File: 2XHE.cif

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data_2XHE
# 
_entry.id   2XHE 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   2XHE         
PDBE  EBI-44243    
WWPDB D_1290044243 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2XHE 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2010-06-14 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Burkhardt, P.'  1 
'Stegmann, C.M.' 2 
'Wahl, M.C.'     3 
'Fasshauer, D.'  4 
# 
_citation.id                        primary 
_citation.title                     'Primordial Neurosecretory Apparatus Identified in the Choanoflagellate Monosiga Brevicollis.' 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_volume            108 
_citation.page_first                15264 
_citation.page_last                 ? 
_citation.year                      2011 
_citation.journal_id_ASTM           PNASA6 
_citation.country                   US 
_citation.journal_id_ISSN           0027-8424 
_citation.journal_id_CSD            0040 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   21876177 
_citation.pdbx_database_id_DOI      10.1073/PNAS.1106189108 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Burkhardt, P.'  1 
primary 'Stegmann, C.M.' 2 
primary 'Cooper, B.'     3 
primary 'Kloepper, T.H.' 4 
primary 'Imig, C.'       5 
primary 'Varoqueaux, F.' 6 
primary 'Wahl, M.C.'     7 
primary 'Fasshauer, D.'  8 
# 
_cell.entry_id           2XHE 
_cell.length_a           146.200 
_cell.length_b           146.200 
_cell.length_c           214.861 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         2XHE 
_symmetry.space_group_name_H-M             'P 65 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                179 
# 
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 UNC18     71997.641 1  ? ? ? ? 
2 polymer man SYNTAXIN1 31979.686 1  ? ? ? ? 
3 water   nat water     18.015    48 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;HMSLKSAVKTVLTNSLRSVADGGDWKVLVVDKPALRMISECARMSEILDLGVTVVEDVSKQRKVLPQFHGVYFIEPTEEN
LDYVIRDFADRTPTYEAAHLFFLSPVPDALMAKLASAKAVKYVKTLKEINTLFIPKEHRVFTLNEPHGLVQYYGSRSSSY
NIDHLVRRLSTLCTTMNVAPIVRYSSTSTPGTERMAMQLQKEIDMSVSQGLINAREGKLKSQFLILDRAVDLKSPLVHEL
TYQAAAYDLLNIENDIYSYSTVDAGGREQQRQVVLGEDDDIWLQMRHLHISEVFRKVKSSFDEFCVSARRLQGLRDSQQG
EGGAGALKQMLKDLPQHREQMQKYSLHLDMSNAINMAFSSTIDSCTKAEQNIVTEEEQDGNKVRDFIGEVASVVVDRRVS
TEDKLRCLMLCVLAKNGTSSHELNNLLDNANIATPSRSAIYNLEMLGATVVADRRGRKPKTMKRIERDMPYVLSRWTPIV
KDLMEYIATGQLDLESYPAVRDGPSVVQPKRASKSVEEDDDGPATSARKRGNWAKNKGNNRSLPSTPSGVAVSGNGAAGA
AESAKPKLFVFINGTVSYNEIRCAYEVSQSSGYEVYIGAHNIATPAEFVELVSLLDKADQDVQVLTQGQGDGGLVITTGS
AQAGLNLAEV
;
;HMSLKSAVKTVLTNSLRSVADGGDWKVLVVDKPALRMISECARMSEILDLGVTVVEDVSKQRKVLPQFHGVYFIEPTEEN
LDYVIRDFADRTPTYEAAHLFFLSPVPDALMAKLASAKAVKYVKTLKEINTLFIPKEHRVFTLNEPHGLVQYYGSRSSSY
NIDHLVRRLSTLCTTMNVAPIVRYSSTSTPGTERMAMQLQKEIDMSVSQGLINAREGKLKSQFLILDRAVDLKSPLVHEL
TYQAAAYDLLNIENDIYSYSTVDAGGREQQRQVVLGEDDDIWLQMRHLHISEVFRKVKSSFDEFCVSARRLQGLRDSQQG
EGGAGALKQMLKDLPQHREQMQKYSLHLDMSNAINMAFSSTIDSCTKAEQNIVTEEEQDGNKVRDFIGEVASVVVDRRVS
TEDKLRCLMLCVLAKNGTSSHELNNLLDNANIATPSRSAIYNLEMLGATVVADRRGRKPKTMKRIERDMPYVLSRWTPIV
KDLMEYIATGQLDLESYPAVRDGPSVVQPKRASKSVEEDDDGPATSARKRGNWAKNKGNNRSLPSTPSGVAVSGNGAAGA
AESAKPKLFVFINGTVSYNEIRCAYEVSQSSGYEVYIGAHNIATPAEFVELVSLLDKADQDVQVLTQGQGDGGLVITTGS
AQAGLNLAEV
;
A ? 
2 'polypeptide(L)' no no 
;MDRLSRLRQMAAENQPAEASDAAGGAEAQIEETSLSAQPEPFMADFFNRVKRIRDNIEDIEQAIEQVAQLHTESLVAVSK
EDRDRLNEKLQDTMARISALGNKIRADLKQIEKENKRAQQEGTFEDGTVSTDLRIRQSQHSSLSRKFVKVMTRYNDVQAE
NKRRYGENVARQCRVVEPSLSDDAIQKVIEHGTEGIFSGMRLEGAEAKLNEIRDRHKDIQQLERSLLELHEMFTDMSTLV
ASQGEMIDRIEFSVEQSHNYVKKATEQVVQARHYQESAR
;
;MDRLSRLRQMAAENQPAEASDAAGGAEAQIEETSLSAQPEPFMADFFNRVKRIRDNIEDIEQAIEQVAQLHTESLVAVSK
EDRDRLNEKLQDTMARISALGNKIRADLKQIEKENKRAQQEGTFEDGTVSTDLRIRQSQHSSLSRKFVKVMTRYNDVQAE
NKRRYGENVARQCRVVEPSLSDDAIQKVIEHGTEGIFSGMRLEGAEAKLNEIRDRHKDIQQLERSLLELHEMFTDMSTLV
ASQGEMIDRIEFSVEQSHNYVKKATEQVVQARHYQESAR
;
B ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   MET n 
1 3   SER n 
1 4   LEU n 
1 5   LYS n 
1 6   SER n 
1 7   ALA n 
1 8   VAL n 
1 9   LYS n 
1 10  THR n 
1 11  VAL n 
1 12  LEU n 
1 13  THR n 
1 14  ASN n 
1 15  SER n 
1 16  LEU n 
1 17  ARG n 
1 18  SER n 
1 19  VAL n 
1 20  ALA n 
1 21  ASP n 
1 22  GLY n 
1 23  GLY n 
1 24  ASP n 
1 25  TRP n 
1 26  LYS n 
1 27  VAL n 
1 28  LEU n 
1 29  VAL n 
1 30  VAL n 
1 31  ASP n 
1 32  LYS n 
1 33  PRO n 
1 34  ALA n 
1 35  LEU n 
1 36  ARG n 
1 37  MET n 
1 38  ILE n 
1 39  SER n 
1 40  GLU n 
1 41  CYS n 
1 42  ALA n 
1 43  ARG n 
1 44  MET n 
1 45  SER n 
1 46  GLU n 
1 47  ILE n 
1 48  LEU n 
1 49  ASP n 
1 50  LEU n 
1 51  GLY n 
1 52  VAL n 
1 53  THR n 
1 54  VAL n 
1 55  VAL n 
1 56  GLU n 
1 57  ASP n 
1 58  VAL n 
1 59  SER n 
1 60  LYS n 
1 61  GLN n 
1 62  ARG n 
1 63  LYS n 
1 64  VAL n 
1 65  LEU n 
1 66  PRO n 
1 67  GLN n 
1 68  PHE n 
1 69  HIS n 
1 70  GLY n 
1 71  VAL n 
1 72  TYR n 
1 73  PHE n 
1 74  ILE n 
1 75  GLU n 
1 76  PRO n 
1 77  THR n 
1 78  GLU n 
1 79  GLU n 
1 80  ASN n 
1 81  LEU n 
1 82  ASP n 
1 83  TYR n 
1 84  VAL n 
1 85  ILE n 
1 86  ARG n 
1 87  ASP n 
1 88  PHE n 
1 89  ALA n 
1 90  ASP n 
1 91  ARG n 
1 92  THR n 
1 93  PRO n 
1 94  THR n 
1 95  TYR n 
1 96  GLU n 
1 97  ALA n 
1 98  ALA n 
1 99  HIS n 
1 100 LEU n 
1 101 PHE n 
1 102 PHE n 
1 103 LEU n 
1 104 SER n 
1 105 PRO n 
1 106 VAL n 
1 107 PRO n 
1 108 ASP n 
1 109 ALA n 
1 110 LEU n 
1 111 MET n 
1 112 ALA n 
1 113 LYS n 
1 114 LEU n 
1 115 ALA n 
1 116 SER n 
1 117 ALA n 
1 118 LYS n 
1 119 ALA n 
1 120 VAL n 
1 121 LYS n 
1 122 TYR n 
1 123 VAL n 
1 124 LYS n 
1 125 THR n 
1 126 LEU n 
1 127 LYS n 
1 128 GLU n 
1 129 ILE n 
1 130 ASN n 
1 131 THR n 
1 132 LEU n 
1 133 PHE n 
1 134 ILE n 
1 135 PRO n 
1 136 LYS n 
1 137 GLU n 
1 138 HIS n 
1 139 ARG n 
1 140 VAL n 
1 141 PHE n 
1 142 THR n 
1 143 LEU n 
1 144 ASN n 
1 145 GLU n 
1 146 PRO n 
1 147 HIS n 
1 148 GLY n 
1 149 LEU n 
1 150 VAL n 
1 151 GLN n 
1 152 TYR n 
1 153 TYR n 
1 154 GLY n 
1 155 SER n 
1 156 ARG n 
1 157 SER n 
1 158 SER n 
1 159 SER n 
1 160 TYR n 
1 161 ASN n 
1 162 ILE n 
1 163 ASP n 
1 164 HIS n 
1 165 LEU n 
1 166 VAL n 
1 167 ARG n 
1 168 ARG n 
1 169 LEU n 
1 170 SER n 
1 171 THR n 
1 172 LEU n 
1 173 CYS n 
1 174 THR n 
1 175 THR n 
1 176 MET n 
1 177 ASN n 
1 178 VAL n 
1 179 ALA n 
1 180 PRO n 
1 181 ILE n 
1 182 VAL n 
1 183 ARG n 
1 184 TYR n 
1 185 SER n 
1 186 SER n 
1 187 THR n 
1 188 SER n 
1 189 THR n 
1 190 PRO n 
1 191 GLY n 
1 192 THR n 
1 193 GLU n 
1 194 ARG n 
1 195 MET n 
1 196 ALA n 
1 197 MET n 
1 198 GLN n 
1 199 LEU n 
1 200 GLN n 
1 201 LYS n 
1 202 GLU n 
1 203 ILE n 
1 204 ASP n 
1 205 MET n 
1 206 SER n 
1 207 VAL n 
1 208 SER n 
1 209 GLN n 
1 210 GLY n 
1 211 LEU n 
1 212 ILE n 
1 213 ASN n 
1 214 ALA n 
1 215 ARG n 
1 216 GLU n 
1 217 GLY n 
1 218 LYS n 
1 219 LEU n 
1 220 LYS n 
1 221 SER n 
1 222 GLN n 
1 223 PHE n 
1 224 LEU n 
1 225 ILE n 
1 226 LEU n 
1 227 ASP n 
1 228 ARG n 
1 229 ALA n 
1 230 VAL n 
1 231 ASP n 
1 232 LEU n 
1 233 LYS n 
1 234 SER n 
1 235 PRO n 
1 236 LEU n 
1 237 VAL n 
1 238 HIS n 
1 239 GLU n 
1 240 LEU n 
1 241 THR n 
1 242 TYR n 
1 243 GLN n 
1 244 ALA n 
1 245 ALA n 
1 246 ALA n 
1 247 TYR n 
1 248 ASP n 
1 249 LEU n 
1 250 LEU n 
1 251 ASN n 
1 252 ILE n 
1 253 GLU n 
1 254 ASN n 
1 255 ASP n 
1 256 ILE n 
1 257 TYR n 
1 258 SER n 
1 259 TYR n 
1 260 SER n 
1 261 THR n 
1 262 VAL n 
1 263 ASP n 
1 264 ALA n 
1 265 GLY n 
1 266 GLY n 
1 267 ARG n 
1 268 GLU n 
1 269 GLN n 
1 270 GLN n 
1 271 ARG n 
1 272 GLN n 
1 273 VAL n 
1 274 VAL n 
1 275 LEU n 
1 276 GLY n 
1 277 GLU n 
1 278 ASP n 
1 279 ASP n 
1 280 ASP n 
1 281 ILE n 
1 282 TRP n 
1 283 LEU n 
1 284 GLN n 
1 285 MET n 
1 286 ARG n 
1 287 HIS n 
1 288 LEU n 
1 289 HIS n 
1 290 ILE n 
1 291 SER n 
1 292 GLU n 
1 293 VAL n 
1 294 PHE n 
1 295 ARG n 
1 296 LYS n 
1 297 VAL n 
1 298 LYS n 
1 299 SER n 
1 300 SER n 
1 301 PHE n 
1 302 ASP n 
1 303 GLU n 
1 304 PHE n 
1 305 CYS n 
1 306 VAL n 
1 307 SER n 
1 308 ALA n 
1 309 ARG n 
1 310 ARG n 
1 311 LEU n 
1 312 GLN n 
1 313 GLY n 
1 314 LEU n 
1 315 ARG n 
1 316 ASP n 
1 317 SER n 
1 318 GLN n 
1 319 GLN n 
1 320 GLY n 
1 321 GLU n 
1 322 GLY n 
1 323 GLY n 
1 324 ALA n 
1 325 GLY n 
1 326 ALA n 
1 327 LEU n 
1 328 LYS n 
1 329 GLN n 
1 330 MET n 
1 331 LEU n 
1 332 LYS n 
1 333 ASP n 
1 334 LEU n 
1 335 PRO n 
1 336 GLN n 
1 337 HIS n 
1 338 ARG n 
1 339 GLU n 
1 340 GLN n 
1 341 MET n 
1 342 GLN n 
1 343 LYS n 
1 344 TYR n 
1 345 SER n 
1 346 LEU n 
1 347 HIS n 
1 348 LEU n 
1 349 ASP n 
1 350 MET n 
1 351 SER n 
1 352 ASN n 
1 353 ALA n 
1 354 ILE n 
1 355 ASN n 
1 356 MET n 
1 357 ALA n 
1 358 PHE n 
1 359 SER n 
1 360 SER n 
1 361 THR n 
1 362 ILE n 
1 363 ASP n 
1 364 SER n 
1 365 CYS n 
1 366 THR n 
1 367 LYS n 
1 368 ALA n 
1 369 GLU n 
1 370 GLN n 
1 371 ASN n 
1 372 ILE n 
1 373 VAL n 
1 374 THR n 
1 375 GLU n 
1 376 GLU n 
1 377 GLU n 
1 378 GLN n 
1 379 ASP n 
1 380 GLY n 
1 381 ASN n 
1 382 LYS n 
1 383 VAL n 
1 384 ARG n 
1 385 ASP n 
1 386 PHE n 
1 387 ILE n 
1 388 GLY n 
1 389 GLU n 
1 390 VAL n 
1 391 ALA n 
1 392 SER n 
1 393 VAL n 
1 394 VAL n 
1 395 VAL n 
1 396 ASP n 
1 397 ARG n 
1 398 ARG n 
1 399 VAL n 
1 400 SER n 
1 401 THR n 
1 402 GLU n 
1 403 ASP n 
1 404 LYS n 
1 405 LEU n 
1 406 ARG n 
1 407 CYS n 
1 408 LEU n 
1 409 MET n 
1 410 LEU n 
1 411 CYS n 
1 412 VAL n 
1 413 LEU n 
1 414 ALA n 
1 415 LYS n 
1 416 ASN n 
1 417 GLY n 
1 418 THR n 
1 419 SER n 
1 420 SER n 
1 421 HIS n 
1 422 GLU n 
1 423 LEU n 
1 424 ASN n 
1 425 ASN n 
1 426 LEU n 
1 427 LEU n 
1 428 ASP n 
1 429 ASN n 
1 430 ALA n 
1 431 ASN n 
1 432 ILE n 
1 433 ALA n 
1 434 THR n 
1 435 PRO n 
1 436 SER n 
1 437 ARG n 
1 438 SER n 
1 439 ALA n 
1 440 ILE n 
1 441 TYR n 
1 442 ASN n 
1 443 LEU n 
1 444 GLU n 
1 445 MET n 
1 446 LEU n 
1 447 GLY n 
1 448 ALA n 
1 449 THR n 
1 450 VAL n 
1 451 VAL n 
1 452 ALA n 
1 453 ASP n 
1 454 ARG n 
1 455 ARG n 
1 456 GLY n 
1 457 ARG n 
1 458 LYS n 
1 459 PRO n 
1 460 LYS n 
1 461 THR n 
1 462 MET n 
1 463 LYS n 
1 464 ARG n 
1 465 ILE n 
1 466 GLU n 
1 467 ARG n 
1 468 ASP n 
1 469 MET n 
1 470 PRO n 
1 471 TYR n 
1 472 VAL n 
1 473 LEU n 
1 474 SER n 
1 475 ARG n 
1 476 TRP n 
1 477 THR n 
1 478 PRO n 
1 479 ILE n 
1 480 VAL n 
1 481 LYS n 
1 482 ASP n 
1 483 LEU n 
1 484 MET n 
1 485 GLU n 
1 486 TYR n 
1 487 ILE n 
1 488 ALA n 
1 489 THR n 
1 490 GLY n 
1 491 GLN n 
1 492 LEU n 
1 493 ASP n 
1 494 LEU n 
1 495 GLU n 
1 496 SER n 
1 497 TYR n 
1 498 PRO n 
1 499 ALA n 
1 500 VAL n 
1 501 ARG n 
1 502 ASP n 
1 503 GLY n 
1 504 PRO n 
1 505 SER n 
1 506 VAL n 
1 507 VAL n 
1 508 GLN n 
1 509 PRO n 
1 510 LYS n 
1 511 ARG n 
1 512 ALA n 
1 513 SER n 
1 514 LYS n 
1 515 SER n 
1 516 VAL n 
1 517 GLU n 
1 518 GLU n 
1 519 ASP n 
1 520 ASP n 
1 521 ASP n 
1 522 GLY n 
1 523 PRO n 
1 524 ALA n 
1 525 THR n 
1 526 SER n 
1 527 ALA n 
1 528 ARG n 
1 529 LYS n 
1 530 ARG n 
1 531 GLY n 
1 532 ASN n 
1 533 TRP n 
1 534 ALA n 
1 535 LYS n 
1 536 ASN n 
1 537 LYS n 
1 538 GLY n 
1 539 ASN n 
1 540 ASN n 
1 541 ARG n 
1 542 SER n 
1 543 LEU n 
1 544 PRO n 
1 545 SER n 
1 546 THR n 
1 547 PRO n 
1 548 SER n 
1 549 GLY n 
1 550 VAL n 
1 551 ALA n 
1 552 VAL n 
1 553 SER n 
1 554 GLY n 
1 555 ASN n 
1 556 GLY n 
1 557 ALA n 
1 558 ALA n 
1 559 GLY n 
1 560 ALA n 
1 561 ALA n 
1 562 GLU n 
1 563 SER n 
1 564 ALA n 
1 565 LYS n 
1 566 PRO n 
1 567 LYS n 
1 568 LEU n 
1 569 PHE n 
1 570 VAL n 
1 571 PHE n 
1 572 ILE n 
1 573 ASN n 
1 574 GLY n 
1 575 THR n 
1 576 VAL n 
1 577 SER n 
1 578 TYR n 
1 579 ASN n 
1 580 GLU n 
1 581 ILE n 
1 582 ARG n 
1 583 CYS n 
1 584 ALA n 
1 585 TYR n 
1 586 GLU n 
1 587 VAL n 
1 588 SER n 
1 589 GLN n 
1 590 SER n 
1 591 SER n 
1 592 GLY n 
1 593 TYR n 
1 594 GLU n 
1 595 VAL n 
1 596 TYR n 
1 597 ILE n 
1 598 GLY n 
1 599 ALA n 
1 600 HIS n 
1 601 ASN n 
1 602 ILE n 
1 603 ALA n 
1 604 THR n 
1 605 PRO n 
1 606 ALA n 
1 607 GLU n 
1 608 PHE n 
1 609 VAL n 
1 610 GLU n 
1 611 LEU n 
1 612 VAL n 
1 613 SER n 
1 614 LEU n 
1 615 LEU n 
1 616 ASP n 
1 617 LYS n 
1 618 ALA n 
1 619 ASP n 
1 620 GLN n 
1 621 ASP n 
1 622 VAL n 
1 623 GLN n 
1 624 VAL n 
1 625 LEU n 
1 626 THR n 
1 627 GLN n 
1 628 GLY n 
1 629 GLN n 
1 630 GLY n 
1 631 ASP n 
1 632 GLY n 
1 633 GLY n 
1 634 LEU n 
1 635 VAL n 
1 636 ILE n 
1 637 THR n 
1 638 THR n 
1 639 GLY n 
1 640 SER n 
1 641 ALA n 
1 642 GLN n 
1 643 ALA n 
1 644 GLY n 
1 645 LEU n 
1 646 ASN n 
1 647 LEU n 
1 648 ALA n 
1 649 GLU n 
1 650 VAL n 
2 1   MET n 
2 2   ASP n 
2 3   ARG n 
2 4   LEU n 
2 5   SER n 
2 6   ARG n 
2 7   LEU n 
2 8   ARG n 
2 9   GLN n 
2 10  MET n 
2 11  ALA n 
2 12  ALA n 
2 13  GLU n 
2 14  ASN n 
2 15  GLN n 
2 16  PRO n 
2 17  ALA n 
2 18  GLU n 
2 19  ALA n 
2 20  SER n 
2 21  ASP n 
2 22  ALA n 
2 23  ALA n 
2 24  GLY n 
2 25  GLY n 
2 26  ALA n 
2 27  GLU n 
2 28  ALA n 
2 29  GLN n 
2 30  ILE n 
2 31  GLU n 
2 32  GLU n 
2 33  THR n 
2 34  SER n 
2 35  LEU n 
2 36  SER n 
2 37  ALA n 
2 38  GLN n 
2 39  PRO n 
2 40  GLU n 
2 41  PRO n 
2 42  PHE n 
2 43  MET n 
2 44  ALA n 
2 45  ASP n 
2 46  PHE n 
2 47  PHE n 
2 48  ASN n 
2 49  ARG n 
2 50  VAL n 
2 51  LYS n 
2 52  ARG n 
2 53  ILE n 
2 54  ARG n 
2 55  ASP n 
2 56  ASN n 
2 57  ILE n 
2 58  GLU n 
2 59  ASP n 
2 60  ILE n 
2 61  GLU n 
2 62  GLN n 
2 63  ALA n 
2 64  ILE n 
2 65  GLU n 
2 66  GLN n 
2 67  VAL n 
2 68  ALA n 
2 69  GLN n 
2 70  LEU n 
2 71  HIS n 
2 72  THR n 
2 73  GLU n 
2 74  SER n 
2 75  LEU n 
2 76  VAL n 
2 77  ALA n 
2 78  VAL n 
2 79  SER n 
2 80  LYS n 
2 81  GLU n 
2 82  ASP n 
2 83  ARG n 
2 84  ASP n 
2 85  ARG n 
2 86  LEU n 
2 87  ASN n 
2 88  GLU n 
2 89  LYS n 
2 90  LEU n 
2 91  GLN n 
2 92  ASP n 
2 93  THR n 
2 94  MET n 
2 95  ALA n 
2 96  ARG n 
2 97  ILE n 
2 98  SER n 
2 99  ALA n 
2 100 LEU n 
2 101 GLY n 
2 102 ASN n 
2 103 LYS n 
2 104 ILE n 
2 105 ARG n 
2 106 ALA n 
2 107 ASP n 
2 108 LEU n 
2 109 LYS n 
2 110 GLN n 
2 111 ILE n 
2 112 GLU n 
2 113 LYS n 
2 114 GLU n 
2 115 ASN n 
2 116 LYS n 
2 117 ARG n 
2 118 ALA n 
2 119 GLN n 
2 120 GLN n 
2 121 GLU n 
2 122 GLY n 
2 123 THR n 
2 124 PHE n 
2 125 GLU n 
2 126 ASP n 
2 127 GLY n 
2 128 THR n 
2 129 VAL n 
2 130 SER n 
2 131 THR n 
2 132 ASP n 
2 133 LEU n 
2 134 ARG n 
2 135 ILE n 
2 136 ARG n 
2 137 GLN n 
2 138 SER n 
2 139 GLN n 
2 140 HIS n 
2 141 SER n 
2 142 SER n 
2 143 LEU n 
2 144 SER n 
2 145 ARG n 
2 146 LYS n 
2 147 PHE n 
2 148 VAL n 
2 149 LYS n 
2 150 VAL n 
2 151 MET n 
2 152 THR n 
2 153 ARG n 
2 154 TYR n 
2 155 ASN n 
2 156 ASP n 
2 157 VAL n 
2 158 GLN n 
2 159 ALA n 
2 160 GLU n 
2 161 ASN n 
2 162 LYS n 
2 163 ARG n 
2 164 ARG n 
2 165 TYR n 
2 166 GLY n 
2 167 GLU n 
2 168 ASN n 
2 169 VAL n 
2 170 ALA n 
2 171 ARG n 
2 172 GLN n 
2 173 CYS n 
2 174 ARG n 
2 175 VAL n 
2 176 VAL n 
2 177 GLU n 
2 178 PRO n 
2 179 SER n 
2 180 LEU n 
2 181 SER n 
2 182 ASP n 
2 183 ASP n 
2 184 ALA n 
2 185 ILE n 
2 186 GLN n 
2 187 LYS n 
2 188 VAL n 
2 189 ILE n 
2 190 GLU n 
2 191 HIS n 
2 192 GLY n 
2 193 THR n 
2 194 GLU n 
2 195 GLY n 
2 196 ILE n 
2 197 PHE n 
2 198 SER n 
2 199 GLY n 
2 200 MET n 
2 201 ARG n 
2 202 LEU n 
2 203 GLU n 
2 204 GLY n 
2 205 ALA n 
2 206 GLU n 
2 207 ALA n 
2 208 LYS n 
2 209 LEU n 
2 210 ASN n 
2 211 GLU n 
2 212 ILE n 
2 213 ARG n 
2 214 ASP n 
2 215 ARG n 
2 216 HIS n 
2 217 LYS n 
2 218 ASP n 
2 219 ILE n 
2 220 GLN n 
2 221 GLN n 
2 222 LEU n 
2 223 GLU n 
2 224 ARG n 
2 225 SER n 
2 226 LEU n 
2 227 LEU n 
2 228 GLU n 
2 229 LEU n 
2 230 HIS n 
2 231 GLU n 
2 232 MET n 
2 233 PHE n 
2 234 THR n 
2 235 ASP n 
2 236 MET n 
2 237 SER n 
2 238 THR n 
2 239 LEU n 
2 240 VAL n 
2 241 ALA n 
2 242 SER n 
2 243 GLN n 
2 244 GLY n 
2 245 GLU n 
2 246 MET n 
2 247 ILE n 
2 248 ASP n 
2 249 ARG n 
2 250 ILE n 
2 251 GLU n 
2 252 PHE n 
2 253 SER n 
2 254 VAL n 
2 255 GLU n 
2 256 GLN n 
2 257 SER n 
2 258 HIS n 
2 259 ASN n 
2 260 TYR n 
2 261 VAL n 
2 262 LYS n 
2 263 LYS n 
2 264 ALA n 
2 265 THR n 
2 266 GLU n 
2 267 GLN n 
2 268 VAL n 
2 269 VAL n 
2 270 GLN n 
2 271 ALA n 
2 272 ARG n 
2 273 HIS n 
2 274 TYR n 
2 275 GLN n 
2 276 GLU n 
2 277 SER n 
2 278 ALA n 
2 279 ARG 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 ? ? ? ? ? ? ? ? ? ? ? ? 'MONOSIGA BREVICOLLIS' 81824 ? ? ? ? ? ? ? ? 'ESCHERICHIA COLI' 469008 ? ? ? ? ? ? 'BL21(DE3)' 
? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample ? ? ? ? ? ? ? ? ? ? ? ? 'MONOSIGA BREVICOLLIS' 81824 ? ? ? ? ? ? ? ? 'ESCHERICHIA COLI' 469008 ? ? ? ? ? ? 'BL21(DE3)' 
? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
1 UNP A9V0L3_MONBE 1 ? ? A9V0L3 ? 
2 UNP A9UTG5_MONBE 2 ? ? A9UTG5 ? 
# 
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 2XHE A 2 ? 650 ? A9V0L3 1 ? 649 ? 1 649 
2 2 2XHE B 1 ? 279 ? A9UTG5 1 ? 279 ? 1 279 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             2XHE 
_struct_ref_seq_dif.mon_id                       HIS 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      1 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   A9V0L3 
_struct_ref_seq_dif.db_mon_id                    ? 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          ? 
_struct_ref_seq_dif.details                      'expression tag' 
_struct_ref_seq_dif.pdbx_auth_seq_num            0 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
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 
# 
_exptl.entry_id          2XHE 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.19 
_exptl_crystal.density_percent_sol   66.9 
_exptl_crystal.description           NONE 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '7.5% PEG-6000, 0.1 M TRIS-HCL PH 7.0, 4.25% MPD, 15% GLYCEROL' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   ? 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0385 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SLS BEAMLINE X10SA' 
_diffrn_source.pdbx_synchrotron_site       SLS 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_wavelength             1.0385 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     2XHE 
_reflns.observed_criterion_sigma_I   2.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             30.00 
_reflns.d_resolution_high            2.80 
_reflns.number_obs                   34089 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.10 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        19.80 
_reflns.B_iso_Wilson_estimate        75.23 
_reflns.pdbx_redundancy              14.7 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             2.80 
_reflns_shell.d_res_low              2.90 
_reflns_shell.percent_possible_all   100.0 
_reflns_shell.Rmerge_I_obs           0.75 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.10 
_reflns_shell.pdbx_redundancy        14.3 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 2XHE 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     34041 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          2.01 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             34.60 
_refine.ls_d_res_high                            2.80 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_R_factor_obs                          0.1910 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1879 
_refine.ls_R_factor_R_free                       0.2503 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1726 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            -9.8979 
_refine.aniso_B[2][2]                            -9.8979 
_refine.aniso_B[3][3]                            19.7957 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.286 
_refine.solvent_model_param_bsol                 57.777 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 3C98' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.39 
_refine.pdbx_overall_phase_error                 23.48 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6267 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             48 
_refine_hist.number_atoms_total               6315 
_refine_hist.d_res_high                       2.80 
_refine_hist.d_res_low                        34.60 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.007  ? ? 6358 'X-RAY DIFFRACTION' ? 
f_angle_d          1.069  ? ? 8570 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 18.073 ? ? 2421 'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.075  ? ? 971  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.004  ? ? 1120 'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' . 2.8000 2.8824  2641 0.2785 100.00 0.3098 . . 141 . . 
'X-RAY DIFFRACTION' . 2.8824 2.9754  2617 0.2322 100.00 0.3303 . . 156 . . 
'X-RAY DIFFRACTION' . 2.9754 3.0817  2634 0.2156 100.00 0.2815 . . 132 . . 
'X-RAY DIFFRACTION' . 3.0817 3.2050  2656 0.2091 100.00 0.2629 . . 152 . . 
'X-RAY DIFFRACTION' . 3.2050 3.3507  2645 0.2022 100.00 0.2900 . . 140 . . 
'X-RAY DIFFRACTION' . 3.3507 3.5272  2656 0.2041 100.00 0.2960 . . 146 . . 
'X-RAY DIFFRACTION' . 3.5272 3.7479  2664 0.1868 100.00 0.2399 . . 151 . . 
'X-RAY DIFFRACTION' . 3.7479 4.0369  2671 0.1787 100.00 0.2556 . . 146 . . 
'X-RAY DIFFRACTION' . 4.0369 4.4424  2716 0.1552 100.00 0.2130 . . 126 . . 
'X-RAY DIFFRACTION' . 4.4424 5.0835  2721 0.1519 100.00 0.2238 . . 144 . . 
'X-RAY DIFFRACTION' . 5.0835 6.3981  2760 0.1855 100.00 0.2399 . . 145 . . 
'X-RAY DIFFRACTION' . 6.3981 34.6048 2934 0.1773 100.00 0.2280 . . 147 . . 
# 
_struct.entry_id                  2XHE 
_struct.title                     'Crystal structure of the Unc18-syntaxin 1 complex from Monosiga brevicollis' 
_struct.pdbx_descriptor           'UNC18, SYNTAXIN1' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2XHE 
_struct_keywords.pdbx_keywords   EXOCYTOSIS 
_struct_keywords.text            'EXOCYTOSIS, EXOCYTOSIS COMPLEX, SNARE, NEURO FUSION, SM PROTEIN, CHOANOFLAGELLATES' 
# 
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 3 ? 
# 
_struct_biol.id   1 
# 
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  1  SER A 3   ? ARG A 17  ? SER A 2   ARG A 16  1 ? 15 
HELX_P HELX_P2  2  ASP A 31  ? GLU A 40  ? ASP A 30  GLU A 39  1 ? 10 
HELX_P HELX_P3  3  ARG A 43  ? ASP A 49  ? ARG A 42  ASP A 48  1 ? 7  
HELX_P HELX_P4  4  THR A 77  ? ASP A 90  ? THR A 76  ASP A 89  1 ? 14 
HELX_P HELX_P5  5  PRO A 107 ? ALA A 117 ? PRO A 106 ALA A 116 1 ? 11 
HELX_P HELX_P6  6  LYS A 118 ? LYS A 121 ? LYS A 117 LYS A 120 5 ? 4  
HELX_P HELX_P7  7  HIS A 147 ? GLY A 154 ? HIS A 146 GLY A 153 1 ? 8  
HELX_P HELX_P8  8  ARG A 156 ? TYR A 160 ? ARG A 155 TYR A 159 5 ? 5  
HELX_P HELX_P9  9  ASN A 161 ? ASN A 177 ? ASN A 160 ASN A 176 1 ? 17 
HELX_P HELX_P10 10 THR A 189 ? SER A 208 ? THR A 188 SER A 207 1 ? 20 
HELX_P HELX_P11 11 ASP A 227 ? ASP A 231 ? ASP A 226 ASP A 230 5 ? 5  
HELX_P HELX_P12 12 THR A 241 ? LEU A 250 ? THR A 240 LEU A 249 1 ? 10 
HELX_P HELX_P13 13 ILE A 281 ? ARG A 286 ? ILE A 280 ARG A 285 1 ? 6  
HELX_P HELX_P14 14 HIS A 289 ? LEU A 311 ? HIS A 288 LEU A 310 1 ? 23 
HELX_P HELX_P15 15 GLY A 323 ? LEU A 334 ? GLY A 322 LEU A 333 1 ? 12 
HELX_P HELX_P16 16 HIS A 337 ? PHE A 358 ? HIS A 336 PHE A 357 1 ? 22 
HELX_P HELX_P17 17 SER A 359 ? GLU A 375 ? SER A 358 GLU A 374 1 ? 17 
HELX_P HELX_P18 18 ASP A 385 ? ASP A 396 ? ASP A 384 ASP A 395 1 ? 12 
HELX_P HELX_P19 19 SER A 400 ? ASN A 416 ? SER A 399 ASN A 415 1 ? 17 
HELX_P HELX_P20 20 SER A 419 ? ALA A 430 ? SER A 418 ALA A 429 1 ? 12 
HELX_P HELX_P21 21 ALA A 433 ? SER A 436 ? ALA A 432 SER A 435 5 ? 4  
HELX_P HELX_P22 22 ARG A 437 ? ASN A 442 ? ARG A 436 ASN A 441 1 ? 6  
HELX_P HELX_P23 23 LEU A 443 ? GLY A 447 ? LEU A 442 GLY A 446 5 ? 5  
HELX_P HELX_P24 24 ALA A 452 ? ARG A 455 ? ALA A 451 ARG A 454 5 ? 4  
HELX_P HELX_P25 25 PRO A 478 ? ALA A 488 ? PRO A 477 ALA A 487 1 ? 11 
HELX_P HELX_P26 26 ASP A 502 ? VAL A 506 ? ASP A 501 VAL A 505 5 ? 5  
HELX_P HELX_P27 27 SER A 577 ? GLN A 589 ? SER A 576 GLN A 588 1 ? 13 
HELX_P HELX_P28 28 THR A 604 ? LEU A 614 ? THR A 603 LEU A 613 1 ? 11 
HELX_P HELX_P29 29 LEU B 4   ? MET B 10  ? LEU B 4   MET B 10  1 ? 7  
HELX_P HELX_P30 30 MET B 43  ? GLU B 73  ? MET B 43  GLU B 73  1 ? 31 
HELX_P HELX_P31 31 SER B 79  ? ARG B 117 ? SER B 79  ARG B 117 1 ? 39 
HELX_P HELX_P32 32 ALA B 118 ? THR B 123 ? ALA B 118 THR B 123 1 ? 6  
HELX_P HELX_P33 33 SER B 130 ? ASN B 168 ? SER B 130 ASN B 168 1 ? 39 
HELX_P HELX_P34 34 ALA B 184 ? GLY B 192 ? ALA B 184 GLY B 192 1 ? 9  
HELX_P HELX_P35 35 ARG B 213 ? THR B 238 ? ARG B 213 THR B 238 1 ? 26 
HELX_P HELX_P36 36 ARG B 249 ? GLN B 256 ? ARG B 249 GLN B 256 1 ? 8  
# 
_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 
AA ? 5 ? 
AB ? 6 ? 
AC ? 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 
AA 1 2 ? parallel      
AA 2 3 ? parallel      
AA 3 4 ? parallel      
AA 4 5 ? parallel      
AB 1 2 ? anti-parallel 
AB 2 3 ? parallel      
AB 3 4 ? parallel      
AB 4 5 ? parallel      
AB 5 6 ? parallel      
AC 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 
AA 1 VAL A 52  ? ASP A 57  ? VAL A 51  ASP A 56  
AA 2 LYS A 26  ? VAL A 30  ? LYS A 25  VAL A 29  
AA 3 HIS A 69  ? ILE A 74  ? HIS A 68  ILE A 73  
AA 4 ALA A 98  ? PHE A 102 ? ALA A 97  PHE A 101 
AA 5 VAL A 123 ? GLU A 128 ? VAL A 122 GLU A 127 
AB 1 ILE A 134 ? GLU A 137 ? ILE A 133 GLU A 136 
AB 2 VAL A 140 ? THR A 142 ? VAL A 139 THR A 141 
AB 3 GLU A 594 ? ILE A 602 ? GLU A 593 ILE A 601 
AB 4 LYS A 567 ? VAL A 576 ? LYS A 566 VAL A 575 
AB 5 GLN A 222 ? LEU A 226 ? GLN A 221 LEU A 225 
AB 6 ILE A 181 ? TYR A 184 ? ILE A 180 TYR A 183 
AC 1 ILE A 256 ? THR A 261 ? ILE A 255 THR A 260 
AC 2 GLN A 269 ? VAL A 274 ? GLN A 268 VAL A 273 
# 
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 
AA 1 2 N THR A 53  ? N THR A 52  O LYS A 26  ? O LYS A 25  
AA 2 3 N VAL A 27  ? N VAL A 26  O HIS A 69  ? O HIS A 68  
AA 3 4 N TYR A 72  ? N TYR A 71  O HIS A 99  ? O HIS A 98  
AA 4 5 O ALA A 98  ? O ALA A 97  N LYS A 124 ? N LYS A 123 
AB 1 2 N GLU A 137 ? N GLU A 136 O VAL A 140 ? O VAL A 139 
AB 2 3 N PHE A 141 ? N PHE A 140 O ILE A 597 ? O ILE A 596 
AB 3 4 N TYR A 596 ? N TYR A 595 O LEU A 568 ? O LEU A 567 
AB 4 5 N PHE A 569 ? N PHE A 568 O GLN A 222 ? O GLN A 221 
AB 5 6 N PHE A 223 ? N PHE A 222 O ILE A 181 ? O ILE A 180 
AC 1 2 N THR A 261 ? N THR A 260 O GLN A 269 ? O GLN A 268 
# 
_database_PDB_matrix.entry_id          2XHE 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    2XHE 
_atom_sites.fract_transf_matrix[1][1]   0.006840 
_atom_sites.fract_transf_matrix[1][2]   0.003949 
_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]   0.007898 
_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]   0.004654 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . HIS A 1 1   ? -16.300 -47.169 4.756   1.00 117.90 ? 0    HIS A N   1 
ATOM   2    C CA  . HIS A 1 1   ? -15.918 -48.056 5.850   1.00 125.00 ? 0    HIS A CA  1 
ATOM   3    C C   . HIS A 1 1   ? -15.663 -47.320 7.163   1.00 126.48 ? 0    HIS A C   1 
ATOM   4    O O   . HIS A 1 1   ? -15.469 -47.960 8.206   1.00 135.51 ? 0    HIS A O   1 
ATOM   5    C CB  . HIS A 1 1   ? -14.655 -48.833 5.491   1.00 126.53 ? 0    HIS A CB  1 
ATOM   6    C CG  . HIS A 1 1   ? -14.912 -50.106 4.754   1.00 125.06 ? 0    HIS A CG  1 
ATOM   7    N ND1 . HIS A 1 1   ? -15.119 -50.145 3.391   1.00 124.34 ? 0    HIS A ND1 1 
ATOM   8    C CD2 . HIS A 1 1   ? -14.970 -51.389 5.184   1.00 119.66 ? 0    HIS A CD2 1 
ATOM   9    C CE1 . HIS A 1 1   ? -15.304 -51.397 3.016   1.00 132.41 ? 0    HIS A CE1 1 
ATOM   10   N NE2 . HIS A 1 1   ? -15.217 -52.172 4.084   1.00 129.31 ? 0    HIS A NE2 1 
ATOM   11   N N   . MET A 1 2   ? -15.648 -45.987 7.111   1.00 108.83 ? 1    MET A N   1 
ATOM   12   C CA  . MET A 1 2   ? -15.275 -45.157 8.269   1.00 105.53 ? 1    MET A CA  1 
ATOM   13   C C   . MET A 1 2   ? -13.754 -45.078 8.543   1.00 85.70  ? 1    MET A C   1 
ATOM   14   O O   . MET A 1 2   ? -13.163 -44.023 8.392   1.00 82.98  ? 1    MET A O   1 
ATOM   15   C CB  . MET A 1 2   ? -16.040 -45.568 9.537   1.00 111.11 ? 1    MET A CB  1 
ATOM   16   C CG  . MET A 1 2   ? -17.473 -45.059 9.605   1.00 113.70 ? 1    MET A CG  1 
ATOM   17   S SD  . MET A 1 2   ? -17.609 -43.265 9.752   1.00 185.26 ? 1    MET A SD  1 
ATOM   18   C CE  . MET A 1 2   ? -16.627 -42.963 11.226  1.00 122.90 ? 1    MET A CE  1 
ATOM   19   N N   . SER A 1 3   ? -13.135 -46.184 8.951   1.00 78.26  ? 2    SER A N   1 
ATOM   20   C CA  . SER A 1 3   ? -11.694 -46.221 9.180   1.00 78.03  ? 2    SER A CA  1 
ATOM   21   C C   . SER A 1 3   ? -10.945 -47.019 8.116   1.00 84.88  ? 2    SER A C   1 
ATOM   22   O O   . SER A 1 3   ? -11.369 -48.120 7.732   1.00 82.94  ? 2    SER A O   1 
ATOM   23   C CB  . SER A 1 3   ? -11.372 -46.802 10.552  1.00 77.59  ? 2    SER A CB  1 
ATOM   24   O OG  . SER A 1 3   ? -10.155 -47.525 10.501  1.00 75.12  ? 2    SER A OG  1 
ATOM   25   N N   . LEU A 1 4   ? -9.825  -46.455 7.663   1.00 78.71  ? 3    LEU A N   1 
ATOM   26   C CA  . LEU A 1 4   ? -8.994  -47.046 6.624   1.00 75.28  ? 3    LEU A CA  1 
ATOM   27   C C   . LEU A 1 4   ? -8.347  -48.307 7.146   1.00 78.04  ? 3    LEU A C   1 
ATOM   28   O O   . LEU A 1 4   ? -8.060  -49.223 6.384   1.00 84.43  ? 3    LEU A O   1 
ATOM   29   C CB  . LEU A 1 4   ? -7.909  -46.065 6.194   1.00 83.47  ? 3    LEU A CB  1 
ATOM   30   C CG  . LEU A 1 4   ? -8.355  -44.676 5.745   1.00 78.09  ? 3    LEU A CG  1 
ATOM   31   C CD1 . LEU A 1 4   ? -7.205  -43.727 5.855   1.00 71.15  ? 3    LEU A CD1 1 
ATOM   32   C CD2 . LEU A 1 4   ? -8.887  -44.718 4.329   1.00 81.56  ? 3    LEU A CD2 1 
ATOM   33   N N   . LYS A 1 5   ? -8.112  -48.352 8.451   1.00 79.18  ? 4    LYS A N   1 
ATOM   34   C CA  . LYS A 1 5   ? -7.608  -49.572 9.067   1.00 73.06  ? 4    LYS A CA  1 
ATOM   35   C C   . LYS A 1 5   ? -8.684  -50.666 9.050   1.00 79.23  ? 4    LYS A C   1 
ATOM   36   O O   . LYS A 1 5   ? -8.386  -51.823 8.760   1.00 84.56  ? 4    LYS A O   1 
ATOM   37   C CB  . LYS A 1 5   ? -7.098  -49.313 10.484  1.00 57.28  ? 4    LYS A CB  1 
ATOM   38   C CG  . LYS A 1 5   ? -5.647  -48.835 10.567  1.00 63.60  ? 4    LYS A CG  1 
ATOM   39   C CD  . LYS A 1 5   ? -5.369  -48.361 11.990  1.00 71.81  ? 4    LYS A CD  1 
ATOM   40   C CE  . LYS A 1 5   ? -4.139  -47.499 12.096  1.00 70.58  ? 4    LYS A CE  1 
ATOM   41   N NZ  . LYS A 1 5   ? -2.930  -48.330 12.254  1.00 77.44  ? 4    LYS A NZ  1 
ATOM   42   N N   . SER A 1 6   ? -9.931  -50.297 9.340   1.00 77.56  ? 5    SER A N   1 
ATOM   43   C CA  . SER A 1 6   ? -11.047 -51.240 9.237   1.00 79.77  ? 5    SER A CA  1 
ATOM   44   C C   . SER A 1 6   ? -11.163 -51.723 7.801   1.00 87.33  ? 5    SER A C   1 
ATOM   45   O O   . SER A 1 6   ? -11.317 -52.916 7.544   1.00 91.50  ? 5    SER A O   1 
ATOM   46   C CB  . SER A 1 6   ? -12.370 -50.592 9.642   1.00 75.50  ? 5    SER A CB  1 
ATOM   47   O OG  . SER A 1 6   ? -12.315 -50.046 10.939  1.00 86.03  ? 5    SER A OG  1 
ATOM   48   N N   . ALA A 1 7   ? -11.084 -50.781 6.868   1.00 82.57  ? 6    ALA A N   1 
ATOM   49   C CA  . ALA A 1 7   ? -11.251 -51.097 5.463   1.00 82.56  ? 6    ALA A CA  1 
ATOM   50   C C   . ALA A 1 7   ? -10.197 -52.094 4.992   1.00 88.60  ? 6    ALA A C   1 
ATOM   51   O O   . ALA A 1 7   ? -10.522 -53.095 4.364   1.00 90.21  ? 6    ALA A O   1 
ATOM   52   C CB  . ALA A 1 7   ? -11.213 -49.838 4.630   1.00 74.65  ? 6    ALA A CB  1 
ATOM   53   N N   . VAL A 1 8   ? -8.936  -51.823 5.300   1.00 82.39  ? 7    VAL A N   1 
ATOM   54   C CA  . VAL A 1 8   ? -7.858  -52.717 4.893   1.00 79.25  ? 7    VAL A CA  1 
ATOM   55   C C   . VAL A 1 8   ? -7.950  -54.084 5.598   1.00 84.52  ? 7    VAL A C   1 
ATOM   56   O O   . VAL A 1 8   ? -7.699  -55.115 4.975   1.00 80.19  ? 7    VAL A O   1 
ATOM   57   C CB  . VAL A 1 8   ? -6.461  -52.033 5.057   1.00 63.52  ? 7    VAL A CB  1 
ATOM   58   C CG1 . VAL A 1 8   ? -5.325  -53.023 4.914   1.00 53.30  ? 7    VAL A CG1 1 
ATOM   59   C CG2 . VAL A 1 8   ? -6.303  -50.930 4.024   1.00 68.77  ? 7    VAL A CG2 1 
ATOM   60   N N   . LYS A 1 9   ? -8.333  -54.098 6.877   1.00 77.24  ? 8    LYS A N   1 
ATOM   61   C CA  . LYS A 1 9   ? -8.445  -55.364 7.598   1.00 82.07  ? 8    LYS A CA  1 
ATOM   62   C C   . LYS A 1 9   ? -9.555  -56.217 6.985   1.00 95.45  ? 8    LYS A C   1 
ATOM   63   O O   . LYS A 1 9   ? -9.464  -57.450 6.953   1.00 93.57  ? 8    LYS A O   1 
ATOM   64   C CB  . LYS A 1 9   ? -8.706  -55.162 9.099   1.00 74.70  ? 8    LYS A CB  1 
ATOM   65   C CG  . LYS A 1 9   ? -8.470  -56.429 9.945   1.00 73.18  ? 8    LYS A CG  1 
ATOM   66   C CD  . LYS A 1 9   ? -9.124  -56.344 11.324  1.00 88.61  ? 8    LYS A CD  1 
ATOM   67   C CE  . LYS A 1 9   ? -8.699  -55.068 12.059  1.00 104.45 ? 8    LYS A CE  1 
ATOM   68   N NZ  . LYS A 1 9   ? -9.251  -54.931 13.445  1.00 100.93 ? 8    LYS A NZ  1 
ATOM   69   N N   . THR A 1 10  ? -10.597 -55.548 6.497   1.00 92.71  ? 9    THR A N   1 
ATOM   70   C CA  . THR A 1 10  ? -11.732 -56.234 5.893   1.00 91.06  ? 9    THR A CA  1 
ATOM   71   C C   . THR A 1 10  ? -11.350 -56.994 4.613   1.00 81.19  ? 9    THR A C   1 
ATOM   72   O O   . THR A 1 10  ? -11.789 -58.120 4.408   1.00 78.81  ? 9    THR A O   1 
ATOM   73   C CB  . THR A 1 10  ? -12.890 -55.267 5.622   1.00 88.86  ? 9    THR A CB  1 
ATOM   74   O OG1 . THR A 1 10  ? -13.309 -54.665 6.854   1.00 88.58  ? 9    THR A OG1 1 
ATOM   75   C CG2 . THR A 1 10  ? -14.055 -56.012 5.011   1.00 88.04  ? 9    THR A CG2 1 
ATOM   76   N N   . VAL A 1 11  ? -10.522 -56.381 3.773   1.00 73.78  ? 10   VAL A N   1 
ATOM   77   C CA  . VAL A 1 11  ? -10.005 -57.019 2.565   1.00 81.83  ? 10   VAL A CA  1 
ATOM   78   C C   . VAL A 1 11  ? -9.143  -58.231 2.897   1.00 91.75  ? 10   VAL A C   1 
ATOM   79   O O   . VAL A 1 11  ? -9.153  -59.239 2.180   1.00 93.78  ? 10   VAL A O   1 
ATOM   80   C CB  . VAL A 1 11  ? -9.117  -56.059 1.761   1.00 80.45  ? 10   VAL A CB  1 
ATOM   81   C CG1 . VAL A 1 11  ? -8.575  -56.763 0.535   1.00 76.11  ? 10   VAL A CG1 1 
ATOM   82   C CG2 . VAL A 1 11  ? -9.878  -54.789 1.385   1.00 77.80  ? 10   VAL A CG2 1 
ATOM   83   N N   . LEU A 1 12  ? -8.369  -58.108 3.970   1.00 85.60  ? 11   LEU A N   1 
ATOM   84   C CA  . LEU A 1 12  ? -7.527  -59.197 4.438   1.00 79.23  ? 11   LEU A CA  1 
ATOM   85   C C   . LEU A 1 12  ? -8.389  -60.344 4.968   1.00 82.31  ? 11   LEU A C   1 
ATOM   86   O O   . LEU A 1 12  ? -8.094  -61.518 4.742   1.00 78.97  ? 11   LEU A O   1 
ATOM   87   C CB  . LEU A 1 12  ? -6.600  -58.698 5.541   1.00 74.83  ? 11   LEU A CB  1 
ATOM   88   C CG  . LEU A 1 12  ? -5.711  -59.753 6.191   1.00 73.99  ? 11   LEU A CG  1 
ATOM   89   C CD1 . LEU A 1 12  ? -4.673  -60.260 5.201   1.00 76.04  ? 11   LEU A CD1 1 
ATOM   90   C CD2 . LEU A 1 12  ? -5.054  -59.195 7.446   1.00 70.31  ? 11   LEU A CD2 1 
ATOM   91   N N   . THR A 1 13  ? -9.448  -59.989 5.685   1.00 79.95  ? 12   THR A N   1 
ATOM   92   C CA  . THR A 1 13  ? -10.321 -60.978 6.287   1.00 86.79  ? 12   THR A CA  1 
ATOM   93   C C   . THR A 1 13  ? -11.147 -61.660 5.210   1.00 95.71  ? 12   THR A C   1 
ATOM   94   O O   . THR A 1 13  ? -11.196 -62.889 5.138   1.00 96.01  ? 12   THR A O   1 
ATOM   95   C CB  . THR A 1 13  ? -11.266 -60.351 7.324   1.00 87.16  ? 12   THR A CB  1 
ATOM   96   O OG1 . THR A 1 13  ? -10.507 -59.866 8.443   1.00 84.59  ? 12   THR A OG1 1 
ATOM   97   C CG2 . THR A 1 13  ? -12.283 -61.390 7.808   1.00 78.08  ? 12   THR A CG2 1 
ATOM   98   N N   . ASN A 1 14  ? -11.787 -60.851 4.373   1.00 96.70  ? 13   ASN A N   1 
ATOM   99   C CA  . ASN A 1 14  ? -12.569 -61.362 3.259   1.00 91.21  ? 13   ASN A CA  1 
ATOM   100  C C   . ASN A 1 14  ? -11.741 -62.225 2.324   1.00 87.66  ? 13   ASN A C   1 
ATOM   101  O O   . ASN A 1 14  ? -12.258 -63.109 1.662   1.00 106.29 ? 13   ASN A O   1 
ATOM   102  C CB  . ASN A 1 14  ? -13.204 -60.221 2.471   1.00 88.04  ? 13   ASN A CB  1 
ATOM   103  C CG  . ASN A 1 14  ? -14.318 -59.538 3.232   1.00 90.39  ? 13   ASN A CG  1 
ATOM   104  O OD1 . ASN A 1 14  ? -14.730 -59.987 4.306   1.00 79.18  ? 13   ASN A OD1 1 
ATOM   105  N ND2 . ASN A 1 14  ? -14.811 -58.432 2.678   1.00 95.50  ? 13   ASN A ND2 1 
ATOM   106  N N   . SER A 1 15  ? -10.450 -61.967 2.257   1.00 86.44  ? 14   SER A N   1 
ATOM   107  C CA  . SER A 1 15  ? -9.604  -62.746 1.376   1.00 92.58  ? 14   SER A CA  1 
ATOM   108  C C   . SER A 1 15  ? -9.184  -64.041 2.057   1.00 95.55  ? 14   SER A C   1 
ATOM   109  O O   . SER A 1 15  ? -9.160  -65.098 1.432   1.00 99.55  ? 14   SER A O   1 
ATOM   110  C CB  . SER A 1 15  ? -8.391  -61.920 0.916   1.00 92.37  ? 14   SER A CB  1 
ATOM   111  O OG  . SER A 1 15  ? -8.788  -60.928 -0.019  1.00 88.44  ? 14   SER A OG  1 
ATOM   112  N N   . LEU A 1 16  ? -8.869  -63.955 3.344   1.00 100.16 ? 15   LEU A N   1 
ATOM   113  C CA  . LEU A 1 16  ? -8.431  -65.122 4.095   1.00 93.95  ? 15   LEU A CA  1 
ATOM   114  C C   . LEU A 1 16  ? -9.569  -66.139 4.175   1.00 93.84  ? 15   LEU A C   1 
ATOM   115  O O   . LEU A 1 16  ? -9.352  -67.342 4.067   1.00 100.34 ? 15   LEU A O   1 
ATOM   116  C CB  . LEU A 1 16  ? -7.921  -64.716 5.489   1.00 80.68  ? 15   LEU A CB  1 
ATOM   117  C CG  . LEU A 1 16  ? -6.407  -64.783 5.784   1.00 78.34  ? 15   LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 16  ? -5.564  -64.992 4.537   1.00 81.45  ? 15   LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 16  ? -5.914  -63.552 6.534   1.00 76.14  ? 15   LEU A CD2 1 
ATOM   120  N N   . ARG A 1 17  ? -10.788 -65.640 4.328   1.00 98.71  ? 16   ARG A N   1 
ATOM   121  C CA  . ARG A 1 17  ? -11.965 -66.491 4.443   1.00 103.61 ? 16   ARG A CA  1 
ATOM   122  C C   . ARG A 1 17  ? -12.518 -66.946 3.088   1.00 108.89 ? 16   ARG A C   1 
ATOM   123  O O   . ARG A 1 17  ? -13.593 -67.534 3.006   1.00 116.83 ? 16   ARG A O   1 
ATOM   124  C CB  . ARG A 1 17  ? -13.030 -65.788 5.283   1.00 103.20 ? 16   ARG A CB  1 
ATOM   125  C CG  . ARG A 1 17  ? -12.570 -65.591 6.712   1.00 109.94 ? 16   ARG A CG  1 
ATOM   126  C CD  . ARG A 1 17  ? -13.475 -64.678 7.512   1.00 120.82 ? 16   ARG A CD  1 
ATOM   127  N NE  . ARG A 1 17  ? -13.058 -64.666 8.912   1.00 135.89 ? 16   ARG A NE  1 
ATOM   128  C CZ  . ARG A 1 17  ? -13.568 -63.871 9.845   1.00 146.31 ? 16   ARG A CZ  1 
ATOM   129  N NH1 . ARG A 1 17  ? -13.120 -63.941 11.093  1.00 147.40 ? 16   ARG A NH1 1 
ATOM   130  N NH2 . ARG A 1 17  ? -14.523 -63.006 9.531   1.00 150.74 ? 16   ARG A NH2 1 
ATOM   131  N N   . SER A 1 18  ? -11.759 -66.689 2.032   1.00 112.04 ? 17   SER A N   1 
ATOM   132  C CA  . SER A 1 18  ? -12.115 -67.139 0.692   1.00 116.33 ? 17   SER A CA  1 
ATOM   133  C C   . SER A 1 18  ? -11.166 -68.238 0.278   1.00 111.91 ? 17   SER A C   1 
ATOM   134  O O   . SER A 1 18  ? -11.349 -68.902 -0.740  1.00 110.16 ? 17   SER A O   1 
ATOM   135  C CB  . SER A 1 18  ? -12.003 -65.989 -0.303  1.00 121.60 ? 17   SER A CB  1 
ATOM   136  O OG  . SER A 1 18  ? -12.944 -64.981 0.000   1.00 131.33 ? 17   SER A OG  1 
ATOM   137  N N   . VAL A 1 19  ? -10.121 -68.409 1.065   1.00 109.15 ? 18   VAL A N   1 
ATOM   138  C CA  . VAL A 1 19  ? -9.149  -69.433 0.764   1.00 104.00 ? 18   VAL A CA  1 
ATOM   139  C C   . VAL A 1 19  ? -9.818  -70.785 0.982   1.00 98.78  ? 18   VAL A C   1 
ATOM   140  O O   . VAL A 1 19  ? -10.306 -71.100 2.072   1.00 94.81  ? 18   VAL A O   1 
ATOM   141  C CB  . VAL A 1 19  ? -7.833  -69.203 1.558   1.00 71.73  ? 18   VAL A CB  1 
ATOM   142  C CG1 . VAL A 1 19  ? -7.009  -70.466 1.665   1.00 69.73  ? 18   VAL A CG1 1 
ATOM   143  C CG2 . VAL A 1 19  ? -7.022  -68.092 0.870   1.00 79.40  ? 18   VAL A CG2 1 
ATOM   144  N N   . ALA A 1 20  ? -9.901  -71.558 -0.090  1.00 100.22 ? 19   ALA A N   1 
ATOM   145  C CA  . ALA A 1 20  ? -10.545 -72.861 -0.021  1.00 95.48  ? 19   ALA A CA  1 
ATOM   146  C C   . ALA A 1 20  ? -9.478  -73.904 0.235   1.00 96.13  ? 19   ALA A C   1 
ATOM   147  O O   . ALA A 1 20  ? -8.911  -74.480 -0.687  1.00 94.87  ? 19   ALA A O   1 
ATOM   148  C CB  . ALA A 1 20  ? -11.303 -73.158 -1.303  1.00 90.97  ? 19   ALA A CB  1 
ATOM   149  N N   . ASP A 1 21  ? -9.191  -74.117 1.507   1.00 105.14 ? 20   ASP A N   1 
ATOM   150  C CA  . ASP A 1 21  ? -8.242  -75.134 1.912   1.00 107.96 ? 20   ASP A CA  1 
ATOM   151  C C   . ASP A 1 21  ? -8.969  -76.260 2.649   1.00 101.36 ? 20   ASP A C   1 
ATOM   152  O O   . ASP A 1 21  ? -10.201 -76.258 2.736   1.00 88.83  ? 20   ASP A O   1 
ATOM   153  C CB  . ASP A 1 21  ? -7.159  -74.522 2.808   1.00 114.51 ? 20   ASP A CB  1 
ATOM   154  C CG  . ASP A 1 21  ? -7.723  -73.887 4.085   1.00 120.52 ? 20   ASP A CG  1 
ATOM   155  O OD1 . ASP A 1 21  ? -8.958  -73.872 4.279   1.00 118.88 ? 20   ASP A OD1 1 
ATOM   156  O OD2 . ASP A 1 21  ? -6.914  -73.396 4.901   1.00 121.03 ? 20   ASP A OD2 1 
ATOM   157  N N   . GLY A 1 22  ? -8.187  -77.228 3.129   1.00 104.09 ? 21   GLY A N   1 
ATOM   158  C CA  . GLY A 1 22  ? -8.606  -78.136 4.176   1.00 104.45 ? 21   GLY A CA  1 
ATOM   159  C C   . GLY A 1 22  ? -8.268  -77.407 5.459   1.00 118.67 ? 21   GLY A C   1 
ATOM   160  O O   . GLY A 1 22  ? -7.215  -76.750 5.537   1.00 122.42 ? 21   GLY A O   1 
ATOM   161  N N   . GLY A 1 23  ? -9.142  -77.525 6.458   1.00 107.76 ? 22   GLY A N   1 
ATOM   162  C CA  . GLY A 1 23  ? -9.169  -76.590 7.578   1.00 101.77 ? 22   GLY A CA  1 
ATOM   163  C C   . GLY A 1 23  ? -8.007  -76.506 8.560   1.00 90.75  ? 22   GLY A C   1 
ATOM   164  O O   . GLY A 1 23  ? -8.231  -76.309 9.755   1.00 87.72  ? 22   GLY A O   1 
ATOM   165  N N   . ASP A 1 24  ? -6.776  -76.641 8.071   1.00 79.95  ? 23   ASP A N   1 
ATOM   166  C CA  . ASP A 1 24  ? -5.605  -76.557 8.932   1.00 91.04  ? 23   ASP A CA  1 
ATOM   167  C C   . ASP A 1 24  ? -5.148  -75.088 8.999   1.00 98.64  ? 23   ASP A C   1 
ATOM   168  O O   . ASP A 1 24  ? -5.732  -74.217 8.349   1.00 98.59  ? 23   ASP A O   1 
ATOM   169  C CB  . ASP A 1 24  ? -4.488  -77.477 8.412   1.00 95.68  ? 23   ASP A CB  1 
ATOM   170  C CG  . ASP A 1 24  ? -3.786  -78.265 9.534   1.00 106.50 ? 23   ASP A CG  1 
ATOM   171  O OD1 . ASP A 1 24  ? -3.652  -77.737 10.669  1.00 107.06 ? 23   ASP A OD1 1 
ATOM   172  O OD2 . ASP A 1 24  ? -3.354  -79.417 9.272   1.00 102.91 ? 23   ASP A OD2 1 
ATOM   173  N N   . TRP A 1 25  ? -4.121  -74.812 9.794   1.00 96.82  ? 24   TRP A N   1 
ATOM   174  C CA  . TRP A 1 25  ? -3.559  -73.468 9.852   1.00 84.07  ? 24   TRP A CA  1 
ATOM   175  C C   . TRP A 1 25  ? -3.095  -73.023 8.470   1.00 80.21  ? 24   TRP A C   1 
ATOM   176  O O   . TRP A 1 25  ? -2.802  -73.867 7.619   1.00 79.97  ? 24   TRP A O   1 
ATOM   177  C CB  . TRP A 1 25  ? -2.391  -73.417 10.837  1.00 74.44  ? 24   TRP A CB  1 
ATOM   178  C CG  . TRP A 1 25  ? -2.814  -73.501 12.267  1.00 77.17  ? 24   TRP A CG  1 
ATOM   179  C CD1 . TRP A 1 25  ? -2.772  -74.603 13.071  1.00 71.88  ? 24   TRP A CD1 1 
ATOM   180  C CD2 . TRP A 1 25  ? -3.346  -72.438 13.069  1.00 73.52  ? 24   TRP A CD2 1 
ATOM   181  N NE1 . TRP A 1 25  ? -3.243  -74.294 14.325  1.00 64.62  ? 24   TRP A NE1 1 
ATOM   182  C CE2 . TRP A 1 25  ? -3.605  -72.973 14.355  1.00 67.19  ? 24   TRP A CE2 1 
ATOM   183  C CE3 . TRP A 1 25  ? -3.622  -71.084 12.827  1.00 62.13  ? 24   TRP A CE3 1 
ATOM   184  C CZ2 . TRP A 1 25  ? -4.131  -72.206 15.401  1.00 69.31  ? 24   TRP A CZ2 1 
ATOM   185  C CZ3 . TRP A 1 25  ? -4.143  -70.319 13.860  1.00 62.66  ? 24   TRP A CZ3 1 
ATOM   186  C CH2 . TRP A 1 25  ? -4.394  -70.883 15.136  1.00 74.97  ? 24   TRP A CH2 1 
ATOM   187  N N   . LYS A 1 26  ? -3.044  -71.705 8.250   1.00 75.43  ? 25   LYS A N   1 
ATOM   188  C CA  . LYS A 1 26  ? -2.514  -71.138 7.006   1.00 68.86  ? 25   LYS A CA  1 
ATOM   189  C C   . LYS A 1 26  ? -1.168  -70.437 7.260   1.00 76.94  ? 25   LYS A C   1 
ATOM   190  O O   . LYS A 1 26  ? -0.876  -69.989 8.383   1.00 73.75  ? 25   LYS A O   1 
ATOM   191  C CB  . LYS A 1 26  ? -3.508  -70.154 6.372   1.00 69.84  ? 25   LYS A CB  1 
ATOM   192  C CG  . LYS A 1 26  ? -4.882  -70.729 6.012   1.00 77.27  ? 25   LYS A CG  1 
ATOM   193  C CD  . LYS A 1 26  ? -5.826  -69.663 5.440   1.00 75.15  ? 25   LYS A CD  1 
ATOM   194  C CE  . LYS A 1 26  ? -7.156  -69.575 6.202   1.00 85.90  ? 25   LYS A CE  1 
ATOM   195  N NZ  . LYS A 1 26  ? -8.204  -70.512 5.675   1.00 86.63  ? 25   LYS A NZ  1 
ATOM   196  N N   . VAL A 1 27  ? -0.342  -70.373 6.219   1.00 68.58  ? 26   VAL A N   1 
ATOM   197  C CA  . VAL A 1 27  ? 0.894   -69.601 6.260   1.00 68.28  ? 26   VAL A CA  1 
ATOM   198  C C   . VAL A 1 27  ? 0.746   -68.362 5.389   1.00 80.44  ? 26   VAL A C   1 
ATOM   199  O O   . VAL A 1 27  ? 0.493   -68.457 4.186   1.00 79.62  ? 26   VAL A O   1 
ATOM   200  C CB  . VAL A 1 27  ? 2.110   -70.414 5.788   1.00 74.33  ? 26   VAL A CB  1 
ATOM   201  C CG1 . VAL A 1 27  ? 3.286   -69.494 5.473   1.00 80.85  ? 26   VAL A CG1 1 
ATOM   202  C CG2 . VAL A 1 27  ? 2.498   -71.450 6.839   1.00 76.65  ? 26   VAL A CG2 1 
ATOM   203  N N   . LEU A 1 28  ? 0.889   -67.195 6.009   1.00 81.36  ? 27   LEU A N   1 
ATOM   204  C CA  . LEU A 1 28  ? 0.733   -65.940 5.298   1.00 75.52  ? 27   LEU A CA  1 
ATOM   205  C C   . LEU A 1 28  ? 2.088   -65.483 4.760   1.00 75.72  ? 27   LEU A C   1 
ATOM   206  O O   . LEU A 1 28  ? 2.905   -64.946 5.497   1.00 71.92  ? 27   LEU A O   1 
ATOM   207  C CB  . LEU A 1 28  ? 0.098   -64.885 6.211   1.00 66.92  ? 27   LEU A CB  1 
ATOM   208  C CG  . LEU A 1 28  ? -0.099  -63.489 5.598   1.00 74.62  ? 27   LEU A CG  1 
ATOM   209  C CD1 . LEU A 1 28  ? -0.780  -63.549 4.226   1.00 75.66  ? 27   LEU A CD1 1 
ATOM   210  C CD2 . LEU A 1 28  ? -0.875  -62.572 6.542   1.00 69.82  ? 27   LEU A CD2 1 
ATOM   211  N N   . VAL A 1 29  ? 2.328   -65.730 3.478   1.00 81.27  ? 28   VAL A N   1 
ATOM   212  C CA  . VAL A 1 29  ? 3.554   -65.282 2.823   1.00 90.47  ? 28   VAL A CA  1 
ATOM   213  C C   . VAL A 1 29  ? 3.386   -63.873 2.264   1.00 84.69  ? 28   VAL A C   1 
ATOM   214  O O   . VAL A 1 29  ? 2.476   -63.598 1.482   1.00 82.08  ? 28   VAL A O   1 
ATOM   215  C CB  . VAL A 1 29  ? 3.966   -66.220 1.689   1.00 97.97  ? 28   VAL A CB  1 
ATOM   216  C CG1 . VAL A 1 29  ? 5.316   -65.796 1.148   1.00 109.99 ? 28   VAL A CG1 1 
ATOM   217  C CG2 . VAL A 1 29  ? 4.019   -67.647 2.185   1.00 87.54  ? 28   VAL A CG2 1 
ATOM   218  N N   . VAL A 1 30  ? 4.277   -62.976 2.655   1.00 84.99  ? 29   VAL A N   1 
ATOM   219  C CA  . VAL A 1 30  ? 3.991   -61.562 2.483   1.00 80.33  ? 29   VAL A CA  1 
ATOM   220  C C   . VAL A 1 30  ? 5.173   -60.778 1.911   1.00 81.42  ? 29   VAL A C   1 
ATOM   221  O O   . VAL A 1 30  ? 6.328   -61.155 2.111   1.00 77.74  ? 29   VAL A O   1 
ATOM   222  C CB  . VAL A 1 30  ? 3.472   -60.967 3.827   1.00 77.26  ? 29   VAL A CB  1 
ATOM   223  C CG1 . VAL A 1 30  ? 4.593   -60.371 4.636   1.00 64.03  ? 29   VAL A CG1 1 
ATOM   224  C CG2 . VAL A 1 30  ? 2.352   -59.967 3.590   1.00 84.08  ? 29   VAL A CG2 1 
ATOM   225  N N   . ASP A 1 31  ? 4.853   -59.712 1.172   1.00 93.85  ? 30   ASP A N   1 
ATOM   226  C CA  . ASP A 1 31  ? 5.810   -58.776 0.554   1.00 91.54  ? 30   ASP A CA  1 
ATOM   227  C C   . ASP A 1 31  ? 6.289   -57.711 1.542   1.00 97.09  ? 30   ASP A C   1 
ATOM   228  O O   . ASP A 1 31  ? 5.778   -57.621 2.656   1.00 104.83 ? 30   ASP A O   1 
ATOM   229  C CB  . ASP A 1 31  ? 5.109   -58.043 -0.586  1.00 89.82  ? 30   ASP A CB  1 
ATOM   230  C CG  . ASP A 1 31  ? 5.912   -58.035 -1.848  1.00 118.23 ? 30   ASP A CG  1 
ATOM   231  O OD1 . ASP A 1 31  ? 7.027   -58.593 -1.843  1.00 137.19 ? 30   ASP A OD1 1 
ATOM   232  O OD2 . ASP A 1 31  ? 5.425   -57.469 -2.850  1.00 126.12 ? 30   ASP A OD2 1 
ATOM   233  N N   . LYS A 1 32  ? 7.250   -56.884 1.137   1.00 98.78  ? 31   LYS A N   1 
ATOM   234  C CA  . LYS A 1 32  ? 7.610   -55.723 1.958   1.00 99.34  ? 31   LYS A CA  1 
ATOM   235  C C   . LYS A 1 32  ? 6.475   -54.696 1.980   1.00 90.07  ? 31   LYS A C   1 
ATOM   236  O O   . LYS A 1 32  ? 6.085   -54.224 3.044   1.00 87.14  ? 31   LYS A O   1 
ATOM   237  C CB  . LYS A 1 32  ? 8.920   -55.084 1.501   1.00 101.60 ? 31   LYS A CB  1 
ATOM   238  C CG  . LYS A 1 32  ? 10.140  -55.964 1.730   1.00 113.66 ? 31   LYS A CG  1 
ATOM   239  C CD  . LYS A 1 32  ? 11.137  -55.284 2.649   1.00 114.55 ? 31   LYS A CD  1 
ATOM   240  C CE  . LYS A 1 32  ? 11.603  -53.951 2.073   1.00 115.48 ? 31   LYS A CE  1 
ATOM   241  N NZ  . LYS A 1 32  ? 12.300  -53.091 3.079   1.00 109.75 ? 31   LYS A NZ  1 
ATOM   242  N N   . PRO A 1 33  ? 5.932   -54.354 0.804   1.00 82.77  ? 32   PRO A N   1 
ATOM   243  C CA  . PRO A 1 33  ? 4.751   -53.484 0.767   1.00 72.54  ? 32   PRO A CA  1 
ATOM   244  C C   . PRO A 1 33  ? 3.551   -54.126 1.438   1.00 79.79  ? 32   PRO A C   1 
ATOM   245  O O   . PRO A 1 33  ? 2.738   -53.422 2.042   1.00 87.04  ? 32   PRO A O   1 
ATOM   246  C CB  . PRO A 1 33  ? 4.468   -53.332 -0.724  1.00 66.40  ? 32   PRO A CB  1 
ATOM   247  C CG  . PRO A 1 33  ? 5.750   -53.635 -1.393  1.00 73.12  ? 32   PRO A CG  1 
ATOM   248  C CD  . PRO A 1 33  ? 6.478   -54.614 -0.538  1.00 76.60  ? 32   PRO A CD  1 
ATOM   249  N N   . ALA A 1 34  ? 3.420   -55.444 1.324   1.00 82.62  ? 33   ALA A N   1 
ATOM   250  C CA  . ALA A 1 34  ? 2.284   -56.116 1.946   1.00 80.69  ? 33   ALA A CA  1 
ATOM   251  C C   . ALA A 1 34  ? 2.481   -56.157 3.452   1.00 80.95  ? 33   ALA A C   1 
ATOM   252  O O   . ALA A 1 34  ? 1.562   -55.879 4.213   1.00 83.96  ? 33   ALA A O   1 
ATOM   253  C CB  . ALA A 1 34  ? 2.105   -57.502 1.386   1.00 72.17  ? 33   ALA A CB  1 
ATOM   254  N N   . LEU A 1 35  ? 3.695   -56.485 3.872   1.00 82.90  ? 34   LEU A N   1 
ATOM   255  C CA  . LEU A 1 35  ? 4.045   -56.496 5.285   1.00 81.91  ? 34   LEU A CA  1 
ATOM   256  C C   . LEU A 1 35  ? 3.635   -55.203 5.971   1.00 84.46  ? 34   LEU A C   1 
ATOM   257  O O   . LEU A 1 35  ? 3.050   -55.221 7.062   1.00 79.53  ? 34   LEU A O   1 
ATOM   258  C CB  . LEU A 1 35  ? 5.551   -56.668 5.452   1.00 73.35  ? 34   LEU A CB  1 
ATOM   259  C CG  . LEU A 1 35  ? 5.986   -57.467 6.680   1.00 72.44  ? 34   LEU A CG  1 
ATOM   260  C CD1 . LEU A 1 35  ? 7.371   -57.023 7.115   1.00 61.76  ? 34   LEU A CD1 1 
ATOM   261  C CD2 . LEU A 1 35  ? 4.988   -57.346 7.827   1.00 64.36  ? 34   LEU A CD2 1 
ATOM   262  N N   . ARG A 1 36  ? 3.968   -54.081 5.335   1.00 82.52  ? 35   ARG A N   1 
ATOM   263  C CA  . ARG A 1 36  ? 3.765   -52.768 5.937   1.00 78.55  ? 35   ARG A CA  1 
ATOM   264  C C   . ARG A 1 36  ? 2.288   -52.477 6.094   1.00 76.23  ? 35   ARG A C   1 
ATOM   265  O O   . ARG A 1 36  ? 1.837   -52.064 7.162   1.00 76.32  ? 35   ARG A O   1 
ATOM   266  C CB  . ARG A 1 36  ? 4.442   -51.667 5.111   1.00 81.25  ? 35   ARG A CB  1 
ATOM   267  C CG  . ARG A 1 36  ? 5.645   -51.025 5.803   1.00 97.31  ? 35   ARG A CG  1 
ATOM   268  C CD  . ARG A 1 36  ? 5.227   -50.169 6.998   1.00 107.08 ? 35   ARG A CD  1 
ATOM   269  N NE  . ARG A 1 36  ? 4.762   -50.973 8.127   1.00 117.98 ? 35   ARG A NE  1 
ATOM   270  C CZ  . ARG A 1 36  ? 4.344   -50.468 9.285   1.00 121.32 ? 35   ARG A CZ  1 
ATOM   271  N NH1 . ARG A 1 36  ? 4.340   -49.152 9.462   1.00 125.90 ? 35   ARG A NH1 1 
ATOM   272  N NH2 . ARG A 1 36  ? 3.935   -51.273 10.268  1.00 111.64 ? 35   ARG A NH2 1 
ATOM   273  N N   . MET A 1 37  ? 1.546   -52.708 5.016   1.00 72.08  ? 36   MET A N   1 
ATOM   274  C CA  . MET A 1 37  ? 0.101   -52.519 4.986   1.00 67.77  ? 36   MET A CA  1 
ATOM   275  C C   . MET A 1 37  ? -0.648  -53.421 6.006   1.00 71.93  ? 36   MET A C   1 
ATOM   276  O O   . MET A 1 37  ? -1.485  -52.955 6.785   1.00 70.90  ? 36   MET A O   1 
ATOM   277  C CB  . MET A 1 37  ? -0.380  -52.747 3.548   1.00 70.75  ? 36   MET A CB  1 
ATOM   278  C CG  . MET A 1 37  ? -1.879  -52.922 3.370   1.00 76.44  ? 36   MET A CG  1 
ATOM   279  S SD  . MET A 1 37  ? -2.309  -52.908 1.619   1.00 107.97 ? 36   MET A SD  1 
ATOM   280  C CE  . MET A 1 37  ? -1.251  -54.206 0.983   1.00 148.84 ? 36   MET A CE  1 
ATOM   281  N N   . ILE A 1 38  ? -0.317  -54.704 6.029   1.00 67.43  ? 37   ILE A N   1 
ATOM   282  C CA  . ILE A 1 38  ? -0.984  -55.619 6.930   1.00 58.77  ? 37   ILE A CA  1 
ATOM   283  C C   . ILE A 1 38  ? -0.600  -55.354 8.379   1.00 70.36  ? 37   ILE A C   1 
ATOM   284  O O   . ILE A 1 38  ? -1.431  -55.463 9.276   1.00 71.84  ? 37   ILE A O   1 
ATOM   285  C CB  . ILE A 1 38  ? -0.717  -57.092 6.526   1.00 64.58  ? 37   ILE A CB  1 
ATOM   286  C CG1 . ILE A 1 38  ? -1.309  -57.364 5.140   1.00 72.61  ? 37   ILE A CG1 1 
ATOM   287  C CG2 . ILE A 1 38  ? -1.307  -58.056 7.536   1.00 50.40  ? 37   ILE A CG2 1 
ATOM   288  C CD1 . ILE A 1 38  ? -0.680  -58.547 4.427   1.00 78.02  ? 37   ILE A CD1 1 
ATOM   289  N N   . SER A 1 39  ? 0.655   -54.977 8.601   1.00 82.45  ? 38   SER A N   1 
ATOM   290  C CA  . SER A 1 39  ? 1.162   -54.766 9.955   1.00 78.70  ? 38   SER A CA  1 
ATOM   291  C C   . SER A 1 39  ? 0.463   -53.598 10.637  1.00 78.45  ? 38   SER A C   1 
ATOM   292  O O   . SER A 1 39  ? 0.378   -53.532 11.861  1.00 78.28  ? 38   SER A O   1 
ATOM   293  C CB  . SER A 1 39  ? 2.672   -54.534 9.930   1.00 79.26  ? 38   SER A CB  1 
ATOM   294  O OG  . SER A 1 39  ? 3.213   -54.593 11.238  1.00 89.45  ? 38   SER A OG  1 
ATOM   295  N N   . GLU A 1 40  ? -0.052  -52.687 9.824   1.00 83.15  ? 39   GLU A N   1 
ATOM   296  C CA  . GLU A 1 40  ? -0.629  -51.452 10.319  1.00 79.49  ? 39   GLU A CA  1 
ATOM   297  C C   . GLU A 1 40  ? -2.132  -51.595 10.545  1.00 79.06  ? 39   GLU A C   1 
ATOM   298  O O   . GLU A 1 40  ? -2.767  -50.723 11.136  1.00 76.24  ? 39   GLU A O   1 
ATOM   299  C CB  . GLU A 1 40  ? -0.325  -50.313 9.337   1.00 71.86  ? 39   GLU A CB  1 
ATOM   300  C CG  . GLU A 1 40  ? -0.368  -48.908 9.938   1.00 83.94  ? 39   GLU A CG  1 
ATOM   301  C CD  . GLU A 1 40  ? 0.705   -48.649 10.988  1.00 86.44  ? 39   GLU A CD  1 
ATOM   302  O OE1 . GLU A 1 40  ? 1.897   -48.821 10.683  1.00 86.93  ? 39   GLU A OE1 1 
ATOM   303  O OE2 . GLU A 1 40  ? 0.351   -48.250 12.118  1.00 93.79  ? 39   GLU A OE2 1 
ATOM   304  N N   . CYS A 1 41  ? -2.708  -52.702 10.085  1.00 86.13  ? 40   CYS A N   1 
ATOM   305  C CA  . CYS A 1 41  ? -4.152  -52.895 10.236  1.00 81.50  ? 40   CYS A CA  1 
ATOM   306  C C   . CYS A 1 41  ? -4.528  -54.061 11.159  1.00 78.70  ? 40   CYS A C   1 
ATOM   307  O O   . CYS A 1 41  ? -5.694  -54.196 11.551  1.00 86.07  ? 40   CYS A O   1 
ATOM   308  C CB  . CYS A 1 41  ? -4.819  -53.055 8.870   1.00 81.18  ? 40   CYS A CB  1 
ATOM   309  S SG  . CYS A 1 41  ? -4.730  -54.718 8.211   1.00 104.90 ? 40   CYS A SG  1 
ATOM   310  N N   . ALA A 1 42  ? -3.538  -54.874 11.529  1.00 67.04  ? 41   ALA A N   1 
ATOM   311  C CA  . ALA A 1 42  ? -3.784  -56.074 12.328  1.00 64.38  ? 41   ALA A CA  1 
ATOM   312  C C   . ALA A 1 42  ? -2.616  -56.447 13.238  1.00 61.26  ? 41   ALA A C   1 
ATOM   313  O O   . ALA A 1 42  ? -1.475  -56.478 12.794  1.00 63.26  ? 41   ALA A O   1 
ATOM   314  C CB  . ALA A 1 42  ? -4.105  -57.249 11.401  1.00 61.26  ? 41   ALA A CB  1 
ATOM   315  N N   . ARG A 1 43  ? -2.905  -56.763 14.499  1.00 61.74  ? 42   ARG A N   1 
ATOM   316  C CA  . ARG A 1 43  ? -1.885  -57.291 15.406  1.00 65.06  ? 42   ARG A CA  1 
ATOM   317  C C   . ARG A 1 43  ? -1.618  -58.763 15.068  1.00 73.27  ? 42   ARG A C   1 
ATOM   318  O O   . ARG A 1 43  ? -2.319  -59.338 14.237  1.00 92.58  ? 42   ARG A O   1 
ATOM   319  C CB  . ARG A 1 43  ? -2.345  -57.156 16.859  1.00 79.40  ? 42   ARG A CB  1 
ATOM   320  C CG  . ARG A 1 43  ? -2.897  -55.789 17.241  1.00 85.44  ? 42   ARG A CG  1 
ATOM   321  C CD  . ARG A 1 43  ? -1.806  -54.720 17.253  1.00 95.33  ? 42   ARG A CD  1 
ATOM   322  N NE  . ARG A 1 43  ? -2.156  -53.561 16.426  1.00 101.04 ? 42   ARG A NE  1 
ATOM   323  C CZ  . ARG A 1 43  ? -1.725  -53.375 15.178  1.00 98.81  ? 42   ARG A CZ  1 
ATOM   324  N NH1 . ARG A 1 43  ? -0.921  -54.270 14.613  1.00 97.93  ? 42   ARG A NH1 1 
ATOM   325  N NH2 . ARG A 1 43  ? -2.094  -52.300 14.493  1.00 94.32  ? 42   ARG A NH2 1 
ATOM   326  N N   . MET A 1 44  ? -0.612  -59.376 15.695  1.00 66.20  ? 43   MET A N   1 
ATOM   327  C CA  . MET A 1 44  ? -0.364  -60.816 15.508  1.00 70.28  ? 43   MET A CA  1 
ATOM   328  C C   . MET A 1 44  ? -1.497  -61.675 16.086  1.00 66.11  ? 43   MET A C   1 
ATOM   329  O O   . MET A 1 44  ? -1.890  -62.678 15.508  1.00 69.04  ? 43   MET A O   1 
ATOM   330  C CB  . MET A 1 44  ? 0.970   -61.247 16.128  1.00 77.84  ? 43   MET A CB  1 
ATOM   331  C CG  . MET A 1 44  ? 2.083   -61.540 15.119  1.00 88.52  ? 43   MET A CG  1 
ATOM   332  S SD  . MET A 1 44  ? 1.694   -62.875 13.966  1.00 101.59 ? 43   MET A SD  1 
ATOM   333  C CE  . MET A 1 44  ? 3.299   -63.217 13.237  1.00 101.59 ? 43   MET A CE  1 
ATOM   334  N N   . SER A 1 45  ? -1.997  -61.264 17.240  1.00 65.77  ? 44   SER A N   1 
ATOM   335  C CA  . SER A 1 45  ? -3.089  -61.932 17.913  1.00 63.10  ? 44   SER A CA  1 
ATOM   336  C C   . SER A 1 45  ? -4.337  -61.985 17.021  1.00 73.83  ? 44   SER A C   1 
ATOM   337  O O   . SER A 1 45  ? -5.095  -62.946 17.077  1.00 72.49  ? 44   SER A O   1 
ATOM   338  C CB  . SER A 1 45  ? -3.385  -61.204 19.234  1.00 69.48  ? 44   SER A CB  1 
ATOM   339  O OG  . SER A 1 45  ? -4.417  -61.832 19.973  1.00 86.10  ? 44   SER A OG  1 
ATOM   340  N N   . GLU A 1 46  ? -4.550  -60.954 16.205  1.00 78.52  ? 45   GLU A N   1 
ATOM   341  C CA  . GLU A 1 46  ? -5.722  -60.897 15.328  1.00 83.55  ? 45   GLU A CA  1 
ATOM   342  C C   . GLU A 1 46  ? -5.507  -61.737 14.079  1.00 84.32  ? 45   GLU A C   1 
ATOM   343  O O   . GLU A 1 46  ? -6.453  -62.075 13.381  1.00 85.10  ? 45   GLU A O   1 
ATOM   344  C CB  . GLU A 1 46  ? -6.037  -59.451 14.921  1.00 91.78  ? 45   GLU A CB  1 
ATOM   345  C CG  . GLU A 1 46  ? -6.772  -58.642 15.975  1.00 109.77 ? 45   GLU A CG  1 
ATOM   346  C CD  . GLU A 1 46  ? -6.924  -57.176 15.599  1.00 127.33 ? 45   GLU A CD  1 
ATOM   347  O OE1 . GLU A 1 46  ? -6.013  -56.617 14.941  1.00 125.06 ? 45   GLU A OE1 1 
ATOM   348  O OE2 . GLU A 1 46  ? -7.955  -56.576 15.977  1.00 136.60 ? 45   GLU A OE2 1 
ATOM   349  N N   . ILE A 1 47  ? -4.248  -62.052 13.801  1.00 86.94  ? 46   ILE A N   1 
ATOM   350  C CA  . ILE A 1 47  ? -3.876  -62.836 12.634  1.00 86.29  ? 46   ILE A CA  1 
ATOM   351  C C   . ILE A 1 47  ? -3.959  -64.318 13.007  1.00 82.12  ? 46   ILE A C   1 
ATOM   352  O O   . ILE A 1 47  ? -4.340  -65.171 12.196  1.00 77.65  ? 46   ILE A O   1 
ATOM   353  C CB  . ILE A 1 47  ? -2.444  -62.444 12.139  1.00 76.11  ? 46   ILE A CB  1 
ATOM   354  C CG1 . ILE A 1 47  ? -2.445  -62.133 10.651  1.00 81.47  ? 46   ILE A CG1 1 
ATOM   355  C CG2 . ILE A 1 47  ? -1.418  -63.513 12.456  1.00 80.36  ? 46   ILE A CG2 1 
ATOM   356  C CD1 . ILE A 1 47  ? -2.963  -60.760 10.346  1.00 90.51  ? 46   ILE A CD1 1 
ATOM   357  N N   . LEU A 1 48  ? -3.608  -64.606 14.256  1.00 83.02  ? 47   LEU A N   1 
ATOM   358  C CA  . LEU A 1 48  ? -3.608  -65.962 14.774  1.00 78.64  ? 47   LEU A CA  1 
ATOM   359  C C   . LEU A 1 48  ? -5.009  -66.517 14.728  1.00 82.51  ? 47   LEU A C   1 
ATOM   360  O O   . LEU A 1 48  ? -5.246  -67.592 14.189  1.00 93.68  ? 47   LEU A O   1 
ATOM   361  C CB  . LEU A 1 48  ? -3.115  -65.972 16.216  1.00 85.04  ? 47   LEU A CB  1 
ATOM   362  C CG  . LEU A 1 48  ? -1.883  -66.829 16.495  1.00 89.41  ? 47   LEU A CG  1 
ATOM   363  C CD1 . LEU A 1 48  ? -1.093  -67.073 15.220  1.00 84.92  ? 47   LEU A CD1 1 
ATOM   364  C CD2 . LEU A 1 48  ? -1.015  -66.180 17.578  1.00 85.33  ? 47   LEU A CD2 1 
ATOM   365  N N   . ASP A 1 49  ? -5.959  -65.792 15.299  1.00 80.28  ? 48   ASP A N   1 
ATOM   366  C CA  . ASP A 1 49  ? -7.306  -66.325 15.301  1.00 100.79 ? 48   ASP A CA  1 
ATOM   367  C C   . ASP A 1 49  ? -8.076  -65.886 14.057  1.00 98.42  ? 48   ASP A C   1 
ATOM   368  O O   . ASP A 1 49  ? -9.272  -65.608 14.079  1.00 101.57 ? 48   ASP A O   1 
ATOM   369  C CB  . ASP A 1 49  ? -8.028  -66.076 16.635  1.00 109.84 ? 48   ASP A CB  1 
ATOM   370  C CG  . ASP A 1 49  ? -8.153  -64.629 16.960  1.00 94.75  ? 48   ASP A CG  1 
ATOM   371  O OD1 . ASP A 1 49  ? -8.175  -63.833 15.999  1.00 91.73  ? 48   ASP A OD1 1 
ATOM   372  O OD2 . ASP A 1 49  ? -8.247  -64.299 18.165  1.00 90.98  ? 48   ASP A OD2 1 
ATOM   373  N N   . LEU A 1 50  ? -7.342  -65.843 12.958  1.00 100.31 ? 49   LEU A N   1 
ATOM   374  C CA  . LEU A 1 50  ? -7.916  -65.695 11.637  1.00 92.94  ? 49   LEU A CA  1 
ATOM   375  C C   . LEU A 1 50  ? -7.411  -66.912 10.886  1.00 85.98  ? 49   LEU A C   1 
ATOM   376  O O   . LEU A 1 50  ? -7.533  -67.016 9.665   1.00 88.49  ? 49   LEU A O   1 
ATOM   377  C CB  . LEU A 1 50  ? -7.408  -64.418 10.985  1.00 82.82  ? 49   LEU A CB  1 
ATOM   378  C CG  . LEU A 1 50  ? -8.384  -63.611 10.132  1.00 86.44  ? 49   LEU A CG  1 
ATOM   379  C CD1 . LEU A 1 50  ? -9.710  -63.427 10.845  1.00 75.52  ? 49   LEU A CD1 1 
ATOM   380  C CD2 . LEU A 1 50  ? -7.765  -62.244 9.770   1.00 88.63  ? 49   LEU A CD2 1 
ATOM   381  N N   . GLY A 1 51  ? -6.816  -67.824 11.647  1.00 73.27  ? 50   GLY A N   1 
ATOM   382  C CA  . GLY A 1 51  ? -6.300  -69.062 11.107  1.00 55.85  ? 50   GLY A CA  1 
ATOM   383  C C   . GLY A 1 51  ? -4.946  -69.085 10.423  1.00 82.55  ? 50   GLY A C   1 
ATOM   384  O O   . GLY A 1 51  ? -4.615  -70.114 9.817   1.00 76.60  ? 50   GLY A O   1 
ATOM   385  N N   . VAL A 1 52  ? -4.176  -67.987 10.479  1.00 72.50  ? 51   VAL A N   1 
ATOM   386  C CA  . VAL A 1 52  ? -2.764  -68.062 10.082  1.00 76.71  ? 51   VAL A CA  1 
ATOM   387  C C   . VAL A 1 52  ? -1.892  -68.212 11.321  1.00 83.17  ? 51   VAL A C   1 
ATOM   388  O O   . VAL A 1 52  ? -2.120  -67.547 12.335  1.00 72.33  ? 51   VAL A O   1 
ATOM   389  C CB  . VAL A 1 52  ? -2.272  -66.871 9.224   1.00 68.16  ? 51   VAL A CB  1 
ATOM   390  C CG1 . VAL A 1 52  ? -3.317  -66.476 8.204   1.00 80.25  ? 51   VAL A CG1 1 
ATOM   391  C CG2 . VAL A 1 52  ? -1.905  -65.689 10.097  1.00 72.22  ? 51   VAL A CG2 1 
ATOM   392  N N   . THR A 1 53  ? -0.903  -69.099 11.228  1.00 90.43  ? 52   THR A N   1 
ATOM   393  C CA  . THR A 1 53  ? -0.032  -69.429 12.355  1.00 83.01  ? 52   THR A CA  1 
ATOM   394  C C   . THR A 1 53  ? 1.351   -68.770 12.273  1.00 71.58  ? 52   THR A C   1 
ATOM   395  O O   . THR A 1 53  ? 1.997   -68.576 13.292  1.00 80.53  ? 52   THR A O   1 
ATOM   396  C CB  . THR A 1 53  ? 0.137   -70.961 12.512  1.00 79.36  ? 52   THR A CB  1 
ATOM   397  O OG1 . THR A 1 53  ? 0.729   -71.254 13.783  1.00 84.17  ? 52   THR A OG1 1 
ATOM   398  C CG2 . THR A 1 53  ? 1.014   -71.528 11.398  1.00 67.27  ? 52   THR A CG2 1 
ATOM   399  N N   . VAL A 1 54  ? 1.809   -68.454 11.065  1.00 67.56  ? 53   VAL A N   1 
ATOM   400  C CA  . VAL A 1 54  ? 3.028   -67.674 10.882  1.00 81.18  ? 53   VAL A CA  1 
ATOM   401  C C   . VAL A 1 54  ? 2.833   -66.664 9.782   1.00 91.56  ? 53   VAL A C   1 
ATOM   402  O O   . VAL A 1 54  ? 1.994   -66.859 8.886   1.00 91.77  ? 53   VAL A O   1 
ATOM   403  C CB  . VAL A 1 54  ? 4.252   -68.506 10.417  1.00 75.34  ? 53   VAL A CB  1 
ATOM   404  C CG1 . VAL A 1 54  ? 5.345   -68.542 11.489  1.00 59.46  ? 53   VAL A CG1 1 
ATOM   405  C CG2 . VAL A 1 54  ? 3.838   -69.874 9.929   1.00 84.24  ? 53   VAL A CG2 1 
ATOM   406  N N   . VAL A 1 55  ? 3.639   -65.602 9.850   1.00 79.18  ? 54   VAL A N   1 
ATOM   407  C CA  . VAL A 1 55  ? 3.820   -64.696 8.733   1.00 73.59  ? 54   VAL A CA  1 
ATOM   408  C C   . VAL A 1 55  ? 5.283   -64.790 8.279   1.00 80.18  ? 54   VAL A C   1 
ATOM   409  O O   . VAL A 1 55  ? 6.204   -64.809 9.100   1.00 76.41  ? 54   VAL A O   1 
ATOM   410  C CB  . VAL A 1 55  ? 3.451   -63.269 9.133   1.00 85.25  ? 54   VAL A CB  1 
ATOM   411  C CG1 . VAL A 1 55  ? 3.339   -62.354 7.893   1.00 75.53  ? 54   VAL A CG1 1 
ATOM   412  C CG2 . VAL A 1 55  ? 2.157   -63.290 9.936   1.00 47.36  ? 54   VAL A CG2 1 
ATOM   413  N N   . GLU A 1 56  ? 5.492   -64.875 6.969   1.00 84.75  ? 55   GLU A N   1 
ATOM   414  C CA  . GLU A 1 56  ? 6.822   -65.104 6.417   1.00 81.90  ? 55   GLU A CA  1 
ATOM   415  C C   . GLU A 1 56  ? 7.126   -64.062 5.359   1.00 86.90  ? 55   GLU A C   1 
ATOM   416  O O   . GLU A 1 56  ? 6.203   -63.487 4.772   1.00 84.07  ? 55   GLU A O   1 
ATOM   417  C CB  . GLU A 1 56  ? 6.892   -66.498 5.786   1.00 90.51  ? 55   GLU A CB  1 
ATOM   418  C CG  . GLU A 1 56  ? 6.605   -67.658 6.744   1.00 97.72  ? 55   GLU A CG  1 
ATOM   419  C CD  . GLU A 1 56  ? 7.793   -68.003 7.632   1.00 106.68 ? 55   GLU A CD  1 
ATOM   420  O OE1 . GLU A 1 56  ? 8.151   -69.205 7.716   1.00 98.16  ? 55   GLU A OE1 1 
ATOM   421  O OE2 . GLU A 1 56  ? 8.374   -67.070 8.237   1.00 112.68 ? 55   GLU A OE2 1 
ATOM   422  N N   . ASP A 1 57  ? 8.416   -63.815 5.120   1.00 89.25  ? 56   ASP A N   1 
ATOM   423  C CA  . ASP A 1 57  ? 8.836   -62.917 4.044   1.00 88.57  ? 56   ASP A CA  1 
ATOM   424  C C   . ASP A 1 57  ? 9.060   -63.707 2.767   1.00 88.97  ? 56   ASP A C   1 
ATOM   425  O O   . ASP A 1 57  ? 9.869   -64.631 2.740   1.00 94.49  ? 56   ASP A O   1 
ATOM   426  C CB  . ASP A 1 57  ? 10.115  -62.150 4.416   1.00 109.94 ? 56   ASP A CB  1 
ATOM   427  C CG  . ASP A 1 57  ? 10.654  -61.285 3.258   1.00 117.92 ? 56   ASP A CG  1 
ATOM   428  O OD1 . ASP A 1 57  ? 9.853   -60.598 2.578   1.00 114.66 ? 56   ASP A OD1 1 
ATOM   429  O OD2 . ASP A 1 57  ? 11.885  -61.291 3.030   1.00 118.97 ? 56   ASP A OD2 1 
ATOM   430  N N   . VAL A 1 58  ? 8.340   -63.336 1.712   1.00 91.44  ? 57   VAL A N   1 
ATOM   431  C CA  . VAL A 1 58  ? 8.415   -64.031 0.430   1.00 94.78  ? 57   VAL A CA  1 
ATOM   432  C C   . VAL A 1 58  ? 9.849   -64.362 0.015   1.00 102.09 ? 57   VAL A C   1 
ATOM   433  O O   . VAL A 1 58  ? 10.096  -65.373 -0.647  1.00 117.30 ? 57   VAL A O   1 
ATOM   434  C CB  . VAL A 1 58  ? 7.731   -63.222 -0.676  1.00 99.67  ? 57   VAL A CB  1 
ATOM   435  C CG1 . VAL A 1 58  ? 8.288   -61.808 -0.715  1.00 92.82  ? 57   VAL A CG1 1 
ATOM   436  C CG2 . VAL A 1 58  ? 7.900   -63.914 -2.015  1.00 110.67 ? 57   VAL A CG2 1 
ATOM   437  N N   . SER A 1 59  ? 10.789  -63.510 0.405   1.00 98.80  ? 58   SER A N   1 
ATOM   438  C CA  . SER A 1 59  ? 12.205  -63.807 0.245   1.00 106.69 ? 58   SER A CA  1 
ATOM   439  C C   . SER A 1 59  ? 12.705  -64.716 1.382   1.00 125.65 ? 58   SER A C   1 
ATOM   440  O O   . SER A 1 59  ? 12.246  -64.603 2.521   1.00 124.58 ? 58   SER A O   1 
ATOM   441  C CB  . SER A 1 59  ? 13.008  -62.512 0.201   1.00 103.49 ? 58   SER A CB  1 
ATOM   442  O OG  . SER A 1 59  ? 14.391  -62.793 0.147   1.00 115.25 ? 58   SER A OG  1 
ATOM   443  N N   . LYS A 1 60  ? 13.634  -65.617 1.058   1.00 137.84 ? 59   LYS A N   1 
ATOM   444  C CA  . LYS A 1 60  ? 14.224  -66.560 2.022   1.00 136.79 ? 59   LYS A CA  1 
ATOM   445  C C   . LYS A 1 60  ? 13.503  -67.905 2.043   1.00 127.72 ? 59   LYS A C   1 
ATOM   446  O O   . LYS A 1 60  ? 14.070  -68.946 1.712   1.00 117.44 ? 59   LYS A O   1 
ATOM   447  C CB  . LYS A 1 60  ? 14.253  -65.975 3.443   1.00 143.07 ? 59   LYS A CB  1 
ATOM   448  C CG  . LYS A 1 60  ? 15.052  -64.690 3.588   1.00 151.20 ? 59   LYS A CG  1 
ATOM   449  C CD  . LYS A 1 60  ? 14.997  -64.147 5.008   1.00 150.25 ? 59   LYS A CD  1 
ATOM   450  C CE  . LYS A 1 60  ? 15.837  -62.883 5.127   1.00 152.01 ? 59   LYS A CE  1 
ATOM   451  N NZ  . LYS A 1 60  ? 15.981  -62.435 6.537   1.00 150.72 ? 59   LYS A NZ  1 
ATOM   452  N N   . GLN A 1 61  ? 12.245  -67.862 2.457   1.00 136.73 ? 60   GLN A N   1 
ATOM   453  C CA  . GLN A 1 61  ? 11.418  -69.052 2.602   1.00 146.74 ? 60   GLN A CA  1 
ATOM   454  C C   . GLN A 1 61  ? 12.171  -70.298 3.015   1.00 154.98 ? 60   GLN A C   1 
ATOM   455  O O   . GLN A 1 61  ? 12.307  -71.231 2.222   1.00 167.90 ? 60   GLN A O   1 
ATOM   456  C CB  . GLN A 1 61  ? 10.653  -69.348 1.313   1.00 147.72 ? 60   GLN A CB  1 
ATOM   457  C CG  . GLN A 1 61  ? 9.172   -69.460 1.539   1.00 134.58 ? 60   GLN A CG  1 
ATOM   458  C CD  . GLN A 1 61  ? 8.614   -68.179 2.092   1.00 115.33 ? 60   GLN A CD  1 
ATOM   459  O OE1 . GLN A 1 61  ? 8.704   -67.910 3.298   1.00 87.46  ? 60   GLN A OE1 1 
ATOM   460  N NE2 . GLN A 1 61  ? 8.055   -67.357 1.207   1.00 115.17 ? 60   GLN A NE2 1 
ATOM   461  N N   . ARG A 1 62  ? 12.658  -70.328 4.248   1.00 149.19 ? 61   ARG A N   1 
ATOM   462  C CA  . ARG A 1 62  ? 13.084  -71.601 4.806   1.00 149.36 ? 61   ARG A CA  1 
ATOM   463  C C   . ARG A 1 62  ? 11.854  -72.292 5.417   1.00 140.13 ? 61   ARG A C   1 
ATOM   464  O O   . ARG A 1 62  ? 10.724  -71.808 5.278   1.00 128.29 ? 61   ARG A O   1 
ATOM   465  C CB  . ARG A 1 62  ? 14.237  -71.441 5.814   1.00 141.31 ? 61   ARG A CB  1 
ATOM   466  C CG  . ARG A 1 62  ? 13.807  -71.281 7.266   1.00 130.99 ? 61   ARG A CG  1 
ATOM   467  C CD  . ARG A 1 62  ? 14.231  -72.468 8.112   1.00 121.99 ? 61   ARG A CD  1 
ATOM   468  N NE  . ARG A 1 62  ? 13.691  -72.371 9.466   1.00 125.73 ? 61   ARG A NE  1 
ATOM   469  C CZ  . ARG A 1 62  ? 13.832  -73.312 10.396  1.00 134.75 ? 61   ARG A CZ  1 
ATOM   470  N NH1 . ARG A 1 62  ? 13.308  -73.139 11.602  1.00 135.03 ? 61   ARG A NH1 1 
ATOM   471  N NH2 . ARG A 1 62  ? 14.494  -74.428 10.120  1.00 136.72 ? 61   ARG A NH2 1 
ATOM   472  N N   . LYS A 1 63  ? 12.088  -73.424 6.073   1.00 136.78 ? 62   LYS A N   1 
ATOM   473  C CA  . LYS A 1 63  ? 11.039  -74.253 6.669   1.00 119.08 ? 62   LYS A CA  1 
ATOM   474  C C   . LYS A 1 63  ? 9.886   -74.561 5.723   1.00 113.44 ? 62   LYS A C   1 
ATOM   475  O O   . LYS A 1 63  ? 8.974   -73.756 5.526   1.00 110.60 ? 62   LYS A O   1 
ATOM   476  C CB  . LYS A 1 63  ? 10.527  -73.680 7.993   1.00 101.12 ? 62   LYS A CB  1 
ATOM   477  C CG  . LYS A 1 63  ? 9.989   -74.749 8.927   1.00 106.25 ? 62   LYS A CG  1 
ATOM   478  C CD  . LYS A 1 63  ? 10.963  -75.925 9.017   1.00 121.14 ? 62   LYS A CD  1 
ATOM   479  C CE  . LYS A 1 63  ? 10.356  -77.113 9.742   1.00 133.14 ? 62   LYS A CE  1 
ATOM   480  N NZ  . LYS A 1 63  ? 10.088  -76.807 11.173  1.00 142.57 ? 62   LYS A NZ  1 
ATOM   481  N N   . VAL A 1 64  ? 9.951   -75.751 5.144   1.00 104.89 ? 63   VAL A N   1 
ATOM   482  C CA  . VAL A 1 64  ? 8.902   -76.252 4.280   1.00 108.66 ? 63   VAL A CA  1 
ATOM   483  C C   . VAL A 1 64  ? 7.746   -76.850 5.103   1.00 117.99 ? 63   VAL A C   1 
ATOM   484  O O   . VAL A 1 64  ? 7.962   -77.658 6.011   1.00 120.41 ? 63   VAL A O   1 
ATOM   485  C CB  . VAL A 1 64  ? 9.495   -77.268 3.293   1.00 107.56 ? 63   VAL A CB  1 
ATOM   486  C CG1 . VAL A 1 64  ? 8.443   -78.285 2.817   1.00 102.60 ? 63   VAL A CG1 1 
ATOM   487  C CG2 . VAL A 1 64  ? 10.161  -76.522 2.134   1.00 94.95  ? 63   VAL A CG2 1 
ATOM   488  N N   . LEU A 1 65  ? 6.522   -76.433 4.785   1.00 112.98 ? 64   LEU A N   1 
ATOM   489  C CA  . LEU A 1 65  ? 5.348   -76.803 5.571   1.00 110.94 ? 64   LEU A CA  1 
ATOM   490  C C   . LEU A 1 65  ? 4.199   -77.314 4.695   1.00 112.49 ? 64   LEU A C   1 
ATOM   491  O O   . LEU A 1 65  ? 3.232   -76.590 4.454   1.00 112.78 ? 64   LEU A O   1 
ATOM   492  C CB  . LEU A 1 65  ? 4.868   -75.595 6.389   1.00 101.73 ? 64   LEU A CB  1 
ATOM   493  C CG  . LEU A 1 65  ? 5.793   -75.069 7.490   1.00 96.43  ? 64   LEU A CG  1 
ATOM   494  C CD1 . LEU A 1 65  ? 5.344   -73.681 8.029   1.00 66.94  ? 64   LEU A CD1 1 
ATOM   495  C CD2 . LEU A 1 65  ? 5.895   -76.107 8.604   1.00 89.56  ? 64   LEU A CD2 1 
ATOM   496  N N   . PRO A 1 66  ? 4.285   -78.571 4.231   1.00 114.43 ? 65   PRO A N   1 
ATOM   497  C CA  . PRO A 1 66  ? 3.296   -79.055 3.261   1.00 116.48 ? 65   PRO A CA  1 
ATOM   498  C C   . PRO A 1 66  ? 1.928   -79.355 3.884   1.00 116.38 ? 65   PRO A C   1 
ATOM   499  O O   . PRO A 1 66  ? 0.969   -79.566 3.148   1.00 120.88 ? 65   PRO A O   1 
ATOM   500  C CB  . PRO A 1 66  ? 3.933   -80.342 2.715   1.00 113.57 ? 65   PRO A CB  1 
ATOM   501  C CG  . PRO A 1 66  ? 5.323   -80.390 3.291   1.00 113.28 ? 65   PRO A CG  1 
ATOM   502  C CD  . PRO A 1 66  ? 5.277   -79.605 4.554   1.00 113.31 ? 65   PRO A CD  1 
ATOM   503  N N   . GLN A 1 67  ? 1.843   -79.356 5.212   1.00 109.90 ? 66   GLN A N   1 
ATOM   504  C CA  . GLN A 1 67  ? 0.589   -79.597 5.922   1.00 105.55 ? 66   GLN A CA  1 
ATOM   505  C C   . GLN A 1 67  ? -0.347  -78.390 5.846   1.00 99.62  ? 66   GLN A C   1 
ATOM   506  O O   . GLN A 1 67  ? -1.563  -78.520 6.020   1.00 100.21 ? 66   GLN A O   1 
ATOM   507  C CB  . GLN A 1 67  ? 0.864   -79.934 7.392   1.00 112.96 ? 66   GLN A CB  1 
ATOM   508  C CG  . GLN A 1 67  ? 1.998   -80.936 7.625   1.00 123.67 ? 66   GLN A CG  1 
ATOM   509  C CD  . GLN A 1 67  ? 3.388   -80.348 7.379   1.00 133.26 ? 66   GLN A CD  1 
ATOM   510  O OE1 . GLN A 1 67  ? 3.534   -79.174 7.035   1.00 126.30 ? 66   GLN A OE1 1 
ATOM   511  N NE2 . GLN A 1 67  ? 4.415   -81.171 7.559   1.00 139.42 ? 66   GLN A NE2 1 
ATOM   512  N N   . PHE A 1 68  ? 0.239   -77.223 5.583   1.00 96.74  ? 67   PHE A N   1 
ATOM   513  C CA  . PHE A 1 68  ? -0.472  -75.945 5.596   1.00 100.52 ? 67   PHE A CA  1 
ATOM   514  C C   . PHE A 1 68  ? -0.570  -75.328 4.210   1.00 98.88  ? 67   PHE A C   1 
