1 55  GLU 55  -66  -66 GLU GLU A . n 
A 1 56  ILE 56  -65  -65 ILE ILE A . n 
A 1 57  PHE 57  -64  -64 PHE PHE A . n 
A 1 58  PHE 58  -63  -63 PHE PHE A . n 
A 1 59  LYS 59  -62  -62 LYS LYS A . n 
A 1 60  ILE 60  -61  -61 ILE ILE A . n 
A 1 61  LYS 61  -60  -60 LYS LYS A . n 
A 1 62  LYS 62  -59  -59 LYS LYS A . n 
A 1 63  THR 63  -58  -58 THR THR A . n 
A 1 64  THR 64  -57  -57 THR THR A . n 
A 1 65  PRO 65  -56  -56 PRO PRO A . n 
A 1 66  LEU 66  -55  -55 LEU LEU A . n 
A 1 67  ARG 67  -54  -54 ARG ARG A . n 
A 1 68  ARG 68  -53  -53 ARG ARG A . n 
A 1 69  LEU 69  -52  -52 LEU LEU A . n 
A 1 70  MET 70  -51  -51 MET MET A . n 
A 1 71  GLU 71  -50  -50 GLU GLU A . n 
A 1 72  ALA 72  -49  -49 ALA ALA A . n 
A 1 73  PHE 73  -48  -48 PHE PHE A . n 
A 1 74  ALA 74  -47  -47 ALA ALA A . n 
A 1 75  LYS 75  -46  -46 LYS LYS A . n 
A 1 76  ARG 76  -45  -45 ARG ARG A . n 
A 1 77  GLN 77  -44  -44 GLN GLN A . n 
A 1 78  GLY 78  -43  -43 GLY GLY A . n 
A 1 79  LYS 79  -42  -42 LYS LYS A . n 
A 1 80  GLU 80  -41  -41 GLU GLU A . n 
A 1 81  MET 81  -40  -40 MET MET A . n 
A 1 82  ASP 82  -39  -39 ASP ASP A . n 
A 1 83  SER 83  -38  -38 SER SER A . n 
A 1 84  LEU 84  -37  -37 LEU LEU A . n 
A 1 85  ARG 85  -36  -36 ARG ARG A . n 
A 1 86  PHE 86  -35  -35 PHE PHE A . n 
A 1 87  LEU 87  -34  -34 LEU LEU A . n 
A 1 88  TYR 88  -33  -33 TYR TYR A . n 
A 1 89  ASP 89  -32  -32 ASP ASP A . n 
A 1 90  GLY 90  -31  -31 GLY GLY A . n 
A 1 91  ILE 91  -30  -30 ILE ILE A . n 
A 1 92  ARG 92  -29  -29 ARG ARG A . n 
A 1 93  ILE 93  -28  -28 ILE ILE A . n 
A 1 94  GLN 94  -27  -27 GLN GLN A . n 
A 1 95  ALA 95  -26  -26 ALA ALA A . n 
A 1 96  ASP 96  -25  -25 ASP ASP A . n 
A 1 97  GLN 97  -24  -24 GLN GLN A . n 
A 1 98  THR 98  -23  -23 THR THR A . n 
A 1 99  PRO 99  -22  -22 PRO PRO A . n 
A 1 100 GLU 100 -21  -21 GLU GLU A . n 
A 1 101 ASP 101 -20  -20 ASP ASP A . n 
A 1 102 LEU 102 -19  -19 LEU LEU A . n 
A 1 103 ASP 103 -18  -18 ASP ASP A . n 
A 1 104 MET 104 -17  -17 MET MET A . n 
A 1 105 GLU 105 -16  -16 GLU GLU A . n 
A 1 106 ASP 106 -15  -15 ASP ASP A . n 
A 1 107 ASN 107 -14  -14 ASN ASN A . n 
A 1 108 ASP 108 -13  -13 ASP ASP A . n 
A 1 109 ILE 109 -12  -12 ILE ILE A . n 
A 1 110 ILE 110 -11  -11 ILE ILE A . n 
A 1 111 GLU 111 -10  -10 GLU GLU A . n 
A 1 112 ALA 112 -9   -9  ALA ALA A . n 
A 1 113 HIS 113 -8   -8  HIS HIS A . n 
A 1 114 ARG 114 -7   -7  ARG ARG A . n 
A 1 115 GLU 115 -6   -6  GLU GLU A . n 
A 1 116 GLN 116 -5   -5  GLN GLN A . n 
A 1 117 ILE 117 -4   -4  ILE ILE A . n 
A 1 118 GLY 118 -3   -3  GLY GLY A . n 
A 1 119 GLY 119 -2   -2  GLY GLY A . n 
A 1 120 GLU 120 -1   -1  GLU GLU A . n 
A 1 121 PHE 121 0    0   PHE PHE A . n 
A 1 122 MET 122 1    1   MET MET A . n 
A 1 123 GLN 123 2    2   GLN GLN A . n 
A 1 124 LYS 124 3    3   LYS LYS A . n 
A 1 125 LEU 125 4    4   LEU LEU A . n 
A 1 126 LEU 126 5    5   LEU LEU A . n 
A 1 127 SER 127 6    6   SER SER A . n 
A 1 128 LEU 128 7    7   LEU LEU A . n 
A 1 129 PRO 129 8    8   PRO PRO A . n 
A 1 130 SER 130 9    9   SER SER A . n 
A 1 131 ASN 131 10   10  ASN ASN A . n 
A 1 132 LEU 132 11   11  LEU LEU A . n 
A 1 133 VAL 133 12   12  VAL VAL A . n 
A 1 134 GLN 134 13   13  GLN GLN A . n 
A 1 135 SER 135 14   14  SER SER A . n 
A 1 136 PHE 136 15   15  PHE PHE A . n 
A 1 137 HIS 137 16   16  HIS HIS A . n 
A 1 138 GLU 138 17   17  GLU GLU A . n 
A 1 139 LEU 139 18   18  LEU LEU A . n 
A 1 140 GLU 140 19   19  GLU GLU A . n 
A 1 141 ARG 141 20   20  ARG ARG A . n 
A 1 142 VAL 142 21   21  VAL VAL A . n 
A 1 143 ASN 143 22   22  ASN ASN A . n 
A 1 144 ARG 144 23   23  ARG ARG A . n 
A 1 145 THR 145 24   24  THR THR A . n 
A 1 146 ASP 146 25   25  ASP ASP A . n 
A 1 147 TRP 147 26   26  TRP TRP A . n 
A 1 148 PHE 148 27   27  PHE PHE A . n 
A 1 149 CYS 149 28   28  CYS CYS A . n 
A 1 150 THR 150 29   29  THR THR A . n 
A 1 151 SER 151 30   30  SER SER A . n 
A 1 152 ASP 152 31   31  ASP ASP A . n 
A 1 153 PRO 153 32   32  PRO PRO A . n 
A 1 154 VAL 154 33   33  VAL VAL A . n 
A 1 155 GLY 155 34   34  GLY GLY A . n 
A 1 156 LYS 156 35   35  LYS LYS A . n 
A 1 157 LYS 157 36   36  LYS LYS A . n 
A 1 158 LEU 158 37   37  LEU LEU A . n 
A 1 159 GLY 159 38   38  GLY GLY A . n 
A 1 160 SER 160 39   39  SER SER A . n 
A 1 161 GLY 161 40   40  GLY GLY A . n 
A 1 162 GLY 162 41   41  GLY GLY A . n 
A 1 163 GLY 163 42   42  GLY GLY A . n 
A 1 164 THR 164 43   43  THR THR A . n 
A 1 165 SER 165 44   44  SER SER A . n 
A 1 166 TRP 166 45   45  TRP TRP A . n 
A 1 167 LEU 167 46   46  LEU LEU A . n 
A 1 168 LEU 168 47   47  LEU LEU A . n 
A 1 169 GLU 169 48   48  GLU GLU A . n 
A 1 170 GLU 170 49   49  GLU GLU A . n 
A 1 171 CYS 171 50   50  CYS CYS A . n 
A 1 172 TYR 172 51   51  TYR TYR A . n 
A 1 173 ASN 173 52   52  ASN ASN A . n 
A 1 174 GLU 174 53   53  GLU GLU A . n 
A 1 175 TYR 175 54   54  TYR TYR A . n 
A 1 176 SER 176 55   55  SER SER A . n 
A 1 177 ASP 177 56   56  ASP ASP A . n 
A 1 178 GLY 178 57   57  GLY GLY A . n 
A 1 179 ALA 179 58   58  ALA ALA A . n 
A 1 180 THR 180 59   59  THR THR A . n 
A 1 181 PHE 181 60   60  PHE PHE A . n 
A 1 182 GLY 182 61   61  GLY GLY A . n 
A 1 183 GLU 183 62   62  GLU GLU A . n 
A 1 184 TRP 184 63   63  TRP TRP A . n 
A 1 185 LEU 185 64   64  LEU LEU A . n 
A 1 186 GLU 186 65   65  GLU GLU A . n 
A 1 187 LYS 187 66   66  LYS LYS A . n 
A 1 188 GLU 188 67   67  GLU GLU A . n 
A 1 189 LYS 189 68   68  LYS LYS A . n 
A 1 190 ARG 190 69   69  ARG ARG A . n 
A 1 191 ILE 191 70   70  ILE ILE A . n 
A 1 192 LEU 192 71   71  LEU LEU A . n 
A 1 193 LEU 193 72   72  LEU LEU A . n 
A 1 194 HIS 194 73   73  HIS HIS A . n 
A 1 195 ALA 195 74   74  ALA ALA A . n 
A 1 196 GLY 196 75   75  GLY GLY A . n 
A 1 197 GLY 197 76   76  GLY GLY A . n 
A 1 198 GLN 198 77   77  GLN GLN A . n 
A 1 199 SER 199 78   78  SER SER A . n 
A 1 200 ARG 200 79   79  ARG ARG A . n 
A 1 201 ARG 201 80   80  ARG ARG A . n 
A 1 202 LEU 202 81   81  LEU LEU A . n 
A 1 203 PRO 203 82   82  PRO PRO A . n 
A 1 204 GLY 204 83   83  GLY GLY A . n 
A 1 205 TYR 205 84   84  TYR TYR A . n 
A 1 206 ALA 206 85   85  ALA ALA A . n 
A 1 207 PRO 207 86   86  PRO PRO A . n 
A 1 208 SER 208 87   87  SER SER A . n 
A 1 209 GLY 209 88   88  GLY GLY A . n 
A 1 210 LYS 210 89   89  LYS LYS A . n 
A 1 211 ILE 211 90   90  ILE ILE A . n 
A 1 212 LEU 212 91   91  LEU LEU A . n 
A 1 213 THR 213 92   92  THR THR A . n 
A 1 214 PRO 214 93   93  PRO PRO A . n 
A 1 215 VAL 215 94   94  VAL VAL A . n 
A 1 216 PRO 216 95   95  PRO PRO A . n 
A 1 217 VAL 217 96   96  VAL VAL A . n 
A 1 218 PHE 218 97   97  PHE PHE A . n 
A 1 219 ARG 219 98   ?   ?   ?   A . n 
A 1 220 TRP 220 99   ?   ?   ?   A . n 
A 1 221 GLU 221 100  ?   ?   ?   A . n 
A 1 222 ARG 222 101  ?   ?   ?   A . n 
A 1 223 GLY 223 102  ?   ?   ?   A . n 
A 1 224 GLN 224 103  ?   ?   ?   A . n 
A 1 225 HIS 225 104  104 HIS HIS A . n 
A 1 226 LEU 226 105  105 LEU LEU A . n 
A 1 227 GLY 227 106  106 GLY GLY A . n 
A 1 228 GLN 228 107  107 GLN GLN A . n 
A 1 229 ASN 229 108  108 ASN ASN A . n 
A 1 230 LEU 230 109  109 LEU LEU A . n 
A 1 231 LEU 231 110  110 LEU LEU A . n 
A 1 232 SER 232 111  111 SER SER A . n 
A 1 233 LEU 233 112  112 LEU LEU A . n 
A 1 234 GLN 234 113  113 GLN GLN A . n 
A 1 235 LEU 235 114  114 LEU LEU A . n 
A 1 236 PRO 236 115  115 PRO PRO A . n 
A 1 237 LEU 237 116  116 LEU LEU A . n 
A 1 238 TYR 238 117  117 TYR TYR A . n 
A 1 239 GLU 239 118  118 GLU GLU A . n 
A 1 240 LYS 240 119  119 LYS LYS A . n 
A 1 241 ILE 241 120  120 ILE ILE A . n 
A 1 242 MET 242 121  121 MET MET A . n 
A 1 243 SER 243 122  122 SER SER A . n 
A 1 244 LEU 244 123  123 LEU LEU A . n 
A 1 245 ALA 245 124  124 ALA ALA A . n 
A 1 246 PRO 246 125  125 PRO PRO A . n 
A 1 247 ASP 247 126  126 ASP ASP A . n 
A 1 248 LYS 248 127  127 LYS LYS A . n 
A 1 249 LEU 249 128  128 LEU LEU A . n 
A 1 250 HIS 250 129  129 HIS HIS A . n 
A 1 251 THR 251 130  130 THR THR A . n 
A 1 252 LEU 252 131  131 LEU LEU A . n 
A 1 253 ILE 253 132  132 ILE ILE A . n 
A 1 254 ALA 254 133  133 ALA ALA A . n 
A 1 255 SER 255 134  134 SER SER A . n 
A 1 256 GLY 256 135  135 GLY GLY A . n 
A 1 257 ASP 257 136  136 ASP ASP A . n 
A 1 258 VAL 258 137  137 VAL VAL A . n 
A 1 259 TYR 259 138  138 TYR TYR A . n 
A 1 260 ILE 260 139  139 ILE ILE A . n 
A 1 261 ARG 261 140  140 ARG ARG A . n 
A 1 262 SER 262 141  141 SER SER A . n 
A 1 263 GLU 263 142  142 GLU GLU A . n 
A 1 264 LYS 264 143  143 LYS LYS A . n 
A 1 265 PRO 265 144  144 PRO PRO A . n 
A 1 266 LEU 266 145  145 LEU LEU A . n 
A 1 267 GLN 267 146  146 GLN GLN A . n 
A 1 268 SER 268 147  147 SER SER A . n 
A 1 269 ILE 269 148  148 ILE ILE A . n 
A 1 270 PRO 270 149  149 PRO PRO A . n 
A 1 271 GLU 271 150  150 GLU GLU A . n 
A 1 272 ALA 272 151  151 ALA ALA A . n 
A 1 273 ASP 273 152  152 ASP ASP A . n 
A 1 274 VAL 274 153  153 VAL VAL A . n 
A 1 275 VAL 275 154  154 VAL VAL A . n 
A 1 276 CYS 276 155  155 CYS CYS A . n 
A 1 277 TYR 277 156  156 TYR TYR A . n 
A 1 278 GLY 278 157  157 GLY GLY A . n 
A 1 279 LEU 279 158  158 LEU LEU A . n 
A 1 280 TRP 280 159  159 TRP TRP A . n 
A 1 281 VAL 281 160  160 VAL VAL A . n 
A 1 282 ASP 282 161  161 ASP ASP A . n 
A 1 283 PRO 283 162  162 PRO PRO A . n 
A 1 284 SER 284 163  163 SER SER A . n 
A 1 285 LEU 285 164  164 LEU LEU A . n 
A 1 286 ALA 286 165  165 ALA ALA A . n 
A 1 287 THR 287 166  166 THR THR A . n 
A 1 288 HIS 288 167  167 HIS HIS A . n 
A 1 289 HIS 289 168  168 HIS HIS A . n 
A 1 290 GLY 290 169  169 GLY GLY A . n 
A 1 291 VAL 291 170  170 VAL VAL A . n 
A 1 292 PHE 292 171  171 PHE PHE A . n 
A 1 293 ALA 293 172  172 ALA ALA A . n 
A 1 294 SER 294 173  173 SER SER A . n 
A 1 295 ASP 295 174  174 ASP ASP A . n 
A 1 296 ARG 296 175  175 ARG ARG A . n 
A 1 297 LYS 297 176  176 LYS LYS A . n 
A 1 298 HIS 298 177  177 HIS HIS A . n 
A 1 299 PRO 299 178  178 PRO PRO A . n 
A 1 300 GLU 300 179  179 GLU GLU A . n 
A 1 301 GLN 301 180  180 GLN GLN A . n 
A 1 302 LEU 302 181  181 LEU LEU A . n 
A 1 303 ASP 303 182  182 ASP ASP A . n 
A 1 304 PHE 304 183  183 PHE PHE A . n 
A 1 305 MET 305 184  184 MET MET A . n 
A 1 306 LEU 306 185  185 LEU LEU A . n 
A 1 307 GLN 307 186  186 GLN GLN A . n 
A 1 308 LYS 308 187  187 LYS LYS A . n 
A 1 309 PRO 309 188  188 PRO PRO A . n 
A 1 310 SER 310 189  189 SER SER A . n 
A 1 311 LEU 311 190  190 LEU LEU A . n 
A 1 312 ALA 312 191  191 ALA ALA A . n 
A 1 313 GLU 313 192  192 GLU GLU A . n 
A 1 314 LEU 314 193  193 LEU LEU A . n 
A 1 315 GLU 315 194  194 GLU GLU A . n 
A 1 316 SER 316 195  195 SER SER A . n 
A 1 317 LEU 317 196  196 LEU LEU A . n 
A 1 318 SER 318 197  197 SER SER A . n 
A 1 319 LYS 319 198  198 LYS LYS A . n 
A 1 320 THR 320 199  199 THR THR A . n 
A 1 321 HIS 321 200  200 HIS HIS A . n 
A 1 322 LEU 322 201  201 LEU LEU A . n 
A 1 323 PHE 323 202  202 PHE PHE A . n 
A 1 324 LEU 324 203  203 LEU LEU A . n 
A 1 325 MET 325 204  204 MET MET A . n 
A 1 326 ASP 326 205  205 ASP ASP A . n 
A 1 327 ILE 327 206  206 ILE ILE A . n 
A 1 328 GLY 328 207  207 GLY GLY A . n 
A 1 329 ILE 329 208  208 ILE ILE A . n 
A 1 330 TRP 330 209  209 TRP TRP A . n 
A 1 331 LEU 331 210  210 LEU LEU A . n 
A 1 332 LEU 332 211  211 LEU LEU A . n 
A 1 333 SER 333 212  212 SER SER A . n 
A 1 334 ASP 334 213  213 ASP ASP A . n 
A 1 335 ARG 335 214  214 ARG ARG A . n 
A 1 336 ALA 336 215  215 ALA ALA A . n 
A 1 337 VAL 337 216  216 VAL VAL A . n 
A 1 338 GLU 338 217  217 GLU GLU A . n 
A 1 339 ILE 339 218  218 ILE ILE A . n 
A 1 340 LEU 340 219  219 LEU LEU A . n 
A 1 341 MET 341 220  220 MET MET A . n 
A 1 342 LYS 342 221  221 LYS LYS A . n 
A 1 343 ARG 343 222  222 ARG ARG A . n 
A 1 344 SER 344 223  223 SER SER A . n 
A 1 345 HIS 345 224  224 HIS HIS A . n 
A 1 346 LYS 346 225  225 LYS LYS A . n 
A 1 347 GLU 347 226  226 GLU GLU A . n 
A 1 348 SER 348 227  227 SER SER A . n 
A 1 349 SER 349 228  228 SER SER A . n 
A 1 350 GLU 350 229  229 GLU GLU A . n 
A 1 351 GLU 351 230  230 GLU GLU A . n 
A 1 352 LEU 352 231  231 LEU LEU A . n 
A 1 353 LYS 353 232  232 LYS LYS A . n 
A 1 354 TYR 354 233  233 TYR TYR A . n 
A 1 355 TYR 355 234  234 TYR TYR A . n 
A 1 356 ASP 356 235  235 ASP ASP A . n 
A 1 357 LEU 357 236  236 LEU LEU A . n 
A 1 358 TYR 358 237  237 TYR TYR A . n 
A 1 359 SER 359 238  238 SER SER A . n 
A 1 360 ASP 360 239  239 ASP ASP A . n 
A 1 361 PHE 361 240  240 PHE PHE A . n 
A 1 362 GLY 362 241  241 GLY GLY A . n 
A 1 363 LEU 363 242  242 LEU LEU A . n 
A 1 364 ALA 364 243  243 ALA ALA A . n 
A 1 365 LEU 365 244  244 LEU LEU A . n 
A 1 366 GLY 366 245  245 GLY GLY A . n 
A 1 367 THR 367 246  246 THR THR A . n 
A 1 368 HIS 368 247  247 HIS HIS A . n 
A 1 369 PRO 369 248  248 PRO PRO A . n 
A 1 370 ARG 370 249  249 ARG ARG A . n 
A 1 371 ILE 371 250  250 ILE ILE A . n 
A 1 372 GLU 372 251  251 GLU GLU A . n 
A 1 373 ASP 373 252  252 ASP ASP A . n 
A 1 374 GLU 374 253  253 GLU GLU A . n 
A 1 375 GLU 375 254  254 GLU GLU A . n 
A 1 376 VAL 376 255  255 VAL VAL A . n 
A 1 377 ASN 377 256  256 ASN ASN A . n 
A 1 378 THR 378 257  257 THR THR A . n 
A 1 379 LEU 379 258  258 LEU LEU A . n 
A 1 380 SER 380 259  259 SER SER A . n 
A 1 381 VAL 381 260  260 VAL VAL A . n 
A 1 382 ALA 382 261  261 ALA ALA A . n 
A 1 383 ILE 383 262  262 ILE ILE A . n 
A 1 384 LEU 384 263  263 LEU LEU A . n 
A 1 385 PRO 385 264  264 PRO PRO A . n 
A 1 386 LEU 386 265  265 LEU LEU A . n 
A 1 387 PRO 387 266  266 PRO PRO A . n 
A 1 388 GLY 388 267  267 GLY GLY A . n 
A 1 389 GLY 389 268  268 GLY GLY A . n 
A 1 390 GLU 390 269  269 GLU GLU A . n 
A 1 391 PHE 391 270  270 PHE PHE A . n 
A 1 392 TYR 392 271  271 TYR TYR A . n 
A 1 393 HIS 393 272  272 HIS HIS A . n 
A 1 394 TYR 394 273  273 TYR TYR A . n 
A 1 395 GLY 395 274  274 GLY GLY A . n 
A 1 396 THR 396 275  275 THR THR A . n 
A 1 397 SER 397 276  276 SER SER A . n 
A 1 398 LYS 398 277  277 LYS LYS A . n 
A 1 399 GLU 399 278  278 GLU GLU A . n 
A 1 400 LEU 400 279  279 LEU LEU A . n 
A 1 401 ILE 401 280  280 ILE ILE A . n 
A 1 402 SER 402 281  281 SER SER A . n 
A 1 403 SER 403 282  282 SER SER A . n 
A 1 404 THR 404 283  283 THR THR A . n 
A 1 405 LEU 405 284  284 LEU LEU A . n 
A 1 406 SER 406 285  285 SER SER A . n 
A 1 407 VAL 407 286  286 VAL VAL A . n 
A 1 408 GLN 408 287  287 GLN GLN A . n 
A 1 409 ASN 409 288  288 ASN ASN A . n 
A 1 410 LYS 410 289  289 LYS LYS A . n 
A 1 411 VAL 411 290  290 VAL VAL A . n 
A 1 412 TYR 412 291  ?   ?   ?   A . n 
A 1 413 ASP 413 292  ?   ?   ?   A . n 
A 1 414 GLN 414 293  ?   ?   ?   A . n 
A 1 415 ARG 415 294  ?   ?   ?   A . n 
A 1 416 ARG 416 295  ?   ?   ?   A . n 
A 1 417 ILE 417 296  ?   ?   ?   A . n 
A 1 418 MET 418 297  ?   ?   ?   A . n 
A 1 419 HIS 419 298  ?   ?   ?   A . n 
A 1 420 ARG 420 299  ?   ?   ?   A . n 
A 1 421 LYS 421 300  ?   ?   ?   A . n 
A 1 422 VAL 422 301  ?   ?   ?   A . n 
A 1 423 LYS 423 302  ?   ?   ?   A . n 
A 1 424 PRO 424 303  ?   ?   ?   A . n 
A 1 425 ASN 425 304  ?   ?   ?   A . n 
A 1 426 PRO 426 305  305 PRO PRO A . n 
A 1 427 ALA 427 306  306 ALA ALA A . n 
A 1 428 MET 428 307  307 MET MET A . n 
A 1 429 PHE 429 308  308 PHE PHE A . n 
A 1 430 VAL 430 309  309 VAL VAL A . n 
A 1 431 GLN 431 310  310 GLN GLN A . n 
A 1 432 ASN 432 311  311 ASN ASN A . n 
A 1 433 ALA 433 312  312 ALA ALA A . n 
A 1 434 VAL 434 313  313 VAL VAL A . n 
A 1 435 VAL 435 314  314 VAL VAL A . n 
A 1 436 ARG 436 315  315 ARG ARG A . n 
A 1 437 ILE 437 316  316 ILE ILE A . n 
A 1 438 PRO 438 317  317 PRO PRO A . n 
A 1 439 LEU 439 318  318 LEU LEU A . n 
A 1 440 CYS 440 319  319 CYS CYS A . n 
A 1 441 ALA 441 320  320 ALA ALA A . n 
A 1 442 GLU 442 321  321 GLU GLU A . n 
A 1 443 ASN 443 322  322 ASN ASN A . n 
A 1 444 ALA 444 323  323 ALA ALA A . n 
A 1 445 ASP 445 324  324 ASP ASP A . n 
A 1 446 LEU 446 325  325 LEU LEU A . n 
A 1 447 TRP 447 326  326 TRP TRP A . n 
A 1 448 ILE 448 327  327 ILE ILE A . n 
A 1 449 GLU 449 328  328 GLU GLU A . n 
A 1 450 ASN 450 329  329 ASN ASN A . n 
A 1 451 SER 451 330  330 SER SER A . n 
A 1 452 HIS 452 331  331 HIS HIS A . n 
A 1 453 ILE 453 332  332 ILE ILE A . n 
A 1 454 GLY 454 333  333 GLY GLY A . n 
A 1 455 PRO 455 334  334 PRO PRO A . n 
A 1 456 LYS 456 335  335 LYS LYS A . n 
A 1 457 TRP 457 336  336 TRP TRP A . n 
A 1 458 LYS 458 337  337 LYS LYS A . n 
A 1 459 ILE 459 338  338 ILE ILE A . n 
A 1 460 ALA 460 339  339 ALA ALA A . n 
A 1 461 SER 461 340  340 SER SER A . n 
A 1 462 ARG 462 341  341 ARG ARG A . n 
A 1 463 HIS 463 342  342 HIS HIS A . n 
A 1 464 ILE 464 343  343 ILE ILE A . n 
A 1 465 ILE 465 344  344 ILE ILE A . n 
A 1 466 THR 466 345  345 THR THR A . n 
A 1 467 GLY 467 346  346 GLY GLY A . n 
A 1 468 VAL 468 347  347 VAL VAL A . n 
A 1 469 PRO 469 348  348 PRO PRO A . n 
A 1 470 GLU 470 349  349 GLU GLU A . n 
A 1 471 ASN 471 350  350 ASN ASN A . n 
A 1 472 ASP 472 351  351 ASP ASP A . n 
A 1 473 TRP 473 352  352 TRP TRP A . n 
A 1 474 SER 474 353  353 SER SER A . n 
A 1 475 LEU 475 354  354 LEU LEU A . n 
A 1 476 ALA 476 355  355 ALA ALA A . n 
A 1 477 VAL 477 356  356 VAL VAL A . n 
A 1 478 PRO 478 357  357 PRO PRO A . n 
A 1 479 ALA 479 358  358 ALA ALA A . n 
A 1 480 GLY 480 359  359 GLY GLY A . n 
A 1 481 VAL 481 360  360 VAL VAL A . n 
A 1 482 CYS 482 361  361 CYS CYS A . n 
A 1 483 VAL 483 362  362 VAL VAL A . n 
A 1 484 ASP 484 363  363 ASP ASP A . n 
A 1 485 VAL 485 364  364 VAL VAL A . n 
A 1 486 VAL 486 365  365 VAL VAL A . n 
A 1 487 PRO 487 366  366 PRO PRO A . n 
A 1 488 MET 488 367  367 MET MET A . n 
A 1 489 GLY 489 368  368 GLY GLY A . n 
A 1 490 ASP 490 369  369 ASP ASP A . n 
A 1 491 LYS 491 370  370 LYS LYS A . n 
A 1 492 GLY 492 371  371 GLY GLY A . n 
A 1 493 PHE 493 372  372 PHE PHE A . n 
A 1 494 VAL 494 373  373 VAL VAL A . n 
A 1 495 ALA 495 374  374 ALA ALA A . n 
A 1 496 ARG 496 375  375 ARG ARG A . n 
A 1 497 PRO 497 376  376 PRO PRO A . n 
A 1 498 TYR 498 377  377 TYR TYR A . n 
A 1 499 GLY 499 378  378 GLY GLY A . n 
A 1 500 LEU 500 379  379 LEU LEU A . n 
A 1 501 ASP 501 380  380 ASP ASP A . n 
A 1 502 ASP 502 381  381 ASP ASP A . n 
A 1 503 VAL 503 382  382 VAL VAL A . n 
A 1 504 PHE 504 383  383 PHE PHE A . n 
A 1 505 LYS 505 384  384 LYS LYS A . n 
A 1 506 GLY 506 385  385 GLY GLY A . n 
A 1 507 ASP 507 386  386 ASP ASP A . n 
A 1 508 LEU 508 387  387 LEU LEU A . n 
A 1 509 ARG 509 388  388 ARG ARG A . n 
A 1 510 ASP 510 389  389 ASP ASP A . n 
A 1 511 SER 511 390  390 SER SER A . n 
A 1 512 LYS 512 391  391 LYS LYS A . n 
A 1 513 THR 513 392  392 THR THR A . n 
A 1 514 THR 514 393  393 THR THR A . n 
A 1 515 LEU 515 394  394 LEU LEU A . n 
A 1 516 THR 516 395  395 THR THR A . n 
A 1 517 GLY 517 396  396 GLY GLY A . n 
A 1 518 ILE 518 397  397 ILE ILE A . n 
A 1 519 PRO 519 398  398 PRO PRO A . n 
A 1 520 PHE 520 399  399 PHE PHE A . n 
A 1 521 GLY 521 400  400 GLY GLY A . n 
A 1 522 GLU 522 401  401 GLU GLU A . n 
A 1 523 TRP 523 402  402 TRP TRP A . n 
A 1 524 MET 524 403  403 MET MET A . n 
A 1 525 SER 525 404  404 SER SER A . n 
A 1 526 LYS 526 405  405 LYS LYS A . n 
A 1 527 ARG 527 406  406 ARG ARG A . n 
A 1 528 GLY 528 407  407 GLY GLY A . n 
A 1 529 LEU 529 408  408 LEU LEU A . n 
A 1 530 SER 530 409  409 SER SER A . n 
A 1 531 TYR 531 410  410 TYR TYR A . n 
A 1 532 THR 532 411  411 THR THR A . n 
A 1 533 ASP 533 412  412 ASP ASP A . n 
A 1 534 LEU 534 413  413 LEU LEU A . n 
A 1 535 LYS 535 414  414 LYS LYS A . n 
A 1 536 GLY 536 415  415 GLY GLY A . n 
A 1 537 ARG 537 416  416 ARG ARG A . n 
A 1 538 THR 538 417  417 THR THR A . n 
A 1 539 ASP 539 418  418 ASP ASP A . n 
A 1 540 ASP 540 419  419 ASP ASP A . n 
A 1 541 LEU 541 420  420 LEU LEU A . n 
A 1 542 GLN 542 421  421 GLN GLN A . n 
A 1 543 ALA 543 422  422 ALA ALA A . n 
A 1 544 VAL 544 423  423 VAL VAL A . n 
A 1 545 SER 545 424  424 SER SER A . n 
A 1 546 VAL 546 425  425 VAL VAL A . n 
A 1 547 PHE 547 426  426 PHE PHE A . n 
A 1 548 PRO 548 427  427 PRO PRO A . n 
A 1 549 MET 549 428  428 MET MET A . n 
A 1 550 VAL 550 429  429 VAL VAL A . n 
A 1 551 ASN 551 430  430 ASN ASN A . n 
A 1 552 SER 552 431  431 SER SER A . n 
A 1 553 VAL 553 432  432 VAL VAL A . n 
A 1 554 GLU 554 433  433 GLU GLU A . n 
A 1 555 GLU 555 434  434 GLU GLU A . n 
A 1 556 LEU 556 435  435 LEU LEU A . n 
A 1 557 GLY 557 436  436 GLY GLY A . n 
A 1 558 LEU 558 437  437 LEU LEU A . n 
A 1 559 VAL 559 438  438 VAL VAL A . n 
A 1 560 LEU 560 439  439 LEU LEU A . n 
A 1 561 ARG 561 440  440 ARG ARG A . n 
A 1 562 TRP 562 441  441 TRP TRP A . n 
A 1 563 MET 563 442  442 MET MET A . n 
A 1 564 LEU 564 443  443 LEU LEU A . n 
A 1 565 SER 565 444  444 SER SER A . n 
A 1 566 GLU 566 445  445 GLU GLU A . n 
A 1 567 PRO 567 446  446 PRO PRO A . n 
A 1 568 GLU 568 447  447 GLU GLU A . n 
A 1 569 LEU 569 448  448 LEU LEU A . n 
A 1 570 GLU 570 449  449 GLU GLU A . n 
A 1 571 GLU 571 450  450 GLU GLU A . n 
A 1 572 GLY 572 451  451 GLY GLY A . n 
A 1 573 LYS 573 452  452 LYS LYS A . n 
A 1 574 ASN 574 453  453 ASN ASN A . n 
A 1 575 ILE 575 454  454 ILE ILE A . n 
A 1 576 TRP 576 455  455 TRP TRP A . n 
A 1 577 LEU 577 456  456 LEU LEU A . n 
A 1 578 ARG 578 457  457 ARG ARG A . n 
A 1 579 SER 579 458  458 SER SER A . n 
A 1 580 GLU 580 459  459 GLU GLU A . n 
A 1 581 HIS 581 460  460 HIS HIS A . n 
A 1 582 PHE 582 461  461 PHE PHE A . n 
A 1 583 SER 583 462  462 SER SER A . n 
A 1 584 ALA 584 463  463 ALA ALA A . n 
A 1 585 ASP 585 464  464 ASP ASP A . n 
A 1 586 GLU 586 465  465 GLU GLU A . n 
A 1 587 ILE 587 466  466 ILE ILE A . n 
A 1 588 SER 588 467  467 SER SER A . n 
A 1 589 ALA 589 468  468 ALA ALA A . n 
A 1 590 GLY 590 469  469 GLY GLY A . n 
A 1 591 ALA 591 470  470 ALA ALA A . n 
A 1 592 ASN 592 471  471 ASN ASN A . n 
A 1 593 LEU 593 472  472 LEU LEU A . n 
A 1 594 LYS 594 473  473 LYS LYS A . n 
A 1 595 ARG 595 474  474 ARG ARG A . n 
A 1 596 LEU 596 475  475 LEU LEU A . n 
A 1 597 TYR 597 476  476 TYR TYR A . n 
A 1 598 ALA 598 477  477 ALA ALA A . n 
A 1 599 GLN 599 478  478 GLN GLN A . n 
A 1 600 ARG 600 479  479 ARG ARG A . n 
A 1 601 GLU 601 480  480 GLU GLU A . n 
A 1 602 GLU 602 481  481 GLU GLU A . n 
A 1 603 PHE 603 482  482 PHE PHE A . n 
A 1 604 ARG 604 483  483 ARG ARG A . n 
A 1 605 LYS 605 484  484 LYS LYS A . n 
A 1 606 GLY 606 485  485 GLY GLY A . n 
A 1 607 ASN 607 486  486 ASN ASN A . n 
A 1 608 TRP 608 487  487 TRP TRP A . n 
A 1 609 LYS 609 488  488 LYS LYS A . n 
A 1 610 ALA 610 489  489 ALA ALA A . n 
A 1 611 LEU 611 490  490 LEU LEU A . n 
A 1 612 ALA 612 491  491 ALA ALA A . n 
A 1 613 VAL 613 492  492 VAL VAL A . n 
A 1 614 ASN 614 493  ?   ?   ?   A . n 
A 1 615 HIS 615 494  ?   ?   ?   A . n 
A 1 616 GLU 616 495  ?   ?   ?   A . n 
A 1 617 LYS 617 496  ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        EPE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   EPE 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 EPE 1   1001 1001 EPE EPE A . 
C 3 ACT 1   1002 1002 ACT ACT A . 
D 4 HOH 1   1101 1101 HOH HOH A . 
D 4 HOH 2   1102 1102 HOH HOH A . 
D 4 HOH 3   1103 1103 HOH HOH A . 
D 4 HOH 4   1104 1104 HOH HOH A . 
D 4 HOH 5   1105 1105 HOH HOH A . 
D 4 HOH 6   1106 1106 HOH HOH A . 
D 4 HOH 7   1107 1107 HOH HOH A . 
D 4 HOH 8   1108 1108 HOH HOH A . 
D 4 HOH 9   1109 1109 HOH HOH A . 
D 4 HOH 10  1110 1110 HOH HOH A . 
D 4 HOH 11  1111 1111 HOH HOH A . 
D 4 HOH 12  1112 1112 HOH HOH A . 
D 4 HOH 13  1113 1113 HOH HOH A . 
D 4 HOH 14  1114 1114 HOH HOH A . 
D 4 HOH 15  1115 1115 HOH HOH A . 
D 4 HOH 16  1116 1116 HOH HOH A . 
D 4 HOH 17  1117 1117 HOH HOH A . 
D 4 HOH 18  1118 1118 HOH HOH A . 
D 4 HOH 19  1119 1119 HOH HOH A . 
D 4 HOH 20  1120 1120 HOH HOH A . 
D 4 HOH 21  1121 1121 HOH HOH A . 
D 4 HOH 22  1122 1122 HOH HOH A . 
D 4 HOH 23  1123 1123 HOH HOH A . 
D 4 HOH 24  1124 1124 HOH HOH A . 
D 4 HOH 25  1125 1125 HOH HOH A . 
D 4 HOH 26  1126 1126 HOH HOH A . 
D 4 HOH 27  1127 1127 HOH HOH A . 
D 4 HOH 28  1128 1128 HOH HOH A . 
D 4 HOH 29  1129 1129 HOH HOH A . 
D 4 HOH 30  1130 1130 HOH HOH A . 
D 4 HOH 31  1131 1131 HOH HOH A . 
D 4 HOH 32  1132 1132 HOH HOH A . 
D 4 HOH 33  1133 1133 HOH HOH A . 
D 4 HOH 34  1134 1134 HOH HOH A . 
D 4 HOH 35  1135 1135 HOH HOH A . 
D 4 HOH 36  1136 1136 HOH HOH A . 
D 4 HOH 37  1137 1137 HOH HOH A . 
D 4 HOH 38  1138 1138 HOH HOH A . 
D 4 HOH 39  1139 1139 HOH HOH A . 
D 4 HOH 40  1140 1140 HOH HOH A . 
D 4 HOH 41  1141 1141 HOH HOH A . 
D 4 HOH 42  1142 1142 HOH HOH A . 
D 4 HOH 43  1143 1143 HOH HOH A . 
D 4 HOH 44  1144 1144 HOH HOH A . 
D 4 HOH 45  1145 1145 HOH HOH A . 
D 4 HOH 46  1146 1146 HOH HOH A . 
D 4 HOH 47  1147 1147 HOH HOH A . 
D 4 HOH 48  1148 1148 HOH HOH A . 
D 4 HOH 49  1149 1149 HOH HOH A . 
D 4 HOH 50  1150 1150 HOH HOH A . 
D 4 HOH 51  1151 1151 HOH HOH A . 
D 4 HOH 52  1152 1152 HOH HOH A . 
D 4 HOH 53  1153 1153 HOH HOH A . 
D 4 HOH 54  1154 1154 HOH HOH A . 
D 4 HOH 55  1155 1155 HOH HOH A . 
D 4 HOH 56  1156 1156 HOH HOH A . 
D 4 HOH 57  1157 1157 HOH HOH A . 
D 4 HOH 58  1158 1158 HOH HOH A . 
D 4 HOH 59  1159 1159 HOH HOH A . 
D 4 HOH 60  1160 1160 HOH HOH A . 
D 4 HOH 61  1161 1161 HOH HOH A . 
D 4 HOH 62  1162 1162 HOH HOH A . 
D 4 HOH 63  1163 1163 HOH HOH A . 
D 4 HOH 64  1164 1164 HOH HOH A . 
D 4 HOH 65  1165 1165 HOH HOH A . 
D 4 HOH 66  1166 1166 HOH HOH A . 
D 4 HOH 67  1167 1167 HOH HOH A . 
D 4 HOH 68  1168 1168 HOH HOH A . 
D 4 HOH 69  1169 1169 HOH HOH A . 
D 4 HOH 70  1170 1170 HOH HOH A . 
D 4 HOH 71  1171 1171 HOH HOH A . 
D 4 HOH 72  1172 1172 HOH HOH A . 
D 4 HOH 73  1173 1173 HOH HOH A . 
D 4 HOH 74  1174 1174 HOH HOH A . 
D 4 HOH 75  1175 1175 HOH HOH A . 
D 4 HOH 76  1176 1176 HOH HOH A . 
D 4 HOH 77  1177 1177 HOH HOH A . 
D 4 HOH 78  1178 1178 HOH HOH A . 
D 4 HOH 79  1179 1179 HOH HOH A . 
D 4 HOH 80  1180 1180 HOH HOH A . 
D 4 HOH 81  1181 1181 HOH HOH A . 
D 4 HOH 82  1182 1182 HOH HOH A . 
D 4 HOH 83  1183 1183 HOH HOH A . 
D 4 HOH 84  1184 1184 HOH HOH A . 
D 4 HOH 85  1185 1185 HOH HOH A . 
D 4 HOH 86  1186 1186 HOH HOH A . 
D 4 HOH 87  1187 1187 HOH HOH A . 
D 4 HOH 88  1188 1188 HOH HOH A . 
D 4 HOH 89  1189 1189 HOH HOH A . 
D 4 HOH 90  1190 1190 HOH HOH A . 
D 4 HOH 91  1191 1191 HOH HOH A . 
D 4 HOH 92  1192 1192 HOH HOH A . 
D 4 HOH 93  1193 1193 HOH HOH A . 
D 4 HOH 94  1194 1194 HOH HOH A . 
D 4 HOH 95  1195 1195 HOH HOH A . 
D 4 HOH 96  1196 1196 HOH HOH A . 
D 4 HOH 97  1197 1197 HOH HOH A . 
D 4 HOH 98  1198 1198 HOH HOH A . 
D 4 HOH 99  1199 1199 HOH HOH A . 
D 4 HOH 100 1200 1200 HOH HOH A . 
D 4 HOH 101 1201 1201 HOH HOH A . 
D 4 HOH 102 1202 1202 HOH HOH A . 
D 4 HOH 103 1203 1203 HOH HOH A . 
D 4 HOH 104 1204 1204 HOH HOH A . 
D 4 HOH 105 1205 1205 HOH HOH A . 
D 4 HOH 106 1206 1206 HOH HOH A . 
D 4 HOH 107 1207 1207 HOH HOH A . 
D 4 HOH 108 1208 1208 HOH HOH A . 
D 4 HOH 109 1209 1209 HOH HOH A . 
D 4 HOH 110 1210 1210 HOH HOH A . 
D 4 HOH 111 1211 1211 HOH HOH A . 
D 4 HOH 112 1212 1212 HOH HOH A . 
D 4 HOH 113 1213 1213 HOH HOH A . 
D 4 HOH 114 1214 1214 HOH HOH A . 
D 4 HOH 115 1215 1215 HOH HOH A . 
D 4 HOH 116 1216 1216 HOH HOH A . 
D 4 HOH 117 1217 1217 HOH HOH A . 
D 4 HOH 118 1218 1218 HOH HOH A . 
D 4 HOH 119 1219 1219 HOH HOH A . 
D 4 HOH 120 1220 1220 HOH HOH A . 
D 4 HOH 121 1221 1221 HOH HOH A . 
D 4 HOH 122 1222 1222 HOH HOH A . 
D 4 HOH 123 1223 1223 HOH HOH A . 
D 4 HOH 124 1224 1224 HOH HOH A . 
D 4 HOH 125 1225 1225 HOH HOH A . 
D 4 HOH 126 1226 1226 HOH HOH A . 
D 4 HOH 127 1227 1227 HOH HOH A . 
D 4 HOH 128 1228 1228 HOH HOH A . 
D 4 HOH 129 1229 1229 HOH HOH A . 
D 4 HOH 130 1230 1230 HOH HOH A . 
D 4 HOH 131 1231 1231 HOH HOH A . 
D 4 HOH 132 1232 1232 HOH HOH A . 
D 4 HOH 133 1233 1233 HOH HOH A . 
D 4 HOH 134 1234 1234 HOH HOH A . 
D 4 HOH 135 1235 1235 HOH HOH A . 
D 4 HOH 136 1236 1236 HOH HOH A . 
D 4 HOH 137 1237 1237 HOH HOH A . 
D 4 HOH 138 1238 1238 HOH HOH A . 
D 4 HOH 139 1239 1239 HOH HOH A . 
D 4 HOH 140 1240 1240 HOH HOH A . 
D 4 HOH 141 1241 1241 HOH HOH A . 
D 4 HOH 142 1242 1242 HOH HOH A . 
D 4 HOH 143 1243 1243 HOH HOH A . 
D 4 HOH 144 1244 1244 HOH HOH A . 
D 4 HOH 145 1245 1245 HOH HOH A . 
D 4 HOH 146 1246 1246 HOH HOH A . 
D 4 HOH 147 1247 1247 HOH HOH A . 
D 4 HOH 148 1248 1248 HOH HOH A . 
D 4 HOH 149 1249 1249 HOH HOH A . 
D 4 HOH 150 1250 1250 HOH HOH A . 
D 4 HOH 151 1251 1251 HOH HOH A . 
D 4 HOH 152 1252 1252 HOH HOH A . 
D 4 HOH 153 1253 1253 HOH HOH A . 
D 4 HOH 154 1254 1254 HOH HOH A . 
D 4 HOH 155 1255 1255 HOH HOH A . 
D 4 HOH 156 1256 1256 HOH HOH A . 
D 4 HOH 157 1257 1257 HOH HOH A . 
D 4 HOH 158 1258 1258 HOH HOH A . 
D 4 HOH 159 1259 1259 HOH HOH A . 
D 4 HOH 160 1260 1260 HOH HOH A . 
D 4 HOH 161 1261 1261 HOH HOH A . 
D 4 HOH 162 1262 1262 HOH HOH A . 
D 4 HOH 163 1263 1263 HOH HOH A . 
D 4 HOH 164 1264 1264 HOH HOH A . 
D 4 HOH 165 1265 1265 HOH HOH A . 
D 4 HOH 166 1266 1266 HOH HOH A . 
D 4 HOH 167 1267 1267 HOH HOH A . 
D 4 HOH 168 1268 1268 HOH HOH A . 
D 4 HOH 169 1269 1269 HOH HOH A . 
D 4 HOH 170 1270 1270 HOH HOH A . 
D 4 HOH 171 1271 1271 HOH HOH A . 
D 4 HOH 172 1272 1272 HOH HOH A . 
D 4 HOH 173 1273 1273 HOH HOH A . 
D 4 HOH 174 1274 1274 HOH HOH A . 
D 4 HOH 175 1275 1275 HOH HOH A . 
D 4 HOH 176 1276 1276 HOH HOH A . 
D 4 HOH 177 1277 1277 HOH HOH A . 
D 4 HOH 178 1278 1278 HOH HOH A . 
D 4 HOH 179 1279 1279 HOH HOH A . 
D 4 HOH 180 1280 1280 HOH HOH A . 
D 4 HOH 181 1281 1281 HOH HOH A . 
D 4 HOH 182 1282 1282 HOH HOH A . 
D 4 HOH 183 1283 1283 HOH HOH A . 
D 4 HOH 184 1284 1284 HOH HOH A . 
D 4 HOH 185 1285 1285 HOH HOH A . 
D 4 HOH 186 1286 1286 HOH HOH A . 
D 4 HOH 187 1287 1287 HOH HOH A . 
D 4 HOH 188 1288 1288 HOH HOH A . 
D 4 HOH 189 1289 1289 HOH HOH A . 
D 4 HOH 190 1290 1290 HOH HOH A . 
D 4 HOH 191 1291 1291 HOH HOH A . 
D 4 HOH 192 1292 1292 HOH HOH A . 
D 4 HOH 193 1293 1293 HOH HOH A . 
D 4 HOH 194 1294 1294 HOH HOH A . 
D 4 HOH 195 1295 1295 HOH HOH A . 
D 4 HOH 196 1296 1296 HOH HOH A . 
D 4 HOH 197 1297 1297 HOH HOH A . 
D 4 HOH 198 1298 1298 HOH HOH A . 
D 4 HOH 199 1299 1299 HOH HOH A . 
D 4 HOH 200 1300 1300 HOH HOH A . 
D 4 HOH 201 1301 1301 HOH HOH A . 
D 4 HOH 202 1302 1302 HOH HOH A . 
D 4 HOH 203 1303 1303 HOH HOH A . 
D 4 HOH 204 1304 1304 HOH HOH A . 
D 4 HOH 205 1305 1305 HOH HOH A . 
D 4 HOH 206 1306 1306 HOH HOH A . 
D 4 HOH 207 1307 1307 HOH HOH A . 
D 4 HOH 208 1308 1308 HOH HOH A . 
D 4 HOH 209 1309 1309 HOH HOH A . 
D 4 HOH 210 1310 1310 HOH HOH A . 
D 4 HOH 211 1311 1311 HOH HOH A . 
D 4 HOH 212 1312 1312 HOH HOH A . 
D 4 HOH 213 1313 1313 HOH HOH A . 
D 4 HOH 214 1314 1314 HOH HOH A . 
D 4 HOH 215 1315 1315 HOH HOH A . 
D 4 HOH 216 1316 1316 HOH HOH A . 
D 4 HOH 217 1317 1317 HOH HOH A . 
D 4 HOH 218 1318 1318 HOH HOH A . 
D 4 HOH 219 1319 1319 HOH HOH A . 
D 4 HOH 220 1320 1320 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.13_2998 1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .         2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .         3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .         4 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? Blu-Ice  ? ? ? .         5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IIS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     86.585 
_cell.length_a_esd                 ? 
_cell.length_b                     109.854 
_cell.length_b_esd                 ? 
_cell.length_c                     144.107 
_cell.length_c_esd                 ? 
_cell.volume                       1370703.790 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9IIS 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IIS 
_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             2.46 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.91 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'PEG 3350, ammonium acetate, HEPES' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RAYONIX MX300HE' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-04-09 
_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   1.0000 
_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                        'NSRRC BEAMLINE BL15A1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL15A1 
_diffrn_source.pdbx_synchrotron_site       NSRRC 
# 
_reflns.B_iso_Wilson_estimate                          56.51 
_reflns.entry_id                                       9IIS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.35 
_reflns.d_resolution_low                               30 
_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                                     28528 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          23.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.970 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.065 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.35 
_reflns_shell.d_res_low                                     2.43 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2831 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.8 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.893 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.771 
_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                               93.08 
_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                                 9IIS 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.36 
_refine.ls_d_res_low                             29.12 
_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                     28436 
_refine.ls_number_reflns_R_free                  1422 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.75 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2052 
_refine.ls_R_factor_R_free                       0.2539 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2026 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          SAD 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_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             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.8686 
_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                            0.2921 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.36 
_refine_hist.d_res_low                        29.12 
_refine_hist.number_atoms_solvent             227 
_refine_hist.number_atoms_total               4617 
_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        4390 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.0026  ? 4491 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6495  ? 6074 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0444  ? 662  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0050  ? 778  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.3276 ? 2698 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.36 2.44  . . 137 2584 95.54 . . . . 0.2954 . . . . . . . . . . . 0.3336 
'X-RAY DIFFRACTION' 2.44 2.54  . . 142 2669 99.22 . . . . 0.2703 . . . . . . . . . . . 0.2784 
'X-RAY DIFFRACTION' 2.54 2.65  . . 141 2683 99.51 . . . . 0.2564 . . . . . . . . . . . 0.3284 
'X-RAY DIFFRACTION' 2.65 2.79  . . 141 2701 99.41 . . . . 0.2402 . . . . . . . . . . . 0.3206 
'X-RAY DIFFRACTION' 2.79 2.97  . . 141 2694 99.51 . . . . 0.2574 . . . . . . . . . . . 0.3298 
'X-RAY DIFFRACTION' 2.97 3.20  . . 142 2710 99.89 . . . . 0.2447 . . . . . . . . . . . 0.3428 
'X-RAY DIFFRACTION' 3.20 3.52  . . 143 2722 99.72 . . . . 0.2201 . . . . . . . . . . . 0.2918 
'X-RAY DIFFRACTION' 3.52 4.03  . . 145 2744 99.79 . . . . 0.1898 . . . . . . . . . . . 0.2540 
'X-RAY DIFFRACTION' 4.03 5.07  . . 143 2733 99.04 . . . . 0.1659 . . . . . . . . . . . 0.1903 
'X-RAY DIFFRACTION' 5.07 29.12 . . 147 2774 96.15 . . . . 0.1829 . . . . . . . . . . . 0.2257 
# 
_struct.entry_id                     9IIS 
_struct.title                        'GDP-fucose pyrophosphorylase part of FKP with a SUMO tag' 
_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        9IIS 
_struct_keywords.text            'GDP-fucose, pyrophosphorylase, HEPES, beta-helix, SUMO, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 ? 
# 
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 SMT3_YEAST   Q12306 ? 1 
;MSDSEVNQEAKPEVKPEVKPETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDSLRFLYDGIRIQADQTPED
LDMEDNDIIEAHREQIGG
;
1 
2 UNP Q58T34_BACFG Q58T34 ? 1 
;MQKLLSLPSNLVQSFHELERVNRTDWFCTSDPVGKKLGSGGGTSWLLEECYNEYSDGATFGEWLEKEKRILLHAGGQSRR
LPGYAPSGKILTPVPVFRWERGQHLGQNLLSLQLPLYEKIMSLAPDKLHTLIASGDVYIRSEKPLQSIPEADVVCYGLWV
DPSLATHHGVFASDRKHPEQLDFMLQKPSLAELESLSKTHLFLMDIGIWLLSDRAVEILMKRSHKESSEELKYYDLYSDF
GLALGTHPRIEDEEVNTLSVAILPLPGGEFYHYGTSKELISSTLSVQNKVYDQRRIMHRKVKPNPAMFVQNAVVRIPLCA
ENADLWIENSHIGPKWKIASRHIITGVPENDWSLAVPAGVCVDVVPMGDKGFVARPYGLDDVFKGDLRDSKTTLTGIPFG
EWMSKRGLSYTDLKGRTDDLQAVSVFPMVNSVEELGLVLRWMLSEPELEEGKNIWLRSEHFSADEISAGANLKRLYAQRE
EFRKGNWKALAVNHEK
;
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 9IIS A 22  ? 119 ? Q12306 1 ? 98  ? -99 -2  
2 2 9IIS A 122 ? 617 ? Q58T34 1 ? 496 ? 1   496 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9IIS MET A 1   ? UNP Q12306 ? ? 'initiating methionine' -120 1  
1 9IIS GLY A 2   ? UNP Q12306 ? ? 'expression tag'        -119 2  
1 9IIS SER A 3   ? UNP Q12306 ? ? 'expression tag'        -118 3  
1 9IIS SER A 4   ? UNP Q12306 ? ? 'expression tag'        -117 4  
1 9IIS HIS A 5   ? UNP Q12306 ? ? 'expression tag'        -116 5  
1 9IIS HIS A 6   ? UNP Q12306 ? ? 'expression tag'        -115 6  
1 9IIS HIS A 7   ? UNP Q12306 ? ? 'expression tag'        -114 7  
1 9IIS HIS A 8   ? UNP Q12306 ? ? 'expression tag'        -113 8  
1 9IIS HIS A 9   ? UNP Q12306 ? ? 'expression tag'        -112 9  
1 9IIS HIS A 10  ? UNP Q12306 ? ? 'expression tag'        -111 10 
1 9IIS GLY A 11  ? UNP Q12306 ? ? 'expression tag'        -110 11 
1 9IIS SER A 12  ? UNP Q12306 ? ? 'expression tag'        -109 12 
1 9IIS GLY A 13  ? UNP Q12306 ? ? 'expression tag'        -108 13 
1 9IIS LEU A 14  ? UNP Q12306 ? ? 'expression tag'        -107 14 
1 9IIS VAL A 15  ? UNP Q12306 ? ? 'expression tag'        -106 15 
1 9IIS PRO A 16  ? UNP Q12306 ? ? 'expression tag'        -105 16 
1 9IIS ARG A 17  ? UNP Q12306 ? ? 'expression tag'        -104 17 
1 9IIS GLY A 18  ? UNP Q12306 ? ? 'expression tag'        -103 18 
1 9IIS SER A 19  ? UNP Q12306 ? ? 'expression tag'        -102 19 
1 9IIS ALA A 20  ? UNP Q12306 ? ? 'expression tag'        -101 20 
1 9IIS SER A 21  ? UNP Q12306 ? ? 'expression tag'        -100 21 
1 9IIS GLU A 120 ? UNP Q12306 ? ? linker                  -1   22 
1 9IIS PHE A 121 ? UNP Q12306 ? ? linker                  0    23 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 430   ? 
1 MORE         2     ? 
1 'SSA (A^2)'  26060 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LEU A 66  ? GLN A 77  ? LEU A -55 GLN A -44 1 ? 12 
HELX_P HELX_P2  AA2 GLU A 80  ? ASP A 82  ? GLU A -41 ASP A -39 5 ? 3  
HELX_P HELX_P3  AA3 PRO A 129 ? GLN A 134 ? PRO A 8   GLN A 13  1 ? 6  
HELX_P HELX_P4  AA4 SER A 135 ? ARG A 141 ? SER A 14  ARG A 20  1 ? 7  
HELX_P HELX_P5  AA5 LEU A 158 ? SER A 176 ? LEU A 37  SER A 55  1 ? 19 
HELX_P HELX_P6  AA6 THR A 180 ? GLU A 188 ? THR A 59  GLU A 67  1 ? 9  
HELX_P HELX_P7  AA7 LEU A 202 ? GLY A 209 ? LEU A 81  GLY A 88  5 ? 8  
HELX_P HELX_P8  AA8 ASN A 229 ? ALA A 245 ? ASN A 108 ALA A 124 1 ? 17 
HELX_P HELX_P9  AA9 ASP A 282 ? THR A 287 ? ASP A 161 THR A 166 1 ? 6  
HELX_P HELX_P10 AB1 SER A 310 ? SER A 316 ? SER A 189 SER A 195 1 ? 7  
HELX_P HELX_P11 AB2 ASP A 334 ? SER A 344 ? ASP A 213 SER A 223 1 ? 11 
HELX_P HELX_P12 AB3 PHE A 361 ? LEU A 365 ? PHE A 240 LEU A 244 5 ? 5  
HELX_P HELX_P13 AB4 ASP A 373 ? THR A 378 ? ASP A 252 THR A 257 1 ? 6  
HELX_P HELX_P14 AB5 THR A 396 ? ASN A 409 ? THR A 275 ASN A 288 1 ? 14 
HELX_P HELX_P15 AB6 PHE A 520 ? LYS A 526 ? PHE A 399 LYS A 405 1 ? 7  
HELX_P HELX_P16 AB7 SER A 530 ? LEU A 534 ? SER A 409 LEU A 413 5 ? 5  
HELX_P HELX_P17 AB8 ASP A 540 ? VAL A 544 ? ASP A 419 VAL A 423 5 ? 5  
HELX_P HELX_P18 AB9 SER A 552 ? LEU A 564 ? SER A 431 LEU A 443 1 ? 13 
HELX_P HELX_P19 AC1 LEU A 569 ? ARG A 578 ? LEU A 448 ARG A 457 1 ? 10 
HELX_P HELX_P20 AC2 SER A 583 ? ALA A 591 ? SER A 462 ALA A 470 1 ? 9  
HELX_P HELX_P21 AC3 ASN A 592 ? TRP A 608 ? ASN A 471 TRP A 487 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 7 ? 
AA3 ? 7 ? 
AA4 ? 2 ? 
AA5 ? 7 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? parallel      
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? parallel      
AA7 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 55  ? LYS A 61  ? GLU A -66 LYS A -60 
AA1 2 HIS A 44  ? SER A 50  ? HIS A -77 SER A -71 
AA1 3 ASP A 108 ? ARG A 114 ? ASP A -13 ARG A -7  
AA1 4 LEU A 84  ? TYR A 88  ? LEU A -37 TYR A -33 
AA1 5 ILE A 91  ? ARG A 92  ? ILE A -30 ARG A -29 
AA2 1 TRP A 147 ? THR A 150 ? TRP A 26  THR A 29  
AA2 2 GLN A 123 ? SER A 127 ? GLN A 2   SER A 6   
AA2 3 ARG A 190 ? HIS A 194 ? ARG A 69  HIS A 73  
AA2 4 LEU A 249 ? ALA A 254 ? LEU A 128 ALA A 133 
AA2 5 HIS A 321 ? SER A 333 ? HIS A 200 SER A 212 
AA2 6 GLY A 290 ? ASP A 295 ? GLY A 169 ASP A 174 
AA2 7 PHE A 304 ? GLN A 307 ? PHE A 183 GLN A 186 
AA3 1 TRP A 147 ? THR A 150 ? TRP A 26  THR A 29  
AA3 2 GLN A 123 ? SER A 127 ? GLN A 2   SER A 6   
AA3 3 ARG A 190 ? HIS A 194 ? ARG A 69  HIS A 73  
AA3 4 LEU A 249 ? ALA A 254 ? LEU A 128 ALA A 133 
AA3 5 HIS A 321 ? SER A 333 ? HIS A 200 SER A 212 
AA3 6 VAL A 274 ? TRP A 280 ? VAL A 153 TRP A 159 
AA3 7 VAL A 381 ? PRO A 385 ? VAL A 260 PRO A 264 
AA4 1 VAL A 258 ? SER A 262 ? VAL A 137 SER A 141 
AA4 2 GLY A 389 ? HIS A 393 ? GLY A 268 HIS A 272 
AA5 1 MET A 428 ? GLN A 431 ? MET A 307 GLN A 310 
AA5 2 LEU A 446 ? GLU A 449 ? LEU A 325 GLU A 328 
AA5 3 HIS A 463 ? THR A 466 ? HIS A 342 THR A 345 
AA5 4 VAL A 481 ? MET A 488 ? VAL A 360 MET A 367 
AA5 5 GLY A 492 ? GLY A 499 ? GLY A 371 GLY A 378 
AA5 6 PHE A 547 ? VAL A 550 ? PHE A 426 VAL A 429 
AA5 7 HIS A 581 ? PHE A 582 ? HIS A 460 PHE A 461 
AA6 1 VAL A 434 ? VAL A 435 ? VAL A 313 VAL A 314 
AA6 2 HIS A 452 ? ILE A 453 ? HIS A 331 ILE A 332 
AA7 1 THR A 514 ? LEU A 515 ? THR A 393 LEU A 394 
AA7 2 ILE A 518 ? PRO A 519 ? ILE A 397 PRO A 398 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ILE A 60  ? O ILE A -61 N ILE A 45  ? N ILE A -76 
AA1 2 3 N LYS A 48  ? N LYS A -73 O ASP A 108 ? O ASP A -13 
AA1 3 4 O GLU A 111 ? O GLU A -10 N LEU A 87  ? N LEU A -34 
AA1 4 5 N TYR A 88  ? N TYR A -33 O ILE A 91  ? O ILE A -30 
AA2 1 2 O PHE A 148 ? O PHE A 27  N LYS A 124 ? N LYS A 3   
AA2 2 3 N SER A 127 ? N SER A 6   O LEU A 193 ? O LEU A 72  
AA2 3 4 N ARG A 190 ? N ARG A 69  O LEU A 252 ? O LEU A 131 
AA2 4 5 N ILE A 253 ? N ILE A 132 O TRP A 330 ? O TRP A 209 
AA2 5 6 O ASP A 326 ? O ASP A 205 N GLY A 290 ? N GLY A 169 
AA2 6 7 N ALA A 293 ? N ALA A 172 O PHE A 304 ? O PHE A 183 
AA3 1 2 O PHE A 148 ? O PHE A 27  N LYS A 124 ? N LYS A 3   
AA3 2 3 N SER A 127 ? N SER A 6   O LEU A 193 ? O LEU A 72  
AA3 3 4 N ARG A 190 ? N ARG A 69  O LEU A 252 ? O LEU A 131 
AA3 4 5 N ILE A 253 ? N ILE A 132 O TRP A 330 ? O TRP A 209 
AA3 5 6 O MET A 325 ? O MET A 204 N LEU A 279 ? N LEU A 158 
AA3 6 7 N CYS A 276 ? N CYS A 155 O LEU A 384 ? O LEU A 263 
AA4 1 2 N TYR A 259 ? N TYR A 138 O TYR A 392 ? O TYR A 271 
AA5 1 2 N PHE A 429 ? N PHE A 308 O ILE A 448 ? O ILE A 327 
AA5 2 3 N TRP A 447 ? N TRP A 326 O ILE A 465 ? O ILE A 344 
AA5 3 4 N THR A 466 ? N THR A 345 O VAL A 483 ? O VAL A 362 
AA5 4 5 N CYS A 482 ? N CYS A 361 O TYR A 498 ? O TYR A 377 
AA5 5 6 N PHE A 493 ? N PHE A 372 O VAL A 550 ? O VAL A 429 
AA5 6 7 N PHE A 547 ? N PHE A 426 O PHE A 582 ? O PHE A 461 
AA6 1 2 N VAL A 434 ? N VAL A 313 O ILE A 453 ? O ILE A 332 
AA7 1 2 N LEU A 515 ? N LEU A 394 O ILE A 518 ? O ILE A 397 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A EPE 1001 ? 5 'binding site for residue EPE A 1001' 
AC2 Software A ACT 1002 ? 2 'binding site for residue ACT A 1002' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1 AC1 5 PRO A 216 ? PRO A 95   . ? 1_555 ? 
2 AC1 5 MET A 428 ? MET A 307  . ? 1_555 ? 
3 AC1 5 PHE A 429 ? PHE A 308  . ? 1_555 ? 
4 AC1 5 VAL A 430 ? VAL A 309  . ? 1_555 ? 
5 AC1 5 HOH D .   ? HOH A 1180 . ? 1_555 ? 
6 AC2 2 HIS A 452 ? HIS A 331  . ? 1_555 ? 
7 AC2 2 ASN A 471 ? ASN A 350  . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   9IIS 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   N 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   VAL 
_pdbx_validate_close_contact.auth_seq_id_1    309 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O1S 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   EPE 
_pdbx_validate_close_contact.auth_seq_id_2    1001 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.30 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A -68 ? ? -108.60 -62.26  
2  1 LYS A -42 ? ? -76.32  -166.10 
3  1 ASP A -32 ? ? 69.68   -1.13   
4  1 GLN A -27 ? ? -74.21  -159.66 
5  1 GLU A -1  ? ? -50.80  106.21  
6  1 ALA A 74  ? ? -147.62 42.83   
7  1 LYS A 89  ? ? 76.27   -46.29  
8  1 LEU A 105 ? ? -120.17 -135.27 
9  1 SER A 141 ? ? -171.17 135.17  
10 1 PRO A 149 ? ? -57.41  171.19  
11 1 GLU A 150 ? ? -108.35 41.62   
12 1 LYS A 187 ? ? 63.76   62.19   
13 1 GLU A 226 ? ? -66.06  -75.84  
14 1 SER A 227 ? ? -68.64  -78.86  
15 1 GLU A 230 ? ? -134.18 -77.99  
16 1 ASP A 239 ? ? -84.75  -74.84  
17 1 TYR A 273 ? ? -141.79 32.15   
18 1 ASN A 288 ? ? -81.67  35.07   
19 1 ALA A 306 ? ? -94.79  52.01   
20 1 ALA A 339 ? ? -133.60 -115.96 
21 1 ARG A 341 ? ? 59.56   77.15   
22 1 LEU A 443 ? ? -105.56 -111.09 
23 1 GLU A 445 ? ? -118.13 70.75   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 1117 ? D HOH . 
2 1 A HOH 1227 ? D HOH . 
3 1 A HOH 1247 ? D HOH . 
4 1 A HOH 1304 ? D HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 25.4724753192 2.46175399768 18.5817429511 1.04493303014  ? 0.00504558258921 ? 0.0445009000648   ? 
0.66698138708  ? -0.223958699386 ? 1.65364837002  ? 0.218607213701 ? 0.118206195414   ? 0.316108153531 ? 0.300130690306 ? 
0.0802872009184 ? 0.744087932147 ? 0.14759990515  ? -0.629964148883 ? 1.30616836953   ? -0.276746608639  ? 0.0267573872768 ? 
-0.08374027953   ? -0.31013946248  ? -0.643333719286 ? 0.0748122995092   ? 
2 'X-RAY DIFFRACTION' ? refined 51.2802353241 23.8547421838 29.9497810226 0.454060438526 ? -0.131773277535  ? -0.00519913679704 ? 
0.717593832203 ? 0.115769872668  ? 0.484921228219 ? 1.93582775337  ? -0.0494805481069 ? -0.36867318698 ? 2.13123800409  ? 
-0.177973684521 ? 1.3936101827   ? 0.142823956191 ? -0.761917137879 ? -0.134640194647 ? 0.163006655296   ? 0.0387224136898 ? 
0.0942235100958  ? -0.170103210835 ? -0.145012780889 ? 0.000144383433277 ? 
3 'X-RAY DIFFRACTION' ? refined 67.7616136628 37.3701966903 5.14989759511 0.4906673164   ? 0.00516379652373 ? 0.0113492666208   ? 
0.46440767397  ? 0.0611420995117 ? 0.483905573379 ? 2.32091582648  ? 0.224344839732   ? -1.11179935195 ? 1.5152087243   ? 
-0.295478560161 ? 2.01745959134  ? 0.165628074774 ? 0.227883799226  ? 0.341012311616  ? -0.0330721957591 ? -0.118327223798 ? 
-0.0114301772047 ? -0.011515470692 ? 0.21406608626   ? 1.12462723624e-05 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid  -78  through   -3 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid   -2  through  290 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid  305  through  492 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1  1 O ? A HOH 1301 ? 5.90 . 
2  1 O ? A HOH 1302 ? 5.92 . 
3  1 O ? A HOH 1303 ? 6.03 . 
4  1 O ? A HOH 1304 ? 6.14 . 
5  1 O ? A HOH 1305 ? 6.37 . 
6  1 O ? A HOH 1306 ? 6.42 . 
7  1 O ? A HOH 1307 ? 6.44 . 
8  1 O ? A HOH 1308 ? 6.77 . 
9  1 O ? A HOH 1309 ? 6.86 . 
10 1 O ? A HOH 1310 ? 7.05 . 
11 1 O ? A HOH 1311 ? 7.13 . 
12 1 O ? A HOH 1312 ? 7.35 . 
13 1 O ? A HOH 1313 ? 7.47 . 
14 1 O ? A HOH 1314 ? 7.48 . 
15 1 O ? A HOH 1315 ? 7.63 . 
16 1 O ? A HOH 1316 ? 7.72 . 
17 1 O ? A HOH 1317 ? 7.96 . 
18 1 O ? A HOH 1318 ? 8.24 . 
19 1 O ? A HOH 1319 ? 8.26 . 
20 1 O ? A HOH 1320 ? 9.13 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -120 ? A MET 1   
2  1 Y 1 A GLY -119 ? A GLY 2   
3  1 Y 1 A SER -118 ? A SER 3   
4  1 Y 1 A SER -117 ? A SER 4   
5  1 Y 1 A HIS -116 ? A HIS 5   
6  1 Y 1 A HIS -115 ? A HIS 6   
7  1 Y 1 A HIS -114 ? A HIS 7   
8  1 Y 1 A HIS -113 ? A HIS 8   
9  1 Y 1 A HIS -112 ? A HIS 9   
10 1 Y 1 A HIS -111 ? A HIS 10  
11 1 Y 1 A GLY -110 ? A GLY 11  
12 1 Y 1 A SER -109 ? A SER 12  
13 1 Y 1 A GLY -108 ? A GLY 13  
14 1 Y 1 A LEU -107 ? A LEU 14  
15 1 Y 1 A VAL -106 ? A VAL 15  
16 1 Y 1 A PRO -105 ? A PRO 16  
17 1 Y 1 A ARG -104 ? A ARG 17  
18 1 Y 1 A GLY -103 ? A GLY 18  
19 1 Y 1 A SER -102 ? A SER 19  
20 1 Y 1 A ALA -101 ? A ALA 20  
21 1 Y 1 A SER -100 ? A SER 21  
22 1 Y 1 A MET -99  ? A MET 22  
23 1 Y 1 A SER -98  ? A SER 23  
24 1 Y 1 A ASP -97  ? A ASP 24  
25 1 Y 1 A SER -96  ? A SER 25  
26 1 Y 1 A GLU -95  ? A GLU 26  
27 1 Y 1 A VAL -94  ? A VAL 27  
28 1 Y 1 A ASN -93  ? A ASN 28  
29 1 Y 1 A GLN -92  ? A GLN 29  
30 1 Y 1 A GLU -91  ? A GLU 30  
31 1 Y 1 A ALA -90  ? A ALA 31  
32 1 Y 1 A LYS -89  ? A LYS 32  
33 1 Y 1 A PRO -88  ? A PRO 33  
34 1 Y 1 A GLU -87  ? A GLU 34  
35 1 Y 1 A VAL -86  ? A VAL 35  
36 1 Y 1 A LYS -85  ? A LYS 36  
37 1 Y 1 A PRO -84  ? A PRO 37  
38 1 Y 1 A GLU -83  ? A GLU 38  
39 1 Y 1 A VAL -82  ? A VAL 39  
40 1 Y 1 A LYS -81  ? A LYS 40  
41 1 Y 1 A PRO -80  ? A PRO 41  
42 1 Y 1 A GLU -79  ? A GLU 42  
43 1 Y 1 A ARG 98   ? A ARG 219 
44 1 Y 1 A TRP 99   ? A TRP 220 
45 1 Y 1 A GLU 100  ? A GLU 221 
46 1 Y 1 A ARG 101  ? A ARG 222 
47 1 Y 1 A GLY 102  ? A GLY 223 
48 1 Y 1 A GLN 103  ? A GLN 224 
49 1 Y 1 A TYR 291  ? A TYR 412 
50 1 Y 1 A ASP 292  ? A ASP 413 
51 1 Y 1 A GLN 293  ? A GLN 414 
52 1 Y 1 A ARG 294  ? A ARG 415 
53 1 Y 1 A ARG 295  ? A ARG 416 
54 1 Y 1 A ILE 296  ? A ILE 417 
55 1 Y 1 A MET 297  ? A MET 418 
56 1 Y 1 A HIS 298  ? A HIS 419 
57 1 Y 1 A ARG 299  ? A ARG 420 
58 1 Y 1 A LYS 300  ? A LYS 421 
59 1 Y 1 A VAL 301  ? A VAL 422 
60 1 Y 1 A LYS 302  ? A LYS 423 
61 1 Y 1 A PRO 303  ? A PRO 424 
62 1 Y 1 A ASN 304  ? A ASN 425 
63 1 Y 1 A ASN 493  ? A ASN 614 
64 1 Y 1 A HIS 494  ? A HIS 615 
65 1 Y 1 A GLU 495  ? A GLU 616 
66 1 Y 1 A LYS 496  ? A LYS 617 
# 
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 
ACT C    C N N 1   
ACT O    O N N 2   
ACT OXT  O N N 3   
ACT CH3  C N N 4   
ACT H1   H N N 5   
ACT H2   H N N 6   
ACT H3   H N N 7   
ALA N    N N N 8   
ALA CA   C N S 9   
ALA C    C N N 10  
ALA O    O N N 11  
ALA CB   C N N 12  
ALA OXT  O N N 13  
ALA H    H N N 14  
ALA H2   H N N 15  
ALA HA   H N N 16  
ALA HB1  H N N 17  
ALA HB2  H N N 18  
ALA HB3  H N N 19  
ALA HXT  H N N 20  
ARG N    N N N 21  
ARG CA   C N S 22  
ARG C    C N N 23  
ARG O    O N N 24  
ARG CB   C N N 25  
ARG CG   C N N 26  
ARG CD   C N N 27  
ARG NE   N N N 28  
ARG CZ   C N N 29  
ARG NH1  N N N 30  
ARG NH2  N N N 31  
ARG OXT  O N N 32  
ARG H    H N N 33  
ARG H2   H N N 34  
ARG HA   H N N 35  
ARG HB2  H N N 36  
ARG HB3  H N N 37  
ARG HG2  H N N 38  
ARG HG3  H N N 39  
ARG HD2  H N N 40  
ARG HD3  H N N 41  
ARG HE   H N N 42  
ARG HH11 H N N 43  
ARG HH12 H N N 44  
ARG HH21 H N N 45  
ARG HH22 H N N 46  
ARG HXT  H N N 47  
ASN N    N N N 48  
ASN CA   C N S 49  
ASN C    C N N 50  
ASN O    O N N 51  
ASN CB   C N N 52  
ASN CG   C N N 53  
ASN OD1  O N N 54  
ASN ND2  N N N 55  
ASN OXT  O N N 56  
ASN H    H N N 57  
ASN H2   H N N 58  
ASN HA   H N N 59  
ASN HB2  H N N 60  
ASN HB3  H N N 61  
ASN HD21 H N N 62  
ASN HD22 H N N 63  
ASN HXT  H N N 64  
ASP N    N N N 65  
ASP CA   C N S 66  
ASP C    C N N 67  
ASP O    O N N 68  
ASP CB   C N N 69  
ASP CG   C N N 70  
ASP OD1  O N N 71  
ASP OD2  O N N 72  
ASP OXT  O N N 73  
ASP H    H N N 74  
ASP H2   H N N 75  
ASP HA   H N N 76  
ASP HB2  H N N 77  
ASP HB3  H N N 78  
ASP HD2  H N N 79  
ASP HXT  H N N 80  
CYS N    N N N 81  
CYS CA   C N R 82  
CYS C    C N N 83  
CYS O    O N N 84  
CYS CB   C N N 85  
CYS SG   S N N 86  
CYS OXT  O N N 87  
CYS H    H N N 88  
CYS H2   H N N 89  
CYS HA   H N N 90  
CYS HB2  H N N 91  
CYS HB3  H N N 92  
CYS HG   H N N 93  
CYS HXT  H N N 94  
EPE N1   N N N 95  
EPE C2   C N N 96  
EPE C3   C N N 97  
EPE N4   N N N 98  
EPE C5   C N N 99  
EPE C6   C N N 100 
EPE C7   C N N 101 
EPE C8   C N N 102 
EPE O8   O N N 103 
EPE C9   C N N 104 
EPE C10  C N N 105 
EPE S    S N N 106 
EPE O1S  O N N 107 
EPE O2S  O N N 108 
EPE O3S  O N N 109 
EPE H21  H N N 110 
EPE H22  H N N 111 
EPE H31  H N N 112 
EPE H32  H N N 113 
EPE H51  H N N 114 
EPE H52  H N N 115 
EPE H61  H N N 116 
EPE H62  H N N 117 
EPE H71  H N N 118 
EPE H72  H N N 119 
EPE H81  H N N 120 
EPE H82  H N N 121 
EPE HO8  H N N 122 
EPE H91  H N N 123 
EPE H92  H N N 124 
EPE H101 H N N 125 
EPE H102 H N N 126 
EPE HOS3 H N N 127 
GLN N    N N N 128 
GLN CA   C N S 129 
GLN C    C N N 130 
GLN O    O N N 131 
GLN CB   C N N 132 
GLN CG   C N N 133 
GLN CD   C N N 134 
GLN OE1  O N N 135 
GLN NE2  N N N 136 
GLN OXT  O N N 137 
GLN H    H N N 138 
GLN H2   H N N 139 
GLN HA   H N N 140 
GLN HB2  H N N 141 
GLN HB3  H N N 142 
GLN HG2  H N N 143 
GLN HG3  H N N 144 
GLN HE21 H N N 145 
GLN HE22 H N N 146 
GLN HXT  H N N 147 
GLU N    N N N 148 
GLU CA   C N S 149 
GLU C    C N N 150 
GLU O    O N N 151 
GLU CB   C N N 152 
GLU CG   C N N 153 
GLU CD   C N N 154 
GLU OE1  O N N 155 
GLU OE2  O N N 156 
GLU OXT  O N N 157 
GLU H    H N N 158 
GLU H2   H N N 159 
GLU HA   H N N 160 
GLU HB2  H N N 161 
GLU HB3  H N N 162 
GLU HG2  H N N 163 
GLU HG3  H N N 164 
GLU HE2  H N N 165 
GLU HXT  H N N 166 
GLY N    N N N 167 
GLY CA   C N N 168 
GLY C    C N N 169 
GLY O    O N N 170 
GLY OXT  O N N 171 
GLY H    H N N 172 
GLY H2   H N N 173 
GLY HA2  H N N 174 
GLY HA3  H N N 175 
GLY HXT  H N N 176 
HIS N    N N N 177 
HIS CA   C N S 178 
HIS C    C N N 179 
HIS O    O N N 180 
HIS CB   C N N 181 
HIS CG   C Y N 182 
HIS ND1  N Y N 183 
HIS CD2  C Y N 184 
HIS CE1  C Y N 185 
HIS NE2  N Y N 186 
HIS OXT  O N N 187 
HIS H    H N N 188 
HIS H2   H N N 189 
HIS HA   H N N 190 
HIS HB2  H N N 191 
HIS HB3  H N N 192 
HIS HD1  H N N 193 
HIS HD2  H N N 194 
HIS HE1  H N N 195 
HIS HE2  H N N 196 
HIS HXT  H N N 197 
HOH O    O N N 198 
HOH H1   H N N 199 
HOH H2   H N N 200 
ILE N    N N N 201 
ILE CA   C N S 202 
ILE C    C N N 203 
ILE O    O N N 204 
ILE CB   C N S 205 
ILE CG1  C N N 206 
ILE CG2  C N N 207 
ILE CD1  C N N 208 
ILE OXT  O N N 209 
ILE H    H N N 210 
ILE H2   H N N 211 
ILE HA   H N N 212 
ILE HB   H N N 213 
ILE HG12 H N N 214 
ILE HG13 H N N 215 
ILE HG21 H N N 216 
ILE HG22 H N N 217 
ILE HG23 H N N 218 
ILE HD11 H N N 219 
ILE HD12 H N N 220 
ILE HD13 H N N 221 
ILE HXT  H N N 222 
LEU N    N N N 223 
LEU CA   C N S 224 
LEU C    C N N 225 
LEU O    O N N 226 
LEU CB   C N N 227 
LEU CG   C N N 228 
LEU CD1  C N N 229 
LEU CD2  C N N 230 
LEU OXT  O N N 231 
LEU H    H N N 232 
LEU H2   H N N 233 
LEU HA   H N N 234 
LEU HB2  H N N 235 
LEU HB3  H N N 236 
LEU HG   H N N 237 
LEU HD11 H N N 238 
LEU HD12 H N N 239 
LEU HD13 H N N 240 
LEU HD21 H N N 241 
LEU HD22 H N N 242 
LEU HD23 H N N 243 
LEU HXT  H N N 244 
LYS N    N N N 245 
LYS CA   C N S 246 
LYS C    C N N 247 
LYS O    O N N 248 
LYS CB   C N N 249 
LYS CG   C N N 250 
LYS CD   C N N 251 
LYS CE   C N N 252 
LYS NZ   N N N 253 
LYS OXT  O N N 254 
LYS H    H N N 255 
LYS H2   H N N 256 
LYS HA   H N N 257 
LYS HB2  H N N 258 
LYS HB3  H N N 259 
LYS HG2  H N N 260 
LYS HG3  H N N 261 
LYS HD2  H N N 262 
LYS HD3  H N N 263 
LYS HE2  H N N 264 
LYS HE3  H N N 265 
LYS HZ1  H N N 266 
LYS HZ2  H N N 267 
LYS HZ3  H N N 268 
LYS HXT  H N N 269 
MET N    N N N 270 
MET CA   C N S 271 
MET C    C N N 272 
MET O    O N N 273 
MET CB   C N N 274 
MET CG   C N N 275 
MET SD   S N N 276 
MET CE   C N N 277 
MET OXT  O N N 278 
MET H    H N N 279 
MET H2   H N N 280 
MET HA   H N N 281 
MET HB2  H N N 282 
MET HB3  H N N 283 
MET HG2  H N N 284 
MET HG3  H N N 285 
MET HE1  H N N 286 
MET HE2  H N N 287 
MET HE3  H N N 288 
MET HXT  H N N 289 
PHE N    N N N 290 
PHE CA   C N S 291 
PHE C    C N N 292 
PHE O    O N N 293 
PHE CB   C N N 294 
PHE CG   C Y N 295 
PHE CD1  C Y N 296 
PHE CD2  C Y N 297 
PHE CE1  C Y N 298 
PHE CE2  C Y N 299 
PHE CZ   C Y N 300 
PHE OXT  O N N 301 
PHE H    H N N 302 
PHE H2   H N N 303 
PHE HA   H N N 304 
PHE HB2  H N N 305 
PHE HB3  H N N 306 
PHE HD1  H N N 307 
PHE HD2  H N N 308 
PHE HE1  H N N 309 
PHE HE2  H N N 310 
PHE HZ   H N N 311 
PHE HXT  H N N 312 
PRO N    N N N 313 
PRO CA   C N S 314 
PRO C    C N N 315 
PRO O    O N N 316 
PRO CB   C N N 317 
PRO CG   C N N 318 
PRO CD   C N N 319 
PRO OXT  O N N 320 
PRO H    H N N 321 
PRO HA   H N N 322 
PRO HB2  H N N 323 
PRO HB3  H N N 324 
PRO HG2  H N N 325 
PRO HG3  H N N 326 
PRO HD2  H N N 327 
PRO HD3  H N N 328 
PRO HXT  H N N 329 
SER N    N N N 330 
SER CA   C N S 331 
SER C    C N N 332 
SER O    O N N 333 
SER CB   C N N 334 
SER OG   O N N 335 
SER OXT  O N N 336 
SER H    H N N 337 
SER H2   H N N 338 
SER HA   H N N 339 
SER HB2  H N N 340 
SER HB3  H N N 341 
SER HG   H N N 342 
SER HXT  H N N 343 
THR N    N N N 344 
THR CA   C N S 345 
THR C    C N N 346 
THR O    O N N 347 
THR CB   C N R 348 
THR OG1  O N N 349 
THR CG2  C N N 350 
THR OXT  O N N 351 
THR H    H N N 352 
THR H2   H N N 353 
THR HA   H N N 354 
THR HB   H N N 355 
THR HG1  H N N 356 
THR HG21 H N N 357 
THR HG22 H N N 358 
THR HG23 H N N 359 
THR HXT  H N N 360 
TRP N    N N N 361 
TRP CA   C N S 362 
TRP C    C N N 363 
TRP O    O N N 364 
TRP CB   C N N 365 
TRP CG   C Y N 366 
TRP CD1  C Y N 367 
TRP CD2  C Y N 368 
TRP NE1  N Y N 369 
TRP CE2  C Y N 370 
TRP CE3  C Y N 371 
TRP CZ2  C Y N 372 
TRP CZ3  C Y N 373 
TRP CH2  C Y N 374 
TRP OXT  O N N 375 
TRP H    H N N 376 
TRP H2   H N N 377 
TRP HA   H N N 378 
TRP HB2  H N N 379 
TRP HB3  H N N 380 
TRP HD1  H N N 381 
TRP HE1  H N N 382 
TRP HE3  H N N 383 
TRP HZ2  H N N 384 
TRP HZ3  H N N 385 
TRP HH2  H N N 386 
TRP HXT  H N N 387 
TYR N    N N N 388 
TYR CA   C N S 389 
TYR C    C N N 390 
TYR O    O N N 391 
TYR CB   C N N 392 
TYR CG   C Y N 393 
TYR CD1  C Y N 394 
TYR CD2  C Y N 395 
TYR CE1  C Y N 396 
TYR CE2  C Y N 397 
TYR CZ   C Y N 398 
TYR OH   O N N 399 
TYR OXT  O N N 400 
TYR H    H N N 401 
TYR H2   H N N 402 
TYR HA   H N N 403 
TYR HB2  H N N 404 
TYR HB3  H N N 405 
TYR HD1  H N N 406 
TYR HD2  H N N 407 
TYR HE1  H N N 408 
TYR HE2  H N N 409 
TYR HH   H N N 410 
TYR HXT  H N N 411 
VAL N    N N N 412 
VAL CA   C N S 413 
VAL C    C N N 414 
VAL O    O N N 415 
VAL CB   C N N 416 
VAL CG1  C N N 417 
VAL CG2  C N N 418 
VAL OXT  O N N 419 
VAL H    H N N 420 
VAL H2   H N N 421 
VAL HA   H N N 422 
VAL HB   H N N 423 
VAL HG11 H N N 424 
VAL HG12 H N N 425 
VAL HG13 H N N 426 
VAL HG21 H N N 427 
VAL HG22 H N N 428 
VAL HG23 H N N 429 
VAL HXT  H N N 430 
# 
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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
EPE N1  C2   sing N N 89  
EPE N1  C6   sing N N 90  
EPE N1  C9   sing N N 91  
EPE C2  C3   sing N N 92  
EPE C2  H21  sing N N 93  
EPE C2  H22  sing N N 94  
EPE C3  N4   sing N N 95  
EPE C3  H31  sing N N 96  
EPE C3  H32  sing N N 97  
EPE N4  C5   sing N N 98  
EPE N4  C7   sing N N 99  
EPE C5  C6   sing N N 100 
EPE C5  H51  sing N N 101 
EPE C5  H52  sing N N 102 
EPE C6  H61  sing N N 103 
EPE C6  H62  sing N N 104 
EPE C7  C8   sing N N 105 
EPE C7  H71  sing N N 106 
EPE C7  H72  sing N N 107 
EPE C8  O8   sing N N 108 
EPE C8  H81  sing N N 109 
EPE C8  H82  sing N N 110 
EPE O8  HO8  sing N N 111 
EPE C9  C10  sing N N 112 
EPE C9  H91  sing N N 113 
EPE C9  H92  sing N N 114 
EPE C10 S    sing N N 115 
EPE C10 H101 sing N N 116 
EPE C10 H102 sing N N 117 
EPE S   O1S  doub N N 118 
EPE S   O2S  doub N N 119 
EPE S   O3S  sing N N 120 
EPE O3S HOS3 sing N N 121 
GLN N   CA   sing N N 122 
GLN N   H    sing N N 123 
GLN N   H2   sing N N 124 
GLN CA  C    sing N N 125 
GLN CA  CB   sing N N 126 
GLN CA  HA   sing N N 127 
GLN C   O    doub N N 128 
GLN C   OXT  sing N N 129 
GLN CB  CG   sing N N 130 
GLN CB  HB2  sing N N 131 
GLN CB  HB3  sing N N 132 
GLN CG  CD   sing N N 133 
GLN CG  HG2  sing N N 134 
GLN CG  HG3  sing N N 135 
GLN CD  OE1  doub N N 136 
GLN CD  NE2  sing N N 137 
GLN NE2 HE21 sing N N 138 
GLN NE2 HE22 sing N N 139 
GLN OXT HXT  sing N N 140 
GLU N   CA   sing N N 141 
GLU N   H    sing N N 142 
GLU N   H2   sing N N 143 
GLU CA  C    sing N N 144 
GLU CA  CB   sing N N 145 
GLU CA  HA   sing N N 146 
GLU C   O    doub N N 147 
GLU C   OXT  sing N N 148 
GLU CB  CG   sing N N 149 
GLU CB  HB2  sing N N 150 
GLU CB  HB3  sing N N 151 
GLU CG  CD   sing N N 152 
GLU CG  HG2  sing N N 153 
GLU CG  HG3  sing N N 154 
GLU CD  OE1  doub N N 155 
GLU CD  OE2  sing N N 156 
GLU OE2 HE2  sing N N 157 
GLU OXT HXT  sing N N 158 
GLY N   CA   sing N N 159 
GLY N   H    sing N N 160 
GLY N   H2   sing N N 161 
GLY CA  C    sing N N 162 
GLY CA  HA2  sing N N 163 
GLY CA  HA3  sing N N 164 
GLY C   O    doub N N 165 
GLY C   OXT  sing N N 166 
GLY OXT HXT  sing N N 167 
HIS N   CA   sing N N 168 
HIS N   H    sing N N 169 
HIS N   H2   sing N N 170 
HIS CA  C    sing N N 171 
HIS CA  CB   sing N N 172 
HIS CA  HA   sing N N 173 
HIS C   O    doub N N 174 
HIS C   OXT  sing N N 175 
HIS CB  CG   sing N N 176 
HIS CB  HB2  sing N N 177 
HIS CB  HB3  sing N N 178 
HIS CG  ND1  sing Y N 179 
HIS CG  CD2  doub Y N 180 
HIS ND1 CE1  doub Y N 181 
HIS ND1 HD1  sing N N 182 
HIS CD2 NE2  sing Y N 183 
HIS CD2 HD2  sing N N 184 
HIS CE1 NE2  sing Y N 185 
HIS CE1 HE1  sing N N 186 
HIS NE2 HE2  sing N N 187 
HIS OXT HXT  sing N N 188 
HOH O   H1   sing N N 189 
HOH O   H2   sing N N 190 
ILE N   CA   sing N N 191 
ILE N   H    sing N N 192 
ILE N   H2   sing N N 193 
ILE CA  C    sing N N 194 
ILE CA  CB   sing N N 195 
ILE CA  HA   sing N N 196 
ILE C   O    doub N N 197 
ILE C   OXT  sing N N 198 
ILE CB  CG1  sing N N 199 
ILE CB  CG2  sing N N 200 
ILE CB  HB   sing N N 201 
ILE CG1 CD1  sing N N 202 
ILE CG1 HG12 sing N N 203 
ILE CG1 HG13 sing N N 204 
ILE CG2 HG21 sing N N 205 
ILE CG2 HG22 sing N N 206 
ILE CG2 HG23 sing N N 207 
ILE CD1 HD11 sing N N 208 
ILE CD1 HD12 sing N N 209 
ILE CD1 HD13 sing N N 210 
ILE OXT HXT  sing N N 211 
LEU N   CA   sing N N 212 
LEU N   H    sing N N 213 
LEU N   H2   sing N N 214 
LEU CA  C    sing N N 215 
LEU CA  CB   sing N N 216 
LEU CA  HA   sing N N 217 
LEU C   O    doub N N 218 
LEU C   OXT  sing N N 219 
LEU CB  CG   sing N N 220 
LEU CB  HB2  sing N N 221 
LEU CB  HB3  sing N N 222 
LEU CG  CD1  sing N N 223 
LEU CG  CD2  sing N N 224 
LEU CG  HG   sing N N 225 
LEU CD1 HD11 sing N N 226 
LEU CD1 HD12 sing N N 227 
LEU CD1 HD13 sing N N 228 
LEU CD2 HD21 sing N N 229 
LEU CD2 HD22 sing N N 230 
LEU CD2 HD23 sing N N 231 
LEU OXT HXT  sing N N 232 
LYS N   CA   sing N N 233 
LYS N   H    sing N N 234 
LYS N   H2   sing N N 235 
LYS CA  C    sing N N 236 
LYS CA  CB   sing N N 237 
LYS CA  HA   sing N N 238 
LYS C   O    doub N N 239 
LYS C   OXT  sing N N 240 
LYS CB  CG   sing N N 241 
LYS CB  HB2  sing N N 242 
LYS CB  HB3  sing N N 243 
LYS CG  CD   sing N N 244 
LYS CG  HG2  sing N N 245 
LYS CG  HG3  sing N N 246 
LYS CD  CE   sing N N 247 
LYS CD  HD2  sing N N 248 
LYS CD  HD3  sing N N 249 
LYS CE  NZ   sing N N 250 
LYS CE  HE2  sing N N 251 
LYS CE  HE3  sing N N 252 
LYS NZ  HZ1  sing N N 253 
LYS NZ  HZ2  sing N N 254 
LYS NZ  HZ3  sing N N 255 
LYS OXT HXT  sing N N 256 
MET N   CA   sing N N 257 
MET N   H    sing N N 258 
MET N   H2   sing N N 259 
MET CA  C    sing N N 260 
MET CA  CB   sing N N 261 
MET CA  HA   sing N N 262 
MET C   O    doub N N 263 
MET C   OXT  sing N N 264 
MET CB  CG   sing N N 265 
MET CB  HB2  sing N N 266 
MET CB  HB3  sing N N 267 
MET CG  SD   sing N N 268 
MET CG  HG2  sing N N 269 
MET CG  HG3  sing N N 270 
MET SD  CE   sing N N 271 
MET CE  HE1  sing N N 272 
MET CE  HE2  sing N N 273 
MET CE  HE3  sing N N 274 
MET OXT HXT  sing N N 275 
PHE N   CA   sing N N 276 
PHE N   H    sing N N 277 
PHE N   H2   sing N N 278 
PHE CA  C    sing N N 279 
PHE CA  CB   sing N N 280 
PHE CA  HA   sing N N 281 
PHE C   O    doub N N 282 
PHE C   OXT  sing N N 283 
PHE CB  CG   sing N N 284 
PHE CB  HB2  sing N N 285 
PHE CB  HB3  sing N N 286 
PHE CG  CD1  doub Y N 287 
PHE CG  CD2  sing Y N 288 
PHE CD1 CE1  sing Y N 289 
PHE CD1 HD1  sing N N 290 
PHE CD2 CE2  doub Y N 291 
PHE CD2 HD2  sing N N 292 
PHE CE1 CZ   doub Y N 293 
PHE CE1 HE1  sing N N 294 
PHE CE2 CZ   sing Y N 295 
PHE CE2 HE2  sing N N 296 
PHE CZ  HZ   sing N N 297 
PHE OXT HXT  sing N N 298 
PRO N   CA   sing N N 299 
PRO N   CD   sing N N 300 
PRO N   H    sing N N 301 
PRO CA  C    sing N N 302 
PRO CA  CB   sing N N 303 
PRO CA  HA   sing N N 304 
PRO C   O    doub N N 305 
PRO C   OXT  sing N N 306 
PRO CB  CG   sing N N 307 
PRO CB  HB2  sing N N 308 
PRO CB  HB3  sing N N 309 
PRO CG  CD   sing N N 310 
PRO CG  HG2  sing N N 311 
PRO CG  HG3  sing N N 312 
PRO CD  HD2  sing N N 313 
PRO CD  HD3  sing N N 314 
PRO OXT HXT  sing N N 315 
SER N   CA   sing N N 316 
SER N   H    sing N N 317 
SER N   H2   sing N N 318 
SER CA  C    sing N N 319 
SER CA  CB   sing N N 320 
SER CA  HA   sing N N 321 
SER C   O    doub N N 322 
SER C   OXT  sing N N 323 
SER CB  OG   sing N N 324 
SER CB  HB2  sing N N 325 
SER CB  HB3  sing N N 326 
SER OG  HG   sing N N 327 
SER OXT HXT  sing N N 328 
THR N   CA   sing N N 329 
THR N   H    sing N N 330 
THR N   H2   sing N N 331 
THR CA  C    sing N N 332 
THR CA  CB   sing N N 333 
THR CA  HA   sing N N 334 
THR C   O    doub N N 335 
THR C   OXT  sing N N 336 
THR CB  OG1  sing N N 337 
THR CB  CG2  sing N N 338 
THR CB  HB   sing N N 339 
THR OG1 HG1  sing N N 340 
THR CG2 HG21 sing N N 341 
THR CG2 HG22 sing N N 342 
THR CG2 HG23 sing N N 343 
THR OXT HXT  sing N N 344 
TRP N   CA   sing N N 345 
TRP N   H    sing N N 346 
TRP N   H2   sing N N 347 
TRP CA  C    sing N N 348 
TRP CA  CB   sing N N 349 
TRP CA  HA   sing N N 350 
TRP C   O    doub N N 351 
TRP C   OXT  sing N N 352 
TRP CB  CG   sing N N 353 
TRP CB  HB2  sing N N 354 
TRP CB  HB3  sing N N 355 
TRP CG  CD1  doub Y N 356 
TRP CG  CD2  sing Y N 357 
TRP CD1 NE1  sing Y N 358 
TRP CD1 HD1  sing N N 359 
TRP CD2 CE2  doub Y N 360 
TRP CD2 CE3  sing Y N 361 
TRP NE1 CE2  sing Y N 362 
TRP NE1 HE1  sing N N 363 
TRP CE2 CZ2  sing Y N 364 
TRP CE3 CZ3  doub Y N 365 
TRP CE3 HE3  sing N N 366 
TRP CZ2 CH2  doub Y N 367 
TRP CZ2 HZ2  sing N N 368 
TRP CZ3 CH2  sing Y N 369 
TRP CZ3 HZ3  sing N N 370 
TRP CH2 HH2  sing N N 371 
TRP OXT HXT  sing N N 372 
TYR N   CA   sing N N 373 
TYR N   H    sing N N 374 
TYR N   H2   sing N N 375 
TYR CA  C    sing N N 376 
TYR CA  CB   sing N N 377 
TYR CA  HA   sing N N 378 
TYR C   O    doub N N 379 
TYR C   OXT  sing N N 380 
TYR CB  CG   sing N N 381 
TYR CB  HB2  sing N N 382 
TYR CB  HB3  sing N N 383 
TYR CG  CD1  doub Y N 384 
TYR CG  CD2  sing Y N 385 
TYR CD1 CE1  sing Y N 386 
TYR CD1 HD1  sing N N 387 
TYR CD2 CE2  doub Y N 388 
TYR CD2 HD2  sing N N 389 
TYR CE1 CZ   doub Y N 390 
TYR CE1 HE1  sing N N 391 
TYR CE2 CZ   sing Y N 392 
TYR CE2 HE2  sing N N 393 
TYR CZ  OH   sing N N 394 
TYR OH  HH   sing N N 395 
TYR OXT HXT  sing N N 396 
VAL N   CA   sing N N 397 
VAL N   H    sing N N 398 
VAL N   H2   sing N N 399 
VAL CA  C    sing N N 400 
VAL CA  CB   sing N N 401 
VAL CA  HA   sing N N 402 
VAL C   O    doub N N 403 
VAL C   OXT  sing N N 404 
VAL CB  CG1  sing N N 405 
VAL CB  CG2  sing N N 406 
VAL CB  HB   sing N N 407 
VAL CG1 HG11 sing N N 408 
VAL CG1 HG12 sing N N 409 
VAL CG1 HG13 sing N N 410 
VAL CG2 HG21 sing N N 411 
VAL CG2 HG22 sing N N 412 
VAL CG2 HG23 sing N N 413 
VAL OXT HXT  sing N N 414 
# 
_pdbx_audit_support.funding_organization   'Academia Sinica (Taiwan)' 
_pdbx_audit_support.country                Taiwan 
_pdbx_audit_support.grant_number           AS-KPQ-105-TPP 
_pdbx_audit_support.ordinal                1 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9IIS 
_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]   0.011549 
_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]   0.009103 
_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]   0.006939 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 25.62398 1.50364  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 19.97189 1.75589  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 15.80542 1.70748  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 1.23737  29.19336 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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 43  ? 14.71863 -12.10630 14.04545  1.000 101.24821 ? -78  THR A N   1 
ATOM   2    C CA  . THR A 1 43  ? 16.12851 -12.35421 13.76641  1.000 109.54556 ? -78  THR A CA  1 
ATOM   3    C C   . THR A 1 43  ? 16.99369 -11.20030 14.27007  1.000 104.47480 ? -78  THR A C   1 
ATOM   4    O O   . THR A 1 43  ? 16.93410 -10.08664 13.74589  1.000 96.14056  ? -78  THR A O   1 
ATOM   5    C CB  . THR A 1 43  ? 16.37877 -12.56762 12.25950  1.000 112.06679 ? -78  THR A CB  1 
ATOM   6    O OG1 . THR A 1 43  ? 17.73324 -12.22283 11.94211  1.000 111.31074 ? -78  THR A OG1 1 
ATOM   7    C CG2 . THR A 1 43  ? 15.42554 -11.71552 11.42901  1.000 112.30582 ? -78  THR A CG2 1 
ATOM   8    N N   . HIS A 1 44  ? 17.79451 -11.47284 15.29439  1.000 104.70276 ? -77  HIS A N   1 
ATOM   9    C CA  . HIS A 1 44  ? 18.50189 -10.43973 16.03458  1.000 99.48302  ? -77  HIS A CA  1 
ATOM   10   C C   . HIS A 1 44  ? 19.98396 -10.45965 15.68348  1.000 90.23423  ? -77  HIS A C   1 
ATOM   11   O O   . HIS A 1 44  ? 20.48433 -11.37127 15.01927  1.000 85.75245  ? -77  HIS A O   1 
ATOM   12   C CB  . HIS A 1 44  ? 18.30778 -10.62157 17.54472  1.000 105.52032 ? -77  HIS A CB  1 
ATOM   13   C CG  . HIS A 1 44  ? 16.91834 -10.32270 18.01608  1.000 113.61223 ? -77  HIS A CG  1 
ATOM   14   N ND1 . HIS A 1 44  ? 15.90410 -9.95465  17.15832  1.000 117.74710 ? -77  HIS A ND1 1 
ATOM   15   C CD2 . HIS A 1 44  ? 16.37652 -10.33170 19.25704  1.000 113.80128 ? -77  HIS A CD2 1 
ATOM   16   C CE1 . HIS A 1 44  ? 14.79636 -9.75474  17.84978  1.000 115.71109 ? -77  HIS A CE1 1 
ATOM   17   N NE2 . HIS A 1 44  ? 15.05633 -9.97531  19.12582  1.000 117.62890 ? -77  HIS A NE2 1 
ATOM   18   N N   . ILE A 1 45  ? 20.68672 -9.43214  16.15101  1.000 93.37127  ? -76  ILE A N   1 
ATOM   19   C CA  . ILE A 1 45  ? 22.09766 -9.23061  15.84991  1.000 85.32879  ? -76  ILE A CA  1 
ATOM   20   C C   . ILE A 1 45  ? 22.77351 -8.66842  17.09324  1.000 86.55476  ? -76  ILE A C   1 
ATOM   21   O O   . ILE A 1 45  ? 22.16947 -7.89502  17.84786  1.000 85.44741  ? -76  ILE A O   1 
ATOM   22   C CB  . ILE A 1 45  ? 22.27612 -8.29814  14.62880  1.000 88.02166  ? -76  ILE A CB  1 
ATOM   23   C CG1 . ILE A 1 45  ? 22.09215 -9.08308  13.32820  1.000 103.10018 ? -76  ILE A CG1 1 
ATOM   24   C CG2 . ILE A 1 45  ? 23.62697 -7.59973  14.63840  1.000 89.52978  ? -76  ILE A CG2 1 
ATOM   25   C CD1 . ILE A 1 45  ? 22.98964 -10.29635 13.21114  1.000 96.98295  ? -76  ILE A CD1 1 
ATOM   26   N N   . ASN A 1 46  ? 24.02473 -9.06973  17.31214  1.000 88.35469  ? -75  ASN A N   1 
ATOM   27   C CA  . ASN A 1 46  ? 24.83189 -8.55654  18.40720  1.000 87.42759  ? -75  ASN A CA  1 
ATOM   28   C C   . ASN A 1 46  ? 25.78754 -7.50300  17.86534  1.000 90.06729  ? -75  ASN A C   1 
ATOM   29   O O   . ASN A 1 46  ? 26.35527 -7.66610  16.78135  1.000 101.39423 ? -75  ASN A O   1 
ATOM   30   C CB  . ASN A 1 46  ? 25.62038 -9.68658  19.07116  1.000 77.49727  ? -75  ASN A CB  1 
ATOM   31   C CG  . ASN A 1 46  ? 24.74076 -10.86021 19.45409  1.000 83.98443  ? -75  ASN A CG  1 
ATOM   32   O OD1 . ASN A 1 46  ? 23.62374 -10.68129 19.93901  1.000 81.41153  ? -75  ASN A OD1 1 
ATOM   33   N ND2 . ASN A 1 46  ? 25.24064 -12.07184 19.23357  1.000 77.06609  ? -75  ASN A ND2 1 
ATOM   34   N N   . LEU A 1 47  ? 25.95943 -6.41991  18.61917  1.000 94.19926  ? -74  LEU A N   1 
ATOM   35   C CA  . LEU A 1 47  ? 26.79602 -5.30648  18.18977  1.000 86.09964  ? -74  LEU A CA  1 
ATOM   36   C C   . LEU A 1 47  ? 27.69626 -4.85370  19.32601  1.000 92.11297  ? -74  LEU A C   1 
ATOM   37   O O   . LEU A 1 47  ? 27.22878 -4.66184  20.45144  1.000 88.61016  ? -74  LEU A O   1 
ATOM   38   C CB  . LEU A 1 47  ? 25.94683 -4.12573  17.71306  1.000 93.45357  ? -74  LEU A CB  1 
ATOM   39   C CG  . LEU A 1 47  ? 25.04606 -4.35748  16.50253  1.000 95.69963  ? -74  LEU A CG  1 
ATOM   40   C CD1 . LEU A 1 47  ? 24.16825 -3.14467  16.27774  1.000 88.61034  ? -74  LEU A CD1 1 
ATOM   41   C CD2 . LEU A 1 47  ? 25.88234 -4.65406  15.26642  1.000 92.08507  ? -74  LEU A CD2 1 
ATOM   42   N N   . LYS A 1 48  ? 28.97916 -4.67605  19.02819  1.000 94.68400  ? -73  LYS A N   1 
ATOM   43   C CA  . LYS A 1 48  ? 29.87917 -4.00411  19.95089  1.000 97.55403  ? -73  LYS A CA  1 
ATOM   44   C C   . LYS A 1 48  ? 29.74010 -2.49784  19.80600  1.000 101.08319 ? -73  LYS A C   1 
ATOM   45   O O   . LYS A 1 48  ? 29.52313 -1.98308  18.70581  1.000 110.48880 ? -73  LYS A O   1 
ATOM   46   C CB  . LYS A 1 48  ? 31.33178 -4.40195  19.69070  1.000 98.17283  ? -73  LYS A CB  1 
ATOM   47   C CG  . LYS A 1 48  ? 31.64268 -5.85444  19.93996  1.000 95.96296  ? -73  LYS A CG  1 
ATOM   48   C CD  . LYS A 1 48  ? 33.12249 -6.06475  20.22026  1.000 90.33193  ? -73  LYS A CD  1 
ATOM   49   C CE  . LYS A 1 48  ? 33.94190 -5.98144  18.94493  1.000 88.12852  ? -73  LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 48  ? 33.59773 -7.08104  18.00434  1.000 91.29365  ? -73  LYS A NZ  1 
ATOM   51   N N   . VAL A 1 49  ? 29.85345 -1.78966  20.92306  1.000 91.20351  ? -72  VAL A N   1 
ATOM   52   C CA  . VAL A 1 49  ? 30.15445 -0.36517  20.90274  1.000 101.30764 ? -72  VAL A CA  1 
ATOM   53   C C   . VAL A 1 49  ? 31.40848 -0.13582  21.73526  1.000 104.75265 ? -72  VAL A C   1 
ATOM   54   O O   . VAL A 1 49  ? 31.53236 -0.66245  22.85005  1.000 103.92771 ? -72  VAL A O   1 
ATOM   55   C CB  . VAL A 1 49  ? 28.97149 0.49609   21.38731  1.000 100.54022 ? -72  VAL A CB  1 
ATOM   56   C CG1 . VAL A 1 49  ? 28.59873 0.16524   22.80012  1.000 108.63852 ? -72  VAL A CG1 1 
ATOM   57   C CG2 . VAL A 1 49  ? 29.30960 1.97789   21.26190  1.000 96.30312  ? -72  VAL A CG2 1 
ATOM   58   N N   . SER A 1 50  ? 32.35765 0.59358   21.15604  1.000 102.24143 ? -71  SER A N   1 
ATOM   59   C CA  . SER A 1 50  ? 33.64206 0.89878   21.76806  1.000 107.71842 ? -71  SER A CA  1 
ATOM   60   C C   . SER A 1 50  ? 33.72846 2.39535   22.02009  1.000 112.29882 ? -71  SER A C   1 
ATOM   61   O O   . SER A 1 50  ? 33.41431 3.19618   21.13270  1.000 115.07146 ? -71  SER A O   1 
ATOM   62   C CB  . SER A 1 50  ? 34.80240 0.44682   20.87753  1.000 106.82318 ? -71  SER A CB  1 
ATOM   63   O OG  . SER A 1 50  ? 36.03944 0.96099   21.34384  1.000 108.72437 ? -71  SER A OG  1 
ATOM   64   N N   . ASP A 1 51  ? 34.14581 2.76726   23.22632  1.000 116.05392 ? -70  ASP A N   1 
ATOM   65   C CA  . ASP A 1 51  ? 34.47827 4.15128   23.53013  1.000 113.18989 ? -70  ASP A CA  1 
ATOM   66   C C   . ASP A 1 51  ? 35.95500 4.45754   23.32848  1.000 111.14448 ? -70  ASP A C   1 
ATOM   67   O O   . ASP A 1 51  ? 36.34713 5.62736   23.40127  1.000 112.40808 ? -70  ASP A O   1 
ATOM   68   C CB  . ASP A 1 51  ? 34.07980 4.48895   24.97008  1.000 117.37933 ? -70  ASP A CB  1 
ATOM   69   C CG  . ASP A 1 51  ? 34.73436 3.57247   25.98778  1.000 113.88392 ? -70  ASP A CG  1 
ATOM   70   O OD1 . ASP A 1 51  ? 35.45202 2.63226   25.58403  1.000 115.56687 ? -70  ASP A OD1 1 
ATOM   71   O OD2 . ASP A 1 51  ? 34.52657 3.79212   27.19872  1.000 119.06643 ? -70  ASP A OD2 1 
ATOM   72   N N   . GLY A 1 52  ? 36.77427 3.43972   23.08339  1.000 105.51458 ? -69  GLY A N   1 
ATOM   73   C CA  . GLY A 1 52  ? 38.20135 3.62144   22.92671  1.000 109.06779 ? -69  GLY A CA  1 
ATOM   74   C C   . GLY A 1 52  ? 38.96431 2.64491   23.79379  1.000 117.58105 ? -69  GLY A C   1 
ATOM   75   O O   . GLY A 1 52  ? 40.07576 2.22779   23.45463  1.000 108.06375 ? -69  GLY A O   1 
ATOM   76   N N   . SER A 1 53  ? 38.36809 2.27408   24.92645  1.000 126.37371 ? -68  SER A N   1 
ATOM   77   C CA  . SER A 1 53  ? 38.98338 1.35271   25.87219  1.000 134.19435 ? -68  SER A CA  1 
ATOM   78   C C   . SER A 1 53  ? 38.29887 -0.00842  25.87665  1.000 130.53609 ? -68  SER A C   1 
ATOM   79   O O   . SER A 1 53  ? 38.92831 -1.01890  25.55065  1.000 137.67939 ? -68  SER A O   1 
ATOM   80   C CB  . SER A 1 53  ? 38.96885 1.96096   27.28162  1.000 140.65253 ? -68  SER A CB  1 
ATOM   81   O OG  . SER A 1 53  ? 37.69286 2.48893   27.59926  1.000 146.58649 ? -68  SER A OG  1 
ATOM   82   N N   . SER A 1 54  ? 37.02048 -0.06202  26.23840  1.000 116.82664 ? -67  SER A N   1 
ATOM   83   C CA  . SER A 1 54  ? 36.27769 -1.30878  26.33002  1.000 108.38615 ? -67  SER A CA  1 
ATOM   84   C C   . SER A 1 54  ? 35.22121 -1.39028  25.23547  1.000 98.92206  ? -67  SER A C   1 
ATOM   85   O O   . SER A 1 54  ? 34.83217 -0.38485  24.63510  1.000 96.11550  ? -67  SER A O   1 
ATOM   86   C CB  . SER A 1 54  ? 35.61446 -1.45205  27.70539  1.000 104.11906 ? -67  SER A CB  1 
ATOM   87   O OG  . SER A 1 54  ? 34.77761 -0.34342  27.98503  1.000 110.46577 ? -67  SER A OG  1 
ATOM   88   N N   . GLU A 1 55  ? 34.76306 -2.61446  24.98389  1.000 86.81568  ? -66  GLU A N   1 
ATOM   89   C CA  . GLU A 1 55  ? 33.71108 -2.89509  24.01646  1.000 93.46568  ? -66  GLU A CA  1 
ATOM   90   C C   . GLU A 1 55  ? 32.56025 -3.57451  24.74353  1.000 96.53462  ? -66  GLU A C   1 
ATOM   91   O O   . GLU A 1 55  ? 32.78026 -4.52166  25.50563  1.000 100.53226 ? -66  GLU A O   1 
ATOM   92   C CB  . GLU A 1 55  ? 34.22809 -3.78451  22.88351  1.000 91.76378  ? -66  GLU A CB  1 
ATOM   93   C CG  . GLU A 1 55  ? 35.41560 -3.20087  22.13268  1.000 92.96987  ? -66  GLU A CG  1 
ATOM   94   C CD  . GLU A 1 55  ? 36.12291 -4.22715  21.27152  1.000 89.83643  ? -66  GLU A CD  1 
ATOM   95   O OE1 . GLU A 1 55  ? 36.06422 -5.42779  21.60979  1.000 92.87174  ? -66  GLU A OE1 1 
ATOM   96   O OE2 . GLU A 1 55  ? 36.73998 -3.83189  20.25964  1.000 95.25293  ? -66  GLU A OE2 1 
ATOM   97   N N   . ILE A 1 56  ? 31.33833 -3.09979  24.50902  1.000 97.41098  ? -65  ILE A N   1 
ATOM   98   C CA  . ILE A 1 56  ? 30.15984 -3.63261  25.18709  1.000 86.74696  ? -65  ILE A CA  1 
ATOM   99   C C   . ILE A 1 56  ? 29.12294 -4.06663  24.15601  1.000 89.67694  ? -65  ILE A C   1 
ATOM   100  O O   . ILE A 1 56  ? 28.88370 -3.36641  23.16557  1.000 88.98967  ? -65  ILE A O   1 
ATOM   101  C CB  . ILE A 1 56  ? 29.57657 -2.60712  26.18677  1.000 86.70868  ? -65  ILE A CB  1 
ATOM   102  C CG1 . ILE A 1 56  ? 28.09186 -2.86571  26.45361  1.000 98.11543  ? -65  ILE A CG1 1 
ATOM   103  C CG2 . ILE A 1 56  ? 29.84458 -1.18625  25.72909  1.000 91.08320  ? -65  ILE A CG2 1 
ATOM   104  C CD1 . ILE A 1 56  ? 27.74365 -2.92644  27.92228  1.000 97.67743  ? -65  ILE A CD1 1 
ATOM   105  N N   . PHE A 1 57  ? 28.52117 -5.23555  24.38964  1.000 84.48422  ? -64  PHE A N   1 
ATOM   106  C CA  . PHE A 1 57  ? 27.65855 -5.91433  23.43029  1.000 92.21387  ? -64  PHE A CA  1 
ATOM   107  C C   . PHE A 1 57  ? 26.18891 -5.60051  23.68503  1.000 98.84786  ? -64  PHE A C   1 
ATOM   108  O O   . PHE A 1 57  ? 25.73299 -5.58091  24.83272  1.000 99.28581  ? -64  PHE A O   1 
ATOM   109  C CB  . PHE A 1 57  ? 27.85870 -7.42978  23.50342  1.000 103.06965 ? -64  PHE A CB  1 
ATOM   110  C CG  . PHE A 1 57  ? 28.93227 -7.95889  22.59399  1.000 107.02208 ? -64  PHE A CG  1 
ATOM   111  C CD1 . PHE A 1 57  ? 28.67732 -8.16077  21.24657  1.000 104.67434 ? -64  PHE A CD1 1 
ATOM   112  C CD2 . PHE A 1 57  ? 30.18749 -8.27402  23.08824  1.000 101.47546 ? -64  PHE A CD2 1 
ATOM   113  C CE1 . PHE A 1 57  ? 29.65559 -8.65937  20.40770  1.000 107.55134 ? -64  PHE A CE1 1 
ATOM   114  C CE2 . PHE A 1 57  ? 31.17119 -8.76955  22.25394  1.000 101.92790 ? -64  PHE A CE2 1 
ATOM   115  C CZ  . PHE A 1 57  ? 30.90379 -8.96738  20.91296  1.000 100.13818 ? -64  PHE A CZ  1 
ATOM   116  N N   . PHE A 1 58  ? 25.45400 -5.36136  22.60077  1.000 90.37099  ? -63  PHE A N   1 
ATOM   117  C CA  . PHE A 1 58  ? 24.00791 -5.17944  22.62456  1.000 90.12637  ? -63  PHE A CA  1 
ATOM   118  C C   . PHE A 1 58  ? 23.36360 -6.16440  21.66027  1.000 88.99011  ? -63  PHE A C   1 
ATOM   119  O O   . PHE A 1 58  ? 23.76535 -6.24497  20.49521  1.000 81.81130  ? -63  PHE A O   1 
ATOM   120  C CB  . PHE A 1 58  ? 23.60906 -3.75235  22.23062  1.000 85.97119  ? -63  PHE A CB  1 
ATOM   121  C CG  . PHE A 1 58  ? 24.10533 -2.68966  23.16973  1.000 90.95223  ? -63  PHE A CG  1 
ATOM   122  C CD1 . PHE A 1 58  ? 25.45174 -2.37805  23.24450  1.000 105.53133 ? -63  PHE A CD1 1 
ATOM   123  C CD2 . PHE A 1 58  ? 23.21565 -1.97670  23.95477  1.000 101.64687 ? -63  PHE A CD2 1 
ATOM   124  C CE1 . PHE A 1 58  ? 25.90305 -1.39730  24.10308  1.000 106.00144 ? -63  PHE A CE1 1 
ATOM   125  C CE2 . PHE A 1 58  ? 23.66264 -0.98956  24.81178  1.000 104.51245 ? -63  PHE A CE2 1 
ATOM   126  C CZ  . PHE A 1 58  ? 25.00828 -0.69999  24.88528  1.000 106.45219 ? -63  PHE A CZ  1 
ATOM   127  N N   . LYS A 1 59  ? 22.37386 -6.91098  22.14222  1.000 93.09167  ? -62  LYS A N   1 
ATOM   128  C CA  . LYS A 1 59  ? 21.48431 -7.66913  21.27171  1.000 97.84132  ? -62  LYS A CA  1 
ATOM   129  C C   . LYS A 1 59  ? 20.33448 -6.76356  20.84955  1.000 99.58628  ? -62  LYS A C   1 
ATOM   130  O O   . LYS A 1 59  ? 19.67181 -6.16907  21.70605  1.000 105.02070 ? -62  LYS A O   1 
ATOM   131  C CB  . LYS A 1 59  ? 20.95257 -8.90887  21.99414  1.000 100.21387 ? -62  LYS A CB  1 
ATOM   132  C CG  . LYS A 1 59  ? 19.88394 -9.68175  21.23230  1.000 107.51189 ? -62  LYS A CG  1 
ATOM   133  C CD  . LYS A 1 59  ? 20.46427 -10.91752 20.56227  1.000 108.34644 ? -62  LYS A CD  1 
ATOM   134  C CE  . LYS A 1 59  ? 21.06123 -11.86852 21.59044  1.000 108.22624 ? -62  LYS A CE  1 
ATOM   135  N NZ  . LYS A 1 59  ? 21.66189 -13.07614 20.95825  1.000 104.28019 ? -62  LYS A NZ  1 
ATOM   136  N N   . ILE A 1 60  ? 20.08016 -6.67429  19.54022  1.000 98.12480  ? -61  ILE A N   1 
ATOM   137  C CA  . ILE A 1 60  ? 18.96523 -5.87288  19.03799  1.000 100.76043 ? -61  ILE A CA  1 
ATOM   138  C C   . ILE A 1 60  ? 18.43451 -6.47615  17.74533  1.000 107.09675 ? -61  ILE A C   1 
ATOM   139  O O   . ILE A 1 60  ? 19.16101 -7.13322  16.99566  1.000 97.38045  ? -61  ILE A O   1 
ATOM   140  C CB  . ILE A 1 60  ? 19.34777 -4.39067  18.79742  1.000 102.22112 ? -61  ILE A CB  1 
ATOM   141  C CG1 . ILE A 1 60  ? 20.62420 -4.28431  17.96634  1.000 99.88677  ? -61  ILE A CG1 1 
ATOM   142  C CG2 . ILE A 1 60  ? 19.44671 -3.60207  20.10448  1.000 101.35041 ? -61  ILE A CG2 1 
ATOM   143  C CD1 . ILE A 1 60  ? 20.79117 -2.92923  17.33725  1.000 108.26869 ? -61  ILE A CD1 1 
ATOM   144  N N   . LYS A 1 61  ? 17.14966 -6.23607  17.48884  1.000 109.48037 ? -60  LYS A N   1 
ATOM   145  C CA  . LYS A 1 61  ? 16.50775 -6.68432  16.26164  1.000 109.27250 ? -60  LYS A CA  1 
ATOM   146  C C   . LYS A 1 61  ? 16.93886 -5.80568  15.09340  1.000 114.13399 ? -60  LYS A C   1 
ATOM   147  O O   . LYS A 1 61  ? 17.11344 -4.59264  15.24195  1.000 121.12006 ? -60  LYS A O   1 
ATOM   148  C CB  . LYS A 1 61  ? 14.98703 -6.64748  16.41739  1.000 120.47043 ? -60  LYS A CB  1 
ATOM   149  C CG  . LYS A 1 61  ? 14.21427 -7.21880  15.24091  1.000 123.03972 ? -60  LYS A CG  1 
ATOM   150  C CD  . LYS A 1 61  ? 12.71413 -7.07362  15.45064  1.000 125.65540 ? -60  LYS A CD  1 
ATOM   151  C CE  . LYS A 1 61  ? 11.93246 -7.59027  14.25217  1.000 126.40263 ? -60  LYS A CE  1 
ATOM   152  N NZ  . LYS A 1 61  ? 10.54410 -7.05350  14.21810  1.000 124.15440 ? -60  LYS A NZ  1 
ATOM   153  N N   . LYS A 1 62  ? 17.11258 -6.42770  13.92397  1.000 112.36432 ? -59  LYS A N   1 
ATOM   154  C CA  . LYS A 1 62  ? 17.65902 -5.72774  12.76533  1.000 112.29154 ? -59  LYS A CA  1 
ATOM   155  C C   . LYS A 1 62  ? 16.76798 -4.59304  12.27429  1.000 117.74727 ? -59  LYS A C   1 
ATOM   156  O O   . LYS A 1 62  ? 17.23533 -3.76061  11.48878  1.000 117.46058 ? -59  LYS A O   1 
ATOM   157  C CB  . LYS A 1 62  ? 17.91391 -6.71895  11.62806  1.000 111.97370 ? -59  LYS A CB  1 
ATOM   158  C CG  . LYS A 1 62  ? 19.05481 -7.68506  11.90510  1.000 110.56308 ? -59  LYS A CG  1 
ATOM   159  C CD  . LYS A 1 62  ? 19.38007 -8.53572  10.68717  1.000 110.54129 ? -59  LYS A CD  1 
ATOM   160  C CE  . LYS A 1 62  ? 18.24908 -9.49620  10.35945  1.000 103.20064 ? -59  LYS A CE  1 
ATOM   161  N NZ  . LYS A 1 62  ? 18.73225 -10.67473 9.58655   1.000 101.48559 ? -59  LYS A NZ  1 
ATOM   162  N N   . THR A 1 63  ? 15.50942 -4.53474  12.70829  1.000 123.25981 ? -58  THR A N   1 
ATOM   163  C CA  . THR A 1 63  ? 14.59674 -3.47032  12.31244  1.000 128.30968 ? -58  THR A CA  1 
ATOM   164  C C   . THR A 1 63  ? 14.24729 -2.54807  13.47309  1.000 131.28387 ? -58  THR A C   1 
ATOM   165  O O   . THR A 1 63  ? 13.33415 -1.72483  13.34767  1.000 138.45605 ? -58  THR A O   1 
ATOM   166  C CB  . THR A 1 63  ? 13.32008 -4.05685  11.70590  1.000 128.62566 ? -58  THR A CB  1 
ATOM   167  O OG1 . THR A 1 63  ? 12.74396 -5.00047  12.61732  1.000 123.22901 ? -58  THR A OG1 1 
ATOM   168  C CG2 . THR A 1 63  ? 13.62703 -4.75102  10.38536  1.000 127.34968 ? -58  THR A CG2 1 
ATOM   169  N N   . THR A 1 64  ? 14.94891 -2.66881  14.59902  1.000 124.42477 ? -57  THR A N   1 
ATOM   170  C CA  . THR A 1 64  ? 14.75861 -1.78136  15.74093  1.000 123.29414 ? -57  THR A CA  1 
ATOM   171  C C   . THR A 1 64  ? 15.65427 -0.55736  15.59322  1.000 124.30285 ? -57  THR A C   1 
ATOM   172  O O   . THR A 1 64  ? 16.84404 -0.70478  15.29159  1.000 123.68408 ? -57  THR A O   1 
ATOM   173  C CB  . THR A 1 64  ? 15.07838 -2.50132  17.04585  1.000 117.31559 ? -57  THR A CB  1 
ATOM   174  O OG1 . THR A 1 64  ? 14.13215 -3.55740  17.25615  1.000 116.17836 ? -57  THR A OG1 1 
ATOM   175  C CG2 . THR A 1 64  ? 15.02505 -1.53631  18.22377  1.000 108.00881 ? -57  THR A CG2 1 
ATOM   176  N N   . PRO A 1 65  ? 15.12794 0.65218   15.78050  1.000 121.14175 ? -56  PRO A N   1 
ATOM   177  C CA  . PRO A 1 65  ? 15.98849 1.83926   15.75273  1.000 122.01331 ? -56  PRO A CA  1 
ATOM   178  C C   . PRO A 1 65  ? 17.08358 1.76414   16.80544  1.000 119.32383 ? -56  PRO A C   1 
ATOM   179  O O   . PRO A 1 65  ? 16.89215 1.23030   17.90027  1.000 124.10961 ? -56  PRO A O   1 
ATOM   180  C CB  . PRO A 1 65  ? 15.01499 2.98607   16.04400  1.000 121.71577 ? -56  PRO A CB  1 
ATOM   181  C CG  . PRO A 1 65  ? 13.69915 2.47869   15.56176  1.000 129.13358 ? -56  PRO A CG  1 
ATOM   182  C CD  . PRO A 1 65  ? 13.70108 1.00569   15.86687  1.000 125.98721 ? -56  PRO A CD  1 
ATOM   183  N N   . LEU A 1 66  ? 18.24874 2.31049   16.45769  1.000 110.26045 ? -55  LEU A N   1 
ATOM   184  C CA  . LEU A 1 66  ? 19.38426 2.30344   17.37152  1.000 109.02612 ? -55  LEU A CA  1 
ATOM   185  C C   . LEU A 1 66  ? 19.20318 3.25985   18.54082  1.000 111.24519 ? -55  LEU A C   1 
ATOM   186  O O   . LEU A 1 66  ? 20.08082 3.31366   19.40970  1.000 115.71192 ? -55  LEU A O   1 
ATOM   187  C CB  . LEU A 1 66  ? 20.66853 2.63678   16.61097  1.000 100.52255 ? -55  LEU A CB  1 
ATOM   188  C CG  . LEU A 1 66  ? 21.11972 1.55280   15.63047  1.000 96.41097  ? -55  LEU A CG  1 
ATOM   189  C CD1 . LEU A 1 66  ? 21.92915 2.14979   14.48946  1.000 100.87928 ? -55  LEU A CD1 1 
ATOM   190  C CD2 . LEU A 1 66  ? 21.91192 0.47644   16.35631  1.000 90.09529  ? -55  LEU A CD2 1 
ATOM   191  N N   . ARG A 1 67  ? 18.10244 4.01681   18.56580  1.000 108.85236 ? -54  ARG A N   1 
ATOM   192  C CA  . ARG A 1 67  ? 17.84281 4.95628   19.65226  1.000 115.52836 ? -54  ARG A CA  1 
ATOM   193  C C   . ARG A 1 67  ? 17.94579 4.27265   21.01079  1.000 109.31192 ? -54  ARG A C   1 
ATOM   194  O O   . ARG A 1 67  ? 18.56292 4.80177   21.94159  1.000 106.64399 ? -54  ARG A O   1 
ATOM   195  C CB  . ARG A 1 67  ? 16.46013 5.58516   19.46262  1.000 120.50457 ? -54  ARG A CB  1 
ATOM   196  C CG  . ARG A 1 67  ? 15.79048 6.06201   20.73993  1.000 127.85333 ? -54  ARG A CG  1 
ATOM   197  C CD  . ARG A 1 67  ? 15.19223 7.44661   20.55792  1.000 134.02735 ? -54  ARG A CD  1 
ATOM   198  N NE  . ARG A 1 67  ? 16.17414 8.50599   20.76262  1.000 143.37662 ? -54  ARG A NE  1 
ATOM   199  C CZ  . ARG A 1 67  ? 16.00562 9.76314   20.36727  1.000 146.68583 ? -54  ARG A CZ  1 
ATOM   200  N NH1 . ARG A 1 67  ? 14.89460 10.11662  19.73523  1.000 146.74593 ? -54  ARG A NH1 1 
ATOM   201  N NH2 . ARG A 1 67  ? 16.95001 10.66490  20.59614  1.000 146.92378 ? -54  ARG A NH2 1 
ATOM   202  N N   . ARG A 1 68  ? 17.33890 3.09018   21.13893  1.000 103.59826 ? -53  ARG A N   1 
ATOM   203  C CA  . ARG A 1 68  ? 17.42316 2.33308   22.38414  1.000 104.31674 ? -53  ARG A CA  1 
ATOM   204  C C   . ARG A 1 68  ? 18.87101 2.01027   22.73643  1.000 114.36880 ? -53  ARG A C   1 
ATOM   205  O O   . ARG A 1 68  ? 19.29983 2.19485   23.88141  1.000 119.28466 ? -53  ARG A O   1 
ATOM   206  C CB  . ARG A 1 68  ? 16.59230 1.05486   22.27088  1.000 107.45717 ? -53  ARG A CB  1 
ATOM   207  C CG  . ARG A 1 68  ? 15.09868 1.31085   22.15784  1.000 116.37288 ? -53  ARG A CG  1 
ATOM   208  C CD  . ARG A 1 68  ? 14.54492 1.92957   23.43092  1.000 124.26584 ? -53  ARG A CD  1 
ATOM   209  N NE  . ARG A 1 68  ? 13.26793 2.60165   23.20278  1.000 129.70267 ? -53  ARG A NE  1 
ATOM   210  C CZ  . ARG A 1 68  ? 12.07841 2.03398   23.37615  1.000 130.35165 ? -53  ARG A CZ  1 
ATOM   211  N NH1 . ARG A 1 68  ? 11.99219 0.77439   23.78356  1.000 125.17038 ? -53  ARG A NH1 1 
ATOM   212  N NH2 . ARG A 1 68  ? 10.97242 2.72735   23.14297  1.000 132.87041 ? -53  ARG A NH2 1 
ATOM   213  N N   . LEU A 1 69  ? 19.64033 1.52660   21.75722  1.000 110.72102 ? -52  LEU A N   1 
ATOM   214  C CA  . LEU A 1 69  ? 21.02316 1.12987   22.01105  1.000 108.93345 ? -52  LEU A CA  1 
ATOM   215  C C   . LEU A 1 69  ? 21.86099 2.32338   22.45104  1.000 107.14841 ? -52  LEU A C   1 
ATOM   216  O O   . LEU A 1 69  ? 22.61284 2.24611   23.43107  1.000 109.94716 ? -52  LEU A O   1 
ATOM   217  C CB  . LEU A 1 69  ? 21.61381 0.48874   20.75170  1.000 105.69479 ? -52  LEU A CB  1 
ATOM   218  C CG  . LEU A 1 69  ? 22.94633 -0.26387  20.81581  1.000 96.82507  ? -52  LEU A CG  1 
ATOM   219  C CD1 . LEU A 1 69  ? 23.00205 -1.29375  19.70332  1.000 92.37922  ? -52  LEU A CD1 1 
ATOM   220  C CD2 . LEU A 1 69  ? 24.13650 0.67899   20.71009  1.000 96.32819  ? -52  LEU A CD2 1 
ATOM   221  N N   . MET A 1 70  ? 21.76268 3.43053   21.71421  1.000 111.64291 ? -51  MET A N   1 
ATOM   222  C CA  . MET A 1 70  ? 22.53934 4.61911   22.04514  1.000 116.67950 ? -51  MET A CA  1 
ATOM   223  C C   . MET A 1 70  ? 22.13437 5.18128   23.40274  1.000 120.17296 ? -51  MET A C   1 
ATOM   224  O O   . MET A 1 70  ? 22.99210 5.60025   24.19057  1.000 120.84864 ? -51  MET A O   1 
ATOM   225  C CB  . MET A 1 70  ? 22.36958 5.65934   20.93867  1.000 122.34567 ? -51  MET A CB  1 
ATOM   226  C CG  . MET A 1 70  ? 22.82607 5.15611   19.57332  1.000 123.60955 ? -51  MET A CG  1 
ATOM   227  S SD  . MET A 1 70  ? 21.98269 5.93617   18.18347  1.000 132.85901 ? -51  MET A SD  1 
ATOM   228  C CE  . MET A 1 70  ? 22.77990 7.53752   18.13982  1.000 135.62778 ? -51  MET A CE  1 
ATOM   229  N N   . GLU A 1 71  ? 20.82935 5.19830   23.69286  1.000 120.75615 ? -50  GLU A N   1 
ATOM   230  C CA  . GLU A 1 71  ? 20.36108 5.63872   25.00320  1.000 121.33484 ? -50  GLU A CA  1 
ATOM   231  C C   . GLU A 1 71  ? 20.93945 4.76728   26.11183  1.000 106.65582 ? -50  GLU A C   1 
ATOM   232  O O   . GLU A 1 71  ? 21.37711 5.27786   27.15044  1.000 103.29481 ? -50  GLU A O   1 
ATOM   233  C CB  . GLU A 1 71  ? 18.82944 5.63484   25.04028  1.000 139.44935 ? -50  GLU A CB  1 
ATOM   234  C CG  . GLU A 1 71  ? 18.20769 4.84516   26.18450  1.000 149.42725 ? -50  GLU A CG  1 
ATOM   235  C CD  . GLU A 1 71  ? 17.02521 4.00855   25.74011  1.000 156.77394 ? -50  GLU A CD  1 
ATOM   236  O OE1 . GLU A 1 71  ? 15.95392 4.58951   25.46481  1.000 161.21672 ? -50  GLU A OE1 1 
ATOM   237  O OE2 . GLU A 1 71  ? 17.16690 2.76888   25.67011  1.000 154.06746 ? -50  GLU A OE2 1 
ATOM   238  N N   . ALA A 1 72  ? 20.96314 3.44759   25.90399  1.000 95.30357  ? -49  ALA A N   1 
ATOM   239  C CA  . ALA A 1 72  ? 21.46798 2.55200   26.93835  1.000 98.50297  ? -49  ALA A CA  1 
ATOM   240  C C   . ALA A 1 72  ? 22.96599 2.73667   27.14099  1.000 105.70030 ? -49  ALA A C   1 
ATOM   241  O O   . ALA A 1 72  ? 23.45456 2.69916   28.27718  1.000 106.52249 ? -49  ALA A O   1 
ATOM   242  C CB  . ALA A 1 72  ? 21.14720 1.10143   26.57998  1.000 91.99242  ? -49  ALA A CB  1 
ATOM   243  N N   . PHE A 1 73  ? 23.71146 2.94227   26.05221  1.000 111.67734 ? -48  PHE A N   1 
ATOM   244  C CA  . PHE A 1 73  ? 25.14883 3.15339   26.18825  1.000 118.10972 ? -48  PHE A CA  1 
ATOM   245  C C   . PHE A 1 73  ? 25.44614 4.47041   26.89042  1.000 118.46540 ? -48  PHE A C   1 
ATOM   246  O O   . PHE A 1 73  ? 26.36741 4.54788   27.71200  1.000 123.18978 ? -48  PHE A O   1 
ATOM   247  C CB  . PHE A 1 73  ? 25.83574 3.11935   24.82570  1.000 123.15499 ? -48  PHE A CB  1 
ATOM   248  C CG  . PHE A 1 73  ? 27.33154 3.23135   24.91038  1.000 131.07588 ? -48  PHE A CG  1 
ATOM   249  C CD1 . PHE A 1 73  ? 28.07941 2.23782   25.52051  1.000 130.10386 ? -48  PHE A CD1 1 
ATOM   250  C CD2 . PHE A 1 73  ? 27.98684 4.34268   24.40975  1.000 131.79590 ? -48  PHE A CD2 1 
ATOM   251  C CE1 . PHE A 1 73  ? 29.45383 2.34009   25.60808  1.000 127.37407 ? -48  PHE A CE1 1 
ATOM   252  C CE2 . PHE A 1 73  ? 29.35966 4.45097   24.49972  1.000 132.34134 ? -48  PHE A CE2 1 
ATOM   253  C CZ  . PHE A 1 73  ? 30.09413 3.44814   25.09573  1.000 130.69217 ? -48  PHE A CZ  1 
ATOM   254  N N   . ALA A 1 74  ? 24.68600 5.52028   26.56864  1.000 118.87034 ? -47  ALA A N   1 
ATOM   255  C CA  . ALA A 1 74  ? 24.82656 6.78180   27.28703  1.000 109.85171 ? -47  ALA A CA  1 
ATOM   256  C C   . ALA A 1 74  ? 24.52466 6.60971   28.76970  1.000 110.70412 ? -47  ALA A C   1 
ATOM   257  O O   . ALA A 1 74  ? 25.26031 7.11792   29.62399  1.000 111.58380 ? -47  ALA A O   1 
ATOM   258  C CB  . ALA A 1 74  ? 23.90962 7.83378   26.67086  1.000 102.93223 ? -47  ALA A CB  1 
ATOM   259  N N   . LYS A 1 75  ? 23.44741 5.88940   29.09305  1.000 122.04376 ? -46  LYS A N   1 
ATOM   260  C CA  . LYS A 1 75  ? 23.10581 5.64269   30.49038  1.000 128.56979 ? -46  LYS A CA  1 
ATOM   261  C C   . LYS A 1 75  ? 24.22602 4.89831   31.20665  1.000 124.54271 ? -46  LYS A C   1 
ATOM   262  O O   . LYS A 1 75  ? 24.54730 5.20449   32.36131  1.000 123.06379 ? -46  LYS A O   1 
ATOM   263  C CB  . LYS A 1 75  ? 21.79264 4.86323   30.57687  1.000 133.45437 ? -46  LYS A CB  1 
ATOM   264  C CG  . LYS A 1 75  ? 21.58323 4.12566   31.89028  1.000 139.16861 ? -46  LYS A CG  1 
ATOM   265  C CD  . LYS A 1 75  ? 20.43444 4.72336   32.68400  1.000 145.49562 ? -46  LYS A CD  1 
ATOM   266  C CE  . LYS A 1 75  ? 20.25997 4.01362   34.01696  1.000 150.07319 ? -46  LYS A CE  1 
ATOM   267  N NZ  . LYS A 1 75  ? 19.20649 4.64887   34.85607  1.000 156.69586 ? -46  LYS A NZ  1 
ATOM   268  N N   . ARG A 1 76  ? 24.83497 3.91932   30.53214  1.000 124.04604 ? -45  ARG A N   1 
ATOM   269  C CA  . ARG A 1 76  ? 25.90210 3.13692   31.14886  1.000 129.02517 ? -45  ARG A CA  1 
ATOM   270  C C   . ARG A 1 76  ? 27.09753 4.00915   31.51602  1.000 127.67614 ? -45  ARG A C   1 
ATOM   271  O O   . ARG A 1 76  ? 27.72136 3.80838   32.56494  1.000 123.12926 ? -45  ARG A O   1 
ATOM   272  C CB  . ARG A 1 76  ? 26.32957 2.01379   30.20493  1.000 126.81560 ? -45  ARG A CB  1 
ATOM   273  C CG  . ARG A 1 76  ? 27.59177 1.28567   30.62678  1.000 124.89813 ? -45  ARG A CG  1 
ATOM   274  C CD  . ARG A 1 76  ? 27.98304 0.24728   29.59488  1.000 129.08505 ? -45  ARG A CD  1 
ATOM   275  N NE  . ARG A 1 76  ? 29.40524 -0.07881  29.64941  1.000 133.93553 ? -45  ARG A NE  1 
ATOM   276  C CZ  . ARG A 1 76  ? 29.90583 -1.14447  30.26613  1.000 134.03832 ? -45  ARG A CZ  1 
ATOM   277  N NH1 . ARG A 1 76  ? 29.09909 -1.99651  30.88465  1.000 131.35783 ? -45  ARG A NH1 1 
ATOM   278  N NH2 . ARG A 1 76  ? 31.21467 -1.35990  30.26167  1.000 138.28930 ? -45  ARG A NH2 1 
ATOM   279  N N   . GLN A 1 77  ? 27.42730 4.98860   30.67275  1.000 127.20740 ? -44  GLN A N   1 
ATOM   280  C CA  . GLN A 1 77  ? 28.58402 5.85064   30.88321  1.000 129.33030 ? -44  GLN A CA  1 
ATOM   281  C C   . GLN A 1 77  ? 28.21145 7.17467   31.54415  1.000 142.51478 ? -44  GLN A C   1 
ATOM   282  O O   . GLN A 1 77  ? 28.87303 8.19244   31.31201  1.000 141.88244 ? -44  GLN A O   1 
ATOM   283  C CB  . GLN A 1 77  ? 29.30660 6.09845   29.55981  1.000 130.15913 ? -44  GLN A CB  1 
ATOM   284  C CG  . GLN A 1 77  ? 29.59425 4.83073   28.77463  1.000 131.69998 ? -44  GLN A CG  1 
ATOM   285  C CD  . GLN A 1 77  ? 30.86850 4.92480   27.96250  1.000 132.89941 ? -44  GLN A CD  1 
ATOM   286  O OE1 . GLN A 1 77  ? 31.14992 5.95100   27.34290  1.000 133.57235 ? -44  GLN A OE1 1 
ATOM   287  N NE2 . GLN A 1 77  ? 31.64951 3.85046   27.96217  1.000 132.62053 ? -44  GLN A NE2 1 
ATOM   288  N N   . GLY A 1 78  ? 27.15817 7.18115   32.36015  1.000 147.64927 ? -43  GLY A N   1 
ATOM   289  C CA  . GLY A 1 78  ? 26.78108 8.34521   33.14176  1.000 145.09505 ? -43  GLY A CA  1 
ATOM   290  C C   . GLY A 1 78  ? 26.25532 9.52994   32.35449  1.000 146.99389 ? -43  GLY A C   1 
ATOM   291  O O   . GLY A 1 78  ? 25.37464 10.25037  32.83404  1.000 148.45633 ? -43  GLY A O   1 
ATOM   292  N N   . LYS A 1 79  ? 26.77804 9.74715   31.15055  1.000 148.37590 ? -42  LYS A N   1 
ATOM   293  C CA  . LYS A 1 79  ? 26.36212 10.87168  30.32236  1.000 151.63155 ? -42  LYS A CA  1 
ATOM   294  C C   . LYS A 1 79  ? 25.00054 10.57129  29.69785  1.000 155.30118 ? -42  LYS A C   1 
ATOM   295  O O   . LYS A 1 79  ? 24.29394 9.64549   30.10445  1.000 158.85800 ? -42  LYS A O   1 
ATOM   296  C CB  . LYS A 1 79  ? 27.42469 11.17591  29.26992  1.000 147.57239 ? -42  LYS A CB  1 
ATOM   297  C CG  . LYS A 1 79  ? 28.79460 11.46795  29.85369  1.000 143.70219 ? -42  LYS A CG  1 
ATOM   298  C CD  . LYS A 1 79  ? 29.77825 11.90760  28.78327  1.000 145.27846 ? -42  LYS A CD  1 
ATOM   299  C CE  . LYS A 1 79  ? 31.07036 12.42049  29.40165  1.000 150.33002 ? -42  LYS A CE  1 
ATOM   300  N NZ  . LYS A 1 79  ? 32.13038 12.64524  28.37943  1.000 152.12749 ? -42  LYS A NZ  1 
ATOM   301  N N   . GLU A 1 80  ? 24.60993 11.35982  28.69897  1.000 158.44237 ? -41  GLU A N   1 
ATOM   302  C CA  . GLU A 1 80  ? 23.36798 11.12948  27.97806  1.000 165.60397 ? -41  GLU A CA  1 
ATOM   303  C C   . GLU A 1 80  ? 23.62074 11.23249  26.47955  1.000 160.67046 ? -41  GLU A C   1 
ATOM   304  O O   . GLU A 1 80  ? 24.64094 11.76442  26.03501  1.000 160.07515 ? -41  GLU A O   1 
ATOM   305  C CB  . GLU A 1 80  ? 22.26826 12.10700  28.41532  1.000 174.53072 ? -41  GLU A CB  1 
ATOM   306  C CG  . GLU A 1 80  ? 20.97629 11.41518  28.82938  1.000 182.18270 ? -41  GLU A CG  1 
ATOM   307  C CD  . GLU A 1 80  ? 20.32472 12.06143  30.03509  1.000 191.25295 ? -41  GLU A CD  1 
ATOM   308  O OE1 . GLU A 1 80  ? 20.80586 13.12837  30.47079  1.000 194.54548 ? -41  GLU A OE1 1 
ATOM   309  O OE2 . GLU A 1 80  ? 19.33250 11.50038  30.54691  1.000 191.73959 ? -41  GLU A OE2 1 
ATOM   310  N N   . MET A 1 81  ? 22.66906 10.69870  25.70574  1.000 156.17254 ? -40  MET A N   1 
ATOM   311  C CA  . MET A 1 81  ? 22.90047 10.43544  24.28666  1.000 151.13764 ? -40  MET A CA  1 
ATOM   312  C C   . MET A 1 81  ? 23.23696 11.70185  23.51020  1.000 148.74491 ? -40  MET A C   1 
ATOM   313  O O   . MET A 1 81  ? 23.93923 11.63673  22.49382  1.000 148.99822 ? -40  MET A O   1 
ATOM   314  C CB  . MET A 1 81  ? 21.67805 9.75241   23.67305  1.000 150.27155 ? -40  MET A CB  1 
ATOM   315  C CG  . MET A 1 81  ? 21.96565 9.05151   22.35622  1.000 147.75940 ? -40  MET A CG  1 
ATOM   316  S SD  . MET A 1 81  ? 20.50550 8.84463   21.32081  1.000 147.58759 ? -40  MET A SD  1 
ATOM   317  C CE  . MET A 1 81  ? 19.33939 8.16162   22.49406  1.000 149.61939 ? -40  MET A CE  1 
ATOM   318  N N   . ASP A 1 82  ? 22.74279 12.85652  23.96253  1.000 145.11243 ? -39  ASP A N   1 
ATOM   319  C CA  . ASP A 1 82  ? 23.05093 14.10819  23.27959  1.000 146.02603 ? -39  ASP A CA  1 
ATOM   320  C C   . ASP A 1 82  ? 24.54394 14.40716  23.29647  1.000 148.09927 ? -39  ASP A C   1 
ATOM   321  O O   . ASP A 1 82  ? 25.05632 15.05675  22.37809  1.000 139.98262 ? -39  ASP A O   1 
ATOM   322  C CB  . ASP A 1 82  ? 22.27518 15.25861  23.92286  1.000 149.67787 ? -39  ASP A CB  1 
ATOM   323  C CG  . ASP A 1 82  ? 22.52844 15.36833  25.41564  1.000 154.15418 ? -39  ASP A CG  1 
ATOM   324  O OD1 . ASP A 1 82  ? 22.87097 14.34050  26.03815  1.000 154.21000 ? -39  ASP A OD1 1 
ATOM   325  O OD2 . ASP A 1 82  ? 22.38521 16.48076  25.96604  1.000 156.95422 ? -39  ASP A OD2 1 
ATOM   326  N N   . SER A 1 83  ? 25.25518 13.94276  24.32040  1.000 157.80158 ? -38  SER A N   1 
ATOM   327  C CA  . SER A 1 83  ? 26.66428 14.25757  24.50598  1.000 163.75893 ? -38  SER A CA  1 
ATOM   328  C C   . SER A 1 83  ? 27.59405 13.27823  23.79776  1.000 155.76712 ? -38  SER A C   1 
ATOM   329  O O   . SER A 1 83  ? 28.81109 13.34689  24.00041  1.000 158.95442 ? -38  SER A O   1 
ATOM   330  C CB  . SER A 1 83  ? 27.00140 14.30391  25.99932  1.000 170.35355 ? -38  SER A CB  1 
ATOM   331  O OG  . SER A 1 83  ? 26.74420 13.05708  26.62133  1.000 171.28060 ? -38  SER A OG  1 
ATOM   332  N N   . LEU A 1 84  ? 27.06134 12.37602  22.97376  1.000 141.57729 ? -37  LEU A N   1 
ATOM   333  C CA  . LEU A 1 84  ? 27.88040 11.37574  22.30613  1.000 132.84625 ? -37  LEU A CA  1 
ATOM   334  C C   . LEU A 1 84  ? 27.62952 11.37068  20.80481  1.000 135.96334 ? -37  LEU A C   1 
ATOM   335  O O   . LEU A 1 84  ? 26.56700 11.77396  20.32409  1.000 135.30939 ? -37  LEU A O   1 
ATOM   336  C CB  . LEU A 1 84  ? 27.62906 9.96816   22.87005  1.000 121.71805 ? -37  LEU A CB  1 
ATOM   337  C CG  . LEU A 1 84  ? 28.05107 9.71076   24.31795  1.000 118.79765 ? -37  LEU A CG  1 
ATOM   338  C CD1 . LEU A 1 84  ? 27.81884 8.25457   24.68761  1.000 111.80584 ? -37  LEU A CD1 1 
ATOM   339  C CD2 . LEU A 1 84  ? 29.50810 10.09209  24.52973  1.000 115.47803 ? -37  LEU A CD2 1 
ATOM   340  N N   . ARG A 1 85  ? 28.64347 10.90784  20.07818  1.000 144.66223 ? -36  ARG A N   1 
ATOM   341  C CA  . ARG A 1 85  ? 28.65467 10.79948  18.62398  1.000 149.27527 ? -36  ARG A CA  1 
ATOM   342  C C   . ARG A 1 85  ? 28.93759 9.34409   18.27664  1.000 139.80237 ? -36  ARG A C   1 
ATOM   343  O O   . ARG A 1 85  ? 30.03258 8.83805   18.55201  1.000 137.56819 ? -36  ARG A O   1 
ATOM   344  C CB  . ARG A 1 85  ? 29.71530 11.71776  18.01847  1.000 157.29679 ? -36  ARG A CB  1 
ATOM   345  C CG  . ARG A 1 85  ? 29.21056 12.69318  16.97303  1.000 167.63766 ? -36  ARG A CG  1 
ATOM   346  C CD  . ARG A 1 85  ? 30.38346 13.28154  16.20175  1.000 175.55983 ? -36  ARG A CD  1 
ATOM   347  N NE  . ARG A 1 85  ? 30.05209 14.54189  15.54542  1.000 182.65904 ? -36  ARG A NE  1 
ATOM   348  C CZ  . ARG A 1 85  ? 30.91277 15.25472  14.82589  1.000 186.85913 ? -36  ARG A CZ  1 
ATOM   349  N NH1 . ARG A 1 85  ? 32.15833 14.82920  14.66659  1.000 186.29914 ? -36  ARG A NH1 1 
ATOM   350  N NH2 . ARG A 1 85  ? 30.52932 16.39324  14.26463  1.000 191.31737 ? -36  ARG A NH2 1 
ATOM   351  N N   . PHE A 1 86  ? 27.95823 8.67481   17.67679  1.000 131.89379 ? -35  PHE A N   1 
ATOM   352  C CA  . PHE A 1 86  ? 28.07510 7.27014   17.30991  1.000 121.69091 ? -35  PHE A CA  1 
ATOM   353  C C   . PHE A 1 86  ? 28.40001 7.17326   15.82414  1.000 118.26013 ? -35  PHE A C   1 
ATOM   354  O O   . PHE A 1 86  ? 27.63856 7.66576   14.98395  1.000 117.55175 ? -35  PHE A O   1 
ATOM   355  C CB  . PHE A 1 86  ? 26.78521 6.52071   17.64026  1.000 120.25708 ? -35  PHE A CB  1 
ATOM   356  C CG  . PHE A 1 86  ? 26.55403 6.34074   19.11427  1.000 112.25846 ? -35  PHE A CG  1 
ATOM   357  C CD1 . PHE A 1 86  ? 25.80273 7.26181   19.82594  1.000 105.01219 ? -35  PHE A CD1 1 
ATOM   358  C CD2 . PHE A 1 86  ? 27.09460 5.25900   19.78974  1.000 106.87760 ? -35  PHE A CD2 1 
ATOM   359  C CE1 . PHE A 1 86  ? 25.58798 7.10560   21.18107  1.000 107.49442 ? -35  PHE A CE1 1 
ATOM   360  C CE2 . PHE A 1 86  ? 26.88404 5.09666   21.14656  1.000 110.33229 ? -35  PHE A CE2 1 
ATOM   361  C CZ  . PHE A 1 86  ? 26.12867 6.02192   21.84293  1.000 115.04242 ? -35  PHE A CZ  1 
ATOM   362  N N   . LEU A 1 87  ? 29.53210 6.55091   15.50670  1.000 115.16763 ? -34  LEU A N   1 
ATOM   363  C CA  . LEU A 1 87  ? 29.98961 6.37905   14.13785  1.000 114.10821 ? -34  LEU A CA  1 
ATOM   364  C C   . LEU A 1 87  ? 30.03381 4.89756   13.79120  1.000 117.24021 ? -34  LEU A C   1 
ATOM   365  O O   . LEU A 1 87  ? 30.38271 4.06114   14.63281  1.000 110.61039 ? -34  LEU A O   1 
ATOM   366  C CB  . LEU A 1 87  ? 31.37605 7.00456   13.94405  1.000 109.13546 ? -34  LEU A CB  1 
ATOM   367  C CG  . LEU A 1 87  ? 31.59248 8.36500   14.61426  1.000 107.01659 ? -34  LEU A CG  1 
ATOM   368  C CD1 . LEU A 1 87  ? 33.03170 8.82877   14.45045  1.000 108.34629 ? -34  LEU A CD1 1 
ATOM   369  C CD2 . LEU A 1 87  ? 30.62657 9.40473   14.07780  1.000 108.42765 ? -34  LEU A CD2 1 
ATOM   370  N N   . TYR A 1 88  ? 29.67802 4.58208   12.54715  1.000 127.46666 ? -33  TYR A N   1 
ATOM   371  C CA  . TYR A 1 88  ? 29.79561 3.23206   12.00733  1.000 131.65984 ? -33  TYR A CA  1 
ATOM   372  C C   . TYR A 1 88  ? 30.34883 3.33703   10.59641  1.000 139.65353 ? -33  TYR A C   1 
ATOM   373  O O   . TYR A 1 88  ? 29.75645 4.01644   9.75293   1.000 143.28246 ? -33  TYR A O   1 
ATOM   374  C CB  . TYR A 1 88  ? 28.44738 2.50590   11.99918  1.000 133.38278 ? -33  TYR A CB  1 
ATOM   375  C CG  . TYR A 1 88  ? 28.49392 1.15912   11.30970  1.000 129.68729 ? -33  TYR A CG  1 
ATOM   376  C CD1 . TYR A 1 88  ? 29.05448 0.05585   11.93968  1.000 126.08440 ? -33  TYR A CD1 1 
ATOM   377  C CD2 . TYR A 1 88  ? 27.99495 0.99492   10.02324  1.000 124.78862 ? -33  TYR A CD2 1 
ATOM   378  C CE1 . TYR A 1 88  ? 29.10427 -1.17610  11.31515  1.000 123.94654 ? -33  TYR A CE1 1 
ATOM   379  C CE2 . TYR A 1 88  ? 28.03976 -0.23306  9.39036   1.000 122.22465 ? -33  TYR A CE2 1 
ATOM   380  C CZ  . TYR A 1 88  ? 28.59743 -1.31508  10.04062  1.000 121.42607 ? -33  TYR A CZ  1 
ATOM   381  O OH  . TYR A 1 88  ? 28.64812 -2.54142  9.41673   1.000 108.19684 ? -33  TYR A OH  1 
ATOM   382  N N   . ASP A 1 89  ? 31.48873 2.68981   10.35086  1.000 144.94716 ? -32  ASP A N   1 
ATOM   383  C CA  . ASP A 1 89  ? 32.22056 2.69671   9.08567   1.000 151.63573 ? -32  ASP A CA  1 
ATOM   384  C C   . ASP A 1 89  ? 32.86049 4.04773   8.78620   1.000 146.62148 ? -32  ASP A C   1 
ATOM   385  O O   . ASP A 1 89  ? 33.53036 4.18441   7.75523   1.000 153.47271 ? -32  ASP A O   1 
ATOM   386  C CB  . ASP A 1 89  ? 31.34089 2.27913   7.89552   1.000 158.62561 ? -32  ASP A CB  1 
ATOM   387  C CG  . ASP A 1 89  ? 32.13547 1.63420   6.77708   1.000 164.14422 ? -32  ASP A CG  1 
ATOM   388  O OD1 . ASP A 1 89  ? 32.99709 0.77969   7.07366   1.000 164.59095 ? -32  ASP A OD1 1 
ATOM   389  O OD2 . ASP A 1 89  ? 31.89111 1.97459   5.60048   1.000 166.13141 ? -32  ASP A OD2 1 
ATOM   390  N N   . GLY A 1 90  ? 32.68272 5.04643   9.64567   1.000 136.21166 ? -31  GLY A N   1 
ATOM   391  C CA  . GLY A 1 90  ? 33.21119 6.38080   9.42531   1.000 126.39983 ? -31  GLY A CA  1 
ATOM   392  C C   . GLY A 1 90  ? 32.16613 7.46873   9.30383   1.000 131.70457 ? -31  GLY A C   1 
ATOM   393  O O   . GLY A 1 90  ? 32.52423 8.65474   9.35938   1.000 130.60028 ? -31  GLY A O   1 
ATOM   394  N N   . ILE A 1 91  ? 30.88951 7.12725   9.14263   1.000 141.04190 ? -30  ILE A N   1 
ATOM   395  C CA  . ILE A 1 91  ? 29.81856 8.10589   8.98467   1.000 149.34602 ? -30  ILE A CA  1 
ATOM   396  C C   . ILE A 1 91  ? 29.07018 8.22809   10.30463  1.000 150.91755 ? -30  ILE A C   1 
ATOM   397  O O   . ILE A 1 91  ? 28.88516 7.23650   11.02261  1.000 146.99434 ? -30  ILE A O   1 
ATOM   398  C CB  . ILE A 1 91  ? 28.87052 7.71289   7.83209   1.000 150.42033 ? -30  ILE A CB  1 
ATOM   399  C CG1 . ILE A 1 91  ? 27.78213 8.77100   7.63477   1.000 155.35554 ? -30  ILE A CG1 1 
ATOM   400  C CG2 . ILE A 1 91  ? 28.25132 6.34416   8.07670   1.000 148.82352 ? -30  ILE A CG2 1 
ATOM   401  C CD1 . ILE A 1 91  ? 26.84888 8.48021   6.47986   1.000 155.07907 ? -30  ILE A CD1 1 
ATOM   402  N N   . ARG A 1 92  ? 28.65584 9.44752   10.64115  1.000 157.98484 ? -29  ARG A N   1 
ATOM   403  C CA  . ARG A 1 92  ? 27.83910 9.65736   11.82765  1.000 162.65767 ? -29  ARG A CA  1 
ATOM   404  C C   . ARG A 1 92  ? 26.41456 9.19757   11.55329  1.000 158.57331 ? -29  ARG A C   1 
ATOM   405  O O   . ARG A 1 92  ? 25.79434 9.61779   10.57131  1.000 162.96288 ? -29  ARG A O   1 
ATOM   406  C CB  . ARG A 1 92  ? 27.85615 11.12687  12.24847  1.000 172.33405 ? -29  ARG A CB  1 
ATOM   407  C CG  . ARG A 1 92  ? 26.90239 11.44340  13.39313  1.000 177.58887 ? -29  ARG A CG  1 
ATOM   408  C CD  . ARG A 1 92  ? 27.10959 12.84991  13.93512  1.000 183.98413 ? -29  ARG A CD  1 
ATOM   409  N NE  . ARG A 1 92  ? 26.87154 13.88212  12.93116  1.000 189.13877 ? -29  ARG A NE  1 
ATOM   410  C CZ  . ARG A 1 92  ? 27.03744 15.18286  13.14860  1.000 195.17853 ? -29  ARG A CZ  1 
ATOM   411  N NH1 . ARG A 1 92  ? 27.44130 15.61145  14.33695  1.000 197.21464 ? -29  ARG A NH1 1 
ATOM   412  N NH2 . ARG A 1 92  ? 26.79850 16.05605  12.18029  1.000 198.55757 ? -29  ARG A NH2 1 
ATOM   413  N N   . ILE A 1 93  ? 25.89864 8.33795   12.42117  1.000 148.07452 ? -28  ILE A N   1 
ATOM   414  C CA  . ILE A 1 93  ? 24.57883 7.75064   12.24155  1.000 141.92742 ? -28  ILE A CA  1 
ATOM   415  C C   . ILE A 1 93  ? 23.58590 8.47046   13.13910  1.000 145.00052 ? -28  ILE A C   1 
ATOM   416  O O   . ILE A 1 93  ? 23.93571 8.99787   14.20158  1.000 145.93851 ? -28  ILE A O   1 
ATOM   417  C CB  . ILE A 1 93  ? 24.59962 6.23562   12.53445  1.000 137.69923 ? -28  ILE A CB  1 
ATOM   418  C CG1 . ILE A 1 93  ? 25.11938 5.97320   13.94989  1.000 134.93056 ? -28  ILE A CG1 1 
ATOM   419  C CG2 . ILE A 1 93  ? 25.44655 5.50799   11.50251  1.000 134.27230 ? -28  ILE A CG2 1 
ATOM   420  C CD1 . ILE A 1 93  ? 25.46336 4.52455   14.22063  1.000 129.40979 ? -28  ILE A CD1 1 
ATOM   421  N N   . GLN A 1 94  ? 22.32816 8.49415   12.70233  1.000 150.72277 ? -27  GLN A N   1 
ATOM   422  C CA  . GLN A 1 94  ? 21.24669 9.07899   13.48398  1.000 155.39054 ? -27  GLN A CA  1 
ATOM   423  C C   . GLN A 1 94  ? 20.87333 8.16694   14.64485  1.000 151.77370 ? -27  GLN A C   1 
ATOM   424  O O   . GLN A 1 94  ? 21.66278 7.30704   15.04861  1.000 157.98317 ? -27  GLN A O   1 
ATOM   425  C CB  . GLN A 1 94  ? 20.03081 9.33477   12.59316  1.000 159.92171 ? -27  GLN A CB  1 
ATOM   426  C CG  . GLN A 1 94  ? 20.36719 10.02886  11.28536  1.000 163.64344 ? -27  GLN A CG  1 
ATOM   427  C CD  . GLN A 1 94  ? 19.39300 9.68645   10.17688  1.000 167.53319 ? -27  GLN A CD  1 
ATOM   428  O OE1 . GLN A 1 94  ? 18.31754 9.14080   10.42521  1.000 169.29484 ? -27  GLN A OE1 1 
ATOM   429  N NE2 . GLN A 1 94  ? 19.76871 10.00033  8.94249   1.000 167.14783 ? -27  GLN A NE2 1 
ATOM   430  N N   . ALA A 1 95  ? 19.66818 8.34156   15.18540  1.000 145.56034 ? -26  ALA A N   1 
ATOM   431  C CA  . ALA A 1 95  ? 19.15257 7.45089   16.21198  1.000 140.52325 ? -26  ALA A CA  1 
ATOM   432  C C   . ALA A 1 95  ? 17.92256 6.67176   15.77945  1.000 141.74278 ? -26  ALA A C   1 
ATOM   433  O O   . ALA A 1 95  ? 17.60790 5.65517   16.40776  1.000 131.87897 ? -26  ALA A O   1 
ATOM   434  C CB  . ALA A 1 95  ? 18.81521 8.23600   17.48965  1.000 141.05355 ? -26  ALA A CB  1 
ATOM   435  N N   . ASP A 1 96  ? 17.22814 7.10722   14.73172  1.000 147.01937 ? -25  ASP A N   1 
ATOM   436  C CA  . ASP A 1 96  ? 16.05371 6.41526   14.22410  1.000 150.97260 ? -25  ASP A CA  1 
ATOM   437  C C   . ASP A 1 96  ? 16.38806 5.45179   13.09329  1.000 146.74077 ? -25  ASP A C   1 
ATOM   438  O O   . ASP A 1 96  ? 15.47800 4.98988   12.39743  1.000 150.75212 ? -25  ASP A O   1 
ATOM   439  C CB  . ASP A 1 96  ? 15.00614 7.42896   13.75878  1.000 156.68759 ? -25  ASP A CB  1 
ATOM   440  C CG  . ASP A 1 96  ? 14.49990 8.30136   14.89061  1.000 161.97761 ? -25  ASP A CG  1 
ATOM   441  O OD1 . ASP A 1 96  ? 14.42493 7.80828   16.03632  1.000 162.51482 ? -25  ASP A OD1 1 
ATOM   442  O OD2 . ASP A 1 96  ? 14.17718 9.48024   14.63433  1.000 165.26179 ? -25  ASP A OD2 1 
ATOM   443  N N   . GLN A 1 97  ? 17.66589 5.14175   12.89506  1.000 140.60534 ? -24  GLN A N   1 
ATOM   444  C CA  . GLN A 1 97  ? 18.08108 4.18787   11.87866  1.000 132.70907 ? -24  GLN A CA  1 
ATOM   445  C C   . GLN A 1 97  ? 18.18779 2.79564   12.48507  1.000 128.21421 ? -24  GLN A C   1 
ATOM   446  O O   . GLN A 1 97  ? 18.63069 2.63171   13.62563  1.000 122.53196 ? -24  GLN A O   1 
ATOM   447  C CB  . GLN A 1 97  ? 19.41746 4.60023   11.25862  1.000 132.32896 ? -24  GLN A CB  1 
ATOM   448  C CG  . GLN A 1 97  ? 19.44014 6.02642   10.72945  1.000 133.63152 ? -24  GLN A CG  1 
ATOM   449  C CD  . GLN A 1 97  ? 20.71684 6.35310   9.97617   1.000 136.50635 ? -24  GLN A CD  1 
ATOM   450  O OE1 . GLN A 1 97  ? 20.69491 6.59233   8.76906   1.000 139.82010 ? -24  GLN A OE1 1 
ATOM   451  N NE2 . GLN A 1 97  ? 21.83785 6.35979   10.68575  1.000 131.13054 ? -24  GLN A NE2 1 
ATOM   452  N N   . THR A 1 98  ? 17.77650 1.79708   11.71337  1.000 127.24263 ? -23  THR A N   1 
ATOM   453  C CA  . THR A 1 98  ? 17.77228 0.39190   12.07904  1.000 126.95256 ? -23  THR A CA  1 
ATOM   454  C C   . THR A 1 98  ? 18.94946 -0.33535  11.43752  1.000 130.99103 ? -23  THR A C   1 
ATOM   455  O O   . THR A 1 98  ? 19.39846 0.03876   10.35003  1.000 128.32725 ? -23  THR A O   1 
ATOM   456  C CB  . THR A 1 98  ? 16.46312 -0.27209  11.64203  1.000 127.61589 ? -23  THR A CB  1 
ATOM   457  O OG1 . THR A 1 98  ? 16.42484 -0.35984  10.21295  1.000 129.87339 ? -23  THR A OG1 1 
ATOM   458  C CG2 . THR A 1 98  ? 15.27349 0.54585   12.12035  1.000 128.93557 ? -23  THR A CG2 1 
ATOM   459  N N   . PRO A 1 99  ? 19.47098 -1.36939  12.10575  1.000 129.31443 ? -22  PRO A N   1 
ATOM   460  C CA  . PRO A 1 99  ? 20.63001 -2.09932  11.56171  1.000 124.75806 ? -22  PRO A CA  1 
ATOM   461  C C   . PRO A 1 99  ? 20.45520 -2.58623  10.13488  1.000 125.70214 ? -22  PRO A C   1 
ATOM   462  O O   . PRO A 1 99  ? 21.43942 -2.64183  9.38576   1.000 121.27072 ? -22  PRO A O   1 
ATOM   463  C CB  . PRO A 1 99  ? 20.77715 -3.27508  12.53538  1.000 123.18066 ? -22  PRO A CB  1 
ATOM   464  C CG  . PRO A 1 99  ? 20.23916 -2.75816  13.81625  1.000 127.44436 ? -22  PRO A CG  1 
ATOM   465  C CD  . PRO A 1 99  ? 19.10876 -1.83692  13.45498  1.000 131.55159 ? -22  PRO A CD  1 
ATOM   466  N N   . GLU A 1 100 ? 19.23521 -2.94799  9.73366   1.000 124.76337 ? -21  GLU A N   1 
ATOM   467  C CA  . GLU A 1 100 ? 19.01408 -3.38206  8.35951   1.000 123.39472 ? -21  GLU A CA  1 
ATOM   468  C C   . GLU A 1 100 ? 19.22255 -2.24343  7.36862   1.000 124.25092 ? -21  GLU A C   1 
ATOM   469  O O   . GLU A 1 100 ? 19.55841 -2.49253  6.20519   1.000 123.31899 ? -21  GLU A O   1 
ATOM   470  C CB  . GLU A 1 100 ? 17.60945 -3.96830  8.21720   1.000 127.69770 ? -21  GLU A CB  1 
ATOM   471  C CG  . GLU A 1 100 ? 17.36902 -4.70044  6.90782   1.000 132.60267 ? -21  GLU A CG  1 
ATOM   472  C CD  . GLU A 1 100 ? 15.91113 -5.05871  6.70139   1.000 137.37398 ? -21  GLU A CD  1 
ATOM   473  O OE1 . GLU A 1 100 ? 15.03619 -4.29223  7.15783   1.000 140.22218 ? -21  GLU A OE1 1 
ATOM   474  O OE2 . GLU A 1 100 ? 15.64068 -6.11008  6.08453   1.000 136.85851 ? -21  GLU A OE2 1 
ATOM   475  N N   . ASP A 1 101 ? 19.03587 -0.99496  7.80721   1.000 126.06148 ? -20  ASP A N   1 
ATOM   476  C CA  . ASP A 1 101 ? 19.20229 0.14049   6.90488   1.000 129.51663 ? -20  ASP A CA  1 