ATOM   515  O O   . PHE A 1 68  ? 0.380   -75.391 3.429   1.00 98.52  ? 67   PHE A O   1 
ATOM   516  C CB  . PHE A 1 68  ? 0.275   -74.930 6.468   1.00 101.36 ? 67   PHE A CB  1 
ATOM   517  C CG  . PHE A 1 68  ? 0.460   -75.350 7.890   1.00 107.31 ? 67   PHE A CG  1 
ATOM   518  C CD1 . PHE A 1 68  ? -0.605  -75.824 8.638   1.00 112.00 ? 67   PHE A CD1 1 
ATOM   519  C CD2 . PHE A 1 68  ? 1.698   -75.227 8.495   1.00 107.32 ? 67   PHE A CD2 1 
ATOM   520  C CE1 . PHE A 1 68  ? -0.431  -76.188 9.959   1.00 116.33 ? 67   PHE A CE1 1 
ATOM   521  C CE2 . PHE A 1 68  ? 1.880   -75.586 9.815   1.00 114.84 ? 67   PHE A CE2 1 
ATOM   522  C CZ  . PHE A 1 68  ? 0.814   -76.066 10.550  1.00 118.42 ? 67   PHE A CZ  1 
ATOM   523  N N   . HIS A 1 69  ? -1.693  -74.678 3.923   1.00 93.33  ? 68   HIS A N   1 
ATOM   524  C CA  . HIS A 1 69  ? -1.798  -73.870 2.707   1.00 94.28  ? 68   HIS A CA  1 
ATOM   525  C C   . HIS A 1 69  ? -1.082  -72.511 2.817   1.00 91.51  ? 68   HIS A C   1 
ATOM   526  O O   . HIS A 1 69  ? -1.291  -71.746 3.772   1.00 89.59  ? 68   HIS A O   1 
ATOM   527  C CB  . HIS A 1 69  ? -3.260  -73.619 2.357   1.00 94.62  ? 68   HIS A CB  1 
ATOM   528  C CG  . HIS A 1 69  ? -3.988  -74.833 1.891   1.00 102.87 ? 68   HIS A CG  1 
ATOM   529  N ND1 . HIS A 1 69  ? -4.525  -74.936 0.627   1.00 102.66 ? 68   HIS A ND1 1 
ATOM   530  C CD2 . HIS A 1 69  ? -4.279  -75.994 2.521   1.00 113.75 ? 68   HIS A CD2 1 
ATOM   531  C CE1 . HIS A 1 69  ? -5.116  -76.108 0.499   1.00 111.78 ? 68   HIS A CE1 1 
ATOM   532  N NE2 . HIS A 1 69  ? -4.979  -76.771 1.633   1.00 117.56 ? 68   HIS A NE2 1 
ATOM   533  N N   . GLY A 1 70  ? -0.262  -72.195 1.823   1.00 90.95  ? 69   GLY A N   1 
ATOM   534  C CA  . GLY A 1 70  ? 0.366   -70.889 1.769   1.00 86.15  ? 69   GLY A CA  1 
ATOM   535  C C   . GLY A 1 70  ? -0.545  -69.852 1.140   1.00 84.10  ? 69   GLY A C   1 
ATOM   536  O O   . GLY A 1 70  ? -1.131  -70.093 0.086   1.00 87.34  ? 69   GLY A O   1 
ATOM   537  N N   . VAL A 1 71  ? -0.683  -68.703 1.794   1.00 78.52  ? 70   VAL A N   1 
ATOM   538  C CA  . VAL A 1 71  ? -1.398  -67.579 1.198   1.00 86.67  ? 70   VAL A CA  1 
ATOM   539  C C   . VAL A 1 71  ? -0.440  -66.408 0.965   1.00 88.04  ? 70   VAL A C   1 
ATOM   540  O O   . VAL A 1 71  ? 0.224   -65.934 1.890   1.00 83.58  ? 70   VAL A O   1 
ATOM   541  C CB  . VAL A 1 71  ? -2.589  -67.110 2.059   1.00 83.71  ? 70   VAL A CB  1 
ATOM   542  C CG1 . VAL A 1 71  ? -3.369  -66.018 1.327   1.00 79.40  ? 70   VAL A CG1 1 
ATOM   543  C CG2 . VAL A 1 71  ? -3.497  -68.278 2.396   1.00 79.29  ? 70   VAL A CG2 1 
ATOM   544  N N   . TYR A 1 72  ? -0.371  -65.943 -0.275  1.00 89.88  ? 71   TYR A N   1 
ATOM   545  C CA  . TYR A 1 72  ? 0.550   -64.870 -0.614  1.00 90.99  ? 71   TYR A CA  1 
ATOM   546  C C   . TYR A 1 72  ? -0.163  -63.546 -0.811  1.00 94.23  ? 71   TYR A C   1 
ATOM   547  O O   . TYR A 1 72  ? -1.106  -63.448 -1.600  1.00 100.31 ? 71   TYR A O   1 
ATOM   548  C CB  . TYR A 1 72  ? 1.323   -65.211 -1.882  1.00 85.34  ? 71   TYR A CB  1 
ATOM   549  C CG  . TYR A 1 72  ? 2.199   -66.436 -1.769  1.00 89.84  ? 71   TYR A CG  1 
ATOM   550  C CD1 . TYR A 1 72  ? 1.649   -67.722 -1.803  1.00 89.19  ? 71   TYR A CD1 1 
ATOM   551  C CD2 . TYR A 1 72  ? 3.579   -66.312 -1.644  1.00 81.01  ? 71   TYR A CD2 1 
ATOM   552  C CE1 . TYR A 1 72  ? 2.450   -68.842 -1.710  1.00 82.67  ? 71   TYR A CE1 1 
ATOM   553  C CE2 . TYR A 1 72  ? 4.388   -67.423 -1.550  1.00 84.30  ? 71   TYR A CE2 1 
ATOM   554  C CZ  . TYR A 1 72  ? 3.820   -68.682 -1.588  1.00 92.70  ? 71   TYR A CZ  1 
ATOM   555  O OH  . TYR A 1 72  ? 4.635   -69.781 -1.493  1.00 99.03  ? 71   TYR A OH  1 
ATOM   556  N N   . PHE A 1 73  ? 0.276   -62.539 -0.065  1.00 87.22  ? 72   PHE A N   1 
ATOM   557  C CA  . PHE A 1 73  ? -0.052  -61.157 -0.377  1.00 94.05  ? 72   PHE A CA  1 
ATOM   558  C C   . PHE A 1 73  ? 1.222   -60.527 -0.932  1.00 98.59  ? 72   PHE A C   1 
ATOM   559  O O   . PHE A 1 73  ? 2.259   -60.471 -0.265  1.00 101.32 ? 72   PHE A O   1 
ATOM   560  C CB  . PHE A 1 73  ? -0.568  -60.422 0.854   1.00 91.27  ? 72   PHE A CB  1 
ATOM   561  C CG  . PHE A 1 73  ? -1.998  -60.719 1.164   1.00 96.99  ? 72   PHE A CG  1 
ATOM   562  C CD1 . PHE A 1 73  ? -2.393  -61.999 1.499   1.00 88.91  ? 72   PHE A CD1 1 
ATOM   563  C CD2 . PHE A 1 73  ? -2.952  -59.718 1.120   1.00 103.35 ? 72   PHE A CD2 1 
ATOM   564  C CE1 . PHE A 1 73  ? -3.715  -62.277 1.784   1.00 88.95  ? 72   PHE A CE1 1 
ATOM   565  C CE2 . PHE A 1 73  ? -4.278  -59.994 1.409   1.00 101.16 ? 72   PHE A CE2 1 
ATOM   566  C CZ  . PHE A 1 73  ? -4.657  -61.277 1.734   1.00 91.70  ? 72   PHE A CZ  1 
ATOM   567  N N   . ILE A 1 74  ? 1.147   -60.065 -2.168  1.00 88.31  ? 73   ILE A N   1 
ATOM   568  C CA  . ILE A 1 74  ? 2.362   -59.917 -2.927  1.00 83.04  ? 73   ILE A CA  1 
ATOM   569  C C   . ILE A 1 74  ? 2.144   -59.053 -4.184  1.00 92.75  ? 73   ILE A C   1 
ATOM   570  O O   . ILE A 1 74  ? 1.019   -58.907 -4.664  1.00 94.23  ? 73   ILE A O   1 
ATOM   571  C CB  . ILE A 1 74  ? 2.923   -61.343 -3.215  1.00 85.59  ? 73   ILE A CB  1 
ATOM   572  C CG1 . ILE A 1 74  ? 4.409   -61.428 -2.896  1.00 92.68  ? 73   ILE A CG1 1 
ATOM   573  C CG2 . ILE A 1 74  ? 2.543   -61.886 -4.627  1.00 76.92  ? 73   ILE A CG2 1 
ATOM   574  C CD1 . ILE A 1 74  ? 5.018   -62.747 -3.318  1.00 109.62 ? 73   ILE A CD1 1 
ATOM   575  N N   . GLU A 1 75  ? 3.217   -58.449 -4.686  1.00 96.38  ? 74   GLU A N   1 
ATOM   576  C CA  . GLU A 1 75  ? 3.117   -57.532 -5.816  1.00 105.54 ? 74   GLU A CA  1 
ATOM   577  C C   . GLU A 1 75  ? 3.357   -58.259 -7.133  1.00 108.86 ? 74   GLU A C   1 
ATOM   578  O O   . GLU A 1 75  ? 4.146   -59.200 -7.183  1.00 111.57 ? 74   GLU A O   1 
ATOM   579  C CB  . GLU A 1 75  ? 4.123   -56.387 -5.664  1.00 112.46 ? 74   GLU A CB  1 
ATOM   580  C CG  . GLU A 1 75  ? 3.510   -55.033 -5.327  1.00 117.34 ? 74   GLU A CG  1 
ATOM   581  C CD  . GLU A 1 75  ? 4.566   -53.988 -4.996  1.00 120.04 ? 74   GLU A CD  1 
ATOM   582  O OE1 . GLU A 1 75  ? 5.639   -54.379 -4.483  1.00 112.21 ? 74   GLU A OE1 1 
ATOM   583  O OE2 . GLU A 1 75  ? 4.323   -52.783 -5.243  1.00 120.12 ? 74   GLU A OE2 1 
ATOM   584  N N   . PRO A 1 76  ? 2.672   -57.820 -8.203  1.00 109.09 ? 75   PRO A N   1 
ATOM   585  C CA  . PRO A 1 76  ? 2.816   -58.376 -9.557  1.00 107.64 ? 75   PRO A CA  1 
ATOM   586  C C   . PRO A 1 76  ? 4.196   -58.105 -10.138 1.00 110.99 ? 75   PRO A C   1 
ATOM   587  O O   . PRO A 1 76  ? 4.287   -57.456 -11.178 1.00 123.57 ? 75   PRO A O   1 
ATOM   588  C CB  . PRO A 1 76  ? 1.774   -57.604 -10.376 1.00 104.41 ? 75   PRO A CB  1 
ATOM   589  C CG  . PRO A 1 76  ? 0.861   -56.989 -9.387  1.00 104.80 ? 75   PRO A CG  1 
ATOM   590  C CD  . PRO A 1 76  ? 1.636   -56.775 -8.136  1.00 105.57 ? 75   PRO A CD  1 
ATOM   591  N N   . THR A 1 77  ? 5.247   -58.599 -9.491  1.00 101.13 ? 76   THR A N   1 
ATOM   592  C CA  . THR A 1 77  ? 6.612   -58.280 -9.898  1.00 98.82  ? 76   THR A CA  1 
ATOM   593  C C   . THR A 1 77  ? 7.461   -59.525 -10.128 1.00 103.08 ? 76   THR A C   1 
ATOM   594  O O   . THR A 1 77  ? 7.409   -60.466 -9.345  1.00 115.89 ? 76   THR A O   1 
ATOM   595  C CB  . THR A 1 77  ? 7.309   -57.411 -8.839  1.00 93.70  ? 76   THR A CB  1 
ATOM   596  O OG1 . THR A 1 77  ? 7.486   -58.175 -7.639  1.00 103.44 ? 76   THR A OG1 1 
ATOM   597  C CG2 . THR A 1 77  ? 6.477   -56.163 -8.538  1.00 72.54  ? 76   THR A CG2 1 
ATOM   598  N N   . GLU A 1 78  ? 8.257   -59.521 -11.192 1.00 106.00 ? 77   GLU A N   1 
ATOM   599  C CA  . GLU A 1 78  ? 9.106   -60.668 -11.498 1.00 110.33 ? 77   GLU A CA  1 
ATOM   600  C C   . GLU A 1 78  ? 9.812   -61.231 -10.262 1.00 105.44 ? 77   GLU A C   1 
ATOM   601  O O   . GLU A 1 78  ? 9.682   -62.410 -9.969  1.00 113.09 ? 77   GLU A O   1 
ATOM   602  C CB  . GLU A 1 78  ? 10.109  -60.356 -12.618 1.00 116.54 ? 77   GLU A CB  1 
ATOM   603  C CG  . GLU A 1 78  ? 10.752  -61.613 -13.213 1.00 124.63 ? 77   GLU A CG  1 
ATOM   604  C CD  . GLU A 1 78  ? 11.401  -61.373 -14.568 1.00 134.98 ? 77   GLU A CD  1 
ATOM   605  O OE1 . GLU A 1 78  ? 11.624  -60.193 -14.926 1.00 142.08 ? 77   GLU A OE1 1 
ATOM   606  O OE2 . GLU A 1 78  ? 11.692  -62.371 -15.271 1.00 130.03 ? 77   GLU A OE2 1 
ATOM   607  N N   . GLU A 1 79  ? 10.542  -60.398 -9.529  1.00 106.76 ? 78   GLU A N   1 
ATOM   608  C CA  . GLU A 1 79  ? 11.256  -60.875 -8.345  1.00 111.42 ? 78   GLU A CA  1 
ATOM   609  C C   . GLU A 1 79  ? 10.387  -61.791 -7.470  1.00 113.94 ? 78   GLU A C   1 
ATOM   610  O O   . GLU A 1 79  ? 10.861  -62.820 -6.982  1.00 112.31 ? 78   GLU A O   1 
ATOM   611  C CB  . GLU A 1 79  ? 11.797  -59.704 -7.520  1.00 120.91 ? 78   GLU A CB  1 
ATOM   612  C CG  . GLU A 1 79  ? 10.724  -58.725 -7.070  1.00 137.48 ? 78   GLU A CG  1 
ATOM   613  C CD  . GLU A 1 79  ? 11.193  -57.780 -5.972  1.00 141.99 ? 78   GLU A CD  1 
ATOM   614  O OE1 . GLU A 1 79  ? 10.606  -57.834 -4.864  1.00 135.74 ? 78   GLU A OE1 1 
ATOM   615  O OE2 . GLU A 1 79  ? 12.135  -56.988 -6.220  1.00 140.74 ? 78   GLU A OE2 1 
ATOM   616  N N   . ASN A 1 80  ? 9.118   -61.421 -7.283  1.00 114.01 ? 79   ASN A N   1 
ATOM   617  C CA  . ASN A 1 80  ? 8.177   -62.219 -6.484  1.00 106.30 ? 79   ASN A CA  1 
ATOM   618  C C   . ASN A 1 80  ? 7.795   -63.555 -7.126  1.00 112.60 ? 79   ASN A C   1 
ATOM   619  O O   . ASN A 1 80  ? 7.873   -64.604 -6.480  1.00 116.81 ? 79   ASN A O   1 
ATOM   620  C CB  . ASN A 1 80  ? 6.902   -61.425 -6.163  1.00 102.15 ? 79   ASN A CB  1 
ATOM   621  C CG  . ASN A 1 80  ? 7.064   -60.492 -4.963  1.00 99.90  ? 79   ASN A CG  1 
ATOM   622  O OD1 . ASN A 1 80  ? 7.915   -60.706 -4.098  1.00 101.12 ? 79   ASN A OD1 1 
ATOM   623  N ND2 . ASN A 1 80  ? 6.229   -59.459 -4.904  1.00 86.68  ? 79   ASN A ND2 1 
ATOM   624  N N   . LEU A 1 81  ? 7.369   -63.519 -8.388  1.00 110.02 ? 80   LEU A N   1 
ATOM   625  C CA  . LEU A 1 81  ? 6.983   -64.749 -9.080  1.00 110.19 ? 80   LEU A CA  1 
ATOM   626  C C   . LEU A 1 81  ? 8.108   -65.763 -9.063  1.00 114.18 ? 80   LEU A C   1 
ATOM   627  O O   . LEU A 1 81  ? 7.863   -66.966 -9.030  1.00 120.07 ? 80   LEU A O   1 
ATOM   628  C CB  . LEU A 1 81  ? 6.547   -64.485 -10.522 1.00 109.68 ? 80   LEU A CB  1 
ATOM   629  C CG  . LEU A 1 81  ? 5.073   -64.135 -10.717 1.00 115.23 ? 80   LEU A CG  1 
ATOM   630  C CD1 . LEU A 1 81  ? 4.711   -62.902 -9.895  1.00 117.44 ? 80   LEU A CD1 1 
ATOM   631  C CD2 . LEU A 1 81  ? 4.763   -63.919 -12.188 1.00 120.33 ? 80   LEU A CD2 1 
ATOM   632  N N   . ASP A 1 82  ? 9.343   -65.278 -9.091  1.00 115.32 ? 81   ASP A N   1 
ATOM   633  C CA  . ASP A 1 82  ? 10.491  -66.170 -9.035  1.00 125.85 ? 81   ASP A CA  1 
ATOM   634  C C   . ASP A 1 82  ? 10.551  -66.869 -7.679  1.00 122.05 ? 81   ASP A C   1 
ATOM   635  O O   . ASP A 1 82  ? 10.916  -68.041 -7.600  1.00 125.86 ? 81   ASP A O   1 
ATOM   636  C CB  . ASP A 1 82  ? 11.795  -65.423 -9.340  1.00 134.99 ? 81   ASP A CB  1 
ATOM   637  C CG  . ASP A 1 82  ? 11.954  -65.100 -10.823 1.00 141.97 ? 81   ASP A CG  1 
ATOM   638  O OD1 . ASP A 1 82  ? 11.089  -65.519 -11.625 1.00 139.38 ? 81   ASP A OD1 1 
ATOM   639  O OD2 . ASP A 1 82  ? 12.947  -64.428 -11.185 1.00 144.12 ? 81   ASP A OD2 1 
ATOM   640  N N   . TYR A 1 83  ? 10.174  -66.157 -6.620  1.00 115.19 ? 82   TYR A N   1 
ATOM   641  C CA  . TYR A 1 83  ? 10.114  -66.752 -5.283  1.00 115.07 ? 82   TYR A CA  1 
ATOM   642  C C   . TYR A 1 83  ? 8.999   -67.793 -5.189  1.00 118.66 ? 82   TYR A C   1 
ATOM   643  O O   . TYR A 1 83  ? 9.131   -68.800 -4.489  1.00 114.76 ? 82   TYR A O   1 
ATOM   644  C CB  . TYR A 1 83  ? 9.910   -65.684 -4.206  1.00 109.04 ? 82   TYR A CB  1 
ATOM   645  C CG  . TYR A 1 83  ? 11.114  -64.803 -3.957  1.00 114.72 ? 82   TYR A CG  1 
ATOM   646  C CD1 . TYR A 1 83  ? 12.331  -65.351 -3.569  1.00 116.41 ? 82   TYR A CD1 1 
ATOM   647  C CD2 . TYR A 1 83  ? 11.027  -63.418 -4.084  1.00 115.26 ? 82   TYR A CD2 1 
ATOM   648  C CE1 . TYR A 1 83  ? 13.434  -64.545 -3.334  1.00 120.44 ? 82   TYR A CE1 1 
ATOM   649  C CE2 . TYR A 1 83  ? 12.124  -62.604 -3.844  1.00 114.66 ? 82   TYR A CE2 1 
ATOM   650  C CZ  . TYR A 1 83  ? 13.323  -63.174 -3.469  1.00 118.19 ? 82   TYR A CZ  1 
ATOM   651  O OH  . TYR A 1 83  ? 14.416  -62.377 -3.229  1.00 116.68 ? 82   TYR A OH  1 
ATOM   652  N N   . VAL A 1 84  ? 7.901   -67.539 -5.893  1.00 117.54 ? 83   VAL A N   1 
ATOM   653  C CA  . VAL A 1 84  ? 6.780   -68.469 -5.924  1.00 105.94 ? 83   VAL A CA  1 
ATOM   654  C C   . VAL A 1 84  ? 7.100   -69.717 -6.744  1.00 115.78 ? 83   VAL A C   1 
ATOM   655  O O   . VAL A 1 84  ? 7.027   -70.830 -6.221  1.00 127.45 ? 83   VAL A O   1 
ATOM   656  C CB  . VAL A 1 84  ? 5.495   -67.801 -6.450  1.00 90.73  ? 83   VAL A CB  1 
ATOM   657  C CG1 . VAL A 1 84  ? 4.366   -68.823 -6.590  1.00 79.48  ? 83   VAL A CG1 1 
ATOM   658  C CG2 . VAL A 1 84  ? 5.085   -66.655 -5.532  1.00 83.04  ? 83   VAL A CG2 1 
ATOM   659  N N   . ILE A 1 85  ? 7.455   -69.552 -8.017  1.00 112.68 ? 84   ILE A N   1 
ATOM   660  C CA  . ILE A 1 85  ? 7.778   -70.720 -8.836  1.00 116.43 ? 84   ILE A CA  1 
ATOM   661  C C   . ILE A 1 85  ? 8.904   -71.520 -8.181  1.00 122.34 ? 84   ILE A C   1 
ATOM   662  O O   . ILE A 1 85  ? 9.087   -72.698 -8.487  1.00 131.19 ? 84   ILE A O   1 
ATOM   663  C CB  . ILE A 1 85  ? 8.157   -70.376 -10.314 1.00 112.19 ? 84   ILE A CB  1 
ATOM   664  C CG1 . ILE A 1 85  ? 9.521   -69.692 -10.392 1.00 126.14 ? 84   ILE A CG1 1 
ATOM   665  C CG2 . ILE A 1 85  ? 7.091   -69.519 -10.987 1.00 106.19 ? 84   ILE A CG2 1 
ATOM   666  C CD1 . ILE A 1 85  ? 9.886   -69.235 -11.789 1.00 134.70 ? 84   ILE A CD1 1 
ATOM   667  N N   . ARG A 1 86  ? 9.643   -70.882 -7.271  1.00 113.68 ? 85   ARG A N   1 
ATOM   668  C CA  . ARG A 1 86  ? 10.773  -71.525 -6.596  1.00 116.75 ? 85   ARG A CA  1 
ATOM   669  C C   . ARG A 1 86  ? 10.359  -72.335 -5.364  1.00 127.68 ? 85   ARG A C   1 
ATOM   670  O O   . ARG A 1 86  ? 10.923  -73.397 -5.094  1.00 134.74 ? 85   ARG A O   1 
ATOM   671  C CB  . ARG A 1 86  ? 11.839  -70.488 -6.234  1.00 122.01 ? 85   ARG A CB  1 
ATOM   672  C CG  . ARG A 1 86  ? 12.765  -70.865 -5.078  1.00 137.59 ? 85   ARG A CG  1 
ATOM   673  C CD  . ARG A 1 86  ? 13.717  -69.703 -4.766  1.00 151.10 ? 85   ARG A CD  1 
ATOM   674  N NE  . ARG A 1 86  ? 14.393  -69.827 -3.475  1.00 158.05 ? 85   ARG A NE  1 
ATOM   675  C CZ  . ARG A 1 86  ? 13.989  -69.232 -2.356  1.00 161.03 ? 85   ARG A CZ  1 
ATOM   676  N NH1 . ARG A 1 86  ? 12.901  -68.471 -2.359  1.00 162.70 ? 85   ARG A NH1 1 
ATOM   677  N NH2 . ARG A 1 86  ? 14.673  -69.398 -1.231  1.00 159.65 ? 85   ARG A NH2 1 
ATOM   678  N N   . ASP A 1 87  ? 9.373   -71.841 -4.622  1.00 126.49 ? 86   ASP A N   1 
ATOM   679  C CA  . ASP A 1 87  ? 8.892   -72.543 -3.436  1.00 122.16 ? 86   ASP A CA  1 
ATOM   680  C C   . ASP A 1 87  ? 8.237   -73.891 -3.796  1.00 121.80 ? 86   ASP A C   1 
ATOM   681  O O   . ASP A 1 87  ? 8.037   -74.753 -2.941  1.00 108.27 ? 86   ASP A O   1 
ATOM   682  C CB  . ASP A 1 87  ? 7.923   -71.654 -2.644  1.00 125.90 ? 86   ASP A CB  1 
ATOM   683  C CG  . ASP A 1 87  ? 8.632   -70.555 -1.857  1.00 135.59 ? 86   ASP A CG  1 
ATOM   684  O OD1 . ASP A 1 87  ? 9.884   -70.515 -1.862  1.00 143.68 ? 86   ASP A OD1 1 
ATOM   685  O OD2 . ASP A 1 87  ? 7.930   -69.733 -1.226  1.00 135.48 ? 86   ASP A OD2 1 
ATOM   686  N N   . PHE A 1 88  ? 7.912   -74.074 -5.069  1.00 129.50 ? 87   PHE A N   1 
ATOM   687  C CA  . PHE A 1 88  ? 7.286   -75.314 -5.510  1.00 133.31 ? 87   PHE A CA  1 
ATOM   688  C C   . PHE A 1 88  ? 8.210   -76.136 -6.409  1.00 144.99 ? 87   PHE A C   1 
ATOM   689  O O   . PHE A 1 88  ? 8.636   -77.226 -6.030  1.00 153.61 ? 87   PHE A O   1 
ATOM   690  C CB  . PHE A 1 88  ? 5.947   -75.025 -6.193  1.00 129.31 ? 87   PHE A CB  1 
ATOM   691  C CG  . PHE A 1 88  ? 4.896   -74.511 -5.251  1.00 127.60 ? 87   PHE A CG  1 
ATOM   692  C CD1 . PHE A 1 88  ? 4.271   -75.368 -4.355  1.00 127.82 ? 87   PHE A CD1 1 
ATOM   693  C CD2 . PHE A 1 88  ? 4.539   -73.175 -5.249  1.00 125.66 ? 87   PHE A CD2 1 
ATOM   694  C CE1 . PHE A 1 88  ? 3.307   -74.903 -3.480  1.00 122.85 ? 87   PHE A CE1 1 
ATOM   695  C CE2 . PHE A 1 88  ? 3.575   -72.702 -4.374  1.00 120.84 ? 87   PHE A CE2 1 
ATOM   696  C CZ  . PHE A 1 88  ? 2.958   -73.567 -3.489  1.00 119.60 ? 87   PHE A CZ  1 
ATOM   697  N N   . ALA A 1 89  ? 8.506   -75.606 -7.592  1.00 142.19 ? 88   ALA A N   1 
ATOM   698  C CA  . ALA A 1 89  ? 9.486   -76.186 -8.512  1.00 140.90 ? 88   ALA A CA  1 
ATOM   699  C C   . ALA A 1 89  ? 10.082  -77.534 -8.085  1.00 141.17 ? 88   ALA A C   1 
ATOM   700  O O   . ALA A 1 89  ? 9.832   -78.559 -8.720  1.00 136.99 ? 88   ALA A O   1 
ATOM   701  C CB  . ALA A 1 89  ? 10.602  -75.182 -8.773  1.00 133.77 ? 88   ALA A CB  1 
ATOM   702  N N   . ASP A 1 90  ? 10.876  -77.515 -7.018  1.00 145.25 ? 89   ASP A N   1 
ATOM   703  C CA  . ASP A 1 90  ? 11.600  -78.695 -6.545  1.00 156.90 ? 89   ASP A CA  1 
ATOM   704  C C   . ASP A 1 90  ? 10.702  -79.905 -6.234  1.00 157.06 ? 89   ASP A C   1 
ATOM   705  O O   . ASP A 1 90  ? 9.476   -79.821 -6.303  1.00 152.80 ? 89   ASP A O   1 
ATOM   706  C CB  . ASP A 1 90  ? 12.446  -78.332 -5.319  1.00 166.29 ? 89   ASP A CB  1 
ATOM   707  C CG  . ASP A 1 90  ? 13.471  -79.399 -4.977  1.00 178.52 ? 89   ASP A CG  1 
ATOM   708  O OD1 . ASP A 1 90  ? 14.281  -79.757 -5.862  1.00 182.92 ? 89   ASP A OD1 1 
ATOM   709  O OD2 . ASP A 1 90  ? 13.469  -79.879 -3.822  1.00 180.60 ? 89   ASP A OD2 1 
ATOM   710  N N   . ARG A 1 91  ? 11.336  -81.028 -5.897  1.00 161.46 ? 90   ARG A N   1 
ATOM   711  C CA  . ARG A 1 91  ? 10.645  -82.280 -5.586  1.00 163.59 ? 90   ARG A CA  1 
ATOM   712  C C   . ARG A 1 91  ? 9.482   -82.079 -4.616  1.00 153.98 ? 90   ARG A C   1 
ATOM   713  O O   . ARG A 1 91  ? 8.316   -82.233 -4.985  1.00 143.31 ? 90   ARG A O   1 
ATOM   714  C CB  . ARG A 1 91  ? 11.641  -83.297 -5.010  1.00 170.16 ? 90   ARG A CB  1 
ATOM   715  C CG  . ARG A 1 91  ? 11.003  -84.462 -4.260  1.00 175.03 ? 90   ARG A CG  1 
ATOM   716  C CD  . ARG A 1 91  ? 10.670  -85.624 -5.179  1.00 179.30 ? 90   ARG A CD  1 
ATOM   717  N NE  . ARG A 1 91  ? 11.872  -86.284 -5.678  1.00 181.67 ? 90   ARG A NE  1 
ATOM   718  C CZ  . ARG A 1 91  ? 11.869  -87.433 -6.346  1.00 182.71 ? 90   ARG A CZ  1 
ATOM   719  N NH1 . ARG A 1 91  ? 10.724  -88.055 -6.591  1.00 181.28 ? 90   ARG A NH1 1 
ATOM   720  N NH2 . ARG A 1 91  ? 13.011  -87.964 -6.764  1.00 184.23 ? 90   ARG A NH2 1 
ATOM   721  N N   . THR A 1 92  ? 9.813   -81.739 -3.374  1.00 153.98 ? 91   THR A N   1 
ATOM   722  C CA  . THR A 1 92  ? 8.812   -81.489 -2.344  1.00 150.34 ? 91   THR A CA  1 
ATOM   723  C C   . THR A 1 92  ? 8.362   -80.028 -2.359  1.00 147.21 ? 91   THR A C   1 
ATOM   724  O O   . THR A 1 92  ? 9.187   -79.111 -2.275  1.00 142.47 ? 91   THR A O   1 
ATOM   725  C CB  . THR A 1 92  ? 9.347   -81.841 -0.940  1.00 145.90 ? 91   THR A CB  1 
ATOM   726  O OG1 . THR A 1 92  ? 9.769   -83.212 -0.916  1.00 152.39 ? 91   THR A OG1 1 
ATOM   727  C CG2 . THR A 1 92  ? 8.271   -81.614 0.123   1.00 131.77 ? 91   THR A CG2 1 
ATOM   728  N N   . PRO A 1 93  ? 7.042   -79.810 -2.466  1.00 142.16 ? 92   PRO A N   1 
ATOM   729  C CA  . PRO A 1 93  ? 6.456   -78.467 -2.479  1.00 137.38 ? 92   PRO A CA  1 
ATOM   730  C C   . PRO A 1 93  ? 6.592   -77.815 -1.106  1.00 129.40 ? 92   PRO A C   1 
ATOM   731  O O   . PRO A 1 93  ? 6.824   -78.520 -0.122  1.00 136.55 ? 92   PRO A O   1 
ATOM   732  C CB  . PRO A 1 93  ? 4.984   -78.737 -2.805  1.00 136.02 ? 92   PRO A CB  1 
ATOM   733  C CG  . PRO A 1 93  ? 4.733   -80.107 -2.283  1.00 125.99 ? 92   PRO A CG  1 
ATOM   734  C CD  . PRO A 1 93  ? 6.014   -80.865 -2.488  1.00 132.71 ? 92   PRO A CD  1 
ATOM   735  N N   . THR A 1 94  ? 6.448   -76.495 -1.037  1.00 115.33 ? 93   THR A N   1 
ATOM   736  C CA  . THR A 1 94  ? 6.673   -75.774 0.214   1.00 103.01 ? 93   THR A CA  1 
ATOM   737  C C   . THR A 1 94  ? 5.406   -75.597 1.042   1.00 93.45  ? 93   THR A C   1 
ATOM   738  O O   . THR A 1 94  ? 5.464   -75.521 2.266   1.00 87.09  ? 93   THR A O   1 
ATOM   739  C CB  . THR A 1 94  ? 7.350   -74.413 -0.023  1.00 104.64 ? 93   THR A CB  1 
ATOM   740  O OG1 . THR A 1 94  ? 8.700   -74.629 -0.453  1.00 107.56 ? 93   THR A OG1 1 
ATOM   741  C CG2 . THR A 1 94  ? 7.368   -73.588 1.258   1.00 105.06 ? 93   THR A CG2 1 
ATOM   742  N N   . TYR A 1 95  ? 4.262   -75.547 0.377   1.00 96.31  ? 94   TYR A N   1 
ATOM   743  C CA  . TYR A 1 95  ? 2.987   -75.583 1.082   1.00 97.82  ? 94   TYR A CA  1 
ATOM   744  C C   . TYR A 1 95  ? 2.038   -76.642 0.440   1.00 101.54 ? 94   TYR A C   1 
ATOM   745  O O   . TYR A 1 95  ? 2.349   -77.186 -0.617  1.00 90.73  ? 94   TYR A O   1 
ATOM   746  C CB  . TYR A 1 95  ? 2.399   -74.165 1.142   1.00 95.14  ? 94   TYR A CB  1 
ATOM   747  C CG  . TYR A 1 95  ? 3.356   -73.136 1.773   1.00 100.43 ? 94   TYR A CG  1 
ATOM   748  C CD1 . TYR A 1 95  ? 3.732   -73.233 3.109   1.00 91.61  ? 94   TYR A CD1 1 
ATOM   749  C CD2 . TYR A 1 95  ? 3.869   -72.068 1.036   1.00 94.27  ? 94   TYR A CD2 1 
ATOM   750  C CE1 . TYR A 1 95  ? 4.591   -72.318 3.691   1.00 91.29  ? 94   TYR A CE1 1 
ATOM   751  C CE2 . TYR A 1 95  ? 4.738   -71.140 1.614   1.00 87.41  ? 94   TYR A CE2 1 
ATOM   752  C CZ  . TYR A 1 95  ? 5.099   -71.267 2.948   1.00 94.45  ? 94   TYR A CZ  1 
ATOM   753  O OH  . TYR A 1 95  ? 5.958   -70.350 3.557   1.00 81.62  ? 94   TYR A OH  1 
ATOM   754  N N   . GLU A 1 96  ? 0.915   -76.967 1.083   1.00 105.00 ? 95   GLU A N   1 
ATOM   755  C CA  . GLU A 1 96  ? -0.046  -77.892 0.474   1.00 103.11 ? 95   GLU A CA  1 
ATOM   756  C C   . GLU A 1 96  ? -0.534  -77.302 -0.847  1.00 106.40 ? 95   GLU A C   1 
ATOM   757  O O   . GLU A 1 96  ? -0.873  -78.030 -1.782  1.00 117.10 ? 95   GLU A O   1 
ATOM   758  C CB  . GLU A 1 96  ? -1.234  -78.213 1.403   1.00 98.70  ? 95   GLU A CB  1 
ATOM   759  C CG  . GLU A 1 96  ? -2.104  -79.407 0.915   1.00 129.31 ? 95   GLU A CG  1 
ATOM   760  C CD  . GLU A 1 96  ? -3.252  -79.807 1.869   1.00 131.70 ? 95   GLU A CD  1 
ATOM   761  O OE1 . GLU A 1 96  ? -4.368  -80.091 1.372   1.00 127.86 ? 95   GLU A OE1 1 
ATOM   762  O OE2 . GLU A 1 96  ? -3.048  -79.853 3.106   1.00 132.21 ? 95   GLU A OE2 1 
ATOM   763  N N   . ALA A 1 97  ? -0.553  -75.975 -0.914  1.00 97.76  ? 96   ALA A N   1 
ATOM   764  C CA  . ALA A 1 97  ? -0.956  -75.251 -2.114  1.00 102.07 ? 96   ALA A CA  1 
ATOM   765  C C   . ALA A 1 97  ? -0.699  -73.752 -1.940  1.00 106.36 ? 96   ALA A C   1 
ATOM   766  O O   . ALA A 1 97  ? -0.421  -73.282 -0.835  1.00 103.54 ? 96   ALA A O   1 
ATOM   767  C CB  . ALA A 1 97  ? -2.426  -75.511 -2.431  1.00 97.06  ? 96   ALA A CB  1 
ATOM   768  N N   . ALA A 1 98  ? -0.789  -73.009 -3.038  1.00 109.97 ? 97   ALA A N   1 
ATOM   769  C CA  . ALA A 1 98  ? -0.576  -71.566 -3.009  1.00 103.42 ? 97   ALA A CA  1 
ATOM   770  C C   . ALA A 1 98  ? -1.857  -70.815 -3.342  1.00 106.88 ? 97   ALA A C   1 
ATOM   771  O O   . ALA A 1 98  ? -2.557  -71.142 -4.303  1.00 110.83 ? 97   ALA A O   1 
ATOM   772  C CB  . ALA A 1 98  ? 0.534   -71.170 -3.974  1.00 89.91  ? 97   ALA A CB  1 
ATOM   773  N N   . HIS A 1 99  ? -2.163  -69.811 -2.533  1.00 101.71 ? 98   HIS A N   1 
ATOM   774  C CA  . HIS A 1 99  ? -3.293  -68.941 -2.800  1.00 103.54 ? 98   HIS A CA  1 
ATOM   775  C C   . HIS A 1 99  ? -2.746  -67.539 -2.979  1.00 100.84 ? 98   HIS A C   1 
ATOM   776  O O   . HIS A 1 99  ? -2.309  -66.903 -2.024  1.00 111.39 ? 98   HIS A O   1 
ATOM   777  C CB  . HIS A 1 99  ? -4.307  -69.008 -1.661  1.00 104.82 ? 98   HIS A CB  1 
ATOM   778  C CG  . HIS A 1 99  ? -4.905  -70.365 -1.475  1.00 106.79 ? 98   HIS A CG  1 
ATOM   779  N ND1 . HIS A 1 99  ? -6.104  -70.735 -2.047  1.00 117.66 ? 98   HIS A ND1 1 
ATOM   780  C CD2 . HIS A 1 99  ? -4.461  -71.450 -0.797  1.00 102.02 ? 98   HIS A CD2 1 
ATOM   781  C CE1 . HIS A 1 99  ? -6.378  -71.985 -1.719  1.00 111.53 ? 98   HIS A CE1 1 
ATOM   782  N NE2 . HIS A 1 99  ? -5.395  -72.442 -0.962  1.00 105.25 ? 98   HIS A NE2 1 
ATOM   783  N N   . LEU A 1 100 ? -2.759  -67.072 -4.221  1.00 97.75  ? 99   LEU A N   1 
ATOM   784  C CA  . LEU A 1 100 ? -2.050  -65.862 -4.593  1.00 88.91  ? 99   LEU A CA  1 
ATOM   785  C C   . LEU A 1 100 ? -2.974  -64.662 -4.707  1.00 85.27  ? 99   LEU A C   1 
ATOM   786  O O   . LEU A 1 100 ? -3.834  -64.606 -5.582  1.00 94.01  ? 99   LEU A O   1 
ATOM   787  C CB  . LEU A 1 100 ? -1.309  -66.087 -5.909  1.00 92.77  ? 99   LEU A CB  1 
ATOM   788  C CG  . LEU A 1 100 ? -0.339  -67.268 -5.888  1.00 90.04  ? 99   LEU A CG  1 
ATOM   789  C CD1 . LEU A 1 100 ? 0.301   -67.472 -7.248  1.00 92.47  ? 99   LEU A CD1 1 
ATOM   790  C CD2 . LEU A 1 100 ? 0.720   -67.050 -4.832  1.00 78.44  ? 99   LEU A CD2 1 
ATOM   791  N N   . PHE A 1 101 ? -2.785  -63.703 -3.811  1.00 79.70  ? 100  PHE A N   1 
ATOM   792  C CA  . PHE A 1 101 ? -3.500  -62.438 -3.867  1.00 92.61  ? 100  PHE A CA  1 
ATOM   793  C C   . PHE A 1 101 ? -2.569  -61.289 -4.280  1.00 98.31  ? 100  PHE A C   1 
ATOM   794  O O   . PHE A 1 101 ? -1.678  -60.898 -3.518  1.00 93.87  ? 100  PHE A O   1 
ATOM   795  C CB  . PHE A 1 101 ? -4.089  -62.133 -2.499  1.00 93.47  ? 100  PHE A CB  1 
ATOM   796  C CG  . PHE A 1 101 ? -5.104  -63.115 -2.057  1.00 99.88  ? 100  PHE A CG  1 
ATOM   797  C CD1 . PHE A 1 101 ? -4.718  -64.338 -1.544  1.00 96.72  ? 100  PHE A CD1 1 
ATOM   798  C CD2 . PHE A 1 101 ? -6.453  -62.818 -2.145  1.00 103.82 ? 100  PHE A CD2 1 
ATOM   799  C CE1 . PHE A 1 101 ? -5.651  -65.240 -1.139  1.00 92.98  ? 100  PHE A CE1 1 
ATOM   800  C CE2 . PHE A 1 101 ? -7.396  -63.723 -1.733  1.00 90.99  ? 100  PHE A CE2 1 
ATOM   801  C CZ  . PHE A 1 101 ? -6.994  -64.934 -1.231  1.00 95.02  ? 100  PHE A CZ  1 
ATOM   802  N N   . PHE A 1 102 ? -2.784  -60.735 -5.470  1.00 101.54 ? 101  PHE A N   1 
ATOM   803  C CA  . PHE A 1 102 ? -1.919  -59.666 -5.966  1.00 97.53  ? 101  PHE A CA  1 
ATOM   804  C C   . PHE A 1 102 ? -2.395  -58.270 -5.583  1.00 101.95 ? 101  PHE A C   1 
ATOM   805  O O   . PHE A 1 102 ? -3.590  -57.968 -5.635  1.00 105.39 ? 101  PHE A O   1 
ATOM   806  C CB  . PHE A 1 102 ? -1.705  -59.795 -7.467  1.00 91.14  ? 101  PHE A CB  1 
ATOM   807  C CG  . PHE A 1 102 ? -0.854  -60.970 -7.845  1.00 98.08  ? 101  PHE A CG  1 
ATOM   808  C CD1 . PHE A 1 102 ? 0.448   -61.070 -7.386  1.00 103.15 ? 101  PHE A CD1 1 
ATOM   809  C CD2 . PHE A 1 102 ? -1.349  -61.976 -8.652  1.00 102.19 ? 101  PHE A CD2 1 
ATOM   810  C CE1 . PHE A 1 102 ? 1.244   -62.151 -7.734  1.00 102.76 ? 101  PHE A CE1 1 
ATOM   811  C CE2 . PHE A 1 102 ? -0.559  -63.061 -9.004  1.00 99.63  ? 101  PHE A CE2 1 
ATOM   812  C CZ  . PHE A 1 102 ? 0.736   -63.151 -8.545  1.00 95.15  ? 101  PHE A CZ  1 
ATOM   813  N N   . LEU A 1 103 ? -1.437  -57.432 -5.190  1.00 106.08 ? 102  LEU A N   1 
ATOM   814  C CA  . LEU A 1 103 ? -1.714  -56.114 -4.625  1.00 103.01 ? 102  LEU A CA  1 
ATOM   815  C C   . LEU A 1 103 ? -2.313  -55.140 -5.642  1.00 106.45 ? 102  LEU A C   1 
ATOM   816  O O   . LEU A 1 103 ? -3.139  -54.295 -5.291  1.00 106.69 ? 102  LEU A O   1 
ATOM   817  C CB  . LEU A 1 103 ? -0.440  -55.539 -4.025  1.00 104.88 ? 102  LEU A CB  1 
ATOM   818  C CG  . LEU A 1 103 ? 0.171   -56.370 -2.905  1.00 102.24 ? 102  LEU A CG  1 
ATOM   819  C CD1 . LEU A 1 103 ? 1.352   -55.630 -2.293  1.00 110.36 ? 102  LEU A CD1 1 
ATOM   820  C CD2 . LEU A 1 103 ? -0.882  -56.631 -1.864  1.00 97.60  ? 102  LEU A CD2 1 
ATOM   821  N N   . SER A 1 104 ? -1.875  -55.249 -6.892  1.00 100.79 ? 103  SER A N   1 
ATOM   822  C CA  . SER A 1 104 ? -2.588  -54.644 -8.012  1.00 107.34 ? 103  SER A CA  1 
ATOM   823  C C   . SER A 1 104 ? -2.483  -55.590 -9.224  1.00 117.46 ? 103  SER A C   1 
ATOM   824  O O   . SER A 1 104 ? -1.752  -56.572 -9.170  1.00 115.73 ? 103  SER A O   1 
ATOM   825  C CB  . SER A 1 104 ? -2.072  -53.227 -8.306  1.00 98.77  ? 103  SER A CB  1 
ATOM   826  O OG  . SER A 1 104 ? -0.661  -53.148 -8.195  1.00 97.85  ? 103  SER A OG  1 
ATOM   827  N N   . PRO A 1 105 ? -3.239  -55.320 -10.302 1.00 121.94 ? 104  PRO A N   1 
ATOM   828  C CA  . PRO A 1 105 ? -3.259  -56.160 -11.510 1.00 116.35 ? 104  PRO A CA  1 
ATOM   829  C C   . PRO A 1 105 ? -1.909  -56.699 -12.012 1.00 114.61 ? 104  PRO A C   1 
ATOM   830  O O   . PRO A 1 105 ? -0.918  -55.978 -12.075 1.00 117.49 ? 104  PRO A O   1 
ATOM   831  C CB  . PRO A 1 105 ? -3.888  -55.235 -12.546 1.00 112.29 ? 104  PRO A CB  1 
ATOM   832  C CG  . PRO A 1 105 ? -4.882  -54.452 -11.742 1.00 115.41 ? 104  PRO A CG  1 
ATOM   833  C CD  . PRO A 1 105 ? -4.251  -54.248 -10.380 1.00 123.11 ? 104  PRO A CD  1 
ATOM   834  N N   . VAL A 1 106 ? -1.908  -57.976 -12.385 1.00 120.60 ? 105  VAL A N   1 
ATOM   835  C CA  . VAL A 1 106 ? -0.720  -58.688 -12.857 1.00 127.36 ? 105  VAL A CA  1 
ATOM   836  C C   . VAL A 1 106 ? -0.620  -58.720 -14.385 1.00 134.82 ? 105  VAL A C   1 
ATOM   837  O O   . VAL A 1 106 ? -1.557  -59.138 -15.068 1.00 133.36 ? 105  VAL A O   1 
ATOM   838  C CB  . VAL A 1 106 ? -0.696  -60.147 -12.320 1.00 115.63 ? 105  VAL A CB  1 
ATOM   839  C CG1 . VAL A 1 106 ? -2.113  -60.681 -12.143 1.00 109.06 ? 105  VAL A CG1 1 
ATOM   840  C CG2 . VAL A 1 106 ? 0.127   -61.059 -13.236 1.00 112.34 ? 105  VAL A CG2 1 
ATOM   841  N N   . PRO A 1 107 ? 0.529   -58.282 -14.923 1.00 139.83 ? 106  PRO A N   1 
ATOM   842  C CA  . PRO A 1 107 ? 0.784   -58.249 -16.366 1.00 140.08 ? 106  PRO A CA  1 
ATOM   843  C C   . PRO A 1 107 ? 0.708   -59.642 -16.975 1.00 136.47 ? 106  PRO A C   1 
ATOM   844  O O   . PRO A 1 107 ? 0.820   -60.632 -16.251 1.00 126.08 ? 106  PRO A O   1 
ATOM   845  C CB  . PRO A 1 107 ? 2.219   -57.716 -16.458 1.00 142.31 ? 106  PRO A CB  1 
ATOM   846  C CG  . PRO A 1 107 ? 2.443   -56.994 -15.185 1.00 142.07 ? 106  PRO A CG  1 
ATOM   847  C CD  . PRO A 1 107 ? 1.670   -57.761 -14.154 1.00 141.73 ? 106  PRO A CD  1 
ATOM   848  N N   . ASP A 1 108 ? 0.534   -59.708 -18.291 1.00 145.46 ? 107  ASP A N   1 
ATOM   849  C CA  . ASP A 1 108 ? 0.364   -60.982 -18.983 1.00 157.60 ? 107  ASP A CA  1 
ATOM   850  C C   . ASP A 1 108 ? 1.682   -61.733 -19.142 1.00 151.50 ? 107  ASP A C   1 
ATOM   851  O O   . ASP A 1 108 ? 1.718   -62.966 -19.075 1.00 142.08 ? 107  ASP A O   1 
ATOM   852  C CB  . ASP A 1 108 ? -0.275  -60.763 -20.357 1.00 169.54 ? 107  ASP A CB  1 
ATOM   853  C CG  . ASP A 1 108 ? -1.619  -60.066 -20.272 1.00 173.93 ? 107  ASP A CG  1 
ATOM   854  O OD1 . ASP A 1 108 ? -2.193  -60.004 -19.163 1.00 173.31 ? 107  ASP A OD1 1 
ATOM   855  O OD2 . ASP A 1 108 ? -2.099  -59.582 -21.318 1.00 175.68 ? 107  ASP A OD2 1 
ATOM   856  N N   . ALA A 1 109 ? 2.761   -60.988 -19.364 1.00 149.78 ? 108  ALA A N   1 
ATOM   857  C CA  . ALA A 1 109 ? 4.071   -61.595 -19.550 1.00 146.93 ? 108  ALA A CA  1 
ATOM   858  C C   . ALA A 1 109 ? 4.445   -62.420 -18.325 1.00 141.06 ? 108  ALA A C   1 
ATOM   859  O O   . ALA A 1 109 ? 5.063   -63.479 -18.445 1.00 136.07 ? 108  ALA A O   1 
ATOM   860  C CB  . ALA A 1 109 ? 5.119   -60.529 -19.822 1.00 145.68 ? 108  ALA A CB  1 
ATOM   861  N N   . LEU A 1 110 ? 4.053   -61.928 -17.151 1.00 141.08 ? 109  LEU A N   1 
ATOM   862  C CA  . LEU A 1 110 ? 4.323   -62.607 -15.885 1.00 142.27 ? 109  LEU A CA  1 
ATOM   863  C C   . LEU A 1 110 ? 3.366   -63.773 -15.680 1.00 143.25 ? 109  LEU A C   1 
ATOM   864  O O   . LEU A 1 110 ? 3.772   -64.855 -15.250 1.00 139.21 ? 109  LEU A O   1 
ATOM   865  C CB  . LEU A 1 110 ? 4.223   -61.630 -14.709 1.00 141.99 ? 109  LEU A CB  1 
ATOM   866  C CG  . LEU A 1 110 ? 5.367   -60.621 -14.539 1.00 150.02 ? 109  LEU A CG  1 
ATOM   867  C CD1 . LEU A 1 110 ? 6.692   -61.355 -14.372 1.00 153.56 ? 109  LEU A CD1 1 
ATOM   868  C CD2 . LEU A 1 110 ? 5.441   -59.620 -15.701 1.00 150.67 ? 109  LEU A CD2 1 
ATOM   869  N N   . MET A 1 111 ? 2.093   -63.544 -15.994 1.00 143.04 ? 110  MET A N   1 
ATOM   870  C CA  . MET A 1 111 ? 1.082   -64.590 -15.919 1.00 135.39 ? 110  MET A CA  1 
ATOM   871  C C   . MET A 1 111 ? 1.576   -65.823 -16.676 1.00 133.04 ? 110  MET A C   1 
ATOM   872  O O   . MET A 1 111 ? 1.478   -66.946 -16.181 1.00 131.65 ? 110  MET A O   1 
ATOM   873  C CB  . MET A 1 111 ? -0.258  -64.090 -16.477 1.00 136.82 ? 110  MET A CB  1 
ATOM   874  C CG  . MET A 1 111 ? -1.497  -64.808 -15.921 1.00 142.21 ? 110  MET A CG  1 
ATOM   875  S SD  . MET A 1 111 ? -2.616  -63.761 -14.947 1.00 136.12 ? 110  MET A SD  1 
ATOM   876  C CE  . MET A 1 111 ? -2.809  -62.358 -16.058 1.00 107.77 ? 110  MET A CE  1 
ATOM   877  N N   . ALA A 1 112 ? 2.132   -65.604 -17.864 1.00 134.76 ? 111  ALA A N   1 
ATOM   878  C CA  . ALA A 1 112 ? 2.692   -66.694 -18.658 1.00 140.47 ? 111  ALA A CA  1 
ATOM   879  C C   . ALA A 1 112 ? 3.823   -67.414 -17.925 1.00 147.80 ? 111  ALA A C   1 
ATOM   880  O O   . ALA A 1 112 ? 3.826   -68.639 -17.842 1.00 153.98 ? 111  ALA A O   1 
ATOM   881  C CB  . ALA A 1 112 ? 3.172   -66.187 -20.007 1.00 140.51 ? 111  ALA A CB  1 
ATOM   882  N N   . LYS A 1 113 ? 4.778   -66.656 -17.393 1.00 149.64 ? 112  LYS A N   1 
ATOM   883  C CA  . LYS A 1 113 ? 5.923   -67.251 -16.701 1.00 149.65 ? 112  LYS A CA  1 
ATOM   884  C C   . LYS A 1 113 ? 5.486   -68.239 -15.623 1.00 149.35 ? 112  LYS A C   1 
ATOM   885  O O   . LYS A 1 113 ? 6.146   -69.256 -15.397 1.00 149.97 ? 112  LYS A O   1 
ATOM   886  C CB  . LYS A 1 113 ? 6.824   -66.171 -16.089 1.00 143.40 ? 112  LYS A CB  1 
ATOM   887  C CG  . LYS A 1 113 ? 8.083   -66.721 -15.421 1.00 138.77 ? 112  LYS A CG  1 
ATOM   888  C CD  . LYS A 1 113 ? 9.094   -65.618 -15.139 1.00 138.24 ? 112  LYS A CD  1 
ATOM   889  C CE  . LYS A 1 113 ? 10.427  -66.190 -14.676 1.00 138.67 ? 112  LYS A CE  1 
ATOM   890  N NZ  . LYS A 1 113 ? 11.512  -65.166 -14.715 1.00 139.34 ? 112  LYS A NZ  1 
ATOM   891  N N   . LEU A 1 114 ? 4.371   -67.929 -14.966 1.00 144.78 ? 113  LEU A N   1 
ATOM   892  C CA  . LEU A 1 114 ? 3.816   -68.779 -13.918 1.00 132.34 ? 113  LEU A CA  1 
ATOM   893  C C   . LEU A 1 114 ? 3.168   -70.021 -14.521 1.00 127.26 ? 113  LEU A C   1 
ATOM   894  O O   . LEU A 1 114 ? 3.292   -71.121 -13.984 1.00 120.82 ? 113  LEU A O   1 
ATOM   895  C CB  . LEU A 1 114 ? 2.772   -68.008 -13.104 1.00 124.61 ? 113  LEU A CB  1 
ATOM   896  C CG  . LEU A 1 114 ? 2.627   -68.296 -11.603 1.00 110.64 ? 113  LEU A CG  1 
ATOM   897  C CD1 . LEU A 1 114 ? 1.219   -67.968 -11.126 1.00 95.43  ? 113  LEU A CD1 1 
ATOM   898  C CD2 . LEU A 1 114 ? 2.962   -69.732 -11.277 1.00 113.98 ? 113  LEU A CD2 1 
ATOM   899  N N   . ALA A 1 115 ? 2.472   -69.834 -15.639 1.00 127.51 ? 114  ALA A N   1 
ATOM   900  C CA  . ALA A 1 115 ? 1.753   -70.925 -16.295 1.00 122.84 ? 114  ALA A CA  1 
ATOM   901  C C   . ALA A 1 115 ? 2.681   -72.031 -16.806 1.00 132.57 ? 114  ALA A C   1 
ATOM   902  O O   . ALA A 1 115 ? 2.296   -73.202 -16.842 1.00 138.33 ? 114  ALA A O   1 
ATOM   903  C CB  . ALA A 1 115 ? 0.885   -70.385 -17.430 1.00 111.91 ? 114  ALA A CB  1 
ATOM   904  N N   . SER A 1 116 ? 3.899   -71.660 -17.196 1.00 133.64 ? 115  SER A N   1 
ATOM   905  C CA  . SER A 1 116 ? 4.846   -72.623 -17.756 1.00 137.33 ? 115  SER A CA  1 
ATOM   906  C C   . SER A 1 116 ? 5.587   -73.413 -16.678 1.00 135.33 ? 115  SER A C   1 
ATOM   907  O O   . SER A 1 116 ? 5.927   -74.577 -16.877 1.00 138.75 ? 115  SER A O   1 
ATOM   908  C CB  . SER A 1 116 ? 5.849   -71.927 -18.680 1.00 143.50 ? 115  SER A CB  1 
ATOM   909  O OG  . SER A 1 116 ? 6.682   -71.041 -17.955 1.00 149.56 ? 115  SER A OG  1 
ATOM   910  N N   . ALA A 1 117 ? 5.832   -72.776 -15.539 1.00 134.16 ? 116  ALA A N   1 
ATOM   911  C CA  . ALA A 1 117 ? 6.536   -73.422 -14.433 1.00 133.98 ? 116  ALA A CA  1 
ATOM   912  C C   . ALA A 1 117 ? 5.645   -74.424 -13.702 1.00 130.51 ? 116  ALA A C   1 
ATOM   913  O O   . ALA A 1 117 ? 4.418   -74.336 -13.761 1.00 129.80 ? 116  ALA A O   1 
ATOM   914  C CB  . ALA A 1 117 ? 7.078   -72.377 -13.458 1.00 129.93 ? 116  ALA A CB  1 
ATOM   915  N N   . LYS A 1 118 ? 6.269   -75.368 -13.005 1.00 127.10 ? 117  LYS A N   1 
ATOM   916  C CA  . LYS A 1 118 ? 5.533   -76.396 -12.274 1.00 127.77 ? 117  LYS A CA  1 
ATOM   917  C C   . LYS A 1 118 ? 4.448   -75.804 -11.372 1.00 130.57 ? 117  LYS A C   1 
ATOM   918  O O   . LYS A 1 118 ? 3.339   -76.339 -11.285 1.00 125.04 ? 117  LYS A O   1 
ATOM   919  C CB  . LYS A 1 118 ? 6.490   -77.259 -11.441 1.00 121.96 ? 117  LYS A CB  1 
ATOM   920  C CG  . LYS A 1 118 ? 5.791   -78.321 -10.594 1.00 114.38 ? 117  LYS A CG  1 
ATOM   921  C CD  . LYS A 1 118 ? 6.776   -79.165 -9.796  1.00 112.49 ? 117  LYS A CD  1 
ATOM   922  C CE  . LYS A 1 118 ? 6.056   -80.295 -9.068  1.00 118.25 ? 117  LYS A CE  1 
ATOM   923  N NZ  . LYS A 1 118 ? 6.983   -81.218 -8.355  1.00 122.54 ? 117  LYS A NZ  1 
ATOM   924  N N   . ALA A 1 119 ? 4.776   -74.699 -10.707 1.00 127.10 ? 118  ALA A N   1 
ATOM   925  C CA  . ALA A 1 119 ? 3.887   -74.092 -9.719  1.00 118.18 ? 118  ALA A CA  1 
ATOM   926  C C   . ALA A 1 119 ? 2.411   -74.045 -10.136 1.00 120.25 ? 118  ALA A C   1 
ATOM   927  O O   . ALA A 1 119 ? 1.521   -74.038 -9.282  1.00 116.31 ? 118  ALA A O   1 
ATOM   928  C CB  . ALA A 1 119 ? 4.380   -72.707 -9.356  1.00 106.65 ? 118  ALA A CB  1 
ATOM   929  N N   . VAL A 1 120 ? 2.151   -74.023 -11.441 1.00 116.44 ? 119  VAL A N   1 
ATOM   930  C CA  . VAL A 1 120 ? 0.790   -73.852 -11.934 1.00 109.17 ? 119  VAL A CA  1 
ATOM   931  C C   . VAL A 1 120 ? -0.198  -74.843 -11.308 1.00 115.32 ? 119  VAL A C   1 
ATOM   932  O O   . VAL A 1 120 ? -1.324  -74.473 -10.966 1.00 117.53 ? 119  VAL A O   1 
ATOM   933  C CB  . VAL A 1 120 ? 0.732   -73.901 -13.476 1.00 117.67 ? 119  VAL A CB  1 
ATOM   934  C CG1 . VAL A 1 120 ? 1.447   -75.130 -14.006 1.00 126.88 ? 119  VAL A CG1 1 
ATOM   935  C CG2 . VAL A 1 120 ? -0.711  -73.850 -13.966 1.00 120.43 ? 119  VAL A CG2 1 
ATOM   936  N N   . LYS A 1 121 ? 0.236   -76.090 -11.137 1.00 119.22 ? 120  LYS A N   1 
ATOM   937  C CA  . LYS A 1 121 ? -0.625  -77.151 -10.616 1.00 118.30 ? 120  LYS A CA  1 
ATOM   938  C C   . LYS A 1 121 ? -1.091  -76.888 -9.189  1.00 117.19 ? 120  LYS A C   1 
ATOM   939  O O   . LYS A 1 121 ? -2.166  -77.338 -8.791  1.00 109.80 ? 120  LYS A O   1 
ATOM   940  C CB  . LYS A 1 121 ? 0.092   -78.501 -10.680 1.00 132.20 ? 120  LYS A CB  1 
ATOM   941  C CG  . LYS A 1 121 ? -0.712  -79.655 -10.085 1.00 147.64 ? 120  LYS A CG  1 
ATOM   942  C CD  . LYS A 1 121 ? 0.029   -80.982 -10.175 1.00 154.65 ? 120  LYS A CD  1 
ATOM   943  C CE  . LYS A 1 121 ? -0.779  -82.098 -9.531  1.00 160.44 ? 120  LYS A CE  1 
ATOM   944  N NZ  . LYS A 1 121 ? -0.199  -83.447 -9.792  1.00 167.83 ? 120  LYS A NZ  1 
ATOM   945  N N   . TYR A 1 122 ? -0.276  -76.151 -8.434  1.00 128.71 ? 121  TYR A N   1 
ATOM   946  C CA  . TYR A 1 122 ? -0.514  -75.885 -7.012  1.00 125.52 ? 121  TYR A CA  1 
ATOM   947  C C   . TYR A 1 122 ? -1.345  -74.627 -6.736  1.00 114.94 ? 121  TYR A C   1 
ATOM   948  O O   . TYR A 1 122 ? -1.881  -74.456 -5.641  1.00 108.21 ? 121  TYR A O   1 
ATOM   949  C CB  . TYR A 1 122 ? 0.819   -75.749 -6.267  1.00 124.81 ? 121  TYR A CB  1 
ATOM   950  C CG  . TYR A 1 122 ? 1.657   -77.007 -6.190  1.00 126.20 ? 121  TYR A CG  1 
ATOM   951  C CD1 . TYR A 1 122 ? 1.526   -77.892 -5.123  1.00 121.57 ? 121  TYR A CD1 1 
ATOM   952  C CD2 . TYR A 1 122 ? 2.599   -77.294 -7.166  1.00 132.62 ? 121  TYR A CD2 1 
ATOM   953  C CE1 . TYR A 1 122 ? 2.304   -79.035 -5.041  1.00 124.09 ? 121  TYR A CE1 1 
ATOM   954  C CE2 . TYR A 1 122 ? 3.376   -78.435 -7.096  1.00 138.36 ? 121  TYR A CE2 1 
ATOM   955  C CZ  . TYR A 1 122 ? 3.226   -79.302 -6.034  1.00 134.56 ? 121  TYR A CZ  1 
ATOM   956  O OH  . TYR A 1 122 ? 4.006   -80.436 -5.974  1.00 135.53 ? 121  TYR A OH  1 
ATOM   957  N N   . VAL A 1 123 ? -1.440  -73.731 -7.708  1.00 113.41 ? 122  VAL A N   1 
ATOM   958  C CA  . VAL A 1 123 ? -2.124  -72.469 -7.446  1.00 116.50 ? 122  VAL A CA  1 
ATOM   959  C C   . VAL A 1 123 ? -3.647  -72.620 -7.511  1.00 109.18 ? 122  VAL A C   1 
ATOM   960  O O   . VAL A 1 123 ? -4.233  -72.772 -8.582  1.00 111.70 ? 122  VAL A O   1 
ATOM   961  C CB  . VAL A 1 123 ? -1.557  -71.276 -8.310  1.00 102.50 ? 122  VAL A CB  1 
ATOM   962  C CG1 . VAL A 1 123 ? -1.089  -71.759 -9.664  1.00 117.02 ? 122  VAL A CG1 1 
ATOM   963  C CG2 . VAL A 1 123 ? -2.566  -70.133 -8.445  1.00 92.78  ? 122  VAL A CG2 1 
ATOM   964  N N   . LYS A 1 124 ? -4.258  -72.615 -6.330  1.00 101.44 ? 123  LYS A N   1 
ATOM   965  C CA  . LYS A 1 124 ? -5.705  -72.604 -6.156  1.00 98.80  ? 123  LYS A CA  1 
ATOM   966  C C   . LYS A 1 124 ? -6.097  -71.181 -5.799  1.00 120.31 ? 123  LYS A C   1 
ATOM   967  O O   . LYS A 1 124 ? -5.500  -70.592 -4.895  1.00 134.96 ? 123  LYS A O   1 
ATOM   968  C CB  . LYS A 1 124 ? -6.079  -73.522 -4.996  1.00 92.40  ? 123  LYS A CB  1 
ATOM   969  C CG  . LYS A 1 124 ? -6.219  -75.003 -5.348  1.00 108.66 ? 123  LYS A CG  1 
ATOM   970  C CD  . LYS A 1 124 ? -4.906  -75.704 -5.692  1.00 116.09 ? 123  LYS A CD  1 
ATOM   971  C CE  . LYS A 1 124 ? -5.189  -77.133 -6.179  1.00 128.14 ? 123  LYS A CE  1 
ATOM   972  N NZ  . LYS A 1 124 ? -3.965  -77.941 -6.447  1.00 133.37 ? 123  LYS A NZ  1 
ATOM   973  N N   . THR A 1 125 ? -7.081  -70.616 -6.491  1.00 123.32 ? 124  THR A N   1 
ATOM   974  C CA  . THR A 1 125 ? -7.406  -69.186 -6.320  1.00 129.77 ? 124  THR A CA  1 
ATOM   975  C C   . THR A 1 125 ? -6.267  -68.214 -6.701  1.00 114.42 ? 124  THR A C   1 
ATOM   976  O O   . THR A 1 125 ? -5.096  -68.438 -6.385  1.00 101.72 ? 124  THR A O   1 
ATOM   977  C CB  . THR A 1 125 ? -7.883  -68.856 -4.872  1.00 150.73 ? 124  THR A CB  1 
ATOM   978  O OG1 . THR A 1 125 ? -9.126  -68.144 -4.923  1.00 168.16 ? 124  THR A OG1 1 
ATOM   979  C CG2 . THR A 1 125 ? -6.854  -68.002 -4.136  1.00 115.45 ? 124  THR A CG2 1 
ATOM   980  N N   . LEU A 1 126 ? -6.634  -67.129 -7.379  1.00 117.22 ? 125  LEU A N   1 
ATOM   981  C CA  . LEU A 1 126 ? -5.690  -66.075 -7.765  1.00 108.37 ? 125  LEU A CA  1 
ATOM   982  C C   . LEU A 1 126 ? -6.472  -64.801 -8.070  1.00 100.54 ? 125  LEU A C   1 
ATOM   983  O O   . LEU A 1 126 ? -7.109  -64.696 -9.115  1.00 97.05  ? 125  LEU A O   1 
ATOM   984  C CB  . LEU A 1 126 ? -4.861  -66.498 -8.984  1.00 112.10 ? 125  LEU A CB  1 
ATOM   985  C CG  . LEU A 1 126 ? -3.779  -65.570 -9.562  1.00 121.62 ? 125  LEU A CG  1 
ATOM   986  C CD1 . LEU A 1 126 ? -2.774  -66.355 -10.388 1.00 120.51 ? 125  LEU A CD1 1 
ATOM   987  C CD2 . LEU A 1 126 ? -4.361  -64.439 -10.403 1.00 125.52 ? 125  LEU A CD2 1 
ATOM   988  N N   . LYS A 1 127 ? -6.425  -63.836 -7.156  1.00 106.08 ? 126  LYS A N   1 
ATOM   989  C CA  . LYS A 1 127 ? -7.199  -62.605 -7.298  1.00 109.95 ? 126  LYS A CA  1 
ATOM   990  C C   . LYS A 1 127 ? -6.332  -61.337 -7.310  1.00 111.05 ? 126  LYS A C   1 
ATOM   991  O O   . LYS A 1 127 ? -5.119  -61.389 -7.088  1.00 102.97 ? 126  LYS A O   1 
ATOM   992  C CB  . LYS A 1 127 ? -8.248  -62.518 -6.186  1.00 106.77 ? 126  LYS A CB  1 
ATOM   993  C CG  . LYS A 1 127 ? -9.068  -63.791 -6.038  1.00 124.53 ? 126  LYS A CG  1 
ATOM   994  C CD  . LYS A 1 127 ? -10.042 -63.679 -4.885  1.00 133.14 ? 126  LYS A CD  1 
ATOM   995  C CE  . LYS A 1 127 ? -10.816 -64.961 -4.688  1.00 134.16 ? 126  LYS A CE  1 
ATOM   996  N NZ  . LYS A 1 127 ? -11.691 -64.844 -3.494  1.00 137.96 ? 126  LYS A NZ  1 
ATOM   997  N N   . GLU A 1 128 ? -6.977  -60.204 -7.588  1.00 106.95 ? 127  GLU A N   1 
ATOM   998  C CA  . GLU A 1 128 ? -6.335  -58.899 -7.569  1.00 96.43  ? 127  GLU A CA  1 
ATOM   999  C C   . GLU A 1 128 ? -7.053  -57.995 -6.569  1.00 110.27 ? 127  GLU A C   1 
ATOM   1000 O O   . GLU A 1 128 ? -8.108  -57.432 -6.865  1.00 121.05 ? 127  GLU A O   1 
ATOM   1001 C CB  . GLU A 1 128 ? -6.350  -58.273 -8.964  1.00 97.29  ? 127  GLU A CB  1 
ATOM   1002 C CG  . GLU A 1 128 ? -5.456  -58.985 -9.974  1.00 107.44 ? 127  GLU A CG  1 
ATOM   1003 C CD  . GLU A 1 128 ? -5.747  -58.576 -11.411 1.00 114.89 ? 127  GLU A CD  1 
ATOM   1004 O OE1 . GLU A 1 128 ? -6.602  -57.687 -11.609 1.00 118.29 ? 127  GLU A OE1 1 
ATOM   1005 O OE2 . GLU A 1 128 ? -5.125  -59.145 -12.341 1.00 111.86 ? 127  GLU A OE2 1 
ATOM   1006 N N   . ILE A 1 129 ? -6.457  -57.863 -5.388  1.00 107.96 ? 128  ILE A N   1 
ATOM   1007 C CA  . ILE A 1 129 ? -7.048  -57.176 -4.243  1.00 112.63 ? 128  ILE A CA  1 
ATOM   1008 C C   . ILE A 1 129 ? -7.281  -55.658 -4.377  1.00 120.20 ? 128  ILE A C   1 
ATOM   1009 O O   . ILE A 1 129 ? -8.200  -55.105 -3.761  1.00 123.47 ? 128  ILE A O   1 
ATOM   1010 C CB  . ILE A 1 129 ? -6.154  -57.410 -3.041  1.00 124.47 ? 128  ILE A CB  1 
ATOM   1011 C CG1 . ILE A 1 129 ? -6.274  -58.861 -2.600  1.00 134.24 ? 128  ILE A CG1 1 
ATOM   1012 C CG2 . ILE A 1 129 ? -6.508  -56.476 -1.916  1.00 131.30 ? 128  ILE A CG2 1 
ATOM   1013 C CD1 . ILE A 1 129 ? -5.420  -59.181 -1.416  1.00 144.50 ? 128  ILE A CD1 1 
ATOM   1014 N N   . ASN A 1 130 ? -6.441  -54.984 -5.160  1.00 113.38 ? 129  ASN A N   1 
ATOM   1015 C CA  . ASN A 1 130 ? -6.553  -53.533 -5.367  1.00 105.14 ? 129  ASN A CA  1 
ATOM   1016 C C   . ASN A 1 130 ? -6.376  -52.664 -4.130  1.00 93.07  ? 129  ASN A C   1 
ATOM   1017 O O   . ASN A 1 130 ? -7.115  -51.701 -3.917  1.00 87.77  ? 129  ASN A O   1 
ATOM   1018 C CB  . ASN A 1 130 ? -7.862  -53.179 -6.058  1.00 104.83 ? 129  ASN A CB  1 
ATOM   1019 C CG  . ASN A 1 130 ? -7.817  -53.463 -7.522  1.00 114.67 ? 129  ASN A CG  1 
ATOM   1020 O OD1 . ASN A 1 130 ? -6.753  -53.410 -8.138  1.00 123.29 ? 129  ASN A OD1 1 
ATOM   1021 N ND2 . ASN A 1 130 ? -8.968  -53.775 -8.100  1.00 119.33 ? 129  ASN A ND2 1 
ATOM   1022 N N   . THR A 1 131 ? -5.379  -53.002 -3.325  1.00 100.46 ? 130  THR A N   1 
ATOM   1023 C CA  . THR A 1 131 ? -5.061  -52.215 -2.148  1.00 93.40  ? 130  THR A CA  1 
ATOM   1024 C C   . THR A 1 131 ? -3.545  -52.181 -1.958  1.00 93.14  ? 130  THR A C   1 
ATOM   1025 O O   . THR A 1 131 ? -2.930  -53.188 -1.611  1.00 105.02 ? 130  THR A O   1 
ATOM   1026 C CB  . THR A 1 131 ? -5.750  -52.776 -0.880  1.00 95.93  ? 130  THR A CB  1 
ATOM   1027 O OG1 . THR A 1 131 ? -5.219  -54.068 -0.579  1.00 108.33 ? 130  THR A OG1 1 
ATOM   1028 C CG2 . THR A 1 131 ? -7.253  -52.908 -1.086  1.00 89.84  ? 130  THR A CG2 1 
ATOM   1029 N N   . LEU A 1 132 ? -2.938  -51.031 -2.229  1.00 84.01  ? 131  LEU A N   1 
ATOM   1030 C CA  . LEU A 1 132 ? -1.523  -50.849 -1.933  1.00 94.27  ? 131  LEU A CA  1 
ATOM   1031 C C   . LEU A 1 132 ? -1.243  -49.428 -1.434  1.00 93.21  ? 131  LEU A C   1 
ATOM   1032 O O   . LEU A 1 132 ? -0.546  -48.638 -2.067  1.00 83.11  ? 131  LEU A O   1 
ATOM   1033 C CB  . LEU A 1 132 ? -0.621  -51.260 -3.109  1.00 97.57  ? 131  LEU A CB  1 
ATOM   1034 C CG  . LEU A 1 132 ? -1.104  -51.132 -4.552  1.00 92.96  ? 131  LEU A CG  1 
ATOM   1035 C CD1 . LEU A 1 132 ? -1.524  -49.711 -4.845  1.00 95.49  ? 131  LEU A CD1 1 
ATOM   1036 C CD2 . LEU A 1 132 ? -0.023  -51.599 -5.529  1.00 85.03  ? 131  LEU A CD2 1 
ATOM   1037 N N   . PHE A 1 133 ? -1.822  -49.134 -0.279  1.00 91.54  ? 132  PHE A N   1 
ATOM   1038 C CA  . PHE A 1 133 ? -1.632  -47.880 0.410   1.00 84.25  ? 132  PHE A CA  1 
ATOM   1039 C C   . PHE A 1 133 ? -1.590  -48.220 1.902   1.00 85.52  ? 132  PHE A C   1 
ATOM   1040 O O   . PHE A 1 133 ? -2.371  -49.049 2.365   1.00 79.61  ? 132  PHE A O   1 
ATOM   1041 C CB  . PHE A 1 133 ? -2.780  -46.913 0.083   1.00 69.94  ? 132  PHE A CB  1 
ATOM   1042 C CG  . PHE A 1 133 ? -4.070  -47.217 0.803   1.00 75.35  ? 132  PHE A CG  1 
ATOM   1043 C CD1 . PHE A 1 133 ? -4.248  -46.855 2.125   1.00 78.73  ? 132  PHE A CD1 1 
ATOM   1044 C CD2 . PHE A 1 133 ? -5.115  -47.842 0.152   1.00 82.20  ? 132  PHE A CD2 1 
ATOM   1045 C CE1 . PHE A 1 133 ? -5.442  -47.129 2.789   1.00 77.83  ? 132  PHE A CE1 1 
ATOM   1046 C CE2 . PHE A 1 133 ? -6.306  -48.111 0.807   1.00 72.75  ? 132  PHE A CE2 1 
ATOM   1047 C CZ  . PHE A 1 133 ? -6.465  -47.749 2.127   1.00 73.49  ? 132  PHE A CZ  1 
ATOM   1048 N N   . ILE A 1 134 ? -0.676  -47.603 2.651   1.00 76.79  ? 133  ILE A N   1 
ATOM   1049 C CA  . ILE A 1 134 ? -0.539  -47.902 4.079   1.00 72.10  ? 133  ILE A CA  1 
ATOM   1050 C C   . ILE A 1 134 ? -1.604  -47.198 4.908   1.00 68.56  ? 133  ILE A C   1 
ATOM   1051 O O   . ILE A 1 134 ? -1.738  -45.988 4.847   1.00 72.17  ? 133  ILE A O   1 
ATOM   1052 C CB  . ILE A 1 134 ? 0.827   -47.486 4.627   1.00 69.34  ? 133  ILE A CB  1 
ATOM   1053 C CG1 . ILE A 1 134 ? 1.946   -47.971 3.713   1.00 69.67  ? 133  ILE A CG1 1 
ATOM   1054 C CG2 . ILE A 1 134 ? 1.010   -48.043 6.020   1.00 69.05  ? 133  ILE A CG2 1 
ATOM   1055 C CD1 . ILE A 1 134 ? 2.058   -49.477 3.669   1.00 81.77  ? 133  ILE A CD1 1 
ATOM   1056 N N   . PRO A 1 135 ? -2.384  -47.959 5.682   1.00 71.99  ? 134  PRO A N   1 
ATOM   1057 C CA  . PRO A 1 135 ? -3.338  -47.271 6.556   1.00 68.90  ? 134  PRO A CA  1 
ATOM   1058 C C   . PRO A 1 135 ? -2.689  -46.938 7.908   1.00 75.26  ? 134  PRO A C   1 
ATOM   1059 O O   . PRO A 1 135 ? -2.764  -47.768 8.822   1.00 77.61  ? 134  PRO A O   1 
ATOM   1060 C CB  . PRO A 1 135 ? -4.452  -48.304 6.716   1.00 71.28  ? 134  PRO A CB  1 
ATOM   1061 C CG  . PRO A 1 135 ? -3.757  -49.638 6.569   1.00 68.63  ? 134  PRO A CG  1 
ATOM   1062 C CD  . PRO A 1 135 ? -2.584  -49.424 5.656   1.00 70.99  ? 134  PRO A CD  1 
ATOM   1063 N N   . LYS A 1 136 ? -2.071  -45.754 8.015   1.00 74.66  ? 135  LYS A N   1 
ATOM   1064 C CA  . LYS A 1 136 ? -1.295  -45.333 9.196   1.00 77.79  ? 135  LYS A CA  1 
ATOM   1065 C C   . LYS A 1 136 ? -2.189  -45.049 10.394  1.00 77.91  ? 135  LYS A C   1 
ATOM   1066 O O   . LYS A 1 136 ? -1.863  -45.397 11.539  1.00 78.09  ? 135  LYS A O   1 
ATOM   1067 C CB  . LYS A 1 136 ? -0.489  -44.054 8.904   1.00 69.01  ? 135  LYS A CB  1 
ATOM   1068 C CG  . LYS A 1 136 ? 0.921   -44.225 8.353   1.00 61.02  ? 135  LYS A CG  1 
ATOM   1069 C CD  . LYS A 1 136 ? 1.830   -45.057 9.231   1.00 64.18  ? 135  LYS A CD  1 
ATOM   1070 C CE  . LYS A 1 136 ? 1.884   -44.569 10.654  1.00 72.72  ? 135  LYS A CE  1 
ATOM   1071 N NZ  . LYS A 1 136 ? 2.609   -45.545 11.519  1.00 80.59  ? 135  LYS A NZ  1 
ATOM   1072 N N   . GLU A 1 137 ? -3.297  -44.373 10.116  1.00 67.92  ? 136  GLU A N   1 
ATOM   1073 C CA  . GLU A 1 137 ? -4.278  -44.034 11.131  1.00 71.05  ? 136  GLU A CA  1 
ATOM   1074 C C   . GLU A 1 137 ? -5.670  -44.185 10.535  1.00 76.19  ? 136  GLU A C   1 
ATOM   1075 O O   . GLU A 1 137 ? -5.828  -44.209 9.313   1.00 83.06  ? 136  GLU A O   1 
ATOM   1076 C CB  . GLU A 1 137 ? -4.068  -42.597 11.616  1.00 65.28  ? 136  GLU A CB  1 
ATOM   1077 C CG  . GLU A 1 137 ? -2.726  -42.380 12.282  1.00 81.07  ? 136  GLU A CG  1 
ATOM   1078 C CD  . GLU A 1 137 ? -2.600  -41.027 12.940  1.00 79.57  ? 136  GLU A CD  1 
ATOM   1079 O OE1 . GLU A 1 137 ? -3.652  -40.416 13.226  1.00 69.50  ? 136  GLU A OE1 1 
ATOM   1080 O OE2 . GLU A 1 137 ? -1.445  -40.594 13.174  1.00 78.16  ? 136  GLU A OE2 1 
ATOM   1081 N N   . HIS A 1 138 ? -6.679  -44.279 11.390  1.00 69.27  ? 137  HIS A N   1 
ATOM   1082 C CA  . HIS A 1 138 ? -8.048  -44.262 10.910  1.00 76.44  ? 137  HIS A CA  1 
ATOM   1083 C C   . HIS A 1 138 ? -8.260  -43.271 9.751   1.00 76.26  ? 137  HIS A C   1 
ATOM   1084 O O   . HIS A 1 138 ? -8.903  -43.609 8.761   1.00 84.06  ? 137  HIS A O   1 
ATOM   1085 C CB  . HIS A 1 138 ? -9.015  -43.980 12.061  1.00 85.77  ? 137  HIS A CB  1 
ATOM   1086 C CG  . HIS A 1 138 ? -8.976  -45.015 13.140  1.00 101.34 ? 137  HIS A CG  1 
ATOM   1087 N ND1 . HIS A 1 138 ? -9.335  -46.329 12.925  1.00 100.70 ? 137  HIS A ND1 1 
ATOM   1088 C CD2 . HIS A 1 138 ? -8.619  -44.933 14.443  1.00 112.59 ? 137  HIS A CD2 1 
ATOM   1089 C CE1 . HIS A 1 138 ? -9.195  -47.012 14.046  1.00 101.81 ? 137  HIS A CE1 1 
ATOM   1090 N NE2 . HIS A 1 138 ? -8.767  -46.188 14.984  1.00 109.18 ? 137  HIS A NE2 1 
ATOM   1091 N N   . ARG A 1 139 ? -7.709  -42.063 9.861   1.00 69.76  ? 138  ARG A N   1 
ATOM   1092 C CA  . ARG A 1 139 ? -7.949  -41.032 8.846   1.00 73.51  ? 138  ARG A CA  1 
ATOM   1093 C C   . ARG A 1 139 ? -6.724  -40.652 8.033   1.00 69.04  ? 138  ARG A C   1 
ATOM   1094 O O   . ARG A 1 139 ? -6.788  -39.721 7.232   1.00 69.64  ? 138  ARG A O   1 
ATOM   1095 C CB  . ARG A 1 139 ? -8.546  -39.764 9.464   1.00 80.82  ? 138  ARG A CB  1 
ATOM   1096 C CG  . ARG A 1 139 ? -9.857  -39.991 10.182  1.00 77.16  ? 138  ARG A CG  1 
ATOM   1097 C CD  . ARG A 1 139 ? -10.731 -38.771 10.114  1.00 78.14  ? 138  ARG A CD  1 
ATOM   1098 N NE  . ARG A 1 139 ? -12.139 -39.130 9.941   1.00 77.75  ? 138  ARG A NE  1 
ATOM   1099 C CZ  . ARG A 1 139 ? -13.011 -39.184 10.942  1.00 84.32  ? 138  ARG A CZ  1 
ATOM   1100 N NH1 . ARG A 1 139 ? -12.632 -38.902 12.191  1.00 97.30  ? 138  ARG A NH1 1 
ATOM   1101 N NH2 . ARG A 1 139 ? -14.264 -39.514 10.700  1.00 81.31  ? 138  ARG A NH2 1 
ATOM   1102 N N   . VAL A 1 140 ? -5.618  -41.365 8.232   1.00 65.20  ? 139  VAL A N   1 
ATOM   1103 C CA  . VAL A 1 140 ? -4.383  -41.044 7.523   1.00 67.03  ? 139  VAL A CA  1 
ATOM   1104 C C   . VAL A 1 140 ? -3.863  -42.211 6.706   1.00 70.02  ? 139  VAL A C   1 
ATOM   1105 O O   . VAL A 1 140 ? -3.619  -43.297 7.238   1.00 72.01  ? 139  VAL A O   1 
ATOM   1106 C CB  . VAL A 1 140 ? -3.235  -40.607 8.473   1.00 68.47  ? 139  VAL A CB  1 
ATOM   1107 C CG1 . VAL A 1 140 ? -2.037  -40.123 7.651   1.00 59.88  ? 139  VAL A CG1 1 
ATOM   1108 C CG2 . VAL A 1 140 ? -3.696  -39.532 9.456   1.00 53.73  ? 139  VAL A CG2 1 
ATOM   1109 N N   . PHE A 1 141 ? -3.676  -41.966 5.414   1.00 69.47  ? 140  PHE A N   1 
ATOM   1110 C CA  . PHE A 1 141 ? -3.067  -42.944 4.529   1.00 60.40  ? 140  PHE A CA  1 
ATOM   1111 C C   . PHE A 1 141 ? -1.705  -42.472 4.051   1.00 67.11  ? 140  PHE A C   1 
ATOM   1112 O O   . PHE A 1 141 ? -1.437  -41.283 3.960   1.00 78.57  ? 140  PHE A O   1 
ATOM   1113 C CB  . PHE A 1 141 ? -3.988  -43.287 3.352   1.00 64.32  ? 140  PHE A CB  1 
ATOM   1114 C CG  . PHE A 1 141 ? -4.257  -42.142 2.426   1.00 63.60  ? 140  PHE A CG  1 
ATOM   1115 C CD1 . PHE A 1 141 ? -5.233  -41.206 2.728   1.00 65.93  ? 140  PHE A CD1 1 
ATOM   1116 C CD2 . PHE A 1 141 ? -3.553  -42.017 1.236   1.00 59.26  ? 140  PHE A CD2 1 
ATOM   1117 C CE1 . PHE A 1 141 ? -5.496  -40.144 1.869   1.00 69.59  ? 140  PHE A CE1 1 
ATOM   1118 C CE2 . PHE A 1 141 ? -3.810  -40.964 0.370   1.00 66.15  ? 140  PHE A CE2 1 
ATOM   1119 C CZ  . PHE A 1 141 ? -4.784  -40.022 0.689   1.00 68.50  ? 140  PHE A CZ  1 
ATOM   1120 N N   . THR A 1 142 ? -0.849  -43.428 3.740   1.00 74.84  ? 141  THR A N   1 
ATOM   1121 C CA  . THR A 1 142 ? 0.553   -43.177 3.516   1.00 66.85  ? 141  THR A CA  1 
ATOM   1122 C C   . THR A 1 142 ? 1.062   -44.120 2.431   1.00 72.15  ? 141  THR A C   1 
ATOM   1123 O O   . THR A 1 142 ? 0.495   -45.179 2.213   1.00 86.71  ? 141  THR A O   1 
ATOM   1124 C CB  . THR A 1 142 ? 1.298   -43.374 4.839   1.00 76.08  ? 141  THR A CB  1 
ATOM   1125 O OG1 . THR A 1 142 ? 1.513   -42.091 5.443   1.00 74.35  ? 141  THR A OG1 1 
ATOM   1126 C CG2 . THR A 1 142 ? 2.631   -44.088 4.649   1.00 82.40  ? 141  THR A CG2 1 
ATOM   1127 N N   . LEU A 1 143 ? 2.117   -43.734 1.733   1.00 69.56  ? 142  LEU A N   1 
ATOM   1128 C CA  . LEU A 1 143 ? 2.617   -44.519 0.613   1.00 65.15  ? 142  LEU A CA  1 
ATOM   1129 C C   . LEU A 1 143 ? 3.934   -45.205 0.949   1.00 70.08  ? 142  LEU A C   1 
ATOM   1130 O O   . LEU A 1 143 ? 4.553   -45.853 0.101   1.00 67.26  ? 142  LEU A O   1 
ATOM   1131 C CB  . LEU A 1 143 ? 2.781   -43.629 -0.613  1.00 59.94  ? 142  LEU A CB  1 
ATOM   1132 C CG  . LEU A 1 143 ? 1.617   -43.545 -1.599  1.00 61.87  ? 142  LEU A CG  1 
ATOM   1133 C CD1 . LEU A 1 143 ? 0.322   -43.955 -0.976  1.00 55.64  ? 142  LEU A CD1 1 
ATOM   1134 C CD2 . LEU A 1 143 ? 1.505   -42.157 -2.193  1.00 68.95  ? 142  LEU A CD2 1 
ATOM   1135 N N   . ASN A 1 144 ? 4.359   -45.047 2.195   1.00 83.90  ? 143  ASN A N   1 
ATOM   1136 C CA  . ASN A 1 144 ? 5.576   -45.685 2.693   1.00 88.98  ? 143  ASN A CA  1 
ATOM   1137 C C   . ASN A 1 144 ? 6.840   -45.248 1.967   1.00 89.02  ? 143  ASN A C   1 
ATOM   1138 O O   . ASN A 1 144 ? 7.869   -45.919 2.020   1.00 94.99  ? 143  ASN A O   1 
ATOM   1139 C CB  . ASN A 1 144 ? 5.459   -47.208 2.656   1.00 86.85  ? 143  ASN A CB  1 
ATOM   1140 C CG  . ASN A 1 144 ? 6.518   -47.879 3.501   1.00 91.87  ? 143  ASN A CG  1 
ATOM   1141 O OD1 . ASN A 1 144 ? 7.060   -47.266 4.420   1.00 75.65  ? 143  ASN A OD1 1 
ATOM   1142 N ND2 . ASN A 1 144 ? 6.818   -49.143 3.201   1.00 106.54 ? 143  ASN A ND2 1 
ATOM   1143 N N   . GLU A 1 145 ? 6.740   -44.118 1.283   1.00 90.38  ? 144  GLU A N   1 
ATOM   1144 C CA  . GLU A 1 145 ? 7.856   -43.514 0.581   1.00 89.91  ? 144  GLU A CA  1 
ATOM   1145 C C   . GLU A 1 145 ? 8.394   -42.366 1.442   1.00 86.72  ? 144  GLU A C   1 
ATOM   1146 O O   . GLU A 1 145 ? 7.843   -41.272 1.428   1.00 70.94  ? 144  GLU A O   1 
ATOM   1147 C CB  . GLU A 1 145 ? 7.350   -42.972 -0.746  1.00 97.05  ? 144  GLU A CB  1 
ATOM   1148 C CG  . GLU A 1 145 ? 8.308   -43.137 -1.888  1.00 117.35 ? 144  GLU A CG  1 
ATOM   1149 C CD  . GLU A 1 145 ? 8.243   -44.516 -2.488  1.00 126.30 ? 144  GLU A CD  1 
ATOM   1150 O OE1 . GLU A 1 145 ? 8.747   -45.461 -1.850  1.00 127.42 ? 144  GLU A OE1 1 
ATOM   1151 O OE2 . GLU A 1 145 ? 7.691   -44.651 -3.601  1.00 134.60 ? 144  GLU A OE2 1 
ATOM   1152 N N   . PRO A 1 146 ? 9.467   -42.614 2.209   1.00 93.68  ? 145  PRO A N   1 
ATOM   1153 C CA  . PRO A 1 146 ? 9.937   -41.604 3.164   1.00 84.14  ? 145  PRO A CA  1 
ATOM   1154 C C   . PRO A 1 146 ? 10.695  -40.457 2.481   1.00 84.91  ? 145  PRO A C   1 
ATOM   1155 O O   . PRO A 1 146 ? 10.927  -39.408 3.094   1.00 89.17  ? 145  PRO A O   1 
ATOM   1156 C CB  . PRO A 1 146 ? 10.878  -42.397 4.088   1.00 81.98  ? 145  PRO A CB  1 
ATOM   1157 C CG  . PRO A 1 146 ? 11.072  -43.755 3.430   1.00 93.43  ? 145  PRO A CG  1 
ATOM   1158 C CD  . PRO A 1 146 ? 10.415  -43.731 2.083   1.00 96.32  ? 145  PRO A CD  1 
ATOM   1159 N N   . HIS A 1 147 ? 11.075  -40.666 1.224   1.00 79.75  ? 146  HIS A N   1 
ATOM   1160 C CA  . HIS A 1 147 ? 11.778  -39.653 0.455   1.00 77.05  ? 146  HIS A CA  1 
ATOM   1161 C C   . HIS A 1 147 ? 10.907  -39.134 -0.683  1.00 72.70  ? 146  HIS A C   1 
ATOM   1162 O O   . HIS A 1 147 ? 11.401  -38.531 -1.634  1.00 62.64  ? 146  HIS A O   1 
ATOM   1163 C CB  . HIS A 1 147 ? 13.114  -40.188 -0.069  1.00 85.50  ? 146  HIS A CB  1 
ATOM   1164 C CG  . HIS A 1 147 ? 14.186  -40.259 0.976   1.00 95.85  ? 146  HIS A CG  1 
ATOM   1165 N ND1 . HIS A 1 147 ? 14.718  -41.452 1.424   1.00 106.12 ? 146  HIS A ND1 1 
ATOM   1166 C CD2 . HIS A 1 147 ? 14.824  -39.281 1.664   1.00 85.89  ? 146  HIS A CD2 1 
ATOM   1167 C CE1 . HIS A 1 147 ? 15.634  -41.203 2.342   1.00 104.95 ? 146  HIS A CE1 1 
ATOM   1168 N NE2 . HIS A 1 147 ? 15.718  -39.893 2.507   1.00 83.79  ? 146  HIS A NE2 1 
ATOM   1169 N N   . GLY A 1 148 ? 9.603   -39.360 -0.562  1.00 71.47  ? 147  GLY A N   1 
ATOM   1170 C CA  . GLY A 1 148 ? 8.646   -38.905 -1.551  1.00 71.24  ? 147  GLY A CA  1 
ATOM   1171 C C   . GLY A 1 148 ? 8.881   -37.475 -2.008  1.00 73.87  ? 147  GLY A C   1 
ATOM   1172 O O   . GLY A 1 148 ? 8.943   -37.208 -3.208  1.00 70.73  ? 147  GLY A O   1 
ATOM   1173 N N   . LEU A 1 149 ? 9.003   -36.563 -1.046  1.00 66.96  ? 148  LEU A N   1 
ATOM   1174 C CA  . LEU A 1 149 ? 9.241   -35.148 -1.320  1.00 61.19  ? 148  LEU A CA  1 
ATOM   1175 C C   . LEU A 1 149 ? 10.411  -34.950 -2.287  1.00 69.43  ? 148  LEU A C   1 
ATOM   1176 O O   . LEU A 1 149 ? 10.307  -34.188 -3.249  1.00 74.14  ? 148  LEU A O   1 
ATOM   1177 C CB  . LEU A 1 149 ? 9.483   -34.399 -0.007  1.00 65.85  ? 148  LEU A CB  1 
ATOM   1178 C CG  . LEU A 1 149 ? 9.152   -32.915 0.194   1.00 60.11  ? 148  LEU A CG  1 
ATOM   1179 C CD1 . LEU A 1 149 ? 10.396  -32.072 0.084   1.00 65.56  ? 148  LEU A CD1 1 
ATOM   1180 C CD2 . LEU A 1 149 ? 8.049   -32.398 -0.726  1.00 59.86  ? 148  LEU A CD2 1 
ATOM   1181 N N   . VAL A 1 150 ? 11.513  -35.648 -2.042  1.00 63.60  ? 149  VAL A N   1 
ATOM   1182 C CA  . VAL A 1 150 ? 12.665  -35.559 -2.925  1.00 66.95  ? 149  VAL A CA  1 
ATOM   1183 C C   . VAL A 1 150 ? 12.408  -36.155 -4.316  1.00 76.01  ? 149  VAL A C   1 
ATOM   1184 O O   . VAL A 1 150 ? 12.641  -35.504 -5.330  1.00 82.79  ? 149  VAL A O   1 
ATOM   1185 C CB  . VAL A 1 150 ? 13.896  -36.225 -2.306  1.00 66.89  ? 149  VAL A CB  1 
ATOM   1186 C CG1 . VAL A 1 150 ? 14.998  -36.313 -3.330  1.00 61.27  ? 149  VAL A CG1 1 
ATOM   1187 C CG2 . VAL A 1 150 ? 14.355  -35.457 -1.077  1.00 62.97  ? 149  VAL A CG2 1 
ATOM   1188 N N   . GLN A 1 151 ? 11.934  -37.396 -4.360  1.00 76.33  ? 150  GLN A N   1 
ATOM   1189 C CA  . GLN A 1 151 ? 11.670  -38.084 -5.624  1.00 75.89  ? 150  GLN A CA  1 
ATOM   1190 C C   . GLN A 1 151 ? 10.709  -37.285 -6.526  1.00 78.87  ? 150  GLN A C   1 
ATOM   1191 O O   . GLN A 1 151 ? 10.710  -37.435 -7.750  1.00 82.97  ? 150  GLN A O   1 
ATOM   1192 C CB  . GLN A 1 151 ? 11.110  -39.494 -5.361  1.00 69.67  ? 150  GLN A CB  1 
ATOM   1193 C CG  . GLN A 1 151 ? 11.922  -40.353 -4.386  1.00 78.03  ? 150  GLN A CG  1 
ATOM   1194 C CD  . GLN A 1 151 ? 11.114  -41.540 -3.802  1.00 98.46  ? 150  GLN A CD  1 
ATOM   1195 O OE1 . GLN A 1 151 ? 9.941   -41.738 -4.130  1.00 84.87  ? 150  GLN A OE1 1 
ATOM   1196 N NE2 . GLN A 1 151 ? 11.749  -42.318 -2.928  1.00 97.89  ? 150  GLN A NE2 1 
ATOM   1197 N N   . TYR A 1 152 ? 9.897   -36.431 -5.919  1.00 72.05  ? 151  TYR A N   1 
ATOM   1198 C CA  . TYR A 1 152 ? 8.837   -35.756 -6.654  1.00 77.32  ? 151  TYR A CA  1 
ATOM   1199 C C   . TYR A 1 152 ? 9.139   -34.298 -7.014  1.00 81.82  ? 151  TYR A C   1 
ATOM   1200 O O   . TYR A 1 152 ? 8.740   -33.826 -8.082  1.00 90.65  ? 151  TYR A O   1 
ATOM   1201 C CB  . TYR A 1 152 ? 7.523   -35.838 -5.876  1.00 68.70  ? 151  TYR A CB  1 
ATOM   1202 C CG  . TYR A 1 152 ? 6.320   -35.394 -6.666  1.00 71.14  ? 151  TYR A CG  1 
ATOM   1203 C CD1 . TYR A 1 152 ? 5.614   -36.301 -7.456  1.00 79.02  ? 151  TYR A CD1 1 
ATOM   1204 C CD2 . TYR A 1 152 ? 5.886   -34.072 -6.629  1.00 65.92  ? 151  TYR A CD2 1 
ATOM   1205 C CE1 . TYR A 1 152 ? 4.509   -35.905 -8.187  1.00 81.38  ? 151  TYR A CE1 1 
ATOM   1206 C CE2 . TYR A 1 152 ? 4.781   -33.666 -7.357  1.00 77.14  ? 151  TYR A CE2 1 
ATOM   1207 C CZ  . TYR A 1 152 ? 4.096   -34.590 -8.135  1.00 87.25  ? 151  TYR A CZ  1 
ATOM   1208 O OH  . TYR A 1 152 ? 2.995   -34.201 -8.861  1.00 92.77  ? 151  TYR A OH  1 
ATOM   1209 N N   . TYR A 1 153 ? 9.817   -33.579 -6.125  1.00 70.48  ? 152  TYR A N   1 
ATOM   1210 C CA  . TYR A 1 153 ? 10.162  -32.185 -6.404  1.00 71.27  ? 152  TYR A CA  1 
ATOM   1211 C C   . TYR A 1 153 ? 11.679  -31.991 -6.540  1.00 73.98  ? 152  TYR A C   1 
ATOM   1212 O O   . TYR A 1 153 ? 12.149  -30.924 -6.953  1.00 66.30  ? 152  TYR A O   1 
ATOM   1213 C CB  . TYR A 1 153 ? 9.613   -31.233 -5.331  1.00 59.53  ? 152  TYR A CB  1 
ATOM   1214 C CG  . TYR A 1 153 ? 8.120   -31.256 -5.132  1.00 65.25  ? 152  TYR A CG  1 
ATOM   1215 C CD1 . TYR A 1 153 ? 7.263   -30.635 -6.033  1.00 63.23  ? 152  TYR A CD1 1 
ATOM   1216 C CD2 . TYR A 1 153 ? 7.563   -31.879 -4.014  1.00 67.07  ? 152  TYR A CD2 1 
ATOM   1217 C CE1 . TYR A 1 153 ? 5.887   -30.645 -5.836  1.00 65.52  ? 152  TYR A CE1 1 
ATOM   1218 C CE2 . TYR A 1 153 ? 6.197   -31.893 -3.804  1.00 60.35  ? 152  TYR A CE2 1 
ATOM   1219 C CZ  . TYR A 1 153 ? 5.363   -31.278 -4.717  1.00 70.20  ? 152  TYR A CZ  1 
ATOM   1220 O OH  . TYR A 1 153 ? 4.006   -31.300 -4.500  1.00 75.38  ? 152  TYR A OH  1 
ATOM   1221 N N   . GLY A 1 154 ? 12.436  -33.024 -6.191  1.00 74.81  ? 153  GLY A N   1 
ATOM   1222 C CA  . GLY A 1 154 ? 13.885  -32.955 -6.241  1.00 83.31  ? 153  GLY A CA  1 
ATOM   1223 C C   . GLY A 1 154 ? 14.451  -32.833 -7.645  1.00 84.64  ? 153  GLY A C   1 
ATOM   1224 O O   . GLY A 1 154 ? 13.707  -32.751 -8.627  1.00 87.73  ? 153  GLY A O   1 
ATOM   1225 N N   . SER A 1 155 ? 15.776  -32.828 -7.739  1.00 73.99  ? 154  SER A N   1 
ATOM   1226 C CA  . SER A 1 155 ? 16.450  -32.647 -9.020  1.00 88.37  ? 154  SER A CA  1 
ATOM   1227 C C   . SER A 1 155 ? 16.487  -33.927 -9.852  1.00 92.08  ? 154  SER A C   1 
ATOM   1228 O O   . SER A 1 155 ? 17.454  -34.180 -10.556 1.00 104.22 ? 154  SER A O   1 
ATOM   1229 C CB  . SER A 1 155 ? 17.874  -32.114 -8.814  1.00 100.00 ? 154  SER A CB  1 
ATOM   1230 O OG  . SER A 1 155 ? 18.743  -33.134 -8.349  1.00 105.04 ? 154  SER A OG  1 
ATOM   1231 N N   . ARG A 1 156 ? 15.437  -34.735 -9.749  1.00 98.55  ? 155  ARG A N   1 
ATOM   1232 C CA  . ARG A 1 156 ? 15.247  -35.905 -10.602 1.00 108.73 ? 155  ARG A CA  1 
ATOM   1233 C C   . ARG A 1 156 ? 13.747  -36.042 -10.845 1.00 101.81 ? 155  ARG A C   1 
ATOM   1234 O O   . ARG A 1 156 ? 13.295  -37.005 -11.458 1.00 91.61  ? 155  ARG A O   1 
ATOM   1235 C CB  . ARG A 1 156 ? 15.774  -37.184 -9.937  1.00 120.69 ? 155  ARG A CB  1 
ATOM   1236 C CG  . ARG A 1 156 ? 17.160  -37.086 -9.302  1.00 137.11 ? 155  ARG A CG  1 
ATOM   1237 C CD  . ARG A 1 156 ? 17.251  -37.935 -8.022  1.00 149.69 ? 155  ARG A CD  1 
ATOM   1238 N NE  . ARG A 1 156 ? 16.898  -39.338 -8.251  1.00 162.43 ? 155  ARG A NE  1 
ATOM   1239 C CZ  . ARG A 1 156 ? 16.566  -40.201 -7.291  1.00 164.36 ? 155  ARG A CZ  1 
ATOM   1240 N NH1 . ARG A 1 156 ? 16.533  -39.812 -6.022  1.00 163.03 ? 155  ARG A NH1 1 
ATOM   1241 N NH2 . ARG A 1 156 ? 16.262  -41.456 -7.602  1.00 163.99 ? 155  ARG A NH2 1 
ATOM   1242 N N   . SER A 1 157 ? 12.994  -35.060 -10.344 1.00 99.23  ? 156  SER A N   1 
ATOM   1243 C CA  . SER A 1 157 ? 11.531  -35.029 -10.409 1.00 92.54  ? 156  SER A CA  1 
ATOM   1244 C C   . SER A 1 157 ? 10.962  -35.344 -11.787 1.00 93.48  ? 156  SER A C   1 
ATOM   1245 O O   . SER A 1 157 ? 9.879   -35.921 -11.902 1.00 95.13  ? 156  SER A O   1 
ATOM   1246 C CB  . SER A 1 157 ? 11.012  -33.666 -9.945  1.00 91.60  ? 156  SER A CB  1 
ATOM   1247 O OG  . SER A 1 157 ? 11.476  -32.622 -10.788 1.00 102.04 ? 156  SER A OG  1 
ATOM   1248 N N   . SER A 1 158 ? 11.692  -34.952 -12.827 1.00 99.06  ? 157  SER A N   1 
ATOM   1249 C CA  . SER A 1 158 ? 11.298  -35.232 -14.203 1.00 107.41 ? 157  SER A CA  1 
ATOM   1250 C C   . SER A 1 158 ? 10.874  -36.696 -14.411 1.00 112.54 ? 157  SER A C   1 
ATOM   1251 O O   . SER A 1 158 ? 9.882   -36.971 -15.084 1.00 117.40 ? 157  SER A O   1 
ATOM   1252 C CB  . SER A 1 158 ? 12.438  -34.878 -15.163 1.00 108.67 ? 157  SER A CB  1 
ATOM   1253 O OG  . SER A 1 158 ? 13.521  -35.780 -15.019 1.00 110.51 ? 157  SER A OG  1 
ATOM   1254 N N   . SER A 1 159 ? 11.621  -37.629 -13.829 1.00 106.27 ? 158  SER A N   1 
ATOM   1255 C CA  . SER A 1 159 ? 11.375  -39.048 -14.061 1.00 105.59 ? 158  SER A CA  1 
ATOM   1256 C C   . SER A 1 159 ? 10.627  -39.756 -12.925 1.00 103.21 ? 158  SER A C   1 
ATOM   1257 O O   . SER A 1 159 ? 10.852  -40.944 -12.675 1.00 92.24  ? 158  SER A O   1 
ATOM   1258 C CB  . SER A 1 159 ? 12.695  -39.769 -14.350 1.00 108.65 ? 158  SER A CB  1 
ATOM   1259 O OG  . SER A 1 159 ? 13.632  -39.566 -13.308 1.00 107.98 ? 158  SER A OG  1 
ATOM   1260 N N   . TYR A 1 160 ? 9.712   -39.050 -12.266 1.00 100.69 ? 159  TYR A N   1 
ATOM   1261 C CA  . TYR A 1 160 ? 9.085   -39.606 -11.071 1.00 96.14  ? 159  TYR A CA  1 
ATOM   1262 C C   . TYR A 1 160 ? 8.260   -40.894 -11.250 1.00 98.78  ? 159  TYR A C   1 
ATOM   1263 O O   . TYR A 1 160 ? 8.262   -41.747 -10.358 1.00 105.46 ? 159  TYR A O   1 
ATOM   1264 C CB  . TYR A 1 160 ? 8.263   -38.560 -10.312 1.00 90.80  ? 159  TYR A CB  1 
ATOM   1265 C CG  . TYR A 1 160 ? 7.485   -39.188 -9.176  1.00 87.52  ? 159  TYR A CG  1 
ATOM   1266 C CD1 . TYR A 1 160 ? 8.132   -39.612 -8.023  1.00 83.40  ? 159  TYR A CD1 1 
ATOM   1267 C CD2 . TYR A 1 160 ? 6.116   -39.397 -9.273  1.00 78.35  ? 159  TYR A CD2 1 
ATOM   1268 C CE1 . TYR A 1 160 ? 7.440   -40.202 -6.998  1.00 74.85  ? 159  TYR A CE1 1 
ATOM   1269 C CE2 . TYR A 1 160 ? 5.415   -39.993 -8.250  1.00 71.85  ? 159  TYR A CE2 1 
ATOM   1270 C CZ  . TYR A 1 160 ? 6.082   -40.392 -7.113  1.00 73.62  ? 159  TYR A CZ  1 
ATOM   1271 O OH  . TYR A 1 160 ? 5.393   -40.989 -6.080  1.00 75.63  ? 159  TYR A OH  1 
ATOM   1272 N N   . ASN A 1 161 ? 7.565   -41.035 -12.379 1.00 90.12  ? 160  ASN A N   1 
ATOM   1273 C CA  . ASN A 1 161 ? 6.587   -42.133 -12.583 1.00 91.95  ? 160  ASN A CA  1 
ATOM   1274 C C   . ASN A 1 161 ? 5.263   -41.886 -11.876 1.00 86.95  ? 160  ASN A C   1 
ATOM   1275 O O   . ASN A 1 161 ? 4.945   -42.553 -10.884 1.00 78.81  ? 160  ASN A O   1 
ATOM   1276 C CB  . ASN A 1 161 ? 7.117   -43.530 -12.169 1.00 77.21  ? 160  ASN A CB  1 
ATOM   1277 C CG  . ASN A 1 161 ? 6.072   -44.663 -12.399 1.00 98.09  ? 160  ASN A CG  1 
ATOM   1278 O OD1 . ASN A 1 161 ? 5.016   -44.445 -13.001 1.00 92.96  ? 160  ASN A OD1 1 
ATOM   1279 N ND2 . ASN A 1 161 ? 6.377   -45.866 -11.913 1.00 91.09  ? 160  ASN A ND2 1 
ATOM   1280 N N   . ILE A 1 162 ? 4.477   -40.945 -12.384 1.00 90.71  ? 161  ILE A N   1 
ATOM   1281 C CA  . ILE A 1 162 ? 3.230   -40.637 -11.708 1.00 94.52  ? 161  ILE A CA  1 
ATOM   1282 C C   . ILE A 1 162 ? 2.159   -41.696 -11.985 1.00 97.82  ? 161  ILE A C   1 
ATOM   1283 O O   . ILE A 1 162 ? 1.068   -41.647 -11.418 1.00 94.66  ? 161  ILE A O   1 
ATOM   1284 C CB  . ILE A 1 162 ? 2.734   -39.198 -11.991 1.00 95.50  ? 161  ILE A CB  1 
ATOM   1285 C CG1 . ILE A 1 162 ? 1.806   -39.155 -13.192 1.00 100.76 ? 161  ILE A CG1 1 
ATOM   1286 C CG2 . ILE A 1 162 ? 3.909   -38.221 -12.136 1.00 85.64  ? 161  ILE A CG2 1 
ATOM   1287 C CD1 . ILE A 1 162 ? 1.070   -37.842 -13.281 1.00 111.25 ? 161  ILE A CD1 1 
ATOM   1288 N N   . ASP A 1 163 ? 2.491   -42.667 -12.837 1.00 108.24 ? 162  ASP A N   1 
ATOM   1289 C CA  . ASP A 1 163 ? 1.607   -43.806 -13.096 1.00 111.24 ? 162  ASP A CA  1 
ATOM   1290 C C   . ASP A 1 163 ? 1.366   -44.621 -11.821 1.00 107.22 ? 162  ASP A C   1 
ATOM   1291 O O   . ASP A 1 163 ? 0.245   -44.669 -11.310 1.00 104.92 ? 162  ASP A O   1 
ATOM   1292 C CB  . ASP A 1 163 ? 2.167   -44.709 -14.209 1.00 120.87 ? 162  ASP A CB  1 
ATOM   1293 C CG  . ASP A 1 163 ? 1.737   -44.267 -15.604 1.00 127.11 ? 162  ASP A CG  1 
ATOM   1294 O OD1 . ASP A 1 163 ? 1.062   -43.220 -15.705 1.00 134.88 ? 162  ASP A OD1 1 
ATOM   1295 O OD2 . ASP A 1 163 ? 2.076   -44.960 -16.597 1.00 117.26 ? 162  ASP A OD2 1 
ATOM   1296 N N   . HIS A 1 164 ? 2.419   -45.255 -11.310 1.00 101.91 ? 163  HIS A N   1 
ATOM   1297 C CA  . HIS A 1 164 ? 2.317   -46.058 -10.096 1.00 96.69  ? 163  HIS A CA  1 
ATOM   1298 C C   . HIS A 1 164 ? 1.708   -45.251 -8.950  1.00 98.05  ? 163  HIS A C   1 
ATOM   1299 O O   . HIS A 1 164 ? 1.119   -45.819 -8.026  1.00 96.05  ? 163  HIS A O   1 
ATOM   1300 C CB  . HIS A 1 164 ? 3.688   -46.615 -9.697  1.00 101.80 ? 163  HIS A CB  1 
ATOM   1301 C CG  . HIS A 1 164 ? 3.625   -47.696 -8.662  1.00 119.85 ? 163  HIS A CG  1 
ATOM   1302 N ND1 . HIS A 1 164 ? 3.144   -48.960 -8.933  1.00 132.67 ? 163  HIS A ND1 1 
ATOM   1303 C CD2 . HIS A 1 164 ? 3.992   -47.707 -7.358  1.00 123.90 ? 163  HIS A CD2 1 
ATOM   1304 C CE1 . HIS A 1 164 ? 3.210   -49.700 -7.839  1.00 133.18 ? 163  HIS A CE1 1 
ATOM   1305 N NE2 . HIS A 1 164 ? 3.722   -48.963 -6.869  1.00 131.12 ? 163  HIS A NE2 1 
ATOM   1306 N N   . LEU A 1 165 ? 1.842   -43.927 -9.019  1.00 90.96  ? 164  LEU A N   1 
ATOM   1307 C CA  . LEU A 1 165 ? 1.256   -43.052 -8.010  1.00 84.18  ? 164  LEU A CA  1 
ATOM   1308 C C   . LEU A 1 165 ? -0.253  -42.938 -8.165  1.00 85.85  ? 164  LEU A C   1 
ATOM   1309 O O   . LEU A 1 165 ? -0.993  -43.017 -7.186  1.00 84.90  ? 164  LEU A O   1 
ATOM   1310 C CB  . LEU A 1 165 ? 1.899   -41.669 -8.051  1.00 86.09  ? 164  LEU A CB  1 
ATOM   1311 C CG  . LEU A 1 165 ? 1.327   -40.600 -7.116  1.00 70.22  ? 164  LEU A CG  1 
ATOM   1312 C CD1 . LEU A 1 165 ? 1.081   -41.134 -5.718  1.00 65.47  ? 164  LEU A CD1 1 
ATOM   1313 C CD2 . LEU A 1 165 ? 2.261   -39.418 -7.076  1.00 67.04  ? 164  LEU A CD2 1 
ATOM   1314 N N   . VAL A 1 166 ? -0.709  -42.750 -9.397  1.00 92.21  ? 165  VAL A N   1 
ATOM   1315 C CA  . VAL A 1 166 ? -2.142  -42.697 -9.672  1.00 92.33  ? 165  VAL A CA  1 
ATOM   1316 C C   . VAL A 1 166 ? -2.855  -43.998 -9.298  1.00 92.49  ? 165  VAL A C   1 
ATOM   1317 O O   . VAL A 1 166 ? -3.945  -43.971 -8.728  1.00 85.51  ? 165  VAL A O   1 
ATOM   1318 C CB  . VAL A 1 166 ? -2.422  -42.365 -11.142 1.00 91.65  ? 165  VAL A CB  1 
ATOM   1319 C CG1 . VAL A 1 166 ? -3.891  -42.608 -11.472 1.00 89.20  ? 165  VAL A CG1 1 
ATOM   1320 C CG2 . VAL A 1 166 ? -2.016  -40.923 -11.434 1.00 91.47  ? 165  VAL A CG2 1 
ATOM   1321 N N   . ARG A 1 167 ? -2.237  -45.135 -9.612  1.00 98.65  ? 166  ARG A N   1 
ATOM   1322 C CA  . ARG A 1 167 ? -2.842  -46.425 -9.302  1.00 104.05 ? 166  ARG A CA  1 
ATOM   1323 C C   . ARG A 1 167 ? -2.865  -46.680 -7.797  1.00 99.80  ? 166  ARG A C   1 