ATOM   477  C C   . ASP A 1 101 ? 20.65510 0.30888   6.47669   1.000 139.75695 ? -20  ASP A C   1 
ATOM   478  O O   . ASP A 1 101 ? 20.93382 0.54549   5.29515   1.000 135.85740 ? -20  ASP A O   1 
ATOM   479  C CB  . ASP A 1 101 ? 18.69144 1.41945   7.56777   1.000 129.12599 ? -20  ASP A CB  1 
ATOM   480  C CG  . ASP A 1 101 ? 17.19004 1.41327   7.76632   1.000 132.87794 ? -20  ASP A CG  1 
ATOM   481  O OD1 . ASP A 1 101 ? 16.46328 1.06781   6.81109   1.000 133.92573 ? -20  ASP A OD1 1 
ATOM   482  O OD2 . ASP A 1 101 ? 16.73650 1.75685   8.87752   1.000 136.15473 ? -20  ASP A OD2 1 
ATOM   483  N N   . LEU A 1 102 ? 21.59514 0.19030   7.41601   1.000 150.99818 ? -19  LEU A N   1 
ATOM   484  C CA  . LEU A 1 102 ? 23.00303 0.43868   7.13581   1.000 158.60359 ? -19  LEU A CA  1 
ATOM   485  C C   . LEU A 1 102 ? 23.80959 -0.84970  7.00239   1.000 153.64948 ? -19  LEU A C   1 
ATOM   486  O O   . LEU A 1 102 ? 25.03951 -0.81791  7.12143   1.000 150.92346 ? -19  LEU A O   1 
ATOM   487  C CB  . LEU A 1 102 ? 23.61181 1.34796   8.20930   1.000 166.36546 ? -19  LEU A CB  1 
ATOM   488  C CG  . LEU A 1 102 ? 23.79116 0.88040   9.65768   1.000 170.89297 ? -19  LEU A CG  1 
ATOM   489  C CD1 . LEU A 1 102 ? 24.70213 1.84497   10.39174  1.000 173.24470 ? -19  LEU A CD1 1 
ATOM   490  C CD2 . LEU A 1 102 ? 22.46790 0.78241   10.38710  1.000 172.02756 ? -19  LEU A CD2 1 
ATOM   491  N N   . ASP A 1 103 ? 23.13766 -1.97443  6.74614   1.000 152.69130 ? -18  ASP A N   1 
ATOM   492  C CA  . ASP A 1 103 ? 23.78343 -3.21254  6.30273   1.000 152.10292 ? -18  ASP A CA  1 
ATOM   493  C C   . ASP A 1 103 ? 24.89968 -3.65938  7.24447   1.000 143.00739 ? -18  ASP A C   1 
ATOM   494  O O   . ASP A 1 103 ? 25.97819 -4.06768  6.80846   1.000 140.74827 ? -18  ASP A O   1 
ATOM   495  C CB  . ASP A 1 103 ? 24.31631 -3.06409  4.87576   1.000 157.00271 ? -18  ASP A CB  1 
ATOM   496  C CG  . ASP A 1 103 ? 23.20910 -2.93001  3.84846   1.000 164.88220 ? -18  ASP A CG  1 
ATOM   497  O OD1 . ASP A 1 103 ? 22.02840 -3.10574  4.21657   1.000 169.04431 ? -18  ASP A OD1 1 
ATOM   498  O OD2 . ASP A 1 103 ? 23.52056 -2.65061  2.67091   1.000 165.94783 ? -18  ASP A OD2 1 
ATOM   499  N N   . MET A 1 104 ? 24.64983 -3.58593  8.54771   1.000 133.82911 ? -17  MET A N   1 
ATOM   500  C CA  . MET A 1 104 ? 25.62148 -4.08021  9.51038   1.000 125.64444 ? -17  MET A CA  1 
ATOM   501  C C   . MET A 1 104 ? 25.24757 -5.48672  9.96273   1.000 119.82622 ? -17  MET A C   1 
ATOM   502  O O   . MET A 1 104 ? 24.07743 -5.87864  9.95182   1.000 113.90264 ? -17  MET A O   1 
ATOM   503  C CB  . MET A 1 104 ? 25.76293 -3.14246  10.71406  1.000 124.36964 ? -17  MET A CB  1 
ATOM   504  C CG  . MET A 1 104 ? 24.49369 -2.51993  11.26413  1.000 121.24919 ? -17  MET A CG  1 
ATOM   505  S SD  . MET A 1 104 ? 24.97081 -1.28030  12.49210  1.000 124.44719 ? -17  MET A SD  1 
ATOM   506  C CE  . MET A 1 104 ? 23.46199 -1.06397  13.42403  1.000 121.38916 ? -17  MET A CE  1 
ATOM   507  N N   . GLU A 1 105 ? 26.26566 -6.24238  10.35766  1.000 112.22887 ? -16  GLU A N   1 
ATOM   508  C CA  . GLU A 1 105 ? 26.15783 -7.66653  10.62364  1.000 105.83904 ? -16  GLU A CA  1 
ATOM   509  C C   . GLU A 1 105 ? 26.62050 -7.97821  12.03983  1.000 98.54581  ? -16  GLU A C   1 
ATOM   510  O O   . GLU A 1 105 ? 27.10216 -7.10995  12.77218  1.000 99.56221  ? -16  GLU A O   1 
ATOM   511  C CB  . GLU A 1 105 ? 26.97814 -8.46837  9.60641   1.000 105.19256 ? -16  GLU A CB  1 
ATOM   512  C CG  . GLU A 1 105 ? 28.36007 -7.88614  9.35327   1.000 114.54549 ? -16  GLU A CG  1 
ATOM   513  C CD  . GLU A 1 105 ? 29.08429 -8.56641  8.20749   1.000 119.59868 ? -16  GLU A CD  1 
ATOM   514  O OE1 . GLU A 1 105 ? 28.75880 -9.73327  7.90147   1.000 118.74138 ? -16  GLU A OE1 1 
ATOM   515  O OE2 . GLU A 1 105 ? 29.97645 -7.92977  7.60784   1.000 119.59833 ? -16  GLU A OE2 1 
ATOM   516  N N   . ASP A 1 106 ? 26.44798 -9.24288  12.41555  1.000 93.06061  ? -15  ASP A N   1 
ATOM   517  C CA  . ASP A 1 106 ? 26.71722 -9.67776  13.77840  1.000 93.54206  ? -15  ASP A CA  1 
ATOM   518  C C   . ASP A 1 106 ? 28.15377 -9.36488  14.18401  1.000 89.14678  ? -15  ASP A C   1 
ATOM   519  O O   . ASP A 1 106 ? 29.07934 -9.43555  13.37035  1.000 88.56146  ? -15  ASP A O   1 
ATOM   520  C CB  . ASP A 1 106 ? 26.44566 -11.17865 13.89983  1.000 77.28840  ? -15  ASP A CB  1 
ATOM   521  C CG  . ASP A 1 106 ? 26.68956 -11.70752 15.29593  1.000 86.84112  ? -15  ASP A CG  1 
ATOM   522  O OD1 . ASP A 1 106 ? 26.21375 -11.08059 16.26496  1.000 91.63121  ? -15  ASP A OD1 1 
ATOM   523  O OD2 . ASP A 1 106 ? 27.34990 -12.76020 15.42287  1.000 93.90967  ? -15  ASP A OD2 1 
ATOM   524  N N   . ASN A 1 107 ? 28.32606 -9.00629  15.45695  1.000 89.87495  ? -14  ASN A N   1 
ATOM   525  C CA  . ASN A 1 107 ? 29.61903 -8.68009  16.05731  1.000 82.06383  ? -14  ASN A CA  1 
ATOM   526  C C   . ASN A 1 107 ? 30.28633 -7.46522  15.41885  1.000 87.69056  ? -14  ASN A C   1 
ATOM   527  O O   . ASN A 1 107 ? 31.50752 -7.30924  15.51392  1.000 92.79500  ? -14  ASN A O   1 
ATOM   528  C CB  . ASN A 1 107 ? 30.57226 -9.87958  16.01666  1.000 83.18780  ? -14  ASN A CB  1 
ATOM   529  C CG  . ASN A 1 107 ? 30.37084 -10.82084 17.18335  1.000 84.10988  ? -14  ASN A CG  1 
ATOM   530  O OD1 . ASN A 1 107 ? 31.31758 -11.17377 17.88007  1.000 81.31428  ? -14  ASN A OD1 1 
ATOM   531  N ND2 . ASN A 1 107 ? 29.12949 -11.23814 17.39874  1.000 81.56710  ? -14  ASN A ND2 1 
ATOM   532  N N   . ASP A 1 108 ? 29.52384 -6.59058  14.76883  1.000 96.32331  ? -13  ASP A N   1 
ATOM   533  C CA  . ASP A 1 108 ? 30.11154 -5.34152  14.31156  1.000 98.20273  ? -13  ASP A CA  1 
ATOM   534  C C   . ASP A 1 108 ? 30.30168 -4.38694  15.48713  1.000 101.18437 ? -13  ASP A C   1 
ATOM   535  O O   . ASP A 1 108 ? 29.69904 -4.54166  16.55304  1.000 99.23902  ? -13  ASP A O   1 
ATOM   536  C CB  . ASP A 1 108 ? 29.24544 -4.68674  13.23407  1.000 99.23869  ? -13  ASP A CB  1 
ATOM   537  C CG  . ASP A 1 108 ? 29.42688 -5.32620  11.86991  1.000 109.32105 ? -13  ASP A CG  1 
ATOM   538  O OD1 . ASP A 1 108 ? 30.30532 -6.20342  11.73282  1.000 109.60200 ? -13  ASP A OD1 1 
ATOM   539  O OD2 . ASP A 1 108 ? 28.69050 -4.95043  10.93307  1.000 113.27567 ? -13  ASP A OD2 1 
ATOM   540  N N   . ILE A 1 109 ? 31.15651 -3.38814  15.28036  1.000 100.12912 ? -12  ILE A N   1 
ATOM   541  C CA  . ILE A 1 109 ? 31.54152 -2.44854  16.32570  1.000 101.85241 ? -12  ILE A CA  1 
ATOM   542  C C   . ILE A 1 109 ? 31.24415 -1.03079  15.85154  1.000 108.32294 ? -12  ILE A C   1 
ATOM   543  O O   . ILE A 1 109 ? 31.64040 -0.64312  14.74538  1.000 111.58628 ? -12  ILE A O   1 
ATOM   544  C CB  . ILE A 1 109 ? 33.02598 -2.61400  16.70386  1.000 105.98058 ? -12  ILE A CB  1 
ATOM   545  C CG1 . ILE A 1 109 ? 33.51579 -1.42715  17.53143  1.000 103.22727 ? -12  ILE A CG1 1 
ATOM   546  C CG2 . ILE A 1 109 ? 33.88325 -2.80470  15.46050  1.000 108.25102 ? -12  ILE A CG2 1 
ATOM   547  C CD1 . ILE A 1 109 ? 34.96621 -1.53805  17.93121  1.000 113.64871 ? -12  ILE A CD1 1 
ATOM   548  N N   . ILE A 1 110 ? 30.54082 -0.26457  16.68654  1.000 105.58949 ? -11  ILE A N   1 
ATOM   549  C CA  . ILE A 1 110 ? 30.31559 1.16084   16.46979  1.000 111.12238 ? -11  ILE A CA  1 
ATOM   550  C C   . ILE A 1 110 ? 31.14208 1.93893   17.48573  1.000 118.57237 ? -11  ILE A C   1 
ATOM   551  O O   . ILE A 1 110 ? 31.27697 1.52279   18.64271  1.000 112.25471 ? -11  ILE A O   1 
ATOM   552  C CB  . ILE A 1 110 ? 28.82171 1.53065   16.56592  1.000 112.31265 ? -11  ILE A CB  1 
ATOM   553  C CG1 . ILE A 1 110 ? 28.22289 1.03909   17.88436  1.000 113.87598 ? -11  ILE A CG1 1 
ATOM   554  C CG2 . ILE A 1 110 ? 28.05538 0.96156   15.38104  1.000 113.65880 ? -11  ILE A CG2 1 
ATOM   555  C CD1 . ILE A 1 110 ? 26.75322 1.36367   18.04301  1.000 115.40088 ? -11  ILE A CD1 1 
ATOM   556  N N   . GLU A 1 111 ? 31.70408 3.06336   17.04913  1.000 125.97829 ? -10  GLU A N   1 
ATOM   557  C CA  . GLU A 1 111 ? 32.60025 3.86559   17.87377  1.000 120.26589 ? -10  GLU A CA  1 
ATOM   558  C C   . GLU A 1 111 ? 31.86718 5.08006   18.43223  1.000 117.30586 ? -10  GLU A C   1 
ATOM   559  O O   . GLU A 1 111 ? 31.24363 5.83481   17.68119  1.000 120.93448 ? -10  GLU A O   1 
ATOM   560  C CB  . GLU A 1 111 ? 33.81762 4.30602   17.06143  1.000 129.10740 ? -10  GLU A CB  1 
ATOM   561  C CG  . GLU A 1 111 ? 34.94988 3.29129   17.05785  1.000 128.16744 ? -10  GLU A CG  1 
ATOM   562  C CD  . GLU A 1 111 ? 36.14389 3.75082   16.24616  1.000 129.06791 ? -10  GLU A CD  1 
ATOM   563  O OE1 . GLU A 1 111 ? 36.25619 4.96763   15.98497  1.000 129.91566 ? -10  GLU A OE1 1 
ATOM   564  O OE2 . GLU A 1 111 ? 36.96733 2.89263   15.86297  1.000 132.05102 ? -10  GLU A OE2 1 
ATOM   565  N N   . ALA A 1 112 ? 31.95449 5.27429   19.74557  1.000 112.13915 ? -9   ALA A N   1 
ATOM   566  C CA  . ALA A 1 112 ? 31.26837 6.36986   20.42928  1.000 114.96511 ? -9   ALA A CA  1 
ATOM   567  C C   . ALA A 1 112 ? 32.30025 7.38266   20.91807  1.000 125.50419 ? -9   ALA A C   1 
ATOM   568  O O   . ALA A 1 112 ? 32.94856 7.17595   21.94785  1.000 121.98360 ? -9   ALA A O   1 
ATOM   569  C CB  . ALA A 1 112 ? 30.42363 5.84259   21.58261  1.000 108.03410 ? -9   ALA A CB  1 
ATOM   570  N N   . HIS A 1 113 ? 32.44716 8.47490   20.17279  1.000 128.68463 ? -8   HIS A N   1 
ATOM   571  C CA  . HIS A 1 113 ? 33.29578 9.59003   20.57023  1.000 129.61550 ? -8   HIS A CA  1 
ATOM   572  C C   . HIS A 1 113 ? 32.48625 10.64113  21.31934  1.000 138.12070 ? -8   HIS A C   1 
ATOM   573  O O   . HIS A 1 113 ? 31.29016 10.80772  21.08464  1.000 135.60473 ? -8   HIS A O   1 
ATOM   574  C CB  . HIS A 1 113 ? 33.95064 10.22958  19.34558  1.000 130.65232 ? -8   HIS A CB  1 
ATOM   575  C CG  . HIS A 1 113 ? 34.80637 9.28923   18.55684  1.000 130.66038 ? -8   HIS A CG  1 
ATOM   576  N ND1 . HIS A 1 113 ? 36.18275 9.30097   18.62368  1.000 129.64831 ? -8   HIS A ND1 1 
ATOM   577  C CD2 . HIS A 1 113 ? 34.48038 8.30619   17.68464  1.000 127.87212 ? -8   HIS A CD2 1 
ATOM   578  C CE1 . HIS A 1 113 ? 36.66801 8.36732   17.82479  1.000 132.06120 ? -8   HIS A CE1 1 
ATOM   579  N NE2 . HIS A 1 113 ? 35.65580 7.74869   17.24386  1.000 125.21968 ? -8   HIS A NE2 1 
ATOM   580  N N   . ARG A 1 114 ? 33.14413 11.34819  22.23440  1.000 147.17792 ? -7   ARG A N   1 
ATOM   581  C CA  . ARG A 1 114 ? 32.48457 12.48301  22.86158  1.000 156.79957 ? -7   ARG A CA  1 
ATOM   582  C C   . ARG A 1 114 ? 32.33915 13.62300  21.85221  1.000 160.81696 ? -7   ARG A C   1 
ATOM   583  O O   . ARG A 1 114 ? 32.94401 13.62029  20.77579  1.000 161.84273 ? -7   ARG A O   1 
ATOM   584  C CB  . ARG A 1 114 ? 33.25808 12.94573  24.09645  1.000 159.70595 ? -7   ARG A CB  1 
ATOM   585  C CG  . ARG A 1 114 ? 33.52295 11.84618  25.11749  1.000 162.38373 ? -7   ARG A CG  1 
ATOM   586  C CD  . ARG A 1 114 ? 34.80946 12.09984  25.88928  1.000 166.05477 ? -7   ARG A CD  1 
ATOM   587  N NE  . ARG A 1 114 ? 35.94446 12.33938  25.00241  1.000 168.90766 ? -7   ARG A NE  1 
ATOM   588  C CZ  . ARG A 1 114 ? 36.91572 11.46079  24.77651  1.000 166.88712 ? -7   ARG A CZ  1 
ATOM   589  N NH1 . ARG A 1 114 ? 36.89793 10.28032  25.38030  1.000 163.79007 ? -7   ARG A NH1 1 
ATOM   590  N NH2 . ARG A 1 114 ? 37.90926 11.76515  23.95163  1.000 165.86847 ? -7   ARG A NH2 1 
ATOM   591  N N   . GLU A 1 115 ? 31.51949 14.61280  22.20864  1.000 166.55399 ? -6   GLU A N   1 
ATOM   592  C CA  . GLU A 1 115 ? 31.25166 15.72929  21.30150  1.000 176.23316 ? -6   GLU A CA  1 
ATOM   593  C C   . GLU A 1 115 ? 31.00637 16.98096  22.13809  1.000 196.16843 ? -6   GLU A C   1 
ATOM   594  O O   . GLU A 1 115 ? 29.92060 17.15330  22.70057  1.000 194.37099 ? -6   GLU A O   1 
ATOM   595  C CB  . GLU A 1 115 ? 30.07145 15.43476  20.38620  1.000 174.16204 ? -6   GLU A CB  1 
ATOM   596  C CG  . GLU A 1 115 ? 29.90792 16.45536  19.26925  1.000 174.41997 ? -6   GLU A CG  1 
ATOM   597  C CD  . GLU A 1 115 ? 28.79516 16.10186  18.30332  1.000 174.67681 ? -6   GLU A CD  1 
ATOM   598  O OE1 . GLU A 1 115 ? 27.74075 15.61586  18.76158  1.000 174.39950 ? -6   GLU A OE1 1 
ATOM   599  O OE2 . GLU A 1 115 ? 28.97394 16.31324  17.08523  1.000 175.48138 ? -6   GLU A OE2 1 
ATOM   600  N N   . GLN A 1 116 ? 32.01521 17.84177  22.21337  1.000 215.22760 ? -5   GLN A N   1 
ATOM   601  C CA  . GLN A 1 116 ? 31.91652 19.12772  22.89233  1.000 235.50958 ? -5   GLN A CA  1 
ATOM   602  C C   . GLN A 1 116 ? 32.33953 20.24475  21.94787  1.000 242.64468 ? -5   GLN A C   1 
ATOM   603  O O   . GLN A 1 116 ? 33.13562 21.11968  22.29323  1.000 245.69769 ? -5   GLN A O   1 
ATOM   604  C CB  . GLN A 1 116 ? 32.76412 19.13233  24.16181  1.000 242.31653 ? -5   GLN A CB  1 
ATOM   605  C CG  . GLN A 1 116 ? 32.34869 18.09136  25.18745  1.000 246.54186 ? -5   GLN A CG  1 
ATOM   606  C CD  . GLN A 1 116 ? 31.03838 18.42999  25.86905  1.000 252.66815 ? -5   GLN A CD  1 
ATOM   607  O OE1 . GLN A 1 116 ? 30.74312 19.59606  26.12611  1.000 256.38796 ? -5   GLN A OE1 1 
ATOM   608  N NE2 . GLN A 1 116 ? 30.24425 17.40737  26.16747  1.000 252.84489 ? -5   GLN A NE2 1 
ATOM   609  N N   . ILE A 1 117 ? 31.79739 20.21585  20.72744  1.000 245.79724 ? -4   ILE A N   1 
ATOM   610  C CA  . ILE A 1 117 ? 32.24087 21.12784  19.67523  1.000 249.41783 ? -4   ILE A CA  1 
ATOM   611  C C   . ILE A 1 117 ? 31.84156 22.56111  20.00698  1.000 259.11425 ? -4   ILE A C   1 
ATOM   612  O O   . ILE A 1 117 ? 32.69534 23.44460  20.14386  1.000 259.56826 ? -4   ILE A O   1 
ATOM   613  C CB  . ILE A 1 117 ? 31.68865 20.67995  18.30815  1.000 243.46414 ? -4   ILE A CB  1 
ATOM   614  C CG1 . ILE A 1 117 ? 31.77787 21.81427  17.28340  1.000 242.15010 ? -4   ILE A CG1 1 
ATOM   615  C CG2 . ILE A 1 117 ? 30.26081 20.13361  18.44135  1.000 242.43559 ? -4   ILE A CG2 1 
ATOM   616  C CD1 . ILE A 1 117 ? 31.42310 21.39085  15.87788  1.000 238.26417 ? -4   ILE A CD1 1 
ATOM   617  N N   . GLY A 1 118 ? 30.54249 22.81374  20.13582  1.000 265.99716 ? -3   GLY A N   1 
ATOM   618  C CA  . GLY A 1 118 ? 30.03813 24.13249  20.45250  1.000 273.05917 ? -3   GLY A CA  1 
ATOM   619  C C   . GLY A 1 118 ? 29.80534 24.32972  21.93530  1.000 277.70329 ? -3   GLY A C   1 
ATOM   620  O O   . GLY A 1 118 ? 30.31003 23.58594  22.78024  1.000 277.72802 ? -3   GLY A O   1 
ATOM   621  N N   . GLY A 1 119 ? 29.02433 25.35515  22.25103  1.000 212.90056 ? -2   GLY A N   1 
ATOM   622  C CA  . GLY A 1 119 ? 28.67080 25.63030  23.62700  1.000 214.77297 ? -2   GLY A CA  1 
ATOM   623  C C   . GLY A 1 119 ? 29.64268 26.57661  24.30529  1.000 210.64515 ? -2   GLY A C   1 
ATOM   624  O O   . GLY A 1 119 ? 30.34320 27.37760  23.67677  1.000 209.62191 ? -2   GLY A O   1 
ATOM   625  N N   . GLU A 1 120 ? 29.65959 26.48076  25.63586  1.000 206.32916 ? -1   GLU A N   1 
ATOM   626  C CA  . GLU A 1 120 ? 30.49322 27.31054  26.49844  1.000 197.26824 ? -1   GLU A CA  1 
ATOM   627  C C   . GLU A 1 120 ? 31.95139 27.31211  26.05498  1.000 169.70594 ? -1   GLU A C   1 
ATOM   628  O O   . GLU A 1 120 ? 32.66588 26.32427  26.25358  1.000 164.07132 ? -1   GLU A O   1 
ATOM   629  C CB  . GLU A 1 120 ? 30.39135 26.82758  27.94873  1.000 208.66989 ? -1   GLU A CB  1 
ATOM   630  C CG  . GLU A 1 120 ? 29.05506 27.11015  28.61540  1.000 216.29436 ? -1   GLU A CG  1 
ATOM   631  C CD  . GLU A 1 120 ? 29.07141 26.81337  30.10401  1.000 221.90376 ? -1   GLU A CD  1 
ATOM   632  O OE1 . GLU A 1 120 ? 30.03978 26.18082  30.57709  1.000 222.23266 ? -1   GLU A OE1 1 
ATOM   633  O OE2 . GLU A 1 120 ? 28.11369 27.21027  30.80076  1.000 225.93701 ? -1   GLU A OE2 1 
ATOM   634  N N   . PHE A 1 121 ? 32.40450 28.41262  25.46153  1.000 149.86817 ? 0    PHE A N   1 
ATOM   635  C CA  . PHE A 1 121 ? 33.75638 28.48832  24.92861  1.000 139.69230 ? 0    PHE A CA  1 
ATOM   636  C C   . PHE A 1 121 ? 34.72385 29.05017  25.95783  1.000 117.29845 ? 0    PHE A C   1 
ATOM   637  O O   . PHE A 1 121 ? 34.41482 30.00779  26.67340  1.000 106.78258 ? 0    PHE A O   1 
ATOM   638  C CB  . PHE A 1 121 ? 33.81587 29.32747  23.65294  1.000 143.30069 ? 0    PHE A CB  1 
ATOM   639  C CG  . PHE A 1 121 ? 34.48965 28.62464  22.51245  1.000 143.73868 ? 0    PHE A CG  1 
ATOM   640  C CD1 . PHE A 1 121 ? 34.60816 27.24460  22.51296  1.000 145.63570 ? 0    PHE A CD1 1 
ATOM   641  C CD2 . PHE A 1 121 ? 35.03611 29.33949  21.46028  1.000 149.44606 ? 0    PHE A CD2 1 
ATOM   642  C CE1 . PHE A 1 121 ? 35.23868 26.58673  21.47654  1.000 150.63393 ? 0    PHE A CE1 1 
ATOM   643  C CE2 . PHE A 1 121 ? 35.66981 28.68720  20.41788  1.000 153.54853 ? 0    PHE A CE2 1 
ATOM   644  C CZ  . PHE A 1 121 ? 35.77101 27.30871  20.42636  1.000 153.96692 ? 0    PHE A CZ  1 
ATOM   645  N N   . MET A 1 122 ? 35.90055 28.43660  26.01748  1.000 102.39068 ? 1    MET A N   1 
ATOM   646  C CA  . MET A 1 122 ? 36.92715 28.81204  26.97286  1.000 81.56487  ? 1    MET A CA  1 
ATOM   647  C C   . MET A 1 122 ? 37.69559 30.02868  26.48005  1.000 74.65371  ? 1    MET A C   1 
ATOM   648  O O   . MET A 1 122 ? 37.90908 30.20132  25.27634  1.000 73.87443  ? 1    MET A O   1 
ATOM   649  C CB  . MET A 1 122 ? 37.88422 27.63989  27.18341  1.000 80.36810  ? 1    MET A CB  1 
ATOM   650  C CG  . MET A 1 122 ? 37.17820 26.34722  27.54425  1.000 93.36283  ? 1    MET A CG  1 
ATOM   651  S SD  . MET A 1 122 ? 37.37495 25.08852  26.26886  1.000 90.73709  ? 1    MET A SD  1 
ATOM   652  C CE  . MET A 1 122 ? 36.23585 23.83652  26.85936  1.000 87.19318  ? 1    MET A CE  1 
ATOM   653  N N   . GLN A 1 123 ? 38.09047 30.88518  27.41766  1.000 73.33251  ? 2    GLN A N   1 
ATOM   654  C CA  . GLN A 1 123 ? 38.95249 32.01255  27.09786  1.000 77.67859  ? 2    GLN A CA  1 
ATOM   655  C C   . GLN A 1 123 ? 40.38783 31.53982  26.89709  1.000 77.41948  ? 2    GLN A C   1 
ATOM   656  O O   . GLN A 1 123 ? 40.87825 30.66898  27.62418  1.000 70.07277  ? 2    GLN A O   1 
ATOM   657  C CB  . GLN A 1 123 ? 38.89090 33.06675  28.20341  1.000 73.10667  ? 2    GLN A CB  1 
ATOM   658  C CG  . GLN A 1 123 ? 38.98663 34.49198  27.68768  1.000 77.80017  ? 2    GLN A CG  1 
ATOM   659  C CD  . GLN A 1 123 ? 39.03536 35.51967  28.79859  1.000 83.36115  ? 2    GLN A CD  1 
ATOM   660  O OE1 . GLN A 1 123 ? 39.15013 35.17622  29.97566  1.000 84.38989  ? 2    GLN A OE1 1 
ATOM   661  N NE2 . GLN A 1 123 ? 38.94200 36.79280  28.42864  1.000 80.46372  ? 2    GLN A NE2 1 
ATOM   662  N N   . LYS A 1 124 ? 41.06369 32.13268  25.91664  1.000 64.20160  ? 3    LYS A N   1 
ATOM   663  C CA  . LYS A 1 124 ? 42.46587 31.84442  25.64175  1.000 69.78797  ? 3    LYS A CA  1 
ATOM   664  C C   . LYS A 1 124 ? 43.32486 32.98464  26.17491  1.000 64.03394  ? 3    LYS A C   1 
ATOM   665  O O   . LYS A 1 124 ? 43.14341 34.14208  25.77968  1.000 59.15862  ? 3    LYS A O   1 
ATOM   666  C CB  . LYS A 1 124 ? 42.70795 31.64774  24.14323  1.000 65.50015  ? 3    LYS A CB  1 
ATOM   667  C CG  . LYS A 1 124 ? 42.39238 30.24995  23.60455  1.000 66.07731  ? 3    LYS A CG  1 
ATOM   668  C CD  . LYS A 1 124 ? 40.91713 29.89587  23.71505  1.000 77.39420  ? 3    LYS A CD  1 
ATOM   669  C CE  . LYS A 1 124 ? 40.06163 30.75907  22.79792  1.000 80.70257  ? 3    LYS A CE  1 
ATOM   670  N NZ  . LYS A 1 124 ? 38.74360 30.12268  22.50226  1.000 68.79375  ? 3    LYS A NZ  1 
ATOM   671  N N   . LEU A 1 125 ? 44.25434 32.65412  27.06810  1.000 56.69478  ? 4    LEU A N   1 
ATOM   672  C CA  . LEU A 1 125 ? 45.20321 33.60528  27.63198  1.000 63.07540  ? 4    LEU A CA  1 
ATOM   673  C C   . LEU A 1 125 ? 46.57883 33.28704  27.06407  1.000 63.54846  ? 4    LEU A C   1 
ATOM   674  O O   . LEU A 1 125 ? 47.05898 32.15719  27.20108  1.000 61.11868  ? 4    LEU A O   1 
ATOM   675  C CB  . LEU A 1 125 ? 45.21904 33.53861  29.16030  1.000 65.11168  ? 4    LEU A CB  1 
ATOM   676  C CG  . LEU A 1 125 ? 43.89613 33.50622  29.93245  1.000 81.72874  ? 4    LEU A CG  1 
ATOM   677  C CD1 . LEU A 1 125 ? 44.12008 33.93471  31.37440  1.000 87.55907  ? 4    LEU A CD1 1 
ATOM   678  C CD2 . LEU A 1 125 ? 42.83132 34.37301  29.28067  1.000 91.58049  ? 4    LEU A CD2 1 
ATOM   679  N N   . LEU A 1 126 ? 47.20879 34.27685  26.43802  1.000 58.34315  ? 5    LEU A N   1 
ATOM   680  C CA  . LEU A 1 126 ? 48.48076 34.08850  25.75291  1.000 60.14469  ? 5    LEU A CA  1 
ATOM   681  C C   . LEU A 1 126 ? 49.55668 34.94263  26.40540  1.000 59.22092  ? 5    LEU A C   1 
ATOM   682  O O   . LEU A 1 126 ? 49.34541 36.13511  26.65109  1.000 54.82659  ? 5    LEU A O   1 
ATOM   683  C CB  . LEU A 1 126 ? 48.36805 34.44859  24.26861  1.000 57.48915  ? 5    LEU A CB  1 
ATOM   684  C CG  . LEU A 1 126 ? 47.54023 33.53809  23.36060  1.000 72.18422  ? 5    LEU A CG  1 
ATOM   685  C CD1 . LEU A 1 126 ? 47.34036 34.19616  22.01025  1.000 71.95607  ? 5    LEU A CD1 1 
ATOM   686  C CD2 . LEU A 1 126 ? 48.20871 32.19336  23.19659  1.000 73.31456  ? 5    LEU A CD2 1 
ATOM   687  N N   . SER A 1 127 ? 50.70575 34.33378  26.68406  1.000 59.33699  ? 6    SER A N   1 
ATOM   688  C CA  . SER A 1 127 ? 51.92864 35.08341  26.94778  1.000 65.05174  ? 6    SER A CA  1 
ATOM   689  C C   . SER A 1 127 ? 52.69262 35.19207  25.63231  1.000 61.35316  ? 6    SER A C   1 
ATOM   690  O O   . SER A 1 127 ? 53.18401 34.18856  25.10712  1.000 59.96656  ? 6    SER A O   1 
ATOM   691  C CB  . SER A 1 127 ? 52.76471 34.40044  28.02560  1.000 64.23160  ? 6    SER A CB  1 
ATOM   692  O OG  . SER A 1 127 ? 53.77527 35.27011  28.50420  1.000 89.20062  ? 6    SER A OG  1 
ATOM   693  N N   . LEU A 1 128 ? 52.76938 36.40303  25.09406  1.000 60.98217  ? 7    LEU A N   1 
ATOM   694  C CA  . LEU A 1 128 ? 53.29602 36.69537  23.77188  1.000 67.06740  ? 7    LEU A CA  1 
ATOM   695  C C   . LEU A 1 128 ? 54.41644 37.72210  23.86042  1.000 73.87932  ? 7    LEU A C   1 
ATOM   696  O O   . LEU A 1 128 ? 54.55868 38.40716  24.88003  1.000 70.83791  ? 7    LEU A O   1 
ATOM   697  C CB  . LEU A 1 128 ? 52.18300 37.23419  22.86154  1.000 52.68315  ? 7    LEU A CB  1 
ATOM   698  C CG  . LEU A 1 128 ? 51.01943 36.29106  22.56515  1.000 56.84059  ? 7    LEU A CG  1 
ATOM   699  C CD1 . LEU A 1 128 ? 50.04682 36.95863  21.60606  1.000 55.76898  ? 7    LEU A CD1 1 
ATOM   700  C CD2 . LEU A 1 128 ? 51.52777 34.96915  22.00735  1.000 54.82950  ? 7    LEU A CD2 1 
ATOM   701  N N   . PRO A 1 129 ? 55.24590 37.84454  22.82155  1.000 67.29985  ? 8    PRO A N   1 
ATOM   702  C CA  . PRO A 1 129 ? 56.17961 38.97655  22.77627  1.000 70.93652  ? 8    PRO A CA  1 
ATOM   703  C C   . PRO A 1 129 ? 55.41278 40.29208  22.78631  1.000 75.90581  ? 8    PRO A C   1 
ATOM   704  O O   . PRO A 1 129 ? 54.34901 40.41452  22.17503  1.000 76.54667  ? 8    PRO A O   1 
ATOM   705  C CB  . PRO A 1 129 ? 56.94263 38.76584  21.46100  1.000 63.18395  ? 8    PRO A CB  1 
ATOM   706  C CG  . PRO A 1 129 ? 56.67788 37.34149  21.07009  1.000 50.09831  ? 8    PRO A CG  1 
ATOM   707  C CD  . PRO A 1 129 ? 55.32349 37.02058  21.60122  1.000 53.55268  ? 8    PRO A CD  1 
ATOM   708  N N   . SER A 1 130 ? 55.95721 41.27718  23.50788  1.000 79.74090  ? 9    SER A N   1 
ATOM   709  C CA  . SER A 1 130 ? 55.20808 42.50306  23.77715  1.000 75.46335  ? 9    SER A CA  1 
ATOM   710  C C   . SER A 1 130 ? 54.81252 43.23414  22.49827  1.000 74.28699  ? 9    SER A C   1 
ATOM   711  O O   . SER A 1 130 ? 53.75295 43.86941  22.45395  1.000 76.17464  ? 9    SER A O   1 
ATOM   712  C CB  . SER A 1 130 ? 56.02551 43.42550  24.68127  1.000 73.94104  ? 9    SER A CB  1 
ATOM   713  O OG  . SER A 1 130 ? 57.33523 43.60178  24.17066  1.000 87.27652  ? 9    SER A OG  1 
ATOM   714  N N   . ASN A 1 131 ? 55.64413 43.16568  21.45468  1.000 69.33375  ? 10   ASN A N   1 
ATOM   715  C CA  . ASN A 1 131 ? 55.30872 43.83266  20.19913  1.000 69.00578  ? 10   ASN A CA  1 
ATOM   716  C C   . ASN A 1 131 ? 54.06908 43.21921  19.55566  1.000 67.65150  ? 10   ASN A C   1 
ATOM   717  O O   . ASN A 1 131 ? 53.29879 43.92365  18.89287  1.000 62.11194  ? 10   ASN A O   1 
ATOM   718  C CB  . ASN A 1 131 ? 56.49876 43.77072  19.24062  1.000 62.95228  ? 10   ASN A CB  1 
ATOM   719  C CG  . ASN A 1 131 ? 56.21690 44.44066  17.90888  1.000 63.17799  ? 10   ASN A CG  1 
ATOM   720  O OD1 . ASN A 1 131 ? 55.66328 45.53872  17.85597  1.000 69.91289  ? 10   ASN A OD1 1 
ATOM   721  N ND2 . ASN A 1 131 ? 56.60632 43.78328  16.82353  1.000 67.45226  ? 10   ASN A ND2 1 
ATOM   722  N N   . LEU A 1 132 ? 53.86724 41.91334  19.73923  1.000 61.08954  ? 11   LEU A N   1 
ATOM   723  C CA  . LEU A 1 132 ? 52.74321 41.20026  19.14779  1.000 58.81563  ? 11   LEU A CA  1 
ATOM   724  C C   . LEU A 1 132 ? 51.46202 41.36974  19.95519  1.000 75.41738  ? 11   LEU A C   1 
ATOM   725  O O   . LEU A 1 132 ? 50.36785 41.21013  19.40192  1.000 64.52657  ? 11   LEU A O   1 
ATOM   726  C CB  . LEU A 1 132 ? 53.09524 39.71383  19.01010  1.000 54.35084  ? 11   LEU A CB  1 
ATOM   727  C CG  . LEU A 1 132 ? 52.04398 38.70189  18.54361  1.000 72.08376  ? 11   LEU A CG  1 
ATOM   728  C CD1 . LEU A 1 132 ? 51.79041 38.81732  17.04977  1.000 56.60690  ? 11   LEU A CD1 1 
ATOM   729  C CD2 . LEU A 1 132 ? 52.47777 37.28896  18.90440  1.000 72.00456  ? 11   LEU A CD2 1 
ATOM   730  N N   . VAL A 1 133 ? 51.58203 41.67880  21.24842  1.000 68.44193  ? 12   VAL A N   1 
ATOM   731  C CA  . VAL A 1 133 ? 50.41205 41.94049  22.08197  1.000 63.52252  ? 12   VAL A CA  1 
ATOM   732  C C   . VAL A 1 133 ? 49.57636 43.06793  21.48710  1.000 74.25169  ? 12   VAL A C   1 
ATOM   733  O O   . VAL A 1 133 ? 48.36199 42.93167  21.29881  1.000 78.02152  ? 12   VAL A O   1 
ATOM   734  C CB  . VAL A 1 133 ? 50.84928 42.25719  23.52344  1.000 65.18559  ? 12   VAL A CB  1 
ATOM   735  C CG1 . VAL A 1 133 ? 49.76764 43.03315  24.25881  1.000 71.31529  ? 12   VAL A CG1 1 
ATOM   736  C CG2 . VAL A 1 133 ? 51.19817 40.97776  24.25942  1.000 60.11614  ? 12   VAL A CG2 1 
ATOM   737  N N   . GLN A 1 134 ? 50.21877 44.19990  21.18349  1.000 91.27378  ? 13   GLN A N   1 
ATOM   738  C CA  . GLN A 1 134 ? 49.52241 45.37141  20.65826  1.000 94.19472  ? 13   GLN A CA  1 
ATOM   739  C C   . GLN A 1 134 ? 48.68218 45.07115  19.42286  1.000 90.74834  ? 13   GLN A C   1 
ATOM   740  O O   . GLN A 1 134 ? 47.77976 45.85054  19.09622  1.000 88.76397  ? 13   GLN A O   1 
ATOM   741  C CB  . GLN A 1 134 ? 50.53664 46.46993  20.32758  1.000 110.81241 ? 13   GLN A CB  1 
ATOM   742  C CG  . GLN A 1 134 ? 51.34782 46.94598  21.51928  1.000 124.34279 ? 13   GLN A CG  1 
ATOM   743  C CD  . GLN A 1 134 ? 50.47799 47.31720  22.70378  1.000 132.70095 ? 13   GLN A CD  1 
ATOM   744  O OE1 . GLN A 1 134 ? 49.46499 48.00199  22.55528  1.000 135.94721 ? 13   GLN A OE1 1 
ATOM   745  N NE2 . GLN A 1 134 ? 50.86978 46.86656  23.88926  1.000 135.55251 ? 13   GLN A NE2 1 
ATOM   746  N N   . SER A 1 135 ? 48.95293 43.96616  18.72690  1.000 81.08990  ? 14   SER A N   1 
ATOM   747  C CA  . SER A 1 135 ? 48.43415 43.76068  17.38286  1.000 72.44503  ? 14   SER A CA  1 
ATOM   748  C C   . SER A 1 135 ? 47.79394 42.39879  17.16038  1.000 57.45956  ? 14   SER A C   1 
ATOM   749  O O   . SER A 1 135 ? 47.16360 42.20644  16.11399  1.000 51.11316  ? 14   SER A O   1 
ATOM   750  C CB  . SER A 1 135 ? 49.54995 43.95139  16.34285  1.000 68.41826  ? 14   SER A CB  1 
ATOM   751  O OG  . SER A 1 135 ? 49.84157 45.32450  16.15591  1.000 80.30603  ? 14   SER A OG  1 
ATOM   752  N N   . PHE A 1 136 ? 47.92963 41.45896  18.10119  1.000 55.16127  ? 15   PHE A N   1 
ATOM   753  C CA  . PHE A 1 136 ? 47.51983 40.07740  17.86096  1.000 57.02407  ? 15   PHE A CA  1 
ATOM   754  C C   . PHE A 1 136 ? 46.05950 39.98294  17.43236  1.000 60.27536  ? 15   PHE A C   1 
ATOM   755  O O   . PHE A 1 136 ? 45.72853 39.24977  16.49199  1.000 61.17590  ? 15   PHE A O   1 
ATOM   756  C CB  . PHE A 1 136 ? 47.76963 39.23929  19.11830  1.000 59.95850  ? 15   PHE A CB  1 
ATOM   757  C CG  . PHE A 1 136 ? 47.07104 37.90587  19.11353  1.000 68.62039  ? 15   PHE A CG  1 
ATOM   758  C CD1 . PHE A 1 136 ? 47.69464 36.78754  18.58673  1.000 70.42240  ? 15   PHE A CD1 1 
ATOM   759  C CD2 . PHE A 1 136 ? 45.80471 37.76397  19.66130  1.000 63.82880  ? 15   PHE A CD2 1 
ATOM   760  C CE1 . PHE A 1 136 ? 47.06050 35.56157  18.58162  1.000 64.73192  ? 15   PHE A CE1 1 
ATOM   761  C CE2 . PHE A 1 136 ? 45.16769 36.54071  19.66020  1.000 48.38432  ? 15   PHE A CE2 1 
ATOM   762  C CZ  . PHE A 1 136 ? 45.79545 35.43829  19.11992  1.000 60.94817  ? 15   PHE A CZ  1 
ATOM   763  N N   . HIS A 1 137 ? 45.17172 40.71680  18.10758  1.000 69.96738  ? 16   HIS A N   1 
ATOM   764  C CA  . HIS A 1 137 ? 43.74797 40.61962  17.79749  1.000 58.86517  ? 16   HIS A CA  1 
ATOM   765  C C   . HIS A 1 137 ? 43.44418 41.11070  16.38760  1.000 70.78617  ? 16   HIS A C   1 
ATOM   766  O O   . HIS A 1 137 ? 42.63230 40.50693  15.67775  1.000 61.58342  ? 16   HIS A O   1 
ATOM   767  C CB  . HIS A 1 137 ? 42.93139 41.39569  18.82802  1.000 55.53018  ? 16   HIS A CB  1 
ATOM   768  C CG  . HIS A 1 137 ? 42.97584 40.80244  20.20215  1.000 63.79542  ? 16   HIS A CG  1 
ATOM   769  N ND1 . HIS A 1 137 ? 43.72208 41.34560  21.22578  1.000 62.28547  ? 16   HIS A ND1 1 
ATOM   770  C CD2 . HIS A 1 137 ? 42.35990 39.71350  20.72252  1.000 69.30152  ? 16   HIS A CD2 1 
ATOM   771  C CE1 . HIS A 1 137 ? 43.56871 40.61442  22.31553  1.000 67.82985  ? 16   HIS A CE1 1 
ATOM   772  N NE2 . HIS A 1 137 ? 42.74602 39.61863  22.03749  1.000 67.23864  ? 16   HIS A NE2 1 
ATOM   773  N N   . GLU A 1 138 ? 44.08126 42.20376  15.96096  1.000 58.75218  ? 17   GLU A N   1 
ATOM   774  C CA  . GLU A 1 138 ? 43.86767 42.68308  14.59837  1.000 58.36627  ? 17   GLU A CA  1 
ATOM   775  C C   . GLU A 1 138 ? 44.48117 41.73877  13.57153  1.000 68.15369  ? 17   GLU A C   1 
ATOM   776  O O   . GLU A 1 138 ? 43.87633 41.47621  12.52556  1.000 69.36398  ? 17   GLU A O   1 
ATOM   777  C CB  . GLU A 1 138 ? 44.43250 44.09349  14.43417  1.000 62.69679  ? 17   GLU A CB  1 
ATOM   778  C CG  . GLU A 1 138 ? 44.13660 44.71882  13.07528  1.000 72.00766  ? 17   GLU A CG  1 
ATOM   779  C CD  . GLU A 1 138 ? 44.76603 46.08920  12.90538  1.000 89.64413  ? 17   GLU A CD  1 
ATOM   780  O OE1 . GLU A 1 138 ? 45.10784 46.72295  13.92705  1.000 97.84399  ? 17   GLU A OE1 1 
ATOM   781  O OE2 . GLU A 1 138 ? 44.91577 46.53417  11.74783  1.000 98.33824  ? 17   GLU A OE2 1 
ATOM   782  N N   . LEU A 1 139 ? 45.68229 41.22161  13.85168  1.000 80.64555  ? 18   LEU A N   1 
ATOM   783  C CA  . LEU A 1 139 ? 46.39787 40.41040  12.86907  1.000 70.41412  ? 18   LEU A CA  1 
ATOM   784  C C   . LEU A 1 139 ? 45.66656 39.10649  12.57347  1.000 56.36331  ? 18   LEU A C   1 
ATOM   785  O O   . LEU A 1 139 ? 45.57417 38.69041  11.41295  1.000 60.14087  ? 18   LEU A O   1 
ATOM   786  C CB  . LEU A 1 139 ? 47.81695 40.12791  13.36184  1.000 62.53348  ? 18   LEU A CB  1 
ATOM   787  C CG  . LEU A 1 139 ? 48.74732 41.34085  13.43996  1.000 73.23203  ? 18   LEU A CG  1 
ATOM   788  C CD1 . LEU A 1 139 ? 50.05252 40.97185  14.12620  1.000 71.71776  ? 18   LEU A CD1 1 
ATOM   789  C CD2 . LEU A 1 139 ? 49.00349 41.92222  12.05758  1.000 63.85130  ? 18   LEU A CD2 1 
ATOM   790  N N   . GLU A 1 140 ? 45.15057 38.44315  13.60452  1.000 47.98728  ? 19   GLU A N   1 
ATOM   791  C CA  . GLU A 1 140 ? 44.46811 37.16835  13.44236  1.000 53.11597  ? 19   GLU A CA  1 
ATOM   792  C C   . GLU A 1 140 ? 42.94938 37.31335  13.47978  1.000 56.96621  ? 19   GLU A C   1 
ATOM   793  O O   . GLU A 1 140 ? 42.24338 36.30143  13.42602  1.000 48.74207  ? 19   GLU A O   1 
ATOM   794  C CB  . GLU A 1 140 ? 44.92973 36.18587  14.52128  1.000 50.25971  ? 19   GLU A CB  1 
ATOM   795  C CG  . GLU A 1 140 ? 46.42820 35.92283  14.51162  1.000 69.88180  ? 19   GLU A CG  1 
ATOM   796  C CD  . GLU A 1 140 ? 46.85120 34.97193  13.40900  1.000 65.81996  ? 19   GLU A CD  1 
ATOM   797  O OE1 . GLU A 1 140 ? 46.01377 34.15658  12.96808  1.000 72.36779  ? 19   GLU A OE1 1 
ATOM   798  O OE2 . GLU A 1 140 ? 48.02064 35.04410  12.97834  1.000 71.31746  ? 19   GLU A OE2 1 
ATOM   799  N N   . ARG A 1 141 ? 42.44304 38.54949  13.54841  1.000 54.60622  ? 20   ARG A N   1 
ATOM   800  C CA  . ARG A 1 141 ? 41.01610 38.86183  13.58526  1.000 73.65593  ? 20   ARG A CA  1 
ATOM   801  C C   . ARG A 1 141 ? 40.26107 37.90305  14.49706  1.000 70.14456  ? 20   ARG A C   1 
ATOM   802  O O   . ARG A 1 141 ? 39.44042 37.09854  14.04380  1.000 65.92143  ? 20   ARG A O   1 
ATOM   803  C CB  . ARG A 1 141 ? 40.43172 38.88250  12.17108  1.000 73.31096  ? 20   ARG A CB  1 
ATOM   804  C CG  . ARG A 1 141 ? 40.90598 40.10381  11.38162  1.000 86.30499  ? 20   ARG A CG  1 
ATOM   805  C CD  . ARG A 1 141 ? 40.77459 39.95170  9.87622   1.000 88.12904  ? 20   ARG A CD  1 
ATOM   806  N NE  . ARG A 1 141 ? 39.43503 39.54246  9.46722   1.000 96.13216  ? 20   ARG A NE  1 
ATOM   807  C CZ  . ARG A 1 141 ? 39.01980 39.52059  8.20487   1.000 99.51644  ? 20   ARG A CZ  1 
ATOM   808  N NH1 . ARG A 1 141 ? 39.84008 39.89282  7.23105   1.000 91.69287  ? 20   ARG A NH1 1 
ATOM   809  N NH2 . ARG A 1 141 ? 37.78347 39.13687  7.91575   1.000 109.01792 ? 20   ARG A NH2 1 
ATOM   810  N N   . VAL A 1 142 ? 40.57542 37.98073  15.78839  1.000 65.93107  ? 21   VAL A N   1 
ATOM   811  C CA  . VAL A 1 142 ? 39.82508 37.35005  16.86092  1.000 71.82159  ? 21   VAL A CA  1 
ATOM   812  C C   . VAL A 1 142 ? 39.35350 38.45246  17.79966  1.000 70.45922  ? 21   VAL A C   1 
ATOM   813  O O   . VAL A 1 142 ? 39.89931 39.55949  17.82152  1.000 65.59952  ? 21   VAL A O   1 
ATOM   814  C CB  . VAL A 1 142 ? 40.65343 36.29727  17.62546  1.000 60.71615  ? 21   VAL A CB  1 
ATOM   815  C CG1 . VAL A 1 142 ? 40.85348 35.05925  16.77275  1.000 57.86812  ? 21   VAL A CG1 1 
ATOM   816  C CG2 . VAL A 1 142 ? 41.98718 36.87702  18.04522  1.000 59.98986  ? 21   VAL A CG2 1 
ATOM   817  N N   . ASN A 1 143 ? 38.32258 38.14116  18.57671  1.000 61.07402  ? 22   ASN A N   1 
ATOM   818  C CA  . ASN A 1 143 ? 37.73807 39.11423  19.48597  1.000 73.17935  ? 22   ASN A CA  1 
ATOM   819  C C   . ASN A 1 143 ? 38.34243 38.98173  20.87905  1.000 69.43196  ? 22   ASN A C   1 
ATOM   820  O O   . ASN A 1 143 ? 38.80603 37.91092  21.28184  1.000 69.39366  ? 22   ASN A O   1 
ATOM   821  C CB  . ASN A 1 143 ? 36.22184 38.93203  19.55498  1.000 76.21179  ? 22   ASN A CB  1 
ATOM   822  C CG  . ASN A 1 143 ? 35.82701 37.54159  20.01224  1.000 88.54052  ? 22   ASN A CG  1 
ATOM   823  O OD1 . ASN A 1 143 ? 35.83371 37.24267  21.20640  1.000 95.19911  ? 22   ASN A OD1 1 
ATOM   824  N ND2 . ASN A 1 143 ? 35.48968 36.67861  19.05943  1.000 95.21158  ? 22   ASN A ND2 1 
ATOM   825  N N   . ARG A 1 144 ? 38.31770 40.09181  21.62034  1.000 87.88363  ? 23   ARG A N   1 
ATOM   826  C CA  . ARG A 1 144 ? 38.94628 40.15777  22.93539  1.000 88.15975  ? 23   ARG A CA  1 
ATOM   827  C C   . ARG A 1 144 ? 38.17868 39.41743  24.02478  1.000 91.56878  ? 23   ARG A C   1 
ATOM   828  O O   . ARG A 1 144 ? 38.73321 39.21723  25.11113  1.000 102.90330 ? 23   ARG A O   1 
ATOM   829  C CB  . ARG A 1 144 ? 39.13752 41.61832  23.34856  1.000 89.47089  ? 23   ARG A CB  1 
ATOM   830  C CG  . ARG A 1 144 ? 40.33711 42.28521  22.69697  1.000 92.62153  ? 23   ARG A CG  1 
ATOM   831  C CD  . ARG A 1 144 ? 40.32441 43.78953  22.90465  1.000 101.46928 ? 23   ARG A CD  1 
ATOM   832  N NE  . ARG A 1 144 ? 41.49248 44.42077  22.29963  1.000 118.14591 ? 23   ARG A NE  1 
ATOM   833  C CZ  . ARG A 1 144 ? 42.66842 44.54904  22.90545  1.000 128.12985 ? 23   ARG A CZ  1 
ATOM   834  N NH1 . ARG A 1 144 ? 42.83086 44.10188  24.14395  1.000 132.19702 ? 23   ARG A NH1 1 
ATOM   835  N NH2 . ARG A 1 144 ? 43.67972 45.13441  22.27775  1.000 130.77923 ? 23   ARG A NH2 1 
ATOM   836  N N   . THR A 1 145 ? 36.93150 39.00952  23.77875  1.000 78.48486  ? 24   THR A N   1 
ATOM   837  C CA  . THR A 1 145 ? 36.22480 38.21388  24.77817  1.000 83.30606  ? 24   THR A CA  1 
ATOM   838  C C   . THR A 1 145 ? 36.82929 36.82053  24.90098  1.000 79.51057  ? 24   THR A C   1 
ATOM   839  O O   . THR A 1 145 ? 37.01869 36.31765  26.01395  1.000 84.77547  ? 24   THR A O   1 
ATOM   840  C CB  . THR A 1 145 ? 34.73292 38.12553  24.44411  1.000 89.25911  ? 24   THR A CB  1 
ATOM   841  O OG1 . THR A 1 145 ? 34.54736 37.35016  23.25392  1.000 88.13676  ? 24   THR A OG1 1 
ATOM   842  C CG2 . THR A 1 145 ? 34.14080 39.51249  24.24286  1.000 79.46446  ? 24   THR A CG2 1 
ATOM   843  N N   . ASP A 1 146 ? 37.13163 36.17853  23.77381  1.000 75.35911  ? 25   ASP A N   1 
ATOM   844  C CA  . ASP A 1 146 ? 37.68389 34.83077  23.78488  1.000 75.81846  ? 25   ASP A CA  1 
ATOM   845  C C   . ASP A 1 146 ? 39.19938 34.79854  23.92697  1.000 68.36213  ? 25   ASP A C   1 
ATOM   846  O O   . ASP A 1 146 ? 39.75334 33.73346  24.21952  1.000 64.77429  ? 25   ASP A O   1 
ATOM   847  C CB  . ASP A 1 146 ? 37.29812 34.08999  22.50144  1.000 82.29095  ? 25   ASP A CB  1 
ATOM   848  C CG  . ASP A 1 146 ? 35.80529 34.01805  22.29841  1.000 94.68938  ? 25   ASP A CG  1 
ATOM   849  O OD1 . ASP A 1 146 ? 35.06364 34.61747  23.10590  1.000 99.32651  ? 25   ASP A OD1 1 
ATOM   850  O OD2 . ASP A 1 146 ? 35.37456 33.36107  21.32867  1.000 101.21048 ? 25   ASP A OD2 1 
ATOM   851  N N   . TRP A 1 147 ? 39.88059 35.92476  23.72879  1.000 67.77439  ? 26   TRP A N   1 
ATOM   852  C CA  . TRP A 1 147 ? 41.33493 35.93554  23.61556  1.000 77.29132  ? 26   TRP A CA  1 
ATOM   853  C C   . TRP A 1 147 ? 41.89589 37.10626  24.40423  1.000 68.14345  ? 26   TRP A C   1 
ATOM   854  O O   . TRP A 1 147 ? 41.62266 38.26558  24.07798  1.000 68.59942  ? 26   TRP A O   1 
ATOM   855  C CB  . TRP A 1 147 ? 41.78076 36.03359  22.15199  1.000 71.11992  ? 26   TRP A CB  1 
ATOM   856  C CG  . TRP A 1 147 ? 41.36131 34.88332  21.28910  1.000 70.75985  ? 26   TRP A CG  1 
ATOM   857  C CD1 . TRP A 1 147 ? 40.14790 34.70793  20.69526  1.000 79.07857  ? 26   TRP A CD1 1 
ATOM   858  C CD2 . TRP A 1 147 ? 42.16591 33.76406  20.89483  1.000 71.22439  ? 26   TRP A CD2 1 
ATOM   859  N NE1 . TRP A 1 147 ? 40.13886 33.54244  19.96843  1.000 83.60866  ? 26   TRP A NE1 1 
ATOM   860  C CE2 . TRP A 1 147 ? 41.36654 32.94477  20.07319  1.000 74.55402  ? 26   TRP A CE2 1 
ATOM   861  C CE3 . TRP A 1 147 ? 43.48130 33.37156  21.16267  1.000 72.02493  ? 26   TRP A CE3 1 
ATOM   862  C CZ2 . TRP A 1 147 ? 41.83749 31.75728  19.51703  1.000 75.16256  ? 26   TRP A CZ2 1 
ATOM   863  C CZ3 . TRP A 1 147 ? 43.94781 32.19060  20.60934  1.000 67.88516  ? 26   TRP A CZ3 1 
ATOM   864  C CH2 . TRP A 1 147 ? 43.12799 31.39855  19.79555  1.000 71.23329  ? 26   TRP A CH2 1 
ATOM   865  N N   . PHE A 1 148 ? 42.66708 36.80424  25.44168  1.000 59.59487  ? 27   PHE A N   1 
ATOM   866  C CA  . PHE A 1 148 ? 43.42188 37.80746  26.17526  1.000 74.34316  ? 27   PHE A CA  1 
ATOM   867  C C   . PHE A 1 148 ? 44.90188 37.49152  26.02367  1.000 63.66304  ? 27   PHE A C   1 
ATOM   868  O O   . PHE A 1 148 ? 45.30271 36.32420  26.06279  1.000 63.89467  ? 27   PHE A O   1 
ATOM   869  C CB  . PHE A 1 148 ? 43.04183 37.84322  27.65995  1.000 61.09925  ? 27   PHE A CB  1 
ATOM   870  C CG  . PHE A 1 148 ? 43.89223 38.77631  28.47565  1.000 68.40682  ? 27   PHE A CG  1 
ATOM   871  C CD1 . PHE A 1 148 ? 43.64371 40.14043  28.46916  1.000 74.27488  ? 27   PHE A CD1 1 
ATOM   872  C CD2 . PHE A 1 148 ? 44.95056 38.29581  29.23426  1.000 73.64408  ? 27   PHE A CD2 1 
ATOM   873  C CE1 . PHE A 1 148 ? 44.42796 41.00888  29.21060  1.000 77.75988  ? 27   PHE A CE1 1 
ATOM   874  C CE2 . PHE A 1 148 ? 45.73882 39.15851  29.97728  1.000 67.83369  ? 27   PHE A CE2 1 
ATOM   875  C CZ  . PHE A 1 148 ? 45.47723 40.51628  29.96441  1.000 75.01560  ? 27   PHE A CZ  1 
ATOM   876  N N   . CYS A 1 149 ? 45.72163 38.52125  25.85688  1.000 66.48026  ? 28   CYS A N   1 
ATOM   877  C CA  . CYS A 1 149 ? 47.15542 38.29271  25.86246  1.000 73.71571  ? 28   CYS A CA  1 
ATOM   878  C C   . CYS A 1 149 ? 47.86458 39.43449  26.56797  1.000 74.03707  ? 28   CYS A C   1 
ATOM   879  O O   . CYS A 1 149 ? 47.33933 40.54272  26.70806  1.000 67.14800  ? 28   CYS A O   1 
ATOM   880  C CB  . CYS A 1 149 ? 47.72181 38.12908  24.44430  1.000 75.07735  ? 28   CYS A CB  1 
ATOM   881  S SG  . CYS A 1 149 ? 47.21730 39.39659  23.26865  1.000 76.13214  ? 28   CYS A SG  1 
ATOM   882  N N   . THR A 1 150 ? 49.07809 39.12973  27.01117  1.000 70.34918  ? 29   THR A N   1 
ATOM   883  C CA  . THR A 1 150 ? 49.96359 40.08242  27.65221  1.000 76.66805  ? 29   THR A CA  1 
ATOM   884  C C   . THR A 1 150 ? 51.39031 39.60573  27.41524  1.000 82.41868  ? 29   THR A C   1 
ATOM   885  O O   . THR A 1 150 ? 51.62573 38.62401  26.70388  1.000 79.48350  ? 29   THR A O   1 
ATOM   886  C CB  . THR A 1 150 ? 49.63676 40.22575  29.14412  1.000 74.54740  ? 29   THR A CB  1 
ATOM   887  O OG1 . THR A 1 150 ? 50.40936 41.29504  29.70473  1.000 88.77364  ? 29   THR A OG1 1 
ATOM   888  C CG2 . THR A 1 150 ? 49.95779 38.93641  29.88240  1.000 68.71573  ? 29   THR A CG2 1 
ATOM   889  N N   . SER A 1 151 ? 52.34541 40.29760  28.02323  1.000 81.16146  ? 30   SER A N   1 
ATOM   890  C CA  . SER A 1 151 ? 53.74439 39.92160  27.93620  1.000 77.94462  ? 30   SER A CA  1 
ATOM   891  C C   . SER A 1 151 ? 54.37640 40.10656  29.30394  1.000 86.36770  ? 30   SER A C   1 
ATOM   892  O O   . SER A 1 151 ? 53.85903 40.83749  30.15287  1.000 85.86223  ? 30   SER A O   1 
ATOM   893  C CB  . SER A 1 151 ? 54.48645 40.75927  26.89011  1.000 76.65446  ? 30   SER A CB  1 
ATOM   894  O OG  . SER A 1 151 ? 54.12251 42.12472  26.99112  1.000 80.28429  ? 30   SER A OG  1 
ATOM   895  N N   . ASP A 1 152 ? 55.48714 39.41279  29.51996  1.000 96.18926  ? 31   ASP A N   1 
ATOM   896  C CA  . ASP A 1 152 ? 56.23734 39.61250  30.74766  1.000 96.57180  ? 31   ASP A CA  1 
ATOM   897  C C   . ASP A 1 152 ? 56.58897 41.09166  30.89141  1.000 97.16066  ? 31   ASP A C   1 
ATOM   898  O O   . ASP A 1 152 ? 56.92074 41.75053  29.89718  1.000 96.13501  ? 31   ASP A O   1 
ATOM   899  C CB  . ASP A 1 152 ? 57.50562 38.75888  30.75336  1.000 105.86582 ? 31   ASP A CB  1 
ATOM   900  C CG  . ASP A 1 152 ? 57.28028 37.38505  31.35759  1.000 110.85959 ? 31   ASP A CG  1 
ATOM   901  O OD1 . ASP A 1 152 ? 56.10651 36.98023  31.49646  1.000 106.07191 ? 31   ASP A OD1 1 
ATOM   902  O OD2 . ASP A 1 152 ? 58.27588 36.71436  31.70360  1.000 119.76586 ? 31   ASP A OD2 1 
ATOM   903  N N   . PRO A 1 153 ? 56.52320 41.64540  32.09944  1.000 95.73705  ? 32   PRO A N   1 
ATOM   904  C CA  . PRO A 1 153 ? 56.81047 43.07367  32.26882  1.000 97.57361  ? 32   PRO A CA  1 
ATOM   905  C C   . PRO A 1 153 ? 58.26205 43.39926  31.95709  1.000 113.95027 ? 32   PRO A C   1 
ATOM   906  O O   . PRO A 1 153 ? 59.17062 42.59673  32.18738  1.000 96.08036  ? 32   PRO A O   1 
ATOM   907  C CB  . PRO A 1 153 ? 56.48946 43.33311  33.74723  1.000 85.09936  ? 32   PRO A CB  1 
ATOM   908  C CG  . PRO A 1 153 ? 55.67706 42.15390  34.19464  1.000 84.00242  ? 32   PRO A CG  1 
ATOM   909  C CD  . PRO A 1 153 ? 56.11970 41.00089  33.35922  1.000 88.82987  ? 32   PRO A CD  1 
ATOM   910  N N   . VAL A 1 154 ? 58.46451 44.60013  31.41397  1.000 145.70565 ? 33   VAL A N   1 
ATOM   911  C CA  . VAL A 1 154 ? 59.77782 45.06324  30.97913  1.000 157.93529 ? 33   VAL A CA  1 
ATOM   912  C C   . VAL A 1 154 ? 60.73195 45.08162  32.16483  1.000 151.98039 ? 33   VAL A C   1 
ATOM   913  O O   . VAL A 1 154 ? 60.55870 45.86631  33.10426  1.000 162.71487 ? 33   VAL A O   1 
ATOM   914  C CB  . VAL A 1 154 ? 59.68725 46.45287  30.32314  1.000 168.48485 ? 33   VAL A CB  1 
ATOM   915  C CG1 . VAL A 1 154 ? 61.00349 46.80403  29.64555  1.000 171.37045 ? 33   VAL A CG1 1 
ATOM   916  C CG2 . VAL A 1 154 ? 58.53428 46.49409  29.32812  1.000 170.79922 ? 33   VAL A CG2 1 
ATOM   917  N N   . GLY A 1 155 ? 61.74015 44.21429  32.13115  1.000 133.86049 ? 34   GLY A N   1 
ATOM   918  C CA  . GLY A 1 155 ? 62.69021 44.12524  33.22069  1.000 126.63573 ? 34   GLY A CA  1 
ATOM   919  C C   . GLY A 1 155 ? 63.12484 42.70675  33.52422  1.000 123.97330 ? 34   GLY A C   1 
ATOM   920  O O   . GLY A 1 155 ? 63.82344 42.07780  32.72369  1.000 120.60883 ? 34   GLY A O   1 
ATOM   921  N N   . LYS A 1 156 ? 62.71775 42.19220  34.68004  1.000 130.11338 ? 35   LYS A N   1 
ATOM   922  C CA  . LYS A 1 156 ? 63.05034 40.83370  35.07885  1.000 133.21863 ? 35   LYS A CA  1 
ATOM   923  C C   . LYS A 1 156 ? 62.00482 39.84785  34.57078  1.000 127.92801 ? 35   LYS A C   1 
ATOM   924  O O   . LYS A 1 156 ? 60.82805 40.18245  34.40932  1.000 125.49120 ? 35   LYS A O   1 
ATOM   925  C CB  . LYS A 1 156 ? 63.16738 40.72926  36.60028  1.000 137.09507 ? 35   LYS A CB  1 
ATOM   926  C CG  . LYS A 1 156 ? 64.05263 39.58756  37.07526  1.000 134.40764 ? 35   LYS A CG  1 
ATOM   927  C CD  . LYS A 1 156 ? 63.37807 38.79008  38.17869  1.000 129.42908 ? 35   LYS A CD  1 
ATOM   928  C CE  . LYS A 1 156 ? 62.96938 39.68885  39.33283  1.000 129.05895 ? 35   LYS A CE  1 
ATOM   929  N NZ  . LYS A 1 156 ? 62.35353 38.91918  40.44843  1.000 123.93456 ? 35   LYS A NZ  1 
ATOM   930  N N   . LYS A 1 157 ? 62.45361 38.62442  34.31387  1.000 127.10254 ? 36   LYS A N   1 
ATOM   931  C CA  . LYS A 1 157 ? 61.59176 37.55758  33.83287  1.000 118.33306 ? 36   LYS A CA  1 
ATOM   932  C C   . LYS A 1 157 ? 61.03017 36.76703  35.00970  1.000 113.36741 ? 36   LYS A C   1 
ATOM   933  O O   . LYS A 1 157 ? 61.59478 36.74780  36.10614  1.000 118.78331 ? 36   LYS A O   1 
ATOM   934  C CB  . LYS A 1 157 ? 62.36209 36.62831  32.89363  1.000 119.20826 ? 36   LYS A CB  1 
ATOM   935  C CG  . LYS A 1 157 ? 63.18394 37.35603  31.83987  1.000 119.55287 ? 36   LYS A CG  1 
ATOM   936  C CD  . LYS A 1 157 ? 63.84441 36.38730  30.87150  1.000 119.11014 ? 36   LYS A CD  1 
ATOM   937  C CE  . LYS A 1 157 ? 64.63969 37.13510  29.81143  1.000 122.28560 ? 36   LYS A CE  1 
ATOM   938  N NZ  . LYS A 1 157 ? 65.35320 36.21408  28.88306  1.000 121.69464 ? 36   LYS A NZ  1 
ATOM   939  N N   . LEU A 1 158 ? 59.89310 36.11385  34.77061  1.000 106.88418 ? 37   LEU A N   1 
ATOM   940  C CA  . LEU A 1 158 ? 59.13990 35.48676  35.84525  1.000 101.03894 ? 37   LEU A CA  1 
ATOM   941  C C   . LEU A 1 158 ? 59.13359 33.96610  35.79877  1.000 94.77745  ? 37   LEU A C   1 
ATOM   942  O O   . LEU A 1 158 ? 58.85273 33.33866  36.82442  1.000 95.02654  ? 37   LEU A O   1 
ATOM   943  C CB  . LEU A 1 158 ? 57.69286 35.99789  35.84052  1.000 90.33416  ? 37   LEU A CB  1 
ATOM   944  C CG  . LEU A 1 158 ? 57.58452 37.52495  35.88553  1.000 88.94624  ? 37   LEU A CG  1 
ATOM   945  C CD1 . LEU A 1 158 ? 56.15490 37.98389  35.65235  1.000 83.28979  ? 37   LEU A CD1 1 
ATOM   946  C CD2 . LEU A 1 158 ? 58.11614 38.06212  37.20745  1.000 95.15072  ? 37   LEU A CD2 1 
ATOM   947  N N   . GLY A 1 159 ? 59.42441 33.36224  34.65383  1.000 87.06448  ? 38   GLY A N   1 
ATOM   948  C CA  . GLY A 1 159 ? 59.47087 31.91859  34.56741  1.000 88.05646  ? 38   GLY A CA  1 
ATOM   949  C C   . GLY A 1 159 ? 58.14423 31.35161  34.11681  1.000 90.05283  ? 38   GLY A C   1 
ATOM   950  O O   . GLY A 1 159 ? 57.20816 32.07208  33.77099  1.000 93.14998  ? 38   GLY A O   1 
ATOM   951  N N   . SER A 1 160 ? 58.06082 30.02248  34.13414  1.000 86.98713  ? 39   SER A N   1 
ATOM   952  C CA  . SER A 1 160 ? 56.80729 29.36991  33.77236  1.000 78.24138  ? 39   SER A CA  1 
ATOM   953  C C   . SER A 1 160 ? 55.73026 29.63918  34.81870  1.000 78.13316  ? 39   SER A C   1 
ATOM   954  O O   . SER A 1 160 ? 54.62014 30.07307  34.48751  1.000 67.92820  ? 39   SER A O   1 
ATOM   955  C CB  . SER A 1 160 ? 57.03472 27.87002  33.59830  1.000 79.80685  ? 39   SER A CB  1 
ATOM   956  O OG  . SER A 1 160 ? 57.89986 27.37320  34.60361  1.000 82.86567  ? 39   SER A OG  1 
ATOM   957  N N   . GLY A 1 161 ? 56.06608 29.45406  36.09617  1.000 81.98172  ? 40   GLY A N   1 
ATOM   958  C CA  . GLY A 1 161 ? 55.08769 29.67661  37.15011  1.000 95.20078  ? 40   GLY A CA  1 
ATOM   959  C C   . GLY A 1 161 ? 54.75784 31.14502  37.34838  1.000 95.19147  ? 40   GLY A C   1 
ATOM   960  O O   . GLY A 1 161 ? 53.58343 31.53150  37.37568  1.000 95.24218  ? 40   GLY A O   1 
ATOM   961  N N   . GLY A 1 162 ? 55.78613 31.97441  37.54249  1.000 85.47755  ? 41   GLY A N   1 
ATOM   962  C CA  . GLY A 1 162 ? 55.55887 33.40736  37.63926  1.000 81.13214  ? 41   GLY A CA  1 
ATOM   963  C C   . GLY A 1 162 ? 54.86095 33.98007  36.41972  1.000 81.29647  ? 41   GLY A C   1 
ATOM   964  O O   . GLY A 1 162 ? 53.99356 34.84795  36.54161  1.000 81.87595  ? 41   GLY A O   1 
ATOM   965  N N   . GLY A 1 163 ? 55.22921 33.50386  35.22751  1.000 85.25579  ? 42   GLY A N   1 
ATOM   966  C CA  . GLY A 1 163 ? 54.52988 33.91354  34.02059  1.000 86.89436  ? 42   GLY A CA  1 
ATOM   967  C C   . GLY A 1 163 ? 53.06116 33.53752  34.02681  1.000 83.23728  ? 42   GLY A C   1 
ATOM   968  O O   . GLY A 1 163 ? 52.20681 34.33973  33.64463  1.000 84.87411  ? 42   GLY A O   1 
ATOM   969  N N   . THR A 1 164 ? 52.74623 32.30891  34.44923  1.000 75.45194  ? 43   THR A N   1 
ATOM   970  C CA  . THR A 1 164 ? 51.34817 31.90197  34.54173  1.000 77.37354  ? 43   THR A CA  1 
ATOM   971  C C   . THR A 1 164 ? 50.58759 32.77825  35.52757  1.000 84.96814  ? 43   THR A C   1 
ATOM   972  O O   . THR A 1 164 ? 49.43943 33.17051  35.27288  1.000 75.98089  ? 43   THR A O   1 
ATOM   973  C CB  . THR A 1 164 ? 51.25928 30.43572  34.95668  1.000 79.07754  ? 43   THR A CB  1 
ATOM   974  O OG1 . THR A 1 164 ? 52.26109 29.67991  34.26529  1.000 86.95488  ? 43   THR A OG1 1 
ATOM   975  C CG2 . THR A 1 164 ? 49.89613 29.88231  34.62424  1.000 85.00611  ? 43   THR A CG2 1 
ATOM   976  N N   . SER A 1 165 ? 51.21163 33.08537  36.66659  1.000 84.60474  ? 44   SER A N   1 
ATOM   977  C CA  . SER A 1 165 ? 50.55469 33.92468  37.66191  1.000 94.32352  ? 44   SER A CA  1 
ATOM   978  C C   . SER A 1 165 ? 50.29889 35.31850  37.10645  1.000 93.02897  ? 44   SER A C   1 
ATOM   979  O O   . SER A 1 165 ? 49.21249 35.88119  37.28897  1.000 91.33457  ? 44   SER A O   1 
ATOM   980  C CB  . SER A 1 165 ? 51.40141 33.99722  38.93239  1.000 99.52771  ? 44   SER A CB  1 
ATOM   981  O OG  . SER A 1 165 ? 51.32719 32.78740  39.66575  1.000 107.64341 ? 44   SER A OG  1 
ATOM   982  N N   . TRP A 1 166 ? 51.29198 35.88615  36.41762  1.000 77.69741  ? 45   TRP A N   1 
ATOM   983  C CA  . TRP A 1 166 ? 51.12684 37.20169  35.80967  1.000 76.69035  ? 45   TRP A CA  1 
ATOM   984  C C   . TRP A 1 166 ? 50.04343 37.18653  34.73870  1.000 76.95703  ? 45   TRP A C   1 
ATOM   985  O O   . TRP A 1 166 ? 49.28598 38.15279  34.59904  1.000 69.99187  ? 45   TRP A O   1 
ATOM   986  C CB  . TRP A 1 166 ? 52.46350 37.66875  35.23329  1.000 68.01345  ? 45   TRP A CB  1 
ATOM   987  C CG  . TRP A 1 166 ? 52.38335 38.86528  34.33806  1.000 71.20638  ? 45   TRP A CG  1 
ATOM   988  C CD1 . TRP A 1 166 ? 52.37036 38.86582  32.97356  1.000 75.16956  ? 45   TRP A CD1 1 
ATOM   989  C CD2 . TRP A 1 166 ? 52.30977 40.23819  34.74017  1.000 78.13159  ? 45   TRP A CD2 1 
ATOM   990  N NE1 . TRP A 1 166 ? 52.29706 40.15347  32.50065  1.000 80.30283  ? 45   TRP A NE1 1 
ATOM   991  C CE2 . TRP A 1 166 ? 52.25744 41.01486  33.56533  1.000 84.68501  ? 45   TRP A CE2 1 
ATOM   992  C CE3 . TRP A 1 166 ? 52.28412 40.88622  35.97845  1.000 84.91984  ? 45   TRP A CE3 1 
ATOM   993  C CZ2 . TRP A 1 166 ? 52.17829 42.40555  33.59267  1.000 89.76564  ? 45   TRP A CZ2 1 
ATOM   994  C CZ3 . TRP A 1 166 ? 52.20594 42.26729  36.00331  1.000 88.98018  ? 45   TRP A CZ3 1 
ATOM   995  C CH2 . TRP A 1 166 ? 52.15316 43.01129  34.81839  1.000 93.70363  ? 45   TRP A CH2 1 
ATOM   996  N N   . LEU A 1 167 ? 49.93456 36.08542  33.99384  1.000 70.87325  ? 46   LEU A N   1 
ATOM   997  C CA  . LEU A 1 167 ? 48.90745 35.97972  32.96292  1.000 72.85361  ? 46   LEU A CA  1 
ATOM   998  C C   . LEU A 1 167 ? 47.51573 35.96330  33.58674  1.000 82.59008  ? 46   LEU A C   1 
ATOM   999  O O   . LEU A 1 167 ? 46.62219 36.71599  33.16979  1.000 85.12358  ? 46   LEU A O   1 
ATOM   1000 C CB  . LEU A 1 167 ? 49.16039 34.72142  32.12900  1.000 68.53692  ? 46   LEU A CB  1 
ATOM   1001 C CG  . LEU A 1 167 ? 48.37946 34.44298  30.84618  1.000 76.16338  ? 46   LEU A CG  1 
ATOM   1002 C CD1 . LEU A 1 167 ? 48.54174 35.57703  29.85303  1.000 80.51492  ? 46   LEU A CD1 1 
ATOM   1003 C CD2 . LEU A 1 167 ? 48.86043 33.13496  30.23767  1.000 56.56266  ? 46   LEU A CD2 1 
ATOM   1004 N N   . LEU A 1 168 ? 47.32484 35.12213  34.60803  1.000 76.86529  ? 47   LEU A N   1 
ATOM   1005 C CA  . LEU A 1 168 ? 46.04271 35.07499  35.30541  1.000 84.49091  ? 47   LEU A CA  1 
ATOM   1006 C C   . LEU A 1 168 ? 45.69625 36.42949  35.91150  1.000 95.68999  ? 47   LEU A C   1 
ATOM   1007 O O   . LEU A 1 168 ? 44.54408 36.87950  35.83586  1.000 101.84032 ? 47   LEU A O   1 
ATOM   1008 C CB  . LEU A 1 168 ? 46.06811 33.99544  36.38706  1.000 78.46318  ? 47   LEU A CB  1 
ATOM   1009 C CG  . LEU A 1 168 ? 46.02175 32.54356  35.91093  1.000 79.13235  ? 47   LEU A CG  1 
ATOM   1010 C CD1 . LEU A 1 168 ? 46.12230 31.60073  37.09724  1.000 62.72790  ? 47   LEU A CD1 1 
ATOM   1011 C CD2 . LEU A 1 168 ? 44.74558 32.28074  35.12404  1.000 76.50527  ? 47   LEU A CD2 1 
ATOM   1012 N N   . GLU A 1 169 ? 46.68468 37.09486  36.51398  1.000 82.81270  ? 48   GLU A N   1 
ATOM   1013 C CA  . GLU A 1 169 ? 46.44274 38.38826  37.14221  1.000 87.35068  ? 48   GLU A CA  1 
ATOM   1014 C C   . GLU A 1 169 ? 46.03432 39.42995  36.10799  1.000 91.60805  ? 48   GLU A C   1 
ATOM   1015 O O   . GLU A 1 169 ? 45.06362 40.17035  36.30764  1.000 89.34223  ? 48   GLU A O   1 
ATOM   1016 C CB  . GLU A 1 169 ? 47.68954 38.83251  37.90580  1.000 96.03070  ? 48   GLU A CB  1 
ATOM   1017 C CG  . GLU A 1 169 ? 47.42858 39.85953  38.98925  1.000 109.63432 ? 48   GLU A CG  1 
ATOM   1018 C CD  . GLU A 1 169 ? 48.54192 39.90830  40.01619  1.000 123.02863 ? 48   GLU A CD  1 
ATOM   1019 O OE1 . GLU A 1 169 ? 49.02678 38.82933  40.41942  1.000 123.13049 ? 48   GLU A OE1 1 
ATOM   1020 O OE2 . GLU A 1 169 ? 48.93625 41.02392  40.41579  1.000 127.72136 ? 48   GLU A OE2 1 
ATOM   1021 N N   . GLU A 1 170 ? 46.78992 39.52825  35.00976  1.000 84.49992  ? 49   GLU A N   1 
ATOM   1022 C CA  . GLU A 1 170 ? 46.50129 40.53730  33.99891  1.000 80.14953  ? 49   GLU A CA  1 
ATOM   1023 C C   . GLU A 1 170 ? 45.16312 40.27625  33.32645  1.000 81.49708  ? 49   GLU A C   1 
ATOM   1024 O O   . GLU A 1 170 ? 44.50924 41.21749  32.86309  1.000 90.41627  ? 49   GLU A O   1 
ATOM   1025 C CB  . GLU A 1 170 ? 47.62179 40.57652  32.96100  1.000 80.73417  ? 49   GLU A CB  1 
ATOM   1026 C CG  . GLU A 1 170 ? 48.81582 41.41575  33.37954  1.000 81.51683  ? 49   GLU A CG  1 
ATOM   1027 C CD  . GLU A 1 170 ? 48.73534 42.84122  32.86988  1.000 91.16037  ? 49   GLU A CD  1 
ATOM   1028 O OE1 . GLU A 1 170 ? 48.75886 43.03618  31.63499  1.000 99.14928  ? 49   GLU A OE1 1 
ATOM   1029 O OE2 . GLU A 1 170 ? 48.64430 43.76694  33.70298  1.000 89.53231  ? 49   GLU A OE2 1 
ATOM   1030 N N   . CYS A 1 171 ? 44.73833 39.01246  33.26654  1.000 73.37423  ? 50   CYS A N   1 
ATOM   1031 C CA  . CYS A 1 171 ? 43.41366 38.71301  32.73617  1.000 79.76240  ? 50   CYS A CA  1 
ATOM   1032 C C   . CYS A 1 171 ? 42.32357 39.15220  33.70696  1.000 86.40207  ? 50   CYS A C   1 
ATOM   1033 O O   . CYS A 1 171 ? 41.36197 39.83254  33.31663  1.000 86.72542  ? 50   CYS A O   1 
ATOM   1034 C CB  . CYS A 1 171 ? 43.29704 37.22146  32.43853  1.000 73.77081  ? 50   CYS A CB  1 
ATOM   1035 S SG  . CYS A 1 171 ? 41.84120 36.79746  31.47805  1.000 80.48164  ? 50   CYS A SG  1 
ATOM   1036 N N   . TYR A 1 172 ? 42.44730 38.74510  34.97493  1.000 92.23463  ? 51   TYR A N   1 
ATOM   1037 C CA  . TYR A 1 172 ? 41.49535 39.16724  35.99748  1.000 94.64093  ? 51   TYR A CA  1 
ATOM   1038 C C   . TYR A 1 172 ? 41.35426 40.68375  36.03659  1.000 95.94667  ? 51   TYR A C   1 
ATOM   1039 O O   . TYR A 1 172 ? 40.24099 41.20901  36.14036  1.000 89.78638  ? 51   TYR A O   1 
ATOM   1040 C CB  . TYR A 1 172 ? 41.92604 38.63097  37.36466  1.000 93.29063  ? 51   TYR A CB  1 
ATOM   1041 C CG  . TYR A 1 172 ? 41.31525 39.36760  38.53540  1.000 105.46933 ? 51   TYR A CG  1 
ATOM   1042 C CD1 . TYR A 1 172 ? 40.03530 39.06029  38.98201  1.000 102.90500 ? 51   TYR A CD1 1 
ATOM   1043 C CD2 . TYR A 1 172 ? 42.01971 40.36485  39.20056  1.000 102.31369 ? 51   TYR A CD2 1 
ATOM   1044 C CE1 . TYR A 1 172 ? 39.47313 39.72696  40.05379  1.000 100.53583 ? 51   TYR A CE1 1 
ATOM   1045 C CE2 . TYR A 1 172 ? 41.46210 41.04031  40.27206  1.000 111.16839 ? 51   TYR A CE2 1 
ATOM   1046 C CZ  . TYR A 1 172 ? 40.18923 40.71585  40.69441  1.000 102.84976 ? 51   TYR A CZ  1 
ATOM   1047 O OH  . TYR A 1 172 ? 39.62947 41.38419  41.75890  1.000 107.58926 ? 51   TYR A OH  1 
ATOM   1048 N N   . ASN A 1 173 ? 42.47191 41.40573  35.93512  1.000 106.72101 ? 52   ASN A N   1 
ATOM   1049 C CA  . ASN A 1 173 ? 42.44070 42.86036  36.02871  1.000 111.03590 ? 52   ASN A CA  1 
ATOM   1050 C C   . ASN A 1 173 ? 41.68415 43.51841  34.88285  1.000 114.99763 ? 52   ASN A C   1 
ATOM   1051 O O   . ASN A 1 173 ? 41.42116 44.72350  34.95271  1.000 119.45008 ? 52   ASN A O   1 
ATOM   1052 C CB  . ASN A 1 173 ? 43.86685 43.41061  36.08261  1.000 116.17692 ? 52   ASN A CB  1 
ATOM   1053 C CG  . ASN A 1 173 ? 44.48899 43.28088  37.45779  1.000 124.75847 ? 52   ASN A CG  1 
ATOM   1054 O OD1 . ASN A 1 173 ? 44.42107 44.20119  38.27204  1.000 130.66801 ? 52   ASN A OD1 1 
ATOM   1055 N ND2 . ASN A 1 173 ? 45.09868 42.13249  37.72490  1.000 125.05432 ? 52   ASN A ND2 1 
ATOM   1056 N N   . GLU A 1 174 ? 41.32730 42.76990  33.83784  1.000 115.30493 ? 53   GLU A N   1 
ATOM   1057 C CA  . GLU A 1 174 ? 40.53506 43.31508  32.74724  1.000 113.28654 ? 53   GLU A CA  1 
ATOM   1058 C C   . GLU A 1 174 ? 39.14177 42.71159  32.63906  1.000 102.85134 ? 53   GLU A C   1 
ATOM   1059 O O   . GLU A 1 174 ? 38.25432 43.35571  32.07082  1.000 101.53044 ? 53   GLU A O   1 
ATOM   1060 C CB  . GLU A 1 174 ? 41.26971 43.13225  31.40911  1.000 111.61266 ? 53   GLU A CB  1 
ATOM   1061 C CG  . GLU A 1 174 ? 40.62280 43.86107  30.23793  1.000 113.03526 ? 53   GLU A CG  1 
ATOM   1062 C CD  . GLU A 1 174 ? 41.51506 43.92464  29.01823  1.000 121.11203 ? 53   GLU A CD  1 
ATOM   1063 O OE1 . GLU A 1 174 ? 42.67664 44.36338  29.15467  1.000 123.41366 ? 53   GLU A OE1 1 
ATOM   1064 O OE2 . GLU A 1 174 ? 41.05446 43.54047  27.92233  1.000 125.66358 ? 53   GLU A OE2 1 
ATOM   1065 N N   . TYR A 1 175 ? 38.91123 41.51601  33.18837  1.000 98.09958  ? 54   TYR A N   1 
ATOM   1066 C CA  . TYR A 1 175 ? 37.58021 40.91583  33.13772  1.000 98.96807  ? 54   TYR A CA  1 
ATOM   1067 C C   . TYR A 1 175 ? 36.97511 40.67488  34.51918  1.000 99.35731  ? 54   TYR A C   1 
ATOM   1068 O O   . TYR A 1 175 ? 36.06321 39.85231  34.64919  1.000 87.97853  ? 54   TYR A O   1 
ATOM   1069 C CB  . TYR A 1 175 ? 37.60594 39.60824  32.34137  1.000 93.15449  ? 54   TYR A CB  1 
ATOM   1070 C CG  . TYR A 1 175 ? 38.20247 39.73560  30.95804  1.000 92.26366  ? 54   TYR A CG  1 
ATOM   1071 C CD1 . TYR A 1 175 ? 37.40815 40.06743  29.86781  1.000 87.53995  ? 54   TYR A CD1 1 
ATOM   1072 C CD2 . TYR A 1 175 ? 39.55657 39.51861  30.73943  1.000 88.32396  ? 54   TYR A CD2 1 
ATOM   1073 C CE1 . TYR A 1 175 ? 37.94730 40.18539  28.59946  1.000 96.77758  ? 54   TYR A CE1 1 
ATOM   1074 C CE2 . TYR A 1 175 ? 40.10447 39.63444  29.47537  1.000 82.94466  ? 54   TYR A CE2 1 
ATOM   1075 C CZ  . TYR A 1 175 ? 39.29683 39.96721  28.40950  1.000 92.85195  ? 54   TYR A CZ  1 
ATOM   1076 O OH  . TYR A 1 175 ? 39.84158 40.08008  27.15059  1.000 93.23038  ? 54   TYR A OH  1 
ATOM   1077 N N   . SER A 1 176 ? 37.45930 41.36584  35.55651  1.000 100.16861 ? 55   SER A N   1 
ATOM   1078 C CA  . SER A 1 176 ? 36.96431 41.10064  36.90672  1.000 99.96872  ? 55   SER A CA  1 
ATOM   1079 C C   . SER A 1 176 ? 35.49412 41.47597  37.04759  1.000 105.40829 ? 55   SER A C   1 
ATOM   1080 O O   . SER A 1 176 ? 34.71535 40.73724  37.66256  1.000 101.20185 ? 55   SER A O   1 
ATOM   1081 C CB  . SER A 1 176 ? 37.79645 41.86025  37.93889  1.000 103.13118 ? 55   SER A CB  1 
ATOM   1082 O OG  . SER A 1 176 ? 37.48623 43.24294  37.92429  1.000 112.29479 ? 55   SER A OG  1 
ATOM   1083 N N   . ASP A 1 177 ? 35.10111 42.61965  36.48349  1.000 100.62902 ? 56   ASP A N   1 
ATOM   1084 C CA  . ASP A 1 177 ? 33.72762 43.12299  36.56352  1.000 111.79670 ? 56   ASP A CA  1 
ATOM   1085 C C   . ASP A 1 177 ? 33.25587 43.24829  38.01321  1.000 112.27514 ? 56   ASP A C   1 
ATOM   1086 O O   . ASP A 1 177 ? 32.08794 43.01416  38.32894  1.000 106.65153 ? 56   ASP A O   1 
ATOM   1087 C CB  . ASP A 1 177 ? 32.76766 42.25265  35.74862  1.000 109.68554 ? 56   ASP A CB  1 
ATOM   1088 C CG  . ASP A 1 177 ? 31.55016 43.02117  35.26933  1.000 112.35111 ? 56   ASP A CG  1 
ATOM   1089 O OD1 . ASP A 1 177 ? 31.52563 44.25832  35.43749  1.000 113.75834 ? 56   ASP A OD1 1 
ATOM   1090 O OD2 . ASP A 1 177 ? 30.61715 42.39208  34.72798  1.000 110.09125 ? 56   ASP A OD2 1 
ATOM   1091 N N   . GLY A 1 178 ? 34.17603 43.61232  38.90679  1.000 111.99061 ? 57   GLY A N   1 
ATOM   1092 C CA  . GLY A 1 178 ? 33.86111 43.84889  40.29825  1.000 123.11479 ? 57   GLY A CA  1 
ATOM   1093 C C   . GLY A 1 178 ? 34.07442 42.67356  41.22968  1.000 124.03147 ? 57   GLY A C   1 
ATOM   1094 O O   . GLY A 1 178 ? 34.24760 42.88533  42.43568  1.000 124.39822 ? 57   GLY A O   1 
ATOM   1095 N N   . ALA A 1 179 ? 34.05168 41.44544  40.71735  1.000 115.99493 ? 58   ALA A N   1 
ATOM   1096 C CA  . ALA A 1 179 ? 34.25045 40.27621  41.55941  1.000 107.48449 ? 58   ALA A CA  1 
ATOM   1097 C C   . ALA A 1 179 ? 35.65481 40.28152  42.16683  1.000 110.53808 ? 58   ALA A C   1 
ATOM   1098 O O   . ALA A 1 179 ? 36.51589 41.09434  41.81922  1.000 110.33478 ? 58   ALA A O   1 
ATOM   1099 C CB  . ALA A 1 179 ? 34.02222 38.99444  40.75912  1.000 95.90135  ? 58   ALA A CB  1 
ATOM   1100 N N   . THR A 1 180 ? 35.87879 39.35491  43.09233  1.000 102.40124 ? 59   THR A N   1 
ATOM   1101 C CA  . THR A 1 180 ? 37.21646 39.12801  43.61234  1.000 110.32723 ? 59   THR A CA  1 
ATOM   1102 C C   . THR A 1 180 ? 37.93084 38.10547  42.73392  1.000 104.30315 ? 59   THR A C   1 
ATOM   1103 O O   . THR A 1 180 ? 37.34873 37.52822  41.81365  1.000 90.46138  ? 59   THR A O   1 
ATOM   1104 C CB  . THR A 1 180 ? 37.16633 38.65274  45.06450  1.000 112.58971 ? 59   THR A CB  1 
ATOM   1105 O OG1 . THR A 1 180 ? 36.52055 37.37577  45.13210  1.000 115.52269 ? 59   THR A OG1 1 
ATOM   1106 C CG2 . THR A 1 180 ? 36.40063 39.64934  45.92258  1.000 112.85756 ? 59   THR A CG2 1 
ATOM   1107 N N   . PHE A 1 181 ? 39.21377 37.88141  43.02167  1.000 113.09922 ? 60   PHE A N   1 
ATOM   1108 C CA  . PHE A 1 181 ? 39.99306 36.98821  42.17057  1.000 116.90055 ? 60   PHE A CA  1 
ATOM   1109 C C   . PHE A 1 181 ? 39.49531 35.55116  42.27229  1.000 114.03255 ? 60   PHE A C   1 
ATOM   1110 O O   . PHE A 1 181 ? 39.32875 34.86802  41.25371  1.000 112.36190 ? 60   PHE A O   1 
ATOM   1111 C CB  . PHE A 1 181 ? 41.47843 37.06544  42.51664  1.000 122.25876 ? 60   PHE A CB  1 
ATOM   1112 C CG  . PHE A 1 181 ? 42.32690 36.18014  41.65647  1.000 120.34955 ? 60   PHE A CG  1 
ATOM   1113 C CD1 . PHE A 1 181 ? 42.80165 36.64178  40.44124  1.000 111.97274 ? 60   PHE A CD1 1 
ATOM   1114 C CD2 . PHE A 1 181 ? 42.62448 34.88268  42.04002  1.000 114.88770 ? 60   PHE A CD2 1 
ATOM   1115 C CE1 . PHE A 1 181 ? 43.56512 35.83606  39.63123  1.000 109.22508 ? 60   PHE A CE1 1 
ATOM   1116 C CE2 . PHE A 1 181 ? 43.38853 34.07067  41.23115  1.000 115.05577 ? 60   PHE A CE2 1 
ATOM   1117 C CZ  . PHE A 1 181 ? 43.85593 34.54879  40.02339  1.000 111.34559 ? 60   PHE A CZ  1 
ATOM   1118 N N   . GLY A 1 182 ? 39.26648 35.06959  43.49580  1.000 109.53175 ? 61   GLY A N   1 
ATOM   1119 C CA  . GLY A 1 182 ? 38.79351 33.70711  43.66420  1.000 103.33244 ? 61   GLY A CA  1 
ATOM   1120 C C   . GLY A 1 182 ? 37.43074 33.48292  43.04396  1.000 99.99186  ? 61   GLY A C   1 
ATOM   1121 O O   . GLY A 1 182 ? 37.14440 32.39441  42.53809  1.000 93.10474  ? 61   GLY A O   1 
ATOM   1122 N N   . GLU A 1 183 ? 36.57694 34.50752  43.06409  1.000 111.29283 ? 62   GLU A N   1 
ATOM   1123 C CA  . GLU A 1 183 ? 35.27570 34.39773  42.41612  1.000 117.79433 ? 62   GLU A CA  1 
ATOM   1124 C C   . GLU A 1 183 ? 35.42148 34.42038  40.90137  1.000 109.87776 ? 62   GLU A C   1 
ATOM   1125 O O   . GLU A 1 183 ? 34.75248 33.65689  40.19586  1.000 101.52420 ? 62   GLU A O   1 
ATOM   1126 C CB  . GLU A 1 183 ? 34.35893 35.52891  42.88204  1.000 123.20850 ? 62   GLU A CB  1 
ATOM   1127 C CG  . GLU A 1 183 ? 34.07056 35.52777  44.37236  1.000 130.47711 ? 62   GLU A CG  1 
ATOM   1128 C CD  . GLU A 1 183 ? 33.20880 36.70118  44.79648  1.000 133.95892 ? 62   GLU A CD  1 
ATOM   1129 O OE1 . GLU A 1 183 ? 33.08448 37.66424  44.01043  1.000 129.63704 ? 62   GLU A OE1 1 
ATOM   1130 O OE2 . GLU A 1 183 ? 32.65551 36.66123  45.91533  1.000 140.59166 ? 62   GLU A OE2 1 
ATOM   1131 N N   . TRP A 1 184 ? 36.28740 35.29688  40.38573  1.000 105.11337 ? 63   TRP A N   1 
ATOM   1132 C CA  . TRP A 1 184 ? 36.49498 35.37988  38.94382  1.000 100.05187 ? 63   TRP A CA  1 
ATOM   1133 C C   . TRP A 1 184 ? 37.05192 34.07940  38.37789  1.000 92.54429  ? 63   TRP A C   1 
ATOM   1134 O O   . TRP A 1 184 ? 36.65073 33.65019  37.29000  1.000 80.36622  ? 63   TRP A O   1 
ATOM   1135 C CB  . TRP A 1 184 ? 37.42541 36.54627  38.61341  1.000 108.92437 ? 63   TRP A CB  1 
ATOM   1136 C CG  . TRP A 1 184 ? 37.92997 36.52179  37.20001  1.000 104.41871 ? 63   TRP A CG  1 
ATOM   1137 C CD1 . TRP A 1 184 ? 37.31214 37.03587  36.09701  1.000 93.45831  ? 63   TRP A CD1 1 
ATOM   1138 C CD2 . TRP A 1 184 ? 39.16598 35.95718  36.74109  1.000 105.71929 ? 63   TRP A CD2 1 
ATOM   1139 N NE1 . TRP A 1 184 ? 38.08348 36.82066  34.97950  1.000 95.66817  ? 63   TRP A NE1 1 
ATOM   1140 C CE2 . TRP A 1 184 ? 39.22728 36.16187  35.34853  1.000 102.23579 ? 63   TRP A CE2 1 
ATOM   1141 C CE3 . TRP A 1 184 ? 40.22447 35.29636  37.37308  1.000 101.90177 ? 63   TRP A CE3 1 
ATOM   1142 C CZ2 . TRP A 1 184 ? 40.30548 35.73047  34.57728  1.000 95.94123  ? 63   TRP A CZ2 1 
ATOM   1143 C CZ3 . TRP A 1 184 ? 41.29382 34.86894  36.60582  1.000 108.11242 ? 63   TRP A CZ3 1 
ATOM   1144 C CH2 . TRP A 1 184 ? 41.32604 35.08757  35.22279  1.000 99.70033  ? 63   TRP A CH2 1 
ATOM   1145 N N   . LEU A 1 185 ? 37.97572 33.43438  39.09774  1.000 92.41001  ? 64   LEU A N   1 
ATOM   1146 C CA  . LEU A 1 185 ? 38.60894 32.23741  38.55001  1.000 95.27475  ? 64   LEU A CA  1 
ATOM   1147 C C   . LEU A 1 185 ? 37.62537 31.07840  38.42284  1.000 108.48444 ? 64   LEU A C   1 
ATOM   1148 O O   . LEU A 1 185 ? 37.75477 30.25869  37.50577  1.000 102.37316 ? 64   LEU A O   1 
ATOM   1149 C CB  . LEU A 1 185 ? 39.80759 31.82663  39.40416  1.000 101.54791 ? 64   LEU A CB  1 
ATOM   1150 C CG  . LEU A 1 185 ? 40.80797 30.90659  38.69521  1.000 105.50249 ? 64   LEU A CG  1 
ATOM   1151 C CD1 . LEU A 1 185 ? 42.09288 31.65118  38.36400  1.000 99.01999  ? 64   LEU A CD1 1 
ATOM   1152 C CD2 . LEU A 1 185 ? 41.10480 29.67054  39.53297  1.000 101.53545 ? 64   LEU A CD2 1 
ATOM   1153 N N   . GLU A 1 186 ? 36.64080 30.99529  39.32390  1.000 106.50217 ? 65   GLU A N   1 
ATOM   1154 C CA  . GLU A 1 186 ? 35.66320 29.90984  39.27613  1.000 98.32417  ? 65   GLU A CA  1 
ATOM   1155 C C   . GLU A 1 186 ? 34.84376 29.91501  37.99141  1.000 96.60813  ? 65   GLU A C   1 
ATOM   1156 O O   . GLU A 1 186 ? 34.33993 28.86463  37.57662  1.000 92.86248  ? 65   GLU A O   1 
ATOM   1157 C CB  . GLU A 1 186 ? 34.71160 29.99576  40.46918  1.000 117.40294 ? 65   GLU A CB  1 
ATOM   1158 C CG  . GLU A 1 186 ? 35.33459 29.74433  41.82295  1.000 124.72099 ? 65   GLU A CG  1 
ATOM   1159 C CD  . GLU A 1 186 ? 34.33024 29.91602  42.94417  1.000 123.84907 ? 65   GLU A CD  1 
ATOM   1160 O OE1 . GLU A 1 186 ? 33.39182 30.72362  42.77739  1.000 122.66836 ? 65   GLU A OE1 1 
ATOM   1161 O OE2 . GLU A 1 186 ? 34.47636 29.24831  43.98833  1.000 129.59775 ? 65   GLU A OE2 1 
ATOM   1162 N N   . LYS A 1 187 ? 34.69669 31.07671  37.35187  1.000 99.45853  ? 66   LYS A N   1 
ATOM   1163 C CA  . LYS A 1 187 ? 33.61391 31.26513  36.39059  1.000 96.93510  ? 66   LYS A CA  1 
ATOM   1164 C C   . LYS A 1 187 ? 33.83312 30.48098  35.09977  1.000 98.16096  ? 66   LYS A C   1 
ATOM   1165 O O   . LYS A 1 187 ? 32.91391 29.81038  34.61588  1.000 108.79552 ? 66   LYS A O   1 
ATOM   1166 C CB  . LYS A 1 187 ? 33.42656 32.75714  36.11140  1.000 101.25539 ? 66   LYS A CB  1 
ATOM   1167 C CG  . LYS A 1 187 ? 33.13342 33.54936  37.37972  1.000 112.73472 ? 66   LYS A CG  1 
ATOM   1168 C CD  . LYS A 1 187 ? 32.67637 34.97100  37.09945  1.000 120.21314 ? 66   LYS A CD  1 
ATOM   1169 C CE  . LYS A 1 187 ? 32.28614 35.67141  38.39579  1.000 131.00798 ? 66   LYS A CE  1 
ATOM   1170 N NZ  . LYS A 1 187 ? 31.83816 37.07609  38.18455  1.000 137.14414 ? 66   LYS A NZ  1 
ATOM   1171 N N   . GLU A 1 188 ? 35.02941 30.54482  34.51941  1.000 99.27833  ? 67   GLU A N   1 
ATOM   1172 C CA  . GLU A 1 188 ? 35.24339 29.94275  33.21120  1.000 103.19171 ? 67   GLU A CA  1 
ATOM   1173 C C   . GLU A 1 188 ? 36.42809 28.98822  33.21713  1.000 96.91769  ? 67   GLU A C   1 
ATOM   1174 O O   . GLU A 1 188 ? 37.34915 29.10327  34.03180  1.000 78.90110  ? 67   GLU A O   1 
ATOM   1175 C CB  . GLU A 1 188 ? 35.46983 31.01005  32.13392  1.000 101.29977 ? 67   GLU A CB  1 
ATOM   1176 C CG  . GLU A 1 188 ? 34.19649 31.66941  31.64415  1.000 117.81810 ? 67   GLU A CG  1 
ATOM   1177 C CD  . GLU A 1 188 ? 34.41410 33.10921  31.23138  1.000 127.82798 ? 67   GLU A CD  1 
ATOM   1178 O OE1 . GLU A 1 188 ? 35.54885 33.60586  31.39203  1.000 122.93480 ? 67   GLU A OE1 1 
ATOM   1179 O OE2 . GLU A 1 188 ? 33.45348 33.74114  30.74322  1.000 130.22748 ? 67   GLU A OE2 1 
ATOM   1180 N N   . LYS A 1 189 ? 36.38130 28.04004  32.28499  1.000 87.08757  ? 68   LYS A N   1 
ATOM   1181 C CA  . LYS A 1 189 ? 37.54948 27.26223  31.90755  1.000 83.11007  ? 68   LYS A CA  1 
ATOM   1182 C C   . LYS A 1 189 ? 38.40361 28.07521  30.94204  1.000 84.40387  ? 68   LYS A C   1 
ATOM   1183 O O   . LYS A 1 189 ? 37.88454 28.73437  30.03770  1.000 73.49216  ? 68   LYS A O   1 
ATOM   1184 C CB  . LYS A 1 189 ? 37.12209 25.94121  31.26942  1.000 82.74290  ? 68   LYS A CB  1 
ATOM   1185 C CG  . LYS A 1 189 ? 36.73640 24.87354  32.27981  1.000 94.29077  ? 68   LYS A CG  1 
ATOM   1186 C CD  . LYS A 1 189 ? 36.04515 23.70285  31.60256  1.000 92.49315  ? 68   LYS A CD  1 
ATOM   1187 C CE  . LYS A 1 189 ? 35.75619 22.58469  32.58993  1.000 91.83126  ? 68   LYS A CE  1 
ATOM   1188 N NZ  . LYS A 1 189 ? 36.98188 22.17367  33.33105  1.000 96.50697  ? 68   LYS A NZ  1 
ATOM   1189 N N   . ARG A 1 190 ? 39.71483 28.05943  31.15978  1.000 67.41708  ? 69   ARG A N   1 
ATOM   1190 C CA  . ARG A 1 190 ? 40.62173 28.93733  30.43621  1.000 77.11536  ? 69   ARG A CA  1 
ATOM   1191 C C   . ARG A 1 190 ? 41.87661 28.17656  30.03778  1.000 68.66553  ? 69   ARG A C   1 
ATOM   1192 O O   . ARG A 1 190 ? 42.38132 27.35197  30.80509  1.000 79.10100  ? 69   ARG A O   1 
ATOM   1193 C CB  . ARG A 1 190 ? 40.96860 30.17084  31.27628  1.000 82.90632  ? 69   ARG A CB  1 
ATOM   1194 C CG  . ARG A 1 190 ? 39.94281 31.28282  31.13358  1.000 86.70315  ? 69   ARG A CG  1 
ATOM   1195 C CD  . ARG A 1 190 ? 40.19530 32.42447  32.09163  1.000 91.43514  ? 69   ARG A CD  1 
ATOM   1196 N NE  . ARG A 1 190 ? 39.86168 32.04315  33.45776  1.000 99.05636  ? 69   ARG A NE  1 
ATOM   1197 C CZ  . ARG A 1 190 ? 38.80379 32.49921  34.11683  1.000 93.18909  ? 69   ARG A CZ  1 
ATOM   1198 N NH1 . ARG A 1 190 ? 38.57285 32.09468  35.35357  1.000 93.48837  ? 69   ARG A NH1 1 
ATOM   1199 N NH2 . ARG A 1 190 ? 37.97745 33.35898  33.53787  1.000 111.30250 ? 69   ARG A NH2 1 
ATOM   1200 N N   . ILE A 1 191 ? 42.36309 28.45907  28.83128  1.000 76.38012  ? 70   ILE A N   1 
ATOM   1201 C CA  . ILE A 1 191 ? 43.52571 27.79421  28.25114  1.000 80.51343  ? 70   ILE A CA  1 
ATOM   1202 C C   . ILE A 1 191 ? 44.64632 28.81790  28.14888  1.000 74.98348  ? 70   ILE A C   1 
ATOM   1203 O O   . ILE A 1 191 ? 44.51361 29.81881  27.43573  1.000 66.61286  ? 70   ILE A O   1 
ATOM   1204 C CB  . ILE A 1 191 ? 43.20426 27.20123  26.87059  1.000 76.39154  ? 70   ILE A CB  1 
ATOM   1205 C CG1 . ILE A 1 191 ? 42.15697 26.09296  26.99424  1.000 76.44248  ? 70   ILE A CG1 1 
ATOM   1206 C CG2 . ILE A 1 191 ? 44.46907 26.68913  26.20080  1.000 63.45233  ? 70   ILE A CG2 1 
ATOM   1207 C CD1 . ILE A 1 191 ? 41.46870 25.75584  25.68633  1.000 71.76523  ? 70   ILE A CD1 1 
ATOM   1208 N N   . LEU A 1 192 ? 45.75055 28.57150  28.84868  1.000 66.17573  ? 71   LEU A N   1 
ATOM   1209 C CA  . LEU A 1 192 ? 46.86576 29.50195  28.92025  1.000 60.03065  ? 71   LEU A CA  1 
ATOM   1210 C C   . LEU A 1 192 ? 48.03165 28.91753  28.13768  1.000 77.32114  ? 71   LEU A C   1 
ATOM   1211 O O   . LEU A 1 192 ? 48.39254 27.75360  28.33668  1.000 72.36793  ? 71   LEU A O   1 
ATOM   1212 C CB  . LEU A 1 192 ? 47.29836 29.76029  30.36814  1.000 59.19000  ? 71   LEU A CB  1 
ATOM   1213 C CG  . LEU A 1 192 ? 46.33841 29.81656  31.56190  1.000 65.42546  ? 71   LEU A CG  1 
ATOM   1214 C CD1 . LEU A 1 192 ? 46.97614 30.61424  32.68435  1.000 61.85106  ? 71   LEU A CD1 1 
ATOM   1215 C CD2 . LEU A 1 192 ? 44.97532 30.39866  31.22965  1.000 82.14405  ? 71   LEU A CD2 1 
ATOM   1216 N N   . LEU A 1 193 ? 48.59244 29.71111  27.23163  1.000 64.25936  ? 72   LEU A N   1 
ATOM   1217 C CA  . LEU A 1 193 ? 49.69402 29.28445  26.38061  1.000 71.55183  ? 72   LEU A CA  1 
ATOM   1218 C C   . LEU A 1 193 ? 50.89035 30.18783  26.62308  1.000 58.12141  ? 72   LEU A C   1 
ATOM   1219 O O   . LEU A 1 193 ? 50.76916 31.41544  26.53605  1.000 56.90905  ? 72   LEU A O   1 
ATOM   1220 C CB  . LEU A 1 193 ? 49.31025 29.32792  24.90007  1.000 80.69856  ? 72   LEU A CB  1 
ATOM   1221 C CG  . LEU A 1 193 ? 48.72712 28.07249  24.25469  1.000 92.13144  ? 72   LEU A CG  1 
ATOM   1222 C CD1 . LEU A 1 193 ? 47.22145 28.20911  24.07948  1.000 77.30827  ? 72   LEU A CD1 1 
ATOM   1223 C CD2 . LEU A 1 193 ? 49.41221 27.81100  22.91963  1.000 80.42930  ? 72   LEU A CD2 1 
ATOM   1224 N N   . HIS A 1 194 ? 52.03925 29.58046  26.91308  1.000 66.28938  ? 73   HIS A N   1 
ATOM   1225 C CA  . HIS A 1 194 ? 53.30001 30.30936  27.01208  1.000 62.94799  ? 73   HIS A CA  1 
ATOM   1226 C C   . HIS A 1 194 ? 53.99254 30.29047  25.65459  1.000 63.36482  ? 73   HIS A C   1 
ATOM   1227 O O   . HIS A 1 194 ? 54.40928 29.23160  25.17177  1.000 70.49336  ? 73   HIS A O   1 
ATOM   1228 C CB  . HIS A 1 194 ? 54.18192 29.70649  28.10016  1.000 64.94042  ? 73   HIS A CB  1 
ATOM   1229 C CG  . HIS A 1 194 ? 53.63050 29.87869  29.48121  1.000 78.27068  ? 73   HIS A CG  1 
ATOM   1230 N ND1 . HIS A 1 194 ? 53.39343 31.11716  30.03835  1.000 71.01701  ? 73   HIS A ND1 1 
ATOM   1231 C CD2 . HIS A 1 194 ? 53.26017 28.96946  30.41392  1.000 74.16494  ? 73   HIS A CD2 1 
ATOM   1232 C CE1 . HIS A 1 194 ? 52.90884 30.96371  31.25769  1.000 76.89804  ? 73   HIS A CE1 1 
ATOM   1233 N NE2 . HIS A 1 194 ? 52.81842 29.67022  31.50994  1.000 77.59073  ? 73   HIS A NE2 1 
ATOM   1234 N N   . ALA A 1 195 ? 54.10806 31.46527  25.03885  1.000 66.98287  ? 74   ALA A N   1 
ATOM   1235 C CA  . ALA A 1 195 ? 54.80711 31.60152  23.76838  1.000 53.71325  ? 74   ALA A CA  1 
ATOM   1236 C C   . ALA A 1 195 ? 55.47402 32.96829  23.68971  1.000 57.74269  ? 74   ALA A C   1 
ATOM   1237 O O   . ALA A 1 195 ? 55.43532 33.63702  22.65166  1.000 68.32953  ? 74   ALA A O   1 
ATOM   1238 C CB  . ALA A 1 195 ? 53.86067 31.39054  22.58449  1.000 59.24415  ? 74   ALA A CB  1 
ATOM   1239 N N   . GLY A 1 196 ? 56.09849 33.39600  24.78618  1.000 56.56069  ? 75   GLY A N   1 
ATOM   1240 C CA  . GLY A 1 196 ? 56.67573 34.72199  24.87909  1.000 60.40776  ? 75   GLY A CA  1 
ATOM   1241 C C   . GLY A 1 196 ? 58.18466 34.78649  24.93438  1.000 59.79525  ? 75   GLY A C   1 
ATOM   1242 O O   . GLY A 1 196 ? 58.73201 35.87448  25.16300  1.000 58.54374  ? 75   GLY A O   1 
ATOM   1243 N N   . GLY A 1 197 ? 58.88367 33.67423  24.73763  1.000 60.76840  ? 76   GLY A N   1 
ATOM   1244 C CA  . GLY A 1 197 ? 60.32773 33.66191  24.80140  1.000 61.42269  ? 76   GLY A CA  1 
ATOM   1245 C C   . GLY A 1 197 ? 60.96067 34.37817  23.61822  1.000 64.91856  ? 76   GLY A C   1 
ATOM   1246 O O   . GLY A 1 197 ? 60.31036 35.07029  22.83393  1.000 66.45246  ? 76   GLY A O   1 
ATOM   1247 N N   . GLN A 1 198 ? 62.27632 34.18614  23.48972  1.000 80.30640  ? 77   GLN A N   1 
ATOM   1248 C CA  . GLN A 1 198 ? 63.04332 34.85711  22.44863  1.000 56.66329  ? 77   GLN A CA  1 
ATOM   1249 C C   . GLN A 1 198 ? 63.10178 34.06541  21.15142  1.000 57.87975  ? 77   GLN A C   1 
ATOM   1250 O O   . GLN A 1 198 ? 63.39148 34.65247  20.10165  1.000 53.04502  ? 77   GLN A O   1 
ATOM   1251 C CB  . GLN A 1 198 ? 64.47326 35.13826  22.92625  1.000 57.15905  ? 77   GLN A CB  1 
ATOM   1252 C CG  . GLN A 1 198 ? 64.58772 36.02461  24.15890  1.000 53.40567  ? 77   GLN A CG  1 
ATOM   1253 C CD  . GLN A 1 198 ? 66.01918 36.10595  24.67377  1.000 68.04006  ? 77   GLN A CD  1 
ATOM   1254 O OE1 . GLN A 1 198 ? 66.48375 35.21390  25.38248  1.000 68.20939  ? 77   GLN A OE1 1 
ATOM   1255 N NE2 . GLN A 1 198 ? 66.72907 37.16686  24.29940  1.000 63.71166  ? 77   GLN A NE2 1 
ATOM   1256 N N   . SER A 1 199 ? 62.83462 32.75929  21.20075  1.000 54.75669  ? 78   SER A N   1 
ATOM   1257 C CA  . SER A 1 199 ? 62.89057 31.88660  20.02590  1.000 67.43893  ? 78   SER A CA  1 
ATOM   1258 C C   . SER A 1 199 ? 64.21664 32.04189  19.28421  1.000 60.05092  ? 78   SER A C   1 
ATOM   1259 O O   . SER A 1 199 ? 64.26155 32.30292  18.07994  1.000 57.35319  ? 78   SER A O   1 
ATOM   1260 C CB  . SER A 1 199 ? 61.70591 32.15427  19.09658  1.000 59.75014  ? 78   SER A CB  1 
ATOM   1261 O OG  . SER A 1 199 ? 60.48028 31.99718  19.79089  1.000 64.75287  ? 78   SER A OG  1 
ATOM   1262 N N   . ARG A 1 200 ? 65.30973 31.89343  20.03640  1.000 60.16934  ? 79   ARG A N   1 
ATOM   1263 C CA  . ARG A 1 200 ? 66.64971 32.05909  19.47789  1.000 49.74563  ? 79   ARG A CA  1 
ATOM   1264 C C   . ARG A 1 200 ? 66.87832 31.15346  18.27452  1.000 50.03035  ? 79   ARG A C   1 
ATOM   1265 O O   . ARG A 1 200 ? 67.46670 31.57595  17.27324  1.000 46.71995  ? 79   ARG A O   1 
ATOM   1266 C CB  . ARG A 1 200 ? 67.69313 31.76827  20.55196  1.000 53.80892  ? 79   ARG A CB  1 
ATOM   1267 C CG  . ARG A 1 200 ? 67.87404 32.88501  21.55299  1.000 59.08293  ? 79   ARG A CG  1 
ATOM   1268 C CD  . ARG A 1 200 ? 68.68696 32.41100  22.73965  1.000 57.87007  ? 79   ARG A CD  1 
ATOM   1269 N NE  . ARG A 1 200 ? 68.70351 33.40573  23.80425  1.000 60.33762  ? 79   ARG A NE  1 
ATOM   1270 C CZ  . ARG A 1 200 ? 69.75813 34.15191  24.10588  1.000 61.46916  ? 79   ARG A CZ  1 
ATOM   1271 N NH1 . ARG A 1 200 ? 70.88849 33.99779  23.43052  1.000 59.66295  ? 79   ARG A NH1 1 
ATOM   1272 N NH2 . ARG A 1 200 ? 69.68556 35.04000  25.08939  1.000 56.83570  ? 79   ARG A NH2 1 
ATOM   1273 N N   . ARG A 1 201 ? 66.42929 29.90512  18.35777  1.000 54.08654  ? 80   ARG A N   1 
ATOM   1274 C CA  . ARG A 1 201 ? 66.71017 28.89392  17.34792  1.000 72.20923  ? 80   ARG A CA  1 
ATOM   1275 C C   . ARG A 1 201 ? 65.66104 28.81103  16.24157  1.000 75.72059  ? 80   ARG A C   1 
ATOM   1276 O O   . ARG A 1 201 ? 65.79854 27.97049  15.34600  1.000 65.83303  ? 80   ARG A O   1 
ATOM   1277 C CB  . ARG A 1 201 ? 66.86220 27.53002  18.02906  1.000 78.51993  ? 80   ARG A CB  1 
ATOM   1278 C CG  . ARG A 1 201 ? 68.08286 27.43291  18.93986  1.000 72.71786  ? 80   ARG A CG  1 
ATOM   1279 C CD  . ARG A 1 201 ? 67.86649 26.41654  20.04678  1.000 82.67781  ? 80   ARG A CD  1 
ATOM   1280 N NE  . ARG A 1 201 ? 66.50272 26.48039  20.57024  1.000 105.33057 ? 80   ARG A NE  1 
ATOM   1281 C CZ  . ARG A 1 201 ? 65.92755 25.52203  21.29001  1.000 95.10099  ? 80   ARG A CZ  1 
ATOM   1282 N NH1 . ARG A 1 201 ? 66.60245 24.41967  21.58867  1.000 99.34790  ? 80   ARG A NH1 1 
ATOM   1283 N NH2 . ARG A 1 201 ? 64.68073 25.67027  21.71956  1.000 80.59846  ? 80   ARG A NH2 1 
ATOM   1284 N N   . LEU A 1 202 ? 64.62520 29.64815  16.26696  1.000 68.50579  ? 81   LEU A N   1 
ATOM   1285 C CA  . LEU A 1 202 ? 63.68256 29.76714  15.15181  1.000 60.14337  ? 81   LEU A CA  1 
ATOM   1286 C C   . LEU A 1 202 ? 63.52514 31.23057  14.75380  1.000 50.82934  ? 81   LEU A C   1 
ATOM   1287 O O   . LEU A 1 202 ? 62.46112 31.82941  14.94825  1.000 64.93232  ? 81   LEU A O   1 
ATOM   1288 C CB  . LEU A 1 202 ? 62.33224 29.14274  15.50722  1.000 57.61198  ? 81   LEU A CB  1 
ATOM   1289 C CG  . LEU A 1 202 ? 61.35810 28.89539  14.35134  1.000 66.40923  ? 81   LEU A CG  1 
ATOM   1290 C CD1 . LEU A 1 202 ? 61.93783 27.89118  13.36936  1.000 52.98817  ? 81   LEU A CD1 1 
ATOM   1291 C CD2 . LEU A 1 202 ? 60.01116 28.41650  14.87324  1.000 75.54371  ? 81   LEU A CD2 1 
ATOM   1292 N N   . PRO A 1 203 ? 64.58243 31.84798  14.21817  1.000 58.33182  ? 82   PRO A N   1 
ATOM   1293 C CA  . PRO A 1 203 ? 64.49471 33.27910  13.87818  1.000 54.56483  ? 82   PRO A CA  1 
ATOM   1294 C C   . PRO A 1 203 ? 63.38227 33.59816  12.89655  1.000 54.67099  ? 82   PRO A C   1 
ATOM   1295 O O   . PRO A 1 203 ? 62.80152 34.68969  12.95980  1.000 51.94770  ? 82   PRO A O   1 
ATOM   1296 C CB  . PRO A 1 203 ? 65.87216 33.58906  13.27322  1.000 51.90630  ? 82   PRO A CB  1 
ATOM   1297 C CG  . PRO A 1 203 ? 66.75307 32.46487  13.67803  1.000 53.22156  ? 82   PRO A CG  1 
ATOM   1298 C CD  . PRO A 1 203 ? 65.88341 31.26683  13.84363  1.000 41.25148  ? 82   PRO A CD  1 
ATOM   1299 N N   . GLY A 1 204 ? 63.09985 32.68770  11.96351  1.000 55.96347  ? 83   GLY A N   1 
ATOM   1300 C CA  . GLY A 1 204 ? 62.10335 32.95576  10.94163  1.000 57.58489  ? 83   GLY A CA  1 
ATOM   1301 C C   . GLY A 1 204 ? 60.75025 33.37074  11.48623  1.000 59.32134  ? 83   GLY A C   1 
ATOM   1302 O O   . GLY A 1 204 ? 60.02734 34.13576  10.84108  1.000 47.50039  ? 83   GLY A O   1 
ATOM   1303 N N   . TYR A 1 205 ? 60.39107 32.90261  12.68563  1.000 48.01446  ? 84   TYR A N   1 
ATOM   1304 C CA  . TYR A 1 205 ? 59.07140 33.21731  13.22237  1.000 56.05627  ? 84   TYR A CA  1 
ATOM   1305 C C   . TYR A 1 205 ? 59.12421 33.67855  14.67488  1.000 75.89293  ? 84   TYR A C   1 
ATOM   1306 O O   . TYR A 1 205 ? 58.08943 33.68343  15.35292  1.000 65.01836  ? 84   TYR A O   1 
ATOM   1307 C CB  . TYR A 1 205 ? 58.13492 32.01821  13.07387  1.000 46.35827  ? 84   TYR A CB  1 
ATOM   1308 C CG  . TYR A 1 205 ? 57.82954 31.74600  11.62384  1.000 60.28525  ? 84   TYR A CG  1 
ATOM   1309 C CD1 . TYR A 1 205 ? 56.91152 32.51927  10.92334  1.000 51.44997  ? 84   TYR A CD1 1 
ATOM   1310 C CD2 . TYR A 1 205 ? 58.47295 30.71959  10.95075  1.000 44.31809  ? 84   TYR A CD2 1 
ATOM   1311 C CE1 . TYR A 1 205 ? 56.64679 32.27126  9.58722   1.000 48.61896  ? 84   TYR A CE1 1 
ATOM   1312 C CE2 . TYR A 1 205 ? 58.21697 30.46407  9.62541   1.000 55.78402  ? 84   TYR A CE2 1 
ATOM   1313 C CZ  . TYR A 1 205 ? 57.30079 31.23788  8.94593   1.000 63.08663  ? 84   TYR A CZ  1 
ATOM   1314 O OH  . TYR A 1 205 ? 57.05408 30.97497  7.61747   1.000 51.81210  ? 84   TYR A OH  1 
ATOM   1315 N N   . ALA A 1 206 ? 60.30629 34.05641  15.16665  1.000 53.59912  ? 85   ALA A N   1 
ATOM   1316 C CA  . ALA A 1 206 ? 60.40873 34.61518  16.51434  1.000 62.05956  ? 85   ALA A CA  1 
ATOM   1317 C C   . ALA A 1 206 ? 59.52341 35.83859  16.71620  1.000 47.16018  ? 85   ALA A C   1 
ATOM   1318 O O   . ALA A 1 206 ? 58.79689 35.88554  17.72437  1.000 46.01670  ? 85   ALA A O   1 
ATOM   1319 C CB  . ALA A 1 206 ? 61.87392 34.93085  16.83767  1.000 46.08666  ? 85   ALA A CB  1 
ATOM   1320 N N   . PRO A 1 207 ? 59.53404 36.85435  15.84315  1.000 50.82629  ? 86   PRO A N   1 
ATOM   1321 C CA  . PRO A 1 207 ? 58.72753 38.05731  16.11426  1.000 57.09183  ? 86   PRO A CA  1 
ATOM   1322 C C   . PRO A 1 207 ? 57.22250 37.81854  16.12334  1.000 62.57451  ? 86   PRO A C   1 
ATOM   1323 O O   . PRO A 1 207 ? 56.48219 38.71299  16.55614  1.000 63.63602  ? 86   PRO A O   1 
ATOM   1324 C CB  . PRO A 1 207 ? 59.13250 39.01455  14.98218  1.000 64.62584  ? 86   PRO A CB  1 
ATOM   1325 C CG  . PRO A 1 207 ? 60.45302 38.48355  14.49320  1.000 46.55870  ? 86   PRO A CG  1 
ATOM   1326 C CD  . PRO A 1 207 ? 60.28816 37.00605  14.58551  1.000 42.29862  ? 86   PRO A CD  1 
ATOM   1327 N N   . SER A 1 208 ? 56.73881 36.66201  15.66507  1.000 60.31635  ? 87   SER A N   1 
ATOM   1328 C CA  . SER A 1 208 ? 55.32083 36.33952  15.76873  1.000 62.02126  ? 87   SER A CA  1 
ATOM   1329 C C   . SER A 1 208 ? 55.06713 35.17416  16.72070  1.000 62.96653  ? 87   SER A C   1 
ATOM   1330 O O   . SER A 1 208 ? 54.00524 34.54819  16.66091  1.000 64.23812  ? 87   SER A O   1 
ATOM   1331 C CB  . SER A 1 208 ? 54.72095 36.05787  14.38787  1.000 51.79287  ? 87   SER A CB  1 
ATOM   1332 O OG  . SER A 1 208 ? 55.27074 34.90243  13.78164  1.000 54.48362  ? 87   SER A OG  1 
ATOM   1333 N N   . GLY A 1 209 ? 56.02999 34.86909  17.59197  1.000 55.00557  ? 88   GLY A N   1 
ATOM   1334 C CA  . GLY A 1 209 ? 55.82895 33.94917  18.69490  1.000 40.20946  ? 88   GLY A CA  1 
ATOM   1335 C C   . GLY A 1 209 ? 55.82357 32.47413  18.36236  1.000 55.42076  ? 88   GLY A C   1 
ATOM   1336 O O   . GLY A 1 209 ? 55.46949 31.67386  19.23633  1.000 47.75149  ? 88   GLY A O   1 
ATOM   1337 N N   . LYS A 1 210 ? 56.17230 32.09316  17.12885  1.000 50.21355  ? 89   LYS A N   1 
ATOM   1338 C CA  . LYS A 1 210 ? 56.25105 30.70269  16.67565  1.000 68.00004  ? 89   LYS A CA  1 
ATOM   1339 C C   . LYS A 1 210 ? 54.87066 30.10901  16.41574  1.000 63.36059  ? 89   LYS A C   1 
ATOM   1340 O O   . LYS A 1 210 ? 54.64982 29.47090  15.38286  1.000 61.32805  ? 89   LYS A O   1 
ATOM   1341 C CB  . LYS A 1 210 ? 56.98142 29.79445  17.67614  1.000 52.20400  ? 89   LYS A CB  1 
ATOM   1342 C CG  . LYS A 1 210 ? 58.47180 29.97288  17.81541  1.000 65.18391  ? 89   LYS A CG  1 
ATOM   1343 C CD  . LYS A 1 210 ? 59.06384 28.68677  18.39456  1.000 79.28683  ? 89   LYS A CD  1 
ATOM   1344 C CE  . LYS A 1 210 ? 60.08226 28.94854  19.48667  1.000 82.61810  ? 89   LYS A CE  1 
ATOM   1345 N NZ  . LYS A 1 210 ? 59.51429 29.77892  20.58566  1.000 70.41668  ? 89   LYS A NZ  1 
ATOM   1346 N N   . ILE A 1 211 ? 53.93238 30.31454  17.34345  1.000 56.95076  ? 90   ILE A N   1 
ATOM   1347 C CA  . ILE A 1 211 ? 52.63209 29.66271  17.24503  1.000 54.48757  ? 90   ILE A CA  1 
ATOM   1348 C C   . ILE A 1 211 ? 51.74654 30.25891  16.16711  1.000 54.00039  ? 90   ILE A C   1 
ATOM   1349 O O   . ILE A 1 211 ? 50.72837 29.65377  15.81226  1.000 60.79806  ? 90   ILE A O   1 
ATOM   1350 C CB  . ILE A 1 211 ? 51.89598 29.71850  18.59794  1.000 55.25341  ? 90   ILE A CB  1 
ATOM   1351 C CG1 . ILE A 1 211 ? 51.69109 31.17026  19.03518  1.000 58.66626  ? 90   ILE A CG1 1 
ATOM   1352 C CG2 . ILE A 1 211 ? 52.67261 28.94737  19.65699  1.000 70.51644  ? 90   ILE A CG2 1 
ATOM   1353 C CD1 . ILE A 1 211 ? 50.96393 31.30860  20.35309  1.000 64.21849  ? 90   ILE A CD1 1 
ATOM   1354 N N   . LEU A 1 212 ? 52.11100 31.41943  15.62269  1.000 53.97573  ? 91   LEU A N   1 
ATOM   1355 C CA  . LEU A 1 212 ? 51.39788 32.00309  14.49450  1.000 53.71157  ? 91   LEU A CA  1 
ATOM   1356 C C   . LEU A 1 212 ? 52.02518 31.63387  13.15699  1.000 52.90797  ? 91   LEU A C   1 
ATOM   1357 O O   . LEU A 1 212 ? 51.87066 32.37467  12.17729  1.000 65.41942  ? 91   LEU A O   1 
ATOM   1358 C CB  . LEU A 1 212 ? 51.32919 33.52115  14.66024  1.000 42.13189  ? 91   LEU A CB  1 
ATOM   1359 C CG  . LEU A 1 212 ? 50.66639 33.95028  15.97353  1.000 51.46674  ? 91   LEU A CG  1 
ATOM   1360 C CD1 . LEU A 1 212 ? 50.53254 35.46054  16.05451  1.000 57.19395  ? 91   LEU A CD1 1 
ATOM   1361 C CD2 . LEU A 1 212 ? 49.30968 33.27390  16.14526  1.000 60.23700  ? 91   LEU A CD2 1 
ATOM   1362 N N   . THR A 1 213 ? 52.73688 30.50694  13.09562  1.000 45.31023  ? 92   THR A N   1 
ATOM   1363 C CA  . THR A 1 213 ? 53.43266 30.09375  11.88218  1.000 66.51053  ? 92   THR A CA  1 
ATOM   1364 C C   . THR A 1 213 ? 52.48703 29.33179  10.96340  1.000 50.42407  ? 92   THR A C   1 
ATOM   1365 O O   . THR A 1 213 ? 51.92617 28.31198  11.38456  1.000 48.72878  ? 92   THR A O   1 
ATOM   1366 C CB  . THR A 1 213 ? 54.62578 29.21302  12.22418  1.000 55.08580  ? 92   THR A CB  1 
ATOM   1367 O OG1 . THR A 1 213 ? 55.47421 29.89745  13.15377  1.000 46.63958  ? 92   THR A OG1 1 
ATOM   1368 C CG2 . THR A 1 213 ? 55.41326 28.85579  10.96699  1.000 41.07076  ? 92   THR A CG2 1 
ATOM   1369 N N   . PRO A 1 214 ? 52.31743 29.74665  9.70886   1.000 47.05888  ? 93   PRO A N   1 
ATOM   1370 C CA  . PRO A 1 214 ? 51.50520 28.95160  8.77902   1.000 51.75800  ? 93   PRO A CA  1 
ATOM   1371 C C   . PRO A 1 214 ? 52.13268 27.58707  8.53973   1.000 70.65699  ? 93   PRO A C   1 
ATOM   1372 O O   . PRO A 1 214 ? 53.34850 27.45941  8.37363   1.000 59.74678  ? 93   PRO A O   1 
ATOM   1373 C CB  . PRO A 1 214 ? 51.49626 29.79785  7.49942   1.000 41.63878  ? 93   PRO A CB  1 
ATOM   1374 C CG  . PRO A 1 214 ? 51.78462 31.18990  7.96568   1.000 45.51033  ? 93   PRO A CG  1 
ATOM   1375 C CD  . PRO A 1 214 ? 52.74448 31.02239  9.11211   1.000 53.09124  ? 93   PRO A CD  1 
ATOM   1376 N N   . VAL A 1 215 ? 51.28824 26.56162  8.51768   1.000 63.65493  ? 94   VAL A N   1 
ATOM   1377 C CA  . VAL A 1 215 ? 51.71111 25.18719  8.28993   1.000 77.49105  ? 94   VAL A CA  1 
ATOM   1378 C C   . VAL A 1 215 ? 50.90704 24.64563  7.11229   1.000 70.95729  ? 94   VAL A C   1 
ATOM   1379 O O   . VAL A 1 215 ? 49.69410 24.85506  7.05878   1.000 76.95399  ? 94   VAL A O   1 
ATOM   1380 C CB  . VAL A 1 215 ? 51.51785 24.30643  9.53836   1.000 76.80121  ? 94   VAL A CB  1 
ATOM   1381 C CG1 . VAL A 1 215 ? 50.24867 24.70899  10.27402  1.000 80.21698  ? 94   VAL A CG1 1 
ATOM   1382 C CG2 . VAL A 1 215 ? 51.48274 22.82894  9.17464   1.000 89.79604  ? 94   VAL A CG2 1 
ATOM   1383 N N   . PRO A 1 216 ? 51.53152 23.97086  6.15180   1.000 67.90577  ? 95   PRO A N   1 
ATOM   1384 C CA  . PRO A 1 216 ? 50.82330 23.55990  4.93446   1.000 75.79488  ? 95   PRO A CA  1 
ATOM   1385 C C   . PRO A 1 216 ? 49.97703 22.31399  5.17874   1.000 81.95008  ? 95   PRO A C   1 
ATOM   1386 O O   . PRO A 1 216 ? 49.89809 21.78749  6.28680   1.000 83.65413  ? 95   PRO A O   1 
ATOM   1387 C CB  . PRO A 1 216 ? 51.95653 23.28098  3.94599   1.000 73.26363  ? 95   PRO A CB  1 
ATOM   1388 C CG  . PRO A 1 216 ? 53.12378 22.92147  4.79646   1.000 77.25577  ? 95   PRO A CG  1 
ATOM   1389 C CD  . PRO A 1 216 ? 52.97306 23.66873  6.09127   1.000 68.19075  ? 95   PRO A CD  1 
ATOM   1390 N N   . VAL A 1 217 ? 49.33702 21.84474  4.10511   1.000 116.55607 ? 96   VAL A N   1 
ATOM   1391 C CA  . VAL A 1 217 ? 48.60945 20.57910  4.10968   1.000 135.45054 ? 96   VAL A CA  1 
ATOM   1392 C C   . VAL A 1 217 ? 48.76011 19.92921  2.74222   1.000 144.23752 ? 96   VAL A C   1 
ATOM   1393 O O   . VAL A 1 217 ? 48.82489 20.60846  1.71373   1.000 142.69552 ? 96   VAL A O   1 
ATOM   1394 C CB  . VAL A 1 217 ? 47.10120 20.72425  4.43679   1.000 135.94180 ? 96   VAL A CB  1 
ATOM   1395 C CG1 . VAL A 1 217 ? 46.53292 19.36917  4.84069   1.000 134.92606 ? 96   VAL A CG1 1 
ATOM   1396 C CG2 . VAL A 1 217 ? 46.83684 21.77219  5.50752   1.000 133.98834 ? 96   VAL A CG2 1 
ATOM   1397 N N   . PHE A 1 218 ? 48.80869 18.60096  2.73877   1.000 154.78232 ? 97   PHE A N   1 
ATOM   1398 C CA  . PHE A 1 218 ? 48.77261 17.82938  1.50430   1.000 165.22739 ? 97   PHE A CA  1 
ATOM   1399 C C   . PHE A 1 218 ? 47.72425 16.72758  1.62255   1.000 165.69844 ? 97   PHE A C   1 
ATOM   1400 O O   . PHE A 1 218 ? 46.58356 16.98362  2.00831   1.000 163.33998 ? 97   PHE A O   1 
ATOM   1401 C CB  . PHE A 1 218 ? 50.14645 17.22962  1.19317   1.000 170.33680 ? 97   PHE A CB  1 
ATOM   1402 C CG  . PHE A 1 218 ? 50.08417 15.90624  0.48051   1.000 176.71107 ? 97   PHE A CG  1 
ATOM   1403 C CD1 . PHE A 1 218 ? 49.60271 15.81946  -0.81811  1.000 179.64144 ? 97   PHE A CD1 1 
ATOM   1404 C CD2 . PHE A 1 218 ? 50.50031 14.74675  1.11346   1.000 177.83342 ? 97   PHE A CD2 1 
ATOM   1405 C CE1 . PHE A 1 218 ? 49.54122 14.60142  -1.47005  1.000 182.02712 ? 97   PHE A CE1 1 
ATOM   1406 C CE2 . PHE A 1 218 ? 50.44213 13.52621  0.46619   1.000 181.15746 ? 97   PHE A CE2 1 
ATOM   1407 C CZ  . PHE A 1 218 ? 49.96203 13.45368  -0.82721  1.000 182.69646 ? 97   PHE A CZ  1 
ATOM   1408 N N   . HIS A 1 225 ? 39.84026 21.55649  7.27940   1.000 125.07722 ? 104  HIS A N   1 
ATOM   1409 C CA  . HIS A 1 225 ? 40.50460 22.78244  7.70352   1.000 126.52603 ? 104  HIS A CA  1 
ATOM   1410 C C   . HIS A 1 225 ? 40.56882 23.79069  6.56502   1.000 131.02051 ? 104  HIS A C   1 
ATOM   1411 O O   . HIS A 1 225 ? 40.24954 23.47649  5.41713   1.000 133.64327 ? 104  HIS A O   1 
ATOM   1412 C CB  . HIS A 1 225 ? 41.91895 22.48166  8.19856   1.000 117.98914 ? 104  HIS A CB  1 
ATOM   1413 C CG  . HIS A 1 225 ? 42.68088 21.56699  7.29381   1.000 114.88393 ? 104  HIS A CG  1 
ATOM   1414 N ND1 . HIS A 1 225 ? 43.03765 20.28580  7.65577   1.000 116.36254 ? 104  HIS A ND1 1 
ATOM   1415 C CD2 . HIS A 1 225 ? 43.12469 21.73805  6.02663   1.000 113.75807 ? 104  HIS A CD2 1 
ATOM   1416 C CE1 . HIS A 1 225 ? 43.68225 19.71252  6.65572   1.000 115.27480 ? 104  HIS A CE1 1 
ATOM   1417 N NE2 . HIS A 1 225 ? 43.74532 20.57153  5.65428   1.000 118.59952 ? 104  HIS A NE2 1 
ATOM   1418 N N   . LEU A 1 226 ? 40.98540 25.00971  6.89861   1.000 127.01383 ? 105  LEU A N   1 
ATOM   1419 C CA  . LEU A 1 226 ? 41.15295 26.06913  5.91328   1.000 113.41897 ? 105  LEU A CA  1 
ATOM   1420 C C   . LEU A 1 226 ? 42.60832 26.51006  5.93871   1.000 91.76856  ? 105  LEU A C   1 
ATOM   1421 O O   . LEU A 1 226 ? 43.50918 25.66552  5.95893   1.000 92.26446  ? 105  LEU A O   1 
ATOM   1422 C CB  . LEU A 1 226 ? 40.21212 27.23434  6.21435   1.000 100.05818 ? 105  LEU A CB  1 
ATOM   1423 C CG  . LEU A 1 226 ? 38.80525 27.09111  5.63651   1.000 95.34225  ? 105  LEU A CG  1 
ATOM   1424 C CD1 . LEU A 1 226 ? 37.86210 28.10333  6.26433   1.000 80.15681  ? 105  LEU A CD1 1 
ATOM   1425 C CD2 . LEU A 1 226 ? 38.84029 27.25321  4.12707   1.000 90.74215  ? 105  LEU A CD2 1 
ATOM   1426 N N   . GLY A 1 227 ? 42.86077 27.81544  5.92686   1.000 87.31424  ? 106  GLY A N   1 
ATOM   1427 C CA  . GLY A 1 227 ? 44.16716 28.29286  6.32251   1.000 87.40534  ? 106  GLY A CA  1 
ATOM   1428 C C   . GLY A 1 227 ? 44.39731 27.99314  7.79040   1.000 93.99983  ? 106  GLY A C   1 
ATOM   1429 O O   . GLY A 1 227 ? 43.47072 28.01513  8.60305   1.000 80.93404  ? 106  GLY A O   1 
ATOM   1430 N N   . GLN A 1 228 ? 45.64474 27.69499  8.14206   1.000 66.21251  ? 107  GLN A N   1 
ATOM   1431 C CA  . GLN A 1 228 ? 45.89202 27.28547  9.51571   1.000 73.87402  ? 107  GLN A CA  1 
ATOM   1432 C C   . GLN A 1 228 ? 47.34242 27.53149  9.89582   1.000 67.40205  ? 107  GLN A C   1 
ATOM   1433 O O   . GLN A 1 228 ? 48.23076 27.61502  9.04256   1.000 60.72383  ? 107  GLN A O   1 
ATOM   1434 C CB  . GLN A 1 228 ? 45.50131 25.82188  9.74279   1.000 79.83161  ? 107  GLN A CB  1 
ATOM   1435 C CG  . GLN A 1 228 ? 46.40374 24.79438  9.10991   1.000 77.93600  ? 107  GLN A CG  1 
ATOM   1436 C CD  . GLN A 1 228 ? 45.90700 23.38728  9.37098   1.000 101.72782 ? 107  GLN A CD  1 
ATOM   1437 O OE1 . GLN A 1 228 ? 45.07899 23.16531  10.25781  1.000 98.51636  ? 107  GLN A OE1 1 
ATOM   1438 N NE2 . GLN A 1 228 ? 46.41091 22.42795  8.60513   1.000 100.50103 ? 107  GLN A NE2 1 
ATOM   1439 N N   . ASN A 1 229 ? 47.55865 27.64984  11.20554  1.000 55.93738  ? 108  ASN A N   1 
ATOM   1440 C CA  . ASN A 1 229 ? 48.89148 27.81559  11.76525  1.000 63.23610  ? 108  ASN A CA  1 
ATOM   1441 C C   . ASN A 1 229 ? 49.10985 26.82033  12.89727  1.000 66.76358  ? 108  ASN A C   1 
ATOM   1442 O O   . ASN A 1 229 ? 48.26338 25.95110  13.13245  1.000 60.44875  ? 108  ASN A O   1 
ATOM   1443 C CB  . ASN A 1 229 ? 49.09612 29.25132  12.25691  1.000 61.66745  ? 108  ASN A CB  1 
ATOM   1444 C CG  . ASN A 1 229 ? 47.92393 29.76702  13.06380  1.000 56.92291  ? 108  ASN A CG  1 
ATOM   1445 O OD1 . ASN A 1 229 ? 47.26104 29.01052  13.77263  1.000 73.10837  ? 108  ASN A OD1 1 
ATOM   1446 N ND2 . ASN A 1 229 ? 47.66250 31.06542  12.96171  1.000 53.92474  ? 108  ASN A ND2 1 
ATOM   1447 N N   . LEU A 1 230 ? 50.24254 26.93428  13.59657  1.000 58.23239  ? 109  LEU A N   1 
ATOM   1448 C CA  . LEU A 1 230 ? 50.54180 26.00461  14.68248  1.000 61.87080  ? 109  LEU A CA  1 
ATOM   1449 C C   . LEU A 1 230 ? 49.48221 26.07355  15.77556  1.000 55.84959  ? 109  LEU A C   1 
ATOM   1450 O O   . LEU A 1 230 ? 48.98658 25.03915  16.24244  1.000 50.29140  ? 109  LEU A O   1 
ATOM   1451 C CB  . LEU A 1 230 ? 51.92959 26.29338  15.26011  1.000 66.16074  ? 109  LEU A CB  1 
ATOM   1452 C CG  . LEU A 1 230 ? 53.09532 25.46614  14.71341  1.000 76.09343  ? 109  LEU A CG  1 
ATOM   1453 C CD1 . LEU A 1 230 ? 52.84630 23.98632  14.96114  1.000 72.20748  ? 109  LEU A CD1 1 
ATOM   1454 C CD2 . LEU A 1 230 ? 53.32068 25.73707  13.23348  1.000 75.21329  ? 109  LEU A CD2 1 
ATOM   1455 N N   . LEU A 1 231 ? 49.14032 27.29006  16.21133  1.000 52.16698  ? 110  LEU A N   1 
ATOM   1456 C CA  . LEU A 1 231 ? 48.15747 27.45512  17.27773  1.000 52.84167  ? 110  LEU A CA  1 
ATOM   1457 C C   . LEU A 1 231 ? 46.81491 26.85211  16.88253  1.000 56.03912  ? 110  LEU A C   1 
ATOM   1458 O O   . LEU A 1 231 ? 46.19074 26.13400  17.67019  1.000 57.78943  ? 110  LEU A O   1 
ATOM   1459 C CB  . LEU A 1 231 ? 48.00689 28.93425  17.63737  1.000 60.47230  ? 110  LEU A CB  1 
ATOM   1460 C CG  . LEU A 1 231 ? 46.96565 29.25022  18.72044  1.000 72.38487  ? 110  LEU A CG  1 
ATOM   1461 C CD1 . LEU A 1 231 ? 47.20613 28.41776  19.97533  1.000 48.38858  ? 110  LEU A CD1 1 
ATOM   1462 C CD2 . LEU A 1 231 ? 46.94802 30.73756  19.06019  1.000 59.80973  ? 110  LEU A CD2 1 
ATOM   1463 N N   . SER A 1 232 ? 46.32180 27.18435  15.68609  1.000 58.77071  ? 111  SER A N   1 
ATOM   1464 C CA  . SER A 1 232 ? 45.02343 26.66177  15.26640  1.000 65.39557  ? 111  SER A CA  1 
ATOM   1465 C C   . SER A 1 232 ? 45.06220 25.15003  15.08512  1.000 67.60163  ? 111  SER A C   1 
ATOM   1466 O O   . SER A 1 232 ? 44.02989 24.48311  15.21879  1.000 57.75393  ? 111  SER A O   1 
ATOM   1467 C CB  . SER A 1 232 ? 44.57333 27.33421  13.97073  1.000 62.55941  ? 111  SER A CB  1 
ATOM   1468 O OG  . SER A 1 232 ? 44.94478 26.55640  12.84496  1.000 64.69739  ? 111  SER A OG  1 
ATOM   1469 N N   . LEU A 1 233 ? 46.24092 24.59391  14.79526  1.000 66.74252  ? 112  LEU A N   1 
ATOM   1470 C CA  . LEU A 1 233 ? 46.37036 23.14668  14.67490  1.000 60.26375  ? 112  LEU A CA  1 
ATOM   1471 C C   . LEU A 1 233 ? 46.33409 22.48130  16.04141  1.000 66.31835  ? 112  LEU A C   1 
ATOM   1472 O O   . LEU A 1 233 ? 45.79120 21.38014  16.19138  1.000 65.28131  ? 112  LEU A O   1 
ATOM   1473 C CB  . LEU A 1 233 ? 47.66632 22.79774  13.94249  1.000 69.62201  ? 112  LEU A CB  1 
ATOM   1474 C CG  . LEU A 1 233 ? 47.74377 21.41807  13.29043  1.000 83.71581  ? 112  LEU A CG  1 
ATOM   1475 C CD1 . LEU A 1 233 ? 46.55616 21.19482  12.37123  1.000 86.50604  ? 112  LEU A CD1 1 
ATOM   1476 C CD2 . LEU A 1 233 ? 49.04801 21.26411  12.52940  1.000 86.20047  ? 112  LEU A CD2 1 
ATOM   1477 N N   . GLN A 1 234 ? 46.91040 23.13612  17.04654  1.000 62.10723  ? 113  GLN A N   1 
ATOM   1478 C CA  . GLN A 1 234 ? 47.11994 22.53063  18.35465  1.000 66.37641  ? 113  GLN A CA  1 
ATOM   1479 C C   . GLN A 1 234 ? 45.91202 22.70665  19.26896  1.000 56.89937  ? 113  GLN A C   1 
ATOM   1480 O O   . GLN A 1 234 ? 45.56572 21.79084  20.02377  1.000 66.07921  ? 113  GLN A O   1 
ATOM   1481 C CB  . GLN A 1 234 ? 48.36538 23.13777  19.00772  1.000 60.03072  ? 113  GLN A CB  1 
ATOM   1482 C CG  . GLN A 1 234 ? 48.58022 22.72076  20.44254  1.000 52.25285  ? 113  GLN A CG  1 
ATOM   1483 C CD  . GLN A 1 234 ? 49.09975 21.30277  20.55104  1.000 67.02308  ? 113  GLN A CD  1 
ATOM   1484 O OE1 . GLN A 1 234 ? 50.31158 21.07373  20.57074  1.000 64.58589  ? 113  GLN A OE1 1 
ATOM   1485 N NE2 . GLN A 1 234 ? 48.18622 20.33977  20.61302  1.000 64.05152  ? 113  GLN A NE2 1 
ATOM   1486 N N   . LEU A 1 235 ? 45.28779 23.88150  19.21872  1.000 48.44209  ? 114  LEU A N   1 
ATOM   1487 C CA  . LEU A 1 235 ? 44.23497 24.25565  20.16253  1.000 68.53619  ? 114  LEU A CA  1 
ATOM   1488 C C   . LEU A 1 235 ? 43.09592 23.24885  20.31903  1.000 66.63388  ? 114  LEU A C   1 
ATOM   1489 O O   . LEU A 1 235 ? 42.61076 23.09238  21.45379  1.000 70.69977  ? 114  LEU A O   1 
ATOM   1490 C CB  . LEU A 1 235 ? 43.67872 25.62816  19.75336  1.000 68.35001  ? 114  LEU A CB  1 
ATOM   1491 C CG  . LEU A 1 235 ? 42.64986 26.30241  20.65931  1.000 68.95073  ? 114  LEU A CG  1 
ATOM   1492 C CD1 . LEU A 1 235 ? 43.24564 26.62961  22.02140  1.000 64.90218  ? 114  LEU A CD1 1 
ATOM   1493 C CD2 . LEU A 1 235 ? 42.11938 27.55674  19.98417  1.000 61.87703  ? 114  LEU A CD2 1 
ATOM   1494 N N   . PRO A 1 236 ? 42.61062 22.56675  19.27107  1.000 57.06820  ? 115  PRO A N   1 
ATOM   1495 C CA  . PRO A 1 236 ? 41.51635 21.60251  19.48524  1.000 64.39659  ? 115  PRO A CA  1 
ATOM   1496 C C   . PRO A 1 236 ? 41.82046 20.53016  20.51585  1.000 67.44581  ? 115  PRO A C   1 
ATOM   1497 O O   . PRO A 1 236 ? 40.90365 20.10301  21.22898  1.000 65.43322  ? 115  PRO A O   1 
ATOM   1498 C CB  . PRO A 1 236 ? 41.31530 21.00219  18.08929  1.000 58.02250  ? 115  PRO A CB  1 
ATOM   1499 C CG  . PRO A 1 236 ? 41.60759 22.13673  17.18830  1.000 63.55552  ? 115  PRO A CG  1 
ATOM   1500 C CD  . PRO A 1 236 ? 42.78224 22.85290  17.83272  1.000 66.68534  ? 115  PRO A CD  1 
ATOM   1501 N N   . LEU A 1 237 ? 43.07298 20.07909  20.62193  1.000 61.23145  ? 116  LEU A N   1 
ATOM   1502 C CA  . LEU A 1 237 ? 43.43343 19.16248  21.70000  1.000 62.39144  ? 116  LEU A CA  1 
ATOM   1503 C C   . LEU A 1 237 ? 43.15991 19.78318  23.06534  1.000 78.01896  ? 116  LEU A C   1 
ATOM   1504 O O   . LEU A 1 237 ? 42.53350 19.15843  23.93137  1.000 78.59098  ? 116  LEU A O   1 
ATOM   1505 C CB  . LEU A 1 237 ? 44.89915 18.75427  21.58232  1.000 70.32595  ? 116  LEU A CB  1 
ATOM   1506 C CG  . LEU A 1 237 ? 45.33334 17.74390  22.64363  1.000 67.19493  ? 116  LEU A CG  1 
ATOM   1507 C CD1 . LEU A 1 237 ? 44.40474 16.53713  22.63485  1.000 66.06219  ? 116  LEU A CD1 1 
ATOM   1508 C CD2 . LEU A 1 237 ? 46.77246 17.32145  22.42581  1.000 60.90090  ? 116  LEU A CD2 1 
ATOM   1509 N N   . TYR A 1 238 ? 43.65447 21.00577  23.28384  1.000 76.37509  ? 117  TYR A N   1 
ATOM   1510 C CA  . TYR A 1 238 ? 43.43951 21.68319  24.55917  1.000 77.62410  ? 117  TYR A CA  1 
ATOM   1511 C C   . TYR A 1 238 ? 41.95382 21.84478  24.85125  1.000 83.05277  ? 117  TYR A C   1 
ATOM   1512 O O   . TYR A 1 238 ? 41.51324 21.66585  25.99245  1.000 87.37383  ? 117  TYR A O   1 
ATOM   1513 C CB  . TYR A 1 238 ? 44.12989 23.04826  24.55643  1.000 71.47266  ? 117  TYR A CB  1 
ATOM   1514 C CG  . TYR A 1 238 ? 45.62300 23.01097  24.30432  1.000 82.26109  ? 117  TYR A CG  1 
ATOM   1515 C CD1 . TYR A 1 238 ? 46.35863 21.84712  24.49955  1.000 79.05957  ? 117  TYR A CD1 1 
ATOM   1516 C CD2 . TYR A 1 238 ? 46.29792 24.14490  23.86776  1.000 80.55984  ? 117  TYR A CD2 1 
ATOM   1517 C CE1 . TYR A 1 238 ? 47.72195 21.81646  24.27108  1.000 65.87156  ? 117  TYR A CE1 1 
ATOM   1518 C CE2 . TYR A 1 238 ? 47.66119 24.12190  23.63566  1.000 68.68744  ? 117  TYR A CE2 1 
ATOM   1519 C CZ  . TYR A 1 238 ? 48.36764 22.95724  23.83986  1.000 68.93384  ? 117  TYR A CZ  1 
ATOM   1520 O OH  . TYR A 1 238 ? 49.72623 22.93512  23.60566  1.000 80.55523  ? 117  TYR A OH  1 
ATOM   1521 N N   . GLU A 1 239 ? 41.16727 22.18556  23.82903  1.000 72.34494  ? 118  GLU A N   1 
ATOM   1522 C CA  . GLU A 1 239 ? 39.74031 22.41207  24.03179  1.000 80.10510  ? 118  GLU A CA  1 
ATOM   1523 C C   . GLU A 1 239 ? 39.02669 21.11470  24.39809  1.000 79.40622  ? 118  GLU A C   1 
ATOM   1524 O O   . GLU A 1 239 ? 38.21465 21.08448  25.33200  1.000 92.73451  ? 118  GLU A O   1 
ATOM   1525 C CB  . GLU A 1 239 ? 39.13670 23.05950  22.78545  1.000 65.54197  ? 118  GLU A CB  1 
ATOM   1526 C CG  . GLU A 1 239 ? 39.62695 24.49361  22.59710  1.000 67.79781  ? 118  GLU A CG  1 
ATOM   1527 C CD  . GLU A 1 239 ? 39.17950 25.12241  21.29455  1.000 84.83628  ? 118  GLU A CD  1 
ATOM   1528 O OE1 . GLU A 1 239 ? 39.04356 26.36474  21.25570  1.000 87.58753  ? 118  GLU A OE1 1 
ATOM   1529 O OE2 . GLU A 1 239 ? 38.96778 24.38217  20.31077  1.000 96.55292  ? 118  GLU A OE2 1 
ATOM   1530 N N   . LYS A 1 240 ? 39.29204 20.03977  23.64996  1.000 70.10094  ? 119  LYS A N   1 
ATOM   1531 C CA  . LYS A 1 240 ? 38.75064 18.72847  23.99627  1.000 73.61023  ? 119  LYS A CA  1 
ATOM   1532 C C   . LYS A 1 240 ? 39.11074 18.33833  25.42825  1.000 74.05392  ? 119  LYS A C   1 
ATOM   1533 O O   . LYS A 1 240 ? 38.24910 17.90028  26.20389  1.000 94.17561  ? 119  LYS A O   1 
ATOM   1534 C CB  . LYS A 1 240 ? 39.26270 17.68420  23.00175  1.000 78.46828  ? 119  LYS A CB  1 
ATOM   1535 C CG  . LYS A 1 240 ? 38.61886 16.31732  23.13841  1.000 100.42710 ? 119  LYS A CG  1 
ATOM   1536 C CD  . LYS A 1 240 ? 38.97151 15.41693  21.96401  1.000 99.66374  ? 119  LYS A CD  1 
ATOM   1537 C CE  . LYS A 1 240 ? 40.41173 14.94062  22.03490  1.000 88.35224  ? 119  LYS A CE  1 
ATOM   1538 N NZ  . LYS A 1 240 ? 40.72844 14.00400  20.92166  1.000 94.57640  ? 119  LYS A NZ  1 
ATOM   1539 N N   . ILE A 1 241 ? 40.38600 18.49613  25.79576  1.000 72.05561  ? 120  ILE A N   1 
ATOM   1540 C CA  . ILE A 1 241 ? 40.82441 18.17519  27.15342  1.000 72.30698  ? 120  ILE A CA  1 
ATOM   1541 C C   . ILE A 1 241 ? 40.02023 18.97214  28.17110  1.000 85.00836  ? 120  ILE A C   1 
ATOM   1542 O O   . ILE A 1 241 ? 39.48933 18.42061  29.14326  1.000 79.66103  ? 120  ILE A O   1 
ATOM   1543 C CB  . ILE A 1 241 ? 42.33320 18.43667  27.31109  1.000 79.05237  ? 120  ILE A CB  1 
ATOM   1544 C CG1 . ILE A 1 241 ? 43.15517 17.31553  26.67189  1.000 73.90193  ? 120  ILE A CG1 1 
ATOM   1545 C CG2 . ILE A 1 241 ? 42.69714 18.58058  28.78497  1.000 67.89938  ? 120  ILE A CG2 1 
ATOM   1546 C CD1 . ILE A 1 241 ? 44.61370 17.67915  26.46536  1.000 69.45018  ? 120  ILE A CD1 1 
ATOM   1547 N N   . MET A 1 242 ? 39.90810 20.28437  27.95349  1.000 80.75478  ? 121  MET A N   1 
ATOM   1548 C CA  . MET A 1 242 ? 39.32947 21.15333  28.96836  1.000 88.20149  ? 121  MET A CA  1 
ATOM   1549 C C   . MET A 1 242 ? 37.82750 20.93984  29.08514  1.000 97.77704  ? 121  MET A C   1 
ATOM   1550 O O   . MET A 1 242 ? 37.25073 21.16037  30.15592  1.000 93.09793  ? 121  MET A O   1 
ATOM   1551 C CB  . MET A 1 242 ? 39.63638 22.61141  28.63078  1.000 89.24945  ? 121  MET A CB  1 
ATOM   1552 C CG  . MET A 1 242 ? 39.70672 23.52279  29.83094  1.000 92.84225  ? 121  MET A CG  1 
ATOM   1553 S SD  . MET A 1 242 ? 40.87394 22.88677  31.04223  1.000 83.77365  ? 121  MET A SD  1 
ATOM   1554 C CE  . MET A 1 242 ? 40.79726 24.18013  32.26921  1.000 77.25536  ? 121  MET A CE  1 
ATOM   1555 N N   . SER A 1 243 ? 37.18329 20.49724  28.00413  1.000 93.74679  ? 122  SER A N   1 
ATOM   1556 C CA  . SER A 1 243 ? 35.79527 20.06348  28.10316  1.000 99.75887  ? 122  SER A CA  1 
ATOM   1557 C C   . SER A 1 243 ? 35.68630 18.78428  28.92398  1.000 103.10863 ? 122  SER A C   1 
ATOM   1558 O O   . SER A 1 243 ? 34.88474 18.70344  29.86235  1.000 103.83573 ? 122  SER A O   1 
ATOM   1559 C CB  . SER A 1 243 ? 35.20447 19.86704  26.70770  1.000 99.21443  ? 122  SER A CB  1 
ATOM   1560 O OG  . SER A 1 243 ? 35.85740 18.81347  26.02230  1.000 105.67050 ? 122  SER A OG  1 
ATOM   1561 N N   . LEU A 1 244 ? 36.49395 17.77237  28.58835  1.000 96.76633  ? 123  LEU A N   1 
ATOM   1562 C CA  . LEU A 1 244 ? 36.44726 16.50699  29.31691  1.000 93.21188  ? 123  LEU A CA  1 
ATOM   1563 C C   . LEU A 1 244 ? 36.85417 16.65812  30.78142  1.000 101.17322 ? 123  LEU A C   1 
ATOM   1564 O O   . LEU A 1 244 ? 36.52518 15.79053  31.59921  1.000 97.72585  ? 123  LEU A O   1 
ATOM   1565 C CB  . LEU A 1 244 ? 37.34515 15.47923  28.62125  1.000 93.09507  ? 123  LEU A CB  1 
ATOM   1566 C CG  . LEU A 1 244 ? 37.37356 14.04431  29.15335  1.000 98.57616  ? 123  LEU A CG  1 
ATOM   1567 C CD1 . LEU A 1 244 ? 35.96442 13.52034  29.39155  1.000 95.42350  ? 123  LEU A CD1 1 
ATOM   1568 C CD2 . LEU A 1 244 ? 38.13204 13.13803  28.19786  1.000 88.15051  ? 123  LEU A CD2 1 
ATOM   1569 N N   . ALA A 1 245 ? 37.53201 17.74818  31.13607  1.000 103.12685 ? 124  ALA A N   1 
ATOM   1570 C CA  . ALA A 1 245 ? 38.02487 17.91737  32.49288  1.000 97.28563  ? 124  ALA A CA  1 
ATOM   1571 C C   . ALA A 1 245 ? 36.87708 18.21463  33.45687  1.000 102.24011 ? 124  ALA A C   1 
ATOM   1572 O O   . ALA A 1 245 ? 35.84383 18.75922  33.05699  1.000 109.49439 ? 124  ALA A O   1 
ATOM   1573 C CB  . ALA A 1 245 ? 39.05204 19.04440  32.54984  1.000 92.64941  ? 124  ALA A CB  1 
ATOM   1574 N N   . PRO A 1 246 ? 37.02653 17.84028  34.72857  1.000 96.58406  ? 125  PRO A N   1 
ATOM   1575 C CA  . PRO A 1 246 ? 36.05088 18.25025  35.74361  1.000 107.85090 ? 125  PRO A CA  1 
ATOM   1576 C C   . PRO A 1 246 ? 35.89133 19.76238  35.79703  1.000 122.25256 ? 125  PRO A C   1 
ATOM   1577 O O   . PRO A 1 246 ? 36.77283 20.52746  35.39887  1.000 104.03822 ? 125  PRO A O   1 
ATOM   1578 C CB  . PRO A 1 246 ? 36.64929 17.70971  37.04541  1.000 101.64515 ? 125  PRO A CB  1 
ATOM   1579 C CG  . PRO A 1 246 ? 37.41968 16.50984  36.61651  1.000 103.49823 ? 125  PRO A CG  1 
ATOM   1580 C CD  . PRO A 1 246 ? 37.97389 16.83852  35.24837  1.000 88.68219  ? 125  PRO A CD  1 
ATOM   1581 N N   . ASP A 1 247 ? 34.74133 20.18933  36.31496  1.000 140.38444 ? 126  ASP A N   1 
ATOM   1582 C CA  . ASP A 1 247 ? 34.38752 21.60204  36.35795  1.000 153.79064 ? 126  ASP A CA  1 
ATOM   1583 C C   . ASP A 1 247 ? 35.00826 22.33470  37.54063  1.000 148.02711 ? 126  ASP A C   1 
ATOM   1584 O O   . ASP A 1 247 ? 34.60019 23.46249  37.83803  1.000 159.46128 ? 126  ASP A O   1 
ATOM   1585 C CB  . ASP A 1 247 ? 32.86474 21.75848  36.38227  1.000 164.86842 ? 126  ASP A CB  1 
ATOM   1586 C CG  . ASP A 1 247 ? 32.22738 21.45587  35.03793  1.000 173.15668 ? 126  ASP A CG  1 
ATOM   1587 O OD1 . ASP A 1 247 ? 32.74505 21.93753  34.00675  1.000 173.45305 ? 126  ASP A OD1 1 
ATOM   1588 O OD2 . ASP A 1 247 ? 31.20512 20.74052  35.01171  1.000 177.94884 ? 126  ASP A OD2 1 
ATOM   1589 N N   . LYS A 1 248 ? 35.97735 21.71950  38.21741  1.000 129.56812 ? 127  LYS A N   1 
ATOM   1590 C CA  . LYS A 1 248 ? 36.79031 22.40019  39.21563  1.000 120.41104 ? 127  LYS A CA  1 
ATOM   1591 C C   . LYS A 1 248 ? 38.14265 22.84486  38.66990  1.000 108.98953 ? 127  LYS A C   1 
ATOM   1592 O O   . LYS A 1 248 ? 38.72393 23.80412  39.19048  1.000 93.12134  ? 127  LYS A O   1 
ATOM   1593 C CB  . LYS A 1 248 ? 36.99262 21.48562  40.43387  1.000 121.31313 ? 127  LYS A CB  1 
ATOM   1594 C CG  . LYS A 1 248 ? 37.83549 22.07640  41.55743  1.000 125.59803 ? 127  LYS A CG  1 
ATOM   1595 C CD  . LYS A 1 248 ? 38.13784 21.04666  42.63918  1.000 135.83381 ? 127  LYS A CD  1 
ATOM   1596 C CE  . LYS A 1 248 ? 39.09854 19.97773  42.14836  1.000 126.94785 ? 127  LYS A CE  1 
ATOM   1597 N NZ  . LYS A 1 248 ? 39.52057 19.07008  43.25008  1.000 128.62190 ? 127  LYS A NZ  1 
ATOM   1598 N N   . LEU A 1 249 ? 38.63623 22.18763  37.62341  1.000 99.49197  ? 128  LEU A N   1 
ATOM   1599 C CA  . LEU A 1 249 ? 39.88617 22.55343  36.95859  1.000 90.37993  ? 128  LEU A CA  1 
ATOM   1600 C C   . LEU A 1 249 ? 39.57597 23.61149  35.90663  1.000 77.53079  ? 128  LEU A C   1 
ATOM   1601 O O   . LEU A 1 249 ? 39.15862 23.29110  34.79158  1.000 78.85272  ? 128  LEU A O   1 
ATOM   1602 C CB  . LEU A 1 249 ? 40.54113 21.32497  36.33957  1.000 93.69630  ? 128  LEU A CB  1 
ATOM   1603 C CG  . LEU A 1 249 ? 40.52266 20.05988  37.19655  1.000 94.54570  ? 128  LEU A CG  1 
ATOM   1604 C CD1 . LEU A 1 249 ? 41.04615 18.86923  36.40900  1.000 96.30643  ? 128  LEU A CD1 1 
ATOM   1605 C CD2 . LEU A 1 249 ? 41.33783 20.26890  38.46211  1.000 96.89313  ? 128  LEU A CD2 1 
ATOM   1606 N N   . HIS A 1 250 ? 39.76410 24.87929  36.26777  1.000 79.20290  ? 129  HIS A N   1 
ATOM   1607 C CA  . HIS A 1 250 ? 39.42317 26.00424  35.40777  1.000 80.39801  ? 129  HIS A CA  1 
ATOM   1608 C C   . HIS A 1 250 ? 40.60982 26.57176  34.63401  1.000 91.47416  ? 129  HIS A C   1 
ATOM   1609 O O   . HIS A 1 250 ? 40.43203 27.53852  33.88803  1.000 75.02335  ? 129  HIS A O   1 
ATOM   1610 C CB  . HIS A 1 250 ? 38.77796 27.11758  36.23889  1.000 86.01927  ? 129  HIS A CB  1 
ATOM   1611 C CG  . HIS A 1 250 ? 37.60839 26.66115  37.05530  1.000 96.24515  ? 129  HIS A CG  1 
ATOM   1612 N ND1 . HIS A 1 250 ? 37.34513 27.14837  38.31750  1.000 98.54719  ? 129  HIS A ND1 1 
ATOM   1613 C CD2 . HIS A 1 250 ? 36.63019 25.76397  36.78702  1.000 93.98705  ? 129  HIS A CD2 1 
ATOM   1614 C CE1 . HIS A 1 250 ? 36.25713 26.56848  38.79304  1.000 96.30800  ? 129  HIS A CE1 1 
ATOM   1615 N NE2 . HIS A 1 250 ? 35.80369 25.72453  37.88378  1.000 98.92828  ? 129  HIS A NE2 1 
ATOM   1616 N N   . THR A 1 251 ? 41.81457 26.02430  34.80025  1.000 80.45497  ? 130  THR A N   1 
ATOM   1617 C CA  . THR A 1 251 ? 43.00821 26.59239  34.17361  1.000 91.30512  ? 130  THR A CA  1 
ATOM   1618 C C   . THR A 1 251 ? 43.86141 25.46853  33.59595  1.000 79.69080  ? 130  THR A C   1 
ATOM   1619 O O   . THR A 1 251 ? 44.40691 24.65531  34.34849  1.000 70.04274  ? 130  THR A O   1 
ATOM   1620 C CB  . THR A 1 251 ? 43.82029 27.42133  35.17285  1.000 92.44347  ? 130  THR A CB  1 
ATOM   1621 O OG1 . THR A 1 251 ? 44.35500 26.56019  36.18486  1.000 106.02050 ? 130  THR A OG1 1 
ATOM   1622 C CG2 . THR A 1 251 ? 42.96225 28.50341  35.82606  1.000 85.83639  ? 130  THR A CG2 1 
ATOM   1623 N N   . LEU A 1 252 ? 43.95804 25.40864  32.26636  1.000 60.78721  ? 131  LEU A N   1 
ATOM   1624 C CA  . LEU A 1 252 ? 44.94494 24.57540  31.58746  1.000 80.68936  ? 131  LEU A CA  1 
ATOM   1625 C C   . LEU A 1 252 ? 46.18629 25.40958  31.28973  1.000 76.09220  ? 131  LEU A C   1 
ATOM   1626 O O   . LEU A 1 252 ? 46.07960 26.56937  30.88450  1.000 64.38229  ? 131  LEU A O   1 
ATOM   1627 C CB  . LEU A 1 252 ? 44.37176 23.99092  30.29073  1.000 73.61497  ? 131  LEU A CB  1 
ATOM   1628 C CG  . LEU A 1 252 ? 45.25108 23.09926  29.39790  1.000 72.14015  ? 131  LEU A CG  1 
ATOM   1629 C CD1 . LEU A 1 252 ? 44.37383 22.14388  28.60379  1.000 57.59123  ? 131  LEU A CD1 1 
ATOM   1630 C CD2 . LEU A 1 252 ? 46.14454 23.88991  28.44562  1.000 59.56914  ? 131  LEU A CD2 1 
ATOM   1631 N N   . ILE A 1 253 ? 47.36110 24.81286  31.48242  1.000 70.50976  ? 132  ILE A N   1 
ATOM   1632 C CA  . ILE A 1 253 ? 48.63957 25.47609  31.23516  1.000 74.37598  ? 132  ILE A CA  1 
ATOM   1633 C C   . ILE A 1 253 ? 49.41139 24.67941  30.19097  1.000 77.30350  ? 132  ILE A C   1 
ATOM   1634 O O   . ILE A 1 253 ? 49.70883 23.49615  30.40211  1.000 65.92641  ? 132  ILE A O   1 
ATOM   1635 C CB  . ILE A 1 253 ? 49.47396 25.61611  32.51627  1.000 70.28892  ? 132  ILE A CB  1 
ATOM   1636 C CG1 . ILE A 1 253 ? 48.70708 26.38728  33.58826  1.000 79.99049  ? 132  ILE A CG1 1 
ATOM   1637 C CG2 . ILE A 1 253 ? 50.77873 26.32408  32.20843  1.000 64.58798  ? 132  ILE A CG2 1 
ATOM   1638 C CD1 . ILE A 1 253 ? 49.41989 26.40251  34.92905  1.000 81.14482  ? 132  ILE A CD1 1 
ATOM   1639 N N   . ALA A 1 254 ? 49.73479 25.32394  29.06983  1.000 71.28810  ? 133  ALA A N   1 
ATOM   1640 C CA  . ALA A 1 254 ? 50.52004 24.72585  28.00161  1.000 65.94619  ? 133  ALA A CA  1 
ATOM   1641 C C   . ALA A 1 254 ? 51.79117 25.53634  27.78924  1.000 70.64521  ? 133  ALA A C   1 
ATOM   1642 O O   . ALA A 1 254 ? 51.75600 26.77360  27.75752  1.000 70.57520  ? 133  ALA A O   1 
ATOM   1643 C CB  . ALA A 1 254 ? 49.72472 24.65575  26.69982  1.000 60.97049  ? 133  ALA A CB  1 
ATOM   1644 N N   . SER A 1 255 ? 52.90900 24.83536  27.63667  1.000 60.26178  ? 134  SER A N   1 
ATOM   1645 C CA  . SER A 1 255 ? 54.19364 25.48532  27.42390  1.000 76.44548  ? 134  SER A CA  1 
ATOM   1646 C C   . SER A 1 255 ? 55.12537 24.49929  26.73328  1.000 72.83794  ? 134  SER A C   1 
ATOM   1647 O O   . SER A 1 255 ? 54.77565 23.33923  26.49667  1.000 72.15218  ? 134  SER A O   1 
ATOM   1648 C CB  . SER A 1 255 ? 54.78937 25.98545  28.74233  1.000 82.40772  ? 134  SER A CB  1 
ATOM   1649 O OG  . SER A 1 255 ? 55.51369 24.95583  29.39180  1.000 79.20366  ? 134  SER A OG  1 
ATOM   1650 N N   . GLY A 1 256 ? 56.32294 24.97536  26.41304  1.000 61.96721  ? 135  GLY A N   1 
ATOM   1651 C CA  . GLY A 1 256 ? 57.22353 24.22375  25.56964  1.000 68.60874  ? 135  GLY A CA  1 
ATOM   1652 C C   . GLY A 1 256 ? 56.98493 24.53525  24.10980  1.000 79.75078  ? 135  GLY A C   1 
ATOM   1653 O O   . GLY A 1 256 ? 56.07795 25.28168  23.72827  1.000 87.57736  ? 135  GLY A O   1 
ATOM   1654 N N   . ASP A 1 257 ? 57.81923 23.94213  23.26772  1.000 72.61012  ? 136  ASP A N   1 
ATOM   1655 C CA  . ASP A 1 257 ? 57.77145 24.19235  21.83498  1.000 81.84822  ? 136  ASP A CA  1 
ATOM   1656 C C   . ASP A 1 257 ? 57.44218 22.91002  21.08337  1.000 77.71687  ? 136  ASP A C   1 
ATOM   1657 O O   . ASP A 1 257 ? 58.03204 22.60183  20.04556  1.000 74.47355  ? 136  ASP A O   1 
ATOM   1658 C CB  . ASP A 1 257 ? 59.08548 24.80091  21.35098  1.000 83.19264  ? 136  ASP A CB  1 
ATOM   1659 C CG  . ASP A 1 257 ? 59.38452 26.13678  22.01016  1.000 84.06480  ? 136  ASP A CG  1 
ATOM   1660 O OD1 . ASP A 1 257 ? 58.45683 26.96597  22.11798  1.000 75.12143  ? 136  ASP A OD1 1 
ATOM   1661 O OD2 . ASP A 1 257 ? 60.54328 26.35563  22.42223  1.000 83.88484  ? 136  ASP A OD2 1 
ATOM   1662 N N   . VAL A 1 258 ? 56.48598 22.14887  21.61078  1.000 84.78636  ? 137  VAL A N   1 
ATOM   1663 C CA  . VAL A 1 258 ? 56.18870 20.80201  21.14282  1.000 81.45608  ? 137  VAL A CA  1 
ATOM   1664 C C   . VAL A 1 258 ? 54.72961 20.74613  20.71082  1.000 70.41357  ? 137  VAL A C   1 
ATOM   1665 O O   . VAL A 1 258 ? 53.84088 21.20604  21.43824  1.000 72.39245  ? 137  VAL A O   1 
ATOM   1666 C CB  . VAL A 1 258 ? 56.49684 19.74750  22.22478  1.000 82.95099  ? 137  VAL A CB  1 
ATOM   1667 C CG1 . VAL A 1 258 ? 55.74227 20.04856  23.51846  1.000 73.41534  ? 137  VAL A CG1 1 
ATOM   1668 C CG2 . VAL A 1 258 ? 56.17123 18.35251  21.71751  1.000 80.66647  ? 137  VAL A CG2 1 
ATOM   1669 N N   . TYR A 1 259 ? 54.49028 20.21152  19.51574  1.000 62.99934  ? 138  TYR A N   1 
ATOM   1670 C CA  . TYR A 1 259 ? 53.14633 20.00837  18.99758  1.000 65.19289  ? 138  TYR A CA  1 
ATOM   1671 C C   . TYR A 1 259 ? 52.69592 18.61299  19.40442  1.000 71.61784  ? 138  TYR A C   1 
ATOM   1672 O O   . TYR A 1 259 ? 53.37279 17.62290  19.09640  1.000 74.72589  ? 138  TYR A O   1 
ATOM   1673 C CB  . TYR A 1 259 ? 53.10360 20.16517  17.47863  1.000 60.05265  ? 138  TYR A CB  1 
ATOM   1674 C CG  . TYR A 1 259 ? 51.80010 19.69894  16.87366  1.000 67.50160  ? 138  TYR A CG  1 
ATOM   1675 C CD1 . TYR A 1 259 ? 50.60440 20.32817  17.19179  1.000 73.80750  ? 138  TYR A CD1 1 
ATOM   1676 C CD2 . TYR A 1 259 ? 51.76107 18.62228  15.99750  1.000 79.84705  ? 138  TYR A CD2 1 
ATOM   1677 C CE1 . TYR A 1 259 ? 49.40400 19.90678  16.64727  1.000 83.74238  ? 138  TYR A CE1 1 
ATOM   1678 C CE2 . TYR A 1 259 ? 50.56270 18.19104  15.44734  1.000 80.11764  ? 138  TYR A CE2 1 
ATOM   1679 C CZ  . TYR A 1 259 ? 49.38810 18.83932  15.77521  1.000 81.75690  ? 138  TYR A CZ  1 
ATOM   1680 O OH  . TYR A 1 259 ? 48.19252 18.41828  15.23526  1.000 94.85429  ? 138  TYR A OH  1 
ATOM   1681 N N   . ILE A 1 260 ? 51.57629 18.54141  20.11643  1.000 63.93217  ? 139  ILE A N   1 
ATOM   1682 C CA  . ILE A 1 260 ? 51.06957 17.30005  20.68391  1.000 73.08953  ? 139  ILE A CA  1 
ATOM   1683 C C   . ILE A 1 260 ? 49.87418 16.83129  19.86608  1.000 74.61978  ? 139  ILE A C   1 
ATOM   1684 O O   . ILE A 1 260 ? 49.02760 17.63605  19.45912  1.000 81.18506  ? 139  ILE A O   1 
ATOM   1685 C CB  . ILE A 1 260 ? 50.69887 17.48399  22.16813  1.000 72.34821  ? 139  ILE A CB  1 
ATOM   1686 C CG1 . ILE A 1 260 ? 51.93918 17.86939  22.96913  1.000 71.57213  ? 139  ILE A CG1 1 
ATOM   1687 C CG2 . ILE A 1 260 ? 50.13169 16.20859  22.73682  1.000 58.26642  ? 139  ILE A CG2 1 
ATOM   1688 C CD1 . ILE A 1 260 ? 53.02623 16.82484  22.92313  1.000 66.72380  ? 139  ILE A CD1 1 
ATOM   1689 N N   . ARG A 1 261 ? 49.80949 15.52315  19.63095  1.000 89.24830  ? 140  ARG A N   1 
ATOM   1690 C CA  . ARG A 1 261 ? 48.81737 14.91570  18.75757  1.000 80.71963  ? 140  ARG A CA  1 
ATOM   1691 C C   . ARG A 1 261 ? 48.35339 13.60999  19.38623  1.000 82.17180  ? 140  ARG A C   1 
ATOM   1692 O O   . ARG A 1 261 ? 49.04604 13.03481  20.22676  1.000 81.73185  ? 140  ARG A O   1 
ATOM   1693 C CB  . ARG A 1 261 ? 49.40088 14.65912  17.36242  1.000 80.34408  ? 140  ARG A CB  1 
ATOM   1694 C CG  . ARG A 1 261 ? 48.39510 14.64491  16.23634  1.000 84.92886  ? 140  ARG A CG  1 
ATOM   1695 C CD  . ARG A 1 261 ? 49.10819 14.57267  14.89919  1.000 87.66884  ? 140  ARG A CD  1 
ATOM   1696 N NE  . ARG A 1 261 ? 48.21927 14.11865  13.83680  1.000 99.85478  ? 140  ARG A NE  1 
ATOM   1697 C CZ  . ARG A 1 261 ? 48.05999 12.84400  13.49809  1.000 103.02043 ? 140  ARG A CZ  1 
ATOM   1698 N NH1 . ARG A 1 261 ? 48.72929 11.89651  14.14203  1.000 95.14358  ? 140  ARG A NH1 1 
ATOM   1699 N NH2 . ARG A 1 261 ? 47.23001 12.51571  12.51820  1.000 111.85132 ? 140  ARG A NH2 1 
ATOM   1700 N N   . SER A 1 262 ? 47.17563 13.14022  18.96868  1.000 80.89791  ? 141  SER A N   1 
ATOM   1701 C CA  . SER A 1 262 ? 46.76151 11.77273  19.26772  1.000 88.81349  ? 141  SER A CA  1 
ATOM   1702 C C   . SER A 1 262 ? 45.49401 11.43114  18.49912  1.000 89.55704  ? 141  SER A C   1 
ATOM   1703 O O   . SER A 1 262 ? 44.55319 12.22715  18.45656  1.000 85.12611  ? 141  SER A O   1 
ATOM   1704 C CB  . SER A 1 262 ? 46.51125 11.56981  20.76829  1.000 86.37480  ? 141  SER A CB  1 
ATOM   1705 O OG  . SER A 1 262 ? 45.21411 12.00574  21.13157  1.000 75.78284  ? 141  SER A OG  1 
ATOM   1706 N N   . GLU A 1 263 ? 45.47940 10.24004  17.90296  1.000 95.69016  ? 142  GLU A N   1 
ATOM   1707 C CA  . GLU A 1 263 ? 44.38134 9.79431   17.05874  1.000 115.79286 ? 142  GLU A CA  1 
ATOM   1708 C C   . GLU A 1 263 ? 43.42916 8.85360   17.78948  1.000 114.22741 ? 142  GLU A C   1 
ATOM   1709 O O   . GLU A 1 263 ? 42.55156 8.25791   17.15677  1.000 116.73809 ? 142  GLU A O   1 
ATOM   1710 C CB  . GLU A 1 263 ? 44.93337 9.13510   15.79220  1.000 122.36343 ? 142  GLU A CB  1 
ATOM   1711 C CG  . GLU A 1 263 ? 45.73784 10.09676  14.91957  1.000 125.12390 ? 142  GLU A CG  1 
ATOM   1712 C CD  . GLU A 1 263 ? 46.32551 9.43678   13.68528  1.000 127.12890 ? 142  GLU A CD  1 
ATOM   1713 O OE1 . GLU A 1 263 ? 47.08123 8.45470   13.83618  1.000 130.34142 ? 142  GLU A OE1 1 
ATOM   1714 O OE2 . GLU A 1 263 ? 46.03769 9.90475   12.56318  1.000 124.05247 ? 142  GLU A OE2 1 
ATOM   1715 N N   . LYS A 1 264 ? 43.58027 8.71257   19.10495  1.000 103.61372 ? 143  LYS A N   1 
ATOM   1716 C CA  . LYS A 1 264 ? 42.71538 7.88451   19.92545  1.000 94.06295  ? 143  LYS A CA  1 
ATOM   1717 C C   . LYS A 1 264 ? 41.99729 8.73734   20.96570  1.000 100.04135 ? 143  LYS A C   1 
ATOM   1718 O O   . LYS A 1 264 ? 42.48335 9.80995   21.33932  1.000 84.06679  ? 143  LYS A O   1 
ATOM   1719 C CB  . LYS A 1 264 ? 43.49984 6.77399   20.63804  1.000 88.20195  ? 143  LYS A CB  1 
ATOM   1720 C CG  . LYS A 1 264 ? 44.13728 5.74701   19.71470  1.000 95.30974  ? 143  LYS A CG  1 
ATOM   1721 C CD  . LYS A 1 264 ? 44.88496 4.69092   20.51785  1.000 104.69574 ? 143  LYS A CD  1 
ATOM   1722 C CE  . LYS A 1 264 ? 45.74316 3.80496   19.63006  1.000 108.77054 ? 143  LYS A CE  1 
ATOM   1723 N NZ  . LYS A 1 264 ? 46.56864 2.85889   20.43280  1.000 113.00800 ? 143  LYS A NZ  1 
ATOM   1724 N N   . PRO A 1 265 ? 40.83473 8.29383   21.43959  1.000 109.26358 ? 144  PRO A N   1 
ATOM   1725 C CA  . PRO A 1 265 ? 40.08673 9.08201   22.42484  1.000 109.55039 ? 144  PRO A CA  1 
ATOM   1726 C C   . PRO A 1 265 ? 40.80035 9.15214   23.76702  1.000 100.04239 ? 144  PRO A C   1 
ATOM   1727 O O   . PRO A 1 265 ? 41.60793 8.29323   24.12615  1.000 103.67050 ? 144  PRO A O   1 
ATOM   1728 C CB  . PRO A 1 265 ? 38.76074 8.32405   22.54831  1.000 106.80516 ? 144  PRO A CB  1 
ATOM   1729 C CG  . PRO A 1 265 ? 38.61316 7.62828   21.23847  1.000 111.78744 ? 144  PRO A CG  1 
ATOM   1730 C CD  . PRO A 1 265 ? 40.00935 7.21856   20.86140  1.000 110.47647 ? 144  PRO A CD  1 
ATOM   1731 N N   . LEU A 1 266 ? 40.48037 10.20860  24.51029  1.000 97.64545  ? 145  LEU A N   1 
ATOM   1732 C CA  . LEU A 1 266 ? 41.08278 10.46344  25.80964  1.000 91.41190  ? 145  LEU A CA  1 
ATOM   1733 C C   . LEU A 1 266 ? 40.44578 9.59634   26.88892  1.000 92.90051  ? 145  LEU A C   1 
ATOM   1734 O O   . LEU A 1 266 ? 39.27696 9.21167   26.79950  1.000 94.49289  ? 145  LEU A O   1 
ATOM   1735 C CB  . LEU A 1 266 ? 40.93000 11.93561  26.18908  1.000 84.85825  ? 145  LEU A CB  1 
ATOM   1736 C CG  . LEU A 1 266 ? 41.46560 12.98863  25.22180  1.000 79.72221  ? 145  LEU A CG  1 
ATOM   1737 C CD1 . LEU A 1 266 ? 41.01476 14.37610  25.65139  1.000 83.98496  ? 145  LEU A CD1 1 
ATOM   1738 C CD2 . LEU A 1 266 ? 42.98131 12.91813  25.14269  1.000 55.99694  ? 145  LEU A CD2 1 
ATOM   1739 N N   . GLN A 1 267 ? 41.22834 9.29978   27.92331  1.000 90.31063  ? 146  GLN A N   1 
ATOM   1740 C CA  . GLN A 1 267 ? 40.69836 8.64736   29.11026  1.000 88.41987  ? 146  GLN A CA  1 
ATOM   1741 C C   . GLN A 1 267 ? 40.01073 9.67735   30.00153  1.000 94.99812  ? 146  GLN A C   1 
ATOM   1742 O O   . GLN A 1 267 ? 40.18743 10.88807  29.84364  1.000 96.49822  ? 146  GLN A O   1 
ATOM   1743 C CB  . GLN A 1 267 ? 41.80233 7.93471   29.89750  1.000 86.93155  ? 146  GLN A CB  1 
ATOM   1744 C CG  . GLN A 1 267 ? 42.71892 8.85900   30.68612  1.000 95.10215  ? 146  GLN A CG  1 
ATOM   1745 C CD  . GLN A 1 267 ? 43.82758 9.45267   29.84161  1.000 88.71330  ? 146  GLN A CD  1 
ATOM   1746 O OE1 . GLN A 1 267 ? 43.58631 10.31164  28.99387  1.000 92.84052  ? 146  GLN A OE1 1 
ATOM   1747 N NE2 . GLN A 1 267 ? 45.05206 8.99184   30.06581  1.000 80.92987  ? 146  GLN A NE2 1 
ATOM   1748 N N   . SER A 1 268 ? 39.20347 9.18381   30.93722  1.000 99.83123  ? 147  SER A N   1 
ATOM   1749 C CA  . SER A 1 268 ? 38.56355 10.07384  31.89437  1.000 101.34154 ? 147  SER A CA  1 
ATOM   1750 C C   . SER A 1 268 ? 39.62127 10.79443  32.72861  1.000 96.78408  ? 147  SER A C   1 
ATOM   1751 O O   . SER A 1 268 ? 40.74624 10.31462  32.90887  1.000 98.43073  ? 147  SER A O   1 
ATOM   1752 C CB  . SER A 1 268 ? 37.61910 9.29193   32.80575  1.000 102.78113 ? 147  SER A CB  1 
ATOM   1753 O OG  . SER A 1 268 ? 36.78000 10.16997  33.53372  1.000 100.27158 ? 147  SER A OG  1 
ATOM   1754 N N   . ILE A 1 269 ? 39.24867 11.96056  33.24224  1.000 93.83712  ? 148  ILE A N   1 
ATOM   1755 C CA  . ILE A 1 269 ? 40.18621 12.89293  33.85526  1.000 100.39228 ? 148  ILE A CA  1 
ATOM   1756 C C   . ILE A 1 269 ? 39.92403 12.90714  35.35988  1.000 111.07012 ? 148  ILE A C   1 
ATOM   1757 O O   . ILE A 1 269 ? 38.85054 13.34865  35.79835  1.000 101.40369 ? 148  ILE A O   1 
ATOM   1758 C CB  . ILE A 1 269 ? 40.06461 14.29671  33.24987  1.000 94.82073  ? 148  ILE A CB  1 
ATOM   1759 C CG1 . ILE A 1 269 ? 40.44154 14.26018  31.76667  1.000 97.44637  ? 148  ILE A CG1 1 
ATOM   1760 C CG2 . ILE A 1 269 ? 40.95425 15.27910  33.99706  1.000 85.88589  ? 148  ILE A CG2 1 
ATOM   1761 C CD1 . ILE A 1 269 ? 40.45454 15.61247  31.09356  1.000 93.58007  ? 148  ILE A CD1 1 
ATOM   1762 N N   . PRO A 1 270 ? 40.85394 12.41537  36.17807  1.000 125.29733 ? 149  PRO A N   1 
ATOM   1763 C CA  . PRO A 1 270 ? 40.65963 12.41510  37.63370  1.000 134.92691 ? 149  PRO A CA  1 
ATOM   1764 C C   . PRO A 1 270 ? 40.41084 13.80953  38.18934  1.000 131.57902 ? 149  PRO A C   1 
ATOM   1765 O O   . PRO A 1 270 ? 40.55125 14.82910  37.51161  1.000 136.51034 ? 149  PRO A O   1 
ATOM   1766 C CB  . PRO A 1 270 ? 41.97340 11.83239  38.16187  1.000 135.54779 ? 149  PRO A CB  1 
ATOM   1767 C CG  . PRO A 1 270 ? 42.47867 10.97844  37.04867  1.000 131.64835 ? 149  PRO A CG  1 
ATOM   1768 C CD  . PRO A 1 270 ? 42.05874 11.66826  35.77658  1.000 127.56741 ? 149  PRO A CD  1 
ATOM   1769 N N   . GLU A 1 271 ? 40.04772 13.84126  39.46899  1.000 115.05730 ? 150  GLU A N   1 
ATOM   1770 C CA  . GLU A 1 271 ? 39.64979 15.06607  40.15369  1.000 108.77817 ? 150  GLU A CA  1 
ATOM   1771 C C   . GLU A 1 271 ? 40.71401 15.51652  41.14949  1.000 110.73469 ? 150  GLU A C   1 
ATOM   1772 O O   . GLU A 1 271 ? 40.40598 15.94495  42.26350  1.000 109.55753 ? 150  GLU A O   1 
ATOM   1773 C CB  . GLU A 1 271 ? 38.30825 14.87582  40.85526  1.000 117.42752 ? 150  GLU A CB  1 
ATOM   1774 C CG  . GLU A 1 271 ? 37.18409 14.42723  39.93044  1.000 119.88414 ? 150  GLU A CG  1 
ATOM   1775 C CD  . GLU A 1 271 ? 35.81880 14.87014  40.41773  1.000 124.33004 ? 150  GLU A CD  1 
ATOM   1776 O OE1 . GLU A 1 271 ? 35.76304 15.79387  41.25572  1.000 122.47794 ? 150  GLU A OE1 1 
ATOM   1777 O OE2 . GLU A 1 271 ? 34.80311 14.30006  39.96303  1.000 130.96492 ? 150  GLU A OE2 1 
ATOM   1778 N N   . ALA A 1 272 ? 41.98028 15.42251  40.75228  1.000 109.70576 ? 151  ALA A N   1 
ATOM   1779 C CA  . ALA A 1 272 ? 43.08115 15.88861  41.57731  1.000 112.73032 ? 151  ALA A CA  1 
ATOM   1780 C C   . ALA A 1 272 ? 43.20746 17.40627  41.47022  1.000 104.97847 ? 151  ALA A C   1 
ATOM   1781 O O   . ALA A 1 272 ? 42.49087 18.06661  40.71331  1.000 101.66622 ? 151  ALA A O   1 
ATOM   1782 C CB  . ALA A 1 272 ? 44.37976 15.19454  41.17097  1.000 114.50474 ? 151  ALA A CB  1 
ATOM   1783 N N   . ASP A 1 273 ? 44.13456 17.97229  42.24401  1.000 105.38566 ? 152  ASP A N   1 
ATOM   1784 C CA  . ASP A 1 273 ? 44.41924 19.39719  42.14349  1.000 103.48659 ? 152  ASP A CA  1 
ATOM   1785 C C   . ASP A 1 273 ? 45.36639 19.71837  40.99828  1.000 104.95992 ? 152  ASP A C   1 
ATOM   1786 O O   . ASP A 1 273 ? 45.36674 20.85307  40.50817  1.000 101.10250 ? 152  ASP A O   1 
ATOM   1787 C CB  . ASP A 1 273 ? 45.01135 19.91116  43.45508  1.000 111.96479 ? 152  ASP A CB  1 
ATOM   1788 C CG  . ASP A 1 273 ? 44.09747 19.67519  44.63597  1.000 117.63156 ? 152  ASP A CG  1 
ATOM   1789 O OD1 . ASP A 1 273 ? 42.90765 20.04439  44.55129  1.000 122.79678 ? 152  ASP A OD1 1 
ATOM   1790 O OD2 . ASP A 1 273 ? 44.56964 19.11886  45.64895  1.000 121.07260 ? 152  ASP A OD2 1 
ATOM   1791 N N   . VAL A 1 274 ? 46.16776 18.74745  40.56551  1.000 89.30204  ? 153  VAL A N   1 
ATOM   1792 C CA  . VAL A 1 274 ? 47.09342 18.91038  39.45175  1.000 82.34281  ? 153  VAL A CA  1 
ATOM   1793 C C   . VAL A 1 274 ? 46.97082 17.66994  38.57935  1.000 87.01524  ? 153  VAL A C   1 
ATOM   1794 O O   . VAL A 1 274 ? 47.13898 16.54821  39.06828  1.000 98.24497  ? 153  VAL A O   1 
ATOM   1795 C CB  . VAL A 1 274 ? 48.54937 19.09681  39.92065  1.000 88.71286  ? 153  VAL A CB  1 
ATOM   1796 C CG1 . VAL A 1 274 ? 49.48114 19.22526  38.72788  1.000 82.94755  ? 153  VAL A CG1 1 
ATOM   1797 C CG2 . VAL A 1 274 ? 48.67770 20.31256  40.82707  1.000 78.51754  ? 153  VAL A CG2 1 
ATOM   1798 N N   . VAL A 1 275 ? 46.66496 17.86337  37.30065  1.000 81.60281  ? 154  VAL A N   1 
ATOM   1799 C CA  . VAL A 1 275 ? 46.65678 16.78713  36.31799  1.000 83.41075  ? 154  VAL A CA  1 
ATOM   1800 C C   . VAL A 1 275 ? 47.72443 17.09782  35.28051  1.000 94.82216  ? 154  VAL A C   1 
ATOM   1801 O O   . VAL A 1 275 ? 47.82225 18.23403  34.81005  1.000 85.69074  ? 154  VAL A O   1 
ATOM   1802 C CB  . VAL A 1 275 ? 45.27556 16.63033  35.65695  1.000 85.66034  ? 154  VAL A CB  1 
ATOM   1803 C CG1 . VAL A 1 275 ? 45.27537 15.44885  34.70148  1.000 86.64358  ? 154  VAL A CG1 1 
ATOM   1804 C CG2 . VAL A 1 275 ? 44.19337 16.47201  36.71881  1.000 98.31265  ? 154  VAL A CG2 1 
ATOM   1805 N N   . CYS A 1 276 ? 48.53178 16.10134  34.93452  1.000 82.73133  ? 155  CYS A N   1 
ATOM   1806 C CA  . CYS A 1 276 ? 49.63232 16.30847  34.00480  1.000 82.99096  ? 155  CYS A CA  1 
ATOM   1807 C C   . CYS A 1 276 ? 49.59770 15.21911  32.95047  1.000 77.60062  ? 155  CYS A C   1 
ATOM   1808 O O   . CYS A 1 276 ? 49.49810 14.03319  33.28523  1.000 74.78332  ? 155  CYS A O   1 
ATOM   1809 C CB  . CYS A 1 276 ? 50.98472 16.29161  34.72355  1.000 86.96969  ? 155  CYS A CB  1 
ATOM   1810 S SG  . CYS A 1 276 ? 51.17660 17.52432  36.02708  1.000 92.89206  ? 155  CYS A SG  1 
ATOM   1811 N N   . TYR A 1 277 ? 49.71213 15.61038  31.68555  1.000 71.93126  ? 156  TYR A N   1 
ATOM   1812 C CA  . TYR A 1 277 ? 49.76254 14.60965  30.63398  1.000 68.48352  ? 156  TYR A CA  1 
ATOM   1813 C C   . TYR A 1 277 ? 51.20654 14.21923  30.35798  1.000 77.99833  ? 156  TYR A C   1 
ATOM   1814 O O   . TYR A 1 277 ? 52.12929 15.02750  30.49672  1.000 75.97338  ? 156  TYR A O   1 
ATOM   1815 C CB  . TYR A 1 277 ? 49.08369 15.11779  29.36222  1.000 66.19898  ? 156  TYR A CB  1 
ATOM   1816 C CG  . TYR A 1 277 ? 47.57471 15.04369  29.43823  1.000 73.58397  ? 156  TYR A CG  1 
ATOM   1817 C CD1 . TYR A 1 277 ? 46.90382 13.87953  29.09157  1.000 81.88569  ? 156  TYR A CD1 1 
ATOM   1818 C CD2 . TYR A 1 277 ? 46.82403 16.12975  29.86831  1.000 61.52954  ? 156  TYR A CD2 1 
ATOM   1819 C CE1 . TYR A 1 277 ? 45.52755 13.79702  29.16786  1.000 72.66344  ? 156  TYR A CE1 1 
ATOM   1820 C CE2 . TYR A 1 277 ? 45.44770 16.05926  29.94510  1.000 77.83209  ? 156  TYR A CE2 1 
ATOM   1821 C CZ  . TYR A 1 277 ? 44.80331 14.88982  29.59388  1.000 81.93566  ? 156  TYR A CZ  1 
ATOM   1822 O OH  . TYR A 1 277 ? 43.43100 14.81469  29.66221  1.000 91.45578  ? 156  TYR A OH  1 
ATOM   1823 N N   . GLY A 1 278 ? 51.39379 12.95979  29.96682  1.000 71.01500  ? 157  GLY A N   1 
ATOM   1824 C CA  . GLY A 1 278 ? 52.72521 12.45837  29.69923  1.000 81.96038  ? 157  GLY A CA  1 
ATOM   1825 C C   . GLY A 1 278 ? 52.69669 11.31084  28.71605  1.000 76.61160  ? 157  GLY A C   1 
ATOM   1826 O O   . GLY A 1 278 ? 51.63811 10.81184  28.32933  1.000 87.55860  ? 157  GLY A O   1 
ATOM   1827 N N   . LEU A 1 279 ? 53.89285 10.90237  28.30850  1.000 78.32807  ? 158  LEU A N   1 
ATOM   1828 C CA  . LEU A 1 279 ? 54.06376 9.75197   27.42800  1.000 82.42124  ? 158  LEU A CA  1 
ATOM   1829 C C   . LEU A 1 279 ? 55.04842 8.77326   28.04892  1.000 78.43667  ? 158  LEU A C   1 
ATOM   1830 O O   . LEU A 1 279 ? 56.13774 9.17742   28.45551  1.000 81.47231  ? 158  LEU A O   1 
ATOM   1831 C CB  . LEU A 1 279 ? 54.55932 10.19746  26.05095  1.000 74.27916  ? 158  LEU A CB  1 
ATOM   1832 C CG  . LEU A 1 279 ? 53.59291 11.11001  25.29903  1.000 76.20989  ? 158  LEU A CG  1 
ATOM   1833 C CD1 . LEU A 1 279 ? 54.19307 11.58170  23.98973  1.000 74.13279  ? 158  LEU A CD1 1 
ATOM   1834 C CD2 . LEU A 1 279 ? 52.28103 10.38242  25.05810  1.000 83.74126  ? 158  LEU A CD2 1 
ATOM   1835 N N   . TRP A 1 280 ? 54.66502 7.49782   28.13851  1.000 71.37116  ? 159  TRP A N   1 
ATOM   1836 C CA  . TRP A 1 280 ? 55.59145 6.46964   28.60718  1.000 73.29120  ? 159  TRP A CA  1 
ATOM   1837 C C   . TRP A 1 280 ? 56.89798 6.54209   27.82696  1.000 87.82622  ? 159  TRP A C   1 
ATOM   1838 O O   . TRP A 1 280 ? 56.89764 6.53047   26.59237  1.000 80.19250  ? 159  TRP A O   1 
ATOM   1839 C CB  . TRP A 1 280 ? 54.96897 5.08141   28.45766  1.000 78.44784  ? 159  TRP A CB  1 
ATOM   1840 C CG  . TRP A 1 280 ? 53.68298 4.90826   29.20406  1.000 98.11602  ? 159  TRP A CG  1 
ATOM   1841 C CD1 . TRP A 1 280 ? 52.42977 4.82825   28.67026  1.000 89.58605  ? 159  TRP A CD1 1 
ATOM   1842 C CD2 . TRP A 1 280 ? 53.52351 4.78863   30.62288  1.000 93.59060  ? 159  TRP A CD2 1 
ATOM   1843 N NE1 . TRP A 1 280 ? 51.50092 4.66670   29.66798  1.000 99.81890  ? 159  TRP A NE1 1 
ATOM   1844 C CE2 . TRP A 1 280 ? 52.14624 4.64090   30.87651  1.000 102.20113 ? 159  TRP A CE2 1 
ATOM   1845 C CE3 . TRP A 1 280 ? 54.41134 4.79405   31.70279  1.000 95.69325  ? 159  TRP A CE3 1 
ATOM   1846 C CZ2 . TRP A 1 280 ? 51.63569 4.49825   32.16563  1.000 103.45894 ? 159  TRP A CZ2 1 
ATOM   1847 C CZ3 . TRP A 1 280 ? 53.90224 4.65201   32.98173  1.000 98.41338  ? 159  TRP A CZ3 1 
ATOM   1848 C CH2 . TRP A 1 280 ? 52.52826 4.50719   33.20209  1.000 92.36285  ? 159  TRP A CH2 1 
ATOM   1849 N N   . VAL A 1 281 ? 58.01558 6.62107   28.54932  1.000 83.61345  ? 160  VAL A N   1 
ATOM   1850 C CA  . VAL A 1 281 ? 59.31502 6.83629   27.92217  1.000 91.62139  ? 160  VAL A CA  1 
ATOM   1851 C C   . VAL A 1 281 ? 60.36786 5.93029   28.54280  1.000 89.07008  ? 160  VAL A C   1 
ATOM   1852 O O   . VAL A 1 281 ? 60.45367 5.80412   29.76958  1.000 71.42304  ? 160  VAL A O   1 
ATOM   1853 C CB  . VAL A 1 281 ? 59.76282 8.30636   28.01507  1.000 88.76820  ? 160  VAL A CB  1 
ATOM   1854 C CG1 . VAL A 1 281 ? 58.96185 9.13903   27.04292  1.000 87.48135  ? 160  VAL A CG1 1 
ATOM   1855 C CG2 . VAL A 1 281 ? 59.62292 8.82258   29.43633  1.000 79.40902  ? 160  VAL A CG2 1 
ATOM   1856 N N   . ASP A 1 282 ? 61.14237 5.27835   27.67954  1.000 89.30215  ? 161  ASP A N   1 
ATOM   1857 C CA  . ASP A 1 282 ? 62.38330 4.63327   28.06534  1.000 80.30667  ? 161  ASP A CA  1 
ATOM   1858 C C   . ASP A 1 282 ? 63.40719 5.70200   28.45405  1.000 85.88489  ? 161  ASP A C   1 
ATOM   1859 O O   . ASP A 1 282 ? 63.35920 6.82464   27.94525  1.000 90.59524  ? 161  ASP A O   1 
ATOM   1860 C CB  . ASP A 1 282 ? 62.90114 3.79141   26.89913  1.000 78.62142  ? 161  ASP A CB  1 
ATOM   1861 C CG  . ASP A 1 282 ? 64.21759 3.10735   27.19589  1.000 91.43705  ? 161  ASP A CG  1 
ATOM   1862 O OD1 . ASP A 1 282 ? 64.21723 2.12446   27.96620  1.000 97.46003  ? 161  ASP A OD1 1 
ATOM   1863 O OD2 . ASP A 1 282 ? 65.25248 3.55158   26.65601  1.000 89.01214  ? 161  ASP A OD2 1 
ATOM   1864 N N   . PRO A 1 283 ? 64.32501 5.39034   29.37486  1.000 87.53105  ? 162  PRO A N   1 
ATOM   1865 C CA  . PRO A 1 283 ? 65.34290 6.38300   29.76580  1.000 94.27186  ? 162  PRO A CA  1 
ATOM   1866 C C   . PRO A 1 283 ? 66.09805 7.01373   28.60428  1.000 95.50328  ? 162  PRO A C   1 
ATOM   1867 O O   . PRO A 1 283 ? 66.45550 8.19938   28.68597  1.000 96.43750  ? 162  PRO A O   1 
ATOM   1868 C CB  . PRO A 1 283 ? 66.27367 5.56190   30.66407  1.000 98.87149  ? 162  PRO A CB  1 
ATOM   1869 C CG  . PRO A 1 283 ? 65.34828 4.61333   31.33868  1.000 92.70094  ? 162  PRO A CG  1 
ATOM   1870 C CD  . PRO A 1 283 ? 64.33072 4.22870   30.28454  1.000 99.15739  ? 162  PRO A CD  1 
ATOM   1871 N N   . SER A 1 284 ? 66.34308 6.25851   27.52568  1.000 94.41627  ? 163  SER A N   1 
ATOM   1872 C CA  . SER A 1 284 ? 67.02881 6.79286   26.35027  1.000 80.52058  ? 163  SER A CA  1 
ATOM   1873 C C   . SER A 1 284 ? 66.39956 8.08399   25.84106  1.000 87.15165  ? 163  SER A C   1 
ATOM   1874 O O   . SER A 1 284 ? 67.08232 8.89785   25.21001  1.000 94.40305  ? 163  SER A O   1 
ATOM   1875 C CB  . SER A 1 284 ? 67.04678 5.74734   25.23268  1.000 86.72304  ? 163  SER A CB  1 
ATOM   1876 O OG  . SER A 1 284 ? 65.73734 5.48158   24.75582  1.000 91.77417  ? 163  SER A OG  1 
ATOM   1877 N N   . LEU A 1 285 ? 65.10642 8.29448   26.10120  1.000 96.81653  ? 164  LEU A N   1 
ATOM   1878 C CA  . LEU A 1 285 ? 64.47215 9.57277   25.81649  1.000 96.87094  ? 164  LEU A CA  1 
ATOM   1879 C C   . LEU A 1 285 ? 64.03114 10.31339  27.06905  1.000 89.59599  ? 164  LEU A C   1 
ATOM   1880 O O   . LEU A 1 285 ? 63.88840 11.53953  27.02269  1.000 94.85072  ? 164  LEU A O   1 
ATOM   1881 C CB  . LEU A 1 285 ? 63.25758 9.37927   24.89464  1.000 93.95636  ? 164  LEU A CB  1 
ATOM   1882 C CG  . LEU A 1 285 ? 62.54970 10.64570  24.39891  1.000 96.60092  ? 164  LEU A CG  1 
ATOM   1883 C CD1 . LEU A 1 285 ? 62.21037 10.51904  22.93160  1.000 104.05241 ? 164  LEU A CD1 1 
ATOM   1884 C CD2 . LEU A 1 285 ? 61.30232 10.94389  25.20123  1.000 103.51514 ? 164  LEU A CD2 1 
ATOM   1885 N N   . ALA A 1 286 ? 63.81405 9.60705   28.18101  1.000 90.15831  ? 165  ALA A N   1 
ATOM   1886 C CA  . ALA A 1 286 ? 63.47667 10.28928  29.42462  1.000 85.25106  ? 165  ALA A CA  1 
ATOM   1887 C C   . ALA A 1 286 ? 64.56375 11.27750  29.81749  1.000 84.90916  ? 165  ALA A C   1 
ATOM   1888 O O   . ALA A 1 286 ? 64.26727 12.34006  30.37601  1.000 84.05156  ? 165  ALA A O   1 
ATOM   1889 C CB  . ALA A 1 286 ? 63.25052 9.27365   30.54522  1.000 75.73958  ? 165  ALA A CB  1 
ATOM   1890 N N   . THR A 1 287 ? 65.82500 10.94967  29.52511  1.000 85.65421  ? 166  THR A N   1 
ATOM   1891 C CA  . THR A 1 287 ? 66.93822 11.75713  30.01092  1.000 96.26182  ? 166  THR A CA  1 
ATOM   1892 C C   . THR A 1 287 ? 66.92825 13.17511  29.44590  1.000 94.01388  ? 166  THR A C   1 
ATOM   1893 O O   . THR A 1 287 ? 67.61864 14.04625  29.98729  1.000 86.67539  ? 166  THR A O   1 
ATOM   1894 C CB  . THR A 1 287 ? 68.26992 11.06438  29.69409  1.000 91.47498  ? 166  THR A CB  1 
ATOM   1895 O OG1 . THR A 1 287 ? 69.35613 11.83323  30.22794  1.000 97.03165  ? 166  THR A OG1 1 
ATOM   1896 C CG2 . THR A 1 287 ? 68.45402 10.89485  28.19995  1.000 77.66522  ? 166  THR A CG2 1 
ATOM   1897 N N   . HIS A 1 288 ? 66.17482 13.42995  28.37351  1.000 77.98089  ? 167  HIS A N   1 
ATOM   1898 C CA  . HIS A 1 288 ? 66.19266 14.72739  27.70970  1.000 69.25601  ? 167  HIS A CA  1 
ATOM   1899 C C   . HIS A 1 288 ? 65.03735 15.63983  28.10967  1.000 68.53305  ? 167  HIS A C   1 
ATOM   1900 O O   . HIS A 1 288 ? 64.89502 16.71703  27.52337  1.000 76.95751  ? 167  HIS A O   1 
ATOM   1901 C CB  . HIS A 1 288 ? 66.17965 14.55773  26.18721  1.000 73.77518  ? 167  HIS A CB  1 
ATOM   1902 C CG  . HIS A 1 288 ? 67.39194 13.87641  25.63299  1.000 90.92940  ? 167  HIS A CG  1 
ATOM   1903 N ND1 . HIS A 1 288 ? 67.52853 12.50567  25.60031  1.000 99.71598  ? 167  HIS A ND1 1 
ATOM   1904 C CD2 . HIS A 1 288 ? 68.52374 14.37970  25.08575  1.000 97.85165  ? 167  HIS A CD2 1 
ATOM   1905 C CE1 . HIS A 1 288 ? 68.69134 12.19328  25.05607  1.000 95.11514  ? 167  HIS A CE1 1 
ATOM   1906 N NE2 . HIS A 1 288 ? 69.31550 13.31246  24.73683  1.000 98.39179  ? 167  HIS A NE2 1 
ATOM   1907 N N   . HIS A 1 289 ? 64.20799 15.25298  29.07874  1.000 71.66666  ? 168  HIS A N   1 
ATOM   1908 C CA  . HIS A 1 289 ? 63.00153 16.02238  29.36352  1.000 79.79641  ? 168  HIS A CA  1 
ATOM   1909 C C   . HIS A 1 289 ? 62.67384 15.95515  30.84843  1.000 82.71441  ? 168  HIS A C   1 
ATOM   1910 O O   . HIS A 1 289 ? 63.36416 15.30213  31.63610  1.000 79.76657  ? 168  HIS A O   1 
ATOM   1911 C CB  . HIS A 1 289 ? 61.80350 15.52049  28.54660  1.000 86.12147  ? 168  HIS A CB  1 
ATOM   1912 C CG  . HIS A 1 289 ? 62.05100 15.46533  27.07283  1.000 83.18081  ? 168  HIS A CG  1 
ATOM   1913 N ND1 . HIS A 1 289 ? 62.69703 14.40963  26.46700  1.000 88.97776  ? 168  HIS A ND1 1 
ATOM   1914 C CD2 . HIS A 1 289 ? 61.74040 16.33535  26.08317  1.000 83.88315  ? 168  HIS A CD2 1 
ATOM   1915 C CE1 . HIS A 1 289 ? 62.77594 14.63249  25.16744  1.000 96.87240  ? 168  HIS A CE1 1 
ATOM   1916 N NE2 . HIS A 1 289 ? 62.20248 15.79396  24.90812  1.000 94.54492  ? 168  HIS A NE2 1 
ATOM   1917 N N   . GLY A 1 290 ? 61.60412 16.65349  31.21997  1.000 79.19967  ? 169  GLY A N   1 
ATOM   1918 C CA  . GLY A 1 290 ? 60.99925 16.44264  32.52028  1.000 84.48328  ? 169  GLY A CA  1 
ATOM   1919 C C   . GLY A 1 290 ? 60.29531 15.09842  32.58061  1.000 93.10862  ? 169  GLY A C   1 
ATOM   1920 O O   . GLY A 1 290 ? 59.60604 14.68831  31.64649  1.000 106.08146 ? 169  GLY A O   1 
ATOM   1921 N N   . VAL A 1 291 ? 60.48030 14.40478  33.69771  1.000 95.23885  ? 170  VAL A N   1 
ATOM   1922 C CA  . VAL A 1 291 ? 60.02920 13.03260  33.87068  1.000 95.97359  ? 170  VAL A CA  1 
ATOM   1923 C C   . VAL A 1 291 ? 59.16481 12.95739  35.11987  1.000 95.61442  ? 170  VAL A C   1 
ATOM   1924 O O   . VAL A 1 291 ? 59.54958 13.46282  36.18020  1.000 100.67553 ? 170  VAL A O   1 
ATOM   1925 C CB  . VAL A 1 291 ? 61.21809 12.05796  33.98196  1.000 86.67482  ? 170  VAL A CB  1 
ATOM   1926 C CG1 . VAL A 1 291 ? 60.72536 10.64177  34.22669  1.000 85.96988  ? 170  VAL A CG1 1 
ATOM   1927 C CG2 . VAL A 1 291 ? 62.08063 12.12362  32.73090  1.000 74.90109  ? 170  VAL A CG2 1 
ATOM   1928 N N   . PHE A 1 292 ? 58.00148 12.33100  34.99069  1.000 94.37179  ? 171  PHE A N   1 
ATOM   1929 C CA  . PHE A 1 292 ? 57.22834 11.87455  36.13428  1.000 99.54482  ? 171  PHE A CA  1 
ATOM   1930 C C   . PHE A 1 292 ? 57.67124 10.45081  36.44002  1.000 103.19827 ? 171  PHE A C   1 
ATOM   1931 O O   . PHE A 1 292 ? 57.57951 9.57320   35.57325  1.000 102.25501 ? 171  PHE A O   1 
ATOM   1932 C CB  . PHE A 1 292 ? 55.72846 11.90591  35.84073  1.000 89.23831  ? 171  PHE A CB  1 
ATOM   1933 C CG  . PHE A 1 292 ? 55.25125 13.18334  35.21361  1.000 91.29298  ? 171  PHE A CG  1 
ATOM   1934 C CD1 . PHE A 1 292 ? 55.34687 14.38838  35.88761  1.000 85.54277  ? 171  PHE A CD1 1 
ATOM   1935 C CD2 . PHE A 1 292 ? 54.68262 13.17147  33.94953  1.000 94.94766  ? 171  PHE A CD2 1 
ATOM   1936 C CE1 . PHE A 1 292 ? 54.89883 15.55932  35.30298  1.000 88.36105  ? 171  PHE A CE1 1 
ATOM   1937 C CE2 . PHE A 1 292 ? 54.23110 14.33721  33.36472  1.000 88.33219  ? 171  PHE A CE2 1 
ATOM   1938 C CZ  . PHE A 1 292 ? 54.33921 15.53208  34.04240  1.000 84.88781  ? 171  PHE A CZ  1 
ATOM   1939 N N   . ALA A 1 293 ? 58.15644 10.22164  37.65580  1.000 109.29220 ? 172  ALA A N   1 
ATOM   1940 C CA  . ALA A 1 293 ? 58.48699 8.88858   38.12936  1.000 111.68848 ? 172  ALA A CA  1 
ATOM   1941 C C   . ALA A 1 293 ? 57.38840 8.41929   39.07010  1.000 116.06965 ? 172  ALA A C   1 
ATOM   1942 O O   . ALA A 1 293 ? 57.04623 9.12042   40.03498  1.000 116.00000 ? 172  ALA A O   1 
ATOM   1943 C CB  . ALA A 1 293 ? 59.84062 8.87639   38.84022  1.000 112.97087 ? 172  ALA A CB  1 
ATOM   1944 N N   . SER A 1 294 ? 56.84492 7.23503   38.78184  1.000 113.49403 ? 173  SER A N   1 
ATOM   1945 C CA  . SER A 1 294 ? 55.80097 6.62458   39.59097  1.000 119.69172 ? 173  SER A CA  1 
ATOM   1946 C C   . SER A 1 294 ? 56.20390 5.20798   39.97692  1.000 130.25361 ? 173  SER A C   1 
ATOM   1947 O O   . SER A 1 294 ? 56.85743 4.50028   39.20846  1.000 123.35715 ? 173  SER A O   1 
ATOM   1948 C CB  . SER A 1 294 ? 54.46034 6.60184   38.84663  1.000 128.34766 ? 173  SER A CB  1 
ATOM   1949 O OG  . SER A 1 294 ? 54.56414 5.89445   37.62399  1.000 132.62021 ? 173  SER A OG  1 
ATOM   1950 N N   . ASP A 1 295 ? 55.79525 4.80081   41.17798  1.000 151.15566 ? 174  ASP A N   1 
ATOM   1951 C CA  . ASP A 1 295 ? 56.13274 3.48039   41.69666  1.000 169.05118 ? 174  ASP A CA  1 
ATOM   1952 C C   . ASP A 1 295 ? 55.63336 2.37754   40.76457  1.000 173.98993 ? 174  ASP A C   1 
ATOM   1953 O O   . ASP A 1 295 ? 54.67630 2.55562   40.00414  1.000 180.36568 ? 174  ASP A O   1 
ATOM   1954 C CB  . ASP A 1 295 ? 55.54145 3.30300   43.09905  1.000 177.37016 ? 174  ASP A CB  1 
ATOM   1955 C CG  . ASP A 1 295 ? 55.71691 1.89537   43.64073  1.000 183.34600 ? 174  ASP A CG  1 
ATOM   1956 O OD1 . ASP A 1 295 ? 56.74348 1.25460   43.32427  1.000 182.83234 ? 174  ASP A OD1 1 
ATOM   1957 O OD2 . ASP A 1 295 ? 54.82537 1.42727   44.37892  1.000 187.24243 ? 174  ASP A OD2 1 
ATOM   1958 N N   . ARG A 1 296 ? 56.30270 1.22153   40.83571  1.000 173.12049 ? 175  ARG A N   1 
ATOM   1959 C CA  . ARG A 1 296 ? 55.96718 0.09935   39.96338  1.000 172.03002 ? 175  ARG A CA  1 
ATOM   1960 C C   . ARG A 1 296 ? 54.54245 -0.39061  40.20036  1.000 185.79719 ? 175  ARG A C   1 
ATOM   1961 O O   . ARG A 1 296 ? 53.84330 -0.76811  39.25306  1.000 179.89210 ? 175  ARG A O   1 
ATOM   1962 C CB  . ARG A 1 296 ? 56.96211 -1.04169  40.18269  1.000 163.94906 ? 175  ARG A CB  1 
ATOM   1963 C CG  . ARG A 1 296 ? 57.21757 -1.91339  38.96318  1.000 155.39287 ? 175  ARG A CG  1 
ATOM   1964 C CD  . ARG A 1 296 ? 58.16027 -1.25975  37.96644  1.000 142.35827 ? 175  ARG A CD  1 
ATOM   1965 N NE  . ARG A 1 296 ? 58.36216 -2.10978  36.79629  1.000 135.22274 ? 175  ARG A NE  1 
ATOM   1966 C CZ  . ARG A 1 296 ? 59.21304 -1.84094  35.81256  1.000 133.15072 ? 175  ARG A CZ  1 
ATOM   1967 N NH1 . ARG A 1 296 ? 59.95253 -0.74172  35.85601  1.000 133.54967 ? 175  ARG A NH1 1 
ATOM   1968 N NH2 . ARG A 1 296 ? 59.32954 -2.67533  34.78853  1.000 133.28166 ? 175  ARG A NH2 1 
ATOM   1969 N N   . LYS A 1 297 ? 54.09449 -0.39783  41.45482  1.000 198.53678 ? 176  LYS A N   1 
ATOM   1970 C CA  . LYS A 1 297 ? 52.76185 -0.88214  41.79178  1.000 208.31619 ? 176  LYS A CA  1 
ATOM   1971 C C   . LYS A 1 297 ? 51.67961 0.18301   41.66688  1.000 199.47649 ? 176  LYS A C   1 
ATOM   1972 O O   . LYS A 1 297 ? 50.49146 -0.16026  41.69719  1.000 208.65294 ? 176  LYS A O   1 
ATOM   1973 C CB  . LYS A 1 297 ? 52.75242 -1.44738  43.21757  1.000 220.28586 ? 176  LYS A CB  1 
ATOM   1974 C CG  . LYS A 1 297 ? 53.60291 -2.69962  43.40853  1.000 229.01811 ? 176  LYS A CG  1 
ATOM   1975 C CD  . LYS A 1 297 ? 52.93194 -3.93049  42.81182  1.000 234.24580 ? 176  LYS A CD  1 
ATOM   1976 C CE  . LYS A 1 297 ? 51.82848 -4.45397  43.72190  1.000 239.30582 ? 176  LYS A CE  1 
ATOM   1977 N NZ  . LYS A 1 297 ? 51.23922 -5.72597  43.21805  1.000 241.73109 ? 176  LYS A NZ  1 
ATOM   1978 N N   . HIS A 1 298 ? 52.05276 1.45509   41.52591  1.000 181.48139 ? 177  HIS A N   1 
ATOM   1979 C CA  . HIS A 1 298 ? 51.10467 2.57003   41.51698  1.000 166.26958 ? 177  HIS A CA  1 
ATOM   1980 C C   . HIS A 1 298 ? 51.30712 3.39549   40.25273  1.000 166.98073 ? 177  HIS A C   1 
ATOM   1981 O O   . HIS A 1 298 ? 51.88411 4.49113   40.29608  1.000 160.03825 ? 177  HIS A O   1 
ATOM   1982 C CB  . HIS A 1 298 ? 51.25466 3.42994   42.77390  1.000 156.28467 ? 177  HIS A CB  1 
ATOM   1983 C CG  . HIS A 1 298 ? 51.15238 2.65517   44.05145  1.000 154.71753 ? 177  HIS A CG  1 
ATOM   1984 N ND1 . HIS A 1 298 ? 52.10476 1.74055   44.44612  1.000 154.82001 ? 177  HIS A ND1 1 
ATOM   1985 C CD2 . HIS A 1 298 ? 50.21010 2.65949   45.02397  1.000 155.21632 ? 177  HIS A CD2 1 
ATOM   1986 C CE1 . HIS A 1 298 ? 51.75501 1.21656   45.60722  1.000 156.96577 ? 177  HIS A CE1 1 
ATOM   1987 N NE2 . HIS A 1 298 ? 50.60889 1.75686   45.97964  1.000 156.76642 ? 177  HIS A NE2 1 
ATOM   1988 N N   . PRO A 1 299 ? 50.83986 2.90102   39.10204  1.000 175.89493 ? 178  PRO A N   1 
ATOM   1989 C CA  . PRO A 1 299 ? 51.10150 3.60625   37.83980  1.000 179.59552 ? 178  PRO A CA  1 
ATOM   1990 C C   . PRO A 1 299 ? 50.20373 4.81515   37.61832  1.000 174.32985 ? 178  PRO A C   1 
ATOM   1991 O O   . PRO A 1 299 ? 50.12701 5.32644   36.49896  1.000 171.06378 ? 178  PRO A O   1 
ATOM   1992 C CB  . PRO A 1 299 ? 50.84428 2.52643   36.78159  1.000 183.21123 ? 178  PRO A CB  1 
ATOM   1993 C CG  . PRO A 1 299 ? 49.80746 1.65967   37.40136  1.000 186.42151 ? 178  PRO A CG  1 
ATOM   1994 C CD  . PRO A 1 299 ? 50.10229 1.64272   38.88691  1.000 185.15491 ? 178  PRO A CD  1 
ATOM   1995 N N   . GLU A 1 300 ? 49.52962 5.29296   38.66127  1.000 172.32875 ? 179  GLU A N   1 
ATOM   1996 C CA  . GLU A 1 300 ? 48.68118 6.47414   38.54668  1.000 169.31278 ? 179  GLU A CA  1 
ATOM   1997 C C   . GLU A 1 300 ? 49.18401 7.64150   39.37800  1.000 159.68096 ? 179  GLU A C   1 
ATOM   1998 O O   . GLU A 1 300 ? 49.30941 8.75515   38.85570  1.000 157.97777 ? 179  GLU A O   1 
ATOM   1999 C CB  . GLU A 1 300 ? 47.23263 6.14439   38.94235  1.000 178.27525 ? 179  GLU A CB  1 
ATOM   2000 C CG  . GLU A 1 300 ? 46.38934 5.59944   37.80738  1.000 183.80941 ? 179  GLU A CG  1 
ATOM   2001 C CD  . GLU A 1 300 ? 44.92104 5.52881   38.16792  1.000 192.62770 ? 179  GLU A CD  1 
ATOM   2002 O OE1 . GLU A 1 300 ? 44.55211 6.02215   39.25354  1.000 195.07190 ? 179  GLU A OE1 1 
ATOM   2003 O OE2 . GLU A 1 300 ? 44.13495 4.98842   37.36428  1.000 194.49131 ? 179  GLU A OE2 1 
ATOM   2004 N N   . GLN A 1 301 ? 49.47740 7.42375   40.65626  1.000 152.50890 ? 180  GLN A N   1 
ATOM   2005 C CA  . GLN A 1 301 ? 49.97038 8.50576   41.49213  1.000 147.55170 ? 180  GLN A CA  1 
ATOM   2006 C C   . GLN A 1 301 ? 51.38082 8.90147   41.07350  1.000 140.46839 ? 180  GLN A C   1 
ATOM   2007 O O   . GLN A 1 301 ? 52.14769 8.09377   40.54216  1.000 135.28402 ? 180  GLN A O   1 
ATOM   2008 C CB  . GLN A 1 301 ? 49.96159 8.09793   42.96355  1.000 155.00413 ? 180  GLN A CB  1 
ATOM   2009 C CG  . GLN A 1 301 ? 48.59683 7.71403   43.50321  1.000 163.90188 ? 180  GLN A CG  1 
ATOM   2010 C CD  . GLN A 1 301 ? 48.59314 7.58727   45.01250  1.000 170.54062 ? 180  GLN A CD  1 
ATOM   2011 O OE1 . GLN A 1 301 ? 49.64244 7.41428   45.63325  1.000 171.72585 ? 180  GLN A OE1 1 
ATOM   2012 N NE2 . GLN A 1 301 ? 47.41166 7.67231   45.61222  1.000 171.65461 ? 180  GLN A NE2 1 
ATOM   2013 N N   . LEU A 1 302 ? 51.71949 10.16287  41.31963  1.000 133.86738 ? 181  LEU A N   1 
ATOM   2014 C CA  . LEU A 1 302 ? 53.06395 10.66278  41.07035  1.000 121.84853 ? 181  LEU A CA  1 
ATOM   2015 C C   . LEU A 1 302 ? 53.92919 10.38718  42.29269  1.000 124.10394 ? 181  LEU A C   1 
ATOM   2016 O O   . LEU A 1 302 ? 53.58193 10.79035  43.40819  1.000 118.90730 ? 181  LEU A O   1 
ATOM   2017 C CB  . LEU A 1 302 ? 53.03353 12.15832  40.75659  1.000 112.07619 ? 181  LEU A CB  1 
ATOM   2018 C CG  . LEU A 1 302 ? 54.35736 12.92109  40.84469  1.000 109.88273 ? 181  LEU A CG  1 
ATOM   2019 C CD1 . LEU A 1 302 ? 55.20134 12.67384  39.60563  1.000 111.60924 ? 181  LEU A CD1 1 
ATOM   2020 C CD2 . LEU A 1 302 ? 54.10971 14.40804  41.03902  1.000 106.28025 ? 181  LEU A CD2 1 
ATOM   2021 N N   . ASP A 1 303 ? 55.04761 9.69168   42.08611  1.000 128.48172 ? 182  ASP A N   1 
ATOM   2022 C CA  . ASP A 1 303 ? 56.02697 9.55291   43.15689  1.000 131.15191 ? 182  ASP A CA  1 
ATOM   2023 C C   . ASP A 1 303 ? 56.88457 10.80878  43.25797  1.000 130.57242 ? 182  ASP A C   1 
ATOM   2024 O O   . ASP A 1 303 ? 56.88937 11.48358  44.29297  1.000 137.09877 ? 182  ASP A O   1 
ATOM   2025 C CB  . ASP A 1 303 ? 56.88833 8.30403   42.94978  1.000 139.81468 ? 182  ASP A CB  1 
ATOM   2026 C CG  . ASP A 1 303 ? 57.54369 7.82995   44.23519  1.000 146.73594 ? 182  ASP A CG  1 
ATOM   2027 O OD1 . ASP A 1 303 ? 57.34995 8.48678   45.28100  1.000 148.04260 ? 182  ASP A OD1 1 
ATOM   2028 O OD2 . ASP A 1 303 ? 58.24903 6.80063   44.20278  1.000 150.41103 ? 182  ASP A OD2 1 
ATOM   2029 N N   . PHE A 1 304 ? 57.61279 11.14552  42.19253  1.000 122.80321 ? 183  PHE A N   1 
ATOM   2030 C CA  . PHE A 1 304 ? 58.34504 12.40939  42.19041  1.000 110.32098 ? 183  PHE A CA  1 
ATOM   2031 C C   . PHE A 1 304 ? 58.64197 12.83449  40.75796  1.000 94.89318  ? 183  PHE A C   1 
ATOM   2032 O O   . PHE A 1 304 ? 58.35989 12.11329  39.80054  1.000 101.03489 ? 183  PHE A O   1 
ATOM   2033 C CB  . PHE A 1 304 ? 59.63228 12.33042  43.02627  1.000 117.70267 ? 183  PHE A CB  1 
ATOM   2034 C CG  . PHE A 1 304 ? 60.48874 11.13132  42.73299  1.000 119.43897 ? 183  PHE A CG  1 
ATOM   2035 C CD1 . PHE A 1 304 ? 60.24729 9.91991   43.36081  1.000 124.30955 ? 183  PHE A CD1 1 
ATOM   2036 C CD2 . PHE A 1 304 ? 61.54560 11.21909  41.84358  1.000 113.82312 ? 183  PHE A CD2 1 
ATOM   2037 C CE1 . PHE A 1 304 ? 61.03756 8.81670   43.09928  1.000 119.83571 ? 183  PHE A CE1 1 
ATOM   2038 C CE2 . PHE A 1 304 ? 62.33934 10.11834  41.57808  1.000 115.47578 ? 183  PHE A CE2 1 
ATOM   2039 C CZ  . PHE A 1 304 ? 62.08439 8.91624   42.20682  1.000 113.45967 ? 183  PHE A CZ  1 
ATOM   2040 N N   . MET A 1 305 ? 59.15175 14.05666  40.62420  1.000 90.73606  ? 184  MET A N   1 
ATOM   2041 C CA  . MET A 1 305 ? 59.53072 14.63168  39.34168  1.000 87.49225  ? 184  MET A CA  1 
ATOM   2042 C C   . MET A 1 305 ? 61.04703 14.70796  39.20154  1.000 103.45151 ? 184  MET A C   1 
ATOM   2043 O O   . MET A 1 305 ? 61.77754 14.81033  40.19071  1.000 98.18889  ? 184  MET A O   1 
ATOM   2044 C CB  . MET A 1 305 ? 58.93463 16.03107  39.16643  1.000 85.35886  ? 184  MET A CB  1 
ATOM   2045 C CG  . MET A 1 305 ? 57.52882 16.03902  38.59109  1.000 103.09210 ? 184  MET A CG  1 
ATOM   2046 S SD  . MET A 1 305 ? 57.05415 17.65915  37.96051  1.000 100.48418 ? 184  MET A SD  1 
ATOM   2047 C CE  . MET A 1 305 ? 55.26973 17.54091  38.08136  1.000 97.56884  ? 184  MET A CE  1 
ATOM   2048 N N   . LEU A 1 306 ? 61.51020 14.64974  37.95430  1.000 109.99716 ? 185  LEU A N   1 
ATOM   2049 C CA  . LEU A 1 306 ? 62.91885 14.78824  37.60985  1.000 98.63185  ? 185  LEU A CA  1 
ATOM   2050 C C   . LEU A 1 306 ? 63.05093 15.72480  36.41793  1.000 95.82935  ? 185  LEU A C   1 
ATOM   2051 O O   . LEU A 1 306 ? 62.23545 15.67537  35.49761  1.000 92.48231  ? 185  LEU A O   1 
ATOM   2052 C CB  . LEU A 1 306 ? 63.55044 13.43330  37.26831  1.000 100.08498 ? 185  LEU A CB  1 
ATOM   2053 C CG  . LEU A 1 306 ? 63.41996 12.29004  38.27537  1.000 98.08817  ? 185  LEU A CG  1 
ATOM   2054 C CD1 . LEU A 1 306 ? 64.03137 11.01335  37.71703  1.000 102.08815 ? 185  LEU A CD1 1 
ATOM   2055 C CD2 . LEU A 1 306 ? 64.08175 12.66304  39.58891  1.000 97.13600  ? 185  LEU A CD2 1 
ATOM   2056 N N   . GLN A 1 307 ? 64.05377 16.59587  36.43918  1.000 85.57457  ? 186  GLN A N   1 
ATOM   2057 C CA  . GLN A 1 307 ? 64.32210 17.49723  35.31692  1.000 81.74517  ? 186  GLN A CA  1 
ATOM   2058 C C   . GLN A 1 307 ? 65.59556 17.04149  34.60946  1.000 79.97729  ? 186  GLN A C   1 
ATOM   2059 O O   . GLN A 1 307 ? 66.70669 17.38944  35.02140  1.000 91.25527  ? 186  GLN A O   1 
ATOM   2060 C CB  . GLN A 1 307 ? 64.41460 18.94896  35.77712  1.000 72.57874  ? 186  GLN A CB  1 
ATOM   2061 C CG  . GLN A 1 307 ? 63.11473 19.49112  36.34367  1.000 85.59441  ? 186  GLN A CG  1 
ATOM   2062 C CD  . GLN A 1 307 ? 61.98160 19.46010  35.32052  1.000 100.46777 ? 186  GLN A CD  1 
ATOM   2063 O OE1 . GLN A 1 307 ? 62.21160 19.58995  34.11453  1.000 86.90647  ? 186  GLN A OE1 1 
ATOM   2064 N NE2 . GLN A 1 307 ? 60.75284 19.28299  35.80055  1.000 90.43268  ? 186  GLN A NE2 1 
ATOM   2065 N N   . LYS A 1 308 ? 65.41881 16.24520  33.55143  1.000 85.30967  ? 187  LYS A N   1 
ATOM   2066 C CA  . LYS A 1 308 ? 66.47866 15.74391  32.68062  1.000 85.12288  ? 187  LYS A CA  1 
ATOM   2067 C C   . LYS A 1 308 ? 67.44181 14.83597  33.43704  1.000 94.18061  ? 187  LYS A C   1 
ATOM   2068 O O   . LYS A 1 308 ? 68.63226 15.15699  33.54609  1.000 85.23328  ? 187  LYS A O   1 
ATOM   2069 C CB  . LYS A 1 308 ? 67.24138 16.90005  32.03047  1.000 88.03092  ? 187  LYS A CB  1 
ATOM   2070 C CG  . LYS A 1 308 ? 66.41397 17.71331  31.05285  1.000 76.80457  ? 187  LYS A CG  1 
ATOM   2071 C CD  . LYS A 1 308 ? 67.29590 18.64044  30.23529  1.000 82.85407  ? 187  LYS A CD  1 
ATOM   2072 C CE  . LYS A 1 308 ? 66.46724 19.58317  29.38250  1.000 80.42472  ? 187  LYS A CE  1 
ATOM   2073 N NZ  . LYS A 1 308 ? 67.32638 20.51850  28.60214  1.000 71.93589  ? 187  LYS A NZ  1 
ATOM   2074 N N   . PRO A 1 309 ? 66.97631 13.70720  33.97342  1.000 97.16234  ? 188  PRO A N   1 
ATOM   2075 C CA  . PRO A 1 309 ? 67.87509 12.81705  34.71805  1.000 93.79026  ? 188  PRO A CA  1 
ATOM   2076 C C   . PRO A 1 309 ? 68.96384 12.24779  33.82152  1.000 103.81443 ? 188  PRO A C   1 
ATOM   2077 O O   . PRO A 1 309 ? 68.90650 12.31168  32.59193  1.000 107.38507 ? 188  PRO A O   1 
ATOM   2078 C CB  . PRO A 1 309 ? 66.94364 11.71441  35.23226  1.000 103.35044 ? 188  PRO A CB  1 
ATOM   2079 C CG  . PRO A 1 309 ? 65.77419 11.74589  34.30389  1.000 97.23857  ? 188  PRO A CG  1 
ATOM   2080 C CD  . PRO A 1 309 ? 65.59957 13.18223  33.92954  1.000 88.80138  ? 188  PRO A CD  1 
ATOM   2081 N N   . SER A 1 310 ? 69.97701 11.67844  34.46257  1.000 110.47876 ? 189  SER A N   1 
ATOM   2082 C CA  . SER A 1 310 ? 71.08357 11.06578  33.74782  1.000 99.04333  ? 189  SER A CA  1 
ATOM   2083 C C   . SER A 1 310 ? 70.74350 9.62073   33.40370  1.000 95.58507  ? 189  SER A C   1 
ATOM   2084 O O   . SER A 1 310 ? 69.90478 8.98420   34.04577  1.000 99.56073  ? 189  SER A O   1 
ATOM   2085 C CB  . SER A 1 310 ? 72.36527 11.12149  34.57539  1.000 99.19770  ? 189  SER A CB  1 
ATOM   2086 O OG  . SER A 1 310 ? 72.27213 10.28462  35.71305  1.000 95.56140  ? 189  SER A OG  1 
ATOM   2087 N N   . LEU A 1 311 ? 71.40824 9.10893   32.36570  1.000 101.01656 ? 190  LEU A N   1 
ATOM   2088 C CA  . LEU A 1 311 ? 71.18587 7.72774   31.95175  1.000 111.37074 ? 190  LEU A CA  1 
ATOM   2089 C C   . LEU A 1 311 ? 71.44095 6.75027   33.09201  1.000 121.80456 ? 190  LEU A C   1 
ATOM   2090 O O   . LEU A 1 311 ? 70.75852 5.72404   33.19359  1.000 114.78789 ? 190  LEU A O   1 
ATOM   2091 C CB  . LEU A 1 311 ? 72.07037 7.39329   30.74966  1.000 108.45431 ? 190  LEU A CB  1 
ATOM   2092 C CG  . LEU A 1 311 ? 72.08476 8.41977   29.61222  1.000 110.54257 ? 190  LEU A CG  1 
ATOM   2093 C CD1 . LEU A 1 311 ? 73.27029 9.37836   29.73712  1.000 119.90096 ? 190  LEU A CD1 1 
ATOM   2094 C CD2 . LEU A 1 311 ? 72.08225 7.72676   28.25746  1.000 109.87996 ? 190  LEU A CD2 1 
ATOM   2095 N N   . ALA A 1 312 ? 72.40498 7.05309   33.96355  1.000 129.59287 ? 191  ALA A N   1 
ATOM   2096 C CA  . ALA A 1 312 ? 72.70311 6.16125   35.07804  1.000 134.63437 ? 191  ALA A CA  1 
ATOM   2097 C C   . ALA A 1 312 ? 71.66811 6.28384   36.19107  1.000 130.47978 ? 191  ALA A C   1 
ATOM   2098 O O   . ALA A 1 312 ? 71.22528 5.26899   36.74091  1.000 138.33819 ? 191  ALA A O   1 
ATOM   2099 C CB  . ALA A 1 312 ? 74.10350 6.44791   35.61875  1.000 141.79273 ? 191  ALA A CB  1 
ATOM   2100 N N   . GLU A 1 313 ? 71.28042 7.51494   36.54261  1.000 113.92270 ? 192  GLU A N   1 
ATOM   2101 C CA  . GLU A 1 313 ? 70.24816 7.71205   37.55803  1.000 108.62662 ? 192  GLU A CA  1 
ATOM   2102 C C   . GLU A 1 313 ? 68.94016 7.02366   37.18550  1.000 113.10946 ? 192  GLU A C   1 
ATOM   2103 O O   . GLU A 1 313 ? 68.18699 6.60095   38.07077  1.000 110.98003 ? 192  GLU A O   1 
ATOM   2104 C CB  . GLU A 1 313 ? 70.01263 9.20671   37.78455  1.000 103.01809 ? 192  GLU A CB  1 
ATOM   2105 C CG  . GLU A 1 313 ? 68.97279 9.51909   38.85248  1.000 104.13831 ? 192  GLU A CG  1 
ATOM   2106 C CD  . GLU A 1 313 ? 68.79994 11.00758  39.09059  1.000 101.65821 ? 192  GLU A CD  1 
ATOM   2107 O OE1 . GLU A 1 313 ? 68.12899 11.37730  40.07837  1.000 99.45818  ? 192  GLU A OE1 1 
ATOM   2108 O OE2 . GLU A 1 313 ? 69.34090 11.80731  38.29701  1.000 92.13885  ? 192  GLU A OE2 1 
ATOM   2109 N N   . LEU A 1 314 ? 68.65933 6.88506   35.88906  1.000 118.78054 ? 193  LEU A N   1 
ATOM   2110 C CA  . LEU A 1 314 ? 67.46360 6.16613   35.46442  1.000 120.47041 ? 193  LEU A CA  1 
ATOM   2111 C C   . LEU A 1 314 ? 67.65664 4.65741   35.55099  1.000 132.70704 ? 193  LEU A C   1 
ATOM   2112 O O   . LEU A 1 314 ? 66.74728 3.93952   35.98188  1.000 136.94150 ? 193  LEU A O   1 
ATOM   2113 C CB  . LEU A 1 314 ? 67.07675 6.58389   34.04581  1.000 118.24238 ? 193  LEU A CB  1 
ATOM   2114 C CG  . LEU A 1 314 ? 66.67729 8.05196   33.89168  1.000 114.43621 ? 193  LEU A CG  1 
ATOM   2115 C CD1 . LEU A 1 314 ? 66.95182 8.55244   32.48392  1.000 105.57799 ? 193  LEU A CD1 1 
ATOM   2116 C CD2 . LEU A 1 314 ? 65.20781 8.22257   34.24433  1.000 98.35986  ? 193  LEU A CD2 1 
ATOM   2117 N N   . GLU A 1 315 ? 68.82760 4.15910   35.14291  1.000 145.69504 ? 194  GLU A N   1 
ATOM   2118 C CA  . GLU A 1 315 ? 69.14606 2.75090   35.35777  1.000 152.59433 ? 194  GLU A CA  1 
ATOM   2119 C C   . GLU A 1 315 ? 69.12130 2.39261   36.83752  1.000 147.33240 ? 194  GLU A C   1 
ATOM   2120 O O   . GLU A 1 315 ? 68.82178 1.24771   37.19492  1.000 151.05806 ? 194  GLU A O   1 
ATOM   2121 C CB  . GLU A 1 315 ? 70.51128 2.42071   34.75272  1.000 160.95376 ? 194  GLU A CB  1 
ATOM   2122 C CG  . GLU A 1 315 ? 70.54606 2.49192   33.23419  1.000 168.00390 ? 194  GLU A CG  1 
ATOM   2123 C CD  . GLU A 1 315 ? 69.33450 1.84779   32.58731  1.000 174.68821 ? 194  GLU A CD  1 
ATOM   2124 O OE1 . GLU A 1 315 ? 69.02337 0.68443   32.91972  1.000 177.89699 ? 194  GLU A OE1 1 
ATOM   2125 O OE2 . GLU A 1 315 ? 68.68459 2.51204   31.75246  1.000 174.41393 ? 194  GLU A OE2 1 
ATOM   2126 N N   . SER A 1 316 ? 69.43146 3.35439   37.70976  1.000 139.73196 ? 195  SER A N   1 
ATOM   2127 C CA  . SER A 1 316 ? 69.39648 3.10903   39.14570  1.000 136.24789 ? 195  SER A CA  1 
ATOM   2128 C C   . SER A 1 316 ? 67.97632 2.96206   39.67479  1.000 134.66585 ? 195  SER A C   1 
ATOM   2129 O O   . SER A 1 316 ? 67.79241 2.44489   40.78112  1.000 139.39335 ? 195  SER A O   1 
ATOM   2130 C CB  . SER A 1 316 ? 70.11292 4.23693   39.88954  1.000 138.28301 ? 195  SER A CB  1 
ATOM   2131 O OG  . SER A 1 316 ? 70.14822 3.98566   41.28341  1.000 145.97219 ? 195  SER A OG  1 
ATOM   2132 N N   . LEU A 1 317 ? 66.97247 3.40130   38.91535  1.000 130.02088 ? 196  LEU A N   1 
ATOM   2133 C CA  . LEU A 1 317 ? 65.57711 3.29018   39.32306  1.000 136.28565 ? 196  LEU A CA  1 
ATOM   2134 C C   . LEU A 1 317 ? 64.75420 2.43445   38.36943  1.000 146.42050 ? 196  LEU A C   1 
ATOM   2135 O O   . LEU A 1 317 ? 63.52559 2.38232   38.50561  1.000 136.41201 ? 196  LEU A O   1 
ATOM   2136 C CB  . LEU A 1 317 ? 64.94724 4.68070   39.44528  1.000 129.58603 ? 196  LEU A CB  1 
ATOM   2137 C CG  . LEU A 1 317 ? 65.50282 5.59228   40.54002  1.000 123.66983 ? 196  LEU A CG  1 
ATOM   2138 C CD1 . LEU A 1 317 ? 64.61065 6.80999   40.73470  1.000 113.05225 ? 196  LEU A CD1 1 
ATOM   2139 C CD2 . LEU A 1 317 ? 65.66850 4.82792   41.84664  1.000 127.23188 ? 196  LEU A CD2 1 
ATOM   2140 N N   . SER A 1 318 ? 65.39641 1.76838   37.40531  1.000 168.84278 ? 197  SER A N   1 
ATOM   2141 C CA  . SER A 1 318 ? 64.65464 1.03512   36.38395  1.000 179.78857 ? 197  SER A CA  1 
ATOM   2142 C C   . SER A 1 318 ? 63.84916 -0.11586  36.97443  1.000 177.84755 ? 197  SER A C   1 
ATOM   2143 O O   . SER A 1 318 ? 62.82323 -0.50626  36.40582  1.000 182.69031 ? 197  SER A O   1 
ATOM   2144 C CB  . SER A 1 318 ? 65.61352 0.51254   35.31329  1.000 189.32115 ? 197  SER A CB  1 
ATOM   2145 O OG  . SER A 1 318 ? 66.49754 -0.45749  35.84792  1.000 198.58055 ? 197  SER A OG  1 
ATOM   2146 N N   . LYS A 1 319 ? 64.29141 -0.67285  38.10447  1.000 171.91989 ? 198  LYS A N   1 
ATOM   2147 C CA  . LYS A 1 319 ? 63.57257 -1.77740  38.72780  1.000 165.24763 ? 198  LYS A CA  1 
ATOM   2148 C C   . LYS A 1 319 ? 62.43314 -1.32218  39.62931  1.000 162.28562 ? 198  LYS A C   1 
ATOM   2149 O O   . LYS A 1 319 ? 61.55651 -2.13318  39.94632  1.000 161.37503 ? 198  LYS A O   1 
ATOM   2150 C CB  . LYS A 1 319 ? 64.53067 -2.64882  39.54585  1.000 164.93390 ? 198  LYS A CB  1 
ATOM   2151 C CG  . LYS A 1 319 ? 65.27537 -3.70607  38.74570  1.000 164.81691 ? 198  LYS A CG  1 
ATOM   2152 C CD  . LYS A 1 319 ? 65.74350 -4.83812  39.65198  1.000 165.60304 ? 198  LYS A CD  1 
ATOM   2153 C CE  . LYS A 1 319 ? 66.66686 -5.80200  38.92361  1.000 159.90235 ? 198  LYS A CE  1 
ATOM   2154 N NZ  . LYS A 1 319 ? 68.02927 -5.23329  38.72820  1.000 153.89295 ? 198  LYS A NZ  1 
ATOM   2155 N N   . THR A 1 320 ? 62.41677 -0.05619  40.04948  1.000 162.73169 ? 199  THR A N   1 
ATOM   2156 C CA  . THR A 1 320 ? 61.46700 0.39511   41.05574  1.000 166.32235 ? 199  THR A CA  1 
ATOM   2157 C C   . THR A 1 320 ? 60.49723 1.46899   40.58282  1.000 163.42168 ? 199  THR A C   1 
ATOM   2158 O O   . THR A 1 320 ? 59.54626 1.77353   41.31147  1.000 166.81699 ? 199  THR A O   1 
ATOM   2159 C CB  . THR A 1 320 ? 62.21056 0.91813   42.29501  1.000 167.27586 ? 199  THR A CB  1 
ATOM   2160 O OG1 . THR A 1 320 ? 63.15797 1.91800   41.90095  1.000 167.96876 ? 199  THR A OG1 1 
ATOM   2161 C CG2 . THR A 1 320 ? 62.93636 -0.21859  43.00034  1.000 172.39241 ? 199  THR A CG2 1 
ATOM   2162 N N   . HIS A 1 321 ? 60.68865 2.04443   39.39891  1.000 152.48746 ? 200  HIS A N   1 
ATOM   2163 C CA  . HIS A 1 321 ? 59.82821 3.12842   38.95083  1.000 138.38520 ? 200  HIS A CA  1 
ATOM   2164 C C   . HIS A 1 321 ? 59.59027 3.02735   37.45300  1.000 134.41399 ? 200  HIS A C   1 
ATOM   2165 O O   . HIS A 1 321 ? 60.36854 2.42067   36.71387  1.000 128.92190 ? 200  HIS A O   1 
ATOM   2166 C CB  . HIS A 1 321 ? 60.42891 4.50389   39.27589  1.000 133.58513 ? 200  HIS A CB  1 
ATOM   2167 C CG  . HIS A 1 321 ? 60.30638 4.89838   40.71454  1.000 131.39977 ? 200  HIS A CG  1 
ATOM   2168 N ND1 . HIS A 1 321 ? 61.08106 4.34333   41.71030  1.000 131.50856 ? 200  HIS A ND1 1 
ATOM   2169 C CD2 . HIS A 1 321 ? 59.50447 5.80364   41.32296  1.000 130.50195 ? 200  HIS A CD2 1 
ATOM   2170 C CE1 . HIS A 1 321 ? 60.75820 4.88613   42.87064  1.000 131.93782 ? 200  HIS A CE1 1 
ATOM   2171 N NE2 . HIS A 1 321 ? 59.80426 5.77559   42.66309  1.000 131.08542 ? 200  HIS A NE2 1 
ATOM   2172 N N   . LEU A 1 322 ? 58.49267 3.63814   37.02056  1.000 141.87474 ? 201  LEU A N   1 
ATOM   2173 C CA  . LEU A 1 322 ? 58.20592 3.89008   35.61999  1.000 139.73560 ? 201  LEU A CA  1 
ATOM   2174 C C   . LEU A 1 322 ? 58.25556 5.38967   35.36173  1.000 126.89203 ? 201  LEU A C   1 
ATOM   2175 O O   . LEU A 1 322 ? 58.04499 6.20804   36.26627  1.000 131.93205 ? 201  LEU A O   1 
ATOM   2176 C CB  . LEU A 1 322 ? 56.83894 3.32465   35.22413  1.000 134.38200 ? 201  LEU A CB  1 
ATOM   2177 C CG  . LEU A 1 322 ? 56.79069 1.81061   35.00816  1.000 136.71434 ? 201  LEU A CG  1 
ATOM   2178 C CD1 . LEU A 1 322 ? 55.45296 1.39245   34.41949  1.000 139.64991 ? 201  LEU A CD1 1 
ATOM   2179 C CD2 . LEU A 1 322 ? 57.93981 1.35106   34.11960  1.000 138.02943 ? 201  LEU A CD2 1 
ATOM   2180 N N   . PHE A 1 323 ? 58.51517 5.73883   34.10368  1.000 109.55659 ? 202  PHE A N   1 
ATOM   2181 C CA  . PHE A 1 323 ? 58.83839 7.10281   33.71115  1.000 103.91091 ? 202  PHE A CA  1 
ATOM   2182 C C   . PHE A 1 323 ? 57.89128 7.57345   32.61870  1.000 102.78412 ? 202  PHE A C   1 
ATOM   2183 O O   . PHE A 1 323 ? 57.63856 6.84516   31.65292  1.000 101.64494 ? 202  PHE A O   1 
ATOM   2184 C CB  . PHE A 1 323 ? 60.28332 7.19124   33.22020  1.000 94.55895  ? 202  PHE A CB  1 
ATOM   2185 C CG  . PHE A 1 323 ? 61.27377 6.55770   34.15067  1.000 102.06594 ? 202  PHE A CG  1 
ATOM   2186 C CD1 . PHE A 1 323 ? 61.50801 7.09463   35.40515  1.000 100.77357 ? 202  PHE A CD1 1 
ATOM   2187 C CD2 . PHE A 1 323 ? 61.96689 5.41933   33.77305  1.000 100.39108 ? 202  PHE A CD2 1 
ATOM   2188 C CE1 . PHE A 1 323 ? 62.41936 6.50947   36.26577  1.000 102.46736 ? 202  PHE A CE1 1 
ATOM   2189 C CE2 . PHE A 1 323 ? 62.87857 4.82904   34.62760  1.000 98.28804  ? 202  PHE A CE2 1 
ATOM   2190 C CZ  . PHE A 1 323 ? 63.10545 5.37462   35.87586  1.000 99.89332  ? 202  PHE A CZ  1 
ATOM   2191 N N   . LEU A 1 324 ? 57.37404 8.78921   32.77311  1.000 99.26164  ? 203  LEU A N   1 
ATOM   2192 C CA  . LEU A 1 324 ? 56.61246 9.46269   31.72859  1.000 99.43680  ? 203  LEU A CA  1 
ATOM   2193 C C   . LEU A 1 324 ? 57.28480 10.78473  31.38470  1.000 94.37514  ? 203  LEU A C   1 
ATOM   2194 O O   . LEU A 1 324 ? 57.64467 11.55163  32.28025  1.000 90.17887  ? 203  LEU A O   1 
ATOM   2195 C CB  . LEU A 1 324 ? 55.16431 9.70234   32.16530  1.000 86.51472  ? 203  LEU A CB  1 
ATOM   2196 C CG  . LEU A 1 324 ? 54.30157 8.44703   32.30524  1.000 88.24689  ? 203  LEU A CG  1 
ATOM   2197 C CD1 . LEU A 1 324 ? 54.06264 8.12725   33.77165  1.000 89.64219  ? 203  LEU A CD1 1 
ATOM   2198 C CD2 . LEU A 1 324 ? 52.98553 8.60828   31.56308  1.000 89.59928  ? 203  LEU A CD2 1 
ATOM   2199 N N   . MET A 1 325 ? 57.46312 11.04262  30.09351  1.000 88.16034  ? 204  MET A N   1 
ATOM   2200 C CA  . MET A 1 325 ? 57.89007 12.35625  29.63362  1.000 77.93141  ? 204  MET A CA  1 
ATOM   2201 C C   . MET A 1 325 ? 56.74087 13.34170  29.76092  1.000 80.21243  ? 204  MET A C   1 
ATOM   2202 O O   . MET A 1 325 ? 55.65678 13.11505  29.20840  1.000 88.15900  ? 204  MET A O   1 
ATOM   2203 C CB  . MET A 1 325 ? 58.36446 12.29818  28.18621  1.000 77.12962  ? 204  MET A CB  1 
ATOM   2204 C CG  . MET A 1 325 ? 58.48899 13.66164  27.52893  1.000 79.39188  ? 204  MET A CG  1 
ATOM   2205 S SD  . MET A 1 325 ? 58.89786 13.56706  25.77627  1.000 88.15126  ? 204  MET A SD  1 
ATOM   2206 C CE  . MET A 1 325 ? 57.86833 12.19588  25.26153  1.000 86.25677  ? 204  MET A CE  1 
ATOM   2207 N N   . ASP A 1 326 ? 56.97414 14.40470  30.52631  1.000 81.74457  ? 205  ASP A N   1 
ATOM   2208 C CA  . ASP A 1 326 ? 56.08883 15.55711  30.55003  1.000 73.31340  ? 205  ASP A CA  1 
ATOM   2209 C C   . ASP A 1 326 ? 56.04174 16.19517  29.16822  1.000 77.82270  ? 205  ASP A C   1 
ATOM   2210 O O   . ASP A 1 326 ? 57.08238 16.48082  28.56630  1.000 77.58495  ? 205  ASP A O   1 
ATOM   2211 C CB  . ASP A 1 326 ? 56.58981 16.56095  31.59181  1.000 65.71949  ? 205  ASP A CB  1 
ATOM   2212 C CG  . ASP A 1 326 ? 55.66130 17.74636  31.77576  1.000 79.30642  ? 205  ASP A CG  1 
ATOM   2213 O OD1 . ASP A 1 326 ? 54.66128 17.86566  31.03738  1.000 83.99423  ? 205  ASP A OD1 1 
ATOM   2214 O OD2 . ASP A 1 326 ? 55.93760 18.56715  32.67598  1.000 76.00307  ? 205  ASP A OD2 1 
ATOM   2215 N N   . ILE A 1 327 ? 54.82960 16.42051  28.66602  1.000 77.17755  ? 206  ILE A N   1 
ATOM   2216 C CA  . ILE A 1 327 ? 54.63480 17.02392  27.35527  1.000 72.41742  ? 206  ILE A CA  1 
ATOM   2217 C C   . ILE A 1 327 ? 54.09125 18.44211  27.46638  1.000 78.71253  ? 206  ILE A C   1 
ATOM   2218 O O   . ILE A 1 327 ? 53.63354 19.01042  26.46698  1.000 77.77295  ? 206  ILE A O   1 
ATOM   2219 C CB  . ILE A 1 327 ? 53.73214 16.15527  26.46590  1.000 73.97146  ? 206  ILE A CB  1 
ATOM   2220 C CG1 . ILE A 1 327 ? 52.38164 15.92322  27.14099  1.000 57.78850  ? 206  ILE A CG1 1 
ATOM   2221 C CG2 . ILE A 1 327 ? 54.41955 14.83353  26.14366  1.000 67.97859  ? 206  ILE A CG2 1 
ATOM   2222 C CD1 . ILE A 1 327 ? 51.42563 15.08880  26.31377  1.000 71.88957  ? 206  ILE A CD1 1 
ATOM   2223 N N   . GLY A 1 328 ? 54.13226 19.02755  28.65920  1.000 70.53919  ? 207  GLY A N   1 
ATOM   2224 C CA  . GLY A 1 328 ? 53.70193 20.39941  28.86797  1.000 67.80556  ? 207  GLY A CA  1 
ATOM   2225 C C   . GLY A 1 328 ? 52.21961 20.65737  28.70876  1.000 67.59286  ? 207  GLY A C   1 
ATOM   2226 O O   . GLY A 1 328 ? 51.83659 21.67054  28.11267  1.000 68.38773  ? 207  GLY A O   1 
ATOM   2227 N N   . ILE A 1 329 ? 51.37191 19.77148  29.22589  1.000 58.38144  ? 208  ILE A N   1 
ATOM   2228 C CA  . ILE A 1 329 ? 49.93720 20.02319  29.32891  1.000 56.14701  ? 208  ILE A CA  1 
ATOM   2229 C C   . ILE A 1 329 ? 49.50168 19.70288  30.75279  1.000 68.56450  ? 208  ILE A C   1 
ATOM   2230 O O   . ILE A 1 329 ? 49.37237 18.52507  31.12494  1.000 76.88277  ? 208  ILE A O   1 
ATOM   2231 C CB  . ILE A 1 329 ? 49.12513 19.21591  28.30793  1.000 62.10700  ? 208  ILE A CB  1 
ATOM   2232 C CG1 . ILE A 1 329 ? 49.57279 19.56955  26.88740  1.000 61.52298  ? 208  ILE A CG1 1 
ATOM   2233 C CG2 . ILE A 1 329 ? 47.63971 19.50184  28.46907  1.000 63.10986  ? 208  ILE A CG2 1 
ATOM   2234 C CD1 . ILE A 1 329 ? 49.15976 18.56487  25.84408  1.000 71.74545  ? 208  ILE A CD1 1 
ATOM   2235 N N   . TRP A 1 330 ? 49.26079 20.74886  31.54189  1.000 62.08495  ? 209  TRP A N   1 
ATOM   2236 C CA  . TRP A 1 330 ? 48.84729 20.63172  32.92954  1.000 68.23685  ? 209  TRP A CA  1 
ATOM   2237 C C   . TRP A 1 330 ? 47.46030 21.23870  33.11377  1.000 84.80644  ? 209  TRP A C   1 
ATOM   2238 O O   . TRP A 1 330 ? 47.02442 22.10172  32.34642  1.000 101.48353 ? 209  TRP A O   1 
ATOM   2239 C CB  . TRP A 1 330 ? 49.84145 21.32528  33.87615  1.000 66.80057  ? 209  TRP A CB  1 
ATOM   2240 C CG  . TRP A 1 330 ? 51.20357 20.67741  33.95422  1.000 81.62054  ? 209  TRP A CG  1 
ATOM   2241 C CD1 . TRP A 1 330 ? 51.78756 19.86876  33.02025  1.000 79.89029  ? 209  TRP A CD1 1 
ATOM   2242 C CD2 . TRP A 1 330 ? 52.15303 20.80068  35.02274  1.000 90.44982  ? 209  TRP A CD2 1 
ATOM   2243 N NE1 . TRP A 1 330 ? 53.03502 19.47896  33.44185  1.000 73.30803  ? 209  TRP A NE1 1 
ATOM   2244 C CE2 . TRP A 1 330 ? 53.28364 20.03714  34.66808  1.000 84.30136  ? 209  TRP A CE2 1 
ATOM   2245 C CE3 . TRP A 1 330 ? 52.15499 21.48035  36.24529  1.000 83.89660  ? 209  TRP A CE3 1 
ATOM   2246 C CZ2 . TRP A 1 330 ? 54.40183 19.93393  35.49141  1.000 90.54622  ? 209  TRP A CZ2 1 
ATOM   2247 C CZ3 . TRP A 1 330 ? 53.26675 21.37699  37.06022  1.000 84.05360  ? 209  TRP A CZ3 1 
ATOM   2248 C CH2 . TRP A 1 330 ? 54.37413 20.61099  36.68012  1.000 86.76042  ? 209  TRP A CH2 1 
ATOM   2249 N N   . LEU A 1 331 ? 46.77477 20.77012  34.15333  1.000 80.74175  ? 210  LEU A N   1 
ATOM   2250 C CA  . LEU A 1 331 ? 45.49076 21.29848  34.59404  1.000 92.60741  ? 210  LEU A CA  1 
ATOM   2251 C C   . LEU A 1 331 ? 45.59225 21.53860  36.09164  1.000 87.86358  ? 210  LEU A C   1 
ATOM   2252 O O   . LEU A 1 331 ? 46.07923 20.67036  36.82307  1.000 87.89836  ? 210  LEU A O   1 
ATOM   2253 C CB  . LEU A 1 331 ? 44.34653 20.32161  34.29530  1.000 97.83716  ? 210  LEU A CB  1 
ATOM   2254 C CG  . LEU A 1 331 ? 44.35983 19.55499  32.97203  1.000 93.98811  ? 210  LEU A CG  1 
ATOM   2255 C CD1 . LEU A 1 331 ? 43.25161 18.51306  32.95477  1.000 96.33967  ? 210  LEU A CD1 1 
ATOM   2256 C CD2 . LEU A 1 331 ? 44.21431 20.50645  31.80799  1.000 90.04678  ? 210  LEU A CD2 1 
ATOM   2257 N N   . LEU A 1 332 ? 45.11881 22.69520  36.55021  1.000 77.42818  ? 211  LEU A N   1 
ATOM   2258 C CA  . LEU A 1 332 ? 45.19806 23.06298  37.95694  1.000 78.18432  ? 211  LEU A CA  1 
ATOM   2259 C C   . LEU A 1 332 ? 43.82042 23.40177  38.51040  1.000 81.91545  ? 211  LEU A C   1 
ATOM   2260 O O   . LEU A 1 332 ? 42.99720 24.02258  37.82980  1.000 73.46322  ? 211  LEU A O   1 
ATOM   2261 C CB  . LEU A 1 332 ? 46.14280 24.25369  38.16538  1.000 69.78022  ? 211  LEU A CB  1 
ATOM   2262 C CG  . LEU A 1 332 ? 47.58963 24.12686  37.67690  1.000 76.56952  ? 211  LEU A CG  1 
ATOM   2263 C CD1 . LEU A 1 332 ? 48.44108 25.23123  38.27756  1.000 66.06490  ? 211  LEU A CD1 1 
ATOM   2264 C CD2 . LEU A 1 332 ? 48.17534 22.76554  38.01943  1.000 74.93423  ? 211  LEU A CD2 1 
ATOM   2265 N N   . SER A 1 333 ? 43.57893 22.97696  39.74785  1.000 82.41828  ? 212  SER A N   1 
ATOM   2266 C CA  . SER A 1 333 ? 42.41321 23.38346  40.51549  1.000 76.82113  ? 212  SER A CA  1 
ATOM   2267 C C   . SER A 1 333 ? 42.62356 24.77479  41.10991  1.000 81.40035  ? 212  SER A C   1 
ATOM   2268 O O   . SER A 1 333 ? 43.74669 25.28410  41.18351  1.000 82.30213  ? 212  SER A O   1 
ATOM   2269 C CB  . SER A 1 333 ? 42.12535 22.37495  41.62740  1.000 84.37797  ? 212  SER A CB  1 
ATOM   2270 O OG  . SER A 1 333 ? 43.08192 22.48175  42.66985  1.000 76.88239  ? 212  SER A OG  1 
ATOM   2271 N N   . ASP A 1 334 ? 41.51195 25.39614  41.52114  1.000 79.14678  ? 213  ASP A N   1 
ATOM   2272 C CA  . ASP A 1 334 ? 41.56735 26.73858  42.09783  1.000 85.98425  ? 213  ASP A CA  1 
ATOM   2273 C C   . ASP A 1 334 ? 42.54362 26.81078  43.26730  1.000 90.69017  ? 213  ASP A C   1 
ATOM   2274 O O   . ASP A 1 334 ? 43.25293 27.80931  43.43450  1.000 97.92776  ? 213  ASP A O   1 
ATOM   2275 C CB  . ASP A 1 334 ? 40.17180 27.17099  42.55434  1.000 94.28946  ? 213  ASP A CB  1 
ATOM   2276 C CG  . ASP A 1 334 ? 39.20444 27.34902  41.39912  1.000 97.81221  ? 213  ASP A CG  1 
ATOM   2277 O OD1 . ASP A 1 334 ? 39.39829 26.70233  40.34787  1.000 91.00768  ? 213  ASP A OD1 1 
ATOM   2278 O OD2 . ASP A 1 334 ? 38.24782 28.14086  41.54493  1.000 94.39925  ? 213  ASP A OD2 1 
ATOM   2279 N N   . ARG A 1 335 ? 42.58819 25.76344  44.09382  1.000 103.43866 ? 214  ARG A N   1 
ATOM   2280 C CA  . ARG A 1 335 ? 43.48360 25.77032  45.24701  1.000 103.86131 ? 214  ARG A CA  1 
ATOM   2281 C C   . ARG A 1 335 ? 44.93619 25.66378  44.80330  1.000 99.66645  ? 214  ARG A C   1 
ATOM   2282 O O   . ARG A 1 335 ? 45.80777 26.38570  45.31030  1.000 90.07698  ? 214  ARG A O   1 
ATOM   2283 C CB  . ARG A 1 335 ? 43.11459 24.62981  46.19745  1.000 98.65864  ? 214  ARG A CB  1 
ATOM   2284 C CG  . ARG A 1 335 ? 44.05421 24.44483  47.37643  1.000 106.55817 ? 214  ARG A CG  1 
ATOM   2285 C CD  . ARG A 1 335 ? 43.47238 23.45521  48.37440  1.000 118.52609 ? 214  ARG A CD  1 
ATOM   2286 N NE  . ARG A 1 335 ? 44.49958 22.65255  49.02917  1.000 125.18541 ? 214  ARG A NE  1 
ATOM   2287 C CZ  . ARG A 1 335 ? 44.74322 21.37887  48.73936  1.000 127.37560 ? 214  ARG A CZ  1 
ATOM   2288 N NH1 . ARG A 1 335 ? 44.02656 20.76052  47.80995  1.000 130.99525 ? 214  ARG A NH1 1 
ATOM   2289 N NH2 . ARG A 1 335 ? 45.69690 20.72013  49.38351  1.000 122.97807 ? 214  ARG A NH2 1 
ATOM   2290 N N   . ALA A 1 336 ? 45.20612 24.76832  43.84928  1.000 92.25708  ? 215  ALA A N   1 
ATOM   2291 C CA  . ALA A 1 336 ? 46.50586 24.73194  43.19124  1.000 92.67709  ? 215  ALA A CA  1 
ATOM   2292 C C   . ALA A 1 336 ? 46.87572 26.09423  42.62455  1.000 82.11249  ? 215  ALA A C   1 
ATOM   2293 O O   . ALA A 1 336 ? 48.02583 26.53038  42.73904  1.000 75.33855  ? 215  ALA A O   1 
ATOM   2294 C CB  . ALA A 1 336 ? 46.50512 23.67278  42.08865  1.000 94.16227  ? 215  ALA A CB  1 
ATOM   2295 N N   . VAL A 1 337 ? 45.91901 26.77251  41.98859  1.000 86.09507  ? 216  VAL A N   1 
ATOM   2296 C CA  . VAL A 1 337 ? 46.21777 28.06159  41.37267  1.000 95.93081  ? 216  VAL A CA  1 
ATOM   2297 C C   . VAL A 1 337 ? 46.59488 29.08259  42.43842  1.000 106.98761 ? 216  VAL A C   1 
ATOM   2298 O O   . VAL A 1 337 ? 47.59070 29.79948  42.30493  1.000 93.43323  ? 216  VAL A O   1 
ATOM   2299 C CB  . VAL A 1 337 ? 45.02668 28.54208  40.52483  1.000 91.67343  ? 216  VAL A CB  1 
ATOM   2300 C CG1 . VAL A 1 337 ? 45.11663 30.04098  40.28078  1.000 85.00517  ? 216  VAL A CG1 1 
ATOM   2301 C CG2 . VAL A 1 337 ? 44.98226 27.78703  39.20718  1.000 93.50543  ? 216  VAL A CG2 1 
ATOM   2302 N N   . GLU A 1 338 ? 45.80615 29.15774  43.51516  1.000 107.74435 ? 217  GLU A N   1 
ATOM   2303 C CA  . GLU A 1 338 ? 46.12239 30.06625  44.61621  1.000 104.21439 ? 217  GLU A CA  1 
ATOM   2304 C C   . GLU A 1 338 ? 47.51202 29.79475  45.18556  1.000 101.67565 ? 217  GLU A C   1 
ATOM   2305 O O   . GLU A 1 338 ? 48.27955 30.73140  45.45390  1.000 92.28481  ? 217  GLU A O   1 
ATOM   2306 C CB  . GLU A 1 338 ? 45.05868 29.95136  45.70913  1.000 105.44405 ? 217  GLU A CB  1 
ATOM   2307 C CG  . GLU A 1 338 ? 45.46778 30.54518  47.05019  1.000 118.35883 ? 217  GLU A CG  1 
ATOM   2308 C CD  . GLU A 1 338 ? 44.38198 30.41567  48.10047  1.000 127.48344 ? 217  GLU A CD  1 
ATOM   2309 O OE1 . GLU A 1 338 ? 43.41043 31.19948  48.05543  1.000 128.99303 ? 217  GLU A OE1 1 
ATOM   2310 O OE2 . GLU A 1 338 ? 44.50058 29.52865  48.97163  1.000 133.09016 ? 217  GLU A OE2 1 
ATOM   2311 N N   . ILE A 1 339 ? 47.85791 28.51721  45.36567  1.000 96.34822  ? 218  ILE A N   1 
ATOM   2312 C CA  . ILE A 1 339 ? 49.14055 28.17491  45.97632  1.000 96.13086  ? 218  ILE A CA  1 
ATOM   2313 C C   . ILE A 1 339 ? 50.29252 28.53157  45.04186  1.000 95.52814  ? 218  ILE A C   1 
ATOM   2314 O O   . ILE A 1 339 ? 51.28547 29.13690  45.46208  1.000 94.06900  ? 218  ILE A O   1 
ATOM   2315 C CB  . ILE A 1 339 ? 49.16707 26.68969  46.37781  1.000 97.33087  ? 218  ILE A CB  1 
ATOM   2316 C CG1 . ILE A 1 339 ? 48.21129 26.44684  47.54921  1.000 111.94612 ? 218  ILE A CG1 1 
ATOM   2317 C CG2 . ILE A 1 339 ? 50.57917 26.25683  46.74114  1.000 93.52818  ? 218  ILE A CG2 1 
ATOM   2318 C CD1 . ILE A 1 339 ? 48.10698 24.99781  47.97175  1.000 117.79156 ? 218  ILE A CD1 1 
ATOM   2319 N N   . LEU A 1 340 ? 50.19175 28.13699  43.76932  1.000 98.72921  ? 219  LEU A N   1 
ATOM   2320 C CA  . LEU A 1 340 ? 51.16309 28.56744  42.76641  1.000 89.97109  ? 219  LEU A CA  1 
ATOM   2321 C C   . LEU A 1 340 ? 51.33415 30.08216  42.76887  1.000 90.34900  ? 219  LEU A C   1 
ATOM   2322 O O   . LEU A 1 340 ? 52.45939 30.59247  42.74415  1.000 95.23974  ? 219  LEU A O   1 
ATOM   2323 C CB  . LEU A 1 340 ? 50.73178 28.08499  41.38013  1.000 83.40949  ? 219  LEU A CB  1 
ATOM   2324 C CG  . LEU A 1 340 ? 51.51884 28.63714  40.18696  1.000 83.30615  ? 219  LEU A CG  1 
ATOM   2325 C CD1 . LEU A 1 340 ? 52.98339 28.25450  40.27956  1.000 94.81998  ? 219  LEU A CD1 1 
ATOM   2326 C CD2 . LEU A 1 340 ? 50.92404 28.16403  38.87186  1.000 77.22234  ? 219  LEU A CD2 1 
ATOM   2327 N N   . MET A 1 341 ? 50.22019 30.81799  42.79265  1.000 94.99261  ? 220  MET A N   1 
ATOM   2328 C CA  . MET A 1 341 ? 50.28453 32.27259  42.70994  1.000 101.59188 ? 220  MET A CA  1 
ATOM   2329 C C   . MET A 1 341 ? 51.00105 32.86885  43.91173  1.000 107.16638 ? 220  MET A C   1 
ATOM   2330 O O   . MET A 1 341 ? 51.81995 33.78170  43.75881  1.000 98.78868  ? 220  MET A O   1 
ATOM   2331 C CB  . MET A 1 341 ? 48.87844 32.85404  42.57607  1.000 92.31992  ? 220  MET A CB  1 
ATOM   2332 C CG  . MET A 1 341 ? 48.22099 32.53871  41.24562  1.000 96.99664  ? 220  MET A CG  1 
ATOM   2333 S SD  . MET A 1 341 ? 46.90666 33.68253  40.81603  1.000 90.03765  ? 220  MET A SD  1 
ATOM   2334 C CE  . MET A 1 341 ? 47.72640 35.25066  41.09248  1.000 99.20813  ? 220  MET A CE  1 
ATOM   2335 N N   . LYS A 1 342 ? 50.71814 32.36658  45.11716  1.000 115.21424 ? 221  LYS A N   1 
ATOM   2336 C CA  . LYS A 1 342 ? 51.42047 32.91130  46.27447  1.000 122.64789 ? 221  LYS A CA  1 
ATOM   2337 C C   . LYS A 1 342 ? 52.88224 32.48135  46.28128  1.000 120.89265 ? 221  LYS A C   1 
ATOM   2338 O O   . LYS A 1 342 ? 53.73717 33.21552  46.78796  1.000 121.68353 ? 221  LYS A O   1 
ATOM   2339 C CB  . LYS A 1 342 ? 50.72410 32.51353  47.57876  1.000 131.67187 ? 221  LYS A CB  1 
ATOM   2340 C CG  . LYS A 1 342 ? 50.74872 31.03694  47.92107  1.000 138.07488 ? 221  LYS A CG  1 
ATOM   2341 C CD  . LYS A 1 342 ? 49.66186 30.71134  48.93394  1.000 146.73622 ? 221  LYS A CD  1 
ATOM   2342 C CE  . LYS A 1 342 ? 49.81464 31.55713  50.19152  1.000 151.28834 ? 221  LYS A CE  1 
ATOM   2343 N NZ  . LYS A 1 342 ? 48.74353 31.28592  51.19124  1.000 154.97711 ? 221  LYS A NZ  1 
ATOM   2344 N N   . ARG A 1 343 ? 53.19073 31.30703  45.72197  1.000 118.73677 ? 222  ARG A N   1 
ATOM   2345 C CA  . ARG A 1 343 ? 54.58309 30.91765  45.52828  1.000 107.56084 ? 222  ARG A CA  1 
ATOM   2346 C C   . ARG A 1 343 ? 55.26118 31.73257  44.43467  1.000 101.15970 ? 222  ARG A C   1 
ATOM   2347 O O   . ARG A 1 343 ? 56.49494 31.76114  44.37372  1.000 109.70744 ? 222  ARG A O   1 
ATOM   2348 C CB  . ARG A 1 343 ? 54.68026 29.42781  45.19787  1.000 110.36151 ? 222  ARG A CB  1 
ATOM   2349 C CG  . ARG A 1 343 ? 54.42346 28.49836  46.37259  1.000 117.04950 ? 222  ARG A CG  1 
ATOM   2350 C CD  . ARG A 1 343 ? 55.45823 28.70691  47.46817  1.000 119.23303 ? 222  ARG A CD  1 
ATOM   2351 N NE  . ARG A 1 343 ? 55.26659 27.78923  48.58738  1.000 122.23721 ? 222  ARG A NE  1 
ATOM   2352 C CZ  . ARG A 1 343 ? 54.69403 28.12368  49.73861  1.000 126.36481 ? 222  ARG A CZ  1 
ATOM   2353 N NH1 . ARG A 1 343 ? 54.26007 29.36191  49.93033  1.000 128.54272 ? 222  ARG A NH1 1 
ATOM   2354 N NH2 . ARG A 1 343 ? 54.56166 27.22199  50.70168  1.000 127.63713 ? 222  ARG A NH2 1 
ATOM   2355 N N   . SER A 1 344 ? 54.48846 32.38939  43.57267  1.000 98.06987  ? 223  SER A N   1 
ATOM   2356 C CA  . SER A 1 344 ? 55.03037 33.28083  42.55627  1.000 100.76976 ? 223  SER A CA  1 
ATOM   2357 C C   . SER A 1 344 ? 55.14434 34.71721  43.04230  1.000 101.79922 ? 223  SER A C   1 
ATOM   2358 O O   . SER A 1 344 ? 55.51682 35.59783  42.25955  1.000 101.56577 ? 223  SER A O   1 
ATOM   2359 C CB  . SER A 1 344 ? 54.17138 33.22752  41.28925  1.000 84.91541  ? 223  SER A CB  1 
ATOM   2360 O OG  . SER A 1 344 ? 54.02518 31.89513  40.83184  1.000 82.75857  ? 223  SER A OG  1 
ATOM   2361 N N   . HIS A 1 345 ? 54.82643 34.97019  44.30646  1.000 106.01447 ? 224  HIS A N   1 
ATOM   2362 C CA  . HIS A 1 345 ? 54.96510 36.28075  44.91540  1.000 125.17052 ? 224  HIS A CA  1 
ATOM   2363 C C   . HIS A 1 345 ? 55.99107 36.19942  46.03641  1.000 144.36067 ? 224  HIS A C   1 
ATOM   2364 O O   . HIS A 1 345 ? 56.29143 35.11907  46.55043  1.000 144.34970 ? 224  HIS A O   1 
ATOM   2365 C CB  . HIS A 1 345 ? 53.62405 36.79001  45.45412  1.000 125.46818 ? 224  HIS A CB  1 
ATOM   2366 C CG  . HIS A 1 345 ? 52.60386 37.04600  44.38878  1.000 122.24056 ? 224  HIS A CG  1 
ATOM   2367 N ND1 . HIS A 1 345 ? 51.95350 36.03171  43.71910  1.000 122.33934 ? 224  HIS A ND1 1 
ATOM   2368 C CD2 . HIS A 1 345 ? 52.11860 38.20300  43.87999  1.000 123.31451 ? 224  HIS A CD2 1 
ATOM   2369 C CE1 . HIS A 1 345 ? 51.11442 36.55264  42.84142  1.000 117.91550 ? 224  HIS A CE1 1 
ATOM   2370 N NE2 . HIS A 1 345 ? 51.19464 37.86854  42.91958  1.000 119.44286 ? 224  HIS A NE2 1 
ATOM   2371 N N   . LYS A 1 346 ? 56.53384 37.35561  46.40875  1.000 162.96265 ? 225  LYS A N   1 
ATOM   2372 C CA  . LYS A 1 346 ? 57.55716 37.40277  47.44147  1.000 180.76465 ? 225  LYS A CA  1 
ATOM   2373 C C   . LYS A 1 346 ? 56.93689 37.14721  48.81653  1.000 188.17242 ? 225  LYS A C   1 
ATOM   2374 O O   . LYS A 1 346 ? 55.71960 37.00781  48.97129  1.000 191.79201 ? 225  LYS A O   1 
ATOM   2375 C CB  . LYS A 1 346 ? 58.27705 38.74883  47.41037  1.000 188.23973 ? 225  LYS A CB  1 
ATOM   2376 C CG  . LYS A 1 346 ? 58.51794 39.29795  46.01225  1.000 191.44004 ? 225  LYS A CG  1 
ATOM   2377 C CD  . LYS A 1 346 ? 58.56761 40.81901  46.02529  1.000 194.05462 ? 225  LYS A CD  1 
ATOM   2378 C CE  . LYS A 1 346 ? 59.26184 41.36799  44.79087  1.000 192.23044 ? 225  LYS A CE  1 
ATOM   2379 N NZ  . LYS A 1 346 ? 60.72540 41.09741  44.80975  1.000 191.18928 ? 225  LYS A NZ  1 
ATOM   2380 N N   . GLU A 1 347 ? 57.79795 37.08483  49.83228  1.000 192.38788 ? 226  GLU A N   1 
ATOM   2381 C CA  . GLU A 1 347 ? 57.35793 36.89601  51.20959  1.000 194.78425 ? 226  GLU A CA  1 
ATOM   2382 C C   . GLU A 1 347 ? 56.56092 38.10033  51.69542  1.000 202.32851 ? 226  GLU A C   1 
ATOM   2383 O O   . GLU A 1 347 ? 55.33017 38.04447  51.78770  1.000 201.91668 ? 226  GLU A O   1 
ATOM   2384 C CB  . GLU A 1 347 ? 58.55727 36.64758  52.12719  1.000 192.47744 ? 226  GLU A CB  1 
ATOM   2385 C CG  . GLU A 1 347 ? 59.12118 35.23602  52.05281  1.000 187.98007 ? 226  GLU A CG  1 
ATOM   2386 C CD  . GLU A 1 347 ? 58.44718 34.28481  53.02352  1.000 187.16914 ? 226  GLU A CD  1 
ATOM   2387 O OE1 . GLU A 1 347 ? 57.74825 33.35817  52.56209  1.000 184.39747 ? 226  GLU A OE1 1 
ATOM   2388 O OE2 . GLU A 1 347 ? 58.61564 34.46281  54.24838  1.000 188.76507 ? 226  GLU A OE2 1 
ATOM   2389 N N   . SER A 1 348 ? 57.25685 39.19348  52.00586  1.000 209.46048 ? 227  SER A N   1 
ATOM   2390 C CA  . SER A 1 348 ? 56.61520 40.39949  52.51453  1.000 215.63991 ? 227  SER A CA  1 
ATOM   2391 C C   . SER A 1 348 ? 55.76830 41.05950  51.43388  1.000 215.04971 ? 227  SER A C   1 
ATOM   2392 O O   . SER A 1 348 ? 54.54026 40.92241  51.43017  1.000 215.49513 ? 227  SER A O   1 
ATOM   2393 C CB  . SER A 1 348 ? 57.66487 41.37990  53.04299  1.000 217.42371 ? 227  SER A CB  1 
ATOM   2394 O OG  . SER A 1 348 ? 58.51163 40.75798  53.99486  1.000 217.40882 ? 227  SER A OG  1 
ATOM   2395 N N   . SER A 1 349 ? 56.41335 41.78577  50.52402  1.000 215.27833 ? 228  SER A N   1 
ATOM   2396 C CA  . SER A 1 349 ? 55.71764 42.31996  49.36218  1.000 215.54494 ? 228  SER A CA  1 
ATOM   2397 C C   . SER A 1 349 ? 55.13901 41.18735  48.52254  1.000 225.71108 ? 228  SER A C   1 
ATOM   2398 O O   . SER A 1 349 ? 55.69786 40.09131  48.44922  1.000 221.87885 ? 228  SER A O   1 
ATOM   2399 C CB  . SER A 1 349 ? 56.66744 43.17132  48.51849  1.000 208.37193 ? 228  SER A CB  1 
ATOM   2400 O OG  . SER A 1 349 ? 56.09994 43.47139  47.25524  1.000 202.08326 ? 228  SER A OG  1 
ATOM   2401 N N   . GLU A 1 350 ? 53.99357 41.45308  47.90058  1.000 236.94840 ? 229  GLU A N   1 
ATOM   2402 C CA  . GLU A 1 350 ? 53.30818 40.48209  47.04924  1.000 242.93659 ? 229  GLU A CA  1 
ATOM   2403 C C   . GLU A 1 350 ? 53.23619 41.06981  45.64273  1.000 238.16338 ? 229  GLU A C   1 
ATOM   2404 O O   . GLU A 1 350 ? 52.24436 41.70396  45.27433  1.000 241.32218 ? 229  GLU A O   1 
ATOM   2405 C CB  . GLU A 1 350 ? 51.91586 40.15394  47.59630  1.000 248.30639 ? 229  GLU A CB  1 
ATOM   2406 C CG  . GLU A 1 350 ? 51.65366 38.66774  47.78920  1.000 250.71798 ? 229  GLU A CG  1 
ATOM   2407 C CD  . GLU A 1 350 ? 50.28111 38.38626  48.36955  1.000 253.71235 ? 229  GLU A CD  1 
ATOM   2408 O OE1 . GLU A 1 350 ? 49.86249 39.11675  49.29188  1.000 256.71108 ? 229  GLU A OE1 1 
ATOM   2409 O OE2 . GLU A 1 350 ? 49.62201 37.43189  47.90580  1.000 252.37506 ? 229  GLU A OE2 1 
ATOM   2410 N N   . GLU A 1 351 ? 54.29246 40.86061  44.85573  1.000 229.02910 ? 230  GLU A N   1 
ATOM   2411 C CA  . GLU A 1 351 ? 54.35273 41.45912  43.52828  1.000 218.01918 ? 230  GLU A CA  1 
ATOM   2412 C C   . GLU A 1 351 ? 54.80368 40.46263  42.46682  1.000 202.22330 ? 230  GLU A C   1 
ATOM   2413 O O   . GLU A 1 351 ? 53.97700 39.93943  41.71294  1.000 203.61215 ? 230  GLU A O   1 
ATOM   2414 C CB  . GLU A 1 351 ? 55.27880 42.67770  43.53485  1.000 222.25339 ? 230  GLU A CB  1 
ATOM   2415 C CG  . GLU A 1 351 ? 55.04514 43.62134  42.36695  1.000 224.50061 ? 230  GLU A CG  1 
ATOM   2416 C CD  . GLU A 1 351 ? 53.57877 43.97923  42.19243  1.000 227.24787 ? 230  GLU A CD  1 
ATOM   2417 O OE1 . GLU A 1 351 ? 52.90247 44.25497  43.20663  1.000 229.89320 ? 230  GLU A OE1 1 
ATOM   2418 O OE2 . GLU A 1 351 ? 53.09915 43.97753  41.03938  1.000 226.18209 ? 230  GLU A OE2 1 
ATOM   2419 N N   . LEU A 1 352 ? 56.10462 40.18772  42.39757  1.000 185.35175 ? 231  LEU A N   1 
ATOM   2420 C CA  . LEU A 1 352 ? 56.63838 39.36620  41.32118  1.000 166.77869 ? 231  LEU A CA  1 
ATOM   2421 C C   . LEU A 1 352 ? 57.89406 38.64577  41.78736  1.000 156.73393 ? 231  LEU A C   1 
ATOM   2422 O O   . LEU A 1 352 ? 58.69138 39.19647  42.55069  1.000 164.31955 ? 231  LEU A O   1 
ATOM   2423 C CB  . LEU A 1 352 ? 56.94476 40.21226  40.07664  1.000 164.31391 ? 231  LEU A CB  1 
ATOM   2424 C CG  . LEU A 1 352 ? 58.03850 41.28312  40.17065  1.000 161.81697 ? 231  LEU A CG  1 
ATOM   2425 C CD1 . LEU A 1 352 ? 59.37991 40.76023  39.66558  1.000 157.97214 ? 231  LEU A CD1 1 
ATOM   2426 C CD2 . LEU A 1 352 ? 57.63218 42.53805  39.41178  1.000 161.37384 ? 231  LEU A CD2 1 
ATOM   2427 N N   . LYS A 1 353 ? 58.05733 37.41144  41.31967  1.000 140.41601 ? 232  LYS A N   1 
ATOM   2428 C CA  . LYS A 1 353 ? 59.24908 36.62207  41.59053  1.000 129.77312 ? 232  LYS A CA  1 
ATOM   2429 C C   . LYS A 1 353 ? 59.38118 35.58430  40.48828  1.000 120.76252 ? 232  LYS A C   1 
ATOM   2430 O O   . LYS A 1 353 ? 58.37673 35.02436  40.04217  1.000 117.43303 ? 232  LYS A O   1 
ATOM   2431 C CB  . LYS A 1 353 ? 59.18147 35.93783  42.96113  1.000 130.86975 ? 232  LYS A CB  1 
ATOM   2432 C CG  . LYS A 1 353 ? 60.50400 35.33225  43.41209  1.000 133.36390 ? 232  LYS A CG  1 
ATOM   2433 C CD  . LYS A 1 353 ? 60.37890 34.63420  44.75821  1.000 127.78528 ? 232  LYS A CD  1 
ATOM   2434 C CE  . LYS A 1 353 ? 59.65528 33.30334  44.62464  1.000 122.95930 ? 232  LYS A CE  1 
ATOM   2435 N NZ  . LYS A 1 353 ? 59.89223 32.41948  45.79954  1.000 118.66740 ? 232  LYS A NZ  1 
ATOM   2436 N N   . TYR A 1 354 ? 60.61116 35.33920  40.04307  1.000 119.16033 ? 233  TYR A N   1 
ATOM   2437 C CA  . TYR A 1 354 ? 60.84264 34.18373  39.18944  1.000 117.37448 ? 233  TYR A CA  1 
ATOM   2438 C C   . TYR A 1 354 ? 60.48253 32.91838  39.95012  1.000 110.44641 ? 233  TYR A C   1 
ATOM   2439 O O   . TYR A 1 354 ? 61.03336 32.64453  41.02110  1.000 119.39895 ? 233  TYR A O   1 
ATOM   2440 C CB  . TYR A 1 354 ? 62.29477 34.12435  38.71451  1.000 114.40509 ? 233  TYR A CB  1 
ATOM   2441 C CG  . TYR A 1 354 ? 62.60969 32.85776  37.93955  1.000 111.46158 ? 233  TYR A CG  1 
ATOM   2442 C CD1 . TYR A 1 354 ? 62.44675 32.80599  36.56115  1.000 110.96470 ? 233  TYR A CD1 1 
ATOM   2443 C CD2 . TYR A 1 354 ? 63.06640 31.71349  38.58705  1.000 112.72479 ? 233  TYR A CD2 1 
ATOM   2444 C CE1 . TYR A 1 354 ? 62.72609 31.65178  35.85026  1.000 108.39079 ? 233  TYR A CE1 1 
ATOM   2445 C CE2 . TYR A 1 354 ? 63.34536 30.55606  37.88498  1.000 114.51058 ? 233  TYR A CE2 1 
ATOM   2446 C CZ  . TYR A 1 354 ? 63.17497 30.53114  36.51722  1.000 113.84259 ? 233  TYR A CZ  1 
ATOM   2447 O OH  . TYR A 1 354 ? 63.45613 29.38243  35.81346  1.000 112.38199 ? 233  TYR A OH  1 
ATOM   2448 N N   . TYR A 1 355 ? 59.55623 32.14833  39.39346  1.000 94.33734  ? 234  TYR A N   1 
ATOM   2449 C CA  . TYR A 1 355 ? 59.16558 30.87280  39.96831  1.000 86.86249  ? 234  TYR A CA  1 
ATOM   2450 C C   . TYR A 1 355 ? 58.97646 29.90753  38.81130  1.000 88.73464  ? 234  TYR A C   1 
ATOM   2451 O O   . TYR A 1 355 ? 58.27413 30.22770  37.84796  1.000 86.33091  ? 234  TYR A O   1 
ATOM   2452 C CB  . TYR A 1 355 ? 57.88014 31.02689  40.78880  1.000 86.64864  ? 234  TYR A CB  1 
ATOM   2453 C CG  . TYR A 1 355 ? 57.49820 29.83290  41.62887  1.000 93.15323  ? 234  TYR A CG  1 
ATOM   2454 C CD1 . TYR A 1 355 ? 58.28202 29.43768  42.70312  1.000 91.33855  ? 234  TYR A CD1 1 
ATOM   2455 C CD2 . TYR A 1 355 ? 56.33885 29.11888  41.36690  1.000 96.09538  ? 234  TYR A CD2 1 
ATOM   2456 C CE1 . TYR A 1 355 ? 57.92968 28.35544  43.48271  1.000 87.83144  ? 234  TYR A CE1 1 
ATOM   2457 C CE2 . TYR A 1 355 ? 55.98057 28.03686  42.13930  1.000 93.28374  ? 234  TYR A CE2 1 
ATOM   2458 C CZ  . TYR A 1 355 ? 56.77985 27.65654  43.19358  1.000 92.54659  ? 234  TYR A CZ  1 
ATOM   2459 O OH  . TYR A 1 355 ? 56.42114 26.57735  43.96701  1.000 100.73502 ? 234  TYR A OH  1 
ATOM   2460 N N   . ASP A 1 356 ? 59.60895 28.74301  38.89129  1.000 94.94985  ? 235  ASP A N   1 
ATOM   2461 C CA  . ASP A 1 356 ? 59.60077 27.78873  37.79182  1.000 93.42473  ? 235  ASP A CA  1 
ATOM   2462 C C   . ASP A 1 356 ? 58.52956 26.74361  38.07199  1.000 96.91763  ? 235  ASP A C   1 
ATOM   2463 O O   . ASP A 1 356 ? 58.59097 26.04066  39.08614  1.000 100.99050 ? 235  ASP A O   1 
ATOM   2464 C CB  . ASP A 1 356 ? 60.97405 27.13897  37.61877  1.000 98.58987  ? 235  ASP A CB  1 
ATOM   2465 C CG  . ASP A 1 356 ? 61.07612 26.30624  36.34925  1.000 93.55086  ? 235  ASP A CG  1 
ATOM   2466 O OD1 . ASP A 1 356 ? 60.05349 26.12460  35.65715  1.000 88.88188  ? 235  ASP A OD1 1 
ATOM   2467 O OD2 . ASP A 1 356 ? 62.18902 25.83387  36.03901  1.000 98.25764  ? 235  ASP A OD2 1 
ATOM   2468 N N   . LEU A 1 357 ? 57.54408 26.65598  37.17716  1.000 94.34031  ? 236  LEU A N   1 
ATOM   2469 C CA  . LEU A 1 357 ? 56.43085 25.73763  37.38520  1.000 91.26936  ? 236  LEU A CA  1 
ATOM   2470 C C   . LEU A 1 357 ? 56.89853 24.28986  37.44047  1.000 92.98918  ? 236  LEU A C   1 
ATOM   2471 O O   . LEU A 1 357 ? 56.31373 23.47343  38.16262  1.000 99.08080  ? 236  LEU A O   1 
ATOM   2472 C CB  . LEU A 1 357 ? 55.39390 25.92292  36.27815  1.000 79.16060  ? 236  LEU A CB  1 
ATOM   2473 C CG  . LEU A 1 357 ? 54.12456 25.07875  36.37321  1.000 76.84482  ? 236  LEU A CG  1 
ATOM   2474 C CD1 . LEU A 1 357 ? 53.34096 25.44201  37.62374  1.000 75.17246  ? 236  LEU A CD1 1 
ATOM   2475 C CD2 . LEU A 1 357 ? 53.27290 25.25685  35.12724  1.000 84.75461  ? 236  LEU A CD2 1 
ATOM   2476 N N   . TYR A 1 358 ? 57.95448 23.95602  36.70077  1.000 89.79429  ? 237  TYR A N   1 
ATOM   2477 C CA  . TYR A 1 358 ? 58.36846 22.57080  36.53549  1.000 95.27989  ? 237  TYR A CA  1 
ATOM   2478 C C   . TYR A 1 358 ? 59.53043 22.17625  37.43479  1.000 108.86661 ? 237  TYR A C   1 
ATOM   2479 O O   . TYR A 1 358 ? 59.67876 20.98711  37.73873  1.000 117.13488 ? 237  TYR A O   1 
ATOM   2480 C CB  . TYR A 1 358 ? 58.74150 22.30488  35.07091  1.000 96.85604  ? 237  TYR A CB  1 
ATOM   2481 C CG  . TYR A 1 358 ? 57.69257 22.78756  34.09227  1.000 94.10844  ? 237  TYR A CG  1 
ATOM   2482 C CD1 . TYR A 1 358 ? 56.62591 21.97413  33.73611  1.000 102.07056 ? 237  TYR A CD1 1 
ATOM   2483 C CD2 . TYR A 1 358 ? 57.76602 24.05542  33.52756  1.000 91.01736  ? 237  TYR A CD2 1 
ATOM   2484 C CE1 . TYR A 1 358 ? 55.65933 22.40727  32.84767  1.000 104.58994 ? 237  TYR A CE1 1 
ATOM   2485 C CE2 . TYR A 1 358 ? 56.80471 24.49703  32.63680  1.000 93.88297  ? 237  TYR A CE2 1 
ATOM   2486 C CZ  . TYR A 1 358 ? 55.75321 23.66909  32.30045  1.000 102.07485 ? 237  TYR A CZ  1 
ATOM   2487 O OH  . TYR A 1 358 ? 54.79217 24.10488  31.41534  1.000 95.24782  ? 237  TYR A OH  1 
ATOM   2488 N N   . SER A 1 359 ? 60.34593 23.13306  37.87219  1.000 114.69601 ? 238  SER A N   1 
ATOM   2489 C CA  . SER A 1 359 ? 61.50879 22.84774  38.70559  1.000 109.20542 ? 238  SER A CA  1 
ATOM   2490 C C   . SER A 1 359 ? 61.34381 23.30536  40.14522  1.000 110.13671 ? 238  SER A C   1 
ATOM   2491 O O   . SER A 1 359 ? 61.83991 22.64552  41.05586  1.000 123.55526 ? 238  SER A O   1 
ATOM   2492 C CB  . SER A 1 359 ? 62.76133 23.50116  38.11024  1.000 104.91183 ? 238  SER A CB  1 
ATOM   2493 O OG  . SER A 1 359 ? 63.21659 22.77992  36.98049  1.000 104.60944 ? 238  SER A OG  1 
ATOM   2494 N N   . ASP A 1 360 ? 60.66802 24.42729  40.37879  1.000 106.03199 ? 239  ASP A N   1 
ATOM   2495 C CA  . ASP A 1 360 ? 60.31071 24.81440  41.74230  1.000 92.73760  ? 239  ASP A CA  1 
ATOM   2496 C C   . ASP A 1 360 ? 59.01340 24.13041  42.15786  1.000 86.04683  ? 239  ASP A C   1 
ATOM   2497 O O   . ASP A 1 360 ? 59.02207 23.18679  42.95181  1.000 81.22290  ? 239  ASP A O   1 
ATOM   2498 C CB  . ASP A 1 360 ? 60.19436 26.33722  41.84956  1.000 98.82072  ? 239  ASP A CB  1 
ATOM   2499 C CG  . ASP A 1 360 ? 61.44605 27.05503  41.38890  1.000 118.29664 ? 239  ASP A CG  1 
ATOM   2500 O OD1 . ASP A 1 360 ? 62.40990 26.37107  40.98539  1.000 127.96363 ? 239  ASP A OD1 1 
ATOM   2501 O OD2 . ASP A 1 360 ? 61.46717 28.30362  41.43785  1.000 119.52473 ? 239  ASP A OD2 1 
ATOM   2502 N N   . PHE A 1 361 ? 57.88685 24.61562  41.63034  1.000 106.28958 ? 240  PHE A N   1 
ATOM   2503 C CA  . PHE A 1 361 ? 56.57500 24.05327  41.94554  1.000 96.44269  ? 240  PHE A CA  1 
ATOM   2504 C C   . PHE A 1 361 ? 56.52163 22.55164  41.67394  1.000 98.39457  ? 240  PHE A C   1 
ATOM   2505 O O   . PHE A 1 361 ? 56.09501 21.76793  42.52949  1.000 101.22772 ? 240  PHE A O   1 
ATOM   2506 C CB  . PHE A 1 361 ? 55.50394 24.79014  41.13648  1.000 104.23253 ? 240  PHE A CB  1 
ATOM   2507 C CG  . PHE A 1 361 ? 54.09133 24.42004  41.49804  1.000 109.78742 ? 240  PHE A CG  1 
ATOM   2508 C CD1 . PHE A 1 361 ? 53.39346 25.14900  42.44907  1.000 113.69410 ? 240  PHE A CD1 1 
ATOM   2509 C CD2 . PHE A 1 361 ? 53.44994 23.36731  40.86519  1.000 110.16521 ? 240  PHE A CD2 1 
ATOM   2510 C CE1 . PHE A 1 361 ? 52.09093 24.81891  42.77771  1.000 120.03821 ? 240  PHE A CE1 1 
ATOM   2511 C CE2 . PHE A 1 361 ? 52.14924 23.03361  41.18808  1.000 112.81405 ? 240  PHE A CE2 1 
ATOM   2512 C CZ  . PHE A 1 361 ? 51.46839 23.76097  42.14554  1.000 117.71837 ? 240  PHE A CZ  1 
ATOM   2513 N N   . GLY A 1 362 ? 56.95194 22.13564  40.48057  1.000 103.28489 ? 241  GLY A N   1 
ATOM   2514 C CA  . GLY A 1 362 ? 56.77603 20.74778  40.07656  1.000 103.22541 ? 241  GLY A CA  1 
ATOM   2515 C C   . GLY A 1 362 ? 57.51294 19.75991  40.96243  1.000 112.74331 ? 241  GLY A C   1 
ATOM   2516 O O   . GLY A 1 362 ? 56.94369 18.75409  41.39484  1.000 109.36518 ? 241  GLY A O   1 
ATOM   2517 N N   . LEU A 1 363 ? 58.79216 20.02937  41.24371  1.000 108.81401 ? 242  LEU A N   1 
ATOM   2518 C CA  . LEU A 1 363 ? 59.59830 19.09850  42.03044  1.000 112.76454 ? 242  LEU A CA  1 
ATOM   2519 C C   . LEU A 1 363 ? 59.08523 18.91329  43.45493  1.000 113.20020 ? 242  LEU A C   1 
ATOM   2520 O O   . LEU A 1 363 ? 59.54307 17.99318  44.14253  1.000 110.37007 ? 242  LEU A O   1 
ATOM   2521 C CB  . LEU A 1 363 ? 61.06184 19.55631  42.07156  1.000 116.16905 ? 242  LEU A CB  1 
ATOM   2522 C CG  . LEU A 1 363 ? 61.89621 19.40947  40.79262  1.000 115.67223 ? 242  LEU A CG  1 
ATOM   2523 C CD1 . LEU A 1 363 ? 63.32500 19.89310  41.01189  1.000 112.66034 ? 242  LEU A CD1 1 
ATOM   2524 C CD2 . LEU A 1 363 ? 61.89028 17.98022  40.29065  1.000 114.74984 ? 242  LEU A CD2 1 
ATOM   2525 N N   . ALA A 1 364 ? 58.15435 19.74804  43.91214  1.000 114.19982 ? 243  ALA A N   1 
ATOM   2526 C CA  . ALA A 1 364 ? 57.59092 19.63906  45.25039  1.000 109.41700 ? 243  ALA A CA  1 
ATOM   2527 C C   . ALA A 1 364 ? 56.34610 18.76056  45.30356  1.000 111.87299 ? 243  ALA A C   1 
ATOM   2528 O O   . ALA A 1 364 ? 55.70986 18.67476  46.35884  1.000 116.91965 ? 243  ALA A O   1 
ATOM   2529 C CB  . ALA A 1 364 ? 57.26749 21.02964  45.80018  1.000 105.37301 ? 243  ALA A CB  1 
ATOM   2530 N N   . LEU A 1 365 ? 55.98306 18.11492  44.19980  1.000 117.21301 ? 244  LEU A N   1 
ATOM   2531 C CA  . LEU A 1 365 ? 54.78528 17.29184  44.13000  1.000 115.80411 ? 244  LEU A CA  1 
ATOM   2532 C C   . LEU A 1 365 ? 55.14797 15.81410  44.20753  1.000 112.60989 ? 244  LEU A C   1 
ATOM   2533 O O   . LEU A 1 365 ? 56.25988 15.40720  43.86132  1.000 119.94852 ? 244  LEU A O   1 
ATOM   2534 C CB  . LEU A 1 365 ? 54.00748 17.56119  42.83927  1.000 110.07508 ? 244  LEU A CB  1 
ATOM   2535 C CG  . LEU A 1 365 ? 53.45477 18.96676  42.60498  1.000 112.30669 ? 244  LEU A CG  1 
ATOM   2536 C CD1 . LEU A 1 365 ? 52.94134 19.10018  41.17929  1.000 102.60741 ? 244  LEU A CD1 1 
ATOM   2537 C CD2 . LEU A 1 365 ? 52.35001 19.27360  43.60066  1.000 115.52245 ? 244  LEU A CD2 1 
ATOM   2538 N N   . GLY A 1 366 ? 54.19590 15.01581  44.66515  1.000 112.71021 ? 245  GLY A N   1 
ATOM   2539 C CA  . GLY A 1 366 ? 54.35728 13.58010  44.75621  1.000 115.65348 ? 245  GLY A CA  1 
ATOM   2540 C C   . GLY A 1 366 ? 54.41913 13.10144  46.19744  1.000 126.67251 ? 245  GLY A C   1 
ATOM   2541 O O   . GLY A 1 366 ? 54.53663 13.87684  47.14716  1.000 119.13871 ? 245  GLY A O   1 
ATOM   2542 N N   . THR A 1 367 ? 54.33802 11.77624  46.33959  1.000 139.35974 ? 246  THR A N   1 
ATOM   2543 C CA  . THR A 1 367 ? 54.39202 11.16294  47.66089  1.000 150.09223 ? 246  THR A CA  1 
ATOM   2544 C C   . THR A 1 367 ? 55.79479 11.18906  48.25331  1.000 150.67053 ? 246  THR A C   1 
ATOM   2545 O O   . THR A 1 367 ? 55.94135 11.03848  49.47074  1.000 159.88930 ? 246  THR A O   1 
ATOM   2546 C CB  . THR A 1 367 ? 53.88269 9.72185   47.59639  1.000 157.09176 ? 246  THR A CB  1 
ATOM   2547 O OG1 . THR A 1 367 ? 54.80784 8.91819   46.85428  1.000 158.28864 ? 246  THR A OG1 1 
ATOM   2548 C CG2 . THR A 1 367 ? 52.52110 9.67028   46.91892  1.000 156.42129 ? 246  THR A CG2 1 
ATOM   2549 N N   . HIS A 1 368 ? 56.82217 11.37404  47.42631  1.000 137.60821 ? 247  HIS A N   1 
ATOM   2550 C CA  . HIS A 1 368 ? 58.20817 11.48931  47.88055  1.000 136.92152 ? 247  HIS A CA  1 
ATOM   2551 C C   . HIS A 1 368 ? 58.86105 12.68033  47.19080  1.000 128.61463 ? 247  HIS A C   1 
ATOM   2552 O O   . HIS A 1 368 ? 59.71254 12.51557  46.30869  1.000 116.68846 ? 247  HIS A O   1 
ATOM   2553 C CB  . HIS A 1 368 ? 58.99111 10.20357  47.60931  1.000 140.78905 ? 247  HIS A CB  1 
ATOM   2554 C CG  . HIS A 1 368 ? 58.49797 9.01867   48.38011  1.000 151.36249 ? 247  HIS A CG  1 
ATOM   2555 N ND1 . HIS A 1 368 ? 57.38331 8.29822   48.00839  1.000 152.02904 ? 247  HIS A ND1 1 
ATOM   2556 C CD2 . HIS A 1 368 ? 58.97083 8.42710   49.50283  1.000 156.41439 ? 247  HIS A CD2 1 
ATOM   2557 C CE1 . HIS A 1 368 ? 57.19014 7.31471   48.86919  1.000 152.45054 ? 247  HIS A CE1 1 
ATOM   2558 N NE2 . HIS A 1 368 ? 58.13944 7.37082   49.78595  1.000 155.68385 ? 247  HIS A NE2 1 
ATOM   2559 N N   . PRO A 1 369 ? 58.47829 13.89964  47.56623  1.000 130.27265 ? 248  PRO A N   1 
ATOM   2560 C CA  . PRO A 1 369 ? 59.02971 15.08049  46.89424  1.000 130.36540 ? 248  PRO A CA  1 
ATOM   2561 C C   . PRO A 1 369 ? 60.52130 15.20783  47.14606  1.000 136.91030 ? 248  PRO A C   1 
ATOM   2562 O O   . PRO A 1 369 ? 61.03823 14.80206  48.18982  1.000 148.68082 ? 248  PRO A O   1 
ATOM   2563 C CB  . PRO A 1 369 ? 58.26109 16.25014  47.52373  1.000 129.77051 ? 248  PRO A CB  1 
ATOM   2564 C CG  . PRO A 1 369 ? 57.14050 15.63373  48.29191  1.000 132.73005 ? 248  PRO A CG  1 
ATOM   2565 C CD  . PRO A 1 369 ? 57.57818 14.26337  48.67013  1.000 132.95105 ? 248  PRO A CD  1 
ATOM   2566 N N   . ARG A 1 370 ? 61.21691 15.78238  46.16781  1.000 132.08420 ? 249  ARG A N   1 
ATOM   2567 C CA  . ARG A 1 370 ? 62.64545 16.01873  46.32377  1.000 133.45518 ? 249  ARG A CA  1 
ATOM   2568 C C   . ARG A 1 370 ? 62.94904 17.35552  46.98670  1.000 144.42473 ? 249  ARG A C   1 
ATOM   2569 O O   . ARG A 1 370 ? 63.87109 17.44297  47.80547  1.000 150.69514 ? 249  ARG A O   1 
ATOM   2570 C CB  . ARG A 1 370 ? 63.34197 15.93726  44.96629  1.000 130.26804 ? 249  ARG A CB  1 
ATOM   2571 C CG  . ARG A 1 370 ? 63.24878 14.57201  44.32385  1.000 127.11352 ? 249  ARG A CG  1 
ATOM   2572 C CD  . ARG A 1 370 ? 64.28131 14.42979  43.23264  1.000 132.39203 ? 249  ARG A CD  1 
ATOM   2573 N NE  . ARG A 1 370 ? 64.77927 13.06280  43.14770  1.000 134.69174 ? 249  ARG A NE  1 
ATOM   2574 C CZ  . ARG A 1 370 ? 65.86236 12.70790  42.46726  1.000 133.24870 ? 249  ARG A CZ  1 
ATOM   2575 N NH1 . ARG A 1 370 ? 66.56626 13.62425  41.81552  1.000 129.68776 ? 249  ARG A NH1 1 
ATOM   2576 N NH2 . ARG A 1 370 ? 66.24293 11.43834  42.44080  1.000 131.11721 ? 249  ARG A NH2 1 
ATOM   2577 N N   . ILE A 1 371 ? 62.19817 18.39977  46.65282  1.000 143.31030 ? 250  ILE A N   1 
ATOM   2578 C CA  . ILE A 1 371 ? 62.30802 19.68308  47.33318  1.000 148.96868 ? 250  ILE A CA  1 
ATOM   2579 C C   . ILE A 1 371 ? 61.07587 19.86312  48.20728  1.000 149.60052 ? 250  ILE A C   1 
ATOM   2580 O O   . ILE A 1 371 ? 59.97414 19.41795  47.86378  1.000 150.17574 ? 250  ILE A O   1 
ATOM   2581 C CB  . ILE A 1 371 ? 62.48416 20.85764  46.34578  1.000 146.96563 ? 250  ILE A CB  1 
ATOM   2582 C CG1 . ILE A 1 371 ? 61.19517 21.13519  45.57434  1.000 146.04383 ? 250  ILE A CG1 1 
ATOM   2583 C CG2 . ILE A 1 371 ? 63.62999 20.57538  45.38584  1.000 146.63410 ? 250  ILE A CG2 1 
ATOM   2584 C CD1 . ILE A 1 371 ? 60.91573 22.61112  45.40305  1.000 143.12708 ? 250  ILE A CD1 1 
ATOM   2585 N N   . GLU A 1 372 ? 61.27158 20.50103  49.35869  1.000 148.37029 ? 251  GLU A N   1 
ATOM   2586 C CA  . GLU A 1 372 ? 60.19476 20.65426  50.32569  1.000 147.74563 ? 251  GLU A CA  1 
ATOM   2587 C C   . GLU A 1 372 ? 59.33542 21.86481  49.99295  1.000 148.72035 ? 251  GLU A C   1 
ATOM   2588 O O   . GLU A 1 372 ? 59.85090 22.94413  49.68575  1.000 146.83175 ? 251  GLU A O   1 
ATOM   2589 C CB  . GLU A 1 372 ? 60.76040 20.80464  51.73633  1.000 153.83456 ? 251  GLU A CB  1 
ATOM   2590 C CG  . GLU A 1 372 ? 61.49899 19.59071  52.26207  1.000 162.87224 ? 251  GLU A CG  1 
ATOM   2591 C CD  . GLU A 1 372 ? 62.17542 19.86699  53.59155  1.000 172.14389 ? 251  GLU A CD  1 
ATOM   2592 O OE1 . GLU A 1 372 ? 62.04845 21.00249  54.09535  1.000 175.31462 ? 251  GLU A OE1 1 
ATOM   2593 O OE2 . GLU A 1 372 ? 62.83592 18.95475  54.13167  1.000 176.18499 ? 251  GLU A OE2 1 
ATOM   2594 N N   . ASP A 1 373 ? 58.02082 21.67831  50.05428  1.000 150.19070 ? 252  ASP A N   1 
ATOM   2595 C CA  . ASP A 1 373 ? 57.08309 22.79425  50.07239  1.000 151.84710 ? 252  ASP A CA  1 
ATOM   2596 C C   . ASP A 1 373 ? 55.86010 22.37424  50.86796  1.000 156.78753 ? 252  ASP A C   1 
ATOM   2597 O O   . ASP A 1 373 ? 55.19330 21.39999  50.50686  1.000 153.84708 ? 252  ASP A O   1 
ATOM   2598 C CB  . ASP A 1 373 ? 56.69254 23.22336  48.65937  1.000 146.14003 ? 252  ASP A CB  1 
ATOM   2599 C CG  . ASP A 1 373 ? 56.27422 24.67874  48.59053  1.000 143.75368 ? 252  ASP A CG  1 
ATOM   2600 O OD1 . ASP A 1 373 ? 55.40863 25.08865  49.39290  1.000 144.81182 ? 252  ASP A OD1 1 
ATOM   2601 O OD2 . ASP A 1 373 ? 56.80868 25.41163  47.73346  1.000 143.02900 ? 252  ASP A OD2 1 
ATOM   2602 N N   . GLU A 1 374 ? 55.58709 23.10225  51.95210  1.000 165.59480 ? 253  GLU A N   1 
ATOM   2603 C CA  . GLU A 1 374 ? 54.48751 22.75320  52.84487  1.000 174.61999 ? 253  GLU A CA  1 
ATOM   2604 C C   . GLU A 1 374 ? 53.16566 22.68788  52.08884  1.000 160.06284 ? 253  GLU A C   1 
ATOM   2605 O O   . GLU A 1 374 ? 52.49106 21.65271  52.07386  1.000 155.93301 ? 253  GLU A O   1 
ATOM   2606 C CB  . GLU A 1 374 ? 54.40372 23.76629  53.98718  1.000 193.13101 ? 253  GLU A CB  1 
ATOM   2607 C CG  . GLU A 1 374 ? 55.73984 24.37398  54.37585  1.000 208.22467 ? 253  GLU A CG  1 
ATOM   2608 C CD  . GLU A 1 374 ? 55.63336 25.30729  55.56646  1.000 222.23506 ? 253  GLU A CD  1 
ATOM   2609 O OE1 . GLU A 1 374 ? 55.29860 24.83257  56.67169  1.000 227.84827 ? 253  GLU A OE1 1 
ATOM   2610 O OE2 . GLU A 1 374 ? 55.88168 26.52001  55.39458  1.000 226.34023 ? 253  GLU A OE2 1 
ATOM   2611 N N   . GLU A 1 375 ? 52.78290 23.79354  51.44717  1.000 150.82729 ? 254  GLU A N   1 
ATOM   2612 C CA  . GLU A 1 375 ? 51.47785 23.87754  50.79969  1.000 143.31994 ? 254  GLU A CA  1 
ATOM   2613 C C   . GLU A 1 375 ? 51.43617 23.12322  49.47562  1.000 136.10667 ? 254  GLU A C   1 
ATOM   2614 O O   . GLU A 1 375 ? 50.41510 22.50848  49.14756  1.000 135.50193 ? 254  GLU A O   1 
ATOM   2615 C CB  . GLU A 1 375 ? 51.10493 25.34424  50.58501  1.000 142.56159 ? 254  GLU A CB  1 
ATOM   2616 C CG  . GLU A 1 375 ? 51.14021 26.16627  51.85913  1.000 147.95084 ? 254  GLU A CG  1 
ATOM   2617 C CD  . GLU A 1 375 ? 50.21740 27.36628  51.81214  1.000 149.52478 ? 254  GLU A CD  1 
ATOM   2618 O OE1 . GLU A 1 375 ? 49.59518 27.59925  50.75565  1.000 144.65174 ? 254  GLU A OE1 1 
ATOM   2619 O OE2 . GLU A 1 375 ? 50.12061 28.08167  52.83135  1.000 159.22099 ? 254  GLU A OE2 1 
ATOM   2620 N N   . VAL A 1 376 ? 52.52044 23.17056  48.69639  1.000 127.24638 ? 255  VAL A N   1 
ATOM   2621 C CA  . VAL A 1 376 ? 52.51624 22.53211  47.38144  1.000 117.14886 ? 255  VAL A CA  1 
ATOM   2622 C C   . VAL A 1 376 ? 52.33959 21.02444  47.51744  1.000 121.41399 ? 255  VAL A C   1 
ATOM   2623 O O   . VAL A 1 376 ? 51.57783 20.40320  46.76519  1.000 114.72058 ? 255  VAL A O   1 
ATOM   2624 C CB  . VAL A 1 376 ? 53.79674 22.89056  46.60485  1.000 94.73564  ? 255  VAL A CB  1 
ATOM   2625 C CG1 . VAL A 1 376 ? 53.87346 22.09681  45.31218  1.000 87.72647  ? 255  VAL A CG1 1 
ATOM   2626 C CG2 . VAL A 1 376 ? 53.83185 24.38130  46.30982  1.000 85.48960  ? 255  VAL A CG2 1 
ATOM   2627 N N   . ASN A 1 377 ? 53.03917 20.41165  48.47668  1.000 123.52498 ? 256  ASN A N   1 
ATOM   2628 C CA  . ASN A 1 377 ? 52.98467 18.96158  48.63202  1.000 126.44584 ? 256  ASN A CA  1 
ATOM   2629 C C   . ASN A 1 377 ? 51.58136 18.45672  48.94500  1.000 118.29677 ? 256  ASN A C   1 
ATOM   2630 O O   . ASN A 1 377 ? 51.27894 17.29070  48.66852  1.000 114.42573 ? 256  ASN A O   1 
ATOM   2631 C CB  . ASN A 1 377 ? 53.95203 18.51410  49.72874  1.000 135.86273 ? 256  ASN A CB  1 
ATOM   2632 C CG  . ASN A 1 377 ? 54.28902 17.04262  49.63820  1.000 140.58049 ? 256  ASN A CG  1 
ATOM   2633 O OD1 . ASN A 1 377 ? 54.16620 16.43378  48.57641  1.000 137.29850 ? 256  ASN A OD1 1 
ATOM   2634 N ND2 . ASN A 1 377 ? 54.71419 16.45996  50.75470  1.000 144.36179 ? 256  ASN A ND2 1 
ATOM   2635 N N   . THR A 1 378 ? 50.72082 19.30062  49.51838  1.000 118.38155 ? 257  THR A N   1 
ATOM   2636 C CA  . THR A 1 378 ? 49.37597 18.86511  49.87712  1.000 127.14791 ? 257  THR A CA  1 
ATOM   2637 C C   . THR A 1 378 ? 48.49177 18.64326  48.65606  1.000 123.99009 ? 257  THR A C   1 
ATOM   2638 O O   . THR A 1 378 ? 47.45538 17.97913  48.76914  1.000 122.02250 ? 257  THR A O   1 
ATOM   2639 C CB  . THR A 1 378 ? 48.72232 19.88732  50.80954  1.000 133.92113 ? 257  THR A CB  1 
ATOM   2640 O OG1 . THR A 1 378 ? 49.71231 20.43172  51.68966  1.000 138.62837 ? 257  THR A OG1 1 
ATOM   2641 C CG2 . THR A 1 378 ? 47.63260 19.22929  51.64661  1.000 130.59950 ? 257  THR A CG2 1 
ATOM   2642 N N   . LEU A 1 379 ? 48.87952 19.17060  47.49678  1.000 129.71522 ? 258  LEU A N   1 
ATOM   2643 C CA  . LEU A 1 379 ? 48.06128 19.03837  46.29905  1.000 122.25558 ? 258  LEU A CA  1 
ATOM   2644 C C   . LEU A 1 379 ? 48.14585 17.61951  45.75053  1.000 107.90189 ? 258  LEU A C   1 
ATOM   2645 O O   . LEU A 1 379 ? 49.23978 17.08665  45.53821  1.000 106.22734 ? 258  LEU A O   1 
ATOM   2646 C CB  . LEU A 1 379 ? 48.50934 20.04397  45.23839  1.000 116.75682 ? 258  LEU A CB  1 
ATOM   2647 C CG  . LEU A 1 379 ? 48.37390 21.52566  45.59882  1.000 110.38454 ? 258  LEU A CG  1 
ATOM   2648 C CD1 . LEU A 1 379 ? 49.07019 22.39774  44.56635  1.000 99.89159  ? 258  LEU A CD1 1 
ATOM   2649 C CD2 . LEU A 1 379 ? 46.91319 21.92135  45.74436  1.000 106.40597 ? 258  LEU A CD2 1 
ATOM   2650 N N   . SER A 1 380 ? 46.98765 17.00499  45.52876  1.000 96.88387  ? 259  SER A N   1 
ATOM   2651 C CA  . SER A 1 380 ? 46.95068 15.72522  44.84316  1.000 92.73353  ? 259  SER A CA  1 
ATOM   2652 C C   . SER A 1 380 ? 47.39377 15.90202  43.39426  1.000 101.24154 ? 259  SER A C   1 
ATOM   2653 O O   . SER A 1 380 ? 47.44601 17.01575  42.86416  1.000 99.05668  ? 259  SER A O   1 
ATOM   2654 C CB  . SER A 1 380 ? 45.54580 15.12326  44.90043  1.000 88.43088  ? 259  SER A CB  1 
ATOM   2655 O OG  . SER A 1 380 ? 44.56216 16.07496  44.52981  1.000 81.10401  ? 259  SER A OG  1 
ATOM   2656 N N   . VAL A 1 381 ? 47.70479 14.78552  42.74430  1.000 100.12768 ? 260  VAL A N   1 
ATOM   2657 C CA  . VAL A 1 381 ? 48.26298 14.83822  41.39934  1.000 101.74381 ? 260  VAL A CA  1 
ATOM   2658 C C   . VAL A 1 381 ? 47.91258 13.55348  40.66405  1.000 106.23469 ? 260  VAL A C   1 
ATOM   2659 O O   . VAL A 1 381 ? 48.01188 12.45345  41.21494  1.000 110.99989 ? 260  VAL A O   1 
ATOM   2660 C CB  . VAL A 1 381 ? 49.78932 15.07261  41.44045  1.000 98.02327  ? 260  VAL A CB  1 
ATOM   2661 C CG1 . VAL A 1 381 ? 50.44370 14.12206  42.42669  1.000 99.78268  ? 260  VAL A CG1 1 
ATOM   2662 C CG2 . VAL A 1 381 ? 50.39933 14.92544  40.05557  1.000 93.75677  ? 260  VAL A CG2 1 
ATOM   2663 N N   . ALA A 1 382 ? 47.48847 13.70928  39.41406  1.000 111.48922 ? 261  ALA A N   1 
ATOM   2664 C CA  . ALA A 1 382 ? 47.20887 12.60045  38.51622  1.000 106.80360 ? 261  ALA A CA  1 
ATOM   2665 C C   . ALA A 1 382 ? 48.09315 12.73272  37.28552  1.000 100.92766 ? 261  ALA A C   1 
ATOM   2666 O O   . ALA A 1 382 ? 48.24433 13.82790  36.73364  1.000 92.74811  ? 261  ALA A O   1 
ATOM   2667 C CB  . ALA A 1 382 ? 45.73157 12.56739  38.10926  1.000 96.43984  ? 261  ALA A CB  1 
ATOM   2668 N N   . ILE A 1 383 ? 48.68465 11.61619  36.87212  1.000 106.50033 ? 262  ILE A N   1 
ATOM   2669 C CA  . ILE A 1 383 ? 49.54716 11.55298  35.69823  1.000 105.07245 ? 262  ILE A CA  1 
ATOM   2670 C C   . ILE A 1 383 ? 48.83806 10.69906  34.65940  1.000 103.78885 ? 262  ILE A C   1 
ATOM   2671 O O   . ILE A 1 383 ? 48.61560 9.50165   34.87803  1.000 107.00918 ? 262  ILE A O   1 
ATOM   2672 C CB  . ILE A 1 383 ? 50.93161 10.97833  36.03665  1.000 101.88162 ? 262  ILE A CB  1 
ATOM   2673 C CG1 . ILE A 1 383 ? 51.59342 11.78416  37.15969  1.000 95.42088  ? 262  ILE A CG1 1 
ATOM   2674 C CG2 . ILE A 1 383 ? 51.81392 10.96288  34.79947  1.000 102.34221 ? 262  ILE A CG2 1 
ATOM   2675 C CD1 . ILE A 1 383 ? 51.57751 13.28562  36.93871  1.000 92.55324  ? 262  ILE A CD1 1 
ATOM   2676 N N   . LEU A 1 384 ? 48.48331 11.30762  33.52958  1.000 100.05971 ? 263  LEU A N   1 
ATOM   2677 C CA  . LEU A 1 384 ? 47.72782 10.60446  32.50408  1.000 99.49390  ? 263  LEU A CA  1 
ATOM   2678 C C   . LEU A 1 384 ? 48.59293 10.34932  31.28225  1.000 91.29447  ? 263  LEU A C   1 
ATOM   2679 O O   . LEU A 1 384 ? 49.09411 11.30505  30.67012  1.000 101.00400 ? 263  LEU A O   1 
ATOM   2680 C CB  . LEU A 1 384 ? 46.48132 11.39584  32.11246  1.000 95.52689  ? 263  LEU A CB  1 
ATOM   2681 C CG  . LEU A 1 384 ? 45.55371 11.80185  33.25710  1.000 95.51546  ? 263  LEU A CG  1 
ATOM   2682 C CD1 . LEU A 1 384 ? 44.34884 12.55782  32.72388  1.000 97.64256  ? 263  LEU A CD1 1 
ATOM   2683 C CD2 . LEU A 1 384 ? 45.12072 10.57843  34.04753  1.000 92.91655  ? 263  LEU A CD2 1 
ATOM   2684 N N   . PRO A 1 385 ? 48.82800 9.09174   30.91680  1.000 85.46369  ? 264  PRO A N   1 
ATOM   2685 C CA  . PRO A 1 385 ? 49.39763 8.81272   29.59562  1.000 76.54963  ? 264  PRO A CA  1 
ATOM   2686 C C   . PRO A 1 385 ? 48.44360 9.29494   28.51623  1.000 87.20192  ? 264  PRO A C   1 
ATOM   2687 O O   . PRO A 1 385 ? 47.22386 9.17375   28.64569  1.000 93.54853  ? 264  PRO A O   1 
ATOM   2688 C CB  . PRO A 1 385 ? 49.55032 7.28730   29.57711  1.000 82.00114  ? 264  PRO A CB  1 
ATOM   2689 C CG  . PRO A 1 385 ? 49.30822 6.82318   30.98049  1.000 85.04971  ? 264  PRO A CG  1 
ATOM   2690 C CD  . PRO A 1 385 ? 48.49138 7.86745   31.66062  1.000 77.89325  ? 264  PRO A CD  1 
ATOM   2691 N N   . LEU A 1 386 ? 49.00034 9.85242   27.44747  1.000 87.40827  ? 265  LEU A N   1 
ATOM   2692 C CA  . LEU A 1 386 ? 48.17008 10.32687  26.35119  1.000 76.74644  ? 265  LEU A CA  1 
ATOM   2693 C C   . LEU A 1 386 ? 47.87959 9.17603   25.39846  1.000 80.53176  ? 265  LEU A C   1 
ATOM   2694 O O   . LEU A 1 386 ? 48.81395 8.65295   24.77596  1.000 78.85179  ? 265  LEU A O   1 
ATOM   2695 C CB  . LEU A 1 386 ? 48.84877 11.46270  25.60822  1.000 84.45019  ? 265  LEU A CB  1 
ATOM   2696 C CG  . LEU A 1 386 ? 48.00120 12.08449  24.49737  1.000 85.12419  ? 265  LEU A CG  1 
ATOM   2697 C CD1 . LEU A 1 386 ? 46.66610 12.58378  25.04135  1.000 74.74446  ? 265  LEU A CD1 1 
ATOM   2698 C CD2 . LEU A 1 386 ? 48.75615 13.20796  23.83397  1.000 71.97719  ? 265  LEU A CD2 1 
ATOM   2699 N N   . PRO A 1 387 ? 46.62457 8.74924   25.25921  1.000 79.88536  ? 266  PRO A N   1 
ATOM   2700 C CA  . PRO A 1 387 ? 46.31797 7.58853   24.40797  1.000 75.05808  ? 266  PRO A CA  1 
ATOM   2701 C C   . PRO A 1 387 ? 46.65475 7.87682   22.95336  1.000 78.91917  ? 266  PRO A C   1 
ATOM   2702 O O   . PRO A 1 387 ? 46.13241 8.81688   22.35110  1.000 86.84552  ? 266  PRO A O   1 
ATOM   2703 C CB  . PRO A 1 387 ? 44.81027 7.38804   24.61649  1.000 77.64370  ? 266  PRO A CB  1 
ATOM   2704 C CG  . PRO A 1 387 ? 44.49990 8.09178   25.90782  1.000 75.79080  ? 266  PRO A CG  1 
ATOM   2705 C CD  . PRO A 1 387 ? 45.43346 9.25710   25.95733  1.000 73.71364  ? 266  PRO A CD  1 
ATOM   2706 N N   . GLY A 1 388 ? 47.52074 7.04345   22.38173  1.000 83.07731  ? 267  GLY A N   1 
ATOM   2707 C CA  . GLY A 1 388 ? 48.03902 7.31824   21.05236  1.000 73.49294  ? 267  GLY A CA  1 
ATOM   2708 C C   . GLY A 1 388 ? 48.82750 8.60352   20.95889  1.000 70.95096  ? 267  GLY A C   1 
ATOM   2709 O O   . GLY A 1 388 ? 48.88272 9.21502   19.88655  1.000 89.77508  ? 267  GLY A O   1 
ATOM   2710 N N   . GLY A 1 389 ? 49.42071 9.04147   22.06632  1.000 81.14916  ? 268  GLY A N   1 
ATOM   2711 C CA  . GLY A 1 389 ? 50.11179 10.31961  22.07445  1.000 79.77538  ? 268  GLY A CA  1 
ATOM   2712 C C   . GLY A 1 389 ? 51.28514 10.34759  21.10917  1.000 80.94666  ? 268  GLY A C   1 
ATOM   2713 O O   . GLY A 1 389 ? 52.04736 9.38540   20.99267  1.000 78.11607  ? 268  GLY A O   1 
ATOM   2714 N N   . GLU A 1 390 ? 51.41853 11.47090  20.40595  1.000 81.09528  ? 269  GLU A N   1 
ATOM   2715 C CA  . GLU A 1 390 ? 52.57129 11.78315  19.57709  1.000 76.71543  ? 269  GLU A CA  1 
ATOM   2716 C C   . GLU A 1 390 ? 53.03684 13.19668  19.89577  1.000 69.16040  ? 269  GLU A C   1 
ATOM   2717 O O   . GLU A 1 390 ? 52.23996 14.05024  20.29842  1.000 75.13843  ? 269  GLU A O   1 
ATOM   2718 C CB  . GLU A 1 390 ? 52.24330 11.67566  18.08381  1.000 81.98169  ? 269  GLU A CB  1 
ATOM   2719 C CG  . GLU A 1 390 ? 51.72656 10.32241  17.64382  1.000 80.91582  ? 269  GLU A CG  1 
ATOM   2720 C CD  . GLU A 1 390 ? 51.04817 10.38011  16.29097  1.000 93.22568  ? 269  GLU A CD  1 
ATOM   2721 O OE1 . GLU A 1 390 ? 49.98861 9.74011   16.12267  1.000 96.16534  ? 269  GLU A OE1 1 
ATOM   2722 O OE2 . GLU A 1 390 ? 51.57703 11.07345  15.39545  1.000 88.15605  ? 269  GLU A OE2 1 
ATOM   2723 N N   . PHE A 1 391 ? 54.32643 13.44946  19.67611  1.000 75.92417  ? 270  PHE A N   1 
ATOM   2724 C CA  . PHE A 1 391 ? 54.91651 14.75022  19.96215  1.000 71.18028  ? 270  PHE A CA  1 
ATOM   2725 C C   . PHE A 1 391 ? 55.93866 15.09302  18.88993  1.000 74.68865  ? 270  PHE A C   1 
ATOM   2726 O O   . PHE A 1 391 ? 56.69167 14.22535  18.43975  1.000 88.13124  ? 270  PHE A O   1 
ATOM   2727 C CB  . PHE A 1 391 ? 55.58706 14.78356  21.34374  1.000 65.91729  ? 270  PHE A CB  1 
ATOM   2728 C CG  . PHE A 1 391 ? 56.80221 13.90698  21.45540  1.000 63.54349  ? 270  PHE A CG  1 
ATOM   2729 C CD1 . PHE A 1 391 ? 56.67538 12.54144  21.64853  1.000 64.47935  ? 270  PHE A CD1 1 
ATOM   2730 C CD2 . PHE A 1 391 ? 58.07558 14.45176  21.36814  1.000 66.72826  ? 270  PHE A CD2 1 
ATOM   2731 C CE1 . PHE A 1 391 ? 57.79387 11.73383  21.75054  1.000 75.41898  ? 270  PHE A CE1 1 
ATOM   2732 C CE2 . PHE A 1 391 ? 59.19691 13.64903  21.46953  1.000 64.59451  ? 270  PHE A CE2 1 
ATOM   2733 C CZ  . PHE A 1 391 ? 59.05598 12.28911  21.66156  1.000 70.29107  ? 270  PHE A CZ  1 
ATOM   2734 N N   . TYR A 1 392 ? 55.95579 16.35975  18.47616  1.000 76.30307  ? 271  TYR A N   1 
ATOM   2735 C CA  . TYR A 1 392 ? 56.88360 16.82116  17.44629  1.000 70.90897  ? 271  TYR A CA  1 
ATOM   2736 C C   . TYR A 1 392 ? 57.38695 18.20460  17.82549  1.000 65.73128  ? 271  TYR A C   1 
ATOM   2737 O O   . TYR A 1 392 ? 56.59706 19.14559  17.91866  1.000 73.43019  ? 271  TYR A O   1 
ATOM   2738 C CB  . TYR A 1 392 ? 56.20706 16.84760  16.07217  1.000 68.60396  ? 271  TYR A CB  1 
ATOM   2739 C CG  . TYR A 1 392 ? 55.60178 15.51896  15.67857  1.000 69.77920  ? 271  TYR A CG  1 
ATOM   2740 C CD1 . TYR A 1 392 ? 56.36336 14.54671  15.04515  1.000 74.90042  ? 271  TYR A CD1 1 
ATOM   2741 C CD2 . TYR A 1 392 ? 54.27004 15.23218  15.95412  1.000 72.52812  ? 271  TYR A CD2 1 
ATOM   2742 C CE1 . TYR A 1 392 ? 55.81360 13.32938  14.69122  1.000 84.70958  ? 271  TYR A CE1 1 
ATOM   2743 C CE2 . TYR A 1 392 ? 53.71263 14.01827  15.60419  1.000 76.15788  ? 271  TYR A CE2 1 
ATOM   2744 C CZ  . TYR A 1 392 ? 54.48867 13.07105  14.97323  1.000 72.09413  ? 271  TYR A CZ  1 
ATOM   2745 O OH  . TYR A 1 392 ? 53.93727 11.86105  14.62349  1.000 70.53778  ? 271  TYR A OH  1 
ATOM   2746 N N   . HIS A 1 393 ? 58.69012 18.33067  18.05147  1.000 70.71775  ? 272  HIS A N   1 
ATOM   2747 C CA  . HIS A 1 393 ? 59.23739 19.59903  18.50984  1.000 63.49626  ? 272  HIS A CA  1 
ATOM   2748 C C   . HIS A 1 393 ? 59.28623 20.61124  17.37029  1.000 68.15342  ? 272  HIS A C   1 
ATOM   2749 O O   . HIS A 1 393 ? 59.41197 20.25511  16.19595  1.000 70.42627  ? 272  HIS A O   1 
ATOM   2750 C CB  . HIS A 1 393 ? 60.63545 19.39478  19.09341  1.000 67.56014  ? 272  HIS A CB  1 
ATOM   2751 C CG  . HIS A 1 393 ? 60.63508 18.74172  20.43887  1.000 69.74827  ? 272  HIS A CG  1 
ATOM   2752 N ND1 . HIS A 1 393 ? 60.39437 19.43851  21.60300  1.000 82.86434  ? 272  HIS A ND1 1 
ATOM   2753 C CD2 . HIS A 1 393 ? 60.83504 17.45389  20.80538  1.000 75.65246  ? 272  HIS A CD2 1 
ATOM   2754 C CE1 . HIS A 1 393 ? 60.44875 18.60873  22.62957  1.000 82.92386  ? 272  HIS A CE1 1 
ATOM   2755 N NE2 . HIS A 1 393 ? 60.71649 17.39862  22.17286  1.000 82.46573  ? 272  HIS A NE2 1 
ATOM   2756 N N   . TYR A 1 394 ? 59.18419 21.89462  17.73008  1.000 65.14768  ? 273  TYR A N   1 
ATOM   2757 C CA  . TYR A 1 394 ? 59.31344 22.96623  16.74852  1.000 67.37666  ? 273  TYR A CA  1 
ATOM   2758 C C   . TYR A 1 394 ? 60.06965 24.16518  17.31793  1.000 77.89589  ? 273  TYR A C   1 
ATOM   2759 O O   . TYR A 1 394 ? 59.82263 25.30855  16.91775  1.000 84.46845  ? 273  TYR A O   1 
ATOM   2760 C CB  . TYR A 1 394 ? 57.93586 23.38756  16.20722  1.000 79.56615  ? 273  TYR A CB  1 
ATOM   2761 C CG  . TYR A 1 394 ? 56.92936 23.88179  17.23339  1.000 78.03046  ? 273  TYR A CG  1 
ATOM   2762 C CD1 . TYR A 1 394 ? 57.00005 25.16922  17.75655  1.000 84.44572  ? 273  TYR A CD1 1 
ATOM   2763 C CD2 . TYR A 1 394 ? 55.89100 23.06204  17.66186  1.000 92.93695  ? 273  TYR A CD2 1 
ATOM   2764 C CE1 . TYR A 1 394 ? 56.07488 25.62026  18.68624  1.000 98.25931  ? 273  TYR A CE1 1 
ATOM   2765 C CE2 . TYR A 1 394 ? 54.96047 23.50557  18.59210  1.000 87.25568  ? 273  TYR A CE2 1 
ATOM   2766 C CZ  . TYR A 1 394 ? 55.05750 24.78431  19.09948  1.000 84.30016  ? 273  TYR A CZ  1 
ATOM   2767 O OH  . TYR A 1 394 ? 54.13642 25.22831  20.02096  1.000 86.20790  ? 273  TYR A OH  1 
ATOM   2768 N N   . GLY A 1 395 ? 61.02108 23.92111  18.22353  1.000 65.17383  ? 274  GLY A N   1 
ATOM   2769 C CA  . GLY A 1 395 ? 61.81675 25.00715  18.76859  1.000 54.19559  ? 274  GLY A CA  1 
ATOM   2770 C C   . GLY A 1 395 ? 62.93910 25.49060  17.87515  1.000 51.35039  ? 274  GLY A C   1 
ATOM   2771 O O   . GLY A 1 395 ? 63.44644 26.59698  18.08663  1.000 78.29833  ? 274  GLY A O   1 
ATOM   2772 N N   . THR A 1 396 ? 63.35148 24.68724  16.89511  1.000 55.22631  ? 275  THR A N   1 
ATOM   2773 C CA  . THR A 1 396 ? 64.49586 24.99867  16.04642  1.000 63.46051  ? 275  THR A CA  1 
ATOM   2774 C C   . THR A 1 396 ? 64.08563 24.91929  14.58000  1.000 64.07282  ? 275  THR A C   1 
ATOM   2775 O O   . THR A 1 396 ? 63.03784 24.36989  14.23018  1.000 56.09509  ? 275  THR A O   1 
ATOM   2776 C CB  . THR A 1 396 ? 65.68464 24.06206  16.31673  1.000 59.89501  ? 275  THR A CB  1 
ATOM   2777 O OG1 . THR A 1 396 ? 65.40625 22.76451  15.77983  1.000 64.59782  ? 275  THR A OG1 1 
ATOM   2778 C CG2 . THR A 1 396 ? 65.95092 23.94124  17.81121  1.000 56.05926  ? 275  THR A CG2 1 
ATOM   2779 N N   . SER A 1 397 ? 64.94046 25.47695  13.71898  1.000 55.30706  ? 276  SER A N   1 
ATOM   2780 C CA  . SER A 1 397 ? 64.65041 25.53437  12.28804  1.000 63.52459  ? 276  SER A CA  1 
ATOM   2781 C C   . SER A 1 397 ? 64.56354 24.13602  11.67664  1.000 78.05771  ? 276  SER A C   1 
ATOM   2782 O O   . SER A 1 397 ? 63.56263 23.77998  11.02378  1.000 80.19988  ? 276  SER A O   1 
ATOM   2783 C CB  . SER A 1 397 ? 65.72925 26.36965  11.60115  1.000 63.15304  ? 276  SER A CB  1 
ATOM   2784 O OG  . SER A 1 397 ? 65.81159 27.65990  12.18645  1.000 55.45988  ? 276  SER A OG  1 
ATOM   2785 N N   . LYS A 1 398 ? 65.61980 23.33427  11.86704  1.000 72.46783  ? 277  LYS A N   1 
ATOM   2786 C CA  . LYS A 1 398 ? 65.60389 21.94541  11.41872  1.000 73.06258  ? 277  LYS A CA  1 
ATOM   2787 C C   . LYS A 1 398 ? 64.34107 21.24884  11.89445  1.000 60.47889  ? 277  LYS A C   1 
ATOM   2788 O O   . LYS A 1 398 ? 63.74185 20.44982  11.16174  1.000 67.57855  ? 277  LYS A O   1 
ATOM   2789 C CB  . LYS A 1 398 ? 66.84384 21.21179  11.93152  1.000 79.38862  ? 277  LYS A CB  1 
ATOM   2790 C CG  . LYS A 1 398 ? 67.55064 20.36254  10.88913  1.000 99.14499  ? 277  LYS A CG  1 
ATOM   2791 C CD  . LYS A 1 398 ? 68.96078 20.00494  11.33769  1.000 98.45464  ? 277  LYS A CD  1 
ATOM   2792 C CE  . LYS A 1 398 ? 69.65165 19.09470  10.33310  1.000 101.04372 ? 277  LYS A CE  1 
ATOM   2793 N NZ  . LYS A 1 398 ? 69.98923 19.80204  9.06573   1.000 92.47354  ? 277  LYS A NZ  1 
ATOM   2794 N N   . GLU A 1 399 ? 63.91480 21.55536  13.12248  1.000 62.64215  ? 278  GLU A N   1 
ATOM   2795 C CA  . GLU A 1 399 ? 62.72648 20.91438  13.66673  1.000 74.08961  ? 278  GLU A CA  1 
ATOM   2796 C C   . GLU A 1 399 ? 61.47279 21.41942  12.97294  1.000 64.79429  ? 278  GLU A C   1 
ATOM   2797 O O   . GLU A 1 399 ? 60.56170 20.63763  12.71570  1.000 72.54309  ? 278  GLU A O   1 
ATOM   2798 C CB  . GLU A 1 399 ? 62.62961 21.12043  15.17666  1.000 73.53552  ? 278  GLU A CB  1 
ATOM   2799 C CG  . GLU A 1 399 ? 63.54800 20.21125  15.97486  1.000 76.22876  ? 278  GLU A CG  1 
ATOM   2800 C CD  . GLU A 1 399 ? 63.55007 20.53851  17.45248  1.000 86.96084  ? 278  GLU A CD  1 
ATOM   2801 O OE1 . GLU A 1 399 ? 64.22437 19.81824  18.21724  1.000 86.44021  ? 278  GLU A OE1 1 
ATOM   2802 O OE2 . GLU A 1 399 ? 62.87606 21.51272  17.85098  1.000 90.42912  ? 278  GLU A OE2 1 
ATOM   2803 N N   . LEU A 1 400 ? 61.38609 22.72058  12.68644  1.000 63.23464  ? 279  LEU A N   1 
ATOM   2804 C CA  . LEU A 1 400 ? 60.26512 23.19941  11.88397  1.000 61.72327  ? 279  LEU A CA  1 
ATOM   2805 C C   . LEU A 1 400 ? 60.09621 22.34764  10.63321  1.000 72.23701  ? 279  LEU A C   1 