ATOM   1324 O O   . ARG A 1 167 ? -3.868  -47.163 -7.265  1.00 92.93  ? 166  ARG A O   1 
ATOM   1325 C CB  . ARG A 1 167 ? -2.155  -47.573 -10.053 1.00 117.27 ? 166  ARG A CB  1 
ATOM   1326 C CG  . ARG A 1 167 ? -0.935  -48.159 -9.362  1.00 131.63 ? 166  ARG A CG  1 
ATOM   1327 C CD  . ARG A 1 167 ? -0.302  -49.250 -10.216 1.00 146.33 ? 166  ARG A CD  1 
ATOM   1328 N NE  . ARG A 1 167 ? 0.103   -48.744 -11.527 1.00 154.63 ? 166  ARG A NE  1 
ATOM   1329 C CZ  . ARG A 1 167 ? 0.601   -49.499 -12.501 1.00 158.70 ? 166  ARG A CZ  1 
ATOM   1330 N NH1 . ARG A 1 167 ? 0.754   -50.805 -12.316 1.00 165.84 ? 166  ARG A NH1 1 
ATOM   1331 N NH2 . ARG A 1 167 ? 0.940   -48.950 -13.662 1.00 152.77 ? 166  ARG A NH2 1 
ATOM   1332 N N   . ARG A 1 168 ? -1.770  -46.351 -7.114  1.00 96.15  ? 167  ARG A N   1 
ATOM   1333 C CA  . ARG A 1 168 ? -1.727  -46.449 -5.656  1.00 86.19  ? 167  ARG A CA  1 
ATOM   1334 C C   . ARG A 1 168 ? -2.892  -45.674 -5.048  1.00 74.11  ? 167  ARG A C   1 
ATOM   1335 O O   . ARG A 1 168 ? -3.591  -46.173 -4.177  1.00 74.94  ? 167  ARG A O   1 
ATOM   1336 C CB  . ARG A 1 168 ? -0.391  -45.936 -5.100  1.00 84.55  ? 167  ARG A CB  1 
ATOM   1337 C CG  . ARG A 1 168 ? 0.635   -47.021 -4.788  1.00 90.64  ? 167  ARG A CG  1 
ATOM   1338 C CD  . ARG A 1 168 ? 1.991   -46.422 -4.430  1.00 103.76 ? 167  ARG A CD  1 
ATOM   1339 N NE  . ARG A 1 168 ? 2.896   -47.412 -3.846  1.00 121.59 ? 167  ARG A NE  1 
ATOM   1340 C CZ  . ARG A 1 168 ? 3.025   -47.632 -2.539  1.00 128.02 ? 167  ARG A CZ  1 
ATOM   1341 N NH1 . ARG A 1 168 ? 2.310   -46.929 -1.672  1.00 124.34 ? 167  ARG A NH1 1 
ATOM   1342 N NH2 . ARG A 1 168 ? 3.868   -48.556 -2.095  1.00 133.95 ? 167  ARG A NH2 1 
ATOM   1343 N N   . LEU A 1 169 ? -3.104  -44.457 -5.529  1.00 72.15  ? 168  LEU A N   1 
ATOM   1344 C CA  . LEU A 1 169 ? -4.158  -43.592 -5.013  1.00 74.05  ? 168  LEU A CA  1 
ATOM   1345 C C   . LEU A 1 169 ? -5.563  -44.059 -5.404  1.00 87.52  ? 168  LEU A C   1 
ATOM   1346 O O   . LEU A 1 169 ? -6.495  -43.950 -4.611  1.00 91.89  ? 168  LEU A O   1 
ATOM   1347 C CB  . LEU A 1 169 ? -3.927  -42.146 -5.464  1.00 72.31  ? 168  LEU A CB  1 
ATOM   1348 C CG  . LEU A 1 169 ? -3.153  -41.211 -4.526  1.00 74.73  ? 168  LEU A CG  1 
ATOM   1349 C CD1 . LEU A 1 169 ? -2.070  -41.923 -3.748  1.00 74.25  ? 168  LEU A CD1 1 
ATOM   1350 C CD2 . LEU A 1 169 ? -2.569  -40.043 -5.302  1.00 78.56  ? 168  LEU A CD2 1 
ATOM   1351 N N   . SER A 1 170 ? -5.728  -44.576 -6.619  1.00 89.29  ? 169  SER A N   1 
ATOM   1352 C CA  . SER A 1 170 ? -7.045  -45.073 -7.018  1.00 97.34  ? 169  SER A CA  1 
ATOM   1353 C C   . SER A 1 170 ? -7.430  -46.262 -6.140  1.00 95.03  ? 169  SER A C   1 
ATOM   1354 O O   . SER A 1 170 ? -8.602  -46.460 -5.831  1.00 101.40 ? 169  SER A O   1 
ATOM   1355 C CB  . SER A 1 170 ? -7.098  -45.428 -8.513  1.00 106.37 ? 169  SER A CB  1 
ATOM   1356 O OG  . SER A 1 170 ? -6.487  -46.673 -8.796  1.00 107.67 ? 169  SER A OG  1 
ATOM   1357 N N   . THR A 1 171 ? -6.421  -47.040 -5.752  1.00 89.92  ? 170  THR A N   1 
ATOM   1358 C CA  . THR A 1 171 ? -6.527  -48.085 -4.730  1.00 87.64  ? 170  THR A CA  1 
ATOM   1359 C C   . THR A 1 171 ? -7.336  -47.607 -3.526  1.00 94.18  ? 170  THR A C   1 
ATOM   1360 O O   . THR A 1 171 ? -8.170  -48.331 -2.999  1.00 100.88 ? 170  THR A O   1 
ATOM   1361 C CB  . THR A 1 171 ? -5.116  -48.504 -4.259  1.00 87.52  ? 170  THR A CB  1 
ATOM   1362 O OG1 . THR A 1 171 ? -4.668  -49.636 -5.008  1.00 84.64  ? 170  THR A OG1 1 
ATOM   1363 C CG2 . THR A 1 171 ? -5.089  -48.832 -2.786  1.00 85.88  ? 170  THR A CG2 1 
ATOM   1364 N N   . LEU A 1 172 ? -7.084  -46.372 -3.113  1.00 93.43  ? 171  LEU A N   1 
ATOM   1365 C CA  . LEU A 1 172 ? -7.764  -45.737 -1.989  1.00 90.72  ? 171  LEU A CA  1 
ATOM   1366 C C   . LEU A 1 172 ? -9.273  -45.702 -2.205  1.00 85.77  ? 171  LEU A C   1 
ATOM   1367 O O   . LEU A 1 172 ? -10.045 -45.724 -1.257  1.00 81.71  ? 171  LEU A O   1 
ATOM   1368 C CB  . LEU A 1 172 ? -7.230  -44.303 -1.837  1.00 97.39  ? 171  LEU A CB  1 
ATOM   1369 C CG  . LEU A 1 172 ? -7.125  -43.620 -0.477  1.00 96.39  ? 171  LEU A CG  1 
ATOM   1370 C CD1 . LEU A 1 172 ? -8.490  -43.192 0.030   1.00 98.55  ? 171  LEU A CD1 1 
ATOM   1371 C CD2 . LEU A 1 172 ? -6.454  -44.550 0.503   1.00 105.05 ? 171  LEU A CD2 1 
ATOM   1372 N N   . CYS A 1 173 ? -9.687  -45.636 -3.465  1.00 94.04  ? 172  CYS A N   1 
ATOM   1373 C CA  . CYS A 1 173 ? -11.095 -45.472 -3.800  1.00 86.50  ? 172  CYS A CA  1 
ATOM   1374 C C   . CYS A 1 173 ? -11.830 -46.801 -3.954  1.00 100.62 ? 172  CYS A C   1 
ATOM   1375 O O   . CYS A 1 173 ? -13.017 -46.901 -3.636  1.00 101.88 ? 172  CYS A O   1 
ATOM   1376 C CB  . CYS A 1 173 ? -11.229 -44.663 -5.079  1.00 74.64  ? 172  CYS A CB  1 
ATOM   1377 S SG  . CYS A 1 173 ? -10.464 -43.059 -5.009  1.00 106.03 ? 172  CYS A SG  1 
ATOM   1378 N N   . THR A 1 174 ? -11.134 -47.819 -4.452  1.00 102.78 ? 173  THR A N   1 
ATOM   1379 C CA  . THR A 1 174 ? -11.738 -49.142 -4.539  1.00 106.73 ? 173  THR A CA  1 
ATOM   1380 C C   . THR A 1 174 ? -11.918 -49.760 -3.144  1.00 104.05 ? 173  THR A C   1 
ATOM   1381 O O   . THR A 1 174 ? -13.016 -50.164 -2.781  1.00 99.86  ? 173  THR A O   1 
ATOM   1382 C CB  . THR A 1 174 ? -10.978 -50.092 -5.504  1.00 91.68  ? 173  THR A CB  1 
ATOM   1383 O OG1 . THR A 1 174 ? -10.089 -50.938 -4.769  1.00 97.87  ? 173  THR A OG1 1 
ATOM   1384 C CG2 . THR A 1 174 ? -10.196 -49.297 -6.534  1.00 93.10  ? 173  THR A CG2 1 
ATOM   1385 N N   . THR A 1 175 ? -10.860 -49.811 -2.343  1.00 107.08 ? 174  THR A N   1 
ATOM   1386 C CA  . THR A 1 175 ? -10.987 -50.430 -1.025  1.00 101.28 ? 174  THR A CA  1 
ATOM   1387 C C   . THR A 1 175 ? -11.912 -49.638 -0.106  1.00 93.62  ? 174  THR A C   1 
ATOM   1388 O O   . THR A 1 175 ? -12.496 -50.187 0.824   1.00 95.46  ? 174  THR A O   1 
ATOM   1389 C CB  . THR A 1 175 ? -9.620  -50.670 -0.341  1.00 87.25  ? 174  THR A CB  1 
ATOM   1390 O OG1 . THR A 1 175 ? -9.655  -50.175 1.001   1.00 86.23  ? 174  THR A OG1 1 
ATOM   1391 C CG2 . THR A 1 175 ? -8.539  -49.977 -1.086  1.00 76.42  ? 174  THR A CG2 1 
ATOM   1392 N N   . MET A 1 176 ? -12.052 -48.349 -0.374  1.00 86.11  ? 175  MET A N   1 
ATOM   1393 C CA  . MET A 1 176 ? -12.937 -47.520 0.426   1.00 89.30  ? 175  MET A CA  1 
ATOM   1394 C C   . MET A 1 176 ? -14.342 -47.563 -0.149  1.00 92.07  ? 175  MET A C   1 
ATOM   1395 O O   . MET A 1 176 ? -15.307 -47.180 0.513   1.00 92.20  ? 175  MET A O   1 
ATOM   1396 C CB  . MET A 1 176 ? -12.429 -46.078 0.458   1.00 97.00  ? 175  MET A CB  1 
ATOM   1397 C CG  . MET A 1 176 ? -12.650 -45.390 1.786   1.00 95.67  ? 175  MET A CG  1 
ATOM   1398 S SD  . MET A 1 176 ? -11.985 -46.364 3.151   1.00 90.71  ? 175  MET A SD  1 
ATOM   1399 C CE  . MET A 1 176 ? -12.618 -45.426 4.535   1.00 92.20  ? 175  MET A CE  1 
ATOM   1400 N N   . ASN A 1 177 ? -14.436 -48.035 -1.390  1.00 96.81  ? 176  ASN A N   1 
ATOM   1401 C CA  . ASN A 1 177 ? -15.699 -48.137 -2.121  1.00 95.81  ? 176  ASN A CA  1 
ATOM   1402 C C   . ASN A 1 177 ? -16.398 -46.792 -2.298  1.00 95.79  ? 176  ASN A C   1 
ATOM   1403 O O   . ASN A 1 177 ? -17.493 -46.570 -1.776  1.00 88.53  ? 176  ASN A O   1 
ATOM   1404 C CB  . ASN A 1 177 ? -16.640 -49.155 -1.474  1.00 102.57 ? 176  ASN A CB  1 
ATOM   1405 C CG  . ASN A 1 177 ? -17.790 -49.542 -2.388  1.00 115.79 ? 176  ASN A CG  1 
ATOM   1406 O OD1 . ASN A 1 177 ? -17.696 -49.401 -3.611  1.00 111.01 ? 176  ASN A OD1 1 
ATOM   1407 N ND2 . ASN A 1 177 ? -18.881 -50.034 -1.801  1.00 117.74 ? 176  ASN A ND2 1 
ATOM   1408 N N   . VAL A 1 178 ? -15.751 -45.903 -3.047  1.00 100.74 ? 177  VAL A N   1 
ATOM   1409 C CA  . VAL A 1 178 ? -16.271 -44.564 -3.288  1.00 99.49  ? 177  VAL A CA  1 
ATOM   1410 C C   . VAL A 1 178 ? -15.686 -44.017 -4.591  1.00 97.79  ? 177  VAL A C   1 
ATOM   1411 O O   . VAL A 1 178 ? -14.541 -44.309 -4.922  1.00 92.88  ? 177  VAL A O   1 
ATOM   1412 C CB  . VAL A 1 178 ? -15.927 -43.639 -2.115  1.00 98.85  ? 177  VAL A CB  1 
ATOM   1413 C CG1 . VAL A 1 178 ? -14.422 -43.480 -1.997  1.00 103.05 ? 177  VAL A CG1 1 
ATOM   1414 C CG2 . VAL A 1 178 ? -16.612 -42.300 -2.279  1.00 102.22 ? 177  VAL A CG2 1 
ATOM   1415 N N   . ALA A 1 179 ? -16.473 -43.248 -5.341  1.00 106.82 ? 178  ALA A N   1 
ATOM   1416 C CA  . ALA A 1 179 ? -16.044 -42.777 -6.664  1.00 107.93 ? 178  ALA A CA  1 
ATOM   1417 C C   . ALA A 1 179 ? -16.034 -41.257 -6.756  1.00 99.22  ? 178  ALA A C   1 
ATOM   1418 O O   . ALA A 1 179 ? -16.968 -40.666 -7.312  1.00 103.10 ? 178  ALA A O   1 
ATOM   1419 C CB  . ALA A 1 179 ? -16.937 -43.362 -7.746  1.00 110.78 ? 178  ALA A CB  1 
ATOM   1420 N N   . PRO A 1 180 ? -14.963 -40.624 -6.237  1.00 91.02  ? 179  PRO A N   1 
ATOM   1421 C CA  . PRO A 1 180 ? -14.923 -39.186 -5.950  1.00 91.18  ? 179  PRO A CA  1 
ATOM   1422 C C   . PRO A 1 180 ? -14.641 -38.286 -7.152  1.00 94.33  ? 179  PRO A C   1 
ATOM   1423 O O   . PRO A 1 180 ? -14.044 -38.721 -8.138  1.00 90.88  ? 179  PRO A O   1 
ATOM   1424 C CB  . PRO A 1 180 ? -13.776 -39.064 -4.929  1.00 81.57  ? 179  PRO A CB  1 
ATOM   1425 C CG  . PRO A 1 180 ? -13.291 -40.479 -4.664  1.00 74.58  ? 179  PRO A CG  1 
ATOM   1426 C CD  . PRO A 1 180 ? -13.701 -41.271 -5.848  1.00 85.21  ? 179  PRO A CD  1 
ATOM   1427 N N   . ILE A 1 181 ? -15.084 -37.034 -7.057  1.00 96.49  ? 180  ILE A N   1 
ATOM   1428 C CA  . ILE A 1 181 ? -14.684 -35.999 -8.003  1.00 99.98  ? 180  ILE A CA  1 
ATOM   1429 C C   . ILE A 1 181 ? -13.294 -35.498 -7.600  1.00 94.21  ? 180  ILE A C   1 
ATOM   1430 O O   . ILE A 1 181 ? -13.043 -35.202 -6.430  1.00 79.41  ? 180  ILE A O   1 
ATOM   1431 C CB  . ILE A 1 181 ? -15.695 -34.826 -8.035  1.00 109.72 ? 180  ILE A CB  1 
ATOM   1432 C CG1 . ILE A 1 181 ? -16.910 -35.184 -8.892  1.00 126.77 ? 180  ILE A CG1 1 
ATOM   1433 C CG2 . ILE A 1 181 ? -15.058 -33.577 -8.603  1.00 108.91 ? 180  ILE A CG2 1 
ATOM   1434 C CD1 . ILE A 1 181 ? -17.705 -36.368 -8.379  1.00 136.90 ? 180  ILE A CD1 1 
ATOM   1435 N N   . VAL A 1 182 ? -12.389 -35.430 -8.571  1.00 95.67  ? 181  VAL A N   1 
ATOM   1436 C CA  . VAL A 1 182 ? -11.016 -35.023 -8.318  1.00 91.18  ? 181  VAL A CA  1 
ATOM   1437 C C   . VAL A 1 182 ? -10.875 -33.499 -8.373  1.00 96.85  ? 181  VAL A C   1 
ATOM   1438 O O   . VAL A 1 182 ? -11.320 -32.864 -9.327  1.00 105.14 ? 181  VAL A O   1 
ATOM   1439 C CB  . VAL A 1 182 ? -10.056 -35.677 -9.330  1.00 95.60  ? 181  VAL A CB  1 
ATOM   1440 C CG1 . VAL A 1 182 ? -8.642  -35.128 -9.173  1.00 103.16 ? 181  VAL A CG1 1 
ATOM   1441 C CG2 . VAL A 1 182 ? -10.063 -37.186 -9.169  1.00 90.97  ? 181  VAL A CG2 1 
ATOM   1442 N N   . ARG A 1 183 ? -10.269 -32.921 -7.338  1.00 91.68  ? 182  ARG A N   1 
ATOM   1443 C CA  . ARG A 1 183 ? -10.023 -31.485 -7.288  1.00 89.48  ? 182  ARG A CA  1 
ATOM   1444 C C   . ARG A 1 183 ? -8.522  -31.209 -7.231  1.00 92.13  ? 182  ARG A C   1 
ATOM   1445 O O   . ARG A 1 183 ? -7.761  -31.968 -6.633  1.00 92.72  ? 182  ARG A O   1 
ATOM   1446 C CB  . ARG A 1 183 ? -10.691 -30.862 -6.060  1.00 86.84  ? 182  ARG A CB  1 
ATOM   1447 C CG  . ARG A 1 183 ? -12.192 -31.072 -5.956  1.00 86.47  ? 182  ARG A CG  1 
ATOM   1448 C CD  . ARG A 1 183 ? -12.964 -30.290 -7.007  1.00 93.33  ? 182  ARG A CD  1 
ATOM   1449 N NE  . ARG A 1 183 ? -13.000 -28.844 -6.776  1.00 94.49  ? 182  ARG A NE  1 
ATOM   1450 C CZ  . ARG A 1 183 ? -13.721 -28.249 -5.828  1.00 88.04  ? 182  ARG A CZ  1 
ATOM   1451 N NH1 . ARG A 1 183 ? -14.449 -28.976 -4.997  1.00 81.72  ? 182  ARG A NH1 1 
ATOM   1452 N NH2 . ARG A 1 183 ? -13.709 -26.926 -5.704  1.00 83.09  ? 182  ARG A NH2 1 
ATOM   1453 N N   . TYR A 1 184 ? -8.101  -30.115 -7.851  1.00 86.94  ? 183  TYR A N   1 
ATOM   1454 C CA  . TYR A 1 184 ? -6.706  -29.704 -7.804  1.00 89.58  ? 183  TYR A CA  1 
ATOM   1455 C C   . TYR A 1 184 ? -6.572  -28.183 -7.845  1.00 86.55  ? 183  TYR A C   1 
ATOM   1456 O O   . TYR A 1 184 ? -7.493  -27.490 -8.253  1.00 84.29  ? 183  TYR A O   1 
ATOM   1457 C CB  . TYR A 1 184 ? -5.916  -30.353 -8.940  1.00 92.82  ? 183  TYR A CB  1 
ATOM   1458 C CG  . TYR A 1 184 ? -6.399  -29.984 -10.318 1.00 103.50 ? 183  TYR A CG  1 
ATOM   1459 C CD1 . TYR A 1 184 ? -7.496  -30.626 -10.885 1.00 107.12 ? 183  TYR A CD1 1 
ATOM   1460 C CD2 . TYR A 1 184 ? -5.751  -29.002 -11.064 1.00 97.39  ? 183  TYR A CD2 1 
ATOM   1461 C CE1 . TYR A 1 184 ? -7.936  -30.295 -12.148 1.00 107.67 ? 183  TYR A CE1 1 
ATOM   1462 C CE2 . TYR A 1 184 ? -6.183  -28.668 -12.327 1.00 98.36  ? 183  TYR A CE2 1 
ATOM   1463 C CZ  . TYR A 1 184 ? -7.277  -29.315 -12.864 1.00 105.65 ? 183  TYR A CZ  1 
ATOM   1464 O OH  . TYR A 1 184 ? -7.714  -28.987 -14.124 1.00 113.48 ? 183  TYR A OH  1 
ATOM   1465 N N   . SER A 1 185 ? -5.432  -27.665 -7.402  1.00 88.04  ? 184  SER A N   1 
ATOM   1466 C CA  . SER A 1 185 ? -5.207  -26.222 -7.441  1.00 94.76  ? 184  SER A CA  1 
ATOM   1467 C C   . SER A 1 185 ? -4.941  -25.708 -8.855  1.00 94.61  ? 184  SER A C   1 
ATOM   1468 O O   . SER A 1 185 ? -4.208  -26.324 -9.623  1.00 94.39  ? 184  SER A O   1 
ATOM   1469 C CB  . SER A 1 185 ? -4.050  -25.831 -6.524  1.00 96.37  ? 184  SER A CB  1 
ATOM   1470 O OG  . SER A 1 185 ? -3.616  -24.514 -6.808  1.00 90.33  ? 184  SER A OG  1 
ATOM   1471 N N   . SER A 1 186 ? -5.542  -24.573 -9.189  1.00 100.90 ? 185  SER A N   1 
ATOM   1472 C CA  . SER A 1 186 ? -5.322  -23.939 -10.485 1.00 109.92 ? 185  SER A CA  1 
ATOM   1473 C C   . SER A 1 186 ? -3.829  -23.742 -10.730 1.00 107.89 ? 185  SER A C   1 
ATOM   1474 O O   . SER A 1 186 ? -3.350  -23.838 -11.867 1.00 101.06 ? 185  SER A O   1 
ATOM   1475 C CB  . SER A 1 186 ? -6.043  -22.589 -10.544 1.00 112.88 ? 185  SER A CB  1 
ATOM   1476 O OG  . SER A 1 186 ? -5.543  -21.702 -9.557  1.00 110.51 ? 185  SER A OG  1 
ATOM   1477 N N   . THR A 1 187 ? -3.103  -23.471 -9.646  1.00 109.30 ? 186  THR A N   1 
ATOM   1478 C CA  . THR A 1 187 ? -1.657  -23.257 -9.698  1.00 102.02 ? 186  THR A CA  1 
ATOM   1479 C C   . THR A 1 187 ? -0.834  -24.524 -9.411  1.00 94.53  ? 186  THR A C   1 
ATOM   1480 O O   . THR A 1 187 ? 0.337   -24.437 -9.068  1.00 91.02  ? 186  THR A O   1 
ATOM   1481 C CB  . THR A 1 187 ? -1.215  -22.098 -8.764  1.00 93.53  ? 186  THR A CB  1 
ATOM   1482 O OG1 . THR A 1 187 ? -1.554  -22.383 -7.396  1.00 84.42  ? 186  THR A OG1 1 
ATOM   1483 C CG2 . THR A 1 187 ? -1.891  -20.802 -9.180  1.00 104.94 ? 186  THR A CG2 1 
ATOM   1484 N N   . SER A 1 188 ? -1.455  -25.693 -9.552  1.00 88.82  ? 187  SER A N   1 
ATOM   1485 C CA  . SER A 1 188 ? -0.740  -26.969 -9.503  1.00 83.34  ? 187  SER A CA  1 
ATOM   1486 C C   . SER A 1 188 ? 0.436   -27.013 -10.478 1.00 85.38  ? 187  SER A C   1 
ATOM   1487 O O   . SER A 1 188 ? 0.392   -26.404 -11.549 1.00 90.86  ? 187  SER A O   1 
ATOM   1488 C CB  . SER A 1 188 ? -1.688  -28.124 -9.835  1.00 83.24  ? 187  SER A CB  1 
ATOM   1489 O OG  . SER A 1 188 ? -2.515  -28.450 -8.727  1.00 102.61 ? 187  SER A OG  1 
ATOM   1490 N N   . THR A 1 189 ? 1.487   -27.740 -10.114 1.00 78.71  ? 188  THR A N   1 
ATOM   1491 C CA  . THR A 1 189 ? 2.557   -28.004 -11.063 1.00 87.57  ? 188  THR A CA  1 
ATOM   1492 C C   . THR A 1 189 ? 1.964   -28.865 -12.165 1.00 92.59  ? 188  THR A C   1 
ATOM   1493 O O   . THR A 1 189 ? 0.982   -29.570 -11.940 1.00 96.58  ? 188  THR A O   1 
ATOM   1494 C CB  . THR A 1 189 ? 3.750   -28.749 -10.421 1.00 83.23  ? 188  THR A CB  1 
ATOM   1495 O OG1 . THR A 1 189 ? 3.408   -30.126 -10.199 1.00 86.90  ? 188  THR A OG1 1 
ATOM   1496 C CG2 . THR A 1 189 ? 4.124   -28.108 -9.109  1.00 65.69  ? 188  THR A CG2 1 
ATOM   1497 N N   . PRO A 1 190 ? 2.542   -28.796 -13.367 1.00 93.29  ? 189  PRO A N   1 
ATOM   1498 C CA  . PRO A 1 190 ? 2.075   -29.638 -14.470 1.00 98.72  ? 189  PRO A CA  1 
ATOM   1499 C C   . PRO A 1 190 ? 2.074   -31.109 -14.077 1.00 102.84 ? 189  PRO A C   1 
ATOM   1500 O O   . PRO A 1 190 ? 1.116   -31.828 -14.372 1.00 99.83  ? 189  PRO A O   1 
ATOM   1501 C CB  . PRO A 1 190 ? 3.110   -29.380 -15.567 1.00 96.51  ? 189  PRO A CB  1 
ATOM   1502 C CG  . PRO A 1 190 ? 3.584   -27.992 -15.297 1.00 99.63  ? 189  PRO A CG  1 
ATOM   1503 C CD  . PRO A 1 190 ? 3.574   -27.836 -13.795 1.00 93.47  ? 189  PRO A CD  1 
ATOM   1504 N N   . GLY A 1 191 ? 3.139   -31.549 -13.415 1.00 110.67 ? 190  GLY A N   1 
ATOM   1505 C CA  . GLY A 1 191 ? 3.219   -32.927 -12.964 1.00 109.80 ? 190  GLY A CA  1 
ATOM   1506 C C   . GLY A 1 191 ? 1.995   -33.317 -12.159 1.00 96.41  ? 190  GLY A C   1 
ATOM   1507 O O   . GLY A 1 191 ? 1.493   -34.436 -12.274 1.00 98.78  ? 190  GLY A O   1 
ATOM   1508 N N   . THR A 1 192 ? 1.513   -32.377 -11.349 1.00 83.05  ? 191  THR A N   1 
ATOM   1509 C CA  . THR A 1 192 ? 0.385   -32.614 -10.467 1.00 75.15  ? 191  THR A CA  1 
ATOM   1510 C C   . THR A 1 192 ? -0.940  -32.577 -11.208 1.00 75.62  ? 191  THR A C   1 
ATOM   1511 O O   . THR A 1 192 ? -1.743  -33.492 -11.072 1.00 76.01  ? 191  THR A O   1 
ATOM   1512 C CB  . THR A 1 192 ? 0.378   -31.633 -9.277  1.00 79.63  ? 191  THR A CB  1 
ATOM   1513 O OG1 . THR A 1 192 ? 1.394   -32.022 -8.348  1.00 76.58  ? 191  THR A OG1 1 
ATOM   1514 C CG2 . THR A 1 192 ? -0.970  -31.655 -8.554  1.00 82.26  ? 191  THR A CG2 1 
ATOM   1515 N N   . GLU A 1 193 ? -1.166  -31.529 -11.992 1.00 83.46  ? 192  GLU A N   1 
ATOM   1516 C CA  . GLU A 1 193 ? -2.370  -31.440 -12.815 1.00 86.74  ? 192  GLU A CA  1 
ATOM   1517 C C   . GLU A 1 193 ? -2.626  -32.751 -13.547 1.00 91.91  ? 192  GLU A C   1 
ATOM   1518 O O   . GLU A 1 193 ? -3.726  -33.307 -13.478 1.00 92.81  ? 192  GLU A O   1 
ATOM   1519 C CB  . GLU A 1 193 ? -2.248  -30.306 -13.829 1.00 94.64  ? 192  GLU A CB  1 
ATOM   1520 C CG  . GLU A 1 193 ? -3.571  -29.877 -14.433 1.00 108.49 ? 192  GLU A CG  1 
ATOM   1521 C CD  . GLU A 1 193 ? -3.408  -28.825 -15.516 1.00 126.60 ? 192  GLU A CD  1 
ATOM   1522 O OE1 . GLU A 1 193 ? -2.256  -28.427 -15.795 1.00 129.72 ? 192  GLU A OE1 1 
ATOM   1523 O OE2 . GLU A 1 193 ? -4.433  -28.398 -16.092 1.00 136.21 ? 192  GLU A OE2 1 
ATOM   1524 N N   . ARG A 1 194 ? -1.602  -33.244 -14.242 1.00 97.60  ? 193  ARG A N   1 
ATOM   1525 C CA  . ARG A 1 194 ? -1.701  -34.495 -14.985 1.00 104.90 ? 193  ARG A CA  1 
ATOM   1526 C C   . ARG A 1 194 ? -2.096  -35.651 -14.067 1.00 108.09 ? 193  ARG A C   1 
ATOM   1527 O O   . ARG A 1 194 ? -2.978  -36.444 -14.399 1.00 114.42 ? 193  ARG A O   1 
ATOM   1528 C CB  . ARG A 1 194 ? -0.383  -34.812 -15.697 1.00 117.81 ? 193  ARG A CB  1 
ATOM   1529 C CG  . ARG A 1 194 ? -0.526  -35.806 -16.848 1.00 137.23 ? 193  ARG A CG  1 
ATOM   1530 C CD  . ARG A 1 194 ? 0.352   -37.045 -16.665 1.00 146.04 ? 193  ARG A CD  1 
ATOM   1531 N NE  . ARG A 1 194 ? 1.759   -36.704 -16.446 1.00 150.66 ? 193  ARG A NE  1 
ATOM   1532 C CZ  . ARG A 1 194 ? 2.755   -37.588 -16.447 1.00 148.56 ? 193  ARG A CZ  1 
ATOM   1533 N NH1 . ARG A 1 194 ? 4.003   -37.184 -16.234 1.00 141.28 ? 193  ARG A NH1 1 
ATOM   1534 N NH2 . ARG A 1 194 ? 2.506   -38.875 -16.664 1.00 150.15 ? 193  ARG A NH2 1 
ATOM   1535 N N   . MET A 1 195 ? -1.442  -35.746 -12.913 1.00 96.32  ? 194  MET A N   1 
ATOM   1536 C CA  . MET A 1 195 ? -1.779  -36.780 -11.946 1.00 93.49  ? 194  MET A CA  1 
ATOM   1537 C C   . MET A 1 195 ? -3.263  -36.745 -11.583 1.00 96.71  ? 194  MET A C   1 
ATOM   1538 O O   . MET A 1 195 ? -3.899  -37.786 -11.477 1.00 107.81 ? 194  MET A O   1 
ATOM   1539 C CB  . MET A 1 195 ? -0.930  -36.635 -10.688 1.00 97.96  ? 194  MET A CB  1 
ATOM   1540 C CG  . MET A 1 195 ? -1.387  -37.513 -9.536  1.00 100.38 ? 194  MET A CG  1 
ATOM   1541 S SD  . MET A 1 195 ? -1.007  -36.751 -7.945  1.00 134.42 ? 194  MET A SD  1 
ATOM   1542 C CE  . MET A 1 195 ? 0.736   -36.399 -8.155  1.00 89.52  ? 194  MET A CE  1 
ATOM   1543 N N   . ALA A 1 196 ? -3.812  -35.547 -11.397 1.00 91.45  ? 195  ALA A N   1 
ATOM   1544 C CA  . ALA A 1 196 ? -5.228  -35.387 -11.071 1.00 88.05  ? 195  ALA A CA  1 
ATOM   1545 C C   . ALA A 1 196 ? -6.121  -35.795 -12.237 1.00 99.86  ? 195  ALA A C   1 
ATOM   1546 O O   . ALA A 1 196 ? -7.177  -36.401 -12.042 1.00 95.82  ? 195  ALA A O   1 
ATOM   1547 C CB  . ALA A 1 196 ? -5.529  -33.958 -10.668 1.00 72.92  ? 195  ALA A CB  1 
ATOM   1548 N N   . MET A 1 197 ? -5.713  -35.443 -13.450 1.00 101.92 ? 196  MET A N   1 
ATOM   1549 C CA  . MET A 1 197 ? -6.479  -35.845 -14.615 1.00 112.61 ? 196  MET A CA  1 
ATOM   1550 C C   . MET A 1 197 ? -6.559  -37.366 -14.621 1.00 112.96 ? 196  MET A C   1 
ATOM   1551 O O   . MET A 1 197 ? -7.643  -37.950 -14.703 1.00 112.82 ? 196  MET A O   1 
ATOM   1552 C CB  . MET A 1 197 ? -5.830  -35.351 -15.918 1.00 114.59 ? 196  MET A CB  1 
ATOM   1553 C CG  . MET A 1 197 ? -5.835  -33.840 -16.133 1.00 108.01 ? 196  MET A CG  1 
ATOM   1554 S SD  . MET A 1 197 ? -7.473  -33.097 -16.087 1.00 138.73 ? 196  MET A SD  1 
ATOM   1555 C CE  . MET A 1 197 ? -7.159  -31.546 -16.927 1.00 140.15 ? 196  MET A CE  1 
ATOM   1556 N N   . GLN A 1 198 ? -5.396  -37.995 -14.509 1.00 108.64 ? 197  GLN A N   1 
ATOM   1557 C CA  . GLN A 1 198 ? -5.271  -39.432 -14.697 1.00 109.00 ? 197  GLN A CA  1 
ATOM   1558 C C   . GLN A 1 198 ? -6.009  -40.211 -13.606 1.00 104.88 ? 197  GLN A C   1 
ATOM   1559 O O   . GLN A 1 198 ? -6.544  -41.299 -13.859 1.00 97.78  ? 197  GLN A O   1 
ATOM   1560 C CB  . GLN A 1 198 ? -3.793  -39.814 -14.736 1.00 111.05 ? 197  GLN A CB  1 
ATOM   1561 C CG  . GLN A 1 198 ? -3.479  -41.048 -15.552 1.00 122.57 ? 197  GLN A CG  1 
ATOM   1562 C CD  . GLN A 1 198 ? -1.980  -41.291 -15.684 1.00 131.48 ? 197  GLN A CD  1 
ATOM   1563 O OE1 . GLN A 1 198 ? -1.193  -40.360 -15.919 1.00 121.56 ? 197  GLN A OE1 1 
ATOM   1564 N NE2 . GLN A 1 198 ? -1.579  -42.552 -15.537 1.00 139.63 ? 197  GLN A NE2 1 
ATOM   1565 N N   . LEU A 1 199 ? -6.038  -39.644 -12.400 1.00 95.31  ? 198  LEU A N   1 
ATOM   1566 C CA  . LEU A 1 199 ? -6.716  -40.262 -11.265 1.00 88.13  ? 198  LEU A CA  1 
ATOM   1567 C C   . LEU A 1 199 ? -8.213  -40.339 -11.528 1.00 99.44  ? 198  LEU A C   1 
ATOM   1568 O O   . LEU A 1 199 ? -8.882  -41.283 -11.104 1.00 111.06 ? 198  LEU A O   1 
ATOM   1569 C CB  . LEU A 1 199 ? -6.473  -39.455 -9.990  1.00 78.63  ? 198  LEU A CB  1 
ATOM   1570 C CG  . LEU A 1 199 ? -6.321  -40.208 -8.662  1.00 77.35  ? 198  LEU A CG  1 
ATOM   1571 C CD1 . LEU A 1 199 ? -7.020  -39.451 -7.547  1.00 77.37  ? 198  LEU A CD1 1 
ATOM   1572 C CD2 . LEU A 1 199 ? -6.844  -41.632 -8.741  1.00 76.00  ? 198  LEU A CD2 1 
ATOM   1573 N N   . GLN A 1 200 ? -8.738  -39.339 -12.225 1.00 94.52  ? 199  GLN A N   1 
ATOM   1574 C CA  . GLN A 1 200 ? -10.162 -39.297 -12.505 1.00 94.33  ? 199  GLN A CA  1 
ATOM   1575 C C   . GLN A 1 200 ? -10.554 -40.425 -13.444 1.00 99.73  ? 199  GLN A C   1 
ATOM   1576 O O   . GLN A 1 200 ? -11.527 -41.129 -13.194 1.00 103.35 ? 199  GLN A O   1 
ATOM   1577 C CB  . GLN A 1 200 ? -10.569 -37.952 -13.087 1.00 98.60  ? 199  GLN A CB  1 
ATOM   1578 C CG  . GLN A 1 200 ? -12.067 -37.741 -13.102 1.00 104.41 ? 199  GLN A CG  1 
ATOM   1579 C CD  . GLN A 1 200 ? -12.653 -37.595 -11.714 1.00 99.92  ? 199  GLN A CD  1 
ATOM   1580 O OE1 . GLN A 1 200 ? -12.564 -36.534 -11.102 1.00 103.12 ? 199  GLN A OE1 1 
ATOM   1581 N NE2 . GLN A 1 200 ? -13.268 -38.661 -11.213 1.00 92.21  ? 199  GLN A NE2 1 
ATOM   1582 N N   . LYS A 1 201 ? -9.783  -40.603 -14.514 1.00 106.77 ? 200  LYS A N   1 
ATOM   1583 C CA  . LYS A 1 201 ? -9.998  -41.706 -15.452 1.00 111.08 ? 200  LYS A CA  1 
ATOM   1584 C C   . LYS A 1 201 ? -9.821  -43.078 -14.800 1.00 111.80 ? 200  LYS A C   1 
ATOM   1585 O O   . LYS A 1 201 ? -10.450 -44.053 -15.215 1.00 114.16 ? 200  LYS A O   1 
ATOM   1586 C CB  . LYS A 1 201 ? -9.055  -41.594 -16.652 1.00 108.07 ? 200  LYS A CB  1 
ATOM   1587 C CG  . LYS A 1 201 ? -9.391  -40.472 -17.602 1.00 115.40 ? 200  LYS A CG  1 
ATOM   1588 C CD  . LYS A 1 201 ? -8.600  -40.607 -18.885 1.00 125.26 ? 200  LYS A CD  1 
ATOM   1589 C CE  . LYS A 1 201 ? -9.075  -39.607 -19.929 1.00 133.55 ? 200  LYS A CE  1 
ATOM   1590 N NZ  . LYS A 1 201 ? -8.378  -39.780 -21.241 1.00 138.49 ? 200  LYS A NZ  1 
ATOM   1591 N N   . GLU A 1 202 ? -8.953  -43.151 -13.794 1.00 103.45 ? 201  GLU A N   1 
ATOM   1592 C CA  . GLU A 1 202 ? -8.677  -44.410 -13.118 1.00 99.68  ? 201  GLU A CA  1 
ATOM   1593 C C   . GLU A 1 202 ? -9.867  -44.855 -12.276 1.00 98.61  ? 201  GLU A C   1 
ATOM   1594 O O   . GLU A 1 202 ? -10.346 -45.982 -12.422 1.00 101.16 ? 201  GLU A O   1 
ATOM   1595 C CB  . GLU A 1 202 ? -7.413  -44.313 -12.257 1.00 106.36 ? 201  GLU A CB  1 
ATOM   1596 C CG  . GLU A 1 202 ? -6.115  -44.692 -12.973 1.00 121.61 ? 201  GLU A CG  1 
ATOM   1597 C CD  . GLU A 1 202 ? -5.843  -46.193 -12.982 1.00 139.14 ? 201  GLU A CD  1 
ATOM   1598 O OE1 . GLU A 1 202 ? -6.806  -46.983 -12.866 1.00 154.84 ? 201  GLU A OE1 1 
ATOM   1599 O OE2 . GLU A 1 202 ? -4.662  -46.586 -13.111 1.00 136.28 ? 201  GLU A OE2 1 
ATOM   1600 N N   . ILE A 1 203 ? -10.351 -43.981 -11.399 1.00 87.74  ? 202  ILE A N   1 
ATOM   1601 C CA  . ILE A 1 203 ? -11.490 -44.350 -10.569 1.00 95.01  ? 202  ILE A CA  1 
ATOM   1602 C C   . ILE A 1 203 ? -12.713 -44.604 -11.450 1.00 103.70 ? 202  ILE A C   1 
ATOM   1603 O O   . ILE A 1 203 ? -13.517 -45.485 -11.168 1.00 106.41 ? 202  ILE A O   1 
ATOM   1604 C CB  . ILE A 1 203 ? -11.830 -43.286 -9.503  1.00 109.80 ? 202  ILE A CB  1 
ATOM   1605 C CG1 . ILE A 1 203 ? -12.927 -42.351 -10.000 1.00 123.19 ? 202  ILE A CG1 1 
ATOM   1606 C CG2 . ILE A 1 203 ? -10.589 -42.495 -9.077  1.00 110.29 ? 202  ILE A CG2 1 
ATOM   1607 C CD1 . ILE A 1 203 ? -13.195 -41.216 -9.059  1.00 129.22 ? 202  ILE A CD1 1 
ATOM   1608 N N   . ASP A 1 204 ? -12.840 -43.835 -12.527 1.00 108.96 ? 203  ASP A N   1 
ATOM   1609 C CA  . ASP A 1 204 ? -13.952 -43.989 -13.457 1.00 108.06 ? 203  ASP A CA  1 
ATOM   1610 C C   . ASP A 1 204 ? -13.871 -45.308 -14.225 1.00 112.68 ? 203  ASP A C   1 
ATOM   1611 O O   . ASP A 1 204 ? -14.883 -45.989 -14.424 1.00 117.10 ? 203  ASP A O   1 
ATOM   1612 C CB  . ASP A 1 204 ? -14.005 -42.802 -14.424 1.00 115.94 ? 203  ASP A CB  1 
ATOM   1613 C CG  . ASP A 1 204 ? -14.537 -41.535 -13.767 1.00 121.86 ? 203  ASP A CG  1 
ATOM   1614 O OD1 . ASP A 1 204 ? -15.048 -41.639 -12.629 1.00 119.58 ? 203  ASP A OD1 1 
ATOM   1615 O OD2 . ASP A 1 204 ? -14.449 -40.445 -14.386 1.00 123.00 ? 203  ASP A OD2 1 
ATOM   1616 N N   . MET A 1 205 ? -12.665 -45.666 -14.653 1.00 113.33 ? 204  MET A N   1 
ATOM   1617 C CA  . MET A 1 205 ? -12.446 -46.935 -15.335 1.00 122.05 ? 204  MET A CA  1 
ATOM   1618 C C   . MET A 1 205 ? -12.661 -48.079 -14.349 1.00 121.80 ? 204  MET A C   1 
ATOM   1619 O O   . MET A 1 205 ? -12.762 -49.239 -14.735 1.00 122.41 ? 204  MET A O   1 
ATOM   1620 C CB  . MET A 1 205 ? -11.040 -46.983 -15.939 1.00 130.58 ? 204  MET A CB  1 
ATOM   1621 C CG  . MET A 1 205 ? -10.799 -48.115 -16.933 1.00 138.54 ? 204  MET A CG  1 
ATOM   1622 S SD  . MET A 1 205 ? -9.733  -49.410 -16.266 1.00 194.70 ? 204  MET A SD  1 
ATOM   1623 C CE  . MET A 1 205 ? -8.492  -48.433 -15.408 1.00 151.90 ? 204  MET A CE  1 
ATOM   1624 N N   . SER A 1 206 ? -12.728 -47.738 -13.067 1.00 122.22 ? 205  SER A N   1 
ATOM   1625 C CA  . SER A 1 206 ? -13.049 -48.705 -12.027 1.00 113.23 ? 205  SER A CA  1 
ATOM   1626 C C   . SER A 1 206 ? -14.560 -48.772 -11.813 1.00 115.74 ? 205  SER A C   1 
ATOM   1627 O O   . SER A 1 206 ? -15.092 -49.829 -11.480 1.00 123.11 ? 205  SER A O   1 
ATOM   1628 C CB  . SER A 1 206 ? -12.344 -48.355 -10.705 1.00 107.57 ? 205  SER A CB  1 
ATOM   1629 O OG  . SER A 1 206 ? -10.995 -48.801 -10.676 1.00 105.94 ? 205  SER A OG  1 
ATOM   1630 N N   . VAL A 1 207 ? -15.250 -47.649 -12.002 1.00 111.21 ? 206  VAL A N   1 
ATOM   1631 C CA  . VAL A 1 207 ? -16.687 -47.598 -11.741 1.00 116.75 ? 206  VAL A CA  1 
ATOM   1632 C C   . VAL A 1 207 ? -17.490 -48.218 -12.885 1.00 131.70 ? 206  VAL A C   1 
ATOM   1633 O O   . VAL A 1 207 ? -18.431 -48.990 -12.657 1.00 133.28 ? 206  VAL A O   1 
ATOM   1634 C CB  . VAL A 1 207 ? -17.189 -46.162 -11.460 1.00 110.22 ? 206  VAL A CB  1 
ATOM   1635 C CG1 . VAL A 1 207 ? -18.634 -46.184 -10.986 1.00 103.54 ? 206  VAL A CG1 1 
ATOM   1636 C CG2 . VAL A 1 207 ? -16.327 -45.498 -10.412 1.00 103.92 ? 206  VAL A CG2 1 
ATOM   1637 N N   . SER A 1 208 ? -17.120 -47.892 -14.118 1.00 134.79 ? 207  SER A N   1 
ATOM   1638 C CA  . SER A 1 208 ? -17.772 -48.520 -15.258 1.00 143.78 ? 207  SER A CA  1 
ATOM   1639 C C   . SER A 1 208 ? -17.290 -49.964 -15.370 1.00 142.56 ? 207  SER A C   1 
ATOM   1640 O O   . SER A 1 208 ? -17.643 -50.683 -16.311 1.00 148.78 ? 207  SER A O   1 
ATOM   1641 C CB  . SER A 1 208 ? -17.492 -47.750 -16.547 1.00 149.51 ? 207  SER A CB  1 
ATOM   1642 O OG  . SER A 1 208 ? -16.106 -47.727 -16.828 1.00 154.75 ? 207  SER A OG  1 
ATOM   1643 N N   . GLN A 1 209 ? -16.483 -50.381 -14.399 1.00 129.07 ? 208  GLN A N   1 
ATOM   1644 C CA  . GLN A 1 209 ? -15.975 -51.743 -14.363 1.00 126.85 ? 208  GLN A CA  1 
ATOM   1645 C C   . GLN A 1 209 ? -16.497 -52.488 -13.138 1.00 122.15 ? 208  GLN A C   1 
ATOM   1646 O O   . GLN A 1 209 ? -16.145 -53.648 -12.906 1.00 120.60 ? 208  GLN A O   1 
ATOM   1647 C CB  . GLN A 1 209 ? -14.446 -51.752 -14.386 1.00 126.24 ? 208  GLN A CB  1 
ATOM   1648 C CG  . GLN A 1 209 ? -13.851 -53.119 -14.672 1.00 134.60 ? 208  GLN A CG  1 
ATOM   1649 C CD  . GLN A 1 209 ? -12.342 -53.094 -14.790 1.00 140.81 ? 208  GLN A CD  1 
ATOM   1650 O OE1 . GLN A 1 209 ? -11.681 -52.166 -14.316 1.00 139.11 ? 208  GLN A OE1 1 
ATOM   1651 N NE2 . GLN A 1 209 ? -11.784 -54.121 -15.421 1.00 144.63 ? 208  GLN A NE2 1 
ATOM   1652 N N   . GLY A 1 210 ? -17.342 -51.818 -12.359 1.00 117.16 ? 209  GLY A N   1 
ATOM   1653 C CA  . GLY A 1 210 ? -17.962 -52.433 -11.196 1.00 118.39 ? 209  GLY A CA  1 
ATOM   1654 C C   . GLY A 1 210 ? -16.991 -52.824 -10.095 1.00 120.18 ? 209  GLY A C   1 
ATOM   1655 O O   . GLY A 1 210 ? -17.182 -53.838 -9.415  1.00 115.63 ? 209  GLY A O   1 
ATOM   1656 N N   . LEU A 1 211 ? -15.943 -52.019 -9.923  1.00 116.66 ? 210  LEU A N   1 
ATOM   1657 C CA  . LEU A 1 211 ? -14.988 -52.219 -8.841  1.00 99.54  ? 210  LEU A CA  1 
ATOM   1658 C C   . LEU A 1 211 ? -15.386 -51.346 -7.669  1.00 98.70  ? 210  LEU A C   1 
ATOM   1659 O O   . LEU A 1 211 ? -14.894 -51.524 -6.549  1.00 95.88  ? 210  LEU A O   1 
ATOM   1660 C CB  . LEU A 1 211 ? -13.569 -51.895 -9.292  1.00 97.78  ? 210  LEU A CB  1 
ATOM   1661 C CG  . LEU A 1 211 ? -12.815 -52.982 -10.059 1.00 99.23  ? 210  LEU A CG  1 
ATOM   1662 C CD1 . LEU A 1 211 ? -11.369 -52.529 -10.310 1.00 100.44 ? 210  LEU A CD1 1 
ATOM   1663 C CD2 . LEU A 1 211 ? -12.861 -54.323 -9.303  1.00 79.70  ? 210  LEU A CD2 1 
ATOM   1664 N N   . ILE A 1 212 ? -16.283 -50.400 -7.941  1.00 107.50 ? 211  ILE A N   1 
ATOM   1665 C CA  . ILE A 1 212 ? -16.910 -49.590 -6.896  1.00 114.27 ? 211  ILE A CA  1 
ATOM   1666 C C   . ILE A 1 212 ? -18.332 -49.163 -7.272  1.00 124.04 ? 211  ILE A C   1 
ATOM   1667 O O   . ILE A 1 212 ? -18.574 -48.639 -8.362  1.00 130.42 ? 211  ILE A O   1 
ATOM   1668 C CB  . ILE A 1 212 ? -16.060 -48.349 -6.504  1.00 132.74 ? 211  ILE A CB  1 
ATOM   1669 C CG1 . ILE A 1 212 ? -15.536 -47.613 -7.736  1.00 117.86 ? 211  ILE A CG1 1 
ATOM   1670 C CG2 . ILE A 1 212 ? -14.886 -48.756 -5.640  1.00 145.49 ? 211  ILE A CG2 1 
ATOM   1671 C CD1 . ILE A 1 212 ? -14.259 -46.852 -7.463  1.00 106.42 ? 211  ILE A CD1 1 
ATOM   1672 N N   . ASN A 1 213 ? -19.266 -49.403 -6.355  1.00 122.97 ? 212  ASN A N   1 
ATOM   1673 C CA  . ASN A 1 213 ? -20.662 -49.024 -6.534  1.00 123.64 ? 212  ASN A CA  1 
ATOM   1674 C C   . ASN A 1 213 ? -21.152 -48.107 -5.408  1.00 120.38 ? 212  ASN A C   1 
ATOM   1675 O O   . ASN A 1 213 ? -21.081 -48.457 -4.233  1.00 123.67 ? 212  ASN A O   1 
ATOM   1676 C CB  . ASN A 1 213 ? -21.546 -50.275 -6.660  1.00 130.09 ? 212  ASN A CB  1 
ATOM   1677 C CG  . ASN A 1 213 ? -21.307 -51.289 -5.541  1.00 143.55 ? 212  ASN A CG  1 
ATOM   1678 O OD1 . ASN A 1 213 ? -20.447 -51.101 -4.683  1.00 146.31 ? 212  ASN A OD1 1 
ATOM   1679 N ND2 . ASN A 1 213 ? -22.077 -52.374 -5.552  1.00 151.76 ? 212  ASN A ND2 1 
ATOM   1680 N N   . ALA A 1 214 ? -21.635 -46.923 -5.766  1.00 126.26 ? 213  ALA A N   1 
ATOM   1681 C CA  . ALA A 1 214 ? -22.093 -45.966 -4.765  1.00 146.65 ? 213  ALA A CA  1 
ATOM   1682 C C   . ALA A 1 214 ? -23.470 -45.441 -5.118  1.00 166.65 ? 213  ALA A C   1 
ATOM   1683 O O   . ALA A 1 214 ? -23.945 -45.647 -6.232  1.00 175.73 ? 213  ALA A O   1 
ATOM   1684 C CB  . ALA A 1 214 ? -21.108 -44.817 -4.640  1.00 150.79 ? 213  ALA A CB  1 
ATOM   1685 N N   . ARG A 1 215 ? -24.113 -44.760 -4.177  1.00 180.48 ? 214  ARG A N   1 
ATOM   1686 C CA  . ARG A 1 215 ? -25.457 -44.247 -4.428  1.00 198.03 ? 214  ARG A CA  1 
ATOM   1687 C C   . ARG A 1 215 ? -25.437 -42.817 -4.969  1.00 194.77 ? 214  ARG A C   1 
ATOM   1688 O O   . ARG A 1 215 ? -26.323 -42.429 -5.734  1.00 202.75 ? 214  ARG A O   1 
ATOM   1689 C CB  . ARG A 1 215 ? -26.342 -44.358 -3.179  1.00 208.79 ? 214  ARG A CB  1 
ATOM   1690 C CG  . ARG A 1 215 ? -27.807 -43.966 -3.405  1.00 216.12 ? 214  ARG A CG  1 
ATOM   1691 C CD  . ARG A 1 215 ? -28.426 -44.695 -4.596  1.00 221.67 ? 214  ARG A CD  1 
ATOM   1692 N NE  . ARG A 1 215 ? -29.811 -44.287 -4.824  1.00 229.63 ? 214  ARG A NE  1 
ATOM   1693 C CZ  . ARG A 1 215 ? -30.572 -44.730 -5.821  1.00 238.34 ? 214  ARG A CZ  1 
ATOM   1694 N NH1 . ARG A 1 215 ? -30.084 -45.600 -6.694  1.00 241.05 ? 214  ARG A NH1 1 
ATOM   1695 N NH2 . ARG A 1 215 ? -31.822 -44.303 -5.946  1.00 242.24 ? 214  ARG A NH2 1 
ATOM   1696 N N   . GLU A 1 216 ? -24.427 -42.044 -4.577  1.00 177.74 ? 215  GLU A N   1 
ATOM   1697 C CA  . GLU A 1 216 ? -24.256 -40.686 -5.091  1.00 174.01 ? 215  GLU A CA  1 
ATOM   1698 C C   . GLU A 1 216 ? -25.284 -39.706 -4.526  1.00 162.37 ? 215  GLU A C   1 
ATOM   1699 O O   . GLU A 1 216 ? -25.996 -39.050 -5.285  1.00 167.68 ? 215  GLU A O   1 
ATOM   1700 C CB  . GLU A 1 216 ? -24.339 -40.675 -6.625  1.00 186.51 ? 215  GLU A CB  1 
ATOM   1701 C CG  . GLU A 1 216 ? -23.198 -41.377 -7.348  1.00 190.74 ? 215  GLU A CG  1 
ATOM   1702 C CD  . GLU A 1 216 ? -22.028 -40.452 -7.623  1.00 191.42 ? 215  GLU A CD  1 
ATOM   1703 O OE1 . GLU A 1 216 ? -21.920 -39.413 -6.940  1.00 190.96 ? 215  GLU A OE1 1 
ATOM   1704 O OE2 . GLU A 1 216 ? -21.217 -40.763 -8.521  1.00 192.69 ? 215  GLU A OE2 1 
ATOM   1705 N N   . GLY A 1 217 ? -25.358 -39.600 -3.202  1.00 147.12 ? 216  GLY A N   1 
ATOM   1706 C CA  . GLY A 1 217 ? -26.275 -38.669 -2.561  1.00 143.86 ? 216  GLY A CA  1 
ATOM   1707 C C   . GLY A 1 217 ? -26.159 -37.232 -3.056  1.00 149.31 ? 216  GLY A C   1 
ATOM   1708 O O   . GLY A 1 217 ? -25.375 -36.937 -3.961  1.00 152.30 ? 216  GLY A O   1 
ATOM   1709 N N   . LYS A 1 218 ? -26.941 -36.332 -2.461  1.00 149.01 ? 217  LYS A N   1 
ATOM   1710 C CA  . LYS A 1 218 ? -26.940 -34.921 -2.856  1.00 147.37 ? 217  LYS A CA  1 
ATOM   1711 C C   . LYS A 1 218 ? -25.531 -34.325 -2.792  1.00 138.73 ? 217  LYS A C   1 
ATOM   1712 O O   . LYS A 1 218 ? -25.102 -33.616 -3.706  1.00 132.34 ? 217  LYS A O   1 
ATOM   1713 C CB  . LYS A 1 218 ? -27.909 -34.106 -1.985  1.00 152.17 ? 217  LYS A CB  1 
ATOM   1714 C CG  . LYS A 1 218 ? -28.162 -32.681 -2.482  1.00 158.50 ? 217  LYS A CG  1 
ATOM   1715 C CD  . LYS A 1 218 ? -29.200 -31.951 -1.632  1.00 163.28 ? 217  LYS A CD  1 
ATOM   1716 C CE  . LYS A 1 218 ? -29.578 -30.595 -2.236  1.00 165.97 ? 217  LYS A CE  1 
ATOM   1717 N NZ  . LYS A 1 218 ? -28.446 -29.616 -2.246  1.00 160.25 ? 217  LYS A NZ  1 
ATOM   1718 N N   . LEU A 1 219 ? -24.821 -34.622 -1.707  1.00 132.01 ? 218  LEU A N   1 
ATOM   1719 C CA  . LEU A 1 219 ? -23.443 -34.176 -1.529  1.00 116.60 ? 218  LEU A CA  1 
ATOM   1720 C C   . LEU A 1 219 ? -22.483 -35.208 -2.120  1.00 115.64 ? 218  LEU A C   1 
ATOM   1721 O O   . LEU A 1 219 ? -22.753 -36.415 -2.082  1.00 116.81 ? 218  LEU A O   1 
ATOM   1722 C CB  . LEU A 1 219 ? -23.150 -33.935 -0.047  1.00 106.04 ? 218  LEU A CB  1 
ATOM   1723 C CG  . LEU A 1 219 ? -23.680 -32.623 0.546   1.00 106.70 ? 218  LEU A CG  1 
ATOM   1724 C CD1 . LEU A 1 219 ? -25.066 -32.302 0.011   1.00 118.35 ? 218  LEU A CD1 1 
ATOM   1725 C CD2 . LEU A 1 219 ? -23.669 -32.624 2.085   1.00 89.27  ? 218  LEU A CD2 1 
ATOM   1726 N N   . LYS A 1 220 ? -21.371 -34.737 -2.679  1.00 111.69 ? 219  LYS A N   1 
ATOM   1727 C CA  . LYS A 1 220 ? -20.467 -35.630 -3.401  1.00 108.15 ? 219  LYS A CA  1 
ATOM   1728 C C   . LYS A 1 220 ? -19.082 -35.826 -2.768  1.00 101.35 ? 219  LYS A C   1 
ATOM   1729 O O   . LYS A 1 220 ? -18.485 -34.899 -2.201  1.00 88.20  ? 219  LYS A O   1 
ATOM   1730 C CB  . LYS A 1 220 ? -20.340 -35.214 -4.873  1.00 104.84 ? 219  LYS A CB  1 
ATOM   1731 C CG  . LYS A 1 220 ? -21.046 -36.161 -5.829  1.00 116.86 ? 219  LYS A CG  1 
ATOM   1732 C CD  . LYS A 1 220 ? -20.807 -35.774 -7.281  1.00 126.98 ? 219  LYS A CD  1 
ATOM   1733 C CE  . LYS A 1 220 ? -21.513 -36.717 -8.255  1.00 121.23 ? 219  LYS A CE  1 
ATOM   1734 N NZ  . LYS A 1 220 ? -20.986 -36.580 -9.648  1.00 115.27 ? 219  LYS A NZ  1 
ATOM   1735 N N   . SER A 1 221 ? -18.597 -37.061 -2.876  1.00 97.27  ? 220  SER A N   1 
ATOM   1736 C CA  . SER A 1 221 ? -17.262 -37.431 -2.441  1.00 97.61  ? 220  SER A CA  1 
ATOM   1737 C C   . SER A 1 221 ? -16.219 -36.847 -3.378  1.00 97.57  ? 220  SER A C   1 
ATOM   1738 O O   . SER A 1 221 ? -16.280 -37.046 -4.591  1.00 97.48  ? 220  SER A O   1 
ATOM   1739 C CB  . SER A 1 221 ? -17.120 -38.950 -2.399  1.00 97.03  ? 220  SER A CB  1 
ATOM   1740 O OG  . SER A 1 221 ? -17.641 -39.476 -1.192  1.00 93.18  ? 220  SER A OG  1 
ATOM   1741 N N   . GLN A 1 222 ? -15.263 -36.124 -2.808  1.00 91.23  ? 221  GLN A N   1 
ATOM   1742 C CA  . GLN A 1 222 ? -14.245 -35.454 -3.607  1.00 89.68  ? 221  GLN A CA  1 
ATOM   1743 C C   . GLN A 1 222 ? -12.848 -35.890 -3.157  1.00 87.95  ? 221  GLN A C   1 
ATOM   1744 O O   . GLN A 1 222 ? -12.657 -36.316 -2.024  1.00 85.02  ? 221  GLN A O   1 
ATOM   1745 C CB  . GLN A 1 222 ? -14.430 -33.934 -3.533  1.00 82.90  ? 221  GLN A CB  1 
ATOM   1746 C CG  . GLN A 1 222 ? -15.886 -33.465 -3.747  1.00 86.79  ? 221  GLN A CG  1 
ATOM   1747 C CD  . GLN A 1 222 ? -16.076 -31.961 -3.521  1.00 91.01  ? 221  GLN A CD  1 
ATOM   1748 O OE1 . GLN A 1 222 ? -15.224 -31.161 -3.904  1.00 93.39  ? 221  GLN A OE1 1 
ATOM   1749 N NE2 . GLN A 1 222 ? -17.194 -31.575 -2.897  1.00 79.37  ? 221  GLN A NE2 1 
ATOM   1750 N N   . PHE A 1 223 ? -11.883 -35.816 -4.064  1.00 91.10  ? 222  PHE A N   1 
ATOM   1751 C CA  . PHE A 1 223 ? -10.525 -36.276 -3.794  1.00 84.61  ? 222  PHE A CA  1 
ATOM   1752 C C   . PHE A 1 223 ? -9.562  -35.151 -4.157  1.00 89.58  ? 222  PHE A C   1 
ATOM   1753 O O   . PHE A 1 223 ? -9.167  -34.994 -5.315  1.00 91.41  ? 222  PHE A O   1 
ATOM   1754 C CB  . PHE A 1 223 ? -10.227 -37.530 -4.616  1.00 87.11  ? 222  PHE A CB  1 
ATOM   1755 C CG  . PHE A 1 223 ? -9.034  -38.313 -4.144  1.00 90.37  ? 222  PHE A CG  1 
ATOM   1756 C CD1 . PHE A 1 223 ? -8.042  -37.716 -3.377  1.00 96.91  ? 222  PHE A CD1 1 
ATOM   1757 C CD2 . PHE A 1 223 ? -8.898  -39.651 -4.484  1.00 84.31  ? 222  PHE A CD2 1 
ATOM   1758 C CE1 . PHE A 1 223 ? -6.944  -38.444 -2.951  1.00 89.77  ? 222  PHE A CE1 1 
ATOM   1759 C CE2 . PHE A 1 223 ? -7.803  -40.382 -4.067  1.00 82.98  ? 222  PHE A CE2 1 
ATOM   1760 C CZ  . PHE A 1 223 ? -6.825  -39.779 -3.299  1.00 85.73  ? 222  PHE A CZ  1 
ATOM   1761 N N   . LEU A 1 224 ? -9.198  -34.365 -3.150  1.00 87.60  ? 223  LEU A N   1 
ATOM   1762 C CA  . LEU A 1 224 ? -8.414  -33.152 -3.343  1.00 85.02  ? 223  LEU A CA  1 
ATOM   1763 C C   . LEU A 1 224 ? -6.927  -33.453 -3.480  1.00 79.95  ? 223  LEU A C   1 
ATOM   1764 O O   . LEU A 1 224 ? -6.319  -34.033 -2.582  1.00 84.97  ? 223  LEU A O   1 
ATOM   1765 C CB  . LEU A 1 224 ? -8.653  -32.205 -2.165  1.00 81.29  ? 223  LEU A CB  1 
ATOM   1766 C CG  . LEU A 1 224 ? -7.902  -30.884 -2.175  1.00 76.63  ? 223  LEU A CG  1 
ATOM   1767 C CD1 . LEU A 1 224 ? -8.074  -30.212 -3.525  1.00 74.40  ? 223  LEU A CD1 1 
ATOM   1768 C CD2 . LEU A 1 224 ? -8.395  -30.002 -1.038  1.00 71.91  ? 223  LEU A CD2 1 
ATOM   1769 N N   . ILE A 1 225 ? -6.343  -33.050 -4.602  1.00 76.41  ? 224  ILE A N   1 
ATOM   1770 C CA  . ILE A 1 225 ? -4.925  -33.299 -4.840  1.00 74.85  ? 224  ILE A CA  1 
ATOM   1771 C C   . ILE A 1 225 ? -4.060  -32.046 -4.782  1.00 71.21  ? 224  ILE A C   1 
ATOM   1772 O O   . ILE A 1 225 ? -4.271  -31.085 -5.508  1.00 72.83  ? 224  ILE A O   1 
ATOM   1773 C CB  . ILE A 1 225 ? -4.686  -34.069 -6.130  1.00 72.21  ? 224  ILE A CB  1 
ATOM   1774 C CG1 . ILE A 1 225 ? -5.191  -35.500 -5.949  1.00 81.08  ? 224  ILE A CG1 1 
ATOM   1775 C CG2 . ILE A 1 225 ? -3.212  -34.075 -6.460  1.00 66.49  ? 224  ILE A CG2 1 
ATOM   1776 C CD1 . ILE A 1 225 ? -4.913  -36.397 -7.114  1.00 98.11  ? 224  ILE A CD1 1 
ATOM   1777 N N   . LEU A 1 226 ? -3.069  -32.084 -3.903  1.00 77.95  ? 225  LEU A N   1 
ATOM   1778 C CA  . LEU A 1 226 ? -2.323  -30.895 -3.527  1.00 74.08  ? 225  LEU A CA  1 
ATOM   1779 C C   . LEU A 1 226 ? -0.814  -31.063 -3.641  1.00 77.67  ? 225  LEU A C   1 
ATOM   1780 O O   . LEU A 1 226 ? -0.251  -32.109 -3.283  1.00 73.10  ? 225  LEU A O   1 
ATOM   1781 C CB  . LEU A 1 226 ? -2.678  -30.496 -2.091  1.00 66.61  ? 225  LEU A CB  1 
ATOM   1782 C CG  . LEU A 1 226 ? -4.105  -29.990 -1.907  1.00 67.01  ? 225  LEU A CG  1 
ATOM   1783 C CD1 . LEU A 1 226 ? -4.483  -29.772 -0.429  1.00 59.12  ? 225  LEU A CD1 1 
ATOM   1784 C CD2 . LEU A 1 226 ? -4.252  -28.719 -2.701  1.00 69.44  ? 225  LEU A CD2 1 
ATOM   1785 N N   . ASP A 1 227 ? -0.170  -30.011 -4.140  1.00 78.21  ? 226  ASP A N   1 
ATOM   1786 C CA  . ASP A 1 227 ? 1.276   -29.869 -4.040  1.00 71.44  ? 226  ASP A CA  1 
ATOM   1787 C C   . ASP A 1 227 ? 1.689   -29.470 -2.617  1.00 72.54  ? 226  ASP A C   1 
ATOM   1788 O O   . ASP A 1 227 ? 0.915   -28.827 -1.892  1.00 66.40  ? 226  ASP A O   1 
ATOM   1789 C CB  . ASP A 1 227 ? 1.757   -28.828 -5.032  1.00 63.23  ? 226  ASP A CB  1 
ATOM   1790 C CG  . ASP A 1 227 ? 1.983   -29.400 -6.408  1.00 73.53  ? 226  ASP A CG  1 
ATOM   1791 O OD1 . ASP A 1 227 ? 2.733   -30.390 -6.512  1.00 76.49  ? 226  ASP A OD1 1 
ATOM   1792 O OD2 . ASP A 1 227 ? 1.427   -28.854 -7.386  1.00 78.13  ? 226  ASP A OD2 1 
ATOM   1793 N N   . ARG A 1 228 ? 2.899   -29.859 -2.213  1.00 63.14  ? 227  ARG A N   1 
ATOM   1794 C CA  . ARG A 1 228 ? 3.383   -29.500 -0.888  1.00 59.40  ? 227  ARG A CA  1 
ATOM   1795 C C   . ARG A 1 228 ? 3.286   -27.991 -0.716  1.00 66.67  ? 227  ARG A C   1 
ATOM   1796 O O   . ARG A 1 228 ? 3.038   -27.500 0.383   1.00 62.61  ? 227  ARG A O   1 
ATOM   1797 C CB  . ARG A 1 228 ? 4.824   -29.973 -0.659  1.00 64.10  ? 227  ARG A CB  1 
ATOM   1798 C CG  . ARG A 1 228 ? 5.142   -30.252 0.805   1.00 54.28  ? 227  ARG A CG  1 
ATOM   1799 C CD  . ARG A 1 228 ? 4.140   -29.516 1.677   1.00 51.20  ? 227  ARG A CD  1 
ATOM   1800 N NE  . ARG A 1 228 ? 3.613   -30.329 2.752   1.00 55.71  ? 227  ARG A NE  1 
ATOM   1801 C CZ  . ARG A 1 228 ? 2.547   -30.007 3.476   1.00 63.76  ? 227  ARG A CZ  1 
ATOM   1802 N NH1 . ARG A 1 228 ? 1.879   -28.890 3.236   1.00 50.49  ? 227  ARG A NH1 1 
ATOM   1803 N NH2 . ARG A 1 228 ? 2.145   -30.815 4.444   1.00 71.70  ? 227  ARG A NH2 1 
ATOM   1804 N N   . ALA A 1 229 ? 3.462   -27.268 -1.822  1.00 75.72  ? 228  ALA A N   1 
ATOM   1805 C CA  . ALA A 1 229 ? 3.433   -25.805 -1.843  1.00 62.38  ? 228  ALA A CA  1 
ATOM   1806 C C   . ALA A 1 229 ? 2.105   -25.174 -1.406  1.00 62.94  ? 228  ALA A C   1 
ATOM   1807 O O   . ALA A 1 229 ? 2.013   -23.958 -1.265  1.00 67.41  ? 228  ALA A O   1 
ATOM   1808 C CB  . ALA A 1 229 ? 3.787   -25.324 -3.212  1.00 61.23  ? 228  ALA A CB  1 
ATOM   1809 N N   . VAL A 1 230 ? 1.073   -25.984 -1.210  1.00 56.70  ? 229  VAL A N   1 
ATOM   1810 C CA  . VAL A 1 230 ? -0.205  -25.460 -0.752  1.00 58.70  ? 229  VAL A CA  1 
ATOM   1811 C C   . VAL A 1 230 ? -0.033  -24.676 0.553   1.00 66.98  ? 229  VAL A C   1 
ATOM   1812 O O   . VAL A 1 230 ? -0.751  -23.701 0.809   1.00 74.47  ? 229  VAL A O   1 
ATOM   1813 C CB  . VAL A 1 230 ? -1.209  -26.599 -0.538  1.00 65.12  ? 229  VAL A CB  1 
ATOM   1814 C CG1 . VAL A 1 230 ? -0.716  -27.541 0.572   1.00 54.39  ? 229  VAL A CG1 1 
ATOM   1815 C CG2 . VAL A 1 230 ? -2.594  -26.044 -0.230  1.00 66.06  ? 229  VAL A CG2 1 
ATOM   1816 N N   . ASP A 1 231 ? 0.939   -25.115 1.354   1.00 61.02  ? 230  ASP A N   1 
ATOM   1817 C CA  . ASP A 1 231 ? 1.215   -24.590 2.697   1.00 59.94  ? 230  ASP A CA  1 
ATOM   1818 C C   . ASP A 1 231 ? 2.593   -25.089 3.190   1.00 63.15  ? 230  ASP A C   1 
ATOM   1819 O O   . ASP A 1 231 ? 2.755   -26.249 3.572   1.00 73.37  ? 230  ASP A O   1 
ATOM   1820 C CB  . ASP A 1 231 ? 0.086   -24.966 3.670   1.00 53.87  ? 230  ASP A CB  1 
ATOM   1821 C CG  . ASP A 1 231 ? 0.393   -24.601 5.128   1.00 64.07  ? 230  ASP A CG  1 
ATOM   1822 O OD1 . ASP A 1 231 ? 1.524   -24.154 5.433   1.00 61.34  ? 230  ASP A OD1 1 
ATOM   1823 O OD2 . ASP A 1 231 ? -0.516  -24.775 5.977   1.00 66.35  ? 230  ASP A OD2 1 
ATOM   1824 N N   . LEU A 1 232 ? 3.583   -24.201 3.164   1.00 54.68  ? 231  LEU A N   1 
ATOM   1825 C CA  . LEU A 1 232 ? 4.955   -24.545 3.505   1.00 56.33  ? 231  LEU A CA  1 
ATOM   1826 C C   . LEU A 1 232 ? 5.279   -24.196 4.953   1.00 60.62  ? 231  LEU A C   1 
ATOM   1827 O O   . LEU A 1 232 ? 6.394   -24.413 5.409   1.00 59.86  ? 231  LEU A O   1 
ATOM   1828 C CB  . LEU A 1 232 ? 5.918   -23.824 2.560   1.00 54.59  ? 231  LEU A CB  1 
ATOM   1829 C CG  . LEU A 1 232 ? 6.523   -24.630 1.413   1.00 57.46  ? 231  LEU A CG  1 
ATOM   1830 C CD1 . LEU A 1 232 ? 5.711   -25.864 1.095   1.00 56.46  ? 231  LEU A CD1 1 
ATOM   1831 C CD2 . LEU A 1 232 ? 6.710   -23.777 0.176   1.00 60.47  ? 231  LEU A CD2 1 
ATOM   1832 N N   . LYS A 1 233 ? 4.287   -23.672 5.668   1.00 57.15  ? 232  LYS A N   1 
ATOM   1833 C CA  . LYS A 1 233 ? 4.462   -23.241 7.048   1.00 56.83  ? 232  LYS A CA  1 
ATOM   1834 C C   . LYS A 1 233 ? 4.093   -24.317 8.064   1.00 60.01  ? 232  LYS A C   1 
ATOM   1835 O O   . LYS A 1 233 ? 4.823   -24.535 9.031   1.00 66.69  ? 232  LYS A O   1 
ATOM   1836 C CB  . LYS A 1 233 ? 3.641   -21.981 7.308   1.00 73.21  ? 232  LYS A CB  1 
ATOM   1837 C CG  . LYS A 1 233 ? 4.157   -20.747 6.592   1.00 74.39  ? 232  LYS A CG  1 
ATOM   1838 C CD  . LYS A 1 233 ? 3.111   -19.656 6.558   1.00 73.18  ? 232  LYS A CD  1 
ATOM   1839 C CE  . LYS A 1 233 ? 3.616   -18.471 5.754   1.00 82.22  ? 232  LYS A CE  1 
ATOM   1840 N NZ  . LYS A 1 233 ? 2.536   -17.493 5.480   1.00 83.60  ? 232  LYS A NZ  1 
ATOM   1841 N N   . SER A 1 234 ? 2.963   -24.986 7.842   1.00 60.26  ? 233  SER A N   1 
ATOM   1842 C CA  . SER A 1 234 ? 2.476   -26.040 8.749   1.00 52.58  ? 233  SER A CA  1 
ATOM   1843 C C   . SER A 1 234 ? 3.498   -27.124 9.113   1.00 56.87  ? 233  SER A C   1 
ATOM   1844 O O   . SER A 1 234 ? 3.576   -27.521 10.276  1.00 58.47  ? 233  SER A O   1 
ATOM   1845 C CB  . SER A 1 234 ? 1.213   -26.677 8.185   1.00 44.99  ? 233  SER A CB  1 
ATOM   1846 O OG  . SER A 1 234 ? 0.125   -25.802 8.328   1.00 57.37  ? 233  SER A OG  1 
ATOM   1847 N N   . PRO A 1 235 ? 4.266   -27.613 8.118   1.00 56.38  ? 234  PRO A N   1 
ATOM   1848 C CA  . PRO A 1 235 ? 5.350   -28.577 8.321   1.00 49.94  ? 234  PRO A CA  1 
ATOM   1849 C C   . PRO A 1 235 ? 6.423   -28.100 9.276   1.00 57.69  ? 234  PRO A C   1 
ATOM   1850 O O   . PRO A 1 235 ? 7.173   -28.941 9.767   1.00 74.71  ? 234  PRO A O   1 
ATOM   1851 C CB  . PRO A 1 235 ? 5.971   -28.703 6.931   1.00 45.05  ? 234  PRO A CB  1 
ATOM   1852 C CG  . PRO A 1 235 ? 4.882   -28.416 6.014   1.00 55.43  ? 234  PRO A CG  1 
ATOM   1853 C CD  . PRO A 1 235 ? 4.012   -27.391 6.685   1.00 58.28  ? 234  PRO A CD  1 
ATOM   1854 N N   . LEU A 1 236 ? 6.499   -26.797 9.545   1.00 47.94  ? 235  LEU A N   1 
ATOM   1855 C CA  . LEU A 1 236 ? 7.631   -26.262 10.303  1.00 53.50  ? 235  LEU A CA  1 
ATOM   1856 C C   . LEU A 1 236 ? 7.324   -25.856 11.745  1.00 50.76  ? 235  LEU A C   1 
ATOM   1857 O O   . LEU A 1 236 ? 8.207   -25.914 12.604  1.00 50.22  ? 235  LEU A O   1 
ATOM   1858 C CB  . LEU A 1 236 ? 8.290   -25.096 9.543   1.00 42.34  ? 235  LEU A CB  1 
ATOM   1859 C CG  . LEU A 1 236 ? 8.969   -25.478 8.224   1.00 46.31  ? 235  LEU A CG  1 
ATOM   1860 C CD1 . LEU A 1 236 ? 9.160   -24.241 7.334   1.00 46.34  ? 235  LEU A CD1 1 
ATOM   1861 C CD2 . LEU A 1 236 ? 10.295  -26.251 8.461   1.00 32.20  ? 235  LEU A CD2 1 
ATOM   1862 N N   . VAL A 1 237 ? 6.080   -25.466 12.008  1.00 46.48  ? 236  VAL A N   1 
ATOM   1863 C CA  . VAL A 1 237 ? 5.711   -24.859 13.293  1.00 58.58  ? 236  VAL A CA  1 
ATOM   1864 C C   . VAL A 1 237 ? 5.690   -25.827 14.481  1.00 64.62  ? 236  VAL A C   1 
ATOM   1865 O O   . VAL A 1 237 ? 5.061   -26.889 14.420  1.00 64.64  ? 236  VAL A O   1 
ATOM   1866 C CB  . VAL A 1 237 ? 4.312   -24.176 13.230  1.00 58.32  ? 236  VAL A CB  1 
ATOM   1867 C CG1 . VAL A 1 237 ? 4.281   -23.075 12.198  1.00 58.39  ? 236  VAL A CG1 1 
ATOM   1868 C CG2 . VAL A 1 237 ? 3.231   -25.186 12.914  1.00 51.35  ? 236  VAL A CG2 1 
ATOM   1869 N N   . HIS A 1 238 ? 6.374   -25.446 15.559  1.00 56.31  ? 237  HIS A N   1 
ATOM   1870 C CA  . HIS A 1 238 ? 6.168   -26.080 16.854  1.00 54.54  ? 237  HIS A CA  1 
ATOM   1871 C C   . HIS A 1 238 ? 4.691   -26.081 17.198  1.00 57.86  ? 237  HIS A C   1 
ATOM   1872 O O   . HIS A 1 238 ? 3.994   -25.083 17.078  1.00 78.73  ? 237  HIS A O   1 
ATOM   1873 C CB  . HIS A 1 238 ? 6.927   -25.355 17.952  1.00 47.01  ? 237  HIS A CB  1 
ATOM   1874 C CG  . HIS A 1 238 ? 8.361   -25.759 18.066  1.00 46.54  ? 237  HIS A CG  1 
ATOM   1875 N ND1 . HIS A 1 238 ? 9.379   -25.079 17.436  1.00 55.40  ? 237  HIS A ND1 1 
ATOM   1876 C CD2 . HIS A 1 238 ? 8.951   -26.760 18.758  1.00 55.03  ? 237  HIS A CD2 1 
ATOM   1877 C CE1 . HIS A 1 238 ? 10.534  -25.644 17.733  1.00 61.33  ? 237  HIS A CE1 1 
ATOM   1878 N NE2 . HIS A 1 238 ? 10.304  -26.663 18.539  1.00 58.91  ? 237  HIS A NE2 1 
ATOM   1879 N N   . GLU A 1 239 ? 4.214   -27.223 17.636  1.00 56.07  ? 238  GLU A N   1 
ATOM   1880 C CA  . GLU A 1 239 ? 2.795   -27.427 17.785  1.00 52.90  ? 238  GLU A CA  1 
ATOM   1881 C C   . GLU A 1 239 ? 2.583   -28.050 19.172  1.00 53.51  ? 238  GLU A C   1 
ATOM   1882 O O   . GLU A 1 239 ? 3.398   -28.859 19.607  1.00 61.61  ? 238  GLU A O   1 
ATOM   1883 C CB  . GLU A 1 239 ? 2.297   -28.295 16.620  1.00 32.08  ? 238  GLU A CB  1 
ATOM   1884 C CG  . GLU A 1 239 ? 0.810   -28.431 16.544  1.00 68.95  ? 238  GLU A CG  1 
ATOM   1885 C CD  . GLU A 1 239 ? 0.161   -27.403 15.645  1.00 77.43  ? 238  GLU A CD  1 
ATOM   1886 O OE1 . GLU A 1 239 ? 0.821   -27.004 14.650  1.00 54.86  ? 238  GLU A OE1 1 
ATOM   1887 O OE2 . GLU A 1 239 ? -1.014  -27.025 15.939  1.00 76.09  ? 238  GLU A OE2 1 
ATOM   1888 N N   . LEU A 1 240 ? 1.524   -27.634 19.867  1.00 45.28  ? 239  LEU A N   1 
ATOM   1889 C CA  . LEU A 1 240 ? 1.296   -28.002 21.265  1.00 56.83  ? 239  LEU A CA  1 
ATOM   1890 C C   . LEU A 1 240 ? 0.139   -28.992 21.505  1.00 64.37  ? 239  LEU A C   1 
ATOM   1891 O O   . LEU A 1 240 ? -0.357  -29.140 22.621  1.00 68.28  ? 239  LEU A O   1 
ATOM   1892 C CB  . LEU A 1 240 ? 1.071   -26.752 22.109  1.00 53.57  ? 239  LEU A CB  1 
ATOM   1893 C CG  . LEU A 1 240 ? 2.306   -25.899 22.382  1.00 57.58  ? 239  LEU A CG  1 
ATOM   1894 C CD1 . LEU A 1 240 ? 2.603   -25.019 21.191  1.00 58.96  ? 239  LEU A CD1 1 
ATOM   1895 C CD2 . LEU A 1 240 ? 2.082   -25.052 23.621  1.00 58.02  ? 239  LEU A CD2 1 
ATOM   1896 N N   . THR A 1 241 ? -0.302  -29.662 20.459  1.00 53.24  ? 240  THR A N   1 
ATOM   1897 C CA  . THR A 1 241 ? -1.239  -30.738 20.653  1.00 48.47  ? 240  THR A CA  1 
ATOM   1898 C C   . THR A 1 241 ? -0.407  -31.998 20.820  1.00 52.46  ? 240  THR A C   1 
ATOM   1899 O O   . THR A 1 241 ? 0.727   -32.061 20.357  1.00 54.24  ? 240  THR A O   1 
ATOM   1900 C CB  . THR A 1 241 ? -2.291  -30.804 19.524  1.00 54.62  ? 240  THR A CB  1 
ATOM   1901 O OG1 . THR A 1 241 ? -1.644  -30.871 18.247  1.00 63.92  ? 240  THR A OG1 1 
ATOM   1902 C CG2 . THR A 1 241 ? -3.151  -29.535 19.560  1.00 48.11  ? 240  THR A CG2 1 
ATOM   1903 N N   . TYR A 1 242 ? -0.975  -32.987 21.499  1.00 56.63  ? 241  TYR A N   1 
ATOM   1904 C CA  . TYR A 1 242 ? -0.224  -34.091 22.096  1.00 46.03  ? 241  TYR A CA  1 
ATOM   1905 C C   . TYR A 1 242 ? 0.599   -34.910 21.127  1.00 50.48  ? 241  TYR A C   1 
ATOM   1906 O O   . TYR A 1 242 ? 1.822   -34.991 21.280  1.00 41.43  ? 241  TYR A O   1 
ATOM   1907 C CB  . TYR A 1 242 ? -1.187  -35.000 22.840  1.00 51.54  ? 241  TYR A CB  1 
ATOM   1908 C CG  . TYR A 1 242 ? -0.564  -36.087 23.689  1.00 52.60  ? 241  TYR A CG  1 
ATOM   1909 C CD1 . TYR A 1 242 ? 0.565   -35.855 24.454  1.00 43.31  ? 241  TYR A CD1 1 
ATOM   1910 C CD2 . TYR A 1 242 ? -1.149  -37.335 23.761  1.00 58.55  ? 241  TYR A CD2 1 
ATOM   1911 C CE1 . TYR A 1 242 ? 1.110   -36.852 25.241  1.00 50.14  ? 241  TYR A CE1 1 
ATOM   1912 C CE2 . TYR A 1 242 ? -0.623  -38.326 24.549  1.00 63.55  ? 241  TYR A CE2 1 
ATOM   1913 C CZ  . TYR A 1 242 ? 0.507   -38.092 25.288  1.00 59.12  ? 241  TYR A CZ  1 
ATOM   1914 O OH  . TYR A 1 242 ? 1.009   -39.117 26.074  1.00 54.81  ? 241  TYR A OH  1 
ATOM   1915 N N   . GLN A 1 243 ? -0.076  -35.537 20.160  1.00 50.24  ? 242  GLN A N   1 
ATOM   1916 C CA  . GLN A 1 243 ? 0.599   -36.316 19.118  1.00 53.73  ? 242  GLN A CA  1 
ATOM   1917 C C   . GLN A 1 243 ? 1.693   -35.484 18.456  1.00 62.67  ? 242  GLN A C   1 
ATOM   1918 O O   . GLN A 1 243 ? 2.868   -35.866 18.438  1.00 50.58  ? 242  GLN A O   1 
ATOM   1919 C CB  . GLN A 1 243 ? -0.385  -36.820 18.042  1.00 46.18  ? 242  GLN A CB  1 
ATOM   1920 C CG  . GLN A 1 243 ? 0.217   -37.919 17.170  1.00 50.92  ? 242  GLN A CG  1 
ATOM   1921 C CD  . GLN A 1 243 ? -0.635  -38.323 15.963  1.00 65.85  ? 242  GLN A CD  1 
ATOM   1922 O OE1 . GLN A 1 243 ? -1.324  -37.502 15.369  1.00 70.48  ? 242  GLN A OE1 1 
ATOM   1923 N NE2 . GLN A 1 243 ? -0.555  -39.595 15.583  1.00 67.39  ? 242  GLN A NE2 1 
ATOM   1924 N N   . ALA A 1 244 ? 1.295   -34.332 17.925  1.00 67.71  ? 243  ALA A N   1 
ATOM   1925 C CA  . ALA A 1 244 ? 2.198   -33.473 17.167  1.00 54.63  ? 243  ALA A CA  1 
ATOM   1926 C C   . ALA A 1 244 ? 3.433   -33.029 17.983  1.00 52.08  ? 243  ALA A C   1 
ATOM   1927 O O   . ALA A 1 244 ? 4.560   -32.996 17.459  1.00 45.88  ? 243  ALA A O   1 
ATOM   1928 C CB  . ALA A 1 244 ? 1.427   -32.271 16.591  1.00 44.68  ? 243  ALA A CB  1 
ATOM   1929 N N   . ALA A 1 245 ? 3.220   -32.710 19.260  1.00 41.36  ? 244  ALA A N   1 
ATOM   1930 C CA  . ALA A 1 245 ? 4.321   -32.293 20.132  1.00 43.16  ? 244  ALA A CA  1 
ATOM   1931 C C   . ALA A 1 245 ? 5.226   -33.450 20.500  1.00 51.80  ? 244  ALA A C   1 
ATOM   1932 O O   . ALA A 1 245 ? 6.424   -33.258 20.703  1.00 62.96  ? 244  ALA A O   1 
ATOM   1933 C CB  . ALA A 1 245 ? 3.820   -31.591 21.413  1.00 38.22  ? 244  ALA A CB  1 
ATOM   1934 N N   . ALA A 1 246 ? 4.653   -34.646 20.612  1.00 52.57  ? 245  ALA A N   1 
ATOM   1935 C CA  . ALA A 1 246 ? 5.428   -35.808 21.010  1.00 48.90  ? 245  ALA A CA  1 
ATOM   1936 C C   . ALA A 1 246 ? 6.412   -36.119 19.905  1.00 58.54  ? 245  ALA A C   1 
ATOM   1937 O O   . ALA A 1 246 ? 7.608   -36.315 20.158  1.00 50.35  ? 245  ALA A O   1 
ATOM   1938 C CB  . ALA A 1 246 ? 4.539   -36.994 21.253  1.00 41.81  ? 245  ALA A CB  1 
ATOM   1939 N N   . TYR A 1 247 ? 5.902   -36.167 18.679  1.00 42.65  ? 246  TYR A N   1 
ATOM   1940 C CA  . TYR A 1 247 ? 6.712   -36.616 17.568  1.00 51.72  ? 246  TYR A CA  1 
ATOM   1941 C C   . TYR A 1 247 ? 7.840   -35.622 17.217  1.00 55.68  ? 246  TYR A C   1 
ATOM   1942 O O   . TYR A 1 247 ? 8.893   -35.999 16.684  1.00 51.92  ? 246  TYR A O   1 
ATOM   1943 C CB  . TYR A 1 247 ? 5.809   -36.927 16.377  1.00 42.92  ? 246  TYR A CB  1 
ATOM   1944 C CG  . TYR A 1 247 ? 5.235   -38.320 16.433  1.00 49.90  ? 246  TYR A CG  1 
ATOM   1945 C CD1 . TYR A 1 247 ? 4.134   -38.604 17.220  1.00 50.66  ? 246  TYR A CD1 1 
ATOM   1946 C CD2 . TYR A 1 247 ? 5.800   -39.355 15.707  1.00 48.21  ? 246  TYR A CD2 1 
ATOM   1947 C CE1 . TYR A 1 247 ? 3.610   -39.869 17.276  1.00 53.41  ? 246  TYR A CE1 1 
ATOM   1948 C CE2 . TYR A 1 247 ? 5.282   -40.635 15.763  1.00 44.06  ? 246  TYR A CE2 1 
ATOM   1949 C CZ  . TYR A 1 247 ? 4.186   -40.893 16.548  1.00 49.91  ? 246  TYR A CZ  1 
ATOM   1950 O OH  . TYR A 1 247 ? 3.647   -42.170 16.603  1.00 50.54  ? 246  TYR A OH  1 
ATOM   1951 N N   . ASP A 1 248 ? 7.588   -34.356 17.536  1.00 51.08  ? 247  ASP A N   1 
ATOM   1952 C CA  . ASP A 1 248 ? 8.528   -33.264 17.370  1.00 47.88  ? 247  ASP A CA  1 
ATOM   1953 C C   . ASP A 1 248 ? 9.610   -33.310 18.452  1.00 50.58  ? 247  ASP A C   1 
ATOM   1954 O O   . ASP A 1 248 ? 10.779  -33.614 18.179  1.00 60.95  ? 247  ASP A O   1 
ATOM   1955 C CB  . ASP A 1 248 ? 7.753   -31.955 17.464  1.00 47.15  ? 247  ASP A CB  1 
ATOM   1956 C CG  . ASP A 1 248 ? 8.499   -30.779 16.865  1.00 55.39  ? 247  ASP A CG  1 
ATOM   1957 O OD1 . ASP A 1 248 ? 9.665   -30.962 16.453  1.00 57.69  ? 247  ASP A OD1 1 
ATOM   1958 O OD2 . ASP A 1 248 ? 7.915   -29.669 16.814  1.00 49.26  ? 247  ASP A OD2 1 
ATOM   1959 N N   . LEU A 1 249 ? 9.194   -33.041 19.685  1.00 43.90  ? 248  LEU A N   1 
ATOM   1960 C CA  . LEU A 1 249 ? 10.105  -32.886 20.817  1.00 39.60  ? 248  LEU A CA  1 
ATOM   1961 C C   . LEU A 1 249 ? 10.780  -34.160 21.358  1.00 48.57  ? 248  LEU A C   1 
ATOM   1962 O O   . LEU A 1 249 ? 11.837  -34.092 21.979  1.00 54.97  ? 248  LEU A O   1 
ATOM   1963 C CB  . LEU A 1 249 ? 9.370   -32.147 21.942  1.00 46.15  ? 248  LEU A CB  1 
ATOM   1964 C CG  . LEU A 1 249 ? 8.779   -30.792 21.500  1.00 44.81  ? 248  LEU A CG  1 
ATOM   1965 C CD1 . LEU A 1 249 ? 7.767   -30.169 22.484  1.00 43.23  ? 248  LEU A CD1 1 
ATOM   1966 C CD2 . LEU A 1 249 ? 9.892   -29.820 21.217  1.00 39.17  ? 248  LEU A CD2 1 
ATOM   1967 N N   . LEU A 1 250 ? 10.168  -35.319 21.145  1.00 52.29  ? 249  LEU A N   1 
ATOM   1968 C CA  . LEU A 1 250 ? 10.695  -36.556 21.714  1.00 43.87  ? 249  LEU A CA  1 
ATOM   1969 C C   . LEU A 1 250 ? 11.276  -37.467 20.655  1.00 51.19  ? 249  LEU A C   1 
ATOM   1970 O O   . LEU A 1 250 ? 11.126  -37.227 19.447  1.00 54.91  ? 249  LEU A O   1 
ATOM   1971 C CB  . LEU A 1 250 ? 9.639   -37.324 22.520  1.00 40.70  ? 249  LEU A CB  1 
ATOM   1972 C CG  . LEU A 1 250 ? 8.798   -36.587 23.560  1.00 50.82  ? 249  LEU A CG  1 
ATOM   1973 C CD1 . LEU A 1 250 ? 7.849   -37.563 24.235  1.00 53.57  ? 249  LEU A CD1 1 
ATOM   1974 C CD2 . LEU A 1 250 ? 9.649   -35.814 24.595  1.00 37.17  ? 249  LEU A CD2 1 
ATOM   1975 N N   . ASN A 1 251 ? 11.949  -38.512 21.124  1.00 38.33  ? 250  ASN A N   1 
ATOM   1976 C CA  . ASN A 1 251 ? 12.577  -39.442 20.218  1.00 61.90  ? 250  ASN A CA  1 
ATOM   1977 C C   . ASN A 1 251 ? 11.637  -40.599 19.918  1.00 68.16  ? 250  ASN A C   1 
ATOM   1978 O O   . ASN A 1 251 ? 11.556  -41.576 20.681  1.00 60.48  ? 250  ASN A O   1 
ATOM   1979 C CB  . ASN A 1 251 ? 13.881  -39.955 20.807  1.00 84.16  ? 250  ASN A CB  1 
ATOM   1980 C CG  . ASN A 1 251 ? 14.946  -40.122 19.759  1.00 110.34 ? 250  ASN A CG  1 
ATOM   1981 O OD1 . ASN A 1 251 ? 14.936  -41.090 18.989  1.00 102.94 ? 250  ASN A OD1 1 
ATOM   1982 N ND2 . ASN A 1 251 ? 15.870  -39.160 19.701  1.00 126.96 ? 250  ASN A ND2 1 
ATOM   1983 N N   . ILE A 1 252 ? 10.914  -40.465 18.811  1.00 63.73  ? 251  ILE A N   1 
ATOM   1984 C CA  . ILE A 1 252 ? 9.934   -41.457 18.404  1.00 63.68  ? 251  ILE A CA  1 
ATOM   1985 C C   . ILE A 1 252 ? 10.292  -41.978 17.024  1.00 73.42  ? 251  ILE A C   1 
ATOM   1986 O O   . ILE A 1 252 ? 9.859   -41.441 16.006  1.00 85.45  ? 251  ILE A O   1 
ATOM   1987 C CB  . ILE A 1 252 ? 8.502   -40.880 18.426  1.00 56.57  ? 251  ILE A CB  1 
ATOM   1988 C CG1 . ILE A 1 252 ? 8.175   -40.361 19.826  1.00 51.82  ? 251  ILE A CG1 1 
ATOM   1989 C CG2 . ILE A 1 252 ? 7.482   -41.928 18.021  1.00 59.05  ? 251  ILE A CG2 1 
ATOM   1990 C CD1 . ILE A 1 252 ? 6.767   -39.920 19.983  1.00 57.43  ? 251  ILE A CD1 1 
ATOM   1991 N N   . GLU A 1 253 ? 11.107  -43.023 17.002  1.00 71.37  ? 252  GLU A N   1 
ATOM   1992 C CA  . GLU A 1 253 ? 11.535  -43.629 15.755  1.00 83.15  ? 252  GLU A CA  1 
ATOM   1993 C C   . GLU A 1 253 ? 10.561  -44.768 15.422  1.00 78.65  ? 252  GLU A C   1 
ATOM   1994 O O   . GLU A 1 253 ? 10.237  -45.594 16.279  1.00 81.99  ? 252  GLU A O   1 
ATOM   1995 C CB  . GLU A 1 253 ? 12.981  -44.129 15.899  1.00 103.44 ? 252  GLU A CB  1 
ATOM   1996 C CG  . GLU A 1 253 ? 13.870  -43.982 14.654  1.00 123.75 ? 252  GLU A CG  1 
ATOM   1997 C CD  . GLU A 1 253 ? 14.412  -42.567 14.435  1.00 131.27 ? 252  GLU A CD  1 
ATOM   1998 O OE1 . GLU A 1 253 ? 13.770  -41.590 14.881  1.00 133.38 ? 252  GLU A OE1 1 
ATOM   1999 O OE2 . GLU A 1 253 ? 15.483  -42.437 13.797  1.00 127.99 ? 252  GLU A OE2 1 
ATOM   2000 N N   . ASN A 1 254 ? 10.070  -44.786 14.187  1.00 73.01  ? 253  ASN A N   1 
ATOM   2001 C CA  . ASN A 1 254 ? 9.101   -45.796 13.735  1.00 70.11  ? 253  ASN A CA  1 
ATOM   2002 C C   . ASN A 1 254 ? 7.947   -46.028 14.700  1.00 63.12  ? 253  ASN A C   1 
ATOM   2003 O O   . ASN A 1 254 ? 7.492   -47.146 14.861  1.00 67.79  ? 253  ASN A O   1 
ATOM   2004 C CB  . ASN A 1 254 ? 9.787   -47.127 13.413  1.00 77.76  ? 253  ASN A CB  1 
ATOM   2005 C CG  . ASN A 1 254 ? 10.982  -46.958 12.487  1.00 93.95  ? 253  ASN A CG  1 
ATOM   2006 O OD1 . ASN A 1 254 ? 10.839  -46.516 11.339  1.00 94.84  ? 253  ASN A OD1 1 
ATOM   2007 N ND2 . ASN A 1 254 ? 12.173  -47.308 12.984  1.00 91.03  ? 253  ASN A ND2 1 
ATOM   2008 N N   . ASP A 1 255 ? 7.484   -44.959 15.336  1.00 71.38  ? 254  ASP A N   1 
ATOM   2009 C CA  . ASP A 1 255 ? 6.306   -45.004 16.195  1.00 61.28  ? 254  ASP A CA  1 
ATOM   2010 C C   . ASP A 1 255 ? 6.550   -45.671 17.551  1.00 69.85  ? 254  ASP A C   1 
ATOM   2011 O O   . ASP A 1 255 ? 5.622   -45.881 18.331  1.00 72.63  ? 254  ASP A O   1 
ATOM   2012 C CB  . ASP A 1 255 ? 5.128   -45.634 15.448  1.00 48.30  ? 254  ASP A CB  1 
ATOM   2013 C CG  . ASP A 1 255 ? 4.714   -44.818 14.237  1.00 66.75  ? 254  ASP A CG  1 
ATOM   2014 O OD1 . ASP A 1 255 ? 4.316   -43.629 14.401  1.00 59.08  ? 254  ASP A OD1 1 
ATOM   2015 O OD2 . ASP A 1 255 ? 4.813   -45.360 13.113  1.00 72.43  ? 254  ASP A OD2 1 
ATOM   2016 N N   . ILE A 1 256 ? 7.811   -45.979 17.832  1.00 70.48  ? 255  ILE A N   1 
ATOM   2017 C CA  . ILE A 1 256 ? 8.194   -46.577 19.105  1.00 59.52  ? 255  ILE A CA  1 
ATOM   2018 C C   . ILE A 1 256 ? 8.701   -45.552 20.119  1.00 59.90  ? 255  ILE A C   1 
ATOM   2019 O O   . ILE A 1 256 ? 9.595   -44.759 19.835  1.00 65.18  ? 255  ILE A O   1 
ATOM   2020 C CB  . ILE A 1 256 ? 9.295   -47.616 18.913  1.00 58.64  ? 255  ILE A CB  1 
ATOM   2021 C CG1 . ILE A 1 256 ? 8.845   -48.699 17.932  1.00 69.81  ? 255  ILE A CG1 1 
ATOM   2022 C CG2 . ILE A 1 256 ? 9.681   -48.203 20.253  1.00 56.86  ? 255  ILE A CG2 1 
ATOM   2023 C CD1 . ILE A 1 256 ? 9.908   -49.724 17.635  1.00 68.76  ? 255  ILE A CD1 1 
ATOM   2024 N N   . TYR A 1 257 ? 8.118   -45.572 21.304  1.00 57.59  ? 256  TYR A N   1 
ATOM   2025 C CA  . TYR A 1 257 ? 8.559   -44.693 22.371  1.00 57.60  ? 256  TYR A CA  1 
ATOM   2026 C C   . TYR A 1 257 ? 9.195   -45.540 23.463  1.00 59.77  ? 256  TYR A C   1 
ATOM   2027 O O   . TYR A 1 257 ? 8.724   -46.642 23.716  1.00 66.57  ? 256  TYR A O   1 
ATOM   2028 C CB  . TYR A 1 257 ? 7.364   -43.901 22.913  1.00 47.12  ? 256  TYR A CB  1 
ATOM   2029 C CG  . TYR A 1 257 ? 7.702   -42.949 24.036  1.00 54.96  ? 256  TYR A CG  1 
ATOM   2030 C CD1 . TYR A 1 257 ? 8.480   -41.809 23.816  1.00 53.98  ? 256  TYR A CD1 1 
ATOM   2031 C CD2 . TYR A 1 257 ? 7.246   -43.183 25.312  1.00 55.16  ? 256  TYR A CD2 1 
ATOM   2032 C CE1 . TYR A 1 257 ? 8.777   -40.941 24.841  1.00 40.16  ? 256  TYR A CE1 1 
ATOM   2033 C CE2 . TYR A 1 257 ? 7.534   -42.321 26.335  1.00 60.06  ? 256  TYR A CE2 1 
ATOM   2034 C CZ  . TYR A 1 257 ? 8.297   -41.204 26.101  1.00 59.25  ? 256  TYR A CZ  1 
ATOM   2035 O OH  . TYR A 1 257 ? 8.577   -40.367 27.154  1.00 71.07  ? 256  TYR A OH  1 
ATOM   2036 N N   . SER A 1 258 ? 10.273  -45.051 24.080  1.00 69.65  ? 257  SER A N   1 
ATOM   2037 C CA  . SER A 1 258 ? 10.902  -45.751 25.216  1.00 75.19  ? 257  SER A CA  1 
ATOM   2038 C C   . SER A 1 258 ? 10.810  -44.957 26.511  1.00 79.14  ? 257  SER A C   1 
ATOM   2039 O O   . SER A 1 258 ? 11.101  -43.760 26.542  1.00 90.10  ? 257  SER A O   1 
ATOM   2040 C CB  . SER A 1 258 ? 12.381  -46.060 24.956  1.00 74.00  ? 257  SER A CB  1 
ATOM   2041 O OG  . SER A 1 258 ? 12.566  -46.833 23.789  1.00 87.11  ? 257  SER A OG  1 
ATOM   2042 N N   . TYR A 1 259 ? 10.426  -45.635 27.582  1.00 75.82  ? 258  TYR A N   1 
ATOM   2043 C CA  . TYR A 1 259 ? 10.424  -45.026 28.899  1.00 86.85  ? 258  TYR A CA  1 
ATOM   2044 C C   . TYR A 1 259 ? 10.899  -46.013 29.970  1.00 115.01 ? 258  TYR A C   1 
ATOM   2045 O O   . TYR A 1 259 ? 11.362  -47.106 29.646  1.00 122.27 ? 258  TYR A O   1 
ATOM   2046 C CB  . TYR A 1 259 ? 9.038   -44.478 29.225  1.00 68.91  ? 258  TYR A CB  1 
ATOM   2047 C CG  . TYR A 1 259 ? 7.977   -45.525 29.332  1.00 69.43  ? 258  TYR A CG  1 
ATOM   2048 C CD1 . TYR A 1 259 ? 7.537   -46.198 28.213  1.00 77.37  ? 258  TYR A CD1 1 
ATOM   2049 C CD2 . TYR A 1 259 ? 7.398   -45.834 30.555  1.00 79.41  ? 258  TYR A CD2 1 
ATOM   2050 C CE1 . TYR A 1 259 ? 6.550   -47.159 28.303  1.00 85.88  ? 258  TYR A CE1 1 
ATOM   2051 C CE2 . TYR A 1 259 ? 6.407   -46.798 30.657  1.00 74.72  ? 258  TYR A CE2 1 
ATOM   2052 C CZ  . TYR A 1 259 ? 5.991   -47.454 29.527  1.00 77.05  ? 258  TYR A CZ  1 
ATOM   2053 O OH  . TYR A 1 259 ? 5.024   -48.420 29.602  1.00 81.95  ? 258  TYR A OH  1 
ATOM   2054 N N   . SER A 1 260 ? 10.799  -45.622 31.238  1.00 124.69 ? 259  SER A N   1 
ATOM   2055 C CA  . SER A 1 260 ? 11.255  -46.471 32.335  1.00 124.25 ? 259  SER A CA  1 
ATOM   2056 C C   . SER A 1 260 ? 10.214  -46.529 33.448  1.00 120.43 ? 259  SER A C   1 
ATOM   2057 O O   . SER A 1 260 ? 9.740   -45.493 33.916  1.00 119.19 ? 259  SER A O   1 
ATOM   2058 C CB  . SER A 1 260 ? 12.592  -45.960 32.889  1.00 125.61 ? 259  SER A CB  1 
ATOM   2059 O OG  . SER A 1 260 ? 13.551  -45.787 31.856  1.00 120.86 ? 259  SER A OG  1 
ATOM   2060 N N   . THR A 1 261 ? 9.847   -47.743 33.851  1.00 121.72 ? 260  THR A N   1 
ATOM   2061 C CA  . THR A 1 261 ? 8.983   -47.946 35.015  1.00 123.10 ? 260  THR A CA  1 
ATOM   2062 C C   . THR A 1 261 ? 9.466   -49.130 35.822  1.00 132.68 ? 260  THR A C   1 
ATOM   2063 O O   . THR A 1 261 ? 10.572  -49.623 35.616  1.00 132.99 ? 260  THR A O   1 
ATOM   2064 C CB  . THR A 1 261 ? 7.506   -48.211 34.648  1.00 112.85 ? 260  THR A CB  1 
ATOM   2065 O OG1 . THR A 1 261 ? 7.432   -49.235 33.645  1.00 109.70 ? 260  THR A OG1 1 
ATOM   2066 C CG2 . THR A 1 261 ? 6.829   -46.939 34.158  1.00 107.87 ? 260  THR A CG2 1 
ATOM   2067 N N   . VAL A 1 262 ? 8.618   -49.589 36.735  1.00 143.26 ? 261  VAL A N   1 
ATOM   2068 C CA  . VAL A 1 262 ? 8.941   -50.725 37.585  1.00 149.75 ? 261  VAL A CA  1 
ATOM   2069 C C   . VAL A 1 262 ? 7.871   -51.804 37.478  1.00 154.23 ? 261  VAL A C   1 
ATOM   2070 O O   . VAL A 1 262 ? 6.707   -51.513 37.188  1.00 146.26 ? 261  VAL A O   1 
ATOM   2071 C CB  . VAL A 1 262 ? 9.063   -50.303 39.060  1.00 147.54 ? 261  VAL A CB  1 
ATOM   2072 C CG1 . VAL A 1 262 ? 10.134  -49.232 39.219  1.00 146.79 ? 261  VAL A CG1 1 
ATOM   2073 C CG2 . VAL A 1 262 ? 7.717   -49.805 39.580  1.00 143.80 ? 261  VAL A CG2 1 
ATOM   2074 N N   . ASP A 1 263 ? 8.277   -53.050 37.703  1.00 167.34 ? 262  ASP A N   1 
ATOM   2075 C CA  . ASP A 1 263 ? 7.334   -54.159 37.820  1.00 173.33 ? 262  ASP A CA  1 
ATOM   2076 C C   . ASP A 1 263 ? 7.194   -54.572 39.285  1.00 177.44 ? 262  ASP A C   1 
ATOM   2077 O O   . ASP A 1 263 ? 7.330   -53.740 40.187  1.00 173.79 ? 262  ASP A O   1 
ATOM   2078 C CB  . ASP A 1 263 ? 7.752   -55.352 36.943  1.00 174.28 ? 262  ASP A CB  1 
ATOM   2079 C CG  . ASP A 1 263 ? 9.163   -55.848 37.239  1.00 173.24 ? 262  ASP A CG  1 
ATOM   2080 O OD1 . ASP A 1 263 ? 9.846   -55.250 38.096  1.00 178.73 ? 262  ASP A OD1 1 
ATOM   2081 O OD2 . ASP A 1 263 ? 9.591   -56.841 36.606  1.00 165.85 ? 262  ASP A OD2 1 
ATOM   2082 N N   . ALA A 1 264 ? 6.914   -55.851 39.520  1.00 185.09 ? 263  ALA A N   1 
ATOM   2083 C CA  . ALA A 1 264 ? 6.852   -56.376 40.880  1.00 186.25 ? 263  ALA A CA  1 
ATOM   2084 C C   . ALA A 1 264 ? 8.044   -55.859 41.686  1.00 187.83 ? 263  ALA A C   1 
ATOM   2085 O O   . ALA A 1 264 ? 7.877   -55.297 42.770  1.00 186.48 ? 263  ALA A O   1 
ATOM   2086 C CB  . ALA A 1 264 ? 6.824   -57.901 40.867  1.00 185.30 ? 263  ALA A CB  1 
ATOM   2087 N N   . GLY A 1 265 ? 9.243   -56.035 41.138  1.00 187.22 ? 264  GLY A N   1 
ATOM   2088 C CA  . GLY A 1 265 ? 10.457  -55.548 41.769  1.00 183.42 ? 264  GLY A CA  1 
ATOM   2089 C C   . GLY A 1 265 ? 11.325  -54.716 40.839  1.00 176.11 ? 264  GLY A C   1 
ATOM   2090 O O   . GLY A 1 265 ? 11.179  -53.493 40.773  1.00 167.04 ? 264  GLY A O   1 
ATOM   2091 N N   . GLY A 1 266 ? 12.226  -55.391 40.126  1.00 178.34 ? 265  GLY A N   1 
ATOM   2092 C CA  . GLY A 1 266 ? 13.149  -54.750 39.204  1.00 178.77 ? 265  GLY A CA  1 
ATOM   2093 C C   . GLY A 1 266 ? 12.707  -53.377 38.741  1.00 179.16 ? 265  GLY A C   1 
ATOM   2094 O O   . GLY A 1 266 ? 11.682  -53.229 38.076  1.00 175.16 ? 265  GLY A O   1 
ATOM   2095 N N   . ARG A 1 267 ? 13.484  -52.364 39.100  1.00 185.69 ? 266  ARG A N   1 
ATOM   2096 C CA  . ARG A 1 267 ? 13.148  -50.992 38.750  1.00 185.91 ? 266  ARG A CA  1 
ATOM   2097 C C   . ARG A 1 267 ? 13.697  -50.642 37.373  1.00 191.03 ? 266  ARG A C   1 
ATOM   2098 O O   . ARG A 1 267 ? 14.173  -51.519 36.650  1.00 188.78 ? 266  ARG A O   1 
ATOM   2099 C CB  . ARG A 1 267 ? 13.688  -50.017 39.801  1.00 182.20 ? 266  ARG A CB  1 
ATOM   2100 C CG  . ARG A 1 267 ? 13.317  -50.372 41.234  1.00 179.30 ? 266  ARG A CG  1 
ATOM   2101 C CD  . ARG A 1 267 ? 14.207  -51.478 41.777  1.00 179.99 ? 266  ARG A CD  1 
ATOM   2102 N NE  . ARG A 1 267 ? 13.759  -51.951 43.084  1.00 177.49 ? 266  ARG A NE  1 
ATOM   2103 C CZ  . ARG A 1 267 ? 14.382  -52.887 43.792  1.00 173.75 ? 266  ARG A CZ  1 
ATOM   2104 N NH1 . ARG A 1 267 ? 15.487  -53.452 43.321  1.00 173.19 ? 266  ARG A NH1 1 
ATOM   2105 N NH2 . ARG A 1 267 ? 13.900  -53.256 44.972  1.00 171.57 ? 266  ARG A NH2 1 
ATOM   2106 N N   . GLU A 1 268 ? 13.634  -49.357 37.028  1.00 198.20 ? 267  GLU A N   1 
ATOM   2107 C CA  . GLU A 1 268 ? 14.060  -48.864 35.716  1.00 200.60 ? 267  GLU A CA  1 
ATOM   2108 C C   . GLU A 1 268 ? 13.972  -49.925 34.620  1.00 199.53 ? 267  GLU A C   1 
ATOM   2109 O O   . GLU A 1 268 ? 14.935  -50.155 33.889  1.00 201.38 ? 267  GLU A O   1 
ATOM   2110 C CB  . GLU A 1 268 ? 15.476  -48.274 35.768  1.00 203.56 ? 267  GLU A CB  1 
ATOM   2111 C CG  . GLU A 1 268 ? 15.582  -46.949 36.508  1.00 204.51 ? 267  GLU A CG  1 
ATOM   2112 C CD  . GLU A 1 268 ? 15.726  -47.128 38.006  1.00 210.51 ? 267  GLU A CD  1 
ATOM   2113 O OE1 . GLU A 1 268 ? 16.053  -48.250 38.443  1.00 218.19 ? 267  GLU A OE1 1 
ATOM   2114 O OE2 . GLU A 1 268 ? 15.520  -46.145 38.746  1.00 208.51 ? 267  GLU A OE2 1 
ATOM   2115 N N   . GLN A 1 269 ? 12.817  -50.578 34.528  1.00 191.68 ? 268  GLN A N   1 
ATOM   2116 C CA  . GLN A 1 269 ? 12.534  -51.483 33.425  1.00 178.00 ? 268  GLN A CA  1 
ATOM   2117 C C   . GLN A 1 269 ? 12.193  -50.641 32.206  1.00 168.41 ? 268  GLN A C   1 
ATOM   2118 O O   . GLN A 1 269 ? 11.176  -49.946 32.193  1.00 168.23 ? 268  GLN A O   1 
ATOM   2119 C CB  . GLN A 1 269 ? 11.360  -52.403 33.768  1.00 170.04 ? 268  GLN A CB  1 
ATOM   2120 C CG  . GLN A 1 269 ? 11.602  -53.308 34.964  1.00 167.25 ? 268  GLN A CG  1 
ATOM   2121 C CD  . GLN A 1 269 ? 12.634  -54.384 34.686  1.00 162.87 ? 268  GLN A CD  1 
ATOM   2122 O OE1 . GLN A 1 269 ? 13.199  -54.449 33.595  1.00 159.23 ? 268  GLN A OE1 1 
ATOM   2123 N NE2 . GLN A 1 269 ? 12.883  -55.239 35.674  1.00 162.31 ? 268  GLN A NE2 1 
ATOM   2124 N N   . GLN A 1 270 ? 13.050  -50.689 31.190  1.00 158.41 ? 269  GLN A N   1 
ATOM   2125 C CA  . GLN A 1 270 ? 12.854  -49.880 29.991  1.00 143.61 ? 269  GLN A CA  1 
ATOM   2126 C C   . GLN A 1 270 ? 11.874  -50.537 29.021  1.00 121.76 ? 269  GLN A C   1 
ATOM   2127 O O   . GLN A 1 270 ? 12.218  -51.501 28.334  1.00 117.09 ? 269  GLN A O   1 
ATOM   2128 C CB  . GLN A 1 270 ? 14.187  -49.597 29.286  1.00 149.68 ? 269  GLN A CB  1 
ATOM   2129 C CG  . GLN A 1 270 ? 15.265  -48.997 30.180  1.00 156.33 ? 269  GLN A CG  1 
ATOM   2130 C CD  . GLN A 1 270 ? 15.951  -50.038 31.059  1.00 165.17 ? 269  GLN A CD  1 
ATOM   2131 O OE1 . GLN A 1 270 ? 15.763  -51.245 30.885  1.00 164.74 ? 269  GLN A OE1 1 
ATOM   2132 N NE2 . GLN A 1 270 ? 16.757  -49.570 32.007  1.00 168.17 ? 269  GLN A NE2 1 
ATOM   2133 N N   . ARG A 1 271 ? 10.652  -50.009 28.979  1.00 105.19 ? 270  ARG A N   1 
ATOM   2134 C CA  . ARG A 1 271 ? 9.643   -50.473 28.035  1.00 94.66  ? 270  ARG A CA  1 
ATOM   2135 C C   . ARG A 1 271 ? 9.755   -49.740 26.703  1.00 88.85  ? 270  ARG A C   1 
ATOM   2136 O O   . ARG A 1 271 ? 10.014  -48.547 26.656  1.00 92.45  ? 270  ARG A O   1 
ATOM   2137 C CB  . ARG A 1 271 ? 8.225   -50.282 28.589  1.00 89.49  ? 270  ARG A CB  1 
ATOM   2138 C CG  . ARG A 1 271 ? 7.829   -51.207 29.728  1.00 101.58 ? 270  ARG A CG  1 
ATOM   2139 C CD  . ARG A 1 271 ? 6.308   -51.205 29.942  1.00 117.60 ? 270  ARG A CD  1 
ATOM   2140 N NE  . ARG A 1 271 ? 5.596   -51.983 28.923  1.00 132.10 ? 270  ARG A NE  1 
ATOM   2141 C CZ  . ARG A 1 271 ? 4.664   -51.500 28.099  1.00 126.85 ? 270  ARG A CZ  1 
ATOM   2142 N NH1 . ARG A 1 271 ? 4.301   -50.222 28.155  1.00 110.21 ? 270  ARG A NH1 1 
ATOM   2143 N NH2 . ARG A 1 271 ? 4.089   -52.307 27.211  1.00 126.47 ? 270  ARG A NH2 1 
ATOM   2144 N N   . GLN A 1 272 ? 9.572   -50.478 25.621  1.00 84.69  ? 271  GLN A N   1 
ATOM   2145 C CA  . GLN A 1 272 ? 9.349   -49.892 24.316  1.00 69.17  ? 271  GLN A CA  1 
ATOM   2146 C C   . GLN A 1 272 ? 7.946   -50.285 23.913  1.00 71.15  ? 271  GLN A C   1 
ATOM   2147 O O   . GLN A 1 272 ? 7.621   -51.464 23.872  1.00 77.64  ? 271  GLN A O   1 
ATOM   2148 C CB  . GLN A 1 272 ? 10.320  -50.467 23.296  1.00 65.18  ? 271  GLN A CB  1 
ATOM   2149 C CG  . GLN A 1 272 ? 11.711  -49.936 23.403  1.00 79.72  ? 271  GLN A CG  1 
ATOM   2150 C CD  . GLN A 1 272 ? 12.627  -50.553 22.375  1.00 91.57  ? 271  GLN A CD  1 
ATOM   2151 O OE1 . GLN A 1 272 ? 12.761  -51.778 22.310  1.00 92.51  ? 271  GLN A OE1 1 
ATOM   2152 N NE2 . GLN A 1 272 ? 13.265  -49.710 21.558  1.00 89.80  ? 271  GLN A NE2 1 
ATOM   2153 N N   . VAL A 1 273 ? 7.106   -49.310 23.617  1.00 67.96  ? 272  VAL A N   1 
ATOM   2154 C CA  . VAL A 1 273 ? 5.778   -49.622 23.136  1.00 65.90  ? 272  VAL A CA  1 
ATOM   2155 C C   . VAL A 1 273 ? 5.589   -48.886 21.815  1.00 68.49  ? 272  VAL A C   1 
ATOM   2156 O O   . VAL A 1 273 ? 6.294   -47.925 21.551  1.00 66.49  ? 272  VAL A O   1 
ATOM   2157 C CB  . VAL A 1 273 ? 4.719   -49.204 24.167  1.00 61.52  ? 272  VAL A CB  1 
ATOM   2158 C CG1 . VAL A 1 273 ? 4.754   -47.717 24.364  1.00 61.26  ? 272  VAL A CG1 1 
ATOM   2159 C CG2 . VAL A 1 273 ? 3.349   -49.635 23.723  1.00 75.26  ? 272  VAL A CG2 1 
ATOM   2160 N N   . VAL A 1 274 ? 4.672   -49.360 20.975  1.00 74.97  ? 273  VAL A N   1 
ATOM   2161 C CA  . VAL A 1 274 ? 4.266   -48.639 19.770  1.00 64.10  ? 273  VAL A CA  1 
ATOM   2162 C C   . VAL A 1 274 ? 3.038   -47.758 20.046  1.00 69.04  ? 273  VAL A C   1 
ATOM   2163 O O   . VAL A 1 274 ? 2.085   -48.184 20.703  1.00 71.08  ? 273  VAL A O   1 
ATOM   2164 C CB  . VAL A 1 274 ? 3.947   -49.599 18.612  1.00 61.05  ? 273  VAL A CB  1 
ATOM   2165 C CG1 . VAL A 1 274 ? 3.450   -48.838 17.410  1.00 72.97  ? 273  VAL A CG1 1 
ATOM   2166 C CG2 . VAL A 1 274 ? 5.169   -50.401 18.239  1.00 58.06  ? 273  VAL A CG2 1 
ATOM   2167 N N   . LEU A 1 275 ? 3.082   -46.518 19.565  1.00 63.21  ? 274  LEU A N   1 
ATOM   2168 C CA  . LEU A 1 275 ? 1.937   -45.624 19.627  1.00 61.09  ? 274  LEU A CA  1 
ATOM   2169 C C   . LEU A 1 275 ? 0.958   -45.962 18.496  1.00 71.70  ? 274  LEU A C   1 
ATOM   2170 O O   . LEU A 1 275 ? 1.324   -45.947 17.309  1.00 76.03  ? 274  LEU A O   1 
ATOM   2171 C CB  . LEU A 1 275 ? 2.407   -44.183 19.484  1.00 65.61  ? 274  LEU A CB  1 
ATOM   2172 C CG  . LEU A 1 275 ? 2.769   -43.369 20.720  1.00 64.22  ? 274  LEU A CG  1 
ATOM   2173 C CD1 . LEU A 1 275 ? 2.976   -44.256 21.924  1.00 56.18  ? 274  LEU A CD1 1 
ATOM   2174 C CD2 . LEU A 1 275 ? 4.003   -42.515 20.432  1.00 57.27  ? 274  LEU A CD2 1 
ATOM   2175 N N   . GLY A 1 276 ? -0.288  -46.261 18.850  1.00 67.96  ? 275  GLY A N   1 
ATOM   2176 C CA  . GLY A 1 276 ? -1.235  -46.726 17.853  1.00 68.98  ? 275  GLY A CA  1 
ATOM   2177 C C   . GLY A 1 276 ? -2.694  -46.764 18.257  1.00 75.36  ? 275  GLY A C   1 
ATOM   2178 O O   . GLY A 1 276 ? -3.062  -46.426 19.378  1.00 77.55  ? 275  GLY A O   1 
ATOM   2179 N N   . GLU A 1 277 ? -3.523  -47.198 17.317  1.00 86.54  ? 276  GLU A N   1 
ATOM   2180 C CA  . GLU A 1 277 ? -4.976  -47.221 17.461  1.00 88.68  ? 276  GLU A CA  1 
ATOM   2181 C C   . GLU A 1 277 ? -5.539  -48.129 18.568  1.00 86.58  ? 276  GLU A C   1 
ATOM   2182 O O   . GLU A 1 277 ? -6.695  -47.979 18.961  1.00 86.96  ? 276  GLU A O   1 
ATOM   2183 C CB  . GLU A 1 277 ? -5.596  -47.659 16.138  1.00 100.40 ? 276  GLU A CB  1 
ATOM   2184 C CG  . GLU A 1 277 ? -5.588  -49.182 15.925  1.00 103.32 ? 276  GLU A CG  1 
ATOM   2185 C CD  . GLU A 1 277 ? -4.336  -49.692 15.219  1.00 111.20 ? 276  GLU A CD  1 
ATOM   2186 O OE1 . GLU A 1 277 ? -3.257  -49.071 15.365  1.00 105.42 ? 276  GLU A OE1 1 
ATOM   2187 O OE2 . GLU A 1 277 ? -4.437  -50.724 14.514  1.00 120.91 ? 276  GLU A OE2 1 
ATOM   2188 N N   . ASP A 1 278 ? -4.763  -49.089 19.056  1.00 80.56  ? 277  ASP A N   1 
ATOM   2189 C CA  . ASP A 1 278 ? -5.322  -50.017 20.036  1.00 84.14  ? 277  ASP A CA  1 
ATOM   2190 C C   . ASP A 1 278 ? -5.051  -49.592 21.478  1.00 79.95  ? 277  ASP A C   1 
ATOM   2191 O O   . ASP A 1 278 ? -5.100  -50.400 22.404  1.00 92.29  ? 277  ASP A O   1 
ATOM   2192 C CB  . ASP A 1 278 ? -4.907  -51.473 19.756  1.00 97.66  ? 277  ASP A CB  1 
ATOM   2193 C CG  . ASP A 1 278 ? -3.413  -51.631 19.522  1.00 114.43 ? 277  ASP A CG  1 
ATOM   2194 O OD1 . ASP A 1 278 ? -2.673  -50.609 19.578  1.00 121.78 ? 277  ASP A OD1 1 
ATOM   2195 O OD2 . ASP A 1 278 ? -2.989  -52.792 19.282  1.00 98.16  ? 277  ASP A OD2 1 
ATOM   2196 N N   . ASP A 1 279 ? -4.789  -48.302 21.647  1.00 71.09  ? 278  ASP A N   1 
ATOM   2197 C CA  . ASP A 1 279 ? -4.499  -47.690 22.940  1.00 57.67  ? 278  ASP A CA  1 
ATOM   2198 C C   . ASP A 1 279 ? -5.495  -46.541 23.124  1.00 62.26  ? 278  ASP A C   1 
ATOM   2199 O O   . ASP A 1 279 ? -5.430  -45.525 22.436  1.00 70.81  ? 278  ASP A O   1 
ATOM   2200 C CB  . ASP A 1 279 ? -3.040  -47.222 22.958  1.00 65.43  ? 278  ASP A CB  1 
ATOM   2201 C CG  . ASP A 1 279 ? -2.701  -46.333 24.142  1.00 73.93  ? 278  ASP A CG  1 
ATOM   2202 O OD1 . ASP A 1 279 ? -3.613  -45.936 24.909  1.00 72.23  ? 278  ASP A OD1 1 
ATOM   2203 O OD2 . ASP A 1 279 ? -1.495  -46.022 24.284  1.00 65.09  ? 278  ASP A OD2 1 
ATOM   2204 N N   . ASP A 1 280 ? -6.437  -46.734 24.039  1.00 63.85  ? 279  ASP A N   1 
ATOM   2205 C CA  . ASP A 1 280 ? -7.614  -45.884 24.145  1.00 58.85  ? 279  ASP A CA  1 
ATOM   2206 C C   . ASP A 1 280 ? -7.292  -44.523 24.724  1.00 63.19  ? 279  ASP A C   1 
ATOM   2207 O O   . ASP A 1 280 ? -7.984  -43.554 24.439  1.00 71.86  ? 279  ASP A O   1 
ATOM   2208 C CB  . ASP A 1 280 ? -8.716  -46.575 24.962  1.00 62.52  ? 279  ASP A CB  1 
ATOM   2209 C CG  . ASP A 1 280 ? -8.160  -47.361 26.151  1.00 98.52  ? 279  ASP A CG  1 
ATOM   2210 O OD1 . ASP A 1 280 ? -7.695  -48.510 25.944  1.00 105.56 ? 279  ASP A OD1 1 
ATOM   2211 O OD2 . ASP A 1 280 ? -8.183  -46.830 27.289  1.00 106.04 ? 279  ASP A OD2 1 
ATOM   2212 N N   . ILE A 1 281 ? -6.256  -44.451 25.550  1.00 58.71  ? 280  ILE A N   1 
ATOM   2213 C CA  . ILE A 1 281 ? -5.802  -43.156 26.040  1.00 60.37  ? 280  ILE A CA  1 
ATOM   2214 C C   . ILE A 1 281 ? -5.130  -42.360 24.908  1.00 64.61  ? 280  ILE A C   1 
ATOM   2215 O O   . ILE A 1 281 ? -5.347  -41.159 24.784  1.00 69.84  ? 280  ILE A O   1 
ATOM   2216 C CB  . ILE A 1 281 ? -4.834  -43.288 27.225  1.00 62.85  ? 280  ILE A CB  1 
ATOM   2217 C CG1 . ILE A 1 281 ? -5.587  -43.705 28.480  1.00 71.59  ? 280  ILE A CG1 1 
ATOM   2218 C CG2 . ILE A 1 281 ? -4.126  -41.973 27.483  1.00 65.44  ? 280  ILE A CG2 1 
ATOM   2219 C CD1 . ILE A 1 281 ? -4.772  -44.620 29.382  1.00 85.95  ? 280  ILE A CD1 1 
ATOM   2220 N N   . TRP A 1 282 ? -4.323  -43.028 24.085  1.00 55.39  ? 281  TRP A N   1 
ATOM   2221 C CA  . TRP A 1 282 ? -3.699  -42.375 22.944  1.00 57.21  ? 281  TRP A CA  1 
ATOM   2222 C C   . TRP A 1 282 ? -4.753  -41.696 22.100  1.00 65.54  ? 281  TRP A C   1 
ATOM   2223 O O   . TRP A 1 282 ? -4.689  -40.478 21.889  1.00 55.66  ? 281  TRP A O   1 
ATOM   2224 C CB  . TRP A 1 282 ? -2.951  -43.379 22.094  1.00 56.19  ? 281  TRP A CB  1 
ATOM   2225 C CG  . TRP A 1 282 ? -2.233  -42.798 20.909  1.00 57.74  ? 281  TRP A CG  1 
ATOM   2226 C CD1 . TRP A 1 282 ? -2.314  -43.229 19.621  1.00 64.74  ? 281  TRP A CD1 1 
ATOM   2227 C CD2 . TRP A 1 282 ? -1.306  -41.706 20.904  1.00 50.87  ? 281  TRP A CD2 1 
ATOM   2228 N NE1 . TRP A 1 282 ? -1.496  -42.486 18.814  1.00 57.51  ? 281  TRP A NE1 1 
ATOM   2229 C CE2 . TRP A 1 282 ? -0.860  -41.542 19.576  1.00 46.35  ? 281  TRP A CE2 1 
ATOM   2230 C CE3 . TRP A 1 282 ? -0.803  -40.857 21.892  1.00 47.88  ? 281  TRP A CE3 1 
ATOM   2231 C CZ2 . TRP A 1 282 ? 0.067   -40.564 19.204  1.00 42.59  ? 281  TRP A CZ2 1 
ATOM   2232 C CZ3 . TRP A 1 282 ? 0.115   -39.879 21.519  1.00 53.06  ? 281  TRP A CZ3 1 
ATOM   2233 C CH2 . TRP A 1 282 ? 0.544   -39.747 20.184  1.00 48.14  ? 281  TRP A CH2 1 
ATOM   2234 N N   . LEU A 1 283 ? -5.712  -42.484 21.606  1.00 66.12  ? 282  LEU A N   1 
ATOM   2235 C CA  . LEU A 1 283 ? -6.917  -41.922 21.014  1.00 66.34  ? 282  LEU A CA  1 
ATOM   2236 C C   . LEU A 1 283 ? -7.501  -40.996 22.065  1.00 76.40  ? 282  LEU A C   1 
ATOM   2237 O O   . LEU A 1 283 ? -7.234  -41.167 23.253  1.00 90.25  ? 282  LEU A O   1 
ATOM   2238 C CB  . LEU A 1 283 ? -7.907  -43.027 20.713  1.00 68.46  ? 282  LEU A CB  1 
ATOM   2239 C CG  . LEU A 1 283 ? -7.819  -43.827 19.408  1.00 75.55  ? 282  LEU A CG  1 
ATOM   2240 C CD1 . LEU A 1 283 ? -6.404  -44.231 19.035  1.00 70.91  ? 282  LEU A CD1 1 
ATOM   2241 C CD2 . LEU A 1 283 ? -8.705  -45.046 19.554  1.00 71.57  ? 282  LEU A CD2 1 
ATOM   2242 N N   . GLN A 1 284 ? -8.278  -40.004 21.658  1.00 68.71  ? 283  GLN A N   1 
ATOM   2243 C CA  . GLN A 1 284 ? -8.938  -39.145 22.651  1.00 84.74  ? 283  GLN A CA  1 
ATOM   2244 C C   . GLN A 1 284 ? -8.005  -38.130 23.283  1.00 79.34  ? 283  GLN A C   1 
ATOM   2245 O O   . GLN A 1 284 ? -8.392  -36.988 23.528  1.00 83.56  ? 283  GLN A O   1 
ATOM   2246 C CB  . GLN A 1 284 ? -9.601  -39.969 23.766  1.00 86.60  ? 283  GLN A CB  1 
ATOM   2247 C CG  . GLN A 1 284 ? -9.036  -39.712 25.159  1.00 76.50  ? 283  GLN A CG  1 
ATOM   2248 C CD  . GLN A 1 284 ? -10.003 -40.140 26.277  1.00 104.08 ? 283  GLN A CD  1 
ATOM   2249 O OE1 . GLN A 1 284 ? -10.040 -39.527 27.353  1.00 100.71 ? 283  GLN A OE1 1 
ATOM   2250 N NE2 . GLN A 1 284 ? -10.789 -41.196 26.020  1.00 109.46 ? 283  GLN A NE2 1 
ATOM   2251 N N   . MET A 1 285 ? -6.779  -38.545 23.553  1.00 71.56  ? 284  MET A N   1 
ATOM   2252 C CA  . MET A 1 285 ? -5.796  -37.620 24.083  1.00 68.59  ? 284  MET A CA  1 
ATOM   2253 C C   . MET A 1 285 ? -4.892  -36.969 23.007  1.00 64.24  ? 284  MET A C   1 
ATOM   2254 O O   . MET A 1 285 ? -4.379  -35.861 23.206  1.00 51.99  ? 284  MET A O   1 
ATOM   2255 C CB  . MET A 1 285 ? -4.970  -38.312 25.160  1.00 56.26  ? 284  MET A CB  1 
ATOM   2256 C CG  . MET A 1 285 ? -4.758  -37.463 26.373  1.00 63.69  ? 284  MET A CG  1 
ATOM   2257 S SD  . MET A 1 285 ? -6.032  -37.648 27.623  1.00 71.35  ? 284  MET A SD  1 
ATOM   2258 C CE  . MET A 1 285 ? -7.539  -37.313 26.729  1.00 155.62 ? 284  MET A CE  1 
ATOM   2259 N N   . ARG A 1 286 ? -4.744  -37.638 21.864  1.00 53.86  ? 285  ARG A N   1 
ATOM   2260 C CA  . ARG A 1 286 ? -3.727  -37.275 20.874  1.00 57.67  ? 285  ARG A CA  1 
ATOM   2261 C C   . ARG A 1 286 ? -3.928  -35.948 20.138  1.00 52.16  ? 285  ARG A C   1 
ATOM   2262 O O   . ARG A 1 286 ? -2.990  -35.425 19.571  1.00 53.24  ? 285  ARG A O   1 
ATOM   2263 C CB  . ARG A 1 286 ? -3.551  -38.404 19.851  1.00 54.66  ? 285  ARG A CB  1 
ATOM   2264 C CG  . ARG A 1 286 ? -4.813  -38.766 19.074  1.00 44.19  ? 285  ARG A CG  1 
ATOM   2265 C CD  . ARG A 1 286 ? -4.481  -39.897 18.133  1.00 53.95  ? 285  ARG A CD  1 
ATOM   2266 N NE  . ARG A 1 286 ? -5.579  -40.356 17.283  1.00 61.94  ? 285  ARG A NE  1 
ATOM   2267 C CZ  . ARG A 1 286 ? -5.416  -41.273 16.332  1.00 71.08  ? 285  ARG A CZ  1 
ATOM   2268 N NH1 . ARG A 1 286 ? -6.440  -41.644 15.576  1.00 64.61  ? 285  ARG A NH1 1 
ATOM   2269 N NH2 . ARG A 1 286 ? -4.210  -41.812 16.131  1.00 67.43  ? 285  ARG A NH2 1 
ATOM   2270 N N   . HIS A 1 287 ? -5.148  -35.430 20.125  1.00 53.60  ? 286  HIS A N   1 
ATOM   2271 C CA  . HIS A 1 287 ? -5.432  -34.160 19.474  1.00 52.42  ? 286  HIS A CA  1 
ATOM   2272 C C   . HIS A 1 287 ? -5.694  -33.032 20.465  1.00 59.88  ? 286  HIS A C   1 
ATOM   2273 O O   . HIS A 1 287 ? -6.075  -31.927 20.075  1.00 67.63  ? 286  HIS A O   1 
ATOM   2274 C CB  . HIS A 1 287 ? -6.631  -34.290 18.557  1.00 43.39  ? 286  HIS A CB  1 
ATOM   2275 C CG  . HIS A 1 287 ? -6.510  -35.396 17.569  1.00 52.48  ? 286  HIS A CG  1 
ATOM   2276 N ND1 . HIS A 1 287 ? -5.328  -35.684 16.922  1.00 51.85  ? 286  HIS A ND1 1 
ATOM   2277 C CD2 . HIS A 1 287 ? -7.424  -36.274 17.093  1.00 69.09  ? 286  HIS A CD2 1 
ATOM   2278 C CE1 . HIS A 1 287 ? -5.516  -36.694 16.096  1.00 52.92  ? 286  HIS A CE1 1 
ATOM   2279 N NE2 . HIS A 1 287 ? -6.781  -37.071 16.179  1.00 72.01  ? 286  HIS A NE2 1 
ATOM   2280 N N   . LEU A 1 288 ? -5.487  -33.320 21.742  1.00 54.27  ? 287  LEU A N   1 
ATOM   2281 C CA  . LEU A 1 288 ? -5.667  -32.333 22.796  1.00 55.19  ? 287  LEU A CA  1 
ATOM   2282 C C   . LEU A 1 288 ? -4.411  -31.505 23.018  1.00 54.03  ? 287  LEU A C   1 
ATOM   2283 O O   . LEU A 1 288 ? -3.312  -31.941 22.710  1.00 52.78  ? 287  LEU A O   1 
ATOM   2284 C CB  . LEU A 1 288 ? -6.064  -33.032 24.101  1.00 54.04  ? 287  LEU A CB  1 
ATOM   2285 C CG  . LEU A 1 288 ? -7.563  -33.309 24.303  1.00 55.47  ? 287  LEU A CG  1 
ATOM   2286 C CD1 . LEU A 1 288 ? -8.324  -33.542 22.999  1.00 41.69  ? 287  LEU A CD1 1 
ATOM   2287 C CD2 . LEU A 1 288 ? -7.746  -34.452 25.239  1.00 41.06  ? 287  LEU A CD2 1 
ATOM   2288 N N   . HIS A 1 289 ? -4.590  -30.302 23.549  1.00 61.76  ? 288  HIS A N   1 
ATOM   2289 C CA  . HIS A 1 289 ? -3.481  -29.452 23.965  1.00 56.91  ? 288  HIS A CA  1 
ATOM   2290 C C   . HIS A 1 289 ? -2.665  -30.127 25.077  1.00 56.30  ? 288  HIS A C   1 
ATOM   2291 O O   . HIS A 1 289 ? -3.236  -30.660 26.019  1.00 62.47  ? 288  HIS A O   1 
ATOM   2292 C CB  . HIS A 1 289 ? -4.046  -28.121 24.484  1.00 67.23  ? 288  HIS A CB  1 
ATOM   2293 C CG  . HIS A 1 289 ? -3.039  -27.010 24.540  1.00 69.56  ? 288  HIS A CG  1 
ATOM   2294 N ND1 . HIS A 1 289 ? -2.188  -26.824 25.611  1.00 59.72  ? 288  HIS A ND1 1 
ATOM   2295 C CD2 . HIS A 1 289 ? -2.737  -26.040 23.646  1.00 64.81  ? 288  HIS A CD2 1 
ATOM   2296 C CE1 . HIS A 1 289 ? -1.413  -25.782 25.378  1.00 66.78  ? 288  HIS A CE1 1 
ATOM   2297 N NE2 . HIS A 1 289 ? -1.721  -25.292 24.190  1.00 77.92  ? 288  HIS A NE2 1 
ATOM   2298 N N   . ILE A 1 290 ? -1.340  -30.083 25.001  1.00 55.59  ? 289  ILE A N   1 
ATOM   2299 C CA  . ILE A 1 290 ? -0.521  -30.783 25.999  1.00 60.98  ? 289  ILE A CA  1 
ATOM   2300 C C   . ILE A 1 290 ? -0.752  -30.404 27.465  1.00 64.64  ? 289  ILE A C   1 
ATOM   2301 O O   . ILE A 1 290 ? -0.587  -31.253 28.338  1.00 72.66  ? 289  ILE A O   1 
ATOM   2302 C CB  . ILE A 1 290 ? 0.986   -30.663 25.732  1.00 58.36  ? 289  ILE A CB  1 
ATOM   2303 C CG1 . ILE A 1 290 ? 1.419   -29.199 25.810  1.00 49.37  ? 289  ILE A CG1 1 
ATOM   2304 C CG2 . ILE A 1 290 ? 1.348   -31.285 24.398  1.00 72.46  ? 289  ILE A CG2 1 
ATOM   2305 C CD1 . ILE A 1 290 ? 2.898   -29.024 25.663  1.00 66.01  ? 289  ILE A CD1 1 
ATOM   2306 N N   . SER A 1 291 ? -1.083  -29.147 27.750  1.00 60.09  ? 290  SER A N   1 
ATOM   2307 C CA  . SER A 1 291 ? -1.317  -28.729 29.143  1.00 75.30  ? 290  SER A CA  1 
ATOM   2308 C C   . SER A 1 291 ? -2.512  -29.482 29.744  1.00 77.25  ? 290  SER A C   1 
ATOM   2309 O O   . SER A 1 291 ? -2.533  -29.869 30.917  1.00 84.10  ? 290  SER A O   1 
ATOM   2310 C CB  . SER A 1 291 ? -1.592  -27.235 29.216  1.00 68.77  ? 290  SER A CB  1 
ATOM   2311 O OG  . SER A 1 291 ? -2.826  -26.948 28.583  1.00 72.75  ? 290  SER A OG  1 
ATOM   2312 N N   . GLU A 1 292 ? -3.507  -29.687 28.903  1.00 58.78  ? 291  GLU A N   1 
ATOM   2313 C CA  . GLU A 1 292 ? -4.710  -30.389 29.277  1.00 56.66  ? 291  GLU A CA  1 
ATOM   2314 C C   . GLU A 1 292 ? -4.476  -31.909 29.355  1.00 64.85  ? 291  GLU A C   1 
ATOM   2315 O O   . GLU A 1 292 ? -5.072  -32.585 30.191  1.00 59.16  ? 291  GLU A O   1 
ATOM   2316 C CB  . GLU A 1 292 ? -5.789  -30.026 28.265  1.00 53.74  ? 291  GLU A CB  1 
ATOM   2317 C CG  . GLU A 1 292 ? -7.075  -30.780 28.355  1.00 85.83  ? 291  GLU A CG  1 
ATOM   2318 C CD  . GLU A 1 292 ? -8.001  -30.392 27.223  1.00 104.74 ? 291  GLU A CD  1 
ATOM   2319 O OE1 . GLU A 1 292 ? -7.594  -29.517 26.420  1.00 106.91 ? 291  GLU A OE1 1 
ATOM   2320 O OE2 . GLU A 1 292 ? -9.118  -30.956 27.135  1.00 108.78 ? 291  GLU A OE2 1 
ATOM   2321 N N   . VAL A 1 293 ? -3.598  -32.436 28.499  1.00 64.32  ? 292  VAL A N   1 
ATOM   2322 C CA  . VAL A 1 293 ? -3.268  -33.861 28.524  1.00 57.75  ? 292  VAL A CA  1 
ATOM   2323 C C   . VAL A 1 293 ? -2.509  -34.238 29.787  1.00 58.79  ? 292  VAL A C   1 
ATOM   2324 O O   . VAL A 1 293 ? -2.865  -35.175 30.480  1.00 58.41  ? 292  VAL A O   1 
ATOM   2325 C CB  . VAL A 1 293 ? -2.435  -34.283 27.310  1.00 55.44  ? 292  VAL A CB  1 
ATOM   2326 C CG1 . VAL A 1 293 ? -1.780  -35.625 27.573  1.00 47.35  ? 292  VAL A CG1 1 
ATOM   2327 C CG2 . VAL A 1 293 ? -3.301  -34.347 26.047  1.00 57.95  ? 292  VAL A CG2 1 
ATOM   2328 N N   . PHE A 1 294 ? -1.449  -33.498 30.065  1.00 72.54  ? 293  PHE A N   1 
ATOM   2329 C CA  . PHE A 1 294 ? -0.736  -33.593 31.328  1.00 84.67  ? 293  PHE A CA  1 
ATOM   2330 C C   . PHE A 1 294 ? -1.684  -33.999 32.461  1.00 79.99  ? 293  PHE A C   1 
ATOM   2331 O O   . PHE A 1 294 ? -1.438  -34.988 33.149  1.00 76.67  ? 293  PHE A O   1 
ATOM   2332 C CB  . PHE A 1 294 ? -0.076  -32.238 31.621  1.00 95.86  ? 293  PHE A CB  1 
ATOM   2333 C CG  . PHE A 1 294 ? 0.911   -32.261 32.748  1.00 119.39 ? 293  PHE A CG  1 
ATOM   2334 C CD1 . PHE A 1 294 ? 2.170   -32.821 32.577  1.00 124.79 ? 293  PHE A CD1 1 
ATOM   2335 C CD2 . PHE A 1 294 ? 0.599   -31.683 33.972  1.00 135.44 ? 293  PHE A CD2 1 
ATOM   2336 C CE1 . PHE A 1 294 ? 3.095   -32.829 33.613  1.00 130.41 ? 293  PHE A CE1 1 
ATOM   2337 C CE2 . PHE A 1 294 ? 1.518   -31.686 35.014  1.00 142.51 ? 293  PHE A CE2 1 
ATOM   2338 C CZ  . PHE A 1 294 ? 2.769   -32.261 34.834  1.00 138.07 ? 293  PHE A CZ  1 
ATOM   2339 N N   . ARG A 1 295 ? -2.779  -33.254 32.636  1.00 75.79  ? 294  ARG A N   1 
ATOM   2340 C CA  . ARG A 1 295 ? -3.642  -33.435 33.811  1.00 67.83  ? 294  ARG A CA  1 
ATOM   2341 C C   . ARG A 1 295 ? -4.831  -34.412 33.680  1.00 72.91  ? 294  ARG A C   1 
ATOM   2342 O O   . ARG A 1 295 ? -5.347  -34.883 34.690  1.00 79.94  ? 294  ARG A O   1 
ATOM   2343 C CB  . ARG A 1 295 ? -4.108  -32.083 34.361  1.00 71.97  ? 294  ARG A CB  1 
ATOM   2344 C CG  . ARG A 1 295 ? -4.990  -31.287 33.419  1.00 80.82  ? 294  ARG A CG  1 
ATOM   2345 C CD  . ARG A 1 295 ? -5.331  -29.904 33.970  1.00 71.80  ? 294  ARG A CD  1 
ATOM   2346 N NE  . ARG A 1 295 ? -5.974  -29.095 32.942  1.00 80.85  ? 294  ARG A NE  1 
ATOM   2347 C CZ  . ARG A 1 295 ? -7.254  -29.221 32.603  1.00 97.87  ? 294  ARG A CZ  1 
ATOM   2348 N NH1 . ARG A 1 295 ? -8.018  -30.119 33.225  1.00 89.16  ? 294  ARG A NH1 1 
ATOM   2349 N NH2 . ARG A 1 295 ? -7.778  -28.448 31.654  1.00 104.74 ? 294  ARG A NH2 1 
ATOM   2350 N N   . LYS A 1 296 ? -5.265  -34.717 32.458  1.00 62.33  ? 295  LYS A N   1 
ATOM   2351 C CA  . LYS A 1 296 ? -6.337  -35.694 32.264  1.00 58.55  ? 295  LYS A CA  1 
ATOM   2352 C C   . LYS A 1 296 ? -5.844  -37.131 32.429  1.00 64.54  ? 295  LYS A C   1 
ATOM   2353 O O   . LYS A 1 296 ? -6.544  -37.975 32.981  1.00 76.28  ? 295  LYS A O   1 
ATOM   2354 C CB  . LYS A 1 296 ? -7.020  -35.537 30.897  1.00 57.06  ? 295  LYS A CB  1 
ATOM   2355 C CG  . LYS A 1 296 ? -7.670  -34.178 30.642  1.00 72.78  ? 295  LYS A CG  1 
ATOM   2356 C CD  . LYS A 1 296 ? -9.104  -34.102 31.117  1.00 93.00  ? 295  LYS A CD  1 
ATOM   2357 C CE  . LYS A 1 296 ? -9.811  -32.904 30.490  1.00 100.73 ? 295  LYS A CE  1 
ATOM   2358 N NZ  . LYS A 1 296 ? -9.936  -33.066 29.015  1.00 100.97 ? 295  LYS A NZ  1 
ATOM   2359 N N   . VAL A 1 297 ? -4.646  -37.414 31.936  1.00 66.94  ? 296  VAL A N   1 
ATOM   2360 C CA  . VAL A 1 297 ? -4.036  -38.725 32.130  1.00 62.67  ? 296  VAL A CA  1 
ATOM   2361 C C   . VAL A 1 297 ? -3.870  -38.996 33.621  1.00 60.08  ? 296  VAL A C   1 
ATOM   2362 O O   . VAL A 1 297 ? -4.164  -40.081 34.099  1.00 51.86  ? 296  VAL A O   1 
ATOM   2363 C CB  . VAL A 1 297 ? -2.670  -38.808 31.441  1.00 56.77  ? 296  VAL A CB  1 
ATOM   2364 C CG1 . VAL A 1 297 ? -1.945  -40.090 31.835  1.00 56.42  ? 296  VAL A CG1 1 
ATOM   2365 C CG2 . VAL A 1 297 ? -2.847  -38.725 29.942  1.00 54.63  ? 296  VAL A CG2 1 
ATOM   2366 N N   . LYS A 1 298 ? -3.402  -37.994 34.355  1.00 58.90  ? 297  LYS A N   1 
ATOM   2367 C CA  . LYS A 1 298 ? -3.314  -38.094 35.805  1.00 57.15  ? 297  LYS A CA  1 
ATOM   2368 C C   . LYS A 1 298 ? -4.705  -38.337 36.438  1.00 59.16  ? 297  LYS A C   1 
ATOM   2369 O O   . LYS A 1 298 ? -4.872  -39.244 37.241  1.00 57.05  ? 297  LYS A O   1 
ATOM   2370 C CB  . LYS A 1 298 ? -2.607  -36.847 36.365  1.00 68.16  ? 297  LYS A CB  1 
ATOM   2371 C CG  . LYS A 1 298 ? -2.338  -36.872 37.864  1.00 86.40  ? 297  LYS A CG  1 
ATOM   2372 C CD  . LYS A 1 298 ? -1.719  -38.182 38.324  1.00 88.91  ? 297  LYS A CD  1 
ATOM   2373 C CE  . LYS A 1 298 ? -1.512  -38.197 39.833  1.00 90.14  ? 297  LYS A CE  1 
ATOM   2374 N NZ  . LYS A 1 298 ? -1.112  -39.548 40.317  1.00 90.73  ? 297  LYS A NZ  1 
ATOM   2375 N N   . SER A 1 299 ? -5.700  -37.546 36.045  1.00 70.61  ? 298  SER A N   1 
ATOM   2376 C CA  . SER A 1 299 ? -7.086  -37.715 36.499  1.00 65.48  ? 298  SER A CA  1 
ATOM   2377 C C   . SER A 1 299 ? -7.654  -39.086 36.160  1.00 67.53  ? 298  SER A C   1 
ATOM   2378 O O   . SER A 1 299 ? -8.256  -39.756 36.986  1.00 66.56  ? 298  SER A O   1 
ATOM   2379 C CB  . SER A 1 299 ? -7.979  -36.663 35.834  1.00 67.47  ? 298  SER A CB  1 
ATOM   2380 O OG  . SER A 1 299 ? -8.076  -35.495 36.623  1.00 87.43  ? 298  SER A OG  1 
ATOM   2381 N N   . SER A 1 300 ? -7.493  -39.464 34.903  1.00 68.14  ? 299  SER A N   1 
ATOM   2382 C CA  . SER A 1 300 ? -8.013  -40.705 34.383  1.00 58.59  ? 299  SER A CA  1 
ATOM   2383 C C   . SER A 1 300 ? -7.347  -41.883 35.104  1.00 67.16  ? 299  SER A C   1 
ATOM   2384 O O   . SER A 1 300 ? -7.991  -42.888 35.411  1.00 59.05  ? 299  SER A O   1 
ATOM   2385 C CB  . SER A 1 300 ? -7.753  -40.733 32.877  1.00 55.94  ? 299  SER A CB  1 
ATOM   2386 O OG  . SER A 1 300 ? -8.291  -41.880 32.249  1.00 70.59  ? 299  SER A OG  1 
ATOM   2387 N N   . PHE A 1 301 ? -6.058  -41.740 35.397  1.00 72.59  ? 300  PHE A N   1 
ATOM   2388 C CA  . PHE A 1 301 ? -5.313  -42.757 36.125  1.00 75.79  ? 300  PHE A CA  1 
ATOM   2389 C C   . PHE A 1 301 ? -5.811  -42.921 37.560  1.00 72.34  ? 300  PHE A C   1 
ATOM   2390 O O   . PHE A 1 301 ? -6.036  -44.041 38.013  1.00 71.43  ? 300  PHE A O   1 
ATOM   2391 C CB  . PHE A 1 301 ? -3.815  -42.433 36.114  1.00 80.74  ? 300  PHE A CB  1 
ATOM   2392 C CG  . PHE A 1 301 ? -2.985  -43.374 36.938  1.00 80.00  ? 300  PHE A CG  1 
ATOM   2393 C CD1 . PHE A 1 301 ? -2.758  -44.670 36.511  1.00 65.35  ? 300  PHE A CD1 1 
ATOM   2394 C CD2 . PHE A 1 301 ? -2.438  -42.964 38.148  1.00 77.79  ? 300  PHE A CD2 1 
ATOM   2395 C CE1 . PHE A 1 301 ? -1.997  -45.535 37.280  1.00 70.53  ? 300  PHE A CE1 1 
ATOM   2396 C CE2 . PHE A 1 301 ? -1.679  -43.830 38.919  1.00 72.27  ? 300  PHE A CE2 1 
ATOM   2397 C CZ  . PHE A 1 301 ? -1.461  -45.116 38.485  1.00 69.87  ? 300  PHE A CZ  1 
ATOM   2398 N N   . ASP A 1 302 ? -5.970  -41.805 38.269  1.00 66.73  ? 301  ASP A N   1 
ATOM   2399 C CA  . ASP A 1 302 ? -6.470  -41.818 39.650  1.00 73.65  ? 301  ASP A CA  1 
ATOM   2400 C C   . ASP A 1 302 ? -7.926  -42.302 39.741  1.00 80.28  ? 301  ASP A C   1 
ATOM   2401 O O   . ASP A 1 302 ? -8.282  -43.051 40.656  1.00 81.77  ? 301  ASP A O   1 
ATOM   2402 C CB  . ASP A 1 302 ? -6.332  -40.434 40.313  1.00 76.28  ? 301  ASP A CB  1 
ATOM   2403 C CG  . ASP A 1 302 ? -4.874  -40.061 40.646  1.00 90.37  ? 301  ASP A CG  1 
ATOM   2404 O OD1 . ASP A 1 302 ? -3.986  -40.940 40.616  1.00 97.00  ? 301  ASP A OD1 1 
ATOM   2405 O OD2 . ASP A 1 302 ? -4.618  -38.875 40.951  1.00 90.21  ? 301  ASP A OD2 1 
ATOM   2406 N N   . GLU A 1 303 ? -8.764  -41.872 38.800  1.00 79.11  ? 302  GLU A N   1 
ATOM   2407 C CA  . GLU A 1 303 ? -10.147 -42.340 38.758  1.00 78.36  ? 302  GLU A CA  1 
ATOM   2408 C C   . GLU A 1 303 ? -10.176 -43.828 38.497  1.00 79.66  ? 302  GLU A C   1 
ATOM   2409 O O   . GLU A 1 303 ? -10.990 -44.542 39.074  1.00 89.80  ? 302  GLU A O   1 
ATOM   2410 C CB  . GLU A 1 303 ? -10.988 -41.594 37.714  1.00 89.13  ? 302  GLU A CB  1 
ATOM   2411 C CG  . GLU A 1 303 ? -11.231 -40.125 38.068  1.00 121.14 ? 302  GLU A CG  1 
ATOM   2412 C CD  . GLU A 1 303 ? -12.048 -39.365 37.022  1.00 139.58 ? 302  GLU A CD  1 
ATOM   2413 O OE1 . GLU A 1 303 ? -13.296 -39.409 37.099  1.00 145.54 ? 302  GLU A OE1 1 
ATOM   2414 O OE2 . GLU A 1 303 ? -11.447 -38.706 36.140  1.00 139.27 ? 302  GLU A OE2 1 
ATOM   2415 N N   . PHE A 1 304 ? -9.278  -44.306 37.640  1.00 85.25  ? 303  PHE A N   1 
ATOM   2416 C CA  . PHE A 1 304 ? -9.265  -45.726 37.299  1.00 79.07  ? 303  PHE A CA  1 
ATOM   2417 C C   . PHE A 1 304 ? -8.949  -46.572 38.519  1.00 73.24  ? 303  PHE A C   1 
ATOM   2418 O O   . PHE A 1 304 ? -9.613  -47.566 38.778  1.00 75.52  ? 303  PHE A O   1 
ATOM   2419 C CB  . PHE A 1 304 ? -8.267  -46.043 36.187  1.00 74.44  ? 303  PHE A CB  1 
ATOM   2420 C CG  . PHE A 1 304 ? -8.230  -47.494 35.825  1.00 76.49  ? 303  PHE A CG  1 
ATOM   2421 C CD1 . PHE A 1 304 ? -7.456  -48.386 36.555  1.00 71.09  ? 303  PHE A CD1 1 
ATOM   2422 C CD2 . PHE A 1 304 ? -8.994  -47.978 34.773  1.00 81.46  ? 303  PHE A CD2 1 
ATOM   2423 C CE1 . PHE A 1 304 ? -7.440  -49.727 36.239  1.00 73.64  ? 303  PHE A CE1 1 
ATOM   2424 C CE2 . PHE A 1 304 ? -8.983  -49.321 34.450  1.00 74.94  ? 303  PHE A CE2 1 
ATOM   2425 C CZ  . PHE A 1 304 ? -8.205  -50.198 35.185  1.00 73.23  ? 303  PHE A CZ  1 
ATOM   2426 N N   . CYS A 1 305 ? -7.930  -46.175 39.267  1.00 72.20  ? 304  CYS A N   1 
ATOM   2427 C CA  . CYS A 1 305 ? -7.537  -46.915 40.457  1.00 85.46  ? 304  CYS A CA  1 
ATOM   2428 C C   . CYS A 1 305 ? -8.647  -46.939 41.496  1.00 91.24  ? 304  CYS A C   1 
ATOM   2429 O O   . CYS A 1 305 ? -9.021  -48.000 41.986  1.00 100.84 ? 304  CYS A O   1 
ATOM   2430 C CB  . CYS A 1 305 ? -6.268  -46.320 41.064  1.00 87.53  ? 304  CYS A CB  1 
ATOM   2431 S SG  . CYS A 1 305 ? -4.819  -46.551 40.049  1.00 90.48  ? 304  CYS A SG  1 
ATOM   2432 N N   . VAL A 1 306 ? -9.164  -45.762 41.830  1.00 90.32  ? 305  VAL A N   1 
ATOM   2433 C CA  . VAL A 1 306 ? -10.239 -45.649 42.804  1.00 90.39  ? 305  VAL A CA  1 
ATOM   2434 C C   . VAL A 1 306 ? -11.426 -46.528 42.429  1.00 91.64  ? 305  VAL A C   1 
ATOM   2435 O O   . VAL A 1 306 ? -11.994 -47.212 43.277  1.00 93.81  ? 305  VAL A O   1 
ATOM   2436 C CB  . VAL A 1 306 ? -10.703 -44.187 42.965  1.00 82.72  ? 305  VAL A CB  1 
ATOM   2437 C CG1 . VAL A 1 306 ? -12.185 -44.129 43.311  1.00 76.02  ? 305  VAL A CG1 1 
ATOM   2438 C CG2 . VAL A 1 306 ? -9.864  -43.483 44.017  1.00 68.46  ? 305  VAL A CG2 1 
ATOM   2439 N N   . SER A 1 307 ? -11.788 -46.508 41.152  1.00 89.48  ? 306  SER A N   1 
ATOM   2440 C CA  . SER A 1 307 ? -12.889 -47.317 40.649  1.00 87.92  ? 306  SER A CA  1 
ATOM   2441 C C   . SER A 1 307 ? -12.573 -48.811 40.666  1.00 86.91  ? 306  SER A C   1 
ATOM   2442 O O   . SER A 1 307 ? -13.423 -49.631 41.017  1.00 89.00  ? 306  SER A O   1 
ATOM   2443 C CB  . SER A 1 307 ? -13.260 -46.880 39.227  1.00 96.71  ? 306  SER A CB  1 
ATOM   2444 O OG  . SER A 1 307 ? -13.840 -47.952 38.496  1.00 109.23 ? 306  SER A OG  1 
ATOM   2445 N N   . ALA A 1 308 ? -11.354 -49.170 40.275  1.00 79.22  ? 307  ALA A N   1 
ATOM   2446 C CA  . ALA A 1 308 ? -11.024 -50.579 40.115  1.00 77.16  ? 307  ALA A CA  1 
ATOM   2447 C C   . ALA A 1 308 ? -10.942 -51.272 41.459  1.00 86.36  ? 307  ALA A C   1 
ATOM   2448 O O   . ALA A 1 308 ? -10.994 -52.492 41.536  1.00 96.56  ? 307  ALA A O   1 
ATOM   2449 C CB  . ALA A 1 308 ? -9.742  -50.751 39.351  1.00 65.05  ? 307  ALA A CB  1 
ATOM   2450 N N   . ARG A 1 309 ? -10.822 -50.487 42.520  1.00 86.07  ? 308  ARG A N   1 
ATOM   2451 C CA  . ARG A 1 309 ? -10.880 -51.047 43.860  1.00 91.73  ? 308  ARG A CA  1 
ATOM   2452 C C   . ARG A 1 309 ? -12.320 -51.223 44.345  1.00 97.33  ? 308  ARG A C   1 
ATOM   2453 O O   . ARG A 1 309 ? -12.618 -52.156 45.087  1.00 96.70  ? 308  ARG A O   1 
ATOM   2454 C CB  . ARG A 1 309 ? -10.059 -50.205 44.834  1.00 88.20  ? 308  ARG A CB  1 
ATOM   2455 C CG  . ARG A 1 309 ? -8.582  -50.420 44.652  1.00 84.82  ? 308  ARG A CG  1 
ATOM   2456 C CD  . ARG A 1 309 ? -7.756  -49.665 45.659  1.00 71.24  ? 308  ARG A CD  1 
ATOM   2457 N NE  . ARG A 1 309 ? -6.525  -50.388 45.947  1.00 82.94  ? 308  ARG A NE  1 
ATOM   2458 C CZ  . ARG A 1 309 ? -6.319  -51.057 47.078  1.00 99.35  ? 308  ARG A CZ  1 
ATOM   2459 N NH1 . ARG A 1 309 ? -7.249  -51.059 48.028  1.00 91.67  ? 308  ARG A NH1 1 
ATOM   2460 N NH2 . ARG A 1 309 ? -5.180  -51.709 47.271  1.00 106.27 ? 308  ARG A NH2 1 
ATOM   2461 N N   . ARG A 1 310 ? -13.215 -50.339 43.913  1.00 104.06 ? 309  ARG A N   1 
ATOM   2462 C CA  . ARG A 1 310 ? -14.616 -50.439 44.309  1.00 110.30 ? 309  ARG A CA  1 
ATOM   2463 C C   . ARG A 1 310 ? -15.339 -51.543 43.546  1.00 113.71 ? 309  ARG A C   1 
ATOM   2464 O O   . ARG A 1 310 ? -16.413 -51.976 43.950  1.00 129.35 ? 309  ARG A O   1 
ATOM   2465 C CB  . ARG A 1 310 ? -15.345 -49.103 44.142  1.00 115.38 ? 309  ARG A CB  1 
ATOM   2466 C CG  . ARG A 1 310 ? -14.962 -48.035 45.159  1.00 123.86 ? 309  ARG A CG  1 
ATOM   2467 C CD  . ARG A 1 310 ? -15.669 -46.720 44.838  1.00 138.45 ? 309  ARG A CD  1 
ATOM   2468 N NE  . ARG A 1 310 ? -15.088 -45.574 45.539  1.00 144.50 ? 309  ARG A NE  1 
ATOM   2469 C CZ  . ARG A 1 310 ? -15.219 -44.310 45.140  1.00 141.59 ? 309  ARG A CZ  1 
ATOM   2470 N NH1 . ARG A 1 310 ? -15.905 -44.028 44.037  1.00 135.42 ? 309  ARG A NH1 1 
ATOM   2471 N NH2 . ARG A 1 310 ? -14.657 -43.327 45.837  1.00 140.48 ? 309  ARG A NH2 1 
ATOM   2472 N N   . LEU A 1 311 ? -14.751 -51.994 42.443  1.00 113.68 ? 310  LEU A N   1 
ATOM   2473 C CA  . LEU A 1 311 ? -15.286 -53.148 41.729  1.00 111.94 ? 310  LEU A CA  1 
ATOM   2474 C C   . LEU A 1 311 ? -15.021 -54.408 42.525  1.00 99.31  ? 310  LEU A C   1 
ATOM   2475 O O   . LEU A 1 311 ? -15.811 -55.339 42.480  1.00 112.23 ? 310  LEU A O   1 
ATOM   2476 C CB  . LEU A 1 311 ? -14.696 -53.273 40.327  1.00 133.99 ? 310  LEU A CB  1 
ATOM   2477 C CG  . LEU A 1 311 ? -15.213 -52.265 39.301  1.00 149.04 ? 310  LEU A CG  1 
ATOM   2478 C CD1 . LEU A 1 311 ? -14.653 -52.587 37.922  1.00 161.62 ? 310  LEU A CD1 1 
ATOM   2479 C CD2 . LEU A 1 311 ? -16.733 -52.252 39.274  1.00 144.38 ? 310  LEU A CD2 1 
ATOM   2480 N N   . GLN A 1 312 ? -13.910 -54.442 43.251  1.00 96.80  ? 311  GLN A N   1 
ATOM   2481 C CA  . GLN A 1 312 ? -13.726 -55.465 44.276  1.00 114.44 ? 311  GLN A CA  1 
ATOM   2482 C C   . GLN A 1 312 ? -14.259 -54.954 45.623  1.00 124.40 ? 311  GLN A C   1 
ATOM   2483 O O   . GLN A 1 312 ? -15.415 -54.536 45.724  1.00 125.07 ? 311  GLN A O   1 
ATOM   2484 C CB  . GLN A 1 312 ? -12.257 -55.864 44.401  1.00 112.64 ? 311  GLN A CB  1 
ATOM   2485 C CG  . GLN A 1 312 ? -11.989 -57.320 44.087  1.00 109.95 ? 311  GLN A CG  1 
ATOM   2486 C CD  . GLN A 1 312 ? -11.289 -57.475 42.767  1.00 105.04 ? 311  GLN A CD  1 
ATOM   2487 O OE1 . GLN A 1 312 ? -11.028 -56.488 42.090  1.00 118.39 ? 311  GLN A OE1 1 
ATOM   2488 N NE2 . GLN A 1 312 ? -10.973 -58.705 42.393  1.00 92.66  ? 311  GLN A NE2 1 
ATOM   2489 N N   . GLY A 1 313 ? -13.415 -54.975 46.649  1.00 125.79 ? 312  GLY A N   1 
ATOM   2490 C CA  . GLY A 1 313 ? -13.802 -54.484 47.957  1.00 128.64 ? 312  GLY A CA  1 
ATOM   2491 C C   . GLY A 1 313 ? -12.599 -54.033 48.756  1.00 138.26 ? 312  GLY A C   1 
ATOM   2492 O O   . GLY A 1 313 ? -12.019 -54.811 49.511  1.00 152.35 ? 312  GLY A O   1 
ATOM   2493 N N   . LEU A 1 314 ? -12.231 -52.766 48.600  1.00 130.33 ? 313  LEU A N   1 
ATOM   2494 C CA  . LEU A 1 314 ? -11.025 -52.236 49.220  1.00 136.12 ? 313  LEU A CA  1 
ATOM   2495 C C   . LEU A 1 314 ? -11.186 -50.714 49.423  1.00 145.04 ? 313  LEU A C   1 
ATOM   2496 O O   . LEU A 1 314 ? -12.301 -50.203 49.322  1.00 152.10 ? 313  LEU A O   1 
ATOM   2497 C CB  . LEU A 1 314 ? -9.820  -52.580 48.330  1.00 138.58 ? 313  LEU A CB  1 
ATOM   2498 C CG  . LEU A 1 314 ? -9.595  -54.059 47.943  1.00 132.93 ? 313  LEU A CG  1 
ATOM   2499 C CD1 . LEU A 1 314 ? -9.111  -54.240 46.506  1.00 122.96 ? 313  LEU A CD1 1 
ATOM   2500 C CD2 . LEU A 1 314 ? -8.632  -54.740 48.908  1.00 138.10 ? 313  LEU A CD2 1 
ATOM   2501 N N   . ARG A 1 315 ? -10.100 -49.998 49.727  1.00 141.79 ? 314  ARG A N   1 
ATOM   2502 C CA  . ARG A 1 315 ? -10.117 -48.522 49.736  1.00 144.54 ? 314  ARG A CA  1 
ATOM   2503 C C   . ARG A 1 315 ? -8.728  -47.886 49.939  1.00 147.73 ? 314  ARG A C   1 
ATOM   2504 O O   . ARG A 1 315 ? -7.941  -48.350 50.761  1.00 153.93 ? 314  ARG A O   1 
ATOM   2505 C CB  . ARG A 1 315 ? -11.105 -47.974 50.768  1.00 152.70 ? 314  ARG A CB  1 
ATOM   2506 C CG  . ARG A 1 315 ? -11.231 -46.450 50.739  1.00 159.51 ? 314  ARG A CG  1 
ATOM   2507 C CD  . ARG A 1 315 ? -12.507 -45.987 50.035  1.00 168.34 ? 314  ARG A CD  1 
ATOM   2508 N NE  . ARG A 1 315 ? -13.711 -46.286 50.815  1.00 180.00 ? 314  ARG A NE  1 
ATOM   2509 C CZ  . ARG A 1 315 ? -14.934 -45.851 50.514  1.00 178.79 ? 314  ARG A CZ  1 
ATOM   2510 N NH1 . ARG A 1 315 ? -15.127 -45.089 49.443  1.00 176.85 ? 314  ARG A NH1 1 
ATOM   2511 N NH2 . ARG A 1 315 ? -15.967 -46.175 51.285  1.00 174.12 ? 314  ARG A NH2 1 
ATOM   2512 N N   . ASP A 1 316 ? -8.446  -46.813 49.200  1.00 143.87 ? 315  ASP A N   1 
ATOM   2513 C CA  . ASP A 1 316 ? -7.094  -46.244 49.119  1.00 145.33 ? 315  ASP A CA  1 
ATOM   2514 C C   . ASP A 1 316 ? -6.721  -45.340 50.284  1.00 147.71 ? 315  ASP A C   1 
ATOM   2515 O O   . ASP A 1 316 ? -6.748  -44.116 50.152  1.00 135.27 ? 315  ASP A O   1 
ATOM   2516 C CB  . ASP A 1 316 ? -6.921  -45.417 47.840  1.00 149.85 ? 315  ASP A CB  1 
ATOM   2517 C CG  . ASP A 1 316 ? -7.240  -46.194 46.581  1.00 153.08 ? 315  ASP A CG  1 
ATOM   2518 O OD1 . ASP A 1 316 ? -8.195  -46.996 46.604  1.00 157.84 ? 315  ASP A OD1 1 
ATOM   2519 O OD2 . ASP A 1 316 ? -6.545  -45.982 45.559  1.00 150.26 ? 315  ASP A OD2 1 
ATOM   2520 N N   . SER A 1 317 ? -6.349  -45.925 51.414  1.00 165.72 ? 316  SER A N   1 
ATOM   2521 C CA  . SER A 1 317 ? -5.878  -45.123 52.538  1.00 179.56 ? 316  SER A CA  1 
ATOM   2522 C C   . SER A 1 317 ? -4.353  -45.046 52.533  1.00 184.01 ? 316  SER A C   1 
ATOM   2523 O O   . SER A 1 317 ? -3.752  -44.287 53.295  1.00 183.76 ? 316  SER A O   1 
ATOM   2524 C CB  . SER A 1 317 ? -6.399  -45.674 53.870  1.00 185.12 ? 316  SER A CB  1 
ATOM   2525 O OG  . SER A 1 317 ? -6.074  -47.044 54.027  1.00 188.10 ? 316  SER A OG  1 
ATOM   2526 N N   . GLN A 1 318 ? -3.736  -45.829 51.653  1.00 186.76 ? 317  GLN A N   1 
ATOM   2527 C CA  . GLN A 1 318 ? -2.284  -45.900 51.576  1.00 190.83 ? 317  GLN A CA  1 
ATOM   2528 C C   . GLN A 1 318 ? -1.747  -45.151 50.370  1.00 190.96 ? 317  GLN A C   1 
ATOM   2529 O O   . GLN A 1 318 ? -1.960  -45.555 49.226  1.00 187.81 ? 317  GLN A O   1 
ATOM   2530 C CB  . GLN A 1 318 ? -1.819  -47.354 51.520  1.00 195.35 ? 317  GLN A CB  1 
ATOM   2531 C CG  . GLN A 1 318 ? -2.263  -48.190 52.703  1.00 201.13 ? 317  GLN A CG  1 
ATOM   2532 C CD  . GLN A 1 318 ? -1.768  -49.617 52.617  1.00 202.05 ? 317  GLN A CD  1 
ATOM   2533 O OE1 . GLN A 1 318 ? -0.960  -49.953 51.751  1.00 200.35 ? 317  GLN A OE1 1 
ATOM   2534 N NE2 . GLN A 1 318 ? -2.249  -50.466 53.517  1.00 203.95 ? 317  GLN A NE2 1 
ATOM   2535 N N   . GLN A 1 319 ? -1.044  -44.059 50.634  1.00 196.63 ? 318  GLN A N   1 
ATOM   2536 C CA  . GLN A 1 319 ? -0.415  -43.292 49.572  1.00 199.08 ? 318  GLN A CA  1 
ATOM   2537 C C   . GLN A 1 319 ? 1.054   -43.040 49.889  1.00 195.75 ? 318  GLN A C   1 
ATOM   2538 O O   . GLN A 1 319 ? 1.396   -42.173 50.691  1.00 192.27 ? 318  GLN A O   1 
ATOM   2539 C CB  . GLN A 1 319 ? -1.168  -41.979 49.331  1.00 203.98 ? 318  GLN A CB  1 
ATOM   2540 C CG  . GLN A 1 319 ? -2.577  -42.182 48.777  1.00 204.97 ? 318  GLN A CG  1 
ATOM   2541 C CD  . GLN A 1 319 ? -3.370  -40.890 48.665  1.00 203.33 ? 318  GLN A CD  1 
ATOM   2542 O OE1 . GLN A 1 319 ? -2.948  -39.840 49.151  1.00 202.72 ? 318  GLN A OE1 1 
ATOM   2543 N NE2 . GLN A 1 319 ? -4.532  -40.966 48.025  1.00 201.24 ? 318  GLN A NE2 1 
ATOM   2544 N N   . GLY A 1 320 ? 1.916   -43.835 49.269  1.00 194.76 ? 319  GLY A N   1 
ATOM   2545 C CA  . GLY A 1 320 ? 3.345   -43.645 49.377  1.00 198.69 ? 319  GLY A CA  1 
ATOM   2546 C C   . GLY A 1 320 ? 3.868   -43.262 48.014  1.00 200.90 ? 319  GLY A C   1 
ATOM   2547 O O   . GLY A 1 320 ? 3.316   -43.679 46.999  1.00 200.81 ? 319  GLY A O   1 
ATOM   2548 N N   . GLU A 1 321 ? 4.921   -42.455 47.990  1.00 213.38 ? 320  GLU A N   1 
ATOM   2549 C CA  . GLU A 1 321 ? 5.532   -42.007 46.740  1.00 220.55 ? 320  GLU A CA  1 
ATOM   2550 C C   . GLU A 1 321 ? 4.499   -41.581 45.689  1.00 213.39 ? 320  GLU A C   1 
ATOM   2551 O O   . GLU A 1 321 ? 4.722   -41.733 44.487  1.00 214.52 ? 320  GLU A O   1 
ATOM   2552 C CB  . GLU A 1 321 ? 6.466   -43.087 46.178  1.00 233.91 ? 320  GLU A CB  1 
ATOM   2553 C CG  . GLU A 1 321 ? 7.585   -43.513 47.132  1.00 247.72 ? 320  GLU A CG  1 
ATOM   2554 C CD  . GLU A 1 321 ? 8.661   -42.449 47.313  1.00 259.37 ? 320  GLU A CD  1 
ATOM   2555 O OE1 . GLU A 1 321 ? 8.642   -41.440 46.577  1.00 262.24 ? 320  GLU A OE1 1 
ATOM   2556 O OE2 . GLU A 1 321 ? 9.532   -42.628 48.191  1.00 265.93 ? 320  GLU A OE2 1 
ATOM   2557 N N   . GLY A 1 322 ? 3.372   -41.050 46.155  1.00 192.89 ? 321  GLY A N   1 
ATOM   2558 C CA  . GLY A 1 322 ? 2.360   -40.494 45.275  1.00 170.11 ? 321  GLY A CA  1 
ATOM   2559 C C   . GLY A 1 322 ? 1.662   -41.518 44.405  1.00 148.23 ? 321  GLY A C   1 
ATOM   2560 O O   . GLY A 1 322 ? 1.066   -42.466 44.908  1.00 145.99 ? 321  GLY A O   1 
ATOM   2561 N N   . GLY A 1 323 ? 1.733   -41.316 43.094  1.00 135.24 ? 322  GLY A N   1 
ATOM   2562 C CA  . GLY A 1 323 ? 1.087   -42.198 42.141  1.00 132.00 ? 322  GLY A CA  1 
ATOM   2563 C C   . GLY A 1 323 ? 1.925   -43.406 41.760  1.00 130.45 ? 322  GLY A C   1 
ATOM   2564 O O   . GLY A 1 323 ? 1.424   -44.349 41.153  1.00 128.14 ? 322  GLY A O   1 
ATOM   2565 N N   . ALA A 1 324 ? 3.208   -43.379 42.105  1.00 128.98 ? 323  ALA A N   1 
ATOM   2566 C CA  . ALA A 1 324 ? 4.073   -44.533 41.882  1.00 121.99 ? 323  ALA A CA  1 
ATOM   2567 C C   . ALA A 1 324 ? 3.691   -45.664 42.839  1.00 118.21 ? 323  ALA A C   1 
ATOM   2568 O O   . ALA A 1 324 ? 3.779   -46.847 42.493  1.00 111.27 ? 323  ALA A O   1 
ATOM   2569 C CB  . ALA A 1 324 ? 5.543   -44.150 42.057  1.00 107.99 ? 323  ALA A CB  1 
ATOM   2570 N N   . GLY A 1 325 ? 3.268   -45.283 44.044  1.00 110.51 ? 324  GLY A N   1 
ATOM   2571 C CA  . GLY A 1 325 ? 2.882   -46.230 45.073  1.00 107.51 ? 324  GLY A CA  1 
ATOM   2572 C C   . GLY A 1 325 ? 1.500   -46.768 44.785  1.00 111.74 ? 324  GLY A C   1 
ATOM   2573 O O   . GLY A 1 325 ? 1.124   -47.851 45.243  1.00 113.36 ? 324  GLY A O   1 
ATOM   2574 N N   . ALA A 1 326 ? 0.740   -45.992 44.022  1.00 107.51 ? 325  ALA A N   1 
ATOM   2575 C CA  . ALA A 1 326 ? -0.553  -46.431 43.536  1.00 97.86  ? 325  ALA A CA  1 
ATOM   2576 C C   . ALA A 1 326 ? -0.316  -47.495 42.469  1.00 103.74 ? 325  ALA A C   1 
ATOM   2577 O O   . ALA A 1 326 ? -1.003  -48.522 42.435  1.00 116.39 ? 325  ALA A O   1 
ATOM   2578 C CB  . ALA A 1 326 ? -1.326  -45.259 42.966  1.00 83.44  ? 325  ALA A CB  1 
ATOM   2579 N N   . LEU A 1 327 ? 0.674   -47.250 41.613  1.00 87.42  ? 326  LEU A N   1 
ATOM   2580 C CA  . LEU A 1 327 ? 1.025   -48.176 40.538  1.00 80.56  ? 326  LEU A CA  1 
ATOM   2581 C C   . LEU A 1 327 ? 1.626   -49.468 41.093  1.00 90.27  ? 326  LEU A C   1 
ATOM   2582 O O   . LEU A 1 327 ? 1.426   -50.548 40.542  1.00 98.28  ? 326  LEU A O   1 
ATOM   2583 C CB  . LEU A 1 327 ? 1.983   -47.511 39.541  1.00 64.28  ? 326  LEU A CB  1 
ATOM   2584 C CG  . LEU A 1 327 ? 2.173   -48.123 38.150  1.00 74.83  ? 326  LEU A CG  1 
ATOM   2585 C CD1 . LEU A 1 327 ? 2.330   -47.023 37.098  1.00 89.37  ? 326  LEU A CD1 1 
ATOM   2586 C CD2 . LEU A 1 327 ? 3.375   -49.070 38.122  1.00 81.14  ? 326  LEU A CD2 1 
ATOM   2587 N N   . LYS A 1 328 ? 2.362   -49.355 42.188  1.00 89.53  ? 327  LYS A N   1 
ATOM   2588 C CA  . LYS A 1 328 ? 2.921   -50.530 42.822  1.00 87.17  ? 327  LYS A CA  1 
ATOM   2589 C C   . LYS A 1 328 ? 1.798   -51.323 43.484  1.00 82.91  ? 327  LYS A C   1 
ATOM   2590 O O   . LYS A 1 328 ? 1.751   -52.542 43.391  1.00 86.73  ? 327  LYS A O   1 
ATOM   2591 C CB  . LYS A 1 328 ? 3.996   -50.126 43.840  1.00 97.37  ? 327  LYS A CB  1 
ATOM   2592 C CG  . LYS A 1 328 ? 4.673   -51.294 44.570  1.00 116.39 ? 327  LYS A CG  1 
ATOM   2593 C CD  . LYS A 1 328 ? 6.196   -51.138 44.643  1.00 123.65 ? 327  LYS A CD  1 
ATOM   2594 C CE  . LYS A 1 328 ? 6.905   -51.901 43.517  1.00 134.59 ? 327  LYS A CE  1 
ATOM   2595 N NZ  . LYS A 1 328 ? 6.536   -51.434 42.144  1.00 138.16 ? 327  LYS A NZ  1 
ATOM   2596 N N   . GLN A 1 329 ? 0.884   -50.621 44.141  1.00 81.83  ? 328  GLN A N   1 
ATOM   2597 C CA  . GLN A 1 329 ? -0.165  -51.273 44.909  1.00 86.50  ? 328  GLN A CA  1 
ATOM   2598 C C   . GLN A 1 329 ? -1.198  -51.883 43.978  1.00 94.27  ? 328  GLN A C   1 
ATOM   2599 O O   . GLN A 1 329 ? -1.868  -52.859 44.322  1.00 98.43  ? 328  GLN A O   1 
ATOM   2600 C CB  . GLN A 1 329 ? -0.838  -50.278 45.856  1.00 87.75  ? 328  GLN A CB  1 
ATOM   2601 C CG  . GLN A 1 329 ? -1.898  -50.885 46.755  1.00 94.65  ? 328  GLN A CG  1 
ATOM   2602 C CD  . GLN A 1 329 ? -2.639  -49.846 47.583  1.00 106.03 ? 328  GLN A CD  1 
ATOM   2603 O OE1 . GLN A 1 329 ? -2.989  -48.776 47.085  1.00 114.82 ? 328  GLN A OE1 1 
ATOM   2604 N NE2 . GLN A 1 329 ? -2.886  -50.163 48.854  1.00 107.16 ? 328  GLN A NE2 1 
ATOM   2605 N N   . MET A 1 330 ? -1.329  -51.307 42.791  1.00 92.58  ? 329  MET A N   1 
ATOM   2606 C CA  . MET A 1 330 ? -2.300  -51.820 41.835  1.00 92.32  ? 329  MET A CA  1 
ATOM   2607 C C   . MET A 1 330 ? -1.789  -53.100 41.173  1.00 84.07  ? 329  MET A C   1 
ATOM   2608 O O   . MET A 1 330 ? -2.531  -54.063 41.031  1.00 82.82  ? 329  MET A O   1 
ATOM   2609 C CB  . MET A 1 330 ? -2.652  -50.760 40.785  1.00 93.25  ? 329  MET A CB  1 
ATOM   2610 C CG  . MET A 1 330 ? -3.919  -51.064 40.000  1.00 92.02  ? 329  MET A CG  1 
ATOM   2611 S SD  . MET A 1 330 ? -5.355  -50.162 40.606  1.00 117.63 ? 329  MET A SD  1 
ATOM   2612 C CE  . MET A 1 330 ? -5.221  -50.416 42.386  1.00 125.51 ? 329  MET A CE  1 
ATOM   2613 N N   . LEU A 1 331 ? -0.520  -53.105 40.774  1.00 80.08  ? 330  LEU A N   1 
ATOM   2614 C CA  . LEU A 1 331 ? 0.096   -54.280 40.165  1.00 76.26  ? 330  LEU A CA  1 
ATOM   2615 C C   . LEU A 1 331 ? 0.214   -55.438 41.155  1.00 89.38  ? 330  LEU A C   1 
ATOM   2616 O O   . LEU A 1 331 ? 0.330   -56.601 40.758  1.00 96.88  ? 330  LEU A O   1 
ATOM   2617 C CB  . LEU A 1 331 ? 1.467   -53.923 39.591  1.00 60.21  ? 330  LEU A CB  1 
ATOM   2618 C CG  . LEU A 1 331 ? 1.364   -53.067 38.322  1.00 73.95  ? 330  LEU A CG  1 
ATOM   2619 C CD1 . LEU A 1 331 ? 2.721   -52.548 37.852  1.00 59.29  ? 330  LEU A CD1 1 
ATOM   2620 C CD2 . LEU A 1 331 ? 0.658   -53.853 37.203  1.00 85.73  ? 330  LEU A CD2 1 
ATOM   2621 N N   . LYS A 1 332 ? 0.185   -55.116 42.443  1.00 83.73  ? 331  LYS A N   1 
ATOM   2622 C CA  . LYS A 1 332 ? 0.236   -56.140 43.469  1.00 86.76  ? 331  LYS A CA  1 
ATOM   2623 C C   . LYS A 1 332 ? -1.164  -56.643 43.805  1.00 96.49  ? 331  LYS A C   1 
ATOM   2624 O O   . LYS A 1 332 ? -1.393  -57.854 43.889  1.00 98.58  ? 331  LYS A O   1 
ATOM   2625 C CB  . LYS A 1 332 ? 0.939   -55.623 44.725  1.00 84.09  ? 331  LYS A CB  1 
ATOM   2626 C CG  . LYS A 1 332 ? 0.888   -56.597 45.906  1.00 103.96 ? 331  LYS A CG  1 
ATOM   2627 C CD  . LYS A 1 332 ? 1.856   -56.216 47.026  1.00 119.46 ? 331  LYS A CD  1 
ATOM   2628 C CE  . LYS A 1 332 ? 1.843   -57.259 48.147  1.00 128.14 ? 331  LYS A CE  1 
ATOM   2629 N NZ  . LYS A 1 332 ? 2.962   -57.071 49.121  1.00 132.30 ? 331  LYS A NZ  1 
ATOM   2630 N N   . ASP A 1 333 ? -2.097  -55.708 43.979  1.00 96.60  ? 332  ASP A N   1 
ATOM   2631 C CA  . ASP A 1 333 ? -3.456  -56.031 44.416  1.00 98.36  ? 332  ASP A CA  1 
ATOM   2632 C C   . ASP A 1 333 ? -4.377  -56.488 43.279  1.00 93.98  ? 332  ASP A C   1 
ATOM   2633 O O   . ASP A 1 333 ? -5.156  -57.428 43.445  1.00 100.69 ? 332  ASP A O   1 
ATOM   2634 C CB  . ASP A 1 333 ? -4.077  -54.853 45.186  1.00 106.55 ? 332  ASP A CB  1 
ATOM   2635 C CG  . ASP A 1 333 ? -3.436  -54.641 46.565  1.00 115.96 ? 332  ASP A CG  1 
ATOM   2636 O OD1 . ASP A 1 333 ? -2.370  -55.243 46.837  1.00 120.64 ? 332  ASP A OD1 1 
ATOM   2637 O OD2 . ASP A 1 333 ? -3.998  -53.872 47.380  1.00 108.11 ? 332  ASP A OD2 1 
ATOM   2638 N N   . LEU A 1 334 ? -4.267  -55.834 42.128  1.00 82.03  ? 333  LEU A N   1 
ATOM   2639 C CA  . LEU A 1 334 ? -5.092  -56.134 40.965  1.00 76.01  ? 333  LEU A CA  1 
ATOM   2640 C C   . LEU A 1 334 ? -4.250  -56.475 39.728  1.00 77.63  ? 333  LEU A C   1 
ATOM   2641 O O   . LEU A 1 334 ? -4.300  -55.763 38.718  1.00 76.05  ? 333  LEU A O   1 
ATOM   2642 C CB  . LEU A 1 334 ? -5.992  -54.936 40.650  1.00 87.81  ? 333  LEU A CB  1 
ATOM   2643 C CG  . LEU A 1 334 ? -7.332  -54.775 41.377  1.00 80.23  ? 333  LEU A CG  1 
ATOM   2644 C CD1 . LEU A 1 334 ? -7.492  -55.812 42.467  1.00 68.72  ? 333  LEU A CD1 1 
ATOM   2645 C CD2 . LEU A 1 334 ? -7.500  -53.355 41.929  1.00 69.62  ? 333  LEU A CD2 1 
ATOM   2646 N N   . PRO A 1 335 ? -3.484  -57.573 39.793  1.00 74.61  ? 334  PRO A N   1 
ATOM   2647 C CA  . PRO A 1 335 ? -2.626  -57.990 38.677  1.00 74.97  ? 334  PRO A CA  1 
ATOM   2648 C C   . PRO A 1 335 ? -3.378  -58.036 37.348  1.00 73.05  ? 334  PRO A C   1 
ATOM   2649 O O   . PRO A 1 335 ? -2.795  -57.760 36.310  1.00 71.00  ? 334  PRO A O   1 
ATOM   2650 C CB  . PRO A 1 335 ? -2.200  -59.404 39.076  1.00 80.54  ? 334  PRO A CB  1 
ATOM   2651 C CG  . PRO A 1 335 ? -2.341  -59.449 40.545  1.00 86.87  ? 334  PRO A CG  1 
ATOM   2652 C CD  . PRO A 1 335 ? -3.489  -58.560 40.885  1.00 82.70  ? 334  PRO A CD  1 
ATOM   2653 N N   . GLN A 1 336 ? -4.650  -58.416 37.394  1.00 77.96  ? 335  GLN A N   1 
ATOM   2654 C CA  . GLN A 1 336 ? -5.550  -58.374 36.242  1.00 71.57  ? 335  GLN A CA  1 
ATOM   2655 C C   . GLN A 1 336 ? -5.350  -57.126 35.380  1.00 73.76  ? 335  GLN A C   1 
ATOM   2656 O O   . GLN A 1 336 ? -5.413  -57.181 34.154  1.00 77.03  ? 335  GLN A O   1 
ATOM   2657 C CB  . GLN A 1 336 ? -6.983  -58.390 36.759  1.00 59.88  ? 335  GLN A CB  1 
ATOM   2658 C CG  . GLN A 1 336 ? -7.023  -58.191 38.261  1.00 65.12  ? 335  GLN A CG  1 
ATOM   2659 C CD  . GLN A 1 336 ? -8.404  -57.934 38.774  1.00 87.14  ? 335  GLN A CD  1 
ATOM   2660 O OE1 . GLN A 1 336 ? -8.653  -58.036 39.972  1.00 91.93  ? 335  GLN A OE1 1 
ATOM   2661 N NE2 . GLN A 1 336 ? -9.326  -57.604 37.870  1.00 97.69  ? 335  GLN A NE2 1 
ATOM   2662 N N   . HIS A 1 337 ? -5.122  -55.992 36.026  1.00 67.36  ? 336  HIS A N   1 
ATOM   2663 C CA  . HIS A 1 337 ? -5.104  -54.734 35.302  1.00 61.59  ? 336  HIS A CA  1 
ATOM   2664 C C   . HIS A 1 337 ? -3.705  -54.295 34.829  1.00 64.58  ? 336  HIS A C   1 
ATOM   2665 O O   . HIS A 1 337 ? -3.525  -53.161 34.408  1.00 53.55  ? 336  HIS A O   1 
ATOM   2666 C CB  . HIS A 1 337 ? -5.758  -53.636 36.142  1.00 55.65  ? 336  HIS A CB  1 
ATOM   2667 C CG  . HIS A 1 337 ? -7.203  -53.884 36.450  1.00 69.84  ? 336  HIS A CG  1 
ATOM   2668 N ND1 . HIS A 1 337 ? -8.119  -54.228 35.484  1.00 75.29  ? 336  HIS A ND1 1 
ATOM   2669 C CD2 . HIS A 1 337 ? -7.887  -53.807 37.618  1.00 67.69  ? 336  HIS A CD2 1 
ATOM   2670 C CE1 . HIS A 1 337 ? -9.311  -54.366 36.045  1.00 77.70  ? 336  HIS A CE1 1 
ATOM   2671 N NE2 . HIS A 1 337 ? -9.196  -54.112 37.334  1.00 77.24  ? 336  HIS A NE2 1 
ATOM   2672 N N   . ARG A 1 338 ? -2.736  -55.203 34.882  1.00 66.68  ? 337  ARG A N   1 
ATOM   2673 C CA  . ARG A 1 338 ? -1.369  -54.921 34.457  1.00 63.39  ? 337  ARG A CA  1 
ATOM   2674 C C   . ARG A 1 338 ? -1.242  -54.129 33.143  1.00 59.65  ? 337  ARG A C   1 
ATOM   2675 O O   . ARG A 1 338 ? -0.362  -53.287 33.015  1.00 72.22  ? 337  ARG A O   1 
ATOM   2676 C CB  . ARG A 1 338 ? -0.564  -56.216 34.347  1.00 64.12  ? 337  ARG A CB  1 
ATOM   2677 C CG  . ARG A 1 338 ? 0.828   -56.015 33.813  1.00 78.55  ? 337  ARG A CG  1 
ATOM   2678 C CD  . ARG A 1 338 ? 1.371   -57.256 33.132  1.00 106.83 ? 337  ARG A CD  1 
ATOM   2679 N NE  . ARG A 1 338 ? 2.389   -56.908 32.139  1.00 127.61 ? 337  ARG A NE  1 
ATOM   2680 C CZ  . ARG A 1 338 ? 2.203   -56.965 30.822  1.00 140.86 ? 337  ARG A CZ  1 
ATOM   2681 N NH1 . ARG A 1 338 ? 1.043   -57.384 30.329  1.00 148.50 ? 337  ARG A NH1 1 
ATOM   2682 N NH2 . ARG A 1 338 ? 3.186   -56.630 29.993  1.00 139.39 ? 337  ARG A NH2 1 
ATOM   2683 N N   . GLU A 1 339 ? -2.105  -54.392 32.172  1.00 64.62  ? 338  GLU A N   1 
ATOM   2684 C CA  . GLU A 1 339 ? -1.987  -53.741 30.869  1.00 67.48  ? 338  GLU A CA  1 
ATOM   2685 C C   . GLU A 1 339 ? -2.536  -52.318 30.833  1.00 68.47  ? 338  GLU A C   1 
ATOM   2686 O O   . GLU A 1 339 ? -1.962  -51.454 30.170  1.00 78.61  ? 338  GLU A O   1 
ATOM   2687 C CB  . GLU A 1 339 ? -2.637  -54.575 29.763  1.00 76.32  ? 338  GLU A CB  1 
ATOM   2688 C CG  . GLU A 1 339 ? -1.738  -55.630 29.168  1.00 93.40  ? 338  GLU A CG  1 
ATOM   2689 C CD  . GLU A 1 339 ? -2.278  -56.176 27.855  1.00 107.52 ? 338  GLU A CD  1 
ATOM   2690 O OE1 . GLU A 1 339 ? -3.318  -55.656 27.379  1.00 112.74 ? 338  GLU A OE1 1 
ATOM   2691 O OE2 . GLU A 1 339 ? -1.656  -57.116 27.301  1.00 103.19 ? 338  GLU A OE2 1 
ATOM   2692 N N   . GLN A 1 340 ? -3.653  -52.079 31.514  1.00 65.89  ? 339  GLN A N   1 
ATOM   2693 C CA  . GLN A 1 340 ? -4.167  -50.722 31.643  1.00 69.06  ? 339  GLN A CA  1 
ATOM   2694 C C   . GLN A 1 340 ? -3.102  -49.883 32.329  1.00 63.62  ? 339  GLN A C   1 
ATOM   2695 O O   . GLN A 1 340 ? -2.891  -48.724 31.996  1.00 75.25  ? 339  GLN A O   1 
ATOM   2696 C CB  . GLN A 1 340 ? -5.475  -50.684 32.443  1.00 68.78  ? 339  GLN A CB  1 
ATOM   2697 C CG  . GLN A 1 340 ? -6.739  -50.631 31.581  1.00 89.62  ? 339  GLN A CG  1 
ATOM   2698 C CD  . GLN A 1 340 ? -6.913  -49.310 30.827  1.00 105.12 ? 339  GLN A CD  1 
ATOM   2699 O OE1 . GLN A 1 340 ? -5.943  -48.682 30.399  1.00 103.08 ? 339  GLN A OE1 1 
ATOM   2700 N NE2 . GLN A 1 340 ? -8.164  -48.897 30.649  1.00 117.32 ? 339  GLN A NE2 1 
ATOM   2701 N N   . MET A 1 341 ? -2.420  -50.504 33.278  1.00 60.79  ? 340  MET A N   1 
ATOM   2702 C CA  . MET A 1 341 ? -1.395  -49.848 34.060  1.00 63.81  ? 340  MET A CA  1 
ATOM   2703 C C   . MET A 1 341 ? -0.227  -49.416 33.197  1.00 64.55  ? 340  MET A C   1 
ATOM   2704 O O   . MET A 1 341 ? 0.231   -48.282 33.296  1.00 68.86  ? 340  MET A O   1 
ATOM   2705 C CB  . MET A 1 341 ? -0.917  -50.768 35.182  1.00 75.76  ? 340  MET A CB  1 
ATOM   2706 C CG  . MET A 1 341 ? -1.222  -50.217 36.549  1.00 86.80  ? 340  MET A CG  1 
ATOM   2707 S SD  . MET A 1 341 ? -2.917  -49.637 36.583  1.00 81.24  ? 340  MET A SD  1 
ATOM   2708 C CE  . MET A 1 341 ? -2.860  -48.545 37.993  1.00 122.10 ? 340  MET A CE  1 
ATOM   2709 N N   . GLN A 1 342 ? 0.261   -50.330 32.367  1.00 65.25  ? 341  GLN A N   1 
ATOM   2710 C CA  . GLN A 1 342 ? 1.324   -50.016 31.435  1.00 64.25  ? 341  GLN A CA  1 
ATOM   2711 C C   . GLN A 1 342 ? 0.869   -48.877 30.536  1.00 62.04  ? 341  GLN A C   1 
ATOM   2712 O O   . GLN A 1 342 ? 1.648   -47.998 30.224  1.00 58.16  ? 341  GLN A O   1 
ATOM   2713 C CB  . GLN A 1 342 ? 1.668   -51.229 30.581  1.00 73.23  ? 341  GLN A CB  1 
ATOM   2714 C CG  . GLN A 1 342 ? 2.447   -52.320 31.278  1.00 81.79  ? 341  GLN A CG  1 
ATOM   2715 C CD  . GLN A 1 342 ? 2.871   -53.411 30.310  1.00 102.58 ? 341  GLN A CD  1 
ATOM   2716 O OE1 . GLN A 1 342 ? 3.977   -53.947 30.409  1.00 118.77 ? 341  GLN A OE1 1 
ATOM   2717 N NE2 . GLN A 1 342 ? 1.998   -53.731 29.349  1.00 99.05  ? 341  GLN A NE2 1 
ATOM   2718 N N   . LYS A 1 343 ? -0.399  -48.889 30.128  1.00 63.24  ? 342  LYS A N   1 
ATOM   2719 C CA  . LYS A 1 343 ? -0.927  -47.836 29.264  1.00 60.59  ? 342  LYS A CA  1 
ATOM   2720 C C   . LYS A 1 343 ? -0.886  -46.456 29.930  1.00 60.13  ? 342  LYS A C   1 
ATOM   2721 O O   . LYS A 1 343 ? -0.512  -45.461 29.305  1.00 69.28  ? 342  LYS A O   1 
ATOM   2722 C CB  . LYS A 1 343 ? -2.338  -48.172 28.774  1.00 65.45  ? 342  LYS A CB  1 
ATOM   2723 C CG  . LYS A 1 343 ? -2.406  -48.364 27.270  1.00 83.84  ? 342  LYS A CG  1 
ATOM   2724 C CD  . LYS A 1 343 ? -3.770  -48.883 26.832  1.00 104.70 ? 342  LYS A CD  1 
ATOM   2725 C CE  . LYS A 1 343 ? -3.802  -50.413 26.718  1.00 109.51 ? 342  LYS A CE  1 
ATOM   2726 N NZ  . LYS A 1 343 ? -3.402  -50.925 25.373  1.00 103.13 ? 342  LYS A NZ  1 
ATOM   2727 N N   . TYR A 1 344 ? -1.257  -46.389 31.200  1.00 50.06  ? 343  TYR A N   1 
ATOM   2728 C CA  . TYR A 1 344 ? -1.196  -45.124 31.908  1.00 48.16  ? 343  TYR A CA  1 
ATOM   2729 C C   . TYR A 1 344 ? 0.236   -44.692 32.199  1.00 60.91  ? 343  TYR A C   1 
ATOM   2730 O O   . TYR A 1 344 ? 0.544   -43.509 32.255  1.00 74.22  ? 343  TYR A O   1 
ATOM   2731 C CB  . TYR A 1 344 ? -1.960  -45.196 33.215  1.00 48.07  ? 343  TYR A CB  1 
ATOM   2732 C CG  . TYR A 1 344 ? -3.454  -45.027 33.088  1.00 65.51  ? 343  TYR A CG  1 
ATOM   2733 C CD1 . TYR A 1 344 ? -4.019  -43.785 32.793  1.00 57.76  ? 343  TYR A CD1 1 
ATOM   2734 C CD2 . TYR A 1 344 ? -4.309  -46.106 33.302  1.00 64.59  ? 343  TYR A CD2 1 
ATOM   2735 C CE1 . TYR A 1 344 ? -5.407  -43.629 32.703  1.00 60.31  ? 343  TYR A CE1 1 
ATOM   2736 C CE2 . TYR A 1 344 ? -5.684  -45.966 33.214  1.00 66.76  ? 343  TYR A CE2 1 
ATOM   2737 C CZ  . TYR A 1 344 ? -6.231  -44.731 32.915  1.00 66.73  ? 343  TYR A CZ  1 
ATOM   2738 O OH  . TYR A 1 344 ? -7.600  -44.622 32.825  1.00 61.90  ? 343  TYR A OH  1 
ATOM   2739 N N   . SER A 1 345 ? 1.119   -45.645 32.423  1.00 63.47  ? 344  SER A N   1 
ATOM   2740 C CA  . SER A 1 345 ? 2.442   -45.261 32.841  1.00 66.06  ? 344  SER A CA  1 
ATOM   2741 C C   . SER A 1 345 ? 3.172   -44.670 31.633  1.00 68.59  ? 344  SER A C   1 
ATOM   2742 O O   . SER A 1 345 ? 3.969   -43.736 31.773  1.00 65.82  ? 344  SER A O   1 
ATOM   2743 C CB  . SER A 1 345 ? 3.175   -46.442 33.481  1.00 55.75  ? 344  SER A CB  1 
ATOM   2744 O OG  . SER A 1 345 ? 3.584   -47.362 32.497  1.00 73.20  ? 344  SER A OG  1 
ATOM   2745 N N   . LEU A 1 346 ? 2.859   -45.198 30.452  1.00 54.08  ? 345  LEU A N   1 
ATOM   2746 C CA  . LEU A 1 346 ? 3.392   -44.681 29.197  1.00 51.67  ? 345  LEU A CA  1 
ATOM   2747 C C   . LEU A 1 346 ? 3.012   -43.217 28.976  1.00 58.88  ? 345  LEU A C   1 
ATOM   2748 O O   . LEU A 1 346 ? 3.880   -42.406 28.675  1.00 68.86  ? 345  LEU A O   1 
ATOM   2749 C CB  . LEU A 1 346 ? 2.949   -45.540 28.005  1.00 45.64  ? 345  LEU A CB  1 
ATOM   2750 C CG  . LEU A 1 346 ? 2.884   -44.852 26.633  1.00 54.35  ? 345  LEU A CG  1 
ATOM   2751 C CD1 . LEU A 1 346 ? 4.265   -44.598 26.076  1.00 44.59  ? 345  LEU A CD1 1 
ATOM   2752 C CD2 . LEU A 1 346 ? 2.065   -45.670 25.629  1.00 50.14  ? 345  LEU A CD2 1 
ATOM   2753 N N   . HIS A 1 347 ? 1.733   -42.872 29.133  1.00 60.27  ? 346  HIS A N   1 
ATOM   2754 C CA  . HIS A 1 347 ? 1.281   -41.479 28.919  1.00 55.31  ? 346  HIS A CA  1 
ATOM   2755 C C   . HIS A 1 347 ? 1.555   -40.510 30.075  1.00 51.86  ? 346  HIS A C   1 
ATOM   2756 O O   . HIS A 1 347 ? 1.725   -39.321 29.848  1.00 62.37  ? 346  HIS A O   1 
ATOM   2757 C CB  . HIS A 1 347 ? -0.183  -41.417 28.477  1.00 48.41  ? 346  HIS A CB  1 
ATOM   2758 C CG  . HIS A 1 347 ? -0.444  -42.155 27.202  1.00 56.97  ? 346  HIS A CG  1 
ATOM   2759 N ND1 . HIS A 1 347 ? -0.123  -41.638 25.965  1.00 60.59  ? 346  HIS A ND1 1 
ATOM   2760 C CD2 . HIS A 1 347 ? -0.961  -43.383 26.972  1.00 48.36  ? 346  HIS A CD2 1 
ATOM   2761 C CE1 . HIS A 1 347 ? -0.447  -42.510 25.027  1.00 57.89  ? 346  HIS A CE1 1 
ATOM   2762 N NE2 . HIS A 1 347 ? -0.946  -43.581 25.612  1.00 53.99  ? 346  HIS A NE2 1 
ATOM   2763 N N   . LEU A 1 348 ? 1.599   -41.011 31.306  1.00 48.95  ? 347  LEU A N   1 
ATOM   2764 C CA  . LEU A 1 348 ? 2.126   -40.240 32.427  1.00 42.31  ? 347  LEU A CA  1 
ATOM   2765 C C   . LEU A 1 348 ? 3.544   -39.777 32.059  1.00 58.29  ? 347  LEU A C   1 
ATOM   2766 O O   . LEU A 1 348 ? 3.888   -38.602 32.175  1.00 68.50  ? 347  LEU A O   1 
ATOM   2767 C CB  . LEU A 1 348 ? 2.188   -41.110 33.673  1.00 43.10  ? 347  LEU A CB  1 
ATOM   2768 C CG  . LEU A 1 348 ? 1.171   -40.943 34.799  1.00 53.28  ? 347  LEU A CG  1 
ATOM   2769 C CD1 . LEU A 1 348 ? 0.003   -40.024 34.433  1.00 46.28  ? 347  LEU A CD1 1 
ATOM   2770 C CD2 . LEU A 1 348 ? 0.700   -42.318 35.252  1.00 46.82  ? 347  LEU A CD2 1 
ATOM   2771 N N   . ASP A 1 349 ? 4.344   -40.728 31.589  1.00 56.49  ? 348  ASP A N   1 
ATOM   2772 C CA  . ASP A 1 349 ? 5.718   -40.502 31.164  1.00 51.64  ? 348  ASP A CA  1 
ATOM   2773 C C   . ASP A 1 349 ? 5.840   -39.555 29.980  1.00 57.06  ? 348  ASP A C   1 
ATOM   2774 O O   . ASP A 1 349 ? 6.618   -38.613 30.017  1.00 65.94  ? 348  ASP A O   1 
ATOM   2775 C CB  . ASP A 1 349 ? 6.347   -41.841 30.766  1.00 55.79  ? 348  ASP A CB  1 
ATOM   2776 C CG  . ASP A 1 349 ? 7.853   -41.797 30.747  1.00 65.89  ? 348  ASP A CG  1 
ATOM   2777 O OD1 . ASP A 1 349 ? 8.457   -42.297 31.728  1.00 69.96  ? 348  ASP A OD1 1 
ATOM   2778 O OD2 . ASP A 1 349 ? 8.429   -41.261 29.764  1.00 68.40  ? 348  ASP A OD2 1 
ATOM   2779 N N   . MET A 1 350 ? 5.096   -39.838 28.917  1.00 62.41  ? 349  MET A N   1 
ATOM   2780 C CA  . MET A 1 350 ? 5.230   -39.085 27.686  1.00 60.21  ? 349  MET A CA  1 
ATOM   2781 C C   . MET A 1 350 ? 4.721   -37.677 27.919  1.00 59.00  ? 349  MET A C   1 
ATOM   2782 O O   . MET A 1 350 ? 5.378   -36.707 27.561  1.00 56.86  ? 349  MET A O   1 
ATOM   2783 C CB  . MET A 1 350 ? 4.483   -39.762 26.541  1.00 54.85  ? 349  MET A CB  1 
ATOM   2784 C CG  . MET A 1 350 ? 5.053   -39.462 25.164  1.00 52.90  ? 349  MET A CG  1 
ATOM   2785 S SD  . MET A 1 350 ? 4.542   -40.670 23.915  1.00 68.12  ? 349  MET A SD  1 
ATOM   2786 C CE  . MET A 1 350 ? 2.971   -39.998 23.402  1.00 53.38  ? 349  MET A CE  1 
ATOM   2787 N N   . SER A 1 351 ? 3.553   -37.577 28.541  1.00 64.66  ? 350  SER A N   1 
ATOM   2788 C CA  . SER A 1 351 ? 3.022   -36.295 28.989  1.00 59.14  ? 350  SER A CA  1 
ATOM   2789 C C   . SER A 1 351 ? 4.084   -35.463 29.713  1.00 57.92  ? 350  SER A C   1 
ATOM   2790 O O   . SER A 1 351 ? 4.345   -34.311 29.368  1.00 48.46  ? 350  SER A O   1 
ATOM   2791 C CB  . SER A 1 351 ? 1.856   -36.530 29.933  1.00 49.12  ? 350  SER A CB  1 
ATOM   2792 O OG  . SER A 1 351 ? 0.682   -36.054 29.331  1.00 77.16  ? 350  SER A OG  1 
ATOM   2793 N N   . ASN A 1 352 ? 4.691   -36.053 30.731  1.00 49.84  ? 351  ASN A N   1 
ATOM   2794 C CA  . ASN A 1 352 ? 5.689   -35.345 31.484  1.00 52.05  ? 351  ASN A CA  1 
ATOM   2795 C C   . ASN A 1 352 ? 6.904   -34.947 30.635  1.00 56.79  ? 351  ASN A C   1 
ATOM   2796 O O   . ASN A 1 352 ? 7.386   -33.809 30.698  1.00 57.43  ? 351  ASN A O   1 
ATOM   2797 C CB  . ASN A 1 352 ? 6.118   -36.153 32.695  1.00 48.29  ? 351  ASN A CB  1 
ATOM   2798 C CG  . ASN A 1 352 ? 6.828   -35.309 33.695  1.00 70.02  ? 351  ASN A CG  1 
ATOM   2799 O OD1 . ASN A 1 352 ? 8.033   -35.451 33.905  1.00 83.71  ? 351  ASN A OD1 1 
ATOM   2800 N ND2 . ASN A 1 352 ? 6.099   -34.369 34.284  1.00 76.56  ? 351  ASN A ND2 1 
ATOM   2801 N N   . ALA A 1 353 ? 7.387   -35.888 29.837  1.00 39.68  ? 352  ALA A N   1 
ATOM   2802 C CA  . ALA A 1 353 ? 8.517   -35.633 28.970  1.00 44.63  ? 352  ALA A CA  1 
ATOM   2803 C C   . ALA A 1 353 ? 8.285   -34.417 28.047  1.00 49.51  ? 352  ALA A C   1 
ATOM   2804 O O   . ALA A 1 353 ? 9.147   -33.555 27.916  1.00 47.99  ? 352  ALA A O   1 
ATOM   2805 C CB  . ALA A 1 353 ? 8.862   -36.888 28.175  1.00 37.85  ? 352  ALA A CB  1 
ATOM   2806 N N   . ILE A 1 354 ? 7.122   -34.356 27.416  1.00 43.83  ? 353  ILE A N   1 
ATOM   2807 C CA  . ILE A 1 354 ? 6.751   -33.196 26.624  1.00 48.16  ? 353  ILE A CA  1 
ATOM   2808 C C   . ILE A 1 354 ? 6.816   -31.917 27.463  1.00 57.15  ? 353  ILE A C   1 
ATOM   2809 O O   . ILE A 1 354 ? 7.442   -30.940 27.058  1.00 60.87  ? 353  ILE A O   1 
ATOM   2810 C CB  . ILE A 1 354 ? 5.341   -33.346 26.000  1.00 44.57  ? 353  ILE A CB  1 
ATOM   2811 C CG1 . ILE A 1 354 ? 5.336   -34.429 24.935  1.00 54.93  ? 353  ILE A CG1 1 
ATOM   2812 C CG2 . ILE A 1 354 ? 4.927   -32.086 25.320  1.00 49.39  ? 353  ILE A CG2 1 
ATOM   2813 C CD1 . ILE A 1 354 ? 3.978   -34.627 24.311  1.00 62.37  ? 353  ILE A CD1 1 
ATOM   2814 N N   . ASN A 1 355 ? 6.177   -31.920 28.628  1.00 53.71  ? 354  ASN A N   1 
ATOM   2815 C CA  . ASN A 1 355 ? 6.170   -30.731 29.474  1.00 54.50  ? 354  ASN A CA  1 
ATOM   2816 C C   . ASN A 1 355 ? 7.581   -30.233 29.782  1.00 58.47  ? 354  ASN A C   1 
ATOM   2817 O O   . ASN A 1 355 ? 7.838   -29.032 29.797  1.00 68.57  ? 354  ASN A O   1 
ATOM   2818 C CB  . ASN A 1 355 ? 5.381   -30.965 30.764  1.00 67.88  ? 354  ASN A CB  1 
ATOM   2819 C CG  . ASN A 1 355 ? 4.038   -30.242 30.764  1.00 89.53  ? 354  ASN A CG  1 
ATOM   2820 O OD1 . ASN A 1 355 ? 3.338   -30.187 29.746  1.00 74.15  ? 354  ASN A OD1 1 
ATOM   2821 N ND2 . ASN A 1 355 ? 3.679   -29.669 31.909  1.00 111.76 ? 354  ASN A ND2 1 
ATOM   2822 N N   . MET A 1 356 ? 8.496   -31.167 30.002  1.00 58.90  ? 355  MET A N   1 
ATOM   2823 C CA  . MET A 1 356 ? 9.870   -30.829 30.319  1.00 60.76  ? 355  MET A CA  1 
ATOM   2824 C C   . MET A 1 356 ? 10.647  -30.332 29.105  1.00 65.50  ? 355  MET A C   1 
ATOM   2825 O O   . MET A 1 356 ? 11.468  -29.426 29.214  1.00 77.35  ? 355  MET A O   1 
ATOM   2826 C CB  . MET A 1 356 ? 10.583  -32.023 30.950  1.00 71.38  ? 355  MET A CB  1 
ATOM   2827 C CG  . MET A 1 356 ? 10.293  -32.203 32.432  1.00 78.23  ? 355  MET A CG  1 
ATOM   2828 S SD  . MET A 1 356 ? 11.310  -33.529 33.103  1.00 144.76 ? 355  MET A SD  1 
ATOM   2829 C CE  . MET A 1 356 ? 10.550  -33.753 34.709  1.00 184.02 ? 355  MET A CE  1 
ATOM   2830 N N   . ALA A 1 357 ? 10.388  -30.928 27.951  1.00 55.22  ? 356  ALA A N   1 
ATOM   2831 C CA  . ALA A 1 357 ? 11.050  -30.518 26.731  1.00 47.83  ? 356  ALA A CA  1 
ATOM   2832 C C   . ALA A 1 357 ? 10.562  -29.134 26.279  1.00 58.54  ? 356  ALA A C   1 
ATOM   2833 O O   . ALA A 1 357 ? 11.248  -28.436 25.540  1.00 59.33  ? 356  ALA A O   1 
ATOM   2834 C CB  . ALA A 1 357 ? 10.847  -31.568 25.626  1.00 26.86  ? 356  ALA A CB  1 
ATOM   2835 N N   . PHE A 1 358 ? 9.373   -28.731 26.714  1.00 56.63  ? 357  PHE A N   1 
ATOM   2836 C CA  . PHE A 1 358 ? 8.891   -27.413 26.335  1.00 58.25  ? 357  PHE A CA  1 
ATOM   2837 C C   . PHE A 1 358 ? 9.468   -26.408 27.288  1.00 59.49  ? 357  PHE A C   1 
ATOM   2838 O O   . PHE A 1 358 ? 8.756   -25.823 28.106  1.00 60.57  ? 357  PHE A O   1 
ATOM   2839 C CB  . PHE A 1 358 ? 7.369   -27.322 26.334  1.00 61.52  ? 357  PHE A CB  1 
ATOM   2840 C CG  . PHE A 1 358 ? 6.836   -26.398 25.295  1.00 58.81  ? 357  PHE A CG  1 
ATOM   2841 C CD1 . PHE A 1 358 ? 6.553   -26.863 24.025  1.00 59.54  ? 357  PHE A CD1 1 
ATOM   2842 C CD2 . PHE A 1 358 ? 6.629   -25.056 25.580  1.00 78.02  ? 357  PHE A CD2 1 
ATOM   2843 C CE1 . PHE A 1 358 ? 6.070   -26.002 23.053  1.00 62.22  ? 357  PHE A CE1 1 
ATOM   2844 C CE2 . PHE A 1 358 ? 6.142   -24.186 24.610  1.00 72.83  ? 357  PHE A CE2 1 
ATOM   2845 C CZ  . PHE A 1 358 ? 5.870   -24.661 23.345  1.00 59.19  ? 357  PHE A CZ  1 
ATOM   2846 N N   . SER A 1 359 ? 10.779  -26.234 27.173  1.00 56.87  ? 358  SER A N   1 
ATOM   2847 C CA  . SER A 1 359 ? 11.535  -25.251 27.940  1.00 56.52  ? 358  SER A CA  1 
ATOM   2848 C C   . SER A 1 359 ? 11.172  -23.814 27.567  1.00 61.37  ? 358  SER A C   1 
ATOM   2849 O O   . SER A 1 359 ? 10.544  -23.557 26.534  1.00 60.28  ? 358  SER A O   1 
ATOM   2850 C CB  . SER A 1 359 ? 13.019  -25.462 27.672  1.00 53.37  ? 358  SER A CB  1 
ATOM   2851 O OG  . SER A 1 359 ? 13.323  -25.226 26.304  1.00 57.14  ? 358  SER A OG  1 
ATOM   2852 N N   . SER A 1 360 ? 11.574  -22.867 28.406  1.00 67.75  ? 359  SER A N   1 
ATOM   2853 C CA  . SER A 1 360 ? 11.473  -21.452 28.035  1.00 68.00  ? 359  SER A CA  1 
ATOM   2854 C C   . SER A 1 360 ? 12.080  -21.189 26.640  1.00 60.68  ? 359  SER A C   1 
ATOM   2855 O O   . SER A 1 360 ? 11.533  -20.415 25.854  1.00 51.02  ? 359  SER A O   1 
ATOM   2856 C CB  . SER A 1 360 ? 12.143  -20.567 29.079  1.00 69.59  ? 359  SER A CB  1 
ATOM   2857 O OG  . SER A 1 360 ? 13.530  -20.855 29.154  1.00 86.19  ? 359  SER A OG  1 
ATOM   2858 N N   . THR A 1 361 ? 13.203  -21.826 26.326  1.00 43.51  ? 360  THR A N   1 
ATOM   2859 C CA  . THR A 1 361 ? 13.752  -21.668 24.992  1.00 50.18  ? 360  THR A CA  1 
ATOM   2860 C C   . THR A 1 361 ? 12.725  -21.975 23.903  1.00 57.18  ? 360  THR A C   1 
ATOM   2861 O O   . THR A 1 361 ? 12.445  -21.129 23.053  1.00 56.55  ? 360  THR A O   1 
ATOM   2862 C CB  . THR A 1 361 ? 14.951  -22.556 24.772  1.00 59.06  ? 360  THR A CB  1 
ATOM   2863 O OG1 . THR A 1 361 ? 15.943  -22.252 25.752  1.00 75.99  ? 360  THR A OG1 1 
ATOM   2864 C CG2 . THR A 1 361 ? 15.505  -22.343 23.375  1.00 50.82  ? 360  THR A CG2 1 
ATOM   2865 N N   . ILE A 1 362 ? 12.186  -23.193 23.925  1.00 49.87  ? 361  ILE A N   1 
ATOM   2866 C CA  . ILE A 1 362 ? 11.208  -23.643 22.933  1.00 55.87  ? 361  ILE A CA  1 
ATOM   2867 C C   . ILE A 1 362 ? 9.976   -22.737 22.864  1.00 56.58  ? 361  ILE A C   1 
ATOM   2868 O O   . ILE A 1 362 ? 9.441   -22.480 21.783  1.00 60.13  ? 361  ILE A O   1 
ATOM   2869 C CB  . ILE A 1 362 ? 10.784  -25.112 23.206  1.00 58.44  ? 361  ILE A CB  1 
ATOM   2870 C CG1 . ILE A 1 362 ? 12.020  -26.013 23.221  1.00 44.30  ? 361  ILE A CG1 1 
ATOM   2871 C CG2 . ILE A 1 362 ? 9.743   -25.595 22.190  1.00 46.47  ? 361  ILE A CG2 1 
ATOM   2872 C CD1 . ILE A 1 362 ? 12.744  -26.099 21.905  1.00 30.14  ? 361  ILE A CD1 1 
ATOM   2873 N N   . ASP A 1 363 ? 9.532   -22.269 24.027  1.00 52.73  ? 362  ASP A N   1 
ATOM   2874 C CA  . ASP A 1 363 ? 8.495   -21.236 24.131  1.00 57.57  ? 362  ASP A CA  1 
ATOM   2875 C C   . ASP A 1 363 ? 8.842   -19.955 23.329  1.00 60.02  ? 362  ASP A C   1 
ATOM   2876 O O   . ASP A 1 363 ? 8.045   -19.501 22.511  1.00 65.19  ? 362  ASP A O   1 
ATOM   2877 C CB  . ASP A 1 363 ? 8.241   -20.931 25.610  1.00 72.15  ? 362  ASP A CB  1 
ATOM   2878 C CG  . ASP A 1 363 ? 6.949   -20.200 25.850  1.00 101.26 ? 362  ASP A CG  1 
ATOM   2879 O OD1 . ASP A 1 363 ? 6.544   -19.400 24.984  1.00 117.29 ? 362  ASP A OD1 1 
ATOM   2880 O OD2 . ASP A 1 363 ? 6.343   -20.415 26.920  1.00 113.74 ? 362  ASP A OD2 1 
ATOM   2881 N N   . SER A 1 364 ? 10.026  -19.382 23.563  1.00 66.41  ? 363  SER A N   1 
ATOM   2882 C CA  . SER A 1 364 ? 10.569  -18.304 22.728  1.00 53.14  ? 363  SER A CA  1 
ATOM   2883 C C   . SER A 1 364 ? 10.462  -18.605 21.229  1.00 62.54  ? 363  SER A C   1 
ATOM   2884 O O   . SER A 1 364 ? 9.941   -17.779 20.481  1.00 67.26  ? 363  SER A O   1 
ATOM   2885 C CB  . SER A 1 364 ? 12.045  -18.066 23.048  1.00 57.78  ? 363  SER A CB  1 
ATOM   2886 O OG  . SER A 1 364 ? 12.226  -17.590 24.365  1.00 74.07  ? 363  SER A OG  1 
ATOM   2887 N N   . CYS A 1 365 ? 10.980  -19.760 20.785  1.00 56.76  ? 364  CYS A N   1 
ATOM   2888 C CA  . CYS A 1 365 ? 10.867  -20.168 19.368  1.00 55.59  ? 364  CYS A CA  1 
ATOM   2889 C C   . CYS A 1 365 ? 9.420   -20.199 18.909  1.00 54.61  ? 364  CYS A C   1 
ATOM   2890 O O   . CYS A 1 365 ? 9.095   -19.740 17.815  1.00 57.53  ? 364  CYS A O   1 
ATOM   2891 C CB  . CYS A 1 365 ? 11.476  -21.551 19.083  1.00 40.18  ? 364  CYS A CB  1 
ATOM   2892 S SG  . CYS A 1 365 ? 13.229  -21.752 19.372  1.00 68.99  ? 364  CYS A SG  1 
ATOM   2893 N N   . THR A 1 366 ? 8.556   -20.757 19.746  1.00 53.97  ? 365  THR A N   1 
ATOM   2894 C CA  . THR A 1 366 ? 7.145   -20.853 19.411  1.00 50.78  ? 365  THR A CA  1 
ATOM   2895 C C   . THR A 1 366 ? 6.470   -19.477 19.280  1.00 54.31  ? 365  THR A C   1 
ATOM   2896 O O   . THR A 1 366 ? 5.780   -19.220 18.295  1.00 55.60  ? 365  THR A O   1 
ATOM   2897 C CB  . THR A 1 366 ? 6.402   -21.786 20.387  1.00 55.89  ? 365  THR A CB  1 
ATOM   2898 O OG1 . THR A 1 366 ? 7.047   -23.067 20.387  1.00 55.50  ? 365  THR A OG1 1 
ATOM   2899 C CG2 . THR A 1 366 ? 4.963   -21.959 19.949  1.00 63.29  ? 365  THR A CG2 1 
ATOM   2900 N N   . LYS A 1 367 ? 6.688   -18.588 20.250  1.00 55.73  ? 366  LYS A N   1 
ATOM   2901 C CA  . LYS A 1 367 ? 6.161   -17.225 20.158  1.00 58.20  ? 366  LYS A CA  1 
ATOM   2902 C C   . LYS A 1 367 ? 6.568   -16.554 18.856  1.00 57.56  ? 366  LYS A C   1 
ATOM   2903 O O   . LYS A 1 367 ? 5.727   -15.979 18.166  1.00 59.20  ? 366  LYS A O   1 
ATOM   2904 C CB  . LYS A 1 367 ? 6.612   -16.369 21.334  1.00 63.99  ? 366  LYS A CB  1 
ATOM   2905 C CG  . LYS A 1 367 ? 6.023   -16.770 22.667  1.00 89.56  ? 366  LYS A CG  1 
ATOM   2906 C CD  . LYS A 1 367 ? 6.605   -15.911 23.778  1.00 111.97 ? 366  LYS A CD  1 
ATOM   2907 C CE  . LYS A 1 367 ? 6.644   -14.436 23.364  1.00 119.64 ? 366  LYS A CE  1 
ATOM   2908 N NZ  . LYS A 1 367 ? 7.721   -13.678 24.081  1.00 120.26 ? 366  LYS A NZ  1 
ATOM   2909 N N   . ALA A 1 368 ? 7.860   -16.638 18.532  1.00 51.18  ? 367  ALA A N   1 
ATOM   2910 C CA  . ALA A 1 368 ? 8.403   -16.071 17.301  1.00 49.13  ? 367  ALA A CA  1 
ATOM   2911 C C   . ALA A 1 368 ? 7.768   -16.707 16.080  1.00 56.51  ? 367  ALA A C   1 
ATOM   2912 O O   . ALA A 1 368 ? 7.366   -16.003 15.154  1.00 59.40  ? 367  ALA A O   1 
ATOM   2913 C CB  . ALA A 1 368 ? 9.924   -16.230 17.249  1.00 49.65  ? 367  ALA A CB  1 
ATOM   2914 N N   . GLU A 1 369 ? 7.691   -18.040 16.083  1.00 49.92  ? 368  GLU A N   1 
ATOM   2915 C CA  . GLU A 1 369 ? 7.047   -18.786 15.004  1.00 50.60  ? 368  GLU A CA  1 
ATOM   2916 C C   . GLU A 1 369 ? 5.583   -18.357 14.783  1.00 62.51  ? 368  GLU A C   1 
ATOM   2917 O O   . GLU A 1 369 ? 5.173   -18.137 13.641  1.00 61.73  ? 368  GLU A O   1 
ATOM   2918 C CB  . GLU A 1 369 ? 7.159   -20.294 15.239  1.00 46.18  ? 368  GLU A CB  1 
ATOM   2919 C CG  . GLU A 1 369 ? 8.551   -20.904 15.013  1.00 56.86  ? 368  GLU A CG  1 
ATOM   2920 C CD  . GLU A 1 369 ? 8.656   -22.356 15.527  1.00 67.51  ? 368  GLU A CD  1 
ATOM   2921 O OE1 . GLU A 1 369 ? 7.607   -22.936 15.879  1.00 58.47  ? 368  GLU A OE1 1 
ATOM   2922 O OE2 . GLU A 1 369 ? 9.782   -22.919 15.577  1.00 84.27  ? 368  GLU A OE2 1 
ATOM   2923 N N   . GLN A 1 370 ? 4.809   -18.224 15.864  1.00 50.37  ? 369  GLN A N   1 
ATOM   2924 C CA  . GLN A 1 370 ? 3.417   -17.790 15.752  1.00 58.03  ? 369  GLN A CA  1 
ATOM   2925 C C   . GLN A 1 370 ? 3.268   -16.377 15.181  1.00 68.01  ? 369  GLN A C   1 
ATOM   2926 O O   . GLN A 1 370 ? 2.408   -16.132 14.333  1.00 63.55  ? 369  GLN A O   1 
ATOM   2927 C CB  . GLN A 1 370 ? 2.693   -17.889 17.099  1.00 59.17  ? 369  GLN A CB  1 
ATOM   2928 C CG  . GLN A 1 370 ? 2.515   -19.312 17.599  1.00 55.43  ? 369  GLN A CG  1 
ATOM   2929 C CD  . GLN A 1 370 ? 1.829   -20.195 16.575  1.00 53.08  ? 369  GLN A CD  1 
ATOM   2930 O OE1 . GLN A 1 370 ? 0.632   -20.063 16.327  1.00 55.12  ? 369  GLN A OE1 1 
ATOM   2931 N NE2 . GLN A 1 370 ? 2.585   -21.087 15.968  1.00 45.60  ? 369  GLN A NE2 1 
ATOM   2932 N N   . ASN A 1 371 ? 4.103   -15.453 15.655  1.00 63.47  ? 370  ASN A N   1 
ATOM   2933 C CA  . ASN A 1 371 ? 4.089   -14.077 15.169  1.00 58.73  ? 370  ASN A CA  1 
ATOM   2934 C C   . ASN A 1 371 ? 4.394   -13.992 13.679  1.00 63.24  ? 370  ASN A C   1 
ATOM   2935 O O   . ASN A 1 371 ? 3.714   -13.303 12.934  1.00 78.41  ? 370  ASN A O   1 
ATOM   2936 C CB  . ASN A 1 371 ? 5.104   -13.227 15.924  1.00 63.54  ? 370  ASN A CB  1 
ATOM   2937 C CG  . ASN A 1 371 ? 4.687   -12.931 17.349  1.00 75.88  ? 370  ASN A CG  1 
ATOM   2938 O OD1 . ASN A 1 371 ? 3.537   -13.159 17.745  1.00 84.43  ? 370  ASN A OD1 1 
ATOM   2939 N ND2 . ASN A 1 371 ? 5.629   -12.407 18.135  1.00 71.16  ? 370  ASN A ND2 1 
ATOM   2940 N N   . ILE A 1 372 ? 5.430   -14.692 13.251  1.00 60.90  ? 371  ILE A N   1 