ATOM   2806 O O   . LEU A 1 400 ? 59.02705 21.76510  10.40439  1.000 66.48839  ? 279  LEU A O   1 
ATOM   2807 C CB  . LEU A 1 400 ? 60.46618 24.66783  11.50070  1.000 76.32798  ? 279  LEU A CB  1 
ATOM   2808 C CG  . LEU A 1 400 ? 59.36735 25.30271  10.63500  1.000 68.74754  ? 279  LEU A CG  1 
ATOM   2809 C CD1 . LEU A 1 400 ? 58.06349 25.42596  11.39665  1.000 60.31064  ? 279  LEU A CD1 1 
ATOM   2810 C CD2 . LEU A 1 400 ? 59.79959 26.65878  10.09474  1.000 64.63331  ? 279  LEU A CD2 1 
ATOM   2811 N N   . ILE A 1 401 ? 61.18467 22.15740  9.87992   1.000 74.43649  ? 280  ILE A N   1 
ATOM   2812 C CA  . ILE A 1 401 ? 61.06913 21.41404  8.62253   1.000 67.85897  ? 280  ILE A CA  1 
ATOM   2813 C C   . ILE A 1 401 ? 60.69292 19.95409  8.87671   1.000 75.98263  ? 280  ILE A C   1 
ATOM   2814 O O   . ILE A 1 401 ? 59.70854 19.44128  8.32046   1.000 85.42395  ? 280  ILE A O   1 
ATOM   2815 C CB  . ILE A 1 401 ? 62.36264 21.52910  7.79678   1.000 60.18232  ? 280  ILE A CB  1 
ATOM   2816 C CG1 . ILE A 1 401 ? 62.60822 22.98408  7.39275   1.000 55.56064  ? 280  ILE A CG1 1 
ATOM   2817 C CG2 . ILE A 1 401 ? 62.28301 20.64562  6.56750   1.000 61.39153  ? 280  ILE A CG2 1 
ATOM   2818 C CD1 . ILE A 1 401 ? 63.96027 23.22189  6.74765   1.000 68.82058  ? 280  ILE A CD1 1 
ATOM   2819 N N   . SER A 1 402 ? 61.44888 19.26819  9.73791   1.000 73.84034  ? 281  SER A N   1 
ATOM   2820 C CA  . SER A 1 402 ? 61.23659 17.83174  9.90551   1.000 76.23500  ? 281  SER A CA  1 
ATOM   2821 C C   . SER A 1 402 ? 59.91087 17.52785  10.59821  1.000 80.52161  ? 281  SER A C   1 
ATOM   2822 O O   . SER A 1 402 ? 59.23044 16.55680  10.24539  1.000 86.46062  ? 281  SER A O   1 
ATOM   2823 C CB  . SER A 1 402 ? 62.40306 17.21691  10.68033  1.000 72.07891  ? 281  SER A CB  1 
ATOM   2824 O OG  . SER A 1 402 ? 62.78020 18.03565  11.77131  1.000 72.27705  ? 281  SER A OG  1 
ATOM   2825 N N   . SER A 1 403 ? 59.51946 18.34549  11.57754  1.000 78.59824  ? 282  SER A N   1 
ATOM   2826 C CA  . SER A 1 403 ? 58.24919 18.15152  12.26251  1.000 76.44390  ? 282  SER A CA  1 
ATOM   2827 C C   . SER A 1 403 ? 57.06836 18.40170  11.33778  1.000 76.17928  ? 282  SER A C   1 
ATOM   2828 O O   . SER A 1 403 ? 56.07617 17.66880  11.39890  1.000 68.42828  ? 282  SER A O   1 
ATOM   2829 C CB  . SER A 1 403 ? 58.16930 19.05828  13.49009  1.000 73.42783  ? 282  SER A CB  1 
ATOM   2830 O OG  . SER A 1 403 ? 58.90116 18.51219  14.57448  1.000 78.47342  ? 282  SER A OG  1 
ATOM   2831 N N   . THR A 1 404 ? 57.13327 19.42865  10.47839  1.000 83.21339  ? 283  THR A N   1 
ATOM   2832 C CA  . THR A 1 404 ? 56.02168 19.60001  9.54950   1.000 80.50828  ? 283  THR A CA  1 
ATOM   2833 C C   . THR A 1 404 ? 55.96324 18.44755  8.55743   1.000 82.57595  ? 283  THR A C   1 
ATOM   2834 O O   . THR A 1 404 ? 54.87158 17.99035  8.20595   1.000 81.81913  ? 283  THR A O   1 
ATOM   2835 C CB  . THR A 1 404 ? 56.09912 20.94322  8.82037   1.000 66.96981  ? 283  THR A CB  1 
ATOM   2836 O OG1 . THR A 1 404 ? 57.25404 20.98026  7.97462   1.000 95.69027  ? 283  THR A OG1 1 
ATOM   2837 C CG2 . THR A 1 404 ? 56.10660 22.09878  9.80300   1.000 59.30519  ? 283  THR A CG2 1 
ATOM   2838 N N   . LEU A 1 405 ? 57.11933 17.93713  8.12051   1.000 89.84863  ? 284  LEU A N   1 
ATOM   2839 C CA  . LEU A 1 405 ? 57.10188 16.74992  7.26695   1.000 88.09270  ? 284  LEU A CA  1 
ATOM   2840 C C   . LEU A 1 405 ? 56.42482 15.57598  7.96825   1.000 86.87248  ? 284  LEU A C   1 
ATOM   2841 O O   . LEU A 1 405 ? 55.54923 14.91247  7.39662   1.000 81.69540  ? 284  LEU A O   1 
ATOM   2842 C CB  . LEU A 1 405 ? 58.52095 16.36663  6.84750   1.000 81.16538  ? 284  LEU A CB  1 
ATOM   2843 C CG  . LEU A 1 405 ? 58.57451 15.11491  5.96374   1.000 89.83960  ? 284  LEU A CG  1 
ATOM   2844 C CD1 . LEU A 1 405 ? 57.70631 15.28998  4.72265   1.000 89.29453  ? 284  LEU A CD1 1 
ATOM   2845 C CD2 . LEU A 1 405 ? 60.00210 14.75280  5.58445   1.000 89.50220  ? 284  LEU A CD2 1 
ATOM   2846 N N   . SER A 1 406 ? 56.81124 15.31614  9.21998   1.000 89.82774  ? 285  SER A N   1 
ATOM   2847 C CA  . SER A 1 406 ? 56.27339 14.16723  9.94309   1.000 98.52292  ? 285  SER A CA  1 
ATOM   2848 C C   . SER A 1 406 ? 54.78013 14.31968  10.20629  1.000 97.53194  ? 285  SER A C   1 
ATOM   2849 O O   . SER A 1 406 ? 54.02326 13.34891  10.09094  1.000 99.26931  ? 285  SER A O   1 
ATOM   2850 C CB  . SER A 1 406 ? 57.03196 13.97251  11.25596  1.000 106.09234 ? 285  SER A CB  1 
ATOM   2851 O OG  . SER A 1 406 ? 58.39643 13.66446  11.02058  1.000 107.80619 ? 285  SER A OG  1 
ATOM   2852 N N   . VAL A 1 407 ? 54.33584 15.52724  10.55880  1.000 90.22208  ? 286  VAL A N   1 
ATOM   2853 C CA  . VAL A 1 407 ? 52.91858 15.74473  10.82464  1.000 79.92254  ? 286  VAL A CA  1 
ATOM   2854 C C   . VAL A 1 407 ? 52.11241 15.62192  9.53899   1.000 99.89897  ? 286  VAL A C   1 
ATOM   2855 O O   . VAL A 1 407 ? 51.04775 14.99190  9.51611   1.000 111.06312 ? 286  VAL A O   1 
ATOM   2856 C CB  . VAL A 1 407 ? 52.70401 17.11012  11.50290  1.000 75.63792  ? 286  VAL A CB  1 
ATOM   2857 C CG1 . VAL A 1 407 ? 51.22504 17.46082  11.53101  1.000 75.73077  ? 286  VAL A CG1 1 
ATOM   2858 C CG2 . VAL A 1 407 ? 53.27051 17.09459  12.91476  1.000 74.49677  ? 286  VAL A CG2 1 
ATOM   2859 N N   . GLN A 1 408 ? 52.60370 16.21955  8.44931   1.000 99.76717  ? 287  GLN A N   1 
ATOM   2860 C CA  . GLN A 1 408 ? 51.92371 16.11281  7.16401   1.000 104.07555 ? 287  GLN A CA  1 
ATOM   2861 C C   . GLN A 1 408 ? 51.80296 14.65981  6.72318   1.000 113.98353 ? 287  GLN A C   1 
ATOM   2862 O O   . GLN A 1 408 ? 50.77956 14.25809  6.15630   1.000 113.68274 ? 287  GLN A O   1 
ATOM   2863 C CB  . GLN A 1 408 ? 52.67121 16.94082  6.11903   1.000 94.58570  ? 287  GLN A CB  1 
ATOM   2864 C CG  . GLN A 1 408 ? 51.86813 17.29375  4.88233   1.000 89.14171  ? 287  GLN A CG  1 
ATOM   2865 C CD  . GLN A 1 408 ? 52.67963 18.09091  3.88221   1.000 95.37736  ? 287  GLN A CD  1 
ATOM   2866 O OE1 . GLN A 1 408 ? 53.63005 17.57972  3.28901   1.000 94.20965  ? 287  GLN A OE1 1 
ATOM   2867 N NE2 . GLN A 1 408 ? 52.31905 19.35587  3.70119   1.000 100.69799 ? 287  GLN A NE2 1 
ATOM   2868 N N   . ASN A 1 409 ? 52.83453 13.85201  6.97748   1.000 111.97852 ? 288  ASN A N   1 
ATOM   2869 C CA  . ASN A 1 409 ? 52.80215 12.45641  6.55314   1.000 113.15132 ? 288  ASN A CA  1 
ATOM   2870 C C   . ASN A 1 409 ? 52.02022 11.58863  7.53326   1.000 116.93447 ? 288  ASN A C   1 
ATOM   2871 O O   . ASN A 1 409 ? 52.36801 10.42518  7.75199   1.000 113.85323 ? 288  ASN A O   1 
ATOM   2872 C CB  . ASN A 1 409 ? 54.22155 11.91544  6.39121   1.000 116.79428 ? 288  ASN A CB  1 
ATOM   2873 C CG  . ASN A 1 409 ? 54.89009 12.40383  5.11928   1.000 118.91802 ? 288  ASN A CG  1 
ATOM   2874 O OD1 . ASN A 1 409 ? 54.34637 13.24111  4.39434   1.000 117.51614 ? 288  ASN A OD1 1 
ATOM   2875 N ND2 . ASN A 1 409 ? 56.07300 11.87637  4.83882   1.000 117.41799 ? 288  ASN A ND2 1 
ATOM   2876 N N   . LYS A 1 410 ? 50.96242 12.13927  8.12581   1.000 122.28993 ? 289  LYS A N   1 
ATOM   2877 C CA  . LYS A 1 410 ? 50.10825 11.37495  9.02620   1.000 121.18770 ? 289  LYS A CA  1 
ATOM   2878 C C   . LYS A 1 410 ? 48.63164 11.55212  8.68938   1.000 126.77669 ? 289  LYS A C   1 
ATOM   2879 O O   . LYS A 1 410 ? 47.82584 10.65105  8.94002   1.000 134.29738 ? 289  LYS A O   1 
ATOM   2880 C CB  . LYS A 1 410 ? 50.36752 11.76705  10.48200  1.000 112.88863 ? 289  LYS A CB  1 
ATOM   2881 C CG  . LYS A 1 410 ? 51.68794 11.24847  11.03426  1.000 110.26662 ? 289  LYS A CG  1 
ATOM   2882 C CD  . LYS A 1 410 ? 51.46884 10.39050  12.26672  1.000 110.75804 ? 289  LYS A CD  1 
ATOM   2883 C CE  . LYS A 1 410 ? 52.48688 9.26503   12.35119  1.000 110.85172 ? 289  LYS A CE  1 
ATOM   2884 N NZ  . LYS A 1 410 ? 53.88246 9.77347   12.23834  1.000 114.24925 ? 289  LYS A NZ  1 
ATOM   2885 N N   . VAL A 1 411 ? 48.26823 12.69480  8.11470   1.000 125.94195 ? 290  VAL A N   1 
ATOM   2886 C CA  . VAL A 1 411 ? 46.89953 12.93084  7.67510   1.000 126.96790 ? 290  VAL A CA  1 
ATOM   2887 C C   . VAL A 1 411 ? 46.87821 13.26142  6.18688   1.000 122.77311 ? 290  VAL A C   1 
ATOM   2888 O O   . VAL A 1 411 ? 47.56436 12.61860  5.39100   1.000 120.16463 ? 290  VAL A O   1 
ATOM   2889 C CB  . VAL A 1 411 ? 46.23650 14.05244  8.49958   1.000 124.24651 ? 290  VAL A CB  1 
ATOM   2890 C CG1 . VAL A 1 411 ? 45.09428 13.49188  9.32864   1.000 119.81651 ? 290  VAL A CG1 1 
ATOM   2891 C CG2 . VAL A 1 411 ? 47.25890 14.73474  9.39210   1.000 112.75556 ? 290  VAL A CG2 1 
ATOM   2892 N N   . PRO A 1 426 ? 59.95255 14.61654  -0.13438  1.000 141.14441 ? 305  PRO A N   1 
ATOM   2893 C CA  . PRO A 1 426 ? 58.65992 15.18171  0.26831   1.000 136.77313 ? 305  PRO A CA  1 
ATOM   2894 C C   . PRO A 1 426 ? 58.80366 16.29496  1.30152   1.000 124.61229 ? 305  PRO A C   1 
ATOM   2895 O O   . PRO A 1 426 ? 57.79695 16.80670  1.79103   1.000 129.19061 ? 305  PRO A O   1 
ATOM   2896 C CB  . PRO A 1 426 ? 57.91708 13.97961  0.86150   1.000 138.66140 ? 305  PRO A CB  1 
ATOM   2897 C CG  . PRO A 1 426 ? 58.98859 13.05230  1.30259   1.000 142.06241 ? 305  PRO A CG  1 
ATOM   2898 C CD  . PRO A 1 426 ? 60.13181 13.23648  0.34884   1.000 143.00682 ? 305  PRO A CD  1 
ATOM   2899 N N   . ALA A 1 427 ? 60.03956 16.66195  1.62903   1.000 99.15430  ? 306  ALA A N   1 
ATOM   2900 C CA  . ALA A 1 427 ? 60.29494 17.63251  2.69235   1.000 86.78063  ? 306  ALA A CA  1 
ATOM   2901 C C   . ALA A 1 427 ? 60.44646 19.04074  2.13282   1.000 79.27265  ? 306  ALA A C   1 
ATOM   2902 O O   . ALA A 1 427 ? 61.40868 19.75224  2.41593   1.000 68.77547  ? 306  ALA A O   1 
ATOM   2903 C CB  . ALA A 1 427 ? 61.53038 17.22621  3.48430   1.000 85.81579  ? 306  ALA A CB  1 
ATOM   2904 N N   . MET A 1 428 ? 59.46672 19.45599  1.33570   1.000 77.71201  ? 307  MET A N   1 
ATOM   2905 C CA  . MET A 1 428 ? 59.49381 20.73919  0.64951   1.000 75.67534  ? 307  MET A CA  1 
ATOM   2906 C C   . MET A 1 428 ? 58.14441 21.40293  0.85656   1.000 78.69859  ? 307  MET A C   1 
ATOM   2907 O O   . MET A 1 428 ? 57.10189 20.76859  0.66454   1.000 95.40981  ? 307  MET A O   1 
ATOM   2908 C CB  . MET A 1 428 ? 59.79911 20.56198  -0.84001  1.000 87.92292  ? 307  MET A CB  1 
ATOM   2909 C CG  . MET A 1 428 ? 61.22490 20.09954  -1.10733  1.000 99.02320  ? 307  MET A CG  1 
ATOM   2910 S SD  . MET A 1 428 ? 61.54698 19.71648  -2.83858  1.000 106.25201 ? 307  MET A SD  1 
ATOM   2911 C CE  . MET A 1 428 ? 61.16068 21.28302  -3.61404  1.000 109.81562 ? 307  MET A CE  1 
ATOM   2912 N N   . PHE A 1 429 ? 58.16583 22.67325  1.24790   1.000 72.42841  ? 308  PHE A N   1 
ATOM   2913 C CA  . PHE A 1 429 ? 56.97106 23.35087  1.73180   1.000 67.96479  ? 308  PHE A CA  1 
ATOM   2914 C C   . PHE A 1 429 ? 56.97011 24.77065  1.19578   1.000 77.94593  ? 308  PHE A C   1 
ATOM   2915 O O   . PHE A 1 429 ? 57.88914 25.54429  1.49113   1.000 61.49350  ? 308  PHE A O   1 
ATOM   2916 C CB  . PHE A 1 429 ? 56.94364 23.35036  3.26075   1.000 65.63599  ? 308  PHE A CB  1 
ATOM   2917 C CG  . PHE A 1 429 ? 57.01398 21.97694  3.86054   1.000 69.12175  ? 308  PHE A CG  1 
ATOM   2918 C CD1 . PHE A 1 429 ? 55.99494 21.06251  3.66179   1.000 62.14139  ? 308  PHE A CD1 1 
ATOM   2919 C CD2 . PHE A 1 429 ? 58.11491 21.59470  4.60791   1.000 78.69019  ? 308  PHE A CD2 1 
ATOM   2920 C CE1 . PHE A 1 429 ? 56.06619 19.79321  4.20797   1.000 60.42627  ? 308  PHE A CE1 1 
ATOM   2921 C CE2 . PHE A 1 429 ? 58.19223 20.32902  5.15535   1.000 78.04964  ? 308  PHE A CE2 1 
ATOM   2922 C CZ  . PHE A 1 429 ? 57.16595 19.42799  4.95690   1.000 69.64629  ? 308  PHE A CZ  1 
ATOM   2923 N N   . VAL A 1 430 ? 55.94357 25.11808  0.42046   1.000 95.45536  ? 309  VAL A N   1 
ATOM   2924 C CA  . VAL A 1 430 ? 55.82735 26.46362  -0.13193  1.000 67.39694  ? 309  VAL A CA  1 
ATOM   2925 C C   . VAL A 1 430 ? 54.46703 27.02490  0.25202   1.000 77.22657  ? 309  VAL A C   1 
ATOM   2926 O O   . VAL A 1 430 ? 53.42904 26.47510  -0.13543  1.000 67.75838  ? 309  VAL A O   1 
ATOM   2927 C CB  . VAL A 1 430 ? 56.00813 26.48161  -1.65794  1.000 69.14887  ? 309  VAL A CB  1 
ATOM   2928 C CG1 . VAL A 1 430 ? 56.08065 27.91344  -2.16521  1.000 51.20514  ? 309  VAL A CG1 1 
ATOM   2929 C CG2 . VAL A 1 430 ? 57.25013 25.69729  -2.05229  1.000 63.79573  ? 309  VAL A CG2 1 
ATOM   2930 N N   . GLN A 1 431 ? 54.47169 28.13840  0.97383   1.000 53.45500  ? 310  GLN A N   1 
ATOM   2931 C CA  . GLN A 1 431 ? 53.24891 28.77372  1.42723   1.000 53.96499  ? 310  GLN A CA  1 
ATOM   2932 C C   . GLN A 1 431 ? 53.33642 30.25625  1.13385   1.000 57.19259  ? 310  GLN A C   1 
ATOM   2933 O O   . GLN A 1 431 ? 54.36724 30.88089  1.39143   1.000 62.96350  ? 310  GLN A O   1 
ATOM   2934 C CB  . GLN A 1 431 ? 53.04626 28.58362  2.92910   1.000 50.35991  ? 310  GLN A CB  1 
ATOM   2935 C CG  . GLN A 1 431 ? 52.67755 27.19001  3.36588   1.000 55.58462  ? 310  GLN A CG  1 
ATOM   2936 C CD  . GLN A 1 431 ? 52.66452 27.07364  4.87486   1.000 59.28632  ? 310  GLN A CD  1 
ATOM   2937 O OE1 . GLN A 1 431 ? 51.60852 27.12333  5.50385   1.000 80.22860  ? 310  GLN A OE1 1 
ATOM   2938 N NE2 . GLN A 1 431 ? 53.84575 26.94023  5.46756   1.000 60.74106  ? 310  GLN A NE2 1 
ATOM   2939 N N   . ASN A 1 432 ? 52.24868 30.81508  0.61137   1.000 51.50730  ? 311  ASN A N   1 
ATOM   2940 C CA  . ASN A 1 432 ? 52.11029 32.25779  0.46124   1.000 55.74939  ? 311  ASN A CA  1 
ATOM   2941 C C   . ASN A 1 432 ? 53.31065 32.83718  -0.28435  1.000 71.35816  ? 311  ASN A C   1 
ATOM   2942 O O   . ASN A 1 432 ? 53.93988 33.80009  0.15689   1.000 62.92908  ? 311  ASN A O   1 
ATOM   2943 C CB  . ASN A 1 432 ? 51.94739 32.92241  1.82748   1.000 66.32185  ? 311  ASN A CB  1 
ATOM   2944 C CG  . ASN A 1 432 ? 50.94058 32.20382  2.70494   1.000 66.20354  ? 311  ASN A CG  1 
ATOM   2945 O OD1 . ASN A 1 432 ? 49.90132 31.75150  2.23207   1.000 78.10575  ? 311  ASN A OD1 1 
ATOM   2946 N ND2 . ASN A 1 432 ? 51.24570 32.09827  3.99343   1.000 57.78802  ? 311  ASN A ND2 1 
ATOM   2947 N N   . ALA A 1 433 ? 53.65857 32.21918  -1.41194  1.000 55.51368  ? 312  ALA A N   1 
ATOM   2948 C CA  . ALA A 1 433 ? 54.90632 32.56222  -2.07624  1.000 61.08952  ? 312  ALA A CA  1 
ATOM   2949 C C   . ALA A 1 433 ? 54.75224 32.53270  -3.58945  1.000 62.39320  ? 312  ALA A C   1 
ATOM   2950 O O   . ALA A 1 433 ? 53.85862 31.88484  -4.14332  1.000 62.11057  ? 312  ALA A O   1 
ATOM   2951 C CB  . ALA A 1 433 ? 56.04140 31.61416  -1.65591  1.000 59.40877  ? 312  ALA A CB  1 
ATOM   2952 N N   . VAL A 1 434 ? 55.65470 33.25842  -4.24545  1.000 59.25110  ? 313  VAL A N   1 
ATOM   2953 C CA  . VAL A 1 434 ? 55.88102 33.17842  -5.68335  1.000 63.14649  ? 313  VAL A CA  1 
ATOM   2954 C C   . VAL A 1 434 ? 57.29421 32.65180  -5.89385  1.000 72.21629  ? 313  VAL A C   1 
ATOM   2955 O O   . VAL A 1 434 ? 58.27080 33.30290  -5.49845  1.000 61.09175  ? 313  VAL A O   1 
ATOM   2956 C CB  . VAL A 1 434 ? 55.69504 34.54107  -6.36979  1.000 72.64799  ? 313  VAL A CB  1 
ATOM   2957 C CG1 . VAL A 1 434 ? 56.35440 34.54200  -7.74321  1.000 61.39106  ? 313  VAL A CG1 1 
ATOM   2958 C CG2 . VAL A 1 434 ? 54.21533 34.88687  -6.47928  1.000 58.52940  ? 313  VAL A CG2 1 
ATOM   2959 N N   . VAL A 1 435 ? 57.40421 31.46762  -6.48724  1.000 68.09230  ? 314  VAL A N   1 
ATOM   2960 C CA  . VAL A 1 435 ? 58.69135 30.84713  -6.77867  1.000 68.54830  ? 314  VAL A CA  1 
ATOM   2961 C C   . VAL A 1 435 ? 58.88031 30.84424  -8.29006  1.000 79.60474  ? 314  VAL A C   1 
ATOM   2962 O O   . VAL A 1 435 ? 58.07058 30.26124  -9.02208  1.000 79.42166  ? 314  VAL A O   1 
ATOM   2963 C CB  . VAL A 1 435 ? 58.77334 29.42385  -6.20598  1.000 60.68434  ? 314  VAL A CB  1 
ATOM   2964 C CG1 . VAL A 1 435 ? 60.11058 28.78766  -6.54550  1.000 66.43158  ? 314  VAL A CG1 1 
ATOM   2965 C CG2 . VAL A 1 435 ? 58.54927 29.44166  -4.70131  1.000 67.67948  ? 314  VAL A CG2 1 
ATOM   2966 N N   . ARG A 1 436 ? 59.94766 31.49113  -8.75958  1.000 68.17166  ? 315  ARG A N   1 
ATOM   2967 C CA  . ARG A 1 436 ? 60.19344 31.63484  -10.18841 1.000 76.05809  ? 315  ARG A CA  1 
ATOM   2968 C C   . ARG A 1 436 ? 61.36655 30.78734  -10.66464 1.000 71.82669  ? 315  ARG A C   1 
ATOM   2969 O O   . ARG A 1 436 ? 61.85531 30.99300  -11.77954 1.000 71.95799  ? 315  ARG A O   1 
ATOM   2970 C CB  . ARG A 1 436 ? 60.43630 33.10390  -10.54551 1.000 64.64567  ? 315  ARG A CB  1 
ATOM   2971 C CG  . ARG A 1 436 ? 59.24575 34.02242  -10.32542 1.000 69.04507  ? 315  ARG A CG  1 
ATOM   2972 C CD  . ARG A 1 436 ? 58.95008 34.83576  -11.57834 1.000 83.24534  ? 315  ARG A CD  1 
ATOM   2973 N NE  . ARG A 1 436 ? 58.02487 35.93496  -11.31488 1.000 101.05946 ? 315  ARG A NE  1 
ATOM   2974 C CZ  . ARG A 1 436 ? 56.69986 35.82233  -11.32608 1.000 110.93950 ? 315  ARG A CZ  1 
ATOM   2975 N NH1 . ARG A 1 436 ? 56.13173 34.65363  -11.59175 1.000 113.87747 ? 315  ARG A NH1 1 
ATOM   2976 N NH2 . ARG A 1 436 ? 55.94098 36.88121  -11.07338 1.000 107.91786 ? 315  ARG A NH2 1 
ATOM   2977 N N   . ILE A 1 437 ? 61.82409 29.84069  -9.85140  1.000 71.65491  ? 316  ILE A N   1 
ATOM   2978 C CA  . ILE A 1 437 ? 62.83263 28.86643  -10.25879 1.000 75.04189  ? 316  ILE A CA  1 
ATOM   2979 C C   . ILE A 1 437 ? 62.17739 27.49233  -10.18655 1.000 72.94193  ? 316  ILE A C   1 
ATOM   2980 O O   . ILE A 1 437 ? 61.24130 27.30014  -9.39733  1.000 69.29944  ? 316  ILE A O   1 
ATOM   2981 C CB  . ILE A 1 437 ? 64.09313 28.94495  -9.37978  1.000 58.92191  ? 316  ILE A CB  1 
ATOM   2982 C CG1 . ILE A 1 437 ? 63.72150 29.24598  -7.92715  1.000 64.43019  ? 316  ILE A CG1 1 
ATOM   2983 C CG2 . ILE A 1 437 ? 65.05506 30.00068  -9.91027  1.000 52.91137  ? 316  ILE A CG2 1 
ATOM   2984 C CD1 . ILE A 1 437 ? 64.19130 28.19132  -6.94964  1.000 72.34501  ? 316  ILE A CD1 1 
ATOM   2985 N N   . PRO A 1 438 ? 62.61864 26.51511  -10.97300 1.000 76.46313  ? 317  PRO A N   1 
ATOM   2986 C CA  . PRO A 1 438 ? 62.14346 25.14386  -10.77008 1.000 76.70814  ? 317  PRO A CA  1 
ATOM   2987 C C   . PRO A 1 438 ? 62.62562 24.57322  -9.44513  1.000 76.79410  ? 317  PRO A C   1 
ATOM   2988 O O   . PRO A 1 438 ? 63.54553 25.08797  -8.80604  1.000 87.47560  ? 317  PRO A O   1 
ATOM   2989 C CB  . PRO A 1 438 ? 62.74164 24.38293  -11.95852 1.000 77.61856  ? 317  PRO A CB  1 
ATOM   2990 C CG  . PRO A 1 438 ? 63.95236 25.18399  -12.32807 1.000 79.90937  ? 317  PRO A CG  1 
ATOM   2991 C CD  . PRO A 1 438 ? 63.53234 26.61116  -12.12393 1.000 75.09776  ? 317  PRO A CD  1 
ATOM   2992 N N   . LEU A 1 439 ? 61.98398 23.47735  -9.04444  1.000 71.76776  ? 318  LEU A N   1 
ATOM   2993 C CA  . LEU A 1 439 ? 62.24957 22.82226  -7.76846  1.000 70.22537  ? 318  LEU A CA  1 
ATOM   2994 C C   . LEU A 1 439 ? 62.24216 21.32013  -7.99282  1.000 86.88604  ? 318  LEU A C   1 
ATOM   2995 O O   . LEU A 1 439 ? 61.24862 20.77049  -8.47732  1.000 101.59703 ? 318  LEU A O   1 
ATOM   2996 C CB  . LEU A 1 439 ? 61.20760 23.20832  -6.71206  1.000 65.76948  ? 318  LEU A CB  1 
ATOM   2997 C CG  . LEU A 1 439 ? 61.24281 24.61789  -6.11580  1.000 73.96102  ? 318  LEU A CG  1 
ATOM   2998 C CD1 . LEU A 1 439 ? 60.33081 24.70438  -4.89490  1.000 60.11723  ? 318  LEU A CD1 1 
ATOM   2999 C CD2 . LEU A 1 439 ? 62.66428 25.01559  -5.74344  1.000 70.19728  ? 318  LEU A CD2 1 
ATOM   3000 N N   . CYS A 1 440 ? 63.33831 20.66194  -7.64167  1.000 92.60891  ? 319  CYS A N   1 
ATOM   3001 C CA  . CYS A 1 440 ? 63.46765 19.21652  -7.75850  1.000 105.62438 ? 319  CYS A CA  1 
ATOM   3002 C C   . CYS A 1 440 ? 63.78956 18.61611  -6.39191  1.000 112.18631 ? 319  CYS A C   1 
ATOM   3003 O O   . CYS A 1 440 ? 63.87118 19.31952  -5.38163  1.000 111.90798 ? 319  CYS A O   1 
ATOM   3004 C CB  . CYS A 1 440 ? 64.53150 18.85483  -8.79925  1.000 108.25801 ? 319  CYS A CB  1 
ATOM   3005 S SG  . CYS A 1 440 ? 66.05449 19.81702  -8.66614  1.000 115.29189 ? 319  CYS A SG  1 
ATOM   3006 N N   . ALA A 1 441 ? 63.97054 17.29261  -6.36681  1.000 115.83587 ? 320  ALA A N   1 
ATOM   3007 C CA  . ALA A 1 441 ? 64.26044 16.59437  -5.11881  1.000 113.80925 ? 320  ALA A CA  1 
ATOM   3008 C C   . ALA A 1 441 ? 65.67411 16.84403  -4.61048  1.000 110.75454 ? 320  ALA A C   1 
ATOM   3009 O O   . ALA A 1 441 ? 66.00766 16.38107  -3.51438  1.000 106.72729 ? 320  ALA A O   1 
ATOM   3010 C CB  . ALA A 1 441 ? 64.03280 15.09123  -5.29010  1.000 119.58799 ? 320  ALA A CB  1 
ATOM   3011 N N   . GLU A 1 442 ? 66.50925 17.55333  -5.37337  1.000 109.62215 ? 321  GLU A N   1 
ATOM   3012 C CA  . GLU A 1 442 ? 67.79159 18.00110  -4.84178  1.000 106.63543 ? 321  GLU A CA  1 
ATOM   3013 C C   . GLU A 1 442 ? 67.60767 19.14242  -3.85107  1.000 91.80248  ? 321  GLU A C   1 
ATOM   3014 O O   . GLU A 1 442 ? 68.37924 19.26359  -2.89304  1.000 96.39720  ? 321  GLU A O   1 
ATOM   3015 C CB  . GLU A 1 442 ? 68.71540 18.42508  -5.98396  1.000 113.10600 ? 321  GLU A CB  1 
ATOM   3016 C CG  . GLU A 1 442 ? 69.36274 17.26655  -6.73009  1.000 130.51003 ? 321  GLU A CG  1 
ATOM   3017 C CD  . GLU A 1 442 ? 68.49284 16.72258  -7.84942  1.000 138.81060 ? 321  GLU A CD  1 
ATOM   3018 O OE1 . GLU A 1 442 ? 69.00951 15.94247  -8.67696  1.000 141.47609 ? 321  GLU A OE1 1 
ATOM   3019 O OE2 . GLU A 1 442 ? 67.29297 17.06558  -7.89949  1.000 140.22178 ? 321  GLU A OE2 1 
ATOM   3020 N N   . ASN A 1 443 ? 66.59618 19.98407  -4.06684  1.000 79.90234  ? 322  ASN A N   1 
ATOM   3021 C CA  . ASN A 1 443 ? 66.25177 21.06391  -3.14372  1.000 78.05706  ? 322  ASN A CA  1 
ATOM   3022 C C   . ASN A 1 443 ? 65.40052 20.53651  -1.98535  1.000 77.91520  ? 322  ASN A C   1 
ATOM   3023 O O   . ASN A 1 443 ? 64.26393 20.95059  -1.76464  1.000 86.94159  ? 322  ASN A O   1 
ATOM   3024 C CB  . ASN A 1 443 ? 65.53810 22.18367  -3.89020  1.000 69.66698  ? 322  ASN A CB  1 
ATOM   3025 C CG  . ASN A 1 443 ? 66.28882 22.62736  -5.13073  1.000 76.84971  ? 322  ASN A CG  1 
ATOM   3026 O OD1 . ASN A 1 443 ? 65.71012 22.75255  -6.21130  1.000 77.56597  ? 322  ASN A OD1 1 
ATOM   3027 N ND2 . ASN A 1 443 ? 67.58555 22.86899  -4.98117  1.000 69.14456  ? 322  ASN A ND2 1 
ATOM   3028 N N   . ALA A 1 444 ? 65.98051 19.61000  -1.23136  1.000 74.91547  ? 323  ALA A N   1 
ATOM   3029 C CA  . ALA A 1 444 ? 65.27049 18.97871  -0.13182  1.000 76.41476  ? 323  ALA A CA  1 
ATOM   3030 C C   . ALA A 1 444 ? 65.42032 19.80055  1.14340   1.000 76.06639  ? 323  ALA A C   1 
ATOM   3031 O O   . ALA A 1 444 ? 66.31043 20.64525  1.26678   1.000 69.48000  ? 323  ALA A O   1 
ATOM   3032 C CB  . ALA A 1 444 ? 65.78373 17.55650  0.09587   1.000 81.01634  ? 323  ALA A CB  1 
ATOM   3033 N N   . ASP A 1 445 ? 64.53299 19.53216  2.10054   1.000 66.47759  ? 324  ASP A N   1 
ATOM   3034 C CA  . ASP A 1 445 ? 64.44573 20.29262  3.34684   1.000 70.20090  ? 324  ASP A CA  1 
ATOM   3035 C C   . ASP A 1 445 ? 64.31736 21.78950  3.05181   1.000 72.45257  ? 324  ASP A C   1 
ATOM   3036 O O   . ASP A 1 445 ? 65.19566 22.59920  3.34393   1.000 71.30231  ? 324  ASP A O   1 
ATOM   3037 C CB  . ASP A 1 445 ? 65.64403 20.00073  4.25502   1.000 69.69610  ? 324  ASP A CB  1 
ATOM   3038 C CG  . ASP A 1 445 ? 65.64919 18.57613  4.76989   1.000 75.63139  ? 324  ASP A CG  1 
ATOM   3039 O OD1 . ASP A 1 445 ? 64.59603 17.91051  4.68907   1.000 81.59024  ? 324  ASP A OD1 1 
ATOM   3040 O OD2 . ASP A 1 445 ? 66.70557 18.12179  5.25642   1.000 90.04488  ? 324  ASP A OD2 1 
ATOM   3041 N N   . LEU A 1 446 ? 63.18016 22.13102  2.45586   1.000 78.93341  ? 325  LEU A N   1 
ATOM   3042 C CA  . LEU A 1 446 ? 62.91035 23.48250  1.99393   1.000 75.93348  ? 325  LEU A CA  1 
ATOM   3043 C C   . LEU A 1 446 ? 61.67242 24.01953  2.69736   1.000 59.90787  ? 325  LEU A C   1 
ATOM   3044 O O   . LEU A 1 446 ? 60.67622 23.30741  2.85164   1.000 70.98078  ? 325  LEU A O   1 
ATOM   3045 C CB  . LEU A 1 446 ? 62.71637 23.50023  0.47191   1.000 64.53753  ? 325  LEU A CB  1 
ATOM   3046 C CG  . LEU A 1 446 ? 62.82670 24.83001  -0.27308  1.000 72.49602  ? 325  LEU A CG  1 
ATOM   3047 C CD1 . LEU A 1 446 ? 64.10302 25.55037  0.11239   1.000 59.92594  ? 325  LEU A CD1 1 
ATOM   3048 C CD2 . LEU A 1 446 ? 62.77389 24.59851  -1.77968  1.000 59.28026  ? 325  LEU A CD2 1 
ATOM   3049 N N   . TRP A 1 447 ? 61.74410 25.27802  3.12612   1.000 57.44326  ? 326  TRP A N   1 
ATOM   3050 C CA  . TRP A 1 447 ? 60.58609 25.99352  3.65397   1.000 58.12983  ? 326  TRP A CA  1 
ATOM   3051 C C   . TRP A 1 447 ? 60.63054 27.40583  3.09345   1.000 61.50197  ? 326  TRP A C   1 
ATOM   3052 O O   . TRP A 1 447 ? 61.49212 28.20263  3.47799   1.000 61.46767  ? 326  TRP A O   1 
ATOM   3053 C CB  . TRP A 1 447 ? 60.59153 26.00084  5.18423   1.000 57.33820  ? 326  TRP A CB  1 
ATOM   3054 C CG  . TRP A 1 447 ? 59.47344 26.77749  5.83529   1.000 53.30685  ? 326  TRP A CG  1 
ATOM   3055 C CD1 . TRP A 1 447 ? 59.30188 28.13414  5.84126   1.000 52.93619  ? 326  TRP A CD1 1 
ATOM   3056 C CD2 . TRP A 1 447 ? 58.38778 26.23508  6.59798   1.000 45.66592  ? 326  TRP A CD2 1 
ATOM   3057 N NE1 . TRP A 1 447 ? 58.17034 28.46662  6.54889   1.000 50.72224  ? 326  TRP A NE1 1 
ATOM   3058 C CE2 . TRP A 1 447 ? 57.59292 27.31854  7.02497   1.000 55.75029  ? 326  TRP A CE2 1 
ATOM   3059 C CE3 . TRP A 1 447 ? 58.00946 24.93835  6.95738   1.000 57.34302  ? 326  TRP A CE3 1 
ATOM   3060 C CZ2 . TRP A 1 447 ? 56.44354 27.14374  7.79499   1.000 43.03616  ? 326  TRP A CZ2 1 
ATOM   3061 C CZ3 . TRP A 1 447 ? 56.86580 24.76492  7.71663   1.000 53.50974  ? 326  TRP A CZ3 1 
ATOM   3062 C CH2 . TRP A 1 447 ? 56.09611 25.86177  8.12837   1.000 52.41832  ? 326  TRP A CH2 1 
ATOM   3063 N N   . ILE A 1 448 ? 59.70693 27.71007  2.18743   1.000 66.67034  ? 327  ILE A N   1 
ATOM   3064 C CA  . ILE A 1 448 ? 59.54853 29.04355  1.62655   1.000 50.97404  ? 327  ILE A CA  1 
ATOM   3065 C C   . ILE A 1 448 ? 58.17707 29.54720  2.03699   1.000 63.11413  ? 327  ILE A C   1 
ATOM   3066 O O   . ILE A 1 448 ? 57.17408 28.85031  1.84335   1.000 63.77120  ? 327  ILE A O   1 
ATOM   3067 C CB  . ILE A 1 448 ? 59.69260 29.02865  0.09473   1.000 56.31385  ? 327  ILE A CB  1 
ATOM   3068 C CG1 . ILE A 1 448 ? 61.01398 28.37069  -0.29900  1.000 46.38444  ? 327  ILE A CG1 1 
ATOM   3069 C CG2 . ILE A 1 448 ? 59.59667 30.44143  -0.47122  1.000 44.65267  ? 327  ILE A CG2 1 
ATOM   3070 C CD1 . ILE A 1 448 ? 61.07870 27.95207  -1.75143  1.000 61.90479  ? 327  ILE A CD1 1 
ATOM   3071 N N   . GLU A 1 449 ? 58.12734 30.75514  2.58784   1.000 58.74237  ? 328  GLU A N   1 
ATOM   3072 C CA  . GLU A 1 449 ? 56.86872 31.27347  3.09975   1.000 50.93505  ? 328  GLU A CA  1 
ATOM   3073 C C   . GLU A 1 449 ? 56.92967 32.78856  3.02891   1.000 65.76907  ? 328  GLU A C   1 
ATOM   3074 O O   . GLU A 1 449 ? 57.92718 33.38771  3.44308   1.000 51.58655  ? 328  GLU A O   1 
ATOM   3075 C CB  . GLU A 1 449 ? 56.61190 30.79032  4.53228   1.000 56.66686  ? 328  GLU A CB  1 
ATOM   3076 C CG  . GLU A 1 449 ? 55.19123 31.01748  5.05885   1.000 46.69216  ? 328  GLU A CG  1 
ATOM   3077 C CD  . GLU A 1 449 ? 54.95668 32.42083  5.57135   1.000 54.51469  ? 328  GLU A CD  1 
ATOM   3078 O OE1 . GLU A 1 449 ? 55.77042 32.91055  6.38440   1.000 62.25190  ? 328  GLU A OE1 1 
ATOM   3079 O OE2 . GLU A 1 449 ? 53.94330 33.03271  5.16941   1.000 56.07252  ? 328  GLU A OE2 1 
ATOM   3080 N N   . ASN A 1 450 ? 55.86588 33.39542  2.49622   1.000 61.57500  ? 329  ASN A N   1 
ATOM   3081 C CA  . ASN A 1 450 ? 55.71584 34.85022  2.47360   1.000 52.39586  ? 329  ASN A CA  1 
ATOM   3082 C C   . ASN A 1 450 ? 56.91260 35.48891  1.76653   1.000 60.18636  ? 329  ASN A C   1 
ATOM   3083 O O   . ASN A 1 450 ? 57.41416 36.54268  2.16774   1.000 47.89509  ? 329  ASN A O   1 
ATOM   3084 C CB  . ASN A 1 450 ? 55.53984 35.40325  3.89203   1.000 47.43290  ? 329  ASN A CB  1 
ATOM   3085 C CG  . ASN A 1 450 ? 55.15641 36.87344  3.91493   1.000 59.80164  ? 329  ASN A CG  1 
ATOM   3086 O OD1 . ASN A 1 450 ? 54.89678 37.47965  2.87565   1.000 65.50087  ? 329  ASN A OD1 1 
ATOM   3087 N ND2 . ASN A 1 450 ? 55.13368 37.45664  5.10758   1.000 50.13595  ? 329  ASN A ND2 1 
ATOM   3088 N N   . SER A 1 451 ? 57.38071 34.82969  0.70493   1.000 50.88930  ? 330  SER A N   1 
ATOM   3089 C CA  . SER A 1 451 ? 58.59467 35.22990  0.00873   1.000 58.76029  ? 330  SER A CA  1 
ATOM   3090 C C   . SER A 1 451 ? 58.38040 35.18716  -1.49762  1.000 58.29097  ? 330  SER A C   1 
ATOM   3091 O O   . SER A 1 451 ? 57.60494 34.37503  -2.00718  1.000 63.32024  ? 330  SER A O   1 
ATOM   3092 C CB  . SER A 1 451 ? 59.77887 34.32960  0.38781   1.000 45.02938  ? 330  SER A CB  1 
ATOM   3093 O OG  . SER A 1 451 ? 60.15637 34.54509  1.73392   1.000 49.01202  ? 330  SER A OG  1 
ATOM   3094 N N   . HIS A 1 452 ? 59.07540 36.08108  -2.20071  1.000 55.15992  ? 331  HIS A N   1 
ATOM   3095 C CA  . HIS A 1 452 ? 59.19431 36.06288  -3.65550  1.000 50.70800  ? 331  HIS A CA  1 
ATOM   3096 C C   . HIS A 1 452 ? 60.59598 35.60832  -4.03898  1.000 56.61758  ? 331  HIS A C   1 
ATOM   3097 O O   . HIS A 1 452 ? 61.57826 36.28553  -3.71730  1.000 60.41183  ? 331  HIS A O   1 
ATOM   3098 C CB  . HIS A 1 452 ? 58.92048 37.44545  -4.23945  1.000 60.14981  ? 331  HIS A CB  1 
ATOM   3099 C CG  . HIS A 1 452 ? 58.89428 37.47636  -5.73592  1.000 66.25238  ? 331  HIS A CG  1 
ATOM   3100 N ND1 . HIS A 1 452 ? 60.03773 37.61035  -6.49596  1.000 61.79331  ? 331  HIS A ND1 1 
ATOM   3101 C CD2 . HIS A 1 452 ? 57.86466 37.41775  -6.61300  1.000 59.61737  ? 331  HIS A CD2 1 
ATOM   3102 C CE1 . HIS A 1 452 ? 59.71469 37.61522  -7.77698  1.000 59.71237  ? 331  HIS A CE1 1 
ATOM   3103 N NE2 . HIS A 1 452 ? 58.40218 37.50281  -7.87523  1.000 63.57925  ? 331  HIS A NE2 1 
ATOM   3104 N N   . ILE A 1 453 ? 60.68594 34.47366  -4.72558  1.000 57.23578  ? 332  ILE A N   1 
ATOM   3105 C CA  . ILE A 1 453 ? 61.95700 33.90549  -5.16447  1.000 52.91731  ? 332  ILE A CA  1 
ATOM   3106 C C   . ILE A 1 453 ? 62.10719 34.15646  -6.66348  1.000 63.54432  ? 332  ILE A C   1 
ATOM   3107 O O   . ILE A 1 453 ? 61.51089 33.45578  -7.48758  1.000 59.82268  ? 332  ILE A O   1 
ATOM   3108 C CB  . ILE A 1 453 ? 62.05364 32.42009  -4.81774  1.000 52.73242  ? 332  ILE A CB  1 
ATOM   3109 C CG1 . ILE A 1 453 ? 61.94172 32.25259  -3.30034  1.000 55.74033  ? 332  ILE A CG1 1 
ATOM   3110 C CG2 . ILE A 1 453 ? 63.35869 31.83581  -5.34021  1.000 65.29921  ? 332  ILE A CG2 1 
ATOM   3111 C CD1 . ILE A 1 453 ? 62.52350 30.97524  -2.77385  1.000 61.97195  ? 332  ILE A CD1 1 
ATOM   3112 N N   . GLY A 1 454 ? 62.91206 35.15788  -7.02073  1.000 56.54311  ? 333  GLY A N   1 
ATOM   3113 C CA  . GLY A 1 454 ? 63.09607 35.56097  -8.39750  1.000 58.73320  ? 333  GLY A CA  1 
ATOM   3114 C C   . GLY A 1 454 ? 63.87018 34.55753  -9.23572  1.000 70.51187  ? 333  GLY A C   1 
ATOM   3115 O O   . GLY A 1 454 ? 64.62801 33.72837  -8.71990  1.000 72.92613  ? 333  GLY A O   1 
ATOM   3116 N N   . PRO A 1 455 ? 63.68993 34.62418  -10.55982 1.000 57.21395  ? 334  PRO A N   1 
ATOM   3117 C CA  . PRO A 1 455 ? 64.25896 33.58825  -11.44308 1.000 63.81573  ? 334  PRO A CA  1 
ATOM   3118 C C   . PRO A 1 455 ? 65.77797 33.50426  -11.44699 1.000 74.13804  ? 334  PRO A C   1 
ATOM   3119 O O   . PRO A 1 455 ? 66.31748 32.48659  -11.89975 1.000 70.66209  ? 334  PRO A O   1 
ATOM   3120 C CB  . PRO A 1 455 ? 63.73128 33.98816  -12.82728 1.000 53.63794  ? 334  PRO A CB  1 
ATOM   3121 C CG  . PRO A 1 455 ? 63.54861 35.46815  -12.72851 1.000 57.85915  ? 334  PRO A CG  1 
ATOM   3122 C CD  . PRO A 1 455 ? 63.04342 35.70349  -11.32511 1.000 50.98384  ? 334  PRO A CD  1 
ATOM   3123 N N   . LYS A 1 456 ? 66.49088 34.52237  -10.97233 1.000 72.62668  ? 335  LYS A N   1 
ATOM   3124 C CA  . LYS A 1 456 ? 67.94599 34.46982  -10.93765 1.000 70.17376  ? 335  LYS A CA  1 
ATOM   3125 C C   . LYS A 1 456 ? 68.48978 34.00399  -9.59516  1.000 71.09458  ? 335  LYS A C   1 
ATOM   3126 O O   . LYS A 1 456 ? 69.69401 34.12214  -9.35484  1.000 73.35667  ? 335  LYS A O   1 
ATOM   3127 C CB  . LYS A 1 456 ? 68.54258 35.82739  -11.31422 1.000 62.87119  ? 335  LYS A CB  1 
ATOM   3128 C CG  . LYS A 1 456 ? 68.17303 36.27800  -12.72293 1.000 72.66030  ? 335  LYS A CG  1 
ATOM   3129 C CD  . LYS A 1 456 ? 68.39157 37.76610  -12.92607 1.000 73.46349  ? 335  LYS A CD  1 
ATOM   3130 C CE  . LYS A 1 456 ? 67.53182 38.29026  -14.06290 1.000 82.54132  ? 335  LYS A CE  1 
ATOM   3131 N NZ  . LYS A 1 456 ? 67.78758 39.73143  -14.33409 1.000 92.15546  ? 335  LYS A NZ  1 
ATOM   3132 N N   . TRP A 1 457 ? 67.63993 33.47460  -8.71960  1.000 63.03999  ? 336  TRP A N   1 
ATOM   3133 C CA  . TRP A 1 457 ? 68.14066 32.89872  -7.48381  1.000 56.81254  ? 336  TRP A CA  1 
ATOM   3134 C C   . TRP A 1 457 ? 68.80302 31.55525  -7.75975  1.000 64.65810  ? 336  TRP A C   1 
ATOM   3135 O O   . TRP A 1 457 ? 68.41381 30.81535  -8.66764  1.000 69.51970  ? 336  TRP A O   1 
ATOM   3136 C CB  . TRP A 1 457 ? 67.01811 32.70093  -6.46121  1.000 53.32121  ? 336  TRP A CB  1 
ATOM   3137 C CG  . TRP A 1 457 ? 66.49422 33.95125  -5.80214  1.000 53.03391  ? 336  TRP A CG  1 
ATOM   3138 C CD1 . TRP A 1 457 ? 66.22687 35.15362  -6.39693  1.000 56.81435  ? 336  TRP A CD1 1 
ATOM   3139 C CD2 . TRP A 1 457 ? 66.17612 34.11256  -4.41238  1.000 48.66006  ? 336  TRP A CD2 1 
ATOM   3140 N NE1 . TRP A 1 457 ? 65.75508 36.04873  -5.46287  1.000 50.26557  ? 336  TRP A NE1 1 
ATOM   3141 C CE2 . TRP A 1 457 ? 65.71851 35.43442  -4.23738  1.000 47.00873  ? 336  TRP A CE2 1 
ATOM   3142 C CE3 . TRP A 1 457 ? 66.23266 33.26497  -3.29961  1.000 54.78776  ? 336  TRP A CE3 1 
ATOM   3143 C CZ2 . TRP A 1 457 ? 65.32017 35.92895  -2.99388  1.000 56.24146  ? 336  TRP A CZ2 1 
ATOM   3144 C CZ3 . TRP A 1 457 ? 65.83611 33.75788  -2.06380  1.000 48.31265  ? 336  TRP A CZ3 1 
ATOM   3145 C CH2 . TRP A 1 457 ? 65.38530 35.07757  -1.92265  1.000 52.93171  ? 336  TRP A CH2 1 
ATOM   3146 N N   . LYS A 1 458 ? 69.82066 31.24932  -6.96327  1.000 65.90591  ? 337  LYS A N   1 
ATOM   3147 C CA  . LYS A 1 458 ? 70.44759 29.93603  -6.93869  1.000 67.31230  ? 337  LYS A CA  1 
ATOM   3148 C C   . LYS A 1 458 ? 70.33221 29.40949  -5.51910  1.000 66.95351  ? 337  LYS A C   1 
ATOM   3149 O O   . LYS A 1 458 ? 70.82444 30.04208  -4.57929  1.000 74.39972  ? 337  LYS A O   1 
ATOM   3150 C CB  . LYS A 1 458 ? 71.90926 29.99071  -7.39020  1.000 73.32682  ? 337  LYS A CB  1 
ATOM   3151 C CG  . LYS A 1 458 ? 72.12217 30.48589  -8.81792  1.000 76.65370  ? 337  LYS A CG  1 
ATOM   3152 C CD  . LYS A 1 458 ? 72.55278 31.94282  -8.88573  1.000 83.55161  ? 337  LYS A CD  1 
ATOM   3153 C CE  . LYS A 1 458 ? 72.56878 32.43519  -10.33036 1.000 98.55377  ? 337  LYS A CE  1 
ATOM   3154 N NZ  . LYS A 1 458 ? 72.11513 33.84805  -10.45994 1.000 92.53487  ? 337  LYS A NZ  1 
ATOM   3155 N N   . ILE A 1 459 ? 69.67677 28.26102  -5.36213  1.000 66.52270  ? 338  ILE A N   1 
ATOM   3156 C CA  . ILE A 1 459 ? 69.50957 27.63657  -4.06030  1.000 66.20551  ? 338  ILE A CA  1 
ATOM   3157 C C   . ILE A 1 459 ? 69.93553 26.17942  -4.15328  1.000 64.32469  ? 338  ILE A C   1 
ATOM   3158 O O   . ILE A 1 459 ? 70.22160 25.65134  -5.22822  1.000 74.17908  ? 338  ILE A O   1 
ATOM   3159 C CB  . ILE A 1 459 ? 68.05883 27.73131  -3.53446  1.000 63.69282  ? 338  ILE A CB  1 
ATOM   3160 C CG1 . ILE A 1 459 ? 67.13750 26.80117  -4.32661  1.000 64.99056  ? 338  ILE A CG1 1 
ATOM   3161 C CG2 . ILE A 1 459 ? 67.55049 29.16926  -3.58643  1.000 48.57521  ? 338  ILE A CG2 1 
ATOM   3162 C CD1 . ILE A 1 459 ? 65.68166 26.86122  -3.88436  1.000 56.42036  ? 338  ILE A CD1 1 
ATOM   3163 N N   . ALA A 1 460 ? 69.96838 25.53658  -2.99082  1.000 62.87881  ? 339  ALA A N   1 
ATOM   3164 C CA  . ALA A 1 460 ? 70.43376 24.16674  -2.84532  1.000 65.98570  ? 339  ALA A CA  1 
ATOM   3165 C C   . ALA A 1 460 ? 69.43378 23.40923  -1.98388  1.000 65.77454  ? 339  ALA A C   1 
ATOM   3166 O O   . ALA A 1 460 ? 68.27310 23.25048  -2.37128  1.000 73.25497  ? 339  ALA A O   1 
ATOM   3167 C CB  . ALA A 1 460 ? 71.83557 24.12942  -2.23319  1.000 61.66690  ? 339  ALA A CB  1 
ATOM   3168 N N   . SER A 1 461 ? 69.86452 22.95560  -0.81122  1.000 59.80491  ? 340  SER A N   1 
ATOM   3169 C CA  . SER A 1 461 ? 68.99951 22.26854  0.13424   1.000 61.15346  ? 340  SER A CA  1 
ATOM   3170 C C   . SER A 1 461 ? 69.17512 22.89586  1.51096   1.000 68.00612  ? 340  SER A C   1 
ATOM   3171 O O   . SER A 1 461 ? 70.11021 23.66509  1.75329   1.000 86.71230  ? 340  SER A O   1 
ATOM   3172 C CB  . SER A 1 461 ? 69.30375 20.76479  0.18436   1.000 69.39090  ? 340  SER A CB  1 
ATOM   3173 O OG  . SER A 1 461 ? 70.62532 20.52788  0.64221   1.000 87.71122  ? 340  SER A OG  1 
ATOM   3174 N N   . ARG A 1 462 ? 68.24795 22.56353  2.41122   1.000 79.59581  ? 341  ARG A N   1 
ATOM   3175 C CA  . ARG A 1 462 ? 68.24895 23.06155  3.78409   1.000 74.64782  ? 341  ARG A CA  1 
ATOM   3176 C C   . ARG A 1 462 ? 68.16766 24.58338  3.81174   1.000 64.19236  ? 341  ARG A C   1 
ATOM   3177 O O   . ARG A 1 462 ? 69.16563 25.26717  4.05378   1.000 62.87691  ? 341  ARG A O   1 
ATOM   3178 C CB  . ARG A 1 462 ? 69.48006 22.56580  4.54684   1.000 74.10870  ? 341  ARG A CB  1 
ATOM   3179 C CG  . ARG A 1 462 ? 69.66582 21.05850  4.49449   1.000 77.40781  ? 341  ARG A CG  1 
ATOM   3180 C CD  . ARG A 1 462 ? 70.56723 20.56794  5.62291   1.000 87.26374  ? 341  ARG A CD  1 
ATOM   3181 N NE  . ARG A 1 462 ? 71.73569 21.42413  5.82085   1.000 91.11288  ? 341  ARG A NE  1 
ATOM   3182 C CZ  . ARG A 1 462 ? 72.77644 21.48154  4.99503   1.000 88.78151  ? 341  ARG A CZ  1 
ATOM   3183 N NH1 . ARG A 1 462 ? 72.80625 20.72863  3.90267   1.000 87.28224  ? 341  ARG A NH1 1 
ATOM   3184 N NH2 . ARG A 1 462 ? 73.79032 22.29332  5.26145   1.000 91.07192  ? 341  ARG A NH2 1 
ATOM   3185 N N   . HIS A 1 463 ? 66.97333 25.11820  3.58155   1.000 63.41875  ? 342  HIS A N   1 
ATOM   3186 C CA  . HIS A 1 463 ? 66.74447 26.55337  3.54946   1.000 56.31617  ? 342  HIS A CA  1 
ATOM   3187 C C   . HIS A 1 463 ? 65.44530 26.86663  4.26879   1.000 57.36581  ? 342  HIS A C   1 
ATOM   3188 O O   . HIS A 1 463 ? 64.48908 26.08813  4.22837   1.000 69.56911  ? 342  HIS A O   1 
ATOM   3189 C CB  . HIS A 1 463 ? 66.63031 27.11208  2.12374   1.000 49.22606  ? 342  HIS A CB  1 
ATOM   3190 C CG  . HIS A 1 463 ? 67.82531 26.86025  1.26371   1.000 59.39625  ? 342  HIS A CG  1 
ATOM   3191 N ND1 . HIS A 1 463 ? 69.08040 27.33841  1.57350   1.000 55.90090  ? 342  HIS A ND1 1 
ATOM   3192 C CD2 . HIS A 1 463 ? 67.95255 26.19442  0.09188   1.000 52.92652  ? 342  HIS A CD2 1 
ATOM   3193 C CE1 . HIS A 1 463 ? 69.93078 26.97101  0.63232   1.000 61.59907  ? 342  HIS A CE1 1 
ATOM   3194 N NE2 . HIS A 1 463 ? 69.27225 26.27562  -0.27744  1.000 66.92636  ? 342  HIS A NE2 1 
ATOM   3195 N N   . ILE A 1 464 ? 65.41461 28.02498  4.91549   1.000 57.39081  ? 343  ILE A N   1 
ATOM   3196 C CA  . ILE A 1 464 ? 64.17178 28.62710  5.36667   1.000 47.83727  ? 343  ILE A CA  1 
ATOM   3197 C C   . ILE A 1 464 ? 64.17749 30.05395  4.84563   1.000 56.01312  ? 343  ILE A C   1 
ATOM   3198 O O   . ILE A 1 464 ? 65.00901 30.87042  5.26194   1.000 64.45471  ? 343  ILE A O   1 
ATOM   3199 C CB  . ILE A 1 464 ? 64.01718 28.59605  6.89002   1.000 53.34100  ? 343  ILE A CB  1 
ATOM   3200 C CG1 . ILE A 1 464 ? 63.80804 27.15838  7.36018   1.000 48.49776  ? 343  ILE A CG1 1 
ATOM   3201 C CG2 . ILE A 1 464 ? 62.84074 29.45934  7.31249   1.000 43.09954  ? 343  ILE A CG2 1 
ATOM   3202 C CD1 . ILE A 1 464 ? 63.70625 27.02682  8.85838   1.000 51.66024  ? 343  ILE A CD1 1 
ATOM   3203 N N   . ILE A 1 465 ? 63.26821 30.35047  3.92374   1.000 57.71096  ? 344  ILE A N   1 
ATOM   3204 C CA  . ILE A 1 465 ? 63.18192 31.65767  3.29100   1.000 54.81351  ? 344  ILE A CA  1 
ATOM   3205 C C   . ILE A 1 465 ? 61.83241 32.24208  3.67671   1.000 56.52633  ? 344  ILE A C   1 
ATOM   3206 O O   . ILE A 1 465 ? 60.78490 31.67916  3.33500   1.000 61.49887  ? 344  ILE A O   1 
ATOM   3207 C CB  . ILE A 1 465 ? 63.33837 31.56708  1.76488   1.000 58.34479  ? 344  ILE A CB  1 
ATOM   3208 C CG1 . ILE A 1 465 ? 64.74861 31.09841  1.40654   1.000 53.86883  ? 344  ILE A CG1 1 
ATOM   3209 C CG2 . ILE A 1 465 ? 63.08955 32.92135  1.12356   1.000 42.15737  ? 344  ILE A CG2 1 
ATOM   3210 C CD1 . ILE A 1 465 ? 64.85330 30.49777  0.02089   1.000 55.77047  ? 344  ILE A CD1 1 
ATOM   3211 N N   . THR A 1 466 ? 61.85623 33.35752  4.39815   1.000 50.35465  ? 345  THR A N   1 
ATOM   3212 C CA  . THR A 1 466 ? 60.64969 33.94778  4.95015   1.000 47.76573  ? 345  THR A CA  1 
ATOM   3213 C C   . THR A 1 466 ? 60.72698 35.45697  4.80852   1.000 48.39644  ? 345  THR A C   1 
ATOM   3214 O O   . THR A 1 466 ? 61.78925 36.04978  5.00980   1.000 55.46025  ? 345  THR A O   1 
ATOM   3215 C CB  . THR A 1 466 ? 60.46364 33.58636  6.43408   1.000 57.36504  ? 345  THR A CB  1 
ATOM   3216 O OG1 . THR A 1 466 ? 61.62927 33.97726  7.17023   1.000 54.37078  ? 345  THR A OG1 1 
ATOM   3217 C CG2 . THR A 1 466 ? 60.22298 32.08483  6.61674   1.000 38.64906  ? 345  THR A CG2 1 
ATOM   3218 N N   . GLY A 1 467 ? 59.60286 36.07176  4.44993   1.000 53.91347  ? 346  GLY A N   1 
ATOM   3219 C CA  . GLY A 1 467 ? 59.49251 37.51296  4.46548   1.000 51.13794  ? 346  GLY A CA  1 
ATOM   3220 C C   . GLY A 1 467 ? 59.98615 38.23233  3.22933   1.000 50.62846  ? 346  GLY A C   1 
ATOM   3221 O O   . GLY A 1 467 ? 59.91990 39.46719  3.19289   1.000 57.56780  ? 346  GLY A O   1 
ATOM   3222 N N   . VAL A 1 468 ? 60.46789 37.51628  2.21631   1.000 43.02187  ? 347  VAL A N   1 
ATOM   3223 C CA  . VAL A 1 468 ? 61.22519 38.14655  1.13529   1.000 47.21663  ? 347  VAL A CA  1 
ATOM   3224 C C   . VAL A 1 468 ? 60.28851 38.82823  0.14289   1.000 48.43036  ? 347  VAL A C   1 
ATOM   3225 O O   . VAL A 1 468 ? 59.49804 38.15829  -0.53681  1.000 54.41731  ? 347  VAL A O   1 
ATOM   3226 C CB  . VAL A 1 468 ? 62.12973 37.12800  0.42340   1.000 55.77604  ? 347  VAL A CB  1 
ATOM   3227 C CG1 . VAL A 1 468 ? 62.72101 37.73700  -0.83680  1.000 51.84268  ? 347  VAL A CG1 1 
ATOM   3228 C CG2 . VAL A 1 468 ? 63.23546 36.64916  1.36301   1.000 50.77979  ? 347  VAL A CG2 1 
ATOM   3229 N N   . PRO A 1 469 ? 60.33895 40.15188  0.03360   1.000 57.87901  ? 348  PRO A N   1 
ATOM   3230 C CA  . PRO A 1 469 ? 59.46353 40.86089  -0.90726  1.000 56.68019  ? 348  PRO A CA  1 
ATOM   3231 C C   . PRO A 1 469 ? 59.85888 40.60750  -2.35615  1.000 63.46919  ? 348  PRO A C   1 
ATOM   3232 O O   . PRO A 1 469 ? 60.90113 40.02387  -2.66474  1.000 53.85354  ? 348  PRO A O   1 
ATOM   3233 C CB  . PRO A 1 469 ? 59.66820 42.32641  -0.52147  1.000 58.90572  ? 348  PRO A CB  1 
ATOM   3234 C CG  . PRO A 1 469 ? 61.09309 42.34755  -0.02711  1.000 49.96473  ? 348  PRO A CG  1 
ATOM   3235 C CD  . PRO A 1 469 ? 61.20743 41.08278  0.77594   1.000 47.94083  ? 348  PRO A CD  1 
ATOM   3236 N N   . GLU A 1 470 ? 58.99347 41.07680  -3.25571  1.000 57.58246  ? 349  GLU A N   1 
ATOM   3237 C CA  . GLU A 1 470 ? 59.19249 40.87086  -4.68509  1.000 60.70187  ? 349  GLU A CA  1 
ATOM   3238 C C   . GLU A 1 470 ? 60.50927 41.48952  -5.13956  1.000 57.63213  ? 349  GLU A C   1 
ATOM   3239 O O   . GLU A 1 470 ? 60.89004 42.57450  -4.69324  1.000 58.26140  ? 349  GLU A O   1 
ATOM   3240 C CB  . GLU A 1 470 ? 58.02282 41.47660  -5.46286  1.000 60.63352  ? 349  GLU A CB  1 
ATOM   3241 C CG  . GLU A 1 470 ? 58.21351 41.53697  -6.97010  1.000 64.42851  ? 349  GLU A CG  1 
ATOM   3242 C CD  . GLU A 1 470 ? 56.93735 41.91156  -7.70010  1.000 72.72822  ? 349  GLU A CD  1 
ATOM   3243 O OE1 . GLU A 1 470 ? 55.85442 41.42225  -7.30687  1.000 65.78568  ? 349  GLU A OE1 1 
ATOM   3244 O OE2 . GLU A 1 470 ? 57.01974 42.70224  -8.66389  1.000 74.66559  ? 349  GLU A OE2 1 
ATOM   3245 N N   . ASN A 1 471 ? 61.19501 40.80011  -6.04959  1.000 62.00563  ? 350  ASN A N   1 
ATOM   3246 C CA  . ASN A 1 471 ? 62.56906 41.13789  -6.39938  1.000 57.34085  ? 350  ASN A CA  1 
ATOM   3247 C C   . ASN A 1 471 ? 62.97699 40.34805  -7.63256  1.000 56.47893  ? 350  ASN A C   1 
ATOM   3248 O O   . ASN A 1 471 ? 62.41562 39.28944  -7.92609  1.000 68.17093  ? 350  ASN A O   1 
ATOM   3249 C CB  . ASN A 1 471 ? 63.52997 40.82532  -5.25190  1.000 48.82188  ? 350  ASN A CB  1 
ATOM   3250 C CG  . ASN A 1 471 ? 63.82468 39.34217  -5.13804  1.000 49.94098  ? 350  ASN A CG  1 
ATOM   3251 O OD1 . ASN A 1 471 ? 64.68873 38.81334  -5.83881  1.000 75.89996  ? 350  ASN A OD1 1 
ATOM   3252 N ND2 . ASN A 1 471 ? 63.10058 38.66026  -4.26086  1.000 54.59556  ? 350  ASN A ND2 1 
ATOM   3253 N N   . ASP A 1 472 ? 63.97171 40.87262  -8.34616  1.000 73.12182  ? 351  ASP A N   1 
ATOM   3254 C CA  . ASP A 1 472 ? 64.63352 40.09298  -9.38573  1.000 78.68748  ? 351  ASP A CA  1 
ATOM   3255 C C   . ASP A 1 472 ? 66.11053 39.91842  -9.04339  1.000 62.98978  ? 351  ASP A C   1 
ATOM   3256 O O   . ASP A 1 472 ? 66.98250 40.09559  -9.89862  1.000 72.60812  ? 351  ASP A O   1 
ATOM   3257 C CB  . ASP A 1 472 ? 64.45378 40.76031  -10.75326 1.000 67.06482  ? 351  ASP A CB  1 
ATOM   3258 C CG  . ASP A 1 472 ? 64.94149 39.89175  -11.89992 1.000 77.12125  ? 351  ASP A CG  1 
ATOM   3259 O OD1 . ASP A 1 472 ? 64.98861 38.65343  -11.73115 1.000 66.20327  ? 351  ASP A OD1 1 
ATOM   3260 O OD2 . ASP A 1 472 ? 65.27499 40.44826  -12.96873 1.000 85.36307  ? 351  ASP A OD2 1 
ATOM   3261 N N   . TRP A 1 473 ? 66.40173 39.58275  -7.79017  1.000 65.39566  ? 352  TRP A N   1 
ATOM   3262 C CA  . TRP A 1 473 ? 67.78508 39.49143  -7.34139  1.000 61.72691  ? 352  TRP A CA  1 
ATOM   3263 C C   . TRP A 1 473 ? 68.49658 38.32282  -8.00881  1.000 65.47348  ? 352  TRP A C   1 
ATOM   3264 O O   . TRP A 1 473 ? 67.90474 37.26462  -8.23826  1.000 60.94658  ? 352  TRP A O   1 
ATOM   3265 C CB  . TRP A 1 473 ? 67.85535 39.30109  -5.83080  1.000 53.64486  ? 352  TRP A CB  1 
ATOM   3266 C CG  . TRP A 1 473 ? 67.29802 40.41617  -5.03307  1.000 61.88714  ? 352  TRP A CG  1 
ATOM   3267 C CD1 . TRP A 1 473 ? 67.19031 41.72470  -5.40189  1.000 56.51261  ? 352  TRP A CD1 1 
ATOM   3268 C CD2 . TRP A 1 473 ? 66.79321 40.32798  -3.69901  1.000 43.52943  ? 352  TRP A CD2 1 
ATOM   3269 N NE1 . TRP A 1 473 ? 66.62802 42.45580  -4.38110  1.000 51.27239  ? 352  TRP A NE1 1 
ATOM   3270 C CE2 . TRP A 1 473 ? 66.37634 41.61831  -3.32448  1.000 52.61357  ? 352  TRP A CE2 1 
ATOM   3271 C CE3 . TRP A 1 473 ? 66.64644 39.27818  -2.78704  1.000 52.53960  ? 352  TRP A CE3 1 
ATOM   3272 C CZ2 . TRP A 1 473 ? 65.83089 41.88939  -2.07333  1.000 52.34269  ? 352  TRP A CZ2 1 
ATOM   3273 C CZ3 . TRP A 1 473 ? 66.10617 39.54781  -1.54650  1.000 43.08938  ? 352  TRP A CZ3 1 
ATOM   3274 C CH2 . TRP A 1 473 ? 65.70143 40.84223  -1.20241  1.000 54.16016  ? 352  TRP A CH2 1 
ATOM   3275 N N   . SER A 1 474 ? 69.78094 38.51229  -8.31367  1.000 60.56912  ? 353  SER A N   1 
ATOM   3276 C CA  . SER A 1 474 ? 70.66454 37.38300  -8.60079  1.000 68.55118  ? 353  SER A CA  1 
ATOM   3277 C C   . SER A 1 474 ? 71.34444 36.99640  -7.29028  1.000 63.45198  ? 353  SER A C   1 
ATOM   3278 O O   . SER A 1 474 ? 72.51337 37.29383  -7.03857  1.000 68.99301  ? 353  SER A O   1 
ATOM   3279 C CB  . SER A 1 474 ? 71.67046 37.74000  -9.68753  1.000 75.66911  ? 353  SER A CB  1 
ATOM   3280 O OG  . SER A 1 474 ? 72.40265 38.90055  -9.33628  1.000 91.97671  ? 353  SER A OG  1 
ATOM   3281 N N   . LEU A 1 475 ? 70.57818 36.33419  -6.43040  1.000 68.83296  ? 354  LEU A N   1 
ATOM   3282 C CA  . LEU A 1 475 ? 71.03891 35.94137  -5.10675  1.000 62.41544  ? 354  LEU A CA  1 
ATOM   3283 C C   . LEU A 1 475 ? 71.30685 34.44426  -5.07160  1.000 74.21762  ? 354  LEU A C   1 
ATOM   3284 O O   . LEU A 1 475 ? 70.42685 33.64489  -5.40862  1.000 61.71513  ? 354  LEU A O   1 
ATOM   3285 C CB  . LEU A 1 475 ? 70.01236 36.31321  -4.03599  1.000 52.75444  ? 354  LEU A CB  1 
ATOM   3286 C CG  . LEU A 1 475 ? 70.35682 35.83810  -2.62237  1.000 61.99548  ? 354  LEU A CG  1 
ATOM   3287 C CD1 . LEU A 1 475 ? 71.61647 36.53123  -2.11394  1.000 58.29255  ? 354  LEU A CD1 1 
ATOM   3288 C CD2 . LEU A 1 475 ? 69.18843 36.05916  -1.66978  1.000 60.83542  ? 354  LEU A CD2 1 
ATOM   3289 N N   . ALA A 1 476 ? 72.51705 34.07028  -4.66553  1.000 64.06245  ? 355  ALA A N   1 
ATOM   3290 C CA  . ALA A 1 476 ? 72.86545 32.67875  -4.42505  1.000 53.44869  ? 355  ALA A CA  1 
ATOM   3291 C C   . ALA A 1 476 ? 72.74673 32.39506  -2.93575  1.000 63.10202  ? 355  ALA A C   1 
ATOM   3292 O O   . ALA A 1 476 ? 73.19831 33.19027  -2.10643  1.000 67.78430  ? 355  ALA A O   1 
ATOM   3293 C CB  . ALA A 1 476 ? 74.28335 32.36767  -4.91181  1.000 50.47894  ? 355  ALA A CB  1 
ATOM   3294 N N   . VAL A 1 477 ? 72.13562 31.26842  -2.59839  1.000 63.48553  ? 356  VAL A N   1 
ATOM   3295 C CA  . VAL A 1 477 ? 71.89175 30.88906  -1.21506  1.000 61.82169  ? 356  VAL A CA  1 
ATOM   3296 C C   . VAL A 1 477 ? 72.56701 29.54875  -0.96107  1.000 75.34011  ? 356  VAL A C   1 
ATOM   3297 O O   . VAL A 1 477 ? 72.07169 28.50222  -1.38270  1.000 67.73210  ? 356  VAL A O   1 
ATOM   3298 C CB  . VAL A 1 477 ? 70.38589 30.81683  -0.90593  1.000 62.51625  ? 356  VAL A CB  1 
ATOM   3299 C CG1 . VAL A 1 477 ? 70.16477 30.49933  0.56686   1.000 60.38456  ? 356  VAL A CG1 1 
ATOM   3300 C CG2 . VAL A 1 477 ? 69.69917 32.12052  -1.29278  1.000 47.84882  ? 356  VAL A CG2 1 
ATOM   3301 N N   . PRO A 1 478 ? 73.70996 29.54429  -0.27247  1.000 64.35716  ? 357  PRO A N   1 
ATOM   3302 C CA  . PRO A 1 478 ? 74.41377 28.28342  -0.00756  1.000 62.35069  ? 357  PRO A CA  1 
ATOM   3303 C C   . PRO A 1 478 ? 73.55119 27.33076  0.80583   1.000 63.57457  ? 357  PRO A C   1 
ATOM   3304 O O   . PRO A 1 478 ? 72.64352 27.74572  1.53070   1.000 63.95413  ? 357  PRO A O   1 
ATOM   3305 C CB  . PRO A 1 478 ? 75.66055 28.72025  0.77573   1.000 58.21733  ? 357  PRO A CB  1 
ATOM   3306 C CG  . PRO A 1 478 ? 75.75580 30.20804  0.59066   1.000 62.65001  ? 357  PRO A CG  1 
ATOM   3307 C CD  . PRO A 1 478 ? 74.35831 30.69255  0.38010   1.000 65.07596  ? 357  PRO A CD  1 
ATOM   3308 N N   . ALA A 1 479 ? 73.83830 26.03690  0.66426   1.000 57.71184  ? 358  ALA A N   1 
ATOM   3309 C CA  . ALA A 1 479 ? 73.15891 25.02654  1.46279   1.000 67.77206  ? 358  ALA A CA  1 
ATOM   3310 C C   . ALA A 1 479 ? 73.25918 25.36006  2.94600   1.000 61.75606  ? 358  ALA A C   1 
ATOM   3311 O O   . ALA A 1 479 ? 74.29754 25.82030  3.42923   1.000 65.64337  ? 358  ALA A O   1 
ATOM   3312 C CB  . ALA A 1 479 ? 73.76238 23.64675  1.18815   1.000 56.52697  ? 358  ALA A CB  1 
ATOM   3313 N N   . GLY A 1 480 ? 72.16674 25.12048  3.67085   1.000 56.35641  ? 359  GLY A N   1 
ATOM   3314 C CA  . GLY A 1 480 ? 72.12771 25.37580  5.09530   1.000 52.67717  ? 359  GLY A CA  1 
ATOM   3315 C C   . GLY A 1 480 ? 71.94205 26.82580  5.48474   1.000 52.71911  ? 359  GLY A C   1 
ATOM   3316 O O   . GLY A 1 480 ? 71.70571 27.10574  6.66747   1.000 62.09718  ? 359  GLY A O   1 
ATOM   3317 N N   . VAL A 1 481 ? 72.02921 27.75564  4.53843   1.000 54.25523  ? 360  VAL A N   1 
ATOM   3318 C CA  . VAL A 1 481 ? 71.78671 29.16872  4.80277   1.000 58.32790  ? 360  VAL A CA  1 
ATOM   3319 C C   . VAL A 1 481 ? 70.30424 29.47430  4.63001   1.000 59.32522  ? 360  VAL A C   1 
ATOM   3320 O O   . VAL A 1 481 ? 69.65679 29.00303  3.68640   1.000 56.14284  ? 360  VAL A O   1 
ATOM   3321 C CB  . VAL A 1 481 ? 72.64823 30.04515  3.87309   1.000 59.22101  ? 360  VAL A CB  1 
ATOM   3322 C CG1 . VAL A 1 481 ? 72.24937 31.50856  3.98414   1.000 53.77712  ? 360  VAL A CG1 1 
ATOM   3323 C CG2 . VAL A 1 481 ? 74.13047 29.86029  4.18808   1.000 47.02664  ? 360  VAL A CG2 1 
ATOM   3324 N N   . CYS A 1 482 ? 69.76487 30.26657  5.55048   1.000 60.47969  ? 361  CYS A N   1 
ATOM   3325 C CA  . CYS A 1 482 ? 68.39635 30.74736  5.51984   1.000 55.15399  ? 361  CYS A CA  1 
ATOM   3326 C C   . CYS A 1 482 ? 68.39172 32.26071  5.33447   1.000 63.36949  ? 361  CYS A C   1 
ATOM   3327 O O   . CYS A 1 482 ? 69.34010 32.95935  5.71452   1.000 62.24133  ? 361  CYS A O   1 
ATOM   3328 C CB  . CYS A 1 482 ? 67.66978 30.37858  6.81861   1.000 48.62548  ? 361  CYS A CB  1 
ATOM   3329 S SG  . CYS A 1 482 ? 67.75998 28.63566  7.27798   1.000 56.69664  ? 361  CYS A SG  1 
ATOM   3330 N N   . VAL A 1 483 ? 67.27310 32.76844  4.81919   1.000 61.22187  ? 362  VAL A N   1 
ATOM   3331 C CA  . VAL A 1 483 ? 67.10718 34.18245  4.49871   1.000 51.06879  ? 362  VAL A CA  1 
ATOM   3332 C C   . VAL A 1 483 ? 65.78088 34.63981  5.08054   1.000 63.66596  ? 362  VAL A C   1 
ATOM   3333 O O   . VAL A 1 483 ? 64.71959 34.16217  4.65948   1.000 61.85250  ? 362  VAL A O   1 
ATOM   3334 C CB  . VAL A 1 483 ? 67.13296 34.44199  2.98154   1.000 58.04489  ? 362  VAL A CB  1 
ATOM   3335 C CG1 . VAL A 1 483 ? 66.80648 35.90366  2.68410   1.000 47.07040  ? 362  VAL A CG1 1 
ATOM   3336 C CG2 . VAL A 1 483 ? 68.48502 34.06167  2.38753   1.000 54.24973  ? 362  VAL A CG2 1 
ATOM   3337 N N   . ASP A 1 484 ? 65.82861 35.56932  6.03030   1.000 62.56893  ? 363  ASP A N   1 
ATOM   3338 C CA  . ASP A 1 484 ? 64.62600 36.16051  6.58333   1.000 46.68071  ? 363  ASP A CA  1 
ATOM   3339 C C   . ASP A 1 484 ? 64.64802 37.66067  6.32683   1.000 52.81742  ? 363  ASP A C   1 
ATOM   3340 O O   . ASP A 1 484 ? 65.70209 38.29888  6.39105   1.000 58.47564  ? 363  ASP A O   1 
ATOM   3341 C CB  . ASP A 1 484 ? 64.51476 35.85228  8.08085   1.000 50.51950  ? 363  ASP A CB  1 
ATOM   3342 C CG  . ASP A 1 484 ? 63.31230 36.49991  8.72565   1.000 65.51073  ? 363  ASP A CG  1 
ATOM   3343 O OD1 . ASP A 1 484 ? 62.18218 36.30677  8.22404   1.000 56.70275  ? 363  ASP A OD1 1 
ATOM   3344 O OD2 . ASP A 1 484 ? 63.50165 37.18683  9.74799   1.000 55.72447  ? 363  ASP A OD2 1 
ATOM   3345 N N   . VAL A 1 485 ? 63.49592 38.21467  5.97339   1.000 58.04769  ? 364  VAL A N   1 
ATOM   3346 C CA  . VAL A 1 485 ? 63.33364 39.65513  5.82859   1.000 50.98423  ? 364  VAL A CA  1 
ATOM   3347 C C   . VAL A 1 485 ? 62.18031 40.07618  6.72475   1.000 50.88711  ? 364  VAL A C   1 
ATOM   3348 O O   . VAL A 1 485 ? 61.13506 39.41405  6.75083   1.000 58.80740  ? 364  VAL A O   1 
ATOM   3349 C CB  . VAL A 1 485 ? 63.09113 40.06900  4.36151   1.000 48.98357  ? 364  VAL A CB  1 
ATOM   3350 C CG1 . VAL A 1 485 ? 62.78344 41.56210  4.27516   1.000 52.70483  ? 364  VAL A CG1 1 
ATOM   3351 C CG2 . VAL A 1 485 ? 64.31323 39.72500  3.50728   1.000 47.37668  ? 364  VAL A CG2 1 
ATOM   3352 N N   . VAL A 1 486 ? 62.36548 41.17123  7.46539   1.000 48.78968  ? 365  VAL A N   1 
ATOM   3353 C CA  . VAL A 1 486 ? 61.38825 41.61163  8.44483   1.000 54.50731  ? 365  VAL A CA  1 
ATOM   3354 C C   . VAL A 1 486 ? 61.05940 43.07847  8.20406   1.000 57.09117  ? 365  VAL A C   1 
ATOM   3355 O O   . VAL A 1 486 ? 61.93629 43.93282  8.32599   1.000 64.18587  ? 365  VAL A O   1 
ATOM   3356 C CB  . VAL A 1 486 ? 61.87409 41.41820  9.89439   1.000 54.56822  ? 365  VAL A CB  1 
ATOM   3357 C CG1 . VAL A 1 486 ? 60.82623 41.93233  10.85587  1.000 50.40483  ? 365  VAL A CG1 1 
ATOM   3358 C CG2 . VAL A 1 486 ? 62.15338 39.96459  10.18234  1.000 45.35712  ? 365  VAL A CG2 1 
ATOM   3359 N N   . PRO A 1 487 ? 59.82572 43.41691  7.82902   1.000 54.59105  ? 366  PRO A N   1 
ATOM   3360 C CA  . PRO A 1 487 ? 59.48762 44.83179  7.64270   1.000 62.70429  ? 366  PRO A CA  1 
ATOM   3361 C C   . PRO A 1 487 ? 59.65780 45.61648  8.93830   1.000 54.44242  ? 366  PRO A C   1 
ATOM   3362 O O   . PRO A 1 487 ? 59.38857 45.11783  10.03346  1.000 58.17336  ? 366  PRO A O   1 
ATOM   3363 C CB  . PRO A 1 487 ? 58.02056 44.79454  7.18506   1.000 54.47632  ? 366  PRO A CB  1 
ATOM   3364 C CG  . PRO A 1 487 ? 57.69772 43.33144  6.95740   1.000 56.98481  ? 366  PRO A CG  1 
ATOM   3365 C CD  . PRO A 1 487 ? 58.62264 42.57514  7.84804   1.000 55.50774  ? 366  PRO A CD  1 
ATOM   3366 N N   . MET A 1 488 ? 60.09028 46.86690  8.79763   1.000 57.37733  ? 367  MET A N   1 
ATOM   3367 C CA  . MET A 1 488 ? 60.48601 47.68997  9.93130   1.000 63.04083  ? 367  MET A CA  1 
ATOM   3368 C C   . MET A 1 488 ? 60.15924 49.13236  9.58243   1.000 64.46132  ? 367  MET A C   1 
ATOM   3369 O O   . MET A 1 488 ? 60.49441 49.59309  8.48773   1.000 64.00387  ? 367  MET A O   1 
ATOM   3370 C CB  . MET A 1 488 ? 61.98072 47.53091  10.24087  1.000 72.35413  ? 367  MET A CB  1 
ATOM   3371 C CG  . MET A 1 488 ? 62.43918 48.16125  11.55068  1.000 73.17724  ? 367  MET A CG  1 
ATOM   3372 S SD  . MET A 1 488 ? 61.75573 47.33412  12.99757  1.000 70.79721  ? 367  MET A SD  1 
ATOM   3373 C CE  . MET A 1 488 ? 62.50798 45.71501  12.86006  1.000 60.58692  ? 367  MET A CE  1 
ATOM   3374 N N   . GLY A 1 489 ? 59.52697 49.84383  10.51105  1.000 68.11990  ? 368  GLY A N   1 
ATOM   3375 C CA  . GLY A 1 489 ? 59.05148 51.16690  10.15860  1.000 64.01215  ? 368  GLY A CA  1 
ATOM   3376 C C   . GLY A 1 489 ? 58.01228 51.10355  9.04164   1.000 66.10618  ? 368  GLY A C   1 
ATOM   3377 O O   . GLY A 1 489 ? 57.46671 50.05437  8.70230   1.000 61.81719  ? 368  GLY A O   1 
ATOM   3378 N N   . ASP A 1 490 ? 57.74358 52.28133  8.47273   1.000 71.36642  ? 369  ASP A N   1 
ATOM   3379 C CA  . ASP A 1 490 ? 56.70748 52.38110  7.44857   1.000 84.22899  ? 369  ASP A CA  1 
ATOM   3380 C C   . ASP A 1 490 ? 57.15387 51.80895  6.10643   1.000 77.47885  ? 369  ASP A C   1 
ATOM   3381 O O   . ASP A 1 490 ? 56.31315 51.33883  5.33167   1.000 76.41284  ? 369  ASP A O   1 
ATOM   3382 C CB  . ASP A 1 490 ? 56.26912 53.83767  7.28304   1.000 91.66365  ? 369  ASP A CB  1 
ATOM   3383 C CG  . ASP A 1 490 ? 55.50736 54.36001  8.49080   1.000 94.08580  ? 369  ASP A CG  1 
ATOM   3384 O OD1 . ASP A 1 490 ? 54.66343 53.61477  9.03465   1.000 93.68551  ? 369  ASP A OD1 1 
ATOM   3385 O OD2 . ASP A 1 490 ? 55.75679 55.51413  8.89979   1.000 96.39769  ? 369  ASP A OD2 1 
ATOM   3386 N N   . LYS A 1 491 ? 58.45773 51.83045  5.80296   1.000 81.76196  ? 370  LYS A N   1 
ATOM   3387 C CA  . LYS A 1 491 ? 58.89632 51.33854  4.50144   1.000 83.58449  ? 370  LYS A CA  1 
ATOM   3388 C C   . LYS A 1 491 ? 60.20284 50.55071  4.52015   1.000 79.44384  ? 370  LYS A C   1 
ATOM   3389 O O   . LYS A 1 491 ? 60.70215 50.19851  3.44405   1.000 92.63388  ? 370  LYS A O   1 
ATOM   3390 C CB  . LYS A 1 491 ? 59.03313 52.50359  3.51284   1.000 89.04663  ? 370  LYS A CB  1 
ATOM   3391 C CG  . LYS A 1 491 ? 59.24426 53.85603  4.16978   1.000 97.39242  ? 370  LYS A CG  1 
ATOM   3392 C CD  . LYS A 1 491 ? 58.90531 54.98820  3.21439   1.000 98.07765  ? 370  LYS A CD  1 
ATOM   3393 C CE  . LYS A 1 491 ? 59.03711 56.34027  3.89277   1.000 101.02962 ? 370  LYS A CE  1 
ATOM   3394 N NZ  . LYS A 1 491 ? 58.49677 57.43594  3.04189   1.000 106.36358 ? 370  LYS A NZ  1 
ATOM   3395 N N   . GLY A 1 492 ? 60.77494 50.25226  5.68504   1.000 78.81372  ? 371  GLY A N   1 
ATOM   3396 C CA  . GLY A 1 492 ? 62.06710 49.59797  5.72196   1.000 66.49429  ? 371  GLY A CA  1 
ATOM   3397 C C   . GLY A 1 492 ? 61.99164 48.07983  5.78790   1.000 71.16525  ? 371  GLY A C   1 
ATOM   3398 O O   . GLY A 1 492 ? 60.96792 47.48845  6.11933   1.000 67.16358  ? 371  GLY A O   1 
ATOM   3399 N N   . PHE A 1 493 ? 63.13650 47.45334  5.52588   1.000 61.84166  ? 372  PHE A N   1 
ATOM   3400 C CA  . PHE A 1 493 ? 63.28964 46.00577  5.58616   1.000 52.94710  ? 372  PHE A CA  1 
ATOM   3401 C C   . PHE A 1 493 ? 64.57235 45.68568  6.33686   1.000 76.31420  ? 372  PHE A C   1 
ATOM   3402 O O   . PHE A 1 493 ? 65.64340 46.18502  5.97402   1.000 63.53153  ? 372  PHE A O   1 
ATOM   3403 C CB  . PHE A 1 493 ? 63.36892 45.38009  4.18477   1.000 59.99364  ? 372  PHE A CB  1 
ATOM   3404 C CG  . PHE A 1 493 ? 62.19052 45.67756  3.30076   1.000 71.52053  ? 372  PHE A CG  1 
ATOM   3405 C CD1 . PHE A 1 493 ? 61.04933 44.89115  3.34971   1.000 67.57975  ? 372  PHE A CD1 1 
ATOM   3406 C CD2 . PHE A 1 493 ? 62.23845 46.72485  2.39425   1.000 58.09129  ? 372  PHE A CD2 1 
ATOM   3407 C CE1 . PHE A 1 493 ? 59.96908 45.15740  2.52162   1.000 53.48482  ? 372  PHE A CE1 1 
ATOM   3408 C CE2 . PHE A 1 493 ? 61.16305 46.99651  1.56755   1.000 61.73795  ? 372  PHE A CE2 1 
ATOM   3409 C CZ  . PHE A 1 493 ? 60.02752 46.21090  1.63059   1.000 52.90756  ? 372  PHE A CZ  1 
ATOM   3410 N N   . VAL A 1 494 ? 64.47706 44.86569  7.37792   1.000 68.61361  ? 373  VAL A N   1 
ATOM   3411 C CA  . VAL A 1 494 ? 65.66545 44.35551  8.04623   1.000 58.28529  ? 373  VAL A CA  1 
ATOM   3412 C C   . VAL A 1 494 ? 66.03313 43.02328  7.41138   1.000 62.68570  ? 373  VAL A C   1 
ATOM   3413 O O   . VAL A 1 494 ? 65.18735 42.12336  7.29399   1.000 51.71505  ? 373  VAL A O   1 
ATOM   3414 C CB  . VAL A 1 494 ? 65.43484 44.20234  9.55828   1.000 51.94653  ? 373  VAL A CB  1 
ATOM   3415 C CG1 . VAL A 1 494 ? 66.61925 43.49283  10.19708  1.000 49.14914  ? 373  VAL A CG1 1 
ATOM   3416 C CG2 . VAL A 1 494 ? 65.21202 45.56287  10.20191  1.000 66.29826  ? 373  VAL A CG2 1 
ATOM   3417 N N   . ALA A 1 495 ? 67.29410 42.90797  6.99529   1.000 60.23812  ? 374  ALA A N   1 
ATOM   3418 C CA  . ALA A 1 495 ? 67.83646 41.69771  6.39233   1.000 67.21196  ? 374  ALA A CA  1 
ATOM   3419 C C   . ALA A 1 495 ? 68.43415 40.82209  7.48476   1.000 54.26447  ? 374  ALA A C   1 
ATOM   3420 O O   . ALA A 1 495 ? 69.41065 41.21650  8.12825   1.000 68.17324  ? 374  ALA A O   1 
ATOM   3421 C CB  . ALA A 1 495 ? 68.89301 42.04458  5.34422   1.000 60.96693  ? 374  ALA A CB  1 
ATOM   3422 N N   . ARG A 1 496 ? 67.87267 39.62811  7.67925   1.000 51.56214  ? 375  ARG A N   1 
ATOM   3423 C CA  . ARG A 1 496 ? 68.32291 38.68348  8.69395   1.000 49.01563  ? 375  ARG A CA  1 
ATOM   3424 C C   . ARG A 1 496 ? 68.67214 37.37240  7.99681   1.000 48.89383  ? 375  ARG A C   1 
ATOM   3425 O O   . ARG A 1 496 ? 67.86599 36.42760  7.97417   1.000 50.42614  ? 375  ARG A O   1 
ATOM   3426 C CB  . ARG A 1 496 ? 67.26089 38.48153  9.77486   1.000 47.72854  ? 375  ARG A CB  1 
ATOM   3427 C CG  . ARG A 1 496 ? 67.72438 37.63182  10.94799  1.000 49.22063  ? 375  ARG A CG  1 
ATOM   3428 C CD  . ARG A 1 496 ? 66.72696 36.53609  11.28170  1.000 57.08711  ? 375  ARG A CD  1 
ATOM   3429 N NE  . ARG A 1 496 ? 65.44897 37.07037  11.74218  1.000 53.46781  ? 375  ARG A NE  1 
ATOM   3430 C CZ  . ARG A 1 496 ? 65.22152 37.47859  12.98652  1.000 61.88486  ? 375  ARG A CZ  1 
ATOM   3431 N NH1 . ARG A 1 496 ? 66.19070 37.41838  13.89327  1.000 53.99838  ? 375  ARG A NH1 1 
ATOM   3432 N NH2 . ARG A 1 496 ? 64.02909 37.94976  13.32703  1.000 47.77663  ? 375  ARG A NH2 1 
ATOM   3433 N N   . PRO A 1 497 ? 69.82591 37.30580  7.34082   1.000 55.61736  ? 376  PRO A N   1 
ATOM   3434 C CA  . PRO A 1 497 ? 70.35093 36.00185  6.94185   1.000 51.24301  ? 376  PRO A CA  1 
ATOM   3435 C C   . PRO A 1 497 ? 70.85298 35.26813  8.17037   1.000 53.10350  ? 376  PRO A C   1 
ATOM   3436 O O   . PRO A 1 497 ? 71.27403 35.88038  9.15545   1.000 50.81099  ? 376  PRO A O   1 
ATOM   3437 C CB  . PRO A 1 497 ? 71.49839 36.36267  5.99620   1.000 48.10917  ? 376  PRO A CB  1 
ATOM   3438 C CG  . PRO A 1 497 ? 72.01221 37.63800  6.57855   1.000 45.95524  ? 376  PRO A CG  1 
ATOM   3439 C CD  . PRO A 1 497 ? 70.75118 38.39003  6.96072   1.000 64.57181  ? 376  PRO A CD  1 
ATOM   3440 N N   . TYR A 1 498 ? 70.80248 33.94440  8.11377   1.000 45.50018  ? 377  TYR A N   1 
ATOM   3441 C CA  . TYR A 1 498 ? 71.31867 33.14587  9.21909   1.000 49.99850  ? 377  TYR A CA  1 
ATOM   3442 C C   . TYR A 1 498 ? 71.50742 31.72731  8.71229   1.000 56.14351  ? 377  TYR A C   1 
ATOM   3443 O O   . TYR A 1 498 ? 71.37566 31.46091  7.51563   1.000 54.61447  ? 377  TYR A O   1 
ATOM   3444 C CB  . TYR A 1 498 ? 70.38954 33.20289  10.43734  1.000 59.89038  ? 377  TYR A CB  1 
ATOM   3445 C CG  . TYR A 1 498 ? 68.99032 32.70211  10.16932  1.000 54.27841  ? 377  TYR A CG  1 
ATOM   3446 C CD1 . TYR A 1 498 ? 68.03358 33.52937  9.59198   1.000 52.81467  ? 377  TYR A CD1 1 
ATOM   3447 C CD2 . TYR A 1 498 ? 68.62279 31.40383  10.49657  1.000 49.79328  ? 377  TYR A CD2 1 
ATOM   3448 C CE1 . TYR A 1 498 ? 66.74941 33.07713  9.34514   1.000 54.87071  ? 377  TYR A CE1 1 
ATOM   3449 C CE2 . TYR A 1 498 ? 67.33342 30.94091  10.25239  1.000 59.89097  ? 377  TYR A CE2 1 
ATOM   3450 C CZ  . TYR A 1 498 ? 66.40504 31.78480  9.67803   1.000 49.98055  ? 377  TYR A CZ  1 
ATOM   3451 O OH  . TYR A 1 498 ? 65.12972 31.33871  9.42598   1.000 54.20519  ? 377  TYR A OH  1 
ATOM   3452 N N   . GLY A 1 499 ? 71.82977 30.81276  9.61697   1.000 58.13619  ? 378  GLY A N   1 
ATOM   3453 C CA  . GLY A 1 499 ? 72.05396 29.44851  9.19371   1.000 63.13765  ? 378  GLY A CA  1 
ATOM   3454 C C   . GLY A 1 499 ? 71.10321 28.48315  9.86271   1.000 56.20174  ? 378  GLY A C   1 
ATOM   3455 O O   . GLY A 1 499 ? 70.52817 28.79468  10.90902  1.000 67.52248  ? 378  GLY A O   1 
ATOM   3456 N N   . LEU A 1 500 ? 70.93150 27.30347  9.26318   1.000 58.83607  ? 379  LEU A N   1 
ATOM   3457 C CA  . LEU A 1 500 ? 69.94304 26.35072  9.75086   1.000 62.98634  ? 379  LEU A CA  1 
ATOM   3458 C C   . LEU A 1 500 ? 70.28951 25.82206  11.13668  1.000 76.96510  ? 379  LEU A C   1 
ATOM   3459 O O   . LEU A 1 500 ? 69.39258 25.37172  11.85682  1.000 72.55368  ? 379  LEU A O   1 
ATOM   3460 C CB  . LEU A 1 500 ? 69.80352 25.19185  8.76379   1.000 61.04047  ? 379  LEU A CB  1 
ATOM   3461 C CG  . LEU A 1 500 ? 68.64359 24.21838  8.98565   1.000 72.96418  ? 379  LEU A CG  1 
ATOM   3462 C CD1 . LEU A 1 500 ? 67.29845 24.88890  8.71131   1.000 59.76994  ? 379  LEU A CD1 1 
ATOM   3463 C CD2 . LEU A 1 500 ? 68.81616 22.98766  8.11382   1.000 78.26932  ? 379  LEU A CD2 1 
ATOM   3464 N N   . ASP A 1 501 ? 71.56226 25.88188  11.53299  1.000 83.42042  ? 380  ASP A N   1 
ATOM   3465 C CA  . ASP A 1 501 ? 71.99495 25.34892  12.81538  1.000 74.74221  ? 380  ASP A CA  1 
ATOM   3466 C C   . ASP A 1 501 ? 72.53120 26.41337  13.76113  1.000 62.87016  ? 380  ASP A C   1 
ATOM   3467 O O   . ASP A 1 501 ? 72.92969 26.07443  14.88199  1.000 73.99500  ? 380  ASP A O   1 
ATOM   3468 C CB  . ASP A 1 501 ? 73.06418 24.26661  12.60630  1.000 81.73002  ? 380  ASP A CB  1 
ATOM   3469 C CG  . ASP A 1 501 ? 72.54963 23.08824  11.80251  1.000 88.04268  ? 380  ASP A CG  1 
ATOM   3470 O OD1 . ASP A 1 501 ? 71.47842 22.54862  12.15197  1.000 88.38018  ? 380  ASP A OD1 1 
ATOM   3471 O OD2 . ASP A 1 501 ? 73.21894 22.70223  10.82003  1.000 94.19518  ? 380  ASP A OD2 1 
ATOM   3472 N N   . ASP A 1 502 ? 72.57916 27.67675  13.34028  1.000 59.39375  ? 381  ASP A N   1 
ATOM   3473 C CA  . ASP A 1 502 ? 72.81742 28.77344  14.26965  1.000 58.24982  ? 381  ASP A CA  1 
ATOM   3474 C C   . ASP A 1 502 ? 71.89069 28.65153  15.47116  1.000 64.90797  ? 381  ASP A C   1 
ATOM   3475 O O   . ASP A 1 502 ? 70.67821 28.48543  15.31695  1.000 64.20780  ? 381  ASP A O   1 
ATOM   3476 C CB  . ASP A 1 502 ? 72.59181 30.11889  13.57434  1.000 62.79822  ? 381  ASP A CB  1 
ATOM   3477 C CG  . ASP A 1 502 ? 73.67503 30.45238  12.56710  1.000 70.35786  ? 381  ASP A CG  1 
ATOM   3478 O OD1 . ASP A 1 502 ? 74.61910 29.64866  12.41189  1.000 67.01934  ? 381  ASP A OD1 1 
ATOM   3479 O OD2 . ASP A 1 502 ? 73.57796 31.52111  11.92495  1.000 64.09684  ? 381  ASP A OD2 1 
ATOM   3480 N N   . VAL A 1 503 ? 72.46200 28.73882  16.67399  1.000 61.26953  ? 382  VAL A N   1 
ATOM   3481 C CA  . VAL A 1 503 ? 71.65229 28.73057  17.88865  1.000 58.44446  ? 382  VAL A CA  1 
ATOM   3482 C C   . VAL A 1 503 ? 71.50620 30.11690  18.49491  1.000 63.65062  ? 382  VAL A C   1 
ATOM   3483 O O   . VAL A 1 503 ? 70.70801 30.28838  19.43046  1.000 68.65087  ? 382  VAL A O   1 
ATOM   3484 C CB  . VAL A 1 503 ? 72.24066 27.77006  18.94569  1.000 69.63002  ? 382  VAL A CB  1 
ATOM   3485 C CG1 . VAL A 1 503 ? 72.13027 26.32768  18.47814  1.000 68.23415  ? 382  VAL A CG1 1 
ATOM   3486 C CG2 . VAL A 1 503 ? 73.69324 28.13593  19.25795  1.000 55.28913  ? 382  VAL A CG2 1 
ATOM   3487 N N   . PHE A 1 504 ? 72.23752 31.10936  17.98555  1.000 72.38122  ? 383  PHE A N   1 
ATOM   3488 C CA  . PHE A 1 504 ? 72.08453 32.51428  18.36027  1.000 61.13611  ? 383  PHE A CA  1 
ATOM   3489 C C   . PHE A 1 504 ? 72.22749 32.69010  19.87194  1.000 64.34879  ? 383  PHE A C   1 
ATOM   3490 O O   . PHE A 1 504 ? 71.31442 33.10822  20.59095  1.000 60.06368  ? 383  PHE A O   1 
ATOM   3491 C CB  . PHE A 1 504 ? 70.78793 33.10836  17.80699  1.000 59.33867  ? 383  PHE A CB  1 
ATOM   3492 C CG  . PHE A 1 504 ? 70.96783 33.71148  16.44296  1.000 59.57324  ? 383  PHE A CG  1 
ATOM   3493 C CD1 . PHE A 1 504 ? 70.85190 32.93545  15.30321  1.000 44.87597  ? 383  PHE A CD1 1 
ATOM   3494 C CD2 . PHE A 1 504 ? 71.33703 35.04267  16.30828  1.000 51.43927  ? 383  PHE A CD2 1 
ATOM   3495 C CE1 . PHE A 1 504 ? 71.04900 33.48822  14.05142  1.000 52.44604  ? 383  PHE A CE1 1 
ATOM   3496 C CE2 . PHE A 1 504 ? 71.54140 35.59875  15.06077  1.000 44.58605  ? 383  PHE A CE2 1 
ATOM   3497 C CZ  . PHE A 1 504 ? 71.39679 34.82096  13.93099  1.000 46.40655  ? 383  PHE A CZ  1 
ATOM   3498 N N   . LYS A 1 505 ? 73.42485 32.34108  20.32621  1.000 62.84399  ? 384  LYS A N   1 
ATOM   3499 C CA  . LYS A 1 505 ? 73.87452 32.42617  21.70313  1.000 72.32944  ? 384  LYS A CA  1 
ATOM   3500 C C   . LYS A 1 505 ? 75.39006 32.38414  21.65153  1.000 69.75265  ? 384  LYS A C   1 
ATOM   3501 O O   . LYS A 1 505 ? 75.96856 31.77229  20.74986  1.000 78.77893  ? 384  LYS A O   1 
ATOM   3502 C CB  . LYS A 1 505 ? 73.33258 31.27216  22.55436  1.000 66.62762  ? 384  LYS A CB  1 
ATOM   3503 C CG  . LYS A 1 505 ? 73.24130 31.55690  24.03921  1.000 72.13456  ? 384  LYS A CG  1 
ATOM   3504 C CD  . LYS A 1 505 ? 72.72310 30.33255  24.78074  1.000 91.35945  ? 384  LYS A CD  1 
ATOM   3505 C CE  . LYS A 1 505 ? 72.07099 30.70011  26.10336  1.000 103.76277 ? 384  LYS A CE  1 
ATOM   3506 N NZ  . LYS A 1 505 ? 70.59113 30.83145  25.97015  1.000 88.70053  ? 384  LYS A NZ  1 
ATOM   3507 N N   . GLY A 1 506 ? 76.03012 33.05302  22.60286  1.000 71.02303  ? 385  GLY A N   1 
ATOM   3508 C CA  . GLY A 1 506 ? 77.47761 33.02870  22.61456  1.000 65.40291  ? 385  GLY A CA  1 
ATOM   3509 C C   . GLY A 1 506 ? 78.14657 34.37935  22.47584  1.000 71.52671  ? 385  GLY A C   1 
ATOM   3510 O O   . GLY A 1 506 ? 77.61300 35.29350  21.83997  1.000 75.69258  ? 385  GLY A O   1 
ATOM   3511 N N   . ASP A 1 507 ? 79.32480 34.50497  23.07959  1.000 69.29897  ? 386  ASP A N   1 
ATOM   3512 C CA  . ASP A 1 507 ? 80.19041 35.64908  22.83757  1.000 63.78302  ? 386  ASP A CA  1 
ATOM   3513 C C   . ASP A 1 507 ? 80.71675 35.60646  21.40711  1.000 62.12870  ? 386  ASP A C   1 
ATOM   3514 O O   . ASP A 1 507 ? 80.95514 34.53085  20.85080  1.000 55.95080  ? 386  ASP A O   1 
ATOM   3515 C CB  . ASP A 1 507 ? 81.34705 35.64897  23.84079  1.000 75.63373  ? 386  ASP A CB  1 
ATOM   3516 C CG  . ASP A 1 507 ? 82.17533 36.91636  23.78390  1.000 80.72470  ? 386  ASP A CG  1 
ATOM   3517 O OD1 . ASP A 1 507 ? 83.09767 36.99084  22.94528  1.000 79.06744  ? 386  ASP A OD1 1 
ATOM   3518 O OD2 . ASP A 1 507 ? 81.90642 37.83751  24.58348  1.000 87.81743  ? 386  ASP A OD2 1 
ATOM   3519 N N   . LEU A 1 508 ? 80.86218 36.78733  20.79634  1.000 58.81119  ? 387  LEU A N   1 
ATOM   3520 C CA  . LEU A 1 508 ? 81.29031 36.86259  19.40245  1.000 74.94045  ? 387  LEU A CA  1 
ATOM   3521 C C   . LEU A 1 508 ? 82.72291 36.38589  19.19504  1.000 80.09291  ? 387  LEU A C   1 
ATOM   3522 O O   . LEU A 1 508 ? 83.06840 35.97318  18.08184  1.000 70.97901  ? 387  LEU A O   1 
ATOM   3523 C CB  . LEU A 1 508 ? 81.15457 38.29459  18.88229  1.000 73.17390  ? 387  LEU A CB  1 
ATOM   3524 C CG  . LEU A 1 508 ? 79.78168 38.95612  18.98484  1.000 80.22734  ? 387  LEU A CG  1 
ATOM   3525 C CD1 . LEU A 1 508 ? 79.85574 40.38447  18.47512  1.000 80.02846  ? 387  LEU A CD1 1 
ATOM   3526 C CD2 . LEU A 1 508 ? 78.74824 38.16277  18.20630  1.000 73.17974  ? 387  LEU A CD2 1 
ATOM   3527 N N   . ARG A 1 509 ? 83.56380 36.44311  20.22377  1.000 69.28972  ? 388  ARG A N   1 
ATOM   3528 C CA  . ARG A 1 509 ? 84.96175 36.05828  20.09545  1.000 73.88750  ? 388  ARG A CA  1 
ATOM   3529 C C   . ARG A 1 509 ? 85.18577 34.56519  20.29534  1.000 71.09005  ? 388  ARG A C   1 
ATOM   3530 O O   . ARG A 1 509 ? 86.33479 34.13879  20.43918  1.000 68.49662  ? 388  ARG A O   1 
ATOM   3531 C CB  . ARG A 1 509 ? 85.82626 36.85808  21.07358  1.000 78.43684  ? 388  ARG A CB  1 
ATOM   3532 C CG  . ARG A 1 509 ? 86.00264 38.31130  20.66629  1.000 96.36666  ? 388  ARG A CG  1 
ATOM   3533 C CD  . ARG A 1 509 ? 86.97673 39.04198  21.57368  1.000 101.89954 ? 388  ARG A CD  1 
ATOM   3534 N NE  . ARG A 1 509 ? 87.44085 40.29216  20.97672  1.000 104.07901 ? 388  ARG A NE  1 
ATOM   3535 C CZ  . ARG A 1 509 ? 86.80800 41.45677  21.08087  1.000 102.29316 ? 388  ARG A CZ  1 
ATOM   3536 N NH1 . ARG A 1 509 ? 85.66649 41.54024  21.74994  1.000 109.03682 ? 388  ARG A NH1 1 
ATOM   3537 N NH2 . ARG A 1 509 ? 87.31459 42.53949  20.50790  1.000 102.90624 ? 388  ARG A NH2 1 
ATOM   3538 N N   . ASP A 1 510 ? 84.12452 33.76704  20.31905  1.000 74.15819  ? 389  ASP A N   1 
ATOM   3539 C CA  . ASP A 1 510 ? 84.24535 32.31999  20.39326  1.000 79.20479  ? 389  ASP A CA  1 
ATOM   3540 C C   . ASP A 1 510 ? 84.00716 31.74751  19.00233  1.000 84.26653  ? 389  ASP A C   1 
ATOM   3541 O O   . ASP A 1 510 ? 83.07972 32.16281  18.30278  1.000 73.05573  ? 389  ASP A O   1 
ATOM   3542 C CB  . ASP A 1 510 ? 83.24990 31.73730  21.40014  1.000 74.07775  ? 389  ASP A CB  1 
ATOM   3543 C CG  . ASP A 1 510 ? 83.50687 30.26986  21.70373  1.000 84.76704  ? 389  ASP A CG  1 
ATOM   3544 O OD1 . ASP A 1 510 ? 84.09492 29.56118  20.85870  1.000 86.87148  ? 389  ASP A OD1 1 
ATOM   3545 O OD2 . ASP A 1 510 ? 83.12206 29.82193  22.80312  1.000 93.53214  ? 389  ASP A OD2 1 
ATOM   3546 N N   . SER A 1 511 ? 84.84670 30.78874  18.60415  1.000 86.24965  ? 390  SER A N   1 
ATOM   3547 C CA  . SER A 1 511 ? 84.73566 30.21925  17.26560  1.000 82.89529  ? 390  SER A CA  1 
ATOM   3548 C C   . SER A 1 511 ? 83.52043 29.31290  17.09936  1.000 74.37183  ? 390  SER A C   1 
ATOM   3549 O O   . SER A 1 511 ? 83.18389 28.96441  15.96232  1.000 72.28735  ? 390  SER A O   1 
ATOM   3550 C CB  . SER A 1 511 ? 86.01191 29.45006  16.91598  1.000 78.81663  ? 390  SER A CB  1 
ATOM   3551 O OG  . SER A 1 511 ? 85.93838 28.10284  17.34912  1.000 89.21704  ? 390  SER A OG  1 
ATOM   3552 N N   . LYS A 1 512 ? 82.85541 28.92764  18.18848  1.000 71.74768  ? 391  LYS A N   1 
ATOM   3553 C CA  . LYS A 1 512 ? 81.63732 28.13294  18.09163  1.000 73.48985  ? 391  LYS A CA  1 
ATOM   3554 C C   . LYS A 1 512 ? 80.38834 28.98724  17.90964  1.000 69.25528  ? 391  LYS A C   1 
ATOM   3555 O O   . LYS A 1 512 ? 79.33998 28.45658  17.52540  1.000 70.48010  ? 391  LYS A O   1 
ATOM   3556 C CB  . LYS A 1 512 ? 81.47789 27.25122  19.33582  1.000 84.78293  ? 391  LYS A CB  1 
ATOM   3557 C CG  . LYS A 1 512 ? 82.55131 26.17809  19.47917  1.000 96.22596  ? 391  LYS A CG  1 
ATOM   3558 C CD  . LYS A 1 512 ? 82.37034 25.38291  20.76487  1.000 96.83463  ? 391  LYS A CD  1 
ATOM   3559 C CE  . LYS A 1 512 ? 83.48067 24.35725  20.94975  1.000 112.38217 ? 391  LYS A CE  1 
ATOM   3560 N NZ  . LYS A 1 512 ? 84.83311 24.98262  20.96489  1.000 115.40837 ? 391  LYS A NZ  1 
ATOM   3561 N N   . THR A 1 513 ? 80.47730 30.28750  18.18027  1.000 55.25545  ? 392  THR A N   1 
ATOM   3562 C CA  . THR A 1 513 ? 79.40371 31.22753  17.88625  1.000 56.59526  ? 392  THR A CA  1 
ATOM   3563 C C   . THR A 1 513 ? 79.37830 31.51432  16.38802  1.000 66.32677  ? 392  THR A C   1 
ATOM   3564 O O   . THR A 1 513 ? 80.34197 32.06364  15.84275  1.000 64.70766  ? 392  THR A O   1 
ATOM   3565 C CB  . THR A 1 513 ? 79.60634 32.51748  18.67665  1.000 65.54902  ? 392  THR A CB  1 
ATOM   3566 O OG1 . THR A 1 513 ? 79.71943 32.21105  20.07169  1.000 74.69617  ? 392  THR A OG1 1 
ATOM   3567 C CG2 . THR A 1 513 ? 78.43158 33.46085  18.46643  1.000 69.48851  ? 392  THR A CG2 1 
ATOM   3568 N N   . THR A 1 514 ? 78.28111 31.15301  15.72352  1.000 60.06661  ? 393  THR A N   1 
ATOM   3569 C CA  . THR A 1 514 ? 78.20945 31.17078  14.27046  1.000 61.99272  ? 393  THR A CA  1 
ATOM   3570 C C   . THR A 1 514 ? 77.11400 32.10889  13.78155  1.000 58.60574  ? 393  THR A C   1 
ATOM   3571 O O   . THR A 1 514 ? 76.09116 32.30424  14.44256  1.000 72.62596  ? 393  THR A O   1 
ATOM   3572 C CB  . THR A 1 514 ? 77.94511 29.76840  13.70731  1.000 68.25531  ? 393  THR A CB  1 
ATOM   3573 O OG1 . THR A 1 514 ? 76.65139 29.31860  14.13340  1.000 56.75125  ? 393  THR A OG1 1 
ATOM   3574 C CG2 . THR A 1 514 ? 79.00527 28.78583  14.18767  1.000 51.09061  ? 393  THR A CG2 1 
ATOM   3575 N N   . LEU A 1 515 ? 77.34411 32.68037  12.60331  1.000 63.77666  ? 394  LEU A N   1 
ATOM   3576 C CA  . LEU A 1 515 ? 76.31617 33.35879  11.82480  1.000 59.16491  ? 394  LEU A CA  1 
ATOM   3577 C C   . LEU A 1 515 ? 76.36255 32.79568  10.41303  1.000 68.40670  ? 394  LEU A C   1 
ATOM   3578 O O   . LEU A 1 515 ? 77.41467 32.83052  9.76675   1.000 80.23552  ? 394  LEU A O   1 
ATOM   3579 C CB  . LEU A 1 515 ? 76.52816 34.87600  11.81624  1.000 51.44769  ? 394  LEU A CB  1 
ATOM   3580 C CG  . LEU A 1 515 ? 75.52880 35.66875  10.97243  1.000 60.59103  ? 394  LEU A CG  1 
ATOM   3581 C CD1 . LEU A 1 515 ? 74.11381 35.52799  11.54584  1.000 56.88936  ? 394  LEU A CD1 1 
ATOM   3582 C CD2 . LEU A 1 515 ? 75.93362 37.13206  10.85958  1.000 41.84787  ? 394  LEU A CD2 1 
ATOM   3583 N N   . THR A 1 516 ? 75.22622 32.27266  9.94519   1.000 60.46838  ? 395  THR A N   1 
ATOM   3584 C CA  . THR A 1 516 ? 75.14044 31.54328  8.67651   1.000 56.77122  ? 395  THR A CA  1 
ATOM   3585 C C   . THR A 1 516 ? 76.11931 30.37101  8.65433   1.000 51.54624  ? 395  THR A C   1 
ATOM   3586 O O   . THR A 1 516 ? 76.72039 30.06154  7.62466   1.000 53.81217  ? 395  THR A O   1 
ATOM   3587 C CB  . THR A 1 516 ? 75.36710 32.45687  7.46497   1.000 58.94756  ? 395  THR A CB  1 
ATOM   3588 O OG1 . THR A 1 516 ? 76.74983 32.82486  7.38481   1.000 53.70489  ? 395  THR A OG1 1 
ATOM   3589 C CG2 . THR A 1 516 ? 74.51699 33.71203  7.56124   1.000 45.07075  ? 395  THR A CG2 1 
ATOM   3590 N N   . GLY A 1 517 ? 76.27705 29.71261  9.80233   1.000 58.07717  ? 396  GLY A N   1 
ATOM   3591 C CA  . GLY A 1 517 ? 77.03832 28.48299  9.89502   1.000 49.18010  ? 396  GLY A CA  1 
ATOM   3592 C C   . GLY A 1 517 ? 78.54384 28.63331  9.87093   1.000 70.11032  ? 396  GLY A C   1 
ATOM   3593 O O   . GLY A 1 517 ? 79.24768 27.61743  9.83183   1.000 61.01475  ? 396  GLY A O   1 
ATOM   3594 N N   . ILE A 1 518 ? 79.06311 29.85703  9.88861   1.000 63.40236  ? 397  ILE A N   1 
ATOM   3595 C CA  . ILE A 1 518 ? 80.50465 30.08749  9.95332   1.000 71.69990  ? 397  ILE A CA  1 
ATOM   3596 C C   . ILE A 1 518 ? 80.80968 30.92884  11.18839  1.000 76.11939  ? 397  ILE A C   1 
ATOM   3597 O O   . ILE A 1 518 ? 79.93213 31.66977  11.65762  1.000 64.20522  ? 397  ILE A O   1 
ATOM   3598 C CB  . ILE A 1 518 ? 81.02596 30.75296  8.66810   1.000 74.59493  ? 397  ILE A CB  1 
ATOM   3599 C CG1 . ILE A 1 518 ? 80.50197 32.18227  8.54383   1.000 75.08542  ? 397  ILE A CG1 1 
ATOM   3600 C CG2 . ILE A 1 518 ? 80.64971 29.93612  7.44099   1.000 64.43222  ? 397  ILE A CG2 1 
ATOM   3601 C CD1 . ILE A 1 518 ? 81.41832 33.08340  7.75267   1.000 81.79670  ? 397  ILE A CD1 1 
ATOM   3602 N N   . PRO A 1 519 ? 82.01467 30.83174  11.75915  1.000 60.87503  ? 398  PRO A N   1 
ATOM   3603 C CA  . PRO A 1 519 ? 82.31376 31.58217  12.98698  1.000 61.01802  ? 398  PRO A CA  1 
ATOM   3604 C C   . PRO A 1 519 ? 82.14737 33.08057  12.77863  1.000 68.44094  ? 398  PRO A C   1 
ATOM   3605 O O   . PRO A 1 519 ? 82.57154 33.63243  11.76050  1.000 56.80763  ? 398  PRO A O   1 
ATOM   3606 C CB  . PRO A 1 519 ? 83.77640 31.21574  13.27630  1.000 71.47563  ? 398  PRO A CB  1 
ATOM   3607 C CG  . PRO A 1 519 ? 83.95550 29.87474  12.63790  1.000 55.29903  ? 398  PRO A CG  1 
ATOM   3608 C CD  . PRO A 1 519 ? 83.11832 29.92783  11.38526  1.000 58.64863  ? 398  PRO A CD  1 
ATOM   3609 N N   . PHE A 1 520 ? 81.49936 33.73256  13.75177  1.000 51.79927  ? 399  PHE A N   1 
ATOM   3610 C CA  . PHE A 1 520 ? 81.21947 35.16322  13.63895  1.000 63.27239  ? 399  PHE A CA  1 
ATOM   3611 C C   . PHE A 1 520 ? 82.47199 35.96106  13.28897  1.000 63.00158  ? 399  PHE A C   1 
ATOM   3612 O O   . PHE A 1 520 ? 82.44564 36.80404  12.38876  1.000 71.24238  ? 399  PHE A O   1 
ATOM   3613 C CB  . PHE A 1 520 ? 80.58791 35.69737  14.92386  1.000 58.99525  ? 399  PHE A CB  1 
ATOM   3614 C CG  . PHE A 1 520 ? 80.05405 37.09667  14.78514  1.000 59.46314  ? 399  PHE A CG  1 
ATOM   3615 C CD1 . PHE A 1 520 ? 78.82687 37.32444  14.18695  1.000 49.90079  ? 399  PHE A CD1 1 
ATOM   3616 C CD2 . PHE A 1 520 ? 80.78679 38.18374  15.23237  1.000 72.09797  ? 399  PHE A CD2 1 
ATOM   3617 C CE1 . PHE A 1 520 ? 78.33526 38.60892  14.04343  1.000 62.08209  ? 399  PHE A CE1 1 
ATOM   3618 C CE2 . PHE A 1 520 ? 80.29861 39.46988  15.09560  1.000 62.75226  ? 399  PHE A CE2 1 
ATOM   3619 C CZ  . PHE A 1 520 ? 79.07156 39.68210  14.50050  1.000 71.16838  ? 399  PHE A CZ  1 
ATOM   3620 N N   . GLY A 1 521 ? 83.56078 35.75411  14.03261  1.000 65.16705  ? 400  GLY A N   1 
ATOM   3621 C CA  . GLY A 1 521 ? 84.78402 36.49815  13.75977  1.000 68.35463  ? 400  GLY A CA  1 
ATOM   3622 C C   . GLY A 1 521 ? 85.25666 36.33591  12.32666  1.000 64.78562  ? 400  GLY A C   1 
ATOM   3623 O O   . GLY A 1 521 ? 85.67934 37.30191  11.68281  1.000 63.88840  ? 400  GLY A O   1 
ATOM   3624 N N   . GLU A 1 522 ? 85.19428 35.10746  11.81002  1.000 55.75398  ? 401  GLU A N   1 
ATOM   3625 C CA  . GLU A 1 522 ? 85.47603 34.86969  10.39827  1.000 57.35649  ? 401  GLU A CA  1 
ATOM   3626 C C   . GLU A 1 522 ? 84.51178 35.63418  9.49355   1.000 64.34193  ? 401  GLU A C   1 
ATOM   3627 O O   . GLU A 1 522 ? 84.92806 36.20457  8.47907   1.000 69.93598  ? 401  GLU A O   1 
ATOM   3628 C CB  . GLU A 1 522 ? 85.43085 33.36867  10.11969  1.000 68.60698  ? 401  GLU A CB  1 
ATOM   3629 C CG  . GLU A 1 522 ? 85.58681 32.97501  8.67179   1.000 71.35854  ? 401  GLU A CG  1 
ATOM   3630 C CD  . GLU A 1 522 ? 85.76514 31.47810  8.51487   1.000 89.16444  ? 401  GLU A CD  1 
ATOM   3631 O OE1 . GLU A 1 522 ? 85.29630 30.92194  7.49770   1.000 102.96838 ? 401  GLU A OE1 1 
ATOM   3632 O OE2 . GLU A 1 522 ? 86.37319 30.85793  9.41552   1.000 74.58307  ? 401  GLU A OE2 1 
ATOM   3633 N N   . TRP A 1 523 ? 83.21135 35.61280  9.81176   1.000 65.16218  ? 402  TRP A N   1 
ATOM   3634 C CA  . TRP A 1 523 ? 82.23863 36.36451  9.01833   1.000 62.58789  ? 402  TRP A CA  1 
ATOM   3635 C C   . TRP A 1 523 ? 82.59393 37.84623  8.98135   1.000 66.59380  ? 402  TRP A C   1 
ATOM   3636 O O   . TRP A 1 523 ? 82.40040 38.51982  7.96204   1.000 69.02390  ? 402  TRP A O   1 
ATOM   3637 C CB  . TRP A 1 523 ? 80.82820 36.15446  9.57283   1.000 61.58557  ? 402  TRP A CB  1 
ATOM   3638 C CG  . TRP A 1 523 ? 79.74023 36.79272  8.74669   1.000 60.39990  ? 402  TRP A CG  1 
ATOM   3639 C CD1 . TRP A 1 523 ? 79.00964 36.19548  7.75833   1.000 50.96981  ? 402  TRP A CD1 1 
ATOM   3640 C CD2 . TRP A 1 523 ? 79.24470 38.13562  8.85254   1.000 58.10847  ? 402  TRP A CD2 1 
ATOM   3641 N NE1 . TRP A 1 523 ? 78.10555 37.08500  7.23161   1.000 55.56728  ? 402  TRP A NE1 1 
ATOM   3642 C CE2 . TRP A 1 523 ? 78.22618 38.28168  7.88803   1.000 55.66166  ? 402  TRP A CE2 1 
ATOM   3643 C CE3 . TRP A 1 523 ? 79.56480 39.22820  9.66454   1.000 51.53212  ? 402  TRP A CE3 1 
ATOM   3644 C CZ2 . TRP A 1 523 ? 77.52750 39.47477  7.71452   1.000 54.57860  ? 402  TRP A CZ2 1 
ATOM   3645 C CZ3 . TRP A 1 523 ? 78.87116 40.41174  9.48696   1.000 58.21219  ? 402  TRP A CZ3 1 
ATOM   3646 C CH2 . TRP A 1 523 ? 77.86320 40.52562  8.52143   1.000 47.98320  ? 402  TRP A CH2 1 
ATOM   3647 N N   . MET A 1 524 ? 83.10033 38.36945  10.09704  1.000 62.90697  ? 403  MET A N   1 
ATOM   3648 C CA  . MET A 1 524 ? 83.50246 39.76787  10.16697  1.000 70.19534  ? 403  MET A CA  1 
ATOM   3649 C C   . MET A 1 524 ? 84.74888 40.02213  9.33202   1.000 70.36509  ? 403  MET A C   1 
ATOM   3650 O O   . MET A 1 524 ? 84.84800 41.04660  8.64739   1.000 69.68416  ? 403  MET A O   1 
ATOM   3651 C CB  . MET A 1 524 ? 83.76620 40.15749  11.62127  1.000 71.90785  ? 403  MET A CB  1 
ATOM   3652 C CG  . MET A 1 524 ? 82.55975 40.12389  12.53976  1.000 87.63935  ? 403  MET A CG  1 
ATOM   3653 S SD  . MET A 1 524 ? 81.84298 41.74869  12.86308  1.000 91.87080  ? 403  MET A SD  1 
ATOM   3654 C CE  . MET A 1 524 ? 81.09771 42.13936  11.29919  1.000 92.03502  ? 403  MET A CE  1 
ATOM   3655 N N   . SER A 1 525 ? 85.71291 39.10199  9.37299   1.000 56.79872  ? 404  SER A N   1 
ATOM   3656 C CA  . SER A 1 525 ? 86.99198 39.40034  8.74117   1.000 64.70817  ? 404  SER A CA  1 
ATOM   3657 C C   . SER A 1 525 ? 86.96248 39.15080  7.23716   1.000 64.28762  ? 404  SER A C   1 
ATOM   3658 O O   . SER A 1 525 ? 87.65654 39.85158  6.49447   1.000 62.66006  ? 404  SER A O   1 
ATOM   3659 C CB  . SER A 1 525 ? 88.11853 38.59850  9.40262   1.000 56.53978  ? 404  SER A CB  1 
ATOM   3660 O OG  . SER A 1 525 ? 87.93200 37.20378  9.25143   1.000 78.75315  ? 404  SER A OG  1 
ATOM   3661 N N   . LYS A 1 526 ? 86.15348 38.19653  6.76109   1.000 65.89507  ? 405  LYS A N   1 
ATOM   3662 C CA  . LYS A 1 526 ? 85.93145 38.06648  5.32050   1.000 80.28950  ? 405  LYS A CA  1 
ATOM   3663 C C   . LYS A 1 526 ? 85.40569 39.34612  4.68368   1.000 72.91587  ? 405  LYS A C   1 
ATOM   3664 O O   . LYS A 1 526 ? 85.52352 39.51221  3.46484   1.000 72.49509  ? 405  LYS A O   1 
ATOM   3665 C CB  . LYS A 1 526 ? 84.96067 36.92274  5.00955   1.000 72.96666  ? 405  LYS A CB  1 
ATOM   3666 C CG  . LYS A 1 526 ? 85.43293 35.54629  5.42927   1.000 87.41886  ? 405  LYS A CG  1 
ATOM   3667 C CD  . LYS A 1 526 ? 84.55002 34.46810  4.80777   1.000 86.15404  ? 405  LYS A CD  1 
ATOM   3668 C CE  . LYS A 1 526 ? 85.03031 33.07497  5.17754   1.000 87.12066  ? 405  LYS A CE  1 
ATOM   3669 N NZ  . LYS A 1 526 ? 84.16263 31.99891  4.62631   1.000 78.17697  ? 405  LYS A NZ  1 
ATOM   3670 N N   . ARG A 1 527 ? 84.82959 40.24819  5.47309   1.000 67.76251  ? 406  ARG A N   1 
ATOM   3671 C CA  . ARG A 1 527 ? 84.22114 41.46758  4.96346   1.000 63.64034  ? 406  ARG A CA  1 
ATOM   3672 C C   . ARG A 1 527 ? 84.98291 42.71574  5.38528   1.000 67.92205  ? 406  ARG A C   1 
ATOM   3673 O O   . ARG A 1 527 ? 84.48249 43.83193  5.20524   1.000 59.90109  ? 406  ARG A O   1 
ATOM   3674 C CB  . ARG A 1 527 ? 82.76298 41.51841  5.41718   1.000 59.40210  ? 406  ARG A CB  1 
ATOM   3675 C CG  . ARG A 1 527 ? 82.04564 40.28271  4.92714   1.000 61.02828  ? 406  ARG A CG  1 
ATOM   3676 C CD  . ARG A 1 527 ? 80.62113 40.13382  5.38975   1.000 53.94499  ? 406  ARG A CD  1 
ATOM   3677 N NE  . ARG A 1 527 ? 79.96429 39.13795  4.55196   1.000 50.53633  ? 406  ARG A NE  1 
ATOM   3678 C CZ  . ARG A 1 527 ? 80.16842 37.82810  4.65484   1.000 53.41703  ? 406  ARG A CZ  1 
ATOM   3679 N NH1 . ARG A 1 527 ? 80.97163 37.34804  5.59689   1.000 53.51919  ? 406  ARG A NH1 1 
ATOM   3680 N NH2 . ARG A 1 527 ? 79.53986 36.99297  3.83753   1.000 55.37951  ? 406  ARG A NH2 1 
ATOM   3681 N N   . GLY A 1 528 ? 86.18322 42.55259  5.93885   1.000 66.34059  ? 407  GLY A N   1 
ATOM   3682 C CA  . GLY A 1 528 ? 86.98845 43.69156  6.32385   1.000 65.45448  ? 407  GLY A CA  1 
ATOM   3683 C C   . GLY A 1 528 ? 86.45568 44.44661  7.51377   1.000 67.95294  ? 407  GLY A C   1 
ATOM   3684 O O   . GLY A 1 528 ? 86.79742 45.61679  7.70128   1.000 83.79428  ? 407  GLY A O   1 
ATOM   3685 N N   . LEU A 1 529 ? 85.62394 43.80769  8.32579   1.000 67.22740  ? 408  LEU A N   1 
ATOM   3686 C CA  . LEU A 1 529 ? 84.97742 44.45658  9.45283   1.000 76.46492  ? 408  LEU A CA  1 
ATOM   3687 C C   . LEU A 1 529 ? 85.66207 44.03096  10.74467  1.000 76.59438  ? 408  LEU A C   1 
ATOM   3688 O O   . LEU A 1 529 ? 86.19425 42.92279  10.85162  1.000 78.85850  ? 408  LEU A O   1 
ATOM   3689 C CB  . LEU A 1 529 ? 83.48527 44.11001  9.49676   1.000 61.37723  ? 408  LEU A CB  1 
ATOM   3690 C CG  . LEU A 1 529 ? 82.61601 44.65551  8.35647   1.000 68.62601  ? 408  LEU A CG  1 
ATOM   3691 C CD1 . LEU A 1 529 ? 81.18342 44.15074  8.45339   1.000 61.88155  ? 408  LEU A CD1 1 
ATOM   3692 C CD2 . LEU A 1 529 ? 82.63420 46.17152  8.33736   1.000 76.89697  ? 408  LEU A CD2 1 
ATOM   3693 N N   . SER A 1 530 ? 85.65942 44.92943  11.72062  1.000 69.59532  ? 409  SER A N   1 
ATOM   3694 C CA  . SER A 1 530 ? 86.19344 44.64628  13.04217  1.000 80.22171  ? 409  SER A CA  1 
ATOM   3695 C C   . SER A 1 530 ? 85.12075 44.91230  14.08820  1.000 78.17604  ? 409  SER A C   1 
ATOM   3696 O O   . SER A 1 530 ? 84.06664 45.48511  13.79906  1.000 75.22281  ? 409  SER A O   1 
ATOM   3697 C CB  . SER A 1 530 ? 87.44977 45.48509  13.32268  1.000 90.36875  ? 409  SER A CB  1 
ATOM   3698 O OG  . SER A 1 530 ? 87.11038 46.82195  13.65007  1.000 89.44869  ? 409  SER A OG  1 
ATOM   3699 N N   . TYR A 1 531 ? 85.39532 44.47840  15.32098  1.000 72.16919  ? 410  TYR A N   1 
ATOM   3700 C CA  . TYR A 1 531 ? 84.47930 44.75290  16.42246  1.000 81.88960  ? 410  TYR A CA  1 
ATOM   3701 C C   . TYR A 1 531 ? 84.31273 46.24369  16.69640  1.000 90.89576  ? 410  TYR A C   1 
ATOM   3702 O O   . TYR A 1 531 ? 83.41771 46.61782  17.46261  1.000 95.15096  ? 410  TYR A O   1 
ATOM   3703 C CB  . TYR A 1 531 ? 84.95289 44.03255  17.68737  1.000 85.15653  ? 410  TYR A CB  1 
ATOM   3704 C CG  . TYR A 1 531 ? 85.08572 42.53180  17.52667  1.000 99.72504  ? 410  TYR A CG  1 
ATOM   3705 C CD1 . TYR A 1 531 ? 83.96387 41.73128  17.33170  1.000 92.15141  ? 410  TYR A CD1 1 
ATOM   3706 C CD2 . TYR A 1 531 ? 86.32938 41.91533  17.56623  1.000 99.49695  ? 410  TYR A CD2 1 
ATOM   3707 C CE1 . TYR A 1 531 ? 84.07934 40.35840  17.18681  1.000 92.87397  ? 410  TYR A CE1 1 
ATOM   3708 C CE2 . TYR A 1 531 ? 86.45511 40.54393  17.42172  1.000 100.14387 ? 410  TYR A CE2 1 
ATOM   3709 C CZ  . TYR A 1 531 ? 85.32847 39.77078  17.23212  1.000 108.62957 ? 410  TYR A CZ  1 
ATOM   3710 O OH  . TYR A 1 531 ? 85.45337 38.40701  17.08643  1.000 108.62218 ? 410  TYR A OH  1 
ATOM   3711 N N   . THR A 1 532 ? 85.13719 47.09997  16.08570  1.000 81.20386  ? 411  THR A N   1 
ATOM   3712 C CA  . THR A 1 532 ? 84.92383 48.54003  16.16743  1.000 84.03461  ? 411  THR A CA  1 
ATOM   3713 C C   . THR A 1 532 ? 83.66549 48.97978  15.43205  1.000 85.33602  ? 411  THR A C   1 
ATOM   3714 O O   . THR A 1 532 ? 83.14485 50.06346  15.71659  1.000 94.34820  ? 411  THR A O   1 
ATOM   3715 C CB  . THR A 1 532 ? 86.13280 49.29593  15.60956  1.000 87.94569  ? 411  THR A CB  1 
ATOM   3716 O OG1 . THR A 1 532 ? 86.18719 49.13910  14.18515  1.000 80.55076  ? 411  THR A OG1 1 
ATOM   3717 C CG2 . THR A 1 532 ? 87.42456 48.77386  16.22819  1.000 101.09635 ? 411  THR A CG2 1 
ATOM   3718 N N   . ASP A 1 533 ? 83.17805 48.17729  14.48777  1.000 89.21211  ? 412  ASP A N   1 
ATOM   3719 C CA  . ASP A 1 533 ? 81.98628 48.50668  13.71727  1.000 90.94776  ? 412  ASP A CA  1 
ATOM   3720 C C   . ASP A 1 533 ? 80.69097 48.05246  14.38166  1.000 82.92313  ? 412  ASP A C   1 
ATOM   3721 O O   . ASP A 1 533 ? 79.61747 48.24781  13.80258  1.000 73.42781  ? 412  ASP A O   1 
ATOM   3722 C CB  . ASP A 1 533 ? 82.08293 47.89871  12.31375  1.000 84.25980  ? 412  ASP A CB  1 
ATOM   3723 C CG  . ASP A 1 533 ? 83.39829 48.22081  11.62577  1.000 95.63195  ? 412  ASP A CG  1 
ATOM   3724 O OD1 . ASP A 1 533 ? 83.70826 49.42019  11.46364  1.000 99.14171  ? 412  ASP A OD1 1 
ATOM   3725 O OD2 . ASP A 1 533 ? 84.12322 47.27609  11.24473  1.000 86.84655  ? 412  ASP A OD2 1 
ATOM   3726 N N   . LEU A 1 534 ? 80.75695 47.45122  15.56887  1.000 89.51831  ? 413  LEU A N   1 
ATOM   3727 C CA  . LEU A 1 534 ? 79.57183 46.97844  16.27983  1.000 87.79243  ? 413  LEU A CA  1 
ATOM   3728 C C   . LEU A 1 534 ? 79.38133 47.81627  17.54041  1.000 105.56977 ? 413  LEU A C   1 
ATOM   3729 O O   . LEU A 1 534 ? 80.12534 47.66094  18.51583  1.000 107.01315 ? 413  LEU A O   1 
ATOM   3730 C CB  . LEU A 1 534 ? 79.69676 45.49549  16.62408  1.000 70.80007  ? 413  LEU A CB  1 
ATOM   3731 C CG  . LEU A 1 534 ? 79.71128 44.50331  15.46033  1.000 72.42274  ? 413  LEU A CG  1 
ATOM   3732 C CD1 . LEU A 1 534 ? 79.85201 43.08006  15.97604  1.000 61.61607  ? 413  LEU A CD1 1 
ATOM   3733 C CD2 . LEU A 1 534 ? 78.45137 44.64355  14.61850  1.000 65.39037  ? 413  LEU A CD2 1 
ATOM   3734 N N   . LYS A 1 535 ? 78.38708 48.70215  17.51391  1.000 112.37742 ? 414  LYS A N   1 
ATOM   3735 C CA  . LYS A 1 535 ? 77.97072 49.42770  18.70839  1.000 119.49623 ? 414  LYS A CA  1 
ATOM   3736 C C   . LYS A 1 535 ? 77.21566 48.50038  19.65392  1.000 112.80410 ? 414  LYS A C   1 
ATOM   3737 O O   . LYS A 1 535 ? 76.20085 47.90675  19.27077  1.000 116.55897 ? 414  LYS A O   1 
ATOM   3738 C CB  . LYS A 1 535 ? 77.09614 50.62069  18.32962  1.000 119.88614 ? 414  LYS A CB  1 
ATOM   3739 C CG  . LYS A 1 535 ? 77.71418 51.56646  17.31649  1.000 129.10638 ? 414  LYS A CG  1 
ATOM   3740 C CD  . LYS A 1 535 ? 76.92656 52.86750  17.24197  1.000 133.12529 ? 414  LYS A CD  1 
ATOM   3741 C CE  . LYS A 1 535 ? 77.67433 53.93273  16.45551  1.000 141.04312 ? 414  LYS A CE  1 
ATOM   3742 N NZ  . LYS A 1 535 ? 76.85947 55.16928  16.29232  1.000 142.55183 ? 414  LYS A NZ  1 
ATOM   3743 N N   . GLY A 1 536 ? 77.70157 48.37360  20.88136  1.000 104.49914 ? 415  GLY A N   1 
ATOM   3744 C CA  . GLY A 1 536 ? 76.97269 47.66394  21.91141  1.000 99.21673  ? 415  GLY A CA  1 
ATOM   3745 C C   . GLY A 1 536 ? 77.65855 46.39941  22.39100  1.000 103.45616 ? 415  GLY A C   1 
ATOM   3746 O O   . GLY A 1 536 ? 78.85571 46.18421  22.19376  1.000 108.65623 ? 415  GLY A O   1 
ATOM   3747 N N   . ARG A 1 537 ? 76.86609 45.54819  23.04183  1.000 108.44392 ? 416  ARG A N   1 
ATOM   3748 C CA  . ARG A 1 537 ? 77.37343 44.36283  23.71598  1.000 110.31555 ? 416  ARG A CA  1 
ATOM   3749 C C   . ARG A 1 537 ? 77.82259 43.31028  22.70674  1.000 89.73838  ? 416  ARG A C   1 
ATOM   3750 O O   . ARG A 1 537 ? 77.45048 43.33453  21.53125  1.000 79.11402  ? 416  ARG A O   1 
ATOM   3751 C CB  . ARG A 1 537 ? 76.29925 43.76932  24.62935  1.000 109.68951 ? 416  ARG A CB  1 
ATOM   3752 C CG  . ARG A 1 537 ? 75.20427 44.74235  25.02886  1.000 111.81524 ? 416  ARG A CG  1 
ATOM   3753 C CD  . ARG A 1 537 ? 73.95263 44.01165  25.49521  1.000 107.78234 ? 416  ARG A CD  1 
ATOM   3754 N NE  . ARG A 1 537 ? 74.22417 42.62140  25.85129  1.000 106.55867 ? 416  ARG A NE  1 
ATOM   3755 C CZ  . ARG A 1 537 ? 73.28692 41.73131  26.16042  1.000 105.03939 ? 416  ARG A CZ  1 
ATOM   3756 N NH1 . ARG A 1 537 ? 72.00632 42.08155  26.16100  1.000 105.08854 ? 416  ARG A NH1 1 
ATOM   3757 N NH2 . ARG A 1 537 ? 73.63177 40.48970  26.47084  1.000 99.57082  ? 416  ARG A NH2 1 
ATOM   3758 N N   . THR A 1 538 ? 78.64995 42.37560  23.18740  1.000 79.65498  ? 417  THR A N   1 
ATOM   3759 C CA  . THR A 1 538 ? 79.19068 41.31976  22.34029  1.000 75.89260  ? 417  THR A CA  1 
ATOM   3760 C C   . THR A 1 538 ? 79.20058 39.96984  23.04854  1.000 75.49873  ? 417  THR A C   1 
ATOM   3761 O O   . THR A 1 538 ? 79.77466 39.01203  22.51377  1.000 78.87234  ? 417  THR A O   1 
ATOM   3762 C CB  . THR A 1 538 ? 80.62445 41.64390  21.87583  1.000 80.69149  ? 417  THR A CB  1 
ATOM   3763 O OG1 . THR A 1 538 ? 81.53224 41.52163  22.97814  1.000 79.25264  ? 417  THR A OG1 1 
ATOM   3764 C CG2 . THR A 1 538 ? 80.73083 43.05103  21.28640  1.000 70.42854  ? 417  THR A CG2 1 
ATOM   3765 N N   . ASP A 1 539 ? 78.58526 39.86223  24.22768  1.000 78.90058  ? 418  ASP A N   1 
ATOM   3766 C CA  . ASP A 1 539 ? 78.58449 38.61724  24.98538  1.000 77.20933  ? 418  ASP A CA  1 
ATOM   3767 C C   . ASP A 1 539 ? 77.55346 37.61032  24.49067  1.000 77.30849  ? 418  ASP A C   1 
ATOM   3768 O O   . ASP A 1 539 ? 77.64242 36.43313  24.85747  1.000 71.15807  ? 418  ASP A O   1 
ATOM   3769 C CB  . ASP A 1 539 ? 78.35267 38.89853  26.47406  1.000 87.14923  ? 418  ASP A CB  1 
ATOM   3770 C CG  . ASP A 1 539 ? 77.17736 39.82251  26.72064  1.000 101.26644 ? 418  ASP A CG  1 
ATOM   3771 O OD1 . ASP A 1 539 ? 77.27319 41.01578  26.36344  1.000 104.64422 ? 418  ASP A OD1 1 
ATOM   3772 O OD2 . ASP A 1 539 ? 76.15738 39.35493  27.27073  1.000 110.78483 ? 418  ASP A OD2 1 
ATOM   3773 N N   . ASP A 1 540 ? 76.58061 38.03443  23.68268  1.000 64.45883  ? 419  ASP A N   1 
ATOM   3774 C CA  . ASP A 1 540 ? 75.45829 37.16525  23.33078  1.000 67.21706  ? 419  ASP A CA  1 
ATOM   3775 C C   . ASP A 1 540 ? 74.95387 37.54822  21.94418  1.000 64.26500  ? 419  ASP A C   1 
ATOM   3776 O O   . ASP A 1 540 ? 74.34806 38.61070  21.77395  1.000 61.42918  ? 419  ASP A O   1 
ATOM   3777 C CB  . ASP A 1 540 ? 74.34919 37.27616  24.37402  1.000 70.50478  ? 419  ASP A CB  1 
ATOM   3778 C CG  . ASP A 1 540 ? 73.11012 36.48480  24.00422  1.000 73.77950  ? 419  ASP A CG  1 
ATOM   3779 O OD1 . ASP A 1 540 ? 73.18330 35.62554  23.09683  1.000 67.37635  ? 419  ASP A OD1 1 
ATOM   3780 O OD2 . ASP A 1 540 ? 72.05522 36.72801  24.62859  1.000 79.07368  ? 419  ASP A OD2 1 
ATOM   3781 N N   . LEU A 1 541 ? 75.20364 36.67251  20.96438  1.000 60.94984  ? 420  LEU A N   1 
ATOM   3782 C CA  . LEU A 1 541 ? 74.85770 36.94303  19.57043  1.000 61.95422  ? 420  LEU A CA  1 
ATOM   3783 C C   . LEU A 1 541 ? 73.40265 37.37289  19.38881  1.000 62.90690  ? 420  LEU A C   1 
ATOM   3784 O O   . LEU A 1 541 ? 73.09529 38.15359  18.48016  1.000 59.68534  ? 420  LEU A O   1 
ATOM   3785 C CB  . LEU A 1 541 ? 75.15408 35.70078  18.72462  1.000 49.72601  ? 420  LEU A CB  1 
ATOM   3786 C CG  . LEU A 1 541 ? 74.78761 35.74468  17.23935  1.000 53.05305  ? 420  LEU A CG  1 
ATOM   3787 C CD1 . LEU A 1 541 ? 75.48715 36.90169  16.54470  1.000 50.05389  ? 420  LEU A CD1 1 
ATOM   3788 C CD2 . LEU A 1 541 ? 75.12477 34.42221  16.56788  1.000 45.03177  ? 420  LEU A CD2 1 
ATOM   3789 N N   . GLN A 1 542 ? 72.49741 36.89301  20.24340  1.000 56.78394  ? 421  GLN A N   1 
ATOM   3790 C CA  . GLN A 1 542 ? 71.09380 37.27548  20.12803  1.000 57.10577  ? 421  GLN A CA  1 
ATOM   3791 C C   . GLN A 1 542 ? 70.87844 38.76427  20.39006  1.000 72.55958  ? 421  GLN A C   1 
ATOM   3792 O O   . GLN A 1 542 ? 69.87089 39.32259  19.93882  1.000 60.35229  ? 421  GLN A O   1 
ATOM   3793 C CB  . GLN A 1 542 ? 70.25494 36.41755  21.08509  1.000 50.52446  ? 421  GLN A CB  1 
ATOM   3794 C CG  . GLN A 1 542 ? 68.78400 36.80937  21.24779  1.000 58.81088  ? 421  GLN A CG  1 
ATOM   3795 C CD  . GLN A 1 542 ? 67.89229 36.37130  20.08740  1.000 69.57588  ? 421  GLN A CD  1 
ATOM   3796 O OE1 . GLN A 1 542 ? 68.30144 35.59147  19.22239  1.000 50.46312  ? 421  GLN A OE1 1 
ATOM   3797 N NE2 . GLN A 1 542 ? 66.65783 36.86872  20.07622  1.000 54.13381  ? 421  GLN A NE2 1 
ATOM   3798 N N   . ALA A 1 543 ? 71.82017 39.42913  21.06248  1.000 67.04642  ? 422  ALA A N   1 
ATOM   3799 C CA  . ALA A 1 543 ? 71.71880 40.85511  21.34788  1.000 63.53445  ? 422  ALA A CA  1 
ATOM   3800 C C   . ALA A 1 543 ? 72.70691 41.69369  20.54489  1.000 61.39348  ? 422  ALA A C   1 
ATOM   3801 O O   . ALA A 1 543 ? 72.79877 42.90602  20.76663  1.000 62.08070  ? 422  ALA A O   1 
ATOM   3802 C CB  . ALA A 1 543 ? 71.91759 41.10663  22.84448  1.000 57.79907  ? 422  ALA A CB  1 
ATOM   3803 N N   . VAL A 1 544 ? 73.43157 41.08889  19.61010  1.000 56.50573  ? 423  VAL A N   1 
ATOM   3804 C CA  . VAL A 1 544 ? 74.42617 41.79764  18.81318  1.000 53.93355  ? 423  VAL A CA  1 
ATOM   3805 C C   . VAL A 1 544 ? 73.74784 42.38295  17.57948  1.000 57.75628  ? 423  VAL A C   1 
ATOM   3806 O O   . VAL A 1 544 ? 73.18822 41.64694  16.75973  1.000 63.32191  ? 423  VAL A O   1 
ATOM   3807 C CB  . VAL A 1 544 ? 75.58780 40.87363  18.42352  1.000 60.92326  ? 423  VAL A CB  1 
ATOM   3808 C CG1 . VAL A 1 544 ? 76.49382 41.56430  17.42204  1.000 59.63522  ? 423  VAL A CG1 1 
ATOM   3809 C CG2 . VAL A 1 544 ? 76.36584 40.46455  19.65914  1.000 59.55192  ? 423  VAL A CG2 1 
ATOM   3810 N N   . SER A 1 545 ? 73.76228 43.71073  17.46679  1.000 62.01058  ? 424  SER A N   1 
ATOM   3811 C CA  . SER A 1 545 ? 73.14754 44.39318  16.33426  1.000 61.64998  ? 424  SER A CA  1 
ATOM   3812 C C   . SER A 1 545 ? 73.93402 44.18352  15.04518  1.000 68.71854  ? 424  SER A C   1 
ATOM   3813 O O   . SER A 1 545 ? 74.82230 44.97983  14.72791  1.000 68.24999  ? 424  SER A O   1 
ATOM   3814 C CB  . SER A 1 545 ? 73.03131 45.89208  16.62195  1.000 61.54775  ? 424  SER A CB  1 
ATOM   3815 O OG  . SER A 1 545 ? 72.13985 46.14621  17.69243  1.000 70.36141  ? 424  SER A OG  1 
ATOM   3816 N N   . VAL A 1 546 ? 73.61374 43.13673  14.28655  1.000 65.75204  ? 425  VAL A N   1 
ATOM   3817 C CA  . VAL A 1 546 ? 74.31355 42.85960  13.03862  1.000 60.54596  ? 425  VAL A CA  1 
ATOM   3818 C C   . VAL A 1 546 ? 73.44499 43.09920  11.81720  1.000 65.33964  ? 425  VAL A C   1 
ATOM   3819 O O   . VAL A 1 546 ? 73.99126 43.27185  10.71613  1.000 67.84589  ? 425  VAL A O   1 
ATOM   3820 C CB  . VAL A 1 546 ? 74.87108 41.42193  12.99210  1.000 70.44404  ? 425  VAL A CB  1 
ATOM   3821 C CG1 . VAL A 1 546 ? 76.16823 41.39114  12.19147  1.000 55.36815  ? 425  VAL A CG1 1 
ATOM   3822 C CG2 . VAL A 1 546 ? 75.05927 40.86112  14.37481  1.000 91.80715  ? 425  VAL A CG2 1 
ATOM   3823 N N   . PHE A 1 547 ? 72.13808 43.11555  11.96146  1.000 69.83636  ? 426  PHE A N   1 
ATOM   3824 C CA  . PHE A 1 547 ? 71.35561 43.01842  10.74360  1.000 53.36707  ? 426  PHE A CA  1 
ATOM   3825 C C   . PHE A 1 547 ? 70.88066 44.39180  10.31727  1.000 55.77995  ? 426  PHE A C   1 
ATOM   3826 O O   . PHE A 1 547 ? 70.33270 45.13768  11.14046  1.000 62.01250  ? 426  PHE A O   1 
ATOM   3827 C CB  . PHE A 1 547 ? 70.16489 42.09489  10.95248  1.000 44.87345  ? 426  PHE A CB  1 
ATOM   3828 C CG  . PHE A 1 547 ? 70.53833 40.75122  11.50301  1.000 43.39542  ? 426  PHE A CG  1 
ATOM   3829 C CD1 . PHE A 1 547 ? 71.06095 39.76897  10.67575  1.000 40.98868  ? 426  PHE A CD1 1 
ATOM   3830 C CD2 . PHE A 1 547 ? 70.34286 40.46013  12.84417  1.000 47.22531  ? 426  PHE A CD2 1 
ATOM   3831 C CE1 . PHE A 1 547 ? 71.40304 38.52374  11.18249  1.000 47.49285  ? 426  PHE A CE1 1 
ATOM   3832 C CE2 . PHE A 1 547 ? 70.67559 39.21903  13.35623  1.000 50.19444  ? 426  PHE A CE2 1 
ATOM   3833 C CZ  . PHE A 1 547 ? 71.20959 38.24872  12.52421  1.000 49.57556  ? 426  PHE A CZ  1 
ATOM   3834 N N   . PRO A 1 548 ? 71.07358 44.75518  9.05375   1.000 63.64554  ? 427  PRO A N   1 
ATOM   3835 C CA  . PRO A 1 548 ? 70.84720 46.13731  8.63420   1.000 61.11922  ? 427  PRO A CA  1 
ATOM   3836 C C   . PRO A 1 548 ? 69.41679 46.36865  8.18236   1.000 53.67018  ? 427  PRO A C   1 
ATOM   3837 O O   . PRO A 1 548 ? 68.75507 45.49361  7.62214   1.000 56.33253  ? 427  PRO A O   1 
ATOM   3838 C CB  . PRO A 1 548 ? 71.82154 46.28961  7.45785   1.000 49.94492  ? 427  PRO A CB  1 
ATOM   3839 C CG  . PRO A 1 548 ? 71.78608 44.93617  6.82971   1.000 55.55837  ? 427  PRO A CG  1 
ATOM   3840 C CD  . PRO A 1 548 ? 71.75648 43.97571  8.00379   1.000 52.84064  ? 427  PRO A CD  1 
ATOM   3841 N N   . MET A 1 549 ? 68.94481 47.58044  8.44698   1.000 59.29815  ? 428  MET A N   1 
ATOM   3842 C CA  . MET A 1 549 ? 67.67942 48.06204  7.91685   1.000 62.10310  ? 428  MET A CA  1 
ATOM   3843 C C   . MET A 1 549 ? 67.94090 48.91035  6.68266   1.000 69.78476  ? 428  MET A C   1 
ATOM   3844 O O   . MET A 1 549 ? 68.75589 49.83886  6.71976   1.000 69.39658  ? 428  MET A O   1 
ATOM   3845 C CB  . MET A 1 549 ? 66.91653 48.87872  8.95877   1.000 72.68661  ? 428  MET A CB  1 
ATOM   3846 C CG  . MET A 1 549 ? 65.49045 49.20300  8.54791   1.000 71.68935  ? 428  MET A CG  1 
ATOM   3847 S SD  . MET A 1 549 ? 64.63238 50.23542  9.74625   1.000 75.01611  ? 428  MET A SD  1 
ATOM   3848 C CE  . MET A 1 549 ? 65.65192 51.70802  9.71665   1.000 90.87734  ? 428  MET A CE  1 
ATOM   3849 N N   . VAL A 1 550 ? 67.24299 48.59167  5.59519   1.000 66.13092  ? 429  VAL A N   1 
ATOM   3850 C CA  . VAL A 1 550 ? 67.40697 49.27725  4.32337   1.000 57.51081  ? 429  VAL A CA  1 
ATOM   3851 C C   . VAL A 1 550 ? 66.02338 49.69166  3.84593   1.000 65.08150  ? 429  VAL A C   1 
ATOM   3852 O O   . VAL A 1 550 ? 65.00219 49.16794  4.29759   1.000 71.03962  ? 429  VAL A O   1 
ATOM   3853 C CB  . VAL A 1 550 ? 68.11525 48.40287  3.26664   1.000 65.03149  ? 429  VAL A CB  1 
ATOM   3854 C CG1 . VAL A 1 550 ? 69.37113 47.77999  3.84761   1.000 56.06202  ? 429  VAL A CG1 1 
ATOM   3855 C CG2 . VAL A 1 550 ? 67.18235 47.32405  2.77080   1.000 56.00848  ? 429  VAL A CG2 1 
ATOM   3856 N N   . ASN A 1 551 ? 65.99396 50.64801  2.92056   1.000 70.17425  ? 430  ASN A N   1 
ATOM   3857 C CA  . ASN A 1 551 ? 64.73499 51.25049  2.50618   1.000 85.24955  ? 430  ASN A CA  1 
ATOM   3858 C C   . ASN A 1 551 ? 64.34386 50.91207  1.07214   1.000 79.29791  ? 430  ASN A C   1 
ATOM   3859 O O   . ASN A 1 551 ? 63.33865 51.43324  0.57926   1.000 87.60411  ? 430  ASN A O   1 
ATOM   3860 C CB  . ASN A 1 551 ? 64.80112 52.76834  2.69589   1.000 98.43822  ? 430  ASN A CB  1 
ATOM   3861 C CG  . ASN A 1 551 ? 64.78356 53.17158  4.16036   1.000 109.00381 ? 430  ASN A CG  1 
ATOM   3862 O OD1 . ASN A 1 551 ? 65.83409 53.35066  4.78185   1.000 116.43231 ? 430  ASN A OD1 1 
ATOM   3863 N ND2 . ASN A 1 551 ? 63.58617 53.30691  4.72189   1.000 95.12587  ? 430  ASN A ND2 1 
ATOM   3864 N N   . SER A 1 552 ? 65.09587 50.05159  0.39023   1.000 79.87010  ? 431  SER A N   1 
ATOM   3865 C CA  . SER A 1 552 ? 64.72662 49.64420  -0.95683  1.000 78.58661  ? 431  SER A CA  1 
ATOM   3866 C C   . SER A 1 552 ? 65.02327 48.16427  -1.14676  1.000 79.82717  ? 431  SER A C   1 
ATOM   3867 O O   . SER A 1 552 ? 65.89970 47.59846  -0.48660  1.000 79.83971  ? 431  SER A O   1 
ATOM   3868 C CB  . SER A 1 552 ? 65.46223 50.46795  -2.02409  1.000 80.50221  ? 431  SER A CB  1 
ATOM   3869 O OG  . SER A 1 552 ? 66.85035 50.19298  -2.02536  1.000 73.74851  ? 431  SER A OG  1 
ATOM   3870 N N   . VAL A 1 553 ? 64.28896 47.54803  -2.07622  1.000 70.06310  ? 432  VAL A N   1 
ATOM   3871 C CA  . VAL A 1 553 ? 64.52054 46.14578  -2.40539  1.000 64.34135  ? 432  VAL A CA  1 
ATOM   3872 C C   . VAL A 1 553 ? 65.85042 45.97534  -3.13194  1.000 61.89112  ? 432  VAL A C   1 
ATOM   3873 O O   . VAL A 1 553 ? 66.50251 44.92720  -3.01841  1.000 66.99480  ? 432  VAL A O   1 
ATOM   3874 C CB  . VAL A 1 553 ? 63.33307 45.61556  -3.23539  1.000 63.92776  ? 432  VAL A CB  1 
ATOM   3875 C CG1 . VAL A 1 553 ? 63.63481 44.24517  -3.81828  1.000 67.09390  ? 432  VAL A CG1 1 
ATOM   3876 C CG2 . VAL A 1 553 ? 62.07484 45.56504  -2.37981  1.000 55.10613  ? 432  VAL A CG2 1 
ATOM   3877 N N   . GLU A 1 554 ? 66.29957 47.01392  -3.84043  1.000 63.62877  ? 433  GLU A N   1 
ATOM   3878 C CA  . GLU A 1 554 ? 67.60888 46.98295  -4.48464  1.000 77.88412  ? 433  GLU A CA  1 
ATOM   3879 C C   . GLU A 1 554 ? 68.71639 46.86673  -3.44573  1.000 65.76971  ? 433  GLU A C   1 
ATOM   3880 O O   . GLU A 1 554 ? 69.51863 45.92562  -3.47474  1.000 61.63514  ? 433  GLU A O   1 
ATOM   3881 C CB  . GLU A 1 554 ? 67.81076 48.23213  -5.34838  1.000 85.05834  ? 433  GLU A CB  1 
ATOM   3882 C CG  . GLU A 1 554 ? 66.89503 48.34359  -6.56601  1.000 108.54503 ? 433  GLU A CG  1 
ATOM   3883 C CD  . GLU A 1 554 ? 65.44027 48.58708  -6.20163  1.000 122.47740 ? 433  GLU A CD  1 
ATOM   3884 O OE1 . GLU A 1 554 ? 64.64142 47.62647  -6.24510  1.000 122.40028 ? 433  GLU A OE1 1 
ATOM   3885 O OE2 . GLU A 1 554 ? 65.09703 49.74097  -5.86741  1.000 124.66002 ? 433  GLU A OE2 1 
ATOM   3886 N N   . GLU A 1 555 ? 68.79604 47.84994  -2.54361  1.000 63.80831  ? 434  GLU A N   1 
ATOM   3887 C CA  . GLU A 1 555 ? 69.73913 47.78132  -1.43270  1.000 70.23959  ? 434  GLU A CA  1 
ATOM   3888 C C   . GLU A 1 555 ? 69.56398 46.50603  -0.62106  1.000 61.41816  ? 434  GLU A C   1 
ATOM   3889 O O   . GLU A 1 555 ? 70.54692 45.93055  -0.14148  1.000 58.33985  ? 434  GLU A O   1 
ATOM   3890 C CB  . GLU A 1 555 ? 69.58367 49.00612  -0.53070  1.000 66.14447  ? 434  GLU A CB  1 
ATOM   3891 C CG  . GLU A 1 555 ? 69.83733 50.33036  -1.22508  1.000 68.69222  ? 434  GLU A CG  1 
ATOM   3892 C CD  . GLU A 1 555 ? 69.85820 51.49273  -0.25504  1.000 80.49234  ? 434  GLU A CD  1 
ATOM   3893 O OE1 . GLU A 1 555 ? 69.54542 51.27920  0.93596   1.000 84.55953  ? 434  GLU A OE1 1 
ATOM   3894 O OE2 . GLU A 1 555 ? 70.18937 52.61821  -0.68368  1.000 97.83628  ? 434  GLU A OE2 1 
ATOM   3895 N N   . LEU A 1 556 ? 68.31878 46.06009  -0.43632  1.000 55.78111  ? 435  LEU A N   1 
ATOM   3896 C CA  . LEU A 1 556 ? 68.08573 44.83556  0.32338   1.000 58.81545  ? 435  LEU A CA  1 
ATOM   3897 C C   . LEU A 1 556 ? 68.78796 43.64678  -0.32172  1.000 50.29384  ? 435  LEU A C   1 
ATOM   3898 O O   . LEU A 1 556 ? 69.46426 42.86825  0.36278   1.000 58.07923  ? 435  LEU A O   1 
ATOM   3899 C CB  . LEU A 1 556 ? 66.58428 44.57566  0.45354   1.000 52.39323  ? 435  LEU A CB  1 
ATOM   3900 C CG  . LEU A 1 556 ? 66.15672 43.27779  1.14452   1.000 50.55468  ? 435  LEU A CG  1 
ATOM   3901 C CD1 . LEU A 1 556 ? 66.87034 43.09361  2.47615   1.000 42.27702  ? 435  LEU A CD1 1 
ATOM   3902 C CD2 . LEU A 1 556 ? 64.64453 43.23943  1.33157   1.000 44.68987  ? 435  LEU A CD2 1 
ATOM   3903 N N   . GLY A 1 557 ? 68.68094 43.51865  -1.64681  1.000 54.10498  ? 436  GLY A N   1 
ATOM   3904 C CA  . GLY A 1 557 ? 69.34938 42.41904  -2.32530  1.000 50.95699  ? 436  GLY A CA  1 
ATOM   3905 C C   . GLY A 1 557 ? 70.85609 42.58162  -2.35000  1.000 62.77146  ? 436  GLY A C   1 
ATOM   3906 O O   . GLY A 1 557 ? 71.59870 41.60791  -2.18299  1.000 49.28482  ? 436  GLY A O   1 
ATOM   3907 N N   . LEU A 1 558 ? 71.32899 43.81368  -2.54658  1.000 53.48333  ? 437  LEU A N   1 
ATOM   3908 C CA  . LEU A 1 558 ? 72.76689 44.05823  -2.53822  1.000 64.80077  ? 437  LEU A CA  1 
ATOM   3909 C C   . LEU A 1 558 ? 73.37238 43.65556  -1.19669  1.000 72.21076  ? 437  LEU A C   1 
ATOM   3910 O O   . LEU A 1 558 ? 74.36970 42.92147  -1.13954  1.000 56.07324  ? 437  LEU A O   1 
ATOM   3911 C CB  . LEU A 1 558 ? 73.04157 45.53257  -2.83981  1.000 61.08637  ? 437  LEU A CB  1 
ATOM   3912 C CG  . LEU A 1 558 ? 72.78935 45.99830  -4.27614  1.000 76.22448  ? 437  LEU A CG  1 
ATOM   3913 C CD1 . LEU A 1 558 ? 72.81804 47.51826  -4.35448  1.000 76.15761  ? 437  LEU A CD1 1 
ATOM   3914 C CD2 . LEU A 1 558 ? 73.80578 45.39146  -5.23742  1.000 63.38279  ? 437  LEU A CD2 1 
ATOM   3915 N N   . VAL A 1 559 ? 72.74841 44.09019  -0.09919  1.000 64.84988  ? 438  VAL A N   1 
ATOM   3916 C CA  . VAL A 1 559 ? 73.30155 43.80307  1.21664   1.000 66.57217  ? 438  VAL A CA  1 
ATOM   3917 C C   . VAL A 1 559 ? 73.12912 42.33055  1.56431   1.000 66.09816  ? 438  VAL A C   1 
ATOM   3918 O O   . VAL A 1 559 ? 73.99268 41.74780  2.22842   1.000 59.91052  ? 438  VAL A O   1 
ATOM   3919 C CB  . VAL A 1 559 ? 72.69271 44.73634  2.28338   1.000 57.66167  ? 438  VAL A CB  1 
ATOM   3920 C CG1 . VAL A 1 559 ? 71.35834 44.21177  2.80433   1.000 49.24758  ? 438  VAL A CG1 1 
ATOM   3921 C CG2 . VAL A 1 559 ? 73.68286 44.93926  3.42609   1.000 44.63591  ? 438  VAL A CG2 1 
ATOM   3922 N N   . LEU A 1 560 ? 72.04188 41.69040  1.11616   1.000 59.98059  ? 439  LEU A N   1 
ATOM   3923 C CA  . LEU A 1 560 ? 71.89983 40.26262  1.37925   1.000 60.47252  ? 439  LEU A CA  1 
ATOM   3924 C C   . LEU A 1 560 ? 72.97738 39.46819  0.65438   1.000 50.87059  ? 439  LEU A C   1 
ATOM   3925 O O   . LEU A 1 560 ? 73.57491 38.55237  1.23151   1.000 58.41806  ? 439  LEU A O   1 
ATOM   3926 C CB  . LEU A 1 560 ? 70.50532 39.78783  0.98138   1.000 43.71759  ? 439  LEU A CB  1 
ATOM   3927 C CG  . LEU A 1 560 ? 69.46946 39.81282  2.10517   1.000 56.75422  ? 439  LEU A CG  1 
ATOM   3928 C CD1 . LEU A 1 560 ? 68.08283 39.51731  1.56666   1.000 52.31884  ? 439  LEU A CD1 1 
ATOM   3929 C CD2 . LEU A 1 560 ? 69.84438 38.81785  3.20222   1.000 45.98168  ? 439  LEU A CD2 1 
ATOM   3930 N N   . ARG A 1 561 ? 73.22744 39.79475  -0.61451  1.000 53.99208  ? 440  ARG A N   1 
ATOM   3931 C CA  . ARG A 1 561 ? 74.32043 39.16459  -1.34245  1.000 64.28012  ? 440  ARG A CA  1 
ATOM   3932 C C   . ARG A 1 561 ? 75.63083 39.35019  -0.59301  1.000 67.64033  ? 440  ARG A C   1 
ATOM   3933 O O   . ARG A 1 561 ? 76.40044 38.39982  -0.40961  1.000 60.02616  ? 440  ARG A O   1 
ATOM   3934 C CB  . ARG A 1 561 ? 74.41992 39.75863  -2.74625  1.000 55.85110  ? 440  ARG A CB  1 
ATOM   3935 C CG  . ARG A 1 561 ? 73.31116 39.35325  -3.69760  1.000 66.84074  ? 440  ARG A CG  1 
ATOM   3936 C CD  . ARG A 1 561 ? 73.27141 40.28489  -4.89848  1.000 61.06165  ? 440  ARG A CD  1 
ATOM   3937 N NE  . ARG A 1 561 ? 74.47985 40.18543  -5.71132  1.000 73.94748  ? 440  ARG A NE  1 
ATOM   3938 C CZ  . ARG A 1 561 ? 74.85846 41.10113  -6.59762  1.000 67.38473  ? 440  ARG A CZ  1 
ATOM   3939 N NH1 . ARG A 1 561 ? 75.96758 40.92558  -7.30326  1.000 61.80493  ? 440  ARG A NH1 1 
ATOM   3940 N NH2 . ARG A 1 561 ? 74.12144 42.18798  -6.78701  1.000 72.56957  ? 440  ARG A NH2 1 
ATOM   3941 N N   . TRP A 1 562 ? 75.89685 40.58355  -0.15342  1.000 67.65277  ? 441  TRP A N   1 
ATOM   3942 C CA  . TRP A 1 562 ? 77.12751 40.87399  0.57234   1.000 60.63468  ? 441  TRP A CA  1 
ATOM   3943 C C   . TRP A 1 562 ? 77.24007 40.08008  1.87001   1.000 68.45719  ? 441  TRP A C   1 
ATOM   3944 O O   . TRP A 1 562 ? 78.34838 39.68829  2.25786   1.000 58.73930  ? 441  TRP A O   1 
ATOM   3945 C CB  . TRP A 1 562 ? 77.21210 42.37059  0.84993   1.000 62.51914  ? 441  TRP A CB  1 
ATOM   3946 C CG  . TRP A 1 562 ? 78.37222 42.76028  1.69065   1.000 76.66236  ? 441  TRP A CG  1 
ATOM   3947 C CD1 . TRP A 1 562 ? 79.66928 42.90054  1.29086   1.000 60.73414  ? 441  TRP A CD1 1 
ATOM   3948 C CD2 . TRP A 1 562 ? 78.34457 43.06864  3.08643   1.000 62.53801  ? 441  TRP A CD2 1 
ATOM   3949 N NE1 . TRP A 1 562 ? 80.45045 43.27829  2.35355   1.000 64.74574  ? 441  TRP A NE1 1 
ATOM   3950 C CE2 . TRP A 1 562 ? 79.66084 43.38843  3.46865   1.000 68.85105  ? 441  TRP A CE2 1 
ATOM   3951 C CE3 . TRP A 1 562 ? 77.33362 43.10524  4.05009   1.000 57.02991  ? 441  TRP A CE3 1 
ATOM   3952 C CZ2 . TRP A 1 562 ? 79.99308 43.74001  4.77578   1.000 74.83060  ? 441  TRP A CZ2 1 
ATOM   3953 C CZ3 . TRP A 1 562 ? 77.66413 43.45227  5.34480   1.000 66.98976  ? 441  TRP A CZ3 1 
ATOM   3954 C CH2 . TRP A 1 562 ? 78.98177 43.76726  5.69680   1.000 62.98132  ? 441  TRP A CH2 1 
ATOM   3955 N N   . MET A 1 563 ? 76.11802 39.82169  2.54990   1.000 52.21403  ? 442  MET A N   1 
ATOM   3956 C CA  . MET A 1 563 ? 76.16579 39.06821  3.79809   1.000 53.22793  ? 442  MET A CA  1 
ATOM   3957 C C   . MET A 1 563 ? 76.25151 37.56478  3.57653   1.000 52.30226  ? 442  MET A C   1 
ATOM   3958 O O   . MET A 1 563 ? 76.55562 36.83309  4.52469   1.000 54.25500  ? 442  MET A O   1 
ATOM   3959 C CB  . MET A 1 563 ? 74.94324 39.38097  4.67258   1.000 54.38427  ? 442  MET A CB  1 
ATOM   3960 C CG  . MET A 1 563 ? 74.77838 40.84846  5.04956   1.000 61.62426  ? 442  MET A CG  1 
ATOM   3961 S SD  . MET A 1 563 ? 73.27634 41.19529  5.99809   1.000 59.56934  ? 442  MET A SD  1 
ATOM   3962 C CE  . MET A 1 563 ? 73.73471 40.57528  7.61589   1.000 53.62923  ? 442  MET A CE  1 
ATOM   3963 N N   . LEU A 1 564 ? 76.00206 37.08857  2.35733   1.000 48.59409  ? 443  LEU A N   1 
ATOM   3964 C CA  . LEU A 1 564 ? 76.17117 35.67399  2.04334   1.000 57.41232  ? 443  LEU A CA  1 
ATOM   3965 C C   . LEU A 1 564 ? 77.42619 35.42515  1.20508   1.000 64.76923  ? 443  LEU A C   1 
ATOM   3966 O O   . LEU A 1 564 ? 78.54647 35.58028  1.70201   1.000 64.22566  ? 443  LEU A O   1 
ATOM   3967 C CB  . LEU A 1 564 ? 74.92178 35.12991  1.34378   1.000 51.47449  ? 443  LEU A CB  1 
ATOM   3968 C CG  . LEU A 1 564 ? 73.60842 35.37940  2.09657   1.000 59.48501  ? 443  LEU A CG  1 
ATOM   3969 C CD1 . LEU A 1 564 ? 72.42069 34.77554  1.35709   1.000 52.11879  ? 443  LEU A CD1 1 
ATOM   3970 C CD2 . LEU A 1 564 ? 73.68575 34.84448  3.52049   1.000 52.64777  ? 443  LEU A CD2 1 