ATOM   2941 C CA  . ILE A 1 372 ? 5.835   -14.698 11.850  1.00 66.30  ? 371  ILE A CA  1 
ATOM   2942 C C   . ILE A 1 372 ? 4.771   -15.300 10.950  1.00 64.91  ? 371  ILE A C   1 
ATOM   2943 O O   . ILE A 1 372 ? 4.523   -14.833 9.839   1.00 66.83  ? 371  ILE A O   1 
ATOM   2944 C CB  . ILE A 1 372 ? 7.098   -15.535 11.667  1.00 57.97  ? 371  ILE A CB  1 
ATOM   2945 C CG1 . ILE A 1 372 ? 8.257   -14.915 12.426  1.00 53.72  ? 371  ILE A CG1 1 
ATOM   2946 C CG2 . ILE A 1 372 ? 7.418   -15.714 10.199  1.00 52.21  ? 371  ILE A CG2 1 
ATOM   2947 C CD1 . ILE A 1 372 ? 9.413   -15.878 12.576  1.00 64.31  ? 371  ILE A CD1 1 
ATOM   2948 N N   . VAL A 1 373 ? 4.145   -16.351 11.450  1.00 68.10  ? 372  VAL A N   1 
ATOM   2949 C CA  . VAL A 1 373 ? 3.284   -17.194 10.638  1.00 63.75  ? 372  VAL A CA  1 
ATOM   2950 C C   . VAL A 1 373 ? 1.846   -16.643 10.525  1.00 68.96  ? 372  VAL A C   1 
ATOM   2951 O O   . VAL A 1 373 ? 1.201   -16.794 9.487   1.00 74.06  ? 372  VAL A O   1 
ATOM   2952 C CB  . VAL A 1 373 ? 3.391   -18.682 11.132  1.00 48.62  ? 372  VAL A CB  1 
ATOM   2953 C CG1 . VAL A 1 373 ? 2.064   -19.255 11.571  1.00 54.39  ? 372  VAL A CG1 1 
ATOM   2954 C CG2 . VAL A 1 373 ? 4.050   -19.531 10.091  1.00 43.06  ? 372  VAL A CG2 1 
ATOM   2955 N N   . THR A 1 374 ? 1.364   -15.968 11.568  1.00 58.51  ? 373  THR A N   1 
ATOM   2956 C CA  . THR A 1 374 ? 0.052   -15.337 11.513  1.00 53.10  ? 373  THR A CA  1 
ATOM   2957 C C   . THR A 1 374 ? 0.196   -13.861 11.177  1.00 69.47  ? 373  THR A C   1 
ATOM   2958 O O   . THR A 1 374 ? -0.775  -13.183 10.830  1.00 74.72  ? 373  THR A O   1 
ATOM   2959 C CB  . THR A 1 374 ? -0.677  -15.430 12.853  1.00 62.25  ? 373  THR A CB  1 
ATOM   2960 O OG1 . THR A 1 374 ? -0.052  -14.550 13.802  1.00 66.09  ? 373  THR A OG1 1 
ATOM   2961 C CG2 . THR A 1 374 ? -0.669  -16.859 13.368  1.00 63.68  ? 373  THR A CG2 1 
ATOM   2962 N N   . GLU A 1 375 ? 1.417   -13.360 11.304  1.00 70.77  ? 374  GLU A N   1 
ATOM   2963 C CA  . GLU A 1 375 ? 1.721   -11.975 10.960  1.00 74.46  ? 374  GLU A CA  1 
ATOM   2964 C C   . GLU A 1 375 ? 1.062   -10.942 11.902  1.00 86.71  ? 374  GLU A C   1 
ATOM   2965 O O   . GLU A 1 375 ? 0.963   -9.764  11.565  1.00 96.47  ? 374  GLU A O   1 
ATOM   2966 C CB  . GLU A 1 375 ? 1.419   -11.692 9.476   1.00 67.52  ? 374  GLU A CB  1 
ATOM   2967 C CG  . GLU A 1 375 ? 2.209   -12.571 8.487   1.00 83.92  ? 374  GLU A CG  1 
ATOM   2968 C CD  . GLU A 1 375 ? 2.181   -12.075 7.028   1.00 95.74  ? 374  GLU A CD  1 
ATOM   2969 O OE1 . GLU A 1 375 ? 1.570   -11.019 6.745   1.00 99.07  ? 374  GLU A OE1 1 
ATOM   2970 O OE2 . GLU A 1 375 ? 2.784   -12.753 6.160   1.00 97.99  ? 374  GLU A OE2 1 
ATOM   2971 N N   . GLU A 1 376 ? 0.632   -11.385 13.084  1.00 79.94  ? 375  GLU A N   1 
ATOM   2972 C CA  . GLU A 1 376 ? 0.269   -10.469 14.163  1.00 88.00  ? 375  GLU A CA  1 
ATOM   2973 C C   . GLU A 1 376 ? 0.672   -11.092 15.496  1.00 91.86  ? 375  GLU A C   1 
ATOM   2974 O O   . GLU A 1 376 ? 0.988   -12.276 15.540  1.00 93.05  ? 375  GLU A O   1 
ATOM   2975 C CB  . GLU A 1 376 ? -1.226  -10.136 14.136  1.00 99.78  ? 375  GLU A CB  1 
ATOM   2976 C CG  . GLU A 1 376 ? -2.138  -11.286 14.505  1.00 109.03 ? 375  GLU A CG  1 
ATOM   2977 C CD  . GLU A 1 376 ? -3.607  -10.900 14.479  1.00 123.59 ? 375  GLU A CD  1 
ATOM   2978 O OE1 . GLU A 1 376 ? -3.938  -9.873  13.848  1.00 127.99 ? 375  GLU A OE1 1 
ATOM   2979 O OE2 . GLU A 1 376 ? -4.433  -11.625 15.085  1.00 128.68 ? 375  GLU A OE2 1 
ATOM   2980 N N   . GLU A 1 377 ? 0.674   -10.302 16.570  1.00 97.37  ? 376  GLU A N   1 
ATOM   2981 C CA  . GLU A 1 377 ? 1.014   -10.803 17.906  1.00 103.75 ? 376  GLU A CA  1 
ATOM   2982 C C   . GLU A 1 377 ? -0.234  -11.300 18.629  1.00 111.33 ? 376  GLU A C   1 
ATOM   2983 O O   . GLU A 1 377 ? -1.325  -11.265 18.064  1.00 125.77 ? 376  GLU A O   1 
ATOM   2984 C CB  . GLU A 1 377 ? 1.671   -9.702  18.740  1.00 105.84 ? 376  GLU A CB  1 
ATOM   2985 C CG  . GLU A 1 377 ? 2.941   -9.114  18.150  1.00 113.45 ? 376  GLU A CG  1 
ATOM   2986 C CD  . GLU A 1 377 ? 3.493   -7.972  18.992  1.00 130.45 ? 376  GLU A CD  1 
ATOM   2987 O OE1 . GLU A 1 377 ? 3.068   -7.845  20.162  1.00 134.31 ? 376  GLU A OE1 1 
ATOM   2988 O OE2 . GLU A 1 377 ? 4.344   -7.199  18.489  1.00 135.24 ? 376  GLU A OE2 1 
ATOM   2989 N N   . GLN A 1 378 ? -0.086  -11.764 19.872  1.00 100.64 ? 377  GLN A N   1 
ATOM   2990 C CA  . GLN A 1 378 ? -1.259  -12.054 20.698  1.00 95.44  ? 377  GLN A CA  1 
ATOM   2991 C C   . GLN A 1 378 ? -2.170  -10.834 20.670  1.00 104.23 ? 377  GLN A C   1 
ATOM   2992 O O   . GLN A 1 378 ? -3.361  -10.951 20.402  1.00 102.25 ? 377  GLN A O   1 
ATOM   2993 C CB  . GLN A 1 378 ? -0.874  -12.320 22.148  1.00 96.97  ? 377  GLN A CB  1 
ATOM   2994 C CG  . GLN A 1 378 ? 0.384   -13.128 22.336  1.00 115.30 ? 377  GLN A CG  1 
ATOM   2995 C CD  . GLN A 1 378 ? 0.683   -13.386 23.801  1.00 126.97 ? 377  GLN A CD  1 
ATOM   2996 O OE1 . GLN A 1 378 ? -0.030  -12.904 24.689  1.00 125.34 ? 377  GLN A OE1 1 
ATOM   2997 N NE2 . GLN A 1 378 ? 1.739   -14.154 24.064  1.00 130.68 ? 377  GLN A NE2 1 
ATOM   2998 N N   . ASP A 1 379 ? -1.578  -9.670  20.953  1.00 112.87 ? 378  ASP A N   1 
ATOM   2999 C CA  . ASP A 1 379 ? -2.247  -8.363  20.944  1.00 117.55 ? 378  ASP A CA  1 
ATOM   3000 C C   . ASP A 1 379 ? -3.137  -8.152  19.734  1.00 113.91 ? 378  ASP A C   1 
ATOM   3001 O O   . ASP A 1 379 ? -4.292  -7.733  19.853  1.00 120.62 ? 378  ASP A O   1 
ATOM   3002 C CB  . ASP A 1 379 ? -1.211  -7.232  20.944  1.00 125.59 ? 378  ASP A CB  1 
ATOM   3003 C CG  . ASP A 1 379 ? -0.364  -7.212  22.195  1.00 135.19 ? 378  ASP A CG  1 
ATOM   3004 O OD1 . ASP A 1 379 ? 0.348   -8.212  22.444  1.00 138.53 ? 378  ASP A OD1 1 
ATOM   3005 O OD2 . ASP A 1 379 ? -0.407  -6.193  22.924  1.00 131.16 ? 378  ASP A OD2 1 
ATOM   3006 N N   . GLY A 1 380 ? -2.573  -8.425  18.566  1.00 100.13 ? 379  GLY A N   1 
ATOM   3007 C CA  . GLY A 1 380 ? -3.228  -8.138  17.311  1.00 91.25  ? 379  GLY A CA  1 
ATOM   3008 C C   . GLY A 1 380 ? -2.390  -7.132  16.552  1.00 92.11  ? 379  GLY A C   1 
ATOM   3009 O O   . GLY A 1 380 ? -2.675  -6.825  15.394  1.00 85.19  ? 379  GLY A O   1 
ATOM   3010 N N   . ASN A 1 381 ? -1.353  -6.616  17.209  1.00 99.91  ? 380  ASN A N   1 
ATOM   3011 C CA  . ASN A 1 381 ? -0.419  -5.700  16.558  1.00 112.71 ? 380  ASN A CA  1 
ATOM   3012 C C   . ASN A 1 381 ? 0.295   -6.343  15.374  1.00 114.07 ? 380  ASN A C   1 
ATOM   3013 O O   . ASN A 1 381 ? 1.114   -7.241  15.544  1.00 115.41 ? 380  ASN A O   1 
ATOM   3014 C CB  . ASN A 1 381 ? 0.594   -5.147  17.560  1.00 118.41 ? 380  ASN A CB  1 
ATOM   3015 C CG  . ASN A 1 381 ? 0.180   -3.797  18.113  1.00 136.03 ? 380  ASN A CG  1 
ATOM   3016 O OD1 . ASN A 1 381 ? -1.015  -3.506  18.263  1.00 137.33 ? 380  ASN A OD1 1 
ATOM   3017 N ND2 . ASN A 1 381 ? 1.168   -2.957  18.412  1.00 139.88 ? 380  ASN A ND2 1 
ATOM   3018 N N   . LYS A 1 382 ? -0.029  -5.882  14.172  1.00 111.49 ? 381  LYS A N   1 
ATOM   3019 C CA  . LYS A 1 382 ? 0.543   -6.454  12.964  1.00 103.35 ? 381  LYS A CA  1 
ATOM   3020 C C   . LYS A 1 382 ? 2.068   -6.523  13.111  1.00 100.10 ? 381  LYS A C   1 
ATOM   3021 O O   . LYS A 1 382 ? 2.674   -5.617  13.682  1.00 102.08 ? 381  LYS A O   1 
ATOM   3022 C CB  . LYS A 1 382 ? 0.131   -5.622  11.741  1.00 100.41 ? 381  LYS A CB  1 
ATOM   3023 C CG  . LYS A 1 382 ? 0.106   -6.385  10.418  1.00 107.99 ? 381  LYS A CG  1 
ATOM   3024 C CD  . LYS A 1 382 ? -0.057  -5.447  9.223   1.00 118.14 ? 381  LYS A CD  1 
ATOM   3025 C CE  . LYS A 1 382 ? 0.228   -6.165  7.906   1.00 124.11 ? 381  LYS A CE  1 
ATOM   3026 N NZ  . LYS A 1 382 ? 0.410   -5.214  6.767   1.00 130.04 ? 381  LYS A NZ  1 
ATOM   3027 N N   . VAL A 1 383 ? 2.675   -7.612  12.632  1.00 93.24  ? 382  VAL A N   1 
ATOM   3028 C CA  . VAL A 1 383 ? 4.135   -7.757  12.632  1.00 91.62  ? 382  VAL A CA  1 
ATOM   3029 C C   . VAL A 1 383 ? 4.673   -7.625  11.215  1.00 88.59  ? 382  VAL A C   1 
ATOM   3030 O O   . VAL A 1 383 ? 4.177   -8.277  10.292  1.00 89.19  ? 382  VAL A O   1 
ATOM   3031 C CB  . VAL A 1 383 ? 4.623   -9.092  13.288  1.00 75.01  ? 382  VAL A CB  1 
ATOM   3032 C CG1 . VAL A 1 383 ? 3.472   -9.992  13.603  1.00 75.94  ? 382  VAL A CG1 1 
ATOM   3033 C CG2 . VAL A 1 383 ? 5.648   -9.813  12.404  1.00 71.30  ? 382  VAL A CG2 1 
ATOM   3034 N N   . ARG A 1 384 ? 5.680   -6.772  11.052  1.00 87.45  ? 383  ARG A N   1 
ATOM   3035 C CA  . ARG A 1 384 ? 6.157   -6.390  9.722   1.00 98.86  ? 383  ARG A CA  1 
ATOM   3036 C C   . ARG A 1 384 ? 7.641   -6.691  9.544   1.00 93.51  ? 383  ARG A C   1 
ATOM   3037 O O   . ARG A 1 384 ? 8.083   -7.074  8.456   1.00 95.39  ? 383  ARG A O   1 
ATOM   3038 C CB  . ARG A 1 384 ? 5.876   -4.905  9.455   1.00 109.87 ? 383  ARG A CB  1 
ATOM   3039 C CG  . ARG A 1 384 ? 4.393   -4.531  9.414   1.00 124.57 ? 383  ARG A CG  1 
ATOM   3040 C CD  . ARG A 1 384 ? 4.193   -3.012  9.434   1.00 144.17 ? 383  ARG A CD  1 
ATOM   3041 N NE  . ARG A 1 384 ? 4.403   -2.440  10.766  1.00 156.45 ? 383  ARG A NE  1 
ATOM   3042 C CZ  . ARG A 1 384 ? 3.430   -1.984  11.555  1.00 160.06 ? 383  ARG A CZ  1 
ATOM   3043 N NH1 . ARG A 1 384 ? 2.165   -2.016  11.150  1.00 158.39 ? 383  ARG A NH1 1 
ATOM   3044 N NH2 . ARG A 1 384 ? 3.723   -1.486  12.751  1.00 158.67 ? 383  ARG A NH2 1 
ATOM   3045 N N   . ASP A 1 385 ? 8.411   -6.511  10.613  1.00 85.52  ? 384  ASP A N   1 
ATOM   3046 C CA  . ASP A 1 385 ? 9.828   -6.860  10.582  1.00 87.09  ? 384  ASP A CA  1 
ATOM   3047 C C   . ASP A 1 385 ? 10.016  -8.335  10.945  1.00 84.03  ? 384  ASP A C   1 
ATOM   3048 O O   . ASP A 1 385 ? 10.277  -8.682  12.101  1.00 78.60  ? 384  ASP A O   1 
ATOM   3049 C CB  . ASP A 1 385 ? 10.637  -5.963  11.523  1.00 90.35  ? 384  ASP A CB  1 
ATOM   3050 C CG  . ASP A 1 385 ? 12.139  -6.178  11.395  1.00 100.06 ? 384  ASP A CG  1 
ATOM   3051 O OD1 . ASP A 1 385 ? 12.572  -6.891  10.458  1.00 104.18 ? 384  ASP A OD1 1 
ATOM   3052 O OD2 . ASP A 1 385 ? 12.889  -5.633  12.235  1.00 104.58 ? 384  ASP A OD2 1 
ATOM   3053 N N   . PHE A 1 386 ? 9.868   -9.200  9.948   1.00 80.73  ? 385  PHE A N   1 
ATOM   3054 C CA  . PHE A 1 386 ? 10.013  -10.634 10.159  1.00 69.98  ? 385  PHE A CA  1 
ATOM   3055 C C   . PHE A 1 386 ? 11.413  -10.978 10.606  1.00 67.33  ? 385  PHE A C   1 
ATOM   3056 O O   . PHE A 1 386 ? 11.603  -11.835 11.455  1.00 75.57  ? 385  PHE A O   1 
ATOM   3057 C CB  . PHE A 1 386 ? 9.626   -11.413 8.902   1.00 67.89  ? 385  PHE A CB  1 
ATOM   3058 C CG  . PHE A 1 386 ? 8.198   -11.195 8.493   1.00 72.62  ? 385  PHE A CG  1 
ATOM   3059 C CD1 . PHE A 1 386 ? 7.164   -11.666 9.279   1.00 72.80  ? 385  PHE A CD1 1 
ATOM   3060 C CD2 . PHE A 1 386 ? 7.890   -10.495 7.340   1.00 69.79  ? 385  PHE A CD2 1 
ATOM   3061 C CE1 . PHE A 1 386 ? 5.852   -11.446 8.913   1.00 76.33  ? 385  PHE A CE1 1 
ATOM   3062 C CE2 . PHE A 1 386 ? 6.589   -10.275 6.973   1.00 57.28  ? 385  PHE A CE2 1 
ATOM   3063 C CZ  . PHE A 1 386 ? 5.567   -10.751 7.755   1.00 67.48  ? 385  PHE A CZ  1 
ATOM   3064 N N   . ILE A 1 387 ? 12.397  -10.282 10.059  1.00 82.81  ? 386  ILE A N   1 
ATOM   3065 C CA  . ILE A 1 387 ? 13.776  -10.531 10.439  1.00 80.17  ? 386  ILE A CA  1 
ATOM   3066 C C   . ILE A 1 387 ? 14.053  -10.136 11.884  1.00 76.37  ? 386  ILE A C   1 
ATOM   3067 O O   . ILE A 1 387 ? 14.848  -10.775 12.560  1.00 82.95  ? 386  ILE A O   1 
ATOM   3068 C CB  . ILE A 1 387 ? 14.745  -9.855  9.479   1.00 75.83  ? 386  ILE A CB  1 
ATOM   3069 C CG1 . ILE A 1 387 ? 14.452  -10.355 8.062   1.00 78.93  ? 386  ILE A CG1 1 
ATOM   3070 C CG2 . ILE A 1 387 ? 16.173  -10.179 9.867   1.00 78.75  ? 386  ILE A CG2 1 
ATOM   3071 C CD1 . ILE A 1 387 ? 15.646  -10.364 7.145   1.00 81.43  ? 386  ILE A CD1 1 
ATOM   3072 N N   . GLY A 1 388 ? 13.378  -9.100  12.363  1.00 65.17  ? 387  GLY A N   1 
ATOM   3073 C CA  . GLY A 1 388 ? 13.493  -8.713  13.755  1.00 54.51  ? 387  GLY A CA  1 
ATOM   3074 C C   . GLY A 1 388 ? 12.916  -9.743  14.710  1.00 69.76  ? 387  GLY A C   1 
ATOM   3075 O O   . GLY A 1 388 ? 13.452  -9.943  15.805  1.00 87.16  ? 387  GLY A O   1 
ATOM   3076 N N   . GLU A 1 389 ? 11.823  -10.391 14.297  1.00 56.86  ? 388  GLU A N   1 
ATOM   3077 C CA  . GLU A 1 389 ? 11.172  -11.436 15.091  1.00 64.84  ? 388  GLU A CA  1 
ATOM   3078 C C   . GLU A 1 389 ? 12.122  -12.564 15.393  1.00 67.69  ? 388  GLU A C   1 
ATOM   3079 O O   . GLU A 1 389 ? 12.127  -13.138 16.476  1.00 79.38  ? 388  GLU A O   1 
ATOM   3080 C CB  . GLU A 1 389 ? 9.975   -12.017 14.344  1.00 72.92  ? 388  GLU A CB  1 
ATOM   3081 C CG  . GLU A 1 389 ? 8.670   -11.309 14.640  1.00 92.61  ? 388  GLU A CG  1 
ATOM   3082 C CD  . GLU A 1 389 ? 8.372   -11.237 16.125  1.00 99.77  ? 388  GLU A CD  1 
ATOM   3083 O OE1 . GLU A 1 389 ? 8.723   -12.189 16.867  1.00 96.53  ? 388  GLU A OE1 1 
ATOM   3084 O OE2 . GLU A 1 389 ? 7.779   -10.220 16.546  1.00 111.06 ? 388  GLU A OE2 1 
ATOM   3085 N N   . VAL A 1 390 ? 12.926  -12.866 14.393  1.00 64.76  ? 389  VAL A N   1 
ATOM   3086 C CA  . VAL A 1 390 ? 13.833  -13.979 14.414  1.00 54.89  ? 389  VAL A CA  1 
ATOM   3087 C C   . VAL A 1 390 ? 15.093  -13.661 15.211  1.00 57.06  ? 389  VAL A C   1 
ATOM   3088 O O   . VAL A 1 390 ? 15.673  -14.538 15.831  1.00 70.81  ? 389  VAL A O   1 
ATOM   3089 C CB  . VAL A 1 390 ? 14.151  -14.380 12.959  1.00 57.21  ? 389  VAL A CB  1 
ATOM   3090 C CG1 . VAL A 1 390 ? 15.609  -14.793 12.778  1.00 61.01  ? 389  VAL A CG1 1 
ATOM   3091 C CG2 . VAL A 1 390 ? 13.182  -15.455 12.506  1.00 59.70  ? 389  VAL A CG2 1 
ATOM   3092 N N   . ALA A 1 391 ? 15.505  -12.403 15.226  1.00 65.23  ? 390  ALA A N   1 
ATOM   3093 C CA  . ALA A 1 391 ? 16.752  -12.042 15.900  1.00 73.66  ? 390  ALA A CA  1 
ATOM   3094 C C   . ALA A 1 391 ? 16.831  -12.585 17.332  1.00 63.68  ? 390  ALA A C   1 
ATOM   3095 O O   . ALA A 1 391 ? 17.829  -13.190 17.702  1.00 64.66  ? 390  ALA A O   1 
ATOM   3096 C CB  . ALA A 1 391 ? 16.969  -10.534 15.871  1.00 74.84  ? 390  ALA A CB  1 
ATOM   3097 N N   . SER A 1 392 ? 15.779  -12.363 18.120  1.00 54.39  ? 391  SER A N   1 
ATOM   3098 C CA  . SER A 1 392 ? 15.681  -12.883 19.485  1.00 66.27  ? 391  SER A CA  1 
ATOM   3099 C C   . SER A 1 392 ? 16.023  -14.377 19.573  1.00 74.89  ? 391  SER A C   1 
ATOM   3100 O O   . SER A 1 392 ? 16.808  -14.797 20.423  1.00 84.59  ? 391  SER A O   1 
ATOM   3101 C CB  . SER A 1 392 ? 14.264  -12.686 20.017  1.00 78.81  ? 391  SER A CB  1 
ATOM   3102 O OG  . SER A 1 392 ? 13.833  -11.352 19.840  1.00 101.28 ? 391  SER A OG  1 
ATOM   3103 N N   . VAL A 1 393 ? 15.404  -15.176 18.710  1.00 55.16  ? 392  VAL A N   1 
ATOM   3104 C CA  . VAL A 1 393 ? 15.660  -16.600 18.665  1.00 52.79  ? 392  VAL A CA  1 
ATOM   3105 C C   . VAL A 1 393 ? 17.102  -16.893 18.259  1.00 56.82  ? 392  VAL A C   1 
ATOM   3106 O O   . VAL A 1 393 ? 17.831  -17.574 18.966  1.00 66.38  ? 392  VAL A O   1 
ATOM   3107 C CB  . VAL A 1 393 ? 14.667  -17.312 17.704  1.00 44.46  ? 392  VAL A CB  1 
ATOM   3108 C CG1 . VAL A 1 393 ? 15.098  -18.763 17.418  1.00 44.46  ? 392  VAL A CG1 1 
ATOM   3109 C CG2 . VAL A 1 393 ? 13.272  -17.286 18.294  1.00 48.66  ? 392  VAL A CG2 1 
ATOM   3110 N N   . VAL A 1 394 ? 17.501  -16.360 17.118  1.00 58.15  ? 393  VAL A N   1 
ATOM   3111 C CA  . VAL A 1 394 ? 18.795  -16.635 16.513  1.00 63.20  ? 393  VAL A CA  1 
ATOM   3112 C C   . VAL A 1 394 ? 20.074  -16.264 17.312  1.00 65.73  ? 393  VAL A C   1 
ATOM   3113 O O   . VAL A 1 394 ? 21.113  -16.918 17.121  1.00 67.83  ? 393  VAL A O   1 
ATOM   3114 C CB  . VAL A 1 394 ? 18.820  -16.063 15.084  1.00 73.81  ? 393  VAL A CB  1 
ATOM   3115 C CG1 . VAL A 1 394 ? 20.140  -15.402 14.787  1.00 75.52  ? 393  VAL A CG1 1 
ATOM   3116 C CG2 . VAL A 1 394 ? 18.499  -17.172 14.079  1.00 79.98  ? 393  VAL A CG2 1 
ATOM   3117 N N   . VAL A 1 395 ? 20.012  -15.252 18.192  1.00 50.45  ? 394  VAL A N   1 
ATOM   3118 C CA  . VAL A 1 395 ? 21.134  -14.963 19.109  1.00 68.59  ? 394  VAL A CA  1 
ATOM   3119 C C   . VAL A 1 395 ? 21.256  -16.004 20.190  1.00 78.27  ? 394  VAL A C   1 
ATOM   3120 O O   . VAL A 1 395 ? 22.363  -16.417 20.558  1.00 84.43  ? 394  VAL A O   1 
ATOM   3121 C CB  . VAL A 1 395 ? 20.993  -13.637 19.932  1.00 74.46  ? 394  VAL A CB  1 
ATOM   3122 C CG1 . VAL A 1 395 ? 21.826  -12.513 19.343  1.00 77.36  ? 394  VAL A CG1 1 
ATOM   3123 C CG2 . VAL A 1 395 ? 19.544  -13.253 20.167  1.00 67.58  ? 394  VAL A CG2 1 
ATOM   3124 N N   . ASP A 1 396 ? 20.095  -16.355 20.737  1.00 73.90  ? 395  ASP A N   1 
ATOM   3125 C CA  . ASP A 1 396 ? 19.947  -17.332 21.806  1.00 68.86  ? 395  ASP A CA  1 
ATOM   3126 C C   . ASP A 1 396 ? 20.730  -18.595 21.473  1.00 61.12  ? 395  ASP A C   1 
ATOM   3127 O O   . ASP A 1 396 ? 20.417  -19.296 20.511  1.00 70.05  ? 395  ASP A O   1 
ATOM   3128 C CB  . ASP A 1 396 ? 18.465  -17.630 22.009  1.00 72.55  ? 395  ASP A CB  1 
ATOM   3129 C CG  . ASP A 1 396 ? 18.163  -18.178 23.374  1.00 78.51  ? 395  ASP A CG  1 
ATOM   3130 O OD1 . ASP A 1 396 ? 19.105  -18.319 24.183  1.00 74.71  ? 395  ASP A OD1 1 
ATOM   3131 O OD2 . ASP A 1 396 ? 16.971  -18.472 23.629  1.00 87.41  ? 395  ASP A OD2 1 
ATOM   3132 N N   . ARG A 1 397 ? 21.779  -18.850 22.251  1.00 65.75  ? 396  ARG A N   1 
ATOM   3133 C CA  . ARG A 1 397 ? 22.748  -19.885 21.918  1.00 75.30  ? 396  ARG A CA  1 
ATOM   3134 C C   . ARG A 1 397 ? 22.318  -21.200 22.516  1.00 74.07  ? 396  ARG A C   1 
ATOM   3135 O O   . ARG A 1 397 ? 22.890  -22.239 22.219  1.00 78.67  ? 396  ARG A O   1 
ATOM   3136 C CB  . ARG A 1 397 ? 24.156  -19.499 22.372  1.00 74.55  ? 396  ARG A CB  1 
ATOM   3137 C CG  . ARG A 1 397 ? 24.225  -18.856 23.738  1.00 84.79  ? 396  ARG A CG  1 
ATOM   3138 C CD  . ARG A 1 397 ? 25.672  -18.737 24.172  1.00 100.45 ? 396  ARG A CD  1 
ATOM   3139 N NE  . ARG A 1 397 ? 26.513  -18.326 23.052  1.00 112.39 ? 396  ARG A NE  1 
ATOM   3140 C CZ  . ARG A 1 397 ? 27.637  -18.934 22.689  1.00 115.36 ? 396  ARG A CZ  1 
ATOM   3141 N NH1 . ARG A 1 397 ? 28.078  -19.989 23.370  1.00 108.04 ? 396  ARG A NH1 1 
ATOM   3142 N NH2 . ARG A 1 397 ? 28.319  -18.478 21.645  1.00 116.75 ? 396  ARG A NH2 1 
ATOM   3143 N N   . ARG A 1 398 ? 21.291  -21.133 23.356  1.00 73.60  ? 397  ARG A N   1 
ATOM   3144 C CA  . ARG A 1 398 ? 20.594  -22.315 23.848  1.00 65.69  ? 397  ARG A CA  1 
ATOM   3145 C C   . ARG A 1 398 ? 19.725  -22.967 22.765  1.00 67.56  ? 397  ARG A C   1 
ATOM   3146 O O   . ARG A 1 398 ? 19.147  -24.026 23.003  1.00 81.96  ? 397  ARG A O   1 
ATOM   3147 C CB  . ARG A 1 398 ? 19.702  -21.946 25.039  1.00 66.33  ? 397  ARG A CB  1 
ATOM   3148 C CG  . ARG A 1 398 ? 20.458  -21.586 26.306  1.00 78.24  ? 397  ARG A CG  1 
ATOM   3149 C CD  . ARG A 1 398 ? 19.758  -20.446 27.057  1.00 96.97  ? 397  ARG A CD  1 
ATOM   3150 N NE  . ARG A 1 398 ? 18.731  -20.909 27.989  1.00 106.43 ? 397  ARG A NE  1 
ATOM   3151 C CZ  . ARG A 1 398 ? 18.951  -21.176 29.276  1.00 115.72 ? 397  ARG A CZ  1 
ATOM   3152 N NH1 . ARG A 1 398 ? 20.169  -21.032 29.794  1.00 116.27 ? 397  ARG A NH1 1 
ATOM   3153 N NH2 . ARG A 1 398 ? 17.955  -21.593 30.049  1.00 117.62 ? 397  ARG A NH2 1 
ATOM   3154 N N   . VAL A 1 399 ? 19.636  -22.350 21.586  1.00 54.59  ? 398  VAL A N   1 
ATOM   3155 C CA  . VAL A 1 399 ? 18.706  -22.802 20.556  1.00 53.34  ? 398  VAL A CA  1 
ATOM   3156 C C   . VAL A 1 399 ? 19.336  -23.703 19.508  1.00 53.05  ? 398  VAL A C   1 
ATOM   3157 O O   . VAL A 1 399 ? 20.306  -23.352 18.869  1.00 65.63  ? 398  VAL A O   1 
ATOM   3158 C CB  . VAL A 1 399 ? 18.002  -21.637 19.848  1.00 61.08  ? 398  VAL A CB  1 
ATOM   3159 C CG1 . VAL A 1 399 ? 17.211  -22.146 18.634  1.00 49.09  ? 398  VAL A CG1 1 
ATOM   3160 C CG2 . VAL A 1 399 ? 17.102  -20.890 20.822  1.00 51.56  ? 398  VAL A CG2 1 
ATOM   3161 N N   . SER A 1 400 ? 18.757  -24.881 19.353  1.00 61.93  ? 399  SER A N   1 
ATOM   3162 C CA  . SER A 1 400 ? 19.193  -25.863 18.378  1.00 53.88  ? 399  SER A CA  1 
ATOM   3163 C C   . SER A 1 400 ? 19.430  -25.228 17.020  1.00 57.33  ? 399  SER A C   1 
ATOM   3164 O O   . SER A 1 400 ? 18.758  -24.266 16.645  1.00 49.81  ? 399  SER A O   1 
ATOM   3165 C CB  . SER A 1 400 ? 18.107  -26.933 18.243  1.00 35.40  ? 399  SER A CB  1 
ATOM   3166 O OG  . SER A 1 400 ? 18.009  -27.410 16.913  1.00 72.01  ? 399  SER A OG  1 
ATOM   3167 N N   . THR A 1 401 ? 20.375  -25.784 16.272  1.00 49.78  ? 400  THR A N   1 
ATOM   3168 C CA  . THR A 1 401 ? 20.527  -25.398 14.883  1.00 55.78  ? 400  THR A CA  1 
ATOM   3169 C C   . THR A 1 401 ? 19.218  -25.627 14.128  1.00 55.95  ? 400  THR A C   1 
ATOM   3170 O O   . THR A 1 401 ? 18.696  -24.722 13.478  1.00 60.63  ? 400  THR A O   1 
ATOM   3171 C CB  . THR A 1 401 ? 21.701  -26.142 14.216  1.00 58.01  ? 400  THR A CB  1 
ATOM   3172 O OG1 . THR A 1 401 ? 22.892  -25.355 14.365  1.00 59.48  ? 400  THR A OG1 1 
ATOM   3173 C CG2 . THR A 1 401 ? 21.419  -26.379 12.724  1.00 46.41  ? 400  THR A CG2 1 
ATOM   3174 N N   . GLU A 1 402 ? 18.686  -26.839 14.235  1.00 55.96  ? 401  GLU A N   1 
ATOM   3175 C CA  . GLU A 1 402 ? 17.399  -27.184 13.643  1.00 55.37  ? 401  GLU A CA  1 
ATOM   3176 C C   . GLU A 1 402 ? 16.283  -26.192 14.027  1.00 54.96  ? 401  GLU A C   1 
ATOM   3177 O O   . GLU A 1 402 ? 15.490  -25.776 13.185  1.00 55.91  ? 401  GLU A O   1 
ATOM   3178 C CB  . GLU A 1 402 ? 17.024  -28.612 14.035  1.00 60.89  ? 401  GLU A CB  1 
ATOM   3179 C CG  . GLU A 1 402 ? 15.636  -29.061 13.573  1.00 81.49  ? 401  GLU A CG  1 
ATOM   3180 C CD  . GLU A 1 402 ? 14.940  -29.941 14.601  1.00 96.93  ? 401  GLU A CD  1 
ATOM   3181 O OE1 . GLU A 1 402 ? 15.363  -31.105 14.782  1.00 106.43 ? 401  GLU A OE1 1 
ATOM   3182 O OE2 . GLU A 1 402 ? 13.972  -29.468 15.232  1.00 95.55  ? 401  GLU A OE2 1 
ATOM   3183 N N   . ASP A 1 403 ? 16.217  -25.795 15.291  1.00 52.43  ? 402  ASP A N   1 
ATOM   3184 C CA  . ASP A 1 403 ? 15.214  -24.806 15.673  1.00 60.62  ? 402  ASP A CA  1 
ATOM   3185 C C   . ASP A 1 403 ? 15.434  -23.455 14.992  1.00 54.91  ? 402  ASP A C   1 
ATOM   3186 O O   . ASP A 1 403 ? 14.489  -22.858 14.480  1.00 49.50  ? 402  ASP A O   1 
ATOM   3187 C CB  . ASP A 1 403 ? 15.119  -24.658 17.187  1.00 66.95  ? 402  ASP A CB  1 
ATOM   3188 C CG  . ASP A 1 403 ? 14.490  -25.866 17.839  1.00 79.47  ? 402  ASP A CG  1 
ATOM   3189 O OD1 . ASP A 1 403 ? 13.681  -26.553 17.168  1.00 63.73  ? 402  ASP A OD1 1 
ATOM   3190 O OD2 . ASP A 1 403 ? 14.809  -26.127 19.019  1.00 96.93  ? 402  ASP A OD2 1 
ATOM   3191 N N   . LYS A 1 404 ? 16.679  -22.989 14.973  1.00 52.44  ? 403  LYS A N   1 
ATOM   3192 C CA  . LYS A 1 404 ? 17.007  -21.767 14.265  1.00 43.55  ? 403  LYS A CA  1 
ATOM   3193 C C   . LYS A 1 404 ? 16.592  -21.909 12.802  1.00 51.36  ? 403  LYS A C   1 
ATOM   3194 O O   . LYS A 1 404 ? 15.873  -21.063 12.272  1.00 49.33  ? 403  LYS A O   1 
ATOM   3195 C CB  . LYS A 1 404 ? 18.495  -21.451 14.380  1.00 47.91  ? 403  LYS A CB  1 
ATOM   3196 C CG  . LYS A 1 404 ? 18.955  -20.956 15.738  1.00 47.29  ? 403  LYS A CG  1 
ATOM   3197 C CD  . LYS A 1 404 ? 20.472  -20.881 15.801  1.00 62.69  ? 403  LYS A CD  1 
ATOM   3198 C CE  . LYS A 1 404 ? 20.941  -20.301 17.137  1.00 87.89  ? 403  LYS A CE  1 
ATOM   3199 N NZ  . LYS A 1 404 ? 22.314  -20.781 17.510  1.00 101.20 ? 403  LYS A NZ  1 
ATOM   3200 N N   . LEU A 1 405 ? 17.025  -22.981 12.147  1.00 45.92  ? 404  LEU A N   1 
ATOM   3201 C CA  . LEU A 1 405 ? 16.567  -23.241 10.782  1.00 56.95  ? 404  LEU A CA  1 
ATOM   3202 C C   . LEU A 1 405 ? 15.058  -23.097 10.588  1.00 59.20  ? 404  LEU A C   1 
ATOM   3203 O O   . LEU A 1 405 ? 14.608  -22.443 9.642   1.00 58.62  ? 404  LEU A O   1 
ATOM   3204 C CB  . LEU A 1 405 ? 17.013  -24.617 10.315  1.00 58.55  ? 404  LEU A CB  1 
ATOM   3205 C CG  . LEU A 1 405 ? 18.380  -24.546 9.655   1.00 65.57  ? 404  LEU A CG  1 
ATOM   3206 C CD1 . LEU A 1 405 ? 18.875  -25.938 9.336   1.00 52.16  ? 404  LEU A CD1 1 
ATOM   3207 C CD2 . LEU A 1 405 ? 18.292  -23.663 8.411   1.00 56.06  ? 404  LEU A CD2 1 
ATOM   3208 N N   . ARG A 1 406 ? 14.279  -23.703 11.481  1.00 51.70  ? 405  ARG A N   1 
ATOM   3209 C CA  . ARG A 1 406 ? 12.820  -23.640 11.367  1.00 52.48  ? 405  ARG A CA  1 
ATOM   3210 C C   . ARG A 1 406 ? 12.287  -22.209 11.387  1.00 53.29  ? 405  ARG A C   1 
ATOM   3211 O O   . ARG A 1 406 ? 11.486  -21.819 10.541  1.00 63.03  ? 405  ARG A O   1 
ATOM   3212 C CB  . ARG A 1 406 ? 12.156  -24.474 12.450  1.00 58.76  ? 405  ARG A CB  1 
ATOM   3213 C CG  . ARG A 1 406 ? 12.370  -25.981 12.300  1.00 53.09  ? 405  ARG A CG  1 
ATOM   3214 C CD  . ARG A 1 406 ? 11.213  -26.677 12.910  1.00 52.48  ? 405  ARG A CD  1 
ATOM   3215 N NE  . ARG A 1 406 ? 11.566  -27.428 14.099  1.00 59.98  ? 405  ARG A NE  1 
ATOM   3216 C CZ  . ARG A 1 406 ? 10.676  -27.842 14.994  1.00 63.30  ? 405  ARG A CZ  1 
ATOM   3217 N NH1 . ARG A 1 406 ? 9.394   -27.539 14.844  1.00 39.53  ? 405  ARG A NH1 1 
ATOM   3218 N NH2 . ARG A 1 406 ? 11.073  -28.547 16.047  1.00 82.38  ? 405  ARG A NH2 1 
ATOM   3219 N N   . CYS A 1 407 ? 12.744  -21.426 12.350  1.00 46.19  ? 406  CYS A N   1 
ATOM   3220 C CA  . CYS A 1 407 ? 12.400  -20.011 12.392  1.00 59.04  ? 406  CYS A CA  1 
ATOM   3221 C C   . CYS A 1 407 ? 12.885  -19.242 11.157  1.00 59.24  ? 406  CYS A C   1 
ATOM   3222 O O   . CYS A 1 407 ? 12.142  -18.442 10.599  1.00 53.31  ? 406  CYS A O   1 
ATOM   3223 C CB  . CYS A 1 407 ? 12.899  -19.357 13.688  1.00 57.46  ? 406  CYS A CB  1 
ATOM   3224 S SG  . CYS A 1 407 ? 11.938  -19.818 15.145  1.00 82.36  ? 406  CYS A SG  1 
ATOM   3225 N N   . LEU A 1 408 ? 14.120  -19.482 10.729  1.00 59.87  ? 407  LEU A N   1 
ATOM   3226 C CA  . LEU A 1 408 ? 14.635  -18.811 9.542   1.00 51.75  ? 407  LEU A CA  1 
ATOM   3227 C C   . LEU A 1 408 ? 13.793  -19.139 8.311   1.00 65.26  ? 407  LEU A C   1 
ATOM   3228 O O   . LEU A 1 408 ? 13.509  -18.252 7.504   1.00 64.74  ? 407  LEU A O   1 
ATOM   3229 C CB  . LEU A 1 408 ? 16.082  -19.206 9.270   1.00 42.84  ? 407  LEU A CB  1 
ATOM   3230 C CG  . LEU A 1 408 ? 17.223  -18.353 9.821   1.00 50.03  ? 407  LEU A CG  1 
ATOM   3231 C CD1 . LEU A 1 408 ? 16.754  -17.103 10.557  1.00 47.48  ? 407  LEU A CD1 1 
ATOM   3232 C CD2 . LEU A 1 408 ? 18.074  -19.212 10.712  1.00 54.58  ? 407  LEU A CD2 1 
ATOM   3233 N N   . MET A 1 409 ? 13.412  -20.411 8.161   1.00 56.66  ? 408  MET A N   1 
ATOM   3234 C CA  . MET A 1 409 ? 12.658  -20.856 6.987   1.00 43.98  ? 408  MET A CA  1 
ATOM   3235 C C   . MET A 1 409 ? 11.287  -20.192 6.962   1.00 52.57  ? 408  MET A C   1 
ATOM   3236 O O   . MET A 1 409 ? 10.784  -19.787 5.919   1.00 60.25  ? 408  MET A O   1 
ATOM   3237 C CB  . MET A 1 409 ? 12.509  -22.384 6.981   1.00 45.02  ? 408  MET A CB  1 
ATOM   3238 C CG  . MET A 1 409 ? 13.798  -23.148 6.759   1.00 45.89  ? 408  MET A CG  1 
ATOM   3239 S SD  . MET A 1 409 ? 13.742  -24.939 7.082   1.00 63.38  ? 408  MET A SD  1 
ATOM   3240 C CE  . MET A 1 409 ? 12.704  -25.540 5.762   1.00 58.37  ? 408  MET A CE  1 
ATOM   3241 N N   . LEU A 1 410 ? 10.674  -20.106 8.129   1.00 53.00  ? 409  LEU A N   1 
ATOM   3242 C CA  . LEU A 1 410 ? 9.387   -19.477 8.240   1.00 46.76  ? 409  LEU A CA  1 
ATOM   3243 C C   . LEU A 1 410 ? 9.536   -18.009 7.860   1.00 61.61  ? 409  LEU A C   1 
ATOM   3244 O O   . LEU A 1 410 ? 8.702   -17.445 7.151   1.00 71.74  ? 409  LEU A O   1 
ATOM   3245 C CB  . LEU A 1 410 ? 8.887   -19.607 9.666   1.00 39.93  ? 409  LEU A CB  1 
ATOM   3246 C CG  . LEU A 1 410 ? 7.798   -20.646 9.919   1.00 50.66  ? 409  LEU A CG  1 
ATOM   3247 C CD1 . LEU A 1 410 ? 7.456   -21.441 8.670   1.00 48.83  ? 409  LEU A CD1 1 
ATOM   3248 C CD2 . LEU A 1 410 ? 8.224   -21.541 11.054  1.00 47.43  ? 409  LEU A CD2 1 
ATOM   3249 N N   . CYS A 1 411 ? 10.618  -17.402 8.333   1.00 62.81  ? 410  CYS A N   1 
ATOM   3250 C CA  . CYS A 1 411 ? 10.946  -16.014 8.027   1.00 64.88  ? 410  CYS A CA  1 
ATOM   3251 C C   . CYS A 1 411 ? 11.032  -15.691 6.521   1.00 64.01  ? 410  CYS A C   1 
ATOM   3252 O O   . CYS A 1 411 ? 10.441  -14.715 6.076   1.00 62.31  ? 410  CYS A O   1 
ATOM   3253 C CB  . CYS A 1 411 ? 12.244  -15.631 8.732   1.00 69.55  ? 410  CYS A CB  1 
ATOM   3254 S SG  . CYS A 1 411 ? 12.596  -13.889 8.793   1.00 77.87  ? 410  CYS A SG  1 
ATOM   3255 N N   . VAL A 1 412 ? 11.745  -16.495 5.730   1.00 56.20  ? 411  VAL A N   1 
ATOM   3256 C CA  . VAL A 1 412 ? 11.850  -16.193 4.301   1.00 59.18  ? 411  VAL A CA  1 
ATOM   3257 C C   . VAL A 1 412 ? 10.565  -16.517 3.539   1.00 63.34  ? 411  VAL A C   1 
ATOM   3258 O O   . VAL A 1 412 ? 10.308  -15.965 2.470   1.00 82.87  ? 411  VAL A O   1 
ATOM   3259 C CB  . VAL A 1 412 ? 13.120  -16.817 3.593   1.00 58.50  ? 411  VAL A CB  1 
ATOM   3260 C CG1 . VAL A 1 412 ? 14.325  -16.840 4.518   1.00 52.08  ? 411  VAL A CG1 1 
ATOM   3261 C CG2 . VAL A 1 412 ? 12.844  -18.184 3.059   1.00 52.83  ? 411  VAL A CG2 1 
ATOM   3262 N N   . LEU A 1 413 ? 9.760   -17.415 4.090   1.00 60.93  ? 412  LEU A N   1 
ATOM   3263 C CA  . LEU A 1 413 ? 8.444   -17.706 3.530   1.00 63.86  ? 412  LEU A CA  1 
ATOM   3264 C C   . LEU A 1 413 ? 7.518   -16.489 3.646   1.00 76.67  ? 412  LEU A C   1 
ATOM   3265 O O   . LEU A 1 413 ? 6.776   -16.169 2.718   1.00 88.17  ? 412  LEU A O   1 
ATOM   3266 C CB  . LEU A 1 413 ? 7.835   -18.889 4.261   1.00 67.92  ? 412  LEU A CB  1 
ATOM   3267 C CG  . LEU A 1 413 ? 7.800   -20.251 3.563   1.00 63.27  ? 412  LEU A CG  1 
ATOM   3268 C CD1 . LEU A 1 413 ? 8.792   -20.333 2.414   1.00 47.07  ? 412  LEU A CD1 1 
ATOM   3269 C CD2 . LEU A 1 413 ? 7.997   -21.360 4.594   1.00 45.04  ? 412  LEU A CD2 1 
ATOM   3270 N N   . ALA A 1 414 ? 7.581   -15.817 4.792   1.00 69.34  ? 413  ALA A N   1 
ATOM   3271 C CA  . ALA A 1 414 ? 6.799   -14.615 5.056   1.00 63.98  ? 413  ALA A CA  1 
ATOM   3272 C C   . ALA A 1 414 ? 7.251   -13.429 4.210   1.00 74.90  ? 413  ALA A C   1 
ATOM   3273 O O   . ALA A 1 414 ? 6.446   -12.818 3.505   1.00 78.30  ? 413  ALA A O   1 
ATOM   3274 C CB  . ALA A 1 414 ? 6.885   -14.260 6.523   1.00 60.00  ? 413  ALA A CB  1 
ATOM   3275 N N   . LYS A 1 415 ? 8.537   -13.100 4.304   1.00 73.38  ? 414  LYS A N   1 
ATOM   3276 C CA  . LYS A 1 415 ? 9.142   -12.030 3.515   1.00 67.65  ? 414  LYS A CA  1 
ATOM   3277 C C   . LYS A 1 415 ? 8.862   -12.154 2.021   1.00 80.47  ? 414  LYS A C   1 
ATOM   3278 O O   . LYS A 1 415 ? 8.742   -11.153 1.325   1.00 98.50  ? 414  LYS A O   1 
ATOM   3279 C CB  . LYS A 1 415 ? 10.649  -11.997 3.730   1.00 63.73  ? 414  LYS A CB  1 
ATOM   3280 C CG  . LYS A 1 415 ? 11.080  -11.428 5.069   1.00 63.40  ? 414  LYS A CG  1 
ATOM   3281 C CD  . LYS A 1 415 ? 12.546  -11.020 5.025   1.00 64.23  ? 414  LYS A CD  1 
ATOM   3282 C CE  . LYS A 1 415 ? 12.744  -9.829  4.071   1.00 71.42  ? 414  LYS A CE  1 
ATOM   3283 N NZ  . LYS A 1 415 ? 11.915  -8.641  4.472   1.00 82.25  ? 414  LYS A NZ  1 
ATOM   3284 N N   . ASN A 1 416 ? 8.776   -13.378 1.524   1.00 87.10  ? 415  ASN A N   1 
ATOM   3285 C CA  . ASN A 1 416 ? 8.445   -13.584 0.127   1.00 93.25  ? 415  ASN A CA  1 
ATOM   3286 C C   . ASN A 1 416 ? 9.377   -12.777 -0.780  1.00 92.78  ? 415  ASN A C   1 
ATOM   3287 O O   . ASN A 1 416 ? 8.933   -12.121 -1.717  1.00 100.45 ? 415  ASN A O   1 
ATOM   3288 C CB  . ASN A 1 416 ? 6.985   -13.190 -0.101  1.00 108.71 ? 415  ASN A CB  1 
ATOM   3289 C CG  . ASN A 1 416 ? 6.559   -13.317 -1.546  1.00 121.16 ? 415  ASN A CG  1 
ATOM   3290 O OD1 . ASN A 1 416 ? 7.071   -14.157 -2.288  1.00 128.72 ? 415  ASN A OD1 1 
ATOM   3291 N ND2 . ASN A 1 416 ? 5.614   -12.475 -1.957  1.00 120.00 ? 415  ASN A ND2 1 
ATOM   3292 N N   . GLY A 1 417 ? 10.675  -12.822 -0.495  1.00 85.84  ? 416  GLY A N   1 
ATOM   3293 C CA  . GLY A 1 417 ? 11.640  -12.047 -1.256  1.00 79.82  ? 416  GLY A CA  1 
ATOM   3294 C C   . GLY A 1 417 ? 12.563  -11.217 -0.374  1.00 76.36  ? 416  GLY A C   1 
ATOM   3295 O O   . GLY A 1 417 ? 12.145  -10.245 0.261   1.00 68.37  ? 416  GLY A O   1 
ATOM   3296 N N   . THR A 1 418 ? 13.831  -11.608 -0.355  1.00 69.07  ? 417  THR A N   1 
ATOM   3297 C CA  . THR A 1 418 ? 14.813  -11.084 0.576   1.00 65.42  ? 417  THR A CA  1 
ATOM   3298 C C   . THR A 1 418 ? 16.117  -11.006 -0.195  1.00 65.50  ? 417  THR A C   1 
ATOM   3299 O O   . THR A 1 418 ? 16.506  -11.970 -0.846  1.00 75.60  ? 417  THR A O   1 
ATOM   3300 C CB  . THR A 1 418 ? 14.983  -12.041 1.781   1.00 73.53  ? 417  THR A CB  1 
ATOM   3301 O OG1 . THR A 1 418 ? 13.706  -12.290 2.381   1.00 90.39  ? 417  THR A OG1 1 
ATOM   3302 C CG2 . THR A 1 418 ? 15.918  -11.465 2.829   1.00 68.58  ? 417  THR A CG2 1 
ATOM   3303 N N   . SER A 1 419 ? 16.795  -9.867  -0.141  1.00 67.46  ? 418  SER A N   1 
ATOM   3304 C CA  . SER A 1 419 ? 17.983  -9.677  -0.972  1.00 83.36  ? 418  SER A CA  1 
ATOM   3305 C C   . SER A 1 419 ? 19.063  -10.720 -0.674  1.00 82.10  ? 418  SER A C   1 
ATOM   3306 O O   . SER A 1 419 ? 19.215  -11.141 0.468   1.00 77.46  ? 418  SER A O   1 
ATOM   3307 C CB  . SER A 1 419 ? 18.551  -8.270  -0.786  1.00 85.11  ? 418  SER A CB  1 
ATOM   3308 O OG  . SER A 1 419 ? 19.081  -8.112  0.519   1.00 87.77  ? 418  SER A OG  1 
ATOM   3309 N N   . SER A 1 420 ? 19.808  -11.131 -1.698  1.00 82.76  ? 419  SER A N   1 
ATOM   3310 C CA  . SER A 1 420 ? 20.902  -12.073 -1.507  1.00 82.45  ? 419  SER A CA  1 
ATOM   3311 C C   . SER A 1 420 ? 21.784  -11.649 -0.352  1.00 87.06  ? 419  SER A C   1 
ATOM   3312 O O   . SER A 1 420 ? 22.279  -12.483 0.405   1.00 96.87  ? 419  SER A O   1 
ATOM   3313 C CB  . SER A 1 420 ? 21.762  -12.168 -2.763  1.00 95.81  ? 419  SER A CB  1 
ATOM   3314 O OG  . SER A 1 420 ? 21.082  -12.848 -3.796  1.00 116.23 ? 419  SER A OG  1 
ATOM   3315 N N   . HIS A 1 421 ? 21.990  -10.346 -0.220  1.00 91.02  ? 420  HIS A N   1 
ATOM   3316 C CA  . HIS A 1 421 ? 22.940  -9.842  0.759   1.00 99.00  ? 420  HIS A CA  1 
ATOM   3317 C C   . HIS A 1 421 ? 22.393  -9.924  2.186   1.00 84.62  ? 420  HIS A C   1 
ATOM   3318 O O   . HIS A 1 421 ? 23.064  -10.413 3.099   1.00 79.13  ? 420  HIS A O   1 
ATOM   3319 C CB  . HIS A 1 421 ? 23.371  -8.411  0.411   1.00 112.42 ? 420  HIS A CB  1 
ATOM   3320 C CG  . HIS A 1 421 ? 24.543  -7.929  1.207   1.00 122.88 ? 420  HIS A CG  1 
ATOM   3321 N ND1 . HIS A 1 421 ? 25.814  -8.440  1.045   1.00 127.33 ? 420  HIS A ND1 1 
ATOM   3322 C CD2 . HIS A 1 421 ? 24.637  -6.987  2.176   1.00 127.12 ? 420  HIS A CD2 1 
ATOM   3323 C CE1 . HIS A 1 421 ? 26.640  -7.833  1.879   1.00 132.11 ? 420  HIS A CE1 1 
ATOM   3324 N NE2 . HIS A 1 421 ? 25.951  -6.946  2.577   1.00 132.26 ? 420  HIS A NE2 1 
ATOM   3325 N N   . GLU A 1 422 ? 21.168  -9.449  2.369   1.00 71.81  ? 421  GLU A N   1 
ATOM   3326 C CA  . GLU A 1 422 ? 20.542  -9.449  3.682   1.00 77.85  ? 421  GLU A CA  1 
ATOM   3327 C C   . GLU A 1 422 ? 20.332  -10.877 4.188   1.00 72.97  ? 421  GLU A C   1 
ATOM   3328 O O   . GLU A 1 422 ? 20.408  -11.135 5.387   1.00 68.99  ? 421  GLU A O   1 
ATOM   3329 C CB  . GLU A 1 422 ? 19.213  -8.696  3.627   1.00 88.08  ? 421  GLU A CB  1 
ATOM   3330 C CG  . GLU A 1 422 ? 18.536  -8.520  4.970   1.00 97.42  ? 421  GLU A CG  1 
ATOM   3331 C CD  . GLU A 1 422 ? 17.214  -7.779  4.851   1.00 112.84 ? 421  GLU A CD  1 
ATOM   3332 O OE1 . GLU A 1 422 ? 16.650  -7.720  3.726   1.00 109.27 ? 421  GLU A OE1 1 
ATOM   3333 O OE2 . GLU A 1 422 ? 16.739  -7.260  5.888   1.00 120.27 ? 421  GLU A OE2 1 
ATOM   3334 N N   . LEU A 1 423 ? 20.087  -11.798 3.260   1.00 69.66  ? 422  LEU A N   1 
ATOM   3335 C CA  . LEU A 1 423 ? 19.905  -13.202 3.590   1.00 61.01  ? 422  LEU A CA  1 
ATOM   3336 C C   . LEU A 1 423 ? 21.212  -13.910 3.955   1.00 69.87  ? 422  LEU A C   1 
ATOM   3337 O O   . LEU A 1 423 ? 21.262  -14.664 4.934   1.00 71.67  ? 422  LEU A O   1 
ATOM   3338 C CB  . LEU A 1 423 ? 19.205  -13.925 2.447   1.00 60.94  ? 422  LEU A CB  1 
ATOM   3339 C CG  . LEU A 1 423 ? 18.810  -15.372 2.751   1.00 60.59  ? 422  LEU A CG  1 
ATOM   3340 C CD1 . LEU A 1 423 ? 18.122  -15.444 4.095   1.00 57.33  ? 422  LEU A CD1 1 
ATOM   3341 C CD2 . LEU A 1 423 ? 17.922  -15.876 1.653   1.00 53.98  ? 422  LEU A CD2 1 
ATOM   3342 N N   . ASN A 1 424 ? 22.265  -13.676 3.175   1.00 73.01  ? 423  ASN A N   1 
ATOM   3343 C CA  . ASN A 1 424 ? 23.566  -14.252 3.492   1.00 74.39  ? 423  ASN A CA  1 
ATOM   3344 C C   . ASN A 1 424 ? 24.068  -13.740 4.846   1.00 76.03  ? 423  ASN A C   1 
ATOM   3345 O O   . ASN A 1 424 ? 24.806  -14.436 5.540   1.00 79.79  ? 423  ASN A O   1 
ATOM   3346 C CB  . ASN A 1 424 ? 24.592  -14.008 2.368   1.00 72.95  ? 423  ASN A CB  1 
ATOM   3347 C CG  . ASN A 1 424 ? 25.826  -14.937 2.471   1.00 90.50  ? 423  ASN A CG  1 
ATOM   3348 O OD1 . ASN A 1 424 ? 25.865  -16.018 1.871   1.00 102.19 ? 423  ASN A OD1 1 
ATOM   3349 N ND2 . ASN A 1 424 ? 26.835  -14.507 3.230   1.00 82.09  ? 423  ASN A ND2 1 
ATOM   3350 N N   . ASN A 1 425 ? 23.645  -12.542 5.240   1.00 72.57  ? 424  ASN A N   1 
ATOM   3351 C CA  . ASN A 1 425 ? 24.073  -11.974 6.524   1.00 74.10  ? 424  ASN A CA  1 
ATOM   3352 C C   . ASN A 1 425 ? 23.293  -12.505 7.706   1.00 76.39  ? 424  ASN A C   1 
ATOM   3353 O O   . ASN A 1 425 ? 23.824  -12.672 8.807   1.00 75.59  ? 424  ASN A O   1 
ATOM   3354 C CB  . ASN A 1 425 ? 23.990  -10.446 6.516   1.00 75.03  ? 424  ASN A CB  1 
ATOM   3355 C CG  . ASN A 1 425 ? 25.297  -9.804  6.153   1.00 89.29  ? 424  ASN A CG  1 
ATOM   3356 O OD1 . ASN A 1 425 ? 25.328  -8.896  5.334   1.00 99.55  ? 424  ASN A OD1 1 
ATOM   3357 N ND2 . ASN A 1 425 ? 26.397  -10.290 6.741   1.00 89.40  ? 424  ASN A ND2 1 
ATOM   3358 N N   . LEU A 1 426 ? 22.012  -12.741 7.471   1.00 70.82  ? 425  LEU A N   1 
ATOM   3359 C CA  . LEU A 1 426 ? 21.155  -13.335 8.480   1.00 60.00  ? 425  LEU A CA  1 
ATOM   3360 C C   . LEU A 1 426 ? 21.661  -14.738 8.799   1.00 61.31  ? 425  LEU A C   1 
ATOM   3361 O O   . LEU A 1 426 ? 21.761  -15.132 9.954   1.00 61.88  ? 425  LEU A O   1 
ATOM   3362 C CB  . LEU A 1 426 ? 19.717  -13.376 7.970   1.00 42.45  ? 425  LEU A CB  1 
ATOM   3363 C CG  . LEU A 1 426 ? 18.659  -13.969 8.886   1.00 57.82  ? 425  LEU A CG  1 
ATOM   3364 C CD1 . LEU A 1 426 ? 18.765  -13.395 10.302  1.00 43.64  ? 425  LEU A CD1 1 
ATOM   3365 C CD2 . LEU A 1 426 ? 17.303  -13.724 8.266   1.00 65.55  ? 425  LEU A CD2 1 
ATOM   3366 N N   . LEU A 1 427 ? 21.996  -15.486 7.760   1.00 54.27  ? 426  LEU A N   1 
ATOM   3367 C CA  . LEU A 1 427 ? 22.522  -16.810 7.957   1.00 50.80  ? 426  LEU A CA  1 
ATOM   3368 C C   . LEU A 1 427 ? 23.878  -16.781 8.674   1.00 61.97  ? 426  LEU A C   1 
ATOM   3369 O O   . LEU A 1 427 ? 24.158  -17.616 9.537   1.00 69.39  ? 426  LEU A O   1 
ATOM   3370 C CB  . LEU A 1 427 ? 22.579  -17.537 6.624   1.00 45.50  ? 426  LEU A CB  1 
ATOM   3371 C CG  . LEU A 1 427 ? 21.359  -18.417 6.327   1.00 49.86  ? 426  LEU A CG  1 
ATOM   3372 C CD1 . LEU A 1 427 ? 20.093  -18.015 7.097   1.00 46.96  ? 426  LEU A CD1 1 
ATOM   3373 C CD2 . LEU A 1 427 ? 21.095  -18.465 4.843   1.00 43.49  ? 426  LEU A CD2 1 
ATOM   3374 N N   . ASP A 1 428 ? 24.707  -15.798 8.351   1.00 72.76  ? 427  ASP A N   1 
ATOM   3375 C CA  . ASP A 1 428 ? 25.967  -15.621 9.073   1.00 77.65  ? 427  ASP A CA  1 
ATOM   3376 C C   . ASP A 1 428 ? 25.774  -15.244 10.557  1.00 70.96  ? 427  ASP A C   1 
ATOM   3377 O O   . ASP A 1 428 ? 26.448  -15.776 11.440  1.00 73.04  ? 427  ASP A O   1 
ATOM   3378 C CB  . ASP A 1 428 ? 26.864  -14.624 8.348   1.00 81.42  ? 427  ASP A CB  1 
ATOM   3379 C CG  . ASP A 1 428 ? 27.497  -15.214 7.086   1.00 101.48 ? 427  ASP A CG  1 
ATOM   3380 O OD1 . ASP A 1 428 ? 27.561  -16.462 6.984   1.00 98.91  ? 427  ASP A OD1 1 
ATOM   3381 O OD2 . ASP A 1 428 ? 27.943  -14.429 6.206   1.00 107.19 ? 427  ASP A OD2 1 
ATOM   3382 N N   . ASN A 1 429 ? 24.838  -14.354 10.846  1.00 60.92  ? 428  ASN A N   1 
ATOM   3383 C CA  . ASN A 1 429 ? 24.627  -13.969 12.231  1.00 64.80  ? 428  ASN A CA  1 
ATOM   3384 C C   . ASN A 1 429 ? 24.074  -15.096 13.072  1.00 67.34  ? 428  ASN A C   1 
ATOM   3385 O O   . ASN A 1 429 ? 24.296  -15.160 14.279  1.00 77.09  ? 428  ASN A O   1 
ATOM   3386 C CB  . ASN A 1 429 ? 23.725  -12.747 12.322  1.00 75.07  ? 428  ASN A CB  1 
ATOM   3387 C CG  . ASN A 1 429 ? 24.375  -11.510 11.747  1.00 73.38  ? 428  ASN A CG  1 
ATOM   3388 O OD1 . ASN A 1 429 ? 25.579  -11.306 11.885  1.00 71.84  ? 428  ASN A OD1 1 
ATOM   3389 N ND2 . ASN A 1 429 ? 23.583  -10.685 11.088  1.00 74.04  ? 428  ASN A ND2 1 
ATOM   3390 N N   . ALA A 1 430 ? 23.357  -15.992 12.417  1.00 69.70  ? 429  ALA A N   1 
ATOM   3391 C CA  . ALA A 1 430 ? 22.743  -17.123 13.083  1.00 62.97  ? 429  ALA A CA  1 
ATOM   3392 C C   . ALA A 1 430 ? 23.716  -18.305 13.293  1.00 71.38  ? 429  ALA A C   1 
ATOM   3393 O O   . ALA A 1 430 ? 23.364  -19.288 13.955  1.00 76.38  ? 429  ALA A O   1 
ATOM   3394 C CB  . ALA A 1 430 ? 21.526  -17.548 12.309  1.00 53.91  ? 429  ALA A CB  1 
ATOM   3395 N N   . ASN A 1 431 ? 24.941  -18.188 12.770  1.00 69.95  ? 430  ASN A N   1 
ATOM   3396 C CA  . ASN A 1 431 ? 25.927  -19.270 12.837  1.00 71.75  ? 430  ASN A CA  1 
ATOM   3397 C C   . ASN A 1 431 ? 25.329  -20.551 12.275  1.00 74.55  ? 430  ASN A C   1 
ATOM   3398 O O   . ASN A 1 431 ? 25.281  -21.588 12.942  1.00 80.04  ? 430  ASN A O   1 
ATOM   3399 C CB  . ASN A 1 431 ? 26.424  -19.518 14.265  1.00 79.32  ? 430  ASN A CB  1 
ATOM   3400 C CG  . ASN A 1 431 ? 27.236  -18.372 14.809  1.00 114.98 ? 430  ASN A CG  1 
ATOM   3401 O OD1 . ASN A 1 431 ? 26.901  -17.801 15.852  1.00 123.62 ? 430  ASN A OD1 1 
ATOM   3402 N ND2 . ASN A 1 431 ? 28.319  -18.025 14.111  1.00 130.14 ? 430  ASN A ND2 1 
ATOM   3403 N N   . ILE A 1 432 ? 24.841  -20.470 11.050  1.00 61.96  ? 431  ILE A N   1 
ATOM   3404 C CA  . ILE A 1 432 ? 24.298  -21.637 10.401  1.00 56.94  ? 431  ILE A CA  1 
ATOM   3405 C C   . ILE A 1 432 ? 25.282  -22.133 9.362   1.00 64.12  ? 431  ILE A C   1 
ATOM   3406 O O   . ILE A 1 432 ? 25.577  -21.441 8.391   1.00 64.40  ? 431  ILE A O   1 
ATOM   3407 C CB  . ILE A 1 432 ? 22.913  -21.344 9.826   1.00 54.24  ? 431  ILE A CB  1 
ATOM   3408 C CG1 . ILE A 1 432 ? 21.927  -21.300 10.985  1.00 53.87  ? 431  ILE A CG1 1 
ATOM   3409 C CG2 . ILE A 1 432 ? 22.483  -22.424 8.817   1.00 45.57  ? 431  ILE A CG2 1 
ATOM   3410 C CD1 . ILE A 1 432 ? 20.700  -20.566 10.678  1.00 60.42  ? 431  ILE A CD1 1 
ATOM   3411 N N   . ALA A 1 433 ? 25.814  -23.327 9.595   1.00 67.58  ? 432  ALA A N   1 
ATOM   3412 C CA  . ALA A 1 433 ? 26.843  -23.884 8.725   1.00 68.47  ? 432  ALA A CA  1 
ATOM   3413 C C   . ALA A 1 433 ? 26.358  -23.965 7.280   1.00 76.80  ? 432  ALA A C   1 
ATOM   3414 O O   . ALA A 1 433 ? 25.211  -24.333 7.017   1.00 79.06  ? 432  ALA A O   1 
ATOM   3415 C CB  . ALA A 1 433 ? 27.295  -25.255 9.230   1.00 59.63  ? 432  ALA A CB  1 
ATOM   3416 N N   . THR A 1 434 ? 27.240  -23.626 6.345   1.00 73.23  ? 433  THR A N   1 
ATOM   3417 C CA  . THR A 1 434 ? 26.846  -23.482 4.947   1.00 72.25  ? 433  THR A CA  1 
ATOM   3418 C C   . THR A 1 434 ? 26.159  -24.720 4.338   1.00 75.48  ? 433  THR A C   1 
ATOM   3419 O O   . THR A 1 434 ? 25.223  -24.592 3.543   1.00 77.11  ? 433  THR A O   1 
ATOM   3420 C CB  . THR A 1 434 ? 28.017  -22.937 4.080   1.00 72.08  ? 433  THR A CB  1 
ATOM   3421 O OG1 . THR A 1 434 ? 29.172  -23.764 4.236   1.00 78.73  ? 433  THR A OG1 1 
ATOM   3422 C CG2 . THR A 1 434 ? 28.383  -21.544 4.533   1.00 67.19  ? 433  THR A CG2 1 
ATOM   3423 N N   . PRO A 1 435 ? 26.611  -25.925 4.711   1.00 77.69  ? 434  PRO A N   1 
ATOM   3424 C CA  . PRO A 1 435 ? 25.880  -27.113 4.257   1.00 71.81  ? 434  PRO A CA  1 
ATOM   3425 C C   . PRO A 1 435 ? 24.434  -27.170 4.752   1.00 74.59  ? 434  PRO A C   1 
ATOM   3426 O O   . PRO A 1 435 ? 23.581  -27.677 4.027   1.00 79.29  ? 434  PRO A O   1 
ATOM   3427 C CB  . PRO A 1 435 ? 26.692  -28.253 4.851   1.00 85.97  ? 434  PRO A CB  1 
ATOM   3428 C CG  . PRO A 1 435 ? 28.097  -27.696 4.903   1.00 90.22  ? 434  PRO A CG  1 
ATOM   3429 C CD  . PRO A 1 435 ? 27.903  -26.277 5.328   1.00 80.44  ? 434  PRO A CD  1 
ATOM   3430 N N   . SER A 1 436 ? 24.156  -26.653 5.947   1.00 73.24  ? 435  SER A N   1 
ATOM   3431 C CA  . SER A 1 436 ? 22.789  -26.659 6.473   1.00 64.87  ? 435  SER A CA  1 
ATOM   3432 C C   . SER A 1 436 ? 21.857  -25.611 5.840   1.00 67.39  ? 435  SER A C   1 
ATOM   3433 O O   . SER A 1 436 ? 20.646  -25.610 6.104   1.00 70.17  ? 435  SER A O   1 
ATOM   3434 C CB  . SER A 1 436 ? 22.779  -26.534 8.005   1.00 60.26  ? 435  SER A CB  1 
ATOM   3435 O OG  . SER A 1 436 ? 23.723  -27.413 8.603   1.00 67.01  ? 435  SER A OG  1 
ATOM   3436 N N   . ARG A 1 437 ? 22.394  -24.736 4.994   1.00 58.89  ? 436  ARG A N   1 
ATOM   3437 C CA  . ARG A 1 437 ? 21.568  -23.660 4.431   1.00 53.76  ? 436  ARG A CA  1 
ATOM   3438 C C   . ARG A 1 437 ? 20.687  -24.091 3.260   1.00 56.79  ? 436  ARG A C   1 
ATOM   3439 O O   . ARG A 1 437 ? 19.854  -23.329 2.788   1.00 60.80  ? 436  ARG A O   1 
ATOM   3440 C CB  . ARG A 1 437 ? 22.418  -22.447 4.043   1.00 51.12  ? 436  ARG A CB  1 
ATOM   3441 C CG  . ARG A 1 437 ? 23.319  -21.982 5.152   1.00 54.54  ? 436  ARG A CG  1 
ATOM   3442 C CD  . ARG A 1 437 ? 23.981  -20.678 4.817   1.00 58.50  ? 436  ARG A CD  1 
ATOM   3443 N NE  . ARG A 1 437 ? 24.794  -20.223 5.933   1.00 62.98  ? 436  ARG A NE  1 
ATOM   3444 C CZ  . ARG A 1 437 ? 25.508  -19.107 5.935   1.00 64.51  ? 436  ARG A CZ  1 
ATOM   3445 N NH1 . ARG A 1 437 ? 25.508  -18.311 4.874   1.00 73.42  ? 436  ARG A NH1 1 
ATOM   3446 N NH2 . ARG A 1 437 ? 26.206  -18.785 7.013   1.00 53.85  ? 436  ARG A NH2 1 
ATOM   3447 N N   . SER A 1 438 ? 20.860  -25.315 2.793   1.00 62.39  ? 437  SER A N   1 
ATOM   3448 C CA  . SER A 1 438 ? 20.034  -25.798 1.699   1.00 65.39  ? 437  SER A CA  1 
ATOM   3449 C C   . SER A 1 438 ? 18.585  -25.955 2.164   1.00 59.53  ? 437  SER A C   1 
ATOM   3450 O O   . SER A 1 438 ? 17.666  -25.992 1.350   1.00 51.95  ? 437  SER A O   1 
ATOM   3451 C CB  . SER A 1 438 ? 20.597  -27.096 1.138   1.00 64.80  ? 437  SER A CB  1 
ATOM   3452 O OG  . SER A 1 438 ? 21.088  -27.903 2.191   1.00 76.25  ? 437  SER A OG  1 
ATOM   3453 N N   . ALA A 1 439 ? 18.385  -26.008 3.480   1.00 59.28  ? 438  ALA A N   1 
ATOM   3454 C CA  . ALA A 1 439 ? 17.035  -25.995 4.054   1.00 52.79  ? 438  ALA A CA  1 
ATOM   3455 C C   . ALA A 1 439 ? 16.272  -24.723 3.721   1.00 57.67  ? 438  ALA A C   1 
ATOM   3456 O O   . ALA A 1 439 ? 15.047  -24.741 3.638   1.00 77.93  ? 438  ALA A O   1 
ATOM   3457 C CB  . ALA A 1 439 ? 17.089  -26.172 5.543   1.00 60.68  ? 438  ALA A CB  1 
ATOM   3458 N N   . ILE A 1 440 ? 16.997  -23.619 3.545   1.00 54.51  ? 439  ILE A N   1 
ATOM   3459 C CA  . ILE A 1 440 ? 16.407  -22.335 3.191   1.00 55.76  ? 439  ILE A CA  1 
ATOM   3460 C C   . ILE A 1 440 ? 16.272  -22.170 1.679   1.00 63.88  ? 439  ILE A C   1 
ATOM   3461 O O   . ILE A 1 440 ? 15.180  -21.941 1.170   1.00 55.81  ? 439  ILE A O   1 
ATOM   3462 C CB  . ILE A 1 440 ? 17.267  -21.176 3.706   1.00 56.32  ? 439  ILE A CB  1 
ATOM   3463 C CG1 . ILE A 1 440 ? 17.566  -21.349 5.192   1.00 57.37  ? 439  ILE A CG1 1 
ATOM   3464 C CG2 . ILE A 1 440 ? 16.567  -19.858 3.451   1.00 44.75  ? 439  ILE A CG2 1 
ATOM   3465 C CD1 . ILE A 1 440 ? 16.389  -21.060 6.069   1.00 54.71  ? 439  ILE A CD1 1 
ATOM   3466 N N   . TYR A 1 441 ? 17.387  -22.292 0.962   1.00 66.97  ? 440  TYR A N   1 
ATOM   3467 C CA  . TYR A 1 441 ? 17.396  -22.024 -0.474  1.00 59.82  ? 440  TYR A CA  1 
ATOM   3468 C C   . TYR A 1 441 ? 16.561  -23.008 -1.288  1.00 66.65  ? 440  TYR A C   1 
ATOM   3469 O O   . TYR A 1 441 ? 15.986  -22.656 -2.317  1.00 65.24  ? 440  TYR A O   1 
ATOM   3470 C CB  . TYR A 1 441 ? 18.830  -21.955 -1.007  1.00 50.78  ? 440  TYR A CB  1 
ATOM   3471 C CG  . TYR A 1 441 ? 19.594  -20.791 -0.429  1.00 61.12  ? 440  TYR A CG  1 
ATOM   3472 C CD1 . TYR A 1 441 ? 19.352  -19.489 -0.861  1.00 51.59  ? 440  TYR A CD1 1 
ATOM   3473 C CD2 . TYR A 1 441 ? 20.536  -20.985 0.570   1.00 57.61  ? 440  TYR A CD2 1 
ATOM   3474 C CE1 . TYR A 1 441 ? 20.025  -18.433 -0.321  1.00 51.98  ? 440  TYR A CE1 1 
ATOM   3475 C CE2 . TYR A 1 441 ? 21.212  -19.927 1.121   1.00 56.10  ? 440  TYR A CE2 1 
ATOM   3476 C CZ  . TYR A 1 441 ? 20.967  -18.647 0.671   1.00 60.46  ? 440  TYR A CZ  1 
ATOM   3477 O OH  . TYR A 1 441 ? 21.672  -17.584 1.222   1.00 67.52  ? 440  TYR A OH  1 
ATOM   3478 N N   . ASN A 1 442 ? 16.478  -24.245 -0.834  1.00 65.25  ? 441  ASN A N   1 
ATOM   3479 C CA  . ASN A 1 442 ? 15.753  -25.223 -1.619  1.00 63.15  ? 441  ASN A CA  1 
ATOM   3480 C C   . ASN A 1 442 ? 14.236  -25.028 -1.611  1.00 63.20  ? 441  ASN A C   1 
ATOM   3481 O O   . ASN A 1 442 ? 13.521  -25.659 -2.391  1.00 64.32  ? 441  ASN A O   1 
ATOM   3482 C CB  . ASN A 1 442 ? 16.160  -26.638 -1.233  1.00 62.39  ? 441  ASN A CB  1 
ATOM   3483 C CG  . ASN A 1 442 ? 17.563  -26.965 -1.668  1.00 63.56  ? 441  ASN A CG  1 
ATOM   3484 O OD1 . ASN A 1 442 ? 18.229  -26.150 -2.316  1.00 70.84  ? 441  ASN A OD1 1 
ATOM   3485 N ND2 . ASN A 1 442 ? 18.030  -28.155 -1.312  1.00 59.26  ? 441  ASN A ND2 1 
ATOM   3486 N N   . LEU A 1 443 ? 13.745  -24.137 -0.754  1.00 60.86  ? 442  LEU A N   1 
ATOM   3487 C CA  . LEU A 1 443 ? 12.334  -23.780 -0.798  1.00 61.16  ? 442  LEU A CA  1 
ATOM   3488 C C   . LEU A 1 443 ? 11.924  -23.295 -2.203  1.00 71.64  ? 442  LEU A C   1 
ATOM   3489 O O   . LEU A 1 443 ? 10.752  -23.401 -2.579  1.00 65.84  ? 442  LEU A O   1 
ATOM   3490 C CB  . LEU A 1 443 ? 12.011  -22.738 0.269   1.00 59.38  ? 442  LEU A CB  1 
ATOM   3491 C CG  . LEU A 1 443 ? 12.054  -23.169 1.742   1.00 59.89  ? 442  LEU A CG  1 
ATOM   3492 C CD1 . LEU A 1 443 ? 11.898  -21.945 2.668   1.00 47.75  ? 442  LEU A CD1 1 
ATOM   3493 C CD2 . LEU A 1 443 ? 10.992  -24.246 2.049   1.00 47.65  ? 442  LEU A CD2 1 
ATOM   3494 N N   . GLU A 1 444 ? 12.892  -22.774 -2.966  1.00 81.42  ? 443  GLU A N   1 
ATOM   3495 C CA  . GLU A 1 444 ? 12.700  -22.407 -4.376  1.00 88.73  ? 443  GLU A CA  1 
ATOM   3496 C C   . GLU A 1 444 ? 12.067  -23.557 -5.156  1.00 80.23  ? 443  GLU A C   1 
ATOM   3497 O O   . GLU A 1 444 ? 11.186  -23.350 -5.987  1.00 84.02  ? 443  GLU A O   1 
ATOM   3498 C CB  . GLU A 1 444 ? 14.036  -22.032 -5.048  1.00 100.56 ? 443  GLU A CB  1 
ATOM   3499 C CG  . GLU A 1 444 ? 14.700  -20.757 -4.516  1.00 120.86 ? 443  GLU A CG  1 
ATOM   3500 C CD  . GLU A 1 444 ? 16.112  -20.521 -5.074  1.00 125.54 ? 443  GLU A CD  1 
ATOM   3501 O OE1 . GLU A 1 444 ? 16.972  -19.971 -4.333  1.00 106.35 ? 443  GLU A OE1 1 
ATOM   3502 O OE2 . GLU A 1 444 ? 16.358  -20.889 -6.248  1.00 133.19 ? 443  GLU A OE2 1 
ATOM   3503 N N   . MET A 1 445 ? 12.532  -24.770 -4.888  1.00 67.91  ? 444  MET A N   1 
ATOM   3504 C CA  . MET A 1 445 ? 12.052  -25.951 -5.598  1.00 73.85  ? 444  MET A CA  1 
ATOM   3505 C C   . MET A 1 445 ? 10.643  -26.382 -5.206  1.00 77.11  ? 444  MET A C   1 
ATOM   3506 O O   . MET A 1 445 ? 10.096  -27.324 -5.794  1.00 84.97  ? 444  MET A O   1 
ATOM   3507 C CB  . MET A 1 445 ? 13.005  -27.116 -5.379  1.00 71.33  ? 444  MET A CB  1 
ATOM   3508 C CG  . MET A 1 445 ? 14.446  -26.738 -5.561  1.00 65.82  ? 444  MET A CG  1 
ATOM   3509 S SD  . MET A 1 445 ? 15.437  -28.159 -6.029  1.00 80.64  ? 444  MET A SD  1 
ATOM   3510 C CE  . MET A 1 445 ? 16.858  -27.798 -5.009  1.00 81.37  ? 444  MET A CE  1 
ATOM   3511 N N   . LEU A 1 446 ? 10.075  -25.714 -4.204  1.00 66.55  ? 445  LEU A N   1 
ATOM   3512 C CA  . LEU A 1 446 ? 8.674   -25.902 -3.843  1.00 65.92  ? 445  LEU A CA  1 
ATOM   3513 C C   . LEU A 1 446 ? 7.901   -24.615 -4.125  1.00 79.55  ? 445  LEU A C   1 
ATOM   3514 O O   . LEU A 1 446 ? 6.852   -24.361 -3.531  1.00 88.15  ? 445  LEU A O   1 
ATOM   3515 C CB  . LEU A 1 446 ? 8.529   -26.316 -2.374  1.00 58.28  ? 445  LEU A CB  1 
ATOM   3516 C CG  . LEU A 1 446 ? 9.295   -27.569 -1.934  1.00 58.17  ? 445  LEU A CG  1 
ATOM   3517 C CD1 . LEU A 1 446 ? 9.278   -27.712 -0.427  1.00 51.29  ? 445  LEU A CD1 1 
ATOM   3518 C CD2 . LEU A 1 446 ? 8.767   -28.840 -2.627  1.00 55.01  ? 445  LEU A CD2 1 
ATOM   3519 N N   . GLY A 1 447 ? 8.446   -23.805 -5.031  1.00 88.34  ? 446  GLY A N   1 
ATOM   3520 C CA  . GLY A 1 447 ? 7.795   -22.600 -5.520  1.00 93.42  ? 446  GLY A CA  1 
ATOM   3521 C C   . GLY A 1 447 ? 7.635   -21.504 -4.486  1.00 102.28 ? 446  GLY A C   1 
ATOM   3522 O O   . GLY A 1 447 ? 6.539   -20.968 -4.315  1.00 120.14 ? 446  GLY A O   1 
ATOM   3523 N N   . ALA A 1 448 ? 8.722   -21.151 -3.807  1.00 89.43  ? 447  ALA A N   1 
ATOM   3524 C CA  . ALA A 1 448 ? 8.623   -20.236 -2.678  1.00 84.25  ? 447  ALA A CA  1 
ATOM   3525 C C   . ALA A 1 448 ? 9.160   -18.852 -2.964  1.00 83.84  ? 447  ALA A C   1 
ATOM   3526 O O   . ALA A 1 448 ? 8.579   -17.855 -2.515  1.00 96.90  ? 447  ALA A O   1 
ATOM   3527 C CB  . ALA A 1 448 ? 9.308   -20.814 -1.465  1.00 86.70  ? 447  ALA A CB  1 
ATOM   3528 N N   . THR A 1 449 ? 10.253  -18.790 -3.718  1.00 66.66  ? 448  THR A N   1 
ATOM   3529 C CA  . THR A 1 449 ? 11.012  -17.531 -3.889  1.00 90.39  ? 448  THR A CA  1 
ATOM   3530 C C   . THR A 1 449 ? 11.533  -17.003 -2.546  1.00 77.84  ? 448  THR A C   1 
ATOM   3531 O O   . THR A 1 449 ? 10.777  -16.544 -1.682  1.00 64.25  ? 448  THR A O   1 
ATOM   3532 C CB  . THR A 1 449 ? 10.265  -16.408 -4.704  1.00 107.77 ? 448  THR A CB  1 
ATOM   3533 O OG1 . THR A 1 449 ? 9.726   -15.412 -3.823  1.00 93.54  ? 448  THR A OG1 1 
ATOM   3534 C CG2 . THR A 1 449 ? 9.164   -16.997 -5.585  1.00 115.38 ? 448  THR A CG2 1 
ATOM   3535 N N   . VAL A 1 450 ? 12.840  -17.110 -2.367  1.00 68.91  ? 449  VAL A N   1 
ATOM   3536 C CA  . VAL A 1 450 ? 13.411  -16.839 -1.073  1.00 74.81  ? 449  VAL A CA  1 
ATOM   3537 C C   . VAL A 1 450 ? 14.285  -15.615 -1.211  1.00 67.68  ? 449  VAL A C   1 
ATOM   3538 O O   . VAL A 1 450 ? 14.140  -14.660 -0.442  1.00 71.89  ? 449  VAL A O   1 
ATOM   3539 C CB  . VAL A 1 450 ? 14.148  -18.085 -0.473  1.00 77.61  ? 449  VAL A CB  1 
ATOM   3540 C CG1 . VAL A 1 450 ? 13.580  -19.387 -1.059  1.00 63.71  ? 449  VAL A CG1 1 
ATOM   3541 C CG2 . VAL A 1 450 ? 15.642  -18.011 -0.676  1.00 73.93  ? 449  VAL A CG2 1 
ATOM   3542 N N   . VAL A 1 451 ? 15.135  -15.632 -2.234  1.00 65.98  ? 450  VAL A N   1 
ATOM   3543 C CA  . VAL A 1 451 ? 15.966  -14.483 -2.591  1.00 78.64  ? 450  VAL A CA  1 
ATOM   3544 C C   . VAL A 1 451 ? 15.198  -13.487 -3.471  1.00 85.37  ? 450  VAL A C   1 
ATOM   3545 O O   . VAL A 1 451 ? 14.511  -13.878 -4.412  1.00 82.44  ? 450  VAL A O   1 
ATOM   3546 C CB  . VAL A 1 451 ? 17.234  -14.916 -3.326  1.00 77.87  ? 450  VAL A CB  1 
ATOM   3547 C CG1 . VAL A 1 451 ? 18.143  -13.721 -3.538  1.00 91.84  ? 450  VAL A CG1 1 
ATOM   3548 C CG2 . VAL A 1 451 ? 17.948  -15.973 -2.534  1.00 67.43  ? 450  VAL A CG2 1 
ATOM   3549 N N   . ALA A 1 452 ? 15.332  -12.199 -3.168  1.00 95.73  ? 451  ALA A N   1 
ATOM   3550 C CA  . ALA A 1 452 ? 14.522  -11.166 -3.808  1.00 98.58  ? 451  ALA A CA  1 
ATOM   3551 C C   . ALA A 1 452 ? 14.806  -11.016 -5.299  1.00 99.25  ? 451  ALA A C   1 
ATOM   3552 O O   . ALA A 1 452 ? 13.946  -10.557 -6.054  1.00 104.96 ? 451  ALA A O   1 
ATOM   3553 C CB  . ALA A 1 452 ? 14.704  -9.837  -3.094  1.00 96.77  ? 451  ALA A CB  1 
ATOM   3554 N N   . ASP A 1 453 ? 16.001  -11.416 -5.723  1.00 85.94  ? 452  ASP A N   1 
ATOM   3555 C CA  . ASP A 1 453 ? 16.382  -11.239 -7.119  1.00 85.02  ? 452  ASP A CA  1 
ATOM   3556 C C   . ASP A 1 453 ? 15.835  -12.336 -8.030  1.00 82.52  ? 452  ASP A C   1 
ATOM   3557 O O   . ASP A 1 453 ? 15.917  -12.250 -9.255  1.00 81.43  ? 452  ASP A O   1 
ATOM   3558 C CB  . ASP A 1 453 ? 17.906  -11.010 -7.283  1.00 130.19 ? 452  ASP A CB  1 
ATOM   3559 C CG  . ASP A 1 453 ? 18.746  -12.263 -7.032  1.00 104.25 ? 452  ASP A CG  1 
ATOM   3560 O OD1 . ASP A 1 453 ? 18.271  -13.372 -7.335  1.00 78.75  ? 452  ASP A OD1 1 
ATOM   3561 O OD2 . ASP A 1 453 ? 19.906  -12.123 -6.568  1.00 100.67 ? 452  ASP A OD2 1 
ATOM   3562 N N   . ARG A 1 454 ? 15.235  -13.352 -7.427  1.00 101.33 ? 453  ARG A N   1 
ATOM   3563 C CA  . ARG A 1 454 ? 14.642  -14.432 -8.202  1.00 111.01 ? 453  ARG A CA  1 
ATOM   3564 C C   . ARG A 1 454 ? 13.197  -14.113 -8.589  1.00 111.25 ? 453  ARG A C   1 
ATOM   3565 O O   . ARG A 1 454 ? 12.568  -14.874 -9.321  1.00 120.58 ? 453  ARG A O   1 
ATOM   3566 C CB  . ARG A 1 454 ? 14.726  -15.756 -7.440  1.00 109.54 ? 453  ARG A CB  1 
ATOM   3567 C CG  . ARG A 1 454 ? 14.572  -16.978 -8.319  1.00 119.51 ? 453  ARG A CG  1 
ATOM   3568 C CD  . ARG A 1 454 ? 14.421  -18.240 -7.486  1.00 130.13 ? 453  ARG A CD  1 
ATOM   3569 N NE  . ARG A 1 454 ? 14.060  -19.384 -8.316  1.00 132.49 ? 453  ARG A NE  1 
ATOM   3570 C CZ  . ARG A 1 454 ? 14.903  -19.974 -9.152  1.00 132.98 ? 453  ARG A CZ  1 
ATOM   3571 N NH1 . ARG A 1 454 ? 16.144  -19.518 -9.260  1.00 131.63 ? 453  ARG A NH1 1 
ATOM   3572 N NH2 . ARG A 1 454 ? 14.509  -21.010 -9.879  1.00 133.62 ? 453  ARG A NH2 1 
ATOM   3573 N N   . ARG A 1 455 ? 12.685  -12.986 -8.096  1.00 102.11 ? 454  ARG A N   1 
ATOM   3574 C CA  . ARG A 1 455 ? 11.327  -12.522 -8.419  1.00 121.27 ? 454  ARG A CA  1 
ATOM   3575 C C   . ARG A 1 455 ? 10.205  -13.208 -7.614  1.00 133.17 ? 454  ARG A C   1 
ATOM   3576 O O   . ARG A 1 455 ? 10.065  -14.437 -7.627  1.00 127.65 ? 454  ARG A O   1 
ATOM   3577 C CB  . ARG A 1 455 ? 11.039  -12.612 -9.925  1.00 116.74 ? 454  ARG A CB  1 
ATOM   3578 C CG  . ARG A 1 455 ? 9.585   -12.337 -10.272 1.00 119.13 ? 454  ARG A CG  1 
ATOM   3579 C CD  . ARG A 1 455 ? 9.321   -12.464 -11.755 1.00 133.45 ? 454  ARG A CD  1 
ATOM   3580 N NE  . ARG A 1 455 ? 7.909   -12.254 -12.054 1.00 152.20 ? 454  ARG A NE  1 
ATOM   3581 C CZ  . ARG A 1 455 ? 7.404   -12.215 -13.282 1.00 169.12 ? 454  ARG A CZ  1 
ATOM   3582 N NH1 . ARG A 1 455 ? 8.200   -12.370 -14.333 1.00 171.66 ? 454  ARG A NH1 1 
ATOM   3583 N NH2 . ARG A 1 455 ? 6.102   -12.019 -13.458 1.00 175.79 ? 454  ARG A NH2 1 
ATOM   3584 N N   . GLY A 1 456 ? 9.403   -12.392 -6.931  1.00 138.76 ? 455  GLY A N   1 
ATOM   3585 C CA  . GLY A 1 456 ? 8.357   -12.877 -6.046  1.00 136.99 ? 455  GLY A CA  1 
ATOM   3586 C C   . GLY A 1 456 ? 7.200   -13.546 -6.760  1.00 146.96 ? 455  GLY A C   1 
ATOM   3587 O O   . GLY A 1 456 ? 6.860   -13.194 -7.894  1.00 146.84 ? 455  GLY A O   1 
ATOM   3588 N N   . ARG A 1 457 ? 6.590   -14.516 -6.084  1.00 156.40 ? 456  ARG A N   1 
ATOM   3589 C CA  . ARG A 1 457 ? 5.484   -15.279 -6.653  1.00 163.32 ? 456  ARG A CA  1 
ATOM   3590 C C   . ARG A 1 457 ? 4.133   -14.690 -6.235  1.00 161.91 ? 456  ARG A C   1 
ATOM   3591 O O   . ARG A 1 457 ? 3.901   -14.420 -5.055  1.00 153.62 ? 456  ARG A O   1 
ATOM   3592 C CB  . ARG A 1 457 ? 5.585   -16.753 -6.248  1.00 166.06 ? 456  ARG A CB  1 
ATOM   3593 C CG  . ARG A 1 457 ? 5.195   -17.713 -7.358  1.00 172.96 ? 456  ARG A CG  1 
ATOM   3594 C CD  . ARG A 1 457 ? 6.143   -17.592 -8.543  1.00 177.96 ? 456  ARG A CD  1 
ATOM   3595 N NE  . ARG A 1 457 ? 5.511   -17.985 -9.802  1.00 184.00 ? 456  ARG A NE  1 
ATOM   3596 C CZ  . ARG A 1 457 ? 5.128   -17.131 -10.748 1.00 188.26 ? 456  ARG A CZ  1 
ATOM   3597 N NH1 . ARG A 1 457 ? 4.560   -17.580 -11.859 1.00 187.21 ? 456  ARG A NH1 1 
ATOM   3598 N NH2 . ARG A 1 457 ? 5.319   -15.827 -10.587 1.00 191.55 ? 456  ARG A NH2 1 
ATOM   3599 N N   . LYS A 1 458 ? 3.247   -14.496 -7.210  1.00 168.71 ? 457  LYS A N   1 
ATOM   3600 C CA  . LYS A 1 458 ? 1.985   -13.794 -6.975  1.00 171.93 ? 457  LYS A CA  1 
ATOM   3601 C C   . LYS A 1 458 ? 1.204   -14.348 -5.781  1.00 165.15 ? 457  LYS A C   1 
ATOM   3602 O O   . LYS A 1 458 ? 0.980   -15.555 -5.680  1.00 157.17 ? 457  LYS A O   1 
ATOM   3603 C CB  . LYS A 1 458 ? 1.129   -13.738 -8.252  1.00 176.95 ? 457  LYS A CB  1 
ATOM   3604 C CG  . LYS A 1 458 ? 1.707   -12.807 -9.328  1.00 176.96 ? 457  LYS A CG  1 
ATOM   3605 C CD  . LYS A 1 458 ? 0.787   -12.643 -10.536 1.00 176.83 ? 457  LYS A CD  1 
ATOM   3606 C CE  . LYS A 1 458 ? 1.421   -11.716 -11.574 1.00 175.22 ? 457  LYS A CE  1 
ATOM   3607 N NZ  . LYS A 1 458 ? 0.565   -11.506 -12.778 1.00 175.69 ? 457  LYS A NZ  1 
ATOM   3608 N N   . PRO A 1 459 ? 0.802   -13.449 -4.867  1.00 167.06 ? 458  PRO A N   1 
ATOM   3609 C CA  . PRO A 1 459 ? 0.183   -13.752 -3.574  1.00 162.51 ? 458  PRO A CA  1 
ATOM   3610 C C   . PRO A 1 459 ? -0.943  -14.773 -3.655  1.00 163.58 ? 458  PRO A C   1 
ATOM   3611 O O   . PRO A 1 459 ? -1.761  -14.748 -4.579  1.00 168.01 ? 458  PRO A O   1 
ATOM   3612 C CB  . PRO A 1 459 ? -0.371  -12.396 -3.131  1.00 162.16 ? 458  PRO A CB  1 
ATOM   3613 C CG  . PRO A 1 459 ? 0.538   -11.413 -3.751  1.00 166.54 ? 458  PRO A CG  1 
ATOM   3614 C CD  . PRO A 1 459 ? 0.918   -11.996 -5.085  1.00 170.96 ? 458  PRO A CD  1 
ATOM   3615 N N   . LYS A 1 460 ? -0.977  -15.665 -2.672  1.00 156.84 ? 459  LYS A N   1 
ATOM   3616 C CA  . LYS A 1 460 ? -2.035  -16.655 -2.571  1.00 154.31 ? 459  LYS A CA  1 
ATOM   3617 C C   . LYS A 1 460 ? -3.355  -15.969 -2.234  1.00 142.95 ? 459  LYS A C   1 
ATOM   3618 O O   . LYS A 1 460 ? -3.508  -15.361 -1.175  1.00 130.46 ? 459  LYS A O   1 
ATOM   3619 C CB  . LYS A 1 460 ? -1.676  -17.709 -1.523  1.00 158.17 ? 459  LYS A CB  1 
ATOM   3620 C CG  . LYS A 1 460 ? -0.323  -18.364 -1.769  1.00 160.70 ? 459  LYS A CG  1 
ATOM   3621 C CD  . LYS A 1 460 ? 0.014   -19.393 -0.706  1.00 160.50 ? 459  LYS A CD  1 
ATOM   3622 C CE  . LYS A 1 460 ? 1.374   -20.011 -0.974  1.00 161.37 ? 459  LYS A CE  1 
ATOM   3623 N NZ  . LYS A 1 460 ? 1.721   -21.027 0.055   1.00 160.36 ? 459  LYS A NZ  1 
ATOM   3624 N N   . THR A 1 461 ? -4.305  -16.069 -3.153  1.00 144.52 ? 460  THR A N   1 
ATOM   3625 C CA  . THR A 1 461 ? -5.580  -15.385 -3.014  1.00 145.74 ? 460  THR A CA  1 
ATOM   3626 C C   . THR A 1 461 ? -6.668  -16.276 -2.406  1.00 139.71 ? 460  THR A C   1 
ATOM   3627 O O   . THR A 1 461 ? -7.508  -16.821 -3.125  1.00 141.25 ? 460  THR A O   1 
ATOM   3628 C CB  . THR A 1 461 ? -6.050  -14.848 -4.379  1.00 150.26 ? 460  THR A CB  1 
ATOM   3629 O OG1 . THR A 1 461 ? -7.449  -14.544 -4.320  1.00 159.63 ? 460  THR A OG1 1 
ATOM   3630 C CG2 . THR A 1 461 ? -5.802  -15.883 -5.473  1.00 143.78 ? 460  THR A CG2 1 
ATOM   3631 N N   . MET A 1 462 ? -6.656  -16.421 -1.083  1.00 124.82 ? 461  MET A N   1 
ATOM   3632 C CA  . MET A 1 462 ? -7.678  -17.216 -0.407  1.00 114.07 ? 461  MET A CA  1 
ATOM   3633 C C   . MET A 1 462 ? -7.956  -16.723 1.020   1.00 104.68 ? 461  MET A C   1 
ATOM   3634 O O   . MET A 1 462 ? -7.064  -16.706 1.868   1.00 101.60 ? 461  MET A O   1 
ATOM   3635 C CB  . MET A 1 462 ? -7.292  -18.701 -0.410  1.00 108.24 ? 461  MET A CB  1 
ATOM   3636 C CG  . MET A 1 462 ? -8.463  -19.671 -0.214  1.00 108.54 ? 461  MET A CG  1 
ATOM   3637 S SD  . MET A 1 462 ? -8.000  -21.168 0.702   1.00 118.95 ? 461  MET A SD  1 
ATOM   3638 C CE  . MET A 1 462 ? -6.548  -21.710 -0.220  1.00 93.92  ? 461  MET A CE  1 
ATOM   3639 N N   . LYS A 1 463 ? -9.200  -16.316 1.266   1.00 100.73 ? 462  LYS A N   1 
ATOM   3640 C CA  . LYS A 1 463 ? -9.655  -15.878 2.585   1.00 99.27  ? 462  LYS A CA  1 
ATOM   3641 C C   . LYS A 1 463 ? -9.537  -17.006 3.633   1.00 101.08 ? 462  LYS A C   1 
ATOM   3642 O O   . LYS A 1 463 ? -9.763  -18.166 3.312   1.00 106.77 ? 462  LYS A O   1 
ATOM   3643 C CB  . LYS A 1 463 ? -11.096 -15.365 2.478   1.00 100.50 ? 462  LYS A CB  1 
ATOM   3644 C CG  . LYS A 1 463 ? -11.791 -15.642 1.116   1.00 139.30 ? 462  LYS A CG  1 
ATOM   3645 C CD  . LYS A 1 463 ? -12.330 -17.087 0.976   1.00 136.93 ? 462  LYS A CD  1 
ATOM   3646 C CE  . LYS A 1 463 ? -13.229 -17.263 -0.268  1.00 127.53 ? 462  LYS A CE  1 
ATOM   3647 N NZ  . LYS A 1 463 ? -13.719 -18.669 -0.479  1.00 111.60 ? 462  LYS A NZ  1 
ATOM   3648 N N   . ARG A 1 464 ? -9.208  -16.669 4.881   1.00 95.22  ? 463  ARG A N   1 
ATOM   3649 C CA  . ARG A 1 464 ? -8.783  -17.680 5.858   1.00 92.69  ? 463  ARG A CA  1 
ATOM   3650 C C   . ARG A 1 464 ? -9.843  -18.228 6.835   1.00 112.20 ? 463  ARG A C   1 
ATOM   3651 O O   . ARG A 1 464 ? -9.511  -18.930 7.793   1.00 131.16 ? 463  ARG A O   1 
ATOM   3652 C CB  . ARG A 1 464 ? -7.574  -17.183 6.667   1.00 82.08  ? 463  ARG A CB  1 
ATOM   3653 C CG  . ARG A 1 464 ? -6.221  -17.234 5.966   1.00 71.40  ? 463  ARG A CG  1 
ATOM   3654 C CD  . ARG A 1 464 ? -5.837  -18.603 5.429   1.00 66.08  ? 463  ARG A CD  1 
ATOM   3655 N NE  . ARG A 1 464 ? -6.268  -19.730 6.255   1.00 75.79  ? 463  ARG A NE  1 
ATOM   3656 C CZ  . ARG A 1 464 ? -5.457  -20.517 6.959   1.00 72.83  ? 463  ARG A CZ  1 
ATOM   3657 N NH1 . ARG A 1 464 ? -4.159  -20.286 6.961   1.00 62.40  ? 463  ARG A NH1 1 
ATOM   3658 N NH2 . ARG A 1 464 ? -5.950  -21.539 7.663   1.00 72.27  ? 463  ARG A NH2 1 
ATOM   3659 N N   . ILE A 1 465 ? -11.107 -17.928 6.602   1.00 113.48 ? 464  ILE A N   1 
ATOM   3660 C CA  . ILE A 1 465 ? -12.169 -18.420 7.483   1.00 131.09 ? 464  ILE A CA  1 
ATOM   3661 C C   . ILE A 1 465 ? -12.223 -17.666 8.808   1.00 139.54 ? 464  ILE A C   1 
ATOM   3662 O O   . ILE A 1 465 ? -13.303 -17.283 9.260   1.00 151.85 ? 464  ILE A O   1 
ATOM   3663 C CB  . ILE A 1 465 ? -12.104 -19.959 7.726   1.00 76.34  ? 464  ILE A CB  1 
ATOM   3664 C CG1 . ILE A 1 465 ? -12.435 -20.721 6.436   1.00 81.63  ? 464  ILE A CG1 1 
ATOM   3665 C CG2 . ILE A 1 465 ? -13.081 -20.402 8.842   1.00 64.77  ? 464  ILE A CG2 1 
ATOM   3666 C CD1 . ILE A 1 465 ? -13.003 -22.119 6.650   1.00 64.75  ? 464  ILE A CD1 1 
ATOM   3667 N N   . GLU A 1 466 ? -11.068 -17.436 9.419   1.00 131.90 ? 465  GLU A N   1 
ATOM   3668 C CA  . GLU A 1 466 ? -11.034 -16.698 10.676  1.00 139.86 ? 465  GLU A CA  1 
ATOM   3669 C C   . GLU A 1 466 ? -11.708 -17.510 11.765  1.00 126.51 ? 465  GLU A C   1 
ATOM   3670 O O   . GLU A 1 466 ? -12.858 -17.937 11.635  1.00 111.72 ? 465  GLU A O   1 
ATOM   3671 C CB  . GLU A 1 466 ? -11.729 -15.339 10.544  1.00 157.32 ? 465  GLU A CB  1 
ATOM   3672 C CG  . GLU A 1 466 ? -10.953 -14.297 9.752   1.00 171.64 ? 465  GLU A CG  1 
ATOM   3673 C CD  . GLU A 1 466 ? -11.679 -12.962 9.694   1.00 186.25 ? 465  GLU A CD  1 
ATOM   3674 O OE1 . GLU A 1 466 ? -12.727 -12.823 10.364  1.00 188.94 ? 465  GLU A OE1 1 
ATOM   3675 O OE2 . GLU A 1 466 ? -11.204 -12.053 8.978   1.00 191.57 ? 465  GLU A OE2 1 
ATOM   3676 N N   . ARG A 1 467 ? -10.985 -17.721 12.852  1.00 120.80 ? 466  ARG A N   1 
ATOM   3677 C CA  . ARG A 1 467 ? -11.451 -18.628 13.880  1.00 105.75 ? 466  ARG A CA  1 
ATOM   3678 C C   . ARG A 1 467 ? -11.203 -18.014 15.245  1.00 109.53 ? 466  ARG A C   1 
ATOM   3679 O O   . ARG A 1 467 ? -10.476 -17.026 15.377  1.00 102.27 ? 466  ARG A O   1 
ATOM   3680 C CB  . ARG A 1 467 ? -10.716 -19.967 13.742  1.00 86.44  ? 466  ARG A CB  1 
ATOM   3681 C CG  . ARG A 1 467 ? -10.510 -20.377 12.289  1.00 77.30  ? 466  ARG A CG  1 
ATOM   3682 C CD  . ARG A 1 467 ? -9.773  -21.676 12.148  1.00 82.43  ? 466  ARG A CD  1 
ATOM   3683 N NE  . ARG A 1 467 ? -9.975  -22.255 10.824  1.00 91.28  ? 466  ARG A NE  1 
ATOM   3684 C CZ  . ARG A 1 467 ? -10.995 -23.047 10.505  1.00 87.97  ? 466  ARG A CZ  1 
ATOM   3685 N NH1 . ARG A 1 467 ? -11.101 -23.538 9.278   1.00 82.82  ? 466  ARG A NH1 1 
ATOM   3686 N NH2 . ARG A 1 467 ? -11.910 -23.351 11.415  1.00 90.34  ? 466  ARG A NH2 1 
ATOM   3687 N N   . ASP A 1 468 ? -11.829 -18.586 16.263  1.00 119.91 ? 467  ASP A N   1 
ATOM   3688 C CA  . ASP A 1 468 ? -11.508 -18.204 17.623  1.00 125.26 ? 467  ASP A CA  1 
ATOM   3689 C C   . ASP A 1 468 ? -10.350 -19.076 18.087  1.00 104.02 ? 467  ASP A C   1 
ATOM   3690 O O   . ASP A 1 468 ? -10.510 -20.285 18.271  1.00 90.36  ? 467  ASP A O   1 
ATOM   3691 C CB  . ASP A 1 468 ? -12.712 -18.390 18.544  1.00 137.68 ? 467  ASP A CB  1 
ATOM   3692 C CG  . ASP A 1 468 ? -12.374 -18.124 19.997  1.00 141.37 ? 467  ASP A CG  1 
ATOM   3693 O OD1 . ASP A 1 468 ? -11.785 -17.050 20.276  1.00 141.85 ? 467  ASP A OD1 1 
ATOM   3694 O OD2 . ASP A 1 468 ? -12.687 -18.991 20.850  1.00 133.34 ? 467  ASP A OD2 1 
ATOM   3695 N N   . MET A 1 469 ? -9.184  -18.463 18.251  1.00 97.76  ? 468  MET A N   1 
ATOM   3696 C CA  . MET A 1 469 ? -8.010  -19.184 18.725  1.00 97.08  ? 468  MET A CA  1 
ATOM   3697 C C   . MET A 1 469 ? -7.594  -18.652 20.097  1.00 94.74  ? 468  MET A C   1 
ATOM   3698 O O   . MET A 1 469 ? -6.879  -17.643 20.201  1.00 84.62  ? 468  MET A O   1 
ATOM   3699 C CB  . MET A 1 469 ? -6.858  -19.089 17.714  1.00 91.60  ? 468  MET A CB  1 
ATOM   3700 C CG  . MET A 1 469 ? -7.189  -19.593 16.303  1.00 77.31  ? 468  MET A CG  1 
ATOM   3701 S SD  . MET A 1 469 ? -7.680  -21.332 16.162  1.00 100.97 ? 468  MET A SD  1 
ATOM   3702 C CE  . MET A 1 469 ? -6.147  -22.221 16.384  1.00 72.89  ? 468  MET A CE  1 
ATOM   3703 N N   . PRO A 1 470 ? -8.061  -19.334 21.154  1.00 91.97  ? 469  PRO A N   1 
ATOM   3704 C CA  . PRO A 1 470 ? -7.840  -19.014 22.569  1.00 97.65  ? 469  PRO A CA  1 
ATOM   3705 C C   . PRO A 1 470 ? -6.359  -19.061 22.983  1.00 87.22  ? 469  PRO A C   1 
ATOM   3706 O O   . PRO A 1 470 ? -5.782  -18.028 23.329  1.00 92.52  ? 469  PRO A O   1 
ATOM   3707 C CB  . PRO A 1 470 ? -8.630  -20.113 23.300  1.00 101.35 ? 469  PRO A CB  1 
ATOM   3708 C CG  . PRO A 1 470 ? -8.699  -21.262 22.325  1.00 83.58  ? 469  PRO A CG  1 
ATOM   3709 C CD  . PRO A 1 470 ? -8.815  -20.590 20.980  1.00 84.29  ? 469  PRO A CD  1 
ATOM   3710 N N   . TYR A 1 471 ? -5.768  -20.252 22.956  1.00 74.43  ? 470  TYR A N   1 
ATOM   3711 C CA  . TYR A 1 471 ? -4.368  -20.452 23.328  1.00 81.82  ? 470  TYR A CA  1 
ATOM   3712 C C   . TYR A 1 471 ? -3.403  -19.500 22.593  1.00 79.11  ? 470  TYR A C   1 
ATOM   3713 O O   . TYR A 1 471 ? -3.425  -19.426 21.364  1.00 80.81  ? 470  TYR A O   1 
ATOM   3714 C CB  . TYR A 1 471 ? -3.963  -21.904 23.046  1.00 72.06  ? 470  TYR A CB  1 
ATOM   3715 C CG  . TYR A 1 471 ? -4.709  -22.960 23.844  1.00 83.05  ? 470  TYR A CG  1 
ATOM   3716 C CD1 . TYR A 1 471 ? -4.298  -23.309 25.125  1.00 77.95  ? 470  TYR A CD1 1 
ATOM   3717 C CD2 . TYR A 1 471 ? -5.802  -23.639 23.298  1.00 91.91  ? 470  TYR A CD2 1 
ATOM   3718 C CE1 . TYR A 1 471 ? -4.957  -24.292 25.846  1.00 88.91  ? 470  TYR A CE1 1 
ATOM   3719 C CE2 . TYR A 1 471 ? -6.470  -24.623 24.010  1.00 88.94  ? 470  TYR A CE2 1 
ATOM   3720 C CZ  . TYR A 1 471 ? -6.045  -24.942 25.290  1.00 100.70 ? 470  TYR A CZ  1 
ATOM   3721 O OH  . TYR A 1 471 ? -6.705  -25.912 26.021  1.00 113.81 ? 470  TYR A OH  1 
ATOM   3722 N N   . VAL A 1 472 ? -2.541  -18.794 23.327  1.00 67.04  ? 471  VAL A N   1 
ATOM   3723 C CA  . VAL A 1 472 ? -1.680  -17.792 22.675  1.00 74.22  ? 471  VAL A CA  1 
ATOM   3724 C C   . VAL A 1 472 ? -0.500  -18.339 21.863  1.00 60.57  ? 471  VAL A C   1 
ATOM   3725 O O   . VAL A 1 472 ? 0.019   -17.632 21.010  1.00 71.61  ? 471  VAL A O   1 
ATOM   3726 C CB  . VAL A 1 472 ? -1.195  -16.656 23.623  1.00 81.02  ? 471  VAL A CB  1 
ATOM   3727 C CG1 . VAL A 1 472 ? -2.358  -15.759 24.008  1.00 85.47  ? 471  VAL A CG1 1 
ATOM   3728 C CG2 . VAL A 1 472 ? -0.500  -17.216 24.851  1.00 85.96  ? 471  VAL A CG2 1 
ATOM   3729 N N   . LEU A 1 473 ? -0.088  -19.577 22.125  1.00 47.27  ? 472  LEU A N   1 
ATOM   3730 C CA  . LEU A 1 473 ? 0.936   -20.254 21.313  1.00 50.15  ? 472  LEU A CA  1 
ATOM   3731 C C   . LEU A 1 473 ? 0.345   -21.179 20.245  1.00 54.15  ? 472  LEU A C   1 
ATOM   3732 O O   . LEU A 1 473 ? 1.062   -21.936 19.583  1.00 62.04  ? 472  LEU A O   1 
ATOM   3733 C CB  . LEU A 1 473 ? 1.898   -21.034 22.200  1.00 47.13  ? 472  LEU A CB  1 
ATOM   3734 C CG  . LEU A 1 473 ? 2.595   -20.168 23.261  1.00 56.08  ? 472  LEU A CG  1 
ATOM   3735 C CD1 . LEU A 1 473 ? 3.391   -21.028 24.236  1.00 55.54  ? 472  LEU A CD1 1 
ATOM   3736 C CD2 . LEU A 1 473 ? 3.488   -19.133 22.615  1.00 48.97  ? 472  LEU A CD2 1 
ATOM   3737 N N   . SER A 1 474 ? -0.966  -21.104 20.068  1.00 49.24  ? 473  SER A N   1 
ATOM   3738 C CA  . SER A 1 474 ? -1.643  -21.965 19.112  1.00 60.70  ? 473  SER A CA  1 
ATOM   3739 C C   . SER A 1 474 ? -2.621  -21.157 18.283  1.00 74.68  ? 473  SER A C   1 
ATOM   3740 O O   . SER A 1 474 ? -3.811  -21.462 18.269  1.00 74.50  ? 473  SER A O   1 
ATOM   3741 C CB  . SER A 1 474 ? -2.394  -23.083 19.837  1.00 54.57  ? 473  SER A CB  1 
ATOM   3742 O OG  . SER A 1 474 ? -1.540  -23.787 20.723  1.00 60.81  ? 473  SER A OG  1 
ATOM   3743 N N   . ARG A 1 475 ? -2.126  -20.125 17.603  1.00 70.91  ? 474  ARG A N   1 
ATOM   3744 C CA  . ARG A 1 475 ? -2.992  -19.231 16.841  1.00 62.11  ? 474  ARG A CA  1 
ATOM   3745 C C   . ARG A 1 475 ? -3.022  -19.589 15.361  1.00 64.03  ? 474  ARG A C   1 
ATOM   3746 O O   . ARG A 1 475 ? -3.915  -19.172 14.629  1.00 67.94  ? 474  ARG A O   1 
ATOM   3747 C CB  . ARG A 1 475 ? -2.544  -17.785 17.028  1.00 62.51  ? 474  ARG A CB  1 
ATOM   3748 C CG  . ARG A 1 475 ? -2.031  -17.510 18.418  1.00 54.04  ? 474  ARG A CG  1 
ATOM   3749 C CD  . ARG A 1 475 ? -2.024  -16.044 18.726  1.00 59.52  ? 474  ARG A CD  1 
ATOM   3750 N NE  . ARG A 1 475 ? -1.279  -15.225 17.765  1.00 58.90  ? 474  ARG A NE  1 
ATOM   3751 C CZ  . ARG A 1 475 ? 0.040   -15.069 17.775  1.00 70.01  ? 474  ARG A CZ  1 
ATOM   3752 N NH1 . ARG A 1 475 ? 0.799   -15.701 18.670  1.00 66.43  ? 474  ARG A NH1 1 
ATOM   3753 N NH2 . ARG A 1 475 ? 0.607   -14.296 16.865  1.00 78.56  ? 474  ARG A NH2 1 
ATOM   3754 N N   . TRP A 1 476 ? -2.042  -20.374 14.928  1.00 65.42  ? 475  TRP A N   1 
ATOM   3755 C CA  . TRP A 1 476 ? -1.965  -20.813 13.540  1.00 59.57  ? 475  TRP A CA  1 
ATOM   3756 C C   . TRP A 1 476 ? -2.875  -22.014 13.242  1.00 64.07  ? 475  TRP A C   1 
ATOM   3757 O O   . TRP A 1 476 ? -2.939  -22.975 14.010  1.00 61.99  ? 475  TRP A O   1 
ATOM   3758 C CB  . TRP A 1 476 ? -0.512  -21.126 13.158  1.00 56.64  ? 475  TRP A CB  1 
ATOM   3759 C CG  . TRP A 1 476 ? -0.384  -21.804 11.838  1.00 46.24  ? 475  TRP A CG  1 
ATOM   3760 C CD1 . TRP A 1 476 ? -0.155  -23.123 11.622  1.00 44.22  ? 475  TRP A CD1 1 
ATOM   3761 C CD2 . TRP A 1 476 ? -0.485  -21.196 10.542  1.00 59.16  ? 475  TRP A CD2 1 
ATOM   3762 N NE1 . TRP A 1 476 ? -0.114  -23.387 10.274  1.00 54.00  ? 475  TRP A NE1 1 
ATOM   3763 C CE2 . TRP A 1 476 ? -0.311  -22.219 9.588   1.00 59.17  ? 475  TRP A CE2 1 
ATOM   3764 C CE3 . TRP A 1 476 ? -0.714  -19.887 10.096  1.00 60.85  ? 475  TRP A CE3 1 
ATOM   3765 C CZ2 . TRP A 1 476 ? -0.359  -21.976 8.216   1.00 57.10  ? 475  TRP A CZ2 1 
ATOM   3766 C CZ3 . TRP A 1 476 ? -0.768  -19.651 8.739   1.00 55.42  ? 475  TRP A CZ3 1 
ATOM   3767 C CH2 . TRP A 1 476 ? -0.591  -20.691 7.813   1.00 62.09  ? 475  TRP A CH2 1 
ATOM   3768 N N   . THR A 1 477 ? -3.572  -21.932 12.114  1.00 67.63  ? 476  THR A N   1 
ATOM   3769 C CA  . THR A 1 477 ? -4.416  -23.004 11.610  1.00 66.09  ? 476  THR A CA  1 
ATOM   3770 C C   . THR A 1 477 ? -3.886  -23.396 10.237  1.00 74.33  ? 476  THR A C   1 
ATOM   3771 O O   . THR A 1 477 ? -3.758  -22.542 9.371   1.00 76.94  ? 476  THR A O   1 
ATOM   3772 C CB  . THR A 1 477 ? -5.865  -22.508 11.406  1.00 63.95  ? 476  THR A CB  1 
ATOM   3773 O OG1 . THR A 1 477 ? -6.380  -21.962 12.628  1.00 77.10  ? 476  THR A OG1 1 
ATOM   3774 C CG2 . THR A 1 477 ? -6.753  -23.626 10.923  1.00 53.69  ? 476  THR A CG2 1 
ATOM   3775 N N   . PRO A 1 478 ? -3.583  -24.684 10.024  1.00 67.35  ? 477  PRO A N   1 
ATOM   3776 C CA  . PRO A 1 478 ? -3.135  -25.122 8.699   1.00 69.74  ? 477  PRO A CA  1 
ATOM   3777 C C   . PRO A 1 478 ? -4.138  -24.796 7.592   1.00 76.63  ? 477  PRO A C   1 
ATOM   3778 O O   . PRO A 1 478 ? -5.353  -24.966 7.737   1.00 76.01  ? 477  PRO A O   1 
ATOM   3779 C CB  . PRO A 1 478 ? -3.006  -26.640 8.862   1.00 67.19  ? 477  PRO A CB  1 
ATOM   3780 C CG  . PRO A 1 478 ? -2.747  -26.838 10.298  1.00 59.57  ? 477  PRO A CG  1 
ATOM   3781 C CD  . PRO A 1 478 ? -3.581  -25.793 10.989  1.00 60.69  ? 477  PRO A CD  1 
ATOM   3782 N N   . ILE A 1 479 ? -3.604  -24.335 6.471   1.00 69.56  ? 478  ILE A N   1 
ATOM   3783 C CA  . ILE A 1 479 ? -4.412  -23.946 5.332   1.00 59.85  ? 478  ILE A CA  1 
ATOM   3784 C C   . ILE A 1 479 ? -5.312  -25.083 4.900   1.00 71.92  ? 478  ILE A C   1 
ATOM   3785 O O   . ILE A 1 479 ? -6.455  -24.867 4.490   1.00 87.38  ? 478  ILE A O   1 
ATOM   3786 C CB  . ILE A 1 479 ? -3.510  -23.497 4.164   1.00 60.97  ? 478  ILE A CB  1 
ATOM   3787 C CG1 . ILE A 1 479 ? -3.064  -22.055 4.379   1.00 52.22  ? 478  ILE A CG1 1 
ATOM   3788 C CG2 . ILE A 1 479 ? -4.233  -23.582 2.824   1.00 59.15  ? 478  ILE A CG2 1 
ATOM   3789 C CD1 . ILE A 1 479 ? -2.298  -21.561 3.244   1.00 62.14  ? 478  ILE A CD1 1 
ATOM   3790 N N   . VAL A 1 480 ? -4.796  -26.300 5.004   1.00 74.77  ? 479  VAL A N   1 
ATOM   3791 C CA  . VAL A 1 480 ? -5.534  -27.464 4.551   1.00 73.38  ? 479  VAL A CA  1 
ATOM   3792 C C   . VAL A 1 480 ? -6.880  -27.598 5.287   1.00 68.47  ? 479  VAL A C   1 
ATOM   3793 O O   . VAL A 1 480 ? -7.819  -28.195 4.772   1.00 60.54  ? 479  VAL A O   1 
ATOM   3794 C CB  . VAL A 1 480 ? -4.674  -28.754 4.640   1.00 70.76  ? 479  VAL A CB  1 
ATOM   3795 C CG1 . VAL A 1 480 ? -4.998  -29.569 5.904   1.00 68.40  ? 479  VAL A CG1 1 
ATOM   3796 C CG2 . VAL A 1 480 ? -4.847  -29.588 3.387   1.00 70.25  ? 479  VAL A CG2 1 
ATOM   3797 N N   . LYS A 1 481 ? -6.990  -27.015 6.475   1.00 65.41  ? 480  LYS A N   1 
ATOM   3798 C CA  . LYS A 1 481 ? -8.250  -27.106 7.202   1.00 74.97  ? 480  LYS A CA  1 
ATOM   3799 C C   . LYS A 1 481 ? -9.313  -26.274 6.510   1.00 73.56  ? 480  LYS A C   1 
ATOM   3800 O O   . LYS A 1 481 ? -10.470 -26.692 6.398   1.00 70.33  ? 480  LYS A O   1 
ATOM   3801 C CB  . LYS A 1 481 ? -8.108  -26.649 8.654   1.00 71.64  ? 480  LYS A CB  1 
ATOM   3802 C CG  . LYS A 1 481 ? -9.279  -27.069 9.518   1.00 57.09  ? 480  LYS A CG  1 
ATOM   3803 C CD  . LYS A 1 481 ? -9.290  -26.342 10.830  1.00 60.13  ? 480  LYS A CD  1 
ATOM   3804 C CE  . LYS A 1 481 ? -10.073 -27.141 11.861  1.00 64.20  ? 480  LYS A CE  1 
ATOM   3805 N NZ  . LYS A 1 481 ? -10.213 -26.388 13.134  1.00 68.45  ? 480  LYS A NZ  1 
ATOM   3806 N N   . ASP A 1 482 ? -8.908  -25.091 6.060   1.00 68.78  ? 481  ASP A N   1 
ATOM   3807 C CA  . ASP A 1 482 ? -9.791  -24.202 5.317   1.00 75.05  ? 481  ASP A CA  1 
ATOM   3808 C C   . ASP A 1 482 ? -10.230 -24.832 3.991   1.00 73.82  ? 481  ASP A C   1 
ATOM   3809 O O   . ASP A 1 482 ? -11.397 -24.750 3.616   1.00 71.74  ? 481  ASP A O   1 
ATOM   3810 C CB  . ASP A 1 482 ? -9.142  -22.825 5.128   1.00 68.73  ? 481  ASP A CB  1 
ATOM   3811 C CG  . ASP A 1 482 ? -8.924  -22.105 6.452   1.00 87.57  ? 481  ASP A CG  1 
ATOM   3812 O OD1 . ASP A 1 482 ? -9.148  -22.721 7.512   1.00 105.79 ? 481  ASP A OD1 1 
ATOM   3813 O OD2 . ASP A 1 482 ? -8.531  -20.927 6.453   1.00 82.97  ? 481  ASP A OD2 1 
ATOM   3814 N N   . LEU A 1 483 ? -9.304  -25.481 3.296   1.00 72.74  ? 482  LEU A N   1 
ATOM   3815 C CA  . LEU A 1 483 ? -9.675  -26.275 2.128   1.00 84.46  ? 482  LEU A CA  1 
ATOM   3816 C C   . LEU A 1 483 ? -10.751 -27.308 2.456   1.00 91.41  ? 482  LEU A C   1 
ATOM   3817 O O   . LEU A 1 483 ? -11.728 -27.445 1.720   1.00 105.38 ? 482  LEU A O   1 
ATOM   3818 C CB  . LEU A 1 483 ? -8.456  -26.982 1.542   1.00 85.88  ? 482  LEU A CB  1 
ATOM   3819 C CG  . LEU A 1 483 ? -7.822  -26.243 0.376   1.00 79.51  ? 482  LEU A CG  1 
ATOM   3820 C CD1 . LEU A 1 483 ? -7.949  -24.773 0.645   1.00 80.49  ? 482  LEU A CD1 1 
ATOM   3821 C CD2 . LEU A 1 483 ? -6.376  -26.656 0.216   1.00 80.36  ? 482  LEU A CD2 1 
ATOM   3822 N N   . MET A 1 484 ? -10.562 -28.039 3.553   1.00 78.50  ? 483  MET A N   1 
ATOM   3823 C CA  . MET A 1 484 ? -11.530 -29.044 3.987   1.00 80.44  ? 483  MET A CA  1 
ATOM   3824 C C   . MET A 1 484 ? -12.923 -28.458 4.209   1.00 85.15  ? 483  MET A C   1 
ATOM   3825 O O   . MET A 1 484 ? -13.885 -28.899 3.584   1.00 83.17  ? 483  MET A O   1 
ATOM   3826 C CB  . MET A 1 484 ? -11.052 -29.749 5.261   1.00 82.38  ? 483  MET A CB  1 
ATOM   3827 C CG  . MET A 1 484 ? -9.933  -30.749 5.030   1.00 82.43  ? 483  MET A CG  1 
ATOM   3828 S SD  . MET A 1 484 ? -9.070  -31.188 6.545   1.00 79.13  ? 483  MET A SD  1 
ATOM   3829 C CE  . MET A 1 484 ? -7.696  -32.107 5.876   1.00 70.18  ? 483  MET A CE  1 
ATOM   3830 N N   . GLU A 1 485 ? -13.020 -27.467 5.096   1.00 89.29  ? 484  GLU A N   1 
ATOM   3831 C CA  . GLU A 1 485 ? -14.299 -26.853 5.456   1.00 81.22  ? 484  GLU A CA  1 
ATOM   3832 C C   . GLU A 1 485 ? -15.004 -26.183 4.278   1.00 92.11  ? 484  GLU A C   1 
ATOM   3833 O O   . GLU A 1 485 ? -16.223 -26.295 4.131   1.00 100.56 ? 484  GLU A O   1 
ATOM   3834 C CB  . GLU A 1 485 ? -14.127 -25.859 6.603   1.00 72.78  ? 484  GLU A CB  1 
ATOM   3835 C CG  . GLU A 1 485 ? -13.856 -26.510 7.946   1.00 85.26  ? 484  GLU A CG  1 
ATOM   3836 C CD  . GLU A 1 485 ? -13.658 -25.494 9.052   1.00 99.63  ? 484  GLU A CD  1 
ATOM   3837 O OE1 . GLU A 1 485 ? -13.883 -24.297 8.794   1.00 110.71 ? 484  GLU A OE1 1 
ATOM   3838 O OE2 . GLU A 1 485 ? -13.283 -25.883 10.179  1.00 101.64 ? 484  GLU A OE2 1 
ATOM   3839 N N   . TYR A 1 486 ? -14.247 -25.489 3.437   1.00 89.24  ? 485  TYR A N   1 
ATOM   3840 C CA  . TYR A 1 486 ? -14.835 -24.904 2.235   1.00 86.97  ? 485  TYR A CA  1 
ATOM   3841 C C   . TYR A 1 486 ? -15.524 -25.972 1.385   1.00 90.85  ? 485  TYR A C   1 
ATOM   3842 O O   . TYR A 1 486 ? -16.652 -25.778 0.950   1.00 95.77  ? 485  TYR A O   1 
ATOM   3843 C CB  . TYR A 1 486 ? -13.787 -24.158 1.412   1.00 83.71  ? 485  TYR A CB  1 
ATOM   3844 C CG  . TYR A 1 486 ? -13.402 -22.810 1.985   1.00 90.28  ? 485  TYR A CG  1 
ATOM   3845 C CD1 . TYR A 1 486 ? -14.342 -22.014 2.634   1.00 90.60  ? 485  TYR A CD1 1 
ATOM   3846 C CD2 . TYR A 1 486 ? -12.102 -22.324 1.860   1.00 84.40  ? 485  TYR A CD2 1 
ATOM   3847 C CE1 . TYR A 1 486 ? -13.995 -20.774 3.152   1.00 87.36  ? 485  TYR A CE1 1 
ATOM   3848 C CE2 . TYR A 1 486 ? -11.747 -21.092 2.369   1.00 85.55  ? 485  TYR A CE2 1 
ATOM   3849 C CZ  . TYR A 1 486 ? -12.697 -20.314 3.011   1.00 93.44  ? 485  TYR A CZ  1 
ATOM   3850 O OH  . TYR A 1 486 ? -12.344 -19.076 3.513   1.00 92.78  ? 485  TYR A OH  1 
ATOM   3851 N N   . ILE A 1 487 ? -14.842 -27.095 1.165   1.00 92.27  ? 486  ILE A N   1 
ATOM   3852 C CA  . ILE A 1 487 ? -15.381 -28.206 0.377   1.00 90.63  ? 486  ILE A CA  1 
ATOM   3853 C C   . ILE A 1 487 ? -16.587 -28.854 1.050   1.00 100.59 ? 486  ILE A C   1 
ATOM   3854 O O   . ILE A 1 487 ? -17.519 -29.302 0.377   1.00 110.11 ? 486  ILE A O   1 
ATOM   3855 C CB  . ILE A 1 487 ? -14.315 -29.287 0.121   1.00 84.68  ? 486  ILE A CB  1 
ATOM   3856 C CG1 . ILE A 1 487 ? -13.286 -28.790 -0.890  1.00 85.27  ? 486  ILE A CG1 1 
ATOM   3857 C CG2 . ILE A 1 487 ? -14.959 -30.574 -0.380  1.00 80.51  ? 486  ILE A CG2 1 
ATOM   3858 C CD1 . ILE A 1 487 ? -12.153 -29.755 -1.129  1.00 80.76  ? 486  ILE A CD1 1 
ATOM   3859 N N   . ALA A 1 488 ? -16.571 -28.896 2.377   1.00 105.04 ? 487  ALA A N   1 
ATOM   3860 C CA  . ALA A 1 488 ? -17.697 -29.432 3.139   1.00 117.96 ? 487  ALA A CA  1 
ATOM   3861 C C   . ALA A 1 488 ? -18.879 -28.463 3.131   1.00 121.94 ? 487  ALA A C   1 
ATOM   3862 O O   . ALA A 1 488 ? -19.784 -28.566 3.956   1.00 119.80 ? 487  ALA A O   1 
ATOM   3863 C CB  . ALA A 1 488 ? -17.274 -29.745 4.574   1.00 115.06 ? 487  ALA A CB  1 
ATOM   3864 N N   . THR A 1 489 ? -18.861 -27.530 2.185   1.00 124.51 ? 488  THR A N   1 
ATOM   3865 C CA  . THR A 1 489 ? -19.833 -26.449 2.124   1.00 121.20 ? 488  THR A CA  1 
ATOM   3866 C C   . THR A 1 489 ? -19.884 -25.931 0.687   1.00 120.51 ? 488  THR A C   1 
ATOM   3867 O O   . THR A 1 489 ? -20.334 -24.815 0.423   1.00 124.51 ? 488  THR A O   1 
ATOM   3868 C CB  . THR A 1 489 ? -19.441 -25.318 3.106   1.00 119.21 ? 488  THR A CB  1 
ATOM   3869 O OG1 . THR A 1 489 ? -19.403 -25.845 4.438   1.00 100.46 ? 488  THR A OG1 1 
ATOM   3870 C CG2 . THR A 1 489 ? -20.437 -24.169 3.059   1.00 134.20 ? 488  THR A CG2 1 
ATOM   3871 N N   . GLY A 1 490 ? -19.413 -26.765 -0.238  1.00 118.82 ? 489  GLY A N   1 
ATOM   3872 C CA  . GLY A 1 490 ? -19.298 -26.399 -1.639  1.00 124.18 ? 489  GLY A CA  1 
ATOM   3873 C C   . GLY A 1 490 ? -18.793 -24.985 -1.869  1.00 131.27 ? 489  GLY A C   1 
ATOM   3874 O O   . GLY A 1 490 ? -18.983 -24.422 -2.944  1.00 146.56 ? 489  GLY A O   1 
ATOM   3875 N N   . GLN A 1 491 ? -18.131 -24.415 -0.868  1.00 120.48 ? 490  GLN A N   1 
ATOM   3876 C CA  . GLN A 1 491 ? -17.785 -23.001 -0.884  1.00 118.48 ? 490  GLN A CA  1 
ATOM   3877 C C   . GLN A 1 491 ? -16.383 -22.732 -1.439  1.00 114.51 ? 490  GLN A C   1 
ATOM   3878 O O   . GLN A 1 491 ? -15.834 -21.641 -1.257  1.00 120.79 ? 490  GLN A O   1 
ATOM   3879 C CB  . GLN A 1 491 ? -17.916 -22.425 0.530   1.00 127.37 ? 490  GLN A CB  1 
ATOM   3880 C CG  . GLN A 1 491 ? -18.323 -20.965 0.575   1.00 138.78 ? 490  GLN A CG  1 
ATOM   3881 C CD  . GLN A 1 491 ? -19.700 -20.731 -0.024  1.00 150.39 ? 490  GLN A CD  1 
ATOM   3882 O OE1 . GLN A 1 491 ? -20.564 -21.614 0.009   1.00 146.00 ? 490  GLN A OE1 1 
ATOM   3883 N NE2 . GLN A 1 491 ? -19.913 -19.534 -0.573  1.00 154.88 ? 490  GLN A NE2 1 
ATOM   3884 N N   . LEU A 1 492 ? -15.808 -23.719 -2.121  1.00 105.49 ? 491  LEU A N   1 
ATOM   3885 C CA  . LEU A 1 492 ? -14.453 -23.589 -2.651  1.00 99.98  ? 491  LEU A CA  1 
ATOM   3886 C C   . LEU A 1 492 ? -14.461 -23.344 -4.159  1.00 101.27 ? 491  LEU A C   1 
ATOM   3887 O O   . LEU A 1 492 ? -14.648 -24.278 -4.940  1.00 95.94  ? 491  LEU A O   1 
ATOM   3888 C CB  . LEU A 1 492 ? -13.630 -24.843 -2.321  1.00 95.82  ? 491  LEU A CB  1 
ATOM   3889 C CG  . LEU A 1 492 ? -12.150 -24.887 -2.723  1.00 84.78  ? 491  LEU A CG  1 
ATOM   3890 C CD1 . LEU A 1 492 ? -11.310 -24.065 -1.773  1.00 70.66  ? 491  LEU A CD1 1 
ATOM   3891 C CD2 . LEU A 1 492 ? -11.646 -26.318 -2.751  1.00 86.61  ? 491  LEU A CD2 1 
ATOM   3892 N N   . ASP A 1 493 ? -14.253 -22.085 -4.552  1.00 109.85 ? 492  ASP A N   1 
ATOM   3893 C CA  . ASP A 1 493 ? -14.207 -21.669 -5.961  1.00 120.97 ? 492  ASP A CA  1 
ATOM   3894 C C   . ASP A 1 493 ? -13.764 -22.766 -6.916  1.00 124.27 ? 492  ASP A C   1 
ATOM   3895 O O   . ASP A 1 493 ? -12.809 -23.491 -6.639  1.00 124.84 ? 492  ASP A O   1 
ATOM   3896 C CB  . ASP A 1 493 ? -13.250 -20.483 -6.148  1.00 126.87 ? 492  ASP A CB  1 
ATOM   3897 C CG  . ASP A 1 493 ? -13.738 -19.222 -5.476  1.00 135.95 ? 492  ASP A CG  1 
ATOM   3898 O OD1 . ASP A 1 493 ? -14.774 -19.276 -4.780  1.00 148.69 ? 492  ASP A OD1 1 
ATOM   3899 O OD2 . ASP A 1 493 ? -13.080 -18.175 -5.644  1.00 129.03 ? 492  ASP A OD2 1 
ATOM   3900 N N   . LEU A 1 494 ? -14.439 -22.867 -8.057  1.00 126.27 ? 493  LEU A N   1 
ATOM   3901 C CA  . LEU A 1 494 ? -13.993 -23.775 -9.106  1.00 119.87 ? 493  LEU A CA  1 
ATOM   3902 C C   . LEU A 1 494 ? -12.829 -23.182 -9.896  1.00 124.77 ? 493  LEU A C   1 
ATOM   3903 O O   . LEU A 1 494 ? -12.108 -23.904 -10.581 1.00 122.41 ? 493  LEU A O   1 
ATOM   3904 C CB  . LEU A 1 494 ? -15.140 -24.143 -10.042 1.00 108.20 ? 493  LEU A CB  1 
ATOM   3905 C CG  . LEU A 1 494 ? -16.124 -25.152 -9.462  1.00 116.22 ? 493  LEU A CG  1 
ATOM   3906 C CD1 . LEU A 1 494 ? -16.849 -24.557 -8.270  1.00 122.55 ? 493  LEU A CD1 1 
ATOM   3907 C CD2 . LEU A 1 494 ? -17.116 -25.587 -10.526 1.00 124.59 ? 493  LEU A CD2 1 
ATOM   3908 N N   . GLU A 1 495 ? -12.651 -21.865 -9.794  1.00 128.78 ? 494  GLU A N   1 
ATOM   3909 C CA  . GLU A 1 495 ? -11.556 -21.186 -10.481 1.00 129.98 ? 494  GLU A CA  1 
ATOM   3910 C C   . GLU A 1 495 ? -10.271 -21.364 -9.696  1.00 120.18 ? 494  GLU A C   1 
ATOM   3911 O O   . GLU A 1 495 ? -9.179  -21.424 -10.264 1.00 114.04 ? 494  GLU A O   1 
ATOM   3912 C CB  . GLU A 1 495 ? -11.858 -19.692 -10.689 1.00 143.41 ? 494  GLU A CB  1 
ATOM   3913 C CG  . GLU A 1 495 ? -12.739 -19.049 -9.618  1.00 153.95 ? 494  GLU A CG  1 
ATOM   3914 C CD  . GLU A 1 495 ? -14.216 -18.992 -10.014 1.00 162.30 ? 494  GLU A CD  1 
ATOM   3915 O OE1 . GLU A 1 495 ? -14.595 -19.632 -11.021 1.00 164.88 ? 494  GLU A OE1 1 
ATOM   3916 O OE2 . GLU A 1 495 ? -14.999 -18.306 -9.318  1.00 160.16 ? 494  GLU A OE2 1 
ATOM   3917 N N   . SER A 1 496 ? -10.418 -21.460 -8.380  1.00 117.43 ? 495  SER A N   1 
ATOM   3918 C CA  . SER A 1 496 ? -9.283  -21.633 -7.488  1.00 98.33  ? 495  SER A CA  1 
ATOM   3919 C C   . SER A 1 496 ? -8.882  -23.108 -7.398  1.00 93.10  ? 495  SER A C   1 
ATOM   3920 O O   . SER A 1 496 ? -7.700  -23.437 -7.381  1.00 90.19  ? 495  SER A O   1 
ATOM   3921 C CB  . SER A 1 496 ? -9.631  -21.091 -6.107  1.00 89.48  ? 495  SER A CB  1 
ATOM   3922 O OG  . SER A 1 496 ? -8.459  -20.706 -5.421  1.00 89.18  ? 495  SER A OG  1 
ATOM   3923 N N   . TYR A 1 497 ? -9.880  -23.988 -7.344  1.00 90.40  ? 496  TYR A N   1 
ATOM   3924 C CA  . TYR A 1 497 ? -9.653  -25.429 -7.300  1.00 87.60  ? 496  TYR A CA  1 
ATOM   3925 C C   . TYR A 1 497 ? -10.654 -26.153 -8.209  1.00 90.99  ? 496  TYR A C   1 
ATOM   3926 O O   . TYR A 1 497 ? -11.710 -26.608 -7.755  1.00 89.40  ? 496  TYR A O   1 
ATOM   3927 C CB  . TYR A 1 497 ? -9.736  -25.954 -5.854  1.00 86.04  ? 496  TYR A CB  1 
ATOM   3928 C CG  . TYR A 1 497 ? -8.569  -25.535 -4.980  1.00 85.59  ? 496  TYR A CG  1 
ATOM   3929 C CD1 . TYR A 1 497 ? -8.535  -24.283 -4.391  1.00 88.26  ? 496  TYR A CD1 1 
ATOM   3930 C CD2 . TYR A 1 497 ? -7.499  -26.388 -4.754  1.00 88.05  ? 496  TYR A CD2 1 
ATOM   3931 C CE1 . TYR A 1 497 ? -7.468  -23.885 -3.601  1.00 90.08  ? 496  TYR A CE1 1 
ATOM   3932 C CE2 . TYR A 1 497 ? -6.422  -26.003 -3.960  1.00 89.50  ? 496  TYR A CE2 1 
ATOM   3933 C CZ  . TYR A 1 497 ? -6.410  -24.747 -3.381  1.00 90.36  ? 496  TYR A CZ  1 
ATOM   3934 O OH  . TYR A 1 497 ? -5.344  -24.339 -2.589  1.00 77.96  ? 496  TYR A OH  1 
ATOM   3935 N N   . PRO A 1 498 ? -10.319 -26.266 -9.503  1.00 96.20  ? 497  PRO A N   1 
ATOM   3936 C CA  . PRO A 1 498 ? -11.217 -26.858 -10.504 1.00 102.30 ? 497  PRO A CA  1 
ATOM   3937 C C   . PRO A 1 498 ? -11.409 -28.352 -10.315 1.00 106.33 ? 497  PRO A C   1 
ATOM   3938 O O   . PRO A 1 498 ? -10.523 -29.030 -9.799  1.00 109.34 ? 497  PRO A O   1 
ATOM   3939 C CB  . PRO A 1 498 ? -10.488 -26.612 -11.833 1.00 104.29 ? 497  PRO A CB  1 
ATOM   3940 C CG  . PRO A 1 498 ? -9.397  -25.650 -11.534 1.00 102.97 ? 497  PRO A CG  1 
ATOM   3941 C CD  . PRO A 1 498 ? -9.046  -25.829 -10.094 1.00 97.58  ? 497  PRO A CD  1 
ATOM   3942 N N   . ALA A 1 499 ? -12.558 -28.861 -10.745 1.00 109.03 ? 498  ALA A N   1 
ATOM   3943 C CA  . ALA A 1 499 ? -12.783 -30.300 -10.779 1.00 97.06  ? 498  ALA A CA  1 
ATOM   3944 C C   . ALA A 1 499 ? -12.372 -30.855 -12.136 1.00 98.58  ? 498  ALA A C   1 
ATOM   3945 O O   . ALA A 1 499 ? -12.390 -30.136 -13.145 1.00 101.63 ? 498  ALA A O   1 
ATOM   3946 C CB  . ALA A 1 499 ? -14.234 -30.609 -10.506 1.00 93.22  ? 498  ALA A CB  1 
ATOM   3947 N N   . VAL A 1 500 ? -11.987 -32.128 -12.161 1.00 94.87  ? 499  VAL A N   1 
ATOM   3948 C CA  . VAL A 1 500 ? -11.739 -32.801 -13.427 1.00 105.85 ? 499  VAL A CA  1 
ATOM   3949 C C   . VAL A 1 500 ? -13.050 -32.895 -14.193 1.00 114.67 ? 499  VAL A C   1 
ATOM   3950 O O   . VAL A 1 500 ? -13.122 -32.551 -15.371 1.00 121.65 ? 499  VAL A O   1 
ATOM   3951 C CB  . VAL A 1 500 ? -11.193 -34.222 -13.233 1.00 106.85 ? 499  VAL A CB  1 
ATOM   3952 C CG1 . VAL A 1 500 ? -10.997 -34.892 -14.587 1.00 105.57 ? 499  VAL A CG1 1 
ATOM   3953 C CG2 . VAL A 1 500 ? -9.889  -34.190 -12.455 1.00 106.80 ? 499  VAL A CG2 1 
ATOM   3954 N N   . ARG A 1 501 ? -14.089 -33.359 -13.506 1.00 111.89 ? 500  ARG A N   1 
ATOM   3955 C CA  . ARG A 1 501 ? -15.407 -33.488 -14.105 1.00 113.48 ? 500  ARG A CA  1 
ATOM   3956 C C   . ARG A 1 501 ? -16.478 -32.976 -13.150 1.00 116.42 ? 500  ARG A C   1 
ATOM   3957 O O   . ARG A 1 501 ? -16.203 -32.699 -11.984 1.00 111.85 ? 500  ARG A O   1 
ATOM   3958 C CB  . ARG A 1 501 ? -15.695 -34.949 -14.448 1.00 109.49 ? 500  ARG A CB  1 
ATOM   3959 C CG  . ARG A 1 501 ? -15.964 -35.808 -13.226 1.00 106.63 ? 500  ARG A CG  1 
ATOM   3960 C CD  . ARG A 1 501 ? -17.050 -36.828 -13.494 1.00 106.71 ? 500  ARG A CD  1 
ATOM   3961 N NE  . ARG A 1 501 ? -17.492 -37.500 -12.275 1.00 109.24 ? 500  ARG A NE  1 
ATOM   3962 C CZ  . ARG A 1 501 ? -16.979 -38.643 -11.830 1.00 111.33 ? 500  ARG A CZ  1 
ATOM   3963 N NH1 . ARG A 1 501 ? -16.001 -39.226 -12.510 1.00 103.19 ? 500  ARG A NH1 1 
ATOM   3964 N NH2 . ARG A 1 501 ? -17.442 -39.200 -10.712 1.00 113.87 ? 500  ARG A NH2 1 
ATOM   3965 N N   . ASP A 1 502 ? -17.701 -32.859 -13.658 1.00 126.44 ? 501  ASP A N   1 
ATOM   3966 C CA  . ASP A 1 502 ? -18.856 -32.479 -12.846 1.00 129.73 ? 501  ASP A CA  1 
ATOM   3967 C C   . ASP A 1 502 ? -18.585 -31.268 -11.960 1.00 119.48 ? 501  ASP A C   1 
ATOM   3968 O O   . ASP A 1 502 ? -19.049 -31.213 -10.826 1.00 118.60 ? 501  ASP A O   1 
ATOM   3969 C CB  . ASP A 1 502 ? -19.333 -33.662 -11.986 1.00 134.80 ? 501  ASP A CB  1 
ATOM   3970 C CG  . ASP A 1 502 ? -20.182 -34.664 -12.769 1.00 136.02 ? 501  ASP A CG  1 
ATOM   3971 O OD1 . ASP A 1 502 ? -20.068 -34.735 -14.013 1.00 132.27 ? 501  ASP A OD1 1 
ATOM   3972 O OD2 . ASP A 1 502 ? -20.968 -35.390 -12.128 1.00 141.24 ? 501  ASP A OD2 1 
ATOM   3973 N N   . GLY A 1 503 ? -17.840 -30.301 -12.481 1.00 118.09 ? 502  GLY A N   1 
ATOM   3974 C CA  . GLY A 1 503 ? -17.536 -29.086 -11.744 1.00 118.90 ? 502  GLY A CA  1 
ATOM   3975 C C   . GLY A 1 503 ? -18.722 -28.420 -11.059 1.00 122.67 ? 502  GLY A C   1 
ATOM   3976 O O   . GLY A 1 503 ? -18.646 -28.079 -9.880  1.00 107.62 ? 502  GLY A O   1 
ATOM   3977 N N   . PRO A 1 504 ? -19.827 -28.215 -11.798 1.00 137.74 ? 503  PRO A N   1 
ATOM   3978 C CA  . PRO A 1 504 ? -21.002 -27.556 -11.211 1.00 138.99 ? 503  PRO A CA  1 
ATOM   3979 C C   . PRO A 1 504 ? -21.692 -28.409 -10.144 1.00 145.65 ? 503  PRO A C   1 
ATOM   3980 O O   . PRO A 1 504 ? -22.735 -28.014 -9.621  1.00 155.68 ? 503  PRO A O   1 
ATOM   3981 C CB  . PRO A 1 504 ? -21.937 -27.367 -12.412 1.00 128.98 ? 503  PRO A CB  1 
ATOM   3982 C CG  . PRO A 1 504 ? -21.061 -27.493 -13.615 1.00 126.48 ? 503  PRO A CG  1 
ATOM   3983 C CD  . PRO A 1 504 ? -19.998 -28.463 -13.240 1.00 131.31 ? 503  PRO A CD  1 
ATOM   3984 N N   . SER A 1 505 ? -21.114 -29.563 -9.828  1.00 138.67 ? 504  SER A N   1 
ATOM   3985 C CA  . SER A 1 505 ? -21.707 -30.479 -8.863  1.00 137.79 ? 504  SER A CA  1 
ATOM   3986 C C   . SER A 1 505 ? -21.326 -30.114 -7.424  1.00 139.49 ? 504  SER A C   1 
ATOM   3987 O O   . SER A 1 505 ? -21.694 -30.811 -6.476  1.00 132.98 ? 504  SER A O   1 
ATOM   3988 C CB  . SER A 1 505 ? -21.297 -31.917 -9.181  1.00 134.60 ? 504  SER A CB  1 
ATOM   3989 O OG  . SER A 1 505 ? -21.949 -32.830 -8.323  1.00 139.52 ? 504  SER A OG  1 
ATOM   3990 N N   . VAL A 1 506 ? -20.580 -29.019 -7.279  1.00 141.17 ? 505  VAL A N   1 
ATOM   3991 C CA  . VAL A 1 506 ? -20.214 -28.467 -5.973  1.00 128.70 ? 505  VAL A CA  1 
ATOM   3992 C C   . VAL A 1 506 ? -20.601 -26.975 -5.938  1.00 137.32 ? 505  VAL A C   1 
ATOM   3993 O O   . VAL A 1 506 ? -19.753 -26.085 -5.785  1.00 119.74 ? 505  VAL A O   1 
ATOM   3994 C CB  . VAL A 1 506 ? -18.710 -28.655 -5.671  1.00 106.20 ? 505  VAL A CB  1 
ATOM   3995 C CG1 . VAL A 1 506 ? -18.423 -28.357 -4.211  1.00 106.09 ? 505  VAL A CG1 1 
ATOM   3996 C CG2 . VAL A 1 506 ? -18.263 -30.076 -6.022  1.00 93.08  ? 505  VAL A CG2 1 
ATOM   3997 N N   . VAL A 1 507 ? -21.897 -26.722 -6.112  1.00 154.16 ? 506  VAL A N   1 
ATOM   3998 C CA  . VAL A 1 507 ? -22.439 -25.367 -6.128  1.00 159.90 ? 506  VAL A CA  1 
ATOM   3999 C C   . VAL A 1 507 ? -22.480 -24.788 -4.722  1.00 156.18 ? 506  VAL A C   1 
ATOM   4000 O O   . VAL A 1 507 ? -22.420 -25.514 -3.731  1.00 141.64 ? 506  VAL A O   1 
ATOM   4001 C CB  . VAL A 1 507 ? -23.874 -25.315 -6.741  1.00 138.51 ? 506  VAL A CB  1 
ATOM   4002 C CG1 . VAL A 1 507 ? -23.825 -25.239 -8.268  1.00 134.49 ? 506  VAL A CG1 1 
ATOM   4003 C CG2 . VAL A 1 507 ? -24.712 -26.503 -6.267  1.00 133.52 ? 506  VAL A CG2 1 
ATOM   4004 N N   . GLN A 1 508 ? -22.591 -23.472 -4.640  1.00 173.22 ? 507  GLN A N   1 
ATOM   4005 C CA  . GLN A 1 508 ? -22.645 -22.820 -3.346  1.00 192.73 ? 507  GLN A CA  1 
ATOM   4006 C C   . GLN A 1 508 ? -23.686 -21.710 -3.320  1.00 203.19 ? 507  GLN A C   1 
ATOM   4007 O O   . GLN A 1 508 ? -23.769 -20.902 -4.247  1.00 201.92 ? 507  GLN A O   1 
ATOM   4008 C CB  . GLN A 1 508 ? -21.261 -22.278 -2.947  1.00 200.63 ? 507  GLN A CB  1 
ATOM   4009 C CG  . GLN A 1 508 ? -20.690 -21.184 -3.860  1.00 203.35 ? 507  GLN A CG  1 
ATOM   4010 C CD  . GLN A 1 508 ? -19.631 -21.698 -4.829  1.00 200.85 ? 507  GLN A CD  1 
ATOM   4011 O OE1 . GLN A 1 508 ? -19.584 -22.888 -5.146  1.00 205.56 ? 507  GLN A OE1 1 
ATOM   4012 N NE2 . GLN A 1 508 ? -18.780 -20.796 -5.307  1.00 192.83 ? 507  GLN A NE2 1 
ATOM   4013 N N   . PRO A 1 509 ? -24.511 -21.693 -2.264  1.00 211.66 ? 508  PRO A N   1 
ATOM   4014 C CA  . PRO A 1 509 ? -25.364 -20.535 -1.988  1.00 215.09 ? 508  PRO A CA  1 
ATOM   4015 C C   . PRO A 1 509 ? -24.478 -19.354 -1.602  1.00 211.92 ? 508  PRO A C   1 
ATOM   4016 O O   . PRO A 1 509 ? -23.694 -19.478 -0.661  1.00 211.61 ? 508  PRO A O   1 
ATOM   4017 C CB  . PRO A 1 509 ? -26.194 -20.991 -0.783  1.00 216.92 ? 508  PRO A CB  1 
ATOM   4018 C CG  . PRO A 1 509 ? -26.135 -22.487 -0.812  1.00 216.31 ? 508  PRO A CG  1 
ATOM   4019 C CD  . PRO A 1 509 ? -24.781 -22.816 -1.352  1.00 212.55 ? 508  PRO A CD  1 
ATOM   4020 N N   . LYS A 1 510 ? -24.591 -18.243 -2.326  1.00 206.80 ? 509  LYS A N   1 
ATOM   4021 C CA  . LYS A 1 510 ? -23.743 -17.068 -2.106  1.00 196.51 ? 509  LYS A CA  1 
ATOM   4022 C C   . LYS A 1 510 ? -23.288 -16.910 -0.653  1.00 192.24 ? 509  LYS A C   1 
ATOM   4023 O O   . LYS A 1 510 ? -22.092 -16.964 -0.353  1.00 182.99 ? 509  LYS A O   1 
ATOM   4024 C CB  . LYS A 1 510 ? -24.459 -15.797 -2.575  1.00 188.86 ? 509  LYS A CB  1 
ATOM   4025 C CG  . LYS A 1 510 ? -24.750 -15.768 -4.066  1.00 182.60 ? 509  LYS A CG  1 
ATOM   4026 C CD  . LYS A 1 510 ? -25.537 -14.529 -4.457  1.00 177.34 ? 509  LYS A CD  1 
ATOM   4027 C CE  . LYS A 1 510 ? -25.878 -14.541 -5.937  1.00 170.99 ? 509  LYS A CE  1 
ATOM   4028 N NZ  . LYS A 1 510 ? -26.805 -13.436 -6.298  1.00 168.74 ? 509  LYS A NZ  1 
ATOM   4029 N N   . GLU A 1 562 ? -23.338 -41.961 11.003  1.00 181.95 ? 561  GLU A N   1 
ATOM   4030 C CA  . GLU A 1 562 ? -22.041 -42.614 11.140  1.00 177.72 ? 561  GLU A CA  1 
ATOM   4031 C C   . GLU A 1 562 ? -21.513 -43.084 9.784   1.00 178.28 ? 561  GLU A C   1 
ATOM   4032 O O   . GLU A 1 562 ? -20.683 -42.413 9.162   1.00 171.50 ? 561  GLU A O   1 
ATOM   4033 C CB  . GLU A 1 562 ? -22.116 -43.782 12.138  1.00 172.84 ? 561  GLU A CB  1 
ATOM   4034 C CG  . GLU A 1 562 ? -23.137 -44.872 11.798  1.00 169.28 ? 561  GLU A CG  1 
ATOM   4035 C CD  . GLU A 1 562 ? -24.573 -44.396 11.906  1.00 164.99 ? 561  GLU A CD  1 
ATOM   4036 O OE1 . GLU A 1 562 ? -24.926 -43.815 12.955  1.00 164.38 ? 561  GLU A OE1 1 
ATOM   4037 O OE2 . GLU A 1 562 ? -25.347 -44.609 10.945  1.00 159.66 ? 561  GLU A OE2 1 
ATOM   4038 N N   . SER A 1 563 ? -22.011 -44.233 9.330   1.00 181.11 ? 562  SER A N   1 
ATOM   4039 C CA  . SER A 1 563 ? -21.584 -44.833 8.068   1.00 172.18 ? 562  SER A CA  1 
ATOM   4040 C C   . SER A 1 563 ? -22.047 -44.007 6.868   1.00 156.34 ? 562  SER A C   1 
ATOM   4041 O O   . SER A 1 563 ? -21.571 -44.202 5.748   1.00 138.86 ? 562  SER A O   1 
ATOM   4042 C CB  . SER A 1 563 ? -22.089 -46.279 7.959   1.00 172.71 ? 562  SER A CB  1 
ATOM   4043 O OG  . SER A 1 563 ? -21.584 -47.085 9.013   1.00 169.20 ? 562  SER A OG  1 
ATOM   4044 N N   . ALA A 1 564 ? -22.982 -43.091 7.111   1.00 157.11 ? 563  ALA A N   1 
ATOM   4045 C CA  . ALA A 1 564 ? -23.422 -42.150 6.088   1.00 149.74 ? 563  ALA A CA  1 
ATOM   4046 C C   . ALA A 1 564 ? -22.355 -41.074 5.906   1.00 153.07 ? 563  ALA A C   1 
ATOM   4047 O O   . ALA A 1 564 ? -21.209 -41.242 6.341   1.00 156.70 ? 563  ALA A O   1 
ATOM   4048 C CB  . ALA A 1 564 ? -24.756 -41.525 6.472   1.00 139.68 ? 563  ALA A CB  1 
ATOM   4049 N N   . LYS A 1 565 ? -22.739 -39.967 5.274   1.00 140.97 ? 564  LYS A N   1 
ATOM   4050 C CA  . LYS A 1 565 ? -21.814 -38.865 4.982   1.00 115.50 ? 564  LYS A CA  1 
ATOM   4051 C C   . LYS A 1 565 ? -20.803 -39.219 3.889   1.00 97.55  ? 564  LYS A C   1 
ATOM   4052 O O   . LYS A 1 565 ? -20.244 -40.321 3.871   1.00 94.58  ? 564  LYS A O   1 
ATOM   4053 C CB  . LYS A 1 565 ? -21.100 -38.360 6.247   1.00 105.16 ? 564  LYS A CB  1 
ATOM   4054 C CG  . LYS A 1 565 ? -22.045 -37.849 7.332   1.00 113.05 ? 564  LYS A CG  1 
ATOM   4055 C CD  . LYS A 1 565 ? -21.411 -36.778 8.215   1.00 110.87 ? 564  LYS A CD  1 
ATOM   4056 C CE  . LYS A 1 565 ? -20.280 -37.311 9.073   1.00 106.21 ? 564  LYS A CE  1 
ATOM   4057 N NZ  . LYS A 1 565 ? -19.439 -36.180 9.569   1.00 101.37 ? 564  LYS A NZ  1 
ATOM   4058 N N   . PRO A 1 566 ? -20.589 -38.277 2.959   1.00 92.14  ? 565  PRO A N   1 
ATOM   4059 C CA  . PRO A 1 566 ? -19.587 -38.336 1.879   1.00 101.85 ? 565  PRO A CA  1 
ATOM   4060 C C   . PRO A 1 566 ? -18.129 -38.261 2.381   1.00 95.01  ? 565  PRO A C   1 
ATOM   4061 O O   . PRO A 1 566 ? -17.840 -37.596 3.384   1.00 74.99  ? 565  PRO A O   1 
ATOM   4062 C CB  . PRO A 1 566 ? -19.897 -37.100 1.020   1.00 97.62  ? 565  PRO A CB  1 
ATOM   4063 C CG  . PRO A 1 566 ? -21.035 -36.394 1.670   1.00 92.86  ? 565  PRO A CG  1 
ATOM   4064 C CD  . PRO A 1 566 ? -21.305 -36.992 3.003   1.00 86.91  ? 565  PRO A CD  1 
ATOM   4065 N N   . LYS A 1 567 ? -17.223 -38.937 1.677   1.00 91.33  ? 566  LYS A N   1 
ATOM   4066 C CA  . LYS A 1 567 ? -15.814 -38.905 2.031   1.00 85.28  ? 566  LYS A CA  1 
ATOM   4067 C C   . LYS A 1 567 ? -15.126 -37.729 1.335   1.00 83.55  ? 566  LYS A C   1 
ATOM   4068 O O   . LYS A 1 567 ? -15.471 -37.365 0.211   1.00 83.88  ? 566  LYS A O   1 
ATOM   4069 C CB  . LYS A 1 567 ? -15.112 -40.219 1.653   1.00 78.05  ? 566  LYS A CB  1 
ATOM   4070 C CG  . LYS A 1 567 ? -15.888 -41.502 1.941   1.00 77.16  ? 566  LYS A CG  1 
ATOM   4071 C CD  . LYS A 1 567 ? -16.008 -41.833 3.418   1.00 78.83  ? 566  LYS A CD  1 
ATOM   4072 C CE  . LYS A 1 567 ? -16.937 -43.035 3.618   1.00 94.83  ? 566  LYS A CE  1 
ATOM   4073 N NZ  . LYS A 1 567 ? -17.370 -43.248 5.036   1.00 103.23 ? 566  LYS A NZ  1 
ATOM   4074 N N   . LEU A 1 568 ? -14.170 -37.120 2.025   1.00 82.77  ? 567  LEU A N   1 
ATOM   4075 C CA  . LEU A 1 568 ? -13.240 -36.208 1.380   1.00 82.13  ? 567  LEU A CA  1 
ATOM   4076 C C   . LEU A 1 568 ? -11.815 -36.696 1.620   1.00 85.62  ? 567  LEU A C   1 
ATOM   4077 O O   . LEU A 1 568 ? -11.317 -36.666 2.748   1.00 84.28  ? 567  LEU A O   1 
ATOM   4078 C CB  . LEU A 1 568 ? -13.408 -34.779 1.888   1.00 73.96  ? 567  LEU A CB  1 
ATOM   4079 C CG  . LEU A 1 568 ? -12.283 -33.840 1.438   1.00 76.71  ? 567  LEU A CG  1 
ATOM   4080 C CD1 . LEU A 1 568 ? -12.102 -33.867 -0.071  1.00 72.70  ? 567  LEU A CD1 1 
ATOM   4081 C CD2 . LEU A 1 568 ? -12.517 -32.423 1.928   1.00 79.72  ? 567  LEU A CD2 1 
ATOM   4082 N N   . PHE A 1 569 ? -11.175 -37.171 0.559   1.00 82.52  ? 568  PHE A N   1 
ATOM   4083 C CA  . PHE A 1 569 ? -9.763  -37.507 0.620   1.00 86.47  ? 568  PHE A CA  1 
ATOM   4084 C C   . PHE A 1 569 ? -8.898  -36.287 0.271   1.00 86.21  ? 568  PHE A C   1 
ATOM   4085 O O   . PHE A 1 569 ? -9.140  -35.597 -0.724  1.00 87.22  ? 568  PHE A O   1 
ATOM   4086 C CB  . PHE A 1 569 ? -9.441  -38.650 -0.343  1.00 89.39  ? 568  PHE A CB  1 
ATOM   4087 C CG  . PHE A 1 569 ? -10.264 -39.888 -0.126  1.00 92.47  ? 568  PHE A CG  1 
ATOM   4088 C CD1 . PHE A 1 569 ? -10.538 -40.343 1.147   1.00 89.67  ? 568  PHE A CD1 1 
ATOM   4089 C CD2 . PHE A 1 569 ? -10.731 -40.622 -1.204  1.00 95.83  ? 568  PHE A CD2 1 
ATOM   4090 C CE1 . PHE A 1 569 ? -11.283 -41.496 1.339   1.00 84.14  ? 568  PHE A CE1 1 
ATOM   4091 C CE2 . PHE A 1 569 ? -11.475 -41.775 -1.011  1.00 86.72  ? 568  PHE A CE2 1 
ATOM   4092 C CZ  . PHE A 1 569 ? -11.751 -42.206 0.260   1.00 77.82  ? 568  PHE A CZ  1 
ATOM   4093 N N   . VAL A 1 570 ? -7.892  -36.013 1.091   1.00 80.10  ? 569  VAL A N   1 
ATOM   4094 C CA  . VAL A 1 570 ? -6.903  -35.003 0.730   1.00 77.15  ? 569  VAL A CA  1 
ATOM   4095 C C   . VAL A 1 570 ? -5.534  -35.650 0.632   1.00 72.39  ? 569  VAL A C   1 
ATOM   4096 O O   . VAL A 1 570 ? -5.073  -36.271 1.590   1.00 76.49  ? 569  VAL A O   1 
ATOM   4097 C CB  . VAL A 1 570 ? -6.829  -33.875 1.755   1.00 65.60  ? 569  VAL A CB  1 
ATOM   4098 C CG1 . VAL A 1 570 ? -5.832  -32.860 1.292   1.00 65.41  ? 569  VAL A CG1 1 
ATOM   4099 C CG2 . VAL A 1 570 ? -8.186  -33.231 1.939   1.00 59.11  ? 569  VAL A CG2 1 
ATOM   4100 N N   . PHE A 1 571 ? -4.897  -35.528 -0.526  1.00 55.87  ? 570  PHE A N   1 
ATOM   4101 C CA  . PHE A 1 571 ? -3.538  -36.031 -0.693  1.00 55.61  ? 570  PHE A CA  1 
ATOM   4102 C C   . PHE A 1 571 ? -2.572  -34.914 -1.059  1.00 69.35  ? 570  PHE A C   1 
ATOM   4103 O O   . PHE A 1 571 ? -2.762  -34.209 -2.049  1.00 71.29  ? 570  PHE A O   1 
ATOM   4104 C CB  . PHE A 1 571 ? -3.489  -37.104 -1.760  1.00 54.49  ? 570  PHE A CB  1 
ATOM   4105 C CG  . PHE A 1 571 ? -2.105  -37.608 -2.053  1.00 61.82  ? 570  PHE A CG  1 
ATOM   4106 C CD1 . PHE A 1 571 ? -1.471  -38.488 -1.185  1.00 64.34  ? 570  PHE A CD1 1 
ATOM   4107 C CD2 . PHE A 1 571 ? -1.445  -37.229 -3.207  1.00 67.81  ? 570  PHE A CD2 1 
ATOM   4108 C CE1 . PHE A 1 571 ? -0.204  -38.978 -1.461  1.00 53.73  ? 570  PHE A CE1 1 
ATOM   4109 C CE2 . PHE A 1 571 ? -0.168  -37.702 -3.487  1.00 69.61  ? 570  PHE A CE2 1 
ATOM   4110 C CZ  . PHE A 1 571 ? 0.448   -38.583 -2.616  1.00 62.98  ? 570  PHE A CZ  1 
ATOM   4111 N N   . ILE A 1 572 ? -1.536  -34.766 -0.246  1.00 77.08  ? 571  ILE A N   1 
ATOM   4112 C CA  . ILE A 1 572 ? -0.498  -33.769 -0.466  1.00 73.11  ? 571  ILE A CA  1 
ATOM   4113 C C   . ILE A 1 572 ? 0.761   -34.481 -0.938  1.00 66.51  ? 571  ILE A C   1 
ATOM   4114 O O   . ILE A 1 572 ? 1.192   -35.452 -0.319  1.00 61.30  ? 571  ILE A O   1 
ATOM   4115 C CB  . ILE A 1 572 ? -0.158  -33.070 0.851   1.00 63.03  ? 571  ILE A CB  1 
ATOM   4116 C CG1 . ILE A 1 572 ? -1.417  -32.458 1.470   1.00 63.70  ? 571  ILE A CG1 1 
ATOM   4117 C CG2 . ILE A 1 572 ? 0.909   -32.047 0.636   1.00 59.85  ? 571  ILE A CG2 1 
ATOM   4118 C CD1 . ILE A 1 572 ? -1.154  -31.685 2.767   1.00 52.38  ? 571  ILE A CD1 1 
ATOM   4119 N N   . ASN A 1 573 ? 1.356   -34.019 -2.030  1.00 60.02  ? 572  ASN A N   1 
ATOM   4120 C CA  . ASN A 1 573 ? 2.589   -34.649 -2.496  1.00 59.64  ? 572  ASN A CA  1 
ATOM   4121 C C   . ASN A 1 573 ? 3.747   -34.482 -1.518  1.00 66.39  ? 572  ASN A C   1 
ATOM   4122 O O   . ASN A 1 573 ? 3.902   -33.433 -0.893  1.00 69.91  ? 572  ASN A O   1 
ATOM   4123 C CB  . ASN A 1 573 ? 2.988   -34.113 -3.864  1.00 66.44  ? 572  ASN A CB  1 
ATOM   4124 C CG  . ASN A 1 573 ? 2.165   -34.707 -4.981  1.00 82.11  ? 572  ASN A CG  1 
ATOM   4125 O OD1 . ASN A 1 573 ? 2.248   -35.906 -5.260  1.00 84.90  ? 572  ASN A OD1 1 
ATOM   4126 N ND2 . ASN A 1 573 ? 1.365   -33.871 -5.635  1.00 86.40  ? 572  ASN A ND2 1 
ATOM   4127 N N   . GLY A 1 574 ? 4.562   -35.522 -1.382  1.00 68.45  ? 573  GLY A N   1 
ATOM   4128 C CA  . GLY A 1 574 ? 5.740   -35.446 -0.540  1.00 68.73  ? 573  GLY A CA  1 
ATOM   4129 C C   . GLY A 1 574 ? 5.549   -35.779 0.935   1.00 70.04  ? 573  GLY A C   1 
ATOM   4130 O O   . GLY A 1 574 ? 6.015   -36.825 1.390   1.00 68.41  ? 573  GLY A O   1 
ATOM   4131 N N   . THR A 1 575 ? 4.863   -34.899 1.669   1.00 63.11  ? 574  THR A N   1 
ATOM   4132 C CA  . THR A 1 575 ? 4.875   -34.888 3.139   1.00 57.72  ? 574  THR A CA  1 
ATOM   4133 C C   . THR A 1 575 ? 3.522   -34.475 3.713   1.00 59.76  ? 574  THR A C   1 
ATOM   4134 O O   . THR A 1 575 ? 2.834   -33.644 3.115   1.00 65.22  ? 574  THR A O   1 
ATOM   4135 C CB  . THR A 1 575 ? 5.965   -33.898 3.660   1.00 58.51  ? 574  THR A CB  1 
ATOM   4136 O OG1 . THR A 1 575 ? 7.128   -34.631 4.065   1.00 68.20  ? 574  THR A OG1 1 
ATOM   4137 C CG2 . THR A 1 575 ? 5.458   -33.024 4.835   1.00 47.86  ? 574  THR A CG2 1 
ATOM   4138 N N   . VAL A 1 576 ? 3.127   -35.058 4.852   1.00 44.71  ? 575  VAL A N   1 
ATOM   4139 C CA  . VAL A 1 576 ? 1.945   -34.569 5.587   1.00 36.36  ? 575  VAL A CA  1 
ATOM   4140 C C   . VAL A 1 576 ? 2.340   -34.330 7.028   1.00 44.15  ? 575  VAL A C   1 
ATOM   4141 O O   . VAL A 1 576 ? 3.197   -35.036 7.556   1.00 49.41  ? 575  VAL A O   1 
ATOM   4142 C CB  . VAL A 1 576 ? 0.688   -35.508 5.510   1.00 54.70  ? 575  VAL A CB  1 
ATOM   4143 C CG1 . VAL A 1 576 ? 0.892   -36.783 6.313   1.00 50.82  ? 575  VAL A CG1 1 
ATOM   4144 C CG2 . VAL A 1 576 ? -0.563  -34.770 6.028   1.00 55.47  ? 575  VAL A CG2 1 
ATOM   4145 N N   . SER A 1 577 ? 1.727   -33.326 7.653   1.00 51.64  ? 576  SER A N   1 
ATOM   4146 C CA  . SER A 1 577 ? 2.130   -32.872 8.989   1.00 52.08  ? 576  SER A CA  1 
ATOM   4147 C C   . SER A 1 577 ? 1.126   -33.326 10.029  1.00 52.80  ? 576  SER A C   1 
ATOM   4148 O O   . SER A 1 577 ? -0.055  -33.450 9.729   1.00 64.11  ? 576  SER A O   1 
ATOM   4149 C CB  . SER A 1 577 ? 2.225   -31.340 9.016   1.00 49.93  ? 576  SER A CB  1 
ATOM   4150 O OG  . SER A 1 577 ? 3.192   -30.865 8.100   1.00 65.00  ? 576  SER A OG  1 
ATOM   4151 N N   . TYR A 1 578 ? 1.575   -33.549 11.257  1.00 58.14  ? 577  TYR A N   1 
ATOM   4152 C CA  . TYR A 1 578 ? 0.655   -33.988 12.309  1.00 54.00  ? 577  TYR A CA  1 
ATOM   4153 C C   . TYR A 1 578 ? -0.454  -32.970 12.604  1.00 55.64  ? 577  TYR A C   1 
ATOM   4154 O O   . TYR A 1 578 ? -1.562  -33.344 12.990  1.00 64.68  ? 577  TYR A O   1 
ATOM   4155 C CB  . TYR A 1 578 ? 1.404   -34.395 13.585  1.00 46.00  ? 577  TYR A CB  1 
ATOM   4156 C CG  . TYR A 1 578 ? 2.140   -35.718 13.464  1.00 57.23  ? 577  TYR A CG  1 
ATOM   4157 C CD1 . TYR A 1 578 ? 1.437   -36.921 13.357  1.00 70.10  ? 577  TYR A CD1 1 
ATOM   4158 C CD2 . TYR A 1 578 ? 3.529   -35.774 13.478  1.00 53.38  ? 577  TYR A CD2 1 
ATOM   4159 C CE1 . TYR A 1 578 ? 2.095   -38.139 13.264  1.00 49.67  ? 577  TYR A CE1 1 
ATOM   4160 C CE2 . TYR A 1 578 ? 4.188   -36.979 13.378  1.00 66.84  ? 577  TYR A CE2 1 
ATOM   4161 C CZ  . TYR A 1 578 ? 3.464   -38.161 13.274  1.00 59.18  ? 577  TYR A CZ  1 
ATOM   4162 O OH  . TYR A 1 578 ? 4.127   -39.360 13.181  1.00 61.46  ? 577  TYR A OH  1 
ATOM   4163 N N   . ASN A 1 579 ? -0.167  -31.688 12.414  1.00 58.53  ? 578  ASN A N   1 
ATOM   4164 C CA  . ASN A 1 579 ? -1.191  -30.658 12.585  1.00 61.64  ? 578  ASN A CA  1 
ATOM   4165 C C   . ASN A 1 579 ? -2.228  -30.668 11.461  1.00 61.02  ? 578  ASN A C   1 
ATOM   4166 O O   . ASN A 1 579 ? -3.376  -30.299 11.667  1.00 71.22  ? 578  ASN A O   1 
ATOM   4167 C CB  . ASN A 1 579 ? -0.582  -29.257 12.795  1.00 70.29  ? 578  ASN A CB  1 
ATOM   4168 C CG  . ASN A 1 579 ? 0.303   -28.792 11.632  1.00 67.18  ? 578  ASN A CG  1 
ATOM   4169 O OD1 . ASN A 1 579 ? 0.627   -29.556 10.722  1.00 57.83  ? 578  ASN A OD1 1 
ATOM   4170 N ND2 . ASN A 1 579 ? 0.699   -27.523 11.675  1.00 59.36  ? 578  ASN A ND2 1 
ATOM   4171 N N   . GLU A 1 580 ? -1.822  -31.109 10.277  1.00 54.26  ? 579  GLU A N   1 
ATOM   4172 C CA  . GLU A 1 580 ? -2.747  -31.232 9.160   1.00 58.29  ? 579  GLU A CA  1 
ATOM   4173 C C   . GLU A 1 580 ? -3.578  -32.504 9.334   1.00 67.98  ? 579  GLU A C   1 
ATOM   4174 O O   . GLU A 1 580 ? -4.735  -32.568 8.934   1.00 72.24  ? 579  GLU A O   1 
ATOM   4175 C CB  . GLU A 1 580 ? -1.986  -31.249 7.828   1.00 52.48  ? 579  GLU A CB  1 
ATOM   4176 C CG  . GLU A 1 580 ? -1.263  -29.958 7.513   1.00 64.51  ? 579  GLU A CG  1 
ATOM   4177 C CD  . GLU A 1 580 ? -0.246  -30.086 6.378   1.00 70.85  ? 579  GLU A CD  1 
ATOM   4178 O OE1 . GLU A 1 580 ? 0.612   -31.000 6.460   1.00 61.61  ? 579  GLU A OE1 1 
ATOM   4179 O OE2 . GLU A 1 580 ? -0.291  -29.253 5.429   1.00 68.61  ? 579  GLU A OE2 1 
ATOM   4180 N N   . ILE A 1 581 ? -2.958  -33.518 9.926   1.00 71.68  ? 580  ILE A N   1 
ATOM   4181 C CA  . ILE A 1 581 ? -3.625  -34.763 10.274  1.00 67.14  ? 580  ILE A CA  1 
ATOM   4182 C C   . ILE A 1 581 ? -4.709  -34.474 11.311  1.00 70.46  ? 580  ILE A C   1 
ATOM   4183 O O   . ILE A 1 581 ? -5.855  -34.898 11.155  1.00 67.69  ? 580  ILE A O   1 
ATOM   4184 C CB  . ILE A 1 581 ? -2.593  -35.809 10.793  1.00 50.97  ? 580  ILE A CB  1 
ATOM   4185 C CG1 . ILE A 1 581 ? -1.744  -36.330 9.621   1.00 50.16  ? 580  ILE A CG1 1 
ATOM   4186 C CG2 . ILE A 1 581 ? -3.280  -36.948 11.565  1.00 41.62  ? 580  ILE A CG2 1 
ATOM   4187 C CD1 . ILE A 1 581 ? -0.609  -37.235 10.022  1.00 39.76  ? 580  ILE A CD1 1 
ATOM   4188 N N   . ARG A 1 582 ? -4.351  -33.731 12.355  1.00 67.05  ? 581  ARG A N   1 
ATOM   4189 C CA  . ARG A 1 582 ? -5.310  -33.348 13.376  1.00 64.28  ? 581  ARG A CA  1 
ATOM   4190 C C   . ARG A 1 582 ? -6.512  -32.683 12.717  1.00 70.07  ? 581  ARG A C   1 
ATOM   4191 O O   . ARG A 1 582 ? -7.648  -32.826 13.168  1.00 75.51  ? 581  ARG A O   1 
ATOM   4192 C CB  . ARG A 1 582 ? -4.674  -32.384 14.376  1.00 59.02  ? 581  ARG A CB  1 
ATOM   4193 C CG  . ARG A 1 582 ? -5.474  -32.190 15.656  1.00 62.84  ? 581  ARG A CG  1 
ATOM   4194 C CD  . ARG A 1 582 ? -4.892  -31.091 16.537  1.00 68.34  ? 581  ARG A CD  1 
ATOM   4195 N NE  . ARG A 1 582 ? -4.931  -29.799 15.853  1.00 71.85  ? 581  ARG A NE  1 
ATOM   4196 C CZ  . ARG A 1 582 ? -3.872  -29.027 15.637  1.00 70.85  ? 581  ARG A CZ  1 
ATOM   4197 N NH1 . ARG A 1 582 ? -2.667  -29.411 16.067  1.00 56.71  ? 581  ARG A NH1 1 
ATOM   4198 N NH2 . ARG A 1 582 ? -4.021  -27.872 14.990  1.00 66.97  ? 581  ARG A NH2 1 
ATOM   4199 N N   . CYS A 1 583 ? -6.258  -31.959 11.636  1.00 65.96  ? 582  CYS A N   1 
ATOM   4200 C CA  . CYS A 1 583 ? -7.309  -31.167 11.002  1.00 68.97  ? 582  CYS A CA  1 
ATOM   4201 C C   . CYS A 1 583 ? -8.396  -32.043 10.401  1.00 69.95  ? 582  CYS A C   1 
ATOM   4202 O O   . CYS A 1 583 ? -9.578  -31.730 10.488  1.00 76.46  ? 582  CYS A O   1 
ATOM   4203 C CB  . CYS A 1 583 ? -6.723  -30.199 9.954   1.00 62.55  ? 582  CYS A CB  1 
ATOM   4204 S SG  . CYS A 1 583 ? -5.941  -28.743 10.693  1.00 88.51  ? 582  CYS A SG  1 
ATOM   4205 N N   . ALA A 1 584 ? -7.985  -33.150 9.801   1.00 70.95  ? 583  ALA A N   1 
ATOM   4206 C CA  . ALA A 1 584 ? -8.916  -34.084 9.202   1.00 60.42  ? 583  ALA A CA  1 
ATOM   4207 C C   . ALA A 1 584 ? -9.847  -34.635 10.273  1.00 67.64  ? 583  ALA A C   1 
ATOM   4208 O O   . ALA A 1 584 ? -11.020 -34.873 10.016  1.00 79.25  ? 583  ALA A O   1 
ATOM   4209 C CB  . ALA A 1 584 ? -8.160  -35.195 8.524   1.00 46.81  ? 583  ALA A CB  1 
ATOM   4210 N N   . TYR A 1 585 ? -9.325  -34.830 11.478  1.00 62.53  ? 584  TYR A N   1 
ATOM   4211 C CA  . TYR A 1 585 ? -10.158 -35.279 12.581  1.00 63.84  ? 584  TYR A CA  1 
ATOM   4212 C C   . TYR A 1 585 ? -11.072 -34.147 13.048  1.00 70.73  ? 584  TYR A C   1 
ATOM   4213 O O   . TYR A 1 585 ? -12.272 -34.335 13.182  1.00 69.25  ? 584  TYR A O   1 
ATOM   4214 C CB  . TYR A 1 585 ? -9.313  -35.818 13.741  1.00 57.92  ? 584  TYR A CB  1 
ATOM   4215 C CG  . TYR A 1 585 ? -8.582  -37.106 13.423  1.00 61.81  ? 584  TYR A CG  1 
ATOM   4216 C CD1 . TYR A 1 585 ? -7.387  -37.089 12.708  1.00 58.35  ? 584  TYR A CD1 1 
ATOM   4217 C CD2 . TYR A 1 585 ? -9.090  -38.345 13.829  1.00 54.18  ? 584  TYR A CD2 1 
ATOM   4218 C CE1 . TYR A 1 585 ? -6.715  -38.259 12.409  1.00 57.13  ? 584  TYR A CE1 1 
ATOM   4219 C CE2 . TYR A 1 585 ? -8.429  -39.529 13.530  1.00 43.92  ? 584  TYR A CE2 1 
ATOM   4220 C CZ  . TYR A 1 585 ? -7.233  -39.477 12.824  1.00 62.00  ? 584  TYR A CZ  1 
ATOM   4221 O OH  . TYR A 1 585 ? -6.545  -40.630 12.516  1.00 65.62  ? 584  TYR A OH  1 
ATOM   4222 N N   . GLU A 1 586 ? -10.514 -32.966 13.284  1.00 72.68  ? 585  GLU A N   1 
ATOM   4223 C CA  . GLU A 1 586 ? -11.333 -31.858 13.753  1.00 67.83  ? 585  GLU A CA  1 
ATOM   4224 C C   . GLU A 1 586 ? -12.501 -31.620 12.803  1.00 78.23  ? 585  GLU A C   1 
ATOM   4225 O O   . GLU A 1 586 ? -13.621 -31.354 13.249  1.00 77.02  ? 585  GLU A O   1 
ATOM   4226 C CB  . GLU A 1 586 ? -10.513 -30.578 13.902  1.00 58.46  ? 585  GLU A CB  1 
ATOM   4227 C CG  . GLU A 1 586 ? -9.345  -30.683 14.866  1.00 73.17  ? 585  GLU A CG  1 
ATOM   4228 C CD  . GLU A 1 586 ? -8.445  -29.454 14.828  1.00 91.42  ? 585  GLU A CD  1 
ATOM   4229 O OE1 . GLU A 1 586 ? -8.498  -28.704 13.827  1.00 93.59  ? 585  GLU A OE1 1 
ATOM   4230 O OE2 . GLU A 1 586 ? -7.683  -29.234 15.797  1.00 101.25 ? 585  GLU A OE2 1 
ATOM   4231 N N   . VAL A 1 587 ? -12.239 -31.730 11.501  1.00 76.93  ? 586  VAL A N   1 
ATOM   4232 C CA  . VAL A 1 587 ? -13.221 -31.354 10.481  1.00 79.28  ? 586  VAL A CA  1 
ATOM   4233 C C   . VAL A 1 587 ? -14.247 -32.446 10.232  1.00 85.01  ? 586  VAL A C   1 
ATOM   4234 O O   . VAL A 1 587 ? -15.364 -32.177 9.790   1.00 92.82  ? 586  VAL A O   1 
ATOM   4235 C CB  . VAL A 1 587 ? -12.540 -30.909 9.162   1.00 73.05  ? 586  VAL A CB  1 
ATOM   4236 C CG1 . VAL A 1 587 ? -13.478 -31.050 7.950   1.00 60.82  ? 586  VAL A CG1 1 
ATOM   4237 C CG2 . VAL A 1 587 ? -12.042 -29.483 9.303   1.00 69.96  ? 586  VAL A CG2 1 
ATOM   4238 N N   . SER A 1 588 ? -13.876 -33.681 10.533  1.00 83.02  ? 587  SER A N   1 
ATOM   4239 C CA  . SER A 1 588 ? -14.842 -34.768 10.497  1.00 82.01  ? 587  SER A CA  1 
ATOM   4240 C C   . SER A 1 588 ? -15.868 -34.603 11.612  1.00 89.84  ? 587  SER A C   1 
ATOM   4241 O O   . SER A 1 588 ? -17.066 -34.662 11.377  1.00 96.58  ? 587  SER A O   1 
ATOM   4242 C CB  . SER A 1 588 ? -14.141 -36.117 10.621  1.00 75.26  ? 587  SER A CB  1 
ATOM   4243 O OG  . SER A 1 588 ? -13.537 -36.487 9.397   1.00 80.09  ? 587  SER A OG  1 
ATOM   4244 N N   . GLN A 1 589 ? -15.390 -34.382 12.827  1.00 101.35 ? 588  GLN A N   1 
ATOM   4245 C CA  . GLN A 1 589 ? -16.268 -34.305 13.984  1.00 107.37 ? 588  GLN A CA  1 
ATOM   4246 C C   . GLN A 1 589 ? -17.020 -32.979 14.059  1.00 110.56 ? 588  GLN A C   1 
ATOM   4247 O O   . GLN A 1 589 ? -17.854 -32.788 14.941  1.00 124.59 ? 588  GLN A O   1 
ATOM   4248 C CB  . GLN A 1 589 ? -15.477 -34.567 15.270  1.00 111.72 ? 588  GLN A CB  1 
ATOM   4249 C CG  . GLN A 1 589 ? -14.824 -35.951 15.302  1.00 124.97 ? 588  GLN A CG  1 
ATOM   4250 C CD  . GLN A 1 589 ? -13.597 -36.015 16.201  1.00 133.33 ? 588  GLN A CD  1 
ATOM   4251 O OE1 . GLN A 1 589 ? -12.851 -37.000 16.185  1.00 132.77 ? 588  GLN A OE1 1 
ATOM   4252 N NE2 . GLN A 1 589 ? -13.378 -34.960 16.984  1.00 133.63 ? 588  GLN A NE2 1 
ATOM   4253 N N   . SER A 1 590 ? -16.739 -32.065 13.136  1.00 104.44 ? 589  SER A N   1 
ATOM   4254 C CA  . SER A 1 590 ? -17.425 -30.771 13.142  1.00 110.52 ? 589  SER A CA  1 
ATOM   4255 C C   . SER A 1 590 ? -18.526 -30.707 12.095  1.00 124.60 ? 589  SER A C   1 
ATOM   4256 O O   . SER A 1 590 ? -19.705 -30.831 12.420  1.00 143.59 ? 589  SER A O   1 
ATOM   4257 C CB  . SER A 1 590 ? -16.449 -29.591 12.990  1.00 104.92 ? 589  SER A CB  1 
ATOM   4258 O OG  . SER A 1 590 ? -15.687 -29.663 11.795  1.00 107.47 ? 589  SER A OG  1 
ATOM   4259 N N   . SER A 1 591 ? -18.149 -30.534 10.837  1.00 118.66 ? 590  SER A N   1 
ATOM   4260 C CA  . SER A 1 591 ? -19.154 -30.408 9.801   1.00 119.62 ? 590  SER A CA  1 
ATOM   4261 C C   . SER A 1 591 ? -19.033 -31.412 8.663   1.00 102.77 ? 590  SER A C   1 
ATOM   4262 O O   . SER A 1 591 ? -17.941 -31.599 8.073   1.00 78.78  ? 590  SER A O   1 
ATOM   4263 C CB  . SER A 1 591 ? -19.177 -28.976 9.236   1.00 134.02 ? 590  SER A CB  1 
ATOM   4264 O OG  . SER A 1 591 ? -20.258 -28.782 8.327   1.00 136.59 ? 590  SER A OG  1 
ATOM   4265 N N   . GLY A 1 592 ? -20.170 -32.067 8.405   1.00 91.64  ? 591  GLY A N   1 
ATOM   4266 C CA  . GLY A 1 592 ? -20.559 -32.490 7.066   1.00 87.18  ? 591  GLY A CA  1 
ATOM   4267 C C   . GLY A 1 592 ? -19.951 -33.731 6.451   1.00 91.20  ? 591  GLY A C   1 
ATOM   4268 O O   . GLY A 1 592 ? -20.627 -34.738 6.310   1.00 91.95  ? 591  GLY A O   1 
ATOM   4269 N N   . TYR A 1 593 ? -18.683 -33.650 6.055   1.00 98.60  ? 592  TYR A N   1 
ATOM   4270 C CA  . TYR A 1 593 ? -18.003 -34.774 5.418   1.00 92.05  ? 592  TYR A CA  1 
ATOM   4271 C C   . TYR A 1 593 ? -17.200 -35.615 6.417   1.00 95.63  ? 592  TYR A C   1 
ATOM   4272 O O   . TYR A 1 593 ? -17.007 -35.221 7.568   1.00 102.32 ? 592  TYR A O   1 
ATOM   4273 C CB  . TYR A 1 593 ? -17.057 -34.256 4.335   1.00 87.95  ? 592  TYR A CB  1 
ATOM   4274 C CG  . TYR A 1 593 ? -17.727 -33.821 3.054   1.00 90.76  ? 592  TYR A CG  1 
ATOM   4275 C CD1 . TYR A 1 593 ? -18.516 -32.679 3.010   1.00 98.09  ? 592  TYR A CD1 1 
ATOM   4276 C CD2 . TYR A 1 593 ? -17.552 -34.542 1.881   1.00 92.79  ? 592  TYR A CD2 1 
ATOM   4277 C CE1 . TYR A 1 593 ? -19.131 -32.275 1.832   1.00 102.74 ? 592  TYR A CE1 1 
ATOM   4278 C CE2 . TYR A 1 593 ? -18.159 -34.149 0.701   1.00 105.38 ? 592  TYR A CE2 1 
ATOM   4279 C CZ  . TYR A 1 593 ? -18.948 -33.015 0.679   1.00 107.61 ? 592  TYR A CZ  1 
ATOM   4280 O OH  . TYR A 1 593 ? -19.548 -32.624 -0.497  1.00 109.21 ? 592  TYR A OH  1 
ATOM   4281 N N   . GLU A 1 594 ? -16.755 -36.786 5.969   1.00 87.15  ? 593  GLU A N   1 
ATOM   4282 C CA  . GLU A 1 594 ? -15.695 -37.527 6.644   1.00 85.10  ? 593  GLU A CA  1 
ATOM   4283 C C   . GLU A 1 594 ? -14.420 -37.263 5.860   1.00 92.58  ? 593  GLU A C   1 
ATOM   4284 O O   . GLU A 1 594 ? -14.381 -37.465 4.647   1.00 90.69  ? 593  GLU A O   1 
ATOM   4285 C CB  . GLU A 1 594 ? -15.970 -39.034 6.659   1.00 86.07  ? 593  GLU A CB  1 
ATOM   4286 C CG  . GLU A 1 594 ? -17.140 -39.478 7.518   1.00 85.13  ? 593  GLU A CG  1 
ATOM   4287 C CD  . GLU A 1 594 ? -16.940 -39.197 8.994   1.00 90.08  ? 593  GLU A CD  1 
ATOM   4288 O OE1 . GLU A 1 594 ? -17.239 -38.066 9.436   1.00 97.19  ? 593  GLU A OE1 1 
ATOM   4289 O OE2 . GLU A 1 594 ? -16.496 -40.114 9.717   1.00 90.20  ? 593  GLU A OE2 1 
ATOM   4290 N N   . VAL A 1 595 ? -13.378 -36.810 6.547   1.00 93.56  ? 594  VAL A N   1 
ATOM   4291 C CA  . VAL A 1 595 ? -12.147 -36.410 5.878   1.00 87.43  ? 594  VAL A CA  1 
ATOM   4292 C C   . VAL A 1 595 ? -11.025 -37.445 6.058   1.00 76.96  ? 594  VAL A C   1 
ATOM   4293 O O   . VAL A 1 595 ? -10.857 -38.018 7.129   1.00 70.42  ? 594  VAL A O   1 
ATOM   4294 C CB  . VAL A 1 595 ? -11.697 -35.016 6.368   1.00 86.55  ? 594  VAL A CB  1 
ATOM   4295 C CG1 . VAL A 1 595 ? -10.599 -34.477 5.501   1.00 75.60  ? 594  VAL A CG1 1 
ATOM   4296 C CG2 . VAL A 1 595 ? -12.879 -34.057 6.366   1.00 91.89  ? 594  VAL A CG2 1 
ATOM   4297 N N   . TYR A 1 596 ? -10.281 -37.701 4.990   1.00 72.88  ? 595  TYR A N   1 
ATOM   4298 C CA  . TYR A 1 596 ? -9.097  -38.546 5.068   1.00 71.56  ? 595  TYR A CA  1 
ATOM   4299 C C   . TYR A 1 596 ? -7.904  -37.824 4.444   1.00 82.32  ? 595  TYR A C   1 
ATOM   4300 O O   . TYR A 1 596 ? -8.017  -37.221 3.371   1.00 84.92  ? 595  TYR A O   1 
ATOM   4301 C CB  . TYR A 1 596 ? -9.344  -39.873 4.368   1.00 67.01  ? 595  TYR A CB  1 
ATOM   4302 C CG  . TYR A 1 596 ? -10.563 -40.584 4.901   1.00 81.21  ? 595  TYR A CG  1 
ATOM   4303 C CD1 . TYR A 1 596 ? -11.821 -40.294 4.403   1.00 85.62  ? 595  TYR A CD1 1 
ATOM   4304 C CD2 . TYR A 1 596 ? -10.458 -41.535 5.912   1.00 82.98  ? 595  TYR A CD2 1 
ATOM   4305 C CE1 . TYR A 1 596 ? -12.944 -40.918 4.891   1.00 90.89  ? 595  TYR A CE1 1 
ATOM   4306 C CE2 . TYR A 1 596 ? -11.576 -42.167 6.409   1.00 88.23  ? 595  TYR A CE2 1 
ATOM   4307 C CZ  . TYR A 1 596 ? -12.823 -41.853 5.892   1.00 94.83  ? 595  TYR A CZ  1 
ATOM   4308 O OH  . TYR A 1 596 ? -13.962 -42.475 6.363   1.00 93.24  ? 595  TYR A OH  1 
ATOM   4309 N N   . ILE A 1 597 ? -6.759  -37.878 5.119   1.00 75.19  ? 596  ILE A N   1 
ATOM   4310 C CA  . ILE A 1 597 ? -5.593  -37.151 4.649   1.00 68.02  ? 596  ILE A CA  1 
ATOM   4311 C C   . ILE A 1 597 ? -4.369  -38.051 4.478   1.00 64.79  ? 596  ILE A C   1 
ATOM   4312 O O   . ILE A 1 597 ? -4.169  -38.996 5.246   1.00 61.07  ? 596  ILE A O   1 
ATOM   4313 C CB  . ILE A 1 597 ? -5.287  -35.951 5.574   1.00 64.56  ? 596  ILE A CB  1 
ATOM   4314 C CG1 . ILE A 1 597 ? -4.356  -34.959 4.876   1.00 54.52  ? 596  ILE A CG1 1 
ATOM   4315 C CG2 . ILE A 1 597 ? -4.759  -36.418 6.934   1.00 59.24  ? 596  ILE A CG2 1 
ATOM   4316 C CD1 . ILE A 1 597 ? -4.379  -33.588 5.494   1.00 59.83  ? 596  ILE A CD1 1 
ATOM   4317 N N   . GLY A 1 598 ? -3.559  -37.758 3.465   1.00 61.48  ? 597  GLY A N   1 
ATOM   4318 C CA  . GLY A 1 598 ? -2.366  -38.544 3.196   1.00 64.38  ? 597  GLY A CA  1 
ATOM   4319 C C   . GLY A 1 598 ? -1.308  -37.928 2.283   1.00 67.28  ? 597  GLY A C   1 
ATOM   4320 O O   . GLY A 1 598 ? -1.484  -36.861 1.687   1.00 67.54  ? 597  GLY A O   1 
ATOM   4321 N N   . ALA A 1 599 ? -0.198  -38.642 2.160   1.00 65.46  ? 598  ALA A N   1 
ATOM   4322 C CA  . ALA A 1 599 ? 0.991   -38.140 1.490   1.00 60.42  ? 598  ALA A CA  1 
ATOM   4323 C C   . ALA A 1 599 ? 1.934   -39.315 1.288   1.00 58.66  ? 598  ALA A C   1 
ATOM   4324 O O   . ALA A 1 599 ? 1.686   -40.396 1.804   1.00 74.29  ? 598  ALA A O   1 
ATOM   4325 C CB  . ALA A 1 599 ? 1.652   -37.089 2.355   1.00 54.05  ? 598  ALA A CB  1 
ATOM   4326 N N   . HIS A 1 600 ? 3.011   -39.115 0.541   1.00 53.54  ? 599  HIS A N   1 
ATOM   4327 C CA  . HIS A 1 600 ? 4.022   -40.153 0.384   1.00 53.29  ? 599  HIS A CA  1 
ATOM   4328 C C   . HIS A 1 600 ? 4.449   -40.662 1.753   1.00 60.39  ? 599  HIS A C   1 
ATOM   4329 O O   . HIS A 1 600 ? 4.618   -41.856 1.953   1.00 74.35  ? 599  HIS A O   1 
ATOM   4330 C CB  . HIS A 1 600 ? 5.230   -39.620 -0.393  1.00 62.75  ? 599  HIS A CB  1 
ATOM   4331 C CG  . HIS A 1 600 ? 4.946   -39.340 -1.835  1.00 60.93  ? 599  HIS A CG  1 
ATOM   4332 N ND1 . HIS A 1 600 ? 4.098   -38.335 -2.244  1.00 69.58  ? 599  HIS A ND1 1 
ATOM   4333 C CD2 . HIS A 1 600 ? 5.396   -39.932 -2.966  1.00 62.12  ? 599  HIS A CD2 1 
ATOM   4334 C CE1 . HIS A 1 600 ? 4.033   -38.323 -3.562  1.00 73.87  ? 599  HIS A CE1 1 
ATOM   4335 N NE2 . HIS A 1 600 ? 4.813   -39.282 -4.026  1.00 69.35  ? 599  HIS A NE2 1 
ATOM   4336 N N   . ASN A 1 601 ? 4.611   -39.753 2.706   1.00 58.47  ? 600  ASN A N   1 
ATOM   4337 C CA  . ASN A 1 601 ? 4.902   -40.164 4.061   1.00 57.43  ? 600  ASN A CA  1 
ATOM   4338 C C   . ASN A 1 601 ? 4.507   -39.078 5.045   1.00 60.06  ? 600  ASN A C   1 
ATOM   4339 O O   . ASN A 1 601 ? 4.203   -37.964 4.641   1.00 65.39  ? 600  ASN A O   1 
ATOM   4340 C CB  . ASN A 1 601 ? 6.379   -40.539 4.202   1.00 67.84  ? 600  ASN A CB  1 
ATOM   4341 C CG  . ASN A 1 601 ? 6.609   -41.716 5.155   1.00 81.78  ? 600  ASN A CG  1 
ATOM   4342 O OD1 . ASN A 1 601 ? 5.681   -42.224 5.791   1.00 92.06  ? 600  ASN A OD1 1 
ATOM   4343 N ND2 . ASN A 1 601 ? 7.856   -42.154 5.249   1.00 85.16  ? 600  ASN A ND2 1 
ATOM   4344 N N   . ILE A 1 602 ? 4.461   -39.426 6.328   1.00 61.11  ? 601  ILE A N   1 
ATOM   4345 C CA  . ILE A 1 602 ? 4.374   -38.433 7.392   1.00 63.69  ? 601  ILE A CA  1 
ATOM   4346 C C   . ILE A 1 602 ? 5.785   -37.925 7.680   1.00 57.81  ? 601  ILE A C   1 
ATOM   4347 O O   . ILE A 1 602 ? 6.736   -38.708 7.799   1.00 63.71  ? 601  ILE A O   1 
ATOM   4348 C CB  . ILE A 1 602 ? 3.768   -39.031 8.695   1.00 59.14  ? 601  ILE A CB  1 
ATOM   4349 C CG1 . ILE A 1 602 ? 2.272   -39.284 8.531   1.00 50.81  ? 601  ILE A CG1 1 
ATOM   4350 C CG2 . ILE A 1 602 ? 4.040   -38.126 9.923   1.00 55.41  ? 601  ILE A CG2 1 
ATOM   4351 C CD1 . ILE A 1 602 ? 1.692   -40.117 9.664   1.00 53.12  ? 601  ILE A CD1 1 
ATOM   4352 N N   . ALA A 1 603 ? 5.933   -36.614 7.776   1.00 55.40  ? 602  ALA A N   1 
ATOM   4353 C CA  . ALA A 1 603 ? 7.213   -36.051 8.203   1.00 55.61  ? 602  ALA A CA  1 
ATOM   4354 C C   . ALA A 1 603 ? 6.995   -35.102 9.357   1.00 46.12  ? 602  ALA A C   1 
ATOM   4355 O O   . ALA A 1 603 ? 6.151   -34.220 9.273   1.00 53.45  ? 602  ALA A O   1 
ATOM   4356 C CB  . ALA A 1 603 ? 7.911   -35.332 7.044   1.00 47.73  ? 602  ALA A CB  1 
ATOM   4357 N N   . THR A 1 604 ? 7.734   -35.307 10.441  1.00 37.47  ? 603  THR A N   1 
ATOM   4358 C CA  . THR A 1 604 ? 7.852   -34.285 11.483  1.00 50.51  ? 603  THR A CA  1 
ATOM   4359 C C   . THR A 1 604 ? 8.577   -33.029 10.965  1.00 54.84  ? 603  THR A C   1 
ATOM   4360 O O   . THR A 1 604 ? 9.106   -33.025 9.858   1.00 43.38  ? 603  THR A O   1 
ATOM   4361 C CB  . THR A 1 604 ? 8.634   -34.827 12.662  1.00 47.13  ? 603  THR A CB  1 
ATOM   4362 O OG1 . THR A 1 604 ? 9.962   -35.153 12.244  1.00 43.25  ? 603  THR A OG1 1 
ATOM   4363 C CG2 . THR A 1 604 ? 7.957   -36.062 13.195  1.00 41.89  ? 603  THR A CG2 1 
ATOM   4364 N N   . PRO A 1 605 ? 8.606   -31.952 11.769  1.00 62.55  ? 604  PRO A N   1 
ATOM   4365 C CA  . PRO A 1 605 ? 9.351   -30.743 11.355  1.00 52.73  ? 604  PRO A CA  1 
ATOM   4366 C C   . PRO A 1 605 ? 10.856  -30.968 11.080  1.00 45.41  ? 604  PRO A C   1 
ATOM   4367 O O   . PRO A 1 605 ? 11.367  -30.512 10.055  1.00 48.01  ? 604  PRO A O   1 
ATOM   4368 C CB  . PRO A 1 605 ? 9.112   -29.771 12.510  1.00 42.81  ? 604  PRO A CB  1 
ATOM   4369 C CG  . PRO A 1 605 ? 7.748   -30.216 13.079  1.00 39.12  ? 604  PRO A CG  1 
ATOM   4370 C CD  . PRO A 1 605 ? 7.791   -31.722 12.979  1.00 50.68  ? 604  PRO A CD  1 
ATOM   4371 N N   . ALA A 1 606 ? 11.546  -31.686 11.955  1.00 43.90  ? 605  ALA A N   1 
ATOM   4372 C CA  . ALA A 1 606 ? 12.911  -32.126 11.669  1.00 41.47  ? 605  ALA A CA  1 
ATOM   4373 C C   . ALA A 1 606 ? 13.034  -32.902 10.351  1.00 53.67  ? 605  ALA A C   1 
ATOM   4374 O O   . ALA A 1 606 ? 13.953  -32.686 9.569   1.00 55.64  ? 605  ALA A O   1 
ATOM   4375 C CB  . ALA A 1 606 ? 13.434  -32.969 12.807  1.00 34.55  ? 605  ALA A CB  1 
ATOM   4376 N N   . GLU A 1 607 ? 12.119  -33.823 10.092  1.00 47.61  ? 606  GLU A N   1 
ATOM   4377 C CA  . GLU A 1 607 ? 12.268  -34.611 8.886   1.00 55.21  ? 606  GLU A CA  1 
ATOM   4378 C C   . GLU A 1 607 ? 12.017  -33.783 7.623   1.00 52.44  ? 606  GLU A C   1 
ATOM   4379 O O   . GLU A 1 607 ? 12.645  -33.999 6.580   1.00 51.27  ? 606  GLU A O   1 
ATOM   4380 C CB  . GLU A 1 607 ? 11.396  -35.863 8.954   1.00 55.09  ? 606  GLU A CB  1 
ATOM   4381 C CG  . GLU A 1 607 ? 11.884  -36.833 10.016  1.00 62.82  ? 606  GLU A CG  1 
ATOM   4382 C CD  . GLU A 1 607 ? 10.931  -38.003 10.260  1.00 75.40  ? 606  GLU A CD  1 
ATOM   4383 O OE1 . GLU A 1 607 ? 9.683   -37.817 10.129  1.00 58.78  ? 606  GLU A OE1 1 
ATOM   4384 O OE2 . GLU A 1 607 ? 11.452  -39.101 10.596  1.00 78.66  ? 606  GLU A OE2 1 
ATOM   4385 N N   . PHE A 1 608 ? 11.094  -32.840 7.729   1.00 46.81  ? 607  PHE A N   1 
ATOM   4386 C CA  . PHE A 1 608 ? 10.788  -31.938 6.627   1.00 54.74  ? 607  PHE A CA  1 
ATOM   4387 C C   . PHE A 1 608 ? 11.962  -31.002 6.313   1.00 60.79  ? 607  PHE A C   1 
ATOM   4388 O O   . PHE A 1 608 ? 12.249  -30.732 5.151   1.00 62.90  ? 607  PHE A O   1 
ATOM   4389 C CB  . PHE A 1 608 ? 9.529   -31.148 6.943   1.00 48.22  ? 607  PHE A CB  1 
ATOM   4390 C CG  . PHE A 1 608 ? 9.108   -30.232 5.860   1.00 51.81  ? 607  PHE A CG  1 
ATOM   4391 C CD1 . PHE A 1 608 ? 8.401   -30.702 4.786   1.00 50.65  ? 607  PHE A CD1 1 
ATOM   4392 C CD2 . PHE A 1 608 ? 9.420   -28.881 5.917   1.00 64.60  ? 607  PHE A CD2 1 
ATOM   4393 C CE1 . PHE A 1 608 ? 8.003   -29.836 3.780   1.00 55.99  ? 607  PHE A CE1 1 
ATOM   4394 C CE2 . PHE A 1 608 ? 9.034   -28.014 4.915   1.00 57.16  ? 607  PHE A CE2 1 
ATOM   4395 C CZ  . PHE A 1 608 ? 8.326   -28.485 3.846   1.00 48.79  ? 607  PHE A CZ  1 
ATOM   4396 N N   . VAL A 1 609 ? 12.641  -30.518 7.348   1.00 51.97  ? 608  VAL A N   1 
ATOM   4397 C CA  . VAL A 1 609 ? 13.872  -29.746 7.165   1.00 54.37  ? 608  VAL A CA  1 
ATOM   4398 C C   . VAL A 1 609 ? 14.966  -30.536 6.405   1.00 59.33  ? 608  VAL A C   1 
ATOM   4399 O O   . VAL A 1 609 ? 15.654  -29.991 5.542   1.00 77.15  ? 608  VAL A O   1 
ATOM   4400 C CB  . VAL A 1 609 ? 14.429  -29.204 8.537   1.00 44.89  ? 608  VAL A CB  1 
ATOM   4401 C CG1 . VAL A 1 609 ? 15.855  -28.806 8.409   1.00 37.08  ? 608  VAL A CG1 1 
ATOM   4402 C CG2 . VAL A 1 609 ? 13.619  -28.008 9.049   1.00 46.34  ? 608  VAL A CG2 1 
ATOM   4403 N N   . GLU A 1 610 ? 15.116  -31.816 6.732   1.00 59.09  ? 609  GLU A N   1 
ATOM   4404 C CA  . GLU A 1 610 ? 16.085  -32.709 6.091   1.00 54.40  ? 609  GLU A CA  1 
ATOM   4405 C C   . GLU A 1 610 ? 15.732  -32.977 4.627   1.00 52.92  ? 609  GLU A C   1 
ATOM   4406 O O   . GLU A 1 610 ? 16.600  -33.101 3.774   1.00 53.29  ? 609  GLU A O   1 
ATOM   4407 C CB  . GLU A 1 610 ? 16.151  -34.044 6.855   1.00 51.11  ? 609  GLU A CB  1 
ATOM   4408 C CG  . GLU A 1 610 ? 17.318  -34.925 6.484   1.00 77.80  ? 609  GLU A CG  1 
ATOM   4409 C CD  . GLU A 1 610 ? 18.642  -34.165 6.539   1.00 115.98 ? 609  GLU A CD  1 
ATOM   4410 O OE1 . GLU A 1 610 ? 18.762  -33.211 7.351   1.00 110.07 ? 609  GLU A OE1 1 
ATOM   4411 O OE2 . GLU A 1 610 ? 19.562  -34.520 5.763   1.00 134.76 ? 609  GLU A OE2 1 
ATOM   4412 N N   . LEU A 1 611 ? 14.441  -33.073 4.351   1.00 48.67  ? 610  LEU A N   1 
ATOM   4413 C CA  . LEU A 1 611 ? 13.960  -33.396 3.030   1.00 50.61  ? 610  LEU A CA  1 
ATOM   4414 C C   . LEU A 1 611 ? 14.210  -32.230 2.118   1.00 57.56  ? 610  LEU A C   1 
ATOM   4415 O O   . LEU A 1 611 ? 14.597  -32.405 0.973   1.00 67.65  ? 610  LEU A O   1 
ATOM   4416 C CB  . LEU A 1 611 ? 12.448  -33.687 3.070   1.00 55.07  ? 610  LEU A CB  1 
ATOM   4417 C CG  . LEU A 1 611 ? 11.889  -35.107 3.134   1.00 52.58  ? 610  LEU A CG  1 
ATOM   4418 C CD1 . LEU A 1 611 ? 12.996  -36.147 3.341   1.00 41.85  ? 610  LEU A CD1 1 
ATOM   4419 C CD2 . LEU A 1 611 ? 10.791  -35.180 4.227   1.00 40.60  ? 610  LEU A CD2 1 
ATOM   4420 N N   . VAL A 1 612 ? 13.937  -31.035 2.625   1.00 63.28  ? 611  VAL A N   1 
ATOM   4421 C CA  . VAL A 1 612 ? 14.037  -29.831 1.824   1.00 56.84  ? 611  VAL A CA  1 
ATOM   4422 C C   . VAL A 1 612 ? 15.496  -29.564 1.529   1.00 56.07  ? 611  VAL A C   1 
ATOM   4423 O O   . VAL A 1 612 ? 15.844  -29.122 0.446   1.00 58.86  ? 611  VAL A O   1 
ATOM   4424 C CB  . VAL A 1 612 ? 13.417  -28.634 2.537   1.00 50.94  ? 611  VAL A CB  1 
ATOM   4425 C CG1 . VAL A 1 612 ? 13.811  -27.362 1.850   1.00 55.66  ? 611  VAL A CG1 1 
ATOM   4426 C CG2 . VAL A 1 612 ? 11.909  -28.769 2.551   1.00 50.22  ? 611  VAL A CG2 1 
ATOM   4427 N N   . SER A 1 613 ? 16.351  -29.870 2.492   1.00 54.90  ? 612  SER A N   1 
ATOM   4428 C CA  . SER A 1 613 ? 17.776  -29.702 2.307   1.00 61.48  ? 612  SER A CA  1 
ATOM   4429 C C   . SER A 1 613 ? 18.341  -30.673 1.261   1.00 71.37  ? 612  SER A C   1 
ATOM   4430 O O   . SER A 1 613 ? 19.420  -30.442 0.704   1.00 88.04  ? 612  SER A O   1 
ATOM   4431 C CB  . SER A 1 613 ? 18.501  -29.837 3.650   1.00 60.54  ? 612  SER A CB  1 
ATOM   4432 O OG  . SER A 1 613 ? 18.639  -31.197 4.013   1.00 75.56  ? 612  SER A OG  1 
ATOM   4433 N N   . LEU A 1 614 ? 17.604  -31.747 0.986   1.00 69.43  ? 613  LEU A N   1 
ATOM   4434 C CA  . LEU A 1 614 ? 18.033  -32.793 0.038   1.00 68.39  ? 613  LEU A CA  1 
ATOM   4435 C C   . LEU A 1 614 ? 17.531  -32.598 -1.403  1.00 68.12  ? 613  LEU A C   1 
ATOM   4436 O O   . LEU A 1 614 ? 17.946  -33.314 -2.311  1.00 75.93  ? 613  LEU A O   1 
ATOM   4437 C CB  . LEU A 1 614 ? 17.609  -34.181 0.536   1.00 59.62  ? 613  LEU A CB  1 
ATOM   4438 C CG  . LEU A 1 614 ? 18.376  -34.724 1.736   1.00 65.62  ? 613  LEU A CG  1 
ATOM   4439 C CD1 . LEU A 1 614 ? 17.784  -36.034 2.233   1.00 58.50  ? 613  LEU A CD1 1 
ATOM   4440 C CD2 . LEU A 1 614 ? 19.830  -34.896 1.374   1.00 77.73  ? 613  LEU A CD2 1 
ATOM   4441 N N   . LEU A 1 615 ? 16.655  -31.620 -1.606  1.00 59.87  ? 614  LEU A N   1 
ATOM   4442 C CA  . LEU A 1 615 ? 16.018  -31.402 -2.903  1.00 62.14  ? 614  LEU A CA  1 
ATOM   4443 C C   . LEU A 1 615 ? 16.979  -31.203 -4.080  1.00 72.99  ? 614  LEU A C   1 
ATOM   4444 O O   . LEU A 1 615 ? 16.603  -31.425 -5.232  1.00 85.31  ? 614  LEU A O   1 
ATOM   4445 C CB  . LEU A 1 615 ? 14.998  -30.259 -2.819  1.00 55.11  ? 614  LEU A CB  1 
ATOM   4446 C CG  . LEU A 1 615 ? 13.801  -30.615 -1.927  1.00 59.57  ? 614  LEU A CG  1 
ATOM   4447 C CD1 . LEU A 1 615 ? 12.981  -29.393 -1.525  1.00 68.38  ? 614  LEU A CD1 1 
ATOM   4448 C CD2 . LEU A 1 615 ? 12.928  -31.672 -2.596  1.00 52.63  ? 614  LEU A CD2 1 
ATOM   4449 N N   . ASP A 1 616 ? 18.215  -30.805 -3.794  1.00 73.57  ? 615  ASP A N   1 
ATOM   4450 C CA  . ASP A 1 616 ? 19.186  -30.526 -4.854  1.00 71.96  ? 615  ASP A CA  1 
ATOM   4451 C C   . ASP A 1 616 ? 20.348  -31.518 -4.857  1.00 71.96  ? 615  ASP A C   1 
ATOM   4452 O O   . ASP A 1 616 ? 21.307  -31.359 -5.596  1.00 79.45  ? 615  ASP A O   1 
ATOM   4453 C CB  . ASP A 1 616 ? 19.690  -29.068 -4.786  1.00 73.85  ? 615  ASP A CB  1 
ATOM   4454 C CG  . ASP A 1 616 ? 20.484  -28.746 -3.509  1.00 82.39  ? 615  ASP A CG  1 
ATOM   4455 O OD1 . ASP A 1 616 ? 20.424  -29.515 -2.517  1.00 82.66  ? 615  ASP A OD1 1 
ATOM   4456 O OD2 . ASP A 1 616 ? 21.174  -27.696 -3.507  1.00 86.94  ? 615  ASP A OD2 1 
ATOM   4457 N N   . LYS A 1 617 ? 20.245  -32.548 -4.029  1.00 77.97  ? 616  LYS A N   1 
ATOM   4458 C CA  . LYS A 1 617 ? 21.308  -33.529 -3.888  1.00 88.19  ? 616  LYS A CA  1 
ATOM   4459 C C   . LYS A 1 617 ? 20.845  -34.932 -4.326  1.00 110.63 ? 616  LYS A C   1 
ATOM   4460 O O   . LYS A 1 617 ? 21.656  -35.818 -4.627  1.00 119.21 ? 616  LYS A O   1 
ATOM   4461 C CB  . LYS A 1 617 ? 21.808  -33.513 -2.437  1.00 83.72  ? 616  LYS A CB  1 
ATOM   4462 C CG  . LYS A 1 617 ? 22.289  -32.133 -2.007  1.00 95.80  ? 616  LYS A CG  1 
ATOM   4463 C CD  . LYS A 1 617 ? 22.584  -32.004 -0.516  1.00 108.29 ? 616  LYS A CD  1 
ATOM   4464 C CE  . LYS A 1 617 ? 22.741  -30.524 -0.137  1.00 114.20 ? 616  LYS A CE  1 
ATOM   4465 N NZ  . LYS A 1 617 ? 23.262  -30.317 1.243   1.00 117.27 ? 616  LYS A NZ  1 
ATOM   4466 N N   . ALA A 1 618 ? 19.640  -35.212 -4.408  1.00 110.23 ? 617  ALA A N   1 
ATOM   4467 N N   . ASP B 2 2   ? -12.128 -65.419 -11.328 1.00 190.20 ? 2    ASP B N   1 
ATOM   4468 C CA  . ASP B 2 2   ? -11.908 -64.746 -12.604 1.00 192.36 ? 2    ASP B CA  1 
ATOM   4469 C C   . ASP B 2 2   ? -10.495 -64.969 -13.131 1.00 182.77 ? 2    ASP B C   1 
ATOM   4470 O O   . ASP B 2 2   ? -10.287 -65.760 -14.052 1.00 181.04 ? 2    ASP B O   1 
ATOM   4471 C CB  . ASP B 2 2   ? -12.185 -63.243 -12.485 1.00 198.69 ? 2    ASP B CB  1 
ATOM   4472 C CG  . ASP B 2 2   ? -13.596 -62.870 -12.914 1.00 201.16 ? 2    ASP B CG  1 
ATOM   4473 O OD1 . ASP B 2 2   ? -14.377 -63.785 -13.256 1.00 200.77 ? 2    ASP B OD1 1 
ATOM   4474 O OD2 . ASP B 2 2   ? -13.920 -61.662 -12.913 1.00 199.45 ? 2    ASP B OD2 1 
ATOM   4475 N N   . ARG B 2 3   ? -9.529  -64.269 -12.543 1.00 171.57 ? 3    ARG B N   1 
ATOM   4476 C CA  . ARG B 2 3   ? -8.157  -64.314 -13.036 1.00 164.70 ? 3    ARG B CA  1 
ATOM   4477 C C   . ARG B 2 3   ? -7.521  -65.685 -12.826 1.00 155.97 ? 3    ARG B C   1 
ATOM   4478 O O   . ARG B 2 3   ? -6.410  -65.929 -13.291 1.00 158.79 ? 3    ARG B O   1 
ATOM   4479 C CB  . ARG B 2 3   ? -7.297  -63.215 -12.400 1.00 168.67 ? 3    ARG B CB  1 
ATOM   4480 C CG  . ARG B 2 3   ? -7.962  -61.842 -12.344 1.00 174.64 ? 3    ARG B CG  1 
ATOM   4481 C CD  . ARG B 2 3   ? -8.707  -61.644 -11.020 1.00 176.97 ? 3    ARG B CD  1 
ATOM   4482 N NE  . ARG B 2 3   ? -9.527  -60.432 -11.002 1.00 173.41 ? 3    ARG B NE  1 
ATOM   4483 C CZ  . ARG B 2 3   ? -10.106 -59.933 -9.911  1.00 162.44 ? 3    ARG B CZ  1 
ATOM   4484 N NH1 . ARG B 2 3   ? -9.948  -60.533 -8.740  1.00 154.69 ? 3    ARG B NH1 1 
ATOM   4485 N NH2 . ARG B 2 3   ? -10.837 -58.829 -9.988  1.00 159.84 ? 3    ARG B NH2 1 
ATOM   4486 N N   . LEU B 2 4   ? -8.225  -66.574 -12.126 1.00 148.05 ? 4    LEU B N   1 
ATOM   4487 C CA  . LEU B 2 4   ? -7.756  -67.951 -11.935 1.00 136.06 ? 4    LEU B CA  1 
ATOM   4488 C C   . LEU B 2 4   ? -8.098  -68.812 -13.144 1.00 138.50 ? 4    LEU B C   1 
ATOM   4489 O O   . LEU B 2 4   ? -7.279  -69.621 -13.585 1.00 137.80 ? 4    LEU B O   1 
ATOM   4490 C CB  . LEU B 2 4   ? -8.336  -68.568 -10.654 1.00 122.60 ? 4    LEU B CB  1 
ATOM   4491 C CG  . LEU B 2 4   ? -7.955  -70.005 -10.236 1.00 104.49 ? 4    LEU B CG  1 
ATOM   4492 C CD1 . LEU B 2 4   ? -8.882  -71.053 -10.861 1.00 111.04 ? 4    LEU B CD1 1 
ATOM   4493 C CD2 . LEU B 2 4   ? -6.476  -70.346 -10.487 1.00 78.36  ? 4    LEU B CD2 1 
ATOM   4494 N N   . SER B 2 5   ? -9.309  -68.639 -13.673 1.00 139.37 ? 5    SER B N   1 
ATOM   4495 C CA  . SER B 2 5   ? -9.706  -69.316 -14.903 1.00 139.90 ? 5    SER B CA  1 
ATOM   4496 C C   . SER B 2 5   ? -8.711  -68.996 -16.010 1.00 142.47 ? 5    SER B C   1 
ATOM   4497 O O   . SER B 2 5   ? -8.181  -69.898 -16.660 1.00 140.05 ? 5    SER B O   1 
ATOM   4498 C CB  . SER B 2 5   ? -11.115 -68.894 -15.337 1.00 141.90 ? 5    SER B CB  1 
ATOM   4499 O OG  . SER B 2 5   ? -12.119 -69.549 -14.578 1.00 143.36 ? 5    SER B OG  1 
ATOM   4500 N N   . ARG B 2 6   ? -8.455  -67.704 -16.202 1.00 147.49 ? 6    ARG B N   1 
ATOM   4501 C CA  . ARG B 2 6   ? -7.579  -67.221 -17.266 1.00 153.48 ? 6    ARG B CA  1 
ATOM   4502 C C   . ARG B 2 6   ? -6.167  -67.804 -17.179 1.00 140.78 ? 6    ARG B C   1 
ATOM   4503 O O   . ARG B 2 6   ? -5.469  -67.893 -18.186 1.00 137.50 ? 6    ARG B O   1 
ATOM   4504 C CB  . ARG B 2 6   ? -7.517  -65.689 -17.255 1.00 172.41 ? 6    ARG B CB  1 
ATOM   4505 C CG  . ARG B 2 6   ? -8.875  -64.987 -17.375 1.00 188.29 ? 6    ARG B CG  1 
ATOM   4506 C CD  . ARG B 2 6   ? -8.762  -63.489 -17.055 1.00 197.60 ? 6    ARG B CD  1 
ATOM   4507 N NE  . ARG B 2 6   ? -10.058 -62.807 -17.039 1.00 201.20 ? 6    ARG B NE  1 
ATOM   4508 C CZ  . ARG B 2 6   ? -10.248 -61.560 -16.612 1.00 199.99 ? 6    ARG B CZ  1 
ATOM   4509 N NH1 . ARG B 2 6   ? -9.226  -60.844 -16.156 1.00 199.19 ? 6    ARG B NH1 1 
ATOM   4510 N NH2 . ARG B 2 6   ? -11.463 -61.027 -16.637 1.00 197.89 ? 6    ARG B NH2 1 
ATOM   4511 N N   . LEU B 2 7   ? -5.752  -68.196 -15.977 1.00 137.77 ? 7    LEU B N   1 
ATOM   4512 C CA  . LEU B 2 7   ? -4.431  -68.800 -15.767 1.00 131.59 ? 7    LEU B CA  1 
ATOM   4513 C C   . LEU B 2 7   ? -4.423  -70.276 -16.166 1.00 129.11 ? 7    LEU B C   1 
ATOM   4514 O O   . LEU B 2 7   ? -3.517  -70.733 -16.861 1.00 124.99 ? 7    LEU B O   1 
ATOM   4515 C CB  . LEU B 2 7   ? -3.975  -68.637 -14.304 1.00 119.03 ? 7    LEU B CB  1 
ATOM   4516 C CG  . LEU B 2 7   ? -2.484  -68.788 -13.953 1.00 109.17 ? 7    LEU B CG  1 
ATOM   4517 C CD1 . LEU B 2 7   ? -2.130  -70.169 -13.440 1.00 97.84  ? 7    LEU B CD1 1 
ATOM   4518 C CD2 . LEU B 2 7   ? -1.587  -68.413 -15.130 1.00 116.70 ? 7    LEU B CD2 1 
ATOM   4519 N N   . ARG B 2 8   ? -5.438  -71.015 -15.725 1.00 131.14 ? 8    ARG B N   1 
ATOM   4520 C CA  . ARG B 2 8   ? -5.528  -72.443 -16.016 1.00 136.07 ? 8    ARG B CA  1 
ATOM   4521 C C   . ARG B 2 8   ? -5.823  -72.702 -17.494 1.00 140.85 ? 8    ARG B C   1 
ATOM   4522 O O   . ARG B 2 8   ? -5.510  -73.770 -18.025 1.00 143.02 ? 8    ARG B O   1 
ATOM   4523 C CB  . ARG B 2 8   ? -6.562  -73.121 -15.108 1.00 135.57 ? 8    ARG B CB  1 
ATOM   4524 C CG  . ARG B 2 8   ? -5.988  -73.630 -13.785 1.00 130.49 ? 8    ARG B CG  1 
ATOM   4525 C CD  . ARG B 2 8   ? -7.074  -73.867 -12.740 1.00 125.72 ? 8    ARG B CD  1 
ATOM   4526 N NE  . ARG B 2 8   ? -6.525  -74.406 -11.497 1.00 124.30 ? 8    ARG B NE  1 
ATOM   4527 C CZ  . ARG B 2 8   ? -7.232  -74.590 -10.386 1.00 126.73 ? 8    ARG B CZ  1 
ATOM   4528 N NH1 . ARG B 2 8   ? -8.518  -74.267 -10.362 1.00 128.25 ? 8    ARG B NH1 1 
ATOM   4529 N NH2 . ARG B 2 8   ? -6.657  -75.094 -9.299  1.00 124.74 ? 8    ARG B NH2 1 
ATOM   4530 N N   . GLN B 2 9   ? -6.426  -71.721 -18.156 1.00 141.07 ? 9    GLN B N   1 
ATOM   4531 C CA  . GLN B 2 9   ? -6.594  -71.778 -19.600 1.00 143.81 ? 9    GLN B CA  1 
ATOM   4532 C C   . GLN B 2 9   ? -5.241  -71.587 -20.271 1.00 157.45 ? 9    GLN B C   1 
ATOM   4533 O O   . GLN B 2 9   ? -4.885  -72.322 -21.190 1.00 164.21 ? 9    GLN B O   1 
ATOM   4534 C CB  . GLN B 2 9   ? -7.562  -70.696 -20.077 1.00 140.94 ? 9    GLN B CB  1 
ATOM   4535 C CG  . GLN B 2 9   ? -7.570  -70.498 -21.586 1.00 145.52 ? 9    GLN B CG  1 
ATOM   4536 C CD  . GLN B 2 9   ? -8.249  -69.204 -22.002 1.00 149.92 ? 9    GLN B CD  1 
ATOM   4537 O OE1 . GLN B 2 9   ? -8.843  -68.509 -21.176 1.00 153.55 ? 9    GLN B OE1 1 
ATOM   4538 N NE2 . GLN B 2 9   ? -8.160  -68.873 -23.289 1.00 146.51 ? 9    GLN B NE2 1 
ATOM   4539 N N   . MET B 2 10  ? -4.487  -70.600 -19.793 1.00 163.76 ? 10   MET B N   1 
ATOM   4540 C CA  . MET B 2 10  ? -3.196  -70.237 -20.375 1.00 165.03 ? 10   MET B CA  1 
ATOM   4541 C C   . MET B 2 10  ? -2.056  -71.171 -19.949 1.00 158.94 ? 10   MET B C   1 
ATOM   4542 O O   . MET B 2 10  ? -0.894  -70.938 -20.283 1.00 154.94 ? 10   MET B O   1 
ATOM   4543 C CB  . MET B 2 10  ? -2.853  -68.781 -20.028 1.00 171.03 ? 10   MET B CB  1 
ATOM   4544 C CG  . MET B 2 10  ? -3.831  -67.755 -20.606 1.00 175.94 ? 10   MET B CG  1 
ATOM   4545 S SD  . MET B 2 10  ? -3.665  -66.101 -19.896 1.00 160.59 ? 10   MET B SD  1 
ATOM   4546 C CE  . MET B 2 10  ? -4.882  -65.197 -20.863 1.00 155.55 ? 10   MET B CE  1 
ATOM   4547 N N   . ALA B 2 11  ? -2.392  -72.228 -19.216 1.00 159.35 ? 11   ALA B N   1 
ATOM   4548 C CA  . ALA B 2 11  ? -1.392  -73.194 -18.773 1.00 160.79 ? 11   ALA B CA  1 
ATOM   4549 C C   . ALA B 2 11  ? -1.660  -74.567 -19.379 1.00 170.90 ? 11   ALA B C   1 
ATOM   4550 O O   . ALA B 2 11  ? -0.791  -75.441 -19.372 1.00 171.14 ? 11   ALA B O   1 
ATOM   4551 C CB  . ALA B 2 11  ? -1.367  -73.277 -17.257 1.00 154.15 ? 11   ALA B CB  1 
ATOM   4552 N N   . ALA B 2 12  ? -2.871  -74.745 -19.902 1.00 178.06 ? 12   ALA B N   1 
ATOM   4553 C CA  . ALA B 2 12  ? -3.259  -75.992 -20.555 1.00 182.87 ? 12   ALA B CA  1 
ATOM   4554 C C   . ALA B 2 12  ? -2.976  -75.939 -22.057 1.00 191.44 ? 12   ALA B C   1 
ATOM   4555 O O   . ALA B 2 12  ? -3.165  -76.928 -22.767 1.00 194.29 ? 12   ALA B O   1 
ATOM   4556 C CB  . ALA B 2 12  ? -4.731  -76.296 -20.295 1.00 181.10 ? 12   ALA B CB  1 
ATOM   4557 N N   . GLU B 2 13  ? -2.525  -74.778 -22.529 1.00 195.97 ? 13   GLU B N   1 