ATOM   3971 N N   . SER A 1 565 ? 77.25613 35.04217  -0.06203  1.000 60.39257  ? 444  SER A N   1 
ATOM   3972 C CA  . SER A 1 565 ? 78.35646 34.50945  -0.85820  1.000 62.15746  ? 444  SER A CA  1 
ATOM   3973 C C   . SER A 1 565 ? 79.21288 35.56437  -1.55097  1.000 62.48838  ? 444  SER A C   1 
ATOM   3974 O O   . SER A 1 565 ? 80.23973 35.20331  -2.13328  1.000 84.24585  ? 444  SER A O   1 
ATOM   3975 C CB  . SER A 1 565 ? 77.82412 33.53890  -1.91914  1.000 69.83948  ? 444  SER A CB  1 
ATOM   3976 O OG  . SER A 1 565 ? 77.07287 32.49212  -1.33201  1.000 85.67361  ? 444  SER A OG  1 
ATOM   3977 N N   . GLU A 1 566 ? 78.84063 36.84556  -1.52238  1.000 58.84913  ? 445  GLU A N   1 
ATOM   3978 C CA  . GLU A 1 566 ? 79.64140 37.90350  -2.14162  1.000 50.47538  ? 445  GLU A CA  1 
ATOM   3979 C C   . GLU A 1 566 ? 80.12285 38.92420  -1.10945  1.000 60.24742  ? 445  GLU A C   1 
ATOM   3980 O O   . GLU A 1 566 ? 79.66074 40.07315  -1.10385  1.000 64.23904  ? 445  GLU A O   1 
ATOM   3981 C CB  . GLU A 1 566 ? 78.85125 38.60077  -3.24814  1.000 53.33982  ? 445  GLU A CB  1 
ATOM   3982 C CG  . GLU A 1 566 ? 78.34563 37.66623  -4.34476  1.000 50.82122  ? 445  GLU A CG  1 
ATOM   3983 C CD  . GLU A 1 566 ? 77.43280 38.37088  -5.33431  1.000 73.38207  ? 445  GLU A CD  1 
ATOM   3984 O OE1 . GLU A 1 566 ? 77.89431 39.32787  -5.99356  1.000 69.48363  ? 445  GLU A OE1 1 
ATOM   3985 O OE2 . GLU A 1 566 ? 76.24911 37.97181  -5.44529  1.000 72.06309  ? 445  GLU A OE2 1 
ATOM   3986 N N   . PRO A 1 567 ? 81.06609 38.54953  -0.23242  1.000 64.99840  ? 446  PRO A N   1 
ATOM   3987 C CA  . PRO A 1 567 ? 81.66732 39.55585  0.66409   1.000 69.85046  ? 446  PRO A CA  1 
ATOM   3988 C C   . PRO A 1 567 ? 82.49143 40.60982  -0.05911  1.000 62.02466  ? 446  PRO A C   1 
ATOM   3989 O O   . PRO A 1 567 ? 82.76142 41.66668  0.52588   1.000 55.05329  ? 446  PRO A O   1 
ATOM   3990 C CB  . PRO A 1 567 ? 82.54804 38.72008  1.60548   1.000 65.76865  ? 446  PRO A CB  1 
ATOM   3991 C CG  . PRO A 1 567 ? 82.74751 37.42273  0.90381   1.000 60.34266  ? 446  PRO A CG  1 
ATOM   3992 C CD  . PRO A 1 567 ? 81.50790 37.18769  0.11128   1.000 50.77869  ? 446  PRO A CD  1 
ATOM   3993 N N   . GLU A 1 568 ? 82.90564 40.35381  -1.30089  1.000 55.03727  ? 447  GLU A N   1 
ATOM   3994 C CA  . GLU A 1 568 ? 83.63432 41.32313  -2.11033  1.000 56.64398  ? 447  GLU A CA  1 
ATOM   3995 C C   . GLU A 1 568 ? 82.75567 42.42937  -2.67782  1.000 76.83778  ? 447  GLU A C   1 
ATOM   3996 O O   . GLU A 1 568 ? 83.29368 43.39143  -3.23901  1.000 73.39174  ? 447  GLU A O   1 
ATOM   3997 C CB  . GLU A 1 568 ? 84.32258 40.60902  -3.27327  1.000 54.55655  ? 447  GLU A CB  1 
ATOM   3998 C CG  . GLU A 1 568 ? 83.34069 40.00571  -4.27634  1.000 53.43125  ? 447  GLU A CG  1 
ATOM   3999 C CD  . GLU A 1 568 ? 82.78802 38.65526  -3.84404  1.000 67.48777  ? 447  GLU A CD  1 
ATOM   4000 O OE1 . GLU A 1 568 ? 82.93348 38.29248  -2.65534  1.000 62.71187  ? 447  GLU A OE1 1 
ATOM   4001 O OE2 . GLU A 1 568 ? 82.19534 37.95753  -4.69570  1.000 71.88088  ? 447  GLU A OE2 1 
ATOM   4002 N N   . LEU A 1 569 ? 81.43394 42.31347  -2.56875  1.000 72.56927  ? 448  LEU A N   1 
ATOM   4003 C CA  . LEU A 1 569 ? 80.52359 43.31825  -3.11449  1.000 63.84646  ? 448  LEU A CA  1 
ATOM   4004 C C   . LEU A 1 569 ? 80.66591 44.60539  -2.31222  1.000 68.97681  ? 448  LEU A C   1 
ATOM   4005 O O   . LEU A 1 569 ? 80.15269 44.72012  -1.19730  1.000 74.41364  ? 448  LEU A O   1 
ATOM   4006 C CB  . LEU A 1 569 ? 79.08821 42.80508  -3.10167  1.000 61.09085  ? 448  LEU A CB  1 
ATOM   4007 C CG  . LEU A 1 569 ? 78.08147 43.65393  -3.87917  1.000 54.82109  ? 448  LEU A CG  1 
ATOM   4008 C CD1 . LEU A 1 569 ? 78.42290 43.67520  -5.36731  1.000 50.09343  ? 448  LEU A CD1 1 
ATOM   4009 C CD2 . LEU A 1 569 ? 76.66067 43.14020  -3.65751  1.000 65.71715  ? 448  LEU A CD2 1 
ATOM   4010 N N   . GLU A 1 570 ? 81.37434 45.57989  -2.88746  1.000 76.07355  ? 449  GLU A N   1 
ATOM   4011 C CA  . GLU A 1 570 ? 81.68545 46.81629  -2.17499  1.000 77.64034  ? 449  GLU A CA  1 
ATOM   4012 C C   . GLU A 1 570 ? 80.42178 47.56124  -1.76029  1.000 80.73773  ? 449  GLU A C   1 
ATOM   4013 O O   . GLU A 1 570 ? 80.29881 48.01066  -0.61169  1.000 86.60847  ? 449  GLU A O   1 
ATOM   4014 C CB  . GLU A 1 570 ? 82.56081 47.71012  -3.05195  1.000 86.09601  ? 449  GLU A CB  1 
ATOM   4015 C CG  . GLU A 1 570 ? 83.24176 48.83970  -2.30481  1.000 96.31244  ? 449  GLU A CG  1 
ATOM   4016 C CD  . GLU A 1 570 ? 84.29143 49.53430  -3.14629  1.000 102.96489 ? 449  GLU A CD  1 
ATOM   4017 O OE1 . GLU A 1 570 ? 84.02781 50.66430  -3.60852  1.000 105.72208 ? 449  GLU A OE1 1 
ATOM   4018 O OE2 . GLU A 1 570 ? 85.37326 48.94495  -3.35589  1.000 105.87438 ? 449  GLU A OE2 1 
ATOM   4019 N N   . GLU A 1 571 ? 79.47442 47.71581  -2.69011  1.000 65.94898  ? 450  GLU A N   1 
ATOM   4020 C CA  . GLU A 1 571 ? 78.27389 48.48593  -2.38378  1.000 78.91756  ? 450  GLU A CA  1 
ATOM   4021 C C   . GLU A 1 571 ? 77.47043 47.84589  -1.26035  1.000 63.82364  ? 450  GLU A C   1 
ATOM   4022 O O   . GLU A 1 571 ? 76.84262 48.55599  -0.47074  1.000 74.81135  ? 450  GLU A O   1 
ATOM   4023 C CB  . GLU A 1 571 ? 77.41044 48.64651  -3.63830  1.000 85.44669  ? 450  GLU A CB  1 
ATOM   4024 C CG  . GLU A 1 571 ? 76.16088 49.51718  -3.46159  1.000 98.02444  ? 450  GLU A CG  1 
ATOM   4025 C CD  . GLU A 1 571 ? 76.43279 50.86917  -2.80278  1.000 104.62061 ? 450  GLU A CD  1 
ATOM   4026 O OE1 . GLU A 1 571 ? 75.48123 51.44659  -2.23524  1.000 102.12904 ? 450  GLU A OE1 1 
ATOM   4027 O OE2 . GLU A 1 571 ? 77.57303 51.37806  -2.88247  1.000 103.58052 ? 450  GLU A OE2 1 
ATOM   4028 N N   . GLY A 1 572 ? 77.46902 46.51473  -1.17746  1.000 57.00309  ? 451  GLY A N   1 
ATOM   4029 C CA  . GLY A 1 572 ? 76.84336 45.85320  -0.04205  1.000 57.15059  ? 451  GLY A CA  1 
ATOM   4030 C C   . GLY A 1 572 ? 77.40395 46.32383  1.28750   1.000 73.00139  ? 451  GLY A C   1 
ATOM   4031 O O   . GLY A 1 572 ? 76.65600 46.67118  2.20823   1.000 74.46321  ? 451  GLY A O   1 
ATOM   4032 N N   . LYS A 1 573 ? 78.73572 46.32014  1.41070   1.000 60.43435  ? 452  LYS A N   1 
ATOM   4033 C CA  . LYS A 1 573 ? 79.37115 46.78721  2.63775   1.000 64.37361  ? 452  LYS A CA  1 
ATOM   4034 C C   . LYS A 1 573 ? 79.05345 48.25189  2.90048   1.000 59.29347  ? 452  LYS A C   1 
ATOM   4035 O O   . LYS A 1 573 ? 78.77165 48.63578  4.04129   1.000 59.98166  ? 452  LYS A O   1 
ATOM   4036 C CB  . LYS A 1 573 ? 80.88512 46.57649  2.56432   1.000 76.97125  ? 452  LYS A CB  1 
ATOM   4037 C CG  . LYS A 1 573 ? 81.62409 46.97481  3.83543   1.000 74.60248  ? 452  LYS A CG  1 
ATOM   4038 C CD  . LYS A 1 573 ? 83.13205 46.82463  3.68757   1.000 82.11278  ? 452  LYS A CD  1 
ATOM   4039 C CE  . LYS A 1 573 ? 83.84554 47.10004  5.00575   1.000 81.22156  ? 452  LYS A CE  1 
ATOM   4040 N NZ  . LYS A 1 573 ? 85.30125 47.34898  4.82291   1.000 91.31518  ? 452  LYS A NZ  1 
ATOM   4041 N N   . ASN A 1 574 ? 79.11829 49.09006  1.86313   1.000 56.89176  ? 453  ASN A N   1 
ATOM   4042 C CA  . ASN A 1 574 ? 78.72547 50.48935  2.01852   1.000 68.76154  ? 453  ASN A CA  1 
ATOM   4043 C C   . ASN A 1 574 ? 77.31685 50.61126  2.59260   1.000 69.97113  ? 453  ASN A C   1 
ATOM   4044 O O   . ASN A 1 574 ? 77.07486 51.39558  3.51715   1.000 78.56738  ? 453  ASN A O   1 
ATOM   4045 C CB  . ASN A 1 574 ? 78.82982 51.21902  0.67905   1.000 62.52337  ? 453  ASN A CB  1 
ATOM   4046 C CG  . ASN A 1 574 ? 80.26557 51.40399  0.22821   1.000 83.95759  ? 453  ASN A CG  1 
ATOM   4047 O OD1 . ASN A 1 574 ? 81.18763 51.42539  1.04554   1.000 75.14161  ? 453  ASN A OD1 1 
ATOM   4048 N ND2 . ASN A 1 574 ? 80.46201 51.54841  -1.07897  1.000 81.52523  ? 453  ASN A ND2 1 
ATOM   4049 N N   . ILE A 1 575 ? 76.37324 49.83979  2.04677   1.000 71.54697  ? 454  ILE A N   1 
ATOM   4050 C CA  . ILE A 1 575 ? 74.99235 49.87099  2.52700   1.000 61.71006  ? 454  ILE A CA  1 
ATOM   4051 C C   . ILE A 1 575 ? 74.93698 49.48622  3.99946   1.000 59.32933  ? 454  ILE A C   1 
ATOM   4052 O O   . ILE A 1 575 ? 74.29963 50.16307  4.81564   1.000 68.21387  ? 454  ILE A O   1 
ATOM   4053 C CB  . ILE A 1 575 ? 74.10810 48.95091  1.66656   1.000 58.00718  ? 454  ILE A CB  1 
ATOM   4054 C CG1 . ILE A 1 575 ? 73.97298 49.52127  0.25433   1.000 63.35537  ? 454  ILE A CG1 1 
ATOM   4055 C CG2 . ILE A 1 575 ? 72.74313 48.76117  2.30804   1.000 57.38661  ? 454  ILE A CG2 1 
ATOM   4056 C CD1 . ILE A 1 575 ? 73.21426 48.63018  -0.69453  1.000 66.66595  ? 454  ILE A CD1 1 
ATOM   4057 N N   . TRP A 1 576 ? 75.60352 48.38629  4.35686   1.000 52.15694  ? 455  TRP A N   1 
ATOM   4058 C CA  . TRP A 1 576 ? 75.58908 47.92044  5.74238   1.000 48.42742  ? 455  TRP A CA  1 
ATOM   4059 C C   . TRP A 1 576 ? 76.17502 48.96879  6.68391   1.000 58.58064  ? 455  TRP A C   1 
ATOM   4060 O O   . TRP A 1 576 ? 75.70521 49.12972  7.81679   1.000 62.18408  ? 455  TRP A O   1 
ATOM   4061 C CB  . TRP A 1 576 ? 76.34939 46.59761  5.85644   1.000 51.24408  ? 455  TRP A CB  1 
ATOM   4062 C CG  . TRP A 1 576 ? 76.31952 45.96510  7.22399   1.000 54.57238  ? 455  TRP A CG  1 
ATOM   4063 C CD1 . TRP A 1 576 ? 75.43458 45.02825  7.67177   1.000 59.20358  ? 455  TRP A CD1 1 
ATOM   4064 C CD2 . TRP A 1 576 ? 77.23654 46.19620  8.30408   1.000 68.89213  ? 455  TRP A CD2 1 
ATOM   4065 N NE1 . TRP A 1 576 ? 75.72964 44.67542  8.96641   1.000 66.08190  ? 455  TRP A NE1 1 
ATOM   4066 C CE2 . TRP A 1 576 ? 76.83371 45.37533  9.37672   1.000 60.77905  ? 455  TRP A CE2 1 
ATOM   4067 C CE3 . TRP A 1 576 ? 78.35500 47.01992  8.46913   1.000 69.15457  ? 455  TRP A CE3 1 
ATOM   4068 C CZ2 . TRP A 1 576 ? 77.50690 45.35682  10.59838  1.000 64.03336  ? 455  TRP A CZ2 1 
ATOM   4069 C CZ3 . TRP A 1 576 ? 79.02196 47.00006  9.68431   1.000 68.99806  ? 455  TRP A CZ3 1 
ATOM   4070 C CH2 . TRP A 1 576 ? 78.59527 46.17394  10.73179  1.000 63.68368  ? 455  TRP A CH2 1 
ATOM   4071 N N   . LEU A 1 577 ? 77.21461 49.67999  6.23751   1.000 60.23074  ? 456  LEU A N   1 
ATOM   4072 C CA  . LEU A 1 577 ? 77.88923 50.64753  7.09891   1.000 71.35559  ? 456  LEU A CA  1 
ATOM   4073 C C   . LEU A 1 577 ? 77.04389 51.89511  7.33751   1.000 74.69262  ? 456  LEU A C   1 
ATOM   4074 O O   . LEU A 1 577 ? 77.14645 52.51372  8.40279   1.000 80.77154  ? 456  LEU A O   1 
ATOM   4075 C CB  . LEU A 1 577 ? 79.23295 51.04702  6.48782   1.000 61.09889  ? 456  LEU A CB  1 
ATOM   4076 C CG  . LEU A 1 577 ? 80.40881 50.07688  6.59705   1.000 67.92347  ? 456  LEU A CG  1 
ATOM   4077 C CD1 . LEU A 1 577 ? 81.55190 50.55165  5.70937   1.000 65.74188  ? 456  LEU A CD1 1 
ATOM   4078 C CD2 . LEU A 1 577 ? 80.86590 49.94564  8.03818   1.000 59.03933  ? 456  LEU A CD2 1 
ATOM   4079 N N   . ARG A 1 578 ? 76.22240 52.29002  6.36485   1.000 74.68002  ? 457  ARG A N   1 
ATOM   4080 C CA  . ARG A 1 578 ? 75.34597 53.44781  6.49646   1.000 80.02208  ? 457  ARG A CA  1 
ATOM   4081 C C   . ARG A 1 578 ? 73.92851 53.09095  6.93375   1.000 82.21912  ? 457  ARG A C   1 
ATOM   4082 O O   . ARG A 1 578 ? 73.03848 53.94477  6.86244   1.000 93.08930  ? 457  ARG A O   1 
ATOM   4083 C CB  . ARG A 1 578 ? 75.30330 54.22055  5.17594   1.000 72.55785  ? 457  ARG A CB  1 
ATOM   4084 C CG  . ARG A 1 578 ? 74.66706 53.45088  4.03016   1.000 72.64758  ? 457  ARG A CG  1 
ATOM   4085 C CD  . ARG A 1 578 ? 74.25660 54.37190  2.89470   1.000 75.32602  ? 457  ARG A CD  1 
ATOM   4086 N NE  . ARG A 1 578 ? 74.72906 53.87560  1.60629   1.000 88.15320  ? 457  ARG A NE  1 
ATOM   4087 C CZ  . ARG A 1 578 ? 73.95071 53.31967  0.68396   1.000 95.91118  ? 457  ARG A CZ  1 
ATOM   4088 N NH1 . ARG A 1 578 ? 74.47471 52.90074  -0.45940  1.000 99.46925  ? 457  ARG A NH1 1 
ATOM   4089 N NH2 . ARG A 1 578 ? 72.65056 53.18205  0.90009   1.000 105.07021 ? 457  ARG A NH2 1 
ATOM   4090 N N   . SER A 1 579 ? 73.69482 51.86411  7.38618   1.000 76.99522  ? 458  SER A N   1 
ATOM   4091 C CA  . SER A 1 579 ? 72.36217 51.41480  7.75788   1.000 66.71306  ? 458  SER A CA  1 
ATOM   4092 C C   . SER A 1 579 ? 72.28113 51.16114  9.25847   1.000 71.35713  ? 458  SER A C   1 
ATOM   4093 O O   . SER A 1 579 ? 73.25589 50.73882  9.88605   1.000 64.77419  ? 458  SER A O   1 
ATOM   4094 C CB  . SER A 1 579 ? 71.98301 50.14262  6.99531   1.000 66.39478  ? 458  SER A CB  1 
ATOM   4095 O OG  . SER A 1 579 ? 71.65920 50.43783  5.64675   1.000 68.84722  ? 458  SER A OG  1 
ATOM   4096 N N   . GLU A 1 580 ? 71.10990 51.43605  9.83156   1.000 80.39775  ? 459  GLU A N   1 
ATOM   4097 C CA  . GLU A 1 580 ? 70.85824 51.07774  11.22215  1.000 83.09726  ? 459  GLU A CA  1 
ATOM   4098 C C   . GLU A 1 580 ? 70.92605 49.56539  11.40330  1.000 71.46300  ? 459  GLU A C   1 
ATOM   4099 O O   . GLU A 1 580 ? 70.49354 48.79863  10.53868  1.000 77.06506  ? 459  GLU A O   1 
ATOM   4100 C CB  . GLU A 1 580 ? 69.49806 51.60867  11.68117  1.000 93.03345  ? 459  GLU A CB  1 
ATOM   4101 C CG  . GLU A 1 580 ? 69.28008 51.48378  13.18723  1.000 100.66367 ? 459  GLU A CG  1 
ATOM   4102 C CD  . GLU A 1 580 ? 67.92487 51.99538  13.64260  1.000 102.49383 ? 459  GLU A CD  1 
ATOM   4103 O OE1 . GLU A 1 580 ? 67.18533 52.55637  12.80697  1.000 103.74692 ? 459  GLU A OE1 1 
ATOM   4104 O OE2 . GLU A 1 580 ? 67.60191 51.83965  14.84035  1.000 98.20244  ? 459  GLU A OE2 1 
ATOM   4105 N N   . HIS A 1 581 ? 71.49236 49.14052  12.52937  1.000 70.50306  ? 460  HIS A N   1 
ATOM   4106 C CA  . HIS A 1 581 ? 71.78986 47.74038  12.79903  1.000 66.95398  ? 460  HIS A CA  1 
ATOM   4107 C C   . HIS A 1 581 ? 70.86585 47.22248  13.89225  1.000 61.87840  ? 460  HIS A C   1 
ATOM   4108 O O   . HIS A 1 581 ? 70.71460 47.86499  14.93696  1.000 76.44024  ? 460  HIS A O   1 
ATOM   4109 C CB  . HIS A 1 581 ? 73.25168 47.57426  13.22177  1.000 64.58798  ? 460  HIS A CB  1 
ATOM   4110 C CG  . HIS A 1 581 ? 74.23247 47.89173  12.13741  1.000 70.62709  ? 460  HIS A CG  1 
ATOM   4111 N ND1 . HIS A 1 581 ? 75.56771 48.12918  12.38562  1.000 88.13295  ? 460  HIS A ND1 1 
ATOM   4112 C CD2 . HIS A 1 581 ? 74.07363 48.00304  10.79784  1.000 77.16260  ? 460  HIS A CD2 1 
ATOM   4113 C CE1 . HIS A 1 581 ? 76.18631 48.38567  11.24689  1.000 77.83215  ? 460  HIS A CE1 1 
ATOM   4114 N NE2 . HIS A 1 581 ? 75.30291 48.31184  10.26768  1.000 82.04830  ? 460  HIS A NE2 1 
ATOM   4115 N N   . PHE A 1 582 ? 70.25683 46.06254  13.65375  1.000 56.13652  ? 461  PHE A N   1 
ATOM   4116 C CA  . PHE A 1 582 ? 69.34475 45.43708  14.60246  1.000 62.61725  ? 461  PHE A CA  1 
ATOM   4117 C C   . PHE A 1 582 ? 69.88164 44.08531  15.05185  1.000 51.73591  ? 461  PHE A C   1 
ATOM   4118 O O   . PHE A 1 582 ? 70.41460 43.31831  14.24434  1.000 56.63193  ? 461  PHE A O   1 
ATOM   4119 C CB  . PHE A 1 582 ? 67.94269 45.22672  13.99786  1.000 54.19999  ? 461  PHE A CB  1 
ATOM   4120 C CG  . PHE A 1 582 ? 67.16235 46.49322  13.77279  1.000 58.96403  ? 461  PHE A CG  1 
ATOM   4121 C CD1 . PHE A 1 582 ? 67.58028 47.43979  12.85037  1.000 52.02111  ? 461  PHE A CD1 1 
ATOM   4122 C CD2 . PHE A 1 582 ? 65.98125 46.71699  14.46858  1.000 58.42871  ? 461  PHE A CD2 1 
ATOM   4123 C CE1 . PHE A 1 582 ? 66.84982 48.59493  12.64331  1.000 61.13774  ? 461  PHE A CE1 1 
ATOM   4124 C CE2 . PHE A 1 582 ? 65.24382 47.86886  14.26559  1.000 53.70714  ? 461  PHE A CE2 1 
ATOM   4125 C CZ  . PHE A 1 582 ? 65.67604 48.80941  13.35202  1.000 58.31935  ? 461  PHE A CZ  1 
ATOM   4126 N N   . SER A 1 583 ? 69.74227 43.80363  16.34493  1.000 49.27089  ? 462  SER A N   1 
ATOM   4127 C CA  . SER A 1 583 ? 69.89282 42.45250  16.85791  1.000 54.96098  ? 462  SER A CA  1 
ATOM   4128 C C   . SER A 1 583 ? 68.59234 41.67702  16.65379  1.000 63.71059  ? 462  SER A C   1 
ATOM   4129 O O   . SER A 1 583 ? 67.54886 42.24208  16.31814  1.000 59.71845  ? 462  SER A O   1 
ATOM   4130 C CB  . SER A 1 583 ? 70.26471 42.47088  18.33742  1.000 52.88333  ? 462  SER A CB  1 
ATOM   4131 O OG  . SER A 1 583 ? 69.22093 43.03321  19.11400  1.000 58.36125  ? 462  SER A OG  1 
ATOM   4132 N N   . ALA A 1 584 ? 68.65522 40.36210  16.87371  1.000 50.20010  ? 463  ALA A N   1 
ATOM   4133 C CA  . ALA A 1 584 ? 67.43707 39.56129  16.81989  1.000 53.39994  ? 463  ALA A CA  1 
ATOM   4134 C C   . ALA A 1 584 ? 66.42220 40.03979  17.85428  1.000 66.66836  ? 463  ALA A C   1 
ATOM   4135 O O   . ALA A 1 584 ? 65.21320 40.09084  17.57660  1.000 67.31346  ? 463  ALA A O   1 
ATOM   4136 C CB  . ALA A 1 584 ? 67.77389 38.08354  17.02382  1.000 43.11437  ? 463  ALA A CB  1 
ATOM   4137 N N   . ASP A 1 585 ? 66.89781 40.41773  19.04717  1.000 53.42162  ? 464  ASP A N   1 
ATOM   4138 C CA  . ASP A 1 585 ? 65.99027 40.92517  20.07057  1.000 65.99940  ? 464  ASP A CA  1 
ATOM   4139 C C   . ASP A 1 585 ? 65.30015 42.19466  19.59503  1.000 59.92195  ? 464  ASP A C   1 
ATOM   4140 O O   . ASP A 1 585 ? 64.08379 42.34138  19.74659  1.000 69.17697  ? 464  ASP A O   1 
ATOM   4141 C CB  . ASP A 1 585 ? 66.73902 41.18707  21.37994  1.000 56.37234  ? 464  ASP A CB  1 
ATOM   4142 C CG  . ASP A 1 585 ? 67.14752 39.90997  22.09073  1.000 60.29942  ? 464  ASP A CG  1 
ATOM   4143 O OD1 . ASP A 1 585 ? 66.46811 38.88002  21.91091  1.000 63.69551  ? 464  ASP A OD1 1 
ATOM   4144 O OD2 . ASP A 1 585 ? 68.13778 39.94251  22.85219  1.000 76.99885  ? 464  ASP A OD2 1 
ATOM   4145 N N   . GLU A 1 586 ? 66.05779 43.11443  18.99356  1.000 59.21133  ? 465  GLU A N   1 
ATOM   4146 C CA  . GLU A 1 586 ? 65.46963 44.36868  18.53837  1.000 53.46265  ? 465  GLU A CA  1 
ATOM   4147 C C   . GLU A 1 586 ? 64.55039 44.15205  17.34234  1.000 60.49648  ? 465  GLU A C   1 
ATOM   4148 O O   . GLU A 1 586 ? 63.54338 44.85936  17.19826  1.000 65.50344  ? 465  GLU A O   1 
ATOM   4149 C CB  . GLU A 1 586 ? 66.57342 45.36933  18.19717  1.000 51.03299  ? 465  GLU A CB  1 
ATOM   4150 C CG  . GLU A 1 586 ? 67.51793 45.65237  19.35353  1.000 57.37532  ? 465  GLU A CG  1 
ATOM   4151 C CD  . GLU A 1 586 ? 68.76236 46.41577  18.93309  1.000 70.97677  ? 465  GLU A CD  1 
ATOM   4152 O OE1 . GLU A 1 586 ? 69.24686 46.19990  17.80146  1.000 67.31696  ? 465  GLU A OE1 1 
ATOM   4153 O OE2 . GLU A 1 586 ? 69.25669 47.23328  19.73731  1.000 72.10962  ? 465  GLU A OE2 1 
ATOM   4154 N N   . ILE A 1 587 ? 64.86011 43.16544  16.49544  1.000 53.56148  ? 466  ILE A N   1 
ATOM   4155 C CA  . ILE A 1 587 ? 63.95893 42.81865  15.39991  1.000 57.57547  ? 466  ILE A CA  1 
ATOM   4156 C C   . ILE A 1 587 ? 62.61442 42.36964  15.95167  1.000 70.70125  ? 466  ILE A C   1 
ATOM   4157 O O   . ILE A 1 587 ? 61.55976 42.89504  15.57416  1.000 63.23498  ? 466  ILE A O   1 
ATOM   4158 C CB  . ILE A 1 587 ? 64.57956 41.73184  14.50406  1.000 53.77986  ? 466  ILE A CB  1 
ATOM   4159 C CG1 . ILE A 1 587 ? 65.80703 42.25814  13.76392  1.000 57.73064  ? 466  ILE A CG1 1 
ATOM   4160 C CG2 . ILE A 1 587 ? 63.54826 41.21338  13.51085  1.000 45.31477  ? 466  ILE A CG2 1 
ATOM   4161 C CD1 . ILE A 1 587 ? 66.48250 41.20311  12.91459  1.000 51.26632  ? 466  ILE A CD1 1 
ATOM   4162 N N   . SER A 1 588 ? 62.62732 41.40252  16.86720  1.000 53.32948  ? 467  SER A N   1 
ATOM   4163 C CA  . SER A 1 588 ? 61.34712 40.89893  17.33706  1.000 51.36012  ? 467  SER A CA  1 
ATOM   4164 C C   . SER A 1 588 ? 60.67671 41.85519  18.31617  1.000 66.44829  ? 467  SER A C   1 
ATOM   4165 O O   . SER A 1 588 ? 59.48636 41.69137  18.60144  1.000 65.67828  ? 467  SER A O   1 
ATOM   4166 C CB  . SER A 1 588 ? 61.52483 39.51804  17.97285  1.000 40.23721  ? 467  SER A CB  1 
ATOM   4167 O OG  . SER A 1 588 ? 62.29039 39.59528  19.15647  1.000 80.77695  ? 467  SER A OG  1 
ATOM   4168 N N   . ALA A 1 589 ? 61.40705 42.85233  18.82162  1.000 65.92455  ? 468  ALA A N   1 
ATOM   4169 C CA  . ALA A 1 589 ? 60.80267 43.92212  19.60546  1.000 64.58590  ? 468  ALA A CA  1 
ATOM   4170 C C   . ALA A 1 589 ? 60.14399 44.99794  18.74658  1.000 72.21247  ? 468  ALA A C   1 
ATOM   4171 O O   . ALA A 1 589 ? 59.17552 45.62522  19.19376  1.000 65.77257  ? 468  ALA A O   1 
ATOM   4172 C CB  . ALA A 1 589 ? 61.85793 44.56270  20.51002  1.000 52.67113  ? 468  ALA A CB  1 
ATOM   4173 N N   . GLY A 1 590 ? 60.63584 45.23185  17.52803  1.000 65.27881  ? 469  GLY A N   1 
ATOM   4174 C CA  . GLY A 1 590 ? 60.10369 46.33247  16.74248  1.000 60.62160  ? 469  GLY A CA  1 
ATOM   4175 C C   . GLY A 1 590 ? 59.44146 45.99673  15.41954  1.000 68.67009  ? 469  GLY A C   1 
ATOM   4176 O O   . GLY A 1 590 ? 58.97596 46.90406  14.72235  1.000 69.43976  ? 469  GLY A O   1 
ATOM   4177 N N   . ALA A 1 591 ? 59.40433 44.71158  15.06115  1.000 66.63225  ? 470  ALA A N   1 
ATOM   4178 C CA  . ALA A 1 591 ? 58.90961 44.28174  13.75607  1.000 67.16970  ? 470  ALA A CA  1 
ATOM   4179 C C   . ALA A 1 591 ? 57.57016 44.93000  13.41471  1.000 70.82209  ? 470  ALA A C   1 
ATOM   4180 O O   . ALA A 1 591 ? 56.70542 45.09802  14.27784  1.000 66.33642  ? 470  ALA A O   1 
ATOM   4181 C CB  . ALA A 1 591 ? 58.77509 42.75779  13.73096  1.000 56.01841  ? 470  ALA A CB  1 
ATOM   4182 N N   . ASN A 1 592 ? 57.40633 45.30082  12.14227  1.000 65.05376  ? 471  ASN A N   1 
ATOM   4183 C CA  . ASN A 1 592 ? 56.12764 45.79759  11.62845  1.000 71.48765  ? 471  ASN A CA  1 
ATOM   4184 C C   . ASN A 1 592 ? 55.30179 44.59731  11.18363  1.000 69.85533  ? 471  ASN A C   1 
ATOM   4185 O O   . ASN A 1 592 ? 55.31495 44.20002  10.01716  1.000 59.04683  ? 471  ASN A O   1 
ATOM   4186 C CB  . ASN A 1 592 ? 56.33832 46.78785  10.49043  1.000 68.48544  ? 471  ASN A CB  1 
ATOM   4187 C CG  . ASN A 1 592 ? 55.09663 47.61343  10.20551  1.000 72.93948  ? 471  ASN A CG  1 
ATOM   4188 O OD1 . ASN A 1 592 ? 53.99231 47.07552  10.09819  1.000 60.41441  ? 471  ASN A OD1 1 
ATOM   4189 N ND2 . ASN A 1 592 ? 55.27096 48.92469  10.07833  1.000 67.74717  ? 471  ASN A ND2 1 
ATOM   4190 N N   . LEU A 1 593 ? 54.57555 44.00758  12.13389  1.000 55.78829  ? 472  LEU A N   1 
ATOM   4191 C CA  . LEU A 1 593 ? 53.83232 42.78485  11.85228  1.000 57.08708  ? 472  LEU A CA  1 
ATOM   4192 C C   . LEU A 1 593 ? 52.69768 43.01392  10.85755  1.000 60.36666  ? 472  LEU A C   1 
ATOM   4193 O O   . LEU A 1 593 ? 52.33177 42.09397  10.11177  1.000 63.21373  ? 472  LEU A O   1 
ATOM   4194 C CB  . LEU A 1 593 ? 53.28879 42.21315  13.15949  1.000 78.23341  ? 472  LEU A CB  1 
ATOM   4195 C CG  . LEU A 1 593 ? 54.36364 41.84451  14.18311  1.000 65.54775  ? 472  LEU A CG  1 
ATOM   4196 C CD1 . LEU A 1 593 ? 53.73287 41.40110  15.49060  1.000 60.81592  ? 472  LEU A CD1 1 
ATOM   4197 C CD2 . LEU A 1 593 ? 55.26838 40.75997  13.62070  1.000 58.98309  ? 472  LEU A CD2 1 
ATOM   4198 N N   . LYS A 1 594 ? 52.13364 44.22323  10.82367  1.000 56.56666  ? 473  LYS A N   1 
ATOM   4199 C CA  . LYS A 1 594 ? 51.04735 44.48881  9.88858   1.000 75.06264  ? 473  LYS A CA  1 
ATOM   4200 C C   . LYS A 1 594 ? 51.52935 44.42925  8.44450   1.000 81.66763  ? 473  LYS A C   1 
ATOM   4201 O O   . LYS A 1 594 ? 50.83536 43.88059  7.58225   1.000 58.09687  ? 473  LYS A O   1 
ATOM   4202 C CB  . LYS A 1 594 ? 50.39832 45.83750  10.19980  1.000 80.08351  ? 473  LYS A CB  1 
ATOM   4203 C CG  . LYS A 1 594 ? 49.60360 45.83593  11.50177  1.000 93.39258  ? 473  LYS A CG  1 
ATOM   4204 C CD  . LYS A 1 594 ? 48.88490 47.15518  11.73950  1.000 89.64161  ? 473  LYS A CD  1 
ATOM   4205 C CE  . LYS A 1 594 ? 48.80536 47.47129  13.22497  1.000 92.45674  ? 473  LYS A CE  1 
ATOM   4206 N NZ  . LYS A 1 594 ? 47.96268 48.66864  13.50414  1.000 107.55960 ? 473  LYS A NZ  1 
ATOM   4207 N N   . ARG A 1 595 ? 52.72611 44.95445  8.16051   1.000 60.12934  ? 474  ARG A N   1 
ATOM   4208 C CA  . ARG A 1 595 ? 53.23917 44.86649  6.79587   1.000 62.84200  ? 474  ARG A CA  1 
ATOM   4209 C C   . ARG A 1 595 ? 53.60966 43.43547  6.43013   1.000 52.05029  ? 474  ARG A C   1 
ATOM   4210 O O   . ARG A 1 595 ? 53.43105 43.02433  5.27589   1.000 61.67611  ? 474  ARG A O   1 
ATOM   4211 C CB  . ARG A 1 595 ? 54.43855 45.79355  6.61521   1.000 60.38340  ? 474  ARG A CB  1 
ATOM   4212 C CG  . ARG A 1 595 ? 54.10395 47.26350  6.75483   1.000 53.66631  ? 474  ARG A CG  1 
ATOM   4213 C CD  . ARG A 1 595 ? 55.36694 48.08446  6.74265   1.000 62.24822  ? 474  ARG A CD  1 
ATOM   4214 N NE  . ARG A 1 595 ? 56.16243 47.80019  5.55404   1.000 68.24701  ? 474  ARG A NE  1 
ATOM   4215 C CZ  . ARG A 1 595 ? 57.47836 47.95443  5.48629   1.000 71.18863  ? 474  ARG A CZ  1 
ATOM   4216 N NH1 . ARG A 1 595 ? 58.14836 48.39302  6.54339   1.000 62.02486  ? 474  ARG A NH1 1 
ATOM   4217 N NH2 . ARG A 1 595 ? 58.12396 47.66593  4.36434   1.000 70.33496  ? 474  ARG A NH2 1 
ATOM   4218 N N   . LEU A 1 596 ? 54.08598 42.65692  7.40279   1.000 49.50902  ? 475  LEU A N   1 
ATOM   4219 C CA  . LEU A 1 596 ? 54.41560 41.25881  7.14603   1.000 63.83693  ? 475  LEU A CA  1 
ATOM   4220 C C   . LEU A 1 596 ? 53.16487 40.47482  6.76834   1.000 58.13535  ? 475  LEU A C   1 
ATOM   4221 O O   . LEU A 1 596 ? 53.14203 39.75586  5.75742   1.000 61.52974  ? 475  LEU A O   1 
ATOM   4222 C CB  . LEU A 1 596 ? 55.09957 40.65090  8.37463   1.000 46.94332  ? 475  LEU A CB  1 
ATOM   4223 C CG  . LEU A 1 596 ? 55.55472 39.19096  8.28219   1.000 52.57584  ? 475  LEU A CG  1 
ATOM   4224 C CD1 . LEU A 1 596 ? 56.85356 39.07314  7.50186   1.000 43.69481  ? 475  LEU A CD1 1 
ATOM   4225 C CD2 . LEU A 1 596 ? 55.70116 38.58144  9.66775   1.000 47.94221  ? 475  LEU A CD2 1 
ATOM   4226 N N   . TYR A 1 597 ? 52.10215 40.62037  7.56772   1.000 60.96577  ? 476  TYR A N   1 
ATOM   4227 C CA  . TYR A 1 597 ? 50.83498 39.97190  7.24366   1.000 53.40213  ? 476  TYR A CA  1 
ATOM   4228 C C   . TYR A 1 597 ? 50.26596 40.47820  5.92261   1.000 45.19757  ? 476  TYR A C   1 
ATOM   4229 O O   . TYR A 1 597 ? 49.73147 39.69027  5.13468   1.000 58.27583  ? 476  TYR A O   1 
ATOM   4230 C CB  . TYR A 1 597 ? 49.83422 40.17707  8.38161   1.000 56.33037  ? 476  TYR A CB  1 
ATOM   4231 C CG  . TYR A 1 597 ? 49.96977 39.17592  9.50748   1.000 57.15304  ? 476  TYR A CG  1 
ATOM   4232 C CD1 . TYR A 1 597 ? 51.11868 39.11835  10.28865  1.000 57.32276  ? 476  TYR A CD1 1 
ATOM   4233 C CD2 . TYR A 1 597 ? 48.93556 38.29775  9.79941   1.000 46.56507  ? 476  TYR A CD2 1 
ATOM   4234 C CE1 . TYR A 1 597 ? 51.23441 38.19908  11.31882  1.000 52.61121  ? 476  TYR A CE1 1 
ATOM   4235 C CE2 . TYR A 1 597 ? 49.04045 37.38247  10.82400  1.000 55.89196  ? 476  TYR A CE2 1 
ATOM   4236 C CZ  . TYR A 1 597 ? 50.18891 37.33454  11.58242  1.000 62.12865  ? 476  TYR A CZ  1 
ATOM   4237 O OH  . TYR A 1 597 ? 50.28399 36.41680  12.60621  1.000 53.37422  ? 476  TYR A OH  1 
ATOM   4238 N N   . ALA A 1 598 ? 50.31125 41.79237  5.68674   1.000 51.35379  ? 477  ALA A N   1 
ATOM   4239 C CA  . ALA A 1 598 ? 49.81134 42.33859  4.42739   1.000 61.85551  ? 477  ALA A CA  1 
ATOM   4240 C C   . ALA A 1 598 ? 50.49476 41.67838  3.23698   1.000 70.60810  ? 477  ALA A C   1 
ATOM   4241 O O   . ALA A 1 598 ? 49.83443 41.25721  2.27961   1.000 82.25931  ? 477  ALA A O   1 
ATOM   4242 C CB  . ALA A 1 598 ? 50.01140 43.85344  4.39451   1.000 66.42828  ? 477  ALA A CB  1 
ATOM   4243 N N   . GLN A 1 599 ? 51.82769 41.61604  3.26623   1.000 63.95739  ? 478  GLN A N   1 
ATOM   4244 C CA  . GLN A 1 599 ? 52.57326 40.97500  2.18751   1.000 60.75895  ? 478  GLN A CA  1 
ATOM   4245 C C   . GLN A 1 599 ? 52.16567 39.51059  2.02504   1.000 58.65384  ? 478  GLN A C   1 
ATOM   4246 O O   . GLN A 1 599 ? 51.95630 39.03215  0.89949   1.000 56.29627  ? 478  GLN A O   1 
ATOM   4247 C CB  . GLN A 1 599 ? 54.07477 41.11023  2.45063   1.000 53.01914  ? 478  GLN A CB  1 
ATOM   4248 C CG  . GLN A 1 599 ? 54.95855 40.37700  1.46488   1.000 54.07841  ? 478  GLN A CG  1 
ATOM   4249 C CD  . GLN A 1 599 ? 56.42958 40.48844  1.81531   1.000 60.75750  ? 478  GLN A CD  1 
ATOM   4250 O OE1 . GLN A 1 599 ? 57.02597 41.56009  1.69938   1.000 54.76878  ? 478  GLN A OE1 1 
ATOM   4251 N NE2 . GLN A 1 599 ? 57.02091 39.38102  2.25569   1.000 47.37098  ? 478  GLN A NE2 1 
ATOM   4252 N N   . ARG A 1 600 ? 52.09909 38.76845  3.13863   1.000 55.24103  ? 479  ARG A N   1 
ATOM   4253 C CA  . ARG A 1 600 ? 51.62762 37.38426  3.08658   1.000 53.50988  ? 479  ARG A CA  1 
ATOM   4254 C C   . ARG A 1 600 ? 50.27890 37.27480  2.37985   1.000 61.04869  ? 479  ARG A C   1 
ATOM   4255 O O   . ARG A 1 600 ? 50.08250 36.41504  1.51083   1.000 54.08103  ? 479  ARG A O   1 
ATOM   4256 C CB  . ARG A 1 600 ? 51.54163 36.80732  4.50048   1.000 55.83287  ? 479  ARG A CB  1 
ATOM   4257 C CG  . ARG A 1 600 ? 51.02371 35.37528  4.56172   1.000 45.84699  ? 479  ARG A CG  1 
ATOM   4258 C CD  . ARG A 1 600 ? 50.90897 34.90946  6.00488   1.000 47.40732  ? 479  ARG A CD  1 
ATOM   4259 N NE  . ARG A 1 600 ? 52.18422 35.05863  6.69873   1.000 66.92630  ? 479  ARG A NE  1 
ATOM   4260 C CZ  . ARG A 1 600 ? 52.33197 35.03987  8.01930   1.000 63.25293  ? 479  ARG A CZ  1 
ATOM   4261 N NH1 . ARG A 1 600 ? 53.53809 35.19062  8.55514   1.000 70.32828  ? 479  ARG A NH1 1 
ATOM   4262 N NH2 . ARG A 1 600 ? 51.28023 34.87421  8.80617   1.000 61.52370  ? 479  ARG A NH2 1 
ATOM   4263 N N   . GLU A 1 601 ? 49.33012 38.13400  2.75652   1.000 47.82825  ? 480  GLU A N   1 
ATOM   4264 C CA  . GLU A 1 601 ? 47.99989 38.07896  2.15895   1.000 51.89204  ? 480  GLU A CA  1 
ATOM   4265 C C   . GLU A 1 601 ? 48.03404 38.44515  0.68389   1.000 69.72848  ? 480  GLU A C   1 
ATOM   4266 O O   . GLU A 1 601 ? 47.24399 37.91299  -0.10405  1.000 56.42842  ? 480  GLU A O   1 
ATOM   4267 C CB  . GLU A 1 601 ? 47.02868 38.98897  2.91306   1.000 56.31389  ? 480  GLU A CB  1 
ATOM   4268 C CG  . GLU A 1 601 ? 45.58460 38.84341  2.44613   1.000 68.77498  ? 480  GLU A CG  1 
ATOM   4269 C CD  . GLU A 1 601 ? 45.08743 37.40883  2.52105   1.000 76.26789  ? 480  GLU A CD  1 
ATOM   4270 O OE1 . GLU A 1 601 ? 45.43591 36.70139  3.49059   1.000 82.13895  ? 480  GLU A OE1 1 
ATOM   4271 O OE2 . GLU A 1 601 ? 44.35889 36.98384  1.59897   1.000 88.28368  ? 480  GLU A OE2 1 
ATOM   4272 N N   . GLU A 1 602 ? 48.92620 39.35443  0.29181   1.000 61.01228  ? 481  GLU A N   1 
ATOM   4273 C CA  . GLU A 1 602 ? 49.03636 39.68288  -1.12401  1.000 64.67074  ? 481  GLU A CA  1 
ATOM   4274 C C   . GLU A 1 602 ? 49.55919 38.48490  -1.90743  1.000 67.26508  ? 481  GLU A C   1 
ATOM   4275 O O   . GLU A 1 602 ? 49.09225 38.20818  -3.02033  1.000 68.66176  ? 481  GLU A O   1 
ATOM   4276 C CB  . GLU A 1 602 ? 49.93754 40.90058  -1.31575  1.000 59.21043  ? 481  GLU A CB  1 
ATOM   4277 C CG  . GLU A 1 602 ? 50.19582 41.25340  -2.77098  1.000 77.08302  ? 481  GLU A CG  1 
ATOM   4278 C CD  . GLU A 1 602 ? 48.91323 41.56099  -3.52703  1.000 102.78542 ? 481  GLU A CD  1 
ATOM   4279 O OE1 . GLU A 1 602 ? 48.08944 42.34838  -3.01103  1.000 96.92116  ? 481  GLU A OE1 1 
ATOM   4280 O OE2 . GLU A 1 602 ? 48.72790 41.01248  -4.63431  1.000 103.22921 ? 481  GLU A OE2 1 
ATOM   4281 N N   . PHE A 1 603 ? 50.47349 37.71645  -1.30609  1.000 65.43272  ? 482  PHE A N   1 
ATOM   4282 C CA  . PHE A 1 603 ? 50.94247 36.49716  -1.96193  1.000 62.64664  ? 482  PHE A CA  1 
ATOM   4283 C C   . PHE A 1 603 ? 49.82864 35.45968  -2.05195  1.000 70.02981  ? 482  PHE A C   1 
ATOM   4284 O O   . PHE A 1 603 ? 49.68865 34.77912  -3.07449  1.000 61.63248  ? 482  PHE A O   1 
ATOM   4285 C CB  . PHE A 1 603 ? 52.14637 35.90348  -1.22634  1.000 55.37865  ? 482  PHE A CB  1 
ATOM   4286 C CG  . PHE A 1 603 ? 53.45495 36.59132  -1.51670  1.000 68.69212  ? 482  PHE A CG  1 
ATOM   4287 C CD1 . PHE A 1 603 ? 53.95935 36.63116  -2.80891  1.000 61.35979  ? 482  PHE A CD1 1 
ATOM   4288 C CD2 . PHE A 1 603 ? 54.20927 37.14142  -0.49232  1.000 64.09720  ? 482  PHE A CD2 1 
ATOM   4289 C CE1 . PHE A 1 603 ? 55.17137 37.24390  -3.08158  1.000 65.64136  ? 482  PHE A CE1 1 
ATOM   4290 C CE2 . PHE A 1 603 ? 55.42412 37.75270  -0.75745  1.000 67.77999  ? 482  PHE A CE2 1 
ATOM   4291 C CZ  . PHE A 1 603 ? 55.90453 37.80583  -2.05516  1.000 66.04772  ? 482  PHE A CZ  1 
ATOM   4292 N N   . ARG A 1 604 ? 49.03494 35.31801  -0.98780  1.000 62.08485  ? 483  ARG A N   1 
ATOM   4293 C CA  . ARG A 1 604 ? 47.88383 34.41675  -1.03191  1.000 56.71236  ? 483  ARG A CA  1 
ATOM   4294 C C   . ARG A 1 604 ? 46.93281 34.80000  -2.15832  1.000 52.41464  ? 483  ARG A C   1 
ATOM   4295 O O   . ARG A 1 604 ? 46.54241 33.95764  -2.97946  1.000 70.20673  ? 483  ARG A O   1 
ATOM   4296 C CB  . ARG A 1 604 ? 47.14336 34.43724  0.30572   1.000 70.56182  ? 483  ARG A CB  1 
ATOM   4297 C CG  . ARG A 1 604 ? 47.95648 33.94223  1.47535   1.000 88.09155  ? 483  ARG A CG  1 
ATOM   4298 C CD  . ARG A 1 604 ? 47.13068 33.92318  2.74932   1.000 89.75027  ? 483  ARG A CD  1 
ATOM   4299 N NE  . ARG A 1 604 ? 47.82120 33.24026  3.83846   1.000 72.40261  ? 483  ARG A NE  1 
ATOM   4300 C CZ  . ARG A 1 604 ? 47.57922 33.46115  5.12550   1.000 84.63661  ? 483  ARG A CZ  1 
ATOM   4301 N NH1 . ARG A 1 604 ? 46.67927 34.36835  5.48297   1.000 85.60466  ? 483  ARG A NH1 1 
ATOM   4302 N NH2 . ARG A 1 604 ? 48.25198 32.79313  6.05526   1.000 78.73210  ? 483  ARG A NH2 1 
ATOM   4303 N N   . LYS A 1 605 ? 46.51599 36.06812  -2.17903  1.000 55.35570  ? 484  LYS A N   1 
ATOM   4304 C CA  . LYS A 1 605 ? 45.60558 36.55016  -3.21051  1.000 68.38090  ? 484  LYS A CA  1 
ATOM   4305 C C   . LYS A 1 605 ? 46.16720 36.26771  -4.59791  1.000 61.59163  ? 484  LYS A C   1 
ATOM   4306 O O   . LYS A 1 605 ? 45.43541 35.83382  -5.49504  1.000 67.62317  ? 484  LYS A O   1 
ATOM   4307 C CB  . LYS A 1 605 ? 45.32581 38.03935  -2.99193  1.000 63.43561  ? 484  LYS A CB  1 
ATOM   4308 C CG  . LYS A 1 605 ? 45.00941 38.85265  -4.22989  1.000 76.54016  ? 484  LYS A CG  1 
ATOM   4309 C CD  . LYS A 1 605 ? 44.50314 40.23118  -3.81421  1.000 88.31145  ? 484  LYS A CD  1 
ATOM   4310 C CE  . LYS A 1 605 ? 43.89961 40.99697  -4.98175  1.000 99.24318  ? 484  LYS A CE  1 
ATOM   4311 N NZ  . LYS A 1 605 ? 43.09082 40.12139  -5.87435  1.000 106.72978 ? 484  LYS A NZ  1 
ATOM   4312 N N   . GLY A 1 606 ? 47.46970 36.49557  -4.79136  1.000 62.02110  ? 485  GLY A N   1 
ATOM   4313 C CA  . GLY A 1 606 ? 48.08171 36.14806  -6.06451  1.000 58.78356  ? 485  GLY A CA  1 
ATOM   4314 C C   . GLY A 1 606 ? 48.02584 34.65815  -6.35237  1.000 57.93203  ? 485  GLY A C   1 
ATOM   4315 O O   . GLY A 1 606 ? 47.85112 34.24421  -7.50048  1.000 70.22703  ? 485  GLY A O   1 
ATOM   4316 N N   . ASN A 1 607 ? 48.16390 33.83197  -5.31127  1.000 60.90024  ? 486  ASN A N   1 
ATOM   4317 C CA  . ASN A 1 607 ? 48.11655 32.38403  -5.48531  1.000 65.41271  ? 486  ASN A CA  1 
ATOM   4318 C C   . ASN A 1 607 ? 46.71023 31.87480  -5.76452  1.000 71.66543  ? 486  ASN A C   1 
ATOM   4319 O O   . ASN A 1 607 ? 46.55773 30.73584  -6.21892  1.000 84.96576  ? 486  ASN A O   1 
ATOM   4320 C CB  . ASN A 1 607 ? 48.65796 31.67705  -4.23895  1.000 78.80449  ? 486  ASN A CB  1 
ATOM   4321 C CG  . ASN A 1 607 ? 50.16791 31.75038  -4.12520  1.000 83.36811  ? 486  ASN A CG  1 
ATOM   4322 O OD1 . ASN A 1 607 ? 50.73212 31.46125  -3.06880  1.000 87.80377  ? 486  ASN A OD1 1 
ATOM   4323 N ND2 . ASN A 1 607 ? 50.83080 32.12687  -5.21278  1.000 75.91713  ? 486  ASN A ND2 1 
ATOM   4324 N N   . TRP A 1 608 ? 45.68455 32.68047  -5.50529  1.000 70.44412  ? 487  TRP A N   1 
ATOM   4325 C CA  . TRP A 1 608 ? 44.32039 32.28366  -5.83599  1.000 75.63316  ? 487  TRP A CA  1 
ATOM   4326 C C   . TRP A 1 608 ? 43.89253 32.69250  -7.23926  1.000 78.56602  ? 487  TRP A C   1 
ATOM   4327 O O   . TRP A 1 608 ? 42.73852 32.45748  -7.61153  1.000 103.25235 ? 487  TRP A O   1 
ATOM   4328 C CB  . TRP A 1 608 ? 43.33809 32.84849  -4.81102  1.000 78.61791  ? 487  TRP A CB  1 
ATOM   4329 C CG  . TRP A 1 608 ? 43.27834 32.01808  -3.57768  1.000 97.64013  ? 487  TRP A CG  1 
ATOM   4330 C CD1 . TRP A 1 608 ? 44.19872 31.97221  -2.57254  1.000 85.34791  ? 487  TRP A CD1 1 
ATOM   4331 C CD2 . TRP A 1 608 ? 42.25641 31.07708  -3.23076  1.000 106.08016 ? 487  TRP A CD2 1 
ATOM   4332 N NE1 . TRP A 1 608 ? 43.80310 31.07488  -1.60983  1.000 91.91050  ? 487  TRP A NE1 1 
ATOM   4333 C CE2 . TRP A 1 608 ? 42.61391 30.51090  -1.99104  1.000 107.49337 ? 487  TRP A CE2 1 
ATOM   4334 C CE3 . TRP A 1 608 ? 41.06935 30.66548  -3.84319  1.000 92.16859  ? 487  TRP A CE3 1 
ATOM   4335 C CZ2 . TRP A 1 608 ? 41.82691 29.55414  -1.35279  1.000 106.38384 ? 487  TRP A CZ2 1 
ATOM   4336 C CZ3 . TRP A 1 608 ? 40.29114 29.71571  -3.20807  1.000 103.42761 ? 487  TRP A CZ3 1 
ATOM   4337 C CH2 . TRP A 1 608 ? 40.67222 29.17110  -1.97631  1.000 97.62718  ? 487  TRP A CH2 1 
ATOM   4338 N N   . LYS A 1 609 ? 44.78268 33.29045  -8.02368  1.000 89.39285  ? 488  LYS A N   1 
ATOM   4339 C CA  . LYS A 1 609 ? 44.47501 33.65305  -9.40437  1.000 81.00089  ? 488  LYS A CA  1 
ATOM   4340 C C   . LYS A 1 609 ? 44.69643 32.42143  -10.27113 1.000 79.04584  ? 488  LYS A C   1 
ATOM   4341 O O   . LYS A 1 609 ? 45.83168 32.07484  -10.60698 1.000 84.37985  ? 488  LYS A O   1 
ATOM   4342 C CB  . LYS A 1 609 ? 45.32950 34.82982  -9.85563  1.000 78.85667  ? 488  LYS A CB  1 
ATOM   4343 C CG  . LYS A 1 609 ? 44.96117 36.12705  -9.16157  1.000 81.26352  ? 488  LYS A CG  1 
ATOM   4344 C CD  . LYS A 1 609 ? 43.47351 36.41051  -9.32768  1.000 72.94262  ? 488  LYS A CD  1 
ATOM   4345 C CE  . LYS A 1 609 ? 43.13273 37.84736  -8.98037  1.000 75.70438  ? 488  LYS A CE  1 
ATOM   4346 N NZ  . LYS A 1 609 ? 41.76330 37.97368  -8.40788  1.000 97.91367  ? 488  LYS A NZ  1 
ATOM   4347 N N   . ALA A 1 610 ? 43.59766 31.75426  -10.62986 1.000 69.91140  ? 489  ALA A N   1 
ATOM   4348 C CA  . ALA A 1 610 ? 43.67153 30.38678  -11.13270 1.000 82.04678  ? 489  ALA A CA  1 
ATOM   4349 C C   . ALA A 1 610 ? 44.33985 30.30544  -12.49768 1.000 88.17394  ? 489  ALA A C   1 
ATOM   4350 O O   . ALA A 1 610 ? 45.00420 29.30747  -12.80289 1.000 95.42060  ? 489  ALA A O   1 
ATOM   4351 C CB  . ALA A 1 610 ? 42.26781 29.79487  -11.21519 1.000 93.05220  ? 489  ALA A CB  1 
ATOM   4352 N N   . LEU A 1 611 ? 44.18570 31.33698  -13.32274 1.000 78.93299  ? 490  LEU A N   1 
ATOM   4353 C CA  . LEU A 1 611 ? 44.70473 31.32349  -14.68260 1.000 88.87841  ? 490  LEU A CA  1 
ATOM   4354 C C   . LEU A 1 611 ? 46.13621 31.84396  -14.78768 1.000 82.34211  ? 490  LEU A C   1 
ATOM   4355 O O   . LEU A 1 611 ? 46.72497 31.77483  -15.87152 1.000 82.55813  ? 490  LEU A O   1 
ATOM   4356 C CB  . LEU A 1 611 ? 43.78550 32.14061  -15.59683 1.000 75.58641  ? 490  LEU A CB  1 
ATOM   4357 C CG  . LEU A 1 611 ? 42.30177 31.75884  -15.55261 1.000 89.14738  ? 490  LEU A CG  1 
ATOM   4358 C CD1 . LEU A 1 611 ? 41.45353 32.79244  -16.27959 1.000 80.71776  ? 490  LEU A CD1 1 
ATOM   4359 C CD2 . LEU A 1 611 ? 42.08421 30.37865  -16.13972 1.000 92.67022  ? 490  LEU A CD2 1 
ATOM   4360 N N   . ALA A 1 612 ? 46.71406 32.34305  -13.69805 1.000 74.64648  ? 491  ALA A N   1 
ATOM   4361 C CA  . ALA A 1 612 ? 48.06250 32.89202  -13.73890 1.000 93.84717  ? 491  ALA A CA  1 
ATOM   4362 C C   . ALA A 1 612 ? 49.09724 31.78255  -13.58677 1.000 109.40806 ? 491  ALA A C   1 
ATOM   4363 O O   . ALA A 1 612 ? 48.96791 30.91045  -12.72092 1.000 103.68351 ? 491  ALA A O   1 
ATOM   4364 C CB  . ALA A 1 612 ? 48.24295 33.93820  -12.63987 1.000 88.27365  ? 491  ALA A CB  1 
ATOM   4365 N N   . VAL A 1 613 ? 50.12786 31.82603  -14.42662 1.000 118.45903 ? 492  VAL A N   1 
ATOM   4366 C CA  . VAL A 1 613 ? 51.17588 30.81292  -14.42661 1.000 129.69181 ? 492  VAL A CA  1 
ATOM   4367 C C   . VAL A 1 613 ? 52.50972 31.43505  -14.02992 1.000 127.83392 ? 492  VAL A C   1 
ATOM   4368 O O   . VAL A 1 613 ? 53.23295 31.96802  -14.87243 1.000 125.32078 ? 492  VAL A O   1 
ATOM   4369 C CB  . VAL A 1 613 ? 51.28273 30.12415  -15.80202 1.000 134.27360 ? 492  VAL A CB  1 
ATOM   4370 C CG1 . VAL A 1 613 ? 52.30752 29.00093  -15.75757 1.000 131.80780 ? 492  VAL A CG1 1 
ATOM   4371 C CG2 . VAL A 1 613 ? 49.92368 29.59674  -16.24165 1.000 135.84673 ? 492  VAL A CG2 1 
HETATM 4372 N N1  . EPE B 2 .   ? 54.20610 22.92912  -4.30519  1.000 134.47784 ? 1001 EPE A N1  1 
HETATM 4373 C C2  . EPE B 2 .   ? 54.93426 24.07662  -4.87425  1.000 131.06407 ? 1001 EPE A C2  1 
HETATM 4374 C C3  . EPE B 2 .   ? 54.89914 24.03844  -6.39806  1.000 131.07659 ? 1001 EPE A C3  1 
HETATM 4375 N N4  . EPE B 2 .   ? 53.93292 23.07582  -6.89067  1.000 133.18017 ? 1001 EPE A N4  1 
HETATM 4376 C C5  . EPE B 2 .   ? 54.08814 21.71208  -6.42899  1.000 131.86905 ? 1001 EPE A C5  1 
HETATM 4377 C C6  . EPE B 2 .   ? 54.60230 21.68754  -4.99323  1.000 132.71801 ? 1001 EPE A C6  1 
HETATM 4378 C C7  . EPE B 2 .   ? 52.61532 23.52897  -7.29501  1.000 123.78360 ? 1001 EPE A C7  1 
HETATM 4379 C C8  . EPE B 2 .   ? 51.82142 22.42024  -7.97765  1.000 122.52547 ? 1001 EPE A C8  1 
HETATM 4380 O O8  . EPE B 2 .   ? 50.51322 22.87265  -8.23813  1.000 115.03617 ? 1001 EPE A O8  1 
HETATM 4381 C C9  . EPE B 2 .   ? 54.53209 22.80832  -2.87590  1.000 138.43534 ? 1001 EPE A C9  1 
HETATM 4382 C C10 . EPE B 2 .   ? 53.43414 23.41765  -2.01051  1.000 142.28018 ? 1001 EPE A C10 1 
HETATM 4383 S S   . EPE B 2 .   ? 53.86552 23.41495  -0.24710  1.000 146.61914 ? 1001 EPE A S   1 
HETATM 4384 O O1S . EPE B 2 .   ? 55.03451 24.27647  0.02145   1.000 116.17735 ? 1001 EPE A O1S 1 
HETATM 4385 O O2S . EPE B 2 .   ? 54.17051 22.04579  0.16986   1.000 147.24066 ? 1001 EPE A O2S 1 
HETATM 4386 O O3S . EPE B 2 .   ? 52.71092 23.89649  0.51115   1.000 151.07229 ? 1001 EPE A O3S 1 
HETATM 4387 C C   . ACT C 3 .   ? 60.00189 39.80458  -10.64596 1.000 87.60634  ? 1002 ACT A C   1 
HETATM 4388 O O   . ACT C 3 .   ? 58.82334 39.58839  -11.04162 1.000 87.83336  ? 1002 ACT A O   1 
HETATM 4389 O OXT . ACT C 3 .   ? 60.93612 38.97356  -10.45247 1.000 86.90481  ? 1002 ACT A OXT 1 
HETATM 4390 C CH3 . ACT C 3 .   ? 60.36928 41.29873  -10.35047 1.000 78.52912  ? 1002 ACT A CH3 1 
HETATM 4391 O O   . HOH D 4 .   ? 70.94499 53.70360  2.39184   1.000 71.11356  ? 1101 HOH A O   1 
HETATM 4392 O O   . HOH D 4 .   ? 51.21801 33.67859  -6.93666  1.000 68.90264  ? 1102 HOH A O   1 
HETATM 4393 O O   . HOH D 4 .   ? 72.20121 20.24435  -1.11984  1.000 82.53916  ? 1103 HOH A O   1 
HETATM 4394 O O   . HOH D 4 .   ? 37.74883 20.60546  6.63063   1.000 82.86885  ? 1104 HOH A O   1 
HETATM 4395 O O   . HOH D 4 .   ? 82.37963 27.10141  14.62846  1.000 75.78456  ? 1105 HOH A O   1 
HETATM 4396 O O   . HOH D 4 .   ? 74.86514 35.01494  -1.79094  1.000 72.08174  ? 1106 HOH A O   1 
HETATM 4397 O O   . HOH D 4 .   ? 51.32686 21.03014  23.29587  1.000 79.71237  ? 1107 HOH A O   1 
HETATM 4398 O O   . HOH D 4 .   ? 61.88887 37.12440  11.66890  1.000 58.42430  ? 1108 HOH A O   1 
HETATM 4399 O O   . HOH D 4 .   ? 68.32281 24.37971  13.90157  1.000 67.26438  ? 1109 HOH A O   1 
HETATM 4400 O O   . HOH D 4 .   ? 83.51871 33.93540  16.57578  1.000 71.37965  ? 1110 HOH A O   1 
HETATM 4401 O O   . HOH D 4 .   ? 37.44427 35.51679  17.94798  1.000 80.32564  ? 1111 HOH A O   1 
HETATM 4402 O O   . HOH D 4 .   ? 45.54653 46.34487  16.39415  1.000 75.31257  ? 1112 HOH A O   1 
HETATM 4403 O O   . HOH D 4 .   ? 58.43484 28.31021  24.27892  1.000 91.73576  ? 1113 HOH A O   1 
HETATM 4404 O O   . HOH D 4 .   ? 46.90078 1.88398   22.76213  1.000 94.04214  ? 1114 HOH A O   1 
HETATM 4405 O O   . HOH D 4 .   ? 54.81209 32.45790  14.33070  1.000 53.97990  ? 1115 HOH A O   1 
HETATM 4406 O O   . HOH D 4 .   ? 48.50099 20.46048  7.96158   1.000 85.32385  ? 1116 HOH A O   1 
HETATM 4407 O O   . HOH D 4 .   ? 43.29300 35.30246  -0.00001  0.500 75.52120  ? 1117 HOH A O   1 
HETATM 4408 O O   . HOH D 4 .   ? 84.16422 36.05331  -2.61963  1.000 72.19408  ? 1118 HOH A O   1 
HETATM 4409 O O   . HOH D 4 .   ? 52.65550 21.59927  25.67488  1.000 65.79969  ? 1119 HOH A O   1 
HETATM 4410 O O   . HOH D 4 .   ? 45.87428 33.25636  10.55172  1.000 55.54211  ? 1120 HOH A O   1 
HETATM 4411 O O   . HOH D 4 .   ? 27.07639 -13.69465 17.81650  1.000 79.48549  ? 1121 HOH A O   1 
HETATM 4412 O O   . HOH D 4 .   ? 80.40260 34.60337  4.39182   1.000 64.94871  ? 1122 HOH A O   1 
HETATM 4413 O O   . HOH D 4 .   ? 57.17706 41.24398  16.96497  1.000 62.61068  ? 1123 HOH A O   1 
HETATM 4414 O O   . HOH D 4 .   ? 69.33136 38.40708  24.61531  1.000 61.49920  ? 1124 HOH A O   1 
HETATM 4415 O O   . HOH D 4 .   ? 62.97768 41.21188  21.86593  1.000 53.50729  ? 1125 HOH A O   1 
HETATM 4416 O O   . HOH D 4 .   ? 52.01922 17.74516  30.80442  1.000 62.01966  ? 1126 HOH A O   1 
HETATM 4417 O O   . HOH D 4 .   ? 65.82186 36.95665  -9.86909  1.000 63.99403  ? 1127 HOH A O   1 
HETATM 4418 O O   . HOH D 4 .   ? 43.351   33.827    -12.872   1.000 63.77952  ? 1128 HOH A O   1 
HETATM 4419 O O   . HOH D 4 .   ? 42.80808 35.94847  -5.93742  1.000 73.56361  ? 1129 HOH A O   1 
HETATM 4420 O O   . HOH D 4 .   ? 42.00663 6.76507   39.58197  1.000 94.61901  ? 1130 HOH A O   1 
HETATM 4421 O O   . HOH D 4 .   ? 67.05706 16.17739  7.07473   1.000 89.48839  ? 1131 HOH A O   1 
HETATM 4422 O O   . HOH D 4 .   ? 71.56676 39.50995  16.50218  1.000 56.03754  ? 1132 HOH A O   1 
HETATM 4423 O O   . HOH D 4 .   ? 63.97743 32.53920  7.28312   1.000 47.60617  ? 1133 HOH A O   1 
HETATM 4424 O O   . HOH D 4 .   ? 48.96598 33.18572  11.22508  1.000 55.84509  ? 1134 HOH A O   1 
HETATM 4425 O O   . HOH D 4 .   ? 77.63526 34.37951  5.01085   1.000 46.62908  ? 1135 HOH A O   1 
HETATM 4426 O O   . HOH D 4 .   ? 27.05625 28.86576  32.69334  1.000 89.98037  ? 1136 HOH A O   1 
HETATM 4427 O O   . HOH D 4 .   ? 63.63412 32.90680  25.47979  1.000 70.59445  ? 1137 HOH A O   1 
HETATM 4428 O O   . HOH D 4 .   ? 59.78920 37.57557  8.55955   1.000 50.26231  ? 1138 HOH A O   1 
HETATM 4429 O O   . HOH D 4 .   ? 23.024   -15.018   22.310    1.000 92.34957  ? 1139 HOH A O   1 
HETATM 4430 O O   . HOH D 4 .   ? 33.78359 32.66247  26.79006  1.000 94.43573  ? 1140 HOH A O   1 
HETATM 4431 O O   . HOH D 4 .   ? 77.18564 30.33911  -3.01274  1.000 91.67960  ? 1141 HOH A O   1 
HETATM 4432 O O   . HOH D 4 .   ? 67.58187 34.42195  16.85378  1.000 46.01152  ? 1142 HOH A O   1 
HETATM 4433 O O   . HOH D 4 .   ? 83.50110 43.61206  2.32319   1.000 68.04397  ? 1143 HOH A O   1 
HETATM 4434 O O   . HOH D 4 .   ? 60.46337 16.22041  18.00981  1.000 61.04993  ? 1144 HOH A O   1 
HETATM 4435 O O   . HOH D 4 .   ? 70.16552 52.37094  4.36860   1.000 71.86328  ? 1145 HOH A O   1 
HETATM 4436 O O   . HOH D 4 .   ? 58.30826 41.89848  21.10870  1.000 69.52492  ? 1146 HOH A O   1 
HETATM 4437 O O   . HOH D 4 .   ? 56.01323 43.63021  0.10403   1.000 68.38884  ? 1147 HOH A O   1 
HETATM 4438 O O   . HOH D 4 .   ? 53.66890 35.04984  -10.30283 1.000 101.13291 ? 1148 HOH A O   1 
HETATM 4439 O O   . HOH D 4 .   ? 68.40507 49.86609  16.68581  1.000 87.61837  ? 1149 HOH A O   1 
HETATM 4440 O O   . HOH D 4 .   ? 56.31331 26.96935  3.76093   1.000 56.78613  ? 1150 HOH A O   1 
HETATM 4441 O O   . HOH D 4 .   ? 48.01227 43.76944  7.66915   1.000 52.12753  ? 1151 HOH A O   1 
HETATM 4442 O O   . HOH D 4 .   ? 55.00511 30.47238  -7.60858  1.000 64.29846  ? 1152 HOH A O   1 
HETATM 4443 O O   . HOH D 4 .   ? 21.40474 -2.60452  0.77323   1.000 97.76393  ? 1153 HOH A O   1 
HETATM 4444 O O   . HOH D 4 .   ? 68.97823 26.26115  15.82840  1.000 67.42274  ? 1154 HOH A O   1 
HETATM 4445 O O   . HOH D 4 .   ? 79.83021 47.21928  -5.47203  1.000 73.74301  ? 1155 HOH A O   1 
HETATM 4446 O O   . HOH D 4 .   ? 68.46359 35.73540  14.40406  1.000 48.87031  ? 1156 HOH A O   1 
HETATM 4447 O O   . HOH D 4 .   ? 77.47991 29.47950  4.90545   1.000 68.75640  ? 1157 HOH A O   1 
HETATM 4448 O O   . HOH D 4 .   ? 36.31889 44.21174  34.03027  1.000 84.89832  ? 1158 HOH A O   1 
HETATM 4449 O O   . HOH D 4 .   ? 24.55408 16.79613  10.52467  1.000 101.52948 ? 1159 HOH A O   1 
HETATM 4450 O O   . HOH D 4 .   ? 74.78630 30.81812  16.55044  1.000 73.92183  ? 1160 HOH A O   1 
HETATM 4451 O O   . HOH D 4 .   ? 47.79028 30.72768  8.02563   1.000 96.02061  ? 1161 HOH A O   1 
HETATM 4452 O O   . HOH D 4 .   ? 45.03548 44.08243  17.94897  1.000 65.10663  ? 1162 HOH A O   1 
HETATM 4453 O O   . HOH D 4 .   ? 46.60210 17.94849  17.85179  1.000 69.89567  ? 1163 HOH A O   1 
HETATM 4454 O O   . HOH D 4 .   ? 42.17415 28.29115  3.11468   1.000 91.05653  ? 1164 HOH A O   1 
HETATM 4455 O O   . HOH D 4 .   ? 37.40485 35.96459  32.22107  1.000 81.83897  ? 1165 HOH A O   1 
HETATM 4456 O O   . HOH D 4 .   ? 65.05351 28.85776  21.54994  1.000 69.45382  ? 1166 HOH A O   1 
HETATM 4457 O O   . HOH D 4 .   ? 38.66349 25.43410  17.54220  1.000 98.22114  ? 1167 HOH A O   1 
HETATM 4458 O O   . HOH D 4 .   ? 55.88050 47.95663  16.12445  1.000 63.21026  ? 1168 HOH A O   1 
HETATM 4459 O O   . HOH D 4 .   ? 64.61491 37.35521  16.42874  1.000 52.99971  ? 1169 HOH A O   1 
HETATM 4460 O O   . HOH D 4 .   ? 39.45227 41.95304  16.07803  1.000 87.34971  ? 1170 HOH A O   1 
HETATM 4461 O O   . HOH D 4 .   ? 47.26788 42.45783  1.30517   1.000 87.85973  ? 1171 HOH A O   1 
HETATM 4462 O O   . HOH D 4 .   ? 73.79314 26.40731  9.57971   1.000 72.90814  ? 1172 HOH A O   1 
HETATM 4463 O O   . HOH D 4 .   ? 55.38049 46.35234  3.02867   1.000 102.02152 ? 1173 HOH A O   1 
HETATM 4464 O O   . HOH D 4 .   ? 18.61379 -14.34156 14.77898  1.000 86.14145  ? 1174 HOH A O   1 
HETATM 4465 O O   . HOH D 4 .   ? 46.29882 16.53461  13.79417  1.000 75.13739  ? 1175 HOH A O   1 
HETATM 4466 O O   . HOH D 4 .   ? 44.41607 41.21278  25.34102  1.000 63.41891  ? 1176 HOH A O   1 
HETATM 4467 O O   . HOH D 4 .   ? 47.51152 43.36533  27.85708  1.000 87.30260  ? 1177 HOH A O   1 
HETATM 4468 O O   . HOH D 4 .   ? 65.06987 35.40604  17.66209  1.000 71.83434  ? 1178 HOH A O   1 
HETATM 4469 O O   . HOH D 4 .   ? 65.77959 16.88898  38.95491  1.000 102.91396 ? 1179 HOH A O   1 
HETATM 4470 O O   . HOH D 4 .   ? 55.37275 23.55941  -9.56870  1.000 83.29890  ? 1180 HOH A O   1 
HETATM 4471 O O   . HOH D 4 .   ? 47.24066 5.38601   13.61183  1.000 88.19352  ? 1181 HOH A O   1 
HETATM 4472 O O   . HOH D 4 .   ? 58.81520 40.50029  24.36450  1.000 80.05936  ? 1182 HOH A O   1 
HETATM 4473 O O   . HOH D 4 .   ? 63.14776 47.85101  17.89788  1.000 80.16713  ? 1183 HOH A O   1 
HETATM 4474 O O   . HOH D 4 .   ? 55.48409 27.80213  21.84410  1.000 73.38946  ? 1184 HOH A O   1 
HETATM 4475 O O   . HOH D 4 .   ? 57.32641 36.20363  11.85367  1.000 53.71842  ? 1185 HOH A O   1 
HETATM 4476 O O   . HOH D 4 .   ? 51.12024 6.71758   25.57506  1.000 96.41200  ? 1186 HOH A O   1 
HETATM 4477 O O   . HOH D 4 .   ? 84.16787 28.23156  6.40465   1.000 83.08537  ? 1187 HOH A O   1 
HETATM 4478 O O   . HOH D 4 .   ? 53.54799 45.73091  14.52638  1.000 74.75605  ? 1188 HOH A O   1 
HETATM 4479 O O   . HOH D 4 .   ? 64.99688 30.73077  22.93197  1.000 61.11612  ? 1189 HOH A O   1 
HETATM 4480 O O   . HOH D 4 .   ? 38.61726 -3.72225  23.95666  1.000 98.62532  ? 1190 HOH A O   1 
HETATM 4481 O O   . HOH D 4 .   ? 48.82279 29.88321  4.96489   1.000 63.00870  ? 1191 HOH A O   1 
HETATM 4482 O O   . HOH D 4 .   ? 65.20168 43.75214  -7.86417  1.000 81.67513  ? 1192 HOH A O   1 
HETATM 4483 O O   . HOH D 4 .   ? 86.09000 49.09351  7.35687   1.000 90.13343  ? 1193 HOH A O   1 
HETATM 4484 O O   . HOH D 4 .   ? 69.50968 16.65094  -1.47230  1.000 84.69065  ? 1194 HOH A O   1 
HETATM 4485 O O   . HOH D 4 .   ? 86.93588 45.45546  2.82917   1.000 85.19826  ? 1195 HOH A O   1 
HETATM 4486 O O   . HOH D 4 .   ? 30.26550 29.24169  32.88418  1.000 92.20253  ? 1196 HOH A O   1 
HETATM 4487 O O   . HOH D 4 .   ? 59.66048 45.38598  22.82848  1.000 83.11038  ? 1197 HOH A O   1 
HETATM 4488 O O   . HOH D 4 .   ? 77.28891 25.74254  2.22796   1.000 75.61075  ? 1198 HOH A O   1 
HETATM 4489 O O   . HOH D 4 .   ? 80.13655 32.75310  1.88660   1.000 98.82011  ? 1199 HOH A O   1 
HETATM 4490 O O   . HOH D 4 .   ? 86.47055 37.27558  1.29762   1.000 73.94926  ? 1200 HOH A O   1 
HETATM 4491 O O   . HOH D 4 .   ? 52.99122 26.30507  23.51856  1.000 87.90040  ? 1201 HOH A O   1 
HETATM 4492 O O   . HOH D 4 .   ? 42.94434 2.98400   39.67457  1.000 92.87181  ? 1202 HOH A O   1 
HETATM 4493 O O   . HOH D 4 .   ? 76.14563 42.34343  29.14636  1.000 84.65994  ? 1203 HOH A O   1 
HETATM 4494 O O   . HOH D 4 .   ? 75.73110 44.31406  -8.73210  1.000 87.89066  ? 1204 HOH A O   1 
HETATM 4495 O O   . HOH D 4 .   ? 82.12726 44.52700  -6.13338  1.000 81.98724  ? 1205 HOH A O   1 
HETATM 4496 O O   . HOH D 4 .   ? 40.15864 41.70931  -6.03260  1.000 62.32443  ? 1206 HOH A O   1 
HETATM 4497 O O   . HOH D 4 .   ? 38.30461 1.23087   18.90352  1.000 82.96430  ? 1207 HOH A O   1 
HETATM 4498 O O   . HOH D 4 .   ? 49.14778 27.98162  3.40895   1.000 75.60234  ? 1208 HOH A O   1 
HETATM 4499 O O   . HOH D 4 .   ? 30.85900 29.18548  20.91102  1.000 95.47496  ? 1209 HOH A O   1 
HETATM 4500 O O   . HOH D 4 .   ? 73.88733 27.59192  -4.04319  1.000 80.04543  ? 1210 HOH A O   1 
HETATM 4501 O O   . HOH D 4 .   ? 55.27794 48.73307  13.42316  1.000 85.02820  ? 1211 HOH A O   1 
HETATM 4502 O O   . HOH D 4 .   ? 75.27990 24.46029  7.36441   1.000 93.31060  ? 1212 HOH A O   1 
HETATM 4503 O O   . HOH D 4 .   ? 55.85117 46.51840  22.60059  1.000 78.30938  ? 1213 HOH A O   1 
HETATM 4504 O O   . HOH D 4 .   ? 46.72923 46.56042  24.04906  1.000 106.46250 ? 1214 HOH A O   1 
HETATM 4505 O O   . HOH D 4 .   ? 68.84795 53.22761  7.29206   1.000 79.28579  ? 1215 HOH A O   1 
HETATM 4506 O O   . HOH D 4 .   ? 45.42592 28.51874  52.16534  1.000 89.95557  ? 1216 HOH A O   1 
HETATM 4507 O O   . HOH D 4 .   ? 71.94690 1.45231   42.84541  1.000 100.73828 ? 1217 HOH A O   1 
HETATM 4508 O O   . HOH D 4 .   ? 73.38008 50.55098  15.11724  1.000 94.93232  ? 1218 HOH A O   1 
HETATM 4509 O O   . HOH D 4 .   ? 61.65566 30.23332  23.31942  1.000 58.94084  ? 1219 HOH A O   1 
HETATM 4510 O O   . HOH D 4 .   ? 39.37092 10.62463  19.24617  1.000 97.93909  ? 1220 HOH A O   1 
HETATM 4511 O O   . HOH D 4 .   ? 71.13825 53.38291  -4.00052  1.000 80.41027  ? 1221 HOH A O   1 
HETATM 4512 O O   . HOH D 4 .   ? 52.23500 26.02045  -3.50623  1.000 86.60902  ? 1222 HOH A O   1 
HETATM 4513 O O   . HOH D 4 .   ? 25.28428 14.62894  30.07606  1.000 93.50199  ? 1223 HOH A O   1 
HETATM 4514 O O   . HOH D 4 .   ? 63.77825 19.94189  22.77867  1.000 88.02965  ? 1224 HOH A O   1 
HETATM 4515 O O   . HOH D 4 .   ? 35.56632 7.58452   27.39435  1.000 94.26490  ? 1225 HOH A O   1 
HETATM 4516 O O   . HOH D 4 .   ? 68.60386 26.10151  -8.43986  1.000 86.14994  ? 1226 HOH A O   1 
HETATM 4517 O O   . HOH D 4 .   ? 86.58500 39.42541  -0.00000  0.500 76.04271  ? 1227 HOH A O   1 
HETATM 4518 O O   . HOH D 4 .   ? 78.69026 55.22409  6.52429   1.000 70.89767  ? 1228 HOH A O   1 
HETATM 4519 O O   . HOH D 4 .   ? 61.03906 38.59086  24.39573  1.000 74.03947  ? 1229 HOH A O   1 
HETATM 4520 O O   . HOH D 4 .   ? 50.92790 44.52871  28.09207  1.000 101.01893 ? 1230 HOH A O   1 
HETATM 4521 O O   . HOH D 4 .   ? 61.08970 53.68476  7.53700   1.000 78.17408  ? 1231 HOH A O   1 
HETATM 4522 O O   . HOH D 4 .   ? 49.63592 11.68823  44.45400  1.000 90.12998  ? 1232 HOH A O   1 
HETATM 4523 O O   . HOH D 4 .   ? 42.35891 48.31686  23.64537  1.000 92.17371  ? 1233 HOH A O   1 
HETATM 4524 O O   . HOH D 4 .   ? 19.92997 -6.04573  3.31012   1.000 90.43707  ? 1234 HOH A O   1 
HETATM 4525 O O   . HOH D 4 .   ? 10.68910 -6.38603  9.79673   1.000 89.20664  ? 1235 HOH A O   1 
HETATM 4526 O O   . HOH D 4 .   ? 87.86664 30.50483  12.84641  1.000 84.21481  ? 1236 HOH A O   1 
HETATM 4527 O O   . HOH D 4 .   ? 55.09445 21.60525  12.77259  1.000 74.81684  ? 1237 HOH A O   1 
HETATM 4528 O O   . HOH D 4 .   ? 72.62405 54.10531  12.02464  1.000 85.90344  ? 1238 HOH A O   1 
HETATM 4529 O O   . HOH D 4 .   ? 19.41931 -15.29561 18.86337  1.000 104.42456 ? 1239 HOH A O   1 
HETATM 4530 O O   . HOH D 4 .   ? 57.29680 21.28380  28.45907  1.000 92.37414  ? 1240 HOH A O   1 
HETATM 4531 O O   . HOH D 4 .   ? 37.75136 44.97782  41.33253  1.000 92.95516  ? 1241 HOH A O   1 
HETATM 4532 O O   . HOH D 4 .   ? 60.44510 44.96779  -7.65938  1.000 99.49343  ? 1242 HOH A O   1 
HETATM 4533 O O   . HOH D 4 .   ? 73.76761 35.58792  27.91146  1.000 98.13071  ? 1243 HOH A O   1 
HETATM 4534 O O   . HOH D 4 .   ? 84.68450 45.01423  0.15362   1.000 85.62684  ? 1244 HOH A O   1 
HETATM 4535 O O   . HOH D 4 .   ? 60.20959 26.78438  49.23232  1.000 92.90635  ? 1245 HOH A O   1 
HETATM 4536 O O   . HOH D 4 .   ? 83.48862 49.90032  19.58959  1.000 92.31329  ? 1246 HOH A O   1 
HETATM 4537 O O   . HOH D 4 .   ? 22.47570 0.00000   -0.00000  0.500 75.41685  ? 1247 HOH A O   1 
HETATM 4538 O O   . HOH D 4 .   ? 46.25816 43.34253  9.91102   1.000 74.03664  ? 1248 HOH A O   1 
HETATM 4539 O O   . HOH D 4 .   ? 77.08452 32.01742  3.56304   1.000 65.79375  ? 1249 HOH A O   1 
HETATM 4540 O O   . HOH D 4 .   ? 52.44850 44.17865  0.27075   1.000 85.24277  ? 1250 HOH A O   1 
HETATM 4541 O O   . HOH D 4 .   ? 59.19205 38.05094  11.21855  1.000 54.24880  ? 1251 HOH A O   1 
HETATM 4542 O O   . HOH D 4 .   ? 46.13227 44.94167  26.33192  1.000 93.56070  ? 1252 HOH A O   1 
HETATM 4543 O O   . HOH D 4 .   ? 56.72007 45.67398  -11.41684 1.000 93.27653  ? 1253 HOH A O   1 
HETATM 4544 O O   . HOH D 4 .   ? 79.98985 49.83538  -6.13141  1.000 84.48978  ? 1254 HOH A O   1 
HETATM 4545 O O   . HOH D 4 .   ? 64.86743 40.14947  26.36206  1.000 95.60331  ? 1255 HOH A O   1 
HETATM 4546 O O   . HOH D 4 .   ? 68.83147 38.67202  27.55291  1.000 92.50696  ? 1256 HOH A O   1 
HETATM 4547 O O   . HOH D 4 .   ? 86.73499 28.73837  4.21757   1.000 99.69021  ? 1257 HOH A O   1 
HETATM 4548 O O   . HOH D 4 .   ? 46.34688 25.63859  -11.31674 1.000 79.15842  ? 1258 HOH A O   1 
HETATM 4549 O O   . HOH D 4 .   ? 41.68065 45.12681  17.77102  1.000 79.94267  ? 1259 HOH A O   1 
HETATM 4550 O O   . HOH D 4 .   ? 49.66383 20.47376  -2.42778  1.000 96.07761  ? 1260 HOH A O   1 
HETATM 4551 O O   . HOH D 4 .   ? 49.39469 8.00062   5.94615   1.000 103.79274 ? 1261 HOH A O   1 
HETATM 4552 O O   . HOH D 4 .   ? 38.61679 25.08912  1.80517   1.000 76.84152  ? 1262 HOH A O   1 
HETATM 4553 O O   . HOH D 4 .   ? 64.62751 47.33266  -10.54272 1.000 87.59162  ? 1263 HOH A O   1 
HETATM 4554 O O   . HOH D 4 .   ? 36.34829 40.21385  15.33929  1.000 71.09170  ? 1264 HOH A O   1 
HETATM 4555 O O   . HOH D 4 .   ? 62.86688 52.46965  13.00201  1.000 87.79650  ? 1265 HOH A O   1 
HETATM 4556 O O   . HOH D 4 .   ? 79.59272 36.61397  -8.90379  1.000 92.31965  ? 1266 HOH A O   1 
HETATM 4557 O O   . HOH D 4 .   ? 69.58121 24.27936  18.38273  1.000 67.91968  ? 1267 HOH A O   1 
HETATM 4558 O O   . HOH D 4 .   ? 79.50768 29.01496  -0.17524  1.000 83.94823  ? 1268 HOH A O   1 
HETATM 4559 O O   . HOH D 4 .   ? 66.74975 16.92424  9.99900   1.000 72.56231  ? 1269 HOH A O   1 
HETATM 4560 O O   . HOH D 4 .   ? 15.21410 -14.32514 19.97648  1.000 100.19871 ? 1270 HOH A O   1 
HETATM 4561 O O   . HOH D 4 .   ? 57.15130 53.64492  12.71098  1.000 89.60279  ? 1271 HOH A O   1 
HETATM 4562 O O   . HOH D 4 .   ? 57.17087 31.64990  -16.94555 1.000 93.22759  ? 1272 HOH A O   1 
HETATM 4563 O O   . HOH D 4 .   ? 55.66762 32.10053  -18.65103 1.000 89.69306  ? 1273 HOH A O   1 
HETATM 4564 O O   . HOH D 4 .   ? 30.145   40.861    45.453    1.000 107.64591 ? 1274 HOH A O   1 
HETATM 4565 O O   . HOH D 4 .   ? 67.17517 14.26451  -12.52526 1.000 86.53462  ? 1275 HOH A O   1 
HETATM 4566 O O   . HOH D 4 .   ? 41.074   21.269    1.468     1.000 104.55753 ? 1276 HOH A O   1 
HETATM 4567 O O   . HOH D 4 .   ? 88.43935 33.67715  4.99778   1.000 87.67212  ? 1277 HOH A O   1 
HETATM 4568 O O   . HOH D 4 .   ? 34.52935 25.71832  16.49155  1.000 98.19103  ? 1278 HOH A O   1 
HETATM 4569 O O   . HOH D 4 .   ? 65.61736 13.10408  47.90404  1.000 80.24146  ? 1279 HOH A O   1 
HETATM 4570 O O   . HOH D 4 .   ? 65.38837 23.95954  52.62013  1.000 92.05876  ? 1280 HOH A O   1 
HETATM 4571 O O   . HOH D 4 .   ? 51.24257 47.23207  4.29355   1.000 80.80026  ? 1281 HOH A O   1 
HETATM 4572 O O   . HOH D 4 .   ? 79.52053 55.67457  12.29275  1.000 96.80860  ? 1282 HOH A O   1 
HETATM 4573 O O   . HOH D 4 .   ? 55.82249 47.96515  25.58886  1.000 97.57695  ? 1283 HOH A O   1 
HETATM 4574 O O   . HOH D 4 .   ? 79.46652 52.87418  19.71895  1.000 95.89731  ? 1284 HOH A O   1 
HETATM 4575 O O   . HOH D 4 .   ? 43.29001 9.22746   7.93638   1.000 91.14891  ? 1285 HOH A O   1 
HETATM 4576 O O   . HOH D 4 .   ? 30.74759 26.77041  17.17511  1.000 89.93249  ? 1286 HOH A O   1 
HETATM 4577 O O   . HOH D 4 .   ? 50.33992 26.42872  -14.10133 1.000 99.77384  ? 1287 HOH A O   1 
HETATM 4578 O O   . HOH D 4 .   ? 21.60473 -14.56068 8.64044   1.000 95.13572  ? 1288 HOH A O   1 
HETATM 4579 O O   . HOH D 4 .   ? 64.08046 30.39103  47.47891  1.000 74.97757  ? 1289 HOH A O   1 
HETATM 4580 O O   . HOH D 4 .   ? 62.88155 29.06908  -16.23364 1.000 83.04335  ? 1290 HOH A O   1 
HETATM 4581 O O   . HOH D 4 .   ? 37.85021 48.05269  36.14095  1.000 102.54715 ? 1291 HOH A O   1 
HETATM 4582 O O   . HOH D 4 .   ? 57.51203 38.05988  -15.89556 1.000 98.70631  ? 1292 HOH A O   1 
HETATM 4583 O O   . HOH D 4 .   ? 47.24770 46.52346  5.03680   1.000 71.01849  ? 1293 HOH A O   1 
HETATM 4584 O O   . HOH D 4 .   ? 68.21163 42.36410  -18.72870 1.000 96.16915  ? 1294 HOH A O   1 
HETATM 4585 O O   . HOH D 4 .   ? 45.07652 37.96057  43.80550  1.000 95.81260  ? 1295 HOH A O   1 
HETATM 4586 O O   . HOH D 4 .   ? 16.86543 7.70940   5.11935   1.000 93.98713  ? 1296 HOH A O   1 
HETATM 4587 O O   . HOH D 4 .   ? 70.06991 19.14191  24.21926  1.000 84.65764  ? 1297 HOH A O   1 
HETATM 4588 O O   . HOH D 4 .   ? 73.98440 16.14127  10.25252  1.000 85.79455  ? 1298 HOH A O   1 
HETATM 4589 O O   . HOH D 4 .   ? 80.48274 43.88685  -8.81722  1.000 85.69913  ? 1299 HOH A O   1 
HETATM 4590 O O   . HOH D 4 .   ? 67.27965 19.18762  42.15469  1.000 83.08806  ? 1300 HOH A O   1 
HETATM 4591 O O   . HOH D 4 .   ? 80.36776 28.15322  -3.59050  1.000 106.49268 ? 1301 HOH A O   1 
HETATM 4592 O O   . HOH D 4 .   ? 69.75687 47.17044  28.17869  1.000 96.73702  ? 1302 HOH A O   1 
HETATM 4593 O O   . HOH D 4 .   ? 67.27271 45.69508  -15.15599 1.000 93.07454  ? 1303 HOH A O   1 
HETATM 4594 O O   . HOH D 4 .   ? 43.29306 44.73215  0.00002   0.500 88.44964  ? 1304 HOH A O   1 
HETATM 4595 O O   . HOH D 4 .   ? 53.90140 40.98734  -15.50190 1.000 93.03674  ? 1305 HOH A O   1 
HETATM 4596 O O   . HOH D 4 .   ? 49.18994 50.85179  7.12451   1.000 102.21077 ? 1306 HOH A O   1 
HETATM 4597 O O   . HOH D 4 .   ? 8.41976  -13.07911 15.04492  1.000 93.13216  ? 1307 HOH A O   1 
HETATM 4598 O O   . HOH D 4 .   ? 59.64461 32.72621  -17.94054 1.000 87.10360  ? 1308 HOH A O   1 
HETATM 4599 O O   . HOH D 4 .   ? 83.32861 27.28569  -0.29309  1.000 78.24519  ? 1309 HOH A O   1 
HETATM 4600 O O   . HOH D 4 .   ? 44.61015 46.37953  1.61324   1.000 84.79683  ? 1310 HOH A O   1 
HETATM 4601 O O   . HOH D 4 .   ? 38.75482 -0.32500  3.01523   1.000 84.16744  ? 1311 HOH A O   1 
HETATM 4602 O O   . HOH D 4 .   ? 42.76331 41.01793  49.08745  1.000 87.96195  ? 1312 HOH A O   1 
HETATM 4603 O O   . HOH D 4 .   ? 4.62681  3.85196   26.92755  1.000 94.51908  ? 1313 HOH A O   1 
HETATM 4604 O O   . HOH D 4 .   ? 68.67212 10.56662  49.46492  1.000 87.84180  ? 1314 HOH A O   1 
HETATM 4605 O O   . HOH D 4 .   ? 77.02333 0.55604   35.20473  1.000 88.31477  ? 1315 HOH A O   1 
HETATM 4606 O O   . HOH D 4 .   ? 64.56583 48.23465  26.17637  1.000 96.49056  ? 1316 HOH A O   1 
HETATM 4607 O O   . HOH D 4 .   ? 79.72727 27.75592  -7.15347  1.000 85.89427  ? 1317 HOH A O   1 
HETATM 4608 O O   . HOH D 4 .   ? 40.31114 6.66672   3.79023   1.000 100.91407 ? 1318 HOH A O   1 
HETATM 4609 O O   . HOH D 4 .   ? 79.06973 23.53286  -5.22360  1.000 105.69159 ? 1319 HOH A O   1 
HETATM 4610 O O   . HOH D 4 .   ? 70.79729 4.76983   50.35445  1.000 94.58415  ? 1320 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . THR A 43  ? 1.33474 1.18386 1.32837 -0.11945 -0.10136 0.08699  -78 THR A N   
2    C CA  . THR A 43  ? 1.45802 1.26218 1.44203 -0.12482 -0.09614 0.08958  -78 THR A CA  
3    C C   . THR A 43  ? 1.37983 1.17309 1.41664 -0.11373 -0.08328 0.06110  -78 THR A C   
4    O O   . THR A 43  ? 1.26857 1.04043 1.34391 -0.09771 -0.07432 0.06020  -78 THR A O   
5    C CB  . THR A 43  ? 1.51599 1.26498 1.47706 -0.12301 -0.09488 0.12422  -78 THR A CB  
6    O OG1 . THR A 43  ? 1.51708 1.22023 1.49199 -0.12064 -0.08486 0.12086  -78 THR A OG1 
7    C CG2 . THR A 43  ? 1.51359 1.25552 1.49800 -0.10728 -0.09203 0.13733  -78 THR A CG2 
8    N N   . HIS A 44  ? 1.37753 1.18527 1.41542 -0.12253 -0.08282 0.03786  -77 HIS A N   
9    C CA  . HIS A 44  ? 1.29448 1.10343 1.38199 -0.11373 -0.07221 0.00635  -77 HIS A CA  
10   C C   . HIS A 44  ? 1.19336 0.95436 1.28077 -0.11660 -0.06483 0.00762  -77 HIS A C   
11   O O   . HIS A 44  ? 1.15983 0.89184 1.20653 -0.12668 -0.06870 0.03025  -77 HIS A O   
12   C CB  . HIS A 44  ? 1.35050 1.21431 1.44448 -0.12069 -0.07649 -0.02418 -77 HIS A CB  
13   C CG  . HIS A 44  ? 1.43214 1.34574 1.53887 -0.11499 -0.08107 -0.03204 -77 HIS A CG  
14   N ND1 . HIS A 44  ? 1.48415 1.39444 1.59527 -0.10454 -0.08195 -0.01289 -77 HIS A ND1 
15   C CD2 . HIS A 44  ? 1.41299 1.38158 1.52936 -0.11817 -0.08497 -0.05723 -77 HIS A CD2 
16   C CE1 . HIS A 44  ? 1.43715 1.39897 1.56038 -0.10132 -0.08622 -0.02602 -77 HIS A CE1 
17   N NE2 . HIS A 44  ? 1.44822 1.44633 1.57481 -0.10953 -0.08794 -0.05299 -77 HIS A NE2 
18   N N   . ILE A 45  ? 1.22008 0.97358 1.35402 -0.10752 -0.05415 -0.01756 -76 ILE A N   
19   C CA  . ILE A 45  ? 1.12994 0.83909 1.27308 -0.10812 -0.04540 -0.01955 -76 ILE A CA  
20   C C   . ILE A 45  ? 1.12678 0.85637 1.30553 -0.10737 -0.03987 -0.05642 -76 ILE A C   
21   O O   . ILE A 45  ? 1.08996 0.85313 1.30353 -0.09880 -0.03802 -0.07915 -76 ILE A O   
22   C CB  . ILE A 45  ? 1.17207 0.83261 1.33974 -0.09408 -0.03555 -0.00364 -76 ILE A CB  
23   C CG1 . ILE A 45  ? 1.38846 1.01637 1.51250 -0.09877 -0.04034 0.03469  -76 ILE A CG1 
24   C CG2 . ILE A 45  ? 1.19248 0.81807 1.39118 -0.09039 -0.02372 -0.01763 -76 ILE A CG2 
25   C CD1 . ILE A 45  ? 1.33182 0.94233 1.41076 -0.11473 -0.04498 0.04628  -76 ILE A CD1 
26   N N   . ASN A 46  ? 1.15921 0.86908 1.32878 -0.11631 -0.03747 -0.06250 -75 ASN A N   
27   C CA  . ASN A 46  ? 1.13225 0.85509 1.33451 -0.11625 -0.03171 -0.09604 -75 ASN A CA  
28   C C   . ASN A 46  ? 1.16772 0.84580 1.40863 -0.10566 -0.01828 -0.09996 -75 ASN A C   
29   O O   . ASN A 46  ? 1.33097 0.96390 1.55764 -0.10603 -0.01481 -0.07681 -75 ASN A O   
30   C CB  . ASN A 46  ? 1.01496 0.74693 1.18265 -0.13336 -0.03824 -0.10184 -75 ASN A CB  
31   C CG  . ASN A 46  ? 1.09972 0.86946 1.22185 -0.14579 -0.05238 -0.09313 -75 ASN A CG  
32   O OD1 . ASN A 46  ? 1.05131 0.86131 1.18065 -0.14274 -0.05672 -0.10055 -75 ASN A OD1 
33   N ND2 . ASN A 46  ? 1.03226 0.78917 1.10674 -0.15996 -0.05982 -0.07726 -75 ASN A ND2 
34   N N   . LEU A 47  ? 1.19972 0.89032 1.48911 -0.09645 -0.01082 -0.12927 -74 LEU A N   
35   C CA  . LEU A 47  ? 1.09677 0.74776 1.42686 -0.08591 0.00191  -0.13551 -74 LEU A CA  
36   C C   . LEU A 47  ? 1.15861 0.82186 1.51941 -0.08752 0.00715  -0.16956 -74 LEU A C   
37   O O   . LEU A 47  ? 1.09458 0.80130 1.47090 -0.08688 0.00425  -0.19470 -74 LEU A O   
38   C CB  . LEU A 47  ? 1.17962 0.82539 1.54580 -0.06843 0.00703  -0.13409 -74 LEU A CB  
39   C CG  . LEU A 47  ? 1.22121 0.85077 1.56417 -0.06426 0.00318  -0.10072 -74 LEU A CG  
40   C CD1 . LEU A 47  ? 1.11734 0.74964 1.49981 -0.04652 0.00741  -0.10530 -74 LEU A CD1 
41   C CD2 . LEU A 47  ? 1.20047 0.77512 1.52322 -0.06758 0.00737  -0.07349 -74 LEU A CD2 
42   N N   . LYS A 48  ? 1.20079 0.82627 1.57050 -0.08963 0.01490  -0.17041 -73 LYS A N   
43   C CA  . LYS A 48  ? 1.22345 0.85316 1.63000 -0.08861 0.02186  -0.20196 -73 LYS A CA  
44   C C   . LYS A 48  ? 1.25515 0.87101 1.71455 -0.07204 0.03187  -0.21421 -73 LYS A C   
45   O O   . LYS A 48  ? 1.38300 0.96525 1.84982 -0.06301 0.03650  -0.19421 -73 LYS A O   
46   C CB  . LYS A 48  ? 1.24629 0.84161 1.64222 -0.09758 0.02622  -0.19831 -73 LYS A CB  
47   C CG  . LYS A 48  ? 1.23093 0.83818 1.57705 -0.11391 0.01650  -0.18996 -73 LYS A CG  
48   C CD  . LYS A 48  ? 1.16541 0.75345 1.51334 -0.12191 0.02090  -0.20075 -73 LYS A CD  
49   C CE  . LYS A 48  ? 1.15694 0.69105 1.50050 -0.12038 0.02843  -0.17746 -73 LYS A CE  
50   N NZ  . LYS A 48  ? 1.21875 0.73886 1.51114 -0.12689 0.02093  -0.14401 -73 LYS A NZ  
51   N N   . VAL A 49  ? 1.10944 0.75089 1.60498 -0.06803 0.03486  -0.24720 -72 VAL A N   
52   C CA  . VAL A 49  ? 1.22675 0.84833 1.77415 -0.05449 0.04552  -0.26321 -72 VAL A CA  
53   C C   . VAL A 49  ? 1.26436 0.88324 1.83252 -0.06010 0.05093  -0.28925 -72 VAL A C   
54   O O   . VAL A 49  ? 1.24467 0.89957 1.80455 -0.06885 0.04573  -0.30909 -72 VAL A O   
55   C CB  . VAL A 49  ? 1.19642 0.84952 1.77413 -0.04090 0.04462  -0.27883 -72 VAL A CB  
56   C CG1 . VAL A 49  ? 1.28092 0.98870 1.85815 -0.04618 0.03829  -0.30566 -72 VAL A CG1 
57   C CG2 . VAL A 49  ? 1.13412 0.76112 1.76384 -0.02652 0.05534  -0.29329 -72 VAL A CG2 
58   N N   . SER A 50  ? 1.23894 0.81421 1.83156 -0.05598 0.06105  -0.28771 -71 SER A N   
59   C CA  . SER A 50  ? 1.30430 0.86972 1.91879 -0.06076 0.06741  -0.30968 -71 SER A CA  
60   C C   . SER A 50  ? 1.34735 0.90321 2.01628 -0.04727 0.07636  -0.33127 -71 SER A C   
61   O O   . SER A 50  ? 1.38621 0.91290 2.07308 -0.03596 0.08157  -0.31844 -71 SER A O   
62   C CB  . SER A 50  ? 1.31380 0.83513 1.90986 -0.06877 0.07191  -0.28975 -71 SER A CB  
63   O OG  . SER A 50  ? 1.33318 0.84336 1.95450 -0.07080 0.07929  -0.30882 -71 SER A OG  
64   N N   . ASP A 51  ? 1.37847 0.95825 2.07280 -0.04852 0.07775  -0.36387 -70 ASP A N   
65   C CA  . ASP A 51  ? 1.32931 0.89836 2.07303 -0.03749 0.08636  -0.38516 -70 ASP A CA  
66   C C   . ASP A 51  ? 1.31043 0.86634 2.04621 -0.04100 0.09215  -0.37414 -70 ASP A C   
67   O O   . ASP A 51  ? 1.31860 0.87193 2.08046 -0.03240 0.09803  -0.37940 -70 ASP A O   
68   C CB  . ASP A 51  ? 1.35938 0.97328 2.12722 -0.03509 0.08360  -0.42111 -70 ASP A CB  
69   C CG  . ASP A 51  ? 1.31247 0.95390 2.06071 -0.05007 0.07881  -0.43670 -70 ASP A CG  
70   O OD1 . ASP A 51  ? 1.34978 0.97545 2.06579 -0.06215 0.07712  -0.42033 -70 ASP A OD1 
71   O OD2 . ASP A 51  ? 1.36009 1.03901 2.12488 -0.04959 0.07652  -0.46561 -70 ASP A OD2 
72   N N   . GLY A 52  ? 1.25354 0.80176 1.95377 -0.05346 0.09012  -0.35962 -69 GLY A N   
73   C CA  . GLY A 52  ? 1.30483 0.84330 1.99595 -0.05703 0.09485  -0.35072 -69 GLY A CA  
74   C C   . GLY A 52  ? 1.41245 0.97233 2.08276 -0.06999 0.09042  -0.36168 -69 GLY A C   
75   O O   . GLY A 52  ? 1.30347 0.85177 1.95069 -0.07621 0.09169  -0.34758 -69 GLY A O   
76   N N   . SER A 53  ? 1.51049 1.10336 2.18778 -0.07394 0.08468  -0.38741 -68 SER A N   
77   C CA  . SER A 53  ? 1.60799 1.22583 2.26495 -0.08627 0.07921  -0.39988 -68 SER A CA  
78   C C   . SER A 53  ? 1.57040 1.19549 2.19388 -0.09782 0.06960  -0.39655 -68 SER A C   
79   O O   . SER A 53  ? 1.67631 1.29159 2.26329 -0.10801 0.06605  -0.38055 -68 SER A O   
80   C CB  . SER A 53  ? 1.66752 1.32256 2.35408 -0.08375 0.07916  -0.43267 -68 SER A CB  
81   O OG  . SER A 53  ? 1.72903 1.39890 2.44169 -0.07584 0.07789  -0.44985 -68 SER A OG  
82   N N   . SER A 54  ? 1.38717 1.03028 2.02143 -0.09685 0.06468  -0.41175 -67 SER A N   
83   C CA  . SER A 54  ? 1.28669 0.95634 1.87516 -0.10581 0.05311  -0.39888 -67 SER A CA  
84   C C   . SER A 54  ? 1.17619 0.83494 1.74746 -0.09897 0.05102  -0.36941 -67 SER A C   
85   O O   . SER A 54  ? 1.13744 0.77706 1.73746 -0.08590 0.05763  -0.36503 -67 SER A O   
86   C CB  . SER A 54  ? 1.21385 0.93748 1.80472 -0.10822 0.04597  -0.42515 -67 SER A CB  
87   O OG  . SER A 54  ? 1.27674 1.01532 1.90513 -0.09432 0.04959  -0.43987 -67 SER A OG  
88   N N   . GLU A 55  ? 1.03496 0.70562 1.55802 -0.10820 0.04125  -0.34905 -66 GLU A N   
89   C CA  . GLU A 55  ? 1.12880 0.79394 1.62852 -0.10393 0.03727  -0.32023 -66 GLU A CA  
90   C C   . GLU A 55  ? 1.15901 0.87422 1.63465 -0.10828 0.02592  -0.32424 -66 GLU A C   
91   O O   . GLU A 55  ? 1.21039 0.95082 1.65856 -0.12110 0.01813  -0.33185 -66 GLU A O   
92   C CB  . GLU A 55  ? 1.13250 0.76121 1.59289 -0.11149 0.03590  -0.28808 -66 GLU A CB  
93   C CG  . GLU A 55  ? 1.15730 0.73680 1.63833 -0.10861 0.04710  -0.28278 -66 GLU A CG  
94   C CD  . GLU A 55  ? 1.14130 0.69071 1.58137 -0.11853 0.04511  -0.25652 -66 GLU A CD  
95   O OE1 . GLU A 55  ? 1.18686 0.75605 1.58579 -0.13016 0.03507  -0.25147 -66 GLU A OE1 
96   O OE2 . GLU A 55  ? 1.22157 0.72740 1.67021 -0.11473 0.05345  -0.24111 -66 GLU A OE2 
97   N N   . ILE A 56  ? 1.16199 0.89172 1.64746 -0.09785 0.02478  -0.31906 -65 ILE A N   
98   C CA  . ILE A 56  ? 1.01671 0.79608 1.48321 -0.10090 0.01469  -0.32348 -65 ILE A CA  
99   C C   . ILE A 56  ? 1.06517 0.83923 1.50292 -0.09850 0.00944  -0.29153 -65 ILE A C   
100  O O   . ILE A 56  ? 1.06111 0.80482 1.51527 -0.08697 0.01538  -0.27621 -65 ILE A O   
101  C CB  . ILE A 56  ? 0.99024 0.80436 1.49994 -0.09044 0.01750  -0.35473 -65 ILE A CB  
102  C CG1 . ILE A 56  ? 1.12459 0.98220 1.62115 -0.08816 0.00924  -0.35201 -65 ILE A CG1 
103  C CG2 . ILE A 56  ? 1.03996 0.82229 1.59849 -0.07463 0.02921  -0.36128 -65 ILE A CG2 
104  C CD1 . ILE A 56  ? 1.09863 1.00951 1.60315 -0.09214 0.00470  -0.38281 -65 ILE A CD1 
105  N N   . PHE A 57  ? 1.00438 0.80736 1.39828 -0.10990 -0.00202 -0.28130 -64 PHE A N   
106  C CA  . PHE A 57  ? 1.11631 0.91397 1.47342 -0.11141 -0.00873 -0.24886 -64 PHE A CA  
107  C C   . PHE A 57  ? 1.18451 1.02129 1.54997 -0.10362 -0.01302 -0.25187 -64 PHE A C   
108  O O   . PHE A 57  ? 1.17189 1.05462 1.54590 -0.10559 -0.01681 -0.27574 -64 PHE A O   
109  C CB  . PHE A 57  ? 1.26990 1.07509 1.57119 -0.12924 -0.01957 -0.23452 -64 PHE A CB  
110  C CG  . PHE A 57  ? 1.34371 1.10085 1.62179 -0.13524 -0.01732 -0.21348 -64 PHE A CG  
111  C CD1 . PHE A 57  ? 1.33213 1.05509 1.58993 -0.13225 -0.01710 -0.18050 -64 PHE A CD1 
112  C CD2 . PHE A 57  ? 1.27762 1.02459 1.55339 -0.14392 -0.01566 -0.22664 -64 PHE A CD2 
113  C CE1 . PHE A 57  ? 1.39033 1.07002 1.62611 -0.13766 -0.01493 -0.16127 -64 PHE A CE1 
114  C CE2 . PHE A 57  ? 1.30468 1.00895 1.55917 -0.14909 -0.01356 -0.20765 -64 PHE A CE2 
115  C CZ  . PHE A 57  ? 1.29993 0.97073 1.53413 -0.14598 -0.01311 -0.17497 -64 PHE A CZ  
116  N N   . PHE A 58  ? 1.08415 0.90271 1.44682 -0.09481 -0.01244 -0.22740 -63 PHE A N   
117  C CA  . PHE A 58  ? 1.06915 0.92124 1.43401 -0.08760 -0.01734 -0.22410 -63 PHE A CA  
118  C C   . PHE A 58  ? 1.07325 0.91733 1.39064 -0.09407 -0.02574 -0.18872 -63 PHE A C   
119  O O   . PHE A 58  ? 1.00155 0.79995 1.30695 -0.09270 -0.02270 -0.16351 -63 PHE A O   
120  C CB  . PHE A 58  ? 1.00484 0.84340 1.41828 -0.06779 -0.00838 -0.22998 -63 PHE A CB  
121  C CG  . PHE A 58  ? 1.04861 0.89628 1.51088 -0.05986 -0.00042 -0.26513 -63 PHE A CG  
122  C CD1 . PHE A 58  ? 1.23853 1.05408 1.71711 -0.06200 0.00733  -0.27546 -63 PHE A CD1 
123  C CD2 . PHE A 58  ? 1.16055 1.04853 1.65304 -0.04981 -0.00060 -0.28773 -63 PHE A CD2 
124  C CE1 . PHE A 58  ? 1.22706 1.05038 1.75013 -0.05498 0.01437  -0.30757 -63 PHE A CE1 
125  C CE2 . PHE A 58  ? 1.17954 1.07497 1.71649 -0.04221 0.00652  -0.32014 -63 PHE A CE2 
126  C CZ  . PHE A 58  ? 1.21002 1.07262 1.76206 -0.04499 0.01390  -0.32991 -63 PHE A CZ  
127  N N   . LYS A 59  ? 1.11957 1.00780 1.40969 -0.10145 -0.03628 -0.18681 -62 LYS A N   
128  C CA  . LYS A 59  ? 1.19309 1.08041 1.44402 -0.10510 -0.04452 -0.15496 -62 LYS A CA  
129  C C   . LYS A 59  ? 1.20274 1.09960 1.48148 -0.08874 -0.04219 -0.15130 -62 LYS A C   
130  O O   . LYS A 59  ? 1.24860 1.18591 1.55580 -0.08179 -0.04184 -0.17479 -62 LYS A O   
131  C CB  . LYS A 59  ? 1.22309 1.15385 1.43073 -0.12154 -0.05739 -0.15439 -62 LYS A CB  
132  C CG  . LYS A 59  ? 1.32646 1.26412 1.49438 -0.12574 -0.06695 -0.12387 -62 LYS A CG  
133  C CD  . LYS A 59  ? 1.36460 1.27227 1.47980 -0.14037 -0.07341 -0.09718 -62 LYS A CD  
134  C CE  . LYS A 59  ? 1.36482 1.29438 1.45289 -0.15746 -0.08030 -0.11150 -62 LYS A CE  
135  N NZ  . LYS A 59  ? 1.34212 1.24153 1.37852 -0.17121 -0.08699 -0.08644 -62 LYS A NZ  
136  N N   . ILE A 60  ? 1.19930 1.05990 1.46910 -0.08254 -0.04096 -0.12200 -61 ILE A N   
137  C CA  . ILE A 60  ? 1.22280 1.08988 1.51576 -0.06702 -0.03966 -0.11555 -61 ILE A CA  
138  C C   . ILE A 60  ? 1.32322 1.16594 1.58004 -0.06887 -0.04492 -0.07736 -61 ILE A C   
139  O O   . ILE A 60  ? 1.22308 1.02745 1.44948 -0.07729 -0.04533 -0.05595 -61 ILE A O   
140  C CB  . ILE A 60  ? 1.23261 1.07125 1.58008 -0.04889 -0.02733 -0.12886 -61 ILE A CB  
141  C CG1 . ILE A 60  ? 1.22313 1.00224 1.56986 -0.05011 -0.01963 -0.11633 -61 ILE A CG1 
142  C CG2 . ILE A 60  ? 1.19646 1.06882 1.58558 -0.04311 -0.02304 -0.16794 -61 ILE A CG2 
143  C CD1 . ILE A 60  ? 1.32624 1.06994 1.71754 -0.03251 -0.00906 -0.11823 -61 ILE A CD1 
144  N N   . LYS A 61  ? 1.34440 1.21016 1.60519 -0.06057 -0.04898 -0.06923 -60 LYS A N   
145  C CA  . LYS A 61  ? 1.35868 1.20379 1.58939 -0.06046 -0.05399 -0.03377 -60 LYS A CA  
146  C C   . LYS A 61  ? 1.43128 1.22045 1.68484 -0.04716 -0.04462 -0.01942 -60 LYS A C   
147  O O   . LYS A 61  ? 1.50682 1.28731 1.80788 -0.03269 -0.03569 -0.03751 -60 LYS A O   
148  C CB  . LYS A 61  ? 1.48541 1.37563 1.71629 -0.05528 -0.06119 -0.03164 -60 LYS A CB  
149  C CG  . LYS A 61  ? 1.53440 1.40988 1.73066 -0.05673 -0.06802 0.00475  -60 LYS A CG  
150  C CD  . LYS A 61  ? 1.55002 1.47252 1.75180 -0.05043 -0.07449 0.00423  -60 LYS A CD  
151  C CE  . LYS A 61  ? 1.57559 1.48252 1.74461 -0.05130 -0.08125 0.04063  -60 LYS A CE  
152  N NZ  . LYS A 61  ? 1.52936 1.47055 1.71740 -0.03908 -0.08440 0.04035  -60 LYS A NZ  
153  N N   . LYS A 62  ? 1.43339 1.18391 1.65204 -0.05238 -0.04688 0.01340  -59 LYS A N   
154  C CA  . LYS A 62  ? 1.44623 1.13968 1.68066 -0.04237 -0.03809 0.02924  -59 LYS A CA  
155  C C   . LYS A 62  ? 1.50432 1.19509 1.77445 -0.02347 -0.03467 0.03103  -59 LYS A C   
156  O O   . LYS A 62  ? 1.50772 1.15388 1.80137 -0.01302 -0.02611 0.03751  -59 LYS A O   
157  C CB  . LYS A 62  ? 1.47069 1.12743 1.65638 -0.05249 -0.04236 0.06496  -59 LYS A CB  
158  C CG  . LYS A 62  ? 1.46724 1.11190 1.62175 -0.06886 -0.04356 0.06463  -59 LYS A CG  
159  C CD  . LYS A 62  ? 1.49584 1.09834 1.60588 -0.07670 -0.04646 0.09981  -59 LYS A CD  
160  C CE  . LYS A 62  ? 1.40995 1.03454 1.47666 -0.08387 -0.05911 0.12295  -59 LYS A CE  
161  N NZ  . LYS A 62  ? 1.41595 1.01016 1.42988 -0.09712 -0.06446 0.15093  -59 LYS A NZ  
162  N N   . THR A 63  ? 1.55724 1.29416 1.83191 -0.01885 -0.04123 0.02549  -58 THR A N   
163  C CA  . THR A 63  ? 1.60923 1.34785 1.91810 -0.00026 -0.03891 0.02566  -58 THR A CA  
164  C C   . THR A 63  ? 1.61813 1.39724 1.97282 0.01051  -0.03577 -0.01032 -58 THR A C   
165  O O   . THR A 63  ? 1.69538 1.48726 2.07806 0.02594  -0.03547 -0.01388 -58 THR A O   
166  C CB  . THR A 63  ? 1.61718 1.37384 1.89617 -0.00116 -0.04896 0.05116  -58 THR A CB  
167  O OG1 . THR A 63  ? 1.53968 1.35035 1.79211 -0.01393 -0.05857 0.04369  -58 THR A OG1 
168  C CG2 . THR A 63  ? 1.63007 1.33933 1.86930 -0.00825 -0.05093 0.08813  -58 THR A CG2 
169  N N   . THR A 64  ? 1.52179 1.32132 1.88446 0.00299  -0.03365 -0.03718 -57 THR A N   
170  C CA  . THR A 64  ? 1.48095 1.31609 1.88757 0.01270  -0.02991 -0.07307 -57 THR A CA  
171  C C   . THR A 64  ? 1.49231 1.28729 1.94333 0.02514  -0.01803 -0.08722 -57 THR A C   
172  O O   . THR A 64  ? 1.49991 1.25524 1.94428 0.01825  -0.01268 -0.08271 -57 THR A O   
173  C CB  . THR A 64  ? 1.39580 1.27253 1.78912 -0.00183 -0.03364 -0.09550 -57 THR A CB  
174  O OG1 . THR A 64  ? 1.38039 1.29870 1.73515 -0.01276 -0.04507 -0.08432 -57 THR A OG1 
175  C CG2 . THR A 64  ? 1.25153 1.16060 1.69171 0.00822  -0.02871 -0.13378 -57 THR A CG2 
176  N N   . PRO A 65  ? 1.43454 1.23781 1.93048 0.04330  -0.01386 -0.10400 -56 PRO A N   
177  C CA  . PRO A 65  ? 1.44320 1.21044 1.98231 0.05456  -0.00295 -0.12011 -56 PRO A CA  
178  C C   . PRO A 65  ? 1.40352 1.17824 1.95201 0.04541  0.00144  -0.14705 -56 PRO A C   
179  O O   . PRO A 65  ? 1.45130 1.27304 1.99126 0.03691  -0.00326 -0.16539 -56 PRO A O   
180  C CB  . PRO A 65  ? 1.41760 1.20788 1.99916 0.07442  -0.00199 -0.13732 -56 PRO A CB  
181  C CG  . PRO A 65  ? 1.51130 1.32632 2.06887 0.07592  -0.01111 -0.11610 -56 PRO A CG  
182  C CD  . PRO A 65  ? 1.47929 1.32030 1.98736 0.05515  -0.01913 -0.10559 -56 PRO A CD  
183  N N   . LEU A 66  ? 1.29861 1.02606 1.86472 0.04692  0.01050  -0.14916 -55 LEU A N   
184  C CA  . LEU A 66  ? 1.27882 1.00795 1.85573 0.03870  0.01533  -0.17382 -55 LEU A CA  
185  C C   . LEU A 66  ? 1.28120 1.04281 1.90279 0.04917  0.01856  -0.21123 -55 LEU A C   
186  O O   . LEU A 66  ? 1.33190 1.09931 1.96532 0.04302  0.02229  -0.23464 -55 LEU A O   
187  C CB  . LEU A 66  ? 1.18898 0.85793 1.77249 0.03742  0.02426  -0.16437 -55 LEU A CB  
188  C CG  . LEU A 66  ? 1.16296 0.80073 1.69949 0.02399  0.02162  -0.13120 -55 LEU A CG  
189  C CD1 . LEU A 66  ? 1.23675 0.81190 1.78431 0.02898  0.03035  -0.11456 -55 LEU A CD1 
190  C CD2 . LEU A 66  ? 1.08734 0.74096 1.59491 0.00556  0.01863  -0.13854 -55 LEU A CD2 
191  N N   . ARG A 67  ? 1.23582 1.01777 1.88230 0.06503  0.01714  -0.21725 -54 ARG A N   
192  C CA  . ARG A 67  ? 1.29554 1.10926 1.98475 0.07643  0.01988  -0.25274 -54 ARG A CA  
193  C C   . ARG A 67  ? 1.20362 1.06766 1.88208 0.06385  0.01595  -0.27647 -54 ARG A C   
194  O O   . ARG A 67  ? 1.15776 1.03013 1.86410 0.06508  0.02085  -0.30611 -54 ARG A O   
195  C CB  . ARG A 67  ? 1.34495 1.18129 2.05238 0.09346  0.01643  -0.25191 -54 ARG A CB  
196  C CG  . ARG A 67  ? 1.41035 1.30175 2.14574 0.10130  0.01490  -0.28568 -54 ARG A CG  
197  C CD  . ARG A 67  ? 1.47592 1.36002 2.25649 0.12442  0.01853  -0.29664 -54 ARG A CD  
198  N NE  . ARG A 67  ? 1.59280 1.44300 2.41186 0.13198  0.02780  -0.31663 -54 ARG A NE  
199  C CZ  . ARG A 67  ? 1.63070 1.45486 2.48783 0.15090  0.03238  -0.32204 -54 ARG A CZ  
200  N NH1 . ARG A 67  ? 1.62852 1.45657 2.49059 0.16468  0.02855  -0.30885 -54 ARG A NH1 
201  N NH2 . ARG A 67  ? 1.63301 1.42661 2.52282 0.15591  0.04046  -0.34039 -54 ARG A NH2 
202  N N   . ARG A 68  ? 1.13376 1.03142 1.77108 0.05130  0.00680  -0.26358 -53 ARG A N   
203  C CA  . ARG A 68  ? 1.13229 1.07703 1.75424 0.03760  0.00215  -0.28353 -53 ARG A CA  
204  C C   . ARG A 68  ? 1.26943 1.19070 1.88536 0.02480  0.00650  -0.29218 -53 ARG A C   
205  O O   . ARG A 68  ? 1.31784 1.26328 1.95115 0.02196  0.00841  -0.32203 -53 ARG A O   
206  C CB  . ARG A 68  ? 1.17743 1.15404 1.75141 0.02491  -0.00877 -0.26298 -53 ARG A CB  
207  C CG  . ARG A 68  ? 1.27665 1.28802 1.85697 0.03626  -0.01389 -0.25896 -53 ARG A CG  
208  C CD  . ARG A 68  ? 1.34835 1.41153 1.96165 0.04428  -0.01349 -0.29439 -53 ARG A CD  
209  N NE  . ARG A 68  ? 1.40292 1.48790 2.03728 0.06123  -0.01528 -0.29388 -53 ARG A NE  
210  C CZ  . ARG A 68  ? 1.40216 1.53369 2.01692 0.05874  -0.02369 -0.28755 -53 ARG A CZ  
211  N NH1 . ARG A 68  ? 1.34092 1.50155 1.91344 0.03941  -0.03132 -0.28087 -53 ARG A NH1 
212  N NH2 . ARG A 68  ? 1.42071 1.56978 2.05798 0.07552  -0.02472 -0.28794 -53 ARG A NH2 
213  N N   . LEU A 69  ? 1.24707 1.12140 1.83841 0.01708  0.00807  -0.26637 -52 LEU A N   
214  C CA  . LEU A 69  ? 1.23507 1.08650 1.81740 0.00436  0.01172  -0.27203 -52 LEU A CA  
215  C C   . LEU A 69  ? 1.20277 1.03513 1.83325 0.01383  0.02189  -0.29871 -52 LEU A C   
216  O O   . LEU A 69  ? 1.23111 1.07707 1.86931 0.00645  0.02363  -0.32267 -52 LEU A O   
217  C CB  . LEU A 69  ? 1.22135 1.02387 1.77070 -0.00331 0.01203  -0.23784 -52 LEU A CB  
218  C CG  . LEU A 69  ? 1.12440 0.90382 1.65069 -0.01906 0.01347  -0.23534 -52 LEU A CG  
219  C CD1 . LEU A 69  ? 1.09292 0.84508 1.57199 -0.02874 0.00880  -0.19864 -52 LEU A CD1 
220  C CD2 . LEU A 69  ? 1.11971 0.85835 1.68198 -0.01337 0.02480  -0.24785 -52 LEU A CD2 
221  N N   . MET A 70  ? 1.26014 1.05920 1.92257 0.02987  0.02844  -0.29430 -51 MET A N   
222  C CA  . MET A 70  ? 1.31594 1.09304 2.02431 0.03931  0.03799  -0.31802 -51 MET A CA  
223  C C   . MET A 70  ? 1.33426 1.15842 2.07334 0.04557  0.03762  -0.35465 -51 MET A C   
224  O O   . MET A 70  ? 1.33540 1.15861 2.09769 0.04387  0.04273  -0.38020 -51 MET A O   
225  C CB  . MET A 70  ? 1.39399 1.12720 2.12739 0.05537  0.04375  -0.30391 -51 MET A CB  
226  C CG  . MET A 70  ? 1.43603 1.12027 2.14030 0.04931  0.04487  -0.26803 -51 MET A CG  
227  S SD  . MET A 70  ? 1.56091 1.21079 2.27634 0.06643  0.04611  -0.24215 -51 MET A SD  
228  C CE  . MET A 70  ? 1.59125 1.20029 2.36170 0.08045  0.05766  -0.26154 -51 MET A CE  
229  N N   . GLU A 71  ? 1.32743 1.19368 2.06707 0.05283  0.03162  -0.35780 -50 GLU A N   
230  C CA  . GLU A 71  ? 1.30971 1.22532 2.07514 0.05820  0.03065  -0.39208 -50 GLU A CA  
231  C C   . GLU A 71  ? 1.11998 1.06666 1.86579 0.04075  0.02753  -0.40895 -50 GLU A C   
232  O O   . GLU A 71  ? 1.06296 1.02581 1.83596 0.04220  0.03105  -0.44028 -50 GLU A O   
233  C CB  . GLU A 71  ? 1.52602 1.48326 2.28916 0.06721  0.02398  -0.38878 -50 GLU A CB  
234  C CG  . GLU A 71  ? 1.63741 1.65819 2.38196 0.05733  0.01642  -0.40414 -50 GLU A CG  
235  C CD  . GLU A 71  ? 1.73290 1.78101 2.44279 0.05374  0.00731  -0.38042 -50 GLU A CD  
236  O OE1 . GLU A 71  ? 1.77882 1.84110 2.50558 0.06864  0.00601  -0.37836 -50 GLU A OE1 
237  O OE2 . GLU A 71  ? 1.71096 1.76636 2.37654 0.03604  0.00114  -0.36397 -50 GLU A OE2 
238  N N   . ALA A 72  ? 0.98964 0.94380 1.68766 0.02404  0.02063  -0.38849 -49 ALA A N   
239  C CA  . ALA A 72  ? 1.02759 1.01146 1.70361 0.00693  0.01653  -0.40308 -49 ALA A CA  
240  C C   . ALA A 72  ? 1.12612 1.07622 1.81379 0.00087  0.02345  -0.41446 -49 ALA A C   
241  O O   . ALA A 72  ? 1.12554 1.09965 1.82218 -0.00535 0.02377  -0.44152 -49 ALA A O   
242  C CB  . ALA A 72  ? 0.95974 0.95516 1.58039 -0.00922 0.00701  -0.37657 -49 ALA A CB  
243  N N   . PHE A 73  ? 1.22020 1.11501 1.90802 0.00242  0.02907  -0.39423 -48 PHE A N   
244  C CA  . PHE A 73  ? 1.30854 1.17033 2.00876 -0.00307 0.03607  -0.40430 -48 PHE A CA  
245  C C   . PHE A 73  ? 1.29548 1.15758 2.04808 0.00935  0.04375  -0.43649 -48 PHE A C   
246  O O   . PHE A 73  ? 1.35040 1.21523 2.11502 0.00298  0.04677  -0.45899 -48 PHE A O   
247  C CB  . PHE A 73  ? 1.39556 1.19868 2.08508 -0.00371 0.04073  -0.37498 -48 PHE A CB  
248  C CG  . PHE A 73  ? 1.50388 1.27378 2.20262 -0.01073 0.04763  -0.38307 -48 PHE A CG  
249  C CD1 . PHE A 73  ? 1.49643 1.27874 2.16818 -0.02752 0.04396  -0.38830 -48 PHE A CD1 
250  C CD2 . PHE A 73  ? 1.51520 1.24238 2.25006 -0.00062 0.05753  -0.38623 -48 PHE A CD2 
251  C CE1 . PHE A 73  ? 1.46848 1.22175 2.14940 -0.03376 0.05018  -0.39615 -48 PHE A CE1 
252  C CE2 . PHE A 73  ? 1.52869 1.22702 2.27266 -0.00746 0.06393  -0.39397 -48 PHE A CE2 
253  C CZ  . PHE A 73  ? 1.51217 1.22401 2.22952 -0.02384 0.06034  -0.39895 -48 PHE A CZ  
254  N N   . ALA A 74  ? 1.29143 1.14966 2.07544 0.02725  0.04671  -0.43900 -47 ALA A N   
255  C CA  . ALA A 74  ? 1.15946 1.02167 1.99274 0.04008  0.05294  -0.47063 -47 ALA A CA  
256  C C   . ALA A 74  ? 1.14965 1.06818 1.98842 0.03625  0.04899  -0.50205 -47 ALA A C   
257  O O   . ALA A 74  ? 1.15137 1.07230 2.01600 0.03591  0.05346  -0.52974 -47 ALA A O   
258  C CB  . ALA A 74  ? 1.06586 0.91782 1.92728 0.06019  0.05505  -0.46616 -47 ALA A CB  
259  N N   . LYS A 75  ? 1.28615 1.25064 2.10032 0.03287  0.04056  -0.49810 -46 LYS A N   
260  C CA  . LYS A 75  ? 1.34964 1.37004 2.16539 0.02801  0.03632  -0.52651 -46 LYS A CA  
261  C C   . LYS A 75  ? 1.30371 1.32654 2.10180 0.01005  0.03562  -0.53713 -46 LYS A C   
262  O O   . LYS A 75  ? 1.27017 1.31750 2.08820 0.00885  0.03704  -0.56824 -46 LYS A O   
263  C CB  . LYS A 75  ? 1.40590 1.47233 2.19243 0.02515  0.02699  -0.51559 -46 LYS A CB  
264  C CG  . LYS A 75  ? 1.46522 1.58727 2.23528 0.01267  0.02072  -0.53633 -46 LYS A CG  
265  C CD  . LYS A 75  ? 1.52056 1.69250 2.31511 0.02472  0.01914  -0.55903 -46 LYS A CD  
266  C CE  . LYS A 75  ? 1.56543 1.79262 2.34404 0.01172  0.01327  -0.58054 -46 LYS A CE  
267  N NZ  . LYS A 75  ? 1.62398 1.90077 2.42898 0.02370  0.01255  -0.60534 -46 LYS A NZ  
268  N N   . ARG A 76  ? 1.31848 1.31568 2.07902 -0.00378 0.03324  -0.51171 -45 ARG A N   
269  C CA  . ARG A 76  ? 1.38780 1.38603 2.12854 -0.02101 0.03178  -0.51973 -45 ARG A CA  
270  C C   . ARG A 76  ? 1.36751 1.33852 2.14508 -0.01781 0.04077  -0.54194 -45 ARG A C   
271  O O   . ARG A 76  ? 1.30263 1.29291 2.08282 -0.02664 0.04020  -0.56539 -45 ARG A O   
272  C CB  . ARG A 76  ? 1.38430 1.35442 2.07969 -0.03417 0.02801  -0.48636 -45 ARG A CB  
273  C CG  . ARG A 76  ? 1.36962 1.32953 2.04641 -0.05043 0.02749  -0.49154 -45 ARG A CG  
274  C CD  . ARG A 76  ? 1.44743 1.37643 2.08079 -0.06142 0.02407  -0.45756 -45 ARG A CD  
275  N NE  . ARG A 76  ? 1.52028 1.42105 2.14760 -0.07190 0.02719  -0.46004 -45 ARG A NE  
276  C CZ  . ARG A 76  ? 1.52664 1.44407 2.12213 -0.08817 0.02068  -0.46359 -45 ARG A CZ  
277  N NH1 . ARG A 76  ? 1.48782 1.44953 2.05365 -0.09657 0.01062  -0.46476 -45 ARG A NH1 
278  N NH2 . ARG A 76  ? 1.59049 1.48031 2.18356 -0.09618 0.02401  -0.46589 -45 ARG A NH2 
279  N N   . GLN A 77  ? 1.36697 1.29318 2.17316 -0.00553 0.04892  -0.53504 -44 GLN A N   
280  C CA  . GLN A 77  ? 1.39256 1.28789 2.23352 -0.00258 0.05775  -0.55320 -44 GLN A CA  
281  C C   . GLN A 77  ? 1.53895 1.44738 2.42858 0.01357  0.06240  -0.58262 -44 GLN A C   
282  O O   . GLN A 77  ? 1.53131 1.40425 2.45533 0.02197  0.07051  -0.59082 -44 GLN A O   
283  C CB  . GLN A 77  ? 1.42289 1.25811 2.26446 -0.00065 0.06407  -0.52783 -44 GLN A CB  
284  C CG  . GLN A 77  ? 1.46374 1.28328 2.25697 -0.01477 0.05955  -0.49641 -44 GLN A CG  
285  C CD  . GLN A 77  ? 1.49649 1.26202 2.29106 -0.01901 0.06664  -0.48298 -44 GLN A CD  
286  O OE1 . GLN A 77  ? 1.50707 1.23569 2.33238 -0.00808 0.07459  -0.48110 -44 GLN A OE1 
287  N NE2 . GLN A 77  ? 1.50582 1.26651 2.26664 -0.03502 0.06363  -0.47364 -44 GLN A NE2 
288  N N   . GLY A 78  ? 1.58615 1.54493 2.47892 0.01804  0.05729  -0.59867 -43 GLY A N   
289  C CA  . GLY A 78  ? 1.53291 1.51051 2.46953 0.03265  0.06080  -0.62948 -43 GLY A CA  
290  C C   . GLY A 78  ? 1.55519 1.50584 2.52407 0.05268  0.06571  -0.62397 -43 GLY A C   
291  O O   . GLY A 78  ? 1.55621 1.53413 2.55032 0.06648  0.06523  -0.64168 -43 GLY A O   
292  N N   . LYS A 79  ? 1.59064 1.48806 2.55890 0.05465  0.07029  -0.59981 -42 LYS A N   
293  C CA  . LYS A 79  ? 1.63253 1.49869 2.63010 0.07300  0.07487  -0.59270 -42 LYS A CA  
294  C C   . LYS A 79  ? 1.67900 1.56318 2.65856 0.08018  0.06884  -0.57145 -42 LYS A C   
295  O O   . LYS A 79  ? 1.71924 1.64667 2.66997 0.07256  0.06138  -0.56834 -42 LYS A O   
296  C CB  . LYS A 79  ? 1.60062 1.40412 2.60234 0.07129  0.08183  -0.57419 -42 LYS A CB  
297  C CG  . LYS A 79  ? 1.55165 1.33707 2.57131 0.06375  0.08783  -0.59441 -42 LYS A CG  
298  C CD  . LYS A 79  ? 1.58991 1.32413 2.60588 0.06141  0.09357  -0.56680 -42 LYS A CD  
299  C CE  . LYS A 79  ? 1.65176 1.38714 2.67296 0.05314  0.09707  -0.57264 -42 LYS A CE  
300  N NZ  . LYS A 79  ? 1.69308 1.38614 2.70094 0.04776  0.10192  -0.54322 -42 LYS A NZ  
301  N N   . GLU A 80  ? 1.72424 1.57531 2.72053 0.09480  0.07178  -0.55647 -41 GLU A N   
302  C CA  . GLU A 80  ? 1.81649 1.67893 2.79678 0.10226  0.06637  -0.53408 -41 GLU A CA  
303  C C   . GLU A 80  ? 1.77557 1.58221 2.74696 0.10464  0.06933  -0.50073 -41 GLU A C   
304  O O   . GLU A 80  ? 1.77856 1.53821 2.76536 0.10456  0.07641  -0.49884 -41 GLU A O   
305  C CB  . GLU A 80  ? 1.90908 1.79945 2.92284 0.12184  0.06543  -0.55361 -41 GLU A CB  
306  C CG  . GLU A 80  ? 1.99395 1.94155 2.98661 0.12135  0.05693  -0.55237 -41 GLU A CG  
307  C CD  . GLU A 80  ? 2.08308 2.07790 3.10577 0.13216  0.05611  -0.58739 -41 GLU A CD  
308  O OE1 . GLU A 80  ? 2.11674 2.09693 3.17817 0.14205  0.06199  -0.61166 -41 GLU A OE1 
309  O OE2 . GLU A 80  ? 2.07712 2.12381 3.08430 0.13057  0.04953  -0.59067 -41 GLU A OE2 
310  N N   . MET A 81  ? 1.72507 1.53823 2.67054 0.10625  0.06367  -0.47413 -40 MET A N   
311  C CA  . MET A 81  ? 1.68416 1.44953 2.60885 0.10396  0.06490  -0.43835 -40 MET A CA  
312  C C   . MET A 81  ? 1.65952 1.37325 2.61886 0.11843  0.07234  -0.43560 -40 MET A C   
313  O O   . MET A 81  ? 1.68239 1.34734 2.63152 0.11406  0.07632  -0.41266 -40 MET A O   
314  C CB  . MET A 81  ? 1.67651 1.46209 2.57104 0.10515  0.05701  -0.41305 -40 MET A CB  
315  C CG  . MET A 81  ? 1.66970 1.41498 2.52950 0.09686  0.05643  -0.37481 -40 MET A CG  
316  S SD  . MET A 81  ? 1.67202 1.42285 2.51278 0.10609  0.04955  -0.34446 -40 MET A SD  
317  C CE  . MET A 81  ? 1.67642 1.50481 2.50362 0.10292  0.04020  -0.36092 -40 MET A CE  
318  N N   . ASP A 82  ? 1.59694 1.32010 2.59658 0.13560  0.07412  -0.45850 -39 ASP A N   
319  C CA  . ASP A 82  ? 1.61364 1.28758 2.64710 0.14960  0.08064  -0.45752 -39 ASP A CA  
320  C C   . ASP A 82  ? 1.64926 1.28296 2.69488 0.14128  0.08867  -0.46452 -39 ASP A C   
321  O O   . ASP A 82  ? 1.55992 1.14392 2.61486 0.14513  0.09379  -0.44955 -39 ASP A O   
322  C CB  . ASP A 82  ? 1.63910 1.33458 2.71339 0.16918  0.08041  -0.48455 -39 ASP A CB  
323  C CG  . ASP A 82  ? 1.67647 1.41244 2.76824 0.16642  0.08086  -0.52179 -39 ASP A CG  
324  O OD1 . ASP A 82  ? 1.67651 1.44061 2.74216 0.14984  0.07841  -0.52515 -39 ASP A OD1 
325  O OD2 . ASP A 82  ? 1.69782 1.43686 2.82887 0.18085  0.08340  -0.54771 -39 ASP A OD2 
326  N N   . SER A 83  ? 1.76557 1.42261 2.80756 0.12872  0.08931  -0.48493 -38 SER A N   
327  C CA  . SER A 83  ? 1.84730 1.47821 2.89658 0.11922  0.09572  -0.49137 -38 SER A CA  
328  C C   . SER A 83  ? 1.76704 1.37054 2.78086 0.10186  0.09718  -0.46567 -38 SER A C   
329  O O   . SER A 83  ? 1.81285 1.40893 2.81777 0.08991  0.10059  -0.46399 -38 SER A O   
330  C CB  . SER A 83  ? 1.91287 1.58427 2.97552 0.11434  0.09531  -0.52580 -38 SER A CB  
331  O OG  . SER A 83  ? 1.92040 1.62915 2.95834 0.10324  0.09008  -0.53224 -38 SER A OG  
332  N N   . LEU A 84  ? 1.59948 1.19612 2.58369 0.09860  0.09332  -0.43986 -37 LEU A N   
333  C CA  . LEU A 84  ? 1.50902 1.08123 2.45730 0.08230  0.09403  -0.41529 -37 LEU A CA  
334  C C   . LEU A 84  ? 1.56746 1.09797 2.50056 0.08620  0.09483  -0.37957 -37 LEU A C   
335  O O   . LEU A 84  ? 1.55662 1.08938 2.49514 0.09920  0.09188  -0.36997 -37 LEU A O   
336  C CB  . LEU A 84  ? 1.36716 0.98286 2.27472 0.06761  0.08611  -0.41219 -37 LEU A CB  
337  C CG  . LEU A 84  ? 1.31500 0.97019 2.22858 0.05933  0.08485  -0.44408 -37 LEU A CG  
338  C CD1 . LEU A 84  ? 1.22936 0.92095 2.09780 0.04384  0.07653  -0.43575 -37 LEU A CD1 
339  C CD2 . LEU A 84  ? 1.27705 0.90134 2.20925 0.05304  0.09276  -0.45721 -37 LEU A CD2 
340  N N   . ARG A 85  ? 1.69674 1.19410 2.60567 0.07399  0.09825  -0.35785 -36 ARG A N   
341  C CA  . ARG A 85  ? 1.77598 1.23552 2.66028 0.07374  0.09913  -0.32021 -36 ARG A CA  
342  C C   . ARG A 85  ? 1.67094 1.12310 2.51781 0.05857  0.09640  -0.30273 -36 ARG A C   
343  O O   . ARG A 85  ? 1.64836 1.10166 2.47694 0.04467  0.09816  -0.30349 -36 ARG A O   
344  C CB  . ARG A 85  ? 1.88743 1.32224 2.76689 0.07215  0.10499  -0.30623 -36 ARG A CB  
345  C CG  . ARG A 85  ? 2.02516 1.43434 2.90997 0.08467  0.10600  -0.28734 -36 ARG A CG  
346  C CD  . ARG A 85  ? 2.13996 1.52198 3.00853 0.07889  0.11109  -0.26934 -36 ARG A CD  
347  N NE  . ARG A 85  ? 2.23173 1.59485 3.11363 0.09100  0.11238  -0.26192 -36 ARG A NE  
348  C CZ  . ARG A 85  ? 2.29646 1.63541 3.16792 0.08840  0.11624  -0.24807 -36 ARG A CZ  
349  N NH1 . ARG A 85  ? 2.29918 1.63135 3.14799 0.07500  0.11939  -0.24011 -36 ARG A NH1 
350  N NH2 . ARG A 85  ? 2.35458 1.67666 3.23795 0.09941  0.11659  -0.24282 -36 ARG A NH2 
351  N N   . PHE A 86  ? 1.57736 1.04047 2.39354 0.05913  0.08941  -0.27874 -35 PHE A N   
352  C CA  . PHE A 86  ? 1.46301 0.93090 2.22979 0.04407  0.08411  -0.25564 -35 PHE A CA  
353  C C   . PHE A 86  ? 1.44278 0.85844 2.19213 0.04307  0.08762  -0.22148 -35 PHE A C   
354  O O   . PHE A 86  ? 1.43788 0.83626 2.19229 0.05433  0.08717  -0.20482 -35 PHE A O   
355  C CB  . PHE A 86  ? 1.43742 0.95293 2.17887 0.04386  0.07355  -0.25105 -35 PHE A CB  
356  C CG  . PHE A 86  ? 1.31550 0.88496 2.06486 0.04087  0.06942  -0.28229 -35 PHE A CG  
357  C CD1 . PHE A 86  ? 1.20267 0.79969 1.98762 0.05470  0.06925  -0.30649 -35 PHE A CD1 
358  C CD2 . PHE A 86  ? 1.24921 0.84136 1.97029 0.02442  0.06559  -0.28773 -35 PHE A CD2 
359  C CE1 . PHE A 86  ? 1.21509 0.86202 2.00719 0.05189  0.06570  -0.33542 -35 PHE A CE1 
360  C CE2 . PHE A 86  ? 1.27434 0.91569 2.00210 0.02124  0.06171  -0.31636 -35 PHE A CE2 
361  C CZ  . PHE A 86  ? 1.31288 0.98198 2.07623 0.03485  0.06197  -0.34023 -35 PHE A CZ  
362  N N   . LEU A 87  ? 1.41862 0.80941 2.14782 0.02985  0.09107  -0.21148 -34 LEU A N   
363  C CA  . LEU A 87  ? 1.42774 0.78317 2.12469 0.02645  0.09314  -0.17626 -34 LEU A CA  
364  C C   . LEU A 87  ? 1.48284 0.83243 2.13932 0.01278  0.08830  -0.15663 -34 LEU A C   
365  O O   . LEU A 87  ? 1.39509 0.77249 2.03511 0.00133  0.08447  -0.16887 -34 LEU A O   
366  C CB  . LEU A 87  ? 1.37004 0.71623 2.06038 0.02266  0.09940  -0.17509 -34 LEU A CB  
367  C CG  . LEU A 87  ? 1.32636 0.68320 2.05659 0.03191  0.10387  -0.20002 -34 LEU A CG  
368  C CD1 . LEU A 87  ? 1.34910 0.69706 2.07050 0.02580  0.10926  -0.19783 -34 LEU A CD1 
369  C CD2 . LEU A 87  ? 1.34065 0.68707 2.09204 0.04762  0.10393  -0.19505 -34 LEU A CD2 
370  N N   . TYR A 88  ? 1.63004 0.95629 2.25682 0.01351  0.08637  -0.12295 -33 TYR A N   
371  C CA  . TYR A 88  ? 1.70129 1.01824 2.28295 0.00067  0.08174  -0.09853 -33 TYR A CA  
372  C C   . TYR A 88  ? 1.82378 1.11446 2.36796 0.00045  0.08373  -0.06672 -33 TYR A C   
373  O O   . TYR A 88  ? 1.87358 1.15034 2.42015 0.01083  0.08413  -0.05200 -33 TYR A O   
374  C CB  . TYR A 88  ? 1.72155 1.07266 2.27373 0.00122  0.07052  -0.08571 -33 TYR A CB  
375  C CG  . TYR A 88  ? 1.69528 1.03848 2.19376 -0.01124 0.06449  -0.05649 -33 TYR A CG  
376  C CD1 . TYR A 88  ? 1.65278 1.01608 2.12177 -0.02603 0.05997  -0.06172 -33 TYR A CD1 
377  C CD2 . TYR A 88  ? 1.65008 0.96440 2.12692 -0.00815 0.06308  -0.02370 -33 TYR A CD2 
378  C CE1 . TYR A 88  ? 1.64510 1.00004 2.06426 -0.03714 0.05399  -0.03536 -33 TYR A CE1 
379  C CE2 . TYR A 88  ? 1.63688 0.94305 2.06405 -0.01939 0.05737  0.00287  -33 TYR A CE2 
380  C CZ  . TYR A 88  ? 1.62964 0.95596 2.02804 -0.03376 0.05279  -0.00317 -33 TYR A CZ  
381  O OH  . TYR A 88  ? 1.48188 0.79908 1.83002 -0.04471 0.04663  0.02296  -33 TYR A OH  
382  N N   . ASP A 89  ? 1.90414 1.18942 2.41378 -0.01097 0.08440  -0.05820 -32 ASP A N   
383  C CA  . ASP A 89  ? 2.00885 1.27265 2.47996 -0.01278 0.08549  -0.03287 -32 ASP A CA  
384  C C   . ASP A 89  ? 1.94159 1.19724 2.43212 -0.00500 0.09183  -0.03945 -32 ASP A C   
385  O O   . ASP A 89  ? 2.04345 1.28209 2.50573 -0.00644 0.09261  -0.02200 -32 ASP A O   
386  C CB  . ASP A 89  ? 2.11332 1.36114 2.55259 -0.01039 0.08042  -0.00199 -32 ASP A CB  
387  C CG  . ASP A 89  ? 2.20629 1.43835 2.59208 -0.01795 0.07811  0.02217  -32 ASP A CG  
388  O OD1 . ASP A 89  ? 2.21779 1.45468 2.58124 -0.02875 0.07683  0.02020  -32 ASP A OD1 
389  O OD2 . ASP A 89  ? 2.24369 1.45930 2.60925 -0.01297 0.07681  0.04184  -32 ASP A OD2 
390  N N   . GLY A 90  ? 1.79035 1.05798 2.32709 0.00278  0.09568  -0.06461 -31 GLY A N   
391  C CA  . GLY A 90  ? 1.66188 0.92179 2.21895 0.00993  0.10117  -0.07119 -31 GLY A CA  
392  C C   . GLY A 90  ? 1.71973 0.97620 2.30824 0.02416  0.10168  -0.07499 -31 GLY A C   
393  O O   . GLY A 90  ? 1.69911 0.95204 2.31106 0.03037  0.10596  -0.08544 -31 GLY A O   
394  N N   . ILE A 91  ? 1.83718 1.09446 2.42731 0.02975  0.09711  -0.06675 -30 ILE A N   
395  C CA  . ILE A 91  ? 1.93371 1.18803 2.55273 0.04448  0.09667  -0.06920 -30 ILE A CA  
396  C C   . ILE A 91  ? 1.93079 1.21060 2.59279 0.05068  0.09554  -0.09832 -30 ILE A C   
397  O O   . ILE A 91  ? 1.87632 1.17231 2.53649 0.04366  0.09243  -0.10685 -30 ILE A O   
398  C CB  . ILE A 91  ? 1.96157 1.20007 2.55365 0.04803  0.09173  -0.03953 -30 ILE A CB  
399  C CG1 . ILE A 91  ? 2.01525 1.25031 2.63724 0.06419  0.09095  -0.04175 -30 ILE A CG1 
400  C CG2 . ILE A 91  ? 1.94374 1.19192 2.51895 0.04124  0.08606  -0.03151 -30 ILE A CG2 
401  C CD1 . ILE A 91  ? 2.02537 1.24535 2.62158 0.06838  0.08593  -0.01261 -30 ILE A CD1 
402  N N   . ARG A 92  ? 2.00621 1.29049 2.70600 0.06361  0.09750  -0.11516 -29 ARG A N   
403  C CA  . ARG A 92  ? 2.04296 1.35333 2.78397 0.07206  0.09566  -0.14434 -29 ARG A CA  
404  C C   . ARG A 92  ? 1.98961 1.30207 2.73338 0.08020  0.08950  -0.13395 -29 ARG A C   
405  O O   . ARG A 92  ? 2.05331 1.34819 2.79035 0.08878  0.08804  -0.11301 -29 ARG A O   
406  C CB  . ARG A 92  ? 2.15154 1.46648 2.92989 0.08393  0.09915  -0.16520 -29 ARG A CB  
407  C CG  . ARG A 92  ? 2.19443 1.53823 3.01490 0.09543  0.09662  -0.19597 -29 ARG A CG  
408  C CD  . ARG A 92  ? 2.26200 1.61234 3.11622 0.10496  0.10010  -0.21845 -29 ARG A CD  
409  N NE  . ARG A 92  ? 2.33570 1.66094 3.18977 0.11463  0.10099  -0.20132 -29 ARG A NE  
410  C CZ  . ARG A 92  ? 2.40476 1.72799 3.28314 0.12287  0.10351  -0.21482 -29 ARG A CZ  
411  N NH1 . ARG A 92  ? 2.41424 1.75994 3.31908 0.12278  0.10552  -0.24491 -29 ARG A NH1 
412  N NH2 . ARG A 92  ? 2.45694 1.75557 3.33177 0.13080  0.10360  -0.19827 -29 ARG A NH2 
413  N N   . ILE A 93  ? 1.84615 1.19004 2.58997 0.07623  0.08426  -0.14707 -28 ILE A N   
414  C CA  . ILE A 93  ? 1.76631 1.14061 2.48567 0.07917  0.07464  -0.13247 -28 ILE A CA  
415  C C   . ILE A 93  ? 1.78112 1.19653 2.53171 0.09281  0.07124  -0.15796 -28 ILE A C   
416  O O   . ILE A 93  ? 1.77668 1.21153 2.55679 0.09499  0.07420  -0.18945 -28 ILE A O   
417  C CB  . ILE A 93  ? 1.71871 1.12201 2.39123 0.06226  0.06757  -0.12315 -28 ILE A CB  
418  C CG1 . ILE A 93  ? 1.66847 1.10942 2.34886 0.05414  0.06734  -0.15472 -28 ILE A CG1 
419  C CG2 . ILE A 93  ? 1.70051 1.06167 2.33956 0.05046  0.07015  -0.09454 -28 ILE A CG2 
420  C CD1 . ILE A 93  ? 1.60719 1.06719 2.24260 0.03591  0.06168  -0.14659 -28 ILE A CD1 
421  N N   . GLN A 94  ? 1.85122 1.28033 2.59523 0.10229  0.06487  -0.14426 -27 GLN A N   
422  C CA  . GLN A 94  ? 1.88757 1.35921 2.65736 0.11565  0.06064  -0.16578 -27 GLN A CA  
423  C C   . GLN A 94  ? 1.82787 1.35928 2.57956 0.10597  0.05386  -0.18169 -27 GLN A C   
424  O O   . GLN A 94  ? 1.91209 1.44964 2.64092 0.08994  0.05393  -0.18382 -27 GLN A O   
425  C CB  . GLN A 94  ? 1.94757 1.41470 2.71403 0.12832  0.05567  -0.14432 -27 GLN A CB  
426  C CG  . GLN A 94  ? 2.01243 1.41801 2.78726 0.13547  0.06117  -0.12224 -27 GLN A CG  
427  C CD  . GLN A 94  ? 2.07316 1.46948 2.82286 0.13962  0.05506  -0.08970 -27 GLN A CD  
428  O OE1 . GLN A 94  ? 2.08693 1.52512 2.82038 0.14059  0.04663  -0.08646 -27 GLN A OE1 
429  N NE2 . GLN A 94  ? 2.08781 1.42929 2.83376 0.14164  0.05923  -0.06520 -27 GLN A NE2 
430  N N   . ALA A 95  ? 1.73110 1.30709 2.49244 0.11553  0.04778  -0.19288 -26 ALA A N   
431  C CA  . ALA A 95  ? 1.65427 1.28904 2.39593 0.10645  0.04051  -0.20529 -26 ALA A CA  
432  C C   . ALA A 95  ? 1.67163 1.33301 2.38094 0.10540  0.03094  -0.18277 -26 ALA A C   
433  O O   . ALA A 95  ? 1.54225 1.24549 2.22306 0.09333  0.02423  -0.18476 -26 ALA A O   
434  C CB  . ALA A 95  ? 1.63455 1.30977 2.41508 0.11646  0.04135  -0.24329 -26 ALA A CB  
435  N N   . ASP A 96  ? 1.74521 1.38341 2.45744 0.11715  0.02985  -0.16134 -25 ASP A N   
436  C CA  . ASP A 96  ? 1.79794 1.45813 2.48020 0.11671  0.02080  -0.13816 -25 ASP A CA  
437  C C   . ASP A 96  ? 1.77079 1.39629 2.40840 0.10408  0.01877  -0.10157 -25 ASP A C   
438  O O   . ASP A 96  ? 1.82787 1.45883 2.44119 0.10493  0.01202  -0.07730 -25 ASP A O   
439  C CB  . ASP A 96  ? 1.86141 1.51984 2.57216 0.13752  0.01978  -0.13616 -25 ASP A CB  
440  C CG  . ASP A 96  ? 1.90125 1.60003 2.65313 0.15074  0.02038  -0.17172 -25 ASP A CG  
441  O OD1 . ASP A 96  ? 1.89363 1.64027 2.64093 0.14278  0.01765  -0.19269 -25 ASP A OD1 
442  O OD2 . ASP A 96  ? 1.93623 1.61844 2.72452 0.16915  0.02339  -0.17879 -25 ASP A OD2 
443  N N   . GLN A 97  ? 1.70852 1.29896 2.33488 0.09258  0.02435  -0.09728 -24 GLN A N   
444  C CA  . GLN A 97  ? 1.63384 1.19152 2.21698 0.07995  0.02275  -0.06419 -24 GLN A CA  
445  C C   . GLN A 97  ? 1.57947 1.17096 2.12112 0.06119  0.01590  -0.06287 -24 GLN A C   
446  O O   . GLN A 97  ? 1.49547 1.11589 2.04429 0.05457  0.01649  -0.08881 -24 GLN A O   
447  C CB  . GLN A 97  ? 1.64522 1.14495 2.23773 0.07786  0.03260  -0.05878 -24 GLN A CB  
448  C CG  . GLN A 97  ? 1.65955 1.12329 2.29455 0.09540  0.03978  -0.06236 -24 GLN A CG  
449  C CD  . GLN A 97  ? 1.71413 1.11881 2.35367 0.09194  0.04912  -0.05250 -24 GLN A CD  
450  O OE1 . GLN A 97  ? 1.77234 1.13429 2.40590 0.09623  0.05111  -0.02698 -24 GLN A OE1 
451  N NE2 . GLN A 97  ? 1.64330 1.04583 2.29323 0.08385  0.05485  -0.07266 -24 GLN A NE2 
452  N N   . THR A 98  ? 1.58337 1.17025 2.08102 0.05260  0.00905  -0.03242 -23 THR A N   
453  C CA  . THR A 98  ? 1.58594 1.19994 2.03774 0.03459  0.00107  -0.02494 -23 THR A CA  
454  C C   . THR A 98  ? 1.66158 1.23288 2.08260 0.02111  0.00387  -0.00638 -23 THR A C   
455  O O   . THR A 98  ? 1.64389 1.16473 2.06724 0.02545  0.00952  0.01265  -23 THR A O   
456  C CB  . THR A 98  ? 1.59628 1.23500 2.01755 0.03379  -0.00939 -0.00270 -23 THR A CB  
457  O OG1 . THR A 98  ? 1.64656 1.23904 2.04900 0.03581  -0.00904 0.03122  -23 THR A OG1 
458  C CG2 . THR A 98  ? 1.58928 1.26622 2.04346 0.04924  -0.01154 -0.01891 -23 THR A CG2 
459  N N   . PRO A 99  ? 1.64348 1.23433 2.03555 0.00479  -0.00006 -0.01206 -22 PRO A N   
460  C CA  . PRO A 99  ? 1.60847 1.16085 1.97092 -0.00802 0.00232  0.00387  -22 PRO A CA  
461  C C   . PRO A 99  ? 1.64437 1.15847 1.97327 -0.00983 0.00007  0.04223  -22 PRO A C   
462  O O   . PRO A 99  ? 1.60635 1.07399 1.92739 -0.01332 0.00608  0.05575  -22 PRO A O   
463  C CB  . PRO A 99  ? 1.58631 1.17740 1.91660 -0.02459 -0.00543 -0.00580 -22 PRO A CB  
464  C CG  . PRO A 99  ? 1.61332 1.25445 1.97453 -0.01919 -0.00648 -0.03836 -22 PRO A CG  
465  C CD  . PRO A 99  ? 1.65381 1.30217 2.04239 -0.00219 -0.00620 -0.03613 -22 PRO A CD  
466  N N   . GLU A 100 ? 1.63310 1.16569 1.94165 -0.00778 -0.00841 0.06022  -21 GLU A N   
467  C CA  . GLU A 100 ? 1.63846 1.13460 1.91537 -0.00900 -0.01084 0.09701  -21 GLU A CA  
468  C C   . GLU A 100 ? 1.65507 1.10331 1.96260 0.00530  -0.00166 0.10622  -21 GLU A C   
469  O O   . GLU A 100 ? 1.66518 1.06942 1.95095 0.00307  0.00005  0.13394  -21 GLU A O   
470  C CB  . GLU A 100 ? 1.69044 1.22017 1.94132 -0.00965 -0.02226 0.11247  -21 GLU A CB  
471  C CG  . GLU A 100 ? 1.77733 1.27515 1.98581 -0.01459 -0.02698 0.15118  -21 GLU A CG  
472  C CD  . GLU A 100 ? 1.83347 1.36253 2.02359 -0.01258 -0.03743 0.16595  -21 GLU A CD  
473  O OE1 . GLU A 100 ? 1.84849 1.40837 2.07094 -0.00054 -0.03795 0.15064  -21 GLU A OE1 
474  O OE2 . GLU A 100 ? 1.84459 1.36764 1.98778 -0.02303 -0.04528 0.19274  -21 GLU A OE2 
475  N N   . ASP A 101 ? 1.65913 1.11439 2.01624 0.01986  0.00413  0.08341  -20 ASP A N   
476  C CA  . ASP A 101 ? 1.70789 1.11783 2.09532 0.03374  0.01236  0.09104  -20 ASP A CA  
477  C C   . ASP A 101 ? 1.85258 1.21361 2.24394 0.02879  0.02224  0.09338  -20 ASP A C   
478  O O   . ASP A 101 ? 1.82081 1.13409 2.20706 0.03172  0.02649  0.11674  -20 ASP A O   
479  C CB  . ASP A 101 ? 1.67886 1.10922 2.11811 0.05024  0.01564  0.06387  -20 ASP A CB  
480  C CG  . ASP A 101 ? 1.71236 1.18514 2.15126 0.05802  0.00674  0.06483  -20 ASP A CG  
481  O OD1 . ASP A 101 ? 1.73740 1.19921 2.15195 0.05932  0.00137  0.09328  -20 ASP A OD1 
482  O OD2 . ASP A 101 ? 1.73086 1.24843 2.19396 0.06283  0.00513  0.03701  -20 ASP A OD2 
483  N N   . LEU A 102 ? 1.98819 1.36055 2.38850 0.02109  0.02600  0.06952  -19 LEU A N   
484  C CA  . LEU A 102 ? 2.09563 1.42566 2.50492 0.01691  0.03591  0.06769  -19 LEU A CA  
485  C C   . LEU A 102 ? 2.05056 1.37229 2.41514 -0.00063 0.03348  0.08086  -19 LEU A C   
486  O O   . LEU A 102 ? 2.02130 1.32108 2.39203 -0.00658 0.04063  0.07269  -19 LEU A O   
487  C CB  . LEU A 102 ? 2.17460 1.51688 2.62965 0.02173  0.04300  0.03132  -19 LEU A CB  
488  C CG  . LEU A 102 ? 2.21570 1.60607 2.67139 0.01347  0.03950  0.00256  -19 LEU A CG  
489  C CD1 . LEU A 102 ? 2.23277 1.61699 2.73275 0.01768  0.04886  -0.02784 -19 LEU A CD1 
490  C CD2 . LEU A 102 ? 2.21178 1.65579 2.66870 0.01810  0.03062  -0.00790 -19 LEU A CD2 
491  N N   . ASP A 103 ? 2.04781 1.38626 2.36750 -0.00882 0.02332  0.10119  -18 ASP A N   
492  C CA  . ASP A 103 ? 2.06184 1.38363 2.33375 -0.02401 0.02015  0.12124  -18 ASP A CA  
493  C C   . ASP A 103 ? 1.94354 1.27643 2.21366 -0.03525 0.02229  0.09975  -18 ASP A C   
494  O O   . ASP A 103 ? 1.93107 1.23168 2.18504 -0.04316 0.02659  0.10879  -18 ASP A O   
495  C CB  . ASP A 103 ? 2.14662 1.41003 2.40874 -0.02237 0.02639  0.14942  -18 ASP A CB  
496  C CG  . ASP A 103 ? 2.25397 1.50555 2.50526 -0.01429 0.02212  0.17610  -18 ASP A CG  
497  O OD1 . ASP A 103 ? 2.29563 1.58556 2.54173 -0.01139 0.01342  0.17484  -18 ASP A OD1 
498  O OD2 . ASP A 103 ? 2.28421 1.50945 2.51160 -0.01095 0.02545  0.19054  -18 ASP A OD2 
499  N N   . MET A 104 ? 1.80634 1.18549 2.09306 -0.03595 0.01924  0.07089  -17 MET A N   
500  C CA  . MET A 104 ? 1.69914 1.09297 1.98181 -0.04714 0.01983  0.05015  -17 MET A CA  
501  C C   . MET A 104 ? 1.63030 1.05748 1.86507 -0.06124 0.00760  0.05639  -17 MET A C   
502  O O   . MET A 104 ? 1.55234 1.00690 1.76855 -0.06094 -0.00141 0.06609  -17 MET A O   
503  C CB  . MET A 104 ? 1.65801 1.07915 1.98832 -0.04053 0.02464  0.01282  -17 MET A CB  
504  C CG  . MET A 104 ? 1.59743 1.05745 1.95204 -0.02951 0.02086  -0.00065 -17 MET A CG  
505  S SD  . MET A 104 ? 1.61239 1.08996 2.02608 -0.02090 0.02919  -0.04346 -17 MET A SD  
506  C CE  . MET A 104 ? 1.54901 1.08746 1.97577 -0.01334 0.02120  -0.06081 -17 MET A CE  
507  N N   . GLU A 105 ? 1.54175 0.96597 1.75646 -0.07377 0.00715  0.05076  -16 GLU A N   
508  C CA  . GLU A 105 ? 1.47091 0.91561 1.63488 -0.08868 -0.00412 0.06017  -16 GLU A CA  
509  C C   . GLU A 105 ? 1.36462 0.84618 1.53349 -0.09703 -0.00670 0.02993  -16 GLU A C   
510  O O   . GLU A 105 ? 1.36109 0.84983 1.57199 -0.09155 0.00074  0.00239  -16 GLU A O   
511  C CB  . GLU A 105 ? 1.48980 0.89113 1.61590 -0.09696 -0.00367 0.08688  -16 GLU A CB  
512  C CG  . GLU A 105 ? 1.61295 0.97541 1.76384 -0.09506 0.00862  0.07966  -16 GLU A CG  
513  C CD  . GLU A 105 ? 1.70357 1.02108 1.81955 -0.10120 0.01000  0.10800  -16 GLU A CD  
514  O OE1 . GLU A 105 ? 1.70773 1.02901 1.77489 -0.11049 0.00006  0.12801  -16 GLU A OE1 
515  O OE2 . GLU A 105 ? 1.70960 0.98790 1.84669 -0.09682 0.02098  0.11028  -16 GLU A OE2 
516  N N   . ASP A 106 ? 1.30240 0.80700 1.42648 -0.11063 -0.01787 0.03573  -15 ASP A N   
517  C CA  . ASP A 106 ? 1.29601 0.83988 1.41828 -0.11980 -0.02259 0.00906  -15 ASP A CA  
518  C C   . ASP A 106 ? 1.23934 0.76428 1.38355 -0.12177 -0.01387 -0.01020 -15 ASP A C   
519  O O   . ASP A 106 ? 1.24858 0.73033 1.38602 -0.12281 -0.00804 0.00374  -15 ASP A O   
520  C CB  . ASP A 106 ? 1.10366 0.66483 1.16812 -0.13525 -0.03613 0.02362  -15 ASP A CB  
521  C CG  . ASP A 106 ? 1.21314 0.81486 1.27156 -0.14580 -0.04215 -0.00247 -15 ASP A CG  
522  O OD1 . ASP A 106 ? 1.25082 0.88980 1.34095 -0.14108 -0.04125 -0.02798 -15 ASP A OD1 
523  O OD2 . ASP A 106 ? 1.31691 0.91314 1.33809 -0.15877 -0.04809 0.00258  -15 ASP A OD2 
524  N N   . ASN A 107 ? 1.22843 0.78691 1.39949 -0.12228 -0.01295 -0.04271 -14 ASN A N   
525  C CA  . ASN A 107 ? 1.12484 0.67348 1.31973 -0.12448 -0.00550 -0.06558 -14 ASN A CA  
526  C C   . ASN A 107 ? 1.19530 0.70374 1.43280 -0.11268 0.00846  -0.06741 -14 ASN A C   
527  O O   . ASN A 107 ? 1.26309 0.74971 1.51299 -0.11540 0.01537  -0.07701 -14 ASN A O   
528  C CB  . ASN A 107 ? 1.15743 0.69265 1.31067 -0.13896 -0.01034 -0.05697 -14 ASN A CB  
529  C CG  . ASN A 107 ? 1.16317 0.74238 1.29025 -0.15136 -0.02172 -0.07157 -14 ASN A CG  
530  O OD1 . ASN A 107 ? 1.12735 0.71040 1.25182 -0.15935 -0.02199 -0.08785 -14 ASN A OD1 
531  N ND2 . ASN A 107 ? 1.12640 0.73927 1.23351 -0.15332 -0.03141 -0.06558 -14 ASN A ND2 
532  N N   . ASP A 108 ? 1.30054 0.79838 1.56092 -0.09975 0.01264  -0.05851 -13 ASP A N   
533  C CA  . ASP A 108 ? 1.32116 0.78442 1.62567 -0.08840 0.02556  -0.06404 -13 ASP A CA  
534  C C   . ASP A 108 ? 1.33481 0.82294 1.68680 -0.08264 0.03067  -0.10077 -13 ASP A C   
535  O O   . ASP A 108 ? 1.29417 0.82809 1.64838 -0.08447 0.02438  -0.12009 -13 ASP A O   
536  C CB  . ASP A 108 ? 1.33820 0.78035 1.65207 -0.07609 0.02801  -0.04291 -13 ASP A CB  
537  C CG  . ASP A 108 ? 1.49173 0.89320 1.76877 -0.07991 0.02736  -0.00699 -13 ASP A CG  
538  O OD1 . ASP A 108 ? 1.51009 0.89704 1.75725 -0.09126 0.02607  0.00074  -13 ASP A OD1 
539  O OD2 . ASP A 108 ? 1.54741 0.93131 1.82523 -0.07131 0.02799  0.01340  -13 ASP A OD2 
540  N N   . ILE A 109 ? 1.31916 0.77626 1.70903 -0.07590 0.04221  -0.11028 -12 ILE A N   
541  C CA  . ILE A 109 ? 1.32027 0.79372 1.75594 -0.07088 0.04812  -0.14484 -12 ILE A CA  
542  C C   . ILE A 109 ? 1.39458 0.84651 1.87469 -0.05482 0.05686  -0.14754 -12 ILE A C   
543  O O   . ILE A 109 ? 1.44951 0.85646 1.93380 -0.05073 0.06365  -0.12843 -12 ILE A O   
544  C CB  . ILE A 109 ? 1.37615 0.83429 1.81633 -0.07974 0.05343  -0.15809 -12 ILE A CB  
545  C CG1 . ILE A 109 ? 1.32204 0.78536 1.81476 -0.07271 0.06173  -0.19066 -12 ILE A CG1 
546  C CG2 . ILE A 109 ? 1.42704 0.83380 1.85221 -0.08240 0.05933  -0.13246 -12 ILE A CG2 
547  C CD1 . ILE A 109 ? 1.45628 0.90595 1.95590 -0.08119 0.06702  -0.20473 -12 ILE A CD1 
548  N N   . ILE A 110 ? 1.33850 0.82241 1.85101 -0.04574 0.05644  -0.17122 -11 ILE A N   
549  C CA  . ILE A 110 ? 1.39847 0.86592 1.95776 -0.03004 0.06439  -0.18024 -11 ILE A CA  
550  C C   . ILE A 110 ? 1.47718 0.95130 2.07673 -0.02867 0.07104  -0.21446 -11 ILE A C   
551  O O   . ILE A 110 ? 1.38568 0.89684 1.98264 -0.03581 0.06692  -0.23673 -11 ILE A O   
552  C CB  . ILE A 110 ? 1.40104 0.89779 1.96853 -0.01871 0.05892  -0.18047 -11 ILE A CB  
553  C CG1 . ILE A 110 ? 1.40343 0.95870 1.96464 -0.02343 0.05073  -0.20277 -11 ILE A CG1 
554  C CG2 . ILE A 110 ? 1.43465 0.91621 1.96766 -0.01826 0.05384  -0.14472 -11 ILE A CG2 
555  C CD1 . ILE A 110 ? 1.40906 0.99744 1.97820 -0.01273 0.04524  -0.20434 -11 ILE A CD1 
556  N N   . GLU A 111 ? 1.57102 1.00856 2.20702 -0.01996 0.08112  -0.21838 -10 GLU A N   
557  C CA  . GLU A 111 ? 1.48605 0.92241 2.16109 -0.01879 0.08833  -0.24867 -10 GLU A CA  
558  C C   . GLU A 111 ? 1.42848 0.88172 2.14689 -0.00371 0.09014  -0.27118 -10 GLU A C   
559  O O   . GLU A 111 ? 1.47599 0.90922 2.20975 0.00872  0.09239  -0.25970 -10 GLU A O   
560  C CB  . GLU A 111 ? 1.61110 1.02096 2.27343 -0.01961 0.09496  -0.23006 -10 GLU A CB  
561  C CG  . GLU A 111 ? 1.61168 1.01994 2.23816 -0.03424 0.09388  -0.22171 -10 GLU A CG  
562  C CD  . GLU A 111 ? 1.63476 1.02291 2.24633 -0.03411 0.09944  -0.20404 -10 GLU A CD  
563  O OE1 . GLU A 111 ? 1.64030 1.02111 2.27480 -0.02443 0.10455  -0.20558 -10 GLU A OE1 
564  O OE2 . GLU A 111 ? 1.68699 1.06705 2.26329 -0.04385 0.09815  -0.18922 -10 GLU A OE2 
565  N N   . ALA A 112 ? 1.34450 0.83378 2.08249 -0.00460 0.08903  -0.30339 -9  ALA A N   
566  C CA  . ALA A 112 ? 1.35977 0.87019 2.13819 0.00936  0.09012  -0.32813 -9  ALA A CA  
567  C C   . ALA A 112 ? 1.48538 0.98938 2.29383 0.01163  0.09762  -0.34696 -9  ALA A C   
568  O O   . ALA A 112 ? 1.43191 0.95984 2.24307 0.00376  0.09728  -0.36838 -9  ALA A O   
569  C CB  . ALA A 112 ? 1.25553 0.82515 2.02413 0.00710  0.08134  -0.34605 -9  ALA A CB  
570  N N   . HIS A 113 ? 1.52923 1.01117 2.34903 0.02141  0.10254  -0.33326 -8  HIS A N   
571  C CA  . HIS A 113 ? 1.53317 1.01794 2.37369 0.02426  0.10778  -0.34491 -8  HIS A CA  
572  C C   . HIS A 113 ? 1.62079 1.12556 2.50161 0.03802  0.10759  -0.37077 -8  HIS A C   
573  O O   . HIS A 113 ? 1.58468 1.09016 2.47752 0.04916  0.10491  -0.37100 -8  HIS A O   
574  C CB  . HIS A 113 ? 1.56193 1.01191 2.39035 0.02599  0.11258  -0.31709 -8  HIS A CB  
575  C CG  . HIS A 113 ? 1.58174 1.01287 2.36989 0.01383  0.11301  -0.29162 -8  HIS A CG  
576  N ND1 . HIS A 113 ? 1.57361 1.00183 2.35060 0.00513  0.11653  -0.28973 -8  HIS A ND1 
577  C CD2 . HIS A 113 ? 1.56257 0.97755 2.31843 0.00932  0.11002  -0.26700 -8  HIS A CD2 
578  C CE1 . HIS A 113 ? 1.62213 1.03400 2.36159 -0.00358 0.11566  -0.26590 -8  HIS A CE1 
579  N NE2 . HIS A 113 ? 1.54313 0.94640 2.26825 -0.00158 0.11168  -0.25138 -8  HIS A NE2 
580  N N   . ARG A 114 ? 1.72289 1.24483 2.62436 0.03760  0.11015  -0.39250 -7  ARG A N   
581  C CA  . ARG A 114 ? 1.82713 1.36500 2.76553 0.05105  0.11031  -0.41480 -7  ARG A CA  
582  C C   . ARG A 114 ? 1.88521 1.39262 2.83248 0.06189  0.11345  -0.39681 -7  ARG A C   
583  O O   . ARG A 114 ? 1.91569 1.39217 2.84143 0.05772  0.11621  -0.36967 -7  ARG A O   
584  C CB  . ARG A 114 ? 1.84951 1.41265 2.80594 0.04696  0.11189  -0.44122 -7  ARG A CB  
585  C CG  . ARG A 114 ? 1.87705 1.47084 2.82195 0.03502  0.10855  -0.45883 -7  ARG A CG  
586  C CD  . ARG A 114 ? 1.91882 1.52335 2.86715 0.02623  0.11135  -0.47002 -7  ARG A CD  
587  N NE  . ARG A 114 ? 1.97049 1.54338 2.90386 0.02108  0.11620  -0.44573 -7  ARG A NE  
588  C CZ  . ARG A 114 ? 1.95669 1.52263 2.86163 0.00843  0.11674  -0.43263 -7  ARG A CZ  
589  N NH1 . ARG A 114 ? 1.91633 1.50312 2.80382 -0.00102 0.11243  -0.44085 -7  ARG A NH1 
590  N NH2 . ARG A 114 ? 1.95675 1.49578 2.84972 0.00524  0.12123  -0.41192 -7  ARG A NH2 
591  N N   . GLU A 115 ? 1.94431 1.46172 2.92227 0.07605  0.11260  -0.41273 -6  GLU A N   
592  C CA  . GLU A 115 ? 2.07313 1.56293 3.06000 0.08721  0.11450  -0.39764 -6  GLU A CA  
593  C C   . GLU A 115 ? 2.30847 1.81427 3.33077 0.09788  0.11476  -0.42309 -6  GLU A C   
594  O O   . GLU A 115 ? 2.27118 1.79976 3.31427 0.10917  0.11125  -0.44145 -6  GLU A O   
595  C CB  . GLU A 115 ? 2.05375 1.53028 3.03333 0.09645  0.11131  -0.37974 -6  GLU A CB  
596  C CG  . GLU A 115 ? 2.06763 1.51132 3.04821 0.10572  0.11300  -0.35892 -6  GLU A CG  
597  C CD  . GLU A 115 ? 2.07900 1.50857 3.04935 0.11405  0.10958  -0.33824 -6  GLU A CD  
598  O OE1 . GLU A 115 ? 2.06427 1.51647 3.04565 0.12099  0.10530  -0.35040 -6  GLU A OE1 
599  O OE2 . GLU A 115 ? 2.10652 1.50356 3.05741 0.11379  0.11095  -0.31011 -6  GLU A OE2 
600  N N   . GLN A 116 ? 2.55157 2.04608 3.58002 0.09446  0.11868  -0.42419 -5  GLN A N   
601  C CA  . GLN A 116 ? 2.79509 2.29855 3.85465 0.10367  0.11908  -0.44502 -5  GLN A CA  
602  C C   . GLN A 116 ? 2.89740 2.36503 3.95696 0.10759  0.12216  -0.42738 -5  GLN A C   
603  O O   . GLN A 116 ? 2.93344 2.39701 4.00494 0.10566  0.12483  -0.43562 -5  GLN A O   
604  C CB  . GLN A 116 ? 2.86896 2.39879 3.93918 0.09497  0.12021  -0.46916 -5  GLN A CB  
605  C CG  . GLN A 116 ? 2.90981 2.47772 3.97994 0.09083  0.11670  -0.48948 -5  GLN A CG  
606  C CD  . GLN A 116 ? 2.96999 2.56534 4.06491 0.10484  0.11257  -0.51232 -5  GLN A CD  
607  O OE1 . GLN A 116 ? 3.00884 2.60484 4.12790 0.11563  0.11259  -0.52360 -5  GLN A OE1 
608  N NE2 . GLN A 116 ? 2.96657 2.58551 4.05487 0.10489  0.10878  -0.51975 -5  GLN A NE2 
609  N N   . ILE A 117 ? 2.95099 2.39211 3.99607 0.11296  0.12150  -0.40260 -4  ILE A N   
610  C CA  . ILE A 117 ? 3.01120 2.41620 4.04934 0.11488  0.12417  -0.38247 -4  ILE A CA  
611  C C   . ILE A 117 ? 3.12485 2.52811 4.19220 0.12772  0.12339  -0.39766 -4  ILE A C   
612  O O   . ILE A 117 ? 3.13149 2.52434 4.20658 0.12500  0.12623  -0.40198 -4  ILE A O   
613  C CB  . ILE A 117 ? 2.95262 2.33185 3.96607 0.11734  0.12296  -0.35234 -4  ILE A CB  
614  C CG1 . ILE A 117 ? 2.94805 2.29317 3.95938 0.12357  0.12425  -0.33574 -4  ILE A CG1 
615  C CG2 . ILE A 117 ? 2.93168 2.32771 3.95206 0.12751  0.11806  -0.35675 -4  ILE A CG2 
616  C CD1 . ILE A 117 ? 2.91729 2.23551 3.90015 0.12397  0.12333  -0.30429 -4  ILE A CD1 
617  N N   . GLY A 118 ? 3.20320 2.61659 4.28689 0.14216  0.11929  -0.40597 -3  GLY A N   
618  C CA  . GLY A 118 ? 3.28386 2.69667 4.39447 0.15581  0.11773  -0.42071 -3  GLY A CA  
619  C C   . GLY A 118 ? 3.32104 2.77157 4.45885 0.15936  0.11601  -0.45468 -3  GLY A C   
620  O O   . GLY A 118 ? 3.31365 2.78892 4.44983 0.14904  0.11684  -0.46783 -3  GLY A O   
621  N N   . GLY A 119 ? 2.40726 2.85912 2.82287 -0.04084 -0.05505 0.19812  -2  GLY A N   
622  C CA  . GLY A 119 ? 2.41659 2.89846 2.84534 -0.03751 -0.03133 0.20091  -2  GLY A CA  
623  C C   . GLY A 119 ? 2.38409 2.84580 2.77366 -0.02980 -0.01255 0.18871  -2  GLY A C   
624  O O   . GLY A 119 ? 2.39255 2.82038 2.75175 -0.02203 -0.01555 0.17777  -2  GLY A O   
625  N N   . GLU A 120 ? 2.32172 2.80550 2.71235 -0.03250 0.00756  0.19082  -1  GLU A N   
626  C CA  . GLU A 120 ? 2.22272 2.69386 2.57872 -0.02692 0.02667  0.17906  -1  GLU A CA  
627  C C   . GLU A 120 ? 1.90123 2.33165 2.21517 -0.03253 0.01925  0.16951  -1  GLU A C   
628  O O   . GLU A 120 ? 1.83482 2.26078 2.13836 -0.04653 0.01431  0.17410  -1  GLU A O   
629  C CB  . GLU A 120 ? 2.35573 2.85680 2.71597 -0.03377 0.04508  0.18535  -1  GLU A CB  
630  C CG  . GLU A 120 ? 2.42689 2.96792 2.82338 -0.02550 0.06019  0.19181  -1  GLU A CG  
631  C CD  . GLU A 120 ? 2.49124 3.05769 2.88240 -0.03060 0.08175  0.19607  -1  GLU A CD  
632  O OE1 . GLU A 120 ? 2.50771 3.06412 2.87200 -0.04243 0.08134  0.19732  -1  GLU A OE1 
633  O OE2 . GLU A 120 ? 2.52465 3.12159 2.93833 -0.02229 0.09934  0.19865  -1  GLU A OE2 
634  N N   . PHE A 121 ? 1.66745 2.06812 1.95874 -0.02151 0.01923  0.15694  0   PHE A N   
635  C CA  . PHE A 121 ? 1.56383 1.92562 1.81822 -0.02620 0.01267  0.14788  0   PHE A CA  
636  C C   . PHE A 121 ? 1.29274 1.64683 1.51723 -0.02672 0.02985  0.13670  0   PHE A C   
637  O O   . PHE A 121 ? 1.15741 1.51992 1.37993 -0.01669 0.04654  0.12922  0   PHE A O   
638  C CB  . PHE A 121 ? 1.62338 1.95402 1.86737 -0.01555 0.00279  0.14127  0   PHE A CB  
639  C CG  . PHE A 121 ? 1.64270 1.94604 1.87267 -0.02429 -0.01630 0.14273  0   PHE A CG  
640  C CD1 . PHE A 121 ? 1.66044 1.97318 1.89987 -0.03925 -0.02657 0.15172  0   PHE A CD1 
641  C CD2 . PHE A 121 ? 1.73516 2.00185 1.94126 -0.01758 -0.02251 0.13502  0   PHE A CD2 
642  C CE1 . PHE A 121 ? 1.73718 2.02339 1.96283 -0.04692 -0.04271 0.15167  0   PHE A CE1 
643  C CE2 . PHE A 121 ? 1.80073 2.04186 1.99156 -0.02538 -0.03830 0.13572  0   PHE A CE2 
644  C CZ  . PHE A 121 ? 1.79957 2.05039 2.00008 -0.03989 -0.04833 0.14331  0   PHE A CZ  
645  N N   . MET A 122 ? 1.11680 1.45489 1.31870 -0.03848 0.02522  0.13518  1   MET A N   
646  C CA  . MET A 122 ? 0.86437 1.19658 1.03815 -0.04153 0.03790  0.12525  1   MET A CA  
647  C C   . MET A 122 ? 0.79712 1.09457 0.94481 -0.03388 0.04125  0.10909  1   MET A C   
648  O O   . MET A 122 ? 0.79773 1.06831 0.94085 -0.03122 0.03009  0.10757  1   MET A O   
649  C CB  . MET A 122 ? 0.85319 1.18333 1.01710 -0.05659 0.03025  0.13147  1   MET A CB  
650  C CG  . MET A 122 ? 0.99915 1.35868 1.18953 -0.06538 0.02575  0.14894  1   MET A CG  
651  S SD  . MET A 122 ? 0.96799 1.31025 1.16936 -0.07546 0.00323  0.15849  1   MET A SD  
652  C CE  . MET A 122 ? 0.89765 1.27879 1.13651 -0.08404 0.00222  0.17809  1   MET A CE  
653  N N   . GLN A 123 ? 0.78627 1.08381 0.91622 -0.03057 0.05713  0.09688  2   GLN A N   
654  C CA  . GLN A 123 ? 0.86088 1.12495 0.96560 -0.02582 0.06182  0.08070  2   GLN A CA  
655  C C   . GLN A 123 ? 0.87152 1.11549 0.95458 -0.03793 0.05421  0.07744  2   GLN A C   
656  O O   . GLN A 123 ? 0.77416 1.03432 0.85397 -0.04878 0.05274  0.08249  2   GLN A O   
657  C CB  . GLN A 123 ? 0.80453 1.07512 0.89807 -0.01937 0.08124  0.06709  2   GLN A CB  
658  C CG  . GLN A 123 ? 0.87763 1.11762 0.96080 -0.00746 0.08838  0.05291  2   GLN A CG  
659  C CD  . GLN A 123 ? 0.95167 1.19429 1.02138 -0.00240 0.10786  0.03690  2   GLN A CD  
660  O OE1 . GLN A 123 ? 0.95918 1.22538 1.02188 -0.00887 0.11549  0.03514  2   GLN A OE1 
661  N NE2 . GLN A 123 ? 0.92512 1.14226 0.98988 0.00936  0.11621  0.02508  2   GLN A NE2 
662  N N   . LYS A 124 ? 0.72050 0.92941 0.78945 -0.03550 0.05013  0.06971  3   LYS A N   
663  C CA  . LYS A 124 ? 0.80467 0.99236 0.85459 -0.04557 0.04488  0.06513  3   LYS A CA  
664  C C   . LYS A 124 ? 0.74422 0.91601 0.77276 -0.04490 0.05724  0.04753  3   LYS A C   
665  O O   . LYS A 124 ? 0.69122 0.84210 0.71444 -0.03523 0.06437  0.03823  3   LYS A O   
666  C CB  . LYS A 124 ? 0.76067 0.91943 0.80861 -0.04480 0.03257  0.06887  3   LYS A CB  
667  C CG  . LYS A 124 ? 0.75971 0.92845 0.82247 -0.05144 0.01753  0.08373  3   LYS A CG  
668  C CD  . LYS A 124 ? 0.88520 1.08136 0.97407 -0.04650 0.01435  0.09471  3   LYS A CD  
669  C CE  . LYS A 124 ? 0.92953 1.11286 1.02393 -0.03315 0.01225  0.09371  3   LYS A CE  
670  N NZ  . LYS A 124 ? 0.76133 0.96818 0.88433 -0.03078 0.00247  0.10658  3   LYS A NZ  
671  N N   . LEU A 125 ? 0.65185 0.83335 0.66895 -0.05529 0.05915  0.04326  4   LEU A N   
672  C CA  . LEU A 125 ? 0.74362 0.91217 0.74079 -0.05783 0.06857  0.02579  4   LEU A CA  
673  C C   . LEU A 125 ? 0.75959 0.90771 0.74725 -0.06743 0.06083  0.02366  4   LEU A C   
674  O O   . LEU A 125 ? 0.72321 0.88428 0.71474 -0.07631 0.05175  0.03332  4   LEU A O   
675  C CB  . LEU A 125 ? 0.76194 0.95980 0.75221 -0.06231 0.07629  0.02146  4   LEU A CB  
676  C CG  . LEU A 125 ? 0.95907 1.18596 0.96030 -0.05513 0.08466  0.02683  4   LEU A CG  
677  C CD1 . LEU A 125 ? 1.03279 1.27716 1.01689 -0.05798 0.09631  0.01517  4   LEU A CD1 
678  C CD2 . LEU A 125 ? 1.08382 1.29902 1.09680 -0.04064 0.09096  0.02472  4   LEU A CD2 
679  N N   . LEU A 126 ? 0.70794 0.82415 0.68469 -0.06539 0.06538  0.01161  5   LEU A N   
680  C CA  . LEU A 126 ? 0.74036 0.83467 0.71019 -0.07332 0.06013  0.00937  5   LEU A CA  
681  C C   . LEU A 126 ? 0.73578 0.82206 0.69229 -0.07977 0.06812  -0.00799 5   LEU A C   
682  O O   . LEU A 126 ? 0.68655 0.76075 0.63586 -0.07450 0.07910  -0.02118 5   LEU A O   
683  C CB  . LEU A 126 ? 0.71823 0.77911 0.68699 -0.06655 0.05816  0.01190  5   LEU A CB  
684  C CG  . LEU A 126 ? 0.89987 0.96308 0.87972 -0.06233 0.04688  0.02797  5   LEU A CG  
685  C CD1 . LEU A 126 ? 0.91036 0.93981 0.88384 -0.05371 0.04665  0.02810  5   LEU A CD1 
686  C CD2 . LEU A 126 ? 0.91022 0.98115 0.89425 -0.07252 0.03622  0.03710  5   LEU A CD2 
687  N N   . SER A 127 ? 0.73558 0.82855 0.69040 -0.09115 0.06235  -0.00820 6   SER A N   
688  C CA  . SER A 127 ? 0.81534 0.89550 0.76083 -0.09889 0.06713  -0.02398 6   SER A CA  
689  C C   . SER A 127 ? 0.77894 0.82686 0.72534 -0.10012 0.06613  -0.02330 6   SER A C   
690  O O   . SER A 127 ? 0.75866 0.80812 0.71167 -0.10435 0.05759  -0.01271 6   SER A O   
691  C CB  . SER A 127 ? 0.79582 0.90406 0.74063 -0.11015 0.06092  -0.02432 6   SER A CB  
692  O OG  . SER A 127 ? 1.11728 1.21836 1.05358 -0.11767 0.06563  -0.04210 6   SER A OG  
693  N N   . LEU A 128 ? 0.78666 0.80431 0.72608 -0.09596 0.07590  -0.03417 7   LEU A N   
694  C CA  . LEU A 128 ? 0.87593 0.85913 0.81320 -0.09486 0.07800  -0.03297 7   LEU A CA  
695  C C   . LEU A 128 ? 0.97055 0.93376 0.90277 -0.10231 0.08728  -0.04927 7   LEU A C   
696  O O   . LEU A 128 ? 0.93025 0.90219 0.85908 -0.10614 0.09262  -0.06328 7   LEU A O   
697  C CB  . LEU A 128 ? 0.70205 0.66359 0.63607 -0.08108 0.08135  -0.02757 7   LEU A CB  
698  C CG  . LEU A 128 ? 0.74668 0.72483 0.68817 -0.07370 0.07148  -0.01146 7   LEU A CG  
699  C CD1 . LEU A 128 ? 0.74171 0.69702 0.68023 -0.06015 0.07390  -0.00713 7   LEU A CD1 
700  C CD2 . LEU A 128 ? 0.71797 0.70117 0.66412 -0.08014 0.06029  0.00013  7   LEU A CD2 
701  N N   . PRO A 129 ? 0.89636 0.83277 0.82796 -0.10524 0.08982  -0.04841 8   PRO A N   
702  C CA  . PRO A 129 ? 0.95124 0.86414 0.87989 -0.11160 0.10079  -0.06353 8   PRO A CA  
703  C C   . PRO A 129 ? 1.02427 0.91514 0.94466 -0.10266 0.11197  -0.07236 8   PRO A C   
704  O O   . PRO A 129 ? 1.03740 0.91712 0.95391 -0.08976 0.11251  -0.06342 8   PRO A O   
705  C CB  . PRO A 129 ? 0.86167 0.74840 0.79062 -0.11336 0.10265  -0.05661 8   PRO A CB  
706  C CG  . PRO A 129 ? 0.68907 0.59224 0.62219 -0.11120 0.09060  -0.04045 8   PRO A CG  
707  C CD  . PRO A 129 ? 0.72611 0.65001 0.65864 -0.10266 0.08426  -0.03424 8   PRO A CD  
708  N N   . SER A 130 ? 1.07529 0.96039 0.99411 -0.10959 0.12046  -0.09036 9   SER A N   
709  C CA  . SER A 130 ? 1.02920 0.89676 0.94130 -0.10130 0.13161  -0.10097 9   SER A CA  
710  C C   . SER A 130 ? 1.02939 0.85650 0.93668 -0.09025 0.13994  -0.09449 9   SER A C   
711  O O   . SER A 130 ? 1.05788 0.87465 0.96177 -0.07715 0.14535  -0.09398 9   SER A O   
712  C CB  . SER A 130 ? 1.01150 0.87554 0.92239 -0.11283 0.13920  -0.12313 9   SER A CB  
713  O OG  . SER A 130 ? 1.18416 1.03152 1.10043 -0.12481 0.14161  -0.12730 9   SER A OG  
714  N N   . ASN A 131 ? 0.97446 0.77859 0.88132 -0.09467 0.14159  -0.08890 10  ASN A N   
715  C CA  . ASN A 131 ? 0.98609 0.75086 0.88495 -0.08418 0.14930  -0.08099 10  ASN A CA  
716  C C   . ASN A 131 ? 0.96839 0.73853 0.86353 -0.06928 0.14044  -0.06340 10  ASN A C   
717  O O   . ASN A 131 ? 0.90857 0.65409 0.79731 -0.05611 0.14536  -0.05799 10  ASN A O   
718  C CB  . ASN A 131 ? 0.91741 0.65931 0.81518 -0.09281 0.15350  -0.07788 10  ASN A CB  
719  C CG  . ASN A 131 ? 0.93826 0.63818 0.82404 -0.08235 0.16191  -0.06828 10  ASN A CG  
720  O OD1 . ASN A 131 ? 1.03306 0.70919 0.91413 -0.07375 0.17122  -0.07205 10  ASN A OD1 
721  N ND2 . ASN A 131 ? 0.99781 0.68749 0.87757 -0.08259 0.15906  -0.05563 10  ASN A ND2 
722  N N   . LEU A 132 ? 0.87295 0.67495 0.77322 -0.07132 0.12690  -0.05407 11  LEU A N   
723  C CA  . LEU A 132 ? 0.84167 0.65198 0.74108 -0.05970 0.11657  -0.03791 11  LEU A CA  
724  C C   . LEU A 132 ? 1.04257 0.87465 0.94830 -0.04991 0.11510  -0.03843 11  LEU A C   
725  O O   . LEU A 132 ? 0.90419 0.73665 0.81088 -0.03754 0.10950  -0.02667 11  LEU A O   
726  C CB  . LEU A 132 ? 0.77588 0.60922 0.67998 -0.06700 0.10362  -0.02826 11  LEU A CB  
727  C CG  . LEU A 132 ? 0.99471 0.84309 0.90105 -0.05910 0.09027  -0.01265 11  LEU A CG  
728  C CD1 . LEU A 132 ? 0.81336 0.63040 0.70705 -0.05068 0.08875  -0.00240 11  LEU A CD1 
729  C CD2 . LEU A 132 ? 0.98141 0.85805 0.89638 -0.06887 0.07951  -0.00747 11  LEU A CD2 
730  N N   . VAL A 133 ? 0.94640 0.79755 0.85653 -0.05533 0.11997  -0.05196 12  VAL A N   
731  C CA  . VAL A 133 ? 0.87580 0.74659 0.79118 -0.04592 0.12202  -0.05427 12  VAL A CA  
732  C C   . VAL A 133 ? 1.02190 0.86418 0.93514 -0.03026 0.13082  -0.05357 12  VAL A C   
733  O O   . VAL A 133 ? 1.06401 0.91642 0.98403 -0.01718 0.12686  -0.04337 12  VAL A O   
734  C CB  . VAL A 133 ? 0.89081 0.78021 0.80573 -0.05512 0.12809  -0.07179 12  VAL A CB  
735  C CG1 . VAL A 133 ? 0.96609 0.86110 0.88247 -0.04381 0.13726  -0.07921 12  VAL A CG1 
736  C CG2 . VAL A 133 ? 0.81242 0.74001 0.73171 -0.06585 0.11678  -0.06738 12  VAL A CG2 
737  N N   . GLN A 134 ? 1.25194 1.05839 1.15765 -0.03135 0.14289  -0.06378 13  GLN A N   
738  C CA  . GLN A 134 ? 1.29999 1.07540 1.20358 -0.01629 0.15279  -0.06337 13  GLN A CA  
739  C C   . GLN A 134 ? 1.25963 1.02580 1.16259 -0.00257 0.14415  -0.04327 13  GLN A C   
740  O O   . GLN A 134 ? 1.23885 0.98982 1.14396 0.01322  0.14888  -0.03926 13  GLN A O   
741  C CB  . GLN A 134 ? 1.52680 1.26146 1.42210 -0.02226 0.16611  -0.07459 13  GLN A CB  
742  C CG  . GLN A 134 ? 1.69606 1.43629 1.59212 -0.03591 0.17457  -0.09674 13  GLN A CG  
743  C CD  . GLN A 134 ? 1.79392 1.55392 1.69419 -0.02928 0.17963  -0.10786 13  GLN A CD  
744  O OE1 . GLN A 134 ? 1.83820 1.58594 1.74123 -0.01308 0.18635  -0.10555 13  GLN A OE1 
745  N NE2 . GLN A 134 ? 1.81962 1.61066 1.72009 -0.04121 0.17675  -0.11963 13  GLN A NE2 
746  N N   . SER A 135 ? 1.13543 0.91014 1.03548 -0.00787 0.13123  -0.03084 14  SER A N   
747  C CA  . SER A 135 ? 1.03367 0.79167 0.92724 0.00248  0.12305  -0.01375 14  SER A CA  
748  C C   . SER A 135 ? 0.83141 0.62028 0.73151 0.00288  0.10542  -0.00038 14  SER A C   
749  O O   . SER A 135 ? 0.75575 0.53506 0.65126 0.01242  0.09642  0.01331  14  SER A O   
750  C CB  . SER A 135 ? 1.00003 0.72227 0.87728 -0.00406 0.12720  -0.01183 14  SER A CB  
751  O OG  . SER A 135 ? 1.16501 0.85041 1.03584 0.00006  0.14278  -0.01870 14  SER A OG  
752  N N   . PHE A 136 ? 0.78701 0.61165 0.69722 -0.00731 0.09988  -0.00366 15  PHE A N   
753  C CA  . PHE A 136 ? 0.79981 0.65038 0.71646 -0.00993 0.08377  0.00867  15  PHE A CA  
754  C C   . PHE A 136 ? 0.83444 0.69533 0.76042 0.00453  0.07477  0.02095  15  PHE A C   
755  O O   . PHE A 136 ? 0.84707 0.70688 0.77046 0.00635  0.06149  0.03308  15  PHE A O   
756  C CB  . PHE A 136 ? 0.82083 0.70873 0.74859 -0.02138 0.08141  0.00365  15  PHE A CB  
757  C CG  . PHE A 136 ? 0.91648 0.83481 0.85597 -0.02252 0.06657  0.01634  15  PHE A CG  
758  C CD1 . PHE A 136 ? 0.94004 0.85923 0.87646 -0.03182 0.05659  0.02282  15  PHE A CD1 
759  C CD2 . PHE A 136 ? 0.84127 0.78730 0.79664 -0.01468 0.06364  0.02140  15  PHE A CD2 
760  C CE1 . PHE A 136 ? 0.85559 0.80020 0.80372 -0.03370 0.04332  0.03387  15  PHE A CE1 
761  C CE2 . PHE A 136 ? 0.63211 0.60567 0.60060 -0.01706 0.05050  0.03315  15  PHE A CE2 
762  C CZ  . PHE A 136 ? 0.79311 0.76499 0.75765 -0.02689 0.04001  0.03921  15  PHE A CZ  
763  N N   . HIS A 137 ? 0.94978 0.82123 0.88743 0.01490  0.08173  0.01745  16  HIS A N   
764  C CA  . HIS A 137 ? 0.79927 0.68596 0.75138 0.02885  0.07321  0.02925  16  HIS A CA  
765  C C   . HIS A 137 ? 0.96440 0.81957 0.90558 0.04050  0.06779  0.03947  16  HIS A C   
766  O O   . HIS A 137 ? 0.84250 0.70796 0.78942 0.04618  0.05261  0.05255  16  HIS A O   
767  C CB  . HIS A 137 ? 0.74654 0.64929 0.71406 0.03852  0.08472  0.02234  16  HIS A CB  
768  C CG  . HIS A 137 ? 0.83582 0.77475 0.81337 0.02883  0.08817  0.01516  16  HIS A CG  
769  N ND1 . HIS A 137 ? 0.81991 0.75667 0.78998 0.02161  0.10200  -0.00134 16  HIS A ND1 
770  C CD2 . HIS A 137 ? 0.88723 0.86515 0.88076 0.02492  0.07947  0.02274  16  HIS A CD2 
771  C CE1 . HIS A 137 ? 0.87521 0.84829 0.85373 0.01433  0.10133  -0.00309 16  HIS A CE1 
772  N NE2 . HIS A 137 ? 0.85441 0.85252 0.84783 0.01624  0.08856  0.01195  16  HIS A NE2 
773  N N   . GLU A 138 ? 0.83029 0.64673 0.75530 0.04385  0.07962  0.03406  17  GLU A N   
774  C CA  . GLU A 138 ? 0.84099 0.62501 0.75165 0.05487  0.07510  0.04520  17  GLU A CA  
775  C C   . GLU A 138 ? 0.97419 0.74820 0.86715 0.04595  0.06309  0.05281  17  GLU A C   
776  O O   . GLU A 138 ? 0.99391 0.76166 0.87994 0.05392  0.04979  0.06570  17  GLU A O   
777  C CB  . GLU A 138 ? 0.91363 0.65688 0.81168 0.05994  0.09262  0.03818  17  GLU A CB  
778  C CG  . GLU A 138 ? 1.04850 0.75669 0.93077 0.07347  0.08951  0.05143  17  GLU A CG  
779  C CD  . GLU A 138 ? 1.29032 0.95536 1.16039 0.07722  0.10818  0.04546  17  GLU A CD  
780  O OE1 . GLU A 138 ? 1.39126 1.05612 1.27025 0.07312  0.12318  0.03024  17  GLU A OE1 
781  O OE2 . GLU A 138 ? 1.41842 1.04888 1.26910 0.08394  0.10797  0.05596  17  GLU A OE2 
782  N N   . LEU A 139 ? 1.13538 0.90798 1.02081 0.02974  0.06742  0.04464  18  LEU A N   
783  C CA  . LEU A 139 ? 1.01640 0.77505 0.88396 0.02161  0.05961  0.05011  18  LEU A CA  
784  C C   . LEU A 139 ? 0.82705 0.61247 0.70202 0.02044  0.03997  0.05983  18  LEU A C   
785  O O   . LEU A 139 ? 0.88527 0.65557 0.74424 0.02266  0.02932  0.06871  18  LEU A O   
786  C CB  . LEU A 139 ? 0.91863 0.67474 0.78262 0.00511  0.06907  0.03900  18  LEU A CB  
787  C CG  . LEU A 139 ? 1.06764 0.79240 0.92244 0.00306  0.08779  0.02911  18  LEU A CG  
788  C CD1 . LEU A 139 ? 1.04472 0.77711 0.90312 -0.01400 0.09469  0.01755  18  LEU A CD1 
789  C CD2 . LEU A 139 ? 0.97078 0.65327 0.80200 0.00961  0.09146  0.03713  18  LEU A CD2 
790  N N   . GLU A 140 ? 0.70031 0.52459 0.59840 0.01638  0.03525  0.05811  19  GLU A N   
791  C CA  . GLU A 140 ? 0.75261 0.60379 0.66177 0.01333  0.01754  0.06673  19  GLU A CA  
792  C C   . GLU A 140 ? 0.78779 0.66054 0.71613 0.02609  0.00829  0.07512  19  GLU A C   
793  O O   . GLU A 140 ? 0.67037 0.56878 0.61283 0.02345  -0.00654 0.08225  19  GLU A O   
794  C CB  . GLU A 140 ? 0.70177 0.58272 0.62516 -0.00079 0.01789  0.06164  19  GLU A CB  
795  C CG  . GLU A 140 ? 0.96039 0.82508 0.86972 -0.01346 0.02525  0.05425  19  GLU A CG  
796  C CD  . GLU A 140 ? 0.91849 0.76860 0.81376 -0.01873 0.01490  0.06002  19  GLU A CD  
797  O OE1 . GLU A 140 ? 0.99539 0.85800 0.89626 -0.01703 -0.00038 0.06853  19  GLU A OE1 
798  O OE2 . GLU A 140 ? 1.00151 0.82753 0.88070 -0.02479 0.02250  0.05544  19  GLU A OE2 
799  N N   . ARG A 141 ? 0.76054 0.62283 0.69142 0.03985  0.01699  0.07455  20  ARG A N   
800  C CA  . ARG A 141 ? 0.98833 0.87012 0.94014 0.05432  0.01035  0.08251  20  ARG A CA  
801  C C   . ARG A 141 ? 0.91871 0.84689 0.89957 0.04904  0.00355  0.08442  20  ARG A C   
802  O O   . ARG A 141 ? 0.85467 0.80210 0.84794 0.04962  -0.01358 0.09439  20  ARG A O   
803  C CB  . ARG A 141 ? 0.99333 0.85843 0.93373 0.06429  -0.00548 0.09519  20  ARG A CB  
804  C CG  . ARG A 141 ? 1.18123 1.00167 1.09630 0.07409  0.00405  0.09572  20  ARG A CG  
805  C CD  . ARG A 141 ? 1.22019 1.01694 1.11138 0.07935  -0.01096 0.10727  20  ARG A CD  
806  N NE  . ARG A 141 ? 1.30763 1.12922 1.21573 0.08846  -0.03133 0.11886  20  ARG A NE  
807  C CZ  . ARG A 141 ? 1.36144 1.16772 1.25201 0.09625  -0.04736 0.13006  20  ARG A CZ  
808  N NH1 . ARG A 141 ? 1.28854 1.05333 1.14204 0.09656  -0.04362 0.13173  20  ARG A NH1 
809  N NH2 . ARG A 141 ? 1.46637 1.29944 1.37637 0.10358  -0.06710 0.13978  20  ARG A NH2 
810  N N   . VAL A 142 ? 0.85629 0.80182 0.84697 0.04295  0.01714  0.07467  21  VAL A N   
811  C CA  . VAL A 142 ? 0.90737 0.89615 0.92537 0.04009  0.01642  0.07597  21  VAL A CA  
812  C C   . VAL A 142 ? 0.88379 0.87992 0.91342 0.05085  0.03336  0.06862  21  VAL A C   
813  O O   . VAL A 142 ? 0.83671 0.80423 0.85155 0.05580  0.04679  0.05951  21  VAL A O   
814  C CB  . VAL A 142 ? 0.76181 0.76682 0.77831 0.02220  0.01705  0.07163  21  VAL A CB  
815  C CG1 . VAL A 142 ? 0.72767 0.73137 0.73969 0.01283  -0.00031 0.07990  21  VAL A CG1 
816  C CG2 . VAL A 142 ? 0.76707 0.74934 0.76294 0.01533  0.03151  0.05837  21  VAL A CG2 
817  N N   . ASN A 143 ? 0.74312 0.77730 0.80012 0.05431  0.03358  0.07236  22  ASN A N   
818  C CA  . ASN A 143 ? 0.88867 0.93301 0.95880 0.06569  0.05027  0.06549  22  ASN A CA  
819  C C   . ASN A 143 ? 0.83738 0.89721 0.90352 0.05477  0.06452  0.05323  22  ASN A C   
820  O O   . ASN A 143 ? 0.83165 0.90886 0.89614 0.03997  0.05895  0.05478  22  ASN A O   
821  C CB  . ASN A 143 ? 0.90446 0.98286 1.00837 0.07711  0.04449  0.07659  22  ASN A CB  
822  C CG  . ASN A 143 ? 1.04111 1.15905 1.16398 0.06503  0.03477  0.08441  22  ASN A CG  
823  O OD1 . ASN A 143 ? 1.11456 1.25768 1.24489 0.05862  0.04559  0.07972  22  ASN A OD1 
824  N ND2 . ASN A 143 ? 1.12193 1.24432 1.25136 0.06146  0.01433  0.09637  22  ASN A ND2 
825  N N   . ARG A 144 ? 1.07410 1.12690 1.13818 0.06267  0.08287  0.04098  23  ARG A N   
826  C CA  . ARG A 144 ? 1.07717 1.14035 1.13215 0.05311  0.09696  0.02687  23  ARG A CA  
827  C C   . ARG A 144 ? 1.09853 1.20751 1.17315 0.05051  0.09968  0.03067  23  ARG A C   
828  O O   . ARG A 144 ? 1.24126 1.36287 1.30573 0.04039  0.10817  0.02145  23  ARG A O   
829  C CB  . ARG A 144 ? 1.10535 1.14363 1.15051 0.06228  0.11592  0.01088  23  ARG A CB  
830  C CG  . ARG A 144 ? 1.16844 1.16213 1.18862 0.05766  0.11792  0.00248  23  ARG A CG  
831  C CD  . ARG A 144 ? 1.29175 1.25696 1.30666 0.06906  0.13572  -0.01107 23  ARG A CD  
832  N NE  . ARG A 144 ? 1.52454 1.44707 1.51740 0.06318  0.13867  -0.01862 23  ARG A NE  
833  C CZ  . ARG A 144 ? 1.65966 1.57280 1.63589 0.04846  0.14544  -0.03378 23  ARG A CZ  
834  N NH1 . ARG A 144 ? 1.70136 1.64410 1.67743 0.03878  0.14915  -0.04297 23  ARG A NH1 
835  N NH2 . ARG A 144 ? 1.71137 1.58622 1.67143 0.04331  0.14851  -0.03933 23  ARG A NH2 
836  N N   . THR A 145 ? 0.91494 1.04977 1.01736 0.05898  0.09278  0.04430  24  THR A N   
837  C CA  . THR A 145 ? 0.95460 1.13361 1.07704 0.05496  0.09587  0.04973  24  THR A CA  
838  C C   . THR A 145 ? 0.90340 1.09680 1.02084 0.03644  0.08367  0.05691  24  THR A C   
839  O O   . THR A 145 ? 0.96301 1.17986 1.07820 0.02741  0.09084  0.05468  24  THR A O   
840  C CB  . THR A 145 ? 1.00970 1.21412 1.16763 0.06806  0.09133  0.06300  24  THR A CB  
841  O OG1 . THR A 145 ? 0.99355 1.19551 1.15973 0.06484  0.06912  0.07704  24  THR A OG1 
842  C CG2 . THR A 145 ? 0.88871 1.07707 1.05351 0.08826  0.10275  0.05732  24  THR A CG2 
843  N N   . ASP A 146 ? 0.85653 1.03551 0.97126 0.03105  0.06559  0.06577  25  ASP A N   
844  C CA  . ASP A 146 ? 0.85975 1.04928 0.97172 0.01455  0.05371  0.07301  25  ASP A CA  
845  C C   . ASP A 146 ? 0.78287 0.94911 0.86547 0.00286  0.05560  0.06306  25  ASP A C   
846  O O   . ASP A 146 ? 0.73455 0.91197 0.81461 -0.01053 0.04920  0.06763  25  ASP A O   
847  C CB  . ASP A 146 ? 0.93982 1.12452 1.06234 0.01368  0.03334  0.08597  25  ASP A CB  
848  C CG  . ASP A 146 ? 1.07715 1.28807 1.23255 0.02376  0.02821  0.09685  25  ASP A CG  
849  O OD1 . ASP A 146 ? 1.12397 1.35519 1.29479 0.03310  0.04214  0.09453  25  ASP A OD1 
850  O OD2 . ASP A 146 ? 1.15584 1.36750 1.32219 0.02225  0.01025  0.10720  25  ASP A OD2 
851  N N   . TRP A 147 ? 0.79262 0.92722 0.85528 0.00750  0.06425  0.05018  26  TRP A N   
852  C CA  . TRP A 147 ? 0.92962 1.03943 0.96767 -0.00337 0.06423  0.04150  26  TRP A CA  
853  C C   . TRP A 147 ? 0.82310 0.92019 0.84585 -0.00161 0.08119  0.02389  26  TRP A C   
854  O O   . TRP A 147 ? 0.83696 0.91235 0.85715 0.01007  0.08953  0.01719  26  TRP A O   
855  C CB  . TRP A 147 ? 0.86665 0.94159 0.89399 -0.00190 0.05422  0.04478  26  TRP A CB  
856  C CG  . TRP A 147 ? 0.85609 0.93860 0.89386 -0.00504 0.03647  0.05954  26  TRP A CG  
857  C CD1 . TRP A 147 ? 0.95163 1.04513 1.00787 0.00384  0.02710  0.07046  26  TRP A CD1 
858  C CD2 . TRP A 147 ? 0.86561 0.94410 0.89649 -0.01800 0.02564  0.06407  26  TRP A CD2 
859  N NE1 . TRP A 147 ? 1.00691 1.10304 1.06680 -0.00389 0.01058  0.08052  26  TRP A NE1 
860  C CE2 . TRP A 147 ? 0.90092 0.98675 0.94504 -0.01689 0.01018  0.07671  26  TRP A CE2 
861  C CE3 . TRP A 147 ? 0.88339 0.95342 0.89981 -0.03022 0.02738  0.05846  26  TRP A CE3 
862  C CZ2 . TRP A 147 ? 0.91072 0.99295 0.95217 -0.02755 -0.00241 0.08281  26  TRP A CZ2 
863  C CZ3 . TRP A 147 ? 0.83190 0.89974 0.84769 -0.03964 0.01532  0.06582  26  TRP A CZ3 
864  C CH2 . TRP A 147 ? 0.86891 0.94145 0.89618 -0.03825 0.00114  0.07736  26  TRP A CH2 
865  N N   . PHE A 148 ? 0.71382 0.82397 0.72655 -0.01313 0.08575  0.01647  27  PHE A N   
866  C CA  . PHE A 148 ? 0.91096 1.00761 0.90613 -0.01520 0.09929  -0.00216 27  PHE A CA  
867  C C   . PHE A 148 ? 0.78596 0.86757 0.76538 -0.02938 0.09384  -0.00711 27  PHE A C   
868  O O   . PHE A 148 ? 0.78280 0.88003 0.76487 -0.03935 0.08316  0.00234  27  PHE A O   
869  C CB  . PHE A 148 ? 0.73296 0.86041 0.72812 -0.01617 0.11013  -0.00873 27  PHE A CB  
870  C CG  . PHE A 148 ? 0.83653 0.95140 0.81121 -0.02068 0.12211  -0.02957 27  PHE A CG  
871  C CD1 . PHE A 148 ? 0.92004 1.01176 0.89031 -0.01027 0.13584  -0.04374 27  PHE A CD1 
872  C CD2 . PHE A 148 ? 0.90402 1.02947 0.86464 -0.03541 0.11898  -0.03515 27  PHE A CD2 
873  C CE1 . PHE A 148 ? 0.97481 1.05321 0.92650 -0.01561 0.14652  -0.06459 27  PHE A CE1 
874  C CE2 . PHE A 148 ? 0.84013 0.95495 0.78228 -0.04068 0.12824  -0.05543 27  PHE A CE2 
875  C CZ  . PHE A 148 ? 0.94072 1.03141 0.87812 -0.03138 0.14213  -0.07091 27  PHE A CZ  
876  N N   . CYS A 149 ? 0.83644 0.88788 0.80162 -0.03034 0.10163  -0.02163 28  CYS A N   
877  C CA  . CYS A 149 ? 0.93546 0.97661 0.88879 -0.04431 0.09814  -0.02782 28  CYS A CA  
878  C C   . CYS A 149 ? 0.94865 0.97581 0.88861 -0.04800 0.11060  -0.04872 28  CYS A C   
879  O O   . CYS A 149 ? 0.86678 0.87988 0.80467 -0.03849 0.12252  -0.05868 28  CYS A O   
880  C CB  . CYS A 149 ? 0.96323 0.97491 0.91446 -0.04529 0.09078  -0.02087 28  CYS A CB  
881  S SG  . CYS A 149 ? 0.99116 0.96246 0.93906 -0.03057 0.09785  -0.02218 28  CYS A SG  
882  N N   . THR A 150 ? 0.90311 0.93447 0.83537 -0.06214 0.10721  -0.05538 29  THR A N   
883  C CA  . THR A 150 ? 0.99121 1.01038 0.91145 -0.06945 0.11597  -0.07593 29  THR A CA  
884  C C   . THR A 150 ? 1.06598 1.08101 0.98454 -0.08377 0.10804  -0.07671 29  THR A C   
885  O O   . THR A 150 ? 1.02544 1.04344 0.95114 -0.08608 0.09776  -0.06187 29  THR A O   
886  C CB  . THR A 150 ? 0.95756 1.00442 0.87048 -0.07115 0.12173  -0.08658 29  THR A CB  
887  O OG1 . THR A 150 ? 1.14724 1.17821 1.04754 -0.07769 0.13052  -0.10911 29  THR A OG1 
888  C CG2 . THR A 150 ? 0.87131 0.95489 0.78468 -0.08098 0.11042  -0.07693 29  THR A CG2 
889  N N   . SER A 151 ? 1.05491 1.06360 0.96526 -0.09353 0.11291  -0.09470 30  SER A N   
890  C CA  . SER A 151 ? 1.01363 1.02233 0.92558 -0.10761 0.10599  -0.09706 30  SER A CA  
891  C C   . SER A 151 ? 1.11580 1.14627 1.01951 -0.11873 0.10533  -0.11268 30  SER A C   
892  O O   . SER A 151 ? 1.11164 1.14565 1.00508 -0.11582 0.11357  -0.12610 30  SER A O   
893  C CB  . SER A 151 ? 1.01024 0.97910 0.92318 -0.10948 0.11265  -0.10342 30  SER A CB  
894  O OG  . SER A 151 ? 1.06678 1.01077 0.97290 -0.10398 0.12623  -0.11845 30  SER A OG  
895  N N   . ASP A 152 ? 1.23360 1.27954 1.14162 -0.13104 0.09511  -0.11072 31  ASP A N   
896  C CA  . ASP A 152 ? 1.23443 1.30049 1.13437 -0.14283 0.09211  -0.12587 31  ASP A CA  
897  C C   . ASP A 152 ? 1.25335 1.29249 1.14582 -0.14655 0.10375  -0.15004 31  ASP A C   
898  O O   . ASP A 152 ? 1.24952 1.25472 1.14845 -0.14586 0.11068  -0.15307 31  ASP A O   
899  C CB  . ASP A 152 ? 1.34332 1.42558 1.25352 -0.15499 0.07928  -0.11993 31  ASP A CB  
900  C CG  . ASP A 152 ? 1.39358 1.51311 1.30547 -0.15493 0.06703  -0.10244 31  ASP A CG  
901  O OD1 . ASP A 152 ? 1.33079 1.46038 1.23908 -0.14523 0.06868  -0.09163 31  ASP A OD1 
902  O OD2 . ASP A 152 ? 1.49766 1.63680 1.41610 -0.16452 0.05597  -0.09894 31  ASP A OD2 
903  N N   . PRO A 153 ? 1.23598 1.28769 1.11390 -0.15065 0.10673  -0.16762 32  PRO A N   
904  C CA  . PRO A 153 ? 1.27092 1.29473 1.14170 -0.15450 0.11841  -0.19237 32  PRO A CA  
905  C C   . PRO A 153 ? 1.47925 1.49054 1.35980 -0.16972 0.11470  -0.20228 32  PRO A C   
906  O O   . PRO A 153 ? 1.24240 1.27792 1.13030 -0.18020 0.10147  -0.19676 32  PRO A O   
907  C CB  . PRO A 153 ? 1.11186 1.15878 0.96274 -0.15708 0.11965  -0.20820 32  PRO A CB  
908  C CG  . PRO A 153 ? 1.08728 1.16940 0.93503 -0.14984 0.11283  -0.18857 32  PRO A CG  
909  C CD  . PRO A 153 ? 1.13976 1.23008 1.00529 -0.15145 0.10063  -0.16560 32  PRO A CD  
910  N N   . VAL A 154 ? 1.89359 1.86634 1.77621 -0.17048 0.12718  -0.21629 33  VAL A N   
911  C CA  . VAL A 154 ? 2.05016 2.00551 1.94516 -0.18461 0.12712  -0.22584 33  VAL A CA  
912  C C   . VAL A 154 ? 1.96703 1.94895 1.85858 -0.20165 0.11715  -0.24337 33  VAL A C   
913  O O   . VAL A 154 ? 2.10832 2.08945 1.98465 -0.20528 0.12150  -0.26485 33  VAL A O   
914  C CB  . VAL A 154 ? 2.19947 2.10707 2.09512 -0.18198 0.14432  -0.23871 33  VAL A CB  
915  C CG1 . VAL A 154 ? 2.23690 2.12523 2.14917 -0.19579 0.14564  -0.24328 33  VAL A CG1 
916  C CG2 . VAL A 154 ? 2.23673 2.12137 2.13149 -0.16277 0.15311  -0.22186 33  VAL A CG2 
917  N N   . GLY A 155 ? 1.72493 1.73074 1.63041 -0.21182 0.10342  -0.23457 34  GLY A N   
918  C CA  . GLY A 155 ? 1.62402 1.65921 1.52834 -0.22778 0.09085  -0.24854 34  GLY A CA  
919  C C   . GLY A 155 ? 1.57400 1.65049 1.48593 -0.23018 0.07301  -0.22990 34  GLY A C   
920  O O   . GLY A 155 ? 1.52390 1.60142 1.45727 -0.23241 0.06840  -0.21574 34  GLY A O   
921  N N   . LYS A 156 ? 1.64658 1.75643 1.54070 -0.22929 0.06382  -0.22936 35  LYS A N   
922  C CA  . LYS A 156 ? 1.67098 1.82033 1.57039 -0.23056 0.04691  -0.21041 35  LYS A CA  
923  C C   . LYS A 156 ? 1.60277 1.75576 1.50215 -0.21501 0.04857  -0.18463 35  LYS A C   
924  O O   . LYS A 156 ? 1.58103 1.71853 1.46854 -0.20326 0.06016  -0.18373 35  LYS A O   
925  C CB  . LYS A 156 ? 1.71546 1.89972 1.59381 -0.23782 0.03554  -0.22093 35  LYS A CB  
926  C CG  . LYS A 156 ? 1.66478 1.88864 1.55346 -0.24488 0.01538  -0.20700 35  LYS A CG  
927  C CD  . LYS A 156 ? 1.59808 1.85617 1.46347 -0.23972 0.00724  -0.19634 35  LYS A CD  
928  C CE  . LYS A 156 ? 1.60309 1.86445 1.43611 -0.24333 0.01130  -0.22032 35  LYS A CE  
929  N NZ  . LYS A 156 ? 1.53515 1.83078 1.34302 -0.23881 0.00443  -0.20956 35  LYS A NZ  
930  N N   . LYS A 157 ? 1.58024 1.75397 1.49511 -0.21515 0.03673  -0.16385 36  LYS A N   
931  C CA  . LYS A 157 ? 1.46646 1.64537 1.38429 -0.20266 0.03606  -0.13905 36  LYS A CA  
932  C C   . LYS A 157 ? 1.39670 1.61205 1.29869 -0.20030 0.02737  -0.12979 36  LYS A C   
933  O O   . LYS A 157 ? 1.45989 1.70136 1.35197 -0.20919 0.01761  -0.13780 36  LYS A O   
934  C CB  . LYS A 157 ? 1.46920 1.64794 1.41223 -0.20365 0.02933  -0.12168 36  LYS A CB  
935  C CG  . LYS A 157 ? 1.47860 1.62607 1.43779 -0.20864 0.03725  -0.13085 36  LYS A CG  
936  C CD  . LYS A 157 ? 1.46562 1.61205 1.44797 -0.20779 0.03293  -0.11314 36  LYS A CD  
937  C CE  . LYS A 157 ? 1.51149 1.62633 1.50847 -0.21258 0.04317  -0.12165 36  LYS A CE  
938  N NZ  . LYS A 157 ? 1.49703 1.61086 1.51594 -0.21186 0.04065  -0.10599 36  LYS A NZ  
939  N N   . LEU A 158 ? 1.31486 1.53202 1.21423 -0.18844 0.03093  -0.11235 37  LEU A N   
940  C CA  . LEU A 158 ? 1.23615 1.48377 1.11909 -0.18488 0.02711  -0.10333 37  LEU A CA  
941  C C   . LEU A 158 ? 1.14518 1.41585 1.04007 -0.18245 0.01578  -0.07628 37  LEU A C   
942  O O   . LEU A 158 ? 1.14252 1.44310 1.02496 -0.18266 0.00968  -0.06749 37  LEU A O   
943  C CB  . LEU A 158 ? 1.10882 1.34446 0.97901 -0.17340 0.04173  -0.10579 37  LEU A CB  
944  C CG  . LEU A 158 ? 1.10381 1.31340 0.96234 -0.17387 0.05482  -0.13224 37  LEU A CG  
945  C CD1 . LEU A 158 ? 1.03894 1.23404 0.89165 -0.16015 0.06972  -0.13184 37  LEU A CD1 
946  C CD2 . LEU A 158 ? 1.18361 1.41089 1.02079 -0.18400 0.05136  -0.15231 37  LEU A CD2 
947  N N   . GLY A 159 ? 1.04478 1.30120 0.96207 -0.18007 0.01360  -0.06297 38  GLY A N   
948  C CA  . GLY A 159 ? 1.04689 1.32168 0.97717 -0.17802 0.00335  -0.03841 38  GLY A CA  
949  C C   . GLY A 159 ? 1.07349 1.34303 1.00508 -0.16739 0.00905  -0.02260 38  GLY A C   
950  O O   . GLY A 159 ? 1.12094 1.37263 1.04570 -0.16073 0.02050  -0.02974 38  GLY A O   
951  N N   . SER A 160 ? 1.02559 1.31156 0.96796 -0.16582 0.00051  -0.00033 39  SER A N   
952  C CA  . SER A 160 ? 0.91406 1.19843 0.86033 -0.15740 0.00432  0.01565  39  SER A CA  
953  C C   . SER A 160 ? 0.91265 1.21570 0.84035 -0.15410 0.01077  0.01443  39  SER A C   
954  O O   . SER A 160 ? 0.78774 1.07975 0.71347 -0.14669 0.02092  0.01231  39  SER A O   
955  C CB  . SER A 160 ? 0.92427 1.22066 0.88736 -0.15772 -0.00613 0.03907  39  SER A CB  
956  O OG  . SER A 160 ? 0.95478 1.27841 0.91532 -0.16405 -0.01658 0.04411  39  SER A OG  
957  N N   . GLY A 161 ? 0.95672 1.28831 0.86990 -0.15924 0.00545  0.01485  40  GLY A N   
958  C CA  . GLY A 161 ? 1.12459 1.47510 1.01750 -0.15625 0.01294  0.01380  40  GLY A CA  
959  C C   . GLY A 161 ? 1.13483 1.47139 1.01062 -0.15448 0.02542  -0.01155 40  GLY A C   
960  O O   . GLY A 161 ? 1.13817 1.47132 1.00927 -0.14668 0.03762  -0.01329 40  GLY A O   
961  N N   . GLY A 162 ? 1.01693 1.34637 0.88446 -0.16184 0.02272  -0.03156 41  GLY A N   
962  C CA  . GLY A 162 ? 0.97285 1.28370 0.82611 -0.16076 0.03492  -0.05705 41  GLY A CA  
963  C C   . GLY A 162 ? 0.98140 1.25947 0.84803 -0.15191 0.04610  -0.05979 41  GLY A C   
964  O O   . GLY A 162 ? 0.99537 1.26310 0.85244 -0.14510 0.05941  -0.07131 41  GLY A O   
965  N N   . GLY A 163 ? 1.02997 1.29115 0.91821 -0.15127 0.04096  -0.04910 42  GLY A N   
966  C CA  . GLY A 163 ? 1.05690 1.28843 0.95626 -0.14230 0.04958  -0.04836 42  GLY A CA  
967  C C   . GLY A 163 ? 1.00689 1.24706 0.90869 -0.13186 0.05554  -0.03541 42  GLY A C   
968  O O   . GLY A 163 ? 1.03345 1.25673 0.93465 -0.12316 0.06661  -0.04248 42  GLY A O   
969  N N   . THR A 164 ? 0.89777 1.16447 0.80458 -0.13249 0.04839  -0.01552 43  THR A N   
970  C CA  . THR A 164 ? 0.91640 1.19512 0.82832 -0.12403 0.05420  -0.00257 43  THR A CA  
971  C C   . THR A 164 ? 1.01510 1.30405 0.90926 -0.11955 0.06750  -0.01570 43  THR A C   
972  O O   . THR A 164 ? 0.90100 1.18515 0.80077 -0.10973 0.07782  -0.01551 43  THR A O   
973  C CB  . THR A 164 ? 0.92636 1.23213 0.84610 -0.12741 0.04479  0.02069  43  THR A CB  
974  O OG1 . THR A 164 ? 1.02462 1.32194 0.95732 -0.13298 0.03246  0.02920  43  THR A OG1 
975  C CG2 . THR A 164 ? 0.99445 1.30650 0.92890 -0.11984 0.04886  0.03644  43  THR A CG2 
976  N N   . SER A 165 ? 1.01269 1.31650 0.88541 -0.12640 0.06727  -0.02741 44  SER A N   
977  C CA  . SER A 165 ? 1.13973 1.45233 0.99181 -0.12257 0.08080  -0.04209 44  SER A CA  
978  C C   . SER A 165 ? 1.13409 1.41523 0.98535 -0.11613 0.09295  -0.06304 44  SER A C   
979  O O   . SER A 165 ? 1.11357 1.39382 0.96291 -0.10625 0.10695  -0.06776 44  SER A O   
980  C CB  . SER A 165 ? 1.20766 1.54005 1.03390 -0.13238 0.07605  -0.05234 44  SER A CB  
981  O OG  . SER A 165 ? 1.30083 1.66541 1.12373 -0.13548 0.06855  -0.03160 44  SER A OG  
982  N N   . TRP A 166 ? 0.94764 1.20252 0.80199 -0.12128 0.08854  -0.07497 45  TRP A N   
983  C CA  . TRP A 166 ? 0.94600 1.16723 0.80065 -0.11553 0.09996  -0.09323 45  TRP A CA  
984  C C   . TRP A 166 ? 0.94793 1.15426 0.82183 -0.10256 0.10541  -0.08113 45  TRP A C   
985  O O   . TRP A 166 ? 0.86533 1.05559 0.73845 -0.09264 0.11859  -0.09141 45  TRP A O   
986  C CB  . TRP A 166 ? 0.84332 1.04071 0.70017 -0.12498 0.09371  -0.10495 45  TRP A CB  
987  C CG  . TRP A 166 ? 0.89528 1.05351 0.75673 -0.11943 0.10413  -0.11848 45  TRP A CG  
988  C CD1 . TRP A 166 ? 0.94862 1.08084 0.82664 -0.11460 0.10325  -0.10952 45  TRP A CD1 
989  C CD2 . TRP A 166 ? 0.99389 1.13281 0.84195 -0.11796 0.11735  -0.14299 45  TRP A CD2 
990  N NE1 . TRP A 166 ? 1.02564 1.12393 0.90158 -0.10992 0.11500  -0.12525 45  TRP A NE1 
991  C CE2 . TRP A 166 ? 1.08587 1.18683 0.94495 -0.11189 0.12405  -0.14616 45  TRP A CE2 
992  C CE3 . TRP A 166 ? 1.08381 1.23252 0.91024 -0.12117 0.12445  -0.16291 45  TRP A CE3 
993  C CZ2 . TRP A 166 ? 1.16235 1.23422 1.01412 -0.10875 0.13786  -0.16754 45  TRP A CZ2 
994  C CZ3 . TRP A 166 ? 1.14755 1.26705 0.96624 -0.11842 0.13819  -0.18609 45  TRP A CZ3 
995  C CH2 . TRP A 166 ? 1.21552 1.29664 1.04814 -0.11217 0.14492  -0.18779 45  TRP A CH2 
996  N N   . LEU A 167 ? 0.86310 1.07508 0.75468 -0.10220 0.09500  -0.05933 46  LEU A N   
997  C CA  . LEU A 167 ? 0.88598 1.08639 0.79573 -0.09088 0.09731  -0.04716 46  LEU A CA  
998  C C   . LEU A 167 ? 1.00125 1.22312 0.91368 -0.08121 0.10720  -0.04211 46  LEU A C   
999  O O   . LEU A 167 ? 1.03543 1.24401 0.95486 -0.06949 0.11710  -0.04607 46  LEU A O   
1000 C CB  . LEU A 167 ? 0.82500 1.02819 0.75091 -0.09449 0.08309  -0.02653 46  LEU A CB  
1001 C CG  . LEU A 167 ? 0.92043 1.10883 0.86460 -0.08587 0.08027  -0.01343 46  LEU A CG  
1002 C CD1 . LEU A 167 ? 0.98865 1.13946 0.93109 -0.08006 0.08581  -0.02514 46  LEU A CD1 
1003 C CD2 . LEU A 167 ? 0.66716 0.85933 0.62263 -0.09235 0.06600  0.00362  46  LEU A CD2 
1004 N N   . LEU A 168 ? 0.91912 1.17478 0.82663 -0.08563 0.10535  -0.03273 47  LEU A N   
1005 C CA  . LEU A 168 ? 1.00708 1.28615 0.91704 -0.07740 0.11666  -0.02764 47  LEU A CA  
1006 C C   . LEU A 168 ? 1.15702 1.42717 1.05160 -0.07047 0.13373  -0.05010 47  LEU A C   
1007 O O   . LEU A 168 ? 1.23105 1.50236 1.13605 -0.05820 0.14578  -0.05000 47  LEU A O   
1008 C CB  . LEU A 168 ? 0.92120 1.23628 0.82376 -0.08478 0.11284  -0.01450 47  LEU A CB  
1009 C CG  . LEU A 168 ? 0.91880 1.24690 0.84097 -0.08919 0.09928  0.01101  47  LEU A CG  
1010 C CD1 . LEU A 168 ? 0.70341 1.06498 0.61498 -0.09633 0.09709  0.02323  47  LEU A CD1 
1011 C CD2 . LEU A 168 ? 0.87636 1.20518 0.82532 -0.07973 0.10186  0.02430  47  LEU A CD2 
1012 N N   . GLU A 169 ? 1.00470 1.26589 0.87591 -0.07819 0.13489  -0.07002 48  GLU A N   
1013 C CA  . GLU A 169 ? 1.07150 1.32163 0.92579 -0.07292 0.15122  -0.09395 48  GLU A CA  
1014 C C   . GLU A 169 ? 1.13257 1.34771 1.00041 -0.06173 0.15923  -0.10212 48  GLU A C   
1015 O O   . GLU A 169 ? 1.10420 1.31611 0.97428 -0.04941 0.17480  -0.10944 48  GLU A O   
1016 C CB  . GLU A 169 ? 1.19154 1.43778 1.01940 -0.08571 0.14775  -0.11400 48  GLU A CB  
1017 C CG  . GLU A 169 ? 1.37208 1.61825 1.17527 -0.08321 0.16376  -0.13807 48  GLU A CG  
1018 C CD  . GLU A 169 ? 1.54778 1.80434 1.32240 -0.09777 0.15682  -0.15306 48  GLU A CD  
1019 O OE1 . GLU A 169 ? 1.54160 1.82464 1.31216 -0.10656 0.14317  -0.13813 48  GLU A OE1 
1020 O OE2 . GLU A 169 ? 1.61936 1.85729 1.37618 -0.10049 0.16439  -0.17972 48  GLU A OE2 
1021 N N   . GLU A 170 ? 1.04872 1.23674 0.92515 -0.06538 0.14959  -0.10093 49  GLU A N   
1022 C CA  . GLU A 170 ? 1.00220 1.15442 0.88870 -0.05516 0.15662  -0.10754 49  GLU A CA  
1023 C C   . GLU A 170 ? 1.00979 1.16746 0.91927 -0.04048 0.15903  -0.09023 49  GLU A C   
1024 O O   . GLU A 170 ? 1.12728 1.26397 1.04416 -0.02760 0.16942  -0.09609 49  GLU A O   
1025 C CB  . GLU A 170 ? 1.01792 1.14214 0.90748 -0.06301 0.14594  -0.10739 49  GLU A CB  
1026 C CG  . GLU A 170 ? 1.03975 1.14572 0.91180 -0.07400 0.14843  -0.13042 49  GLU A CG  
1027 C CD  . GLU A 170 ? 1.17535 1.24160 1.04673 -0.06665 0.16142  -0.14687 49  GLU A CD  
1028 O OE1 . GLU A 170 ? 1.28137 1.32088 1.16498 -0.06163 0.15955  -0.13887 49  GLU A OE1 
1029 O OE2 . GLU A 170 ? 1.16124 1.22181 1.01877 -0.06573 0.17387  -0.16772 49  GLU A OE2 
1030 N N   . CYS A 171 ? 0.89328 1.07892 0.81569 -0.04222 0.14919  -0.06872 50  CYS A N   
1031 C CA  . CYS A 171 ? 0.96271 1.15877 0.90912 -0.02960 0.15062  -0.05263 50  CYS A CA  
1032 C C   . CYS A 171 ? 1.03960 1.25627 0.98702 -0.01954 0.16775  -0.05804 50  CYS A C   
1033 O O   . CYS A 171 ? 1.04137 1.25000 1.00379 -0.00479 0.17714  -0.05875 50  CYS A O   
1034 C CB  . CYS A 171 ? 0.87426 1.09363 0.83507 -0.03603 0.13553  -0.02932 50  CYS A CB  
1035 S SG  . CYS A 171 ? 0.94555 1.17315 0.93924 -0.02331 0.13194  -0.00936 50  CYS A SG  
1036 N N   . TYR A 172 ? 1.10949 1.35379 1.04122 -0.02677 0.17221  -0.06093 51  TYR A N   
1037 C CA  . TYR A 172 ? 1.13447 1.39865 1.06280 -0.01799 0.19075  -0.06773 51  TYR A CA  
1038 C C   . TYR A 172 ? 1.16311 1.39892 1.08351 -0.00753 0.20687  -0.09095 51  TYR A C   
1039 O O   . TYR A 172 ? 1.07906 1.31945 1.01296 0.00722  0.22159  -0.09222 51  TYR A O   
1040 C CB  . TYR A 172 ? 1.11645 1.40834 1.01983 -0.02912 0.19265  -0.07063 51  TYR A CB  
1041 C CG  . TYR A 172 ? 1.27234 1.57565 1.15937 -0.02211 0.21404  -0.08654 51  TYR A CG  
1042 C CD1 . TYR A 172 ? 1.22533 1.55729 1.12730 -0.01242 0.22683  -0.07538 51  TYR A CD1 
1043 C CD2 . TYR A 172 ? 1.24829 1.53385 1.10531 -0.02561 0.22204  -0.11339 51  TYR A CD2 
1044 C CE1 . TYR A 172 ? 1.19716 1.53942 1.08332 -0.00535 0.24835  -0.09033 51  TYR A CE1 
1045 C CE2 . TYR A 172 ? 1.36341 1.65760 1.20288 -0.01908 0.24244  -0.12967 51  TYR A CE2 
1046 C CZ  . TYR A 172 ? 1.24399 1.56642 1.09741 -0.00845 0.25618  -0.11793 51  TYR A CZ  
1047 O OH  . TYR A 172 ? 1.30727 1.63810 1.14253 -0.00126 0.27839  -0.13450 51  TYR A OH  
1048 N N   . ASN A 173 ? 1.31602 1.52186 1.21703 -0.01485 0.20468  -0.10928 52  ASN A N   
1049 C CA  . ASN A 173 ? 1.38378 1.55932 1.27576 -0.00666 0.22036  -0.13291 52  ASN A CA  
1050 C C   . ASN A 173 ? 1.43391 1.58474 1.35073 0.00966  0.22446  -0.12754 52  ASN A C   
1051 O O   . ASN A 173 ? 1.49928 1.62590 1.41338 0.01989  0.23973  -0.14453 52  ASN A O   
1052 C CB  . ASN A 173 ? 1.46538 1.61406 1.33475 -0.02030 0.21521  -0.15215 52  ASN A CB  
1053 C CG  . ASN A 173 ? 1.57742 1.74570 1.41714 -0.03285 0.21688  -0.16673 52  ASN A CG  
1054 O OD1 . ASN A 173 ? 1.66114 1.82149 1.48216 -0.03067 0.23175  -0.18964 52  ASN A OD1 
1055 N ND2 . ASN A 173 ? 1.57454 1.76798 1.40898 -0.04577 0.20135  -0.15357 52  ASN A ND2 
1056 N N   . GLU A 174 ? 1.42846 1.58394 1.36866 0.01257  0.21100  -0.10463 53  GLU A N   
1057 C CA  . GLU A 174 ? 1.40163 1.53762 1.36513 0.02870  0.21270  -0.09704 53  GLU A CA  
1058 C C   . GLU A 174 ? 1.24938 1.41695 1.24156 0.04046  0.21328  -0.07772 53  GLU A C   
1059 O O   . GLU A 174 ? 1.22932 1.38697 1.24141 0.05716  0.21954  -0.07474 53  GLU A O   
1060 C CB  . GLU A 174 ? 1.38853 1.49710 1.35514 0.02367  0.19607  -0.08793 53  GLU A CB  
1061 C CG  . GLU A 174 ? 1.40964 1.49134 1.39384 0.04001  0.19727  -0.08188 53  GLU A CG  
1062 C CD  . GLU A 174 ? 1.52503 1.57286 1.50381 0.03453  0.18491  -0.07770 53  GLU A CD  
1063 O OE1 . GLU A 174 ? 1.56842 1.59324 1.52750 0.02350  0.18668  -0.09240 53  GLU A OE1 
1064 O OE2 . GLU A 174 ? 1.57863 1.62327 1.57274 0.04097  0.17358  -0.05996 53  GLU A OE2 
1065 N N   . TYR A 175 ? 1.17505 1.38074 1.17154 0.03241  0.20732  -0.06422 54  TYR A N   
1066 C CA  . TYR A 175 ? 1.16521 1.40323 1.19189 0.04193  0.20850  -0.04594 54  TYR A CA  
1067 C C   . TYR A 175 ? 1.15920 1.43331 1.18262 0.04234  0.22433  -0.04839 54  TYR A C   
1068 O O   . TYR A 175 ? 0.99602 1.30397 1.04279 0.04446  0.22362  -0.03078 54  TYR A O   
1069 C CB  . TYR A 175 ? 1.08175 1.33321 1.12449 0.03343  0.18704  -0.02292 54  TYR A CB  
1070 C CG  . TYR A 175 ? 1.08169 1.29899 1.12492 0.03251  0.17147  -0.01941 54  TYR A CG  
1071 C CD1 . TYR A 175 ? 1.01788 1.22416 1.08408 0.04616  0.16691  -0.01023 54  TYR A CD1 
1072 C CD2 . TYR A 175 ? 1.04601 1.24312 1.06678 0.01832  0.16147  -0.02468 54  TYR A CD2 
1073 C CE1 . TYR A 175 ? 1.14664 1.32105 1.20942 0.04556  0.15336  -0.00649 54  TYR A CE1 
1074 C CE2 . TYR A 175 ? 0.98857 1.15436 1.00859 0.01763  0.14934  -0.02131 54  TYR A CE2 
1075 C CZ  . TYR A 175 ? 1.11170 1.26547 1.15078 0.03117  0.14559  -0.01222 54  TYR A CZ  
1076 O OH  . TYR A 175 ? 1.12861 1.25062 1.16310 0.03061  0.13412  -0.00836 54  TYR A OH  
1077 N N   . SER A 176 ? 1.18126 1.44898 1.17571 0.03978  0.23886  -0.06998 55  SER A N   
1078 C CA  . SER A 176 ? 1.17054 1.47206 1.15575 0.03920  0.25424  -0.07259 55  SER A CA  
1079 C C   . SER A 176 ? 1.22407 1.54352 1.23744 0.05767  0.27195  -0.06850 55  SER A C   
1080 O O   . SER A 176 ? 1.15392 1.51144 1.17984 0.05804  0.27834  -0.05550 55  SER A O   
1081 C CB  . SER A 176 ? 1.22840 1.51626 1.17385 0.03303  0.26557  -0.09913 55  SER A CB  
1082 O OG  . SER A 176 ? 1.35389 1.61479 1.29801 0.04685  0.28272  -0.11945 55  SER A OG  
1083 N N   . ASP A 177 ? 1.16852 1.46118 1.19374 0.07337  0.28059  -0.07863 56  ASP A N   
1084 C CA  . ASP A 177 ? 1.29531 1.60223 1.35023 0.09331  0.29817  -0.07615 56  ASP A CA  
1085 C C   . ASP A 177 ? 1.29723 1.63020 1.33852 0.09586  0.32232  -0.08704 56  ASP A C   
1086 O O   . ASP A 177 ? 1.20639 1.57131 1.27458 0.10632  0.33479  -0.07652 56  ASP A O   
1087 C CB  . ASP A 177 ? 1.24547 1.57882 1.34326 0.09815  0.28573  -0.04855 56  ASP A CB  
1088 C CG  . ASP A 177 ? 1.26695 1.60076 1.40112 0.12085  0.29655  -0.04572 56  ASP A CG  
1089 O OD1 . ASP A 177 ? 1.29624 1.60399 1.42207 0.13341  0.31284  -0.06469 56  ASP A OD1 
1090 O OD2 . ASP A 177 ? 1.21679 1.57697 1.38920 0.12616  0.28851  -0.02465 56  ASP A OD2 
1091 N N   . GLY A 178 ? 1.31202 1.63217 1.31094 0.08584  0.32900  -0.10840 57  GLY A N   
1092 C CA  . GLY A 178 ? 1.45384 1.79298 1.43098 0.08775  0.35226  -0.12256 57  GLY A CA  
1093 C C   . GLY A 178 ? 1.45946 1.83532 1.41785 0.07250  0.34897  -0.11167 57  GLY A C   
1094 O O   . GLY A 178 ? 1.47246 1.85684 1.39727 0.06907  0.36426  -0.12726 57  GLY A O   
1095 N N   . ALA A 179 ? 1.34411 1.74105 1.32211 0.06352  0.32987  -0.08538 58  ALA A N   
1096 C CA  . ALA A 179 ? 1.23037 1.66084 1.19271 0.04931  0.32624  -0.07216 58  ALA A CA  
1097 C C   . ALA A 179 ? 1.28973 1.70580 1.20441 0.03302  0.31747  -0.08730 58  ALA A C   
1098 O O   . ALA A 179 ? 1.30465 1.68513 1.20243 0.03082  0.31179  -0.10645 58  ALA A O   
1099 C CB  . ALA A 179 ? 1.06650 1.51601 1.06131 0.04256  0.30594  -0.04201 58  ALA A CB  
1100 N N   . THR A 180 ? 1.18386 1.62895 1.07797 0.02135  0.31625  -0.07766 59  THR A N   
1101 C CA  . THR A 180 ? 1.30022 1.73793 1.15378 0.00479  0.30319  -0.08647 59  THR A CA  
1102 C C   . THR A 180 ? 1.21986 1.65524 1.08794 -0.00729 0.27565  -0.06621 59  THR A C   
1103 O O   . THR A 180 ? 1.03013 1.47095 0.93603 -0.00363 0.26754  -0.04587 59  THR A O   
1104 C CB  . THR A 180 ? 1.32949 1.79842 1.14998 -0.00133 0.31463  -0.08566 59  THR A CB  
1105 O OG1 . THR A 180 ? 1.34751 1.85143 1.19040 -0.00403 0.31204  -0.05506 59  THR A OG1 
1106 C CG2 . THR A 180 ? 1.33705 1.80821 1.14282 0.01152  0.34407  -0.10632 59  THR A CG2 
1107 N N   . PHE A 181 ? 1.34393 1.77134 1.18199 -0.02181 0.26095  -0.07249 60  PHE A N   
1108 C CA  . PHE A 181 ? 1.38961 1.81136 1.24072 -0.03259 0.23590  -0.05578 60  PHE A CA  
1109 C C   . PHE A 181 ? 1.33609 1.79104 1.20558 -0.03708 0.22975  -0.02530 60  PHE A C   
1110 O O   . PHE A 181 ? 1.30518 1.75784 1.20622 -0.03781 0.21633  -0.00702 60  PHE A O   
1111 C CB  . PHE A 181 ? 1.47280 1.88185 1.29063 -0.04669 0.22223  -0.06898 60  PHE A CB  
1112 C CG  . PHE A 181 ? 1.44612 1.84872 1.27789 -0.05688 0.19822  -0.05297 60  PHE A CG  
1113 C CD1 . PHE A 181 ? 1.34571 1.71560 1.19314 -0.05586 0.18853  -0.05872 60  PHE A CD1 
1114 C CD2 . PHE A 181 ? 1.36912 1.79726 1.19884 -0.06671 0.18651  -0.03146 60  PHE A CD2 
1115 C CE1 . PHE A 181 ? 1.30899 1.67223 1.16883 -0.06446 0.16838  -0.04481 60  PHE A CE1 
1116 C CE2 . PHE A 181 ? 1.36893 1.78966 1.21300 -0.07496 0.16579  -0.01742 60  PHE A CE2 
1117 C CZ  . PHE A 181 ? 1.32772 1.71626 1.18664 -0.07378 0.15711  -0.02472 60  PHE A CZ  
1118 N N   . GLY A 182 ? 1.27601 1.76088 1.12482 -0.04061 0.23954  -0.01952 61  GLY A N   
1119 C CA  . GLY A 182 ? 1.18155 1.69718 1.04743 -0.04551 0.23537  0.01016  61  GLY A CA  
1120 C C   . GLY A 182 ? 1.12041 1.64809 1.03073 -0.03521 0.24372  0.02551  61  GLY A C   
1121 O O   . GLY A 182 ? 1.01957 1.55993 0.95805 -0.03986 0.23270  0.04982  61  GLY A O   
1122 N N   . GLU A 183 ? 1.26200 1.78578 1.18085 -0.02114 0.26282  0.01129  62  GLU A N   
1123 C CA  . GLU A 183 ? 1.32500 1.86081 1.28984 -0.01019 0.26970  0.02473  62  GLU A CA  
1124 C C   . GLU A 183 ? 1.22319 1.73390 1.21776 -0.00849 0.25038  0.02881  62  GLU A C   
1125 O O   . GLU A 183 ? 1.10078 1.62397 1.13271 -0.00825 0.24217  0.04937  62  GLU A O   
1126 C CB  . GLU A 183 ? 1.39222 1.93067 1.35847 0.00580  0.29611  0.00795  62  GLU A CB  
1127 C CG  . GLU A 183 ? 1.48551 2.04986 1.42217 0.00562  0.31836  0.00368  62  GLU A CG  
1128 C CD  . GLU A 183 ? 1.52951 2.09314 1.46717 0.02242  0.34579  -0.01535 62  GLU A CD  
1129 O OE1 . GLU A 183 ? 1.47848 2.01538 1.43175 0.03337  0.34608  -0.02935 62  GLU A OE1 
1130 O OE2 . GLU A 183 ? 1.61010 2.19915 1.53259 0.02518  0.36786  -0.01591 62  GLU A OE2 
1131 N N   . TRP A 184 ? 1.18036 1.65529 1.15817 -0.00772 0.24318  0.00917  63  TRP A N   
1132 C CA  . TRP A 184 ? 1.11746 1.56592 1.11814 -0.00592 0.22583  0.01235  63  TRP A CA  
1133 C C   . TRP A 184 ? 1.01813 1.47022 1.02791 -0.01931 0.20321  0.03261  63  TRP A C   
1134 O O   . TRP A 184 ? 0.85499 1.30287 0.89570 -0.01749 0.19112  0.04592  63  TRP A O   
1135 C CB  . TRP A 184 ? 1.25068 1.65987 1.22808 -0.00432 0.22421  -0.01225 63  TRP A CB  
1136 C CG  . TRP A 184 ? 1.19848 1.57867 1.19028 -0.00574 0.20506  -0.00836 63  TRP A CG  
1137 C CD1 . TRP A 184 ? 1.05655 1.41979 1.07465 0.00617  0.20329  -0.00660 63  TRP A CD1 
1138 C CD2 . TRP A 184 ? 1.22413 1.58908 1.20364 -0.01935 0.18552  -0.00544 63  TRP A CD2 
1139 N NE1 . TRP A 184 ? 1.09249 1.43007 1.11239 0.00038  0.18429  -0.00290 63  TRP A NE1 
1140 C CE2 . TRP A 184 ? 1.18291 1.52107 1.18051 -0.01517 0.17394  -0.00253 63  TRP A CE2 
1141 C CE3 . TRP A 184 ? 1.18140 1.55354 1.13685 -0.03404 0.17680  -0.00445 63  TRP A CE3 
1142 C CZ2 . TRP A 184 ? 1.11180 1.42973 1.10380 -0.02531 0.15591  0.00044  63  TRP A CZ2 
1143 C CZ3 . TRP A 184 ? 1.26707 1.62022 1.22049 -0.04361 0.15815  -0.00113 63  TRP A CZ3 
1144 C CH2 . TRP A 184 ? 1.16354 1.48964 1.13498 -0.03929 0.14880  0.00085  63  TRP A CH2 
1145 N N   . LEU A 185 ? 1.02283 1.48244 1.00589 -0.03253 0.19684  0.03509  64  LEU A N   
1146 C CA  . LEU A 185 ? 1.05648 1.51581 1.04772 -0.04455 0.17576  0.05298  64  LEU A CA  
1147 C C   . LEU A 185 ? 1.20358 1.69058 1.22775 -0.04599 0.17388  0.07895  64  LEU A C   
1148 O O   . LEU A 185 ? 1.12143 1.60202 1.16627 -0.05140 0.15688  0.09302  64  LEU A O   
1149 C CB  . LEU A 185 ? 1.14614 1.60910 1.10312 -0.05712 0.16950  0.05068  64  LEU A CB  
1150 C CG  . LEU A 185 ? 1.19870 1.64984 1.16007 -0.06818 0.14702  0.06206  64  LEU A CG  
1151 C CD1 . LEU A 185 ? 1.13382 1.55481 1.07368 -0.07175 0.13882  0.04229  64  LEU A CD1 
1152 C CD2 . LEU A 185 ? 1.14252 1.61956 1.09581 -0.07872 0.14191  0.08093  64  LEU A CD2 
1153 N N   . GLU A 186 ? 1.16652 1.68375 1.19633 -0.04165 0.19177  0.08508  65  GLU A N   
1154 C CA  . GLU A 186 ? 1.04220 1.58777 1.10590 -0.04402 0.19180  0.10994  65  GLU A CA  
1155 C C   . GLU A 186 ? 1.00855 1.54769 1.11443 -0.03730 0.18370  0.11635  65  GLU A C   
1156 O O   . GLU A 186 ? 0.94632 1.49984 1.08219 -0.04304 0.17462  0.13670  65  GLU A O   
1157 C CB  . GLU A 186 ? 1.27314 1.85179 1.33585 -0.03910 0.21593  0.11337  65  GLU A CB  
1158 C CG  . GLU A 186 ? 1.37488 1.96710 1.39685 -0.04670 0.22388  0.11260  65  GLU A CG  
1159 C CD  . GLU A 186 ? 1.35429 1.97760 1.37381 -0.04046 0.25021  0.11485  65  GLU A CD  
1160 O OE1 . GLU A 186 ? 1.33178 1.95818 1.37088 -0.02740 0.26528  0.10599  65  GLU A OE1 
1161 O OE2 . GLU A 186 ? 1.42712 2.07177 1.42523 -0.04801 0.25642  0.12603  65  GLU A OE2 
1162 N N   . LYS A 187 ? 1.05100 1.56832 1.15964 -0.02539 0.18628  0.09957  66  LYS A N   
1163 C CA  . LYS A 187 ? 1.00479 1.52438 1.15392 -0.01526 0.18402  0.10547  66  LYS A CA  
1164 C C   . LYS A 187 ? 1.01848 1.52378 1.18741 -0.02204 0.15944  0.11755  66  LYS A C   
1165 O O   . LYS A 187 ? 1.13490 1.65817 1.34067 -0.02236 0.15357  0.13362  66  LYS A O   
1166 C CB  . LYS A 187 ? 1.06805 1.56667 1.21252 0.00042  0.19424  0.08494  66  LYS A CB  
1167 C CG  . LYS A 187 ? 1.21541 1.72708 1.34091 0.00788  0.22007  0.07124  66  LYS A CG  
1168 C CD  . LYS A 187 ? 1.31442 1.80852 1.44461 0.02545  0.23266  0.05340  66  LYS A CD  
1169 C CE  . LYS A 187 ? 1.45196 1.96083 1.56492 0.03303  0.26012  0.03983  66  LYS A CE  
1170 N NZ  . LYS A 187 ? 1.53427 2.02432 1.65227 0.05105  0.27437  0.02162  66  LYS A NZ  
1171 N N   . GLU A 188 ? 1.05094 1.52441 1.19677 -0.02784 0.14509  0.10964  67  GLU A N   
1172 C CA  . GLU A 188 ? 1.10126 1.55692 1.26263 -0.03247 0.12337  0.11812  67  GLU A CA  
1173 C C   . GLU A 188 ? 1.03126 1.47690 1.17428 -0.04735 0.10984  0.12364  67  GLU A C   
1174 O O   . GLU A 188 ? 0.81408 1.25691 0.92690 -0.05258 0.11451  0.11608  67  GLU A O   
1175 C CB  . GLU A 188 ? 1.09023 1.51162 1.24709 -0.02248 0.11795  0.10409  67  GLU A CB  
1176 C CG  . GLU A 188 ? 1.28705 1.71594 1.47356 -0.00755 0.12312  0.10495  67  GLU A CG  
1177 C CD  . GLU A 188 ? 1.42853 1.82745 1.60090 0.00552  0.12922  0.08684  67  GLU A CD  
1178 O OE1 . GLU A 188 ? 1.38602 1.75938 1.52556 0.00179  0.13065  0.07266  67  GLU A OE1 
1179 O OE2 . GLU A 188 ? 1.45045 1.85146 1.64615 0.01945  0.13239  0.08731  67  GLU A OE2 
1180 N N   . LYS A 189 ? 0.90194 1.34246 1.06452 -0.05385 0.09251  0.13668  68  LYS A N   
1181 C CA  . LYS A 189 ? 0.86254 1.28439 1.01087 -0.06531 0.07757  0.13979  68  LYS A CA  
1182 C C   . LYS A 189 ? 0.89753 1.28137 1.02806 -0.06136 0.07014  0.12430  68  LYS A C   
1183 O O   . LYS A 189 ? 0.76049 1.13046 0.90142 -0.05205 0.06766  0.11942  68  LYS A O   
1184 C CB  . LYS A 189 ? 0.84618 1.27523 1.02244 -0.07359 0.06324  0.15840  68  LYS A CB  
1185 C CG  . LYS A 189 ? 0.97793 1.43890 1.16579 -0.08231 0.06866  0.17585  68  LYS A CG  
1186 C CD  . LYS A 189 ? 0.94109 1.40993 1.16329 -0.08948 0.05623  0.19309  68  LYS A CD  
1187 C CE  . LYS A 189 ? 0.91946 1.41668 1.15303 -0.09936 0.06189  0.21199  68  LYS A CE  
1188 N NZ  . LYS A 189 ? 0.99064 1.48189 1.19429 -0.10649 0.06201  0.21350  68  LYS A NZ  
1189 N N   . ARG A 190 ? 0.69652 1.06442 0.80060 -0.06814 0.06713  0.11709  69  ARG A N   
1190 C CA  . ARG A 190 ? 0.83723 1.17052 0.92228 -0.06515 0.06387  0.10116  69  ARG A CA  
1191 C C   . ARG A 190 ? 0.73925 1.05594 0.81379 -0.07582 0.05100  0.10380  69  ARG A C   
1192 O O   . ARG A 190 ? 0.86789 1.19994 0.93765 -0.08476 0.04928  0.11162  69  ARG A O   
1193 C CB  . ARG A 190 ? 0.91945 1.24952 0.98109 -0.06011 0.07884  0.08288  69  ARG A CB  
1194 C CG  . ARG A 190 ? 0.96504 1.29369 1.03559 -0.04595 0.09040  0.07480  69  ARG A CG  
1195 C CD  . ARG A 190 ? 1.03305 1.35998 1.08109 -0.04144 0.10691  0.05632  69  ARG A CD  
1196 N NE  . ARG A 190 ? 1.12015 1.48024 1.16330 -0.04470 0.11758  0.06026  69  ARG A NE  
1197 C CZ  . ARG A 190 ? 1.03645 1.41667 1.08765 -0.03560 0.13354  0.05867  69  ARG A CZ  
1198 N NH1 . ARG A 190 ? 1.03304 1.44268 1.07640 -0.03940 0.14370  0.06304  69  ARG A NH1 
1199 N NH2 . ARG A 190 ? 1.26364 1.63468 1.33067 -0.02212 0.13983  0.05336  69  ARG A NH2 
1200 N N   . ILE A 191 ? 0.84849 1.13392 0.91969 -0.07413 0.04261  0.09800  70  ILE A N   
1201 C CA  . ILE A 191 ? 0.90972 1.17605 0.97338 -0.08264 0.03132  0.09964  70  ILE A CA  
1202 C C   . ILE A 191 ? 0.85557 1.09725 0.89621 -0.08186 0.03574  0.08222  70  ILE A C   
1203 O O   . ILE A 191 ? 0.75863 0.97785 0.79451 -0.07403 0.03905  0.07217  70  ILE A O   
1204 C CB  . ILE A 191 ? 0.85853 1.10778 0.93622 -0.08231 0.01839  0.10735  70  ILE A CB  
1205 C CG1 . ILE A 191 ? 0.84240 1.11650 0.94557 -0.08557 0.01283  0.12443  70  ILE A CG1 
1206 C CG2 . ILE A 191 ? 0.70614 0.93128 0.77348 -0.08935 0.00959  0.10602  70  ILE A CG2 
1207 C CD1 . ILE A 191 ? 0.78222 1.04353 0.90100 -0.08325 0.00085  0.12965  70  ILE A CD1 
1208 N N   . LEU A 192 ? 0.74694 0.99284 0.77460 -0.09007 0.03546  0.07928  71  LEU A N   
1209 C CA  . LEU A 192 ? 0.68182 0.90897 0.69010 -0.09150 0.03971  0.06244  71  LEU A CA  
1210 C C   . LEU A 192 ? 0.90755 1.11530 0.91500 -0.09828 0.02981  0.06442  71  LEU A C   
1211 O O   . LEU A 192 ? 0.83836 1.05830 0.85300 -0.10513 0.02182  0.07659  71  LEU A O   
1212 C CB  . LEU A 192 ? 0.66886 0.91751 0.66258 -0.09597 0.04649  0.05560  71  LEU A CB  
1213 C CG  . LEU A 192 ? 0.73803 1.01718 0.73066 -0.09304 0.05588  0.05836  71  LEU A CG  
1214 C CD1 . LEU A 192 ? 0.69831 0.98404 0.66770 -0.09583 0.06388  0.04240  71  LEU A CD1 
1215 C CD2 . LEU A 192 ? 0.94583 1.22506 0.95020 -0.08178 0.06405  0.05797  71  LEU A CD2 
1216 N N   . LEU A 193 ? 0.75497 0.93194 0.75465 -0.09585 0.03133  0.05327  72  LEU A N   
1217 C CA  . LEU A 193 ? 0.85469 1.01056 0.85339 -0.10112 0.02458  0.05372  72  LEU A CA  
1218 C C   . LEU A 193 ? 0.69320 0.83651 0.67865 -0.10503 0.03041  0.03792  72  LEU A C   
1219 O O   . LEU A 193 ? 0.68594 0.81414 0.66221 -0.10030 0.03933  0.02481  72  LEU A O   
1220 C CB  . LEU A 193 ? 0.97889 1.10697 0.98032 -0.09537 0.02099  0.05626  72  LEU A CB  
1221 C CG  . LEU A 193 ? 1.11796 1.24947 1.13315 -0.09620 0.01008  0.07162  72  LEU A CG  
1222 C CD1 . LEU A 193 ? 0.92395 1.06447 0.94894 -0.08844 0.00935  0.07727  72  LEU A CD1 
1223 C CD2 . LEU A 193 ? 0.98169 1.08208 0.99217 -0.09715 0.00500  0.07104  72  LEU A CD2 
1224 N N   . HIS A 194 ? 0.79426 0.94362 0.78082 -0.11365 0.02527  0.03941  73  HIS A N   
1225 C CA  . HIS A 194 ? 0.75842 0.89625 0.73707 -0.11905 0.02888  0.02530  73  HIS A CA  
1226 C C   . HIS A 194 ? 0.77329 0.87991 0.75437 -0.11913 0.02814  0.02458  73  HIS A C   
1227 O O   . HIS A 194 ? 0.86081 0.96664 0.85097 -0.12188 0.02091  0.03503  73  HIS A O   
1228 C CB  . HIS A 194 ? 0.77434 0.93858 0.75452 -0.12787 0.02321  0.02746  73  HIS A CB  
1229 C CG  . HIS A 194 ? 0.93633 1.12939 0.90822 -0.12828 0.02551  0.02592  73  HIS A CG  
1230 N ND1 . HIS A 194 ? 0.84971 1.04075 0.80786 -0.12642 0.03501  0.00942  73  HIS A ND1 
1231 C CD2 . HIS A 194 ? 0.87351 1.09685 0.84758 -0.13016 0.02064  0.03890  73  HIS A CD2 
1232 C CE1 . HIS A 194 ? 0.91719 1.13665 0.86793 -0.12704 0.03609  0.01138  73  HIS A CE1 
1233 N NE2 . HIS A 194 ? 0.91610 1.15600 0.87599 -0.12937 0.02753  0.02993  73  HIS A NE2 
1234 N N   . ALA A 195 ? 0.83101 0.91068 0.80336 -0.11581 0.03668  0.01242  74  ALA A N   
1235 C CA  . ALA A 195 ? 0.67379 0.72206 0.64501 -0.11587 0.03859  0.01084  74  ALA A CA  
1236 C C   . ALA A 195 ? 0.73457 0.76205 0.69734 -0.11759 0.04933  -0.00556 74  ALA A C   
1237 O O   . ALA A 195 ? 0.88128 0.87759 0.83734 -0.11288 0.05566  -0.00851 74  ALA A O   
1238 C CB  . ALA A 195 ? 0.75094 0.77992 0.72015 -0.10715 0.03651  0.01952  74  ALA A CB  
1239 N N   . GLY A 196 ? 0.71424 0.75815 0.67666 -0.12478 0.05124  -0.01624 75  GLY A N   
1240 C CA  . GLY A 196 ? 0.77106 0.79727 0.72688 -0.12791 0.06131  -0.03350 75  GLY A CA  
1241 C C   . GLY A 196 ? 0.76132 0.78632 0.72430 -0.13912 0.06143  -0.04097 75  GLY A C   
1242 O O   . GLY A 196 ? 0.75041 0.76388 0.71011 -0.14406 0.06917  -0.05655 75  GLY A O   
1243 N N   . GLY A 197 ? 0.76594 0.80236 0.74062 -0.14341 0.05347  -0.03076 76  GLY A N   
1244 C CA  . GLY A 197 ? 0.76950 0.80873 0.75555 -0.15353 0.05311  -0.03658 76  GLY A CA  
1245 C C   . GLY A 197 ? 0.82553 0.82905 0.81203 -0.15421 0.06413  -0.04241 76  GLY A C   
1246 O O   . GLY A 197 ? 0.85837 0.83326 0.83326 -0.14705 0.07246  -0.04373 76  GLY A O   
1247 N N   . GLN A 198 ? 1.01458 1.02087 1.01583 -0.16279 0.06433  -0.04485 77  GLN A N   
1248 C CA  . GLN A 198 ? 0.72467 0.69965 0.72863 -0.16526 0.07639  -0.05042 77  GLN A CA  
1249 C C   . GLN A 198 ? 0.74624 0.70220 0.75073 -0.15939 0.07855  -0.03757 77  GLN A C   
1250 O O   . GLN A 198 ? 0.69743 0.62141 0.69663 -0.15815 0.09032  -0.03975 77  GLN A O   
1251 C CB  . GLN A 198 ? 0.72056 0.70817 0.74305 -0.17815 0.07718  -0.06065 77  GLN A CB  
1252 C CG  . GLN A 198 ? 0.66831 0.67179 0.68907 -0.18611 0.07526  -0.07670 77  GLN A CG  
1253 C CD  . GLN A 198 ? 0.84022 0.86249 0.88250 -0.19970 0.07208  -0.08542 77  GLN A CD  
1254 O OE1 . GLN A 198 ? 0.82706 0.88284 0.88174 -0.20327 0.05933  -0.07969 77  GLN A OE1 
1255 N NE2 . GLN A 198 ? 0.79047 0.79137 0.83891 -0.20732 0.08348  -0.09841 77  GLN A NE2 
1256 N N   . SER A 199 ? 0.69917 0.67263 0.70871 -0.15594 0.06808  -0.02447 78  SER A N   
1257 C CA  . SER A 199 ? 0.86555 0.82189 0.87493 -0.15079 0.06911  -0.01342 78  SER A CA  
1258 C C   . SER A 199 ? 0.77349 0.71425 0.79392 -0.15604 0.07948  -0.01715 78  SER A C   
1259 O O   . SER A 199 ? 0.75360 0.66223 0.76334 -0.15218 0.08979  -0.01610 78  SER A O   
1260 C CB  . SER A 199 ? 0.78451 0.71333 0.77239 -0.14071 0.07214  -0.00918 78  SER A CB  
1261 O OG  . SER A 199 ? 0.84418 0.79004 0.82610 -0.13591 0.06333  -0.00539 78  SER A OG  
1262 N N   . ARG A 200 ? 0.75955 0.72476 0.80185 -0.16497 0.07673  -0.02127 79  ARG A N   
1263 C CA  . ARG A 200 ? 0.62488 0.58132 0.68390 -0.17111 0.08681  -0.02529 79  ARG A CA  
1264 C C   . ARG A 200 ? 0.63453 0.57258 0.69381 -0.16523 0.09187  -0.01529 79  ARG A C   
1265 O O   . ARG A 200 ? 0.60197 0.51359 0.65959 -0.16577 0.10622  -0.01794 79  ARG A O   
1266 C CB  . ARG A 200 ? 0.65517 0.64810 0.74122 -0.18049 0.07870  -0.02845 79  ARG A CB  
1267 C CG  . ARG A 200 ? 0.71743 0.72281 0.80463 -0.18941 0.07754  -0.04293 79  ARG A CG  
1268 C CD  . ARG A 200 ? 0.68071 0.72754 0.79055 -0.19741 0.06442  -0.04390 79  ARG A CD  
1269 N NE  . ARG A 200 ? 0.70875 0.76911 0.81469 -0.20584 0.06082  -0.05867 79  ARG A NE  
1270 C CZ  . ARG A 200 ? 0.71521 0.78206 0.83827 -0.21760 0.06352  -0.07168 79  ARG A CZ  
1271 N NH1 . ARG A 200 ? 0.68531 0.74855 0.83306 -0.22191 0.07048  -0.07039 79  ARG A NH1 
1272 N NH2 . ARG A 200 ? 0.65524 0.73267 0.77159 -0.22536 0.05955  -0.08650 79  ARG A NH2 
1273 N N   . ARG A 201 ? 0.68120 0.63183 0.74200 -0.15986 0.08110  -0.00401 80  ARG A N   
1274 C CA  . ARG A 201 ? 0.91481 0.85091 0.97791 -0.15487 0.08454  0.00438  80  ARG A CA  
1275 C C   . ARG A 201 ? 0.97945 0.88345 1.01413 -0.14612 0.08730  0.00861  80  ARG A C   
1276 O O   . ARG A 201 ? 0.86021 0.74900 0.89214 -0.14183 0.09000  0.01426  80  ARG A O   
1277 C CB  . ARG A 201 ? 0.97848 0.94401 1.06091 -0.15425 0.07134  0.01435  80  ARG A CB  
1278 C CG  . ARG A 201 ? 0.88433 0.88131 0.99730 -0.16184 0.06802  0.01229  80  ARG A CG  
1279 C CD  . ARG A 201 ? 0.99486 1.02621 1.12031 -0.16134 0.05128  0.02225  80  ARG A CD  
1280 N NE  . ARG A 201 ? 1.28730 1.32291 1.39187 -0.15841 0.04261  0.02504  80  ARG A NE  
1281 C CZ  . ARG A 201 ? 1.14962 1.20658 1.25720 -0.15604 0.02988  0.03625  80  ARG A CZ  
1282 N NH1 . ARG A 201 ? 1.18998 1.26491 1.31987 -0.15579 0.02347  0.04618  80  ARG A NH1 
1283 N NH2 . ARG A 201 ? 0.97069 1.03120 1.06049 -0.15366 0.02430  0.03825  80  ARG A NH2 
1284 N N   . LEU A 202 ? 0.89862 0.79194 0.91235 -0.14307 0.08645  0.00574  81  LEU A N   
1285 C CA  . LEU A 202 ? 0.81222 0.67419 0.79876 -0.13480 0.08907  0.00916  81  LEU A CA  
1286 C C   . LEU A 202 ? 0.70805 0.54529 0.67793 -0.13403 0.10043  0.00179  81  LEU A C   
1287 O O   . LEU A 202 ? 0.89245 0.72639 0.84829 -0.12946 0.09647  0.00132  81  LEU A O   
1288 C CB  . LEU A 202 ? 0.77859 0.65284 0.75757 -0.12940 0.07429  0.01652  81  LEU A CB  
1289 C CG  . LEU A 202 ? 0.90687 0.75443 0.86195 -0.12114 0.07235  0.02188  81  LEU A CG  
1290 C CD1 . LEU A 202 ? 0.74270 0.57419 0.69642 -0.12010 0.07529  0.02561  81  LEU A CD1 
1291 C CD2 . LEU A 202 ? 1.01732 0.88227 0.97074 -0.11738 0.05767  0.02831  81  LEU A CD2 
1292 N N   . PRO A 203 ? 0.80780 0.62755 0.78099 -0.13839 0.11550  -0.00367 82  PRO A N   
1293 C CA  . PRO A 203 ? 0.77321 0.56767 0.73233 -0.13840 0.12751  -0.01013 82  PRO A CA  
1294 C C   . PRO A 203 ? 0.79505 0.55918 0.72302 -0.12788 0.12824  -0.00461 82  PRO A C   
1295 O O   . PRO A 203 ? 0.76883 0.51984 0.68510 -0.12504 0.13169  -0.00785 82  PRO A O   
1296 C CB  . PRO A 203 ? 0.74100 0.52078 0.71042 -0.14484 0.14434  -0.01398 82  PRO A CB  
1297 C CG  . PRO A 203 ? 0.73976 0.54671 0.73571 -0.14954 0.13943  -0.01202 82  PRO A CG  
1298 C CD  . PRO A 203 ? 0.58522 0.40599 0.57616 -0.14299 0.12353  -0.00344 82  PRO A CD  
1299 N N   . GLY A 204 ? 0.82014 0.57178 0.73444 -0.12191 0.12511  0.00334  83  GLY A N   
1300 C CA  . GLY A 204 ? 0.86051 0.58344 0.74401 -0.11212 0.12440  0.00887  83  GLY A CA  
1301 C C   . GLY A 204 ? 0.88152 0.61373 0.75869 -0.10616 0.11282  0.01042  83  GLY A C   
1302 O O   . GLY A 204 ? 0.74697 0.45532 0.60251 -0.09855 0.11516  0.01294  83  GLY A O   
1303 N N   . TYR A 205 ? 0.72033 0.48745 0.61655 -0.10899 0.10091  0.00958  84  TYR A N   
1304 C CA  . TYR A 205 ? 0.81975 0.59816 0.71198 -0.10291 0.09099  0.01142  84  TYR A CA  
1305 C C   . TYR A 205 ? 1.05544 0.86222 0.96592 -0.10829 0.08969  0.00406  84  TYR A C   
1306 O O   . TYR A 205 ? 0.91112 0.73589 0.82339 -0.10429 0.08098  0.00569  84  TYR A O   
1307 C CB  . TYR A 205 ? 0.69315 0.48436 0.58389 -0.09852 0.07539  0.02045  84  TYR A CB  
1308 C CG  . TYR A 205 ? 0.88756 0.64846 0.75455 -0.09208 0.07500  0.02620  84  TYR A CG  
1309 C CD1 . TYR A 205 ? 0.78982 0.52949 0.63556 -0.08293 0.07437  0.02926  84  TYR A CD1 
1310 C CD2 . TYR A 205 ? 0.68862 0.44171 0.55356 -0.09470 0.07526  0.02841  84  TYR A CD2 
1311 C CE1 . TYR A 205 ? 0.77146 0.48367 0.59216 -0.07716 0.07273  0.03456  84  TYR A CE1 
1312 C CE2 . TYR A 205 ? 0.85182 0.57629 0.69143 -0.08922 0.07503  0.03225  84  TYR A CE2 
1313 C CZ  . TYR A 205 ? 0.95873 0.66324 0.77504 -0.08075 0.07308  0.03541  84  TYR A CZ  
1314 O OH  . TYR A 205 ? 0.83478 0.51115 0.62269 -0.07541 0.07153  0.03931  84  TYR A OH  
1315 N N   . ALA A 206 ? 0.76681 0.57880 0.69091 -0.11752 0.09816  -0.00431 85  ALA A N   
1316 C CA  . ALA A 206 ? 0.86144 0.69760 0.79893 -0.12332 0.09713  -0.01340 85  ALA A CA  
1317 C C   . ALA A 206 ? 0.68062 0.50476 0.60650 -0.11744 0.10141  -0.01863 85  ALA A C   
1318 O O   . ALA A 206 ? 0.65702 0.50444 0.58697 -0.11606 0.09465  -0.02082 85  ALA A O   
1319 C CB  . ALA A 206 ? 0.65253 0.49243 0.60612 -0.13475 0.10559  -0.02242 85  ALA A CB  
1320 N N   . PRO A 207 ? 0.74356 0.53228 0.65532 -0.11339 0.11323  -0.02044 86  PRO A N   
1321 C CA  . PRO A 207 ? 0.82958 0.60652 0.73313 -0.10716 0.11804  -0.02568 86  PRO A CA  
1322 C C   . PRO A 207 ? 0.89895 0.68375 0.79485 -0.09516 0.10786  -0.01757 86  PRO A C   
1323 O O   . PRO A 207 ? 0.91417 0.69616 0.80755 -0.08926 0.11093  -0.02210 86  PRO A O   
1324 C CB  . PRO A 207 ? 0.94382 0.67817 0.83350 -0.10483 0.13275  -0.02564 86  PRO A CB  
1325 C CG  . PRO A 207 ? 0.71404 0.44447 0.61050 -0.11418 0.13832  -0.02539 86  PRO A CG  
1326 C CD  . PRO A 207 ? 0.64950 0.40593 0.55173 -0.11385 0.12426  -0.01752 86  PRO A CD  
1327 N N   . SER A 208 ? 0.86783 0.66224 0.76168 -0.09144 0.09630  -0.00627 87  SER A N   
1328 C CA  . SER A 208 ? 0.88566 0.69326 0.77761 -0.08180 0.08530  0.00138  87  SER A CA  
1329 C C   . SER A 208 ? 0.87931 0.72616 0.78697 -0.08636 0.07320  0.00462  87  SER A C   
1330 O O   . SER A 208 ? 0.89062 0.75042 0.79972 -0.08044 0.06265  0.01334  87  SER A O   
1331 C CB  . SER A 208 ? 0.76947 0.55375 0.64467 -0.07277 0.08058  0.01241  87  SER A CB  
1332 O OG  . SER A 208 ? 0.80415 0.58814 0.67784 -0.07750 0.07530  0.01774  87  SER A OG  
1333 N N   . GLY A 209 ? 0.76780 0.63410 0.68806 -0.09698 0.07427  -0.00150 88  GLY A N   
1334 C CA  . GLY A 209 ? 0.56313 0.46722 0.49742 -0.10133 0.06440  0.00133  88  GLY A CA  
1335 C C   . GLY A 209 ? 0.74991 0.66525 0.69058 -0.10292 0.05352  0.01286  88  GLY A C   
1336 O O   . GLY A 209 ? 0.63895 0.58454 0.59086 -0.10529 0.04502  0.01786  88  GLY A O   
1337 N N   . LYS A 210 ? 0.69478 0.58553 0.62757 -0.10152 0.05419  0.01728  89  LYS A N   
1338 C CA  . LYS A 210 ? 0.91696 0.81229 0.85444 -0.10309 0.04523  0.02652  89  LYS A CA  
1339 C C   . LYS A 210 ? 0.85687 0.75838 0.79217 -0.09664 0.03374  0.03582  89  LYS A C   
1340 O O   . LYS A 210 ? 0.83925 0.72449 0.76644 -0.09408 0.02867  0.04137  89  LYS A O   
1341 C CB  . LYS A 210 ? 0.70061 0.62547 0.65743 -0.11149 0.04068  0.02803  89  LYS A CB  
1342 C CG  . LYS A 210 ? 0.86304 0.78591 0.82775 -0.11898 0.04861  0.02121  89  LYS A CG  
1343 C CD  . LYS A 210 ? 1.02722 0.97480 1.01052 -0.12446 0.04083  0.02778  89  LYS A CD  
1344 C CE  . LYS A 210 ? 1.05692 1.02737 1.05482 -0.13241 0.04247  0.02159  89  LYS A CE  
1345 N NZ  . LYS A 210 ? 0.89761 0.88588 0.89202 -0.13319 0.04170  0.01540  89  LYS A NZ  
1346 N N   . ILE A 211 ? 0.76525 0.69059 0.70803 -0.09431 0.02979  0.03703  90  ILE A N   
1347 C CA  . ILE A 211 ? 0.72852 0.66611 0.67565 -0.08969 0.01857  0.04647  90  ILE A CA  
1348 C C   . ILE A 211 ? 0.73479 0.64930 0.66767 -0.08005 0.01701  0.04825  90  ILE A C   
1349 O O   . ILE A 211 ? 0.81763 0.73857 0.75385 -0.07662 0.00607  0.05616  90  ILE A O   
1350 C CB  . ILE A 211 ? 0.72231 0.69412 0.68295 -0.08987 0.01678  0.04772  90  ILE A CB  
1351 C CG1 . ILE A 211 ? 0.76905 0.73680 0.72320 -0.08492 0.02706  0.03808  90  ILE A CG1 
1352 C CG2 . ILE A 211 ? 0.90298 0.90001 0.87631 -0.09907 0.01537  0.04894  90  ILE A CG2 
1353 C CD1 . ILE A 211 ? 0.82533 0.82499 0.78968 -0.08427 0.02759  0.03772  90  ILE A CD1 
1354 N N   . LEU A 212 ? 0.74844 0.63619 0.66620 -0.07582 0.02715  0.04173  91  LEU A N   
1355 C CA  . LEU A 212 ? 0.75906 0.62136 0.66038 -0.06598 0.02566  0.04483  91  LEU A CA  
1356 C C   . LEU A 212 ? 0.76527 0.59689 0.64810 -0.06665 0.02568  0.04660  91  LEU A C   
1357 O O   . LEU A 212 ? 0.93983 0.74283 0.80297 -0.05947 0.02910  0.04734  91  LEU A O   
1358 C CB  . LEU A 212 ? 0.61924 0.46776 0.51382 -0.05971 0.03742  0.03822  91  LEU A CB  
1359 C CG  . LEU A 212 ? 0.72270 0.59970 0.63309 -0.05805 0.03906  0.03483  91  LEU A CG  
1360 C CD1 . LEU A 212 ? 0.80347 0.66276 0.70688 -0.05079 0.05106  0.02760  91  LEU A CD1 
1361 C CD2 . LEU A 212 ? 0.82140 0.72324 0.74409 -0.05312 0.02630  0.04421  91  LEU A CD2 
1362 N N   . THR A 213 ? 0.66583 0.50199 0.55376 -0.07455 0.02267  0.04761  92  THR A N   
1363 C CA  . THR A 213 ? 0.94979 0.75716 0.82015 -0.07556 0.02488  0.04787  92  THR A CA  
1364 C C   . THR A 213 ? 0.75178 0.55231 0.61179 -0.07145 0.01060  0.05468  92  THR A C   
1365 O O   . THR A 213 ? 0.71749 0.54068 0.59330 -0.07476 -0.00123 0.05906  92  THR A O   
1366 C CB  . THR A 213 ? 0.79846 0.61351 0.68104 -0.08493 0.02865  0.04550  92  THR A CB  
1367 O OG1 . THR A 213 ? 0.68401 0.50965 0.57843 -0.08970 0.03945  0.03884  92  THR A OG1 
1368 C CG2 . THR A 213 ? 0.63743 0.42136 0.50171 -0.08532 0.03419  0.04454  92  THR A CG2 
1369 N N   . PRO A 214 ? 0.72827 0.49796 0.56179 -0.06505 0.01091  0.05588  93  PRO A N   
1370 C CA  . PRO A 214 ? 0.79421 0.55670 0.61566 -0.06243 -0.00423 0.06095  93  PRO A CA  
1371 C C   . PRO A 214 ? 1.03313 0.79426 0.85725 -0.07044 -0.00726 0.05963  93  PRO A C   
1372 O O   . PRO A 214 ? 0.90089 0.64848 0.72073 -0.07458 0.00504  0.05511  93  PRO A O   
1373 C CB  . PRO A 214 ? 0.68935 0.41556 0.47718 -0.05428 -0.00003 0.06176  93  PRO A CB  
1374 C CG  . PRO A 214 ? 0.73957 0.46089 0.52872 -0.05034 0.01421  0.05948  93  PRO A CG  
1375 C CD  . PRO A 214 ? 0.82128 0.56181 0.63414 -0.05960 0.02421  0.05333  93  PRO A CD  
1376 N N   . VAL A 215 ? 0.93672 0.71188 0.77000 -0.07257 -0.02334 0.06359  94  VAL A N   
1377 C CA  . VAL A 215 ? 1.11125 0.88431 0.94875 -0.07975 -0.02784 0.06260  94  VAL A CA  
1378 C C   . VAL A 215 ? 1.04099 0.79690 0.85816 -0.07762 -0.04239 0.06358  94  VAL A C   
1379 O O   . VAL A 215 ? 1.11234 0.87949 0.93207 -0.07377 -0.05570 0.06804  94  VAL A O   
1380 C CB  . VAL A 215 ? 1.07937 0.88735 0.95138 -0.08672 -0.03358 0.06639  94  VAL A CB  
1381 C CG1 . VAL A 215 ? 1.10789 0.94371 0.99628 -0.08380 -0.04258 0.07190  94  VAL A CG1 
1382 C CG2 . VAL A 215 ? 1.24331 1.04821 1.12031 -0.09280 -0.04321 0.06733  94  VAL A CG2 
1383 N N   . PRO A 216 ? 1.01797 0.74729 0.81485 -0.07983 -0.04047 0.05906  95  PRO A N   
1384 C CA  . PRO A 216 ? 1.13324 0.84244 0.90418 -0.07779 -0.05424 0.05814  95  PRO A CA  
1385 C C   . PRO A 216 ? 1.19816 0.92587 0.98970 -0.08444 -0.07233 0.05993  95  PRO A C   
1386 O O   . PRO A 216 ? 1.19914 0.95495 1.02439 -0.08995 -0.07353 0.06341  95  PRO A O   
1387 C CB  . PRO A 216 ? 1.12238 0.79650 0.86481 -0.07835 -0.04188 0.05123  95  PRO A CB  
1388 C CG  . PRO A 216 ? 1.16139 0.84573 0.92824 -0.08376 -0.02715 0.04922  95  PRO A CG  
1389 C CD  . PRO A 216 ? 1.02701 0.74206 0.82186 -0.08352 -0.02413 0.05385  95  PRO A CD  
1390 N N   . VAL A 217 ? 1.64939 1.36016 1.41904 -0.08428 -0.08670 0.05761  96  VAL A N   
1391 C CA  . VAL A 217 ? 1.87988 1.60122 1.66540 -0.09208 -0.10399 0.05733  96  VAL A CA  
1392 C C   . VAL A 217 ? 2.01438 1.70109 1.76490 -0.09355 -0.10993 0.04894  96  VAL A C   
1393 O O   . VAL A 217 ? 2.01603 1.67723 1.72852 -0.08682 -0.10867 0.04636  96  VAL A O   
1394 C CB  . VAL A 217 ? 1.87009 1.61979 1.67528 -0.09143 -0.12302 0.06428  96  VAL A CB  
1395 C CG1 . VAL A 217 ? 1.84170 1.60903 1.67584 -0.10206 -0.13636 0.06528  96  VAL A CG1 
1396 C CG2 . VAL A 217 ? 1.82885 1.60611 1.65599 -0.08597 -0.11583 0.07149  96  VAL A CG2 
1397 N N   . PHE A 218 ? 2.14461 1.82938 1.90703 -0.10235 -0.11608 0.04475  97  PHE A N   
1398 C CA  . PHE A 218 ? 2.29744 1.95130 2.02915 -0.10523 -0.12459 0.03519  97  PHE A CA  
1399 C C   . PHE A 218 ? 2.29110 1.95952 2.04517 -0.11459 -0.14612 0.03492  97  PHE A C   
1400 O O   . PHE A 218 ? 2.24563 1.94110 2.01944 -0.11506 -0.16123 0.04192  97  PHE A O   
1401 C CB  . PHE A 218 ? 2.37525 2.00203 2.09474 -0.10681 -0.10629 0.02704  97  PHE A CB  
1402 C CG  . PHE A 218 ? 2.46647 2.07179 2.17595 -0.11396 -0.11509 0.01717  97  PHE A CG  
1403 C CD1 . PHE A 218 ? 2.52613 2.10486 2.19456 -0.11324 -0.12723 0.00884  97  PHE A CD1 
1404 C CD2 . PHE A 218 ? 2.46855 2.07938 2.20893 -0.12131 -0.11159 0.01614  97  PHE A CD2 
1405 C CE1 . PHE A 218 ? 2.56697 2.12431 2.22492 -0.12051 -0.13542 -0.00224 97  PHE A CE1 
1406 C CE2 . PHE A 218 ? 2.52081 2.10933 2.25303 -0.12797 -0.11890 0.00618  97  PHE A CE2 
1407 C CZ  . PHE A 218 ? 2.56318 2.12456 2.25389 -0.12796 -0.13070 -0.00400 97  PHE A CZ  
1408 N N   . HIS A 225 ? 1.61555 1.55202 1.58480 -0.08576 -0.19293 0.10655  104 HIS A N   
1409 C CA  . HIS A 225 ? 1.64037 1.57034 1.59670 -0.07520 -0.17368 0.10650  104 HIS A CA  
1410 C C   . HIS A 225 ? 1.71917 1.62068 1.63833 -0.06344 -0.17622 0.10433  104 HIS A C   
1411 O O   . HIS A 225 ? 1.76513 1.64941 1.66329 -0.06382 -0.19234 0.10213  104 HIS A O   
1412 C CB  . HIS A 225 ? 1.54025 1.45533 1.48747 -0.08065 -0.15524 0.10153  104 HIS A CB  
1413 C CG  . HIS A 225 ? 1.51943 1.40319 1.44244 -0.08787 -0.15869 0.09431  104 HIS A CG  
1414 N ND1 . HIS A 225 ? 1.53193 1.41880 1.47052 -0.09972 -0.15928 0.09322  104 HIS A ND1 
1415 C CD2 . HIS A 225 ? 1.53024 1.37809 1.41396 -0.08442 -0.16118 0.08792  104 HIS A CD2 
1416 C CE1 . HIS A 225 ? 1.53837 1.39219 1.44936 -0.10299 -0.16148 0.08535  104 HIS A CE1 
1417 N NE2 . HIS A 225 ? 1.59993 1.43004 1.47627 -0.09406 -0.16248 0.08181  104 HIS A NE2 
1418 N N   . LEU A 226 ? 1.67330 1.56916 1.58349 -0.05322 -0.16015 0.10502  105 LEU A N   
1419 C CA  . LEU A 226 ? 1.52265 1.38931 1.39744 -0.04142 -0.15884 0.10457  105 LEU A CA  
1420 C C   . LEU A 226 ? 1.26638 1.10436 1.11605 -0.04134 -0.13716 0.09850  105 LEU A C   
1421 O O   . LEU A 226 ? 1.27815 1.10529 1.12219 -0.05111 -0.13154 0.09285  105 LEU A O   
1422 C CB  . LEU A 226 ? 1.34251 1.22712 1.23212 -0.02810 -0.15964 0.11179  105 LEU A CB  
1423 C CG  . LEU A 226 ? 1.27273 1.17499 1.17485 -0.02393 -0.18373 0.11836  105 LEU A CG  
1424 C CD1 . LEU A 226 ? 1.06248 0.99121 0.99190 -0.01142 -0.18162 0.12591  105 LEU A CD1 
1425 C CD2 . LEU A 226 ? 1.23943 1.10867 1.09969 -0.01888 -0.19667 0.11777  105 LEU A CD2 
1426 N N   . GLY A 227 ? 1.21864 1.04388 1.05502 -0.03053 -0.12463 0.09966  106 GLY A N   
1427 C CA  . GLY A 227 ? 1.22906 1.03730 1.05464 -0.03201 -0.10230 0.09417  106 GLY A CA  
1428 C C   . GLY A 227 ? 1.29126 1.12961 1.15070 -0.03908 -0.09280 0.09267  106 GLY A C   
1429 O O   . GLY A 227 ? 1.10517 0.97575 0.99420 -0.03768 -0.09772 0.09712  106 GLY A O   
1430 N N   . GLN A 228 ? 0.94382 0.77277 0.79919 -0.04660 -0.07898 0.08681  107 GLN A N   
1431 C CA  . GLN A 228 ? 1.02124 0.87929 0.90635 -0.05392 -0.07215 0.08617  107 GLN A CA  
1432 C C   . GLN A 228 ? 0.94612 0.79115 0.82370 -0.05813 -0.05401 0.07965  107 GLN A C   
1433 O O   . GLN A 228 ? 0.88009 0.69442 0.73272 -0.05839 -0.04761 0.07555  107 GLN A O   
1434 C CB  . GLN A 228 ? 1.08356 0.96099 0.98868 -0.06381 -0.08501 0.08911  107 GLN A CB  
1435 C CG  . GLN A 228 ? 1.07144 0.92722 0.96254 -0.07187 -0.08561 0.08487  107 GLN A CG  
1436 C CD  . GLN A 228 ? 1.35923 1.23326 1.27270 -0.08137 -0.09844 0.08823  107 GLN A CD  
1437 O OE1 . GLN A 228 ? 1.29808 1.20442 1.24067 -0.08344 -0.10350 0.09426  107 GLN A OE1 
1438 N NE2 . GLN A 228 ? 1.35522 1.20777 1.25559 -0.08728 -0.10261 0.08428  107 GLN A NE2 
1439 N N   . ASN A 229 ? 0.78507 0.65528 0.68502 -0.06156 -0.04578 0.07880  108 ASN A N   
1440 C CA  . ASN A 229 ? 0.87930 0.74489 0.77849 -0.06688 -0.03072 0.07274  108 ASN A CA  
1441 C C   . ASN A 229 ? 0.90568 0.80085 0.83018 -0.07605 -0.03221 0.07485  108 ASN A C   
1442 O O   . ASN A 229 ? 0.81360 0.72875 0.75443 -0.07880 -0.04397 0.08120  108 ASN A O   
1443 C CB  . ASN A 229 ? 0.86146 0.72418 0.75745 -0.06113 -0.01727 0.06813  108 ASN A CB  
1444 C CG  . ASN A 229 ? 0.78687 0.67579 0.70015 -0.05530 -0.02024 0.07123  108 ASN A CG  
1445 O OD1 . ASN A 229 ? 0.97480 0.89351 0.90948 -0.05882 -0.02802 0.07605  108 ASN A OD1 
1446 N ND2 . ASN A 229 ? 0.75556 0.63283 0.66050 -0.04607 -0.01282 0.06882  108 ASN A ND2 
1447 N N   . LEU A 230 ? 0.79519 0.69360 0.72377 -0.08106 -0.02073 0.07024  109 LEU A N   
1448 C CA  . LEU A 230 ? 0.82480 0.75061 0.77539 -0.08914 -0.02225 0.07354  109 LEU A CA  
1449 C C   . LEU A 230 ? 0.73095 0.69054 0.70054 -0.08819 -0.02613 0.07865  109 LEU A C   
1450 O O   . LEU A 230 ? 0.64763 0.62845 0.63477 -0.09296 -0.03437 0.08632  109 LEU A O   
1451 C CB  . LEU A 230 ? 0.87904 0.80426 0.83051 -0.09372 -0.01008 0.06744  109 LEU A CB  
1452 C CG  . LEU A 230 ? 1.01099 0.92017 0.96004 -0.09889 -0.00784 0.06630  109 LEU A CG  
1453 C CD1 . LEU A 230 ? 0.95131 0.87538 0.91687 -0.10406 -0.01830 0.07440  109 LEU A CD1 
1454 C CD2 . LEU A 230 ? 1.02039 0.89233 0.94504 -0.09473 -0.00503 0.06248  109 LEU A CD2 
1455 N N   . LEU A 231 ? 0.68371 0.64788 0.65052 -0.08209 -0.01891 0.07449  110 LEU A N   
1456 C CA  . LEU A 231 ? 0.67601 0.67196 0.65977 -0.08019 -0.01971 0.07822  110 LEU A CA  
1457 C C   . LEU A 231 ? 0.70893 0.71593 0.70437 -0.07770 -0.03257 0.08717  110 LEU A C   
1458 O O   . LEU A 231 ? 0.71470 0.75064 0.73039 -0.08163 -0.03695 0.09444  110 LEU A O   
1459 C CB  . LEU A 231 ? 0.77600 0.76894 0.75273 -0.07265 -0.00880 0.07059  110 LEU A CB  
1460 C CG  . LEU A 231 ? 0.91126 0.93533 0.90371 -0.06894 -0.00685 0.07284  110 LEU A CG  
1461 C CD1 . LEU A 231 ? 0.59240 0.64728 0.59887 -0.07771 -0.00653 0.07653  110 LEU A CD1 
1462 C CD2 . LEU A 231 ? 0.75731 0.77377 0.74142 -0.06140 0.00562  0.06316  110 LEU A CD2 
1463 N N   . SER A 232 ? 0.75481 0.74013 0.73808 -0.07113 -0.03876 0.08716  111 SER A N   
1464 C CA  . SER A 232 ? 0.83060 0.82771 0.82642 -0.06906 -0.05284 0.09501  111 SER A CA  
1465 C C   . SER A 232 ? 0.85357 0.85553 0.85946 -0.07913 -0.06371 0.10048  111 SER A C   
1466 O O   . SER A 232 ? 0.71520 0.73796 0.74122 -0.08144 -0.07415 0.10788  111 SER A O   
1467 C CB  . SER A 232 ? 0.80925 0.78088 0.78684 -0.05983 -0.05881 0.09396  111 SER A CB  
1468 O OG  . SER A 232 ? 0.84942 0.79727 0.81152 -0.06406 -0.06792 0.09372  111 SER A OG  
1469 N N   . LEU A 233 ? 0.85282 0.83590 0.84720 -0.08525 -0.06075 0.09695  112 LEU A N   
1470 C CA  . LEU A 233 ? 0.76668 0.75174 0.77133 -0.09448 -0.06934 0.10157  112 LEU A CA  
1471 C C   . LEU A 233 ? 0.82426 0.84166 0.85388 -0.10114 -0.06688 0.10863  112 LEU A C   
1472 O O   . LEU A 233 ? 0.80063 0.83121 0.84855 -0.10757 -0.07581 0.11634  112 LEU A O   
1473 C CB  . LEU A 233 ? 0.90174 0.85617 0.88741 -0.09743 -0.06512 0.09553  112 LEU A CB  
1474 C CG  . LEU A 233 ? 1.08337 1.02609 1.07135 -0.10440 -0.07499 0.09751  112 LEU A CG  
1475 C CD1 . LEU A 233 ? 1.12145 1.05886 1.10652 -0.10297 -0.09023 0.09897  112 LEU A CD1 
1476 C CD2 . LEU A 233 ? 1.13222 1.04329 1.09971 -0.10511 -0.06765 0.09029  112 LEU A CD2 
1477 N N   . GLN A 234 ? 0.76674 0.79654 0.79652 -0.10010 -0.05491 0.10617  113 GLN A N   
1478 C CA  . GLN A 234 ? 0.80561 0.86343 0.85296 -0.10636 -0.05158 0.11266  113 GLN A CA  
1479 C C   . GLN A 234 ? 0.66868 0.75934 0.73390 -0.10472 -0.05159 0.11935  113 GLN A C   
1480 O O   . GLN A 234 ? 0.77088 0.88479 0.85504 -0.11089 -0.05424 0.12937  113 GLN A O   
1481 C CB  . GLN A 234 ? 0.72904 0.78540 0.76646 -0.10675 -0.03984 0.10592  113 GLN A CB  
1482 C CG  . GLN A 234 ? 0.61578 0.70272 0.66687 -0.11189 -0.03642 0.11220  113 GLN A CG  
1483 C CD  . GLN A 234 ? 0.79810 0.88733 0.86114 -0.11952 -0.04214 0.12118  113 GLN A CD  
1484 O OE1 . GLN A 234 ? 0.77166 0.85162 0.83069 -0.12213 -0.03918 0.11867  113 GLN A OE1 
1485 N NE2 . GLN A 234 ? 0.75075 0.85218 0.83073 -0.12307 -0.05010 0.13198  113 GLN A NE2 
1486 N N   . LEU A 235 ? 0.56281 0.65504 0.62273 -0.09607 -0.04738 0.11440  114 LEU A N   
1487 C CA  . LEU A 235 ? 0.80159 0.92501 0.87746 -0.09271 -0.04352 0.11881  114 LEU A CA  
1488 C C   . LEU A 235 ? 0.76095 0.90800 0.86283 -0.09715 -0.05267 0.13111  114 LEU A C   
1489 O O   . LEU A 235 ? 0.79713 0.97466 0.91448 -0.09897 -0.04703 0.13767  114 LEU A O   
1490 C CB  . LEU A 235 ? 0.80506 0.91976 0.87217 -0.08107 -0.03926 0.11159  114 LEU A CB  
1491 C CG  . LEU A 235 ? 0.79858 0.94145 0.87979 -0.07460 -0.03196 0.11318  114 LEU A CG  
1492 C CD1 . LEU A 235 ? 0.74332 0.90238 0.82029 -0.07706 -0.01862 0.10914  114 LEU A CD1 
1493 C CD2 . LEU A 235 ? 0.71650 0.84448 0.79006 -0.06201 -0.02990 0.10708  114 LEU A CD2 
1494 N N   . PRO A 236 ? 0.64169 0.77723 0.74941 -0.09948 -0.06612 0.13445  115 PRO A N   
1495 C CA  . PRO A 236 ? 0.71694 0.87669 0.85315 -0.10534 -0.07469 0.14593  115 PRO A CA  
1496 C C   . PRO A 236 ? 0.74445 0.92303 0.89516 -0.11533 -0.07150 0.15566  115 PRO A C   
1497 O O   . PRO A 236 ? 0.70105 0.90906 0.87605 -0.11858 -0.07103 0.16587  115 PRO A O   
1498 C CB  . PRO A 236 ? 0.64510 0.78126 0.77824 -0.10801 -0.09037 0.14460  115 PRO A CB  
1499 C CG  . PRO A 236 ? 0.73254 0.84256 0.83972 -0.09797 -0.08943 0.13423  115 PRO A CG  
1500 C CD  . PRO A 236 ? 0.78072 0.88321 0.86981 -0.09541 -0.07400 0.12754  115 PRO A CD  
1501 N N   . LEU A 237 ? 0.67516 0.83839 0.81297 -0.11996 -0.06888 0.15386  116 LEU A N   
1502 C CA  . LEU A 237 ? 0.67967 0.86139 0.82953 -0.12783 -0.06514 0.16435  116 LEU A CA  
1503 C C   . LEU A 237 ? 0.86635 1.07889 1.01913 -0.12496 -0.05312 0.16744  116 LEU A C   
1504 O O   . LEU A 237 ? 0.85824 1.09783 1.03004 -0.12968 -0.05115 0.17978  116 LEU A O   
1505 C CB  . LEU A 237 ? 0.79203 0.95266 0.92738 -0.13098 -0.06383 0.16105  116 LEU A CB  
1506 C CG  . LEU A 237 ? 0.74243 0.92051 0.89016 -0.13830 -0.06155 0.17358  116 LEU A CG  
1507 C CD1 . LEU A 237 ? 0.71604 0.90454 0.88948 -0.14588 -0.06927 0.18691  116 LEU A CD1 
1508 C CD2 . LEU A 237 ? 0.67321 0.83049 0.81026 -0.14026 -0.06130 0.17059  116 LEU A CD2 
1509 N N   . TYR A 238 ? 0.85375 1.06139 0.98677 -0.11767 -0.04415 0.15606  117 TYR A N   
1510 C CA  . TYR A 238 ? 0.86129 1.09530 0.99278 -0.11459 -0.03206 0.15600  117 TYR A CA  
1511 C C   . TYR A 238 ? 0.91489 1.17421 1.06653 -0.11120 -0.03002 0.16222  117 TYR A C   
1512 O O   . TYR A 238 ? 0.95675 1.24526 1.11780 -0.11303 -0.02216 0.17021  117 TYR A O   
1513 C CB  . TYR A 238 ? 0.79607 1.01572 0.90384 -0.10738 -0.02363 0.14029  117 TYR A CB  
1514 C CG  . TYR A 238 ? 0.94598 1.14318 1.03638 -0.11067 -0.02415 0.13338  117 TYR A CG  
1515 C CD1 . TYR A 238 ? 0.90340 1.10147 0.99903 -0.11877 -0.02919 0.14193  117 TYR A CD1 
1516 C CD2 . TYR A 238 ? 0.93823 1.11341 1.00926 -0.10547 -0.01894 0.11887  117 TYR A CD2 
1517 C CE1 . TYR A 238 ? 0.74647 0.92638 0.82997 -0.12104 -0.02917 0.13595  117 TYR A CE1 
1518 C CE2 . TYR A 238 ? 0.79815 0.95488 0.85678 -0.10892 -0.01852 0.11276  117 TYR A CE2 
1519 C CZ  . TYR A 238 ? 0.79774 0.95805 0.86338 -0.11642 -0.02373 0.12121  117 TYR A CZ  
1520 O OH  . TYR A 238 ? 0.95327 1.09735 1.01011 -0.11915 -0.02289 0.11545  117 TYR A OH  
1521 N N   . GLU A 239 ? 0.78022 1.02970 0.93886 -0.10596 -0.03688 0.15915  118 GLU A N   
1522 C CA  . GLU A 239 ? 0.86246 1.13723 1.04394 -0.10161 -0.03540 0.16470  118 GLU A CA  
1523 C C   . GLU A 239 ? 0.83633 1.13444 1.04630 -0.11143 -0.04035 0.18064  118 GLU A C   
1524 O O   . GLU A 239 ? 0.98876 1.31844 1.21629 -0.11136 -0.03177 0.18872  118 GLU A O   
1525 C CB  . GLU A 239 ? 0.68331 0.94146 0.86553 -0.09340 -0.04395 0.15843  118 GLU A CB  
1526 C CG  . GLU A 239 ? 0.72645 0.96547 0.88409 -0.08234 -0.03563 0.14447  118 GLU A CG  
1527 C CD  . GLU A 239 ? 0.95050 1.16855 1.10434 -0.07372 -0.04465 0.13965  118 GLU A CD  
1528 O OE1 . GLU A 239 ? 0.99065 1.20212 1.13515 -0.06243 -0.03684 0.13184  118 GLU A OE1 
1529 O OE2 . GLU A 239 ? 1.10078 1.30791 1.25988 -0.07808 -0.05962 0.14360  118 GLU A OE2 
1530 N N   . LYS A 240 ? 0.72203 1.00402 0.93746 -0.12000 -0.05329 0.18513  119 LYS A N   
1531 C CA  . LYS A 240 ? 0.75158 1.05134 0.99393 -0.13094 -0.05778 0.20029  119 LYS A CA  
1532 C C   . LYS A 240 ? 0.74982 1.07157 0.99233 -0.13537 -0.04556 0.21024  119 LYS A C   
1533 O O   . LYS A 240 ? 0.98722 1.33851 1.25251 -0.13923 -0.04025 0.22285  119 LYS A O   
1534 C CB  . LYS A 240 ? 0.82249 1.09461 1.06434 -0.13918 -0.07197 0.20066  119 LYS A CB  
1535 C CG  . LYS A 240 ? 1.08624 1.37120 1.35833 -0.15114 -0.07861 0.21507  119 LYS A CG  
1536 C CD  . LYS A 240 ? 1.08721 1.34127 1.35829 -0.15810 -0.09355 0.21186  119 LYS A CD  
1537 C CE  . LYS A 240 ? 0.95858 1.18894 1.20946 -0.16046 -0.09100 0.21012  119 LYS A CE  
1538 N NZ  . LYS A 240 ? 1.04773 1.24740 1.29834 -0.16702 -0.10372 0.20660  119 LYS A NZ  
1539 N N   . ILE A 241 ? 0.73732 1.04589 0.95458 -0.13492 -0.04103 0.20522  120 ILE A N   
1540 C CA  . ILE A 241 ? 0.73521 1.06403 0.94809 -0.13849 -0.03102 0.21437  120 ILE A CA  
1541 C C   . ILE A 241 ? 0.88522 1.24463 1.10008 -0.13282 -0.01717 0.21508  120 ILE A C   
1542 O O   . ILE A 241 ? 0.80394 1.19067 1.03215 -0.13725 -0.01014 0.22908  120 ILE A O   
1543 C CB  . ILE A 241 ? 0.83593 1.14662 1.02108 -0.13749 -0.02963 0.20612  120 ILE A CB  
1544 C CG1 . ILE A 241 ? 0.77735 1.06521 0.96537 -0.14449 -0.04019 0.21083  120 ILE A CG1 
1545 C CG2 . ILE A 241 ? 0.69030 1.02521 0.86436 -0.13795 -0.01847 0.21130  120 ILE A CG2 
1546 C CD1 . ILE A 241 ? 0.73612 1.00206 0.90061 -0.14225 -0.04028 0.20008  120 ILE A CD1 
1547 N N   . MET A 242 ? 0.83755 1.19169 1.03908 -0.12263 -0.01196 0.20018  121 MET A N   
1548 C CA  . MET A 242 ? 0.92447 1.30384 1.12294 -0.11597 0.00331  0.19771  121 MET A CA  
1549 C C   . MET A 242 ? 1.02612 1.43249 1.25647 -0.11519 0.00639  0.20796  121 MET A C   
1550 O O   . MET A 242 ? 0.95597 1.39071 1.19062 -0.11314 0.02045  0.21282  121 MET A O   
1551 C CB  . MET A 242 ? 0.95048 1.31283 1.12777 -0.10509 0.00811  0.17849  121 MET A CB  
1552 C CG  . MET A 242 ? 0.99622 1.37494 1.15643 -0.09975 0.02456  0.17118  121 MET A CG  
1553 S SD  . MET A 242 ? 0.88530 1.27316 1.02457 -0.10884 0.02768  0.17675  121 MET A SD  
1554 C CE  . MET A 242 ? 0.80503 1.20893 0.92139 -0.10128 0.04625  0.16346  121 MET A CE  
1555 N N   . SER A 243 ? 0.96995 1.36890 1.22310 -0.11714 -0.00651 0.21123  122 SER A N   
1556 C CA  . SER A 243 ? 1.02465 1.45162 1.31412 -0.11925 -0.00588 0.22322  122 SER A CA  
1557 C C   . SER A 243 ? 1.05536 1.50177 1.36053 -0.13145 -0.00309 0.24173  122 SER A C   
1558 O O   . SER A 243 ? 1.04847 1.52688 1.36994 -0.13196 0.00960  0.25190  122 SER A O   
1559 C CB  . SER A 243 ? 1.01585 1.42929 1.32456 -0.11958 -0.02309 0.22138  122 SER A CB  
1560 O OG  . SER A 243 ? 1.10616 1.49632 1.41252 -0.12989 -0.03730 0.22445  122 SER A OG  
1561 N N   . LEU A 244 ? 0.98314 1.40980 1.28374 -0.14097 -0.01372 0.24686  123 LEU A N   
1562 C CA  . LEU A 244 ? 0.92829 1.36936 1.24397 -0.15248 -0.01165 0.26582  123 LEU A CA  
1563 C C   . LEU A 244 ? 1.02868 1.48963 1.32581 -0.15141 0.00454  0.27222  123 LEU A C   
1564 O O   . LEU A 244 ? 0.97360 1.45481 1.28473 -0.15903 0.01069  0.29026  123 LEU A O   
1565 C CB  . LEU A 244 ? 0.93783 1.34936 1.25000 -0.16096 -0.02579 0.26818  123 LEU A CB  
1566 C CG  . LEU A 244 ? 0.99909 1.41747 1.32889 -0.17325 -0.02638 0.28821  123 LEU A CG  
1567 C CD1 . LEU A 244 ? 0.93706 1.38333 1.30527 -0.17974 -0.02327 0.30218  123 LEU A CD1 
1568 C CD2 . LEU A 244 ? 0.87838 1.26306 1.20787 -0.17981 -0.04132 0.28684  123 LEU A CD2 
1569 N N   . ALA A 245 ? 1.06572 1.52135 1.33128 -0.14249 0.01163  0.25795  124 ALA A N   
1570 C CA  . ALA A 245 ? 0.99373 1.46609 1.23658 -0.14186 0.02489  0.26176  124 ALA A CA  
1571 C C   . ALA A 245 ? 1.04065 1.54853 1.29547 -0.13900 0.04188  0.26893  124 ALA A C   
1572 O O   . ALA A 245 ? 1.12265 1.64003 1.39761 -0.13335 0.04501  0.26432  124 ALA A O   
1573 C CB  . ALA A 245 ? 0.95245 1.40827 1.15954 -0.13411 0.02687  0.24221  124 ALA A CB  
1574 N N   . PRO A 246 ? 0.96594 1.49459 1.20922 -0.14249 0.05323  0.28114  125 PRO A N   
1575 C CA  . PRO A 246 ? 1.09611 1.65796 1.34377 -0.13857 0.07260  0.28593  125 PRO A CA  
1576 C C   . PRO A 246 ? 1.28425 1.84599 1.51480 -0.12572 0.08228  0.26432  125 PRO A C   
1577 O O   . PRO A 246 ? 1.06989 1.60762 1.27546 -0.12075 0.07642  0.24647  125 PRO A O   
1578 C CB  . PRO A 246 ? 1.02081 1.59649 1.24475 -0.14366 0.08073  0.29919  125 PRO A CB  
1579 C CG  . PRO A 246 ? 1.04847 1.60571 1.27828 -0.15336 0.06488  0.31164  125 PRO A CG  
1580 C CD  . PRO A 246 ? 0.87153 1.39564 1.10234 -0.15087 0.04845  0.29478  125 PRO A CD  
1581 N N   . ASP A 247 ? 1.49970 2.08868 1.74559 -0.12031 0.09849  0.26642  126 ASP A N   
1582 C CA  . ASP A 247 ? 1.67236 2.26254 1.90844 -0.10701 0.10965  0.24707  126 ASP A CA  
1583 C C   . ASP A 247 ? 1.61167 2.20679 1.80589 -0.10274 0.12425  0.23662  126 ASP A C   
1584 O O   . ASP A 247 ? 1.75756 2.35789 1.94336 -0.09194 0.13814  0.22180  126 ASP A O   
1585 C CB  . ASP A 247 ? 1.79077 2.40893 2.06455 -0.10192 0.12141  0.25335  126 ASP A CB  
1586 C CG  . ASP A 247 ? 1.88543 2.49569 2.19804 -0.10291 0.10508  0.25608  126 ASP A CG  
1587 O OD1 . ASP A 247 ? 1.90187 2.48268 2.20588 -0.09886 0.09077  0.24241  126 ASP A OD1 
1588 O OD2 . ASP A 247 ? 1.92535 2.55914 2.27676 -0.10813 0.10652  0.27191  126 ASP A OD2 
1589 N N   . LYS A 248 ? 1.38714 1.98056 1.55531 -0.11077 0.12099  0.24377  127 LYS A N   
1590 C CA  . LYS A 248 ? 1.28571 1.87937 1.40999 -0.10813 0.12949  0.23158  127 LYS A CA  
1591 C C   . LYS A 248 ? 1.15994 1.72181 1.25935 -0.10846 0.11470  0.21498  127 LYS A C   
1592 O O   . LYS A 248 ? 0.97156 1.52797 1.03866 -0.10405 0.12073  0.19693  127 LYS A O   
1593 C CB  . LYS A 248 ? 1.29475 1.91064 1.40396 -0.11620 0.13569  0.25101  127 LYS A CB  
1594 C CG  . LYS A 248 ? 1.36382 1.98320 1.42513 -0.11479 0.14276  0.24002  127 LYS A CG  
1595 C CD  . LYS A 248 ? 1.49221 2.13102 1.53784 -0.12311 0.14485  0.26220  127 LYS A CD  
1596 C CE  . LYS A 248 ? 1.38306 2.00580 1.43458 -0.13202 0.12388  0.27569  127 LYS A CE  
1597 N NZ  . LYS A 248 ? 1.40507 2.04483 1.43714 -0.13873 0.12506  0.29692  127 LYS A NZ  
1598 N N   . LEU A 249 ? 1.04168 1.58232 1.15624 -0.11376 0.09631  0.21989  128 LEU A N   
1599 C CA  . LEU A 249 ? 0.94255 1.45253 1.03895 -0.11417 0.08275  0.20530  128 LEU A CA  
1600 C C   . LEU A 249 ? 0.78411 1.27339 0.88832 -0.10519 0.08166  0.18701  128 LEU A C   
1601 O O   . LEU A 249 ? 0.79624 1.27366 0.92614 -0.10507 0.07187  0.19094  128 LEU A O   
1602 C CB  . LEU A 249 ? 0.98488 1.48154 1.09361 -0.12328 0.06558  0.21948  128 LEU A CB  
1603 C CG  . LEU A 249 ? 0.98731 1.50469 1.10031 -0.13183 0.06627  0.24370  128 LEU A CG  
1604 C CD1 . LEU A 249 ? 1.00944 1.50948 1.14028 -0.13957 0.04974  0.25652  128 LEU A CD1 
1605 C CD2 . LEU A 249 ? 1.02499 1.55460 1.10191 -0.13282 0.07170  0.24231  128 LEU A CD2 
1606 N N   . HIS A 250 ? 0.81463 1.29889 0.89582 -0.09764 0.09165  0.16706  129 HIS A N   
1607 C CA  . HIS A 250 ? 0.83438 1.29941 0.92097 -0.08759 0.09342  0.15014  129 HIS A CA  
1608 C C   . HIS A 250 ? 0.99198 1.42261 1.06102 -0.08781 0.08290  0.13435  129 HIS A C   
1609 O O   . HIS A 250 ? 0.78960 1.20061 0.86034 -0.07951 0.08420  0.12070  129 HIS A O   
1610 C CB  . HIS A 250 ? 0.90474 1.38326 0.98033 -0.07795 0.11333  0.13736  129 HIS A CB  
1611 C CG  . HIS A 250 ? 1.01705 1.53069 1.10914 -0.07691 0.12700  0.15186  129 HIS A CG  
1612 N ND1 . HIS A 250 ? 1.04611 1.58005 1.11819 -0.07350 0.14585  0.14639  129 HIS A ND1 
1613 C CD2 . HIS A 250 ? 0.97059 1.50275 1.09775 -0.07933 0.12529  0.17136  129 HIS A CD2 
1614 C CE1 . HIS A 250 ? 1.00037 1.56430 1.09459 -0.07338 0.15637  0.16288  129 HIS A CE1 
1615 N NE2 . HIS A 250 ? 1.02182 1.58572 1.15128 -0.07728 0.14392  0.17839  129 HIS A NE2 
1616 N N   . THR A 251 ? 0.86018 1.28333 0.91341 -0.09661 0.07328  0.13636  130 THR A N   
1617 C CA  . THR A 251 ? 1.01299 1.40615 1.05004 -0.09748 0.06536  0.12105  130 THR A CA  
1618 C C   . THR A 251 ? 0.86717 1.24966 0.91105 -0.10620 0.04945  0.13267  130 THR A C   
1619 O O   . THR A 251 ? 0.74224 1.13923 0.77983 -0.11346 0.04607  0.14344  130 THR A O   
1620 C CB  . THR A 251 ? 1.03729 1.43243 1.04272 -0.09836 0.07269  0.10490  130 THR A CB  
1621 O OG1 . THR A 251 ? 1.20597 1.62226 1.20007 -0.10671 0.06969  0.11648  130 THR A OG1 
1622 C CG2 . THR A 251 ? 0.95301 1.35810 0.95028 -0.08947 0.09029  0.09246  130 THR A CG2 
1623 N N   . LEU A 252 ? 0.63213 0.98915 0.68835 -0.10488 0.04009  0.13102  131 LEU A N   
1624 C CA  . LEU A 252 ? 0.88907 1.22883 0.94792 -0.11171 0.02662  0.13654  131 LEU A CA  
1625 C C   . LEU A 252 ? 0.84529 1.16151 0.88436 -0.11162 0.02540  0.11900  131 LEU A C   
1626 O O   . LEU A 252 ? 0.70491 1.00513 0.73619 -0.10518 0.03121  0.10349  131 LEU A O   
1627 C CB  . LEU A 252 ? 0.79714 1.12168 0.87822 -0.11101 0.01737  0.14402  131 LEU A CB  
1628 C CG  . LEU A 252 ? 0.78422 1.08710 0.86968 -0.11694 0.00442  0.14886  131 LEU A CG  
1629 C CD1 . LEU A 252 ? 0.59238 0.89363 0.70219 -0.11891 -0.00383 0.16167  131 LEU A CD1 
1630 C CD2 . LEU A 252 ? 0.64036 0.91104 0.71195 -0.11401 0.00213  0.13288  131 LEU A CD2 
1631 N N   . ILE A 253 ? 0.77723 1.09143 0.81039 -0.11871 0.01808  0.12218  132 ILE A N   
1632 C CA  . ILE A 253 ? 0.83751 1.13241 0.85603 -0.12037 0.01631  0.10706  132 ILE A CA  
1633 C C   . ILE A 253 ? 0.87795 1.15215 0.90708 -0.12392 0.00563  0.11281  132 ILE A C   
1634 O O   . ILE A 253 ? 0.72740 1.01131 0.76619 -0.12902 -0.00157 0.12782  132 ILE A O   
1635 C CB  . ILE A 253 ? 0.78514 1.09915 0.78637 -0.12542 0.01759  0.10326  132 ILE A CB  
1636 C CG1 . ILE A 253 ? 0.90608 1.23986 0.89333 -0.12190 0.02946  0.09633  132 ILE A CG1 
1637 C CG2 . ILE A 253 ? 0.72282 1.01780 0.71343 -0.12810 0.01533  0.08705  132 ILE A CG2 
1638 C CD1 . ILE A 253 ? 0.92006 1.27576 0.88731 -0.12739 0.02951  0.09412  132 ILE A CD1 
1639 N N   . ALA A 254 ? 0.81236 1.05710 0.83916 -0.12082 0.00557  0.10123  133 ALA A N   
1640 C CA  . ALA A 254 ? 0.75019 0.97189 0.78357 -0.12332 -0.00212 0.10361  133 ALA A CA  
1641 C C   . ALA A 254 ? 0.81934 1.02391 0.84095 -0.12494 0.00036  0.08844  133 ALA A C   
1642 O O   . ALA A 254 ? 0.82568 1.02029 0.83557 -0.12156 0.00802  0.07362  133 ALA A O   
1643 C CB  . ALA A 254 ? 0.69178 0.89203 0.73279 -0.11852 -0.00469 0.10519  133 ALA A CB  
1644 N N   . SER A 255 ? 0.68728 0.88818 0.71421 -0.13006 -0.00558 0.09239  134 SER A N   
1645 C CA  . SER A 255 ? 0.89890 1.08608 0.91960 -0.13277 -0.00353 0.07942  134 SER A CA  
1646 C C   . SER A 255 ? 0.85289 1.02882 0.88580 -0.13571 -0.00981 0.08679  134 SER A C   
1647 O O   . SER A 255 ? 0.83960 1.01777 0.88408 -0.13578 -0.01580 0.10107  134 SER A O   
1648 C CB  . SER A 255 ? 0.96963 1.18004 0.98145 -0.13724 -0.00221 0.07252  134 SER A CB  
1649 O OG  . SER A 255 ? 0.91954 1.15005 0.93978 -0.14232 -0.01050 0.08439  134 SER A OG  
1650 N N   . GLY A 256 ? 0.71981 0.88317 0.75149 -0.13828 -0.00754 0.07652  135 GLY A N   
1651 C CA  . GLY A 256 ? 0.80532 0.95313 0.84837 -0.13957 -0.01040 0.08074  135 GLY A CA  
1652 C C   . GLY A 256 ? 0.95980 1.07286 0.99750 -0.13526 -0.00565 0.07524  135 GLY A C   
1653 O O   . GLY A 256 ? 1.06645 1.16802 1.09307 -0.13081 -0.00163 0.06989  135 GLY A O   
1654 N N   . ASP A 257 ? 0.87253 0.96849 0.91783 -0.13596 -0.00595 0.07702  136 ASP A N   
1655 C CA  . ASP A 257 ? 1.00379 1.06520 1.04087 -0.13222 -0.00097 0.07170  136 ASP A CA  
1656 C C   . ASP A 257 ? 0.95288 1.00335 0.99665 -0.13067 -0.00690 0.08240  136 ASP A C   
1657 O O   . ASP A 257 ? 0.92018 0.94640 0.96308 -0.12969 -0.00393 0.08031  136 ASP A O   
1658 C CB  . ASP A 257 ? 1.02619 1.07172 1.06304 -0.13440 0.00721  0.06126  136 ASP A CB  
1659 C CG  . ASP A 257 ? 1.03716 1.08956 1.06736 -0.13701 0.01324  0.04875  136 ASP A CG  
1660 O OD1 . ASP A 257 ? 0.92930 0.97842 0.94655 -0.13375 0.01585  0.04390  136 ASP A OD1 
1661 O OD2 . ASP A 257 ? 1.02891 1.09011 1.06822 -0.14235 0.01523  0.04342  136 ASP A OD2 
1662 N N   . VAL A 258 ? 1.03441 1.10222 1.08486 -0.13082 -0.01460 0.09358  137 VAL A N   
1663 C CA  . VAL A 258 ? 0.99082 1.05255 1.05159 -0.13122 -0.02141 0.10459  137 VAL A CA  
1664 C C   . VAL A 258 ? 0.85427 0.91124 0.90989 -0.12875 -0.02588 0.10753  137 VAL A C   
1665 O O   . VAL A 258 ? 0.87310 0.94961 0.92788 -0.12799 -0.02651 0.10930  137 VAL A O   
1666 C CB  . VAL A 258 ? 0.99481 1.08317 1.07378 -0.13500 -0.02726 0.11796  137 VAL A CB  
1667 C CG1 . VAL A 258 ? 0.86368 0.98352 0.94225 -0.13633 -0.02921 0.12310  137 VAL A CG1 
1668 C CG2 . VAL A 258 ? 0.96511 1.04377 1.05607 -0.13572 -0.03349 0.12901  137 VAL A CG2 
1669 N N   . TYR A 259 ? 0.77004 0.80144 0.82220 -0.12741 -0.02882 0.10732  138 TYR A N   
1670 C CA  . TYR A 259 ? 0.80006 0.82692 0.85006 -0.12592 -0.03561 0.11047  138 TYR A CA  
1671 C C   . TYR A 259 ? 0.87050 0.91075 0.93990 -0.13065 -0.04390 0.12382  138 TYR A C   
1672 O O   . TYR A 259 ? 0.91106 0.94003 0.98815 -0.13309 -0.04549 0.12725  138 TYR A O   
1673 C CB  . TYR A 259 ? 0.75221 0.74398 0.78553 -0.12260 -0.03582 0.10266  138 TYR A CB  
1674 C CG  . TYR A 259 ? 0.84784 0.83524 0.88167 -0.12232 -0.04606 0.10662  138 TYR A CG  
1675 C CD1 . TYR A 259 ? 0.92194 0.92540 0.95701 -0.11959 -0.04923 0.10838  138 TYR A CD1 
1676 C CD2 . TYR A 259 ? 1.01042 0.97836 1.04504 -0.12493 -0.05267 0.10806  138 TYR A CD2 
1677 C CE1 . TYR A 259 ? 1.04666 1.04929 1.08588 -0.11975 -0.05973 0.11224  138 TYR A CE1 
1678 C CE2 . TYR A 259 ? 1.01423 0.97935 1.05052 -0.12597 -0.06368 0.11074  138 TYR A CE2 
1679 C CZ  . TYR A 259 ? 1.02764 1.01140 1.06735 -0.12353 -0.06769 0.11323  138 TYR A CZ  
1680 O OH  . TYR A 259 ? 1.19172 1.17568 1.23663 -0.12494 -0.07968 0.11613  138 TYR A OH  
1681 N N   . ILE A 260 ? 0.76218 0.82617 0.84078 -0.13182 -0.04793 0.13160  139 ILE A N   
1682 C CA  . ILE A 260 ? 0.86596 0.94630 0.96481 -0.13712 -0.05438 0.14597  139 ILE A CA  
1683 C C   . ILE A 260 ? 0.88690 0.95780 0.99051 -0.13844 -0.06281 0.14790  139 ILE A C   
1684 O O   . ILE A 260 ? 0.97300 1.04297 1.06870 -0.13466 -0.06399 0.14235  139 ILE A O   
1685 C CB  . ILE A 260 ? 0.84172 0.95829 0.94889 -0.13851 -0.05174 0.15474  139 ILE A CB  
1686 C CG1 . ILE A 260 ? 0.83037 0.95668 0.93237 -0.13823 -0.04585 0.15232  139 ILE A CG1 
1687 C CG2 . ILE A 260 ? 0.65111 0.78359 0.77915 -0.14420 -0.05720 0.17135  139 ILE A CG2 
1688 C CD1 . ILE A 260 ? 0.76805 0.88685 0.88029 -0.14091 -0.04808 0.15863  139 ILE A CD1 
1689 N N   . ARG A 261 ? 1.06976 1.13368 1.18759 -0.14382 -0.06917 0.15578  140 ARG A N   
1690 C CA  . ARG A 261 ? 0.96399 1.01563 1.08736 -0.14694 -0.07883 0.15625  140 ARG A CA  
1691 C C   . ARG A 261 ? 0.96899 1.03498 1.11819 -0.15470 -0.08379 0.17125  140 ARG A C   
1692 O O   . ARG A 261 ? 0.95673 1.03282 1.11589 -0.15669 -0.07994 0.18059  140 ARG A O   
1693 C CB  . ARG A 261 ? 0.97714 0.99057 1.08499 -0.14583 -0.08115 0.14534  140 ARG A CB  
1694 C CG  . ARG A 261 ? 1.04282 1.04048 1.14361 -0.14638 -0.09119 0.13950  140 ARG A CG  
1695 C CD  . ARG A 261 ? 1.09794 1.05707 1.17601 -0.14408 -0.09107 0.12730  140 ARG A CD  
1696 N NE  . ARG A 261 ? 1.25948 1.20181 1.33273 -0.14708 -0.10346 0.12305  140 ARG A NE  
1697 C CZ  . ARG A 261 ? 1.29976 1.23012 1.38442 -0.15438 -0.11086 0.12487  140 ARG A CZ  
1698 N NH1 . ARG A 261 ? 1.19329 1.12601 1.29573 -0.15834 -0.10626 0.13230  140 ARG A NH1 
1699 N NH2 . ARG A 261 ? 1.41854 1.33420 1.49710 -0.15772 -0.12340 0.11928  140 ARG A NH2 
1700 N N   . SER A 262 ? 0.94859 1.01556 1.10960 -0.15926 -0.09277 0.17414  141 SER A N   
1701 C CA  . SER A 262 ? 1.03899 1.11057 1.22495 -0.16810 -0.09816 0.18685  141 SER A CA  
1702 C C   . SER A 262 ? 1.04639 1.11393 1.24244 -0.17334 -0.10962 0.18517  141 SER A C   
1703 O O   . SER A 262 ? 0.98511 1.06829 1.18100 -0.17076 -0.11205 0.18295  141 SER A O   
1704 C CB  . SER A 262 ? 0.99034 1.09719 1.19432 -0.17067 -0.09263 0.20337  141 SER A CB  
1705 O OG  . SER A 262 ? 0.84421 0.97652 1.05867 -0.17171 -0.09396 0.20744  141 SER A OG  
1706 N N   . GLU A 263 ? 1.12763 1.17438 1.33378 -0.18067 -0.11689 0.18599  142 GLU A N   
1707 C CA  . GLU A 263 ? 1.38168 1.42083 1.59709 -0.18731 -0.12990 0.18244  142 GLU A CA  
1708 C C   . GLU A 263 ? 1.34270 1.40432 1.59310 -0.19777 -0.13363 0.19797  142 GLU A C   
1709 O O   . GLU A 263 ? 1.37191 1.42756 1.63604 -0.20588 -0.14527 0.19617  142 GLU A O   
1710 C CB  . GLU A 263 ? 1.48350 1.48136 1.68440 -0.18938 -0.13597 0.17009  142 GLU A CB  
1711 C CG  . GLU A 263 ? 1.53806 1.51264 1.70344 -0.17954 -0.13211 0.15462  142 GLU A CG  
1712 C CD  . GLU A 263 ? 1.58289 1.51620 1.73123 -0.18105 -0.13585 0.14214  142 GLU A CD  
1713 O OE1 . GLU A 263 ? 1.62537 1.54437 1.78264 -0.18408 -0.13147 0.14518  142 GLU A OE1 
1714 O OE2 . GLU A 263 ? 1.55790 1.47256 1.68297 -0.17860 -0.14279 0.12945  142 GLU A OE2 
1715 N N   . LYS A 264 ? 1.19489 1.28238 1.45958 -0.19823 -0.12411 0.21327  143 LYS A N   
1716 C CA  . LYS A 264 ? 1.05526 1.16622 1.35249 -0.20774 -0.12465 0.23043  143 LYS A CA  
1717 C C   . LYS A 264 ? 1.11525 1.26649 1.41937 -0.20428 -0.11728 0.23894  143 LYS A C   
1718 O O   . LYS A 264 ? 0.91687 1.07692 1.20036 -0.19458 -0.10939 0.23399  143 LYS A O   
1719 C CB  . LYS A 264 ? 0.97894 1.08431 1.28802 -0.21189 -0.11895 0.24441  143 LYS A CB  
1720 C CG  . LYS A 264 ? 1.08242 1.14821 1.39071 -0.21591 -0.12467 0.23782  143 LYS A CG  
1721 C CD  . LYS A 264 ? 1.19746 1.26008 1.52043 -0.21841 -0.11829 0.25399  143 LYS A CD  
1722 C CE  . LYS A 264 ? 1.26412 1.28541 1.58326 -0.21919 -0.12101 0.24575  143 LYS A CE  
1723 N NZ  . LYS A 264 ? 1.31394 1.33233 1.64753 -0.21913 -0.11429 0.26231  143 LYS A NZ  
1724 N N   . PRO A 265 ? 1.21410 1.38981 1.54762 -0.21229 -0.11890 0.25109  144 PRO A N   
1725 C CA  . PRO A 265 ? 1.20219 1.41683 1.54339 -0.20865 -0.11018 0.25897  144 PRO A CA  
1726 C C   . PRO A 265 ? 1.07845 1.31036 1.41234 -0.20519 -0.09630 0.27111  144 PRO A C   
1727 O O   . PRO A 265 ? 1.12779 1.34866 1.46256 -0.20848 -0.09426 0.28008  144 PRO A O   
1728 C CB  . PRO A 265 ? 1.14857 1.38219 1.52736 -0.22011 -0.11502 0.27051  144 PRO A CB  
1729 C CG  . PRO A 265 ? 1.22010 1.42326 1.60406 -0.22738 -0.13069 0.26037  144 PRO A CG  
1730 C CD  . PRO A 265 ? 1.22322 1.39072 1.58365 -0.22479 -0.13013 0.25410  144 PRO A CD  
1731 N N   . LEU A 266 ? 1.04152 1.30088 1.36768 -0.19800 -0.08701 0.27109  145 LEU A N   
1732 C CA  . LEU A 266 ? 0.96005 1.23863 1.27456 -0.19410 -0.07432 0.28029  145 LEU A CA  
1733 C C   . LEU A 266 ? 0.96195 1.26668 1.30116 -0.20227 -0.06786 0.30262  145 LEU A C   
1734 O O   . LEU A 266 ? 0.96835 1.28677 1.33519 -0.20917 -0.06982 0.30954  145 LEU A O   
1735 C CB  . LEU A 266 ? 0.87739 1.17367 1.17317 -0.18368 -0.06609 0.27016  145 LEU A CB  
1736 C CG  . LEU A 266 ? 0.82837 1.10155 1.09917 -0.17477 -0.06999 0.24914  145 LEU A CG  
1737 C CD1 . LEU A 266 ? 0.87949 1.17239 1.13917 -0.16547 -0.06117 0.24128  145 LEU A CD1 
1738 C CD2 . LEU A 266 ? 0.54298 0.79331 0.79133 -0.17233 -0.06959 0.24375  145 LEU A CD2 
1739 N N   . GLN A 267 ? 0.92980 1.24237 1.25922 -0.20155 -0.06014 0.31455  146 GLN A N   
1740 C CA  . GLN A 267 ? 0.89122 1.23099 1.23734 -0.20754 -0.05128 0.33704  146 GLN A CA  
1741 C C   . GLN A 267 ? 0.96538 1.33975 1.30437 -0.20200 -0.03901 0.33713  146 GLN A C   
1742 O O   . GLN A 267 ? 0.99111 1.36655 1.30883 -0.19274 -0.03692 0.32028  146 GLN A O   
1743 C CB  . GLN A 267 ? 0.87706 1.21257 1.21338 -0.20801 -0.04850 0.35121  146 GLN A CB  
1744 C CG  . GLN A 267 ? 0.98765 1.33436 1.29144 -0.19856 -0.04197 0.34599  146 GLN A CG  
1745 C CD  . GLN A 267 ? 0.92269 1.24274 1.20526 -0.19169 -0.04878 0.32571  146 GLN A CD  
1746 O OE1 . GLN A 267 ? 0.98054 1.29091 1.25608 -0.18754 -0.05157 0.30696  146 GLN A OE1 
1747 N NE2 . GLN A 267 ? 0.83103 1.13948 1.10446 -0.19017 -0.05115 0.33037  146 GLN A NE2 
1748 N N   . SER A 268 ? 1.01126 1.41306 1.36881 -0.20777 -0.02975 0.35634  147 SER A N   
1749 C CA  . SER A 268 ? 1.02156 1.45710 1.37186 -0.20242 -0.01556 0.35775  147 SER A CA  
1750 C C   . SER A 268 ? 0.97514 1.41482 1.28740 -0.19396 -0.00892 0.35296  147 SER A C   
1751 O O   . SER A 268 ? 1.00557 1.43079 1.30356 -0.19437 -0.01332 0.35737  147 SER A O   
1752 C CB  . SER A 268 ? 1.02201 1.48533 1.39787 -0.21081 -0.00509 0.38155  147 SER A CB  
1753 O OG  . SER A 268 ? 0.98000 1.47575 1.35412 -0.20559 0.00923  0.38074  147 SER A OG  
1754 N N   . ILE A 269 ? 0.93610 1.39609 1.23319 -0.18618 0.00155  0.34340  148 ILE A N   
1755 C CA  . ILE A 269 ? 1.03096 1.49263 1.29085 -0.17792 0.00640  0.33228  148 ILE A CA  
1756 C C   . ILE A 269 ? 1.15924 1.65311 1.40781 -0.17795 0.02153  0.34660  148 ILE A C   
1757 O O   . ILE A 269 ? 1.02587 1.54400 1.28301 -0.17617 0.03374  0.34805  148 ILE A O   
1758 C CB  . ILE A 269 ? 0.96688 1.42201 1.21386 -0.16846 0.00698  0.30768  148 ILE A CB  
1759 C CG1 . ILE A 269 ? 1.00951 1.43092 1.26209 -0.16825 -0.00795 0.29456  148 ILE A CG1 
1760 C CG2 . ILE A 269 ? 0.86477 1.32355 1.07495 -0.16136 0.01340  0.29595  148 ILE A CG2 
1761 C CD1 . ILE A 269 ? 0.96918 1.37944 1.20699 -0.15870 -0.00821 0.27176  148 ILE A CD1 
1762 N N   . PRO A 270 ? 1.34504 1.84091 1.57477 -0.17961 0.02141  0.35810  149 PRO A N   
1763 C CA  . PRO A 270 ? 1.46242 1.98830 1.67589 -0.17955 0.03530  0.37232  149 PRO A CA  
1764 C C   . PRO A 270 ? 1.42289 1.96548 1.61103 -0.17108 0.04721  0.35480  149 PRO A C   
1765 O O   . PRO A 270 ? 1.49223 2.02180 1.67274 -0.16469 0.04426  0.33164  149 PRO A O   
1766 C CB  . PRO A 270 ? 1.47951 1.99815 1.67254 -0.18074 0.02799  0.38222  149 PRO A CB  
1767 C CG  . PRO A 270 ? 1.43301 1.92134 1.64769 -0.18483 0.01304  0.38383  149 PRO A CG  
1768 C CD  . PRO A 270 ? 1.38316 1.85421 1.60961 -0.18213 0.00817  0.36164  149 PRO A CD  
1769 N N   . GLU A 271 ? 1.20912 1.77989 1.38265 -0.17095 0.06174  0.36651  150 GLU A N   
1770 C CA  . GLU A 271 ? 1.13111 1.72053 1.28144 -0.16335 0.07644  0.35186  150 GLU A CA  
1771 C C   . GLU A 271 ? 1.16896 1.76359 1.27486 -0.16046 0.07734  0.34660  150 GLU A C   
1772 O O   . GLU A 271 ? 1.15403 1.77210 1.23655 -0.15791 0.09197  0.34790  150 GLU A O   
1773 C CB  . GLU A 271 ? 1.22526 1.84473 1.39172 -0.16479 0.09486  0.36658  150 GLU A CB  
1774 C CG  . GLU A 271 ? 1.24077 1.85958 1.45470 -0.16864 0.09348  0.37224  150 GLU A CG  
1775 C CD  . GLU A 271 ? 1.28198 1.93051 1.51148 -0.16561 0.11317  0.37455  150 GLU A CD  
1776 O OE1 . GLU A 271 ? 1.26292 1.92673 1.46396 -0.15808 0.12769  0.36458  150 GLU A OE1 
1777 O OE2 . GLU A 271 ? 1.34938 2.00623 1.62046 -0.17086 0.11433  0.38565  150 GLU A OE2 
1778 N N   . ALA A 272 ? 1.16695 1.74036 1.26101 -0.16099 0.06161  0.34015  151 ALA A N   
1779 C CA  . ALA A 272 ? 1.21696 1.79456 1.27173 -0.15884 0.05902  0.33291  151 ALA A CA  
1780 C C   . ALA A 272 ? 1.12760 1.70041 1.16069 -0.15177 0.06355  0.30252  151 ALA A C   
1781 O O   . ALA A 272 ? 1.08313 1.64773 1.13199 -0.14761 0.06810  0.28846  151 ALA A O   
1782 C CB  . ALA A 272 ? 1.24548 1.80398 1.30120 -0.16195 0.04078  0.33817  151 ALA A CB  
1783 N N   . ASP A 273 ? 1.14320 1.72095 1.14003 -0.15047 0.06178  0.29237  152 ASP A N   
1784 C CA  . ASP A 273 ? 1.12899 1.69844 1.10458 -0.14494 0.06484  0.26251  152 ASP A CA  
1785 C C   . ASP A 273 ? 1.15499 1.69460 1.13841 -0.14463 0.05008  0.24656  152 ASP A C   
1786 O O   . ASP A 273 ? 1.11255 1.63837 1.09051 -0.13991 0.05306  0.22276  152 ASP A O   
1787 C CB  . ASP A 273 ? 1.24479 1.83180 1.17757 -0.14486 0.06869  0.25608  152 ASP A CB  
1788 C CG  . ASP A 273 ? 1.31127 1.92762 1.23057 -0.14459 0.08547  0.27069  152 ASP A CG  
1789 O OD1 . ASP A 273 ? 1.37004 1.99331 1.30237 -0.14054 0.10117  0.26781  152 ASP A OD1 
1790 O OD2 . ASP A 273 ? 1.35704 1.99019 1.25297 -0.14808 0.08321  0.28574  152 ASP A OD2 
1791 N N   . VAL A 274 ? 0.95601 1.48468 0.95239 -0.14916 0.03545  0.25956  153 VAL A N   
1792 C CA  . VAL A 274 ? 0.87413 1.37471 0.87981 -0.14912 0.02251  0.24687  153 VAL A CA  
1793 C C   . VAL A 274 ? 0.92690 1.41403 0.96525 -0.15249 0.01404  0.26491  153 VAL A C   
1794 O O   . VAL A 274 ? 1.06384 1.56076 1.10827 -0.15660 0.01009  0.28767  153 VAL A O   
1795 C CB  . VAL A 274 ? 0.96222 1.46295 0.94552 -0.15104 0.01226  0.24030  153 VAL A CB  
1796 C CG1 . VAL A 274 ? 0.89436 1.36655 0.89071 -0.15105 0.00097  0.22832  153 VAL A CG1 
1797 C CG2 . VAL A 274 ? 0.84017 1.35364 0.78950 -0.14904 0.01991  0.22092  153 VAL A CG2 
1798 N N   . VAL A 275 ? 0.85947 1.32336 0.91770 -0.15073 0.01132  0.25499  154 VAL A N   
1799 C CA  . VAL A 275 ? 0.87893 1.32469 0.96561 -0.15411 0.00205  0.26697  154 VAL A CA  
1800 C C   . VAL A 275 ? 1.03325 1.45029 1.11928 -0.15270 -0.00790 0.25133  154 VAL A C   
1801 O O   . VAL A 275 ? 0.92494 1.33041 1.00051 -0.14848 -0.00537 0.23006  154 VAL A O   
1802 C CB  . VAL A 275 ? 0.89964 1.34377 1.01129 -0.15404 0.00675  0.27025  154 VAL A CB  
1803 C CG1 . VAL A 275 ? 0.90924 1.33431 1.04851 -0.15891 -0.00356 0.28207  154 VAL A CG1 
1804 C CG2 . VAL A 275 ? 1.04918 1.52403 1.16222 -0.15502 0.01948  0.28414  154 VAL A CG2 
1805 N N   . CYS A 276 ? 0.88028 1.28530 0.97783 -0.15588 -0.01800 0.26217  155 CYS A N   
1806 C CA  . CYS A 276 ? 0.89211 1.27139 0.98978 -0.15458 -0.02604 0.24888  155 CYS A CA  
1807 C C   . CYS A 276 ? 0.82300 1.17974 0.94574 -0.15694 -0.03311 0.25800  155 CYS A C   
1808 O O   . CYS A 276 ? 0.78060 1.14315 0.91767 -0.16066 -0.03601 0.27868  155 CYS A O   
1809 C CB  . CYS A 276 ? 0.94430 1.33203 1.02812 -0.15519 -0.03156 0.24976  155 CYS A CB  
1810 S SG  . CYS A 276 ? 1.02172 1.43524 1.07252 -0.15390 -0.02530 0.23725  155 CYS A SG  
1811 N N   . TYR A 277 ? 0.75892 1.08858 0.88557 -0.15483 -0.03564 0.24267  156 TYR A N   
1812 C CA  . TYR A 277 ? 0.71660 1.02213 0.86332 -0.15709 -0.04249 0.24845  156 TYR A CA  
1813 C C   . TYR A 277 ? 0.84199 1.13264 0.98895 -0.15654 -0.04840 0.24739  156 TYR A C   
1814 O O   . TYR A 277 ? 0.82114 1.11206 0.95344 -0.15393 -0.04776 0.23490  156 TYR A O   
1815 C CB  . TYR A 277 ? 0.69392 0.97752 0.84382 -0.15509 -0.04276 0.23408  156 TYR A CB  
1816 C CG  . TYR A 277 ? 0.77913 1.07584 0.94088 -0.15661 -0.03973 0.24037  156 TYR A CG  
1817 C CD1 . TYR A 277 ? 0.87784 1.17058 1.06287 -0.16215 -0.04439 0.25426  156 TYR A CD1 
1818 C CD2 . TYR A 277 ? 0.62420 0.93757 0.77607 -0.15265 -0.03180 0.23227  156 TYR A CD2 
1819 C CE1 . TYR A 277 ? 0.75124 1.05849 0.95115 -0.16441 -0.04187 0.26039  156 TYR A CE1 
1820 C CE2 . TYR A 277 ? 0.82096 1.14886 0.98745 -0.15349 -0.02840 0.23856  156 TYR A CE2 
1821 C CZ  . TYR A 277 ? 0.86528 1.19124 1.05666 -0.15972 -0.03378 0.25289  156 TYR A CZ  
1822 O OH  . TYR A 277 ? 0.97417 1.31678 1.18395 -0.16136 -0.03069 0.25929  156 TYR A OH  
1823 N N   . GLY A 278 ? 0.75157 1.02922 0.91746 -0.15917 -0.05377 0.26050  157 GLY A N   
1824 C CA  . GLY A 278 ? 0.89313 1.15714 1.06385 -0.15776 -0.05857 0.26146  157 GLY A CA  
1825 C C   . GLY A 278 ? 0.82773 1.06468 1.01848 -0.15956 -0.06274 0.26724  157 GLY A C   
1826 O O   . GLY A 278 ? 0.96486 1.19541 1.16656 -0.16322 -0.06331 0.27211  157 GLY A O   
1827 N N   . LEU A 279 ? 0.85283 1.07399 1.04929 -0.15708 -0.06552 0.26581  158 LEU A N   
1828 C CA  . LEU A 279 ? 0.90778 1.10129 1.12257 -0.15800 -0.06862 0.27064  158 LEU A CA  
1829 C C   . LEU A 279 ? 0.85070 1.04951 1.08003 -0.15633 -0.07158 0.28772  158 LEU A C   
1830 O O   . LEU A 279 ? 0.88729 1.09657 1.11173 -0.15240 -0.07213 0.28523  158 LEU A O   
1831 C CB  . LEU A 279 ? 0.81719 0.97955 1.02553 -0.15504 -0.06739 0.25002  158 LEU A CB  
1832 C CG  . LEU A 279 ? 0.84931 1.00277 1.04354 -0.15568 -0.06565 0.23424  158 LEU A CG  
1833 C CD1 . LEU A 279 ? 0.83662 0.95940 1.02069 -0.15222 -0.06375 0.21537  158 LEU A CD1 
1834 C CD2 . LEU A 279 ? 0.94188 1.09178 1.14813 -0.16101 -0.06906 0.24236  158 LEU A CD2 
1835 N N   . TRP A 280 ? 0.75699 0.94915 1.00564 -0.15937 -0.07383 0.30548  159 TRP A N   
1836 C CA  . TRP A 280 ? 0.77564 0.96816 1.04093 -0.15660 -0.07668 0.32298  159 TRP A CA  
1837 C C   . TRP A 280 ? 0.96516 1.13790 1.23394 -0.15054 -0.07656 0.31055  159 TRP A C   