ATOM   4558 C CA  . GLU B 2 13  ? -2.130  -74.593 -23.926 1.00 194.76 ? 13   GLU B CA  1 
ATOM   4559 C C   . GLU B 2 13  ? -0.636  -74.859 -24.106 1.00 192.58 ? 13   GLU B C   1 
ATOM   4560 O O   . GLU B 2 13  ? 0.008   -74.293 -24.992 1.00 187.48 ? 13   GLU B O   1 
ATOM   4561 C CB  . GLU B 2 13  ? -2.455  -73.173 -24.397 1.00 192.37 ? 13   GLU B CB  1 
ATOM   4562 C CG  . GLU B 2 13  ? -3.930  -72.808 -24.352 1.00 190.60 ? 13   GLU B CG  1 
ATOM   4563 C CD  . GLU B 2 13  ? -4.176  -71.353 -24.715 1.00 188.30 ? 13   GLU B CD  1 
ATOM   4564 O OE1 . GLU B 2 13  ? -3.189  -70.632 -24.981 1.00 184.56 ? 13   GLU B OE1 1 
ATOM   4565 O OE2 . GLU B 2 13  ? -5.353  -70.932 -24.731 1.00 188.50 ? 13   GLU B OE2 1 
ATOM   4566 N N   . ASN B 2 14  ? -0.094  -75.717 -23.248 1.00 194.82 ? 14   ASN B N   1 
ATOM   4567 C CA  . ASN B 2 14  ? 1.316   -76.078 -23.288 1.00 193.08 ? 14   ASN B CA  1 
ATOM   4568 C C   . ASN B 2 14  ? 1.457   -77.592 -23.384 1.00 186.71 ? 14   ASN B C   1 
ATOM   4569 O O   . ASN B 2 14  ? 2.393   -78.106 -23.999 1.00 183.36 ? 14   ASN B O   1 
ATOM   4570 C CB  . ASN B 2 14  ? 2.030   -75.565 -22.033 1.00 194.77 ? 14   ASN B CB  1 
ATOM   4571 C CG  . ASN B 2 14  ? 1.790   -74.083 -21.785 1.00 191.73 ? 14   ASN B CG  1 
ATOM   4572 O OD1 . ASN B 2 14  ? 1.612   -73.652 -20.644 1.00 186.95 ? 14   ASN B OD1 1 
ATOM   4573 N ND2 . ASN B 2 14  ? 1.780   -73.297 -22.857 1.00 192.85 ? 14   ASN B ND2 1 
ATOM   4574 N N   . GLN B 2 15  ? 0.506   -78.293 -22.770 1.00 183.35 ? 15   GLN B N   1 
ATOM   4575 C CA  . GLN B 2 15  ? 0.472   -79.752 -22.770 1.00 177.98 ? 15   GLN B CA  1 
ATOM   4576 C C   . GLN B 2 15  ? -0.422  -80.285 -23.889 1.00 166.87 ? 15   GLN B C   1 
ATOM   4577 O O   . GLN B 2 15  ? -1.625  -80.475 -23.702 1.00 155.31 ? 15   GLN B O   1 
ATOM   4578 C CB  . GLN B 2 15  ? -0.031  -80.268 -21.419 1.00 179.31 ? 15   GLN B CB  1 
ATOM   4579 C CG  . GLN B 2 15  ? 0.715   -79.708 -20.215 1.00 177.94 ? 15   GLN B CG  1 
ATOM   4580 C CD  . GLN B 2 15  ? 0.046   -80.068 -18.901 1.00 176.83 ? 15   GLN B CD  1 
ATOM   4581 O OE1 . GLN B 2 15  ? -0.955  -80.789 -18.878 1.00 177.19 ? 15   GLN B OE1 1 
ATOM   4582 N NE2 . GLN B 2 15  ? 0.593   -79.565 -17.797 1.00 171.10 ? 15   GLN B NE2 1 
ATOM   4583 N N   . PRO B 2 39  ? 3.593   -86.863 4.071   1.00 155.74 ? 39   PRO B N   1 
ATOM   4584 C CA  . PRO B 2 39  ? 4.124   -85.710 4.808   1.00 157.30 ? 39   PRO B CA  1 
ATOM   4585 C C   . PRO B 2 39  ? 4.214   -85.998 6.303   1.00 166.33 ? 39   PRO B C   1 
ATOM   4586 O O   . PRO B 2 39  ? 3.517   -86.885 6.793   1.00 164.58 ? 39   PRO B O   1 
ATOM   4587 C CB  . PRO B 2 39  ? 3.088   -84.617 4.537   1.00 148.55 ? 39   PRO B CB  1 
ATOM   4588 C CG  . PRO B 2 39  ? 2.505   -84.980 3.220   1.00 149.57 ? 39   PRO B CG  1 
ATOM   4589 C CD  . PRO B 2 39  ? 2.490   -86.485 3.170   1.00 153.16 ? 39   PRO B CD  1 
ATOM   4590 N N   . GLU B 2 40  ? 5.065   -85.259 7.011   1.00 175.66 ? 40   GLU B N   1 
ATOM   4591 C CA  . GLU B 2 40  ? 5.261   -85.453 8.450   1.00 179.10 ? 40   GLU B CA  1 
ATOM   4592 C C   . GLU B 2 40  ? 4.356   -84.537 9.280   1.00 173.41 ? 40   GLU B C   1 
ATOM   4593 O O   . GLU B 2 40  ? 3.957   -83.468 8.819   1.00 175.26 ? 40   GLU B O   1 
ATOM   4594 C CB  . GLU B 2 40  ? 6.732   -85.235 8.830   1.00 182.07 ? 40   GLU B CB  1 
ATOM   4595 C CG  . GLU B 2 40  ? 7.705   -86.223 8.192   1.00 184.21 ? 40   GLU B CG  1 
ATOM   4596 C CD  . GLU B 2 40  ? 7.499   -87.654 8.668   1.00 185.39 ? 40   GLU B CD  1 
ATOM   4597 O OE1 . GLU B 2 40  ? 6.852   -87.850 9.718   1.00 184.76 ? 40   GLU B OE1 1 
ATOM   4598 O OE2 . GLU B 2 40  ? 7.990   -88.584 7.994   1.00 186.16 ? 40   GLU B OE2 1 
ATOM   4599 N N   . PRO B 2 41  ? 4.035   -84.954 10.515  1.00 162.31 ? 41   PRO B N   1 
ATOM   4600 C CA  . PRO B 2 41  ? 3.114   -84.219 11.392  1.00 155.06 ? 41   PRO B CA  1 
ATOM   4601 C C   . PRO B 2 41  ? 3.506   -82.755 11.594  1.00 144.67 ? 41   PRO B C   1 
ATOM   4602 O O   . PRO B 2 41  ? 2.810   -81.854 11.112  1.00 140.37 ? 41   PRO B O   1 
ATOM   4603 C CB  . PRO B 2 41  ? 3.229   -84.971 12.720  1.00 157.82 ? 41   PRO B CB  1 
ATOM   4604 C CG  . PRO B 2 41  ? 3.644   -86.347 12.338  1.00 157.96 ? 41   PRO B CG  1 
ATOM   4605 C CD  . PRO B 2 41  ? 4.542   -86.181 11.152  1.00 159.30 ? 41   PRO B CD  1 
ATOM   4606 N N   . PHE B 2 42  ? 4.603   -82.537 12.314  1.00 136.12 ? 42   PHE B N   1 
ATOM   4607 C CA  . PHE B 2 42  ? 5.083   -81.196 12.655  1.00 128.61 ? 42   PHE B CA  1 
ATOM   4608 C C   . PHE B 2 42  ? 4.400   -80.621 13.894  1.00 113.20 ? 42   PHE B C   1 
ATOM   4609 O O   . PHE B 2 42  ? 3.327   -80.023 13.810  1.00 88.53  ? 42   PHE B O   1 
ATOM   4610 C CB  . PHE B 2 42  ? 4.956   -80.226 11.478  1.00 126.39 ? 42   PHE B CB  1 
ATOM   4611 C CG  . PHE B 2 42  ? 5.386   -78.826 11.805  1.00 124.75 ? 42   PHE B CG  1 
ATOM   4612 C CD1 . PHE B 2 42  ? 6.716   -78.541 12.074  1.00 118.04 ? 42   PHE B CD1 1 
ATOM   4613 C CD2 . PHE B 2 42  ? 4.464   -77.796 11.850  1.00 127.51 ? 42   PHE B CD2 1 
ATOM   4614 C CE1 . PHE B 2 42  ? 7.117   -77.260 12.382  1.00 109.92 ? 42   PHE B CE1 1 
ATOM   4615 C CE2 . PHE B 2 42  ? 4.860   -76.508 12.156  1.00 125.11 ? 42   PHE B CE2 1 
ATOM   4616 C CZ  . PHE B 2 42  ? 6.190   -76.241 12.423  1.00 116.90 ? 42   PHE B CZ  1 
ATOM   4617 N N   . MET B 2 43  ? 5.038   -80.825 15.043  1.00 118.89 ? 43   MET B N   1 
ATOM   4618 C CA  . MET B 2 43  ? 4.572   -80.277 16.310  1.00 115.61 ? 43   MET B CA  1 
ATOM   4619 C C   . MET B 2 43  ? 3.131   -80.674 16.630  1.00 101.14 ? 43   MET B C   1 
ATOM   4620 O O   . MET B 2 43  ? 2.325   -79.856 17.075  1.00 91.68  ? 43   MET B O   1 
ATOM   4621 C CB  . MET B 2 43  ? 4.739   -78.763 16.299  1.00 123.89 ? 43   MET B CB  1 
ATOM   4622 C CG  . MET B 2 43  ? 6.128   -78.336 15.860  1.00 126.50 ? 43   MET B CG  1 
ATOM   4623 S SD  . MET B 2 43  ? 6.736   -76.922 16.786  1.00 133.67 ? 43   MET B SD  1 
ATOM   4624 C CE  . MET B 2 43  ? 5.600   -75.674 16.226  1.00 45.13  ? 43   MET B CE  1 
ATOM   4625 N N   . ALA B 2 44  ? 2.827   -81.949 16.419  1.00 98.19  ? 44   ALA B N   1 
ATOM   4626 C CA  . ALA B 2 44  ? 1.475   -82.466 16.614  1.00 104.74 ? 44   ALA B CA  1 
ATOM   4627 C C   . ALA B 2 44  ? 0.933   -82.238 18.025  1.00 103.59 ? 44   ALA B C   1 
ATOM   4628 O O   . ALA B 2 44  ? -0.190  -81.763 18.197  1.00 106.26 ? 44   ALA B O   1 
ATOM   4629 C CB  . ALA B 2 44  ? 1.410   -83.938 16.250  1.00 107.22 ? 44   ALA B CB  1 
ATOM   4630 N N   . ASP B 2 45  ? 1.721   -82.574 19.038  1.00 95.65  ? 45   ASP B N   1 
ATOM   4631 C CA  . ASP B 2 45  ? 1.249   -82.383 20.402  1.00 89.21  ? 45   ASP B CA  1 
ATOM   4632 C C   . ASP B 2 45  ? 1.003   -80.914 20.706  1.00 92.87  ? 45   ASP B C   1 
ATOM   4633 O O   . ASP B 2 45  ? 0.029   -80.576 21.376  1.00 90.76  ? 45   ASP B O   1 
ATOM   4634 C CB  . ASP B 2 45  ? 2.209   -82.978 21.428  1.00 97.89  ? 45   ASP B CB  1 
ATOM   4635 C CG  . ASP B 2 45  ? 1.545   -83.191 22.784  1.00 122.48 ? 45   ASP B CG  1 
ATOM   4636 O OD1 . ASP B 2 45  ? 0.327   -82.918 22.912  1.00 122.55 ? 45   ASP B OD1 1 
ATOM   4637 O OD2 . ASP B 2 45  ? 2.236   -83.641 23.723  1.00 138.41 ? 45   ASP B OD2 1 
ATOM   4638 N N   . PHE B 2 46  ? 1.888   -80.043 20.217  1.00 97.68  ? 46   PHE B N   1 
ATOM   4639 C CA  . PHE B 2 46  ? 1.752   -78.603 20.443  1.00 94.52  ? 46   PHE B CA  1 
ATOM   4640 C C   . PHE B 2 46  ? 0.439   -78.015 19.897  1.00 88.89  ? 46   PHE B C   1 
ATOM   4641 O O   . PHE B 2 46  ? -0.329  -77.392 20.642  1.00 83.84  ? 46   PHE B O   1 
ATOM   4642 C CB  . PHE B 2 46  ? 2.959   -77.843 19.887  1.00 96.10  ? 46   PHE B CB  1 
ATOM   4643 C CG  . PHE B 2 46  ? 2.766   -76.353 19.840  1.00 94.42  ? 46   PHE B CG  1 
ATOM   4644 C CD1 . PHE B 2 46  ? 2.967   -75.578 20.969  1.00 95.56  ? 46   PHE B CD1 1 
ATOM   4645 C CD2 . PHE B 2 46  ? 2.374   -75.728 18.667  1.00 91.77  ? 46   PHE B CD2 1 
ATOM   4646 C CE1 . PHE B 2 46  ? 2.785   -74.208 20.930  1.00 92.00  ? 46   PHE B CE1 1 
ATOM   4647 C CE2 . PHE B 2 46  ? 2.190   -74.363 18.622  1.00 91.35  ? 46   PHE B CE2 1 
ATOM   4648 C CZ  . PHE B 2 46  ? 2.396   -73.601 19.755  1.00 92.59  ? 46   PHE B CZ  1 
ATOM   4649 N N   . PHE B 2 47  ? 0.170   -78.207 18.609  1.00 81.56  ? 47   PHE B N   1 
ATOM   4650 C CA  . PHE B 2 47  ? -1.062  -77.663 18.033  1.00 88.33  ? 47   PHE B CA  1 
ATOM   4651 C C   . PHE B 2 47  ? -2.306  -78.229 18.714  1.00 88.92  ? 47   PHE B C   1 
ATOM   4652 O O   . PHE B 2 47  ? -3.390  -77.628 18.672  1.00 86.86  ? 47   PHE B O   1 
ATOM   4653 C CB  . PHE B 2 47  ? -1.103  -77.859 16.522  1.00 78.78  ? 47   PHE B CB  1 
ATOM   4654 C CG  . PHE B 2 47  ? -0.168  -76.960 15.787  1.00 81.99  ? 47   PHE B CG  1 
ATOM   4655 C CD1 . PHE B 2 47  ? -0.574  -75.691 15.397  1.00 81.23  ? 47   PHE B CD1 1 
ATOM   4656 C CD2 . PHE B 2 47  ? 1.130   -77.362 15.513  1.00 80.03  ? 47   PHE B CD2 1 
ATOM   4657 C CE1 . PHE B 2 47  ? 0.286   -74.852 14.725  1.00 77.71  ? 47   PHE B CE1 1 
ATOM   4658 C CE2 . PHE B 2 47  ? 1.995   -76.529 14.841  1.00 79.32  ? 47   PHE B CE2 1 
ATOM   4659 C CZ  . PHE B 2 47  ? 1.570   -75.269 14.444  1.00 82.25  ? 47   PHE B CZ  1 
ATOM   4660 N N   . ASN B 2 48  ? -2.119  -79.388 19.342  1.00 74.59  ? 48   ASN B N   1 
ATOM   4661 C CA  . ASN B 2 48  ? -3.101  -80.003 20.214  1.00 66.35  ? 48   ASN B CA  1 
ATOM   4662 C C   . ASN B 2 48  ? -3.413  -79.141 21.437  1.00 79.02  ? 48   ASN B C   1 
ATOM   4663 O O   . ASN B 2 48  ? -4.580  -78.869 21.740  1.00 75.71  ? 48   ASN B O   1 
ATOM   4664 C CB  . ASN B 2 48  ? -2.537  -81.326 20.693  1.00 85.13  ? 48   ASN B CB  1 
ATOM   4665 C CG  . ASN B 2 48  ? -3.408  -82.492 20.342  1.00 99.60  ? 48   ASN B CG  1 
ATOM   4666 O OD1 . ASN B 2 48  ? -3.865  -82.627 19.203  1.00 100.98 ? 48   ASN B OD1 1 
ATOM   4667 N ND2 . ASN B 2 48  ? -3.634  -83.365 21.320  1.00 101.32 ? 48   ASN B ND2 1 
ATOM   4668 N N   . ARG B 2 49  ? -2.366  -78.726 22.153  1.00 82.86  ? 49   ARG B N   1 
ATOM   4669 C CA  . ARG B 2 49  ? -2.554  -77.920 23.350  1.00 87.08  ? 49   ARG B CA  1 
ATOM   4670 C C   . ARG B 2 49  ? -3.247  -76.606 23.012  1.00 94.90  ? 49   ARG B C   1 
ATOM   4671 O O   . ARG B 2 49  ? -4.136  -76.162 23.743  1.00 99.26  ? 49   ARG B O   1 
ATOM   4672 C CB  . ARG B 2 49  ? -1.231  -77.602 24.056  1.00 93.42  ? 49   ARG B CB  1 
ATOM   4673 C CG  . ARG B 2 49  ? -0.146  -78.651 23.972  1.00 96.19  ? 49   ARG B CG  1 
ATOM   4674 C CD  . ARG B 2 49  ? 0.885   -78.392 25.061  1.00 92.10  ? 49   ARG B CD  1 
ATOM   4675 N NE  . ARG B 2 49  ? 0.396   -78.886 26.339  1.00 94.40  ? 49   ARG B NE  1 
ATOM   4676 C CZ  . ARG B 2 49  ? 0.701   -80.088 26.817  1.00 106.31 ? 49   ARG B CZ  1 
ATOM   4677 N NH1 . ARG B 2 49  ? 1.516   -80.873 26.120  1.00 104.43 ? 49   ARG B NH1 1 
ATOM   4678 N NH2 . ARG B 2 49  ? 0.212   -80.503 27.986  1.00 106.04 ? 49   ARG B NH2 1 
ATOM   4679 N N   . VAL B 2 50  ? -2.844  -75.959 21.923  1.00 83.73  ? 50   VAL B N   1 
ATOM   4680 C CA  . VAL B 2 50  ? -3.443  -74.659 21.652  1.00 85.25  ? 50   VAL B CA  1 
ATOM   4681 C C   . VAL B 2 50  ? -4.891  -74.770 21.161  1.00 76.61  ? 50   VAL B C   1 
ATOM   4682 O O   . VAL B 2 50  ? -5.734  -73.941 21.522  1.00 66.11  ? 50   VAL B O   1 
ATOM   4683 C CB  . VAL B 2 50  ? -2.529  -73.679 20.838  1.00 102.94 ? 50   VAL B CB  1 
ATOM   4684 C CG1 . VAL B 2 50  ? -1.205  -73.467 21.571  1.00 96.09  ? 50   VAL B CG1 1 
ATOM   4685 C CG2 . VAL B 2 50  ? -2.278  -74.153 19.436  1.00 45.47  ? 50   VAL B CG2 1 
ATOM   4686 N N   . LYS B 2 51  ? -5.190  -75.812 20.383  1.00 78.43  ? 51   LYS B N   1 
ATOM   4687 C CA  . LYS B 2 51  ? -6.585  -76.172 20.121  1.00 73.42  ? 51   LYS B CA  1 
ATOM   4688 C C   . LYS B 2 51  ? -7.313  -76.352 21.459  1.00 80.48  ? 51   LYS B C   1 
ATOM   4689 O O   . LYS B 2 51  ? -8.357  -75.736 21.690  1.00 78.12  ? 51   LYS B O   1 
ATOM   4690 C CB  . LYS B 2 51  ? -6.687  -77.457 19.303  1.00 65.07  ? 51   LYS B CB  1 
ATOM   4691 C CG  . LYS B 2 51  ? -7.522  -77.329 18.032  1.00 71.97  ? 51   LYS B CG  1 
ATOM   4692 C CD  . LYS B 2 51  ? -8.897  -76.767 18.319  1.00 80.07  ? 51   LYS B CD  1 
ATOM   4693 C CE  . LYS B 2 51  ? -9.592  -76.378 17.026  1.00 90.52  ? 51   LYS B CE  1 
ATOM   4694 N NZ  . LYS B 2 51  ? -11.074 -76.308 17.196  1.00 102.35 ? 51   LYS B NZ  1 
ATOM   4695 N N   . ARG B 2 52  ? -6.750  -77.186 22.337  1.00 75.03  ? 52   ARG B N   1 
ATOM   4696 C CA  . ARG B 2 52  ? -7.310  -77.396 23.670  1.00 68.20  ? 52   ARG B CA  1 
ATOM   4697 C C   . ARG B 2 52  ? -7.556  -76.076 24.398  1.00 75.77  ? 52   ARG B C   1 
ATOM   4698 O O   . ARG B 2 52  ? -8.660  -75.865 24.917  1.00 71.08  ? 52   ARG B O   1 
ATOM   4699 C CB  . ARG B 2 52  ? -6.411  -78.305 24.522  1.00 83.05  ? 52   ARG B CB  1 
ATOM   4700 C CG  . ARG B 2 52  ? -7.166  -79.396 25.300  1.00 91.98  ? 52   ARG B CG  1 
ATOM   4701 C CD  . ARG B 2 52  ? -6.524  -79.747 26.644  1.00 91.48  ? 52   ARG B CD  1 
ATOM   4702 N NE  . ARG B 2 52  ? -5.065  -79.843 26.606  1.00 94.68  ? 52   ARG B NE  1 
ATOM   4703 C CZ  . ARG B 2 52  ? -4.381  -80.701 25.853  1.00 105.05 ? 52   ARG B CZ  1 
ATOM   4704 N NH1 . ARG B 2 52  ? -3.053  -80.708 25.898  1.00 102.30 ? 52   ARG B NH1 1 
ATOM   4705 N NH2 . ARG B 2 52  ? -5.020  -81.545 25.046  1.00 105.91 ? 52   ARG B NH2 1 
ATOM   4706 N N   . ILE B 2 53  ? -6.530  -75.207 24.440  1.00 65.72  ? 53   ILE B N   1 
ATOM   4707 C CA  . ILE B 2 53  ? -6.622  -73.906 25.113  1.00 66.81  ? 53   ILE B CA  1 
ATOM   4708 C C   . ILE B 2 53  ? -7.696  -73.026 24.466  1.00 73.21  ? 53   ILE B C   1 
ATOM   4709 O O   . ILE B 2 53  ? -8.579  -72.508 25.160  1.00 72.07  ? 53   ILE B O   1 
ATOM   4710 C CB  . ILE B 2 53  ? -5.246  -73.149 25.161  1.00 76.51  ? 53   ILE B CB  1 
ATOM   4711 C CG1 . ILE B 2 53  ? -4.188  -73.973 25.893  1.00 76.11  ? 53   ILE B CG1 1 
ATOM   4712 C CG2 . ILE B 2 53  ? -5.368  -71.780 25.847  1.00 54.70  ? 53   ILE B CG2 1 
ATOM   4713 C CD1 . ILE B 2 53  ? -2.797  -73.608 25.518  1.00 63.37  ? 53   ILE B CD1 1 
ATOM   4714 N N   . ARG B 2 54  ? -7.639  -72.863 23.143  1.00 79.59  ? 54   ARG B N   1 
ATOM   4715 C CA  . ARG B 2 54  ? -8.684  -72.099 22.459  1.00 78.19  ? 54   ARG B CA  1 
ATOM   4716 C C   . ARG B 2 54  ? -10.054 -72.639 22.858  1.00 85.50  ? 54   ARG B C   1 
ATOM   4717 O O   . ARG B 2 54  ? -10.918 -71.885 23.310  1.00 89.96  ? 54   ARG B O   1 
ATOM   4718 C CB  . ARG B 2 54  ? -8.537  -72.135 20.935  1.00 66.86  ? 54   ARG B CB  1 
ATOM   4719 C CG  . ARG B 2 54  ? -7.252  -71.553 20.402  1.00 61.67  ? 54   ARG B CG  1 
ATOM   4720 C CD  . ARG B 2 54  ? -7.438  -70.967 19.017  1.00 66.02  ? 54   ARG B CD  1 
ATOM   4721 N NE  . ARG B 2 54  ? -6.539  -69.837 18.838  1.00 81.40  ? 54   ARG B NE  1 
ATOM   4722 C CZ  . ARG B 2 54  ? -5.216  -69.946 18.784  1.00 89.77  ? 54   ARG B CZ  1 
ATOM   4723 N NH1 . ARG B 2 54  ? -4.656  -71.151 18.868  1.00 84.49  ? 54   ARG B NH1 1 
ATOM   4724 N NH2 . ARG B 2 54  ? -4.456  -68.855 18.647  1.00 85.74  ? 54   ARG B NH2 1 
ATOM   4725 N N   . ASP B 2 55  ? -10.236 -73.951 22.702  1.00 90.33  ? 55   ASP B N   1 
ATOM   4726 C CA  . ASP B 2 55  ? -11.507 -74.609 23.030  1.00 92.37  ? 55   ASP B CA  1 
ATOM   4727 C C   . ASP B 2 55  ? -11.954 -74.405 24.480  1.00 85.69  ? 55   ASP B C   1 
ATOM   4728 O O   . ASP B 2 55  ? -13.108 -74.057 24.727  1.00 69.15  ? 55   ASP B O   1 
ATOM   4729 C CB  . ASP B 2 55  ? -11.465 -76.104 22.691  1.00 97.68  ? 55   ASP B CB  1 
ATOM   4730 C CG  . ASP B 2 55  ? -11.637 -76.376 21.202  1.00 111.91 ? 55   ASP B CG  1 
ATOM   4731 O OD1 . ASP B 2 55  ? -12.064 -75.457 20.471  1.00 115.78 ? 55   ASP B OD1 1 
ATOM   4732 O OD2 . ASP B 2 55  ? -11.339 -77.511 20.768  1.00 116.12 ? 55   ASP B OD2 1 
ATOM   4733 N N   . ASN B 2 56  ? -11.048 -74.622 25.431  1.00 82.32  ? 56   ASN B N   1 
ATOM   4734 C CA  . ASN B 2 56  ? -11.363 -74.396 26.834  1.00 79.03  ? 56   ASN B CA  1 
ATOM   4735 C C   . ASN B 2 56  ? -11.777 -72.952 27.084  1.00 92.19  ? 56   ASN B C   1 
ATOM   4736 O O   . ASN B 2 56  ? -12.762 -72.706 27.792  1.00 100.02 ? 56   ASN B O   1 
ATOM   4737 C CB  . ASN B 2 56  ? -10.173 -74.743 27.727  1.00 86.10  ? 56   ASN B CB  1 
ATOM   4738 C CG  . ASN B 2 56  ? -9.919  -76.228 27.818  1.00 91.96  ? 56   ASN B CG  1 
ATOM   4739 O OD1 . ASN B 2 56  ? -10.679 -77.033 27.285  1.00 99.81  ? 56   ASN B OD1 1 
ATOM   4740 N ND2 . ASN B 2 56  ? -8.848  -76.603 28.506  1.00 91.63  ? 56   ASN B ND2 1 
ATOM   4741 N N   . ILE B 2 57  ? -11.016 -72.005 26.518  1.00 85.88  ? 57   ILE B N   1 
ATOM   4742 C CA  . ILE B 2 57  ? -11.315 -70.577 26.659  1.00 81.21  ? 57   ILE B CA  1 
ATOM   4743 C C   . ILE B 2 57  ? -12.747 -70.275 26.205  1.00 79.01  ? 57   ILE B C   1 
ATOM   4744 O O   . ILE B 2 57  ? -13.526 -69.684 26.956  1.00 75.83  ? 57   ILE B O   1 
ATOM   4745 C CB  . ILE B 2 57  ? -10.300 -69.674 25.897  1.00 81.02  ? 57   ILE B CB  1 
ATOM   4746 C CG1 . ILE B 2 57  ? -8.974  -69.582 26.641  1.00 75.95  ? 57   ILE B CG1 1 
ATOM   4747 C CG2 . ILE B 2 57  ? -10.828 -68.254 25.719  1.00 72.00  ? 57   ILE B CG2 1 
ATOM   4748 C CD1 . ILE B 2 57  ? -7.918  -68.849 25.847  1.00 72.95  ? 57   ILE B CD1 1 
ATOM   4749 N N   . GLU B 2 58  ? -13.095 -70.690 24.986  1.00 77.50  ? 58   GLU B N   1 
ATOM   4750 C CA  . GLU B 2 58  ? -14.475 -70.557 24.501  1.00 88.40  ? 58   GLU B CA  1 
ATOM   4751 C C   . GLU B 2 58  ? -15.495 -71.194 25.463  1.00 95.22  ? 58   GLU B C   1 
ATOM   4752 O O   . GLU B 2 58  ? -16.527 -70.596 25.767  1.00 95.82  ? 58   GLU B O   1 
ATOM   4753 C CB  . GLU B 2 58  ? -14.632 -71.138 23.091  1.00 92.64  ? 58   GLU B CB  1 
ATOM   4754 C CG  . GLU B 2 58  ? -13.822 -70.432 22.014  1.00 116.25 ? 58   GLU B CG  1 
ATOM   4755 C CD  . GLU B 2 58  ? -14.144 -70.938 20.609  1.00 141.31 ? 58   GLU B CD  1 
ATOM   4756 O OE1 . GLU B 2 58  ? -15.188 -71.608 20.432  1.00 144.43 ? 58   GLU B OE1 1 
ATOM   4757 O OE2 . GLU B 2 58  ? -13.354 -70.661 19.678  1.00 152.80 ? 58   GLU B OE2 1 
ATOM   4758 N N   . ASP B 2 59  ? -15.204 -72.403 25.941  1.00 95.48  ? 59   ASP B N   1 
ATOM   4759 C CA  . ASP B 2 59  ? -16.051 -73.053 26.936  1.00 90.94  ? 59   ASP B CA  1 
ATOM   4760 C C   . ASP B 2 59  ? -16.246 -72.144 28.144  1.00 87.98  ? 59   ASP B C   1 
ATOM   4761 O O   . ASP B 2 59  ? -17.380 -71.818 28.505  1.00 77.50  ? 59   ASP B O   1 
ATOM   4762 C CB  . ASP B 2 59  ? -15.458 -74.395 27.374  1.00 100.41 ? 59   ASP B CB  1 
ATOM   4763 C CG  . ASP B 2 59  ? -15.681 -75.504 26.345  1.00 120.53 ? 59   ASP B CG  1 
ATOM   4764 O OD1 . ASP B 2 59  ? -16.527 -75.323 25.437  1.00 122.92 ? 59   ASP B OD1 1 
ATOM   4765 O OD2 . ASP B 2 59  ? -15.009 -76.559 26.446  1.00 123.34 ? 59   ASP B OD2 1 
ATOM   4766 N N   . ILE B 2 60  ? -15.138 -71.731 28.759  1.00 83.18  ? 60   ILE B N   1 
ATOM   4767 C CA  . ILE B 2 60  ? -15.194 -70.811 29.889  1.00 81.64  ? 60   ILE B CA  1 
ATOM   4768 C C   . ILE B 2 60  ? -16.036 -69.567 29.570  1.00 89.12  ? 60   ILE B C   1 
ATOM   4769 O O   . ILE B 2 60  ? -16.844 -69.135 30.392  1.00 83.61  ? 60   ILE B O   1 
ATOM   4770 C CB  . ILE B 2 60  ? -13.791 -70.383 30.355  1.00 83.82  ? 60   ILE B CB  1 
ATOM   4771 C CG1 . ILE B 2 60  ? -12.964 -71.598 30.767  1.00 86.01  ? 60   ILE B CG1 1 
ATOM   4772 C CG2 . ILE B 2 60  ? -13.881 -69.398 31.510  1.00 77.13  ? 60   ILE B CG2 1 
ATOM   4773 C CD1 . ILE B 2 60  ? -11.705 -71.225 31.538  1.00 79.06  ? 60   ILE B CD1 1 
ATOM   4774 N N   . GLU B 2 61  ? -15.855 -68.999 28.377  1.00 95.81  ? 61   GLU B N   1 
ATOM   4775 C CA  . GLU B 2 61  ? -16.612 -67.812 27.971  1.00 95.25  ? 61   GLU B CA  1 
ATOM   4776 C C   . GLU B 2 61  ? -18.117 -68.009 28.080  1.00 108.41 ? 61   GLU B C   1 
ATOM   4777 O O   . GLU B 2 61  ? -18.823 -67.131 28.570  1.00 116.30 ? 61   GLU B O   1 
ATOM   4778 C CB  . GLU B 2 61  ? -16.257 -67.383 26.550  1.00 90.73  ? 61   GLU B CB  1 
ATOM   4779 C CG  . GLU B 2 61  ? -14.953 -66.626 26.454  1.00 107.54 ? 61   GLU B CG  1 
ATOM   4780 C CD  . GLU B 2 61  ? -14.843 -65.819 25.181  1.00 119.43 ? 61   GLU B CD  1 
ATOM   4781 O OE1 . GLU B 2 61  ? -15.238 -64.631 25.202  1.00 119.42 ? 61   GLU B OE1 1 
ATOM   4782 O OE2 . GLU B 2 61  ? -14.364 -66.372 24.165  1.00 123.86 ? 61   GLU B OE2 1 
ATOM   4783 N N   . GLN B 2 62  ? -18.598 -69.159 27.607  1.00 111.05 ? 62   GLN B N   1 
ATOM   4784 C CA  . GLN B 2 62  ? -20.016 -69.505 27.672  1.00 106.61 ? 62   GLN B CA  1 
ATOM   4785 C C   . GLN B 2 62  ? -20.426 -69.756 29.121  1.00 104.34 ? 62   GLN B C   1 
ATOM   4786 O O   . GLN B 2 62  ? -21.444 -69.248 29.589  1.00 107.70 ? 62   GLN B O   1 
ATOM   4787 C CB  . GLN B 2 62  ? -20.298 -70.749 26.825  1.00 122.67 ? 62   GLN B CB  1 
ATOM   4788 C CG  . GLN B 2 62  ? -21.314 -70.548 25.698  1.00 143.15 ? 62   GLN B CG  1 
ATOM   4789 C CD  . GLN B 2 62  ? -20.773 -69.705 24.545  1.00 154.84 ? 62   GLN B CD  1 
ATOM   4790 O OE1 . GLN B 2 62  ? -19.561 -69.604 24.344  1.00 161.14 ? 62   GLN B OE1 1 
ATOM   4791 N NE2 . GLN B 2 62  ? -21.678 -69.100 23.778  1.00 154.03 ? 62   GLN B NE2 1 
ATOM   4792 N N   . ALA B 2 63  ? -19.617 -70.541 29.825  1.00 95.30  ? 63   ALA B N   1 
ATOM   4793 C CA  . ALA B 2 63  ? -19.838 -70.836 31.236  1.00 91.28  ? 63   ALA B CA  1 
ATOM   4794 C C   . ALA B 2 63  ? -19.965 -69.574 32.099  1.00 98.71  ? 63   ALA B C   1 
ATOM   4795 O O   . ALA B 2 63  ? -20.835 -69.489 32.965  1.00 111.10 ? 63   ALA B O   1 
ATOM   4796 C CB  . ALA B 2 63  ? -18.717 -71.735 31.763  1.00 78.98  ? 63   ALA B CB  1 
ATOM   4797 N N   . ILE B 2 64  ? -19.087 -68.606 31.868  1.00 88.13  ? 64   ILE B N   1 
ATOM   4798 C CA  . ILE B 2 64  ? -19.113 -67.354 32.612  1.00 99.42  ? 64   ILE B CA  1 
ATOM   4799 C C   . ILE B 2 64  ? -20.466 -66.653 32.489  1.00 103.27 ? 64   ILE B C   1 
ATOM   4800 O O   . ILE B 2 64  ? -21.039 -66.211 33.485  1.00 99.27  ? 64   ILE B O   1 
ATOM   4801 C CB  . ILE B 2 64  ? -17.968 -66.397 32.154  1.00 104.98 ? 64   ILE B CB  1 
ATOM   4802 C CG1 . ILE B 2 64  ? -16.641 -66.793 32.807  1.00 97.02  ? 64   ILE B CG1 1 
ATOM   4803 C CG2 . ILE B 2 64  ? -18.293 -64.951 32.484  1.00 99.56  ? 64   ILE B CG2 1 
ATOM   4804 C CD1 . ILE B 2 64  ? -15.434 -66.378 32.003  1.00 95.43  ? 64   ILE B CD1 1 
ATOM   4805 N N   . GLU B 2 65  ? -20.980 -66.560 31.268  1.00 112.52 ? 65   GLU B N   1 
ATOM   4806 C CA  . GLU B 2 65  ? -22.221 -65.826 31.024  1.00 120.13 ? 65   GLU B CA  1 
ATOM   4807 C C   . GLU B 2 65  ? -23.451 -66.601 31.497  1.00 121.17 ? 65   GLU B C   1 
ATOM   4808 O O   . GLU B 2 65  ? -24.577 -66.119 31.394  1.00 126.20 ? 65   GLU B O   1 
ATOM   4809 C CB  . GLU B 2 65  ? -22.351 -65.438 29.546  1.00 125.45 ? 65   GLU B CB  1 
ATOM   4810 C CG  . GLU B 2 65  ? -21.139 -64.677 28.982  1.00 133.47 ? 65   GLU B CG  1 
ATOM   4811 C CD  . GLU B 2 65  ? -20.825 -63.379 29.728  1.00 136.80 ? 65   GLU B CD  1 
ATOM   4812 O OE1 . GLU B 2 65  ? -21.753 -62.781 30.318  1.00 136.31 ? 65   GLU B OE1 1 
ATOM   4813 O OE2 . GLU B 2 65  ? -19.646 -62.953 29.715  1.00 136.06 ? 65   GLU B OE2 1 
ATOM   4814 N N   . GLN B 2 66  ? -23.226 -67.799 32.026  1.00 115.58 ? 66   GLN B N   1 
ATOM   4815 C CA  . GLN B 2 66  ? -24.295 -68.587 32.621  1.00 115.63 ? 66   GLN B CA  1 
ATOM   4816 C C   . GLN B 2 66  ? -24.247 -68.472 34.139  1.00 118.64 ? 66   GLN B C   1 
ATOM   4817 O O   . GLN B 2 66  ? -25.280 -68.481 34.809  1.00 124.68 ? 66   GLN B O   1 
ATOM   4818 C CB  . GLN B 2 66  ? -24.192 -70.051 32.188  1.00 123.76 ? 66   GLN B CB  1 
ATOM   4819 C CG  . GLN B 2 66  ? -24.510 -70.291 30.713  1.00 128.74 ? 66   GLN B CG  1 
ATOM   4820 C CD  . GLN B 2 66  ? -23.887 -71.569 30.185  1.00 128.47 ? 66   GLN B CD  1 
ATOM   4821 O OE1 . GLN B 2 66  ? -23.505 -72.452 30.961  1.00 131.80 ? 66   GLN B OE1 1 
ATOM   4822 N NE2 . GLN B 2 66  ? -23.768 -71.670 28.861  1.00 119.44 ? 66   GLN B NE2 1 
ATOM   4823 N N   . VAL B 2 67  ? -23.040 -68.371 34.682  1.00 120.36 ? 67   VAL B N   1 
ATOM   4824 C CA  . VAL B 2 67  ? -22.880 -68.060 36.095  1.00 116.37 ? 67   VAL B CA  1 
ATOM   4825 C C   . VAL B 2 67  ? -23.463 -66.671 36.346  1.00 109.85 ? 67   VAL B C   1 
ATOM   4826 O O   . VAL B 2 67  ? -23.933 -66.371 37.436  1.00 106.92 ? 67   VAL B O   1 
ATOM   4827 C CB  . VAL B 2 67  ? -21.400 -68.111 36.537  1.00 109.97 ? 67   VAL B CB  1 
ATOM   4828 C CG1 . VAL B 2 67  ? -21.278 -67.825 38.017  1.00 106.12 ? 67   VAL B CG1 1 
ATOM   4829 C CG2 . VAL B 2 67  ? -20.795 -69.468 36.215  1.00 107.17 ? 67   VAL B CG2 1 
ATOM   4830 N N   . ALA B 2 68  ? -23.446 -65.827 35.321  1.00 118.43 ? 68   ALA B N   1 
ATOM   4831 C CA  . ALA B 2 68  ? -24.023 -64.491 35.435  1.00 120.33 ? 68   ALA B CA  1 
ATOM   4832 C C   . ALA B 2 68  ? -25.501 -64.568 35.826  1.00 130.09 ? 68   ALA B C   1 
ATOM   4833 O O   . ALA B 2 68  ? -25.909 -64.007 36.844  1.00 132.90 ? 68   ALA B O   1 
ATOM   4834 C CB  . ALA B 2 68  ? -23.844 -63.713 34.138  1.00 101.00 ? 68   ALA B CB  1 
ATOM   4835 N N   . GLN B 2 69  ? -26.296 -65.273 35.024  1.00 132.79 ? 69   GLN B N   1 
ATOM   4836 C CA  . GLN B 2 69  ? -27.721 -65.443 35.312  1.00 135.92 ? 69   GLN B CA  1 
ATOM   4837 C C   . GLN B 2 69  ? -27.974 -66.166 36.632  1.00 132.96 ? 69   GLN B C   1 
ATOM   4838 O O   . GLN B 2 69  ? -28.723 -65.681 37.481  1.00 134.15 ? 69   GLN B O   1 
ATOM   4839 C CB  . GLN B 2 69  ? -28.419 -66.192 34.179  1.00 136.79 ? 69   GLN B CB  1 
ATOM   4840 C CG  . GLN B 2 69  ? -28.326 -65.495 32.845  1.00 145.84 ? 69   GLN B CG  1 
ATOM   4841 C CD  . GLN B 2 69  ? -29.041 -66.256 31.754  1.00 154.65 ? 69   GLN B CD  1 
ATOM   4842 O OE1 . GLN B 2 69  ? -29.652 -67.297 32.004  1.00 151.94 ? 69   GLN B OE1 1 
ATOM   4843 N NE2 . GLN B 2 69  ? -28.970 -65.740 30.529  1.00 158.15 ? 69   GLN B NE2 1 
ATOM   4844 N N   . LEU B 2 70  ? -27.351 -67.328 36.800  1.00 126.85 ? 70   LEU B N   1 
ATOM   4845 C CA  . LEU B 2 70  ? -27.542 -68.125 38.008  1.00 128.24 ? 70   LEU B CA  1 
ATOM   4846 C C   . LEU B 2 70  ? -27.379 -67.310 39.293  1.00 135.72 ? 70   LEU B C   1 
ATOM   4847 O O   . LEU B 2 70  ? -27.952 -67.653 40.328  1.00 145.75 ? 70   LEU B O   1 
ATOM   4848 C CB  . LEU B 2 70  ? -26.596 -69.329 38.017  1.00 122.30 ? 70   LEU B CB  1 
ATOM   4849 C CG  . LEU B 2 70  ? -26.811 -70.397 36.945  1.00 116.32 ? 70   LEU B CG  1 
ATOM   4850 C CD1 . LEU B 2 70  ? -25.911 -71.595 37.209  1.00 107.55 ? 70   LEU B CD1 1 
ATOM   4851 C CD2 . LEU B 2 70  ? -28.274 -70.823 36.899  1.00 121.46 ? 70   LEU B CD2 1 
ATOM   4852 N N   . HIS B 2 71  ? -26.600 -66.234 39.223  1.00 132.72 ? 71   HIS B N   1 
ATOM   4853 C CA  . HIS B 2 71  ? -26.377 -65.367 40.377  1.00 133.78 ? 71   HIS B CA  1 
ATOM   4854 C C   . HIS B 2 71  ? -27.519 -64.379 40.599  1.00 139.46 ? 71   HIS B C   1 
ATOM   4855 O O   . HIS B 2 71  ? -28.081 -64.307 41.697  1.00 141.55 ? 71   HIS B O   1 
ATOM   4856 C CB  . HIS B 2 71  ? -25.064 -64.600 40.231  1.00 132.71 ? 71   HIS B CB  1 
ATOM   4857 C CG  . HIS B 2 71  ? -23.878 -65.322 40.783  1.00 130.40 ? 71   HIS B CG  1 
ATOM   4858 N ND1 . HIS B 2 71  ? -23.830 -65.792 42.079  1.00 134.54 ? 71   HIS B ND1 1 
ATOM   4859 C CD2 . HIS B 2 71  ? -22.688 -65.643 40.224  1.00 125.81 ? 71   HIS B CD2 1 
ATOM   4860 C CE1 . HIS B 2 71  ? -22.667 -66.378 42.290  1.00 132.91 ? 71   HIS B CE1 1 
ATOM   4861 N NE2 . HIS B 2 71  ? -21.954 -66.303 41.179  1.00 127.29 ? 71   HIS B NE2 1 
ATOM   4862 N N   . THR B 2 72  ? -27.845 -63.612 39.559  1.00 140.87 ? 72   THR B N   1 
ATOM   4863 C CA  . THR B 2 72  ? -28.899 -62.603 39.643  1.00 147.82 ? 72   THR B CA  1 
ATOM   4864 C C   . THR B 2 72  ? -30.271 -63.260 39.725  1.00 154.07 ? 72   THR B C   1 
ATOM   4865 O O   . THR B 2 72  ? -31.279 -62.595 39.971  1.00 157.26 ? 72   THR B O   1 
ATOM   4866 C CB  . THR B 2 72  ? -28.876 -61.633 38.437  1.00 148.48 ? 72   THR B CB  1 
ATOM   4867 O OG1 . THR B 2 72  ? -29.093 -62.363 37.221  1.00 142.34 ? 72   THR B OG1 1 
ATOM   4868 C CG2 . THR B 2 72  ? -27.542 -60.874 38.366  1.00 145.94 ? 72   THR B CG2 1 
ATOM   4869 N N   . GLU B 2 73  ? -30.293 -64.573 39.518  1.00 154.98 ? 73   GLU B N   1 
ATOM   4870 C CA  . GLU B 2 73  ? -31.521 -65.351 39.587  1.00 154.48 ? 73   GLU B CA  1 
ATOM   4871 C C   . GLU B 2 73  ? -31.771 -65.832 41.019  1.00 158.78 ? 73   GLU B C   1 
ATOM   4872 O O   . GLU B 2 73  ? -32.914 -66.075 41.410  1.00 168.93 ? 73   GLU B O   1 
ATOM   4873 C CB  . GLU B 2 73  ? -31.450 -66.532 38.613  1.00 154.20 ? 73   GLU B CB  1 
ATOM   4874 C CG  . GLU B 2 73  ? -32.779 -67.224 38.341  1.00 158.41 ? 73   GLU B CG  1 
ATOM   4875 C CD  . GLU B 2 73  ? -32.660 -68.339 37.312  1.00 159.88 ? 73   GLU B CD  1 
ATOM   4876 O OE1 . GLU B 2 73  ? -31.870 -68.187 36.352  1.00 151.87 ? 73   GLU B OE1 1 
ATOM   4877 O OE2 . GLU B 2 73  ? -33.360 -69.367 37.464  1.00 164.65 ? 73   GLU B OE2 1 
ATOM   4878 N N   . SER B 2 74  ? -30.701 -65.960 41.801  1.00 151.83 ? 74   SER B N   1 
ATOM   4879 C CA  . SER B 2 74  ? -30.832 -66.322 43.210  1.00 147.26 ? 74   SER B CA  1 
ATOM   4880 C C   . SER B 2 74  ? -31.282 -65.128 44.049  1.00 151.94 ? 74   SER B C   1 
ATOM   4881 O O   . SER B 2 74  ? -31.280 -65.187 45.276  1.00 153.29 ? 74   SER B O   1 
ATOM   4882 C CB  . SER B 2 74  ? -29.531 -66.911 43.763  1.00 135.89 ? 74   SER B CB  1 
ATOM   4883 O OG  . SER B 2 74  ? -29.359 -68.256 43.355  1.00 126.89 ? 74   SER B OG  1 
ATOM   4884 N N   . LEU B 2 75  ? -31.659 -64.042 43.381  1.00 154.64 ? 75   LEU B N   1 
ATOM   4885 C CA  . LEU B 2 75  ? -32.315 -62.936 44.062  1.00 164.18 ? 75   LEU B CA  1 
ATOM   4886 C C   . LEU B 2 75  ? -33.791 -63.282 44.199  1.00 177.17 ? 75   LEU B C   1 
ATOM   4887 O O   . LEU B 2 75  ? -34.433 -63.690 43.229  1.00 173.70 ? 75   LEU B O   1 
ATOM   4888 C CB  . LEU B 2 75  ? -32.127 -61.624 43.299  1.00 164.61 ? 75   LEU B CB  1 
ATOM   4889 C CG  . LEU B 2 75  ? -32.765 -60.378 43.926  1.00 162.87 ? 75   LEU B CG  1 
ATOM   4890 C CD1 . LEU B 2 75  ? -31.920 -59.130 43.676  1.00 154.75 ? 75   LEU B CD1 1 
ATOM   4891 C CD2 . LEU B 2 75  ? -34.194 -60.184 43.425  1.00 164.27 ? 75   LEU B CD2 1 
ATOM   4892 N N   . VAL B 2 76  ? -34.316 -63.119 45.411  1.00 192.44 ? 76   VAL B N   1 
ATOM   4893 C CA  . VAL B 2 76  ? -35.659 -63.583 45.768  1.00 202.50 ? 76   VAL B CA  1 
ATOM   4894 C C   . VAL B 2 76  ? -35.921 -65.009 45.241  1.00 207.46 ? 76   VAL B C   1 
ATOM   4895 O O   . VAL B 2 76  ? -35.254 -65.961 45.659  1.00 203.74 ? 76   VAL B O   1 
ATOM   4896 C CB  . VAL B 2 76  ? -36.775 -62.550 45.378  1.00 219.22 ? 76   VAL B CB  1 
ATOM   4897 C CG1 . VAL B 2 76  ? -36.864 -62.348 43.867  1.00 218.58 ? 76   VAL B CG1 1 
ATOM   4898 C CG2 . VAL B 2 76  ? -38.124 -62.954 45.963  1.00 220.41 ? 76   VAL B CG2 1 
ATOM   4899 N N   . ALA B 2 77  ? -36.884 -65.156 44.337  1.00 210.73 ? 77   ALA B N   1 
ATOM   4900 C CA  . ALA B 2 77  ? -37.158 -66.442 43.703  1.00 210.10 ? 77   ALA B CA  1 
ATOM   4901 C C   . ALA B 2 77  ? -37.659 -67.504 44.680  1.00 213.51 ? 77   ALA B C   1 
ATOM   4902 O O   . ALA B 2 77  ? -37.100 -68.596 44.753  1.00 218.77 ? 77   ALA B O   1 
ATOM   4903 C CB  . ALA B 2 77  ? -35.923 -66.942 42.958  1.00 206.16 ? 77   ALA B CB  1 
ATOM   4904 N N   . VAL B 2 78  ? -38.712 -67.178 45.424  1.00 211.56 ? 78   VAL B N   1 
ATOM   4905 C CA  . VAL B 2 78  ? -39.379 -68.144 46.297  1.00 213.57 ? 78   VAL B CA  1 
ATOM   4906 C C   . VAL B 2 78  ? -38.421 -68.881 47.241  1.00 218.20 ? 78   VAL B C   1 
ATOM   4907 O O   . VAL B 2 78  ? -38.425 -70.111 47.310  1.00 216.89 ? 78   VAL B O   1 
ATOM   4908 C CB  . VAL B 2 78  ? -40.193 -69.176 45.478  1.00 208.92 ? 78   VAL B CB  1 
ATOM   4909 C CG1 . VAL B 2 78  ? -41.148 -69.945 46.379  1.00 209.01 ? 78   VAL B CG1 1 
ATOM   4910 C CG2 . VAL B 2 78  ? -40.967 -68.480 44.374  1.00 206.40 ? 78   VAL B CG2 1 
ATOM   4911 N N   . SER B 2 79  ? -37.599 -68.118 47.957  1.00 221.73 ? 79   SER B N   1 
ATOM   4912 C CA  . SER B 2 79  ? -36.733 -68.657 49.013  1.00 222.13 ? 79   SER B CA  1 
ATOM   4913 C C   . SER B 2 79  ? -35.969 -69.939 48.646  1.00 221.07 ? 79   SER B C   1 
ATOM   4914 O O   . SER B 2 79  ? -35.406 -70.045 47.555  1.00 226.92 ? 79   SER B O   1 
ATOM   4915 C CB  . SER B 2 79  ? -37.534 -68.867 50.302  1.00 223.34 ? 79   SER B CB  1 
ATOM   4916 O OG  . SER B 2 79  ? -36.678 -69.148 51.397  1.00 221.94 ? 79   SER B OG  1 
ATOM   4917 N N   . LYS B 2 80  ? -35.955 -70.904 49.567  1.00 210.30 ? 80   LYS B N   1 
ATOM   4918 C CA  . LYS B 2 80  ? -35.102 -72.091 49.453  1.00 201.09 ? 80   LYS B CA  1 
ATOM   4919 C C   . LYS B 2 80  ? -35.612 -73.130 48.454  1.00 200.36 ? 80   LYS B C   1 
ATOM   4920 O O   . LYS B 2 80  ? -34.911 -74.092 48.129  1.00 197.83 ? 80   LYS B O   1 
ATOM   4921 C CB  . LYS B 2 80  ? -34.900 -72.741 50.825  1.00 194.77 ? 80   LYS B CB  1 
ATOM   4922 C CG  . LYS B 2 80  ? -33.895 -73.878 50.826  1.00 193.25 ? 80   LYS B CG  1 
ATOM   4923 C CD  . LYS B 2 80  ? -33.969 -74.675 52.109  1.00 194.86 ? 80   LYS B CD  1 
ATOM   4924 C CE  . LYS B 2 80  ? -33.705 -73.798 53.317  1.00 191.89 ? 80   LYS B CE  1 
ATOM   4925 N NZ  . LYS B 2 80  ? -33.883 -74.567 54.580  1.00 193.41 ? 80   LYS B NZ  1 
ATOM   4926 N N   . GLU B 2 81  ? -36.836 -72.939 47.975  1.00 202.79 ? 81   GLU B N   1 
ATOM   4927 C CA  . GLU B 2 81  ? -37.400 -73.824 46.965  1.00 204.67 ? 81   GLU B CA  1 
ATOM   4928 C C   . GLU B 2 81  ? -36.433 -73.969 45.800  1.00 200.30 ? 81   GLU B C   1 
ATOM   4929 O O   . GLU B 2 81  ? -36.088 -75.080 45.393  1.00 196.96 ? 81   GLU B O   1 
ATOM   4930 C CB  . GLU B 2 81  ? -38.737 -73.275 46.458  1.00 206.78 ? 81   GLU B CB  1 
ATOM   4931 C CG  . GLU B 2 81  ? -39.876 -73.366 47.459  1.00 206.57 ? 81   GLU B CG  1 
ATOM   4932 C CD  . GLU B 2 81  ? -40.302 -74.795 47.720  1.00 208.08 ? 81   GLU B CD  1 
ATOM   4933 O OE1 . GLU B 2 81  ? -41.195 -75.006 48.567  1.00 209.07 ? 81   GLU B OE1 1 
ATOM   4934 O OE2 . GLU B 2 81  ? -39.743 -75.709 47.076  1.00 208.41 ? 81   GLU B OE2 1 
ATOM   4935 N N   . ASP B 2 82  ? -35.991 -72.829 45.279  1.00 199.42 ? 82   ASP B N   1 
ATOM   4936 C CA  . ASP B 2 82  ? -35.127 -72.793 44.106  1.00 196.80 ? 82   ASP B CA  1 
ATOM   4937 C C   . ASP B 2 82  ? -33.672 -72.449 44.451  1.00 196.63 ? 82   ASP B C   1 
ATOM   4938 O O   . ASP B 2 82  ? -32.768 -72.740 43.672  1.00 199.92 ? 82   ASP B O   1 
ATOM   4939 C CB  . ASP B 2 82  ? -35.676 -71.807 43.062  1.00 189.62 ? 82   ASP B CB  1 
ATOM   4940 C CG  . ASP B 2 82  ? -37.104 -72.131 42.635  1.00 182.55 ? 82   ASP B CG  1 
ATOM   4941 O OD1 . ASP B 2 82  ? -37.429 -71.937 41.443  1.00 177.74 ? 82   ASP B OD1 1 
ATOM   4942 O OD2 . ASP B 2 82  ? -37.901 -72.578 43.486  1.00 180.57 ? 82   ASP B OD2 1 
ATOM   4943 N N   . ARG B 2 83  ? -33.449 -71.833 45.611  1.00 191.53 ? 83   ARG B N   1 
ATOM   4944 C CA  . ARG B 2 83  ? -32.095 -71.471 46.035  1.00 187.53 ? 83   ARG B CA  1 
ATOM   4945 C C   . ARG B 2 83  ? -31.139 -72.660 45.981  1.00 188.59 ? 83   ARG B C   1 
ATOM   4946 O O   . ARG B 2 83  ? -30.039 -72.557 45.437  1.00 193.56 ? 83   ARG B O   1 
ATOM   4947 C CB  . ARG B 2 83  ? -32.092 -70.893 47.451  1.00 187.36 ? 83   ARG B CB  1 
ATOM   4948 C CG  . ARG B 2 83  ? -32.378 -69.404 47.551  1.00 187.79 ? 83   ARG B CG  1 
ATOM   4949 C CD  . ARG B 2 83  ? -31.941 -68.874 48.914  1.00 190.71 ? 83   ARG B CD  1 
ATOM   4950 N NE  . ARG B 2 83  ? -32.263 -69.807 49.995  1.00 195.75 ? 83   ARG B NE  1 
ATOM   4951 C CZ  . ARG B 2 83  ? -31.414 -70.701 50.497  1.00 196.62 ? 83   ARG B CZ  1 
ATOM   4952 N NH1 . ARG B 2 83  ? -30.177 -70.788 50.022  1.00 193.58 ? 83   ARG B NH1 1 
ATOM   4953 N NH2 . ARG B 2 83  ? -31.800 -71.510 51.477  1.00 198.30 ? 83   ARG B NH2 1 
ATOM   4954 N N   . ASP B 2 84  ? -31.555 -73.780 46.564  1.00 183.24 ? 84   ASP B N   1 
ATOM   4955 C CA  . ASP B 2 84  ? -30.739 -74.986 46.552  1.00 181.12 ? 84   ASP B CA  1 
ATOM   4956 C C   . ASP B 2 84  ? -30.620 -75.537 45.134  1.00 174.84 ? 84   ASP B C   1 
ATOM   4957 O O   . ASP B 2 84  ? -29.605 -76.134 44.775  1.00 173.70 ? 84   ASP B O   1 
ATOM   4958 C CB  . ASP B 2 84  ? -31.321 -76.049 47.490  1.00 187.95 ? 84   ASP B CB  1 
ATOM   4959 C CG  . ASP B 2 84  ? -31.151 -75.693 48.958  1.00 189.90 ? 84   ASP B CG  1 
ATOM   4960 O OD1 . ASP B 2 84  ? -30.322 -74.809 49.269  1.00 188.90 ? 84   ASP B OD1 1 
ATOM   4961 O OD2 . ASP B 2 84  ? -31.845 -76.306 49.801  1.00 189.38 ? 84   ASP B OD2 1 
ATOM   4962 N N   . ARG B 2 85  ? -31.662 -75.331 44.332  1.00 171.44 ? 85   ARG B N   1 
ATOM   4963 C CA  . ARG B 2 85  ? -31.674 -75.790 42.943  1.00 170.58 ? 85   ARG B CA  1 
ATOM   4964 C C   . ARG B 2 85  ? -30.658 -75.019 42.097  1.00 164.09 ? 85   ARG B C   1 
ATOM   4965 O O   . ARG B 2 85  ? -30.071 -75.561 41.160  1.00 163.05 ? 85   ARG B O   1 
ATOM   4966 C CB  . ARG B 2 85  ? -33.080 -75.656 42.339  1.00 173.97 ? 85   ARG B CB  1 
ATOM   4967 C CG  . ARG B 2 85  ? -34.134 -76.614 42.913  1.00 179.38 ? 85   ARG B CG  1 
ATOM   4968 C CD  . ARG B 2 85  ? -34.210 -77.930 42.128  1.00 186.24 ? 85   ARG B CD  1 
ATOM   4969 N NE  . ARG B 2 85  ? -35.201 -78.860 42.677  1.00 190.50 ? 85   ARG B NE  1 
ATOM   4970 C CZ  . ARG B 2 85  ? -35.420 -80.094 42.221  1.00 189.15 ? 85   ARG B CZ  1 
ATOM   4971 N NH1 . ARG B 2 85  ? -34.720 -80.568 41.197  1.00 185.70 ? 85   ARG B NH1 1 
ATOM   4972 N NH2 . ARG B 2 85  ? -36.343 -80.860 42.791  1.00 188.29 ? 85   ARG B NH2 1 
ATOM   4973 N N   . LEU B 2 86  ? -30.455 -73.751 42.437  1.00 160.53 ? 86   LEU B N   1 
ATOM   4974 C CA  . LEU B 2 86  ? -29.513 -72.900 41.719  1.00 153.60 ? 86   LEU B CA  1 
ATOM   4975 C C   . LEU B 2 86  ? -28.085 -73.076 42.231  1.00 155.99 ? 86   LEU B C   1 
ATOM   4976 O O   . LEU B 2 86  ? -27.174 -73.334 41.446  1.00 162.96 ? 86   LEU B O   1 
ATOM   4977 C CB  . LEU B 2 86  ? -29.932 -71.428 41.803  1.00 140.00 ? 86   LEU B CB  1 
ATOM   4978 C CG  . LEU B 2 86  ? -31.235 -71.055 41.091  1.00 127.30 ? 86   LEU B CG  1 
ATOM   4979 C CD1 . LEU B 2 86  ? -31.463 -69.550 41.156  1.00 122.38 ? 86   LEU B CD1 1 
ATOM   4980 C CD2 . LEU B 2 86  ? -31.235 -71.548 39.645  1.00 119.44 ? 86   LEU B CD2 1 
ATOM   4981 N N   . ASN B 2 87  ? -27.891 -72.941 43.541  1.00 146.52 ? 87   ASN B N   1 
ATOM   4982 C CA  . ASN B 2 87  ? -26.571 -73.137 44.135  1.00 139.49 ? 87   ASN B CA  1 
ATOM   4983 C C   . ASN B 2 87  ? -25.956 -74.485 43.743  1.00 141.67 ? 87   ASN B C   1 
ATOM   4984 O O   . ASN B 2 87  ? -24.770 -74.720 43.959  1.00 143.19 ? 87   ASN B O   1 
ATOM   4985 C CB  . ASN B 2 87  ? -26.634 -73.004 45.658  1.00 138.49 ? 87   ASN B CB  1 
ATOM   4986 C CG  . ASN B 2 87  ? -25.338 -72.467 46.255  1.00 142.59 ? 87   ASN B CG  1 
ATOM   4987 O OD1 . ASN B 2 87  ? -24.512 -71.874 45.557  1.00 140.95 ? 87   ASN B OD1 1 
ATOM   4988 N ND2 . ASN B 2 87  ? -25.163 -72.663 47.558  1.00 143.07 ? 87   ASN B ND2 1 
ATOM   4989 N N   . GLU B 2 88  ? -26.772 -75.362 43.162  1.00 144.20 ? 88   GLU B N   1 
ATOM   4990 C CA  . GLU B 2 88  ? -26.320 -76.677 42.711  1.00 145.73 ? 88   GLU B CA  1 
ATOM   4991 C C   . GLU B 2 88  ? -25.647 -76.564 41.345  1.00 137.98 ? 88   GLU B C   1 
ATOM   4992 O O   . GLU B 2 88  ? -24.666 -77.258 41.061  1.00 129.82 ? 88   GLU B O   1 
ATOM   4993 C CB  . GLU B 2 88  ? -27.507 -77.645 42.631  1.00 153.79 ? 88   GLU B CB  1 
ATOM   4994 C CG  . GLU B 2 88  ? -27.135 -79.124 42.569  1.00 159.14 ? 88   GLU B CG  1 
ATOM   4995 C CD  . GLU B 2 88  ? -26.904 -79.727 43.944  1.00 169.69 ? 88   GLU B CD  1 
ATOM   4996 O OE1 . GLU B 2 88  ? -26.759 -78.955 44.918  1.00 175.71 ? 88   GLU B OE1 1 
ATOM   4997 O OE2 . GLU B 2 88  ? -26.871 -80.972 44.054  1.00 171.02 ? 88   GLU B OE2 1 
ATOM   4998 N N   . LYS B 2 89  ? -26.196 -75.694 40.499  1.00 139.20 ? 89   LYS B N   1 
ATOM   4999 C CA  . LYS B 2 89  ? -25.609 -75.393 39.196  1.00 142.81 ? 89   LYS B CA  1 
ATOM   5000 C C   . LYS B 2 89  ? -24.375 -74.504 39.362  1.00 137.73 ? 89   LYS B C   1 
ATOM   5001 O O   . LYS B 2 89  ? -23.316 -74.786 38.801  1.00 133.08 ? 89   LYS B O   1 
ATOM   5002 C CB  . LYS B 2 89  ? -26.626 -74.691 38.283  1.00 147.41 ? 89   LYS B CB  1 
ATOM   5003 C CG  . LYS B 2 89  ? -27.861 -75.505 37.909  1.00 152.17 ? 89   LYS B CG  1 
ATOM   5004 C CD  . LYS B 2 89  ? -28.748 -74.755 36.904  1.00 153.40 ? 89   LYS B CD  1 
ATOM   5005 C CE  . LYS B 2 89  ? -29.939 -75.606 36.456  1.00 158.98 ? 89   LYS B CE  1 
ATOM   5006 N NZ  . LYS B 2 89  ? -30.784 -74.950 35.412  1.00 157.16 ? 89   LYS B NZ  1 
ATOM   5007 N N   . LEU B 2 90  ? -24.526 -73.429 40.134  1.00 133.11 ? 90   LEU B N   1 
ATOM   5008 C CA  . LEU B 2 90  ? -23.443 -72.481 40.372  1.00 127.87 ? 90   LEU B CA  1 
ATOM   5009 C C   . LEU B 2 90  ? -22.133 -73.169 40.715  1.00 133.07 ? 90   LEU B C   1 
ATOM   5010 O O   . LEU B 2 90  ? -21.143 -73.012 40.004  1.00 142.08 ? 90   LEU B O   1 
ATOM   5011 C CB  . LEU B 2 90  ? -23.795 -71.514 41.503  1.00 126.99 ? 90   LEU B CB  1 
ATOM   5012 C CG  . LEU B 2 90  ? -24.653 -70.288 41.205  1.00 127.96 ? 90   LEU B CG  1 
ATOM   5013 C CD1 . LEU B 2 90  ? -24.868 -69.506 42.488  1.00 126.66 ? 90   LEU B CD1 1 
ATOM   5014 C CD2 . LEU B 2 90  ? -24.000 -69.416 40.148  1.00 130.47 ? 90   LEU B CD2 1 
ATOM   5015 N N   . GLN B 2 91  ? -22.116 -73.919 41.811  1.00 127.73 ? 91   GLN B N   1 
ATOM   5016 C CA  . GLN B 2 91  ? -20.867 -74.512 42.264  1.00 127.03 ? 91   GLN B CA  1 
ATOM   5017 C C   . GLN B 2 91  ? -20.495 -75.692 41.390  1.00 118.95 ? 91   GLN B C   1 
ATOM   5018 O O   . GLN B 2 91  ? -19.471 -76.338 41.606  1.00 113.96 ? 91   GLN B O   1 
ATOM   5019 C CB  . GLN B 2 91  ? -20.934 -74.911 43.738  1.00 135.85 ? 91   GLN B CB  1 
ATOM   5020 C CG  . GLN B 2 91  ? -21.982 -75.943 44.074  1.00 146.38 ? 91   GLN B CG  1 
ATOM   5021 C CD  . GLN B 2 91  ? -22.277 -75.975 45.559  1.00 152.41 ? 91   GLN B CD  1 
ATOM   5022 O OE1 . GLN B 2 91  ? -22.002 -75.007 46.276  1.00 146.49 ? 91   GLN B OE1 1 
ATOM   5023 N NE2 . GLN B 2 91  ? -22.838 -77.087 46.033  1.00 154.45 ? 91   GLN B NE2 1 
ATOM   5024 N N   . ASP B 2 92  ? -21.329 -75.960 40.392  1.00 121.71 ? 92   ASP B N   1 
ATOM   5025 C CA  . ASP B 2 92  ? -21.052 -77.019 39.434  1.00 128.52 ? 92   ASP B CA  1 
ATOM   5026 C C   . ASP B 2 92  ? -20.356 -76.432 38.213  1.00 120.40 ? 92   ASP B C   1 
ATOM   5027 O O   . ASP B 2 92  ? -19.317 -76.928 37.778  1.00 121.00 ? 92   ASP B O   1 
ATOM   5028 C CB  . ASP B 2 92  ? -22.338 -77.746 39.040  1.00 140.27 ? 92   ASP B CB  1 
ATOM   5029 C CG  . ASP B 2 92  ? -22.073 -79.005 38.239  1.00 152.66 ? 92   ASP B CG  1 
ATOM   5030 O OD1 . ASP B 2 92  ? -21.338 -78.928 37.229  1.00 154.05 ? 92   ASP B OD1 1 
ATOM   5031 O OD2 . ASP B 2 92  ? -22.604 -80.072 38.619  1.00 157.84 ? 92   ASP B OD2 1 
ATOM   5032 N N   . THR B 2 93  ? -20.928 -75.365 37.667  1.00 119.92 ? 93   THR B N   1 
ATOM   5033 C CA  . THR B 2 93  ? -20.273 -74.623 36.593  1.00 118.69 ? 93   THR B CA  1 
ATOM   5034 C C   . THR B 2 93  ? -18.994 -73.960 37.105  1.00 112.71 ? 93   THR B C   1 
ATOM   5035 O O   . THR B 2 93  ? -17.974 -73.981 36.424  1.00 124.20 ? 93   THR B O   1 
ATOM   5036 C CB  . THR B 2 93  ? -21.205 -73.563 35.971  1.00 116.80 ? 93   THR B CB  1 
ATOM   5037 O OG1 . THR B 2 93  ? -21.607 -72.633 36.979  1.00 125.56 ? 93   THR B OG1 1 
ATOM   5038 C CG2 . THR B 2 93  ? -22.450 -74.216 35.382  1.00 115.43 ? 93   THR B CG2 1 
ATOM   5039 N N   . MET B 2 94  ? -19.057 -73.389 38.309  1.00 94.39  ? 94   MET B N   1 
ATOM   5040 C CA  . MET B 2 94  ? -17.901 -72.770 38.954  1.00 98.26  ? 94   MET B CA  1 
ATOM   5041 C C   . MET B 2 94  ? -16.703 -73.701 39.025  1.00 98.43  ? 94   MET B C   1 
ATOM   5042 O O   . MET B 2 94  ? -15.564 -73.285 38.824  1.00 113.16 ? 94   MET B O   1 
ATOM   5043 C CB  . MET B 2 94  ? -18.244 -72.328 40.377  1.00 103.31 ? 94   MET B CB  1 
ATOM   5044 C CG  . MET B 2 94  ? -18.887 -70.957 40.488  1.00 98.00  ? 94   MET B CG  1 
ATOM   5045 S SD  . MET B 2 94  ? -18.897 -70.389 42.196  1.00 125.34 ? 94   MET B SD  1 
ATOM   5046 C CE  . MET B 2 94  ? -20.047 -69.025 42.069  1.00 117.46 ? 94   MET B CE  1 
ATOM   5047 N N   . ALA B 2 95  ? -16.968 -74.959 39.340  1.00 94.34  ? 95   ALA B N   1 
ATOM   5048 C CA  . ALA B 2 95  ? -15.922 -75.959 39.474  1.00 93.42  ? 95   ALA B CA  1 
ATOM   5049 C C   . ALA B 2 95  ? -15.398 -76.353 38.112  1.00 89.20  ? 95   ALA B C   1 
ATOM   5050 O O   . ALA B 2 95  ? -14.239 -76.732 37.975  1.00 88.84  ? 95   ALA B O   1 
ATOM   5051 C CB  . ALA B 2 95  ? -16.456 -77.174 40.194  1.00 91.36  ? 95   ALA B CB  1 
ATOM   5052 N N   . ARG B 2 96  ? -16.261 -76.287 37.105  1.00 92.80  ? 96   ARG B N   1 
ATOM   5053 C CA  . ARG B 2 96  ? -15.825 -76.592 35.751  1.00 103.71 ? 96   ARG B CA  1 
ATOM   5054 C C   . ARG B 2 96  ? -14.945 -75.468 35.205  1.00 104.29 ? 96   ARG B C   1 
ATOM   5055 O O   . ARG B 2 96  ? -13.854 -75.711 34.688  1.00 107.37 ? 96   ARG B O   1 
ATOM   5056 C CB  . ARG B 2 96  ? -17.011 -76.848 34.825  1.00 101.72 ? 96   ARG B CB  1 
ATOM   5057 C CG  . ARG B 2 96  ? -16.585 -77.392 33.461  1.00 114.98 ? 96   ARG B CG  1 
ATOM   5058 C CD  . ARG B 2 96  ? -17.519 -78.482 32.959  1.00 119.24 ? 96   ARG B CD  1 
ATOM   5059 N NE  . ARG B 2 96  ? -18.907 -78.181 33.294  1.00 120.58 ? 96   ARG B NE  1 
ATOM   5060 C CZ  . ARG B 2 96  ? -19.620 -77.213 32.720  1.00 113.96 ? 96   ARG B CZ  1 
ATOM   5061 N NH1 . ARG B 2 96  ? -19.069 -76.439 31.769  1.00 86.84  ? 96   ARG B NH1 1 
ATOM   5062 N NH2 . ARG B 2 96  ? -20.883 -77.014 33.105  1.00 110.80 ? 96   ARG B NH2 1 
ATOM   5063 N N   . ILE B 2 97  ? -15.431 -74.238 35.334  1.00 91.90  ? 97   ILE B N   1 
ATOM   5064 C CA  . ILE B 2 97  ? -14.683 -73.062 34.928  1.00 79.32  ? 97   ILE B CA  1 
ATOM   5065 C C   . ILE B 2 97  ? -13.309 -73.090 35.574  1.00 81.21  ? 97   ILE B C   1 
ATOM   5066 O O   . ILE B 2 97  ? -12.314 -72.700 34.972  1.00 92.48  ? 97   ILE B O   1 
ATOM   5067 C CB  . ILE B 2 97  ? -15.429 -71.780 35.314  1.00 76.67  ? 97   ILE B CB  1 
ATOM   5068 C CG1 . ILE B 2 97  ? -16.753 -71.718 34.550  1.00 71.52  ? 97   ILE B CG1 1 
ATOM   5069 C CG2 . ILE B 2 97  ? -14.549 -70.533 35.048  1.00 73.11  ? 97   ILE B CG2 1 
ATOM   5070 C CD1 . ILE B 2 97  ? -17.551 -70.465 34.760  1.00 79.81  ? 97   ILE B CD1 1 
ATOM   5071 N N   . SER B 2 98  ? -13.265 -73.575 36.803  1.00 78.21  ? 98   SER B N   1 
ATOM   5072 C CA  . SER B 2 98  ? -12.017 -73.731 37.523  1.00 78.37  ? 98   SER B CA  1 
ATOM   5073 C C   . SER B 2 98  ? -11.153 -74.865 36.949  1.00 85.31  ? 98   SER B C   1 
ATOM   5074 O O   . SER B 2 98  ? -9.969  -74.675 36.675  1.00 77.01  ? 98   SER B O   1 
ATOM   5075 C CB  . SER B 2 98  ? -12.314 -73.946 39.008  1.00 77.31  ? 98   SER B CB  1 
ATOM   5076 O OG  . SER B 2 98  ? -11.184 -74.449 39.689  1.00 88.54  ? 98   SER B OG  1 
ATOM   5077 N N   . ALA B 2 99  ? -11.750 -76.040 36.759  1.00 90.58  ? 99   ALA B N   1 
ATOM   5078 C CA  . ALA B 2 99  ? -11.042 -77.183 36.181  1.00 85.46  ? 99   ALA B CA  1 
ATOM   5079 C C   . ALA B 2 99  ? -10.512 -76.875 34.774  1.00 83.15  ? 99   ALA B C   1 
ATOM   5080 O O   . ALA B 2 99  ? -9.408  -77.293 34.408  1.00 76.47  ? 99   ALA B O   1 
ATOM   5081 C CB  . ALA B 2 99  ? -11.943 -78.405 36.163  1.00 77.33  ? 99   ALA B CB  1 
ATOM   5082 N N   . LEU B 2 100 ? -11.314 -76.151 33.994  1.00 77.97  ? 100  LEU B N   1 
ATOM   5083 C CA  . LEU B 2 100 ? -10.909 -75.673 32.679  1.00 78.99  ? 100  LEU B CA  1 
ATOM   5084 C C   . LEU B 2 100 ? -9.802  -74.627 32.794  1.00 87.96  ? 100  LEU B C   1 
ATOM   5085 O O   . LEU B 2 100 ? -8.842  -74.632 32.021  1.00 91.04  ? 100  LEU B O   1 
ATOM   5086 C CB  . LEU B 2 100 ? -12.106 -75.087 31.938  1.00 76.45  ? 100  LEU B CB  1 
ATOM   5087 C CG  . LEU B 2 100 ? -13.006 -76.130 31.273  1.00 85.89  ? 100  LEU B CG  1 
ATOM   5088 C CD1 . LEU B 2 100 ? -14.227 -75.494 30.641  1.00 57.66  ? 100  LEU B CD1 1 
ATOM   5089 C CD2 . LEU B 2 100 ? -12.201 -76.861 30.239  1.00 89.04  ? 100  LEU B CD2 1 
ATOM   5090 N N   . GLY B 2 101 ? -9.945  -73.734 33.768  1.00 85.67  ? 101  GLY B N   1 
ATOM   5091 C CA  . GLY B 2 101 ? -8.919  -72.757 34.073  1.00 86.17  ? 101  GLY B CA  1 
ATOM   5092 C C   . GLY B 2 101 ? -7.561  -73.376 34.366  1.00 85.26  ? 101  GLY B C   1 
ATOM   5093 O O   . GLY B 2 101 ? -6.564  -73.008 33.747  1.00 87.45  ? 101  GLY B O   1 
ATOM   5094 N N   . ASN B 2 102 ? -7.516  -74.315 35.305  1.00 82.33  ? 102  ASN B N   1 
ATOM   5095 C CA  . ASN B 2 102 ? -6.258  -74.945 35.688  1.00 82.76  ? 102  ASN B CA  1 
ATOM   5096 C C   . ASN B 2 102 ? -5.581  -75.702 34.554  1.00 78.77  ? 102  ASN B C   1 
ATOM   5097 O O   . ASN B 2 102 ? -4.353  -75.747 34.479  1.00 76.49  ? 102  ASN B O   1 
ATOM   5098 C CB  . ASN B 2 102 ? -6.448  -75.846 36.910  1.00 92.23  ? 102  ASN B CB  1 
ATOM   5099 C CG  . ASN B 2 102 ? -6.723  -75.051 38.172  1.00 107.50 ? 102  ASN B CG  1 
ATOM   5100 O OD1 . ASN B 2 102 ? -7.722  -75.276 38.856  1.00 113.28 ? 102  ASN B OD1 1 
ATOM   5101 N ND2 . ASN B 2 102 ? -5.845  -74.095 38.476  1.00 107.58 ? 102  ASN B ND2 1 
ATOM   5102 N N   . LYS B 2 103 ? -6.372  -76.296 33.669  1.00 83.14  ? 103  LYS B N   1 
ATOM   5103 C CA  . LYS B 2 103 ? -5.793  -77.002 32.540  1.00 88.41  ? 103  LYS B CA  1 
ATOM   5104 C C   . LYS B 2 103 ? -5.118  -75.984 31.631  1.00 85.71  ? 103  LYS B C   1 
ATOM   5105 O O   . LYS B 2 103 ? -3.964  -76.154 31.248  1.00 85.30  ? 103  LYS B O   1 
ATOM   5106 C CB  . LYS B 2 103 ? -6.858  -77.800 31.777  1.00 91.88  ? 103  LYS B CB  1 
ATOM   5107 C CG  . LYS B 2 103 ? -6.474  -79.265 31.483  1.00 92.74  ? 103  LYS B CG  1 
ATOM   5108 C CD  . LYS B 2 103 ? -5.342  -79.386 30.477  1.00 97.53  ? 103  LYS B CD  1 
ATOM   5109 C CE  . LYS B 2 103 ? -4.327  -80.452 30.888  1.00 106.13 ? 103  LYS B CE  1 
ATOM   5110 N NZ  . LYS B 2 103 ? -4.867  -81.838 30.826  1.00 116.34 ? 103  LYS B NZ  1 
ATOM   5111 N N   . ILE B 2 104 ? -5.848  -74.923 31.301  1.00 79.16  ? 104  ILE B N   1 
ATOM   5112 C CA  . ILE B 2 104 ? -5.317  -73.840 30.477  1.00 79.43  ? 104  ILE B CA  1 
ATOM   5113 C C   . ILE B 2 104 ? -4.014  -73.319 31.064  1.00 77.68  ? 104  ILE B C   1 
ATOM   5114 O O   . ILE B 2 104 ? -3.040  -73.092 30.341  1.00 71.17  ? 104  ILE B O   1 
ATOM   5115 C CB  . ILE B 2 104 ? -6.310  -72.661 30.369  1.00 74.96  ? 104  ILE B CB  1 
ATOM   5116 C CG1 . ILE B 2 104 ? -7.388  -72.961 29.326  1.00 73.33  ? 104  ILE B CG1 1 
ATOM   5117 C CG2 . ILE B 2 104 ? -5.581  -71.398 29.988  1.00 72.20  ? 104  ILE B CG2 1 
ATOM   5118 C CD1 . ILE B 2 104 ? -8.681  -72.199 29.542  1.00 68.57  ? 104  ILE B CD1 1 
ATOM   5119 N N   . ARG B 2 105 ? -3.997  -73.137 32.381  1.00 74.79  ? 105  ARG B N   1 
ATOM   5120 C CA  . ARG B 2 105 ? -2.802  -72.624 33.033  1.00 77.55  ? 105  ARG B CA  1 
ATOM   5121 C C   . ARG B 2 105 ? -1.645  -73.620 32.946  1.00 81.22  ? 105  ARG B C   1 
ATOM   5122 O O   . ARG B 2 105 ? -0.484  -73.235 32.780  1.00 93.85  ? 105  ARG B O   1 
ATOM   5123 C CB  . ARG B 2 105 ? -3.075  -72.178 34.478  1.00 64.07  ? 105  ARG B CB  1 
ATOM   5124 C CG  . ARG B 2 105 ? -1.802  -71.826 35.226  1.00 80.11  ? 105  ARG B CG  1 
ATOM   5125 C CD  . ARG B 2 105 ? -2.012  -70.726 36.228  1.00 90.01  ? 105  ARG B CD  1 
ATOM   5126 N NE  . ARG B 2 105 ? -3.095  -71.031 37.154  1.00 95.15  ? 105  ARG B NE  1 
ATOM   5127 C CZ  . ARG B 2 105 ? -3.086  -70.679 38.435  1.00 106.58 ? 105  ARG B CZ  1 
ATOM   5128 N NH1 . ARG B 2 105 ? -2.045  -70.012 38.943  1.00 98.92  ? 105  ARG B NH1 1 
ATOM   5129 N NH2 . ARG B 2 105 ? -4.115  -70.996 39.213  1.00 113.04 ? 105  ARG B NH2 1 
ATOM   5130 N N   . ALA B 2 106 ? -1.962  -74.901 33.034  1.00 77.49  ? 106  ALA B N   1 
ATOM   5131 C CA  . ALA B 2 106 ? -0.924  -75.916 32.996  1.00 82.85  ? 106  ALA B CA  1 
ATOM   5132 C C   . ALA B 2 106 ? -0.415  -76.135 31.575  1.00 89.61  ? 106  ALA B C   1 
ATOM   5133 O O   . ALA B 2 106 ? 0.771   -76.403 31.369  1.00 92.01  ? 106  ALA B O   1 
ATOM   5134 C CB  . ALA B 2 106 ? -1.425  -77.209 33.603  1.00 64.76  ? 106  ALA B CB  1 
ATOM   5135 N N   . ASP B 2 107 ? -1.312  -76.027 30.599  1.00 87.17  ? 107  ASP B N   1 
ATOM   5136 C CA  . ASP B 2 107 ? -0.910  -76.143 29.205  1.00 91.06  ? 107  ASP B CA  1 
ATOM   5137 C C   . ASP B 2 107 ? -0.030  -74.948 28.840  1.00 91.47  ? 107  ASP B C   1 
ATOM   5138 O O   . ASP B 2 107 ? 0.975   -75.109 28.152  1.00 95.83  ? 107  ASP B O   1 
ATOM   5139 C CB  . ASP B 2 107 ? -2.121  -76.250 28.258  1.00 94.55  ? 107  ASP B CB  1 
ATOM   5140 C CG  . ASP B 2 107 ? -2.756  -77.646 28.246  1.00 100.45 ? 107  ASP B CG  1 
ATOM   5141 O OD1 . ASP B 2 107 ? -2.060  -78.645 28.536  1.00 103.35 ? 107  ASP B OD1 1 
ATOM   5142 O OD2 . ASP B 2 107 ? -3.964  -77.740 27.932  1.00 98.32  ? 107  ASP B OD2 1 
ATOM   5143 N N   . LEU B 2 108 ? -0.395  -73.752 29.308  1.00 84.19  ? 108  LEU B N   1 
ATOM   5144 C CA  . LEU B 2 108 ? 0.443   -72.570 29.075  1.00 84.42  ? 108  LEU B CA  1 
ATOM   5145 C C   . LEU B 2 108 ? 1.835   -72.744 29.691  1.00 95.04  ? 108  LEU B C   1 
ATOM   5146 O O   . LEU B 2 108 ? 2.837   -72.671 28.979  1.00 98.00  ? 108  LEU B O   1 
ATOM   5147 C CB  . LEU B 2 108 ? -0.218  -71.291 29.595  1.00 77.03  ? 108  LEU B CB  1 
ATOM   5148 C CG  . LEU B 2 108 ? -1.392  -70.783 28.761  1.00 74.76  ? 108  LEU B CG  1 
ATOM   5149 C CD1 . LEU B 2 108 ? -2.011  -69.533 29.374  1.00 67.09  ? 108  LEU B CD1 1 
ATOM   5150 C CD2 . LEU B 2 108 ? -0.983  -70.559 27.305  1.00 65.24  ? 108  LEU B CD2 1 
ATOM   5151 N N   . LYS B 2 109 ? 1.894   -72.984 31.003  1.00 94.07  ? 109  LYS B N   1 
ATOM   5152 C CA  . LYS B 2 109 ? 3.173   -73.205 31.677  1.00 86.55  ? 109  LYS B CA  1 
ATOM   5153 C C   . LYS B 2 109 ? 4.012   -74.243 30.956  1.00 85.38  ? 109  LYS B C   1 
ATOM   5154 O O   . LYS B 2 109 ? 5.209   -74.051 30.760  1.00 87.11  ? 109  LYS B O   1 
ATOM   5155 C CB  . LYS B 2 109 ? 2.987   -73.582 33.150  1.00 91.93  ? 109  LYS B CB  1 
ATOM   5156 C CG  . LYS B 2 109 ? 2.884   -72.367 34.068  1.00 110.52 ? 109  LYS B CG  1 
ATOM   5157 C CD  . LYS B 2 109 ? 2.625   -72.747 35.517  1.00 123.01 ? 109  LYS B CD  1 
ATOM   5158 C CE  . LYS B 2 109 ? 2.370   -71.505 36.369  1.00 127.69 ? 109  LYS B CE  1 
ATOM   5159 N NZ  . LYS B 2 109 ? 2.001   -71.849 37.774  1.00 129.61 ? 109  LYS B NZ  1 
ATOM   5160 N N   . GLN B 2 110 ? 3.381   -75.338 30.547  1.00 88.00  ? 110  GLN B N   1 
ATOM   5161 C CA  . GLN B 2 110 ? 4.091   -76.390 29.834  1.00 89.46  ? 110  GLN B CA  1 
ATOM   5162 C C   . GLN B 2 110 ? 4.761   -75.825 28.573  1.00 90.00  ? 110  GLN B C   1 
ATOM   5163 O O   . GLN B 2 110 ? 5.911   -76.156 28.274  1.00 88.57  ? 110  GLN B O   1 
ATOM   5164 C CB  . GLN B 2 110 ? 3.148   -77.561 29.512  1.00 105.62 ? 110  GLN B CB  1 
ATOM   5165 C CG  . GLN B 2 110 ? 3.760   -78.690 28.661  1.00 118.94 ? 110  GLN B CG  1 
ATOM   5166 C CD  . GLN B 2 110 ? 5.097   -79.197 29.197  1.00 124.08 ? 110  GLN B CD  1 
ATOM   5167 O OE1 . GLN B 2 110 ? 5.381   -79.106 30.399  1.00 124.90 ? 110  GLN B OE1 1 
ATOM   5168 N NE2 . GLN B 2 110 ? 5.927   -79.735 28.299  1.00 114.76 ? 110  GLN B NE2 1 
ATOM   5169 N N   . ILE B 2 111 ? 4.055   -74.954 27.851  1.00 90.23  ? 111  ILE B N   1 
ATOM   5170 C CA  . ILE B 2 111 ? 4.593   -74.385 26.615  1.00 89.77  ? 111  ILE B CA  1 
ATOM   5171 C C   . ILE B 2 111 ? 5.709   -73.387 26.914  1.00 92.10  ? 111  ILE B C   1 
ATOM   5172 O O   . ILE B 2 111 ? 6.667   -73.268 26.146  1.00 83.77  ? 111  ILE B O   1 
ATOM   5173 C CB  . ILE B 2 111 ? 3.506   -73.708 25.747  1.00 85.02  ? 111  ILE B CB  1 
ATOM   5174 C CG1 . ILE B 2 111 ? 2.330   -74.659 25.516  1.00 82.37  ? 111  ILE B CG1 1 
ATOM   5175 C CG2 . ILE B 2 111 ? 4.090   -73.276 24.412  1.00 87.69  ? 111  ILE B CG2 1 
ATOM   5176 C CD1 . ILE B 2 111 ? 1.251   -74.107 24.587  1.00 76.11  ? 111  ILE B CD1 1 
ATOM   5177 N N   . GLU B 2 112 ? 5.580   -72.683 28.037  1.00 96.68  ? 112  GLU B N   1 
ATOM   5178 C CA  . GLU B 2 112 ? 6.600   -71.743 28.478  1.00 101.52 ? 112  GLU B CA  1 
ATOM   5179 C C   . GLU B 2 112 ? 7.914   -72.475 28.677  1.00 104.84 ? 112  GLU B C   1 
ATOM   5180 O O   . GLU B 2 112 ? 8.897   -72.186 28.001  1.00 105.04 ? 112  GLU B O   1 
ATOM   5181 C CB  . GLU B 2 112 ? 6.190   -71.063 29.780  1.00 111.50 ? 112  GLU B CB  1 
ATOM   5182 C CG  . GLU B 2 112 ? 7.189   -70.027 30.254  1.00 130.20 ? 112  GLU B CG  1 
ATOM   5183 C CD  . GLU B 2 112 ? 7.014   -69.690 31.717  1.00 142.37 ? 112  GLU B CD  1 
ATOM   5184 O OE1 . GLU B 2 112 ? 6.146   -70.324 32.361  1.00 143.44 ? 112  GLU B OE1 1 
ATOM   5185 O OE2 . GLU B 2 112 ? 7.743   -68.800 32.220  1.00 142.77 ? 112  GLU B OE2 1 
ATOM   5186 N N   . LYS B 2 113 ? 7.922   -73.425 29.608  1.00 111.61 ? 113  LYS B N   1 
ATOM   5187 C CA  . LYS B 2 113 ? 9.084   -74.282 29.820  1.00 116.00 ? 113  LYS B CA  1 
ATOM   5188 C C   . LYS B 2 113 ? 9.572   -74.880 28.501  1.00 108.85 ? 113  LYS B C   1 
ATOM   5189 O O   . LYS B 2 113 ? 10.766  -74.885 28.220  1.00 104.74 ? 113  LYS B O   1 
ATOM   5190 C CB  . LYS B 2 113 ? 8.767   -75.391 30.830  1.00 126.84 ? 113  LYS B CB  1 
ATOM   5191 C CG  . LYS B 2 113 ? 8.516   -74.883 32.251  1.00 137.79 ? 113  LYS B CG  1 
ATOM   5192 C CD  . LYS B 2 113 ? 8.180   -76.021 33.219  1.00 143.34 ? 113  LYS B CD  1 
ATOM   5193 C CE  . LYS B 2 113 ? 7.910   -75.493 34.630  1.00 139.11 ? 113  LYS B CE  1 
ATOM   5194 N NZ  . LYS B 2 113 ? 7.475   -76.563 35.574  1.00 137.29 ? 113  LYS B NZ  1 
ATOM   5195 N N   . GLU B 2 114 ? 8.643   -75.377 27.691  1.00 112.22 ? 114  GLU B N   1 
ATOM   5196 C CA  . GLU B 2 114 ? 8.995   -75.938 26.387  1.00 117.72 ? 114  GLU B CA  1 
ATOM   5197 C C   . GLU B 2 114 ? 9.773   -74.929 25.541  1.00 112.29 ? 114  GLU B C   1 
ATOM   5198 O O   . GLU B 2 114 ? 10.780  -75.283 24.924  1.00 109.40 ? 114  GLU B O   1 
ATOM   5199 C CB  . GLU B 2 114 ? 7.743   -76.413 25.634  1.00 120.33 ? 114  GLU B CB  1 
ATOM   5200 C CG  . GLU B 2 114 ? 7.530   -77.924 25.627  1.00 121.96 ? 114  GLU B CG  1 
ATOM   5201 C CD  . GLU B 2 114 ? 6.241   -78.333 24.918  1.00 132.72 ? 114  GLU B CD  1 
ATOM   5202 O OE1 . GLU B 2 114 ? 5.334   -77.483 24.793  1.00 133.19 ? 114  GLU B OE1 1 
ATOM   5203 O OE2 . GLU B 2 114 ? 6.130   -79.504 24.487  1.00 138.88 ? 114  GLU B OE2 1 
ATOM   5204 N N   . ASN B 2 115 ? 9.301   -73.682 25.518  1.00 106.78 ? 115  ASN B N   1 
ATOM   5205 C CA  . ASN B 2 115 ? 9.942   -72.612 24.748  1.00 101.29 ? 115  ASN B CA  1 
ATOM   5206 C C   . ASN B 2 115 ? 11.279  -72.195 25.359  1.00 105.43 ? 115  ASN B C   1 
ATOM   5207 O O   . ASN B 2 115 ? 12.299  -72.127 24.673  1.00 108.42 ? 115  ASN B O   1 
ATOM   5208 C CB  . ASN B 2 115 ? 9.015   -71.388 24.620  1.00 94.37  ? 115  ASN B CB  1 
ATOM   5209 C CG  . ASN B 2 115 ? 7.787   -71.656 23.749  1.00 98.24  ? 115  ASN B CG  1 
ATOM   5210 O OD1 . ASN B 2 115 ? 7.580   -72.769 23.261  1.00 100.95 ? 115  ASN B OD1 1 
ATOM   5211 N ND2 . ASN B 2 115 ? 6.965   -70.631 23.561  1.00 95.13  ? 115  ASN B ND2 1 
ATOM   5212 N N   . LYS B 2 116 ? 11.259  -71.918 26.658  1.00 107.94 ? 116  LYS B N   1 
ATOM   5213 C CA  . LYS B 2 116 ? 12.451  -71.524 27.397  1.00 102.60 ? 116  LYS B CA  1 
ATOM   5214 C C   . LYS B 2 116 ? 13.583  -72.527 27.181  1.00 106.96 ? 116  LYS B C   1 
ATOM   5215 O O   . LYS B 2 116 ? 14.719  -72.143 26.912  1.00 117.20 ? 116  LYS B O   1 
ATOM   5216 C CB  . LYS B 2 116 ? 12.117  -71.394 28.885  1.00 100.91 ? 116  LYS B CB  1 
ATOM   5217 C CG  . LYS B 2 116 ? 13.077  -70.532 29.672  1.00 118.14 ? 116  LYS B CG  1 
ATOM   5218 C CD  . LYS B 2 116 ? 12.405  -69.914 30.896  1.00 125.89 ? 116  LYS B CD  1 
ATOM   5219 C CE  . LYS B 2 116 ? 13.344  -68.915 31.577  1.00 131.08 ? 116  LYS B CE  1 
ATOM   5220 N NZ  . LYS B 2 116 ? 12.675  -68.110 32.643  1.00 127.84 ? 116  LYS B NZ  1 
ATOM   5221 N N   . ARG B 2 117 ? 13.261  -73.812 27.288  1.00 107.13 ? 117  ARG B N   1 
ATOM   5222 C CA  . ARG B 2 117 ? 14.235  -74.877 27.080  1.00 121.50 ? 117  ARG B CA  1 
ATOM   5223 C C   . ARG B 2 117 ? 14.437  -75.163 25.599  1.00 119.29 ? 117  ARG B C   1 
ATOM   5224 O O   . ARG B 2 117 ? 14.704  -76.306 25.212  1.00 124.61 ? 117  ARG B O   1 
ATOM   5225 C CB  . ARG B 2 117 ? 13.788  -76.167 27.775  1.00 144.37 ? 117  ARG B CB  1 
ATOM   5226 C CG  . ARG B 2 117 ? 13.847  -76.147 29.301  1.00 160.47 ? 117  ARG B CG  1 
ATOM   5227 C CD  . ARG B 2 117 ? 13.703  -77.563 29.863  1.00 172.92 ? 117  ARG B CD  1 
ATOM   5228 N NE  . ARG B 2 117 ? 14.850  -78.407 29.523  1.00 181.99 ? 117  ARG B NE  1 
ATOM   5229 C CZ  . ARG B 2 117 ? 14.901  -79.726 29.704  1.00 182.59 ? 117  ARG B CZ  1 
ATOM   5230 N NH1 . ARG B 2 117 ? 13.862  -80.372 30.217  1.00 182.47 ? 117  ARG B NH1 1 
ATOM   5231 N NH2 . ARG B 2 117 ? 15.993  -80.401 29.365  1.00 180.25 ? 117  ARG B NH2 1 
ATOM   5232 N N   . ALA B 2 118 ? 14.300  -74.131 24.772  1.00 110.55 ? 118  ALA B N   1 
ATOM   5233 C CA  . ALA B 2 118 ? 14.447  -74.285 23.327  1.00 108.78 ? 118  ALA B CA  1 
ATOM   5234 C C   . ALA B 2 118 ? 15.029  -73.035 22.676  1.00 121.02 ? 118  ALA B C   1 
ATOM   5235 O O   . ALA B 2 118 ? 15.315  -73.032 21.476  1.00 121.71 ? 118  ALA B O   1 
ATOM   5236 C CB  . ALA B 2 118 ? 13.113  -74.643 22.689  1.00 99.61  ? 118  ALA B CB  1 
ATOM   5237 N N   . GLN B 2 119 ? 15.194  -71.979 23.472  1.00 126.65 ? 119  GLN B N   1 
ATOM   5238 C CA  . GLN B 2 119 ? 15.790  -70.735 22.999  1.00 129.19 ? 119  GLN B CA  1 
ATOM   5239 C C   . GLN B 2 119 ? 17.148  -70.997 22.352  1.00 136.75 ? 119  GLN B C   1 
ATOM   5240 O O   . GLN B 2 119 ? 17.307  -70.865 21.138  1.00 134.74 ? 119  GLN B O   1 
ATOM   5241 C CB  . GLN B 2 119 ? 15.956  -69.751 24.161  1.00 133.03 ? 119  GLN B CB  1 
ATOM   5242 C CG  . GLN B 2 119 ? 14.663  -69.357 24.862  1.00 136.55 ? 119  GLN B CG  1 
ATOM   5243 C CD  . GLN B 2 119 ? 13.860  -68.324 24.088  1.00 140.91 ? 119  GLN B CD  1 
ATOM   5244 O OE1 . GLN B 2 119 ? 14.408  -67.560 23.287  1.00 135.40 ? 119  GLN B OE1 1 
ATOM   5245 N NE2 . GLN B 2 119 ? 12.551  -68.293 24.329  1.00 144.39 ? 119  GLN B NE2 1 
ATOM   5246 N N   . GLN B 2 120 ? 18.118  -71.383 23.176  1.00 148.15 ? 120  GLN B N   1 
ATOM   5247 C CA  . GLN B 2 120 ? 19.506  -71.545 22.745  1.00 155.43 ? 120  GLN B CA  1 
ATOM   5248 C C   . GLN B 2 120 ? 19.645  -72.465 21.529  1.00 147.37 ? 120  GLN B C   1 
ATOM   5249 O O   . GLN B 2 120 ? 20.553  -72.304 20.710  1.00 146.62 ? 120  GLN B O   1 
ATOM   5250 C CB  . GLN B 2 120 ? 20.364  -72.066 23.907  1.00 164.57 ? 120  GLN B CB  1 
ATOM   5251 C CG  . GLN B 2 120 ? 20.036  -71.449 25.274  1.00 169.88 ? 120  GLN B CG  1 
ATOM   5252 C CD  . GLN B 2 120 ? 18.881  -72.150 25.988  1.00 171.42 ? 120  GLN B CD  1 
ATOM   5253 O OE1 . GLN B 2 120 ? 17.732  -71.711 25.919  1.00 169.47 ? 120  GLN B OE1 1 
ATOM   5254 N NE2 . GLN B 2 120 ? 19.187  -73.241 26.683  1.00 172.20 ? 120  GLN B NE2 1 
ATOM   5255 N N   . GLU B 2 121 ? 18.736  -73.424 21.418  1.00 143.91 ? 121  GLU B N   1 
ATOM   5256 C CA  . GLU B 2 121 ? 18.783  -74.405 20.343  1.00 155.33 ? 121  GLU B CA  1 
ATOM   5257 C C   . GLU B 2 121 ? 18.116  -73.869 19.082  1.00 156.14 ? 121  GLU B C   1 
ATOM   5258 O O   . GLU B 2 121 ? 18.504  -74.215 17.966  1.00 159.32 ? 121  GLU B O   1 
ATOM   5259 C CB  . GLU B 2 121 ? 18.107  -75.715 20.776  1.00 164.77 ? 121  GLU B CB  1 
ATOM   5260 C CG  . GLU B 2 121 ? 18.887  -76.539 21.804  1.00 174.23 ? 121  GLU B CG  1 
ATOM   5261 C CD  . GLU B 2 121 ? 18.913  -75.911 23.194  1.00 183.43 ? 121  GLU B CD  1 
ATOM   5262 O OE1 . GLU B 2 121 ? 18.026  -75.087 23.499  1.00 188.30 ? 121  GLU B OE1 1 
ATOM   5263 O OE2 . GLU B 2 121 ? 19.820  -76.249 23.987  1.00 183.64 ? 121  GLU B OE2 1 
ATOM   5264 N N   . GLY B 2 122 ? 17.112  -73.020 19.268  1.00 152.29 ? 122  GLY B N   1 
ATOM   5265 C CA  . GLY B 2 122 ? 16.333  -72.503 18.159  1.00 147.42 ? 122  GLY B CA  1 
ATOM   5266 C C   . GLY B 2 122 ? 16.841  -71.183 17.612  1.00 143.89 ? 122  GLY B C   1 
ATOM   5267 O O   . GLY B 2 122 ? 16.191  -70.577 16.759  1.00 137.90 ? 122  GLY B O   1 
ATOM   5268 N N   . THR B 2 123 ? 17.994  -70.734 18.109  1.00 145.22 ? 123  THR B N   1 
ATOM   5269 C CA  . THR B 2 123 ? 18.659  -69.540 17.585  1.00 144.64 ? 123  THR B CA  1 
ATOM   5270 C C   . THR B 2 123 ? 20.010  -69.902 16.976  1.00 153.87 ? 123  THR B C   1 
ATOM   5271 O O   . THR B 2 123 ? 20.874  -70.474 17.645  1.00 154.26 ? 123  THR B O   1 
ATOM   5272 C CB  . THR B 2 123 ? 18.885  -68.481 18.673  1.00 135.75 ? 123  THR B CB  1 
ATOM   5273 O OG1 . THR B 2 123 ? 19.800  -68.992 19.651  1.00 137.69 ? 123  THR B OG1 1 
ATOM   5274 C CG2 . THR B 2 123 ? 17.572  -68.112 19.346  1.00 129.46 ? 123  THR B CG2 1 
ATOM   5275 N N   . PHE B 2 124 ? 20.186  -69.562 15.703  1.00 162.84 ? 124  PHE B N   1 
ATOM   5276 C CA  . PHE B 2 124 ? 21.392  -69.920 14.969  1.00 172.24 ? 124  PHE B CA  1 
ATOM   5277 C C   . PHE B 2 124 ? 22.261  -68.690 14.745  1.00 172.76 ? 124  PHE B C   1 
ATOM   5278 O O   . PHE B 2 124 ? 22.793  -68.486 13.652  1.00 173.28 ? 124  PHE B O   1 
ATOM   5279 C CB  . PHE B 2 124 ? 21.018  -70.545 13.623  1.00 181.77 ? 124  PHE B CB  1 
ATOM   5280 C CG  . PHE B 2 124 ? 19.998  -71.648 13.728  1.00 192.35 ? 124  PHE B CG  1 
ATOM   5281 C CD1 . PHE B 2 124 ? 18.651  -71.384 13.546  1.00 194.85 ? 124  PHE B CD1 1 
ATOM   5282 C CD2 . PHE B 2 124 ? 20.386  -72.949 14.014  1.00 198.75 ? 124  PHE B CD2 1 
ATOM   5283 C CE1 . PHE B 2 124 ? 17.710  -72.395 13.643  1.00 199.16 ? 124  PHE B CE1 1 
ATOM   5284 C CE2 . PHE B 2 124 ? 19.448  -73.967 14.114  1.00 200.25 ? 124  PHE B CE2 1 
ATOM   5285 C CZ  . PHE B 2 124 ? 18.109  -73.689 13.928  1.00 200.55 ? 124  PHE B CZ  1 
ATOM   5286 N N   . GLU B 2 125 ? 22.409  -67.880 15.790  1.00 170.99 ? 125  GLU B N   1 
ATOM   5287 C CA  . GLU B 2 125 ? 23.049  -66.575 15.665  1.00 170.32 ? 125  GLU B CA  1 
ATOM   5288 C C   . GLU B 2 125 ? 22.281  -65.761 14.644  1.00 167.25 ? 125  GLU B C   1 
ATOM   5289 O O   . GLU B 2 125 ? 21.082  -65.965 14.458  1.00 170.69 ? 125  GLU B O   1 
ATOM   5290 C CB  . GLU B 2 125 ? 24.503  -66.713 15.225  1.00 173.20 ? 125  GLU B CB  1 
ATOM   5291 C CG  . GLU B 2 125 ? 25.371  -67.469 16.203  1.00 179.73 ? 125  GLU B CG  1 
ATOM   5292 C CD  . GLU B 2 125 ? 26.738  -67.768 15.637  1.00 183.26 ? 125  GLU B CD  1 
ATOM   5293 O OE1 . GLU B 2 125 ? 27.088  -67.167 14.600  1.00 184.66 ? 125  GLU B OE1 1 
ATOM   5294 O OE2 . GLU B 2 125 ? 27.459  -68.603 16.224  1.00 183.53 ? 125  GLU B OE2 1 
ATOM   5295 N N   . ASP B 2 126 ? 22.974  -64.845 13.977  1.00 159.54 ? 126  ASP B N   1 
ATOM   5296 C CA  . ASP B 2 126 ? 22.357  -64.020 12.946  1.00 155.11 ? 126  ASP B CA  1 
ATOM   5297 C C   . ASP B 2 126 ? 21.234  -63.183 13.542  1.00 154.30 ? 126  ASP B C   1 
ATOM   5298 O O   . ASP B 2 126 ? 20.688  -62.304 12.875  1.00 153.85 ? 126  ASP B O   1 
ATOM   5299 C CB  . ASP B 2 126 ? 21.793  -64.888 11.814  1.00 156.46 ? 126  ASP B CB  1 
ATOM   5300 C CG  . ASP B 2 126 ? 22.753  -65.979 11.373  1.00 161.28 ? 126  ASP B CG  1 
ATOM   5301 O OD1 . ASP B 2 126 ? 23.921  -65.971 11.816  1.00 166.74 ? 126  ASP B OD1 1 
ATOM   5302 O OD2 . ASP B 2 126 ? 22.334  -66.851 10.581  1.00 158.40 ? 126  ASP B OD2 1 
ATOM   5303 N N   . GLY B 2 127 ? 20.892  -63.465 14.798  1.00 154.66 ? 127  GLY B N   1 
ATOM   5304 C CA  . GLY B 2 127 ? 19.770  -62.827 15.465  1.00 149.48 ? 127  GLY B CA  1 
ATOM   5305 C C   . GLY B 2 127 ? 18.449  -63.517 15.163  1.00 141.90 ? 127  GLY B C   1 
ATOM   5306 O O   . GLY B 2 127 ? 17.445  -63.275 15.836  1.00 140.42 ? 127  GLY B O   1 
ATOM   5307 N N   . THR B 2 128 ? 18.459  -64.385 14.152  1.00 130.75 ? 128  THR B N   1 
ATOM   5308 C CA  . THR B 2 128 ? 17.248  -65.045 13.672  1.00 118.19 ? 128  THR B CA  1 
ATOM   5309 C C   . THR B 2 128 ? 16.835  -66.199 14.580  1.00 113.77 ? 128  THR B C   1 
ATOM   5310 O O   . THR B 2 128 ? 17.622  -66.660 15.412  1.00 116.05 ? 128  THR B O   1 
ATOM   5311 C CB  . THR B 2 128 ? 17.426  -65.578 12.233  1.00 116.22 ? 128  THR B CB  1 
ATOM   5312 O OG1 . THR B 2 128 ? 18.223  -66.770 12.249  1.00 123.84 ? 128  THR B OG1 1 
ATOM   5313 C CG2 . THR B 2 128 ? 18.093  -64.533 11.350  1.00 105.20 ? 128  THR B CG2 1 
ATOM   5314 N N   . VAL B 2 129 ? 15.596  -66.659 14.418  1.00 106.50 ? 129  VAL B N   1 
ATOM   5315 C CA  . VAL B 2 129 ? 15.083  -67.771 15.208  1.00 105.67 ? 129  VAL B CA  1 
ATOM   5316 C C   . VAL B 2 129 ? 14.758  -68.975 14.318  1.00 117.64 ? 129  VAL B C   1 
ATOM   5317 O O   . VAL B 2 129 ? 15.598  -69.430 13.546  1.00 133.98 ? 129  VAL B O   1 
ATOM   5318 C CB  . VAL B 2 129 ? 13.861  -67.352 16.053  1.00 101.19 ? 129  VAL B CB  1 
ATOM   5319 C CG1 . VAL B 2 129 ? 13.522  -68.418 17.087  1.00 103.24 ? 129  VAL B CG1 1 
ATOM   5320 C CG2 . VAL B 2 129 ? 14.150  -66.049 16.757  1.00 94.05  ? 129  VAL B CG2 1 
ATOM   5321 N N   . SER B 2 130 ? 13.544  -69.492 14.421  1.00 109.44 ? 130  SER B N   1 
ATOM   5322 C CA  . SER B 2 130 ? 13.206  -70.725 13.738  1.00 106.38 ? 130  SER B CA  1 
ATOM   5323 C C   . SER B 2 130 ? 11.702  -70.868 13.726  1.00 106.91 ? 130  SER B C   1 
ATOM   5324 O O   . SER B 2 130 ? 11.060  -70.806 14.773  1.00 106.97 ? 130  SER B O   1 
ATOM   5325 C CB  . SER B 2 130 ? 13.831  -71.918 14.459  1.00 107.59 ? 130  SER B CB  1 
ATOM   5326 O OG  . SER B 2 130 ? 12.959  -72.430 15.453  1.00 105.90 ? 130  SER B OG  1 
ATOM   5327 N N   . THR B 2 131 ? 11.144  -71.061 12.537  1.00 100.96 ? 131  THR B N   1 
ATOM   5328 C CA  . THR B 2 131 ? 9.699   -71.039 12.362  1.00 97.86  ? 131  THR B CA  1 
ATOM   5329 C C   . THR B 2 131 ? 8.981   -71.807 13.485  1.00 98.83  ? 131  THR B C   1 
ATOM   5330 O O   . THR B 2 131 ? 7.927   -71.385 13.957  1.00 96.44  ? 131  THR B O   1 
ATOM   5331 C CB  . THR B 2 131 ? 9.300   -71.533 10.944  1.00 93.02  ? 131  THR B CB  1 
ATOM   5332 O OG1 . THR B 2 131 ? 10.166  -70.933 9.967   1.00 97.80  ? 131  THR B OG1 1 
ATOM   5333 C CG2 . THR B 2 131 ? 7.859   -71.161 10.620  1.00 82.70  ? 131  THR B CG2 1 
ATOM   5334 N N   . ASP B 2 132 ? 9.572   -72.913 13.933  1.00 108.47 ? 132  ASP B N   1 
ATOM   5335 C CA  . ASP B 2 132 ? 9.036   -73.678 15.061  1.00 105.70 ? 132  ASP B CA  1 
ATOM   5336 C C   . ASP B 2 132 ? 8.870   -72.782 16.286  1.00 98.48  ? 132  ASP B C   1 
ATOM   5337 O O   . ASP B 2 132 ? 7.766   -72.614 16.804  1.00 93.10  ? 132  ASP B O   1 
ATOM   5338 C CB  . ASP B 2 132 ? 9.964   -74.847 15.421  1.00 109.77 ? 132  ASP B CB  1 
ATOM   5339 C CG  . ASP B 2 132 ? 10.358  -75.684 14.214  1.00 120.37 ? 132  ASP B CG  1 
ATOM   5340 O OD1 . ASP B 2 132 ? 11.292  -75.279 13.481  1.00 122.94 ? 132  ASP B OD1 1 
ATOM   5341 O OD2 . ASP B 2 132 ? 9.743   -76.755 14.006  1.00 123.14 ? 132  ASP B OD2 1 
ATOM   5342 N N   . LEU B 2 133 ? 9.982   -72.207 16.737  1.00 95.46  ? 133  LEU B N   1 
ATOM   5343 C CA  . LEU B 2 133 ? 10.002  -71.394 17.950  1.00 91.51  ? 133  LEU B CA  1 
ATOM   5344 C C   . LEU B 2 133 ? 9.238   -70.072 17.787  1.00 89.87  ? 133  LEU B C   1 
ATOM   5345 O O   . LEU B 2 133 ? 8.604   -69.595 18.733  1.00 88.94  ? 133  LEU B O   1 
ATOM   5346 C CB  . LEU B 2 133 ? 11.447  -71.158 18.419  1.00 85.46  ? 133  LEU B CB  1 
ATOM   5347 C CG  . LEU B 2 133 ? 11.651  -70.286 19.660  1.00 90.38  ? 133  LEU B CG  1 
ATOM   5348 C CD1 . LEU B 2 133 ? 10.854  -70.807 20.832  1.00 92.05  ? 133  LEU B CD1 1 
ATOM   5349 C CD2 . LEU B 2 133 ? 13.117  -70.214 20.016  1.00 102.45 ? 133  LEU B CD2 1 
ATOM   5350 N N   . ARG B 2 134 ? 9.289   -69.491 16.591  1.00 80.90  ? 134  ARG B N   1 
ATOM   5351 C CA  . ARG B 2 134 ? 8.518   -68.285 16.301  1.00 77.06  ? 134  ARG B CA  1 
ATOM   5352 C C   . ARG B 2 134 ? 7.019   -68.521 16.495  1.00 81.41  ? 134  ARG B C   1 
ATOM   5353 O O   . ARG B 2 134 ? 6.348   -67.745 17.186  1.00 74.97  ? 134  ARG B O   1 
ATOM   5354 C CB  . ARG B 2 134 ? 8.799   -67.793 14.882  1.00 81.67  ? 134  ARG B CB  1 
ATOM   5355 C CG  . ARG B 2 134 ? 10.165  -67.135 14.700  1.00 90.04  ? 134  ARG B CG  1 
ATOM   5356 C CD  . ARG B 2 134 ? 10.406  -66.785 13.237  1.00 88.82  ? 134  ARG B CD  1 
ATOM   5357 N NE  . ARG B 2 134 ? 9.290   -66.020 12.689  1.00 82.19  ? 134  ARG B NE  1 
ATOM   5358 C CZ  . ARG B 2 134 ? 8.881   -66.096 11.427  1.00 78.23  ? 134  ARG B CZ  1 
ATOM   5359 N NH1 . ARG B 2 134 ? 9.496   -66.909 10.577  1.00 80.27  ? 134  ARG B NH1 1 
ATOM   5360 N NH2 . ARG B 2 134 ? 7.850   -65.368 11.021  1.00 69.72  ? 134  ARG B NH2 1 
ATOM   5361 N N   . ILE B 2 135 ? 6.509   -69.594 15.881  1.00 77.86  ? 135  ILE B N   1 
ATOM   5362 C CA  . ILE B 2 135 ? 5.111   -69.999 16.008  1.00 72.07  ? 135  ILE B CA  1 
ATOM   5363 C C   . ILE B 2 135 ? 4.738   -70.269 17.458  1.00 78.63  ? 135  ILE B C   1 
ATOM   5364 O O   . ILE B 2 135 ? 3.722   -69.784 17.949  1.00 85.14  ? 135  ILE B O   1 
ATOM   5365 C CB  . ILE B 2 135 ? 4.816   -71.256 15.166  1.00 76.48  ? 135  ILE B CB  1 