1838 O O   . TRP A 280 ? 0.87838 1.02092 1.14765 -0.15022 -0.07443 0.29529  159 TRP A O   
1839 C CB  . TRP A 280 ? 0.83879 1.01568 1.12619 -0.16094 -0.07794 0.33981  159 TRP A CB  
1840 C CG  . TRP A 280 ? 1.08102 1.27740 1.36954 -0.16766 -0.07679 0.35385  159 TRP A CG  
1841 C CD1 . TRP A 280 ? 0.97435 1.16211 1.26740 -0.17436 -0.07586 0.34955  159 TRP A CD1 
1842 C CD2 . TRP A 280 ? 1.01382 1.24280 1.29940 -0.16839 -0.07606 0.37489  159 TRP A CD2 
1843 N NE1 . TRP A 280 ? 1.09439 1.30796 1.39032 -0.17929 -0.07338 0.36671  159 TRP A NE1 
1844 C CE2 . TRP A 280 ? 1.11848 1.35675 1.40794 -0.17562 -0.07281 0.38252  159 TRP A CE2 
1845 C CE3 . TRP A 280 ? 1.03475 1.28686 1.31430 -0.16366 -0.07816 0.38818  159 TRP A CE3 
1846 C CZ2 . TRP A 280 ? 1.12541 1.39394 1.41162 -0.17808 -0.06956 0.40307  159 TRP A CZ2 
1847 C CZ3 . TRP A 280 ? 1.06140 1.34300 1.33485 -0.16605 -0.07653 0.40841  159 TRP A CZ3 
1848 C CH2 . TRP A 280 ? 0.98143 1.27038 1.25756 -0.17310 -0.07127 0.41574  159 TRP A CH2 
1849 N N   . VAL A 281 ? 0.90500 1.09581 1.17612 -0.14574 -0.07882 0.31716  160 VAL A N   
1850 C CA  . VAL A 281 ? 1.00888 1.18721 1.28510 -0.13990 -0.07774 0.30518  160 VAL A CA  
1851 C C   . VAL A 281 ? 0.96645 1.15395 1.26386 -0.13452 -0.08201 0.32398  160 VAL A C   
1852 O O   . VAL A 281 ? 0.73325 0.95044 1.03006 -0.13435 -0.08719 0.34138  160 VAL A O   
1853 C CB  . VAL A 281 ? 0.97441 1.16763 1.23075 -0.13924 -0.07604 0.28660  160 VAL A CB  
1854 C CG1 . VAL A 281 ? 0.97015 1.14437 1.20937 -0.14202 -0.07084 0.26610  160 VAL A CG1 
1855 C CG2 . VAL A 281 ? 0.84719 1.07883 1.09116 -0.14105 -0.08004 0.29576  160 VAL A CG2 
1856 N N   . ASP A 282 ? 0.97203 1.13337 1.28768 -0.12962 -0.07957 0.32087  161 ASP A N   
1857 C CA  . ASP A 282 ? 0.84821 1.01693 1.18614 -0.12224 -0.08261 0.33387  161 ASP A CA  
1858 C C   . ASP A 282 ? 0.91257 1.10663 1.24403 -0.11958 -0.08462 0.32399  161 ASP A C   
1859 O O   . ASP A 282 ? 0.97912 1.17016 1.29293 -0.12223 -0.08035 0.30233  161 ASP A O   
1860 C CB  . ASP A 282 ? 0.83268 0.96403 1.19055 -0.11734 -0.07692 0.32867  161 ASP A CB  
1861 C CG  . ASP A 282 ? 0.98388 1.12121 1.36911 -0.10811 -0.07883 0.34152  161 ASP A CG  
1862 O OD1 . ASP A 282 ? 1.05194 1.19746 1.45364 -0.10562 -0.08401 0.36596  161 ASP A OD1 
1863 O OD2 . ASP A 282 ? 0.95210 1.08625 1.34370 -0.10308 -0.07477 0.32801  161 ASP A OD2 
1864 N N   . PRO A 283 ? 0.92007 1.13984 1.26587 -0.11472 -0.09173 0.33994  162 PRO A N   
1865 C CA  . PRO A 283 ? 0.99789 1.24357 1.34044 -0.11333 -0.09519 0.33007  162 PRO A CA  
1866 C C   . PRO A 283 ? 1.01845 1.24462 1.36562 -0.11144 -0.08693 0.30646  162 PRO A C   
1867 O O   . PRO A 283 ? 1.02982 1.27024 1.36413 -0.11446 -0.08652 0.29043  162 PRO A O   
1868 C CB  . PRO A 283 ? 1.04073 1.30909 1.40684 -0.10655 -0.10455 0.35360  162 PRO A CB  
1869 C CG  . PRO A 283 ? 0.96270 1.23232 1.32719 -0.10788 -0.10790 0.37742  162 PRO A CG  
1870 C CD  . PRO A 283 ? 1.05805 1.28952 1.41996 -0.11156 -0.09848 0.36918  162 PRO A CD  
1871 N N   . SER A 284 ? 1.01010 1.20289 1.37440 -0.10683 -0.07945 0.30362  163 SER A N   
1872 C CA  . SER A 284 ? 0.84034 1.01176 1.20731 -0.10473 -0.06938 0.28192  163 SER A CA  
1873 C C   . SER A 284 ? 0.93685 1.10107 1.27344 -0.11154 -0.06404 0.25961  163 SER A C   
1874 O O   . SER A 284 ? 1.03127 1.18972 1.36589 -0.11116 -0.05713 0.24218  163 SER A O   
1875 C CB  . SER A 284 ? 0.92724 1.05891 1.30893 -0.09987 -0.06103 0.28116  163 SER A CB  
1876 O OG  . SER A 284 ? 1.00522 1.11268 1.36910 -0.10524 -0.05927 0.27833  163 SER A OG  
1877 N N   . LEU A 285 ? 1.06659 1.23111 1.38089 -0.11750 -0.06646 0.26051  164 LEU A N   
1878 C CA  . LEU A 285 ? 1.07716 1.23993 1.36357 -0.12301 -0.06275 0.24187  164 LEU A CA  
1879 C C   . LEU A 285 ? 0.97883 1.17620 1.24921 -0.12763 -0.06966 0.24581  164 LEU A C   
1880 O O   . LEU A 285 ? 1.05024 1.25227 1.30139 -0.13106 -0.06674 0.22954  164 LEU A O   
1881 C CB  . LEU A 285 ? 1.05521 1.18728 1.32742 -0.12573 -0.05840 0.23535  164 LEU A CB  
1882 C CG  . LEU A 285 ? 1.10026 1.22515 1.34498 -0.12976 -0.05400 0.21636  164 LEU A CG  
1883 C CD1 . LEU A 285 ? 1.21027 1.29585 1.44739 -0.12896 -0.04707 0.20341  164 LEU A CD1 
1884 C CD2 . LEU A 285 ? 1.18663 1.33002 1.41645 -0.13461 -0.05891 0.22231  164 LEU A CD2 
1885 N N   . ALA A 286 ? 0.97622 1.19654 1.25285 -0.12760 -0.07794 0.26694  165 ALA A N   
1886 C CA  . ALA A 286 ? 0.90864 1.16281 1.16771 -0.13157 -0.08387 0.27058  165 ALA A CA  
1887 C C   . ALA A 286 ? 0.89787 1.17325 1.15504 -0.13197 -0.08647 0.25902  165 ALA A C   
1888 O O   . ALA A 286 ? 0.88864 1.18079 1.12415 -0.13651 -0.08716 0.24871  165 ALA A O   
1889 C CB  . ALA A 286 ? 0.77863 1.05369 1.04543 -0.13061 -0.09198 0.29743  165 ALA A CB  
1890 N N   . THR A 287 ? 0.89950 1.17427 1.18070 -0.12744 -0.08753 0.25988  166 THR A N   
1891 C CA  . THR A 287 ? 1.02416 1.32379 1.30957 -0.12854 -0.09204 0.25158  166 THR A CA  
1892 C C   . THR A 287 ? 1.00462 1.29498 1.27250 -0.13357 -0.08410 0.22543  166 THR A C   
1893 O O   . THR A 287 ? 0.90504 1.21755 1.17069 -0.13713 -0.08805 0.21616  166 THR A O   
1894 C CB  . THR A 287 ? 0.95193 1.25182 1.27189 -0.12200 -0.09344 0.25813  166 THR A CB  
1895 O OG1 . THR A 287 ? 1.01041 1.33848 1.33787 -0.12402 -0.09943 0.25081  166 THR A OG1 
1896 C CG2 . THR A 287 ? 0.78639 1.04788 1.11665 -0.11877 -0.08021 0.24604  166 THR A CG2 
1897 N N   . HIS A 288 ? 0.81645 1.07438 1.07209 -0.13413 -0.07357 0.21356  167 HIS A N   
1898 C CA  . HIS A 288 ? 0.71559 0.96002 0.95580 -0.13771 -0.06487 0.19034  167 HIS A CA  
1899 C C   . HIS A 288 ? 0.71511 0.96348 0.92535 -0.14236 -0.06396 0.18222  167 HIS A C   
1900 O O   . HIS A 288 ? 0.83147 1.06516 1.02741 -0.14466 -0.05616 0.16389  167 HIS A O   
1901 C CB  . HIS A 288 ? 0.78491 0.98989 1.02831 -0.13457 -0.05332 0.18109  167 HIS A CB  
1902 C CG  . HIS A 288 ? 0.99515 1.19266 1.26709 -0.12956 -0.05022 0.18415  167 HIS A CG  
1903 N ND1 . HIS A 288 ? 1.10120 1.29399 1.39357 -0.12398 -0.05323 0.20098  167 HIS A ND1 
1904 C CD2 . HIS A 288 ? 1.07968 1.27337 1.36487 -0.12902 -0.04320 0.17260  167 HIS A CD2 
1905 C CE1 . HIS A 288 ? 1.03683 1.22338 1.35373 -0.11932 -0.04807 0.19928  167 HIS A CE1 
1906 N NE2 . HIS A 288 ? 1.07894 1.26701 1.39249 -0.12248 -0.04177 0.18237  167 HIS A NE2 
1907 N N   . HIS A 289 ? 0.75168 1.01879 0.95254 -0.14335 -0.07057 0.19571  168 HIS A N   
1908 C CA  . HIS A 289 ? 0.86281 1.13148 1.03761 -0.14650 -0.06759 0.18864  168 HIS A CA  
1909 C C   . HIS A 289 ? 0.89172 1.19491 1.05614 -0.14876 -0.07551 0.20031  168 HIS A C   
1910 O O   . HIS A 289 ? 0.84316 1.16847 1.01914 -0.14793 -0.08442 0.21473  168 HIS A O   
1911 C CB  . HIS A 289 ? 0.95264 1.19588 1.12370 -0.14481 -0.06266 0.19202  168 HIS A CB  
1912 C CG  . HIS A 289 ? 0.92508 1.13306 1.10235 -0.14230 -0.05551 0.18184  168 HIS A CG  
1913 N ND1 . HIS A 289 ? 0.99641 1.18967 1.19467 -0.13882 -0.05570 0.18967  168 HIS A ND1 
1914 C CD2 . HIS A 289 ? 0.94662 1.13034 1.11021 -0.14229 -0.04745 0.16469  168 HIS A CD2 
1915 C CE1 . HIS A 289 ? 1.10790 1.26953 1.30328 -0.13718 -0.04765 0.17687  168 HIS A CE1 
1916 N NE2 . HIS A 289 ? 1.08760 1.24308 1.26159 -0.13926 -0.04299 0.16234  168 HIS A NE2 
1917 N N   . GLY A 290 ? 0.85327 1.16093 0.99502 -0.15106 -0.07177 0.19415  169 GLY A N   
1918 C CA  . GLY A 290 ? 0.91490 1.25105 1.04402 -0.15259 -0.07644 0.20708  169 GLY A CA  
1919 C C   . GLY A 290 ? 1.02100 1.35526 1.16144 -0.15056 -0.07825 0.23023  169 GLY A C   
1920 O O   . GLY A 290 ? 1.19105 1.50078 1.33878 -0.14935 -0.07335 0.23093  169 GLY A O   
1921 N N   . VAL A 291 ? 1.03895 1.39915 1.18055 -0.15059 -0.08582 0.24959  170 VAL A N   
1922 C CA  . VAL A 291 ? 1.04374 1.40338 1.19944 -0.14893 -0.08825 0.27455  170 VAL A CA  
1923 C C   . VAL A 291 ? 1.03643 1.42249 1.17400 -0.15116 -0.08844 0.28815  170 VAL A C   
1924 O O   . VAL A 291 ? 1.09730 1.51040 1.21752 -0.15240 -0.09300 0.28757  170 VAL A O   
1925 C CB  . VAL A 291 ? 0.91692 1.28053 1.09581 -0.14528 -0.09694 0.28988  170 VAL A CB  
1926 C CG1 . VAL A 291 ? 0.90392 1.26538 1.09717 -0.14362 -0.09884 0.31678  170 VAL A CG1 
1927 C CG2 . VAL A 291 ? 0.77029 1.10787 0.96775 -0.14264 -0.09445 0.27612  170 VAL A CG2 
1928 N N   . PHE A 292 ? 1.02193 1.40045 1.16332 -0.15210 -0.08328 0.29991  171 PHE A N   
1929 C CA  . PHE A 292 ? 1.08300 1.48497 1.21428 -0.15384 -0.08256 0.31981  171 PHE A CA  
1930 C C   . PHE A 292 ? 1.12204 1.52580 1.27323 -0.15194 -0.08939 0.34721  171 PHE A C   
1931 O O   . PHE A 292 ? 1.11040 1.48945 1.28538 -0.15107 -0.08873 0.35376  171 PHE A O   
1932 C CB  . PHE A 292 ? 0.95551 1.34988 1.08526 -0.15635 -0.07285 0.31956  171 PHE A CB  
1933 C CG  . PHE A 292 ? 0.98905 1.37338 1.10629 -0.15655 -0.06589 0.29320  171 PHE A CG  
1934 C CD1 . PHE A 292 ? 0.91885 1.32055 1.01083 -0.15672 -0.06327 0.27797  171 PHE A CD1 
1935 C CD2 . PHE A 292 ? 1.04031 1.39688 1.17039 -0.15645 -0.06219 0.28386  171 PHE A CD2 
1936 C CE1 . PHE A 292 ? 0.96174 1.35193 1.04365 -0.15613 -0.05620 0.25473  171 PHE A CE1 
1937 C CE2 . PHE A 292 ? 0.96357 1.31040 1.08225 -0.15562 -0.05622 0.26165  171 PHE A CE2 
1938 C CZ  . PHE A 292 ? 0.92221 1.28531 1.01782 -0.15515 -0.05274 0.24756  171 PHE A CZ  
1939 N N   . ALA A 293 ? 1.19336 1.62506 1.33419 -0.15108 -0.09613 0.36298  172 ALA A N   
1940 C CA  . ALA A 293 ? 1.21671 1.65312 1.37383 -0.14856 -0.10240 0.39253  172 ALA A CA  
1941 C C   . ALA A 293 ? 1.27087 1.72332 1.41593 -0.15148 -0.09714 0.41376  172 ALA A C   
1942 O O   . ALA A 293 ? 1.27117 1.74892 1.38738 -0.15337 -0.09496 0.41133  172 ALA A O   
1943 C CB  . ALA A 293 ? 1.22645 1.68414 1.38179 -0.14480 -0.11499 0.39868  172 ALA A CB  
1944 N N   . SER A 294 ? 1.23602 1.67291 1.40333 -0.15215 -0.09426 0.43402  173 SER A N   
1945 C CA  . SER A 294 ? 1.31209 1.76152 1.47413 -0.15556 -0.08798 0.45733  173 SER A CA  
1946 C C   . SER A 294 ? 1.44022 1.88724 1.62159 -0.15299 -0.09349 0.48950  173 SER A C   
1947 O O   . SER A 294 ? 1.35160 1.77550 1.55991 -0.14970 -0.09831 0.49216  173 SER A O   
1948 C CB  . SER A 294 ? 1.42397 1.85606 1.59660 -0.16086 -0.07694 0.45068  173 SER A CB  
1949 O OG  . SER A 294 ? 1.47919 1.87792 1.68185 -0.16088 -0.07846 0.44812  173 SER A OG  
1950 N N   . ASP A 295 ? 1.70210 2.17226 1.86886 -0.15410 -0.09170 0.51434  174 ASP A N   
1951 C CA  . ASP A 295 ? 1.92377 2.39361 2.10580 -0.15125 -0.09645 0.54831  174 ASP A CA  
1952 C C   . ASP A 295 ? 1.98542 2.42146 2.20394 -0.15357 -0.09156 0.55721  174 ASP A C   
1953 O O   . ASP A 295 ? 2.06867 2.48886 2.29555 -0.15960 -0.08298 0.54409  174 ASP A O   
1954 C CB  . ASP A 295 ? 2.02771 2.52488 2.18666 -0.15184 -0.09180 0.56591  174 ASP A CB  
1955 C CG  . ASP A 295 ? 2.09859 2.59057 2.27715 -0.14698 -0.09385 0.59068  174 ASP A CG  
1956 O OD1 . ASP A 295 ? 2.08898 2.56922 2.28859 -0.14114 -0.10365 0.59869  174 ASP A OD1 
1957 O OD2 . ASP A 295 ? 2.14714 2.64637 2.32085 -0.14867 -0.08494 0.60242  174 ASP A OD2 
1958 N N   . ARG A 296 ? 1.97048 2.39491 2.21240 -0.14742 -0.09746 0.57399  175 ARG A N   
1959 C CA  . ARG A 296 ? 1.95648 2.34602 2.23386 -0.14799 -0.09371 0.57702  175 ARG A CA  
1960 C C   . ARG A 296 ? 2.13034 2.51707 2.41203 -0.15396 -0.08283 0.58138  175 ARG A C   
1961 O O   . ARG A 296 ? 2.05742 2.41776 2.35990 -0.15864 -0.07799 0.57229  175 ARG A O   
1962 C CB  . ARG A 296 ? 1.84963 2.23068 2.14901 -0.13925 -0.10103 0.59566  175 ARG A CB  
1963 C CG  . ARG A 296 ? 1.74273 2.08380 2.07769 -0.13745 -0.10061 0.59147  175 ARG A CG  
1964 C CD  . ARG A 296 ? 1.58026 1.90878 1.91993 -0.13508 -0.10596 0.57541  175 ARG A CD  
1965 N NE  . ARG A 296 ? 1.49265 1.78100 1.86419 -0.13317 -0.10382 0.56949  175 ARG A NE  
1966 C CZ  . ARG A 296 ? 1.46897 1.73864 1.85151 -0.12956 -0.10632 0.55519  175 ARG A CZ  
1967 N NH1 . ARG A 296 ? 1.47301 1.76245 1.83882 -0.12589 -0.11096 0.53632  175 ARG A NH1 
1968 N NH2 . ARG A 296 ? 1.47431 1.70599 1.88380 -0.12804 -0.10302 0.55048  175 ARG A NH2 
1969 N N   . LYS A 297 ? 2.28921 2.70289 2.55139 -0.15391 -0.07905 0.59480  176 LYS A N   
1970 C CA  . LYS A 297 ? 2.41143 2.82515 2.67848 -0.15911 -0.06805 0.60148  176 LYS A CA  
1971 C C   . LYS A 297 ? 2.30095 2.72669 2.55155 -0.16596 -0.05915 0.58468  176 LYS A C   
1972 O O   . LYS A 297 ? 2.41483 2.83783 2.67521 -0.17096 -0.04982 0.58694  176 LYS A O   
1973 C CB  . LYS A 297 ? 2.56011 2.99556 2.81419 -0.15552 -0.06632 0.62509  176 LYS A CB  
1974 C CG  . LYS A 297 ? 2.66814 3.09052 2.94299 -0.14870 -0.07302 0.64515  176 LYS A CG  
1975 C CD  . LYS A 297 ? 2.73316 3.12464 3.04248 -0.15165 -0.06729 0.65168  176 LYS A CD  
1976 C CE  . LYS A 297 ? 2.79515 3.19698 3.10039 -0.15546 -0.05659 0.66758  176 LYS A CE  
1977 N NZ  . LYS A 297 ? 2.82450 3.19652 3.16366 -0.15866 -0.05180 0.67539  176 LYS A NZ  
1978 N N   . HIS A 298 ? 2.07634 2.51539 2.30374 -0.16624 -0.06151 0.56813  177 HIS A N   
1979 C CA  . HIS A 298 ? 1.88497 2.33847 2.09404 -0.17143 -0.05241 0.55216  177 HIS A CA  
1980 C C   . HIS A 298 ? 1.89793 2.33521 2.11136 -0.17427 -0.05490 0.52920  177 HIS A C   
1981 O O   . HIS A 298 ? 1.81374 2.26322 2.00376 -0.17263 -0.05782 0.51464  177 HIS A O   
1982 C CB  . HIS A 298 ? 1.75990 2.24865 1.92955 -0.16920 -0.05038 0.55358  177 HIS A CB  
1983 C CG  . HIS A 298 ? 1.73750 2.24202 1.89904 -0.16605 -0.04821 0.57610  177 HIS A CG  
1984 N ND1 . HIS A 298 ? 1.73737 2.23849 1.90660 -0.16050 -0.05774 0.59411  177 HIS A ND1 
1985 C CD2 . HIS A 298 ? 1.74257 2.26589 1.88905 -0.16738 -0.03686 0.58391  177 HIS A CD2 
1986 C CE1 . HIS A 298 ? 1.76316 2.27981 1.92102 -0.15888 -0.05278 0.61228  177 HIS A CE1 
1987 N NE2 . HIS A 298 ? 1.76105 2.29097 1.90439 -0.16314 -0.03980 0.60649  177 HIS A NE2 
1988 N N   . PRO A 299 ? 2.01092 2.41903 2.25325 -0.17784 -0.05419 0.52176  178 PRO A N   
1989 C CA  . PRO A 299 ? 2.06274 2.45162 2.30945 -0.17941 -0.05718 0.49809  178 PRO A CA  
1990 C C   . PRO A 299 ? 1.99737 2.39680 2.22957 -0.18167 -0.05016 0.47510  178 PRO A C   
1991 O O   . PRO A 299 ? 1.96053 2.34057 2.19854 -0.18153 -0.05192 0.45132  178 PRO A O   
1992 C CB  . PRO A 299 ? 2.10885 2.46270 2.38965 -0.18214 -0.05916 0.49888  178 PRO A CB  
1993 C CG  . PRO A 299 ? 2.14387 2.50313 2.43617 -0.18429 -0.05323 0.51354  178 PRO A CG  
1994 C CD  . PRO A 299 ? 2.12472 2.51423 2.39609 -0.18000 -0.05150 0.53218  178 PRO A CD  
1995 N N   . GLU A 300 ? 1.96857 2.39793 2.18121 -0.18305 -0.04171 0.48190  179 GLU A N   
1996 C CA  . GLU A 300 ? 1.93095 2.37198 2.13019 -0.18374 -0.03383 0.46083  179 GLU A CA  
1997 C C   . GLU A 300 ? 1.81326 2.27789 1.97600 -0.17856 -0.03271 0.44845  179 GLU A C   
1998 O O   . GLU A 300 ? 1.79695 2.25708 1.94841 -0.17570 -0.03302 0.42150  179 GLU A O   
1999 C CB  . GLU A 300 ? 2.03587 2.49113 2.24664 -0.19027 -0.02179 0.47527  179 GLU A CB  
2000 C CG  . GLU A 300 ? 2.10247 2.53433 2.34713 -0.19547 -0.02245 0.47033  179 GLU A CG  
2001 C CD  . GLU A 300 ? 2.20571 2.65242 2.46085 -0.19844 -0.01175 0.47398  179 GLU A CD  
2002 O OE1 . GLU A 300 ? 2.23409 2.70901 2.46875 -0.19634 -0.00190 0.47901  179 GLU A OE1 
2003 O OE2 . GLU A 300 ? 2.22528 2.65568 2.50883 -0.20294 -0.01312 0.47121  179 GLU A OE2 
2004 N N   . GLN A 301 ? 1.72100 2.20974 1.86391 -0.17750 -0.03159 0.46724  180 GLN A N   
2005 C CA  . GLN A 301 ? 1.66299 2.17419 1.76911 -0.17351 -0.03153 0.45457  180 GLN A CA  
2006 C C   . GLN A 301 ? 1.57863 2.07900 1.67953 -0.16901 -0.04487 0.43861  180 GLN A C   
2007 O O   . GLN A 301 ? 1.51196 1.99449 1.63373 -0.16774 -0.05429 0.44680  180 GLN A O   
2008 C CB  . GLN A 301 ? 1.75539 2.29486 1.83920 -0.17369 -0.02826 0.47989  180 GLN A CB  
2009 C CG  . GLN A 301 ? 1.86231 2.41468 1.95054 -0.17768 -0.01318 0.49589  180 GLN A CG  
2010 C CD  . GLN A 301 ? 1.94756 2.52513 2.00708 -0.17427 -0.00937 0.50865  180 GLN A CD  
2011 O OE1 . GLN A 301 ? 1.96588 2.55100 2.00792 -0.17083 -0.01995 0.51619  180 GLN A OE1 
2012 N NE2 . GLN A 301 ? 1.95873 2.54968 2.01368 -0.17501 0.00569  0.51104  180 GLN A NE2 
2013 N N   . LEU A 302 ? 1.50034 2.01145 1.57457 -0.16668 -0.04478 0.41528  181 LEU A N   
2014 C CA  . LEU A 302 ? 1.35204 1.85784 1.41981 -0.16341 -0.05652 0.39950  181 LEU A CA  
2015 C C   . LEU A 302 ? 1.37908 1.90949 1.42681 -0.16181 -0.06510 0.41560  181 LEU A C   
2016 O O   . LEU A 302 ? 1.31473 1.87058 1.33262 -0.16256 -0.06024 0.41916  181 LEU A O   
2017 C CB  . LEU A 302 ? 1.23474 1.73902 1.28463 -0.16258 -0.05255 0.36668  181 LEU A CB  
2018 C CG  . LEU A 302 ? 1.21065 1.71795 1.24644 -0.16074 -0.06266 0.34897  181 LEU A CG  
2019 C CD1 . LEU A 302 ? 1.23271 1.71277 1.29516 -0.15917 -0.07031 0.34092  181 LEU A CD1 
2020 C CD2 . LEU A 302 ? 1.17161 1.68534 1.18121 -0.16097 -0.05581 0.32131  181 LEU A CD2 
2021 N N   . ASP A 303 ? 1.43153 1.95482 1.49536 -0.15916 -0.07781 0.42558  182 ASP A N   
2022 C CA  . ASP A 303 ? 1.46330 2.01074 1.50914 -0.15680 -0.08915 0.43803  182 ASP A CA  
2023 C C   . ASP A 303 ? 1.45952 2.01649 1.48515 -0.15645 -0.09584 0.41015  182 ASP A C   
2024 O O   . ASP A 303 ? 1.54518 2.12708 1.53687 -0.15767 -0.09621 0.40534  182 ASP A O   
2025 C CB  . ASP A 303 ? 1.56678 2.10496 1.64058 -0.15308 -0.10021 0.46116  182 ASP A CB  
2026 C CG  . ASP A 303 ? 1.65087 2.21691 1.70751 -0.15034 -0.11061 0.48540  182 ASP A CG  
2027 O OD1 . ASP A 303 ? 1.67078 2.26319 1.69098 -0.15199 -0.10954 0.48283  182 ASP A OD1 
2028 O OD2 . ASP A 303 ? 1.69167 2.25288 1.77038 -0.14609 -0.11985 0.50708  182 ASP A OD2 
2029 N N   . PHE A 304 ? 1.36128 1.89798 1.40670 -0.15529 -0.10052 0.39100  183 PHE A N   
2030 C CA  . PHE A 304 ? 1.20651 1.74942 1.23576 -0.15633 -0.10490 0.36267  183 PHE A CA  
2031 C C   . PHE A 304 ? 1.01344 1.52638 1.06569 -0.15589 -0.10258 0.34050  183 PHE A C   
2032 O O   . PHE A 304 ? 1.09052 1.57905 1.16929 -0.15445 -0.09916 0.34704  183 PHE A O   
2033 C CB  . PHE A 304 ? 1.29465 1.86164 1.31588 -0.15505 -0.12120 0.36945  183 PHE A CB  
2034 C CG  . PHE A 304 ? 1.30794 1.86927 1.36093 -0.15046 -0.13184 0.39149  183 PHE A CG  
2035 C CD1 . PHE A 304 ? 1.36546 1.93498 1.42276 -0.14781 -0.13422 0.42490  183 PHE A CD1 
2036 C CD2 . PHE A 304 ? 1.23270 1.78020 1.31186 -0.14839 -0.13842 0.37934  183 PHE A CD2 
2037 C CE1 . PHE A 304 ? 1.30088 1.86360 1.38872 -0.14255 -0.14343 0.44545  183 PHE A CE1 
2038 C CE2 . PHE A 304 ? 1.24513 1.78732 1.35510 -0.14301 -0.14696 0.39919  183 PHE A CE2 
2039 C CZ  . PHE A 304 ? 1.21570 1.76496 1.33029 -0.13976 -0.14975 0.43212  183 PHE A CZ  
2040 N N   . MET A 305 ? 0.96466 1.47866 1.00424 -0.15769 -0.10352 0.31332  184 MET A N   
2041 C CA  . MET A 305 ? 0.92687 1.41409 0.98335 -0.15751 -0.10076 0.29092  184 MET A CA  
2042 C C   . MET A 305 ? 1.12315 1.61433 1.19321 -0.15691 -0.11270 0.28534  184 MET A C   
2043 O O   . MET A 305 ? 1.05137 1.56957 1.10979 -0.15798 -0.12349 0.28939  184 MET A O   
2044 C CB  . MET A 305 ? 0.90878 1.39020 0.94426 -0.16007 -0.09070 0.26340  184 MET A CB  
2045 C CG  . MET A 305 ? 1.13844 1.60306 1.17553 -0.15929 -0.07754 0.26260  184 MET A CG  
2046 S SD  . MET A 305 ? 1.11558 1.56396 1.13840 -0.15993 -0.06656 0.22918  184 MET A SD  
2047 C CE  . MET A 305 ? 1.08005 1.52963 1.09749 -0.15867 -0.05337 0.23698  184 MET A CE  
2048 N N   . LEU A 306 ? 1.20651 1.67129 1.30159 -0.15521 -0.11068 0.27612  185 LEU A N   
2049 C CA  . LEU A 306 ? 1.05636 1.52163 1.16957 -0.15454 -0.11892 0.26840  185 LEU A CA  
2050 C C   . LEU A 306 ? 1.02807 1.46659 1.14642 -0.15601 -0.11010 0.24195  185 LEU A C   
2051 O O   . LEU A 306 ? 0.99351 1.40542 1.11498 -0.15477 -0.09995 0.23787  185 LEU A O   
2052 C CB  . LEU A 306 ? 1.06612 1.52549 1.21117 -0.14909 -0.12509 0.29052  185 LEU A CB  
2053 C CG  . LEU A 306 ? 1.03391 1.51352 1.17947 -0.14623 -0.13305 0.32146  185 LEU A CG  
2054 C CD1 . LEU A 306 ? 1.07732 1.54342 1.25815 -0.13999 -0.13680 0.34029  185 LEU A CD1 
2055 C CD2 . LEU A 306 ? 1.01555 1.53253 1.14265 -0.14797 -0.14578 0.32476  185 LEU A CD2 
2056 N N   . GLN A 307 ? 0.89565 1.34141 1.01439 -0.15907 -0.11412 0.22423  186 GLN A N   
2057 C CA  . GLN A 307 ? 0.85369 1.27391 0.97834 -0.16067 -0.10536 0.20038  186 GLN A CA  
2058 C C   . GLN A 307 ? 0.82285 1.23621 0.97971 -0.15830 -0.10916 0.20207  186 GLN A C   
2059 O O   . GLN A 307 ? 0.95642 1.38916 1.12171 -0.16098 -0.11755 0.19662  186 GLN A O   
2060 C CB  . GLN A 307 ? 0.74220 1.17149 0.84397 -0.16685 -0.10382 0.17650  186 GLN A CB  
2061 C CG  . GLN A 307 ? 0.91635 1.34852 0.98732 -0.16800 -0.09682 0.17203  186 GLN A CG  
2062 C CD  . GLN A 307 ? 1.11454 1.51644 1.18634 -0.16449 -0.08393 0.17023  186 GLN A CD  
2063 O OE1 . GLN A 307 ? 0.94697 1.32169 1.03339 -0.16301 -0.07831 0.16175  186 GLN A OE1 
2064 N NE2 . GLN A 307 ? 0.99078 1.39835 1.04690 -0.16320 -0.07929 0.17856  186 GLN A NE2 
2065 N N   . LYS A 308 ? 0.89319 1.27955 1.06865 -0.15337 -0.10289 0.20938  187 LYS A N   
2066 C CA  . LYS A 308 ? 0.88491 1.25817 1.09120 -0.14970 -0.10241 0.21042  187 LYS A CA  
2067 C C   . LYS A 308 ? 0.98354 1.38342 1.21147 -0.14638 -0.11558 0.22999  187 LYS A C   
2068 O O   . LYS A 308 ? 0.85978 1.27465 1.10404 -0.14744 -0.12126 0.22395  187 LYS A O   
2069 C CB  . LYS A 308 ? 0.92385 1.28777 1.13315 -0.15353 -0.09645 0.18609  187 LYS A CB  
2070 C CG  . LYS A 308 ? 0.79798 1.13006 0.99018 -0.15492 -0.08267 0.16845  187 LYS A CG  
2071 C CD  . LYS A 308 ? 0.87651 1.19443 1.07714 -0.15767 -0.07518 0.14830  187 LYS A CD  
2072 C CE  . LYS A 308 ? 0.86259 1.15070 1.04249 -0.15890 -0.06240 0.13135  187 LYS A CE  
2073 N NZ  . LYS A 308 ? 0.75774 1.03081 0.94469 -0.16199 -0.05383 0.11293  187 LYS A NZ  
2074 N N   . PRO A 309 ? 1.01813 1.42511 1.24849 -0.14235 -0.12087 0.25419  188 PRO A N   
2075 C CA  . PRO A 309 ? 0.96021 1.39228 1.21111 -0.13792 -0.13402 0.27530  188 PRO A CA  
2076 C C   . PRO A 309 ? 1.07911 1.49791 1.36746 -0.13199 -0.13237 0.27671  188 PRO A C   
2077 O O   . PRO A 309 ? 1.13213 1.51889 1.42912 -0.13074 -0.12013 0.26469  188 PRO A O   
2078 C CB  . PRO A 309 ? 1.08315 1.51538 1.32831 -0.13474 -0.13569 0.30064  188 PRO A CB  
2079 C CG  . PRO A 309 ? 1.01996 1.41875 1.25591 -0.13607 -0.12202 0.29254  188 PRO A CG  
2080 C CD  . PRO A 309 ? 0.92166 1.31443 1.13795 -0.14173 -0.11509 0.26446  188 PRO A CD  
2081 N N   . SER A 310 ? 1.14749 1.59218 1.45801 -0.12775 -0.14486 0.29207  189 SER A N   
2082 C CA  . SER A 310 ? 0.99206 1.42904 1.34210 -0.12073 -0.14370 0.29584  189 SER A CA  
2083 C C   . SER A 310 ? 0.94943 1.36569 1.31667 -0.11219 -0.14060 0.31797  189 SER A C   
2084 O O   . SER A 310 ? 1.00333 1.42263 1.35689 -0.11161 -0.14440 0.33622  189 SER A O   
2085 C CB  . SER A 310 ? 0.97419 1.45023 1.34464 -0.11938 -0.15933 0.30242  189 SER A CB  
2086 O OG  . SER A 310 ? 0.92060 1.42150 1.28880 -0.11526 -0.17351 0.32924  189 SER A OG  
2087 N N   . LEU A 311 ? 1.01550 1.40933 1.41333 -0.10579 -0.13249 0.31573  190 LEU A N   
2088 C CA  . LEU A 311 ? 1.14807 1.51847 1.56504 -0.09752 -0.12861 0.33438  190 LEU A CA  
2089 C C   . LEU A 311 ? 1.26721 1.66376 1.69705 -0.09149 -0.14299 0.36460  190 LEU A C   
2090 O O   . LEU A 311 ? 1.18295 1.56481 1.61366 -0.08812 -0.14199 0.38357  190 LEU A O   
2091 C CB  . LEU A 311 ? 1.10844 1.45478 1.55754 -0.09074 -0.11784 0.32601  190 LEU A CB  
2092 C CG  . LEU A 311 ? 1.14609 1.46936 1.58466 -0.09587 -0.10368 0.29681  190 LEU A CG  
2093 C CD1 . LEU A 311 ? 1.25157 1.60023 1.70389 -0.09826 -0.10628 0.28346  190 LEU A CD1 
2094 C CD2 . LEU A 311 ? 1.14716 1.42802 1.59976 -0.08997 -0.08863 0.29186  190 LEU A CD2 
2095 N N   . ALA A 312 ? 1.34963 1.78491 1.78940 -0.09041 -0.15690 0.36996  191 ALA A N   
2096 C CA  . ALA A 312 ? 1.40094 1.86318 1.85137 -0.08393 -0.17213 0.40005  191 ALA A CA  
2097 C C   . ALA A 312 ? 1.35570 1.83439 1.76755 -0.09003 -0.17928 0.41123  191 ALA A C   
2098 O O   . ALA A 312 ? 1.45517 1.93367 1.86738 -0.08547 -0.18314 0.43779  191 ALA A O   
2099 C CB  . ALA A 312 ? 1.47082 1.97105 1.94561 -0.08068 -0.18630 0.40192  191 ALA A CB  
2100 N N   . GLU A 313 ? 1.15248 1.64480 1.53126 -0.10015 -0.18004 0.39158  192 GLU A N   
2101 C CA  . GLU A 313 ? 1.09349 1.60031 1.43351 -0.10594 -0.18401 0.39953  192 GLU A CA  
2102 C C   . GLU A 313 ? 1.16374 1.64001 1.49390 -0.10623 -0.17202 0.40888  192 GLU A C   
2103 O O   . GLU A 313 ? 1.13953 1.62678 1.45043 -0.10727 -0.17540 0.42811  192 GLU A O   
2104 C CB  . GLU A 313 ? 1.02902 1.54813 1.33707 -0.11635 -0.18311 0.37226  192 GLU A CB  
2105 C CG  . GLU A 313 ? 1.05167 1.58703 1.31808 -0.12210 -0.18556 0.37765  192 GLU A CG  
2106 C CD  . GLU A 313 ? 1.02674 1.57294 1.26287 -0.13159 -0.18420 0.34949  192 GLU A CD  
2107 O OE1 . GLU A 313 ? 1.00440 1.56883 1.20572 -0.13604 -0.18712 0.35167  192 GLU A OE1 
2108 O OE2 . GLU A 313 ? 0.90609 1.44172 1.15305 -0.13451 -0.17932 0.32531  192 GLU A OE2 
2109 N N   . LEU A 314 ? 1.24381 1.68229 1.58702 -0.10566 -0.15811 0.39595  193 LEU A N   
2110 C CA  . LEU A 314 ? 1.27663 1.68573 1.61496 -0.10651 -0.14812 0.40426  193 LEU A CA  
2111 C C   . LEU A 314 ? 1.42554 1.82505 1.79167 -0.09812 -0.15076 0.43313  193 LEU A C   
2112 O O   . LEU A 314 ? 1.48337 1.87797 1.84182 -0.09931 -0.14955 0.45231  193 LEU A O   
2113 C CB  . LEU A 314 ? 1.26042 1.63269 1.59956 -0.10932 -0.13383 0.37924  193 LEU A CB  
2114 C CG  . LEU A 314 ? 1.22058 1.59651 1.53096 -0.11741 -0.12921 0.35198  193 LEU A CG  
2115 C CD1 . LEU A 314 ? 1.11575 1.46139 1.43435 -0.11753 -0.11815 0.32748  193 LEU A CD1 
2116 C CD2 . LEU A 314 ? 1.02714 1.40100 1.30908 -0.12349 -0.12483 0.35385  193 LEU A CD2 
2117 N N   . GLU A 315 ? 1.57976 1.97598 1.98001 -0.08948 -0.15340 0.43687  194 GLU A N   
2118 C CA  . GLU A 315 ? 1.65968 2.04991 2.08830 -0.07997 -0.15716 0.46592  194 GLU A CA  
2119 C C   . GLU A 315 ? 1.58507 2.01011 2.00278 -0.07837 -0.17120 0.49435  194 GLU A C   
2120 O O   . GLU A 315 ? 1.63130 2.04859 2.05963 -0.07359 -0.17232 0.52187  194 GLU A O   
2121 C CB  . GLU A 315 ? 1.75370 2.14007 2.22173 -0.06996 -0.15783 0.46381  194 GLU A CB  
2122 C CG  . GLU A 315 ? 1.85208 2.19862 2.33268 -0.06967 -0.14201 0.44027  194 GLU A CG  
2123 C CD  . GLU A 315 ? 1.95269 2.26000 2.42467 -0.07315 -0.13092 0.44101  194 GLU A CD  
2124 O OE1 . GLU A 315 ? 1.99230 2.29020 2.47678 -0.06896 -0.13256 0.46568  194 GLU A OE1 
2125 O OE2 . GLU A 315 ? 1.96256 2.24866 2.41571 -0.08038 -0.12107 0.41726  194 GLU A OE2 
2126 N N   . SER A 316 ? 1.48383 1.94619 1.87916 -0.08254 -0.18181 0.48817  195 SER A N   
2127 C CA  . SER A 316 ? 1.43387 1.93082 1.81211 -0.08156 -0.19564 0.51360  195 SER A CA  
2128 C C   . SER A 316 ? 1.42612 1.91841 1.77216 -0.08837 -0.18940 0.52392  195 SER A C   
2129 O O   . SER A 316 ? 1.48320 1.99620 1.81691 -0.08647 -0.19754 0.55098  195 SER A O   
2130 C CB  . SER A 316 ? 1.45214 1.98912 1.81287 -0.08532 -0.20883 0.50049  195 SER A CB  
2131 O OG  . SER A 316 ? 1.54442 2.11571 1.88615 -0.08389 -0.22350 0.52505  195 SER A OG  
2132 N N   . LEU A 317 ? 1.38026 1.84688 1.71306 -0.09599 -0.17508 0.50391  196 LEU A N   
2133 C CA  . LEU A 317 ? 1.46973 1.93197 1.77654 -0.10278 -0.16754 0.51205  196 LEU A CA  
2134 C C   . LEU A 317 ? 1.60556 2.02721 1.93054 -0.10359 -0.15471 0.51550  196 LEU A C   
2135 O O   . LEU A 317 ? 1.48660 1.90154 1.79489 -0.11034 -0.14674 0.51875  196 LEU A O   
2136 C CB  . LEU A 317 ? 1.39303 1.86649 1.66417 -0.11211 -0.16303 0.48548  196 LEU A CB  
2137 C CG  . LEU A 317 ? 1.31342 1.82721 1.55825 -0.11395 -0.17497 0.48075  196 LEU A CG  
2138 C CD1 . LEU A 317 ? 1.18915 1.70929 1.39703 -0.12302 -0.16750 0.45791  196 LEU A CD1 
2139 C CD2 . LEU A 317 ? 1.35208 1.89324 1.58892 -0.10977 -0.18651 0.51430  196 LEU A CD2 
2140 N N   . SER A 318 ? 1.88707 2.28185 2.24633 -0.09715 -0.15230 0.51406  197 SER A N   
2141 C CA  . SER A 318 ? 2.03422 2.38772 2.40921 -0.09892 -0.14048 0.51218  197 SER A CA  
2142 C C   . SER A 318 ? 2.01029 2.35768 2.38943 -0.09975 -0.13903 0.54308  197 SER A C   
2143 O O   . SER A 318 ? 2.07980 2.40046 2.46114 -0.10580 -0.12945 0.54094  197 SER A O   
2144 C CB  . SER A 318 ? 2.15230 2.47905 2.56199 -0.09079 -0.13800 0.50505  197 SER A CB  
2145 O OG  . SER A 318 ? 2.25811 2.59329 2.69376 -0.08038 -0.14610 0.53174  197 SER A OG  
2146 N N   . LYS A 319 ? 1.92653 2.29836 2.30728 -0.09411 -0.14867 0.57244  198 LYS A N   
2147 C CA  . LYS A 319 ? 1.84257 2.20887 2.22721 -0.09475 -0.14664 0.60463  198 LYS A CA  
2148 C C   . LYS A 319 ? 1.80961 2.19730 2.15920 -0.10402 -0.14323 0.60936  198 LYS A C   
2149 O O   . LYS A 319 ? 1.80018 2.17839 2.15294 -0.10703 -0.13515 0.61965  198 LYS A O   
2150 C CB  . LYS A 319 ? 1.82798 2.20914 2.22962 -0.08374 -0.15597 0.62963  198 LYS A CB  
2151 C CG  . LYS A 319 ? 1.82257 2.17296 2.26676 -0.07406 -0.15415 0.63492  198 LYS A CG  
2152 C CD  . LYS A 319 ? 1.82472 2.18371 2.28373 -0.06540 -0.15788 0.65951  198 LYS A CD  
2153 C CE  . LYS A 319 ? 1.74700 2.07967 2.24890 -0.05385 -0.15681 0.66419  198 LYS A CE  
2154 N NZ  . LYS A 319 ? 1.66017 2.01075 2.17631 -0.04474 -0.16740 0.65908  198 LYS A NZ  
2155 N N   . THR A 320 ? 1.81649 2.23208 2.13449 -0.10810 -0.14638 0.59200  199 THR A N   
2156 C CA  . THR A 320 ? 1.86545 2.30563 2.14841 -0.11513 -0.14349 0.59907  199 THR A CA  
2157 C C   . THR A 320 ? 1.83683 2.27334 2.09911 -0.12440 -0.13324 0.56967  199 THR A C   
2158 O O   . THR A 320 ? 1.88287 2.33584 2.11958 -0.13033 -0.12758 0.57505  199 THR A O   
2159 C CB  . THR A 320 ? 1.87223 2.35336 2.13012 -0.11146 -0.15564 0.60436  199 THR A CB  
2160 O OG1 . THR A 320 ? 1.87835 2.36928 2.13442 -0.10976 -0.16357 0.57927  199 THR A OG1 
2161 C CG2 . THR A 320 ? 1.92932 2.41567 2.20513 -0.10247 -0.16204 0.62758  199 THR A CG2 
2162 N N   . HIS A 321 ? 1.70195 2.11754 1.97434 -0.12529 -0.12997 0.53987  200 HIS A N   
2163 C CA  . HIS A 321 ? 1.53082 1.94367 1.78351 -0.13275 -0.12134 0.51239  200 HIS A CA  
2164 C C   . HIS A 321 ? 1.48610 1.86087 1.76015 -0.13430 -0.11444 0.49281  200 HIS A C   
2165 O O   . HIS A 321 ? 1.41509 1.76813 1.71522 -0.12896 -0.11685 0.49268  200 HIS A O   
2166 C CB  . HIS A 321 ? 1.47030 1.90752 1.69780 -0.13275 -0.12646 0.48939  200 HIS A CB  
2167 C CG  . HIS A 321 ? 1.44083 1.91537 1.63639 -0.13407 -0.13087 0.50095  200 HIS A CG  
2168 N ND1 . HIS A 321 ? 1.43519 1.93253 1.62901 -0.12884 -0.14245 0.52545  200 HIS A ND1 
2169 C CD2 . HIS A 321 ? 1.43434 1.92715 1.59699 -0.13958 -0.12508 0.49091  200 HIS A CD2 
2170 C CE1 . HIS A 321 ? 1.44224 1.97009 1.60071 -0.13167 -0.14396 0.52968  200 HIS A CE1 
2171 N NE2 . HIS A 321 ? 1.43870 1.96395 1.57800 -0.13814 -0.13272 0.50844  200 HIS A NE2 
2172 N N   . LEU A 322 ? 1.58709 1.95453 1.84897 -0.14126 -0.10569 0.47622  201 LEU A N   
2173 C CA  . LEU A 322 ? 1.56701 1.90290 1.83941 -0.14340 -0.10013 0.45225  201 LEU A CA  
2174 C C   . LEU A 322 ? 1.40915 1.75364 1.65854 -0.14475 -0.09841 0.42268  201 LEU A C   
2175 O O   . LEU A 322 ? 1.47201 1.84467 1.69613 -0.14652 -0.09858 0.42024  201 LEU A O   
2176 C CB  . LEU A 322 ? 1.50220 1.82062 1.78308 -0.15038 -0.09245 0.45770  201 LEU A CB  
2177 C CG  . LEU A 322 ? 1.52952 1.82523 1.83977 -0.15015 -0.09261 0.48024  201 LEU A CG  
2178 C CD1 . LEU A 322 ? 1.56979 1.84610 1.89017 -0.15878 -0.08574 0.47933  201 LEU A CD1 
2179 C CD2 . LEU A 322 ? 1.54774 1.81758 1.87916 -0.14316 -0.09631 0.47337  201 LEU A CD2 
2180 N N   . PHE A 323 ? 1.19574 1.51384 1.45307 -0.14393 -0.09593 0.40010  202 PHE A N   
2181 C CA  . PHE A 323 ? 1.12907 1.44994 1.36913 -0.14395 -0.09448 0.37236  202 PHE A CA  
2182 C C   . PHE A 323 ? 1.12413 1.42094 1.36025 -0.14773 -0.08699 0.35295  202 PHE A C   
2183 O O   . PHE A 323 ? 1.11371 1.38140 1.36694 -0.14817 -0.08502 0.35278  202 PHE A O   
2184 C CB  . PHE A 323 ? 1.00876 1.32246 1.26159 -0.13825 -0.09875 0.36337  202 PHE A CB  
2185 C CG  . PHE A 323 ? 1.09312 1.42824 1.35667 -0.13332 -0.10784 0.38428  202 PHE A CG  
2186 C CD1 . PHE A 323 ? 1.07119 1.44235 1.31539 -0.13401 -0.11422 0.39014  202 PHE A CD1 
2187 C CD2 . PHE A 323 ? 1.06762 1.38661 1.36018 -0.12755 -0.11030 0.39809  202 PHE A CD2 
2188 C CE1 . PHE A 323 ? 1.08255 1.47499 1.33575 -0.12911 -0.12446 0.41041  202 PHE A CE1 
2189 C CE2 . PHE A 323 ? 1.03018 1.36974 1.33458 -0.12180 -0.11948 0.41891  202 PHE A CE2 
2190 C CZ  . PHE A 323 ? 1.04459 1.42180 1.32910 -0.12262 -0.12736 0.42563  202 PHE A CZ  
2191 N N   . LEU A 324 ? 1.08321 1.39179 1.29649 -0.15019 -0.08325 0.33646  203 LEU A N   
2192 C CA  . LEU A 324 ? 1.09424 1.38229 1.30162 -0.15227 -0.07727 0.31595  203 LEU A CA  
2193 C C   . LEU A 324 ? 1.03551 1.32288 1.22744 -0.15030 -0.07579 0.29156  203 LEU A C   
2194 O O   . LEU A 324 ? 0.97939 1.29154 1.15546 -0.15030 -0.07708 0.28806  203 LEU A O   
2195 C CB  . LEU A 324 ? 0.92969 1.23033 1.12715 -0.15668 -0.07237 0.31959  203 LEU A CB  
2196 C CG  . LEU A 324 ? 0.94674 1.24401 1.16223 -0.16048 -0.07204 0.34160  203 LEU A CG  
2197 C CD1 . LEU A 324 ? 0.95603 1.28508 1.16489 -0.16181 -0.07171 0.36382  203 LEU A CD1 
2198 C CD2 . LEU A 324 ? 0.96693 1.25177 1.18566 -0.16467 -0.06761 0.33329  203 LEU A CD2 
2199 N N   . MET A 325 ? 0.96524 1.22349 1.16096 -0.14903 -0.07291 0.27475  204 MET A N   
2200 C CA  . MET A 325 ? 0.84235 1.09564 1.02304 -0.14795 -0.06935 0.25131  204 MET A CA  
2201 C C   . MET A 325 ? 0.87553 1.13519 1.03699 -0.15005 -0.06440 0.24104  204 MET A C   
2202 O O   . MET A 325 ? 0.97956 1.22675 1.14333 -0.15136 -0.06218 0.24169  204 MET A O   
2203 C CB  . MET A 325 ? 0.84109 1.05992 1.02956 -0.14566 -0.06644 0.23815  204 MET A CB  
2204 C CG  . MET A 325 ? 0.87900 1.08697 1.05056 -0.14512 -0.06079 0.21470  204 MET A CG  
2205 S SD  . MET A 325 ? 1.00262 1.16830 1.17843 -0.14241 -0.05585 0.20059  204 MET A SD  
2206 C CE  . MET A 325 ? 0.98047 1.12842 1.16848 -0.14385 -0.05900 0.21368  204 MET A CE  
2207 N N   . ASP A 326 ? 0.89399 1.17402 1.03791 -0.15036 -0.06305 0.23186  205 ASP A N   
2208 C CA  . ASP A 326 ? 0.79248 1.07524 0.91786 -0.15079 -0.05677 0.21766  205 ASP A CA  
2209 C C   . ASP A 326 ? 0.86058 1.11235 0.98397 -0.14885 -0.05250 0.19934  205 ASP A C   
2210 O O   . ASP A 326 ? 0.86179 1.09900 0.98708 -0.14767 -0.05224 0.18901  205 ASP A O   
2211 C CB  . ASP A 326 ? 0.69439 1.00116 0.80150 -0.15163 -0.05630 0.20902  205 ASP A CB  
2212 C CG  . ASP A 326 ? 0.87149 1.18240 0.95939 -0.15133 -0.04863 0.19495  205 ASP A CG  
2213 O OD1 . ASP A 326 ? 0.93522 1.23102 1.02515 -0.14980 -0.04410 0.19165  205 ASP A OD1 
2214 O OD2 . ASP A 326 ? 0.82905 1.15871 0.90002 -0.15244 -0.04745 0.18684  205 ASP A OD2 
2215 N N   . ILE A 327 ? 0.85660 1.09921 0.97659 -0.14839 -0.04904 0.19606  206 ILE A N   
2216 C CA  . ILE A 327 ? 0.80756 1.02113 0.92285 -0.14600 -0.04582 0.18048  206 ILE A CA  
2217 C C   . ILE A 327 ? 0.89210 1.10915 0.98947 -0.14388 -0.03948 0.16542  206 ILE A C   
2218 O O   . ILE A 327 ? 0.88918 1.08476 0.98108 -0.14112 -0.03673 0.15471  206 ILE A O   
2219 C CB  . ILE A 327 ? 0.82929 1.02513 0.95615 -0.14656 -0.04867 0.18730  206 ILE A CB  
2220 C CG1 . ILE A 327 ? 0.61606 0.83262 0.74703 -0.14852 -0.04864 0.19836  206 ILE A CG1 
2221 C CG2 . ILE A 327 ? 0.75162 0.93562 0.89563 -0.14798 -0.05355 0.19837  206 ILE A CG2 
2222 C CD1 . ILE A 327 ? 0.79489 0.99675 0.93984 -0.15060 -0.05266 0.20459  206 ILE A CD1 
2223 N N   . GLY A 328 ? 0.78343 1.02617 0.87056 -0.14474 -0.03710 0.16433  207 GLY A N   
2224 C CA  . GLY A 328 ? 0.75353 0.99907 0.82370 -0.14245 -0.02999 0.14896  207 GLY A CA  
2225 C C   . GLY A 328 ? 0.75052 0.99759 0.82011 -0.13948 -0.02601 0.14982  207 GLY A C   
2226 O O   . GLY A 328 ? 0.76829 1.00081 0.82933 -0.13544 -0.02096 0.13616  207 GLY A O   
2227 N N   . ILE A 329 ? 0.62443 0.88917 0.70463 -0.14123 -0.02788 0.16632  208 ILE A N   
2228 C CA  . ILE A 329 ? 0.59199 0.86653 0.67480 -0.13885 -0.02330 0.16853  208 ILE A CA  
2229 C C   . ILE A 329 ? 0.73859 1.04659 0.81996 -0.14113 -0.01981 0.18104  208 ILE A C   
2230 O O   . ILE A 329 ? 0.83597 1.15496 0.93026 -0.14520 -0.02382 0.19952  208 ILE A O   
2231 C CB  . ILE A 329 ? 0.66618 0.92649 0.76711 -0.13938 -0.02857 0.17647  208 ILE A CB  
2232 C CG1 . ILE A 329 ? 0.67141 0.89765 0.76853 -0.13671 -0.03156 0.16364  208 ILE A CG1 
2233 C CG2 . ILE A 329 ? 0.67181 0.94662 0.77946 -0.13700 -0.02425 0.17923  208 ILE A CG2 
2234 C CD1 . ILE A 329 ? 0.80183 1.01030 0.91388 -0.13883 -0.03931 0.17066  208 ILE A CD1 
2235 N N   . TRP A 330 ? 0.65712 0.97990 0.72192 -0.13843 -0.01151 0.17106  209 TRP A N   
2236 C CA  . TRP A 330 ? 0.72705 1.08132 0.78432 -0.13984 -0.00603 0.18020  209 TRP A CA  
2237 C C   . TRP A 330 ? 0.93276 1.29819 0.99131 -0.13531 0.00426  0.17741  209 TRP A C   
2238 O O   . TRP A 330 ? 1.14901 1.49881 1.20810 -0.12999 0.00755  0.16385  209 TRP A O   
2239 C CB  . TRP A 330 ? 0.71314 1.07811 0.74687 -0.14093 -0.00463 0.16981  209 TRP A CB  
2240 C CG  . TRP A 330 ? 0.90129 1.26386 0.93606 -0.14528 -0.01487 0.17521  209 TRP A CG  
2241 C CD1 . TRP A 330 ? 0.88003 1.22334 0.93209 -0.14666 -0.02309 0.18147  209 TRP A CD1 
2242 C CD2 . TRP A 330 ? 1.01244 1.39325 1.03098 -0.14829 -0.01808 0.17436  209 TRP A CD2 
2243 N NE1 . TRP A 330 ? 0.79527 1.14439 0.84571 -0.14958 -0.03040 0.18537  209 TRP A NE1 
2244 C CE2 . TRP A 330 ? 0.93326 1.30623 0.96358 -0.15086 -0.02857 0.18148  209 TRP A CE2 
2245 C CE3 . TRP A 330 ? 0.92992 1.33317 0.92460 -0.14896 -0.01338 0.16778  209 TRP A CE3 
2246 C CZ2 . TRP A 330 ? 1.00992 1.39881 1.03161 -0.15387 -0.03568 0.18338  209 TRP A CZ2 
2247 C CZ3 . TRP A 330 ? 0.93098 1.34896 0.91372 -0.15280 -0.02113 0.16873  209 TRP A CZ3 
2248 C CH2 . TRP A 330 ? 0.96241 1.37419 0.95991 -0.15513 -0.03276 0.17703  209 TRP A CH2 
2249 N N   . LEU A 331 ? 0.87164 1.26486 0.93132 -0.13699 0.00987  0.19146  210 LEU A N   
2250 C CA  . LEU A 331 ? 1.01563 1.42616 1.07687 -0.13266 0.02200  0.19049  210 LEU A CA  
2251 C C   . LEU A 331 ? 0.95414 1.39153 0.99274 -0.13344 0.03075  0.19206  210 LEU A C   
2252 O O   . LEU A 331 ? 0.95147 1.40264 0.98564 -0.13880 0.02665  0.20731  210 LEU A O   
2253 C CB  . LEU A 331 ? 1.06936 1.48870 1.15930 -0.13478 0.02154  0.20898  210 LEU A CB  
2254 C CG  . LEU A 331 ? 1.02084 1.41676 1.13352 -0.13750 0.00935  0.21389  210 LEU A CG  
2255 C CD1 . LEU A 331 ? 1.03667 1.44641 1.17739 -0.14188 0.00913  0.23324  210 LEU A CD1 
2256 C CD2 . LEU A 331 ? 0.97894 1.35093 1.09150 -0.13123 0.00760  0.19574  210 LEU A CD2 
2257 N N   . LEU A 332 ? 0.82471 1.26896 0.84825 -0.12772 0.04290  0.17677  211 LEU A N   
2258 C CA  . LEU A 332 ? 0.83527 1.30306 0.83232 -0.12799 0.05231  0.17443  211 LEU A CA  
2259 C C   . LEU A 332 ? 0.87453 1.36274 0.87514 -0.12276 0.06890  0.17648  211 LEU A C   
2260 O O   . LEU A 332 ? 0.76531 1.24512 0.78084 -0.11616 0.07471  0.16798  211 LEU A O   
2261 C CB  . LEU A 332 ? 0.74181 1.19802 0.71150 -0.12663 0.05267  0.14989  211 LEU A CB  
2262 C CG  . LEU A 332 ? 0.83521 1.27291 0.80118 -0.13153 0.03809  0.14454  211 LEU A CG  
2263 C CD1 . LEU A 332 ? 0.71236 1.14812 0.64969 -0.13229 0.03997  0.12242  211 LEU A CD1 
2264 C CD2 . LEU A 332 ? 0.80857 1.25803 0.78055 -0.13808 0.02709  0.16686  211 LEU A CD2 
2265 N N   . SER A 333 ? 0.87620 1.39189 0.86342 -0.12530 0.07669  0.18874  212 SER A N   
2266 C CA  . SER A 333 ? 0.79881 1.33705 0.78300 -0.12029 0.09543  0.18910  212 SER A CA  
2267 C C   . SER A 333 ? 0.86793 1.40436 0.82055 -0.11468 0.10608  0.16340  212 SER A C   
2268 O O   . SER A 333 ? 0.89147 1.41447 0.82117 -0.11694 0.09831  0.14822  212 SER A O   
2269 C CB  . SER A 333 ? 0.88667 1.45385 0.86546 -0.12552 0.10085  0.21291  212 SER A CB  
2270 O OG  . SER A 333 ? 0.80144 1.37712 0.74263 -0.12874 0.09884  0.20969  212 SER A OG  
2271 N N   . ASP A 334 ? 0.83450 1.38444 0.78828 -0.10736 0.12454  0.15807  213 ASP A N   
2272 C CA  . ASP A 334 ? 0.93162 1.47859 0.85680 -0.10113 0.13726  0.13269  213 ASP A CA  
2273 C C   . ASP A 334 ? 1.00209 1.55845 0.88527 -0.10703 0.13562  0.12692  213 ASP A C   
2274 O O   . ASP A 334 ? 1.10677 1.64917 0.96487 -0.10634 0.13515  0.10297  213 ASP A O   
2275 C CB  . ASP A 334 ? 1.02772 1.59358 0.96126 -0.09237 0.15941  0.13228  213 ASP A CB  
2276 C CG  . ASP A 334 ? 1.06180 1.61859 1.03603 -0.08499 0.16058  0.13377  213 ASP A CG  
2277 O OD1 . ASP A 334 ? 0.97186 1.51510 0.97091 -0.08882 0.14433  0.14387  213 ASP A OD1 
2278 O OD2 . ASP A 334 ? 1.01407 1.57750 0.99517 -0.07495 0.17766  0.12458  213 ASP A OD2 
2279 N N   . ARG A 335 ? 1.15841 1.73838 1.03342 -0.11314 0.13431  0.14893  214 ARG A N   
2280 C CA  . ARG A 335 ? 1.17362 1.76540 1.00723 -0.11853 0.13119  0.14571  214 ARG A CA  
2281 C C   . ARG A 335 ? 1.12827 1.70219 0.95641 -0.12506 0.10928  0.14005  214 ARG A C   
2282 O O   . ARG A 335 ? 1.01837 1.58855 0.81559 -0.12740 0.10542  0.12077  214 ARG A O   
2283 C CB  . ARG A 335 ? 1.10000 1.72111 0.92747 -0.12265 0.13549  0.17394  214 ARG A CB  
2284 C CG  . ARG A 335 ? 1.20950 1.84497 0.99425 -0.12843 0.12923  0.17580  214 ARG A CG  
2285 C CD  . ARG A 335 ? 1.35423 2.01893 1.13029 -0.13066 0.13841  0.20386  214 ARG A CD  
2286 N NE  . ARG A 335 ? 1.44269 2.11722 1.19657 -0.13773 0.12272  0.21971  214 ARG A NE  
2287 C CZ  . ARG A 335 ? 1.46224 2.13835 1.23910 -0.14244 0.11054  0.24776  214 ARG A CZ  
2288 N NH1 . ARG A 335 ? 1.49590 2.16409 1.31723 -0.14201 0.11209  0.26165  214 ARG A NH1 
2289 N NH2 . ARG A 335 ? 1.41044 2.09594 1.16623 -0.14745 0.09641  0.26187  214 ARG A NH2 
2290 N N   . ALA A 336 ? 1.02776 1.59067 0.88692 -0.12826 0.09513  0.15604  215 ALA A N   
2291 C CA  . ALA A 336 ? 1.03898 1.58175 0.90058 -0.13289 0.07631  0.14939  215 ALA A CA  
2292 C C   . ALA A 336 ? 0.91544 1.43387 0.77059 -0.12961 0.07777  0.11897  215 ALA A C   
2293 O O   . ALA A 336 ? 0.83805 1.34820 0.67628 -0.13400 0.06802  0.10475  215 ALA A O   
2294 C CB  . ALA A 336 ? 1.04941 1.58008 0.94825 -0.13487 0.06494  0.16839  215 ALA A CB  
2295 N N   . VAL A 337 ? 0.96463 1.47131 0.83528 -0.12197 0.08955  0.10944  216 VAL A N   
2296 C CA  . VAL A 337 ? 1.09926 1.57965 0.96602 -0.11810 0.09177  0.08245  216 VAL A CA  
2297 C C   . VAL A 337 ? 1.25008 1.73559 1.07937 -0.11873 0.09967  0.05993  216 VAL A C   
2298 O O   . VAL A 337 ? 1.08831 1.55701 0.90472 -0.12239 0.09292  0.04051  216 VAL A O   
2299 C CB  . VAL A 337 ? 1.04093 1.50976 0.93248 -0.10841 0.10276  0.07951  216 VAL A CB  
2300 C CG1 . VAL A 337 ? 0.96779 1.41407 0.84795 -0.10252 0.11109  0.05109  216 VAL A CG1 
2301 C CG2 . VAL A 337 ? 1.05800 1.51173 0.98305 -0.10907 0.09059  0.09379  216 VAL A CG2 
2302 N N   . GLU A 338 ? 1.25796 1.76666 1.06918 -0.11570 0.11456  0.06176  217 GLU A N   
2303 C CA  . GLU A 338 ? 1.22454 1.73915 0.99599 -0.11667 0.12257  0.03992  217 GLU A CA  
2304 C C   . GLU A 338 ? 1.19853 1.71891 0.94577 -0.12728 0.10529  0.03785  217 GLU A C   
2305 O O   . GLU A 338 ? 1.09073 1.60017 0.81550 -0.13070 0.10279  0.01293  217 GLU A O   
2306 C CB  . GLU A 338 ? 1.23647 1.77819 0.99174 -0.11213 0.14137  0.04683  217 GLU A CB  
2307 C CG  . GLU A 338 ? 1.41192 1.96585 1.11933 -0.11520 0.14728  0.02956  217 GLU A CG  
2308 C CD  . GLU A 338 ? 1.52441 2.10464 1.21474 -0.11007 0.16820  0.03702  217 GLU A CD  
2309 O OE1 . GLU A 338 ? 1.54323 2.11896 1.23896 -0.10045 0.18824  0.02448  217 GLU A OE1 
2310 O OE2 . GLU A 338 ? 1.59313 2.19860 1.26509 -0.11519 0.16529  0.05619  217 GLU A OE2 
2311 N N   . ILE A 339 ? 1.12332 1.66073 0.87675 -0.13268 0.09276  0.06399  218 ILE A N   
2312 C CA  . ILE A 339 ? 1.12433 1.67161 0.85660 -0.14173 0.07552  0.06518  218 ILE A CA  
2313 C C   . ILE A 339 ? 1.11991 1.64275 0.86697 -0.14615 0.06023  0.05201  218 ILE A C   
2314 O O   . ILE A 339 ? 1.10896 1.63037 0.83486 -0.15220 0.05204  0.03364  218 ILE A O   
2315 C CB  . ILE A 339 ? 1.12992 1.70033 0.86788 -0.14491 0.06694  0.09877  218 ILE A CB  
2316 C CG1 . ILE A 339 ? 1.31400 1.91124 1.02819 -0.14223 0.08271  0.10977  218 ILE A CG1 
2317 C CG2 . ILE A 339 ? 1.08332 1.66113 0.80919 -0.15305 0.04578  0.10259  218 ILE A CG2 
2318 C CD1 . ILE A 339 ? 1.37884 1.99772 1.09898 -0.14498 0.07710  0.14479  218 ILE A CD1 
2319 N N   . LEU A 340 ? 1.15456 1.65864 0.93807 -0.14379 0.05605  0.06140  219 LEU A N   
2320 C CA  . LEU A 340 ? 1.04728 1.52528 0.84593 -0.14678 0.04548  0.04814  219 LEU A CA  
2321 C C   . LEU A 340 ? 1.06358 1.52311 0.84616 -0.14613 0.05367  0.01575  219 LEU A C   
2322 O O   . LEU A 340 ? 1.13083 1.58148 0.90636 -0.15287 0.04420  -0.00017 219 LEU A O   
2323 C CB  . LEU A 340 ? 0.95843 1.41668 0.79407 -0.14234 0.04458  0.06034  219 LEU A CB  
2324 C CG  . LEU A 340 ? 0.96218 1.38944 0.81363 -0.14351 0.03821  0.04628  219 LEU A CG  
2325 C CD1 . LEU A 340 ? 1.10717 1.53760 0.95796 -0.15209 0.02151  0.04724  219 LEU A CD1 
2326 C CD2 . LEU A 340 ? 0.88086 1.28969 0.76354 -0.13831 0.03854  0.05836  219 LEU A CD2 
2327 N N   . MET A 341 ? 1.12566 1.57903 0.90460 -0.13802 0.07169  0.00579  220 MET A N   
2328 C CA  . MET A 341 ? 1.22060 1.65210 0.98733 -0.13606 0.08132  -0.02451 220 MET A CA  
2329 C C   . MET A 341 ? 1.29982 1.74255 1.02946 -0.14341 0.07948  -0.04409 220 MET A C   
2330 O O   . MET A 341 ? 1.20211 1.62641 0.92499 -0.14854 0.07605  -0.06740 220 MET A O   
2331 C CB  . MET A 341 ? 1.10341 1.52908 0.87525 -0.12434 0.10159  -0.02881 220 MET A CB  
2332 C CG  . MET A 341 ? 1.15578 1.56535 0.96431 -0.11718 0.10211  -0.01524 220 MET A CG  
2333 S SD  . MET A 341 ? 1.07033 1.46265 0.88804 -0.10305 0.12317  -0.02896 220 MET A SD  
2334 C CE  . MET A 341 ? 1.20350 1.57048 0.99548 -0.10567 0.12833  -0.06498 220 MET A CE  
2335 N N   . LYS A 342 ? 1.40013 1.87282 1.10467 -0.14466 0.08152  -0.03506 221 LYS A N   
2336 C CA  . LYS A 342 ? 1.50340 1.98754 1.16913 -0.15218 0.07795  -0.05420 221 LYS A CA  
2337 C C   . LYS A 342 ? 1.47889 1.96874 1.14573 -0.16346 0.05444  -0.05161 221 LYS A C   
2338 O O   . LYS A 342 ? 1.49663 1.98485 1.14195 -0.17140 0.04786  -0.07441 221 LYS A O   
2339 C CB  . LYS A 342 ? 1.61800 2.13253 1.25240 -0.15012 0.08714  -0.04512 221 LYS A CB  
2340 C CG  . LYS A 342 ? 1.68840 2.23054 1.32727 -0.15216 0.07678  -0.01099 221 LYS A CG  
2341 C CD  . LYS A 342 ? 1.79749 2.36407 1.41375 -0.14692 0.09331  0.00052  221 LYS A CD  
2342 C CE  . LYS A 342 ? 1.86853 2.44469 1.43505 -0.14964 0.10005  -0.02356 221 LYS A CE  
2343 N NZ  . LYS A 342 ? 1.91564 2.51517 1.45762 -0.14403 0.11885  -0.01319 221 LYS A NZ  
2344 N N   . ARG A 343 ? 1.44054 1.93708 1.13383 -0.16437 0.04162  -0.02478 222 ARG A N   
2345 C CA  . ARG A 343 ? 1.29496 1.79415 0.99772 -0.17340 0.02028  -0.02193 222 ARG A CA  
2346 C C   . ARG A 343 ? 1.21709 1.68499 0.94153 -0.17606 0.01801  -0.04108 222 ARG A C   
2347 O O   . ARG A 343 ? 1.32339 1.79228 1.05271 -0.18470 0.00268  -0.04706 222 ARG A O   
2348 C CB  . ARG A 343 ? 1.31808 1.83040 1.04476 -0.17236 0.00928  0.01203  222 ARG A CB  
2349 C CG  . ARG A 343 ? 1.39897 1.94467 1.10370 -0.17269 0.00612  0.03368  222 ARG A CG  
2350 C CD  . ARG A 343 ? 1.43031 1.99649 1.10351 -0.18122 -0.00806 0.02379  222 ARG A CD  
2351 N NE  . ARG A 343 ? 1.46562 2.06348 1.11535 -0.18120 -0.01207 0.04666  222 ARG A NE  
2352 C CZ  . ARG A 343 ? 1.52584 2.14036 1.13509 -0.18049 -0.00207 0.04054  222 ARG A CZ  
2353 N NH1 . ARG A 343 ? 1.56435 2.16639 1.15330 -0.17952 0.01256  0.01089  222 ARG A NH1 
2354 N NH2 . ARG A 343 ? 1.53960 2.18221 1.12782 -0.18044 -0.00593 0.06425  222 ARG A NH2 
2355 N N   . SER A 344 ? 1.18224 1.62327 0.92070 -0.16870 0.03296  -0.04978 223 SER A N   
2356 C CA  . SER A 344 ? 1.22160 1.63026 0.97694 -0.17047 0.03381  -0.06836 223 SER A CA  
2357 C C   . SER A 344 ? 1.24696 1.64214 0.97881 -0.17349 0.04282  -0.10130 223 SER A C   
2358 O O   . SER A 344 ? 1.24979 1.61560 0.99364 -0.17489 0.04623  -0.11839 223 SER A O   
2359 C CB  . SER A 344 ? 1.01959 1.40434 0.80247 -0.16052 0.04380  -0.05909 223 SER A CB  
2360 O OG  . SER A 344 ? 0.98162 1.37695 0.78588 -0.15837 0.03576  -0.03025 223 SER A OG  
2361 N N   . HIS A 345 ? 1.30523 1.71970 1.00314 -0.17456 0.04753  -0.11055 224 HIS A N   
2362 C CA  . HIS A 345 ? 1.56043 1.96351 1.23197 -0.17839 0.05553  -0.14337 224 HIS A CA  
2363 C C   . HIS A 345 ? 1.80441 2.23192 1.44872 -0.19094 0.03951  -0.15227 224 HIS A C   
2364 O O   . HIS A 345 ? 1.79587 2.25301 1.43575 -0.19362 0.02598  -0.13078 224 HIS A O   
2365 C CB  . HIS A 345 ? 1.57106 1.97346 1.22270 -0.16790 0.07739  -0.15074 224 HIS A CB  
2366 C CG  . HIS A 345 ? 1.52923 1.90770 1.20766 -0.15525 0.09278  -0.14528 224 HIS A CG  
2367 N ND1 . HIS A 345 ? 1.51942 1.90496 1.22395 -0.14793 0.09213  -0.11630 224 HIS A ND1 
2368 C CD2 . HIS A 345 ? 1.55146 1.89908 1.23484 -0.14852 0.10843  -0.16487 224 HIS A CD2 
2369 C CE1 . HIS A 345 ? 1.46480 1.82673 1.18872 -0.13744 0.10550  -0.11841 224 HIS A CE1 
2370 N NE2 . HIS A 345 ? 1.49599 1.83455 1.20775 -0.13692 0.11581  -0.14681 224 HIS A NE2 
2371 N N   . LYS A 346 ? 2.05031 2.46471 1.67682 -0.19878 0.04049  -0.18409 225 LYS A N   
2372 C CA  . LYS A 346 ? 2.27699 2.71355 1.87769 -0.21196 0.02356  -0.19623 225 LYS A CA  
2373 C C   . LYS A 346 ? 2.37589 2.84046 1.93334 -0.20971 0.02769  -0.19461 225 LYS A C   
2374 O O   . LYS A 346 ? 2.42405 2.88990 1.97327 -0.19823 0.04559  -0.18580 225 LYS A O   
2375 C CB  . LYS A 346 ? 2.38145 2.79386 1.97695 -0.22205 0.02396  -0.23240 225 LYS A CB  
2376 C CG  . LYS A 346 ? 2.42141 2.79727 2.05517 -0.22108 0.02956  -0.23741 225 LYS A CG  
2377 C CD  . LYS A 346 ? 2.46870 2.81243 2.09206 -0.22524 0.04200  -0.27364 225 LYS A CD  
2378 C CE  . LYS A 346 ? 2.44447 2.75603 2.10339 -0.22974 0.04169  -0.28023 225 LYS A CE  
2379 N NZ  . LYS A 346 ? 2.42182 2.74807 2.09443 -0.24537 0.01956  -0.28158 225 LYS A NZ  
2380 N N   . GLU A 347 ? 2.43065 2.91908 1.96013 -0.22098 0.01074  -0.20295 226 GLU A N   
2381 C CA  . GLU A 347 ? 2.46781 2.98314 1.94996 -0.22041 0.01304  -0.20340 226 GLU A CA  
2382 C C   . GLU A 347 ? 2.57982 3.07639 2.03135 -0.21673 0.03568  -0.23421 226 GLU A C   
2383 O O   . GLU A 347 ? 2.57749 3.07217 2.02226 -0.20436 0.05693  -0.22680 226 GLU A O   
2384 C CB  . GLU A 347 ? 2.43696 2.98055 1.89576 -0.23401 -0.01272 -0.20753 226 GLU A CB  
2385 C CG  . GLU A 347 ? 2.36419 2.93622 1.84198 -0.23457 -0.03332 -0.17142 226 GLU A CG  
2386 C CD  . GLU A 347 ? 2.35400 2.95669 1.80089 -0.22828 -0.03142 -0.14628 226 GLU A CD  
2387 O OE1 . GLU A 347 ? 2.31071 2.91634 1.77922 -0.21846 -0.02399 -0.11590 226 GLU A OE1 
2388 O OE2 . GLU A 347 ? 2.38285 3.00627 1.78309 -0.23360 -0.03724 -0.15690 226 GLU A OE2 
2389 N N   . SER A 348 ? 2.68038 3.16294 2.11523 -0.22749 0.03168  -0.26919 227 SER A N   
2390 C CA  . SER A 348 ? 2.77565 3.23780 2.17988 -0.22498 0.05257  -0.30206 227 SER A CA  
2391 C C   . SER A 348 ? 2.77024 3.19504 2.20564 -0.21315 0.07565  -0.30678 227 SER A C   
2392 O O   . SER A 348 ? 2.77666 3.20077 2.21040 -0.19892 0.09619  -0.29617 227 SER A O   
2393 C CB  . SER A 348 ? 2.80809 3.26244 2.19058 -0.24124 0.04043  -0.33879 227 SER A CB  
2394 O OG  . SER A 348 ? 2.80466 3.29538 2.16051 -0.25240 0.01591  -0.33349 227 SER A OG  
2395 N N   . SER A 349 ? 2.77361 3.16803 2.23795 -0.21886 0.07254  -0.32211 228 SER A N   
2396 C CA  . SER A 349 ? 2.77779 3.13671 2.27523 -0.20751 0.09116  -0.32203 228 SER A CA  
2397 C C   . SER A 349 ? 2.89220 3.26102 2.42277 -0.19634 0.09122  -0.28352 228 SER A C   
2398 O O   . SER A 349 ? 2.83170 3.22500 2.37368 -0.20086 0.07271  -0.25901 228 SER A O   
2399 C CB  . SER A 349 ? 2.68919 3.01593 2.21207 -0.21730 0.08528  -0.34131 228 SER A CB  
2400 O OG  . SER A 349 ? 2.60836 2.90340 2.16648 -0.20615 0.09943  -0.33375 228 SER A OG  
2401 N N   . GLU A 350 ? 3.03557 3.38531 2.58208 -0.18144 0.11204  -0.27848 229 GLU A N   
2402 C CA  . GLU A 350 ? 3.09860 3.45456 2.67732 -0.17050 0.11371  -0.24470 229 GLU A CA  
2403 C C   . GLU A 350 ? 3.03853 3.35678 2.65381 -0.16511 0.11996  -0.24714 229 GLU A C   
2404 O O   . GLU A 350 ? 3.08301 3.38088 2.70525 -0.15259 0.13944  -0.25269 229 GLU A O   
2405 C CB  . GLU A 350 ? 3.16526 3.53790 2.73134 -0.15708 0.13194  -0.23287 229 GLU A CB  
2406 C CG  . GLU A 350 ? 3.18230 3.58975 2.75409 -0.15539 0.12297  -0.19727 229 GLU A CG  
2407 C CD  . GLU A 350 ? 3.21818 3.64300 2.77874 -0.14328 0.14262  -0.18622 229 GLU A CD  
2408 O OE1 . GLU A 350 ? 3.26684 3.69282 2.79419 -0.14092 0.15773  -0.20740 229 GLU A OE1 
2409 O OE2 . GLU A 350 ? 3.18876 3.62606 2.77428 -0.13646 0.14349  -0.15684 229 GLU A OE2 
2410 N N   . GLU A 351 ? 2.91799 3.22738 2.55670 -0.17406 0.10375  -0.24234 230 GLU A N   
2411 C CA  . GLU A 351 ? 2.78065 3.05289 2.45020 -0.17030 0.10924  -0.24539 230 GLU A CA  
2412 C C   . GLU A 351 ? 2.56869 2.84367 2.27120 -0.17116 0.09542  -0.21836 230 GLU A C   
2413 O O   . GLU A 351 ? 2.58068 2.85261 2.30305 -0.15974 0.10079  -0.19738 230 GLU A O   
2414 C CB  . GLU A 351 ? 2.84513 3.09054 2.50894 -0.18152 0.10892  -0.27718 230 GLU A CB  
2415 C CG  . GLU A 351 ? 2.88054 3.08210 2.56736 -0.17485 0.12221  -0.28541 230 GLU A CG  
2416 C CD  . GLU A 351 ? 2.91926 3.10861 2.60652 -0.15648 0.14332  -0.28253 230 GLU A CD  
2417 O OE1 . GLU A 351 ? 2.95765 3.15848 2.61876 -0.15198 0.15438  -0.29397 230 GLU A OE1 
2418 O OE2 . GLU A 351 ? 2.90362 3.07282 2.61744 -0.14623 0.14882  -0.26858 230 GLU A OE2 
2419 N N   . LEU A 352 ? 2.35066 2.63188 2.05999 -0.18458 0.07765  -0.21910 231 LEU A N   
2420 C CA  . LEU A 352 ? 2.10551 2.38446 1.84686 -0.18553 0.06637  -0.19709 231 LEU A CA  
2421 C C   . LEU A 352 ? 1.96919 2.27485 1.71113 -0.19881 0.04499  -0.19157 231 LEU A C   
2422 O O   . LEU A 352 ? 2.06852 2.38084 1.79403 -0.21049 0.03802  -0.21232 231 LEU A O   
2423 C CB  . LEU A 352 ? 2.08033 2.31863 1.84422 -0.18509 0.07323  -0.20694 231 LEU A CB  
2424 C CG  . LEU A 352 ? 2.05568 2.27562 1.81700 -0.19848 0.07125  -0.23479 231 LEU A CG  
2425 C CD1 . LEU A 352 ? 1.99741 2.22346 1.78135 -0.21010 0.05455  -0.22721 231 LEU A CD1 
2426 C CD2 . LEU A 352 ? 2.06258 2.23878 1.83010 -0.19268 0.08915  -0.25116 231 LEU A CD2 
2427 N N   . LYS A 353 ? 1.75080 2.07160 1.51277 -0.19678 0.03428  -0.16372 232 LYS A N   
2428 C CA  . LYS A 353 ? 1.60530 1.95046 1.37503 -0.20714 0.01388  -0.15431 232 LYS A CA  
2429 C C   . LYS A 353 ? 1.48148 1.82329 1.28365 -0.20246 0.00850  -0.12788 232 LYS A C   
2430 O O   . LYS A 353 ? 1.43827 1.77677 1.24689 -0.19157 0.01596  -0.11005 232 LYS A O   
2431 C CB  . LYS A 353 ? 1.61510 1.99939 1.35797 -0.20950 0.00423  -0.14631 232 LYS A CB  
2432 C CG  . LYS A 353 ? 1.63631 2.04699 1.38391 -0.22086 -0.01821 -0.14095 232 LYS A CG  
2433 C CD  . LYS A 353 ? 1.56275 2.01153 1.28098 -0.22197 -0.02785 -0.13044 232 LYS A CD  
2434 C CE  . LYS A 353 ? 1.49377 1.95723 1.22090 -0.21197 -0.02755 -0.09629 232 LYS A CE  
2435 N NZ  . LYS A 353 ? 1.43371 1.93548 1.13963 -0.21463 -0.04157 -0.08036 232 LYS A NZ  
2436 N N   . TYR A 354 ? 1.45384 1.79645 1.27725 -0.21083 -0.00402 -0.12619 233 TYR A N   
2437 C CA  . TYR A 354 ? 1.42121 1.76612 1.27236 -0.20696 -0.01091 -0.10038 233 TYR A CA  
2438 C C   . TYR A 354 ? 1.32490 1.70307 1.16849 -0.20339 -0.02003 -0.07625 233 TYR A C   
2439 O O   . TYR A 354 ? 1.43331 1.84073 1.26257 -0.20993 -0.03252 -0.07608 233 TYR A O   
2440 C CB  . TYR A 354 ? 1.37576 1.71988 1.25124 -0.21661 -0.02230 -0.10320 233 TYR A CB  
2441 C CG  . TYR A 354 ? 1.32785 1.67642 1.23076 -0.21246 -0.02960 -0.07701 233 TYR A CG  
2442 C CD1 . TYR A 354 ? 1.32463 1.64319 1.24833 -0.20670 -0.02066 -0.07113 233 TYR A CD1 
2443 C CD2 . TYR A 354 ? 1.33156 1.71316 1.23830 -0.21391 -0.04523 -0.05818 233 TYR A CD2 
2444 C CE1 . TYR A 354 ? 1.28363 1.60420 1.23052 -0.20293 -0.02647 -0.04912 233 TYR A CE1 
2445 C CE2 . TYR A 354 ? 1.34505 1.72833 1.27750 -0.20959 -0.05083 -0.03507 233 TYR A CE2 
2446 C CZ  . TYR A 354 ? 1.34032 1.69266 1.29252 -0.20434 -0.04112 -0.03159 233 TYR A CZ  
2447 O OH  . TYR A 354 ? 1.31392 1.66602 1.29006 -0.20015 -0.04596 -0.01048 233 TYR A OH  
2448 N N   . TYR A 355 ? 1.11925 1.49270 0.97244 -0.19334 -0.01418 -0.05550 234 TYR A N   
2449 C CA  . TYR A 355 ? 1.01623 1.41726 0.86688 -0.18978 -0.02124 -0.02982 234 TYR A CA  
2450 C C   . TYR A 355 ? 1.03445 1.42276 0.91430 -0.18372 -0.02175 -0.00816 234 TYR A C   
2451 O O   . TYR A 355 ? 1.00968 1.37185 0.89865 -0.17739 -0.01050 -0.01017 234 TYR A O   
2452 C CB  . TYR A 355 ? 1.01871 1.43015 0.84340 -0.18384 -0.00995 -0.02938 234 TYR A CB  
2453 C CG  . TYR A 355 ? 1.09348 1.53607 0.90985 -0.18183 -0.01604 -0.00453 234 TYR A CG  
2454 C CD1 . TYR A 355 ? 1.06598 1.53777 0.86670 -0.18858 -0.03020 -0.00048 234 TYR A CD1 
2455 C CD2 . TYR A 355 ? 1.12797 1.57113 0.95209 -0.17343 -0.00775 0.01523  234 TYR A CD2 
2456 C CE1 . TYR A 355 ? 1.01556 1.51451 0.80713 -0.18637 -0.03507 0.02392  234 TYR A CE1 
2457 C CE2 . TYR A 355 ? 1.08559 1.55578 0.90298 -0.17223 -0.01192 0.03880  234 TYR A CE2 
2458 C CZ  . TYR A 355 ? 1.07296 1.57012 0.87326 -0.17838 -0.02510 0.04370  234 TYR A CZ  
2459 O OH  . TYR A 355 ? 1.17077 1.69359 0.96311 -0.17679 -0.02864 0.06901  234 TYR A OH  
2460 N N   . ASP A 356 ? 1.10256 1.50838 0.99672 -0.18540 -0.03505 0.01205  235 ASP A N   
2461 C CA  . ASP A 356 ? 1.07833 1.47080 1.00058 -0.18074 -0.03657 0.03080  235 ASP A CA  
2462 C C   . ASP A 356 ? 1.11886 1.52387 1.03969 -0.17446 -0.03489 0.05434  235 ASP A C   
2463 O O   . ASP A 356 ? 1.16430 1.59738 1.07549 -0.17594 -0.04259 0.06838  235 ASP A O   
2464 C CB  . ASP A 356 ? 1.13389 1.53496 1.07713 -0.18566 -0.05073 0.03840  235 ASP A CB  
2465 C CG  . ASP A 356 ? 1.06711 1.44841 1.03899 -0.18102 -0.05023 0.05286  235 ASP A CG  
2466 O OD1 . ASP A 356 ? 1.01317 1.37652 0.98742 -0.17458 -0.04113 0.05881  235 ASP A OD1 
2467 O OD2 . ASP A 356 ? 1.11892 1.50305 1.11138 -0.18378 -0.05905 0.05774  235 ASP A OD2 
2468 N N   . LEU A 357 ? 1.08983 1.47431 1.02036 -0.16780 -0.02504 0.05896  236 LEU A N   
2469 C CA  . LEU A 357 ? 1.04676 1.44203 0.97903 -0.16274 -0.02217 0.07992  236 LEU A CA  
2470 C C   . LEU A 357 ? 1.05868 1.46687 1.00762 -0.16380 -0.03388 0.10487  236 LEU A C   
2471 O O   . LEU A 357 ? 1.13057 1.55889 1.07516 -0.16266 -0.03484 0.12360  236 LEU A O   
2472 C CB  . LEU A 357 ? 0.89792 1.26806 0.84177 -0.15614 -0.01187 0.07918  236 LEU A CB  
2473 C CG  . LEU A 357 ? 0.86337 1.24312 0.81327 -0.15152 -0.00780 0.09879  236 LEU A CG  
2474 C CD1 . LEU A 357 ? 0.84180 1.24536 0.76905 -0.15054 0.00020  0.09722  236 LEU A CD1 
2475 C CD2 . LEU A 357 ? 0.96714 1.32128 0.93187 -0.14570 -0.00115 0.09710  236 LEU A CD2 
2476 N N   . TYR A 358 ? 1.01552 1.41204 0.98422 -0.16572 -0.04181 0.10589  237 TYR A N   
2477 C CA  . TYR A 358 ? 1.07623 1.47864 1.06534 -0.16510 -0.05130 0.12910  237 TYR A CA  
2478 C C   . TYR A 358 ? 1.24013 1.66795 1.22835 -0.16933 -0.06470 0.13569  237 TYR A C   
2479 O O   . TYR A 358 ? 1.33696 1.77780 1.33584 -0.16802 -0.07242 0.15863  237 TYR A O   
2480 C CB  . TYR A 358 ? 1.09796 1.47048 1.11165 -0.16303 -0.05057 0.12815  237 TYR A CB  
2481 C CG  . TYR A 358 ? 1.07191 1.41832 1.08547 -0.15882 -0.03935 0.12025  237 TYR A CG  
2482 C CD1 . TYR A 358 ? 1.17143 1.51332 1.19347 -0.15510 -0.03692 0.13570  237 TYR A CD1 
2483 C CD2 . TYR A 358 ? 1.04191 1.36843 1.04791 -0.15872 -0.03177 0.09794  237 TYR A CD2 
2484 C CE1 . TYR A 358 ? 1.21012 1.53072 1.23310 -0.15110 -0.02868 0.12903  237 TYR A CE1 
2485 C CE2 . TYR A 358 ? 1.08600 1.38943 1.09169 -0.15383 -0.02267 0.09232  237 TYR A CE2 
2486 C CZ  . TYR A 358 ? 1.18750 1.48920 1.20168 -0.14988 -0.02188 0.10784  237 TYR A CZ  
2487 O OH  . TYR A 358 ? 1.10765 1.38876 1.12257 -0.14489 -0.01475 0.10266  237 TYR A OH  
2488 N N   . SER A 359 ? 1.31531 1.75055 1.29207 -0.17444 -0.06818 0.11661  238 SER A N   
2489 C CA  . SER A 359 ? 1.23699 1.69826 1.21406 -0.17893 -0.08294 0.12109  238 SER A CA  
2490 C C   . SER A 359 ? 1.25034 1.73967 1.19469 -0.18258 -0.08637 0.11621  238 SER A C   
2491 O O   . SER A 359 ? 1.41283 1.92945 1.35226 -0.18393 -0.09890 0.13098  238 SER A O   
2492 C CB  . SER A 359 ? 1.18059 1.63201 1.17357 -0.18361 -0.08699 0.10340  238 SER A CB  
2493 O OG  . SER A 359 ? 1.17247 1.60567 1.19653 -0.18021 -0.08722 0.11305  238 SER A OG  
2494 N N   . ASP A 360 ? 1.20841 1.69119 1.12913 -0.18376 -0.07542 0.09575  239 ASP A N   
2495 C CA  . ASP A 360 ? 1.04354 1.55084 0.92923 -0.18621 -0.07574 0.09117  239 ASP A CA  
2496 C C   . ASP A 360 ? 0.95976 1.47506 0.83457 -0.18037 -0.06701 0.11066  239 ASP A C   
2497 O O   . ASP A 360 ? 0.89290 1.43177 0.76144 -0.17981 -0.07451 0.13288  239 ASP A O   
2498 C CB  . ASP A 360 ? 1.13114 1.62690 0.99670 -0.18990 -0.06676 0.05926  239 ASP A CB  
2499 C CG  . ASP A 360 ? 1.37650 1.86260 1.25563 -0.19689 -0.07385 0.03962  239 ASP A CG  
2500 O OD1 . ASP A 360 ? 1.48897 1.97916 1.39390 -0.19833 -0.08543 0.05080  239 ASP A OD1 
2501 O OD2 . ASP A 360 ? 1.40056 1.87482 1.26601 -0.20096 -0.06708 0.01308  239 ASP A OD2 
2502 N N   . PHE A 361 ? 1.22287 1.71916 1.09649 -0.17594 -0.05092 0.10310  240 PHE A N   
2503 C CA  . PHE A 361 ? 1.09769 1.60136 0.96533 -0.17077 -0.04073 0.12000  240 PHE A CA  
2504 C C   . PHE A 361 ? 1.11313 1.62119 1.00423 -0.16858 -0.04731 0.15084  240 PHE A C   
2505 O O   . PHE A 361 ? 1.14514 1.67470 1.02636 -0.16789 -0.04792 0.17152  240 PHE A O   
2506 C CB  . PHE A 361 ? 1.20261 1.68231 1.07544 -0.16580 -0.02447 0.10702  240 PHE A CB  
2507 C CG  . PHE A 361 ? 1.27145 1.76069 1.13928 -0.16083 -0.01223 0.12049  240 PHE A CG  
2508 C CD1 . PHE A 361 ? 1.32608 1.82860 1.16518 -0.15954 -0.00068 0.10980  240 PHE A CD1 
2509 C CD2 . PHE A 361 ? 1.26945 1.75379 1.16254 -0.15772 -0.01139 0.14272  240 PHE A CD2 
2510 C CE1 . PHE A 361 ? 1.40352 1.91649 1.24090 -0.15485 0.01217  0.12247  240 PHE A CE1 
2511 C CE2 . PHE A 361 ? 1.29979 1.79446 1.19217 -0.15414 0.00007  0.15517  240 PHE A CE2 
2512 C CZ  . PHE A 361 ? 1.36581 1.87571 1.23124 -0.15247 0.01232  0.14560  240 PHE A CZ  
2513 N N   . GLY A 362 ? 1.17212 1.65849 1.09374 -0.16749 -0.05139 0.15419  241 GLY A N   
2514 C CA  . GLY A 362 ? 1.16399 1.64839 1.10972 -0.16504 -0.05542 0.18102  241 GLY A CA  
2515 C C   . GLY A 362 ? 1.27670 1.78569 1.22134 -0.16664 -0.06862 0.20267  241 GLY A C   
2516 O O   . GLY A 362 ? 1.22946 1.74955 1.17637 -0.16501 -0.06808 0.22715  241 GLY A O   
2517 N N   . LEU A 363 ? 1.22452 1.74275 1.16717 -0.16990 -0.08088 0.19478  242 LEU A N   
2518 C CA  . LEU A 363 ? 1.26604 1.80815 1.21035 -0.17046 -0.09561 0.21599  242 LEU A CA  
2519 C C   . LEU A 363 ? 1.27256 1.84381 1.18472 -0.17109 -0.09576 0.22861  242 LEU A C   
2520 O O   . LEU A 363 ? 1.23017 1.82116 1.14223 -0.17034 -0.10695 0.25173  242 LEU A O   
2521 C CB  . LEU A 363 ? 1.30501 1.85428 1.25461 -0.17423 -0.10927 0.20266  242 LEU A CB  
2522 C CG  . LEU A 363 ? 1.29439 1.82080 1.27983 -0.17326 -0.11196 0.19765  242 LEU A CG  
2523 C CD1 . LEU A 363 ? 1.24994 1.78961 1.24103 -0.17786 -0.12519 0.18520  242 LEU A CD1 
2524 C CD2 . LEU A 363 ? 1.27580 1.79469 1.28948 -0.16798 -0.11470 0.22467  242 LEU A CD2 
2525 N N   . ALA A 364 ? 1.29341 1.86750 1.17817 -0.17179 -0.08307 0.21486  243 ALA A N   
2526 C CA  . ALA A 364 ? 1.23529 1.83589 1.08617 -0.17215 -0.08013 0.22525  243 ALA A CA  
2527 C C   . ALA A 364 ? 1.26437 1.86529 1.12100 -0.16853 -0.06821 0.24936  243 ALA A C   
2528 O O   . ALA A 364 ? 1.33071 1.95208 1.15963 -0.16844 -0.06179 0.25885  243 ALA A O   
2529 C CB  . ALA A 364 ? 1.19414 1.79855 1.01100 -0.17465 -0.07128 0.19639  243 ALA A CB  
2530 N N   . LEU A 365 ? 1.32774 1.90669 1.21913 -0.16608 -0.06475 0.25896  244 LEU A N   
2531 C CA  . LEU A 365 ? 1.30673 1.88416 1.20914 -0.16400 -0.05379 0.28027  244 LEU A CA  
2532 C C   . LEU A 365 ? 1.25827 1.83966 1.18073 -0.16336 -0.06340 0.31240  244 LEU A C   
2533 O O   . LEU A 365 ? 1.34742 1.92375 1.28632 -0.16300 -0.07722 0.31598  244 LEU A O   
2534 C CB  . LEU A 365 ? 1.23512 1.78483 1.16241 -0.16222 -0.04361 0.26890  244 LEU A CB  
2535 C CG  . LEU A 365 ? 1.27089 1.81223 1.18402 -0.16121 -0.03192 0.23966  244 LEU A CG  
2536 C CD1 . LEU A 365 ? 1.14839 1.66055 1.08967 -0.15890 -0.02671 0.23124  244 LEU A CD1 
2537 C CD2 . LEU A 365 ? 1.31327 1.87452 1.20154 -0.16023 -0.01764 0.24192  244 LEU A CD2 
2538 N N   . GLY A 366 ? 1.25652 1.84671 1.17925 -0.16305 -0.05506 0.33609  245 GLY A N   
2539 C CA  . GLY A 366 ? 1.28678 1.87817 1.22936 -0.16247 -0.06149 0.36845  245 GLY A CA  
2540 C C   . GLY A 366 ? 1.42584 2.04679 1.34035 -0.16266 -0.06395 0.39146  245 GLY A C   
2541 O O   . GLY A 366 ? 1.33590 1.97754 1.21329 -0.16345 -0.06350 0.38092  245 GLY A O   
2542 N N   . THR A 367 ? 1.58057 2.20175 1.51272 -0.16196 -0.06649 0.42378  246 THR A N   
2543 C CA  . THR A 367 ? 1.71611 2.36332 1.62339 -0.16156 -0.06894 0.45088  246 THR A CA  
2544 C C   . THR A 367 ? 1.72324 2.38608 1.61548 -0.15961 -0.08868 0.45284  246 THR A C   
2545 O O   . THR A 367 ? 1.84215 2.52990 1.70301 -0.15906 -0.09236 0.46727  246 THR A O   
2546 C CB  . THR A 367 ? 1.79843 2.43853 1.73181 -0.16151 -0.06522 0.48604  246 THR A CB  
2547 O OG1 . THR A 367 ? 1.80833 2.43043 1.77549 -0.15897 -0.07899 0.49514  246 THR A OG1 
2548 C CG2 . THR A 367 ? 1.78806 2.41321 1.74203 -0.16449 -0.04762 0.48318  246 THR A CG2 
2549 N N   . HIS A 368 ? 1.55483 2.20392 1.46973 -0.15836 -0.10123 0.43810  247 HIS A N   
2550 C CA  . HIS A 368 ? 1.54355 2.20857 1.45028 -0.15684 -0.12092 0.43680  247 HIS A CA  
2551 C C   . HIS A 368 ? 1.44030 2.09619 1.35028 -0.15889 -0.12501 0.40001  247 HIS A C   
2552 O O   . HIS A 368 ? 1.28371 1.92465 1.22527 -0.15725 -0.13362 0.39448  247 HIS A O   
2553 C CB  . HIS A 368 ? 1.58340 2.24243 1.52351 -0.15222 -0.13351 0.46431  247 HIS A CB  
2554 C CG  . HIS A 368 ? 1.71550 2.38297 1.65262 -0.15000 -0.13076 0.50146  247 HIS A CG  
2555 N ND1 . HIS A 368 ? 1.72370 2.37295 1.67976 -0.15078 -0.11516 0.51490  247 HIS A ND1 
2556 C CD2 . HIS A 368 ? 1.77765 2.46144 1.70395 -0.14587 -0.13836 0.51748  247 HIS A CD2 
2557 C CE1 . HIS A 368 ? 1.72701 2.38135 1.68406 -0.14741 -0.11321 0.53782  247 HIS A CE1 
2558 N NE2 . HIS A 368 ? 1.76755 2.44232 1.70540 -0.14406 -0.12686 0.54064  247 HIS A NE2 
2559 N N   . PRO A 369 ? 1.46936 2.13281 1.34760 -0.16243 -0.11773 0.37424  248 PRO A N   
2560 C CA  . PRO A 369 ? 1.47321 2.12519 1.35488 -0.16500 -0.11973 0.33906  248 PRO A CA  
2561 C C   . PRO A 369 ? 1.55050 2.21683 1.43463 -0.16587 -0.14036 0.33453  248 PRO A C   
2562 O O   . PRO A 369 ? 1.69680 2.38972 1.56268 -0.16539 -0.15328 0.35127  248 PRO A O   
2563 C CB  . PRO A 369 ? 1.47592 2.13647 1.31830 -0.16813 -0.10747 0.31692  248 PRO A CB  
2564 C CG  . PRO A 369 ? 1.51534 2.18784 1.33995 -0.16667 -0.09556 0.34024  248 PRO A CG  
2565 C CD  . PRO A 369 ? 1.51065 2.19350 1.34738 -0.16406 -0.10686 0.37613  248 PRO A CD  
2566 N N   . ARG A 370 ? 1.48725 2.13645 1.39490 -0.16719 -0.14348 0.31216  249 ARG A N   
2567 C CA  . ARG A 370 ? 1.49750 2.16086 1.41233 -0.16893 -0.16212 0.30462  249 ARG A CA  
2568 C C   . ARG A 370 ? 1.64256 2.32104 1.52389 -0.17559 -0.16571 0.27557  249 ARG A C   
2569 O O   . ARG A 370 ? 1.71734 2.42228 1.58610 -0.17808 -0.18319 0.27637  249 ARG A O   
2570 C CB  . ARG A 370 ? 1.45083 2.08955 1.40922 -0.16743 -0.16322 0.29597  249 ARG A CB  
2571 C CG  . ARG A 370 ? 1.40449 2.02810 1.39715 -0.16098 -0.16214 0.32331  249 ARG A CG  
2572 C CD  . ARG A 370 ? 1.46350 2.07078 1.49602 -0.15899 -0.16731 0.31648  249 ARG A CD  
2573 N NE  . ARG A 370 ? 1.48260 2.09080 1.54427 -0.15234 -0.17554 0.34594  249 ARG A NE  
2574 C CZ  . ARG A 370 ? 1.45453 2.05645 1.55186 -0.14888 -0.18284 0.34667  249 ARG A CZ  
2575 N NH1 . ARG A 370 ? 1.40812 2.00337 1.51605 -0.15230 -0.18278 0.32001  249 ARG A NH1 
2576 N NH2 . ARG A 370 ? 1.41890 2.02066 1.54229 -0.14181 -0.18913 0.37435  249 ARG A NH2 
2577 N N   . ILE A 371 ? 1.63863 2.30068 1.50583 -0.17851 -0.15012 0.24972  250 ILE A N   
2578 C CA  . ILE A 371 ? 1.71829 2.39136 1.55047 -0.18482 -0.15052 0.22133  250 ILE A CA  
2579 C C   . ILE A 371 ? 1.73671 2.41825 1.52917 -0.18402 -0.13674 0.22397  250 ILE A C   
2580 O O   . ILE A 371 ? 1.74614 2.41475 1.54511 -0.17967 -0.12120 0.23639  250 ILE A O   
2581 C CB  . ILE A 371 ? 1.69707 2.34452 1.54244 -0.18855 -0.14277 0.18787  250 ILE A CB  
2582 C CG1 . ILE A 371 ? 1.69359 2.31319 1.54221 -0.18498 -0.12075 0.18161  250 ILE A CG1 
2583 C CG2 . ILE A 371 ? 1.68209 2.31959 1.56975 -0.18865 -0.15311 0.18797  250 ILE A CG2 
2584 C CD1 . ILE A 371 ? 1.66707 2.27235 1.49876 -0.18883 -0.10979 0.14705  250 ILE A CD1 
2585 N N   . GLU A 372 ? 1.72719 2.43162 1.47858 -0.18849 -0.14253 0.21220  251 GLU A N   
2586 C CA  . GLU A 372 ? 1.72937 2.44531 1.43898 -0.18752 -0.12942 0.21517  251 GLU A CA  
2587 C C   . GLU A 372 ? 1.75242 2.44855 1.44972 -0.18856 -0.10932 0.18477  251 GLU A C   
2588 O O   . GLU A 372 ? 1.73216 2.41790 1.42888 -0.19335 -0.11131 0.15421  251 GLU A O   
2589 C CB  . GLU A 372 ? 1.81004 2.55871 1.47627 -0.19153 -0.14408 0.21527  251 GLU A CB  
2590 C CG  . GLU A 372 ? 1.91469 2.68678 1.58694 -0.18912 -0.16390 0.24884  251 GLU A CG  
2591 C CD  . GLU A 372 ? 2.03578 2.83997 1.66494 -0.19356 -0.18134 0.24529  251 GLU A CD  
2592 O OE1 . GLU A 372 ? 2.08685 2.89294 1.68137 -0.19902 -0.17688 0.21497  251 GLU A OE1 
2593 O OE2 . GLU A 372 ? 2.07981 2.89614 1.71827 -0.18933 -0.19571 0.26846  251 GLU A OE2 
2594 N N   . ASP A 373 ? 1.77530 2.46634 1.46492 -0.18393 -0.08963 0.19391  252 ASP A N   
2595 C CA  . ASP A 373 ? 1.80675 2.48614 1.47660 -0.18346 -0.06965 0.16819  252 ASP A CA  
2596 C C   . ASP A 373 ? 1.87279 2.56605 1.51837 -0.17937 -0.05333 0.18572  252 ASP A C   
2597 O O   . ASP A 373 ? 1.82873 2.51912 1.49763 -0.17520 -0.04669 0.21213  252 ASP A O   
2598 C CB  . ASP A 373 ? 1.73328 2.37976 1.43961 -0.18087 -0.05874 0.15474  252 ASP A CB  
2599 C CG  . ASP A 373 ? 1.71376 2.34568 1.40254 -0.18166 -0.04490 0.11985  252 ASP A CG  
2600 O OD1 . ASP A 373 ? 1.73464 2.37594 1.39161 -0.17974 -0.03056 0.11417  252 ASP A OD1 
2601 O OD2 . ASP A 373 ? 1.70568 2.31597 1.41279 -0.18388 -0.04731 0.09848  252 ASP A OD2 
2602 N N   . GLU A 374 ? 1.99491 2.70298 1.59396 -0.18105 -0.04656 0.17063  253 GLU A N   
2603 C CA  . GLU A 374 ? 2.11315 2.83751 1.68411 -0.17743 -0.02987 0.18661  253 GLU A CA  
2604 C C   . GLU A 374 ? 1.92527 2.63296 1.52343 -0.17159 -0.00720 0.19111  253 GLU A C   
2605 O O   . GLU A 374 ? 1.86581 2.57954 1.47940 -0.16861 -0.00069 0.22109  253 GLU A O   
2606 C CB  . GLU A 374 ? 2.36143 3.09904 1.87763 -0.17995 -0.02375 0.16211  253 GLU A CB  
2607 C CG  . GLU A 374 ? 2.55705 3.30149 2.05305 -0.18740 -0.04578 0.14082  253 GLU A CG  
2608 C CD  . GLU A 374 ? 2.74943 3.50694 2.18755 -0.19058 -0.04030 0.11661  253 GLU A CD  
2609 O OE1 . GLU A 374 ? 2.82490 3.59602 2.23627 -0.18699 -0.03674 0.13142  253 GLU A OE1 
2610 O OE2 . GLU A 374 ? 2.80898 3.55172 2.23919 -0.19433 -0.03826 0.08045  253 GLU A OE2 
2611 N N   . GLU A 375 ? 1.81279 2.49935 1.41862 -0.17005 0.00459  0.16175  254 GLU A N   
2612 C CA  . GLU A 375 ? 1.71438 2.38767 1.34346 -0.16391 0.02597  0.16336  254 GLU A CA  
2613 C C   . GLU A 375 ? 1.61189 2.26650 1.29305 -0.16233 0.02063  0.17917  254 GLU A C   
2614 O O   . GLU A 375 ? 1.59713 2.25106 1.30027 -0.15863 0.03252  0.19751  254 GLU A O   
2615 C CB  . GLU A 375 ? 1.71379 2.37034 1.33257 -0.16170 0.03982  0.12709  254 GLU A CB  
2616 C CG  . GLU A 375 ? 1.79470 2.46624 1.36052 -0.16346 0.04616  0.10727  254 GLU A CG  
2617 C CD  . GLU A 375 ? 1.82208 2.48045 1.37872 -0.15803 0.06917  0.08009  254 GLU A CD  
2618 O OE1 . GLU A 375 ? 1.75516 2.39312 1.34783 -0.15274 0.07851  0.07680  254 GLU A OE1 
2619 O OE2 . GLU A 375 ? 1.95628 2.62432 1.46908 -0.15866 0.07770  0.06178  254 GLU A OE2 
2620 N N   . VAL A 376 ? 1.49791 2.13729 1.19958 -0.16541 0.00343  0.17154  255 VAL A N   
2621 C CA  . VAL A 376 ? 1.36142 1.98014 1.10956 -0.16377 -0.00089 0.18311  255 VAL A CA  
2622 C C   . VAL A 376 ? 1.40605 2.03657 1.17056 -0.16350 -0.00562 0.22005  255 VAL A C   
2623 O O   . VAL A 376 ? 1.31453 1.93416 1.11017 -0.16100 0.00109  0.23431  255 VAL A O   
2624 C CB  . VAL A 376 ? 1.07799 1.67963 0.84191 -0.16720 -0.01716 0.16751  255 VAL A CB  
2625 C CG1 . VAL A 376 ? 0.98125 1.56263 0.78932 -0.16547 -0.02213 0.18148  255 VAL A CG1 
2626 C CG2 . VAL A 376 ? 0.97005 1.55472 0.72345 -0.16751 -0.00985 0.13190  255 VAL A CG2 
2627 N N   . ASN A 377 ? 1.43225 2.08473 1.17640 -0.16623 -0.01776 0.23630  256 ASN A N   
2628 C CA  . ASN A 377 ? 1.46086 2.12274 1.22077 -0.16582 -0.02318 0.27271  256 ASN A CA  
2629 C C   . ASN A 377 ? 1.35469 2.02446 1.11559 -0.16351 -0.00419 0.29160  256 ASN A C   
2630 O O   . ASN A 377 ? 1.29750 1.96552 1.08464 -0.16332 -0.00487 0.31951  256 ASN A O   
2631 C CB  . ASN A 377 ? 1.58108 2.26726 1.31382 -0.16821 -0.03925 0.28648  256 ASN A CB  
2632 C CG  . ASN A 377 ? 1.63164 2.32092 1.38886 -0.16732 -0.05006 0.32204  256 ASN A CG  
2633 O OD1 . ASN A 377 ? 1.58328 2.25224 1.38120 -0.16604 -0.05026 0.33069  256 ASN A OD1 
2634 N ND2 . ASN A 377 ? 1.67996 2.39372 1.41141 -0.16778 -0.05916 0.34293  256 ASN A ND2 
2635 N N   . THR A 378 ? 1.36172 2.03996 1.09628 -0.16190 0.01343  0.27691  257 THR A N   
2636 C CA  . THR A 378 ? 1.46850 2.15749 1.20505 -0.15978 0.03316  0.29460  257 THR A CA  
2637 C C   . THR A 378 ? 1.41973 2.08919 1.20213 -0.15779 0.04159  0.29681  257 THR A C   
2638 O O   . THR A 378 ? 1.38733 2.06484 1.18413 -0.15736 0.05442  0.31739  257 THR A O   
2639 C CB  . THR A 378 ? 1.56289 2.26620 1.25931 -0.15768 0.05103  0.27620  257 THR A CB  
2640 O OG1 . THR A 378 ? 1.63298 2.34762 1.28664 -0.16023 0.03991  0.26233  257 THR A OG1 
2641 C CG2 . THR A 378 ? 1.51698 2.24168 1.20353 -0.15658 0.06905  0.30149  257 THR A CG2 
2642 N N   . LEU A 379 ? 1.49284 2.13743 1.29831 -0.15700 0.03441  0.27668  258 LEU A N   
2643 C CA  . LEU A 379 ? 1.39130 2.01688 1.23698 -0.15497 0.04070  0.27666  258 LEU A CA  
2644 C C   . LEU A 379 ? 1.20036 1.81948 1.07994 -0.15774 0.03135  0.30505  258 LEU A C   
2645 O O   . LEU A 379 ? 1.17961 1.79170 1.06485 -0.15980 0.01456  0.31162  258 LEU A O   
2646 C CB  . LEU A 379 ? 1.32688 1.92667 1.18267 -0.15309 0.03569  0.24725  258 LEU A CB  
2647 C CG  . LEU A 379 ? 1.25558 1.85525 1.08328 -0.15010 0.04594  0.21657  258 LEU A CG  
2648 C CD1 . LEU A 379 ? 1.12843 1.70088 0.96612 -0.14946 0.03823  0.19094  258 LEU A CD1 
2649 C CD2 . LEU A 379 ? 1.20187 1.80867 1.03240 -0.14505 0.06746  0.21452  258 LEU A CD2 
2650 N N   . SER A 380 ? 1.05190 1.67354 0.95570 -0.15789 0.04255  0.32160  259 SER A N   
2651 C CA  . SER A 380 ? 0.99097 1.60140 0.93108 -0.16106 0.03479  0.34495  259 SER A CA  
2652 C C   . SER A 380 ? 1.09980 1.67995 1.06697 -0.16035 0.02391  0.32924  259 SER A C   
2653 O O   . SER A 380 ? 1.07772 1.64617 1.03982 -0.15718 0.02554  0.30248  259 SER A O   
2654 C CB  . SER A 380 ? 0.92593 1.54608 0.88796 -0.16259 0.04974  0.36349  259 SER A CB  
2655 O OG  . SER A 380 ? 0.83134 1.45099 0.79926 -0.15894 0.06311  0.34426  259 SER A OG  
2656 N N   . VAL A 381 ? 1.08097 1.64700 1.07643 -0.16315 0.01360  0.34635  260 VAL A N   
2657 C CA  . VAL A 381 ? 1.10377 1.64046 1.12157 -0.16255 0.00281  0.33301  260 VAL A CA  
2658 C C   . VAL A 381 ? 1.15332 1.67586 1.20725 -0.16596 -0.00119 0.35323  260 VAL A C   
2659 O O   . VAL A 381 ? 1.20896 1.73970 1.26882 -0.16888 -0.00350 0.37911  260 VAL A O   
2660 C CB  . VAL A 381 ? 1.06332 1.59420 1.06692 -0.16176 -0.01118 0.32370  260 VAL A CB  
2661 C CG1 . VAL A 381 ? 1.08288 1.63092 1.07748 -0.16350 -0.01860 0.34862  260 VAL A CG1 
2662 C CG2 . VAL A 381 ? 1.01108 1.51155 1.03971 -0.16130 -0.02096 0.31415  260 VAL A CG2 
2663 N N   . ALA A 382 ? 1.21956 1.71981 1.29671 -0.16564 -0.00207 0.34112  261 ALA A N   
2664 C CA  . ALA A 382 ? 1.15512 1.63670 1.26623 -0.16936 -0.00741 0.35434  261 ALA A CA  
2665 C C   . ALA A 382 ? 1.08787 1.53913 1.20779 -0.16760 -0.01866 0.33819  261 ALA A C   
2666 O O   . ALA A 382 ? 0.99086 1.43237 1.10078 -0.16394 -0.01813 0.31422  261 ALA A O   
2667 C CB  . ALA A 382 ? 1.01593 1.49999 1.14836 -0.17148 0.00180  0.35600  261 ALA A CB  
2668 N N   . ILE A 383 ? 1.15752 1.59315 1.29586 -0.16989 -0.02768 0.35179  262 ILE A N   
2669 C CA  . ILE A 383 ? 1.14591 1.55193 1.29443 -0.16828 -0.03709 0.33915  262 ILE A CA  
2670 C C   . ILE A 383 ? 1.12713 1.51147 1.30491 -0.17210 -0.03889 0.34459  262 ILE A C   
2671 O O   . ILE A 383 ? 1.16193 1.54604 1.35789 -0.17636 -0.04012 0.36646  262 ILE A O   
2672 C CB  . ILE A 383 ? 1.10672 1.51121 1.25311 -0.16682 -0.04616 0.34840  262 ILE A CB  
2673 C CG1 . ILE A 383 ? 1.02642 1.45581 1.14333 -0.16431 -0.04616 0.34374  262 ILE A CG1 
2674 C CG2 . ILE A 383 ? 1.11889 1.49318 1.27647 -0.16464 -0.05343 0.33417  262 ILE A CG2 
2675 C CD1 . ILE A 383 ? 0.99675 1.42583 1.09401 -0.16185 -0.04191 0.31548  262 ILE A CD1 
2676 N N   . LEU A 384 ? 1.08486 1.45024 1.26671 -0.17085 -0.03943 0.32491  263 LEU A N   
2677 C CA  . LEU A 384 ? 1.07588 1.42154 1.28289 -0.17499 -0.04234 0.32712  263 LEU A CA  
2678 C C   . LEU A 384 ? 0.98147 1.29334 1.19396 -0.17356 -0.05071 0.31581  263 LEU A C   
2679 O O   . LEU A 384 ? 1.11324 1.41318 1.31127 -0.16889 -0.05148 0.29528  263 LEU A O   
2680 C CB  . LEU A 384 ? 1.02308 1.37429 1.23222 -0.17471 -0.03719 0.31556  263 LEU A CB  
2681 C CG  . LEU A 384 ? 1.01353 1.39842 1.21720 -0.17492 -0.02623 0.32365  263 LEU A CG  
2682 C CD1 . LEU A 384 ? 1.03679 1.42532 1.24786 -0.17339 -0.02183 0.31174  263 LEU A CD1 
2683 C CD2 . LEU A 384 ? 0.97015 1.36987 1.19039 -0.18152 -0.02353 0.35096  263 LEU A CD2 
2684 N N   . PRO A 385 ? 0.90667 1.20148 1.13907 -0.17724 -0.05594 0.32850  264 PRO A N   
2685 C CA  . PRO A 385 ? 0.80320 1.06319 1.04215 -0.17627 -0.06222 0.31606  264 PRO A CA  
2686 C C   . PRO A 385 ? 0.94195 1.18827 1.18306 -0.17766 -0.06330 0.30035  264 PRO A C   
2687 O O   . PRO A 385 ? 1.01442 1.27289 1.26711 -0.18221 -0.06166 0.30636  264 PRO A O   
2688 C CB  . PRO A 385 ? 0.86876 1.11585 1.13105 -0.18078 -0.06592 0.33515  264 PRO A CB  
2689 C CG  . PRO A 385 ? 0.89670 1.17278 1.16202 -0.18306 -0.06198 0.35908  264 PRO A CG  
2690 C CD  . PRO A 385 ? 0.80156 1.10642 1.05160 -0.18262 -0.05516 0.35473  264 PRO A CD  
2691 N N   . LEU A 386 ? 0.95624 1.17823 1.18665 -0.17360 -0.06604 0.28081  265 LEU A N   
2692 C CA  . LEU A 386 ? 0.82640 1.03365 1.05596 -0.17398 -0.06858 0.26609  265 LEU A CA  
2693 C C   . LEU A 386 ? 0.87688 1.05808 1.12488 -0.17978 -0.07567 0.26874  265 LEU A C   
2694 O O   . LEU A 386 ? 0.86440 1.01974 1.11187 -0.17856 -0.07830 0.26479  265 LEU A O   
2695 C CB  . LEU A 386 ? 0.93664 1.12803 1.14406 -0.16715 -0.06763 0.24476  265 LEU A CB  
2696 C CG  . LEU A 386 ? 0.95154 1.12861 1.15418 -0.16603 -0.07058 0.23022  265 LEU A CG  
2697 C CD1 . LEU A 386 ? 0.80913 1.01309 1.01772 -0.16684 -0.06804 0.23420  265 LEU A CD1 
2698 C CD2 . LEU A 386 ? 0.79828 0.95871 0.97782 -0.15911 -0.06808 0.21138  265 LEU A CD2 
2699 N N   . PRO A 387 ? 0.86095 1.04793 1.12641 -0.18632 -0.07862 0.27468  266 PRO A N   
2700 C CA  . PRO A 387 ? 0.80187 0.96396 1.08603 -0.19356 -0.08616 0.27683  266 PRO A CA  
2701 C C   . PRO A 387 ? 0.86661 0.99511 1.13685 -0.19071 -0.09203 0.25604  266 PRO A C   
2702 O O   . PRO A 387 ? 0.97116 1.09940 1.22917 -0.18769 -0.09410 0.24245  266 PRO A O   
2703 C CB  . PRO A 387 ? 0.82117 1.00293 1.12601 -0.20108 -0.08784 0.28508  266 PRO A CB  
2704 C CG  . PRO A 387 ? 0.78667 1.00593 1.08710 -0.19796 -0.07844 0.29446  266 PRO A CG  
2705 C CD  . PRO A 387 ? 0.77034 0.98871 1.04173 -0.18791 -0.07450 0.28053  266 PRO A CD  
2706 N N   . GLY A 388 ? 0.92843 1.02780 1.20033 -0.19121 -0.09420 0.25421  267 GLY A N   
2707 C CA  . GLY A 388 ? 0.82393 0.89023 1.07824 -0.18749 -0.09736 0.23458  267 GLY A CA  
2708 C C   . GLY A 388 ? 0.79992 0.86755 1.02835 -0.17801 -0.09164 0.22182  267 GLY A C   
2709 O O   . GLY A 388 ? 1.05125 1.09834 1.26146 -0.17465 -0.09353 0.20515  267 GLY A O   
2710 N N   . GLY A 389 ? 0.92208 1.01342 1.14780 -0.17409 -0.08486 0.22939  268 GLY A N   
2711 C CA  . GLY A 389 ? 0.91100 1.00580 1.11430 -0.16650 -0.07932 0.21705  268 GLY A CA  
2712 C C   . GLY A 389 ? 0.94017 1.00400 1.13144 -0.16211 -0.07750 0.20419  268 GLY A C   
2713 O O   . GLY A 389 ? 0.90568 0.95499 1.10739 -0.16266 -0.07741 0.20914  268 GLY A O   
2714 N N   . GLU A 390 ? 0.95275 1.00596 1.12254 -0.15729 -0.07501 0.18801  269 GLU A N   
2715 C CA  . GLU A 390 ? 0.91062 0.93830 1.06592 -0.15241 -0.07025 0.17516  269 GLU A CA  
2716 C C   . GLU A 390 ? 0.81664 0.85587 0.95527 -0.14730 -0.06345 0.16647  269 GLU A C   
2717 O O   . GLU A 390 ? 0.88857 0.94539 1.02095 -0.14663 -0.06341 0.16523  269 GLU A O   
2718 C CB  . GLU A 390 ? 0.99293 0.98664 1.13536 -0.15241 -0.07387 0.16246  269 GLU A CB  
2719 C CG  . GLU A 390 ? 0.97962 0.95801 1.13680 -0.15855 -0.08137 0.16766  269 GLU A CG  
2720 C CD  . GLU A 390 ? 1.14956 1.10132 1.29128 -0.15973 -0.08790 0.15482  269 GLU A CD  
2721 O OE1 . GLU A 390 ? 1.18275 1.13516 1.33593 -0.16628 -0.09732 0.15863  269 GLU A OE1 
2722 O OE2 . GLU A 390 ? 1.10035 1.03094 1.21824 -0.15441 -0.08379 0.14119  269 GLU A OE2 
2723 N N   . PHE A 391 ? 0.90792 0.93611 1.04074 -0.14375 -0.05708 0.15978  270 PHE A N   
2724 C CA  . PHE A 391 ? 0.84948 0.88633 0.96872 -0.14015 -0.05020 0.15075  270 PHE A CA  
2725 C C   . PHE A 391 ? 0.90750 0.91553 1.01480 -0.13660 -0.04342 0.13778  270 PHE A C   
2726 O O   . PHE A 391 ? 1.08033 1.07220 1.19605 -0.13625 -0.04203 0.13899  270 PHE A O   
2727 C CB  . PHE A 391 ? 0.76902 0.83644 0.89909 -0.14094 -0.04871 0.15953  270 PHE A CB  
2728 C CG  . PHE A 391 ? 0.73501 0.79902 0.88034 -0.14045 -0.04793 0.16557  270 PHE A CG  
2729 C CD1 . PHE A 391 ? 0.74081 0.80434 0.90478 -0.14251 -0.05290 0.17969  270 PHE A CD1 
2730 C CD2 . PHE A 391 ? 0.77684 0.83824 0.92030 -0.13782 -0.04184 0.15749  270 PHE A CD2 
2731 C CE1 . PHE A 391 ? 0.87518 0.93517 1.05522 -0.14063 -0.05188 0.18601  270 PHE A CE1 
2732 C CE2 . PHE A 391 ? 0.74429 0.80470 0.90531 -0.13640 -0.04109 0.16357  270 PHE A CE2 
2733 C CZ  . PHE A 391 ? 0.81071 0.87021 0.98983 -0.13713 -0.04614 0.17802  270 PHE A CZ  
2734 N N   . TYR A 392 ? 0.93677 0.93750 1.02490 -0.13367 -0.03806 0.12572  271 TYR A N   
2735 C CA  . TYR A 392 ? 0.88207 0.85535 0.95680 -0.13048 -0.02967 0.11370  271 TYR A CA  
2736 C C   . TYR A 392 ? 0.81662 0.79879 0.88207 -0.12899 -0.02201 0.10555  271 TYR A C   
2737 O O   . TYR A 392 ? 0.91681 0.90333 0.96988 -0.12770 -0.02225 0.10158  271 TYR A O   
2738 C CB  . TYR A 392 ? 0.86968 0.81186 0.92510 -0.12858 -0.03140 0.10628  271 TYR A CB  
2739 C CG  . TYR A 392 ? 0.88501 0.81736 0.94892 -0.13143 -0.04015 0.11231  271 TYR A CG  
2740 C CD1 . TYR A 392 ? 0.95571 0.86609 1.02407 -0.13138 -0.03748 0.11103  271 TYR A CD1 
2741 C CD2 . TYR A 392 ? 0.91373 0.85883 0.98317 -0.13443 -0.05044 0.11890  271 TYR A CD2 
2742 C CE1 . TYR A 392 ? 1.08108 0.98005 1.15745 -0.13467 -0.04526 0.11526  271 TYR A CE1 
2743 C CE2 . TYR A 392 ? 0.95952 0.89529 1.03884 -0.13852 -0.05871 0.12384  271 TYR A CE2 
2744 C CZ  . TYR A 392 ? 0.91524 0.82681 0.99720 -0.13884 -0.05631 0.12157  271 TYR A CZ  
2745 O OH  . TYR A 392 ? 0.89616 0.79592 0.98803 -0.14354 -0.06431 0.12521  271 TYR A OH  
2746 N N   . HIS A 393 ? 0.87617 0.86125 0.94954 -0.12923 -0.01523 0.10293  272 HIS A N   
2747 C CA  . HIS A 393 ? 0.78321 0.77825 0.85110 -0.12957 -0.00851 0.09479  272 HIS A CA  
2748 C C   . HIS A 393 ? 0.85931 0.82487 0.90533 -0.12661 0.00033  0.08241  272 HIS A C   
2749 O O   . HIS A 393 ? 0.90072 0.83775 0.93740 -0.12426 0.00357  0.07942  272 HIS A O   
2750 C CB  . HIS A 393 ? 0.82375 0.83308 0.91014 -0.13155 -0.00522 0.09601  272 HIS A CB  
2751 C CG  . HIS A 393 ? 0.83424 0.87735 0.93853 -0.13418 -0.01384 0.10823  272 HIS A CG  
2752 N ND1 . HIS A 393 ? 0.99184 1.06272 1.09391 -0.13672 -0.01665 0.10828  272 HIS A ND1 
2753 C CD2 . HIS A 393 ? 0.89964 0.95206 1.02275 -0.13434 -0.01990 0.12129  272 HIS A CD2 
2754 C CE1 . HIS A 393 ? 0.97901 1.07582 1.09589 -0.13842 -0.02433 0.12141  272 HIS A CE1 
2755 N NE2 . HIS A 393 ? 0.97211 1.05821 1.10301 -0.13688 -0.02652 0.13024  272 HIS A NE2 
2756 N N   . TYR A 394 ? 0.82249 0.79390 0.85892 -0.12662 0.00474  0.07519  273 TYR A N   
2757 C CA  . TYR A 394 ? 0.86662 0.81037 0.88302 -0.12380 0.01435  0.06466  273 TYR A CA  
2758 C C   . TYR A 394 ? 0.99674 0.94860 1.01435 -0.12642 0.02278  0.05604  273 TYR A C   
2759 O O   . TYR A 394 ? 1.09061 1.02685 1.09196 -0.12433 0.02942  0.04838  273 TYR A O   
2760 C CB  . TYR A 394 ? 1.03136 0.96290 1.02889 -0.11934 0.01010  0.06445  273 TYR A CB  
2761 C CG  . TYR A 394 ? 1.00264 0.95939 1.00277 -0.11907 0.00460  0.06681  273 TYR A CG  
2762 C CD1 . TYR A 394 ? 1.08397 1.04621 1.07838 -0.11864 0.01122  0.05908  273 TYR A CD1 
2763 C CD2 . TYR A 394 ? 1.18281 1.15681 1.19157 -0.11934 -0.00611 0.07638  273 TYR A CD2 
2764 C CE1 . TYR A 394 ? 1.25110 1.23532 1.24699 -0.11759 0.00788  0.06023  273 TYR A CE1 
2765 C CE2 . TYR A 394 ? 1.10196 1.09970 1.11366 -0.11864 -0.00916 0.07875  273 TYR A CE2 
2766 C CZ  . TYR A 394 ? 1.06531 1.06794 1.06977 -0.11728 -0.00186 0.07033  273 TYR A CZ  
2767 O OH  . TYR A 394 ? 1.08123 1.10649 1.08779 -0.11585 -0.00326 0.07166  273 TYR A OH  
2768 N N   . GLY A 395 ? 0.82128 0.79648 0.85855 -0.13114 0.02231  0.05714  274 GLY A N   
2769 C CA  . GLY A 395 ? 0.67835 0.66202 0.71882 -0.13526 0.02913  0.04769  274 GLY A CA  
2770 C C   . GLY A 395 ? 0.64991 0.61069 0.69048 -0.13636 0.04199  0.03982  274 GLY A C   
2771 O O   . GLY A 395 ? 0.99176 0.95179 1.03144 -0.13996 0.04943  0.03029  274 GLY A O   
2772 N N   . THR A 396 ? 0.70481 0.64658 0.74695 -0.13372 0.04571  0.04317  275 THR A N   
2773 C CA  . THR A 396 ? 0.81496 0.73667 0.85958 -0.13461 0.05967  0.03700  275 THR A CA  
2774 C C   . THR A 396 ? 0.84348 0.72719 0.86381 -0.12889 0.06653  0.03624  275 THR A C   
2775 O O   . THR A 396 ? 0.74974 0.62530 0.75632 -0.12473 0.05823  0.04115  275 THR A O   
2776 C CB  . THR A 396 ? 0.75496 0.69253 0.82825 -0.13675 0.05995  0.04114  275 THR A CB  
2777 O OG1 . THR A 396 ? 0.81755 0.74544 0.89143 -0.13204 0.05582  0.04912  275 THR A OG1 
2778 C CG2 . THR A 396 ? 0.68577 0.66347 0.78075 -0.14160 0.04915  0.04452  275 THR A CG2 
2779 N N   . SER A 397 ? 0.74180 0.60271 0.75690 -0.12919 0.08186  0.03004  276 SER A N   
2780 C CA  . SER A 397 ? 0.86776 0.69071 0.85518 -0.12382 0.09008  0.02875  276 SER A CA  
2781 C C   . SER A 397 ? 1.05520 0.86884 1.04181 -0.12011 0.08602  0.03386  276 SER A C   
2782 O O   . SER A 397 ? 1.09553 0.89202 1.05969 -0.11581 0.07925  0.03602  276 SER A O   
2783 C CB  . SER A 397 ? 0.87040 0.67363 0.85550 -0.12576 0.10931  0.02211  276 SER A CB  
2784 O OG  . SER A 397 ? 0.76995 0.58004 0.75724 -0.13014 0.11301  0.01655  276 SER A OG  
2785 N N   . LYS A 398 ? 0.97229 0.79674 0.98442 -0.12171 0.08995  0.03542  277 LYS A N   
2786 C CA  . LYS A 398 ? 0.98124 0.79785 0.99695 -0.11826 0.08645  0.03988  277 LYS A CA  
2787 C C   . LYS A 398 ? 0.81932 0.64682 0.83178 -0.11748 0.06819  0.04666  277 LYS A C   
2788 O O   . LYS A 398 ? 0.92032 0.72868 0.91867 -0.11441 0.06381  0.04798  277 LYS A O   
2789 C CB  . LYS A 398 ? 1.04291 0.87905 1.09445 -0.11972 0.09028  0.04264  277 LYS A CB  
2790 C CG  . LYS A 398 ? 1.30096 1.11310 1.35300 -0.11535 0.10218  0.04102  277 LYS A CG  
2791 C CD  . LYS A 398 ? 1.27289 1.10480 1.36314 -0.11628 0.11001  0.04255  277 LYS A CD  
2792 C CE  . LYS A 398 ? 1.31262 1.12100 1.40558 -0.11075 0.12317  0.04083  277 LYS A CE  
2793 N NZ  . LYS A 398 ? 1.22398 0.99900 1.29059 -0.10919 0.14263  0.03213  277 LYS A NZ  
2794 N N   . GLU A 399 ? 0.83228 0.69044 0.85740 -0.12075 0.05778  0.05054  278 GLU A N   
2795 C CA  . GLU A 399 ? 0.97267 0.84443 0.99797 -0.12060 0.04189  0.05806  278 GLU A CA  
2796 C C   . GLU A 399 ? 0.87113 0.72370 0.86706 -0.11773 0.03782  0.05572  278 GLU A C   
2797 O O   . GLU A 399 ? 0.97262 0.82054 0.96314 -0.11656 0.02763  0.06011  278 GLU A O   
2798 C CB  . GLU A 399 ? 0.94651 0.85646 0.99104 -0.12453 0.03350  0.06296  278 GLU A CB  
2799 C CG  . GLU A 399 ? 0.96260 0.89611 1.03763 -0.12653 0.03074  0.06996  278 GLU A CG  
2800 C CD  . GLU A 399 ? 1.08131 1.05217 1.17064 -0.13060 0.02293  0.07393  278 GLU A CD  
2801 O OE1 . GLU A 399 ? 1.05916 1.05263 1.17254 -0.13193 0.01837  0.08143  278 GLU A OE1 
2802 O OE2 . GLU A 399 ? 1.12763 1.10489 1.20338 -0.13199 0.02140  0.06965  278 GLU A OE2 
2803 N N   . LEU A 400 ? 0.86073 0.70269 0.83921 -0.11666 0.04497  0.04934  279 LEU A N   
2804 C CA  . LEU A 400 ? 0.85794 0.67912 0.80815 -0.11239 0.04139  0.04799  279 LEU A CA  
2805 C C   . LEU A 400 ? 1.00647 0.79890 0.93931 -0.10944 0.04051  0.04763  279 LEU A C   
2806 O O   . LEU A 400 ? 0.93671 0.72727 0.86228 -0.10830 0.02784  0.05112  279 LEU A O   
2807 C CB  . LEU A 400 ? 1.05401 0.85936 0.98675 -0.11063 0.05285  0.04143  279 LEU A CB  
2808 C CG  . LEU A 400 ? 0.97551 0.75833 0.87826 -0.10476 0.04966  0.04111  279 LEU A CG  
2809 C CD1 . LEU A 400 ? 0.85965 0.66454 0.76734 -0.10347 0.03573  0.04558  279 LEU A CD1 
2810 C CD2 . LEU A 400 ? 0.93661 0.69733 0.82184 -0.10267 0.06403  0.03570  279 LEU A CD2 
2811 N N   . ILE A 401 ? 1.04242 0.81442 0.97141 -0.10885 0.05378  0.04322  280 ILE A N   
2812 C CA  . ILE A 401 ? 0.97656 0.71770 0.88407 -0.10579 0.05478  0.04081  280 ILE A CA  
2813 C C   . ILE A 401 ? 1.07141 0.82116 0.99443 -0.10750 0.04252  0.04538  280 ILE A C   
2814 O O   . ILE A 401 ? 1.20026 0.93790 1.10756 -0.10666 0.03138  0.04572  280 ILE A O   
2815 C CB  . ILE A 401 ? 0.88926 0.60728 0.79012 -0.10445 0.07429  0.03491  280 ILE A CB  
2816 C CG1 . ILE A 401 ? 0.84168 0.54581 0.72357 -0.10312 0.08676  0.03113  280 ILE A CG1 
2817 C CG2 . ILE A 401 ? 0.92266 0.60928 0.80066 -0.10133 0.07584  0.03136  280 ILE A CG2 
2818 C CD1 . ILE A 401 ? 1.01581 0.70222 0.89684 -0.10304 0.10825  0.02631  280 ILE A CD1 
2819 N N   . SER A 402 ? 1.02642 0.79760 0.98157 -0.11016 0.04359  0.04945  281 SER A N   
2820 C CA  . SER A 402 ? 1.05034 0.82505 1.02119 -0.11138 0.03448  0.05441  281 SER A CA  
2821 C C   . SER A 402 ? 1.09608 0.89048 1.07290 -0.11412 0.01664  0.06174  281 SER A C   
2822 O O   . SER A 402 ? 1.17507 0.96009 1.14996 -0.11522 0.00712  0.06346  281 SER A O   
2823 C CB  . SER A 402 ? 0.98006 0.77357 0.98504 -0.11239 0.04006  0.05880  281 SER A CB  
2824 O OG  . SER A 402 ? 0.96696 0.79047 0.98876 -0.11477 0.04080  0.06168  281 SER A OG  
2825 N N   . SER A 403 ? 1.06018 0.88150 1.04469 -0.11560 0.01257  0.06556  282 SER A N   
2826 C CA  . SER A 403 ? 1.02390 0.86581 1.01481 -0.11782 -0.00209 0.07273  282 SER A CA  
2827 C C   . SER A 403 ? 1.03521 0.85850 1.00076 -0.11588 -0.00969 0.06943  282 SER A C   
2828 O O   . SER A 403 ? 0.93342 0.76219 0.90436 -0.11825 -0.02244 0.07425  282 SER A O   
2829 C CB  . SER A 403 ? 0.97154 0.84480 0.97359 -0.11907 -0.00222 0.07583  282 SER A CB  
2830 O OG  . SER A 403 ? 1.01807 0.91656 1.04700 -0.12201 -0.00217 0.08243  282 SER A OG  
2831 N N   . THR A 404 ? 1.14040 0.94223 1.07910 -0.11176 -0.00264 0.06203  283 THR A N   
2832 C CA  . THR A 404 ? 1.12023 0.90449 1.03422 -0.10922 -0.01171 0.05994  283 THR A CA  
2833 C C   . THR A 404 ? 1.15828 0.91760 1.06164 -0.11041 -0.01636 0.05673  283 THR A C   
2834 O O   . THR A 404 ? 1.15133 0.90830 1.04913 -0.11179 -0.03060 0.05790  283 THR A O   
2835 C CB  . THR A 404 ? 0.96465 0.72949 0.85040 -0.10376 -0.00325 0.05440  283 THR A CB  
2836 O OG1 . THR A 404 ? 1.34260 1.08011 1.21308 -0.10227 0.01153  0.04798  283 THR A OG1 
2837 C CG2 . THR A 404 ? 0.85664 0.64372 0.75297 -0.10293 0.00140  0.05604  283 THR A CG2 
2838 N N   . LEU A 405 ? 1.25672 0.99808 1.15904 -0.11017 -0.00460 0.05219  284 LEU A N   
2839 C CA  . LEU A 405 ? 1.24531 0.96255 1.13926 -0.11145 -0.00808 0.04801  284 LEU A CA  
2840 C C   . LEU A 405 ? 1.21484 0.95019 1.13572 -0.11700 -0.02217 0.05504  284 LEU A C   
2841 O O   . LEU A 405 ? 1.15614 0.87969 1.06822 -0.11966 -0.03454 0.05307  284 LEU A O   
2842 C CB  . LEU A 405 ? 1.16354 0.86227 1.05811 -0.10954 0.00904  0.04266  284 LEU A CB  
2843 C CG  . LEU A 405 ? 1.28575 0.95669 1.17106 -0.11029 0.00759  0.03665  284 LEU A CG  
2844 C CD1 . LEU A 405 ? 1.30153 0.94467 1.14658 -0.10921 -0.00025 0.02913  284 LEU A CD1 
2845 C CD2 . LEU A 405 ? 1.28592 0.93998 1.17477 -0.10717 0.02662  0.03149  284 LEU A CD2 
2846 N N   . SER A 406 ? 1.23164 0.99601 1.18540 -0.11928 -0.02085 0.06365  285 SER A N   
2847 C CA  . SER A 406 ? 1.32725 1.10824 1.30793 -0.12455 -0.03206 0.07238  285 SER A CA  
2848 C C   . SER A 406 ? 1.30901 1.10615 1.29061 -0.12778 -0.04756 0.07716  285 SER A C   
2849 O O   . SER A 406 ? 1.32891 1.12378 1.31909 -0.13272 -0.05896 0.07970  285 SER A O   
2850 C CB  . SER A 406 ? 1.40290 1.21279 1.41533 -0.12542 -0.02718 0.08200  285 SER A CB  
2851 O OG  . SER A 406 ? 1.42703 1.22423 1.44489 -0.12247 -0.01413 0.07861  285 SER A OG  
2852 N N   . VAL A 407 ? 1.21324 1.02669 1.18810 -0.12514 -0.04773 0.07823  286 VAL A N   
2853 C CA  . VAL A 407 ? 1.07568 0.90684 1.05417 -0.12698 -0.06111 0.08302  286 VAL A CA  
2854 C C   . VAL A 407 ? 1.34498 1.15116 1.29957 -0.12676 -0.07126 0.07606  286 VAL A C   
2855 O O   . VAL A 407 ? 1.48065 1.29405 1.44519 -0.13157 -0.08542 0.07941  286 VAL A O   
2856 C CB  . VAL A 407 ? 1.01475 0.86738 0.99177 -0.12290 -0.05696 0.08485  286 VAL A CB  
2857 C CG1 . VAL A 407 ? 1.01106 0.87769 0.98867 -0.12264 -0.06939 0.08822  286 VAL A CG1 
2858 C CG2 . VAL A 407 ? 0.98206 0.86443 0.98405 -0.12485 -0.05101 0.09231  286 VAL A CG2 
2859 N N   . GLN A 408 ? 1.36370 1.14067 1.28632 -0.12160 -0.06445 0.06655  287 GLN A N   
2860 C CA  . GLN A 408 ? 1.43618 1.18747 1.33075 -0.12095 -0.07447 0.05948  287 GLN A CA  
2861 C C   . GLN A 408 ? 1.56500 1.30114 1.46472 -0.12755 -0.08252 0.05625  287 GLN A C   
2862 O O   . GLN A 408 ? 1.56512 1.29598 1.45832 -0.13114 -0.09833 0.05404  287 GLN A O   
2863 C CB  . GLN A 408 ? 1.33844 1.05920 1.19618 -0.11417 -0.06256 0.05089  287 GLN A CB  
2864 C CG  . GLN A 408 ? 1.28847 0.98725 1.11126 -0.11114 -0.07311 0.04554  287 GLN A CG  
2865 C CD  . GLN A 408 ? 1.39048 1.05798 1.17545 -0.10438 -0.05909 0.03874  287 GLN A CD  
2866 O OE1 . GLN A 408 ? 1.38842 1.03106 1.16005 -0.10461 -0.04788 0.03178  287 GLN A OE1 
2867 N NE2 . GLN A 408 ? 1.46315 1.13131 1.23160 -0.09797 -0.05834 0.04128  287 GLN A NE2 
2868 N N   . ASN A 409 ? 1.53757 1.26657 1.45054 -0.12928 -0.07223 0.05574  288 ASN A N   
2869 C CA  . ASN A 409 ? 1.55672 1.26743 1.47509 -0.13503 -0.07791 0.05186  288 ASN A CA  
2870 C C   . ASN A 409 ? 1.58358 1.32047 1.53893 -0.14284 -0.08960 0.06252  288 ASN A C   
2871 O O   . ASN A 409 ? 1.54033 1.27090 1.51468 -0.14720 -0.08860 0.06429  288 ASN A O   
2872 C CB  . ASN A 409 ? 1.60901 1.30010 1.52854 -0.13248 -0.06124 0.04746  288 ASN A CB  
2873 C CG  . ASN A 409 ? 1.66071 1.31707 1.54056 -0.12659 -0.05026 0.03485  288 ASN A CG  
2874 O OD1 . ASN A 409 ? 1.65620 1.30326 1.50562 -0.12386 -0.05484 0.03047  288 ASN A OD1 
2875 N ND2 . ASN A 409 ? 1.64799 1.28508 1.52829 -0.12407 -0.03512 0.02976  288 ASN A ND2 
2876 N N   . LYS A 410 ? 1.63804 1.40376 1.60466 -0.14432 -0.09965 0.07021  289 LYS A N   
2877 C CA  . LYS A 410 ? 1.60393 1.39567 1.60498 -0.15213 -0.11008 0.08114  289 LYS A CA  
2878 C C   . LYS A 410 ? 1.67172 1.47335 1.67186 -0.15587 -0.12754 0.08123  289 LYS A C   
2879 O O   . LYS A 410 ? 1.75600 1.56719 1.77949 -0.16456 -0.13887 0.08611  289 LYS A O   
2880 C CB  . LYS A 410 ? 1.47847 1.30565 1.50513 -0.15065 -0.10232 0.09405  289 LYS A CB  
2881 C CG  . LYS A 410 ? 1.44191 1.26650 1.48122 -0.14931 -0.08930 0.09748  289 LYS A CG  
2882 C CD  . LYS A 410 ? 1.42747 1.27820 1.50263 -0.15505 -0.09197 0.11248  289 LYS A CD  
2883 C CE  . LYS A 410 ? 1.42921 1.26456 1.51810 -0.15585 -0.08539 0.11476  289 LYS A CE  
2884 N NZ  . LYS A 410 ? 1.47880 1.30513 1.55702 -0.14818 -0.07103 0.10951  289 LYS A NZ  
2885 N N   . VAL A 411 ? 1.67015 1.46967 1.64540 -0.14942 -0.12992 0.07647  290 VAL A N   
2886 C CA  . VAL A 411 ? 1.68083 1.48921 1.65416 -0.15140 -0.14742 0.07624  290 VAL A CA  
2887 C C   . VAL A 411 ? 1.65261 1.42772 1.58448 -0.14757 -0.15336 0.06352  290 VAL A C   
2888 O O   . VAL A 411 ? 1.63706 1.37964 1.54900 -0.14913 -0.15012 0.05372  290 VAL A O   
2889 C CB  . VAL A 411 ? 1.63057 1.47352 1.61671 -0.14617 -0.14692 0.08531  290 VAL A CB  
2890 C CG1 . VAL A 411 ? 1.55078 1.42688 1.57483 -0.15389 -0.15763 0.09584  290 VAL A CG1 
2891 C CG2 . VAL A 411 ? 1.48086 1.33376 1.46958 -0.14030 -0.12834 0.08915  290 VAL A CG2 
2892 N N   . PRO A 426 ? 1.97680 1.66974 1.71631 -0.03761 0.07185  -0.14446 305 PRO A N   
2893 C CA  . PRO A 426 ? 1.90990 1.62254 1.66432 -0.05234 0.06007  -0.14382 305 PRO A CA  
2894 C C   . PRO A 426 ? 1.74361 1.47379 1.51729 -0.04283 0.05169  -0.12258 305 PRO A C   
2895 O O   . PRO A 426 ? 1.79199 1.53654 1.58013 -0.05246 0.04389  -0.12001 305 PRO A O   
2896 C CB  . PRO A 426 ? 1.94625 1.62337 1.69887 -0.06475 0.07153  -0.15586 305 PRO A CB  
2897 C CG  . PRO A 426 ? 2.00570 1.64336 1.74866 -0.05000 0.08857  -0.15272 305 PRO A CG  
2898 C CD  . PRO A 426 ? 2.01865 1.66518 1.74977 -0.03662 0.08991  -0.15226 305 PRO A CD  
2899 N N   . ALA A 427 ? 1.42110 1.15084 1.19547 -0.02473 0.05391  -0.10832 306 ALA A N   
2900 C CA  . ALA A 427 ? 1.25472 0.99734 1.04521 -0.01647 0.04770  -0.08992 306 ALA A CA  
2901 C C   . ALA A 427 ? 1.14403 0.92464 0.94332 -0.01367 0.03492  -0.08105 306 ALA A C   
2902 O O   . ALA A 427 ? 1.00581 0.79673 0.81062 -0.00136 0.03308  -0.06767 306 ALA A O   
2903 C CB  . ALA A 427 ? 1.24992 0.97268 1.03801 0.00031  0.05685  -0.07882 306 ALA A CB  
2904 N N   . MET A 428 ? 1.11615 0.91881 0.91773 -0.02564 0.02613  -0.08797 307 MET A N   
2905 C CA  . MET A 428 ? 1.07613 0.91410 0.88509 -0.02332 0.01491  -0.07926 307 MET A CA  
2906 C C   . MET A 428 ? 1.10239 0.96019 0.92761 -0.03453 0.00547  -0.07806 307 MET A C   
2907 O O   . MET A 428 ? 1.31520 1.17083 1.13911 -0.04809 0.00483  -0.09049 307 MET A O   
2908 C CB  . MET A 428 ? 1.23279 1.08286 1.02502 -0.02384 0.01398  -0.08747 307 MET A CB  
2909 C CG  . MET A 428 ? 1.38271 1.21791 1.16181 -0.01032 0.02400  -0.08641 307 MET A CG  
2910 S SD  . MET A 428 ? 1.47899 1.32382 1.23428 -0.01205 0.02615  -0.09922 307 MET A SD  
2911 C CE  . MET A 428 ? 1.50583 1.39669 1.26997 -0.01344 0.01053  -0.08663 307 MET A CE  
2912 N N   . PHE A 429 ? 1.01105 0.88815 0.85275 -0.02916 -0.00093 -0.06344 308 PHE A N   
2913 C CA  . PHE A 429 ? 0.94314 0.83512 0.80409 -0.03666 -0.00710 -0.05976 308 PHE A CA  
2914 C C   . PHE A 429 ? 1.05521 0.97805 0.92832 -0.03134 -0.01568 -0.04669 308 PHE A C   
2915 O O   . PHE A 429 ? 0.84530 0.76882 0.72235 -0.02111 -0.01443 -0.03525 308 PHE A O   
2916 C CB  . PHE A 429 ? 0.91696 0.78942 0.78749 -0.03518 -0.00133 -0.05495 308 PHE A CB  
2917 C CG  . PHE A 429 ? 0.97588 0.81586 0.83457 -0.03853 0.00852  -0.06445 308 PHE A CG  
2918 C CD1 . PHE A 429 ? 0.89093 0.72311 0.74706 -0.05204 0.01062  -0.07793 308 PHE A CD1 
2919 C CD2 . PHE A 429 ? 1.10702 0.92503 0.95782 -0.02818 0.01602  -0.05919 308 PHE A CD2 
2920 C CE1 . PHE A 429 ? 0.88389 0.68261 0.72942 -0.05514 0.02164  -0.08592 308 PHE A CE1 
2921 C CE2 . PHE A 429 ? 1.11281 0.89965 0.95307 -0.02945 0.02619  -0.06546 308 PHE A CE2 
2922 C CZ  . PHE A 429 ? 1.01128 0.78630 0.84866 -0.04291 0.02980  -0.07879 308 PHE A CZ  
2923 N N   . VAL A 430 ? 1.26597 1.21499 1.14591 -0.03842 -0.02409 -0.04771 309 VAL A N   
2924 C CA  . VAL A 430 ? 0.89656 0.87502 0.78919 -0.03259 -0.03160 -0.03328 309 VAL A CA  
2925 C C   . VAL A 430 ? 1.00763 1.00322 0.92341 -0.03842 -0.03652 -0.02938 309 VAL A C   
2926 O O   . VAL A 430 ? 0.88305 0.89111 0.80035 -0.04925 -0.04124 -0.03843 309 VAL A O   
2927 C CB  . VAL A 430 ? 0.91618 0.91703 0.79413 -0.03218 -0.03777 -0.03407 309 VAL A CB  
2928 C CG1 . VAL A 430 ? 0.67592 0.70337 0.56628 -0.02357 -0.04344 -0.01561 309 VAL A CG1 
2929 C CG2 . VAL A 430 ? 0.86261 0.84451 0.71683 -0.02765 -0.03076 -0.04132 309 VAL A CG2 
2930 N N   . GLN A 431 ? 0.69961 0.69725 0.63418 -0.03162 -0.03496 -0.01631 310 GLN A N   
2931 C CA  . GLN A 431 ? 0.69300 0.70532 0.65211 -0.03467 -0.03718 -0.01111 310 GLN A CA  
2932 C C   . GLN A 431 ? 0.72232 0.75328 0.69746 -0.02451 -0.03950 0.00660  310 GLN A C   
2933 O O   . GLN A 431 ? 0.80004 0.81941 0.77287 -0.01645 -0.03488 0.01401  310 GLN A O   
2934 C CB  . GLN A 431 ? 0.65273 0.64061 0.62010 -0.03739 -0.02860 -0.01469 310 GLN A CB  
2935 C CG  . GLN A 431 ? 0.72863 0.69776 0.68557 -0.04809 -0.02474 -0.02996 310 GLN A CG  
2936 C CD  . GLN A 431 ? 0.78225 0.72643 0.74393 -0.04884 -0.01538 -0.03074 310 GLN A CD  
2937 O OE1 . GLN A 431 ? 1.04116 0.98855 1.01862 -0.05505 -0.01307 -0.03214 310 GLN A OE1 
2938 N NE2 . GLN A 431 ? 0.81269 0.73426 0.76093 -0.04233 -0.00992 -0.02917 310 GLN A NE2 
2939 N N   . ASN A 432 ? 0.63472 0.69491 0.62742 -0.02505 -0.04612 0.01385  311 ASN A N   
2940 C CA  . ASN A 432 ? 0.67645 0.75245 0.68932 -0.01475 -0.04633 0.03233  311 ASN A CA  
2941 C C   . ASN A 432 ? 0.87823 0.95448 0.87857 -0.00575 -0.04625 0.04210  311 ASN A C   
2942 O O   . ASN A 432 ? 0.77238 0.83746 0.78118 0.00175  -0.03966 0.05212  311 ASN A O   
2943 C CB  . ASN A 432 ? 0.81032 0.86745 0.84215 -0.01229 -0.03652 0.03545  311 ASN A CB  
2944 C CG  . ASN A 432 ? 0.80790 0.85919 0.84834 -0.02183 -0.03397 0.02421  311 ASN A CG  
2945 O OD1 . ASN A 432 ? 0.94884 1.02230 0.99652 -0.02829 -0.04053 0.02072  311 ASN A OD1 
2946 N ND2 . ASN A 432 ? 0.71104 0.73407 0.75057 -0.02347 -0.02437 0.01864  311 ASN A ND2 
2947 N N   . ALA A 433 ? 0.68066 0.76880 0.65981 -0.00760 -0.05258 0.03795  312 ALA A N   
2948 C CA  . ALA A 433 ? 0.75715 0.84274 0.72123 -0.00016 -0.05073 0.04482  312 ALA A CA  
2949 C C   . ALA A 433 ? 0.76795 0.88363 0.71908 0.00072  -0.05972 0.04959  312 ALA A C   
2950 O O   . ALA A 433 ? 0.75947 0.89456 0.70588 -0.00715 -0.06803 0.04176  312 ALA A O   
2951 C CB  . ALA A 433 ? 0.75226 0.80942 0.69558 -0.00232 -0.04444 0.03150  312 ALA A CB  
2952 N N   . VAL A 434 ? 0.72867 0.84894 0.67366 0.00957  -0.05766 0.06249  313 VAL A N   
2953 C CA  . VAL A 434 ? 0.77660 0.92067 0.70200 0.01131  -0.06376 0.06675  313 VAL A CA  
2954 C C   . VAL A 434 ? 0.90554 1.03057 0.80779 0.01289  -0.05672 0.05932  313 VAL A C   
2955 O O   . VAL A 434 ? 0.76753 0.87807 0.67560 0.01980  -0.04868 0.06790  313 VAL A O   
2956 C CB  . VAL A 434 ? 0.88436 1.05283 0.82311 0.02165  -0.06612 0.09150  313 VAL A CB  
2957 C CG1 . VAL A 434 ? 0.74399 0.93022 0.65837 0.02515  -0.06876 0.09755  313 VAL A CG1 
2958 C CG2 . VAL A 434 ? 0.68956 0.88584 0.64846 0.02092  -0.07505 0.09916  313 VAL A CG2 
2959 N N   . VAL A 435 ? 0.86167 0.98656 0.73897 0.00603  -0.05888 0.04271  314 VAL A N   
2960 C CA  . VAL A 435 ? 0.88042 0.98873 0.73538 0.00830  -0.05128 0.03470  314 VAL A CA  
2961 C C   . VAL A 435 ? 1.01972 1.15281 0.85210 0.00953  -0.05524 0.03779  314 VAL A C   
2962 O O   . VAL A 435 ? 1.01575 1.16715 0.83476 0.00136  -0.06343 0.02848  314 VAL A O   
2963 C CB  . VAL A 435 ? 0.79353 0.87591 0.63628 0.00048  -0.04709 0.01224  314 VAL A CB  
2964 C CG1 . VAL A 435 ? 0.87870 0.94507 0.70032 0.00498  -0.03803 0.00531  314 VAL A CG1 
2965 C CG2 . VAL A 435 ? 0.88284 0.94268 0.74599 -0.00068 -0.04330 0.01070  314 VAL A CG2 
2966 N N   . ARG A 436 ? 0.87591 1.01088 0.70343 0.01870  -0.04924 0.05041  315 ARG A N   
2967 C CA  . ARG A 436 ? 0.97496 1.13428 0.78063 0.02113  -0.05161 0.05643  315 ARG A CA  
2968 C C   . ARG A 436 ? 0.93454 1.08033 0.71421 0.02210  -0.04233 0.04389  315 ARG A C   
2969 O O   . ARG A 436 ? 0.93691 1.09928 0.69789 0.02578  -0.04077 0.05011  315 ARG A O   
2970 C CB  . ARG A 436 ? 0.82039 0.99591 0.63994 0.03129  -0.05074 0.08327  315 ARG A CB  
2971 C CG  . ARG A 436 ? 0.86203 1.05512 0.70625 0.03278  -0.05898 0.09863  315 ARG A CG  
2972 C CD  . ARG A 436 ? 1.03259 1.25992 0.87044 0.03883  -0.06479 0.11923  315 ARG A CD  
2973 N NE  . ARG A 436 ? 1.24397 1.48536 1.11047 0.04453  -0.06926 0.13941  315 ARG A NE  
2974 C CZ  . ARG A 436 ? 1.35859 1.62154 1.23506 0.04071  -0.08061 0.13897  315 ARG A CZ  
2975 N NH1 . ARG A 436 ? 1.39824 1.67109 1.25750 0.02912  -0.08922 0.11819  315 ARG A NH1 
2976 N NH2 . ARG A 436 ? 1.30689 1.58161 1.21188 0.04828  -0.08246 0.15922  315 ARG A NH2 
2977 N N   . ILE A 437 ? 0.94265 1.05911 0.72080 0.01971  -0.03528 0.02738  316 ILE A N   
2978 C CA  . ILE A 437 ? 0.99828 1.10001 0.75295 0.02109  -0.02541 0.01346  316 ILE A CA  
2979 C C   . ILE A 437 ? 0.98126 1.06920 0.72100 0.01021  -0.02662 -0.01091 316 ILE A C   
2980 O O   . ILE A 437 ? 0.93248 1.01410 0.68648 0.00323  -0.03227 -0.01591 316 ILE A O   
2981 C CB  . ILE A 437 ? 0.79752 0.87656 0.56468 0.02971  -0.01416 0.01740  316 ILE A CB  
2982 C CG1 . ILE A 437 ? 0.86334 0.92719 0.65752 0.02854  -0.01629 0.02051  316 ILE A CG1 
2983 C CG2 . ILE A 437 ? 0.71535 0.80867 0.48637 0.03886  -0.00923 0.03633  316 ILE A CG2 
2984 C CD1 . ILE A 437 ? 0.97353 1.00782 0.76743 0.02849  -0.00917 0.00670  316 ILE A CD1 
2985 N N   . PRO A 438 ? 1.03731 1.11892 0.74902 0.00785  -0.02017 -0.02704 317 PRO A N   
2986 C CA  . PRO A 438 ? 1.05179 1.11200 0.75077 -0.00263 -0.01769 -0.05162 317 PRO A CA  
2987 C C   . PRO A 438 ? 1.05984 1.08460 0.77338 0.00139  -0.00855 -0.05606 317 PRO A C   
2988 O O   . PRO A 438 ? 1.19269 1.20979 0.92119 0.01258  -0.00296 -0.04297 317 PRO A O   
2989 C CB  . PRO A 438 ? 1.07473 1.13436 0.74006 -0.00357 -0.00960 -0.06594 317 PRO A CB  
2990 C CG  . PRO A 438 ? 1.10055 1.16896 0.76667 0.01055  -0.00271 -0.04847 317 PRO A CG  
2991 C CD  . PRO A 438 ? 1.02364 1.11668 0.71306 0.01395  -0.01354 -0.02428 317 PRO A CD  
2992 N N   . LEU A 439 ? 1.00474 1.00882 0.71328 -0.00869 -0.00702 -0.07479 318 LEU A N   
2993 C CA  . LEU A 439 ? 0.99249 0.96270 0.71306 -0.00610 0.00112  -0.07909 318 LEU A CA  
2994 C C   . LEU A 439 ? 1.21989 1.16217 0.91921 -0.01284 0.01134  -0.10275 318 LEU A C   
2995 O O   . LEU A 439 ? 1.40876 1.35488 1.09659 -0.02770 0.00670  -0.11851 318 LEU A O   
2996 C CB  . LEU A 439 ? 0.92773 0.89895 0.67227 -0.01237 -0.00753 -0.07373 318 LEU A CB  
2997 C CG  . LEU A 439 ? 1.01747 1.00544 0.78727 -0.00508 -0.01404 -0.05149 318 LEU A CG  
2998 C CD1 . LEU A 439 ? 0.83794 0.81732 0.62892 -0.01078 -0.01790 -0.05041 318 LEU A CD1 
2999 C CD2 . LEU A 439 ? 0.97093 0.95029 0.74595 0.00895  -0.00574 -0.03982 318 LEU A CD2 
3000 N N   . CYS A 440 ? 1.30286 1.21772 0.99813 -0.00220 0.02564  -0.10517 319 CYS A N   
3001 C CA  . CYS A 440 ? 1.48480 1.36659 1.16185 -0.00582 0.03901  -0.12618 319 CYS A CA  
3002 C C   . CYS A 440 ? 1.57412 1.42254 1.26591 0.00091  0.04771  -0.12339 319 CYS A C   
3003 O O   . CYS A 440 ? 1.56154 1.41490 1.27555 0.00677  0.04223  -0.10681 319 CYS A O   
3004 C CB  . CYS A 440 ? 1.52633 1.40574 1.18124 0.00254  0.05103  -0.13232 319 CYS A CB  
3005 S SG  . CYS A 440 ? 1.60609 1.49969 1.27478 0.02384  0.05523  -0.10829 319 CYS A SG  
3006 N N   . ALA A 441 ? 1.63656 1.44996 1.31472 -0.00007 0.06217  -0.13984 320 ALA A N   
3007 C CA  . ALA A 441 ? 1.61827 1.39813 1.30784 0.00698  0.07179  -0.13662 320 ALA A CA  
3008 C C   . ALA A 441 ? 1.57680 1.35444 1.27692 0.02812  0.07893  -0.11936 320 ALA A C   
3009 O O   . ALA A 441 ? 1.52972 1.28485 1.24058 0.03616  0.08536  -0.11267 320 ALA A O   
3010 C CB  . ALA A 441 ? 1.71033 1.45092 1.38255 0.00011  0.08704  -0.15862 320 ALA A CB  
3011 N N   . GLU A 442 ? 1.55513 1.35723 1.25278 0.03697  0.07801  -0.11139 321 GLU A N   
3012 C CA  . GLU A 442 ? 1.51009 1.31869 1.22287 0.05506  0.08185  -0.09304 321 GLU A CA  
3013 C C   . GLU A 442 ? 1.30776 1.13600 1.04431 0.05495  0.06816  -0.07482 321 GLU A C   
3014 O O   . GLU A 442 ? 1.36180 1.18718 1.11368 0.06613  0.07031  -0.06172 321 GLU A O   
3015 C CB  . GLU A 442 ? 1.58811 1.41755 1.29185 0.06308  0.08621  -0.09041 321 GLU A CB  
3016 C CG  . GLU A 442 ? 1.82284 1.62937 1.50658 0.06979  0.10481  -0.10514 321 GLU A CG  
3017 C CD  . GLU A 442 ? 1.93892 1.73987 1.59537 0.05427  0.10611  -0.12795 321 GLU A CD  
3018 O OE1 . GLU A 442 ? 1.98417 1.77056 1.62073 0.05807  0.12132  -0.14169 321 GLU A OE1 
3019 O OE2 . GLU A 442 ? 1.95353 1.76567 1.60859 0.03802  0.09228  -0.13264 321 GLU A OE2 
3020 N N   . ASN A 443 ? 1.14899 0.99803 0.88890 0.04254  0.05445  -0.07389 322 ASN A N   
3021 C CA  . ASN A 443 ? 1.11323 0.97766 0.87492 0.04073  0.04283  -0.05911 322 ASN A CA  
3022 C C   . ASN A 443 ? 1.11627 0.95922 0.88493 0.03379  0.04168  -0.06300 322 ASN A C   
3023 O O   . ASN A 443 ? 1.22581 1.07654 1.00103 0.02229  0.03242  -0.06431 322 ASN A O   
3024 C CB  . ASN A 443 ? 0.99609 0.89105 0.75988 0.03251  0.03060  -0.05489 322 ASN A CB  
3025 C CG  . ASN A 443 ? 1.08381 0.99905 0.83708 0.03823  0.03279  -0.05141 322 ASN A CG  
3026 O OD1 . ASN A 443 ? 1.09249 1.02288 0.83179 0.03090  0.02837  -0.05752 322 ASN A OD1 
3027 N ND2 . ASN A 443 ? 0.98311 0.90099 0.74308 0.05109  0.03958  -0.04106 322 ASN A ND2 
3028 N N   . ALA A 444 ? 1.08737 0.90372 0.85536 0.04187  0.05207  -0.06350 323 ALA A N   
3029 C CA  . ALA A 444 ? 1.11288 0.90553 0.88500 0.03641  0.05361  -0.06639 323 ALA A CA  
3030 C C   . ALA A 444 ? 1.09913 0.90096 0.89009 0.04007  0.04683  -0.05036 323 ALA A C   
3031 O O   . ALA A 444 ? 1.00600 0.82724 0.80668 0.04874  0.04352  -0.03763 323 ALA A O   
3032 C CB  . ALA A 444 ? 1.18639 0.94383 0.94803 0.04399  0.06924  -0.07307 323 ALA A CB  
3033 N N   . ASP A 445 ? 0.98092 0.76846 0.77646 0.03223  0.04556  -0.05201 324 ASP A N   
3034 C CA  . ASP A 445 ? 1.02058 0.81550 0.83124 0.03258  0.03935  -0.03971 324 ASP A CA  
3035 C C   . ASP A 445 ? 1.03441 0.86114 0.85732 0.02946  0.02816  -0.03233 324 ASP A C   
3036 O O   . ASP A 445 ? 1.01177 0.85366 0.84373 0.03685  0.02550  -0.02083 324 ASP A O   
3037 C CB  . ASP A 445 ? 1.01592 0.80294 0.82927 0.04683  0.04481  -0.02815 324 ASP A CB  
3038 C CG  . ASP A 445 ? 1.10562 0.85868 0.90935 0.05079  0.05653  -0.03200 324 ASP A CG  
3039 O OD1 . ASP A 445 ? 1.18968 0.92358 0.98680 0.03975  0.05994  -0.04364 324 ASP A OD1 
3040 O OD2 . ASP A 445 ? 1.29041 1.03656 1.09432 0.06497  0.06275  -0.02270 324 ASP A OD2 
3041 N N   . LEU A 446 ? 1.11278 0.94966 0.93667 0.01795  0.02208  -0.03905 325 LEU A N   
3042 C CA  . LEU A 446 ? 1.06160 0.92700 0.89653 0.01536  0.01275  -0.03196 325 LEU A CA  
3043 C C   . LEU A 446 ? 0.85292 0.72215 0.70115 0.00562  0.00710  -0.03123 325 LEU A C   
3044 O O   . LEU A 446 ? 0.99782 0.85572 0.84341 -0.00349 0.00816  -0.04086 325 LEU A O   
3045 C CB  . LEU A 446 ? 0.91571 0.79623 0.74019 0.01258  0.01022  -0.03810 325 LEU A CB  
3046 C CG  . LEU A 446 ? 1.00401 0.91422 0.83629 0.01440  0.00296  -0.02759 325 LEU A CG  
3047 C CD1 . LEU A 446 ? 0.84013 0.75590 0.68089 0.02489  0.00530  -0.01470 325 LEU A CD1 
3048 C CD2 . LEU A 446 ? 0.83774 0.76078 0.65386 0.01271  0.00199  -0.03414 325 LEU A CD2 
3049 N N   . TRP A 447 ? 0.81151 0.69615 0.67492 0.00720  0.00236  -0.02022 326 TRP A N   
3050 C CA  . TRP A 447 ? 0.81289 0.70462 0.69116 -0.00053 -0.00208 -0.01841 326 TRP A CA  
3051 C C   . TRP A 447 ? 0.84338 0.75933 0.73408 0.00180  -0.00752 -0.00806 326 TRP A C   
3052 O O   . TRP A 447 ? 0.83955 0.75903 0.73692 0.00731  -0.00651 0.00081  326 TRP A O   
3053 C CB  . TRP A 447 ? 0.80592 0.68248 0.69018 -0.00103 0.00148  -0.01589 326 TRP A CB  
3054 C CG  . TRP A 447 ? 0.74771 0.62995 0.64776 -0.00801 -0.00071 -0.01415 326 TRP A CG  
3055 C CD1 . TRP A 447 ? 0.73244 0.63085 0.64804 -0.00742 -0.00387 -0.00610 326 TRP A CD1 
3056 C CD2 . TRP A 447 ? 0.65399 0.52434 0.55677 -0.01613 0.00203  -0.02035 326 TRP A CD2 
3057 N NE1 . TRP A 447 ? 0.70052 0.59810 0.62859 -0.01376 -0.00305 -0.00724 326 TRP A NE1 
3058 C CE2 . TRP A 447 ? 0.77194 0.65378 0.69254 -0.01949 0.00028  -0.01589 326 TRP A CE2 
3059 C CE3 . TRP A 447 ? 0.81208 0.66203 0.70467 -0.02092 0.00719  -0.02897 326 TRP A CE3 
3060 C CZ2 . TRP A 447 ? 0.61012 0.48617 0.53889 -0.02722 0.00325  -0.01990 326 TRP A CZ2 
3061 C CZ3 . TRP A 447 ? 0.76300 0.60675 0.66337 -0.02965 0.00985  -0.03264 326 TRP A CZ3 
3062 C CH2 . TRP A 447 ? 0.73841 0.59640 0.65685 -0.03263 0.00772  -0.02818 326 TRP A CH2 
3063 N N   . ILE A 448 ? 0.90189 0.83516 0.79612 -0.00270 -0.01307 -0.00875 327 ILE A N   
3064 C CA  . ILE A 448 ? 0.69119 0.64708 0.59850 -0.00003 -0.01766 0.00296  327 ILE A CA  
3065 C C   . ILE A 448 ? 0.83659 0.80007 0.76139 -0.00593 -0.02076 0.00437  327 ILE A C   
3066 O O   . ILE A 448 ? 0.84456 0.81070 0.76776 -0.01336 -0.02353 -0.00417 327 ILE A O   
3067 C CB  . ILE A 448 ? 0.75626 0.73100 0.65240 0.00194  -0.02174 0.00409  327 ILE A CB  
3068 C CG1 . ILE A 448 ? 0.63947 0.60503 0.51789 0.00788  -0.01656 0.00079  327 ILE A CG1 
3069 C CG2 . ILE A 448 ? 0.59663 0.59366 0.50631 0.00630  -0.02535 0.01936  327 ILE A CG2 
3070 C CD1 . ILE A 448 ? 0.83754 0.81622 0.69834 0.00780  -0.01860 -0.00362 327 ILE A CD1 
3071 N N   . GLU A 449 ? 0.77408 0.74134 0.71653 -0.00306 -0.01944 0.01461  328 GLU A N   
3072 C CA  . GLU A 449 ? 0.66708 0.63980 0.62842 -0.00705 -0.02003 0.01647  328 GLU A CA  
3073 C C   . GLU A 449 ? 0.84549 0.82868 0.82475 -0.00120 -0.01880 0.03057  328 GLU A C   
3074 O O   . GLU A 449 ? 0.66877 0.64279 0.64850 0.00240  -0.01422 0.03505  328 GLU A O   
3075 C CB  . GLU A 449 ? 0.74638 0.69747 0.70923 -0.01206 -0.01426 0.00877  328 GLU A CB  
3076 C CG  . GLU A 449 ? 0.61248 0.56844 0.59317 -0.01750 -0.01351 0.00768  328 GLU A CG  
3077 C CD  . GLU A 449 ? 0.70346 0.66312 0.70473 -0.01363 -0.00958 0.01748  328 GLU A CD  
3078 O OE1 . GLU A 449 ? 0.80683 0.75185 0.80660 -0.01165 -0.00401 0.01890  328 GLU A OE1 
3079 O OE2 . GLU A 449 ? 0.71108 0.68879 0.73063 -0.01273 -0.01165 0.02357  328 GLU A OE2 
3080 N N   . ASN A 450 ? 0.78058 0.78354 0.77545 -0.00040 -0.02251 0.03780  329 ASN A N   
3081 C CA  . ASN A 450 ? 0.65499 0.66558 0.67024 0.00593  -0.01944 0.05233  329 ASN A CA  
3082 C C   . ASN A 450 ? 0.75496 0.76808 0.76376 0.01236  -0.01838 0.06204  329 ASN A C   
3083 O O   . ASN A 450 ? 0.59828 0.60333 0.61819 0.01563  -0.01172 0.06987  329 ASN A O   
3084 C CB  . ASN A 450 ? 0.59386 0.58539 0.62298 0.00410  -0.01054 0.05026  329 ASN A CB  
3085 C CG  . ASN A 450 ? 0.74099 0.73744 0.79375 0.01011  -0.00515 0.06370  329 ASN A CG  
3086 O OD1 . ASN A 450 ? 0.80396 0.81983 0.86494 0.01657  -0.00861 0.07671  329 ASN A OD1 
3087 N ND2 . ASN A 450 ? 0.62135 0.59934 0.68425 0.00821  0.00424  0.06085  329 ASN A ND2 
3088 N N   . SER A 451 ? 0.63983 0.66358 0.63015 0.01324  -0.02391 0.06056  330 SER A N   
3089 C CA  . SER A 451 ? 0.74164 0.76796 0.72302 0.01865  -0.02209 0.06822  330 SER A CA  
3090 C C   . SER A 451 ? 0.73049 0.78184 0.70246 0.02202  -0.02887 0.07538  330 SER A C   
3091 O O   . SER A 451 ? 0.79302 0.85658 0.75628 0.01787  -0.03600 0.06803  330 SER A O   
3092 C CB  . SER A 451 ? 0.57919 0.58907 0.54265 0.01694  -0.01922 0.05737  330 SER A CB  
3093 O OG  . SER A 451 ? 0.63348 0.62412 0.60463 0.01457  -0.01342 0.05369  330 SER A OG  
3094 N N   . HIS A 452 ? 0.68769 0.74718 0.66095 0.02863  -0.02626 0.08966  331 HIS A N   
3095 C CA  . HIS A 452 ? 0.62839 0.71063 0.58765 0.03254  -0.03116 0.09756  331 HIS A CA  
3096 C C   . HIS A 452 ? 0.71196 0.78741 0.65184 0.03379  -0.02687 0.09334  331 HIS A C   
3097 O O   . HIS A 452 ? 0.76092 0.82667 0.70779 0.03672  -0.01934 0.10006  331 HIS A O   
3098 C CB  . HIS A 452 ? 0.73752 0.83504 0.71286 0.04034  -0.02990 0.11980  331 HIS A CB  
3099 C CG  . HIS A 452 ? 0.81085 0.93530 0.77114 0.04468  -0.03575 0.13017  331 HIS A CG  
3100 N ND1 . HIS A 452 ? 0.75874 0.88521 0.70391 0.04826  -0.03142 0.13596  331 HIS A ND1 
3101 C CD2 . HIS A 452 ? 0.71818 0.87105 0.67595 0.04582  -0.04557 0.13640  331 HIS A CD2 
3102 C CE1 . HIS A 452 ? 0.72802 0.88124 0.65954 0.05143  -0.03784 0.14492  331 HIS A CE1 
3103 N NE2 . HIS A 452 ? 0.76882 0.93949 0.70742 0.04988  -0.04723 0.14545  331 HIS A NE2 
3104 N N   . ILE A 453 ? 0.72572 0.80664 0.64234 0.03111  -0.03083 0.08174  332 ILE A N   
3105 C CA  . ILE A 453 ? 0.67921 0.75466 0.57675 0.03327  -0.02576 0.07660  332 ILE A CA  
3106 C C   . ILE A 453 ? 0.81098 0.91006 0.69335 0.03728  -0.02788 0.08611  332 ILE A C   
3107 O O   . ILE A 453 ? 0.76514 0.87808 0.62976 0.03386  -0.03438 0.07869  332 ILE A O   
3108 C CB  . ILE A 453 ? 0.68750 0.74737 0.56872 0.02822  -0.02549 0.05607  332 ILE A CB  
3109 C CG1 . ILE A 453 ? 0.72826 0.76581 0.62380 0.02508  -0.02290 0.04962  332 ILE A CG1 
3110 C CG2 . ILE A 453 ? 0.85427 0.90960 0.71720 0.03240  -0.01884 0.05171  332 ILE A CG2 
3111 C CD1 . ILE A 453 ? 0.81842 0.83560 0.70063 0.02361  -0.01872 0.03451  332 ILE A CD1 
3112 N N   . GLY A 454 ? 0.71862 0.82271 0.60705 0.04357  -0.02195 0.10225  333 GLY A N   
3113 C CA  . GLY A 454 ? 0.74335 0.86989 0.61835 0.04828  -0.02251 0.11489  333 GLY A CA  
3114 C C   . GLY A 454 ? 0.90116 1.03065 0.74731 0.04814  -0.01986 0.10363  333 GLY A C   
3115 O O   . GLY A 454 ? 0.93964 1.05119 0.78004 0.04696  -0.01437 0.08960  333 GLY A O   
3116 N N   . PRO A 455 ? 0.73130 0.88423 0.55834 0.04999  -0.02310 0.11025  334 PRO A N   
3117 C CA  . PRO A 455 ? 0.82413 0.98045 0.62012 0.04879  -0.02030 0.09674  334 PRO A CA  
3118 C C   . PRO A 455 ? 0.95990 1.10482 0.75218 0.05403  -0.00729 0.09673  334 PRO A C   
3119 O O   . PRO A 455 ? 0.92482 1.06534 0.69468 0.05358  -0.00246 0.08202  334 PRO A O   
3120 C CB  . PRO A 455 ? 0.69060 0.87824 0.46916 0.05013  -0.02660 0.10850  334 PRO A CB  
3121 C CG  . PRO A 455 ? 0.73298 0.92961 0.53580 0.05666  -0.02652 0.13475  334 PRO A CG  
3122 C CD  . PRO A 455 ? 0.64242 0.81991 0.47482 0.05431  -0.02805 0.13196  334 PRO A CD  
3123 N N   . LYS A 456 ? 0.93497 1.07541 0.74910 0.05858  -0.00065 0.11206  335 LYS A N   
3124 C CA  . LYS A 456 ? 0.90608 1.03973 0.72047 0.06280  0.01134  0.11258  335 LYS A CA  
3125 C C   . LYS A 456 ? 0.91994 1.03126 0.75007 0.06147  0.01461  0.10147  335 LYS A C   
3126 O O   . LYS A 456 ? 0.94708 1.05518 0.78496 0.06484  0.02358  0.10419  335 LYS A O   
3127 C CB  . LYS A 456 ? 0.80558 0.94989 0.63335 0.06714  0.01794  0.13559  335 LYS A CB  
3128 C CG  . LYS A 456 ? 0.92773 1.09580 0.73723 0.07024  0.01627  0.14955  335 LYS A CG  
3129 C CD  . LYS A 456 ? 0.92945 1.10457 0.75726 0.07411  0.02159  0.17531  335 LYS A CD  
3130 C CE  . LYS A 456 ? 1.04104 1.23963 0.85553 0.07748  0.01553  0.19174  335 LYS A CE  
3131 N NZ  . LYS A 456 ? 1.15561 1.35878 0.98710 0.08254  0.02300  0.21900  335 LYS A NZ  
3132 N N   . TRP A 457 ? 0.82067 0.91869 0.65587 0.05659  0.00758  0.08980  336 TRP A N   
3133 C CA  . TRP A 457 ? 0.74503 0.82287 0.59071 0.05584  0.01047  0.07934  336 TRP A CA  
3134 C C   . TRP A 457 ? 0.85367 0.92349 0.67956 0.05878  0.01625  0.06430  336 TRP A C   
3135 O O   . TRP A 457 ? 0.92181 0.99533 0.72429 0.05772  0.01541  0.05496  336 TRP A O   
3136 C CB  . TRP A 457 ? 0.70173 0.76686 0.55737 0.04982  0.00268  0.07189  336 TRP A CB  
3137 C CG  . TRP A 457 ? 0.68971 0.75573 0.56960 0.04768  -0.00018 0.08431  336 TRP A CG  
3138 C CD1 . TRP A 457 ? 0.72991 0.81014 0.61864 0.04951  -0.00054 0.10132  336 TRP A CD1 
3139 C CD2 . TRP A 457 ? 0.63359 0.68395 0.53132 0.04371  -0.00150 0.08062  336 TRP A CD2 
3140 N NE1 . TRP A 457 ? 0.64178 0.71417 0.55391 0.04711  -0.00112 0.10757  336 TRP A NE1 
3141 C CE2 . TRP A 457 ? 0.60477 0.65947 0.52188 0.04300  -0.00185 0.09428  336 TRP A CE2 
3142 C CE3 . TRP A 457 ? 0.71697 0.74950 0.61521 0.04104  -0.00155 0.06765  336 TRP A CE3 
3143 C CZ2 . TRP A 457 ? 0.71981 0.76128 0.65583 0.03894  -0.00178 0.09326  336 TRP A CZ2 
3144 C CZ3 . TRP A 457 ? 0.63273 0.65434 0.54859 0.03689  -0.00258 0.06783  336 TRP A CZ3 
3145 C CH2 . TRP A 457 ? 0.68369 0.70968 0.61779 0.03549  -0.00249 0.07952  336 TRP A CH2 
3146 N N   . LYS A 458 ? 0.86969 0.92900 0.70544 0.06250  0.02261  0.06197  337 LYS A N   
3147 C CA  . LYS A 458 ? 0.89600 0.94317 0.71839 0.06708  0.02933  0.04851  337 LYS A CA  
3148 C C   . LYS A 458 ? 0.89393 0.92181 0.72819 0.06577  0.02714  0.04177  337 LYS A C   
3149 O O   . LYS A 458 ? 0.98112 1.00983 0.83590 0.06601  0.02666  0.04970  337 LYS A O   
3150 C CB  . LYS A 458 ? 0.96861 1.02540 0.79207 0.07545  0.04035  0.05450  337 LYS A CB  
3151 C CG  . LYS A 458 ? 1.00899 1.08494 0.81856 0.07726  0.04451  0.06203  337 LYS A CG  
3152 C CD  . LYS A 458 ? 1.08452 1.17678 0.91328 0.07681  0.04531  0.08145  337 LYS A CD  
3153 C CE  . LYS A 458 ? 1.27382 1.38463 1.08615 0.07838  0.04882  0.09063  337 LYS A CE  
3154 N NZ  . LYS A 458 ? 1.18937 1.31110 1.01544 0.07508  0.04459  0.10882  337 LYS A NZ  
3155 N N   . ILE A 459 ? 0.89875 0.90945 0.71935 0.06346  0.02621  0.02702  338 ILE A N   
3156 C CA  . ILE A 459 ? 0.89873 0.88950 0.72728 0.06257  0.02520  0.02097  338 ILE A CA  
3157 C C   . ILE A 459 ? 0.88617 0.85866 0.69922 0.06824  0.03392  0.00838  338 ILE A C   
3158 O O   . ILE A 459 ? 1.01641 0.99038 0.81168 0.07135  0.04049  0.00193  338 ILE A O   
3159 C CB  . ILE A 459 ? 0.86829 0.85184 0.69991 0.05265  0.01607  0.01648  338 ILE A CB  
3160 C CG1 . ILE A 459 ? 0.89379 0.87116 0.70440 0.04710  0.01495  0.00213  338 ILE A CG1 
3161 C CG2 . ILE A 459 ? 0.66612 0.66677 0.51274 0.04843  0.00916  0.02915  338 ILE A CG2 
3162 C CD1 . ILE A 459 ? 0.78461 0.75893 0.60018 0.03676  0.00615  -0.00232 338 ILE A CD1 
3163 N N   . ALA A 460 ? 0.87188 0.82591 0.69132 0.06979  0.03492  0.00521  339 ALA A N   
3164 C CA  . ALA A 460 ? 0.92179 0.85464 0.73073 0.07707  0.04471  -0.00398 339 ALA A CA  
3165 C C   . ALA A 460 ? 0.92806 0.83684 0.73424 0.07056  0.04228  -0.01292 339 ALA A C   
3166 O O   . ALA A 460 ? 1.02750 0.93168 0.82417 0.06004  0.03787  -0.02249 339 ALA A O   
3167 C CB  . ALA A 460 ? 0.86098 0.79856 0.68352 0.08943  0.05076  0.00607  339 ALA A CB  
3168 N N   . SER A 461 ? 0.85394 0.74951 0.66886 0.07637  0.04494  -0.00905 340 SER A N   
3169 C CA  . SER A 461 ? 0.87931 0.75159 0.69265 0.07087  0.04390  -0.01504 340 SER A CA  
3170 C C   . SER A 461 ? 0.95856 0.83619 0.78918 0.07129  0.03787  -0.00350 340 SER A C   
3171 O O   . SER A 461 ? 1.18485 1.08175 1.02807 0.07667  0.03582  0.00770  340 SER A O   
3172 C CB  . SER A 461 ? 0.99727 0.84100 0.79827 0.07832  0.05638  -0.02337 340 SER A CB  
3173 O OG  . SER A 461 ? 1.22592 1.07177 1.03494 0.09356  0.06287  -0.01295 340 SER A OG  
3174 N N   . ARG A 462 ? 1.11090 0.97190 0.94147 0.06426  0.03543  -0.00715 341 ARG A N   
3175 C CA  . ARG A 462 ? 1.04338 0.90662 0.88628 0.06289  0.03034  0.00149  341 ARG A CA  
3176 C C   . ARG A 462 ? 0.89820 0.78583 0.75498 0.05681  0.02159  0.00839  341 ARG A C   
3177 O O   . ARG A 462 ? 0.87242 0.77703 0.73958 0.06154  0.02016  0.01772  341 ARG A O   
3178 C CB  . ARG A 462 ? 1.03599 0.89753 0.88227 0.07580  0.03505  0.01048  341 ARG A CB  
3179 C CG  . ARG A 462 ? 1.09070 0.92573 0.92472 0.08452  0.04617  0.00573  341 ARG A CG  
3180 C CD  . ARG A 462 ? 1.21484 1.04680 1.05399 0.09656  0.04913  0.01736  341 ARG A CD  
3181 N NE  . ARG A 462 ? 1.24865 1.11121 1.10201 0.10291  0.04411  0.02928  341 ARG A NE  
3182 C CZ  . ARG A 462 ? 1.21253 1.09053 1.07023 0.11249  0.04842  0.03254  341 ARG A CZ  
3183 N NH1 . ARG A 462 ? 1.20171 1.06614 1.04848 0.11753  0.05834  0.02425  341 ARG A NH1 
3184 N NH2 . ARG A 462 ? 1.22665 1.13414 1.09952 0.11610  0.04352  0.04328  341 ARG A NH2 
3185 N N   . HIS A 463 ? 0.88721 0.77676 0.74565 0.04615  0.01639  0.00405  342 HIS A N   
3186 C CA  . HIS A 463 ? 0.78633 0.69504 0.65839 0.04077  0.00995  0.01062  342 HIS A CA  
3187 C C   . HIS A 463 ? 0.79993 0.70197 0.67774 0.03092  0.00602  0.00758  342 HIS A C   
3188 O O   . HIS A 463 ? 0.96133 0.85015 0.83183 0.02600  0.00682  -0.00099 342 HIS A O   
3189 C CB  . HIS A 463 ? 0.69169 0.61677 0.56191 0.04014  0.00831  0.01142  342 HIS A CB  
3190 C CG  . HIS A 463 ? 0.81991 0.75309 0.68379 0.04925  0.01348  0.01388  342 HIS A CG  
3191 N ND1 . HIS A 463 ? 0.76851 0.71316 0.64231 0.05563  0.01545  0.02311  342 HIS A ND1 
3192 C CD2 . HIS A 463 ? 0.74313 0.67590 0.59194 0.05245  0.01774  0.00773  342 HIS A CD2 
3193 C CE1 . HIS A 463 ? 0.84088 0.79207 0.70753 0.06341  0.02125  0.02354  342 HIS A CE1 
3194 N NE2 . HIS A 463 ? 0.91655 0.85954 0.76681 0.06184  0.02317  0.01394  342 HIS A NE2 
3195 N N   . ILE A 464 ? 0.79253 0.70379 0.68427 0.02744  0.00281  0.01402  343 ILE A N   
3196 C CA  . ILE A 464 ? 0.66911 0.57884 0.56965 0.01890  0.00004  0.01244  343 ILE A CA  
3197 C C   . ILE A 464 ? 0.76225 0.68958 0.67641 0.01775  -0.00243 0.02019  343 ILE A C   
3198 O O   . ILE A 464 ? 0.86425 0.79789 0.78684 0.01872  -0.00163 0.02633  343 ILE A O   
3199 C CB  . ILE A 464 ? 0.74186 0.63970 0.64515 0.01543  0.00131  0.01173  343 ILE A CB  
3200 C CG1 . ILE A 464 ? 0.69155 0.56969 0.58146 0.01644  0.00485  0.00556  343 ILE A CG1 
3201 C CG2 . ILE A 464 ? 0.60779 0.50667 0.52313 0.00750  0.00011  0.01107  343 ILE A CG2 
3202 C CD1 . ILE A 464 ? 0.73559 0.60242 0.62484 0.01387  0.00661  0.00627  343 ILE A CD1 
3203 N N   . ILE A 465 ? 0.78005 0.71605 0.69666 0.01547  -0.00519 0.02038  344 ILE A N   
3204 C CA  . ILE A 465 ? 0.73383 0.68583 0.66301 0.01596  -0.00666 0.02991  344 ILE A CA  
3205 C C   . ILE A 465 ? 0.75112 0.70317 0.69345 0.01064  -0.00818 0.03029  344 ILE A C   
3206 O O   . ILE A 465 ? 0.81445 0.76822 0.75401 0.00756  -0.01121 0.02516  344 ILE A O   
3207 C CB  . ILE A 465 ? 0.77647 0.74326 0.69710 0.01995  -0.00857 0.03293  344 ILE A CB  
3208 C CG1 . ILE A 465 ? 0.72306 0.69052 0.63319 0.02622  -0.00493 0.03333  344 ILE A CG1 
3209 C CG2 . ILE A 465 ? 0.56171 0.54445 0.49562 0.02104  -0.00970 0.04517  344 ILE A CG2 
3210 C CD1 . ILE A 465 ? 0.74961 0.72564 0.64377 0.02948  -0.00513 0.03082  344 ILE A CD1 
3211 N N   . THR A 466 ? 0.66846 0.61893 0.62586 0.00905  -0.00534 0.03562  345 THR A N   
3212 C CA  . THR A 466 ? 0.63168 0.57975 0.60345 0.00505  -0.00427 0.03583  345 THR A CA  
3213 C C   . THR A 466 ? 0.63189 0.58586 0.62109 0.00670  -0.00079 0.04644  345 THR A C   
3214 O O   . THR A 466 ? 0.72141 0.67340 0.71243 0.00701  0.00253  0.04979  345 THR A O   
3215 C CB  . THR A 466 ? 0.75941 0.69027 0.72994 -0.00019 -0.00082 0.02764  345 THR A CB  
3216 O OG1 . THR A 466 ? 0.72380 0.64922 0.69282 -0.00057 0.00207  0.02836  345 THR A OG1 
3217 C CG2 . THR A 466 ? 0.53061 0.45236 0.48551 -0.00186 -0.00249 0.01839  345 THR A CG2 
3218 N N   . GLY A 467 ? 0.69448 0.65623 0.69776 0.00776  -0.00100 0.05218  346 GLY A N   
3219 C CA  . GLY A 467 ? 0.65272 0.61525 0.67504 0.00990  0.00474  0.06254  346 GLY A CA  
3220 C C   . GLY A 467 ? 0.64065 0.61702 0.66597 0.01611  0.00430  0.07627  346 GLY A C   
3221 O O   . GLY A 467 ? 0.72352 0.69829 0.76550 0.01846  0.01061  0.08646  346 GLY A O   
3222 N N   . VAL A 468 ? 0.54557 0.53406 0.55500 0.01891  -0.00153 0.07706  347 VAL A N   
3223 C CA  . VAL A 468 ? 0.59515 0.59521 0.60366 0.02418  -0.00040 0.08958  347 VAL A CA  
3224 C C   . VAL A 468 ? 0.60150 0.61869 0.61995 0.03012  -0.00262 0.10391  347 VAL A C   
3225 O O   . VAL A 468 ? 0.67477 0.70728 0.68556 0.03114  -0.01056 0.10261  347 VAL A O   
3226 C CB  . VAL A 468 ? 0.70863 0.71529 0.69532 0.02548  -0.00417 0.08473  347 VAL A CB  
3227 C CG1 . VAL A 468 ? 0.65453 0.67634 0.63891 0.03119  -0.00287 0.09851  347 VAL A CG1 
3228 C CG2 . VAL A 468 ? 0.65194 0.64481 0.63265 0.02208  -0.00103 0.07518  347 VAL A CG2 
3229 N N   . PRO A 469 ? 0.71585 0.73162 0.75167 0.03392  0.00440  0.11806  348 PRO A N   
3230 C CA  . PRO A 469 ? 0.69119 0.72439 0.73801 0.04174  0.00283  0.13518  348 PRO A CA  
3231 C C   . PRO A 469 ? 0.77549 0.83024 0.80581 0.04662  -0.00287 0.14441  348 PRO A C   
3232 O O   . PRO A 469 ? 0.65987 0.71405 0.67228 0.04457  -0.00333 0.13843  348 PRO A O   
3233 C CB  . PRO A 469 ? 0.71681 0.73586 0.78548 0.04422  0.01505  0.14707  348 PRO A CB  
3234 C CG  . PRO A 469 ? 0.61105 0.61487 0.67252 0.03775  0.02071  0.13931  348 PRO A CG  
3235 C CD  . PRO A 469 ? 0.59225 0.59023 0.63905 0.03085  0.01475  0.11936  348 PRO A CD  
3236 N N   . GLU A 470 ? 0.69181 0.76738 0.72868 0.05380  -0.00683 0.16003  349 GLU A N   
3237 C CA  . GLU A 470 ? 0.72906 0.82886 0.74847 0.05845  -0.01303 0.16985  349 GLU A CA  
3238 C C   . GLU A 470 ? 0.69377 0.78769 0.70830 0.06099  -0.00438 0.17969  349 GLU A C   
3239 O O   . GLU A 470 ? 0.70085 0.77928 0.73353 0.06250  0.00636  0.18911  349 GLU A O   
3240 C CB  . GLU A 470 ? 0.71597 0.84087 0.74696 0.06671  -0.01827 0.18852  349 GLU A CB  
3241 C CG  . GLU A 470 ? 0.76073 0.91275 0.77450 0.07268  -0.02366 0.20331  349 GLU A CG  
3242 C CD  . GLU A 470 ? 0.85235 1.03534 0.87566 0.08023  -0.03224 0.22022  349 GLU A CD  
3243 O OE1 . GLU A 470 ? 0.75843 0.95096 0.79016 0.07694  -0.03999 0.21156  349 GLU A OE1 
3244 O OE2 . GLU A 470 ? 0.87147 1.07078 0.89470 0.08961  -0.03102 0.24325  349 GLU A OE2 
3245 N N   . ASN A 471 ? 0.75316 0.85939 0.74338 0.06083  -0.00802 0.17699  350 ASN A N   
3246 C CA  . ASN A 471 ? 0.69794 0.79894 0.68181 0.06162  0.00057  0.18234  350 ASN A CA  
3247 C C   . ASN A 471 ? 0.68988 0.81059 0.64547 0.06333  -0.00434 0.18111  350 ASN A C   
3248 O O   . ASN A 471 ? 0.84016 0.97124 0.77878 0.06070  -0.01380 0.16854  350 ASN A O   
3249 C CB  . ASN A 471 ? 0.59662 0.67459 0.58380 0.05446  0.00641  0.16653  350 ASN A CB  
3250 C CG  . ASN A 471 ? 0.61800 0.69569 0.58384 0.05034  0.00039  0.14647  350 ASN A CG  
3251 O OD1 . ASN A 471 ? 0.95028 1.03509 0.89848 0.05165  0.00157  0.14435  350 ASN A OD1 
3252 N ND2 . ASN A 471 ? 0.67946 0.74781 0.64712 0.04573  -0.00464 0.13208  350 ASN A ND2 
3253 N N   . ASP A 472 ? 0.90097 1.02591 0.85142 0.06684  0.00338  0.19340  351 ASP A N   
3254 C CA  . ASP A 472 ? 0.97597 1.11533 0.89847 0.06776  0.00215  0.18946  351 ASP A CA  
3255 C C   . ASP A 472 ? 0.78182 0.90822 0.70328 0.06527  0.01199  0.18255  351 ASP A C   
3256 O O   . ASP A 472 ? 0.90396 1.03983 0.81498 0.06838  0.01852  0.19115  351 ASP A O   
3257 C CB  . ASP A 472 ? 0.82404 0.98691 0.73721 0.07511  0.00215  0.21167  351 ASP A CB  
3258 C CG  . ASP A 472 ? 0.95660 1.13683 0.83683 0.07554  0.00016  0.20596  351 ASP A CG  
3259 O OD1 . ASP A 472 ? 0.82497 1.00153 0.68893 0.07042  -0.00432 0.18369  351 ASP A OD1 
3260 O OD2 . ASP A 472 ? 1.05905 1.25529 0.92907 0.08106  0.00426  0.22380  351 ASP A OD2 
3261 N N   . TRP A 473 ? 0.81499 0.92197 0.74778 0.05982  0.01322  0.16790  352 TRP A N   
3262 C CA  . TRP A 473 ? 0.77028 0.86839 0.70667 0.05745  0.02158  0.16265  352 TRP A CA  
3263 C C   . TRP A 473 ? 0.82317 0.92948 0.73504 0.05952  0.02179  0.15217  352 TRP A C   
3264 O O   . TRP A 473 ? 0.77123 0.87957 0.66489 0.05933  0.01470  0.13946  352 TRP A O   
3265 C CB  . TRP A 473 ? 0.66940 0.74816 0.62070 0.05127  0.02104  0.14915  352 TRP A CB  
3266 C CG  . TRP A 473 ? 0.76976 0.83671 0.74496 0.04820  0.02340  0.15604  352 TRP A CG  
3267 C CD1 . TRP A 473 ? 0.69649 0.76420 0.68653 0.05024  0.03003  0.17432  352 TRP A CD1 
3268 C CD2 . TRP A 473 ? 0.53888 0.58930 0.52574 0.04266  0.02102  0.14452  352 TRP A CD2 
3269 N NE1 . TRP A 473 ? 0.62867 0.67994 0.63951 0.04640  0.03247  0.17377  352 TRP A NE1 
3270 C CE2 . TRP A 473 ? 0.64972 0.69118 0.65818 0.04141  0.02679  0.15518  352 TRP A CE2 
3271 C CE3 . TRP A 473 ? 0.65817 0.69949 0.63860 0.03893  0.01568  0.12673  352 TRP A CE3 
3272 C CZ2 . TRP A 473 ? 0.64720 0.67168 0.66990 0.03606  0.02750  0.14704  352 TRP A CZ2 
3273 C CZ3 . TRP A 473 ? 0.53908 0.56502 0.53310 0.03364  0.01564  0.12014  352 TRP A CZ3 
3274 C CH2 . TRP A 473 ? 0.67511 0.69320 0.68953 0.03202  0.02151  0.12950  352 TRP A CH2 
3275 N N   . SER A 474 ? 0.75948 0.86996 0.67191 0.06107  0.03118  0.15692  353 SER A N   
3276 C CA  . SER A 474 ? 0.86527 0.97878 0.76058 0.06339  0.03422  0.14478  353 SER A CA  
3277 C C   . SER A 474 ? 0.80034 0.90035 0.71020 0.06018  0.03557  0.13341  353 SER A C   
3278 O O   . SER A 474 ? 0.86547 0.96857 0.78739 0.05987  0.04307  0.13681  353 SER A O   
3279 C CB  . SER A 474 ? 0.95273 1.08146 0.84089 0.06768  0.04425  0.15657  353 SER A CB  
3280 O OG  . SER A 474 ? 1.15145 1.27951 1.06374 0.06516  0.05228  0.16981  353 SER A OG  
3281 N N   . LEU A 475 ? 0.87311 0.95994 0.78229 0.05736  0.02794  0.12043  354 LEU A N   
3282 C CA  . LEU A 475 ? 0.79211 0.86642 0.71297 0.05443  0.02761  0.11046  354 LEU A CA  
3283 C C   . LEU A 475 ? 0.94908 1.01817 0.85268 0.05841  0.02716  0.09576  354 LEU A C   
3284 O O   . LEU A 475 ? 0.79808 0.86209 0.68473 0.05857  0.02242  0.08674  354 LEU A O   
3285 C CB  . LEU A 475 ? 0.67005 0.73088 0.60350 0.04845  0.02135  0.10739  354 LEU A CB  
3286 C CG  . LEU A 475 ? 0.78857 0.83689 0.73009 0.04498  0.01998  0.09668  354 LEU A CG  
3287 C CD1 . LEU A 475 ? 0.73411 0.78797 0.69277 0.04236  0.02578  0.10203  354 LEU A CD1 
3288 C CD2 . LEU A 475 ? 0.77587 0.81059 0.72501 0.03939  0.01451  0.09212  354 LEU A CD2 
3289 N N   . ALA A 476 ? 0.81806 0.88881 0.72720 0.06147  0.03265  0.09359  355 ALA A N   
3290 C CA  . ALA A 476 ? 0.69032 0.75299 0.58751 0.06675  0.03401  0.08115  355 ALA A CA  
3291 C C   . ALA A 476 ? 0.81322 0.86275 0.72162 0.06360  0.02932  0.07510  355 ALA A C   
3292 O O   . ALA A 476 ? 0.86479 0.91835 0.79235 0.05930  0.02865  0.08066  355 ALA A O   
3293 C CB  . ALA A 476 ? 0.64855 0.72356 0.54586 0.07440  0.04367  0.08402  355 ALA A CB  
3294 N N   . VAL A 477 ? 0.82763 0.86134 0.72319 0.06482  0.02663  0.06343  356 VAL A N   
3295 C CA  . VAL A 477 ? 0.80893 0.82880 0.71121 0.06217  0.02251  0.05801  356 VAL A CA  
3296 C C   . VAL A 477 ? 0.98574 0.99735 0.87949 0.07071  0.02720  0.05137  356 VAL A C   
3297 O O   . VAL A 477 ? 0.89972 0.89771 0.77608 0.07329  0.02921  0.04183  356 VAL A O   
3298 C CB  . VAL A 477 ? 0.82396 0.83006 0.72131 0.05519  0.01586  0.05167  356 VAL A CB  
3299 C CG1 . VAL A 477 ? 0.79945 0.79164 0.70325 0.05210  0.01283  0.04717  356 VAL A CG1 
3300 C CG2 . VAL A 477 ? 0.63209 0.64724 0.53871 0.04940  0.01257  0.06003  356 VAL A CG2 
3301 N N   . PRO A 478 ? 0.83958 0.85963 0.74607 0.07521  0.02950  0.05641  357 PRO A N   
3302 C CA  . PRO A 478 ? 0.81818 0.83165 0.71921 0.08588  0.03489  0.05292  357 PRO A CA  
3303 C C   . PRO A 478 ? 0.84511 0.83409 0.73634 0.08496  0.03220  0.04439  357 PRO A C   
3304 O O   . PRO A 478 ? 0.85153 0.83293 0.74551 0.07585  0.02526  0.04268  357 PRO A O   
3305 C CB  . PRO A 478 ? 0.75263 0.78546 0.67390 0.08855  0.03466  0.06221  357 PRO A CB  
3306 C CG  . PRO A 478 ? 0.79846 0.84811 0.73384 0.07890  0.03184  0.06927  357 PRO A CG  
3307 C CD  . PRO A 478 ? 0.83634 0.87237 0.76389 0.06999  0.02706  0.06532  357 PRO A CD  
3308 N N   . ALA A 479 ? 0.77916 0.75445 0.65918 0.09470  0.03939  0.03914  358 ALA A N   
3309 C CA  . ALA A 479 ? 0.91789 0.86792 0.78922 0.09486  0.03922  0.03233  358 ALA A CA  
3310 C C   . ALA A 479 ? 0.83654 0.78932 0.72059 0.09222  0.03252  0.03885  358 ALA A C   
3311 O O   . ALA A 479 ? 0.87433 0.84705 0.77277 0.09600  0.03106  0.04814  358 ALA A O   
3312 C CB  . ALA A 479 ? 0.78364 0.71902 0.64511 0.10813  0.05049  0.02865  358 ALA A CB  
3313 N N   . GLY A 480 ? 0.77625 0.71046 0.65458 0.08484  0.02859  0.03345  359 GLY A N   
3314 C CA  . GLY A 480 ? 0.72694 0.66152 0.61304 0.08135  0.02290  0.03815  359 GLY A CA  
3315 C C   . GLY A 480 ? 0.71772 0.66868 0.61669 0.07021  0.01524  0.04149  359 GLY A C   
3316 O O   . GLY A 480 ? 0.83582 0.78507 0.73852 0.06466  0.01068  0.04271  359 GLY A O   
3317 N N   . VAL A 481 ? 0.73039 0.69569 0.63537 0.06669  0.01481  0.04303  360 VAL A N   
3318 C CA  . VAL A 481 ? 0.77393 0.75059 0.69168 0.05616  0.00985  0.04611  360 VAL A CA  
3319 C C   . VAL A 481 ? 0.79236 0.75590 0.70583 0.04778  0.00739  0.04037  360 VAL A C   
3320 O O   . VAL A 481 ? 0.75772 0.71456 0.66089 0.04900  0.00889  0.03577  360 VAL A O   
3321 C CB  . VAL A 481 ? 0.77472 0.77279 0.70262 0.05716  0.01212  0.05290  360 VAL A CB  
3322 C CG1 . VAL A 481 ? 0.69948 0.70386 0.63995 0.04617  0.00927  0.05586  360 VAL A CG1 
3323 C CG2 . VAL A 481 ? 0.61127 0.62721 0.54831 0.06414  0.01403  0.05922  360 VAL A CG2 
3324 N N   . CYS A 482 ? 0.80495 0.76635 0.72665 0.03894  0.00383  0.04024  361 CYS A N   
3325 C CA  . CYS A 482 ? 0.74004 0.69259 0.66297 0.03133  0.00199  0.03659  361 CYS A CA  
3326 C C   . CYS A 482 ? 0.83531 0.79901 0.77343 0.02550  0.00170  0.04230  361 CYS A C   
3327 O O   . CYS A 482 ? 0.81424 0.78842 0.76223 0.02355  0.00239  0.04660  361 CYS A O   
3328 C CB  . CYS A 482 ? 0.66347 0.60064 0.58344 0.02641  0.00075  0.03131  361 CYS A CB  
3329 S SG  . CYS A 482 ? 0.77678 0.69712 0.68032 0.03323  0.00303  0.02687  361 CYS A SG  
3330 N N   . VAL A 483 ? 0.80793 0.76912 0.74910 0.02217  0.00103  0.04240  362 VAL A N   
3331 C CA  . VAL A 483 ? 0.67198 0.64058 0.62782 0.01838  0.00245  0.04942  362 VAL A CA  
3332 C C   . VAL A 483 ? 0.83264 0.79104 0.79533 0.01271  0.00206  0.04664  362 VAL A C   
3333 O O   . VAL A 483 ? 0.81209 0.76787 0.77015 0.01351  -0.00020 0.04405  362 VAL A O   
3334 C CB  . VAL A 483 ? 0.75678 0.73766 0.71100 0.02325  0.00308  0.05664  362 VAL A CB  
3335 C CG1 . VAL A 483 ? 0.61090 0.59654 0.58102 0.02034  0.00560  0.06601  362 VAL A CG1 
3336 C CG2 . VAL A 483 ? 0.70694 0.69867 0.65564 0.02910  0.00549  0.05958  362 VAL A CG2 
3337 N N   . ASP A 484 ? 0.81648 0.77014 0.79072 0.00642  0.00483  0.04651  363 ASP A N   
3338 C CA  . ASP A 484 ? 0.61548 0.55944 0.59873 0.00173  0.00687  0.04443  363 ASP A CA  
3339 C C   . ASP A 484 ? 0.68672 0.63278 0.68732 -0.00045 0.01222  0.05212  363 ASP A C   
3340 O O   . ASP A 484 ? 0.75528 0.70533 0.76119 -0.00313 0.01509  0.05494  363 ASP A O   
3341 C CB  . ASP A 484 ? 0.66957 0.60126 0.64868 -0.00429 0.00767  0.03541  363 ASP A CB  
3342 C CG  . ASP A 484 ? 0.85968 0.78083 0.84860 -0.00918 0.01187  0.03247  363 ASP A CG  
3343 O OD1 . ASP A 484 ? 0.74698 0.66827 0.73920 -0.00662 0.01111  0.03363  363 ASP A OD1 
3344 O OD2 . ASP A 484 ? 0.73665 0.65057 0.73005 -0.01596 0.01622  0.02839  363 ASP A OD2 
3345 N N   . VAL A 485 ? 0.75017 0.69450 0.76088 0.00103  0.01410  0.05644  364 VAL A N   
3346 C CA  . VAL A 485 ? 0.65548 0.59724 0.68444 0.00008  0.02132  0.06459  364 VAL A CA  
3347 C C   . VAL A 485 ? 0.65518 0.58395 0.69434 -0.00317 0.02606  0.05992  364 VAL A C   
3348 O O   . VAL A 485 ? 0.75598 0.68577 0.79266 -0.00108 0.02255  0.05703  364 VAL A O   
3349 C CB  . VAL A 485 ? 0.62400 0.57908 0.65807 0.00802  0.02060  0.07877  364 VAL A CB  
3350 C CG1 . VAL A 485 ? 0.66628 0.61531 0.72096 0.00846  0.02980  0.08904  364 VAL A CG1 
3351 C CG2 . VAL A 485 ? 0.60306 0.57036 0.62668 0.01081  0.01817  0.08295  364 VAL A CG2 
3352 N N   . VAL A 486 ? 0.62879 0.54522 0.67978 -0.00905 0.03501  0.05828  365 VAL A N   
3353 C CA  . VAL A 486 ? 0.70311 0.60495 0.76297 -0.01270 0.04195  0.05200  365 VAL A CA  
3354 C C   . VAL A 486 ? 0.73149 0.62495 0.81276 -0.01114 0.05320  0.06064  365 VAL A C   
3355 O O   . VAL A 486 ? 0.82190 0.70845 0.90842 -0.01651 0.05973  0.06112  365 VAL A O   
3356 C CB  . VAL A 486 ? 0.71109 0.60132 0.76094 -0.02317 0.04395  0.03741  365 VAL A CB  
3357 C CG1 . VAL A 486 ? 0.66078 0.53533 0.71905 -0.02680 0.05310  0.03067  365 VAL A CG1 
3358 C CG2 . VAL A 486 ? 0.59904 0.49555 0.62878 -0.02301 0.03426  0.03116  365 VAL A CG2 
3359 N N   . PRO A 487 ? 0.69475 0.58922 0.79024 -0.00368 0.05633  0.06842  366 PRO A N   
3360 C CA  . PRO A 487 ? 0.79362 0.67764 0.91122 -0.00033 0.06901  0.07824  366 PRO A CA  
3361 C C   . PRO A 487 ? 0.69536 0.55514 0.81807 -0.01052 0.08191  0.06571  366 PRO A C   
3362 O O   . PRO A 487 ? 0.74811 0.60050 0.86171 -0.01720 0.08196  0.05125  366 PRO A O   
3363 C CB  . PRO A 487 ? 0.68173 0.57516 0.81296 0.01013  0.06827  0.08748  366 PRO A CB  
3364 C CG  . PRO A 487 ? 0.71324 0.62403 0.82789 0.01059  0.05390  0.08219  366 PRO A CG  
3365 C CD  . PRO A 487 ? 0.70419 0.60643 0.79842 0.00038  0.05068  0.06647  366 PRO A CD  
3366 N N   . MET A 488 ? 0.73226 0.57887 0.86895 -0.01220 0.09387  0.07126  367 MET A N   
3367 C CA  . MET A 488 ? 0.81088 0.63384 0.95054 -0.02463 0.10680  0.05764  367 MET A CA  
3368 C C   . MET A 488 ? 0.82674 0.63191 0.99058 -0.02023 0.12381  0.06844  367 MET A C   
3369 O O   . MET A 488 ? 0.81594 0.62737 0.98855 -0.01339 0.12449  0.08522  367 MET A O   
3370 C CB  . MET A 488 ? 0.93256 0.75861 1.05796 -0.03741 0.10213  0.04841  367 MET A CB  
3371 C CG  . MET A 488 ? 0.95031 0.75681 1.07328 -0.05363 0.11215  0.03021  367 MET A CG  
3372 S SD  . MET A 488 ? 0.92740 0.72916 1.03341 -0.05942 0.10945  0.01163  367 MET A SD  
3373 C CE  . MET A 488 ? 0.79714 0.62558 0.87931 -0.05843 0.08841  0.01101  367 MET A CE  
3374 N N   . GLY A 489 ? 0.87744 0.65934 1.05146 -0.02387 0.13877  0.05923  368 GLY A N   
3375 C CA  . GLY A 489 ? 0.82335 0.58621 1.02260 -0.01679 0.15674  0.07110  368 GLY A CA  
3376 C C   . GLY A 489 ? 0.83905 0.61885 1.05384 0.00309  0.15307  0.09404  368 GLY A C   
3377 O O   . GLY A 489 ? 0.77931 0.58334 0.98613 0.00966  0.13804  0.09709  368 GLY A O   
3378 N N   . ASP A 490 ? 0.90239 0.66896 1.14025 0.01226  0.16782  0.11057  369 ASP A N   
3379 C CA  . ASP A 490 ? 1.05365 0.83762 1.30904 0.03212  0.16563  0.13452  369 ASP A CA  
3380 C C   . ASP A 490 ? 0.96146 0.77552 1.20687 0.03891  0.14871  0.15127  369 ASP A C   
3381 O O   . ASP A 490 ? 0.93792 0.77804 1.18738 0.05198  0.13823  0.16545  369 ASP A O   
3382 C CB  . ASP A 490 ? 1.14646 0.90590 1.43045 0.04168  0.18808  0.14917  369 ASP A CB  
3383 C CG  . ASP A 490 ? 1.18194 0.91425 1.47864 0.03924  0.20602  0.13474  369 ASP A CG  
3384 O OD1 . ASP A 490 ? 1.17396 0.91802 1.46763 0.04079  0.19970  0.12580  369 ASP A OD1 
3385 O OD2 . ASP A 490 ? 1.21834 0.91655 1.52778 0.03511  0.22762  0.13167  369 ASP A OD2 
3386 N N   . LYS A 491 ? 1.02042 0.83337 1.25279 0.02977  0.14596  0.14950  370 LYS A N   
3387 C CA  . LYS A 491 ? 1.03775 0.87806 1.26003 0.03660  0.13223  0.16538  370 LYS A CA  
3388 C C   . LYS A 491 ? 0.99022 0.83962 1.18867 0.02414  0.12113  0.15302  370 LYS A C   
3389 O O   . LYS A 491 ? 1.15358 1.02332 1.34277 0.02889  0.11212  0.16502  370 LYS A O   
3390 C CB  . LYS A 491 ? 1.10313 0.93757 1.34267 0.04659  0.14404  0.19034  370 LYS A CB  
3391 C CG  . LYS A 491 ? 1.21513 1.01162 1.47372 0.04109  0.16762  0.18807  370 LYS A CG  
3392 C CD  . LYS A 491 ? 1.21867 1.00843 1.49940 0.05635  0.18102  0.21694  370 LYS A CD  
3393 C CE  . LYS A 491 ? 1.26346 1.01067 1.56454 0.05097  0.20714  0.21377  370 LYS A CE  
3394 N NZ  . LYS A 491 ? 1.32587 1.06389 1.65157 0.06902  0.22218  0.24394  370 LYS A NZ  
3395 N N   . GLY A 492 ? 0.98983 0.82686 1.17787 0.00908  0.12158  0.13028  371 GLY A N   
3396 C CA  . GLY A 492 ? 0.83676 0.68380 1.00592 -0.00152 0.11228  0.12064  371 GLY A CA  
3397 C C   . GLY A 492 ? 0.89593 0.76426 1.04377 -0.00089 0.09426  0.11163  371 GLY A C   
3398 O O   . GLY A 492 ? 0.84472 0.71649 0.99070 0.00337  0.08941  0.10724  371 GLY A O   
3399 N N   . PHE A 493 ? 0.77853 0.65994 0.91123 -0.00592 0.08577  0.10820  372 PHE A N   
3400 C CA  . PHE A 493 ? 0.66715 0.56554 0.77906 -0.00574 0.07066  0.09943  372 PHE A CA  
3401 C C   . PHE A 493 ? 0.96669 0.86495 1.06795 -0.01795 0.06840  0.08586  372 PHE A C   
3402 O O   . PHE A 493 ? 0.80252 0.70396 0.90743 -0.02230 0.07202  0.09014  372 PHE A O   
3403 C CB  . PHE A 493 ? 0.75173 0.67291 0.85484 0.00470  0.06118  0.11271  372 PHE A CB  
3404 C CG  . PHE A 493 ? 0.89207 0.82066 1.00472 0.01689  0.06111  0.12831  372 PHE A CG  
3405 C CD1 . PHE A 493 ? 0.84058 0.77772 0.94943 0.02164  0.05298  0.12500  372 PHE A CD1 
3406 C CD2 . PHE A 493 ? 0.71739 0.64662 0.84320 0.02357  0.06898  0.14741  372 PHE A CD2 
3407 C CE1 . PHE A 493 ? 0.65451 0.60407 0.77360 0.03257  0.05146  0.13998  372 PHE A CE1 
3408 C CE2 . PHE A 493 ? 0.75695 0.69705 0.89176 0.03599  0.06786  0.16400  372 PHE A CE2 
3409 C CZ  . PHE A 493 ? 0.64209 0.59423 0.77393 0.04039  0.05838  0.16006  372 PHE A CZ  
3410 N N   . VAL A 494 ? 0.87389 0.77028 0.96284 -0.02343 0.06263  0.07062  373 VAL A N   
3411 C CA  . VAL A 494 ? 0.74496 0.64755 0.82207 -0.03275 0.05755  0.05972  373 VAL A CA  
3412 C C   . VAL A 494 ? 0.79964 0.72131 0.86082 -0.02514 0.04529  0.06230  373 VAL A C   
3413 O O   . VAL A 494 ? 0.66299 0.58674 0.71521 -0.01845 0.03910  0.06125  373 VAL A O   
3414 C CB  . VAL A 494 ? 0.67083 0.56150 0.74140 -0.04258 0.05855  0.04307  373 VAL A CB  
3415 C CG1 . VAL A 494 ? 0.63591 0.53888 0.69265 -0.04988 0.05053  0.03428  373 VAL A CG1 
3416 C CG2 . VAL A 494 ? 0.85468 0.72456 0.93979 -0.05174 0.07270  0.03802  373 VAL A CG2 
3417 N N   . ALA A 495 ? 0.76495 0.70012 0.82370 -0.02660 0.04301  0.06522  374 ALA A N   
3418 C CA  . ALA A 495 ? 0.85239 0.80447 0.89688 -0.01931 0.03386  0.06715  374 ALA A CA  
3419 C C   . ALA A 495 ? 0.69116 0.64656 0.72409 -0.02411 0.02775  0.05547  374 ALA A C   
3420 O O   . ALA A 495 ? 0.86427 0.82456 0.90144 -0.03312 0.02896  0.05109  374 ALA A O   
3421 C CB  . ALA A 495 ? 0.76691 0.73326 0.81630 -0.01707 0.03622  0.07768  374 ALA A CB  
3422 N N   . ARG A 496 ? 0.66214 0.61621 0.68078 -0.01838 0.02126  0.05110  375 ARG A N   
3423 C CA  . ARG A 496 ? 0.63337 0.58940 0.63960 -0.02049 0.01576  0.04259  375 ARG A CA  
3424 C C   . ARG A 496 ? 0.63292 0.59835 0.62647 -0.00993 0.01012  0.04558  375 ARG A C   
3425 O O   . ARG A 496 ? 0.65853 0.61632 0.64112 -0.00494 0.00733  0.04265  375 ARG A O   
3426 C CB  . ARG A 496 ? 0.62418 0.56443 0.62485 -0.02446 0.01616  0.03383  375 ARG A CB  
3427 C CG  . ARG A 496 ? 0.64710 0.58882 0.63424 -0.02733 0.01137  0.02654  375 ARG A CG  
3428 C CD  . ARG A 496 ? 0.75467 0.68540 0.72899 -0.02270 0.00917  0.02303  375 ARG A CD  
3429 N NE  . ARG A 496 ? 0.71223 0.62791 0.69139 -0.02728 0.01445  0.01845  375 ARG A NE  
3430 C CZ  . ARG A 496 ? 0.82250 0.72932 0.79953 -0.03609 0.01800  0.01050  375 ARG A CZ  
3431 N NH1 . ARG A 496 ? 0.72307 0.63650 0.69212 -0.04212 0.01525  0.00636  375 ARG A NH1 
3432 N NH2 . ARG A 496 ? 0.64638 0.53963 0.62928 -0.03887 0.02444  0.00670  375 ARG A NH2 
3433 N N   . PRO A 497 ? 0.71213 0.69330 0.70777 -0.00647 0.00978  0.05124  376 PRO A N   
3434 C CA  . PRO A 497 ? 0.65830 0.64709 0.64161 0.00325  0.00605  0.05210  376 PRO A CA  
3435 C C   . PRO A 497 ? 0.68375 0.67376 0.66017 0.00211  0.00206  0.04682  376 PRO A C   
3436 O O   . PRO A 497 ? 0.65136 0.64546 0.63377 -0.00695 0.00136  0.04379  376 PRO A O   
3437 C CB  . PRO A 497 ? 0.61006 0.61681 0.60106 0.00625  0.00876  0.06008  376 PRO A CB  
3438 C CG  . PRO A 497 ? 0.57599 0.58727 0.58283 -0.00529 0.01166  0.06036  376 PRO A CG  
3439 C CD  . PRO A 497 ? 0.81696 0.80931 0.82717 -0.01143 0.01421  0.05696  376 PRO A CD  
3440 N N   . TYR A 498 ? 0.59318 0.57942 0.55620 0.01109  -0.00016 0.04580  377 TYR A N   
3441 C CA  . TYR A 498 ? 0.65194 0.64006 0.60771 0.01269  -0.00357 0.04390  377 TYR A CA  
3442 C C   . TYR A 498 ? 0.73486 0.71946 0.67887 0.02557  -0.00302 0.04568  377 TYR A C   
3443 O O   . TYR A 498 ? 0.71676 0.70004 0.65831 0.03150  -0.00015 0.04692  377 TYR A O   
3444 C CB  . TYR A 498 ? 0.78428 0.75719 0.73409 0.00503  -0.00473 0.03721  377 TYR A CB  
3445 C CG  . TYR A 498 ? 0.72255 0.67533 0.66446 0.00667  -0.00284 0.03329  377 TYR A CG  
3446 C CD1 . TYR A 498 ? 0.70336 0.65019 0.65317 0.00241  -0.00029 0.03227  377 TYR A CD1 
3447 C CD2 . TYR A 498 ? 0.67441 0.61508 0.60242 0.01238  -0.00318 0.03133  377 TYR A CD2 
3448 C CE1 . TYR A 498 ? 0.73549 0.66885 0.68049 0.00322  0.00055  0.02891  377 TYR A CE1 
3449 C CE2 . TYR A 498 ? 0.80973 0.73369 0.73216 0.01182  -0.00129 0.02680  377 TYR A CE2 
3450 C CZ  . TYR A 498 ? 0.68171 0.60415 0.61318 0.00692  -0.00010 0.02536  377 TYR A CZ  
3451 O OH  . TYR A 498 ? 0.74013 0.65095 0.66847 0.00578  0.00089  0.02115  377 TYR A OH  
3452 N N   . GLY A 499 ? 0.76346 0.74608 0.69938 0.03002  -0.00499 0.04599  378 GLY A N   
3453 C CA  . GLY A 499 ? 0.83249 0.80828 0.75817 0.04292  -0.00231 0.04790  378 GLY A CA  
3454 C C   . GLY A 499 ? 0.75720 0.70942 0.66880 0.04384  -0.00140 0.04364  378 GLY A C   
3455 O O   . GLY A 499 ? 0.90333 0.84936 0.81285 0.03571  -0.00376 0.04092  378 GLY A O   
3456 N N   . LEU A 500 ? 0.79873 0.73657 0.70021 0.05306  0.00329  0.04243  379 LEU A N   
3457 C CA  . LEU A 500 ? 0.86395 0.77655 0.75269 0.05269  0.00593  0.03773  379 LEU A CA  
3458 C C   . LEU A 500 ? 1.04360 0.95362 0.92710 0.05567  0.00478  0.04309  379 LEU A C   
3459 O O   . LEU A 500 ? 0.99697 0.88821 0.87153 0.05165  0.00633  0.04003  379 LEU A O   
3460 C CB  . LEU A 500 ? 0.84777 0.74463 0.72685 0.06097  0.01260  0.03414  379 LEU A CB  
3461 C CG  . LEU A 500 ? 1.01221 0.88091 0.87919 0.05802  0.01683  0.02699  379 LEU A CG  
3462 C CD1 . LEU A 500 ? 0.84535 0.71082 0.71482 0.04502  0.01395  0.01910  379 LEU A CD1 
3463 C CD2 . LEU A 500 ? 1.08805 0.94080 0.94503 0.06687  0.02498  0.02319  379 LEU A CD2 
3464 N N   . ASP A 501 ? 1.11654 1.04729 1.00576 0.06239  0.00200  0.05176  380 ASP A N   
3465 C CA  . ASP A 501 ? 1.00768 0.94095 0.89124 0.06678  -0.00016 0.05917  380 ASP A CA  
3466 C C   . ASP A 501 ? 0.84660 0.80503 0.73716 0.05777  -0.00838 0.06148  380 ASP A C   
3467 O O   . ASP A 501 ? 0.98695 0.95278 0.87174 0.06020  -0.01185 0.06803  380 ASP A O   
3468 C CB  . ASP A 501 ? 1.09472 1.03241 0.97824 0.08453  0.00370  0.06906  380 ASP A CB  
3469 C CG  . ASP A 501 ? 1.18763 1.09593 1.06166 0.09290  0.01375  0.06525  380 ASP A CG  
3470 O OD1 . ASP A 501 ? 1.20459 1.08627 1.06718 0.08840  0.01727  0.06018  380 ASP A OD1 
3471 O OD2 . ASP A 501 ? 1.26309 1.17485 1.14105 0.10315  0.01896  0.06653  380 ASP A OD2 
3472 N N   . ASP A 502 ? 0.79417 0.76611 0.69641 0.04727  -0.01114 0.05654  381 ASP A N   
3473 C CA  . ASP A 502 ? 0.77234 0.76135 0.67954 0.03450  -0.01720 0.05454  381 ASP A CA  
3474 C C   . ASP A 502 ? 0.86665 0.83954 0.76002 0.02724  -0.01756 0.05041  381 ASP A C   
3475 O O   . ASP A 502 ? 0.86798 0.81638 0.75525 0.02417  -0.01281 0.04434  381 ASP A O   
3476 C CB  . ASP A 502 ? 0.82415 0.81761 0.74429 0.02323  -0.01649 0.04808  381 ASP A CB  
3477 C CG  . ASP A 502 ? 0.90796 0.92276 0.84256 0.02787  -0.01629 0.05309  381 ASP A CG  
3478 O OD1 . ASP A 502 ? 0.86098 0.88871 0.79674 0.04009  -0.01670 0.06092  381 ASP A OD1 
3479 O OD2 . ASP A 502 ? 0.82386 0.84219 0.76934 0.01992  -0.01463 0.05004  381 ASP A OD2 
3480 N N   . VAL A 503 ? 0.81688 0.80583 0.70526 0.02402  -0.02323 0.05380  382 VAL A N   
3481 C CA  . VAL A 503 ? 0.79027 0.76657 0.66379 0.01591  -0.02315 0.04973  382 VAL A CA  
3482 C C   . VAL A 503 ? 0.85210 0.83725 0.72908 -0.00182 -0.02552 0.03982  382 VAL A C   
3483 O O   . VAL A 503 ? 0.92355 0.89631 0.78857 -0.01039 -0.02359 0.03386  382 VAL A O   
3484 C CB  . VAL A 503 ? 0.93336 0.91871 0.79355 0.02447  -0.02698 0.06063  382 VAL A CB  
3485 C CG1 . VAL A 503 ? 0.92385 0.89036 0.77838 0.04160  -0.02112 0.06940  382 VAL A CG1 
3486 C CG2 . VAL A 503 ? 0.73594 0.75998 0.60482 0.02520  -0.03608 0.06734  382 VAL A CG2 
3487 N N   . PHE A 504 ? 0.95091 0.95537 0.84387 -0.00795 -0.02811 0.03743  383 PHE A N   
3488 C CA  . PHE A 504 ? 0.80521 0.81343 0.70425 -0.02547 -0.02770 0.02661  383 PHE A CA  
3489 C C   . PHE A 504 ? 0.84750 0.86531 0.73214 -0.03576 -0.03216 0.02252  383 PHE A C   
3490 O O   . PHE A 504 ? 0.80206 0.80318 0.67690 -0.04579 -0.02782 0.01323  383 PHE A O   
3491 C CB  . PHE A 504 ? 0.78990 0.77133 0.69337 -0.03045 -0.01932 0.01856  383 PHE A CB  
3492 C CG  . PHE A 504 ? 0.78605 0.76978 0.70768 -0.02855 -0.01660 0.01993  383 PHE A CG  
3493 C CD1 . PHE A 504 ? 0.60109 0.57910 0.52490 -0.01541 -0.01504 0.02638  383 PHE A CD1 
3494 C CD2 . PHE A 504 ? 0.67555 0.66784 0.61107 -0.04035 -0.01507 0.01496  383 PHE A CD2 
3495 C CE1 . PHE A 504 ? 0.69085 0.67305 0.62880 -0.01361 -0.01257 0.02852  383 PHE A CE1 
3496 C CE2 . PHE A 504 ? 0.58261 0.57741 0.53405 -0.03812 -0.01185 0.01832  383 PHE A CE2 
3497 C CZ  . PHE A 504 ? 0.60680 0.59772 0.55871 -0.02443 -0.01101 0.02558  383 PHE A CZ  
3498 N N   . LYS A 505 ? 0.81887 0.86640 0.70251 -0.03252 -0.04086 0.03020  384 LYS A N   
3499 C CA  . LYS A 505 ? 0.93702 1.00433 0.80684 -0.04117 -0.04810 0.02891  384 LYS A CA  
3500 C C   . LYS A 505 ? 0.88696 0.99489 0.76843 -0.03822 -0.05795 0.03745  384 LYS A C   
3501 O O   . LYS A 505 ? 0.99464 1.11017 0.88843 -0.02323 -0.05814 0.04831  384 LYS A O   
3502 C CB  . LYS A 505 ? 0.87654 0.93135 0.72365 -0.03203 -0.04792 0.03617  384 LYS A CB  
3503 C CG  . LYS A 505 ? 0.95010 1.01380 0.77688 -0.04477 -0.05183 0.03059  384 LYS A CG  
3504 C CD  . LYS A 505 ? 1.20544 1.25571 1.01009 -0.03368 -0.05034 0.04083  384 LYS A CD  
3505 C CE  . LYS A 505 ? 1.37222 1.41651 1.15378 -0.04776 -0.04871 0.03163  384 LYS A CE  
3506 N NZ  . LYS A 505 ? 1.19568 1.20106 0.97348 -0.05161 -0.03582 0.02199  384 LYS A NZ  
3507 N N   . GLY A 506 ? 0.89506 1.03027 0.77322 -0.05321 -0.06564 0.03172  385 GLY A N   
3508 C CA  . GLY A 506 ? 0.80484 0.98404 0.69613 -0.05164 -0.07598 0.03996  385 GLY A CA  
3509 C C   . GLY A 506 ? 0.86957 1.06995 0.77817 -0.07169 -0.07799 0.02816  385 GLY A C   
3510 O O   . GLY A 506 ? 0.92670 1.10436 0.84491 -0.08130 -0.06897 0.01716  385 GLY A O   
3511 N N   . ASP A 507 ? 0.82484 1.06991 0.73830 -0.07818 -0.08964 0.03111  386 ASP A N   
3512 C CA  . ASP A 507 ? 0.73925 1.01056 0.67365 -0.09627 -0.09202 0.02213  386 ASP A CA  
3513 C C   . ASP A 507 ? 0.70835 0.98297 0.66929 -0.08469 -0.08703 0.03094  386 ASP A C   
3514 O O   . ASP A 507 ? 0.62796 0.90552 0.59239 -0.06206 -0.08728 0.04679  386 ASP A O   
3515 C CB  . ASP A 507 ? 0.87204 1.19602 0.80568 -0.10523 -0.10723 0.02452  386 ASP A CB  
3516 C CG  . ASP A 507 ? 0.92090 1.27203 0.87424 -0.12941 -0.10962 0.01155  386 ASP A CG  
3517 O OD1 . ASP A 507 ? 0.88284 1.25856 0.86280 -0.12504 -0.11061 0.01929  386 ASP A OD1 
3518 O OD2 . ASP A 507 ? 1.01576 1.36293 0.95797 -0.15343 -0.10940 -0.00699 386 ASP A OD2 
3519 N N   . LEU A 508 ? 0.66150 0.93280 0.64026 -0.10023 -0.08081 0.02043  387 LEU A N   
3520 C CA  . LEU A 508 ? 0.85765 1.12985 0.85989 -0.09086 -0.07436 0.02816  387 LEU A CA  
3521 C C   . LEU A 508 ? 0.90053 1.22115 0.92148 -0.08244 -0.08275 0.04145  387 LEU A C   
3522 O O   . LEU A 508 ? 0.77982 1.10172 0.81534 -0.06677 -0.07760 0.05222  387 LEU A O   
3523 C CB  . LEU A 508 ? 0.83500 1.09335 0.85192 -0.11039 -0.06507 0.01523  387 LEU A CB  
3524 C CG  . LEU A 508 ? 0.94408 1.15584 0.94835 -0.11894 -0.05470 0.00241  387 LEU A CG  
3525 C CD1 . LEU A 508 ? 0.93877 1.14087 0.96107 -0.13721 -0.04497 -0.00775 387 LEU A CD1 
3526 C CD2 . LEU A 508 ? 0.86900 1.04666 0.86484 -0.09813 -0.04804 0.01061  387 LEU A CD2 
3527 N N   . ARG A 509 ? 0.74973 1.11198 0.77099 -0.09249 -0.09527 0.04092  388 ARG A N   
3528 C CA  . ARG A 509 ? 0.78350 1.19789 0.82599 -0.08536 -0.10396 0.05399  388 ARG A CA  
3529 C C   . ARG A 509 ? 0.74662 1.17313 0.78134 -0.05792 -0.10968 0.07339  388 ARG A C   
3530 O O   . ARG A 509 ? 0.69266 1.16671 0.74318 -0.05019 -0.11850 0.08603  388 ARG A O   
3531 C CB  . ARG A 509 ? 0.82379 1.28337 0.87308 -0.11024 -0.11571 0.04465  388 ARG A CB  
3532 C CG  . ARG A 509 ? 1.04614 1.50240 1.11295 -0.13634 -0.10860 0.02830  388 ARG A CG  
3533 C CD  . ARG A 509 ? 1.09687 1.60204 1.17280 -0.16222 -0.12035 0.01837  388 ARG A CD  
3534 N NE  . ARG A 509 ? 1.11499 1.62385 1.21569 -0.18430 -0.11247 0.00693  388 ARG A NE  
3535 C CZ  . ARG A 509 ? 1.10537 1.58022 1.20108 -0.20742 -0.10260 -0.01281 388 ARG A CZ  
3536 N NH1 . ARG A 509 ? 1.21329 1.64909 1.28052 -0.21120 -0.09942 -0.02394 388 ARG A NH1 
3537 N NH2 . ARG A 509 ? 1.10364 1.58251 1.22382 -0.22634 -0.09444 -0.02089 388 ARG A NH2 
3538 N N   . ASP A 510 ? 0.80669 1.19199 0.81899 -0.04316 -0.10422 0.07648  389 ASP A N   
3539 C CA  . ASP A 510 ? 0.87222 1.25990 0.87731 -0.01609 -0.10605 0.09501  389 ASP A CA  
3540 C C   . ASP A 510 ? 0.94284 1.30235 0.95656 0.00340  -0.09320 0.10161  389 ASP A C   
3541 O O   . ASP A 510 ? 0.81577 1.13542 0.82460 -0.00138 -0.08310 0.09146  389 ASP A O   
3542 C CB  . ASP A 510 ? 0.82671 1.18764 0.80027 -0.01352 -0.10771 0.09427  389 ASP A CB  
3543 C CG  . ASP A 510 ? 0.96225 1.33026 0.92826 0.01281  -0.11045 0.11498  389 ASP A CG  
3544 O OD1 . ASP A 510 ? 0.98108 1.35610 0.96354 0.03318  -0.10605 0.12831  389 ASP A OD1 
3545 O OD2 . ASP A 510 ? 1.08169 1.44732 1.02478 0.01347  -0.11589 0.11834  389 ASP A OD2 
3546 N N   . SER A 511 ? 0.95644 1.33783 0.98282 0.02567  -0.09329 0.11874  390 SER A N   
3547 C CA  . SER A 511 ? 0.91938 1.27700 0.95327 0.04382  -0.08044 0.12398  390 SER A CA  
3548 C C   . SER A 511 ? 0.83654 1.14266 0.84659 0.05681  -0.07196 0.12380  390 SER A C   
3549 O O   . SER A 511 ? 0.81846 1.09804 0.83009 0.06733  -0.06072 0.12344  390 SER A O   
3550 C CB  . SER A 511 ? 0.84796 1.24359 0.90313 0.06438  -0.08112 0.14173  390 SER A CB  
3551 O OG  . SER A 511 ? 0.98636 1.37402 1.02946 0.08736  -0.08086 0.15608  390 SER A OG  
3552 N N   . LYS A 512 ? 0.81535 1.10766 0.80307 0.05532  -0.07666 0.12361  391 LYS A N   
3553 C CA  . LYS A 512 ? 0.86101 1.10429 0.82697 0.06440  -0.06817 0.12211  391 LYS A CA  
3554 C C   . LYS A 512 ? 0.82277 1.03060 0.77802 0.04636  -0.06341 0.10434  391 LYS A C   
3555 O O   . LYS A 512 ? 0.85602 1.02376 0.79814 0.05223  -0.05504 0.10119  391 LYS A O   
3556 C CB  . LYS A 512 ? 1.01029 1.25385 0.95722 0.07255  -0.07362 0.13219  391 LYS A CB  
3557 C CG  . LYS A 512 ? 1.14279 1.41435 1.09900 0.09592  -0.07602 0.15329  391 LYS A CG  
3558 C CD  . LYS A 512 ? 1.15692 1.42935 1.09301 0.10345  -0.08153 0.16508  391 LYS A CD  
3559 C CE  . LYS A 512 ? 1.33974 1.64301 1.28726 0.12825  -0.08401 0.18868  391 LYS A CE  
3560 N NZ  . LYS A 512 ? 1.34956 1.71262 1.32281 0.12455  -0.09499 0.19372  391 LYS A NZ  
3561 N N   . THR A 513 ? 0.63857 0.86061 0.60028 0.02458  -0.06792 0.09281  392 THR A N   
3562 C CA  . THR A 513 ? 0.66745 0.85849 0.62442 0.00867  -0.06187 0.07720  392 THR A CA  
3563 C C   . THR A 513 ? 0.78957 0.96917 0.76137 0.01272  -0.05297 0.07600  392 THR A C   
3564 O O   . THR A 513 ? 0.75343 0.95995 0.74522 0.00979  -0.05366 0.07815  392 THR A O   
3565 C CB  . THR A 513 ? 0.77381 0.98302 0.73373 -0.01549 -0.06783 0.06547  392 THR A CB  
3566 O OG1 . THR A 513 ? 0.88989 1.11447 0.83376 -0.01921 -0.07695 0.06702  392 THR A OG1 
3567 C CG2 . THR A 513 ? 0.83699 1.01118 0.79208 -0.03001 -0.05989 0.05045  392 THR A CG2 
3568 N N   . THR A 514 ? 0.72617 0.86797 0.68812 0.01868  -0.04465 0.07271  393 THR A N   
3569 C CA  . THR A 514 ? 0.75112 0.88200 0.72232 0.02572  -0.03648 0.07340  393 THR A CA  
3570 C C   . THR A 514 ? 0.71732 0.82225 0.68718 0.01343  -0.03109 0.06260  393 THR A C   
3571 O O   . THR A 514 ? 0.90595 0.98974 0.86376 0.00537  -0.03098 0.05512  393 THR A O   
3572 C CB  . THR A 514 ? 0.84011 0.95173 0.80155 0.04587  -0.03086 0.08010  393 THR A CB  
3573 O OG1 . THR A 514 ? 0.71192 0.78988 0.65449 0.04472  -0.02864 0.07462  393 THR A OG1 
3574 C CG2 . THR A 514 ? 0.61406 0.74905 0.57810 0.06105  -0.03443 0.09301  393 THR A CG2 
3575 N N   . LEU A 515 ? 0.77751 0.88527 0.76044 0.01305  -0.02590 0.06309  394 LEU A N   
3576 C CA  . LEU A 515 ? 0.72739 0.81079 0.70982 0.00732  -0.01960 0.05711  394 LEU A CA  
3577 C C   . LEU A 515 ? 0.84585 0.92431 0.82899 0.02081  -0.01365 0.06238  394 LEU A C   
3578 O O   . LEU A 515 ? 0.98448 1.08457 0.97953 0.02586  -0.01195 0.06867  394 LEU A O   
3579 C CB  . LEU A 515 ? 0.62190 0.71371 0.61916 -0.00955 -0.01822 0.05248  394 LEU A CB  
3580 C CG  . LEU A 515 ? 0.74458 0.81348 0.74412 -0.01381 -0.01103 0.04935  394 LEU A CG  
3581 C CD1 . LEU A 515 ? 0.71165 0.75249 0.69739 -0.01620 -0.01046 0.04232  394 LEU A CD1 
3582 C CD2 . LEU A 515 ? 0.49882 0.57575 0.51546 -0.02866 -0.00739 0.04716  394 LEU A CD2 
3583 N N   . THR A 516 ? 0.75859 0.81011 0.72882 0.02581  -0.01021 0.05921  395 THR A N   
3584 C CA  . THR A 516 ? 0.71583 0.76004 0.68117 0.03816  -0.00480 0.06189  395 THR A CA  
3585 C C   . THR A 516 ? 0.64654 0.70181 0.61017 0.05305  -0.00388 0.06825  395 THR A C   
3586 O O   . THR A 516 ? 0.67153 0.73459 0.63850 0.06236  0.00138  0.07215  395 THR A O   
3587 C CB  . THR A 516 ? 0.73696 0.78977 0.71301 0.03538  -0.00035 0.06436  395 THR A CB  
3588 O OG1 . THR A 516 ? 0.65599 0.73713 0.64742 0.03566  -0.00009 0.07057  395 THR A OG1 
3589 C CG2 . THR A 516 ? 0.56270 0.60586 0.54392 0.02183  -0.00019 0.06044  395 THR A CG2 
3590 N N   . GLY A 517 ? 0.73087 0.78677 0.68903 0.05610  -0.00811 0.07006  396 GLY A N   
3591 C CA  . GLY A 517 ? 0.61710 0.67874 0.57278 0.07243  -0.00630 0.07754  396 GLY A CA  
3592 C C   . GLY A 517 ? 0.86434 0.96196 0.83757 0.07800  -0.00782 0.08667  396 GLY A C   
3593 O O   . GLY A 517 ? 0.74661 0.85091 0.72076 0.09406  -0.00484 0.09450  396 GLY A O   
3594 N N   . ILE A 518 ? 0.76646 0.88745 0.75509 0.06536  -0.01139 0.08615  397 ILE A N   
3595 C CA  . ILE A 518 ? 0.85205 1.01189 0.86034 0.06780  -0.01365 0.09435  397 ILE A CA  
3596 C C   . ILE A 518 ? 0.89852 1.07974 0.91393 0.05192  -0.02367 0.09243  397 ILE A C   
3597 O O   . ILE A 518 ? 0.75566 0.92016 0.76369 0.03694  -0.02595 0.08329  397 ILE A O   
3598 C CB  . ILE A 518 ? 0.88014 1.05178 0.90235 0.06656  -0.00669 0.09554  397 ILE A CB  
3599 C CG1 . ILE A 518 ? 0.88653 1.05298 0.91340 0.04707  -0.00735 0.08850  397 ILE A CG1 
3600 C CG2 . ILE A 518 ? 0.76239 0.91231 0.77343 0.08063  0.00325  0.09537  397 ILE A CG2 
3601 C CD1 . ILE A 518 ? 0.95666 1.14754 1.00371 0.04163  -0.00289 0.09246  397 ILE A CD1 
3602 N N   . PRO A 519 ? 0.68825 0.90706 0.71767 0.05442  -0.02961 0.10031  398 PRO A N   
3603 C CA  . PRO A 519 ? 0.68106 0.92261 0.71474 0.03769  -0.04014 0.09697  398 PRO A CA  
3604 C C   . PRO A 519 ? 0.77195 1.01341 0.81508 0.01564  -0.03891 0.08667  398 PRO A C   
3605 O O   . PRO A 519 ? 0.61721 0.86586 0.67537 0.01398  -0.03247 0.08794  398 PRO A O   
3606 C CB  . PRO A 519 ? 0.79178 1.08010 0.84387 0.04595  -0.04569 0.10887  398 PRO A CB  
3607 C CG  . PRO A 519 ? 0.59082 0.87029 0.64000 0.07166  -0.03850 0.11952  398 PRO A CG  
3608 C CD  . PRO A 519 ? 0.64823 0.89096 0.68919 0.07366  -0.02701 0.11275  398 PRO A CD  
3609 N N   . PHE A 520 ? 0.56788 0.79892 0.60133 -0.00102 -0.04366 0.07662  399 PHE A N   
3610 C CA  . PHE A 520 ? 0.71287 0.93708 0.75411 -0.02198 -0.04047 0.06594  399 PHE A CA  
3611 C C   . PHE A 520 ? 0.68901 0.94908 0.75569 -0.03155 -0.04053 0.06812  399 PHE A C   
3612 O O   . PHE A 520 ? 0.79211 1.04449 0.87029 -0.03820 -0.03221 0.06639  399 PHE A O   
3613 C CB  . PHE A 520 ? 0.66623 0.88071 0.69461 -0.03869 -0.04551 0.05442  399 PHE A CB  
3614 C CG  . PHE A 520 ? 0.67630 0.87278 0.71025 -0.05808 -0.03901 0.04264  399 PHE A CG  
3615 C CD1 . PHE A 520 ? 0.57047 0.72855 0.59699 -0.05581 -0.03037 0.03921  399 PHE A CD1 
3616 C CD2 . PHE A 520 ? 0.82433 1.04279 0.87228 -0.07852 -0.04090 0.03537  399 PHE A CD2 
3617 C CE1 . PHE A 520 ? 0.72825 0.86891 0.76168 -0.07132 -0.02303 0.03051  399 PHE A CE1 
3618 C CE2 . PHE A 520 ? 0.71089 0.90870 0.76471 -0.09572 -0.03260 0.02483  399 PHE A CE2 
3619 C CZ  . PHE A 520 ? 0.83299 0.99125 0.87984 -0.09097 -0.02327 0.02331  399 PHE A CZ  
3620 N N   . GLY A 521 ? 0.69963 1.00047 0.77595 -0.03347 -0.04988 0.07229  400 GLY A N   
3621 C CA  . GLY A 521 ? 0.71836 1.05752 0.82128 -0.04426 -0.05035 0.07396  400 GLY A CA  
3622 C C   . GLY A 521 ? 0.66700 1.00955 0.78501 -0.03124 -0.04030 0.08351  400 GLY A C   
3623 O O   . GLY A 521 ? 0.64708 0.99744 0.78295 -0.04311 -0.03381 0.08183  400 GLY A O   
3624 N N   . GLU A 522 ? 0.55756 0.89304 0.66779 -0.00703 -0.03766 0.09341  401 GLU A N   
3625 C CA  . GLU A 522 ? 0.57601 0.90854 0.69474 0.00635  -0.02647 0.10080  401 GLU A CA  
3626 C C   . GLU A 522 ? 0.67914 0.97505 0.79051 -0.00066 -0.01676 0.09455  401 GLU A C   
3627 O O   . GLU A 522 ? 0.74334 1.04558 0.86833 -0.00272 -0.00812 0.09792  401 GLU A O   
3628 C CB  . GLU A 522 ? 0.72487 1.04960 0.83229 0.03253  -0.02442 0.10966  401 GLU A CB  
3629 C CG  . GLU A 522 ? 0.76157 1.07808 0.87165 0.04744  -0.01184 0.11516  401 GLU A CG  
3630 C CD  . GLU A 522 ? 0.99089 1.30388 1.09308 0.07256  -0.00884 0.12326  401 GLU A CD  
3631 O OE1 . GLU A 522 ? 1.17847 1.46522 1.26864 0.08463  0.00126  0.12274  401 GLU A OE1 
3632 O OE2 . GLU A 522 ? 0.79656 1.13304 0.90422 0.08012  -0.01623 0.13022  401 GLU A OE2 
3633 N N   . TRP A 523 ? 0.70904 0.96761 0.79922 -0.00299 -0.01751 0.08695  402 TRP A N   
3634 C CA  . TRP A 523 ? 0.68901 0.91551 0.77353 -0.00896 -0.00927 0.08244  402 TRP A CA  
3635 C C   . TRP A 523 ? 0.73085 0.96601 0.83340 -0.02966 -0.00575 0.07862  402 TRP A C   
3636 O O   . TRP A 523 ? 0.76363 0.98729 0.87167 -0.03169 0.00366  0.08124  402 TRP A O   
3637 C CB  . TRP A 523 ? 0.69554 0.88626 0.75817 -0.00980 -0.01162 0.07468  402 TRP A CB  
3638 C CG  . TRP A 523 ? 0.69269 0.85242 0.74982 -0.01272 -0.00389 0.07196  402 TRP A CG  
3639 C CD1 . TRP A 523 ? 0.58404 0.72357 0.62901 0.00042  0.00086  0.07492  402 TRP A CD1 
3640 C CD2 . TRP A 523 ? 0.66590 0.81229 0.72967 -0.02948 0.00006  0.06618  402 TRP A CD2 
3641 N NE1 . TRP A 523 ? 0.64949 0.76794 0.69388 -0.00639 0.00616  0.07296  402 TRP A NE1 
3642 C CE2 . TRP A 523 ? 0.64596 0.76650 0.70243 -0.02371 0.00660  0.06826  402 TRP A CE2 
3643 C CE3 . TRP A 523 ? 0.57639 0.72996 0.65163 -0.04903 -0.00066 0.05912  402 TRP A CE3 
3644 C CZ2 . TRP A 523 ? 0.63663 0.73856 0.69855 -0.03453 0.01275  0.06587  402 TRP A CZ2 
3645 C CZ3 . TRP A 523 ? 0.66697 0.79805 0.74678 -0.06078 0.00695  0.05483  402 TRP A CZ3 
3646 C CH2 . TRP A 523 ? 0.54788 0.65344 0.62183 -0.05240 0.01374  0.05934  402 TRP A CH2 
3647 N N   . MET A 524 ? 0.67480 0.92961 0.78577 -0.04577 -0.01280 0.07236  403 MET A N   
3648 C CA  . MET A 524 ? 0.75858 1.02110 0.88742 -0.06792 -0.00873 0.06674  403 MET A CA  
3649 C C   . MET A 524 ? 0.74200 1.03660 0.89496 -0.06792 -0.00353 0.07559  403 MET A C   
3650 O O   . MET A 524 ? 0.73114 1.01957 0.89697 -0.07851 0.00640  0.07613  403 MET A O   
3651 C CB  . MET A 524 ? 0.77491 1.05294 0.90433 -0.08625 -0.01830 0.05582  403 MET A CB  
3652 C CG  . MET A 524 ? 0.99218 1.23886 1.09886 -0.09023 -0.02153 0.04545  403 MET A CG  
3653 S SD  . MET A 524 ? 1.05477 1.27168 1.16422 -0.11542 -0.01267 0.03062  403 MET A SD  
3654 C CE  . MET A 524 ? 1.06637 1.25090 1.17965 -0.10480 0.00168  0.03938  403 MET A CE  
3655 N N   . SER A 525 ? 0.55620 0.88527 0.71661 -0.05547 -0.00897 0.08363  404 SER A N   
3656 C CA  . SER A 525 ? 0.63539 1.00096 0.82227 -0.05764 -0.00422 0.09131  404 SER A CA  
3657 C C   . SER A 525 ? 0.63376 0.98823 0.82065 -0.04187 0.00839  0.10132  404 SER A C   
3658 O O   . SER A 525 ? 0.60159 0.97127 0.80793 -0.04877 0.01731  0.10605  404 SER A O   
3659 C CB  . SER A 525 ? 0.51228 0.92460 0.71138 -0.05076 -0.01452 0.09701  404 SER A CB  
3660 O OG  . SER A 525 ? 0.80021 1.20714 0.98492 -0.02490 -0.01636 0.10497  404 SER A OG  
3661 N N   . LYS A 526 ? 0.67043 0.99824 0.83504 -0.02224 0.00999  0.10402  405 LYS A N   
3662 C CA  . LYS A 526 ? 0.85951 1.17226 1.01887 -0.01003 0.02199  0.11098  405 LYS A CA  
3663 C C   . LYS A 526 ? 0.77238 1.06390 0.93419 -0.02384 0.03089  0.10995  405 LYS A C   
3664 O O   . LYS A 526 ? 0.76736 1.05656 0.93056 -0.01772 0.04160  0.11773  405 LYS A O   
3665 C CB  . LYS A 526 ? 0.78554 1.06895 0.91791 0.00900  0.02152  0.11054  405 LYS A CB  
3666 C CG  . LYS A 526 ? 0.96501 1.26295 1.09355 0.02657  0.01643  0.11385  405 LYS A CG  
3667 C CD  . LYS A 526 ? 0.96777 1.23445 1.07123 0.04444  0.02028  0.11322  405 LYS A CD  
3668 C CE  . LYS A 526 ? 0.97778 1.25437 1.07804 0.06318  0.01805  0.11738  405 LYS A CE  
3669 N NZ  . LYS A 526 ? 0.88380 1.12714 0.95943 0.07847  0.02282  0.11470  405 LYS A NZ  
3670 N N   . ARG A 527 ? 0.71246 0.98792 0.87428 -0.04163 0.02773  0.10113  406 ARG A N   
3671 C CA  . ARG A 527 ? 0.66774 0.91834 0.83196 -0.05344 0.03709  0.10083  406 ARG A CA  
3672 C C   . ARG A 527 ? 0.70876 0.97466 0.89731 -0.07680 0.04072  0.09725  406 ARG A C   
3673 O O   . ARG A 527 ? 0.61372 0.85616 0.80609 -0.08922 0.04902  0.09562  406 ARG A O   
3674 C CB  . ARG A 527 ? 0.63348 0.84609 0.77744 -0.05366 0.03382  0.09332  406 ARG A CB  
3675 C CG  . ARG A 527 ? 0.66609 0.86506 0.78764 -0.03255 0.03102  0.09628  406 ARG A CG  
3676 C CD  . ARG A 527 ? 0.59373 0.75974 0.69619 -0.03128 0.02700  0.08924  406 ARG A CD  
3677 N NE  . ARG A 527 ? 0.56103 0.71424 0.64488 -0.01320 0.02749  0.09320  406 ARG A NE  
3678 C CZ  . ARG A 527 ? 0.59882 0.75886 0.67192 0.00053  0.02269  0.09296  406 ARG A CZ  
3679 N NH1 . ARG A 527 ? 0.59117 0.77188 0.67043 0.00001  0.01610  0.09099  406 ARG A NH1 
3680 N NH2 . ARG A 527 ? 0.63415 0.78001 0.69000 0.01455  0.02462  0.09464  406 ARG A NH2 
3681 N N   . GLY A 528 ? 0.66975 0.97500 0.87589 -0.08322 0.03516  0.09621  407 GLY A N   
3682 C CA  . GLY A 528 ? 0.64415 0.96796 0.87486 -0.10747 0.03839  0.09154  407 GLY A CA  
3683 C C   . GLY A 528 ? 0.68268 0.98947 0.90975 -0.12807 0.03377  0.07624  407 GLY A C   
3684 O O   . GLY A 528 ? 0.87765 1.18458 1.12157 -0.15053 0.04040  0.07025  407 GLY A O   
3685 N N   . LEU A 529 ? 0.68612 0.97698 0.89124 -0.12160 0.02385  0.06918  408 LEU A N   
3686 C CA  . LEU A 529 ? 0.81241 1.08319 1.00972 -0.13933 0.02068  0.05392  408 LEU A CA  
3687 C C   . LEU A 529 ? 0.80234 1.10757 1.00033 -0.14809 0.00593  0.04548  408 LEU A C   
3688 O O   . LEU A 529 ? 0.82215 1.15594 1.01817 -0.13285 -0.00363 0.05286  408 LEU A O   
3689 C CB  . LEU A 529 ? 0.64384 0.87249 0.81572 -0.12721 0.02091  0.05189  408 LEU A CB  
3690 C CG  . LEU A 529 ? 0.74808 0.94165 0.91775 -0.12034 0.03420  0.05940  408 LEU A CG  
3691 C CD1 . LEU A 529 ? 0.68165 0.84163 0.82794 -0.10749 0.03208  0.05767  408 LEU A CD1 
3692 C CD2 . LEU A 529 ? 0.85283 1.03037 1.03853 -0.14141 0.04650  0.05460  408 LEU A CD2 
3693 N N   . SER A 530 ? 0.71360 1.01642 0.91428 -0.17274 0.00475  0.03022  409 SER A N   
3694 C CA  . SER A 530 ? 0.83859 1.17320 1.03627 -0.18406 -0.00991 0.02046  409 SER A CA  
3695 C C   . SER A 530 ? 0.83107 1.13352 1.00574 -0.19352 -0.01191 0.00518  409 SER A C   
3696 O O   . SER A 530 ? 0.81128 1.06894 0.97790 -0.19419 -0.00071 0.00129  409 SER A O   
3697 C CB  . SER A 530 ? 0.94538 1.31859 1.16963 -0.20931 -0.01057 0.01407  409 SER A CB  
3698 O OG  . SER A 530 ? 0.94145 1.28801 1.16918 -0.23550 -0.00068 -0.00167 409 SER A OG  
3699 N N   . TYR A 531 ? 0.75022 1.07760 0.91428 -0.20007 -0.02610 -0.00258 410 TYR A N   
3700 C CA  . TYR A 531 ? 0.88964 1.19079 1.03101 -0.21133 -0.02776 -0.01847 410 TYR A CA  
3701 C C   . TYR A 531 ? 1.00857 1.28759 1.15747 -0.23981 -0.01618 -0.03623 410 TYR A C   
3702 O O   . TYR A 531 ? 1.07861 1.32725 1.20945 -0.24880 -0.01296 -0.05025 410 TYR A O   
3703 C CB  . TYR A 531 ? 0.92298 1.26113 1.05145 -0.21414 -0.04552 -0.02218 410 TYR A CB  
3704 C CG  . TYR A 531 ? 1.10413 1.46048 1.22449 -0.18530 -0.05556 -0.00430 410 TYR A CG  
3705 C CD1 . TYR A 531 ? 1.02726 1.34767 1.12640 -0.16408 -0.05291 0.00170  410 TYR A CD1 
3706 C CD2 . TYR A 531 ? 1.07858 1.48782 1.21403 -0.17935 -0.06667 0.00664  410 TYR A CD2 
3707 C CE1 . TYR A 531 ? 1.03472 1.36762 1.12645 -0.13866 -0.06009 0.01706  410 TYR A CE1 
3708 C CE2 . TYR A 531 ? 1.08449 1.50708 1.21344 -0.15186 -0.07366 0.02340  410 TYR A CE2 
3709 C CZ  . TYR A 531 ? 1.21289 1.59524 1.31930 -0.13203 -0.06983 0.02805  410 TYR A CZ  
3710 O OH  . TYR A 531 ? 1.21175 1.60358 1.31182 -0.10563 -0.07488 0.04380  410 TYR A OH  
3711 N N   . THR A 532 ? 0.87282 1.16439 1.04817 -0.25409 -0.00823 -0.03603 411 THR A N   
3712 C CA  . THR A 532 ? 0.91531 1.17793 1.09969 -0.27942 0.00670  -0.05123 411 THR A CA  
3713 C C   . THR A 532 ? 0.95263 1.15846 1.13129 -0.26821 0.02333  -0.04715 411 THR A C   
3714 O O   . THR A 532 ? 1.07799 1.24950 1.25731 -0.28541 0.03642  -0.06074 411 THR A O   
3715 C CB  . THR A 532 ? 0.94535 1.23500 1.16118 -0.29658 0.01247  -0.04979 411 THR A CB  
3716 O OG1 . THR A 532 ? 0.84957 1.13200 1.07899 -0.27713 0.02174  -0.02967 411 THR A OG1 
3717 C CG2 . THR A 532 ? 1.08746 1.44082 1.31293 -0.30488 -0.00518 -0.05063 411 THR A CG2 
3718 N N   . ASP A 533 ? 1.00659 1.20271 1.18036 -0.24007 0.02356  -0.02888 412 ASP A N   
3719 C CA  . ASP A 533 ? 1.04591 1.19473 1.21496 -0.22741 0.03725  -0.02249 412 ASP A CA  
3720 C C   . ASP A 533 ? 0.96238 1.08228 1.10604 -0.21794 0.03453  -0.02858 412 ASP A C   
3721 O O   . ASP A 533 ? 0.85549 0.93919 0.99524 -0.20622 0.04444  -0.02295 412 ASP A O   
3722 C CB  . ASP A 533 ? 0.95730 1.11154 1.13265 -0.20350 0.03908  -0.00079 412 ASP A CB  
3723 C CG  . ASP A 533 ? 1.08232 1.26864 1.28261 -0.21066 0.04207  0.00693  412 ASP A CG  
3724 O OD1 . ASP A 533 ? 1.12419 1.30064 1.34211 -0.23000 0.05468  0.00216  412 ASP A OD1 
3725 O OD2 . ASP A 533 ? 0.95866 1.17924 1.16187 -0.19691 0.03313  0.01788  412 ASP A OD2 
3726 N N   . LEU A 534 ? 1.04592 1.18263 1.17274 -0.22244 0.02155  -0.03884 413 LEU A N   
3727 C CA  . LEU A 534 ? 1.04060 1.15222 1.14289 -0.21452 0.01934  -0.04474 413 LEU A CA  
3728 C C   . LEU A 534 ? 1.27242 1.37235 1.36640 -0.23949 0.02283  -0.06728 413 LEU A C   
3729 O O   . LEU A 534 ? 1.28245 1.41342 1.37014 -0.25387 0.01160  -0.07743 413 LEU A O   
3730 C CB  . LEU A 534 ? 0.82248 0.95937 0.90823 -0.19695 0.00294  -0.03661 413 LEU A CB  
3731 C CG  . LEU A 534 ? 0.84010 0.98294 0.92870 -0.17063 0.00042  -0.01663 413 LEU A CG  
3732 C CD1 . LEU A 534 ? 0.70160 0.86587 0.77366 -0.15540 -0.01397 -0.01058 413 LEU A CD1 
3733 C CD2 . LEU A 534 ? 0.76568 0.86786 0.85100 -0.15743 0.01157  -0.01085 413 LEU A CD2 
3734 N N   . LYS A 535 ? 1.37325 1.42950 1.46708 -0.24430 0.03872  -0.07490 414 LYS A N   
3735 C CA  . LYS A 535 ? 1.47370 1.51083 1.55578 -0.26517 0.04479  -0.09737 414 LYS A CA  
3736 C C   . LYS A 535 ? 1.39886 1.43439 1.45280 -0.25626 0.03550  -0.10155 414 LYS A C   
3737 O O   . LYS A 535 ? 1.45583 1.47079 1.50209 -0.23527 0.03732  -0.09128 414 LYS A O   
3738 C CB  . LYS A 535 ? 1.49130 1.48002 1.58381 -0.26964 0.06683  -0.10213 414 LYS A CB  
3739 C CG  . LYS A 535 ? 1.60045 1.58440 1.72061 -0.27651 0.07888  -0.09524 414 LYS A CG  
3740 C CD  . LYS A 535 ? 1.66457 1.59958 1.79400 -0.28523 0.10203  -0.10328 414 LYS A CD  
3741 C CE  . LYS A 535 ? 1.75768 1.68733 1.91399 -0.29787 0.11556  -0.09947 414 LYS A CE  
3742 N NZ  . LYS A 535 ? 1.79037 1.66878 1.95717 -0.30268 0.14001  -0.10378 414 LYS A NZ  
3743 N N   . GLY A 536 ? 1.29123 1.34965 1.32961 -0.27274 0.02566  -0.11624 415 GLY A N   
3744 C CA  . GLY A 536 ? 1.23531 1.28925 1.24523 -0.26802 0.01946  -0.12217 415 GLY A CA  
3745 C C   . GLY A 536 ? 1.27906 1.37649 1.27531 -0.25932 -0.00137 -0.11314 415 GLY A C   
3746 O O   . GLY A 536 ? 1.32760 1.46502 1.33582 -0.26231 -0.01239 -0.10681 415 GLY A O   
3747 N N   . ARG A 537 ? 1.35313 1.44235 1.32489 -0.24774 -0.00581 -0.11160 416 ARG A N   
3748 C CA  . ARG A 537 ? 1.37057 1.49590 1.32501 -0.23980 -0.02380 -0.10367 416 ARG A CA  
3749 C C   . ARG A 537 ? 1.09962 1.24381 1.06623 -0.21507 -0.03210 -0.08004 416 ARG A C   
3750 O O   . ARG A 537 ? 0.96671 1.09066 0.94860 -0.20148 -0.02389 -0.06997 416 ARG A O   
3751 C CB  . ARG A 537 ? 1.37904 1.48451 1.30416 -0.23369 -0.02312 -0.10746 416 ARG A CB  
3752 C CG  . ARG A 537 ? 1.42251 1.48518 1.34077 -0.24607 -0.00573 -0.12572 416 ARG A CG  
3753 C CD  . ARG A 537 ? 1.38696 1.42497 1.28331 -0.23238 -0.00212 -0.12326 416 ARG A CD  
3754 N NE  . ARG A 537 ? 1.36824 1.43233 1.24817 -0.21735 -0.01757 -0.10862 416 ARG A NE  
3755 C CZ  . ARG A 537 ? 1.36030 1.40825 1.22247 -0.20283 -0.01649 -0.10197 416 ARG A CZ  
3756 N NH1 . ARG A 537 ? 1.37480 1.38386 1.23423 -0.20143 -0.00157 -0.10895 416 ARG A NH1 
3757 N NH2 . ARG A 537 ? 1.28791 1.35884 1.13649 -0.18945 -0.02950 -0.08764 416 ARG A NH2 
3758 N N   . THR A 538 ? 0.96095 1.14548 0.92010 -0.20910 -0.04826 -0.07100 417 THR A N   
3759 C CA  . THR A 538 ? 0.90294 1.10767 0.87296 -0.18570 -0.05563 -0.04940 417 THR A CA  
3760 C C   . THR A 538 ? 0.89929 1.12094 0.84837 -0.16991 -0.06767 -0.03807 417 THR A C   
3761 O O   . THR A 538 ? 0.93267 1.17462 0.88950 -0.15060 -0.07427 -0.02037 417 THR A O   
3762 C CB  . THR A 538 ? 0.94138 1.18776 0.93677 -0.19276 -0.06186 -0.04502 417 THR A CB  
3763 O OG1 . THR A 538 ? 0.91075 1.20141 0.89909 -0.20549 -0.07640 -0.04923 417 THR A OG1 
3764 C CG2 . THR A 538 ? 0.80946 1.04079 0.82571 -0.21159 -0.04930 -0.05655 417 THR A CG2 
3765 N N   . ASP A 539 ? 0.95417 1.16687 0.87682 -0.17701 -0.06933 -0.04717 418 ASP A N   
3766 C CA  . ASP A 539 ? 0.93490 1.16268 0.83602 -0.16286 -0.07981 -0.03538 418 ASP A CA  
3767 C C   . ASP A 539 ? 0.95042 1.14385 0.84310 -0.13918 -0.07325 -0.02338 418 ASP A C   
3768 O O   . ASP A 539 ? 0.87337 1.07731 0.75300 -0.12312 -0.08037 -0.00934 418 ASP A O   
3769 C CB  . ASP A 539 ? 1.06804 1.30151 0.94173 -0.18074 -0.08379 -0.04956 418 ASP A CB  
3770 C CG  . ASP A 539 ? 1.26469 1.45415 1.12883 -0.19498 -0.06858 -0.06918 418 ASP A CG  
3771 O OD1 . ASP A 539 ? 1.30540 1.48513 1.18547 -0.21192 -0.06031 -0.08331 418 ASP A OD1 
3772 O OD2 . ASP A 539 ? 1.40112 1.56526 1.24294 -0.18884 -0.06373 -0.06986 418 ASP A OD2 
3773 N N   . ASP A 540 ? 0.79843 0.95209 0.69862 -0.13689 -0.05976 -0.02810 419 ASP A N   
3774 C CA  . ASP A 540 ? 0.84756 0.96822 0.73817 -0.11867 -0.05328 -0.02028 419 ASP A CA  
3775 C C   . ASP A 540 ? 0.81192 0.90740 0.72245 -0.11212 -0.04284 -0.01883 419 ASP A C   
3776 O O   . ASP A 540 ? 0.78117 0.85458 0.69828 -0.12393 -0.03290 -0.03066 419 ASP A O   
3777 C CB  . ASP A 540 ? 0.90542 1.00117 0.77227 -0.12674 -0.04755 -0.03144 419 ASP A CB  
3778 C CG  . ASP A 540 ? 0.96066 1.02216 0.82046 -0.11085 -0.03961 -0.02509 419 ASP A CG  
3779 O OD1 . ASP A 540 ? 0.87738 0.93708 0.74554 -0.09270 -0.04075 -0.01126 419 ASP A OD1 
3780 O OD2 . ASP A 540 ? 1.04054 1.07726 0.88664 -0.11736 -0.03151 -0.03487 419 ASP A OD2 
3781 N N   . LEU A 541 ? 0.76587 0.86478 0.68517 -0.09286 -0.04455 -0.00394 420 LEU A N   
3782 C CA  . LEU A 541 ? 0.77874 0.85990 0.71534 -0.08561 -0.03634 -0.00068 420 LEU A CA  
3783 C C   . LEU A 541 ? 0.80478 0.84756 0.73784 -0.08765 -0.02530 -0.00828 420 LEU A C   
3784 O O   . LEU A 541 ? 0.76322 0.79285 0.71170 -0.08955 -0.01759 -0.00985 420 LEU A O   
3785 C CB  . LEU A 541 ? 0.62134 0.70783 0.56019 -0.06373 -0.03911 0.01485  420 LEU A CB  
3786 C CG  . LEU A 541 ? 0.66449 0.73483 0.61646 -0.05405 -0.03167 0.01944  420 LEU A CG  
3787 C CD1 . LEU A 541 ? 0.61516 0.69833 0.58834 -0.06387 -0.02880 0.01742  420 LEU A CD1 
3788 C CD2 . LEU A 541 ? 0.56186 0.63714 0.51199 -0.03363 -0.03384 0.03236  420 LEU A CD2 
3789 N N   . GLN A 542 ? 0.73923 0.76518 0.65312 -0.08698 -0.02391 -0.01196 421 GLN A N   
3790 C CA  . GLN A 542 ? 0.75478 0.74755 0.66743 -0.08853 -0.01317 -0.01873 421 GLN A CA  
3791 C C   . GLN A 542 ? 0.95094 0.93390 0.87209 -0.10621 -0.00492 -0.03253 421 GLN A C   
3792 O O   . GLN A 542 ? 0.80189 0.76004 0.73119 -0.10591 0.00537  -0.03577 421 GLN A O   
3793 C CB  . GLN A 542 ? 0.68320 0.66282 0.57368 -0.08508 -0.01279 -0.01959 421 GLN A CB  
3794 C CG  . GLN A 542 ? 0.79907 0.74803 0.68745 -0.08851 -0.00141 -0.02784 421 GLN A CG  
3795 C CD  . GLN A 542 ? 0.93767 0.86937 0.83653 -0.07545 0.00316  -0.02085 421 GLN A CD  
3796 O OE1 . GLN A 542 ? 0.69173 0.63101 0.59463 -0.06319 -0.00182 -0.01045 421 GLN A OE1 
3797 N NE2 . GLN A 542 ? 0.74797 0.65762 0.65125 -0.07826 0.01300  -0.02697 421 GLN A NE2 
3798 N N   . ALA A 543 ? 0.87464 0.87718 0.79563 -0.12155 -0.00872 -0.04044 422 ALA A N   
3799 C CA  . ALA A 543 ? 0.83122 0.82279 0.76002 -0.14022 0.00050  -0.05529 422 ALA A CA  
3800 C C   . ALA A 543 ? 0.79189 0.79746 0.74332 -0.14701 0.00102  -0.05405 422 ALA A C   
3801 O O   . ALA A 543 ? 0.80065 0.79794 0.76020 -0.16409 0.00918  -0.06645 422 ALA A O   
3802 C CB  . ALA A 543 ? 0.76244 0.76220 0.67146 -0.15728 -0.00199 -0.06958 422 ALA A CB  
3803 N N   . VAL A 544 ? 0.72008 0.74479 0.68209 -0.13437 -0.00583 -0.03976 423 VAL A N   
3804 C CA  . VAL A 544 ? 0.67490 0.71561 0.65872 -0.14001 -0.00499 -0.03685 423 VAL A CA  
3805 C C   . VAL A 544 ? 0.72633 0.74195 0.72620 -0.13317 0.00668  -0.03138 423 VAL A C   
3806 O O   . VAL A 544 ? 0.79990 0.80719 0.79885 -0.11540 0.00648  -0.02023 423 VAL A O   
3807 C CB  . VAL A 544 ? 0.75033 0.82621 0.73827 -0.12927 -0.01684 -0.02377 423 VAL A CB  
3808 C CG1 . VAL A 544 ? 0.72117 0.81136 0.73334 -0.13296 -0.01376 -0.01900 423 VAL A CG1 
3809 C CG2 . VAL A 544 ? 0.72721 0.83310 0.70239 -0.13722 -0.02879 -0.02780 423 VAL A CG2 
3810 N N   . SER A 545 ? 0.77978 0.78272 0.79362 -0.14762 0.01733  -0.03932 424 SER A N   
3811 C CA  . SER A 545 ? 0.77749 0.75747 0.80746 -0.14140 0.02919  -0.03243 424 SER A CA  
3812 C C   . SER A 545 ? 0.85624 0.85423 0.90053 -0.13144 0.02661  -0.01731 424 SER A C   
3813 O O   . SER A 545 ? 0.84148 0.85004 0.90167 -0.14221 0.03034  -0.01746 424 SER A O   
3814 C CB  . SER A 545 ? 0.77904 0.73881 0.82069 -0.15973 0.04310  -0.04441 424 SER A CB  
3815 O OG  . SER A 545 ? 0.90221 0.84029 0.93091 -0.16725 0.04879  -0.05853 424 SER A OG  
3816 N N   . VAL A 546 ? 0.81958 0.82043 0.85827 -0.11194 0.02148  -0.00499 425 VAL A N   
3817 C CA  . VAL A 546 ? 0.74467 0.76187 0.79393 -0.10143 0.02003  0.00874  425 VAL A CA  
3818 C C   . VAL A 546 ? 0.80982 0.80777 0.86502 -0.08982 0.02790  0.01876  425 VAL A C   
3819 O O   . VAL A 546 ? 0.83474 0.84243 0.90066 -0.08468 0.03049  0.02940  425 VAL A O   
3820 C CB  . VAL A 546 ? 0.86600 0.90602 0.90453 -0.08795 0.00835  0.01553  425 VAL A CB  
3821 C CG1 . VAL A 546 ? 0.66118 0.72890 0.71366 -0.08553 0.00679  0.02459  425 VAL A CG1 
3822 C CG2 . VAL A 546 ? 1.13803 1.18809 1.16213 -0.09350 -0.00034 0.00717  425 VAL A CG2 
3823 N N   . PHE A 547 ? 0.87690 0.85074 0.92583 -0.08550 0.03170  0.01646  426 PHE A N   
3824 C CA  . PHE A 547 ? 0.67046 0.63469 0.72256 -0.07151 0.03516  0.02809  426 PHE A CA  
3825 C C   . PHE A 547 ? 0.70176 0.64746 0.77016 -0.07633 0.04798  0.03109  426 PHE A C   
3826 O O   . PHE A 547 ? 0.78592 0.71287 0.85740 -0.08593 0.05521  0.02156  426 PHE A O   
3827 C CB  . PHE A 547 ? 0.57137 0.52431 0.60931 -0.06155 0.03111  0.02662  426 PHE A CB  
3828 C CG  . PHE A 547 ? 0.55393 0.51956 0.57534 -0.05690 0.02060  0.02375  426 PHE A CG  
3829 C CD1 . PHE A 547 ? 0.52013 0.50060 0.53665 -0.04493 0.01479  0.03206  426 PHE A CD1 
3830 C CD2 . PHE A 547 ? 0.60767 0.56906 0.61762 -0.06382 0.01776  0.01328  426 PHE A CD2 
3831 C CE1 . PHE A 547 ? 0.60421 0.59356 0.60675 -0.03918 0.00694  0.03069  426 PHE A CE1 
3832 C CE2 . PHE A 547 ? 0.64675 0.61883 0.64158 -0.05820 0.00894  0.01311  426 PHE A CE2 
3833 C CZ  . PHE A 547 ? 0.63543 0.62067 0.62754 -0.04542 0.00383  0.02222  426 PHE A CZ  
3834 N N   . PRO A 548 ? 0.79673 0.74624 0.87527 -0.06944 0.05220  0.04459  427 PRO A N   
3835 C CA  . PRO A 548 ? 0.76442 0.69738 0.86045 -0.07425 0.06574  0.04993  427 PRO A CA  
3836 C C   . PRO A 548 ? 0.67541 0.58995 0.77386 -0.06329 0.07077  0.05719  427 PRO A C   
3837 O O   . PRO A 548 ? 0.71025 0.63094 0.79919 -0.05004 0.06348  0.06329  427 PRO A O   
3838 C CB  . PRO A 548 ? 0.61458 0.56456 0.71854 -0.07085 0.06715  0.06322  427 PRO A CB  
3839 C CG  . PRO A 548 ? 0.68501 0.65212 0.77383 -0.05606 0.05585  0.06885  427 PRO A CG  
3840 C CD  . PRO A 548 ? 0.65404 0.62489 0.72878 -0.05865 0.04606  0.05533  427 PRO A CD  
3841 N N   . MET A 549 ? 0.74948 0.64159 0.86199 -0.06948 0.08404  0.05610  428 MET A N   
3842 C CA  . MET A 549 ? 0.78742 0.66359 0.90863 -0.05846 0.09141  0.06646  428 MET A CA  
3843 C C   . MET A 549 ? 0.88005 0.75582 1.01563 -0.05303 0.10003  0.08496  428 MET A C   
3844 O O   . MET A 549 ? 0.87358 0.74227 1.02091 -0.06396 0.11010  0.08478  428 MET A O   
3845 C CB  . MET A 549 ? 0.92778 0.77721 1.05676 -0.06611 0.10308  0.05535  428 MET A CB  
3846 C CG  . MET A 549 ? 0.91623 0.75263 1.05501 -0.05263 0.10948  0.06578  428 MET A CG  
3847 S SD  . MET A 549 ? 0.96568 0.76871 1.11588 -0.06049 0.12680  0.05280  428 MET A SD  
3848 C CE  . MET A 549 ? 1.16740 0.95177 1.33376 -0.07476 0.14377  0.05207  428 MET A CE  
3849 N N   . VAL A 550 ? 0.83147 0.71556 0.96564 -0.03697 0.09628  0.10093  429 VAL A N   
3850 C CA  . VAL A 550 ? 0.71795 0.60496 0.86224 -0.02930 0.10315  0.12140  429 VAL A CA  
3851 C C   . VAL A 550 ? 0.81384 0.69191 0.96706 -0.01578 0.10760  0.13479  429 VAL A C   
3852 O O   . VAL A 550 ? 0.89104 0.76794 1.04020 -0.01098 0.10207  0.12870  429 VAL A O   
3853 C CB  . VAL A 550 ? 0.80858 0.72277 0.93956 -0.02234 0.09269  0.13000  429 VAL A CB  
3854 C CG1 . VAL A 550 ? 0.69351 0.62039 0.81620 -0.03323 0.08646  0.11629  429 VAL A CG1 
3855 C CG2 . VAL A 550 ? 0.69469 0.62218 0.81119 -0.00907 0.08030  0.13299  429 VAL A CG2 
3856 N N   . ASN A 551 ? 0.87550 0.74865 1.04216 -0.00929 0.11810  0.15446  430 ASN A N   
3857 C CA  . ASN A 551 ? 1.06494 0.92943 1.24472 0.00406  0.12454  0.16987  430 ASN A CA  
3858 C C   . ASN A 551 ? 0.98356 0.87199 1.15741 0.02022  0.11658  0.19175  430 ASN A C   
3859 O O   . ASN A 551 ? 1.08529 0.97229 1.27098 0.03291  0.12083  0.20845  430 ASN A O   
3860 C CB  . ASN A 551 ? 1.23422 1.06921 1.43677 0.00014  0.14582  0.17676  430 ASN A CB  
3861 C CG  . ASN A 551 ? 1.37470 1.18363 1.58332 -0.01449 0.15492  0.15418  430 ASN A CG  
3862 O OD1 . ASN A 551 ? 1.47173 1.27406 1.67810 -0.03148 0.15823  0.13948  430 ASN A OD1 
3863 N ND2 . ASN A 551 ? 1.20068 0.99684 1.41682 -0.00839 0.15896  0.15095  430 ASN A ND2 
3864 N N   . SER A 552 ? 0.98911 0.90076 1.14483 0.02044  0.10541  0.19223  431 SER A N   
3865 C CA  . SER A 552 ? 0.96810 0.90403 1.11380 0.03424  0.09713  0.21025  431 SER A CA  
3866 C C   . SER A 552 ? 0.98448 0.94288 1.10571 0.03351  0.08066  0.19807  431 SER A C   
3867 O O   . SER A 552 ? 0.98772 0.94489 1.10094 0.02337  0.07777  0.18130  431 SER A O   
3868 C CB  . SER A 552 ? 0.98995 0.92857 1.14021 0.03757  0.10690  0.23132  431 SER A CB  
3869 O OG  . SER A 552 ? 0.90546 0.84913 1.04752 0.02723  0.10734  0.22325  431 SER A OG  
3870 N N   . VAL A 553 ? 0.85758 0.83723 0.96727 0.04445  0.07027  0.20709  432 VAL A N   
3871 C CA  . VAL A 553 ? 0.78668 0.78571 0.87228 0.04430  0.05641  0.19612  432 VAL A CA  
3872 C C   . VAL A 553 ? 0.75610 0.76554 0.82994 0.04257  0.05826  0.19966  432 VAL A C   
3873 O O   . VAL A 553 ? 0.82349 0.84066 0.88134 0.03893  0.05157  0.18596  432 VAL A O   
3874 C CB  . VAL A 553 ? 0.77751 0.79700 0.85446 0.05451  0.04556  0.20390  432 VAL A CB  
3875 C CG1 . VAL A 553 ? 0.82014 0.85859 0.87053 0.05424  0.03357  0.19401  432 VAL A CG1 
3876 C CG2 . VAL A 553 ? 0.66434 0.67613 0.75331 0.05481  0.04298  0.19675  432 VAL A CG2 
3877 N N   . GLU A 554 ? 0.77534 0.78392 0.85834 0.04530  0.06891  0.21836  433 GLU A N   
3878 C CA  . GLU A 554 ? 0.95537 0.97330 1.03057 0.04282  0.07333  0.22261  433 GLU A CA  
3879 C C   . GLU A 554 ? 0.80333 0.81125 0.88437 0.02985  0.07684  0.20542  433 GLU A C   
3880 O O   . GLU A 554 ? 0.75137 0.77164 0.81884 0.02762  0.07127  0.19500  433 GLU A O   
3881 C CB  . GLU A 554 ? 1.04314 1.05899 1.12970 0.04741  0.08619  0.24729  433 GLU A CB  
3882 C CG  . GLU A 554 ? 1.33779 1.37049 1.41594 0.06149  0.08213  0.26832  433 GLU A CG  
3883 C CD  . GLU A 554 ? 1.51226 1.53972 1.60160 0.06793  0.07805  0.27156  433 GLU A CD  
3884 O OE1 . GLU A 554 ? 1.51068 1.55280 1.58718 0.07112  0.06405  0.26266  433 GLU A OE1 
3885 O OE2 . GLU A 554 ? 1.53868 1.54698 1.65086 0.06956  0.08992  0.28278  433 GLU A OE2 
3886 N N   . GLU A 555 ? 0.77879 0.76518 0.88045 0.02125  0.08681  0.20278  434 GLU A N   
3887 C CA  . GLU A 555 ? 0.86074 0.83978 0.96826 0.00726  0.08868  0.18512  434 GLU A CA  
3888 C C   . GLU A 555 ? 0.75202 0.73612 0.84547 0.00567  0.07548  0.16534  434 GLU A C   
3889 O O   . GLU A 555 ? 0.71192 0.70379 0.80094 -0.00105 0.07220  0.15378  434 GLU A O   
3890 C CB  . GLU A 555 ? 0.81028 0.76323 0.93968 -0.00244 0.10098  0.18263  434 GLU A CB  
3891 C CG  . GLU A 555 ? 0.84052 0.78322 0.98625 -0.00222 0.11691  0.20199  434 GLU A CG  
3892 C CD  . GLU A 555 ? 0.99252 0.90637 1.15946 -0.01456 0.13102  0.19564  434 GLU A CD  
3893 O OE1 . GLU A 555 ? 1.04749 0.95051 1.21487 -0.02221 0.12766  0.17656  434 GLU A OE1 
3894 O OE2 . GLU A 555 ? 1.21136 1.11230 1.39367 -0.01706 0.14645  0.20943  434 GLU A OE2 
3895 N N   . LEU A 556 ? 0.68373 0.66420 0.77149 0.01188  0.06834  0.16214  435 LEU A N   
3896 C CA  . LEU A 556 ? 0.72584 0.70878 0.80010 0.01039  0.05716  0.14452  435 LEU A CA  
3897 C C   . LEU A 556 ? 0.61785 0.62011 0.67298 0.01476  0.04937  0.14175  435 LEU A C   
3898 O O   . LEU A 556 ? 0.71775 0.72260 0.76639 0.01033  0.04508  0.12875  435 LEU A O   
3899 C CB  . LEU A 556 ? 0.64660 0.62478 0.71933 0.01642  0.05187  0.14359  435 LEU A CB  
3900 C CG  . LEU A 556 ? 0.62769 0.60699 0.68617 0.01543  0.04127  0.12710  435 LEU A CG  
3901 C CD1 . LEU A 556 ? 0.52591 0.49535 0.58508 0.00482  0.04205  0.11150  435 LEU A CD1 
3902 C CD2 . LEU A 556 ? 0.55364 0.52817 0.61620 0.01955  0.03841  0.12708  435 LEU A CD2 
3903 N N   . GLY A 557 ? 0.66456 0.68083 0.71035 0.02378  0.04841  0.15447  436 GLY A N   
3904 C CA  . GLY A 557 ? 0.62554 0.65831 0.65228 0.02813  0.04333  0.15107  436 GLY A CA  
3905 C C   . GLY A 557 ? 0.77113 0.81121 0.80268 0.02381  0.04979  0.15179  436 GLY A C   
3906 O O   . GLY A 557 ? 0.60074 0.64906 0.62280 0.02429  0.04626  0.14226  436 GLY A O   
3907 N N   . LEU A 558 ? 0.64892 0.68624 0.69696 0.01961  0.06017  0.16355  437 LEU A N   
3908 C CA  . LEU A 558 ? 0.78647 0.83281 0.84285 0.01354  0.06701  0.16435  437 LEU A CA  
3909 C C   . LEU A 558 ? 0.87899 0.92330 0.94138 0.00430  0.06313  0.14753  437 LEU A C   
3910 O O   . LEU A 558 ? 0.67088 0.73028 0.72936 0.00458  0.06098  0.14220  437 LEU A O   
3911 C CB  . LEU A 558 ? 0.73544 0.77471 0.81085 0.00824  0.08002  0.17884  437 LEU A CB  
3912 C CG  . LEU A 558 ? 0.92675 0.97283 0.99660 0.01771  0.08582  0.19964  437 LEU A CG  
3913 C CD1 . LEU A 558 ? 0.92373 0.95521 1.01471 0.01262  0.09973  0.21417  437 LEU A CD1 
3914 C CD2 . LEU A 558 ? 0.76093 0.82911 0.81822 0.02216  0.08743  0.20385  437 LEU A CD2 
3915 N N   . VAL A 559 ? 0.78864 0.81555 0.85981 -0.00311 0.06220  0.13933  438 VAL A N   
3916 C CA  . VAL A 559 ? 0.80923 0.83555 0.88466 -0.01292 0.05837  0.12410  438 VAL A CA  
3917 C C   . VAL A 559 ? 0.80726 0.83941 0.86476 -0.00616 0.04720  0.11370  438 VAL A C   
3918 O O   . VAL A 559 ? 0.72558 0.76814 0.78261 -0.00934 0.04336  0.10572  438 VAL A O   
3919 C CB  . VAL A 559 ? 0.69934 0.70430 0.78724 -0.02360 0.06233  0.11746  438 VAL A CB  
3920 C CG1 . VAL A 559 ? 0.60057 0.59210 0.67851 -0.01880 0.05575  0.11037  438 VAL A CG1 
3921 C CG2 . VAL A 559 ? 0.52993 0.53910 0.62693 -0.03817 0.06243  0.10535  438 VAL A CG2 
3922 N N   . LEU A 560 ? 0.73636 0.76300 0.77962 0.00313  0.04211  0.11417  439 LEU A N   
3923 C CA  . LEU A 560 ? 0.74734 0.77675 0.77359 0.00898  0.03345  0.10435  439 LEU A CA  
3924 C C   . LEU A 560 ? 0.62251 0.66974 0.64060 0.01576  0.03374  0.10652  439 LEU A C   
3925 O O   . LEU A 560 ? 0.71801 0.77044 0.73117 0.01734  0.02993  0.09880  439 LEU A O   
3926 C CB  . LEU A 560 ? 0.54195 0.56294 0.55618 0.01542  0.02872  0.10374  439 LEU A CB  
3927 C CG  . LEU A 560 ? 0.71169 0.71613 0.72858 0.01057  0.02556  0.09485  439 LEU A CG  
3928 C CD1 . LEU A 560 ? 0.65916 0.65979 0.66892 0.01624  0.02173  0.09654  439 LEU A CD1 
3929 C CD2 . LEU A 560 ? 0.57868 0.58072 0.58769 0.00820  0.02044  0.08216  439 LEU A CD2 
3930 N N   . ARG A 561 ? 0.65941 0.71629 0.67576 0.02073  0.03905  0.11780  440 ARG A N   
3931 C CA  . ARG A 561 ? 0.78598 0.86021 0.79616 0.02698  0.04199  0.12026  440 ARG A CA  
3932 C C   . ARG A 561 ? 0.81930 0.90527 0.84546 0.02074  0.04440  0.11820  440 ARG A C   
3933 O O   . ARG A 561 ? 0.72051 0.81749 0.74271 0.02582  0.04261  0.11350  440 ARG A O   
3934 C CB  . ARG A 561 ? 0.67712 0.76017 0.68480 0.03112  0.04912  0.13424  440 ARG A CB  
3935 C CG  . ARG A 561 ? 0.82377 0.90396 0.81191 0.03874  0.04549  0.13666  440 ARG A CG  
3936 C CD  . ARG A 561 ? 0.74779 0.83585 0.73642 0.04110  0.05235  0.15359  440 ARG A CD  
3937 N NE  . ARG A 561 ? 0.90643 1.01100 0.89223 0.04436  0.06043  0.15960  440 ARG A NE  
3938 C CZ  . ARG A 561 ? 0.81898 0.93182 0.80951 0.04466  0.06947  0.17555  440 ARG A CZ  
3939 N NH1 . ARG A 561 ? 0.74396 0.87270 0.73164 0.04761  0.07758  0.18007  440 ARG A NH1 
3940 N NH2 . ARG A 561 ? 0.88457 0.98956 0.88319 0.04279  0.07152  0.18797  440 ARG A NH2 
3941 N N   . TRP A 562 ? 0.81360 0.89797 0.85893 0.00947  0.04894  0.12177  441 TRP A N   
3942 C CA  . TRP A 562 ? 0.71423 0.81303 0.77658 0.00057  0.05059  0.11912  441 TRP A CA  
3943 C C   . TRP A 562 ? 0.81391 0.91357 0.87358 -0.00132 0.04146  0.10674  441 TRP A C   
3944 O O   . TRP A 562 ? 0.68171 0.80139 0.74872 -0.00192 0.03994  0.10512  441 TRP A O   
3945 C CB  . TRP A 562 ? 0.73383 0.82582 0.81580 -0.01347 0.05775  0.12280  441 TRP A CB  
3946 C CG  . TRP A 562 ? 0.90184 1.00899 1.00198 -0.02631 0.05855  0.11776  441 TRP A CG  
3947 C CD1 . TRP A 562 ? 0.68760 0.81905 0.80098 -0.02889 0.06373  0.12328  441 TRP A CD1 
3948 C CD2 . TRP A 562 ? 0.72238 0.82418 0.82960 -0.03943 0.05389  0.10568  441 TRP A CD2 
3949 N NE1 . TRP A 562 ? 0.72894 0.87249 0.85862 -0.04342 0.06151  0.11537  441 TRP A NE1 
3950 C CE2 . TRP A 562 ? 0.78865 0.91404 0.91334 -0.05036 0.05528  0.10411  441 TRP A CE2 
3951 C CE3 . TRP A 562 ? 0.66196 0.74280 0.76212 -0.04347 0.04903  0.09576  441 TRP A CE3 
3952 C CZ2 . TRP A 562 ? 0.86009 0.98958 0.99356 -0.06591 0.05083  0.09232  441 TRP A CZ2 
3953 C CZ3 . TRP A 562 ? 0.78504 0.86764 0.89263 -0.05811 0.04593  0.08417  441 TRP A CZ3 
3954 C CH2 . TRP A 562 ? 0.72089 0.82800 0.84412 -0.06957 0.04630  0.08221  441 TRP A CH2 
3955 N N   . MET A 563 ? 0.61798 0.69816 0.66776 -0.00173 0.03559  0.09909  442 MET A N   
3956 C CA  . MET A 563 ? 0.63251 0.71236 0.67755 -0.00326 0.02756  0.08873  442 MET A CA  
3957 C C   . MET A 563 ? 0.62485 0.70854 0.65386 0.01065  0.02330  0.08704  442 MET A C   
3958 O O   . MET A 563 ? 0.64930 0.73688 0.67527 0.01176  0.01764  0.08158  442 MET A O   
3959 C CB  . MET A 563 ? 0.65615 0.71311 0.69710 -0.00968 0.02465  0.08108  442 MET A CB  
3960 C CG  . MET A 563 ? 0.74569 0.79356 0.80219 -0.02356 0.03055  0.08064  442 MET A CG  
3961 S SD  . MET A 563 ? 0.73042 0.75052 0.78242 -0.02897 0.02970  0.07176  442 MET A SD  
3962 C CE  . MET A 563 ? 0.65526 0.68124 0.70117 -0.03642 0.02171  0.05876  442 MET A CE  
3963 N N   . LEU A 564 ? 0.58203 0.66431 0.60002 0.02110  0.02653  0.09163  443 LEU A N   
3964 C CA  . LEU A 564 ? 0.69822 0.78202 0.70117 0.03388  0.02520  0.08900  443 LEU A CA  
3965 C C   . LEU A 564 ? 0.78268 0.88794 0.79032 0.04136  0.03158  0.09561  443 LEU A C   
3966 O O   . LEU A 564 ? 0.76422 0.88885 0.78722 0.03908  0.03202  0.09802  443 LEU A O   
3967 C CB  . LEU A 564 ? 0.63525 0.70126 0.61928 0.03939  0.02422  0.08592  443 LEU A CB  
3968 C CG  . LEU A 564 ? 0.74400 0.79067 0.72549 0.03262  0.01898  0.08015  443 LEU A CG  
3969 C CD1 . LEU A 564 ? 0.66038 0.69476 0.62514 0.03742  0.01735  0.07705  443 LEU A CD1 
3970 C CD2 . LEU A 564 ? 0.65924 0.70036 0.64078 0.02997  0.01395  0.07280  443 LEU A CD2 
3971 N N   . SER A 565 ? 0.73197 0.83607 0.72661 0.04986  0.03671  0.09831  444 SER A N   
3972 C CA  . SER A 565 ? 0.74853 0.87005 0.74311 0.05957  0.04409  0.10252  444 SER A CA  
3973 C C   . SER A 565 ? 0.74106 0.88211 0.75111 0.05527  0.05179  0.11304  444 SER A C   
3974 O O   . SER A 565 ? 1.00953 1.16833 1.02309 0.06267  0.05900  0.11714  444 SER A O   
3975 C CB  . SER A 565 ? 0.85739 0.96835 0.82784 0.07000  0.04745  0.09861  444 SER A CB  
3976 O OG  . SER A 565 ? 1.06892 1.16067 1.02562 0.07341  0.04205  0.08857  444 SER A OG  
3977 N N   . GLU A 566 ? 0.69273 0.83033 0.71294 0.04396  0.05210  0.11799  445 GLU A N   
3978 C CA  . GLU A 566 ? 0.57606 0.72957 0.61221 0.03851  0.06088  0.12877  445 GLU A CA  
3979 C C   . GLU A 566 ? 0.68970 0.84912 0.75031 0.02367  0.05964  0.12874  445 GLU A C   
3980 O O   . GLU A 566 ? 0.74115 0.89001 0.80963 0.01365  0.06228  0.13258  445 GLU A O   
3981 C CB  . GLU A 566 ? 0.61875 0.76270 0.64522 0.03863  0.06556  0.13716  445 GLU A CB  
3982 C CG  . GLU A 566 ? 0.59675 0.73738 0.59684 0.05090  0.06639  0.13609  445 GLU A CG  
3983 C CD  . GLU A 566 ? 0.88821 1.02216 0.87781 0.05066  0.06829  0.14514  445 GLU A CD  
3984 O OE1 . GLU A 566 ? 0.83279 0.97590 0.83137 0.04791  0.07683  0.15804  445 GLU A OE1 
3985 O OE2 . GLU A 566 ? 0.88134 1.00215 0.85458 0.05316  0.06133  0.14023  445 GLU A OE2 
3986 N N   . PRO A 567 ? 0.73978 0.91674 0.81313 0.02173  0.05616  0.12457  446 PRO A N   
3987 C CA  . PRO A 567 ? 0.78987 0.97750 0.88663 0.00532  0.05540  0.12355  446 PRO A CA  
3988 C C   . PRO A 567 ? 0.67955 0.88209 0.79502 -0.00264 0.06645  0.13334  446 PRO A C   
3989 O O   . PRO A 567 ? 0.58457 0.78888 0.71832 -0.01908 0.06800  0.13208  446 PRO A O   
3990 C CB  . PRO A 567 ? 0.72848 0.93796 0.83247 0.00793  0.04829  0.11866  446 PRO A CB  
3991 C CG  . PRO A 567 ? 0.66287 0.87682 0.75306 0.02709  0.05033  0.12096  446 PRO A CG  
3992 C CD  . PRO A 567 ? 0.55894 0.74499 0.62543 0.03378  0.05188  0.11992  446 PRO A CD  
3993 N N   . GLU A 568 ? 0.58924 0.80178 0.70015 0.00764  0.07519  0.14245  447 GLU A N   
3994 C CA  . GLU A 568 ? 0.60005 0.82546 0.72670 0.00112  0.08752  0.15359  447 GLU A CA  
3995 C C   . GLU A 568 ? 0.86481 1.06689 0.98779 -0.00479 0.09367  0.16096  447 GLU A C   
3996 O O   . GLU A 568 ? 0.81417 1.02268 0.95170 -0.01233 0.10491  0.17112  447 GLU A O   
3997 C CB  . GLU A 568 ? 0.56991 0.81332 0.68967 0.01546  0.09587  0.16096  447 GLU A CB  
3998 C CG  . GLU A 568 ? 0.57195 0.79684 0.66135 0.02923  0.09676  0.16251  447 GLU A CG  
3999 C CD  . GLU A 568 ? 0.75977 0.97458 0.82988 0.04060  0.08700  0.15113  447 GLU A CD  
4000 O OE1 . GLU A 568 ? 0.69583 0.91262 0.77431 0.03769  0.07829  0.14305  447 GLU A OE1 
4001 O OE2 . GLU A 568 ? 0.82691 1.03161 0.87262 0.05178  0.08838  0.15023  447 GLU A OE2 
4002 N N   . LEU A 569 ? 0.82524 1.00152 0.93055 -0.00099 0.08745  0.15739  448 LEU A N   
4003 C CA  . LEU A 569 ? 0.72262 0.87805 0.82521 -0.00384 0.09294  0.16630  448 LEU A CA  
4004 C C   . LEU A 569 ? 0.78284 0.92917 0.90879 -0.02171 0.09726  0.16529  448 LEU A C   
4005 O O   . LEU A 569 ? 0.85535 0.98806 0.98396 -0.02917 0.09029  0.15410  448 LEU A O   
4006 C CB  . LEU A 569 ? 0.70193 0.83640 0.78285 0.00459  0.08427  0.16193  448 LEU A CB  
4007 C CG  . LEU A 569 ? 0.62973 0.74775 0.70547 0.00654  0.08913  0.17403  448 LEU A CG  
4008 C CD1 . LEU A 569 ? 0.56889 0.69984 0.63459 0.01527  0.09767  0.18872  448 LEU A CD1 
4009 C CD2 . LEU A 569 ? 0.77896 0.88008 0.83791 0.01288  0.07904  0.16785  448 LEU A CD2 
4010 N N   . GLU A 570 ? 0.86506 1.01796 1.00742 -0.02931 0.11008  0.17651  449 GLU A N   
4011 C CA  . GLU A 570 ? 0.87963 1.02428 1.04606 -0.04851 0.11668  0.17442  449 GLU A CA  
4012 C C   . GLU A 570 ? 0.93084 1.04189 1.09494 -0.05204 0.11704  0.17304  449 GLU A C   
4013 O O   . GLU A 570 ? 1.00555 1.10515 1.18002 -0.06554 0.11477  0.16067  449 GLU A O   
4014 C CB  . GLU A 570 ? 0.97800 1.13239 1.16087 -0.05478 0.13262  0.18898  449 GLU A CB  
4015 C CG  . GLU A 570 ? 1.09856 1.25135 1.30953 -0.07742 0.14039  0.18432  449 GLU A CG  
4016 C CD  . GLU A 570 ? 1.17180 1.33973 1.40067 -0.08424 0.15616  0.19786  449 GLU A CD  
4017 O OE1 . GLU A 570 ? 1.21107 1.35785 1.44804 -0.09025 0.17008  0.20947  449 GLU A OE1 
4018 O OE2 . GLU A 570 ? 1.19544 1.39627 1.43103 -0.08286 0.15567  0.19788  449 GLU A OE2 
4019 N N   . GLU A 571 ? 0.75286 0.84930 0.90360 -0.03992 0.12030  0.18585  450 GLU A N   
4020 C CA  . GLU A 571 ? 0.92673 0.99313 1.07865 -0.04134 0.12239  0.18739  450 GLU A CA  
4021 C C   . GLU A 571 ? 0.74192 0.79809 0.88499 -0.04113 0.10931  0.17026  450 GLU A C   
4022 O O   . GLU A 571 ? 0.88579 0.91940 1.03730 -0.04929 0.11178  0.16432  450 GLU A O   
4023 C CB  . GLU A 571 ? 1.01613 1.07563 1.15482 -0.02630 0.12622  0.20606  450 GLU A CB  
4024 C CG  . GLU A 571 ? 1.18346 1.21435 1.32667 -0.02506 0.13008  0.21193  450 GLU A CG  
4025 C CD  . GLU A 571 ? 1.26570 1.27525 1.43416 -0.04129 0.14378  0.21122  450 GLU A CD  
4026 O OE1 . GLU A 571 ? 1.24064 1.22496 1.41484 -0.04255 0.14613  0.20881  450 GLU A OE1 
4027 O OE2 . GLU A 571 ? 1.24500 1.26233 1.42826 -0.05301 0.15344  0.21311  450 GLU A OE2 
4028 N N   . GLY A 572 ? 0.65635 0.72714 0.78236 -0.03176 0.09693  0.16233  451 GLY A N   
4029 C CA  . GLY A 572 ? 0.66359 0.72616 0.78171 -0.03265 0.08534  0.14629  451 GLY A CA  
4030 C C   . GLY A 572 ? 0.85975 0.92074 0.99322 -0.05010 0.08517  0.13273  451 GLY A C   
4031 O O   . GLY A 572 ? 0.88450 0.92575 1.01901 -0.05660 0.08369  0.12333  451 GLY A O   
4032 N N   . LYS A 573 ? 0.68895 0.77296 0.83432 -0.05824 0.08663  0.13103  452 LYS A N   
4033 C CA  . LYS A 573 ? 0.73255 0.82072 0.89264 -0.07688 0.08559  0.11778  452 LYS A CA  
4034 C C   . LYS A 573 ? 0.67148 0.73455 0.84686 -0.09190 0.09785  0.11724  452 LYS A C   
4035 O O   . LYS A 573 ? 0.68363 0.73344 0.86196 -0.10463 0.09639  0.10309  452 LYS A O   
4036 C CB  . LYS A 573 ? 0.87626 0.99864 1.04965 -0.08265 0.08552  0.11851  452 LYS A CB  
4037 C CG  . LYS A 573 ? 0.83739 0.97155 1.02561 -0.10302 0.08211  0.10424  452 LYS A CG  
4038 C CD  . LYS A 573 ? 0.91392 1.08670 1.11929 -0.10875 0.08227  0.10679  452 LYS A CD  
4039 C CE  . LYS A 573 ? 0.89239 1.08287 1.11079 -0.12920 0.07577  0.09175  452 LYS A CE  
4040 N NZ  . LYS A 573 ? 0.99984 1.22744 1.24228 -0.13997 0.07902  0.09485  452 LYS A NZ  
4041 N N   . ASN A 574 ? 0.64049 0.69589 0.82525 -0.09075 0.11125  0.13261  453 ASN A N   
4042 C CA  . ASN A 574 ? 0.79560 0.82193 0.99509 -0.10260 0.12544  0.13435  453 ASN A CA  
4043 C C   . ASN A 574 ? 0.82378 0.82050 1.01430 -0.09809 0.12354  0.12851  453 ASN A C   
4044 O O   . ASN A 574 ? 0.93662 0.91231 1.13626 -0.11235 0.12949  0.11691  453 ASN A O   
4045 C CB  . ASN A 574 ? 0.71578 0.73702 0.92280 -0.09679 0.13986  0.15606  453 ASN A CB  
4046 C CG  . ASN A 574 ? 0.97389 1.02063 1.19548 -0.10595 0.14629  0.16102  453 ASN A CG  
4047 O OD1 . ASN A 574 ? 0.85278 0.91568 1.08658 -0.12233 0.14356  0.14745  453 ASN A OD1 
4048 N ND2 . ASN A 574 ? 0.94142 0.99415 1.16202 -0.09577 0.15496  0.18092  453 ASN A ND2 
4049 N N   . ILE A 575 ? 0.85003 0.84545 1.02298 -0.07892 0.11597  0.13572  454 ILE A N   
4050 C CA  . ILE A 575 ? 0.73582 0.70724 0.90164 -0.07320 0.11380  0.13141  454 ILE A CA  
4051 C C   . ILE A 575 ? 0.70793 0.67691 0.86941 -0.08390 0.10550  0.10955  454 ILE A C   
4052 O O   . ILE A 575 ? 0.82678 0.77151 0.99352 -0.09205 0.11135  0.10051  454 ILE A O   
4053 C CB  . ILE A 575 ? 0.69289 0.67068 0.84044 -0.05246 0.10500  0.14154  454 ILE A CB  
4054 C CG1 . ILE A 575 ? 0.75969 0.73722 0.91030 -0.04236 0.11425  0.16420  454 ILE A CG1 
4055 C CG2 . ILE A 575 ? 0.69341 0.65285 0.83416 -0.04750 0.10028  0.13447  454 ILE A CG2 
4056 C CD1 . ILE A 575 ? 0.80433 0.79303 0.93564 -0.02395 0.10513  0.17370  454 ILE A CD1 
4057 N N   . TRP A 576 ? 0.61215 0.60619 0.76339 -0.08325 0.09257  0.10143  455 TRP A N   
4058 C CA  . TRP A 576 ? 0.56678 0.56209 0.71116 -0.09207 0.08351  0.08272  455 TRP A CA  
4059 C C   . TRP A 576 ? 0.69270 0.68115 0.85195 -0.11478 0.09104  0.07020  455 TRP A C   
4060 O O   . TRP A 576 ? 0.74443 0.71891 0.89938 -0.12401 0.08990  0.05521  455 TRP A O   
4061 C CB  . TRP A 576 ? 0.59610 0.62155 0.72939 -0.08603 0.06981  0.07989  455 TRP A CB  
4062 C CG  . TRP A 576 ? 0.64020 0.66981 0.76349 -0.09208 0.05924  0.06388  455 TRP A CG  
4063 C CD1 . TRP A 576 ? 0.70728 0.72946 0.81272 -0.08232 0.05070  0.05917  455 TRP A CD1 
4064 C CD2 . TRP A 576 ? 0.81443 0.85895 0.94421 -0.10954 0.05595  0.05134  455 TRP A CD2 
4065 N NE1 . TRP A 576 ? 0.79389 0.82365 0.89327 -0.09159 0.04304  0.04573  455 TRP A NE1 
4066 C CE2 . TRP A 576 ? 0.71695 0.76198 0.83040 -0.10828 0.04527  0.04058  455 TRP A CE2 
4067 C CE3 . TRP A 576 ? 0.80692 0.86586 0.95478 -0.12706 0.06096  0.04814  455 TRP A CE3 
4068 C CZ2 . TRP A 576 ? 0.75309 0.81397 0.86592 -0.12301 0.03863  0.02761  455 TRP A CZ2 
4069 C CZ3 . TRP A 576 ? 0.79903 0.87491 0.94768 -0.14298 0.05380  0.03372  455 TRP A CZ3 
4070 C CH2 . TRP A 576 ? 0.73730 0.81475 0.86764 -0.14040 0.04232  0.02402  455 TRP A CH2 
4071 N N   . LEU A 577 ? 0.70453 0.70320 0.88077 -0.12517 0.09935  0.07522  456 LEU A N   
4072 C CA  . LEU A 577 ? 0.84164 0.83681 1.03273 -0.14958 0.10641  0.06165  456 LEU A CA  
4073 C C   . LEU A 577 ? 0.89455 0.84944 1.09399 -0.15758 0.12236  0.05842  456 LEU A C   
4074 O O   . LEU A 577 ? 0.97403 0.91729 1.17762 -0.17692 0.12655  0.04070  456 LEU A O   
4075 C CB  . LEU A 577 ? 0.69801 0.71633 0.90714 -0.15899 0.11193  0.06862  456 LEU A CB  
4076 C CG  . LEU A 577 ? 0.77007 0.83204 0.97868 -0.15880 0.09861  0.06697  456 LEU A CG  
4077 C CD1 . LEU A 577 ? 0.72921 0.81096 0.95772 -0.16455 0.10761  0.07820  456 LEU A CD1 
4078 C CD2 . LEU A 577 ? 0.65312 0.72958 0.86053 -0.17632 0.08881  0.04677  456 LEU A CD2 
4079 N N   . ARG A 578 ? 0.90050 0.83446 1.10254 -0.14304 0.13196  0.07532  457 ARG A N   
4080 C CA  . ARG A 578 ? 0.97798 0.87273 1.18976 -0.14642 0.14854  0.07575  457 ARG A CA  
4081 C C   . ARG A 578 ? 1.01623 0.89228 1.21544 -0.13394 0.14479  0.07221  457 ARG A C   
4082 O O   . ARG A 578 ? 1.16144 1.00631 1.36922 -0.13069 0.15859  0.07685  457 ARG A O   
4083 C CB  . ARG A 578 ? 0.88269 0.76635 1.10783 -0.13770 0.16298  0.09914  457 ARG A CB  
4084 C CG  . ARG A 578 ? 0.88401 0.77920 1.09706 -0.11229 0.15524  0.11921  457 ARG A CG  
4085 C CD  . ARG A 578 ? 0.92011 0.79740 1.14454 -0.10239 0.17083  0.14274  457 ARG A CD  
4086 N NE  . ARG A 578 ? 1.07616 0.97873 1.29453 -0.08984 0.16673  0.16160  457 ARG A NE  
4087 C CZ  . ARG A 578 ? 1.17624 1.08639 1.38156 -0.06895 0.16024  0.17732  457 ARG A CZ  
4088 N NH1 . ARG A 578 ? 1.21605 1.14921 1.41412 -0.05974 0.15779  0.19238  457 ARG A NH1 
4089 N NH2 . ARG A 578 ? 1.29880 1.19511 1.49828 -0.05795 0.15649  0.17744  457 ARG A NH2 
4090 N N   . SER A 579 ? 0.95028 0.84424 1.13094 -0.12663 0.12769  0.06487  458 SER A N   
4091 C CA  . SER A 579 ? 0.82867 0.70840 0.99773 -0.11482 0.12363  0.06213  458 SER A CA  
4092 C C   . SER A 579 ? 0.89204 0.76826 1.05094 -0.12795 0.11849  0.03908  458 SER A C   
4093 O O   . SER A 579 ? 0.80338 0.70105 0.95670 -0.13982 0.10949  0.02779  458 SER A O   
4094 C CB  . SER A 579 ? 0.82282 0.72299 0.97690 -0.09460 0.10930  0.07340  458 SER A CB  
4095 O OG  . SER A 579 ? 0.85228 0.75111 1.01250 -0.08060 0.11486  0.09465  458 SER A OG  
4096 N N   . GLU A 580 ? 1.01574 0.86645 1.17255 -0.12542 0.12465  0.03295  459 GLU A N   
4097 C CA  . GLU A 580 ? 1.05563 0.90293 1.19876 -0.13525 0.11969  0.01228  459 GLU A CA  
4098 C C   . GLU A 580 ? 0.90599 0.77998 1.02929 -0.12602 0.10022  0.01162  459 GLU A C   
4099 O O   . GLU A 580 ? 0.97537 0.85862 1.09413 -0.10814 0.09316  0.02547  459 GLU A O   
4100 C CB  . GLU A 580 ? 1.19135 1.00660 1.33691 -0.13138 0.13152  0.00798  459 GLU A CB  
4101 C CG  . GLU A 580 ? 1.29518 1.10264 1.42694 -0.14481 0.13072  -0.01509 459 GLU A CG  
4102 C CD  . GLU A 580 ? 1.32766 1.10384 1.46279 -0.14019 0.14418  -0.01956 459 GLU A CD  
4103 O OE1 . GLU A 580 ? 1.34351 1.10371 1.49469 -0.12702 0.15480  -0.00426 459 GLU A OE1 
4104 O OE2 . GLU A 580 ? 1.28014 1.04908 1.40202 -0.14923 0.14451  -0.03763 459 GLU A OE2 
4105 N N   . HIS A 581 ? 0.89374 0.78023 1.00482 -0.13874 0.09197  -0.00449 460 HIS A N   
4106 C CA  . HIS A 581 ? 0.84602 0.75851 0.93941 -0.13161 0.07455  -0.00481 460 HIS A CA  
4107 C C   . HIS A 581 ? 0.79111 0.69254 0.86745 -0.13123 0.07149  -0.01639 460 HIS A C   
4108 O O   . HIS A 581 ? 0.98113 0.86843 1.05482 -0.14612 0.07830  -0.03206 460 HIS A O   
4109 C CB  . HIS A 581 ? 0.80649 0.74798 0.89958 -0.14483 0.06623  -0.01097 460 HIS A CB  
4110 C CG  . HIS A 581 ? 0.87223 0.82966 0.98162 -0.14422 0.06831  0.00125  460 HIS A CG  
4111 N ND1 . HIS A 581 ? 1.08303 1.06497 1.20065 -0.15910 0.06529  -0.00359 460 HIS A ND1 
4112 C CD2 . HIS A 581 ? 0.95291 0.90730 1.07161 -0.13079 0.07328  0.01848  460 HIS A CD2 
4113 C CE1 . HIS A 581 ? 0.94440 0.93608 1.07678 -0.15484 0.06956  0.01010  460 HIS A CE1 
4114 N NE2 . HIS A 581 ? 1.00361 0.97837 1.13548 -0.13753 0.07448  0.02377  460 HIS A NE2 
4115 N N   . PHE A 582 ? 0.72048 0.62775 0.78471 -0.11517 0.06229  -0.00940 461 PHE A N   
4116 C CA  . PHE A 582 ? 0.81107 0.70901 0.85909 -0.11327 0.05955  -0.01806 461 PHE A CA  
4117 C C   . PHE A 582 ? 0.67167 0.59258 0.70149 -0.10928 0.04440  -0.01845 461 PHE A C   
4118 O O   . PHE A 582 ? 0.72776 0.66658 0.75742 -0.09851 0.03629  -0.00735 461 PHE A O   
4119 C CB  . PHE A 582 ? 0.70898 0.59062 0.75975 -0.09799 0.06367  -0.00956 461 PHE A CB  
4120 C CG  . PHE A 582 ? 0.77191 0.62853 0.83992 -0.09943 0.07963  -0.00872 461 PHE A CG  
4121 C CD1 . PHE A 582 ? 0.67902 0.53235 0.76520 -0.09965 0.08758  0.00084  461 PHE A CD1 
4122 C CD2 . PHE A 582 ? 0.77241 0.60837 0.83925 -0.09930 0.08789  -0.01614 461 PHE A CD2 
4123 C CE1 . PHE A 582 ? 0.79714 0.62569 0.90013 -0.09915 0.10354  0.00366  461 PHE A CE1 
4124 C CE2 . PHE A 582 ? 0.71449 0.52699 0.79915 -0.09851 0.10394  -0.01418 461 PHE A CE2 
4125 C CZ  . PHE A 582 ? 0.76831 0.57638 0.87118 -0.09798 0.11179  -0.00379 461 PHE A CZ  
4126 N N   . SER A 583 ? 0.64614 0.56576 0.66017 -0.11754 0.04173  -0.03081 462 SER A N   
4127 C CA  . SER A 583 ? 0.71948 0.65423 0.71456 -0.11070 0.02945  -0.02931 462 SER A CA  
4128 C C   . SER A 583 ? 0.83791 0.75696 0.82584 -0.09699 0.03047  -0.02469 462 SER A C   
4129 O O   . SER A 583 ? 0.79102 0.68992 0.78809 -0.09445 0.04005  -0.02449 462 SER A O   
4130 C CB  . SER A 583 ? 0.69617 0.63768 0.67547 -0.12524 0.02614  -0.04302 462 SER A CB  
4131 O OG  . SER A 583 ? 0.77579 0.69223 0.74945 -0.13251 0.03657  -0.05476 462 SER A OG  
4132 N N   . ALA A 584 ? 0.66859 0.59758 0.64120 -0.08816 0.02100  -0.02054 463 ALA A N   
4133 C CA  . ALA A 584 ? 0.71653 0.63098 0.68144 -0.07798 0.02216  -0.01809 463 ALA A CA  
4134 C C   . ALA A 584 ? 0.89289 0.78786 0.85234 -0.08629 0.03087  -0.02928 463 ALA A C   
4135 O O   . ALA A 584 ? 0.90452 0.78343 0.86965 -0.08097 0.03757  -0.02829 463 ALA A O   
4136 C CB  . ALA A 584 ? 0.58796 0.51363 0.53656 -0.06887 0.01232  -0.01266 463 ALA A CB  
4137 N N   . ASP A 585 ? 0.72768 0.62563 0.67646 -0.09977 0.03122  -0.04033 464 ASP A N   
4138 C CA  . ASP A 585 ? 0.89563 0.77459 0.83745 -0.10864 0.04123  -0.05261 464 ASP A CA  
4139 C C   . ASP A 585 ? 0.81848 0.67766 0.78062 -0.11132 0.05510  -0.05583 464 ASP A C   
4140 O O   . ASP A 585 ? 0.94067 0.78166 0.90609 -0.10808 0.06454  -0.05808 464 ASP A O   
4141 C CB  . ASP A 585 ? 0.77622 0.66436 0.70131 -0.12442 0.03889  -0.06506 464 ASP A CB  
4142 C CG  . ASP A 585 ? 0.82791 0.73275 0.73044 -0.12045 0.02712  -0.06091 464 ASP A CG  
4143 O OD1 . ASP A 585 ? 0.87495 0.77378 0.77141 -0.10790 0.02555  -0.05278 464 ASP A OD1 
4144 O OD2 . ASP A 585 ? 1.03670 0.96108 0.92782 -0.13029 0.01979  -0.06557 464 ASP A OD2 
4145 N N   . GLU A 586 ? 0.80313 0.66594 0.78069 -0.11645 0.05733  -0.05477 465 GLU A N   
4146 C CA  . GLU A 586 ? 0.73043 0.57266 0.72825 -0.11824 0.07196  -0.05599 465 GLU A CA  
4147 C C   . GLU A 586 ? 0.81627 0.65353 0.82879 -0.10121 0.07353  -0.04126 465 GLU A C   
4148 O O   . GLU A 586 ? 0.88135 0.70006 0.90742 -0.09817 0.08581  -0.04098 465 GLU A O   
4149 C CB  . GLU A 586 ? 0.69391 0.54087 0.70424 -0.12889 0.07460  -0.05767 465 GLU A CB  
4150 C CG  . GLU A 586 ? 0.77566 0.63154 0.77281 -0.14820 0.07220  -0.07347 465 GLU A CG  
4151 C CD  . GLU A 586 ? 0.93961 0.80732 0.94986 -0.15915 0.07184  -0.07385 465 GLU A CD  
4152 O OE1 . GLU A 586 ? 0.88490 0.76550 0.90734 -0.14935 0.06668  -0.05913 465 GLU A OE1 
4153 O OE2 . GLU A 586 ? 0.95580 0.82023 0.96381 -0.17858 0.07734  -0.08962 465 GLU A OE2 
4154 N N   . ILE A 587 ? 0.72355 0.57812 0.73342 -0.08990 0.06152  -0.02921 466 ILE A N   
4155 C CA  . ILE A 587 ? 0.77142 0.62483 0.79135 -0.07508 0.06108  -0.01674 466 ILE A CA  
4156 C C   . ILE A 587 ? 0.94290 0.78489 0.95854 -0.07146 0.06494  -0.02052 466 ILE A C   
4157 O O   . ILE A 587 ? 0.84663 0.67831 0.87770 -0.06595 0.07342  -0.01668 466 ILE A O   
4158 C CB  . ILE A 587 ? 0.71892 0.59202 0.73245 -0.06544 0.04807  -0.00640 466 ILE A CB  
4159 C CG1 . ILE A 587 ? 0.76198 0.64747 0.78405 -0.06734 0.04627  -0.00045 466 ILE A CG1 
4160 C CG2 . ILE A 587 ? 0.60981 0.48301 0.62894 -0.05232 0.04645  0.00340  466 ILE A CG2 
4161 C CD1 . ILE A 587 ? 0.67599 0.58052 0.69137 -0.05767 0.03534  0.00868  466 ILE A CD1 
4162 N N   . SER A 588 ? 0.72861 0.57334 0.72433 -0.07419 0.05940  -0.02705 467 SER A N   
4163 C CA  . SER A 588 ? 0.70809 0.54300 0.70036 -0.07090 0.06360  -0.02969 467 SER A CA  
4164 C C   . SER A 588 ? 0.90404 0.72072 0.89997 -0.07934 0.07806  -0.04101 467 SER A C   
4165 O O   . SER A 588 ? 0.89607 0.70392 0.89548 -0.07604 0.08484  -0.04242 467 SER A O   
4166 C CB  . SER A 588 ? 0.57261 0.41399 0.54223 -0.07029 0.05474  -0.03127 467 SER A CB  
4167 O OG  . SER A 588 ? 1.09129 0.93399 1.04388 -0.08105 0.05394  -0.04061 467 SER A OG  
4168 N N   . ALA A 589 ? 0.89930 0.71027 0.89526 -0.09073 0.08386  -0.04980 468 ALA A N   
4169 C CA  . ALA A 589 ? 0.88737 0.67766 0.88894 -0.09884 0.10034  -0.06150 468 ALA A CA  
4170 C C   . ALA A 589 ? 0.97876 0.75650 1.00849 -0.09192 0.11241  -0.05439 468 ALA A C   
4171 O O   . ALA A 589 ? 0.89998 0.66003 0.93906 -0.09188 0.12731  -0.05982 468 ALA A O   
4172 C CB  . ALA A 589 ? 0.74118 0.52968 0.73040 -0.11593 0.10235  -0.07578 468 ALA A CB  
4173 N N   . GLY A 590 ? 0.88330 0.67002 0.92697 -0.08518 0.10732  -0.04138 469 GLY A N   
4174 C CA  . GLY A 590 ? 0.81955 0.59446 0.88934 -0.07844 0.11938  -0.03270 469 GLY A CA  
4175 C C   . GLY A 590 ? 0.91234 0.69947 0.99734 -0.06170 0.11371  -0.01392 469 GLY A C   
4176 O O   . GLY A 590 ? 0.91712 0.69696 1.02432 -0.05426 0.12318  -0.00376 469 GLY A O   
4177 N N   . ALA A 591 ? 0.88437 0.69002 0.95732 -0.05590 0.09881  -0.00905 470 ALA A N   
4178 C CA  . ALA A 591 ? 0.88267 0.70363 0.96585 -0.04228 0.09112  0.00695  470 ALA A CA  
4179 C C   . ALA A 591 ? 0.92292 0.73844 1.02956 -0.03289 0.10135  0.01490  470 ALA A C   
4180 O O   . ALA A 591 ? 0.86867 0.67243 0.97938 -0.03472 0.11118  0.00702  470 ALA A O   
4181 C CB  . ALA A 591 ? 0.74242 0.57780 0.80822 -0.03968 0.07741  0.00607  470 ALA A CB  
4182 N N   . ASN A 592 ? 0.84118 0.66702 0.96355 -0.02217 0.09935  0.03154  471 ASN A N   
4183 C CA  . ASN A 592 ? 0.91388 0.74220 1.06012 -0.01041 0.10606  0.04332  471 ASN A CA  
4184 C C   . ASN A 592 ? 0.88717 0.73735 1.02967 -0.00439 0.09329  0.04703  471 ASN A C   
4185 O O   . ASN A 592 ? 0.74344 0.61367 0.88640 0.00284  0.08226  0.05900  471 ASN A O   
4186 C CB  . ASN A 592 ? 0.86916 0.69975 1.03323 -0.00157 0.11001  0.06111  471 ASN A CB  
4187 C CG  . ASN A 592 ? 0.91697 0.74525 1.10915 0.01059  0.12140  0.07348  471 ASN A CG  
4188 O OD1 . ASN A 592 ? 0.75090 0.59405 0.95052 0.01747  0.11714  0.07694  471 ASN A OD1 
4189 N ND2 . ASN A 592 ? 0.85151 0.66161 1.06097 0.01337  0.13661  0.08074  471 ASN A ND2 
4190 N N   . LEU A 593 ? 0.71194 0.55802 0.84975 -0.00855 0.09548  0.03585  472 LEU A N   
4191 C CA  . LEU A 593 ? 0.72389 0.58827 0.85689 -0.00609 0.08438  0.03649  472 LEU A CA  
4192 C C   . LEU A 593 ? 0.75084 0.63478 0.90804 0.00567  0.08281  0.05151  472 LEU A C   
4193 O O   . LEU A 593 ? 0.78100 0.68637 0.93447 0.00809  0.07006  0.05558  472 LEU A O   
4194 C CB  . LEU A 593 ? 0.99818 0.85191 1.12242 -0.01373 0.08980  0.02204  472 LEU A CB  
4195 C CG  . LEU A 593 ? 0.85120 0.69038 0.94894 -0.02516 0.08924  0.00818  472 LEU A CG  
4196 C CD1 . LEU A 593 ? 0.79772 0.62614 0.88687 -0.03194 0.09657  -0.00428 472 LEU A CD1 
4197 C CD2 . LEU A 593 ? 0.77081 0.62185 0.84843 -0.02605 0.07356  0.00958  472 LEU A CD2 
4198 N N   . LYS A 594 ? 0.69645 0.57415 0.87867 0.01301  0.09579  0.05996  473 LYS A N   
4199 C CA  . LYS A 594 ? 0.91486 0.81495 1.12223 0.02573  0.09394  0.07671  473 LYS A CA  
4200 C C   . LYS A 594 ? 0.99260 0.91336 1.19704 0.03234  0.08102  0.09191  473 LYS A C   
4201 O O   . LYS A 594 ? 0.68292 0.63176 0.89273 0.03785  0.06965  0.10068  473 LYS A O   
4202 C CB  . LYS A 594 ? 0.97341 0.86005 1.20935 0.03401  0.11269  0.08394  473 LYS A CB  
4203 C CG  . LYS A 594 ? 1.14471 1.01686 1.38692 0.02959  0.12608  0.07034  473 LYS A CG  
4204 C CD  . LYS A 594 ? 1.09144 0.95032 1.36421 0.03965  0.14637  0.07798  473 LYS A CD  
4205 C CE  . LYS A 594 ? 1.13873 0.96762 1.40659 0.03059  0.16435  0.05882  473 LYS A CE  
4206 N NZ  . LYS A 594 ? 1.32425 1.13925 1.62328 0.04115  0.18641  0.06482  473 LYS A NZ  
4207 N N   . ARG A 595 ? 0.72695 0.63585 0.92185 0.03073  0.08245  0.09448  474 ARG A N   
4208 C CA  . ARG A 595 ? 0.75662 0.68496 0.94613 0.03661  0.07120  0.10865  474 ARG A CA  
4209 C C   . ARG A 595 ? 0.62312 0.56718 0.78737 0.03064  0.05454  0.10047  474 ARG A C   
4210 O O   . ARG A 595 ? 0.73776 0.70651 0.89914 0.03601  0.04307  0.11041  474 ARG A O   
4211 C CB  . ARG A 595 ? 0.73193 0.64333 0.91904 0.03551  0.07866  0.11333  474 ARG A CB  
4212 C CG  . ARG A 595 ? 0.64396 0.53816 0.85695 0.04245  0.09642  0.12384  474 ARG A CG  
4213 C CD  . ARG A 595 ? 0.76078 0.63481 0.96957 0.03717  0.10480  0.12430  474 ARG A CD  
4214 N NE  . ARG A 595 ? 0.83471 0.72677 1.03160 0.03986  0.09352  0.13562  474 ARG A NE  
4215 C CZ  . ARG A 595 ? 0.87890 0.76244 1.06350 0.03201  0.09426  0.13211  474 ARG A CZ  
4216 N NH1 . ARG A 595 ? 0.77180 0.63056 0.95430 0.02000  0.10441  0.11720  474 ARG A NH1 
4217 N NH2 . ARG A 595 ? 0.86550 0.76710 1.03981 0.03552  0.08499  0.14302  474 ARG A NH2 
4218 N N   . LEU A 596 ? 0.60184 0.53194 0.74733 0.01982  0.05366  0.08260  475 LEU A N   
4219 C CA  . LEU A 596 ? 0.78751 0.72809 0.90992 0.01482  0.04032  0.07448  475 LEU A CA  
4220 C C   . LEU A 596 ? 0.70647 0.66764 0.83477 0.01657  0.03273  0.07512  475 LEU A C   
4221 O O   . LEU A 596 ? 0.74591 0.72698 0.86496 0.01790  0.02092  0.07831  475 LEU A O   
4222 C CB  . LEU A 596 ? 0.58641 0.50720 0.69002 0.00438  0.04254  0.05753  475 LEU A CB  
4223 C CG  . LEU A 596 ? 0.66421 0.58973 0.74370 -0.00021 0.03161  0.04890  475 LEU A CG  
4224 C CD1 . LEU A 596 ? 0.55480 0.48496 0.62044 0.00133  0.02568  0.05281  475 LEU A CD1 
4225 C CD2 . LEU A 596 ? 0.61571 0.52373 0.68215 -0.00869 0.03532  0.03457  475 LEU A CD2 
4226 N N   . TYR A 597 ? 0.73823 0.69579 0.88240 0.01581  0.04008  0.07143  476 TYR A N   
4227 C CA  . TYR A 597 ? 0.63145 0.61143 0.78616 0.01658  0.03382  0.07247  476 TYR A CA  
4228 C C   . TYR A 597 ? 0.51209 0.52133 0.68389 0.02702  0.02722  0.09056  476 TYR A C   
4229 O O   . TYR A 597 ? 0.67013 0.70498 0.83911 0.02589  0.01503  0.09158  476 TYR A O   
4230 C CB  . TYR A 597 ? 0.66589 0.63692 0.83748 0.01462  0.04535  0.06645  476 TYR A CB  
4231 C CG  . TYR A 597 ? 0.68843 0.64213 0.84099 0.00316  0.04724  0.04884  476 TYR A CG  
4232 C CD1 . TYR A 597 ? 0.70602 0.63503 0.83696 -0.00276 0.05096  0.03947  476 TYR A CD1 
4233 C CD2 . TYR A 597 ? 0.54953 0.51313 0.70659 -0.00189 0.04556  0.04260  476 TYR A CD2 
4234 C CE1 . TYR A 597 ? 0.65713 0.57190 0.76996 -0.01192 0.05253  0.02588  476 TYR A CE1 
4235 C CE2 . TYR A 597 ? 0.67922 0.62581 0.81861 -0.01176 0.04851  0.02853  476 TYR A CE2 
4236 C CZ  . TYR A 597 ? 0.77396 0.69606 0.89059 -0.01601 0.05189  0.02095  476 TYR A CZ  
4237 O OH  . TYR A 597 ? 0.67434 0.58098 0.77266 -0.02462 0.05470  0.00928  476 TYR A OH  
4238 N N   . ALA A 598 ? 0.58492 0.59126 0.77503 0.03693  0.03566  0.10513  477 ALA A N   
4239 C CA  . ALA A 598 ? 0.70310 0.73804 0.90909 0.04861  0.02975  0.12558  477 ALA A CA  
4240 C C   . ALA A 598 ? 0.81575 0.86831 0.99873 0.04730  0.01495  0.12837  477 ALA A C   
4241 O O   . ALA A 598 ? 0.95190 1.03674 1.13684 0.04988  0.00290  0.13539  477 ALA A O   
4242 C CB  . ALA A 598 ? 0.75898 0.78051 0.98448 0.05939  0.04342  0.14113  477 ALA A CB  
4243 N N   . GLN A 599 ? 0.74509 0.77846 0.90653 0.04318  0.01610  0.12296  478 GLN A N   
4244 C CA  . GLN A 599 ? 0.70768 0.75496 0.84593 0.04204  0.00440  0.12421  478 GLN A CA  
4245 C C   . GLN A 599 ? 0.68191 0.74278 0.80389 0.03351  -0.00747 0.11018  478 GLN A C   
4246 O O   . GLN A 599 ? 0.64629 0.73320 0.75951 0.03445  -0.01894 0.11442  478 GLN A O   
4247 C CB  . GLN A 599 ? 0.62337 0.64685 0.74426 0.03837  0.00949  0.11898  478 GLN A CB  
4248 C CG  . GLN A 599 ? 0.64147 0.67586 0.73741 0.03700  -0.00014 0.11801  478 GLN A CG  
4249 C CD  . GLN A 599 ? 0.73747 0.75110 0.81994 0.03339  0.00538  0.11280  478 GLN A CD  
4250 O OE1 . GLN A 599 ? 0.66126 0.66721 0.75249 0.03716  0.01332  0.12340  478 GLN A OE1 
4251 N NE2 . GLN A 599 ? 0.57749 0.58241 0.63998 0.02603  0.00177  0.09699  478 GLN A NE2 
4252 N N   . ARG A 600 ? 0.64697 0.68918 0.76276 0.02435  -0.00419 0.09290  479 ARG A N   
4253 C CA  . ARG A 600 ? 0.62652 0.67730 0.72932 0.01544  -0.01285 0.07928  479 ARG A CA  
4254 C C   . ARG A 600 ? 0.70530 0.78975 0.82452 0.01676  -0.02103 0.08565  479 ARG A C   
4255 O O   . ARG A 600 ? 0.61468 0.71917 0.72098 0.01207  -0.03235 0.08144  479 ARG A O   
4256 C CB  . ARG A 600 ? 0.66535 0.69119 0.76485 0.00703  -0.00553 0.06371  479 ARG A CB  
4257 C CG  . ARG A 600 ? 0.54152 0.57126 0.62920 -0.00293 -0.01173 0.04971  479 ARG A CG  
4258 C CD  . ARG A 600 ? 0.57048 0.57508 0.65570 -0.01002 -0.00287 0.03740  479 ARG A CD  
4259 N NE  . ARG A 600 ? 0.83170 0.81017 0.90103 -0.00965 0.00292  0.03395  479 ARG A NE  
4260 C CZ  . ARG A 600 ? 0.79359 0.74967 0.86006 -0.01366 0.01179  0.02662  479 ARG A CZ  
4261 N NH1 . ARG A 600 ? 0.89407 0.83203 0.94606 -0.01368 0.01503  0.02422  479 ARG A NH1 
4262 N NH2 . ARG A 600 ? 0.76857 0.72251 0.84655 -0.01800 0.01743  0.02187  479 ARG A NH2 
4263 N N   . GLU A 601 ? 0.52562 0.61764 0.67399 0.02278  -0.01499 0.09523  480 GLU A N   
4264 C CA  . GLU A 601 ? 0.55824 0.68667 0.72675 0.02470  -0.02282 0.10270  480 GLU A CA  
4265 C C   . GLU A 601 ? 0.77411 0.93427 0.94098 0.03261  -0.03385 0.11917  480 GLU A C   
4266 O O   . GLU A 601 ? 0.59347 0.78824 0.76232 0.02952  -0.04628 0.12018  480 GLU A O   
4267 C CB  . GLU A 601 ? 0.60262 0.73185 0.80520 0.03170  -0.01190 0.11098  480 GLU A CB  
4268 C CG  . GLU A 601 ? 0.73868 0.90854 0.96591 0.03305  -0.01971 0.11785  480 GLU A CG  
4269 C CD  . GLU A 601 ? 0.83392 1.01414 1.04977 0.01734  -0.02851 0.09955  480 GLU A CD  
4270 O OE1 . GLU A 601 ? 0.92317 1.07325 1.12448 0.00730  -0.02191 0.08224  480 GLU A OE1 
4271 O OE2 . GLU A 601 ? 0.97157 1.19037 1.19243 0.01455  -0.04191 0.10267  480 GLU A OE2 
4272 N N   . GLU A 602 ? 0.66828 0.81863 0.83128 0.04200  -0.02938 0.13226  481 GLU A N   
4273 C CA  . GLU A 602 ? 0.70659 0.88619 0.86441 0.04964  -0.03912 0.14898  481 GLU A CA  
4274 C C   . GLU A 602 ? 0.74737 0.93614 0.87226 0.03980  -0.05119 0.13605  481 GLU A C   
4275 O O   . GLU A 602 ? 0.75506 0.97922 0.87455 0.03992  -0.06391 0.14189  481 GLU A O   
4276 C CB  . GLU A 602 ? 0.64205 0.80516 0.80252 0.06077  -0.02940 0.16549  481 GLU A CB  
4277 C CG  . GLU A 602 ? 0.86234 1.05266 1.01380 0.06897  -0.03785 0.18408  481 GLU A CG  
4278 C CD  . GLU A 602 ? 1.16658 1.40013 1.33867 0.07729  -0.04714 0.20170  481 GLU A CD  
4279 O OE1 . GLU A 602 ? 1.08108 1.31632 1.28517 0.08591  -0.03955 0.21282  481 GLU A OE1 
4280 O OE2 . GLU A 602 ? 1.16624 1.43337 1.32263 0.07524  -0.06181 0.20428  481 GLU A OE2 
4281 N N   . PHE A 603 ? 0.74172 0.89988 0.84454 0.03088  -0.04714 0.11765  482 PHE A N   
4282 C CA  . PHE A 603 ? 0.71512 0.87759 0.78757 0.02170  -0.05603 0.10342  482 PHE A CA  
4283 C C   . PHE A 603 ? 0.80158 0.98419 0.87505 0.01071  -0.06518 0.09062  482 PHE A C   
4284 O O   . PHE A 603 ? 0.69313 0.89884 0.74978 0.00524  -0.07616 0.08601  482 PHE A O   
4285 C CB  . PHE A 603 ? 0.64231 0.76758 0.69425 0.01640  -0.04849 0.08828  482 PHE A CB  
4286 C CG  . PHE A 603 ? 0.81836 0.93083 0.86079 0.02376  -0.04294 0.09748  482 PHE A CG  
4287 C CD1 . PHE A 603 ? 0.72480 0.85546 0.75113 0.02767  -0.04881 0.10550  482 PHE A CD1 
4288 C CD2 . PHE A 603 ? 0.76805 0.85119 0.81616 0.02530  -0.03166 0.09681  482 PHE A CD2 
4289 C CE1 . PHE A 603 ? 0.78520 0.90493 0.80394 0.03367  -0.04265 0.11410  482 PHE A CE1 
4290 C CE2 . PHE A 603 ? 0.82029 0.89365 0.86140 0.03021  -0.02649 0.10441  482 PHE A CE2 
4291 C CZ  . PHE A 603 ? 0.79689 0.88831 0.82431 0.03463  -0.03156 0.11352  482 PHE A CZ  
4292 N N   . ARG A 604 ? 0.69746 0.87159 0.78989 0.00621  -0.06009 0.08379  483 ARG A N   
4293 C CA  . ARG A 604 ? 0.62039 0.81561 0.71882 -0.00510 -0.06767 0.07272  483 ARG A CA  
4294 C C   . ARG A 604 ? 0.54495 0.78918 0.65739 -0.00144 -0.08032 0.08664  483 ARG A C   
4295 O O   . ARG A 604 ? 0.76615 1.03560 0.86579 -0.01147 -0.09226 0.07783  483 ARG A O   
4296 C CB  . ARG A 604 ? 0.79312 0.97374 0.91416 -0.00830 -0.05814 0.06731  483 ARG A CB  
4297 C CG  . ARG A 604 ? 1.03492 1.17121 1.14094 -0.01330 -0.04695 0.05321  483 ARG A CG  
4298 C CD  . ARG A 604 ? 1.05293 1.17797 1.17921 -0.01727 -0.03756 0.04790  483 ARG A CD  
4299 N NE  . ARG A 604 ? 0.85209 0.93844 0.96043 -0.02381 -0.02858 0.03366  483 ARG A NE  
4300 C CZ  . ARG A 604 ? 1.01036 1.07628 1.12917 -0.02462 -0.01697 0.03063  483 ARG A CZ  
4301 N NH1 . ARG A 604 ? 1.00874 1.08695 1.15689 -0.01896 -0.01151 0.03988  483 ARG A NH1 
4302 N NH2 . ARG A 604 ? 0.95272 0.98638 1.05236 -0.03024 -0.01018 0.01910  483 ARG A NH2 
4303 N N   . LYS A 605 ? 0.56837 0.82700 0.70790 0.01270  -0.07742 0.10840  484 LYS A N   
4304 C CA  . LYS A 605 ? 0.71139 1.01941 0.86736 0.01918  -0.08925 0.12602  484 LYS A CA  
4305 C C   . LYS A 605 ? 0.62810 0.95701 0.75509 0.01822  -0.10142 0.12870  484 LYS A C   
4306 O O   . LYS A 605 ? 0.69134 1.06198 0.81606 0.01239  -0.11599 0.12864  484 LYS A O   
4307 C CB  . LYS A 605 ? 0.63721 0.94845 0.82460 0.03762  -0.08067 0.15118  484 LYS A CB  
4308 C CG  . LYS A 605 ? 0.78660 1.13895 0.98263 0.05090  -0.09008 0.17709  484 LYS A CG  
4309 C CD  . LYS A 605 ? 0.92304 1.27577 1.15662 0.06890  -0.07888 0.20065  484 LYS A CD  
4310 C CE  . LYS A 605 ? 1.04056 1.44084 1.28939 0.08348  -0.08878 0.22935  484 LYS A CE  
4311 N NZ  . LYS A 605 ? 1.12017 1.57233 1.36275 0.07368  -0.10940 0.22492  484 LYS A NZ  
4312 N N   . GLY A 606 ? 0.65014 0.95212 0.75426 0.02302  -0.09548 0.13037  485 GLY A N   
4313 C CA  . GLY A 606 ? 0.61387 0.93229 0.68735 0.02138  -0.10490 0.13074  485 GLY A CA  
4314 C C   . GLY A 606 ? 0.61092 0.93196 0.65827 0.00334  -0.11280 0.10474  485 GLY A C   
4315 O O   . GLY A 606 ? 0.76218 1.11481 0.79131 -0.00171 -0.12508 0.10318  485 GLY A O   
4316 N N   . ASN A 607 ? 0.66075 0.94801 0.70517 -0.00691 -0.10512 0.08397  486 ASN A N   
4317 C CA  . ASN A 607 ? 0.72714 1.01004 0.74820 -0.02424 -0.10960 0.05861  486 ASN A CA  
4318 C C   . ASN A 607 ? 0.78915 1.10988 0.82393 -0.03621 -0.12118 0.05215  486 ASN A C   
4319 O O   . ASN A 607 ? 0.96263 1.28859 0.97710 -0.05197 -0.12714 0.03211  486 ASN A O   
4320 C CB  . ASN A 607 ? 0.91455 1.14954 0.93012 -0.03031 -0.09691 0.04118  486 ASN A CB  
4321 C CG  . ASN A 607 ? 0.99095 1.19164 0.98501 -0.02332 -0.08780 0.04086  486 ASN A CG  
4322 O OD1 . ASN A 607 ? 1.05986 1.22402 1.05226 -0.02411 -0.07731 0.03270  486 ASN A OD1 
4323 N ND2 . ASN A 607 ? 0.89748 1.11196 0.87506 -0.01657 -0.09179 0.05029  486 ASN A ND2 
4324 N N   . TRP A 608 ? 0.75319 1.10053 0.82283 -0.02955 -0.12373 0.06809  487 TRP A N   
4325 C CA  . TRP A 608 ? 0.79865 1.18977 0.88530 -0.04030 -0.13591 0.06441  487 TRP A CA  
4326 C C   . TRP A 608 ? 0.81845 1.26419 0.90251 -0.03651 -0.15251 0.07939  487 TRP A C   
4327 O O   . TRP A 608 ? 1.11088 1.60135 1.21088 -0.04486 -0.16480 0.07876  487 TRP A O   
4328 C CB  . TRP A 608 ? 0.82103 1.21687 0.94923 -0.03547 -0.12979 0.07324  487 TRP A CB  
4329 C CG  . TRP A 608 ? 1.07404 1.43213 1.20372 -0.04745 -0.11846 0.05260  487 TRP A CG  
4330 C CD1 . TRP A 608 ? 0.93914 1.24518 1.05852 -0.04440 -0.10349 0.04629  487 TRP A CD1 
4331 C CD2 . TRP A 608 ? 1.17295 1.54359 1.31402 -0.06520 -0.12118 0.03589  487 TRP A CD2 
4332 N NE1 . TRP A 608 ? 1.02820 1.31307 1.15091 -0.05780 -0.09652 0.02820  487 TRP A NE1 
4333 C CE2 . TRP A 608 ? 1.20855 1.53077 1.34493 -0.07101 -0.10636 0.02133  487 TRP A CE2 
4334 C CE3 . TRP A 608 ? 0.97553 1.39548 1.13098 -0.07739 -0.13474 0.03221  487 TRP A CE3 
4335 C CZ2 . TRP A 608 ? 1.19277 1.51135 1.33798 -0.08805 -0.10329 0.00409  487 TRP A CZ2 
4336 C CZ3 . TRP A 608 ? 1.11556 1.53284 1.28137 -0.09562 -0.13197 0.01356  487 TRP A CZ3 
4337 C CH2 . TRP A 608 ? 1.06114 1.42659 1.22165 -0.10057 -0.11567 0.00008  487 TRP A CH2 
4338 N N   . LYS A 609 ? 0.96214 1.40763 1.02675 -0.02461 -0.15330 0.09330  488 LYS A N   
4339 C CA  . LYS A 609 ? 0.84142 1.33820 0.89804 -0.02064 -0.16885 0.10852  488 LYS A CA  
4340 C C   . LYS A 609 ? 0.82655 1.33225 0.84458 -0.03955 -0.17821 0.08423  488 LYS A C   
4341 O O   . LYS A 609 ? 0.91471 1.39215 0.89918 -0.04025 -0.17259 0.07526  488 LYS A O   
4342 C CB  . LYS A 609 ? 0.81777 1.30863 0.86979 -0.00009 -0.16375 0.13459  488 LYS A CB  
4343 C CG  . LYS A 609 ? 0.83601 1.32382 0.92781 0.01851  -0.15500 0.16003  488 LYS A CG  
4344 C CD  . LYS A 609 ? 0.70186 1.24203 0.82759 0.02038  -0.16648 0.17279  488 LYS A CD  
4345 C CE  . LYS A 609 ? 0.72300 1.26718 0.88624 0.04290  -0.15823 0.20374  488 LYS A CE  
4346 N NZ  . LYS A 609 ? 0.98114 1.55306 1.18608 0.04345  -0.16042 0.20803  488 LYS A NZ  
4347 N N   . ALA A 610 ? 0.69564 1.24127 0.71941 -0.05554 -0.19179 0.07277  489 ALA A N   
4348 C CA  . ALA A 610 ? 0.86071 1.40494 0.85175 -0.07853 -0.19716 0.04209  489 ALA A CA  
4349 C C   . ALA A 610 ? 0.94565 1.50764 0.89692 -0.07867 -0.20515 0.04248  489 ALA A C   
4350 O O   . ALA A 610 ? 1.05752 1.59465 0.97338 -0.09175 -0.20135 0.01777  489 ALA A O   
4351 C CB  . ALA A 610 ? 0.97927 1.56701 0.98928 -0.09683 -0.21030 0.03077  489 ALA A CB  
4352 N N   . LEU A 611 ? 0.81319 1.41670 0.76921 -0.06368 -0.21487 0.07069  490 LEU A N   
4353 C CA  . LEU A 611 ? 0.94371 1.57138 0.86188 -0.06365 -0.22350 0.07365  490 LEU A CA  
4354 C C   . LEU A 611 ? 0.88107 1.46942 0.77813 -0.04776 -0.20958 0.08421  490 LEU A C   
4355 O O   . LEU A 611 ? 0.89113 1.49242 0.75328 -0.04770 -0.21346 0.08496  490 LEU A O   
4356 C CB  . LEU A 611 ? 0.74752 1.44480 0.67962 -0.05565 -0.24199 0.10066  490 LEU A CB  
4357 C CG  . LEU A 611 ? 0.89396 1.64080 0.85244 -0.07003 -0.25761 0.09433  490 LEU A CG  
4358 C CD1 . LEU A 611 ? 0.75738 1.57148 0.73804 -0.05560 -0.27382 0.12855  490 LEU A CD1 
4359 C CD2 . LEU A 611 ? 0.94514 1.70447 0.87144 -0.09896 -0.26696 0.05888  490 LEU A CD2 
4360 N N   . ALA A 612 ? 0.79248 1.33469 0.70906 -0.03551 -0.19331 0.09140  491 ALA A N   
4361 C CA  . ALA A 612 ? 1.05246 1.55978 0.95353 -0.02127 -0.18001 0.10201  491 ALA A CA  
4362 C C   . ALA A 612 ? 1.27519 1.73821 1.14362 -0.03237 -0.16952 0.07321  491 ALA A C   
4363 O O   . ALA A 612 ? 1.21088 1.64482 1.08379 -0.04412 -0.16386 0.05053  491 ALA A O   
4364 C CB  . ALA A 612 ? 0.97961 1.45863 0.91576 -0.00465 -0.16726 0.12135  491 ALA A CB  
4365 N N   . VAL A 613 ? 1.40220 1.86008 1.23861 -0.02766 -0.16583 0.07548  492 VAL A N   
4366 C CA  . VAL A 613 ? 1.56798 1.98706 1.37266 -0.03571 -0.15501 0.05038  492 VAL A CA  
4367 C C   . VAL A 613 ? 1.55685 1.93869 1.36157 -0.02020 -0.13914 0.06257  492 VAL A C   
4368 O O   . VAL A 613 ? 1.52776 1.91901 1.31484 -0.01095 -0.13717 0.07664  492 VAL A O   
4369 C CB  . VAL A 613 ? 1.63128 2.07617 1.39434 -0.04649 -0.16286 0.03686  492 VAL A CB  
4370 C CG1 . VAL A 613 ? 1.62449 2.02666 1.35694 -0.05455 -0.14960 0.00920  492 VAL A CG1 
4371 C CG2 . VAL A 613 ? 1.63630 2.12459 1.40067 -0.06334 -0.18034 0.02562  492 VAL A CG2 
# 