ATOM   5366 C CG1 . ILE B 2 135 ? 4.729   -70.889 13.685  1.00 74.98  ? 135  ILE B CG1 1 
ATOM   5367 C CG2 . ILE B 2 135 ? 3.520   -71.928 15.608  1.00 72.35  ? 135  ILE B CG2 1 
ATOM   5368 C CD1 . ILE B 2 135 ? 4.927   -72.055 12.752  1.00 65.71  ? 135  ILE B CD1 1 
ATOM   5369 N N   . ARG B 2 136 ? 5.565   -71.044 18.145  1.00 78.84  ? 136  ARG B N   1 
ATOM   5370 C CA  . ARG B 2 136 ? 5.321   -71.333 19.551  1.00 88.19  ? 136  ARG B CA  1 
ATOM   5371 C C   . ARG B 2 136 ? 5.180   -70.049 20.371  1.00 85.67  ? 136  ARG B C   1 
ATOM   5372 O O   . ARG B 2 136 ? 4.286   -69.930 21.209  1.00 81.51  ? 136  ARG B O   1 
ATOM   5373 C CB  . ARG B 2 136 ? 6.450   -72.195 20.121  1.00 100.59 ? 136  ARG B CB  1 
ATOM   5374 C CG  . ARG B 2 136 ? 6.592   -73.567 19.475  1.00 97.05  ? 136  ARG B CG  1 
ATOM   5375 C CD  . ARG B 2 136 ? 7.798   -74.320 20.030  1.00 94.76  ? 136  ARG B CD  1 
ATOM   5376 N NE  . ARG B 2 136 ? 7.485   -75.730 20.222  1.00 101.35 ? 136  ARG B NE  1 
ATOM   5377 C CZ  . ARG B 2 136 ? 6.949   -76.229 21.329  1.00 94.45  ? 136  ARG B CZ  1 
ATOM   5378 N NH1 . ARG B 2 136 ? 6.683   -75.428 22.351  1.00 88.36  ? 136  ARG B NH1 1 
ATOM   5379 N NH2 . ARG B 2 136 ? 6.678   -77.526 21.409  1.00 91.13  ? 136  ARG B NH2 1 
ATOM   5380 N N   . GLN B 2 137 ? 6.067   -69.089 20.121  1.00 87.93  ? 137  GLN B N   1 
ATOM   5381 C CA  . GLN B 2 137 ? 6.078   -67.839 20.873  1.00 81.94  ? 137  GLN B CA  1 
ATOM   5382 C C   . GLN B 2 137 ? 4.866   -66.952 20.608  1.00 78.21  ? 137  GLN B C   1 
ATOM   5383 O O   . GLN B 2 137 ? 4.314   -66.379 21.544  1.00 81.34  ? 137  GLN B O   1 
ATOM   5384 C CB  . GLN B 2 137 ? 7.374   -67.072 20.631  1.00 86.34  ? 137  GLN B CB  1 
ATOM   5385 C CG  . GLN B 2 137 ? 8.559   -67.651 21.385  1.00 92.13  ? 137  GLN B CG  1 
ATOM   5386 C CD  . GLN B 2 137 ? 9.884   -67.015 21.001  1.00 90.45  ? 137  GLN B CD  1 
ATOM   5387 O OE1 . GLN B 2 137 ? 9.974   -66.266 20.022  1.00 92.18  ? 137  GLN B OE1 1 
ATOM   5388 N NE2 . GLN B 2 137 ? 10.924  -67.324 21.769  1.00 80.70  ? 137  GLN B NE2 1 
ATOM   5389 N N   . SER B 2 138 ? 4.436   -66.843 19.353  1.00 68.35  ? 138  SER B N   1 
ATOM   5390 C CA  . SER B 2 138 ? 3.241   -66.051 19.066  1.00 67.65  ? 138  SER B CA  1 
ATOM   5391 C C   . SER B 2 138 ? 1.963   -66.711 19.577  1.00 78.96  ? 138  SER B C   1 
ATOM   5392 O O   . SER B 2 138 ? 1.054   -66.020 20.035  1.00 88.03  ? 138  SER B O   1 
ATOM   5393 C CB  . SER B 2 138 ? 3.128   -65.684 17.587  1.00 64.74  ? 138  SER B CB  1 
ATOM   5394 O OG  . SER B 2 138 ? 3.362   -66.802 16.769  1.00 79.40  ? 138  SER B OG  1 
ATOM   5395 N N   . GLN B 2 139 ? 1.901   -68.041 19.513  1.00 78.01  ? 139  GLN B N   1 
ATOM   5396 C CA  . GLN B 2 139 ? 0.790   -68.788 20.106  1.00 75.99  ? 139  GLN B CA  1 
ATOM   5397 C C   . GLN B 2 139 ? 0.752   -68.586 21.622  1.00 75.62  ? 139  GLN B C   1 
ATOM   5398 O O   . GLN B 2 139 ? -0.299  -68.293 22.208  1.00 76.16  ? 139  GLN B O   1 
ATOM   5399 C CB  . GLN B 2 139 ? 0.905   -70.294 19.810  1.00 71.53  ? 139  GLN B CB  1 
ATOM   5400 C CG  . GLN B 2 139 ? 0.714   -70.721 18.352  1.00 72.65  ? 139  GLN B CG  1 
ATOM   5401 C CD  . GLN B 2 139 ? -0.725  -70.596 17.862  1.00 73.74  ? 139  GLN B CD  1 
ATOM   5402 O OE1 . GLN B 2 139 ? -1.645  -70.311 18.629  1.00 70.51  ? 139  GLN B OE1 1 
ATOM   5403 N NE2 . GLN B 2 139 ? -0.916  -70.802 16.570  1.00 74.58  ? 139  GLN B NE2 1 
ATOM   5404 N N   . HIS B 2 140 ? 1.906   -68.759 22.256  1.00 61.47  ? 140  HIS B N   1 
ATOM   5405 C CA  . HIS B 2 140 ? 1.991   -68.665 23.707  1.00 65.75  ? 140  HIS B CA  1 
ATOM   5406 C C   . HIS B 2 140 ? 1.553   -67.286 24.203  1.00 78.67  ? 140  HIS B C   1 
ATOM   5407 O O   . HIS B 2 140 ? 0.792   -67.175 25.170  1.00 72.23  ? 140  HIS B O   1 
ATOM   5408 C CB  . HIS B 2 140 ? 3.412   -68.975 24.178  1.00 73.86  ? 140  HIS B CB  1 
ATOM   5409 C CG  . HIS B 2 140 ? 3.554   -69.023 25.667  1.00 90.44  ? 140  HIS B CG  1 
ATOM   5410 N ND1 . HIS B 2 140 ? 2.487   -68.851 26.520  1.00 96.68  ? 140  HIS B ND1 1 
ATOM   5411 C CD2 . HIS B 2 140 ? 4.636   -69.223 26.454  1.00 102.64 ? 140  HIS B CD2 1 
ATOM   5412 C CE1 . HIS B 2 140 ? 2.905   -68.941 27.771  1.00 103.40 ? 140  HIS B CE1 1 
ATOM   5413 N NE2 . HIS B 2 140 ? 4.205   -69.170 27.758  1.00 108.76 ? 140  HIS B NE2 1 
ATOM   5414 N N   . SER B 2 141 ? 2.036   -66.239 23.531  1.00 82.66  ? 141  SER B N   1 
ATOM   5415 C CA  . SER B 2 141 ? 1.711   -64.869 23.898  1.00 75.31  ? 141  SER B CA  1 
ATOM   5416 C C   . SER B 2 141 ? 0.235   -64.580 23.697  1.00 78.38  ? 141  SER B C   1 
ATOM   5417 O O   . SER B 2 141 ? -0.473  -64.197 24.631  1.00 79.60  ? 141  SER B O   1 
ATOM   5418 C CB  . SER B 2 141 ? 2.538   -63.889 23.074  1.00 88.98  ? 141  SER B CB  1 
ATOM   5419 O OG  . SER B 2 141 ? 3.907   -63.974 23.431  1.00 111.15 ? 141  SER B OG  1 
ATOM   5420 N N   . SER B 2 142 ? -0.227  -64.767 22.469  1.00 74.04  ? 142  SER B N   1 
ATOM   5421 C CA  . SER B 2 142 ? -1.606  -64.466 22.125  1.00 70.61  ? 142  SER B CA  1 
ATOM   5422 C C   . SER B 2 142 ? -2.615  -65.084 23.111  1.00 77.00  ? 142  SER B C   1 
ATOM   5423 O O   . SER B 2 142 ? -3.538  -64.407 23.575  1.00 77.80  ? 142  SER B O   1 
ATOM   5424 C CB  . SER B 2 142 ? -1.892  -64.922 20.697  1.00 68.94  ? 142  SER B CB  1 
ATOM   5425 O OG  . SER B 2 142 ? -3.211  -64.576 20.313  1.00 87.19  ? 142  SER B OG  1 
ATOM   5426 N N   . LEU B 2 143 ? -2.432  -66.362 23.430  1.00 65.98  ? 143  LEU B N   1 
ATOM   5427 C CA  . LEU B 2 143 ? -3.414  -67.094 24.224  1.00 74.81  ? 143  LEU B CA  1 
ATOM   5428 C C   . LEU B 2 143 ? -3.382  -66.711 25.705  1.00 70.40  ? 143  LEU B C   1 
ATOM   5429 O O   . LEU B 2 143 ? -4.427  -66.657 26.370  1.00 59.67  ? 143  LEU B O   1 
ATOM   5430 C CB  . LEU B 2 143 ? -3.228  -68.611 24.050  1.00 80.65  ? 143  LEU B CB  1 
ATOM   5431 C CG  . LEU B 2 143 ? -3.570  -69.173 22.665  1.00 85.04  ? 143  LEU B CG  1 
ATOM   5432 C CD1 . LEU B 2 143 ? -3.106  -70.612 22.524  1.00 82.42  ? 143  LEU B CD1 1 
ATOM   5433 C CD2 . LEU B 2 143 ? -5.064  -69.057 22.381  1.00 91.02  ? 143  LEU B CD2 1 
ATOM   5434 N N   . SER B 2 144 ? -2.187  -66.454 26.225  1.00 65.22  ? 144  SER B N   1 
ATOM   5435 C CA  . SER B 2 144 ? -2.072  -65.986 27.594  1.00 72.63  ? 144  SER B CA  1 
ATOM   5436 C C   . SER B 2 144 ? -2.875  -64.705 27.767  1.00 68.80  ? 144  SER B C   1 
ATOM   5437 O O   . SER B 2 144 ? -3.588  -64.538 28.752  1.00 65.84  ? 144  SER B O   1 
ATOM   5438 C CB  . SER B 2 144 ? -0.616  -65.766 27.960  1.00 72.61  ? 144  SER B CB  1 
ATOM   5439 O OG  . SER B 2 144 ? 0.098   -66.977 27.836  1.00 75.57  ? 144  SER B OG  1 
ATOM   5440 N N   . ARG B 2 145 ? -2.775  -63.809 26.794  1.00 64.12  ? 145  ARG B N   1 
ATOM   5441 C CA  . ARG B 2 145 ? -3.568  -62.591 26.827  1.00 63.19  ? 145  ARG B CA  1 
ATOM   5442 C C   . ARG B 2 145 ? -5.044  -62.937 26.750  1.00 60.77  ? 145  ARG B C   1 
ATOM   5443 O O   . ARG B 2 145 ? -5.811  -62.562 27.636  1.00 75.55  ? 145  ARG B O   1 
ATOM   5444 C CB  . ARG B 2 145 ? -3.150  -61.596 25.726  1.00 72.68  ? 145  ARG B CB  1 
ATOM   5445 C CG  . ARG B 2 145 ? -1.797  -60.896 25.981  1.00 69.55  ? 145  ARG B CG  1 
ATOM   5446 C CD  . ARG B 2 145 ? -1.506  -59.730 24.999  1.00 105.68 ? 145  ARG B CD  1 
ATOM   5447 N NE  . ARG B 2 145 ? -1.222  -60.181 23.634  1.00 118.86 ? 145  ARG B NE  1 
ATOM   5448 C CZ  . ARG B 2 145 ? -0.113  -60.827 23.262  1.00 126.66 ? 145  ARG B CZ  1 
ATOM   5449 N NH1 . ARG B 2 145 ? 0.834   -61.114 24.156  1.00 122.03 ? 145  ARG B NH1 1 
ATOM   5450 N NH2 . ARG B 2 145 ? 0.048   -61.198 21.991  1.00 124.21 ? 145  ARG B NH2 1 
ATOM   5451 N N   . LYS B 2 146 ? -5.441  -63.666 25.709  1.00 62.26  ? 146  LYS B N   1 
ATOM   5452 C CA  . LYS B 2 146 ? -6.839  -64.094 25.565  1.00 67.66  ? 146  LYS B CA  1 
ATOM   5453 C C   . LYS B 2 146 ? -7.350  -64.678 26.884  1.00 73.63  ? 146  LYS B C   1 
ATOM   5454 O O   . LYS B 2 146 ? -8.455  -64.359 27.314  1.00 81.02  ? 146  LYS B O   1 
ATOM   5455 C CB  . LYS B 2 146 ? -7.013  -65.086 24.404  1.00 76.41  ? 146  LYS B CB  1 
ATOM   5456 C CG  . LYS B 2 146 ? -8.464  -65.407 24.028  1.00 105.03 ? 146  LYS B CG  1 
ATOM   5457 C CD  . LYS B 2 146 ? -9.221  -64.193 23.481  1.00 128.55 ? 146  LYS B CD  1 
ATOM   5458 C CE  . LYS B 2 146 ? -10.141 -63.558 24.533  1.00 137.26 ? 146  LYS B CE  1 
ATOM   5459 N NZ  . LYS B 2 146 ? -10.739 -62.257 24.085  1.00 141.30 ? 146  LYS B NZ  1 
ATOM   5460 N N   . PHE B 2 147 ? -6.524  -65.493 27.539  1.00 67.27  ? 147  PHE B N   1 
ATOM   5461 C CA  . PHE B 2 147 ? -6.876  -66.084 28.829  1.00 70.94  ? 147  PHE B CA  1 
ATOM   5462 C C   . PHE B 2 147 ? -7.118  -65.084 29.982  1.00 78.26  ? 147  PHE B C   1 
ATOM   5463 O O   . PHE B 2 147 ? -8.165  -65.141 30.633  1.00 77.96  ? 147  PHE B O   1 
ATOM   5464 C CB  . PHE B 2 147 ? -5.859  -67.155 29.245  1.00 68.31  ? 147  PHE B CB  1 
ATOM   5465 C CG  . PHE B 2 147 ? -6.244  -67.884 30.496  1.00 72.00  ? 147  PHE B CG  1 
ATOM   5466 C CD1 . PHE B 2 147 ? -7.510  -68.427 30.631  1.00 77.62  ? 147  PHE B CD1 1 
ATOM   5467 C CD2 . PHE B 2 147 ? -5.353  -68.019 31.543  1.00 67.89  ? 147  PHE B CD2 1 
ATOM   5468 C CE1 . PHE B 2 147 ? -7.875  -69.089 31.786  1.00 73.21  ? 147  PHE B CE1 1 
ATOM   5469 C CE2 . PHE B 2 147 ? -5.715  -68.684 32.700  1.00 61.63  ? 147  PHE B CE2 1 
ATOM   5470 C CZ  . PHE B 2 147 ? -6.973  -69.211 32.823  1.00 69.33  ? 147  PHE B CZ  1 
ATOM   5471 N N   . VAL B 2 148 ? -6.159  -64.190 30.237  1.00 78.51  ? 148  VAL B N   1 
ATOM   5472 C CA  . VAL B 2 148 ? -6.285  -63.181 31.299  1.00 73.05  ? 148  VAL B CA  1 
ATOM   5473 C C   . VAL B 2 148 ? -7.522  -62.303 31.068  1.00 78.06  ? 148  VAL B C   1 
ATOM   5474 O O   . VAL B 2 148 ? -8.218  -61.921 32.018  1.00 77.77  ? 148  VAL B O   1 
ATOM   5475 C CB  . VAL B 2 148 ? -4.988  -62.297 31.431  1.00 63.37  ? 148  VAL B CB  1 
ATOM   5476 C CG1 . VAL B 2 148 ? -5.201  -61.073 32.351  1.00 57.05  ? 148  VAL B CG1 1 
ATOM   5477 C CG2 . VAL B 2 148 ? -3.804  -63.121 31.938  1.00 61.32  ? 148  VAL B CG2 1 
ATOM   5478 N N   . LYS B 2 149 ? -7.804  -62.003 29.802  1.00 73.27  ? 149  LYS B N   1 
ATOM   5479 C CA  . LYS B 2 149 ? -8.949  -61.165 29.459  1.00 73.41  ? 149  LYS B CA  1 
ATOM   5480 C C   . LYS B 2 149 ? -10.276 -61.864 29.721  1.00 82.73  ? 149  LYS B C   1 
ATOM   5481 O O   . LYS B 2 149 ? -11.216 -61.230 30.178  1.00 91.29  ? 149  LYS B O   1 
ATOM   5482 C CB  . LYS B 2 149 ? -8.865  -60.684 28.006  1.00 84.36  ? 149  LYS B CB  1 
ATOM   5483 C CG  . LYS B 2 149 ? -10.061 -59.856 27.545  1.00 101.54 ? 149  LYS B CG  1 
ATOM   5484 C CD  . LYS B 2 149 ? -9.993  -59.540 26.044  1.00 116.59 ? 149  LYS B CD  1 
ATOM   5485 C CE  . LYS B 2 149 ? -8.906  -58.502 25.708  1.00 122.32 ? 149  LYS B CE  1 
ATOM   5486 N NZ  . LYS B 2 149 ? -7.515  -59.049 25.611  1.00 118.14 ? 149  LYS B NZ  1 
ATOM   5487 N N   . VAL B 2 150 ? -10.350 -63.166 29.435  1.00 92.00  ? 150  VAL B N   1 
ATOM   5488 C CA  . VAL B 2 150 ? -11.564 -63.947 29.698  1.00 92.05  ? 150  VAL B CA  1 
ATOM   5489 C C   . VAL B 2 150 ? -11.771 -64.087 31.185  1.00 79.27  ? 150  VAL B C   1 
ATOM   5490 O O   . VAL B 2 150 ? -12.877 -63.905 31.686  1.00 81.55  ? 150  VAL B O   1 
ATOM   5491 C CB  . VAL B 2 150 ? -11.546 -65.380 29.077  1.00 75.73  ? 150  VAL B CB  1 
ATOM   5492 C CG1 . VAL B 2 150 ? -12.808 -66.119 29.451  1.00 78.28  ? 150  VAL B CG1 1 
ATOM   5493 C CG2 . VAL B 2 150 ? -11.462 -65.319 27.570  1.00 84.17  ? 150  VAL B CG2 1 
ATOM   5494 N N   . MET B 2 151 ? -10.702 -64.414 31.892  1.00 73.92  ? 151  MET B N   1 
ATOM   5495 C CA  . MET B 2 151 ? -10.808 -64.604 33.329  1.00 78.12  ? 151  MET B CA  1 
ATOM   5496 C C   . MET B 2 151 ? -11.151 -63.304 34.024  1.00 84.48  ? 151  MET B C   1 
ATOM   5497 O O   . MET B 2 151 ? -11.723 -63.297 35.107  1.00 91.51  ? 151  MET B O   1 
ATOM   5498 C CB  . MET B 2 151 ? -9.526  -65.201 33.902  1.00 70.80  ? 151  MET B CB  1 
ATOM   5499 C CG  . MET B 2 151 ? -9.279  -66.622 33.416  1.00 79.70  ? 151  MET B CG  1 
ATOM   5500 S SD  . MET B 2 151 ? -10.768 -67.668 33.474  1.00 100.54 ? 151  MET B SD  1 
ATOM   5501 C CE  . MET B 2 151 ? -10.659 -68.310 35.146  1.00 66.65  ? 151  MET B CE  1 
ATOM   5502 N N   . THR B 2 152 ? -10.803 -62.196 33.394  1.00 83.16  ? 152  THR B N   1 
ATOM   5503 C CA  . THR B 2 152 ? -11.080 -60.907 33.987  1.00 87.10  ? 152  THR B CA  1 
ATOM   5504 C C   . THR B 2 152 ? -12.573 -60.676 33.931  1.00 87.82  ? 152  THR B C   1 
ATOM   5505 O O   . THR B 2 152 ? -13.141 -60.037 34.812  1.00 88.56  ? 152  THR B O   1 
ATOM   5506 C CB  . THR B 2 152 ? -10.319 -59.782 33.272  1.00 87.17  ? 152  THR B CB  1 
ATOM   5507 O OG1 . THR B 2 152 ? -8.917  -59.950 33.510  1.00 93.59  ? 152  THR B OG1 1 
ATOM   5508 C CG2 . THR B 2 152 ? -10.750 -58.422 33.795  1.00 80.76  ? 152  THR B CG2 1 
ATOM   5509 N N   . ARG B 2 153 ? -13.207 -61.210 32.893  1.00 89.07  ? 153  ARG B N   1 
ATOM   5510 C CA  . ARG B 2 153 ? -14.657 -61.117 32.777  1.00 91.15  ? 153  ARG B CA  1 
ATOM   5511 C C   . ARG B 2 153 ? -15.279 -61.903 33.924  1.00 92.71  ? 153  ARG B C   1 
ATOM   5512 O O   . ARG B 2 153 ? -16.223 -61.442 34.561  1.00 90.65  ? 153  ARG B O   1 
ATOM   5513 C CB  . ARG B 2 153 ? -15.137 -61.633 31.421  1.00 90.46  ? 153  ARG B CB  1 
ATOM   5514 C CG  . ARG B 2 153 ? -16.644 -61.624 31.254  1.00 107.25 ? 153  ARG B CG  1 
ATOM   5515 C CD  . ARG B 2 153 ? -17.252 -60.299 31.695  1.00 120.08 ? 153  ARG B CD  1 
ATOM   5516 N NE  . ARG B 2 153 ? -18.710 -60.305 31.576  1.00 128.25 ? 153  ARG B NE  1 
ATOM   5517 C CZ  . ARG B 2 153 ? -19.528 -59.521 32.276  1.00 128.53 ? 153  ARG B CZ  1 
ATOM   5518 N NH1 . ARG B 2 153 ? -19.037 -58.660 33.162  1.00 125.86 ? 153  ARG B NH1 1 
ATOM   5519 N NH2 . ARG B 2 153 ? -20.841 -59.602 32.095  1.00 127.50 ? 153  ARG B NH2 1 
ATOM   5520 N N   . TYR B 2 154 ? -14.716 -63.078 34.196  1.00 94.06  ? 154  TYR B N   1 
ATOM   5521 C CA  . TYR B 2 154 ? -15.133 -63.912 35.321  1.00 95.12  ? 154  TYR B CA  1 
ATOM   5522 C C   . TYR B 2 154 ? -14.934 -63.170 36.643  1.00 95.70  ? 154  TYR B C   1 
ATOM   5523 O O   . TYR B 2 154 ? -15.876 -62.979 37.407  1.00 93.66  ? 154  TYR B O   1 
ATOM   5524 C CB  . TYR B 2 154 ? -14.342 -65.222 35.314  1.00 91.47  ? 154  TYR B CB  1 
ATOM   5525 C CG  . TYR B 2 154 ? -14.795 -66.269 36.312  1.00 88.49  ? 154  TYR B CG  1 
ATOM   5526 C CD1 . TYR B 2 154 ? -16.121 -66.675 36.378  1.00 89.13  ? 154  TYR B CD1 1 
ATOM   5527 C CD2 . TYR B 2 154 ? -13.880 -66.882 37.163  1.00 92.84  ? 154  TYR B CD2 1 
ATOM   5528 C CE1 . TYR B 2 154 ? -16.530 -67.652 37.288  1.00 96.12  ? 154  TYR B CE1 1 
ATOM   5529 C CE2 . TYR B 2 154 ? -14.276 -67.858 38.072  1.00 98.45  ? 154  TYR B CE2 1 
ATOM   5530 C CZ  . TYR B 2 154 ? -15.601 -68.241 38.132  1.00 100.06 ? 154  TYR B CZ  1 
ATOM   5531 O OH  . TYR B 2 154 ? -15.990 -69.209 39.039  1.00 94.09  ? 154  TYR B OH  1 
ATOM   5532 N N   . ASN B 2 155 ? -13.703 -62.747 36.906  1.00 98.77  ? 155  ASN B N   1 
ATOM   5533 C CA  . ASN B 2 155 ? -13.396 -61.987 38.112  1.00 94.41  ? 155  ASN B CA  1 
ATOM   5534 C C   . ASN B 2 155 ? -14.371 -60.831 38.317  1.00 96.63  ? 155  ASN B C   1 
ATOM   5535 O O   . ASN B 2 155 ? -14.719 -60.497 39.452  1.00 92.37  ? 155  ASN B O   1 
ATOM   5536 C CB  . ASN B 2 155 ? -11.953 -61.470 38.063  1.00 87.72  ? 155  ASN B CB  1 
ATOM   5537 C CG  . ASN B 2 155 ? -11.571 -60.669 39.295  1.00 87.83  ? 155  ASN B CG  1 
ATOM   5538 O OD1 . ASN B 2 155 ? -11.808 -59.457 39.361  1.00 95.52  ? 155  ASN B OD1 1 
ATOM   5539 N ND2 . ASN B 2 155 ? -10.948 -61.336 40.270  1.00 84.57  ? 155  ASN B ND2 1 
ATOM   5540 N N   . ASP B 2 156 ? -14.820 -60.230 37.218  1.00 99.87  ? 156  ASP B N   1 
ATOM   5541 C CA  . ASP B 2 156 ? -15.701 -59.071 37.301  1.00 104.53 ? 156  ASP B CA  1 
ATOM   5542 C C   . ASP B 2 156 ? -17.125 -59.442 37.689  1.00 116.74 ? 156  ASP B C   1 
ATOM   5543 O O   . ASP B 2 156 ? -17.737 -58.744 38.490  1.00 121.35 ? 156  ASP B O   1 
ATOM   5544 C CB  . ASP B 2 156 ? -15.683 -58.262 36.003  1.00 111.52 ? 156  ASP B CB  1 
ATOM   5545 C CG  . ASP B 2 156 ? -14.643 -57.147 36.023  1.00 125.81 ? 156  ASP B CG  1 
ATOM   5546 O OD1 . ASP B 2 156 ? -14.024 -56.910 37.088  1.00 121.11 ? 156  ASP B OD1 1 
ATOM   5547 O OD2 . ASP B 2 156 ? -14.448 -56.500 34.971  1.00 135.94 ? 156  ASP B OD2 1 
ATOM   5548 N N   . VAL B 2 157 ? -17.642 -60.540 37.136  1.00 118.24 ? 157  VAL B N   1 
ATOM   5549 C CA  . VAL B 2 157 ? -18.995 -61.006 37.465  1.00 110.30 ? 157  VAL B CA  1 
ATOM   5550 C C   . VAL B 2 157 ? -19.081 -61.588 38.881  1.00 111.27 ? 157  VAL B C   1 
ATOM   5551 O O   . VAL B 2 157 ? -20.124 -61.498 39.528  1.00 114.76 ? 157  VAL B O   1 
ATOM   5552 C CB  . VAL B 2 157 ? -19.546 -62.011 36.414  1.00 108.04 ? 157  VAL B CB  1 
ATOM   5553 C CG1 . VAL B 2 157 ? -18.568 -63.137 36.186  1.00 114.19 ? 157  VAL B CG1 1 
ATOM   5554 C CG2 . VAL B 2 157 ? -20.903 -62.564 36.840  1.00 110.49 ? 157  VAL B CG2 1 
ATOM   5555 N N   . GLN B 2 158 ? -17.984 -62.167 39.367  1.00 109.88 ? 158  GLN B N   1 
ATOM   5556 C CA  . GLN B 2 158 ? -17.929 -62.662 40.747  1.00 107.85 ? 158  GLN B CA  1 
ATOM   5557 C C   . GLN B 2 158 ? -17.979 -61.530 41.775  1.00 108.61 ? 158  GLN B C   1 
ATOM   5558 O O   . GLN B 2 158 ? -18.883 -61.475 42.606  1.00 118.88 ? 158  GLN B O   1 
ATOM   5559 C CB  . GLN B 2 158 ? -16.696 -63.545 40.978  1.00 99.58  ? 158  GLN B CB  1 
ATOM   5560 C CG  . GLN B 2 158 ? -16.733 -64.887 40.237  1.00 100.71 ? 158  GLN B CG  1 
ATOM   5561 C CD  . GLN B 2 158 ? -17.867 -65.813 40.697  1.00 99.33  ? 158  GLN B CD  1 
ATOM   5562 O OE1 . GLN B 2 158 ? -17.646 -66.758 41.454  1.00 99.10  ? 158  GLN B OE1 1 
ATOM   5563 N NE2 . GLN B 2 158 ? -19.077 -65.547 40.225  1.00 93.17  ? 158  GLN B NE2 1 
ATOM   5564 N N   . ALA B 2 159 ? -17.010 -60.628 41.720  1.00 106.85 ? 159  ALA B N   1 
ATOM   5565 C CA  . ALA B 2 159 ? -17.009 -59.470 42.608  1.00 108.65 ? 159  ALA B CA  1 
ATOM   5566 C C   . ALA B 2 159 ? -18.250 -58.595 42.422  1.00 114.35 ? 159  ALA B C   1 
ATOM   5567 O O   . ALA B 2 159 ? -18.776 -58.051 43.388  1.00 112.93 ? 159  ALA B O   1 
ATOM   5568 C CB  . ALA B 2 159 ? -15.754 -58.655 42.404  1.00 100.71 ? 159  ALA B CB  1 
ATOM   5569 N N   . GLU B 2 160 ? -18.704 -58.461 41.178  1.00 125.27 ? 160  GLU B N   1 
ATOM   5570 C CA  . GLU B 2 160 ? -19.917 -57.705 40.861  1.00 136.06 ? 160  GLU B CA  1 
ATOM   5571 C C   . GLU B 2 160 ? -21.112 -58.250 41.627  1.00 137.86 ? 160  GLU B C   1 
ATOM   5572 O O   . GLU B 2 160 ? -21.898 -57.487 42.191  1.00 138.41 ? 160  GLU B O   1 
ATOM   5573 C CB  . GLU B 2 160 ? -20.198 -57.758 39.355  1.00 148.99 ? 160  GLU B CB  1 
ATOM   5574 C CG  . GLU B 2 160 ? -21.510 -57.125 38.899  1.00 161.59 ? 160  GLU B CG  1 
ATOM   5575 C CD  . GLU B 2 160 ? -21.649 -57.097 37.373  1.00 174.58 ? 160  GLU B CD  1 
ATOM   5576 O OE1 . GLU B 2 160 ? -22.794 -57.138 36.875  1.00 177.62 ? 160  GLU B OE1 1 
ATOM   5577 O OE2 . GLU B 2 160 ? -20.614 -57.037 36.669  1.00 178.14 ? 160  GLU B OE2 1 
ATOM   5578 N N   . ASN B 2 161 ? -21.239 -59.576 41.640  1.00 137.27 ? 161  ASN B N   1 
ATOM   5579 C CA  . ASN B 2 161 ? -22.335 -60.243 42.338  1.00 136.49 ? 161  ASN B CA  1 
ATOM   5580 C C   . ASN B 2 161 ? -22.127 -60.311 43.852  1.00 134.85 ? 161  ASN B C   1 
ATOM   5581 O O   . ASN B 2 161 ? -23.091 -60.236 44.608  1.00 138.20 ? 161  ASN B O   1 
ATOM   5582 C CB  . ASN B 2 161 ? -22.597 -61.645 41.760  1.00 131.84 ? 161  ASN B CB  1 
ATOM   5583 C CG  . ASN B 2 161 ? -23.642 -61.640 40.643  1.00 127.20 ? 161  ASN B CG  1 
ATOM   5584 O OD1 . ASN B 2 161 ? -23.389 -62.116 39.535  1.00 131.73 ? 161  ASN B OD1 1 
ATOM   5585 N ND2 . ASN B 2 161 ? -24.820 -61.104 40.935  1.00 117.89 ? 161  ASN B ND2 1 
ATOM   5586 N N   . LYS B 2 162 ? -20.876 -60.441 44.292  1.00 125.18 ? 162  LYS B N   1 
ATOM   5587 C CA  . LYS B 2 162 ? -20.580 -60.526 45.722  1.00 121.67 ? 162  LYS B CA  1 
ATOM   5588 C C   . LYS B 2 162 ? -20.856 -59.210 46.447  1.00 126.69 ? 162  LYS B C   1 
ATOM   5589 O O   . LYS B 2 162 ? -21.137 -59.195 47.648  1.00 122.21 ? 162  LYS B O   1 
ATOM   5590 C CB  . LYS B 2 162 ? -19.132 -60.951 45.958  1.00 117.56 ? 162  LYS B CB  1 
ATOM   5591 C CG  . LYS B 2 162 ? -18.715 -60.906 47.420  1.00 114.07 ? 162  LYS B CG  1 
ATOM   5592 C CD  . LYS B 2 162 ? -17.236 -60.623 47.541  1.00 119.23 ? 162  LYS B CD  1 
ATOM   5593 C CE  . LYS B 2 162 ? -16.906 -59.914 48.842  1.00 125.44 ? 162  LYS B CE  1 
ATOM   5594 N NZ  . LYS B 2 162 ? -15.617 -59.165 48.727  1.00 128.63 ? 162  LYS B NZ  1 
ATOM   5595 N N   . ARG B 2 163 ? -20.764 -58.107 45.711  1.00 136.70 ? 163  ARG B N   1 
ATOM   5596 C CA  . ARG B 2 163 ? -21.036 -56.787 46.267  1.00 142.46 ? 163  ARG B CA  1 
ATOM   5597 C C   . ARG B 2 163 ? -22.535 -56.605 46.507  1.00 148.85 ? 163  ARG B C   1 
ATOM   5598 O O   . ARG B 2 163 ? -22.942 -56.061 47.533  1.00 152.04 ? 163  ARG B O   1 
ATOM   5599 C CB  . ARG B 2 163 ? -20.485 -55.693 45.345  1.00 141.63 ? 163  ARG B CB  1 
ATOM   5600 C CG  . ARG B 2 163 ? -20.842 -54.268 45.748  1.00 145.19 ? 163  ARG B CG  1 
ATOM   5601 C CD  . ARG B 2 163 ? -19.909 -53.243 45.093  1.00 151.70 ? 163  ARG B CD  1 
ATOM   5602 N NE  . ARG B 2 163 ? -19.470 -53.645 43.756  1.00 152.25 ? 163  ARG B NE  1 
ATOM   5603 C CZ  . ARG B 2 163 ? -20.229 -53.593 42.665  1.00 152.12 ? 163  ARG B CZ  1 
ATOM   5604 N NH1 . ARG B 2 163 ? -21.485 -53.167 42.741  1.00 156.18 ? 163  ARG B NH1 1 
ATOM   5605 N NH2 . ARG B 2 163 ? -19.736 -53.980 41.497  1.00 144.35 ? 163  ARG B NH2 1 
ATOM   5606 N N   . ARG B 2 164 ? -23.350 -57.073 45.564  1.00 148.98 ? 164  ARG B N   1 
ATOM   5607 C CA  . ARG B 2 164 ? -24.803 -57.002 45.704  1.00 153.14 ? 164  ARG B CA  1 
ATOM   5608 C C   . ARG B 2 164 ? -25.377 -58.234 46.412  1.00 158.83 ? 164  ARG B C   1 
ATOM   5609 O O   . ARG B 2 164 ? -26.542 -58.239 46.811  1.00 161.07 ? 164  ARG B O   1 
ATOM   5610 C CB  . ARG B 2 164 ? -25.482 -56.800 44.344  1.00 150.57 ? 164  ARG B CB  1 
ATOM   5611 C CG  . ARG B 2 164 ? -25.210 -57.900 43.332  1.00 149.87 ? 164  ARG B CG  1 
ATOM   5612 C CD  . ARG B 2 164 ? -26.306 -57.968 42.274  1.00 152.06 ? 164  ARG B CD  1 
ATOM   5613 N NE  . ARG B 2 164 ? -26.510 -56.697 41.581  1.00 154.60 ? 164  ARG B NE  1 
ATOM   5614 C CZ  . ARG B 2 164 ? -26.092 -56.435 40.344  1.00 150.35 ? 164  ARG B CZ  1 
ATOM   5615 N NH1 . ARG B 2 164 ? -26.330 -55.248 39.801  1.00 143.72 ? 164  ARG B NH1 1 
ATOM   5616 N NH2 . ARG B 2 164 ? -25.441 -57.358 39.648  1.00 148.06 ? 164  ARG B NH2 1 
ATOM   5617 N N   . TYR B 2 165 ? -24.554 -59.270 46.564  1.00 156.65 ? 165  TYR B N   1 
ATOM   5618 C CA  . TYR B 2 165 ? -24.927 -60.475 47.306  1.00 147.67 ? 165  TYR B CA  1 
ATOM   5619 C C   . TYR B 2 165 ? -24.728 -60.218 48.787  1.00 136.97 ? 165  TYR B C   1 
ATOM   5620 O O   . TYR B 2 165 ? -24.766 -61.135 49.602  1.00 121.66 ? 165  TYR B O   1 
ATOM   5621 C CB  . TYR B 2 165 ? -24.048 -61.650 46.890  1.00 148.87 ? 165  TYR B CB  1 
ATOM   5622 C CG  . TYR B 2 165 ? -24.794 -62.874 46.417  1.00 151.30 ? 165  TYR B CG  1 
ATOM   5623 C CD1 . TYR B 2 165 ? -25.425 -62.893 45.180  1.00 152.44 ? 165  TYR B CD1 1 
ATOM   5624 C CD2 . TYR B 2 165 ? -24.837 -64.021 47.192  1.00 156.23 ? 165  TYR B CD2 1 
ATOM   5625 C CE1 . TYR B 2 165 ? -26.094 -64.014 44.736  1.00 159.44 ? 165  TYR B CE1 1 
ATOM   5626 C CE2 . TYR B 2 165 ? -25.501 -65.146 46.760  1.00 166.21 ? 165  TYR B CE2 1 
ATOM   5627 C CZ  . TYR B 2 165 ? -26.129 -65.139 45.530  1.00 170.93 ? 165  TYR B CZ  1 
ATOM   5628 O OH  . TYR B 2 165 ? -26.797 -66.265 45.098  1.00 181.34 ? 165  TYR B OH  1 
ATOM   5629 N N   . GLY B 2 166 ? -24.481 -58.958 49.117  1.00 142.70 ? 166  GLY B N   1 
ATOM   5630 C CA  . GLY B 2 166 ? -24.359 -58.529 50.492  1.00 144.28 ? 166  GLY B CA  1 
ATOM   5631 C C   . GLY B 2 166 ? -25.242 -57.321 50.700  1.00 149.31 ? 166  GLY B C   1 
ATOM   5632 O O   . GLY B 2 166 ? -25.799 -57.133 51.775  1.00 153.70 ? 166  GLY B O   1 
ATOM   5633 N N   . GLU B 2 167 ? -25.376 -56.507 49.656  1.00 155.98 ? 167  GLU B N   1 
ATOM   5634 C CA  . GLU B 2 167 ? -26.200 -55.302 49.712  1.00 167.91 ? 167  GLU B CA  1 
ATOM   5635 C C   . GLU B 2 167 ? -27.687 -55.632 49.660  1.00 176.71 ? 167  GLU B C   1 
ATOM   5636 O O   . GLU B 2 167 ? -28.401 -55.497 50.654  1.00 175.84 ? 167  GLU B O   1 
ATOM   5637 C CB  . GLU B 2 167 ? -25.853 -54.351 48.563  1.00 170.89 ? 167  GLU B CB  1 
ATOM   5638 C CG  . GLU B 2 167 ? -24.516 -53.638 48.709  1.00 176.60 ? 167  GLU B CG  1 
ATOM   5639 C CD  . GLU B 2 167 ? -24.213 -52.720 47.533  1.00 179.06 ? 167  GLU B CD  1 
ATOM   5640 O OE1 . GLU B 2 167 ? -25.000 -52.716 46.561  1.00 180.55 ? 167  GLU B OE1 1 
ATOM   5641 O OE2 . GLU B 2 167 ? -23.187 -52.004 47.581  1.00 176.25 ? 167  GLU B OE2 1 
ATOM   5642 N N   . ASN B 2 168 ? -28.149 -56.060 48.489  1.00 194.79 ? 168  ASN B N   1 
ATOM   5643 C CA  . ASN B 2 168 ? -29.567 -56.336 48.276  1.00 196.87 ? 168  ASN B CA  1 
ATOM   5644 C C   . ASN B 2 168 ? -29.988 -57.757 48.664  1.00 191.39 ? 168  ASN B C   1 
ATOM   5645 O O   . ASN B 2 168 ? -30.993 -58.266 48.161  1.00 193.44 ? 168  ASN B O   1 
ATOM   5646 C CB  . ASN B 2 168 ? -29.965 -56.048 46.820  1.00 199.84 ? 168  ASN B CB  1 
ATOM   5647 C CG  . ASN B 2 168 ? -29.912 -54.565 46.474  1.00 197.24 ? 168  ASN B CG  1 
ATOM   5648 O OD1 . ASN B 2 168 ? -29.694 -53.716 47.339  1.00 196.45 ? 168  ASN B OD1 1 
ATOM   5649 N ND2 . ASN B 2 168 ? -30.118 -54.250 45.200  1.00 194.68 ? 168  ASN B ND2 1 
ATOM   5650 N N   . VAL B 2 169 ? -29.223 -58.396 49.548  1.00 182.39 ? 169  VAL B N   1 
ATOM   5651 C CA  . VAL B 2 169 ? -29.600 -59.718 50.054  1.00 181.92 ? 169  VAL B CA  1 
ATOM   5652 C C   . VAL B 2 169 ? -29.218 -59.956 51.518  1.00 180.89 ? 169  VAL B C   1 
ATOM   5653 O O   . VAL B 2 169 ? -30.045 -60.407 52.307  1.00 186.11 ? 169  VAL B O   1 
ATOM   5654 C CB  . VAL B 2 169 ? -29.051 -60.873 49.182  1.00 178.36 ? 169  VAL B CB  1 
ATOM   5655 C CG1 . VAL B 2 169 ? -29.194 -62.198 49.918  1.00 174.02 ? 169  VAL B CG1 1 
ATOM   5656 C CG2 . VAL B 2 169 ? -29.775 -60.930 47.841  1.00 177.04 ? 169  VAL B CG2 1 
ATOM   5657 N N   . ALA B 2 170 ? -27.974 -59.665 51.883  1.00 172.58 ? 170  ALA B N   1 
ATOM   5658 C CA  . ALA B 2 170 ? -27.529 -59.891 53.257  1.00 166.55 ? 170  ALA B CA  1 
ATOM   5659 C C   . ALA B 2 170 ? -27.906 -58.730 54.170  1.00 168.06 ? 170  ALA B C   1 
ATOM   5660 O O   . ALA B 2 170 ? -28.479 -58.934 55.237  1.00 168.02 ? 170  ALA B O   1 
ATOM   5661 C CB  . ALA B 2 170 ? -26.034 -60.142 53.305  1.00 163.60 ? 170  ALA B CB  1 
ATOM   5662 N N   . ARG B 2 171 ? -27.580 -57.513 53.748  1.00 173.26 ? 171  ARG B N   1 
ATOM   5663 C CA  . ARG B 2 171 ? -27.906 -56.322 54.526  1.00 179.10 ? 171  ARG B CA  1 
ATOM   5664 C C   . ARG B 2 171 ? -29.410 -56.063 54.540  1.00 183.98 ? 171  ARG B C   1 
ATOM   5665 O O   . ARG B 2 171 ? -30.002 -55.895 55.605  1.00 187.43 ? 171  ARG B O   1 
ATOM   5666 C CB  . ARG B 2 171 ? -27.164 -55.091 53.990  1.00 181.94 ? 171  ARG B CB  1 
ATOM   5667 C CG  . ARG B 2 171 ? -25.655 -55.095 54.223  1.00 180.27 ? 171  ARG B CG  1 
ATOM   5668 C CD  . ARG B 2 171 ? -24.998 -53.872 53.588  1.00 178.44 ? 171  ARG B CD  1 
ATOM   5669 N NE  . ARG B 2 171 ? -23.543 -53.893 53.712  1.00 178.35 ? 171  ARG B NE  1 
ATOM   5670 C CZ  . ARG B 2 171 ? -22.740 -52.928 53.274  1.00 178.06 ? 171  ARG B CZ  1 
ATOM   5671 N NH1 . ARG B 2 171 ? -23.249 -51.855 52.680  1.00 177.81 ? 171  ARG B NH1 1 
ATOM   5672 N NH2 . ARG B 2 171 ? -21.427 -53.034 53.430  1.00 175.82 ? 171  ARG B NH2 1 
ATOM   5673 N N   . GLN B 2 172 ? -30.026 -56.033 53.360  1.00 186.24 ? 172  GLN B N   1 
ATOM   5674 C CA  . GLN B 2 172 ? -31.466 -55.796 53.256  1.00 188.16 ? 172  GLN B CA  1 
ATOM   5675 C C   . GLN B 2 172 ? -32.266 -56.889 53.964  1.00 186.65 ? 172  GLN B C   1 
ATOM   5676 O O   . GLN B 2 172 ? -33.491 -56.810 54.067  1.00 182.77 ? 172  GLN B O   1 
ATOM   5677 C CB  . GLN B 2 172 ? -31.910 -55.666 51.792  1.00 192.21 ? 172  GLN B CB  1 
ATOM   5678 C CG  . GLN B 2 172 ? -31.466 -54.372 51.108  1.00 192.48 ? 172  GLN B CG  1 
ATOM   5679 C CD  . GLN B 2 172 ? -32.159 -54.139 49.771  1.00 192.50 ? 172  GLN B CD  1 
ATOM   5680 O OE1 . GLN B 2 172 ? -33.032 -54.910 49.366  1.00 193.45 ? 172  GLN B OE1 1 
ATOM   5681 N NE2 . GLN B 2 172 ? -31.773 -53.068 49.083  1.00 188.49 ? 172  GLN B NE2 1 
ATOM   5682 N N   . CYS B 2 173 ? -31.564 -57.909 54.446  1.00 188.54 ? 173  CYS B N   1 
ATOM   5683 C CA  . CYS B 2 173 ? -32.183 -58.940 55.268  1.00 187.95 ? 173  CYS B CA  1 
ATOM   5684 C C   . CYS B 2 173 ? -32.091 -58.525 56.731  1.00 182.03 ? 173  CYS B C   1 
ATOM   5685 O O   . CYS B 2 173 ? -31.837 -59.349 57.610  1.00 176.02 ? 173  CYS B O   1 
ATOM   5686 C CB  . CYS B 2 173 ? -31.504 -60.297 55.053  1.00 189.79 ? 173  CYS B CB  1 
ATOM   5687 S SG  . CYS B 2 173 ? -32.622 -61.649 54.576  1.00 154.99 ? 173  CYS B SG  1 
ATOM   5688 N N   . ARG B 2 174 ? -32.283 -57.232 56.977  1.00 181.45 ? 174  ARG B N   1 
ATOM   5689 C CA  . ARG B 2 174 ? -32.350 -56.707 58.334  1.00 181.32 ? 174  ARG B CA  1 
ATOM   5690 C C   . ARG B 2 174 ? -33.809 -56.511 58.734  1.00 188.64 ? 174  ARG B C   1 
ATOM   5691 O O   . ARG B 2 174 ? -34.138 -55.622 59.519  1.00 192.31 ? 174  ARG B O   1 
ATOM   5692 C CB  . ARG B 2 174 ? -31.573 -55.394 58.458  1.00 176.27 ? 174  ARG B CB  1 
ATOM   5693 C CG  . ARG B 2 174 ? -32.135 -54.250 57.631  1.00 175.62 ? 174  ARG B CG  1 
ATOM   5694 C CD  . ARG B 2 174 ? -31.183 -53.058 57.618  1.00 172.45 ? 174  ARG B CD  1 
ATOM   5695 N NE  . ARG B 2 174 ? -31.668 -51.985 56.751  1.00 169.16 ? 174  ARG B NE  1 
ATOM   5696 C CZ  . ARG B 2 174 ? -30.977 -50.889 56.456  1.00 162.26 ? 174  ARG B CZ  1 
ATOM   5697 N NH1 . ARG B 2 174 ? -29.760 -50.720 56.955  1.00 163.00 ? 174  ARG B NH1 1 
ATOM   5698 N NH2 . ARG B 2 174 ? -31.500 -49.965 55.658  1.00 154.72 ? 174  ARG B NH2 1 
ATOM   5699 N N   . VAL B 2 175 ? -34.680 -57.350 58.179  1.00 190.70 ? 175  VAL B N   1 
ATOM   5700 C CA  . VAL B 2 175 ? -36.088 -57.364 58.553  1.00 191.49 ? 175  VAL B CA  1 
ATOM   5701 C C   . VAL B 2 175 ? -36.229 -58.013 59.932  1.00 195.92 ? 175  VAL B C   1 
ATOM   5702 O O   . VAL B 2 175 ? -37.290 -58.527 60.295  1.00 194.90 ? 175  VAL B O   1 
ATOM   5703 C CB  . VAL B 2 175 ? -36.937 -58.127 57.511  1.00 187.13 ? 175  VAL B CB  1 
ATOM   5704 C CG1 . VAL B 2 175 ? -36.670 -59.625 57.596  1.00 185.87 ? 175  VAL B CG1 1 
ATOM   5705 C CG2 . VAL B 2 175 ? -38.417 -57.828 57.699  1.00 186.15 ? 175  VAL B CG2 1 
ATOM   5706 N N   . VAL B 2 176 ? -35.135 -57.982 60.693  1.00 196.35 ? 176  VAL B N   1 
ATOM   5707 C CA  . VAL B 2 176 ? -35.087 -58.542 62.040  1.00 191.97 ? 176  VAL B CA  1 
ATOM   5708 C C   . VAL B 2 176 ? -34.578 -57.502 63.045  1.00 192.50 ? 176  VAL B C   1 
ATOM   5709 O O   . VAL B 2 176 ? -35.047 -57.439 64.184  1.00 194.97 ? 176  VAL B O   1 
ATOM   5710 C CB  . VAL B 2 176 ? -34.196 -59.804 62.096  1.00 180.87 ? 176  VAL B CB  1 
ATOM   5711 C CG1 . VAL B 2 176 ? -34.033 -60.281 63.531  1.00 181.72 ? 176  VAL B CG1 1 
ATOM   5712 C CG2 . VAL B 2 176 ? -34.777 -60.908 61.218  1.00 170.73 ? 176  VAL B CG2 1 
ATOM   5713 N N   . GLU B 2 177 ? -33.617 -56.689 62.616  1.00 188.75 ? 177  GLU B N   1 
ATOM   5714 C CA  . GLU B 2 177 ? -33.095 -55.609 63.446  1.00 188.65 ? 177  GLU B CA  1 
ATOM   5715 C C   . GLU B 2 177 ? -33.339 -54.255 62.788  1.00 193.53 ? 177  GLU B C   1 
ATOM   5716 O O   . GLU B 2 177 ? -33.093 -54.085 61.594  1.00 195.34 ? 177  GLU B O   1 
ATOM   5717 C CB  . GLU B 2 177 ? -31.597 -55.791 63.704  1.00 186.26 ? 177  GLU B CB  1 
ATOM   5718 C CG  . GLU B 2 177 ? -31.243 -56.959 64.611  1.00 181.91 ? 177  GLU B CG  1 
ATOM   5719 C CD  . GLU B 2 177 ? -29.765 -56.995 64.955  1.00 177.33 ? 177  GLU B CD  1 
ATOM   5720 O OE1 . GLU B 2 177 ? -29.004 -56.161 64.418  1.00 174.39 ? 177  GLU B OE1 1 
ATOM   5721 O OE2 . GLU B 2 177 ? -29.364 -57.856 65.766  1.00 175.86 ? 177  GLU B OE2 1 
ATOM   5722 N N   . PRO B 2 178 ? -33.826 -53.284 63.572  1.00 196.29 ? 178  PRO B N   1 
ATOM   5723 C CA  . PRO B 2 178 ? -34.074 -51.919 63.089  1.00 199.89 ? 178  PRO B CA  1 
ATOM   5724 C C   . PRO B 2 178 ? -32.781 -51.140 62.830  1.00 202.66 ? 178  PRO B C   1 
ATOM   5725 O O   . PRO B 2 178 ? -32.842 -49.951 62.508  1.00 200.14 ? 178  PRO B O   1 
ATOM   5726 C CB  . PRO B 2 178 ? -34.854 -51.272 64.243  1.00 198.31 ? 178  PRO B CB  1 
ATOM   5727 C CG  . PRO B 2 178 ? -35.324 -52.414 65.106  1.00 194.61 ? 178  PRO B CG  1 
ATOM   5728 C CD  . PRO B 2 178 ? -34.285 -53.473 64.958  1.00 193.61 ? 178  PRO B CD  1 
ATOM   5729 N N   . SER B 2 179 ? -31.635 -51.806 62.966  1.00 207.58 ? 179  SER B N   1 
ATOM   5730 C CA  . SER B 2 179 ? -30.327 -51.163 62.807  1.00 210.36 ? 179  SER B CA  1 
ATOM   5731 C C   . SER B 2 179 ? -30.207 -50.353 61.512  1.00 219.13 ? 179  SER B C   1 
ATOM   5732 O O   . SER B 2 179 ? -30.455 -50.871 60.421  1.00 220.98 ? 179  SER B O   1 
ATOM   5733 C CB  . SER B 2 179 ? -29.204 -52.204 62.896  1.00 203.95 ? 179  SER B CB  1 
ATOM   5734 O OG  . SER B 2 179 ? -29.417 -53.276 61.993  1.00 200.50 ? 179  SER B OG  1 
ATOM   5735 N N   . LEU B 2 180 ? -29.817 -49.085 61.645  1.00 224.39 ? 180  LEU B N   1 
ATOM   5736 C CA  . LEU B 2 180 ? -29.727 -48.163 60.508  1.00 226.97 ? 180  LEU B CA  1 
ATOM   5737 C C   . LEU B 2 180 ? -28.531 -48.435 59.590  1.00 234.97 ? 180  LEU B C   1 
ATOM   5738 O O   . LEU B 2 180 ? -28.381 -49.537 59.060  1.00 238.37 ? 180  LEU B O   1 
ATOM   5739 C CB  . LEU B 2 180 ? -29.695 -46.703 60.983  1.00 218.63 ? 180  LEU B CB  1 
ATOM   5740 C CG  . LEU B 2 180 ? -30.928 -46.139 61.697  1.00 211.89 ? 180  LEU B CG  1 
ATOM   5741 C CD1 . LEU B 2 180 ? -30.716 -44.670 62.033  1.00 207.28 ? 180  LEU B CD1 1 
ATOM   5742 C CD2 . LEU B 2 180 ? -32.182 -46.321 60.855  1.00 211.05 ? 180  LEU B CD2 1 
ATOM   5743 N N   . SER B 2 181 ? -27.686 -47.423 59.406  1.00 238.36 ? 181  SER B N   1 
ATOM   5744 C CA  . SER B 2 181 ? -26.589 -47.501 58.441  1.00 242.36 ? 181  SER B CA  1 
ATOM   5745 C C   . SER B 2 181 ? -25.331 -48.186 58.980  1.00 246.12 ? 181  SER B C   1 
ATOM   5746 O O   . SER B 2 181 ? -24.752 -49.042 58.310  1.00 247.67 ? 181  SER B O   1 
ATOM   5747 C CB  . SER B 2 181 ? -26.237 -46.105 57.912  1.00 241.89 ? 181  SER B CB  1 
ATOM   5748 O OG  . SER B 2 181 ? -25.745 -45.269 58.945  1.00 239.78 ? 181  SER B OG  1 
ATOM   5749 N N   . ASP B 2 182 ? -24.912 -47.808 60.184  1.00 246.74 ? 182  ASP B N   1 
ATOM   5750 C CA  . ASP B 2 182 ? -23.658 -48.308 60.749  1.00 244.97 ? 182  ASP B CA  1 
ATOM   5751 C C   . ASP B 2 182 ? -23.794 -49.661 61.459  1.00 244.64 ? 182  ASP B C   1 
ATOM   5752 O O   . ASP B 2 182 ? -22.914 -50.513 61.347  1.00 244.08 ? 182  ASP B O   1 
ATOM   5753 C CB  . ASP B 2 182 ? -23.033 -47.268 61.687  1.00 241.30 ? 182  ASP B CB  1 
ATOM   5754 C CG  . ASP B 2 182 ? -22.612 -46.000 60.959  1.00 238.44 ? 182  ASP B CG  1 
ATOM   5755 O OD1 . ASP B 2 182 ? -22.671 -45.976 59.711  1.00 237.95 ? 182  ASP B OD1 1 
ATOM   5756 O OD2 . ASP B 2 182 ? -22.221 -45.026 61.636  1.00 237.06 ? 182  ASP B OD2 1 
ATOM   5757 N N   . ASP B 2 183 ? -24.893 -49.857 62.183  1.00 244.48 ? 183  ASP B N   1 
ATOM   5758 C CA  . ASP B 2 183 ? -25.111 -51.103 62.921  1.00 242.41 ? 183  ASP B CA  1 
ATOM   5759 C C   . ASP B 2 183 ? -25.509 -52.274 62.018  1.00 238.00 ? 183  ASP B C   1 
ATOM   5760 O O   . ASP B 2 183 ? -25.747 -53.384 62.497  1.00 237.21 ? 183  ASP B O   1 
ATOM   5761 C CB  . ASP B 2 183 ? -26.154 -50.909 64.028  1.00 243.08 ? 183  ASP B CB  1 
ATOM   5762 C CG  . ASP B 2 183 ? -25.608 -50.139 65.217  1.00 243.09 ? 183  ASP B CG  1 
ATOM   5763 O OD1 . ASP B 2 183 ? -24.414 -49.771 65.195  1.00 244.59 ? 183  ASP B OD1 1 
ATOM   5764 O OD2 . ASP B 2 183 ? -26.373 -49.906 66.176  1.00 240.86 ? 183  ASP B OD2 1 
ATOM   5765 N N   . ALA B 2 184 ? -25.581 -52.019 60.716  1.00 233.82 ? 184  ALA B N   1 
ATOM   5766 C CA  . ALA B 2 184 ? -25.881 -53.063 59.742  1.00 229.48 ? 184  ALA B CA  1 
ATOM   5767 C C   . ALA B 2 184 ? -24.671 -53.302 58.845  1.00 226.94 ? 184  ALA B C   1 
ATOM   5768 O O   . ALA B 2 184 ? -24.588 -54.318 58.155  1.00 226.90 ? 184  ALA B O   1 
ATOM   5769 C CB  . ALA B 2 184 ? -27.099 -52.687 58.910  1.00 228.31 ? 184  ALA B CB  1 
ATOM   5770 N N   . ILE B 2 185 ? -23.741 -52.349 58.861  1.00 223.65 ? 185  ILE B N   1 
ATOM   5771 C CA  . ILE B 2 185 ? -22.488 -52.464 58.121  1.00 220.00 ? 185  ILE B CA  1 
ATOM   5772 C C   . ILE B 2 185 ? -21.364 -52.890 59.063  1.00 214.70 ? 185  ILE B C   1 
ATOM   5773 O O   . ILE B 2 185 ? -20.414 -53.561 58.655  1.00 215.61 ? 185  ILE B O   1 
ATOM   5774 C CB  . ILE B 2 185 ? -22.099 -51.127 57.437  1.00 210.51 ? 185  ILE B CB  1 
ATOM   5775 C CG1 . ILE B 2 185 ? -23.148 -50.720 56.399  1.00 210.35 ? 185  ILE B CG1 1 
ATOM   5776 C CG2 . ILE B 2 185 ? -20.727 -51.233 56.782  1.00 208.89 ? 185  ILE B CG2 1 
ATOM   5777 C CD1 . ILE B 2 185 ? -22.837 -49.409 55.699  1.00 208.13 ? 185  ILE B CD1 1 
ATOM   5778 N N   . GLN B 2 186 ? -21.480 -52.500 60.329  1.00 205.93 ? 186  GLN B N   1 
ATOM   5779 C CA  . GLN B 2 186 ? -20.467 -52.824 61.325  1.00 197.76 ? 186  GLN B CA  1 
ATOM   5780 C C   . GLN B 2 186 ? -20.705 -54.217 61.890  1.00 198.46 ? 186  GLN B C   1 
ATOM   5781 O O   . GLN B 2 186 ? -19.840 -54.778 62.562  1.00 198.66 ? 186  GLN B O   1 
ATOM   5782 C CB  . GLN B 2 186 ? -20.476 -51.796 62.458  1.00 189.46 ? 186  GLN B CB  1 
ATOM   5783 C CG  . GLN B 2 186 ? -19.114 -51.540 63.086  1.00 182.42 ? 186  GLN B CG  1 
ATOM   5784 C CD  . GLN B 2 186 ? -18.255 -50.597 62.258  1.00 174.56 ? 186  GLN B CD  1 
ATOM   5785 O OE1 . GLN B 2 186 ? -18.612 -49.437 62.045  1.00 168.19 ? 186  GLN B OE1 1 
ATOM   5786 N NE2 . GLN B 2 186 ? -17.113 -51.091 61.795  1.00 172.13 ? 186  GLN B NE2 1 
ATOM   5787 N N   . LYS B 2 187 ? -21.882 -54.772 61.614  1.00 200.26 ? 187  LYS B N   1 
ATOM   5788 C CA  . LYS B 2 187 ? -22.245 -56.092 62.124  1.00 202.73 ? 187  LYS B CA  1 
ATOM   5789 C C   . LYS B 2 187 ? -22.284 -57.181 61.039  1.00 206.41 ? 187  LYS B C   1 
ATOM   5790 O O   . LYS B 2 187 ? -21.713 -58.259 61.215  1.00 209.25 ? 187  LYS B O   1 
ATOM   5791 C CB  . LYS B 2 187 ? -23.576 -56.033 62.887  1.00 199.34 ? 187  LYS B CB  1 
ATOM   5792 C CG  . LYS B 2 187 ? -23.516 -55.261 64.208  1.00 193.70 ? 187  LYS B CG  1 
ATOM   5793 C CD  . LYS B 2 187 ? -24.829 -55.375 64.977  1.00 188.44 ? 187  LYS B CD  1 
ATOM   5794 C CE  . LYS B 2 187 ? -24.775 -54.641 66.310  1.00 181.05 ? 187  LYS B CE  1 
ATOM   5795 N NZ  . LYS B 2 187 ? -26.043 -54.810 67.076  1.00 176.16 ? 187  LYS B NZ  1 
ATOM   5796 N N   . VAL B 2 188 ? -22.948 -56.901 59.921  1.00 202.00 ? 188  VAL B N   1 
ATOM   5797 C CA  . VAL B 2 188 ? -23.071 -57.888 58.848  1.00 193.70 ? 188  VAL B CA  1 
ATOM   5798 C C   . VAL B 2 188 ? -21.716 -58.258 58.225  1.00 190.53 ? 188  VAL B C   1 
ATOM   5799 O O   . VAL B 2 188 ? -21.504 -59.407 57.834  1.00 188.82 ? 188  VAL B O   1 
ATOM   5800 C CB  . VAL B 2 188 ? -24.060 -57.423 57.753  1.00 188.22 ? 188  VAL B CB  1 
ATOM   5801 C CG1 . VAL B 2 188 ? -24.133 -58.443 56.629  1.00 188.83 ? 188  VAL B CG1 1 
ATOM   5802 C CG2 . VAL B 2 188 ? -25.441 -57.189 58.350  1.00 181.68 ? 188  VAL B CG2 1 
ATOM   5803 N N   . ILE B 2 189 ? -20.804 -57.291 58.144  1.00 190.98 ? 189  ILE B N   1 
ATOM   5804 C CA  . ILE B 2 189 ? -19.474 -57.526 57.572  1.00 196.23 ? 189  ILE B CA  1 
ATOM   5805 C C   . ILE B 2 189 ? -18.677 -58.592 58.335  1.00 199.75 ? 189  ILE B C   1 
ATOM   5806 O O   . ILE B 2 189 ? -17.902 -59.344 57.739  1.00 201.12 ? 189  ILE B O   1 
ATOM   5807 C CB  . ILE B 2 189 ? -18.621 -56.222 57.504  1.00 159.42 ? 189  ILE B CB  1 
ATOM   5808 C CG1 . ILE B 2 189 ? -19.215 -55.218 56.512  1.00 154.58 ? 189  ILE B CG1 1 
ATOM   5809 C CG2 . ILE B 2 189 ? -17.179 -56.534 57.115  1.00 157.11 ? 189  ILE B CG2 1 
ATOM   5810 C CD1 . ILE B 2 189 ? -18.390 -53.946 56.370  1.00 146.87 ? 189  ILE B CD1 1 
ATOM   5811 N N   . GLU B 2 190 ? -18.872 -58.655 59.650  1.00 198.88 ? 190  GLU B N   1 
ATOM   5812 C CA  . GLU B 2 190 ? -18.066 -59.528 60.508  1.00 196.29 ? 190  GLU B CA  1 
ATOM   5813 C C   . GLU B 2 190 ? -18.532 -60.989 60.512  1.00 191.57 ? 190  GLU B C   1 
ATOM   5814 O O   . GLU B 2 190 ? -17.722 -61.905 60.353  1.00 187.91 ? 190  GLU B O   1 
ATOM   5815 C CB  . GLU B 2 190 ? -18.003 -58.968 61.935  1.00 196.82 ? 190  GLU B CB  1 
ATOM   5816 C CG  . GLU B 2 190 ? -17.266 -57.633 62.043  1.00 196.46 ? 190  GLU B CG  1 
ATOM   5817 C CD  . GLU B 2 190 ? -17.399 -56.987 63.413  1.00 195.32 ? 190  GLU B CD  1 
ATOM   5818 O OE1 . GLU B 2 190 ? -18.247 -57.440 64.213  1.00 194.90 ? 190  GLU B OE1 1 
ATOM   5819 O OE2 . GLU B 2 190 ? -16.657 -56.019 63.686  1.00 192.79 ? 190  GLU B OE2 1 
ATOM   5820 N N   . HIS B 2 191 ? -19.832 -61.204 60.699  1.00 189.75 ? 191  HIS B N   1 
ATOM   5821 C CA  . HIS B 2 191 ? -20.392 -62.551 60.636  1.00 188.35 ? 191  HIS B CA  1 
ATOM   5822 C C   . HIS B 2 191 ? -20.246 -63.102 59.220  1.00 176.45 ? 191  HIS B C   1 
ATOM   5823 O O   . HIS B 2 191 ? -19.880 -64.262 59.030  1.00 174.06 ? 191  HIS B O   1 
ATOM   5824 C CB  . HIS B 2 191 ? -21.872 -62.556 61.046  1.00 199.26 ? 191  HIS B CB  1 
ATOM   5825 C CG  . HIS B 2 191 ? -22.106 -62.376 62.518  1.00 207.91 ? 191  HIS B CG  1 
ATOM   5826 N ND1 . HIS B 2 191 ? -22.366 -63.432 63.367  1.00 211.14 ? 191  HIS B ND1 1 
ATOM   5827 C CD2 . HIS B 2 191 ? -22.143 -61.261 63.286  1.00 209.44 ? 191  HIS B CD2 1 
ATOM   5828 C CE1 . HIS B 2 191 ? -22.543 -62.976 64.595  1.00 210.94 ? 191  HIS B CE1 1 
ATOM   5829 N NE2 . HIS B 2 191 ? -22.412 -61.662 64.573  1.00 209.37 ? 191  HIS B NE2 1 
ATOM   5830 N N   . GLY B 2 192 ? -20.535 -62.254 58.234  1.00 164.54 ? 192  GLY B N   1 
ATOM   5831 C CA  . GLY B 2 192 ? -20.445 -62.623 56.833  1.00 149.78 ? 192  GLY B CA  1 
ATOM   5832 C C   . GLY B 2 192 ? -19.178 -62.098 56.192  1.00 135.39 ? 192  GLY B C   1 
ATOM   5833 O O   . GLY B 2 192 ? -18.121 -62.089 56.824  1.00 127.13 ? 192  GLY B O   1 
ATOM   5834 N N   . ASN B 2 210 ? -33.007 -67.681 58.743  1.00 150.68 ? 210  ASN B N   1 
ATOM   5835 C CA  . ASN B 2 210 ? -33.082 -69.027 58.171  1.00 166.49 ? 210  ASN B CA  1 
ATOM   5836 C C   . ASN B 2 210 ? -32.238 -69.175 56.900  1.00 174.65 ? 210  ASN B C   1 
ATOM   5837 O O   . ASN B 2 210 ? -31.266 -69.935 56.877  1.00 173.88 ? 210  ASN B O   1 
ATOM   5838 C CB  . ASN B 2 210 ? -34.541 -69.434 57.891  1.00 169.14 ? 210  ASN B CB  1 
ATOM   5839 C CG  . ASN B 2 210 ? -35.298 -69.862 59.153  1.00 168.19 ? 210  ASN B CG  1 
ATOM   5840 O OD1 . ASN B 2 210 ? -34.794 -70.636 59.970  1.00 165.82 ? 210  ASN B OD1 1 
ATOM   5841 N ND2 . ASN B 2 210 ? -36.523 -69.368 59.300  1.00 165.19 ? 210  ASN B ND2 1 
ATOM   5842 N N   . GLU B 2 211 ? -32.620 -68.449 55.848  1.00 179.90 ? 211  GLU B N   1 
ATOM   5843 C CA  . GLU B 2 211 ? -31.922 -68.491 54.559  1.00 179.68 ? 211  GLU B CA  1 
ATOM   5844 C C   . GLU B 2 211 ? -30.794 -67.470 54.522  1.00 178.55 ? 211  GLU B C   1 
ATOM   5845 O O   . GLU B 2 211 ? -29.985 -67.442 53.591  1.00 172.28 ? 211  GLU B O   1 
ATOM   5846 C CB  . GLU B 2 211 ? -32.888 -68.201 53.408  1.00 179.87 ? 211  GLU B CB  1 
ATOM   5847 C CG  . GLU B 2 211 ? -33.347 -66.748 53.347  1.00 179.76 ? 211  GLU B CG  1 
ATOM   5848 C CD  . GLU B 2 211 ? -33.904 -66.360 51.990  1.00 182.17 ? 211  GLU B CD  1 
ATOM   5849 O OE1 . GLU B 2 211 ? -33.768 -67.158 51.038  1.00 183.16 ? 211  GLU B OE1 1 
ATOM   5850 O OE2 . GLU B 2 211 ? -34.473 -65.253 51.876  1.00 182.36 ? 211  GLU B OE2 1 
ATOM   5851 N N   . ILE B 2 212 ? -30.763 -66.615 55.536  1.00 180.64 ? 212  ILE B N   1 
ATOM   5852 C CA  . ILE B 2 212 ? -29.711 -65.626 55.674  1.00 178.46 ? 212  ILE B CA  1 
ATOM   5853 C C   . ILE B 2 212 ? -28.459 -66.306 56.220  1.00 178.00 ? 212  ILE B C   1 
ATOM   5854 O O   . ILE B 2 212 ? -27.420 -65.674 56.398  1.00 173.23 ? 212  ILE B O   1 
ATOM   5855 C CB  . ILE B 2 212 ? -30.147 -64.497 56.620  1.00 179.94 ? 212  ILE B CB  1 
ATOM   5856 C CG1 . ILE B 2 212 ? -29.189 -63.313 56.514  1.00 183.37 ? 212  ILE B CG1 1 
ATOM   5857 C CG2 . ILE B 2 212 ? -30.247 -65.010 58.050  1.00 180.17 ? 212  ILE B CG2 1 
ATOM   5858 C CD1 . ILE B 2 212 ? -29.020 -62.804 55.100  1.00 189.84 ? 212  ILE B CD1 1 
ATOM   5859 N N   . ARG B 2 213 ? -28.573 -67.605 56.481  1.00 181.92 ? 213  ARG B N   1 
ATOM   5860 C CA  . ARG B 2 213 ? -27.464 -68.399 56.997  1.00 181.98 ? 213  ARG B CA  1 
ATOM   5861 C C   . ARG B 2 213 ? -26.680 -69.012 55.842  1.00 178.76 ? 213  ARG B C   1 
ATOM   5862 O O   . ARG B 2 213 ? -25.472 -69.231 55.943  1.00 173.32 ? 213  ARG B O   1 
ATOM   5863 C CB  . ARG B 2 213 ? -27.996 -69.498 57.922  1.00 187.71 ? 213  ARG B CB  1 
ATOM   5864 C CG  . ARG B 2 213 ? -26.933 -70.291 58.670  1.00 189.90 ? 213  ARG B CG  1 
ATOM   5865 C CD  . ARG B 2 213 ? -27.563 -71.129 59.776  1.00 190.83 ? 213  ARG B CD  1 
ATOM   5866 N NE  . ARG B 2 213 ? -28.401 -70.311 60.650  1.00 188.27 ? 213  ARG B NE  1 
ATOM   5867 C CZ  . ARG B 2 213 ? -29.719 -70.186 60.522  1.00 186.84 ? 213  ARG B CZ  1 
ATOM   5868 N NH1 . ARG B 2 213 ? -30.361 -70.839 59.560  1.00 188.01 ? 213  ARG B NH1 1 
ATOM   5869 N NH2 . ARG B 2 213 ? -30.397 -69.410 61.358  1.00 181.94 ? 213  ARG B NH2 1 
ATOM   5870 N N   . ASP B 2 214 ? -27.379 -69.280 54.743  1.00 183.15 ? 214  ASP B N   1 
ATOM   5871 C CA  . ASP B 2 214 ? -26.766 -69.881 53.563  1.00 187.54 ? 214  ASP B CA  1 
ATOM   5872 C C   . ASP B 2 214 ? -26.043 -68.851 52.699  1.00 185.73 ? 214  ASP B C   1 
ATOM   5873 O O   . ASP B 2 214 ? -25.045 -69.171 52.053  1.00 190.23 ? 214  ASP B O   1 
ATOM   5874 C CB  . ASP B 2 214 ? -27.810 -70.628 52.724  1.00 191.89 ? 214  ASP B CB  1 
ATOM   5875 C CG  . ASP B 2 214 ? -28.289 -71.907 53.385  1.00 191.60 ? 214  ASP B CG  1 
ATOM   5876 O OD1 . ASP B 2 214 ? -28.125 -72.044 54.618  1.00 189.19 ? 214  ASP B OD1 1 
ATOM   5877 O OD2 . ASP B 2 214 ? -28.831 -72.776 52.668  1.00 193.63 ? 214  ASP B OD2 1 
ATOM   5878 N N   . ARG B 2 215 ? -26.546 -67.619 52.681  1.00 176.92 ? 215  ARG B N   1 
ATOM   5879 C CA  . ARG B 2 215 ? -25.908 -66.564 51.898  1.00 167.64 ? 215  ARG B CA  1 
ATOM   5880 C C   . ARG B 2 215 ? -24.472 -66.325 52.348  1.00 161.14 ? 215  ARG B C   1 
ATOM   5881 O O   . ARG B 2 215 ? -23.643 -65.884 51.557  1.00 166.00 ? 215  ARG B O   1 
ATOM   5882 C CB  . ARG B 2 215 ? -26.717 -65.262 51.927  1.00 164.61 ? 215  ARG B CB  1 
ATOM   5883 C CG  . ARG B 2 215 ? -27.977 -65.308 51.076  1.00 167.49 ? 215  ARG B CG  1 
ATOM   5884 C CD  . ARG B 2 215 ? -27.664 -65.791 49.667  1.00 173.97 ? 215  ARG B CD  1 
ATOM   5885 N NE  . ARG B 2 215 ? -28.835 -66.345 48.989  1.00 182.22 ? 215  ARG B NE  1 
ATOM   5886 C CZ  . ARG B 2 215 ? -29.583 -65.684 48.109  1.00 185.45 ? 215  ARG B CZ  1 
ATOM   5887 N NH1 . ARG B 2 215 ? -29.290 -64.431 47.789  1.00 183.11 ? 215  ARG B NH1 1 
ATOM   5888 N NH2 . ARG B 2 215 ? -30.626 -66.278 47.546  1.00 190.17 ? 215  ARG B NH2 1 
ATOM   5889 N N   . HIS B 2 216 ? -24.176 -66.621 53.612  1.00 153.69 ? 216  HIS B N   1 
ATOM   5890 C CA  . HIS B 2 216 ? -22.803 -66.533 54.108  1.00 154.71 ? 216  HIS B CA  1 
ATOM   5891 C C   . HIS B 2 216 ? -21.924 -67.553 53.398  1.00 160.80 ? 216  HIS B C   1 
ATOM   5892 O O   . HIS B 2 216 ? -20.840 -67.221 52.915  1.00 163.72 ? 216  HIS B O   1 
ATOM   5893 C CB  . HIS B 2 216 ? -22.732 -66.746 55.626  1.00 151.86 ? 216  HIS B CB  1 
ATOM   5894 C CG  . HIS B 2 216 ? -21.333 -66.791 56.167  1.00 148.76 ? 216  HIS B CG  1 
ATOM   5895 N ND1 . HIS B 2 216 ? -20.592 -65.655 56.416  1.00 144.20 ? 216  HIS B ND1 1 
ATOM   5896 C CD2 . HIS B 2 216 ? -20.543 -67.837 56.510  1.00 149.05 ? 216  HIS B CD2 1 
ATOM   5897 C CE1 . HIS B 2 216 ? -19.405 -65.998 56.885  1.00 144.27 ? 216  HIS B CE1 1 
ATOM   5898 N NE2 . HIS B 2 216 ? -19.349 -67.316 56.952  1.00 148.41 ? 216  HIS B NE2 1 
ATOM   5899 N N   . LYS B 2 217 ? -22.395 -68.796 53.341  1.00 161.40 ? 217  LYS B N   1 
ATOM   5900 C CA  . LYS B 2 217 ? -21.684 -69.848 52.625  1.00 157.70 ? 217  LYS B CA  1 
ATOM   5901 C C   . LYS B 2 217 ? -21.556 -69.477 51.150  1.00 150.93 ? 217  LYS B C   1 
ATOM   5902 O O   . LYS B 2 217 ? -20.668 -69.965 50.451  1.00 151.64 ? 217  LYS B O   1 
ATOM   5903 C CB  . LYS B 2 217 ? -22.401 -71.198 52.775  1.00 156.96 ? 217  LYS B CB  1 
ATOM   5904 C CG  . LYS B 2 217 ? -22.328 -71.812 54.168  1.00 152.94 ? 217  LYS B CG  1 
ATOM   5905 C CD  . LYS B 2 217 ? -23.587 -71.535 54.979  1.00 154.66 ? 217  LYS B CD  1 
ATOM   5906 C CE  . LYS B 2 217 ? -23.641 -72.417 56.229  1.00 160.60 ? 217  LYS B CE  1 
ATOM   5907 N NZ  . LYS B 2 217 ? -24.972 -72.409 56.919  1.00 159.95 ? 217  LYS B NZ  1 
ATOM   5908 N N   . ASP B 2 218 ? -22.449 -68.606 50.690  1.00 143.15 ? 218  ASP B N   1 
ATOM   5909 C CA  . ASP B 2 218 ? -22.474 -68.186 49.294  1.00 143.96 ? 218  ASP B CA  1 
ATOM   5910 C C   . ASP B 2 218 ? -21.530 -67.011 49.034  1.00 142.25 ? 218  ASP B C   1 
ATOM   5911 O O   . ASP B 2 218 ? -21.005 -66.862 47.930  1.00 148.89 ? 218  ASP B O   1 
ATOM   5912 C CB  . ASP B 2 218 ? -23.902 -67.829 48.864  1.00 146.65 ? 218  ASP B CB  1 
ATOM   5913 C CG  . ASP B 2 218 ? -24.770 -69.057 48.616  1.00 149.74 ? 218  ASP B CG  1 
ATOM   5914 O OD1 . ASP B 2 218 ? -24.215 -70.151 48.372  1.00 149.19 ? 218  ASP B OD1 1 
ATOM   5915 O OD2 . ASP B 2 218 ? -26.012 -68.921 48.656  1.00 151.58 ? 218  ASP B OD2 1 
ATOM   5916 N N   . ILE B 2 219 ? -21.320 -66.179 50.049  1.00 129.76 ? 219  ILE B N   1 
ATOM   5917 C CA  . ILE B 2 219 ? -20.402 -65.050 49.937  1.00 121.59 ? 219  ILE B CA  1 
ATOM   5918 C C   . ILE B 2 219 ? -18.947 -65.508 50.010  1.00 122.11 ? 219  ILE B C   1 
ATOM   5919 O O   . ILE B 2 219 ? -18.108 -65.047 49.241  1.00 135.08 ? 219  ILE B O   1 
ATOM   5920 C CB  . ILE B 2 219 ? -20.674 -63.963 51.012  1.00 128.21 ? 219  ILE B CB  1 
ATOM   5921 C CG1 . ILE B 2 219 ? -21.631 -62.896 50.472  1.00 127.29 ? 219  ILE B CG1 1 
ATOM   5922 C CG2 . ILE B 2 219 ? -19.373 -63.298 51.465  1.00 125.07 ? 219  ILE B CG2 1 
ATOM   5923 C CD1 . ILE B 2 219 ? -22.913 -63.450 49.909  1.00 130.26 ? 219  ILE B CD1 1 
ATOM   5924 N N   . GLN B 2 220 ? -18.651 -66.418 50.928  1.00 115.27 ? 220  GLN B N   1 
ATOM   5925 C CA  . GLN B 2 220 ? -17.288 -66.904 51.089  1.00 120.72 ? 220  GLN B CA  1 
ATOM   5926 C C   . GLN B 2 220 ? -16.878 -67.811 49.925  1.00 119.60 ? 220  GLN B C   1 
ATOM   5927 O O   . GLN B 2 220 ? -15.696 -68.111 49.751  1.00 118.66 ? 220  GLN B O   1 
ATOM   5928 C CB  . GLN B 2 220 ? -17.137 -67.634 52.423  1.00 139.55 ? 220  GLN B CB  1 
ATOM   5929 C CG  . GLN B 2 220 ? -18.000 -68.884 52.532  1.00 159.44 ? 220  GLN B CG  1 
ATOM   5930 C CD  . GLN B 2 220 ? -18.056 -69.443 53.942  1.00 168.67 ? 220  GLN B CD  1 
ATOM   5931 O OE1 . GLN B 2 220 ? -17.792 -68.734 54.918  1.00 173.13 ? 220  GLN B OE1 1 
ATOM   5932 N NE2 . GLN B 2 220 ? -18.411 -70.721 54.056  1.00 165.84 ? 220  GLN B NE2 1 
ATOM   5933 N N   . GLN B 2 221 ? -17.853 -68.257 49.136  1.00 119.13 ? 221  GLN B N   1 
ATOM   5934 C CA  . GLN B 2 221 ? -17.551 -68.967 47.893  1.00 123.06 ? 221  GLN B CA  1 
ATOM   5935 C C   . GLN B 2 221 ? -16.925 -67.975 46.915  1.00 119.71 ? 221  GLN B C   1 
ATOM   5936 O O   . GLN B 2 221 ? -15.783 -68.138 46.479  1.00 116.58 ? 221  GLN B O   1 
ATOM   5937 C CB  . GLN B 2 221 ? -18.815 -69.590 47.284  1.00 127.73 ? 221  GLN B CB  1 
ATOM   5938 C CG  . GLN B 2 221 ? -19.074 -71.054 47.661  1.00 135.78 ? 221  GLN B CG  1 
ATOM   5939 C CD  . GLN B 2 221 ? -18.372 -72.046 46.741  1.00 138.04 ? 221  GLN B CD  1 
ATOM   5940 O OE1 . GLN B 2 221 ? -17.144 -72.086 46.674  1.00 139.99 ? 221  GLN B OE1 1 
ATOM   5941 N NE2 . GLN B 2 221 ? -19.154 -72.858 46.034  1.00 134.10 ? 221  GLN B NE2 1 
ATOM   5942 N N   . LEU B 2 222 ? -17.686 -66.934 46.591  1.00 115.31 ? 222  LEU B N   1 
ATOM   5943 C CA  . LEU B 2 222 ? -17.215 -65.858 45.736  1.00 114.24 ? 222  LEU B CA  1 
ATOM   5944 C C   . LEU B 2 222 ? -15.871 -65.307 46.203  1.00 122.62 ? 222  LEU B C   1 
ATOM   5945 O O   . LEU B 2 222 ? -15.147 -64.685 45.429  1.00 132.65 ? 222  LEU B O   1 
ATOM   5946 C CB  . LEU B 2 222 ? -18.248 -64.735 45.703  1.00 109.54 ? 222  LEU B CB  1 
ATOM   5947 C CG  . LEU B 2 222 ? -19.640 -65.185 45.278  1.00 116.41 ? 222  LEU B CG  1 
ATOM   5948 C CD1 . LEU B 2 222 ? -20.542 -63.987 45.087  1.00 122.99 ? 222  LEU B CD1 1 
ATOM   5949 C CD2 . LEU B 2 222 ? -19.552 -65.989 43.999  1.00 122.85 ? 222  LEU B CD2 1 
ATOM   5950 N N   . GLU B 2 223 ? -15.541 -65.539 47.468  1.00 120.12 ? 223  GLU B N   1 
ATOM   5951 C CA  . GLU B 2 223 ? -14.301 -65.028 48.041  1.00 124.22 ? 223  GLU B CA  1 
ATOM   5952 C C   . GLU B 2 223 ? -13.085 -65.905 47.748  1.00 123.74 ? 223  GLU B C   1 
ATOM   5953 O O   . GLU B 2 223 ? -12.003 -65.390 47.469  1.00 125.71 ? 223  GLU B O   1 
ATOM   5954 C CB  . GLU B 2 223 ? -14.448 -64.805 49.549  1.00 129.72 ? 223  GLU B CB  1 
ATOM   5955 C CG  . GLU B 2 223 ? -14.987 -63.438 49.930  1.00 128.06 ? 223  GLU B CG  1 
ATOM   5956 C CD  . GLU B 2 223 ? -13.974 -62.320 49.721  1.00 131.82 ? 223  GLU B CD  1 
ATOM   5957 O OE1 . GLU B 2 223 ? -13.105 -62.442 48.826  1.00 120.89 ? 223  GLU B OE1 1 
ATOM   5958 O OE2 . GLU B 2 223 ? -14.053 -61.312 50.457  1.00 141.35 ? 223  GLU B OE2 1 
ATOM   5959 N N   . ARG B 2 224 ? -13.246 -67.223 47.828  1.00 127.32 ? 224  ARG B N   1 
ATOM   5960 C CA  . ARG B 2 224 ? -12.147 -68.110 47.457  1.00 125.88 ? 224  ARG B CA  1 
ATOM   5961 C C   . ARG B 2 224 ? -12.100 -68.246 45.940  1.00 118.84 ? 224  ARG B C   1 
ATOM   5962 O O   . ARG B 2 224 ? -11.132 -68.755 45.375  1.00 117.91 ? 224  ARG B O   1 
ATOM   5963 C CB  . ARG B 2 224 ? -12.218 -69.470 48.166  1.00 126.83 ? 224  ARG B CB  1 
ATOM   5964 C CG  . ARG B 2 224 ? -13.580 -70.133 48.176  1.00 139.49 ? 224  ARG B CG  1 
ATOM   5965 C CD  . ARG B 2 224 ? -13.489 -71.520 48.803  1.00 149.68 ? 224  ARG B CD  1 
ATOM   5966 N NE  . ARG B 2 224 ? -14.797 -72.027 49.207  1.00 155.77 ? 224  ARG B NE  1 
ATOM   5967 C CZ  . ARG B 2 224 ? -15.398 -71.699 50.347  1.00 155.39 ? 224  ARG B CZ  1 
ATOM   5968 N NH1 . ARG B 2 224 ? -14.804 -70.859 51.185  1.00 149.52 ? 224  ARG B NH1 1 
ATOM   5969 N NH2 . ARG B 2 224 ? -16.590 -72.204 50.647  1.00 154.16 ? 224  ARG B NH2 1 
ATOM   5970 N N   . SER B 2 225 ? -13.150 -67.765 45.284  1.00 109.90 ? 225  SER B N   1 
ATOM   5971 C CA  . SER B 2 225 ? -13.126 -67.623 43.840  1.00 106.28 ? 225  SER B CA  1 
ATOM   5972 C C   . SER B 2 225 ? -12.197 -66.458 43.497  1.00 107.59 ? 225  SER B C   1 
ATOM   5973 O O   . SER B 2 225 ? -11.206 -66.629 42.790  1.00 106.51 ? 225  SER B O   1 
ATOM   5974 C CB  . SER B 2 225 ? -14.532 -67.376 43.293  1.00 102.58 ? 225  SER B CB  1 
ATOM   5975 O OG  . SER B 2 225 ? -14.606 -67.717 41.917  1.00 109.63 ? 225  SER B OG  1 
ATOM   5976 N N   . LEU B 2 226 ? -12.512 -65.275 44.020  1.00 105.97 ? 226  LEU B N   1 
ATOM   5977 C CA  . LEU B 2 226 ? -11.677 -64.093 43.818  1.00 96.69  ? 226  LEU B CA  1 
ATOM   5978 C C   . LEU B 2 226 ? -10.220 -64.349 44.210  1.00 94.65  ? 226  LEU B C   1 
ATOM   5979 O O   . LEU B 2 226 ? -9.297  -63.806 43.601  1.00 95.00  ? 226  LEU B O   1 
ATOM   5980 C CB  . LEU B 2 226 ? -12.242 -62.899 44.586  1.00 90.00  ? 226  LEU B CB  1 
ATOM   5981 C CG  . LEU B 2 226 ? -13.629 -62.446 44.122  1.00 97.82  ? 226  LEU B CG  1 
ATOM   5982 C CD1 . LEU B 2 226 ? -14.240 -61.483 45.121  1.00 94.54  ? 226  LEU B CD1 1 
ATOM   5983 C CD2 . LEU B 2 226 ? -13.582 -61.825 42.730  1.00 102.45 ? 226  LEU B CD2 1 
ATOM   5984 N N   . LEU B 2 227 ? -10.015 -65.195 45.211  1.00 94.00  ? 227  LEU B N   1 
ATOM   5985 C CA  . LEU B 2 227 ? -8.665  -65.532 45.647  1.00 100.10 ? 227  LEU B CA  1 
ATOM   5986 C C   . LEU B 2 227 ? -7.903  -66.408 44.647  1.00 99.92  ? 227  LEU B C   1 
ATOM   5987 O O   . LEU B 2 227 ? -6.743  -66.145 44.351  1.00 97.33  ? 227  LEU B O   1 
ATOM   5988 C CB  . LEU B 2 227 ? -8.697  -66.181 47.030  1.00 105.11 ? 227  LEU B CB  1 
ATOM   5989 C CG  . LEU B 2 227 ? -7.921  -65.366 48.064  1.00 113.37 ? 227  LEU B CG  1 
ATOM   5990 C CD1 . LEU B 2 227 ? -8.375  -65.683 49.489  1.00 114.96 ? 227  LEU B CD1 1 
ATOM   5991 C CD2 . LEU B 2 227 ? -6.413  -65.563 47.873  1.00 110.49 ? 227  LEU B CD2 1 
ATOM   5992 N N   . GLU B 2 228 ? -8.552  -67.454 44.143  1.00 106.21 ? 228  GLU B N   1 
ATOM   5993 C CA  . GLU B 2 228 ? -7.961  -68.298 43.107  1.00 114.59 ? 228  GLU B CA  1 
ATOM   5994 C C   . GLU B 2 228 ? -7.563  -67.429 41.914  1.00 106.73 ? 228  GLU B C   1 
ATOM   5995 O O   . GLU B 2 228 ? -6.430  -67.483 41.427  1.00 104.31 ? 228  GLU B O   1 
ATOM   5996 C CB  . GLU B 2 228 ? -8.961  -69.372 42.653  1.00 128.33 ? 228  GLU B CB  1 
ATOM   5997 C CG  . GLU B 2 228 ? -8.754  -70.764 43.246  1.00 141.95 ? 228  GLU B CG  1 
ATOM   5998 C CD  . GLU B 2 228 ? -9.166  -70.866 44.709  1.00 146.32 ? 228  GLU B CD  1 
ATOM   5999 O OE1 . GLU B 2 228 ? -8.903  -69.916 45.477  1.00 140.80 ? 228  GLU B OE1 1 
ATOM   6000 O OE2 . GLU B 2 228 ? -9.744  -71.908 45.094  1.00 149.68 ? 228  GLU B OE2 1 
ATOM   6001 N N   . LEU B 2 229 ? -8.519  -66.630 41.453  1.00 96.72  ? 229  LEU B N   1 
ATOM   6002 C CA  . LEU B 2 229 ? -8.308  -65.696 40.360  1.00 93.54  ? 229  LEU B CA  1 
ATOM   6003 C C   . LEU B 2 229 ? -7.125  -64.769 40.617  1.00 84.44  ? 229  LEU B C   1 
ATOM   6004 O O   . LEU B 2 229 ? -6.209  -64.689 39.795  1.00 75.37  ? 229  LEU B O   1 
ATOM   6005 C CB  . LEU B 2 229 ? -9.568  -64.868 40.146  1.00 94.65  ? 229  LEU B CB  1 
ATOM   6006 C CG  . LEU B 2 229 ? -10.731 -65.672 39.577  1.00 90.96  ? 229  LEU B CG  1 
ATOM   6007 C CD1 . LEU B 2 229 ? -11.951 -64.783 39.408  1.00 90.61  ? 229  LEU B CD1 1 
ATOM   6008 C CD2 . LEU B 2 229 ? -10.321 -66.322 38.252  1.00 82.81  ? 229  LEU B CD2 1 
ATOM   6009 N N   . HIS B 2 230 ? -7.154  -64.071 41.752  1.00 70.03  ? 230  HIS B N   1 
ATOM   6010 C CA  . HIS B 2 230 ? -6.029  -63.235 42.158  1.00 76.08  ? 230  HIS B CA  1 
ATOM   6011 C C   . HIS B 2 230 ? -4.704  -63.981 42.083  1.00 78.13  ? 230  HIS B C   1 
ATOM   6012 O O   . HIS B 2 230 ? -3.750  -63.510 41.464  1.00 83.90  ? 230  HIS B O   1 
ATOM   6013 C CB  . HIS B 2 230 ? -6.225  -62.689 43.569  1.00 84.01  ? 230  HIS B CB  1 
ATOM   6014 C CG  . HIS B 2 230 ? -5.075  -61.865 44.053  1.00 97.99  ? 230  HIS B CG  1 
ATOM   6015 N ND1 . HIS B 2 230 ? -5.092  -60.488 44.041  1.00 108.77 ? 230  HIS B ND1 1 
ATOM   6016 C CD2 . HIS B 2 230 ? -3.863  -62.225 44.536  1.00 105.49 ? 230  HIS B CD2 1 
ATOM   6017 C CE1 . HIS B 2 230 ? -3.942  -60.034 44.506  1.00 113.75 ? 230  HIS B CE1 1 
ATOM   6018 N NE2 . HIS B 2 230 ? -3.178  -61.068 44.812  1.00 113.78 ? 230  HIS B NE2 1 
ATOM   6019 N N   . GLU B 2 231 ? -4.642  -65.139 42.726  1.00 79.77  ? 231  GLU B N   1 
ATOM   6020 C CA  . GLU B 2 231 ? -3.441  -65.949 42.687  1.00 83.85  ? 231  GLU B CA  1 
ATOM   6021 C C   . GLU B 2 231 ? -3.042  -66.175 41.242  1.00 76.63  ? 231  GLU B C   1 
ATOM   6022 O O   . GLU B 2 231 ? -1.866  -66.089 40.892  1.00 80.77  ? 231  GLU B O   1 
ATOM   6023 C CB  . GLU B 2 231 ? -3.667  -67.292 43.384  1.00 100.47 ? 231  GLU B CB  1 
ATOM   6024 C CG  . GLU B 2 231 ? -2.455  -68.213 43.346  1.00 118.25 ? 231  GLU B CG  1 
ATOM   6025 C CD  . GLU B 2 231 ? -2.828  -69.649 43.027  1.00 137.47 ? 231  GLU B CD  1 
ATOM   6026 O OE1 . GLU B 2 231 ? -3.109  -70.421 43.973  1.00 140.55 ? 231  GLU B OE1 1 
ATOM   6027 O OE2 . GLU B 2 231 ? -2.839  -70.006 41.827  1.00 142.29 ? 231  GLU B OE2 1 
ATOM   6028 N N   . MET B 2 232 ? -4.028  -66.463 40.402  1.00 78.63  ? 232  MET B N   1 
ATOM   6029 C CA  . MET B 2 232 ? -3.760  -66.762 38.997  1.00 90.40  ? 232  MET B CA  1 
ATOM   6030 C C   . MET B 2 232 ? -3.234  -65.526 38.262  1.00 92.66  ? 232  MET B C   1 
ATOM   6031 O O   . MET B 2 232 ? -2.154  -65.548 37.661  1.00 87.69  ? 232  MET B O   1 
ATOM   6032 C CB  . MET B 2 232 ? -5.023  -67.301 38.319  1.00 90.11  ? 232  MET B CB  1 
ATOM   6033 C CG  . MET B 2 232 ? -4.841  -67.699 36.860  1.00 93.77  ? 232  MET B CG  1 
ATOM   6034 S SD  . MET B 2 232 ? -4.956  -66.309 35.717  1.00 151.12 ? 232  MET B SD  1 
ATOM   6035 C CE  . MET B 2 232 ? -6.662  -65.813 35.940  1.00 75.93  ? 232  MET B CE  1 
ATOM   6036 N N   . PHE B 2 233 ? -4.008  -64.447 38.320  1.00 87.75  ? 233  PHE B N   1 
ATOM   6037 C CA  . PHE B 2 233 ? -3.610  -63.191 37.711  1.00 78.39  ? 233  PHE B CA  1 
ATOM   6038 C C   . PHE B 2 233 ? -2.196  -62.813 38.129  1.00 80.19  ? 233  PHE B C   1 
ATOM   6039 O O   . PHE B 2 233 ? -1.431  -62.262 37.333  1.00 81.59  ? 233  PHE B O   1 
ATOM   6040 C CB  . PHE B 2 233 ? -4.585  -62.075 38.084  1.00 69.95  ? 233  PHE B CB  1 
ATOM   6041 C CG  . PHE B 2 233 ? -5.924  -62.174 37.398  1.00 76.32  ? 233  PHE B CG  1 
ATOM   6042 C CD1 . PHE B 2 233 ? -6.011  -62.363 36.027  1.00 72.64  ? 233  PHE B CD1 1 
ATOM   6043 C CD2 . PHE B 2 233 ? -7.095  -62.036 38.121  1.00 68.25  ? 233  PHE B CD2 1 
ATOM   6044 C CE1 . PHE B 2 233 ? -7.235  -62.428 35.399  1.00 71.69  ? 233  PHE B CE1 1 
ATOM   6045 C CE2 . PHE B 2 233 ? -8.313  -62.098 37.502  1.00 72.12  ? 233  PHE B CE2 1 
ATOM   6046 C CZ  . PHE B 2 233 ? -8.385  -62.303 36.137  1.00 78.43  ? 233  PHE B CZ  1 
ATOM   6047 N N   . THR B 2 234 ? -1.842  -63.117 39.372  1.00 76.42  ? 234  THR B N   1 
ATOM   6048 C CA  . THR B 2 234 ? -0.531  -62.731 39.873  1.00 86.39  ? 234  THR B CA  1 
ATOM   6049 C C   . THR B 2 234 ? 0.616   -63.350 39.066  1.00 97.59  ? 234  THR B C   1 
ATOM   6050 O O   . THR B 2 234 ? 1.417   -62.629 38.464  1.00 100.13 ? 234  THR B O   1 
ATOM   6051 C CB  . THR B 2 234 ? -0.364  -63.030 41.371  1.00 82.82  ? 234  THR B CB  1 
ATOM   6052 O OG1 . THR B 2 234 ? -1.351  -62.307 42.121  1.00 88.71  ? 234  THR B OG1 1 
ATOM   6053 C CG2 . THR B 2 234 ? 1.009   -62.604 41.827  1.00 69.80  ? 234  THR B CG2 1 
ATOM   6054 N N   . ASP B 2 235 ? 0.699   -64.675 39.036  1.00 105.43 ? 235  ASP B N   1 
ATOM   6055 C CA  . ASP B 2 235 ? 1.770   -65.308 38.273  1.00 117.35 ? 235  ASP B CA  1 
ATOM   6056 C C   . ASP B 2 235 ? 1.509   -65.283 36.762  1.00 114.48 ? 235  ASP B C   1 
ATOM   6057 O O   . ASP B 2 235 ? 2.376   -65.676 35.983  1.00 117.85 ? 235  ASP B O   1 
ATOM   6058 C CB  . ASP B 2 235 ? 2.075   -66.730 38.769  1.00 123.83 ? 235  ASP B CB  1 
ATOM   6059 C CG  . ASP B 2 235 ? 1.059   -67.744 38.302  1.00 132.76 ? 235  ASP B CG  1 
ATOM   6060 O OD1 . ASP B 2 235 ? -0.025  -67.820 38.919  1.00 139.43 ? 235  ASP B OD1 1 
ATOM   6061 O OD2 . ASP B 2 235 ? 1.349   -68.473 37.327  1.00 134.67 ? 235  ASP B OD2 1 
ATOM   6062 N N   . MET B 2 236 ? 0.332   -64.816 36.345  1.00 101.19 ? 236  MET B N   1 
ATOM   6063 C CA  . MET B 2 236 ? 0.079   -64.631 34.916  1.00 93.90  ? 236  MET B CA  1 
ATOM   6064 C C   . MET B 2 236 ? 0.654   -63.302 34.451  1.00 96.35  ? 236  MET B C   1 
ATOM   6065 O O   . MET B 2 236 ? 1.112   -63.176 33.314  1.00 88.56  ? 236  MET B O   1 
ATOM   6066 C CB  . MET B 2 236 ? -1.412  -64.717 34.569  1.00 95.89  ? 236  MET B CB  1 
ATOM   6067 C CG  . MET B 2 236 ? -2.010  -66.144 34.538  1.00 113.79 ? 236  MET B CG  1 
ATOM   6068 S SD  . MET B 2 236 ? -1.210  -67.410 33.496  1.00 110.45 ? 236  MET B SD  1 
ATOM   6069 C CE  . MET B 2 236 ? -0.961  -66.507 31.955  1.00 67.89  ? 236  MET B CE  1 
ATOM   6070 N N   . SER B 2 237 ? 0.628   -62.313 35.341  1.00 103.22 ? 237  SER B N   1 
ATOM   6071 C CA  . SER B 2 237 ? 1.173   -60.997 35.044  1.00 92.28  ? 237  SER B CA  1 
ATOM   6072 C C   . SER B 2 237 ? 2.681   -61.070 34.972  1.00 95.74  ? 237  SER B C   1 
ATOM   6073 O O   . SER B 2 237 ? 3.270   -60.735 33.956  1.00 108.62 ? 237  SER B O   1 
ATOM   6074 C CB  . SER B 2 237 ? 0.744   -59.980 36.097  1.00 93.59  ? 237  SER B CB  1 
ATOM   6075 O OG  . SER B 2 237 ? -0.666  -59.848 36.115  1.00 98.09  ? 237  SER B OG  1 
ATOM   6076 N N   . THR B 2 238 ? 3.314   -61.522 36.045  1.00 102.25 ? 238  THR B N   1 
ATOM   6077 C CA  . THR B 2 238 ? 4.769   -61.612 36.051  1.00 115.54 ? 238  THR B CA  1 
ATOM   6078 C C   . THR B 2 238 ? 5.260   -62.597 34.983  1.00 121.63 ? 238  THR B C   1 
ATOM   6079 O O   . THR B 2 238 ? 6.459   -62.691 34.713  1.00 110.68 ? 238  THR B O   1 
ATOM   6080 C CB  . THR B 2 238 ? 5.308   -62.025 37.439  1.00 115.60 ? 238  THR B CB  1 
ATOM   6081 O OG1 . THR B 2 238 ? 5.374   -63.455 37.527  1.00 117.36 ? 238  THR B OG1 1 
ATOM   6082 C CG2 . THR B 2 238 ? 4.412   -61.463 38.554  1.00 109.77 ? 238  THR B CG2 1 
ATOM   6083 N N   . LEU B 2 239 ? 4.318   -63.320 34.379  1.00 137.82 ? 239  LEU B N   1 
ATOM   6084 C CA  . LEU B 2 239 ? 4.620   -64.353 33.386  1.00 148.16 ? 239  LEU B CA  1 
ATOM   6085 C C   . LEU B 2 239 ? 4.817   -63.739 32.007  1.00 142.17 ? 239  LEU B C   1 
ATOM   6086 O O   . LEU B 2 239 ? 5.359   -64.373 31.098  1.00 133.19 ? 239  LEU B O   1 
ATOM   6087 C CB  . LEU B 2 239 ? 3.485   -65.383 33.335  1.00 159.21 ? 239  LEU B CB  1 
ATOM   6088 C CG  . LEU B 2 239 ? 3.741   -66.761 32.714  1.00 165.25 ? 239  LEU B CG  1 
ATOM   6089 C CD1 . LEU B 2 239 ? 3.763   -66.714 31.185  1.00 165.26 ? 239  LEU B CD1 1 
ATOM   6090 C CD2 . LEU B 2 239 ? 5.021   -67.372 33.276  1.00 165.81 ? 239  LEU B CD2 1 
ATOM   6091 N N   . VAL B 2 240 ? 4.361   -62.502 31.860  1.00 147.32 ? 240  VAL B N   1 
ATOM   6092 C CA  . VAL B 2 240 ? 4.529   -61.758 30.623  1.00 150.13 ? 240  VAL B CA  1 
ATOM   6093 C C   . VAL B 2 240 ? 5.827   -60.948 30.695  1.00 156.40 ? 240  VAL B C   1 
ATOM   6094 O O   . VAL B 2 240 ? 6.361   -60.518 29.674  1.00 157.74 ? 240  VAL B O   1 
ATOM   6095 C CB  . VAL B 2 240 ? 3.351   -60.808 30.393  1.00 142.10 ? 240  VAL B CB  1 
ATOM   6096 C CG1 . VAL B 2 240 ? 3.706   -59.444 30.920  1.00 140.47 ? 240  VAL B CG1 1 
ATOM   6097 C CG2 . VAL B 2 240 ? 2.991   -60.742 28.915  1.00 137.67 ? 240  VAL B CG2 1 
ATOM   6098 N N   . ALA B 2 241 ? 6.328   -60.739 31.908  1.00 163.14 ? 241  ALA B N   1 
ATOM   6099 C CA  . ALA B 2 241 ? 7.637   -60.131 32.089  1.00 171.94 ? 241  ALA B CA  1 
ATOM   6100 C C   . ALA B 2 241 ? 8.643   -60.942 31.288  1.00 181.27 ? 241  ALA B C   1 
ATOM   6101 O O   . ALA B 2 241 ? 8.448   -62.138 31.070  1.00 179.06 ? 241  ALA B O   1 
ATOM   6102 C CB  . ALA B 2 241 ? 8.021   -60.107 33.562  1.00 171.60 ? 241  ALA B CB  1 
ATOM   6103 N N   . SER B 2 242 ? 9.714   -60.289 30.846  1.00 191.02 ? 242  SER B N   1 
ATOM   6104 C CA  . SER B 2 242 ? 10.711  -60.928 29.988  1.00 193.11 ? 242  SER B CA  1 
ATOM   6105 C C   . SER B 2 242 ? 10.062  -61.686 28.825  1.00 190.55 ? 242  SER B C   1 
ATOM   6106 O O   . SER B 2 242 ? 10.646  -62.619 28.273  1.00 191.18 ? 242  SER B O   1 
ATOM   6107 C CB  . SER B 2 242 ? 11.639  -61.844 30.797  1.00 195.20 ? 242  SER B CB  1 
ATOM   6108 O OG  . SER B 2 242 ? 10.913  -62.819 31.526  1.00 196.12 ? 242  SER B OG  1 
ATOM   6109 N N   . GLN B 2 243 ? 8.847   -61.274 28.468  1.00 182.33 ? 243  GLN B N   1 
ATOM   6110 C CA  . GLN B 2 243 ? 8.154   -61.796 27.297  1.00 173.74 ? 243  GLN B CA  1 
ATOM   6111 C C   . GLN B 2 243 ? 7.426   -60.655 26.604  1.00 174.94 ? 243  GLN B C   1 
ATOM   6112 O O   . GLN B 2 243 ? 6.960   -59.719 27.252  1.00 179.63 ? 243  GLN B O   1 
ATOM   6113 C CB  . GLN B 2 243 ? 7.159   -62.893 27.685  1.00 165.63 ? 243  GLN B CB  1 
ATOM   6114 C CG  . GLN B 2 243 ? 6.298   -63.399 26.532  1.00 161.31 ? 243  GLN B CG  1 
ATOM   6115 C CD  . GLN B 2 243 ? 5.400   -64.566 26.931  1.00 161.16 ? 243  GLN B CD  1 
ATOM   6116 O OE1 . GLN B 2 243 ? 4.237   -64.633 26.531  1.00 154.93 ? 243  GLN B OE1 1 
ATOM   6117 N NE2 . GLN B 2 243 ? 5.938   -65.488 27.726  1.00 162.23 ? 243  GLN B NE2 1 
ATOM   6118 N N   . GLY B 2 244 ? 7.352   -60.723 25.282  1.00 171.20 ? 244  GLY B N   1 
ATOM   6119 C CA  . GLY B 2 244 ? 6.584   -59.759 24.520  1.00 167.07 ? 244  GLY B CA  1 
ATOM   6120 C C   . GLY B 2 244 ? 6.985   -58.297 24.632  1.00 158.43 ? 244  GLY B C   1 
ATOM   6121 O O   . GLY B 2 244 ? 8.134   -57.934 24.366  1.00 151.56 ? 244  GLY B O   1 
ATOM   6122 N N   . GLU B 2 245 ? 6.017   -57.469 25.029  1.00 152.58 ? 245  GLU B N   1 
ATOM   6123 C CA  . GLU B 2 245 ? 6.091   -56.005 24.927  1.00 143.66 ? 245  GLU B CA  1 
ATOM   6124 C C   . GLU B 2 245 ? 5.979   -55.550 23.463  1.00 129.75 ? 245  GLU B C   1 
ATOM   6125 O O   . GLU B 2 245 ? 5.489   -54.450 23.172  1.00 110.10 ? 245  GLU B O   1 
ATOM   6126 C CB  . GLU B 2 245 ? 7.361   -55.442 25.588  1.00 140.60 ? 245  GLU B CB  1 
ATOM   6127 C CG  . GLU B 2 245 ? 8.491   -55.094 24.614  1.00 139.01 ? 245  GLU B CG  1 
ATOM   6128 C CD  . GLU B 2 245 ? 9.678   -54.407 25.287  1.00 135.20 ? 245  GLU B CD  1 
ATOM   6129 O OE1 . GLU B 2 245 ? 9.515   -53.893 26.414  1.00 132.91 ? 245  GLU B OE1 1 
ATOM   6130 O OE2 . GLU B 2 245 ? 10.773  -54.378 24.685  1.00 131.10 ? 245  GLU B OE2 1 
ATOM   6131 N N   . MET B 2 246 ? 6.403   -56.431 22.555  1.00 125.81 ? 246  MET B N   1 
ATOM   6132 C CA  . MET B 2 246 ? 6.567   -56.108 21.142  1.00 106.50 ? 246  MET B CA  1 
ATOM   6133 C C   . MET B 2 246 ? 6.131   -57.268 20.231  1.00 105.28 ? 246  MET B C   1 
ATOM   6134 O O   . MET B 2 246 ? 5.998   -57.099 19.012  1.00 95.59  ? 246  MET B O   1 
ATOM   6135 C CB  . MET B 2 246 ? 8.038   -55.758 20.877  1.00 84.97  ? 246  MET B CB  1 
ATOM   6136 C CG  . MET B 2 246 ? 8.277   -54.904 19.645  1.00 92.92  ? 246  MET B CG  1 
ATOM   6137 S SD  . MET B 2 246 ? 7.496   -53.270 19.697  1.00 104.66 ? 246  MET B SD  1 
ATOM   6138 C CE  . MET B 2 246 ? 8.787   -52.270 20.426  1.00 63.05  ? 246  MET B CE  1 
ATOM   6139 N N   . ILE B 2 247 ? 5.908   -58.441 20.829  1.00 106.26 ? 247  ILE B N   1 
ATOM   6140 C CA  . ILE B 2 247 ? 5.591   -59.663 20.077  1.00 102.46 ? 247  ILE B CA  1 
ATOM   6141 C C   . ILE B 2 247 ? 4.255   -59.616 19.313  1.00 93.05  ? 247  ILE B C   1 
ATOM   6142 O O   . ILE B 2 247 ? 4.117   -60.245 18.257  1.00 95.19  ? 247  ILE B O   1 
ATOM   6143 C CB  . ILE B 2 247 ? 5.662   -60.938 20.975  1.00 99.63  ? 247  ILE B CB  1 
ATOM   6144 C CG1 . ILE B 2 247 ? 5.353   -62.203 20.160  1.00 97.58  ? 247  ILE B CG1 1 
ATOM   6145 C CG2 . ILE B 2 247 ? 4.718   -60.822 22.164  1.00 91.22  ? 247  ILE B CG2 1 
ATOM   6146 C CD1 . ILE B 2 247 ? 5.963   -63.470 20.739  1.00 90.68  ? 247  ILE B CD1 1 
ATOM   6147 N N   . ASP B 2 248 ? 3.281   -58.876 19.835  1.00 72.89  ? 248  ASP B N   1 
ATOM   6148 C CA  . ASP B 2 248 ? 2.019   -58.701 19.129  1.00 79.32  ? 248  ASP B CA  1 
ATOM   6149 C C   . ASP B 2 248 ? 2.160   -57.898 17.832  1.00 77.76  ? 248  ASP B C   1 
ATOM   6150 O O   . ASP B 2 248 ? 1.188   -57.717 17.101  1.00 78.91  ? 248  ASP B O   1 
ATOM   6151 C CB  . ASP B 2 248 ? 0.966   -58.051 20.027  1.00 92.01  ? 248  ASP B CB  1 
ATOM   6152 C CG  . ASP B 2 248 ? -0.452  -58.458 19.643  1.00 103.79 ? 248  ASP B CG  1 
ATOM   6153 O OD1 . ASP B 2 248 ? -0.612  -59.561 19.074  1.00 99.65  ? 248  ASP B OD1 1 
ATOM   6154 O OD2 . ASP B 2 248 ? -1.402  -57.687 19.912  1.00 112.61 ? 248  ASP B OD2 1 
ATOM   6155 N N   . ARG B 2 249 ? 3.362   -57.409 17.551  1.00 81.92  ? 249  ARG B N   1 
ATOM   6156 C CA  . ARG B 2 249 ? 3.608   -56.644 16.330  1.00 75.76  ? 249  ARG B CA  1 
ATOM   6157 C C   . ARG B 2 249 ? 4.076   -57.573 15.221  1.00 71.91  ? 249  ARG B C   1 
ATOM   6158 O O   . ARG B 2 249 ? 5.012   -58.350 15.420  1.00 76.17  ? 249  ARG B O   1 
ATOM   6159 C CB  . ARG B 2 249 ? 4.627   -55.532 16.596  1.00 77.72  ? 249  ARG B CB  1 
ATOM   6160 C CG  . ARG B 2 249 ? 3.991   -54.204 17.000  1.00 85.65  ? 249  ARG B CG  1 
ATOM   6161 C CD  . ARG B 2 249 ? 3.306   -53.543 15.801  1.00 91.88  ? 249  ARG B CD  1 
ATOM   6162 N NE  . ARG B 2 249 ? 2.236   -52.628 16.195  1.00 93.26  ? 249  ARG B NE  1 
ATOM   6163 C CZ  . ARG B 2 249 ? 1.547   -51.878 15.336  1.00 99.79  ? 249  ARG B CZ  1 
ATOM   6164 N NH1 . ARG B 2 249 ? 1.820   -51.936 14.033  1.00 100.35 ? 249  ARG B NH1 1 
ATOM   6165 N NH2 . ARG B 2 249 ? 0.590   -51.067 15.776  1.00 97.63  ? 249  ARG B NH2 1 
ATOM   6166 N N   . ILE B 2 250 ? 3.410   -57.522 14.067  1.00 74.16  ? 250  ILE B N   1 
ATOM   6167 C CA  . ILE B 2 250 ? 3.711   -58.473 12.992  1.00 77.17  ? 250  ILE B CA  1 
ATOM   6168 C C   . ILE B 2 250 ? 5.135   -58.258 12.521  1.00 92.60  ? 250  ILE B C   1 
ATOM   6169 O O   . ILE B 2 250 ? 5.958   -59.175 12.558  1.00 94.67  ? 250  ILE B O   1 
ATOM   6170 C CB  . ILE B 2 250 ? 2.770   -58.353 11.779  1.00 71.34  ? 250  ILE B CB  1 
ATOM   6171 C CG1 . ILE B 2 250 ? 1.310   -58.539 12.180  1.00 77.45  ? 250  ILE B CG1 1 
ATOM   6172 C CG2 . ILE B 2 250 ? 3.105   -59.405 10.745  1.00 81.36  ? 250  ILE B CG2 1 
ATOM   6173 C CD1 . ILE B 2 250 ? 0.356   -58.401 11.007  1.00 66.77  ? 250  ILE B CD1 1 
ATOM   6174 N N   . GLU B 2 251 ? 5.421   -57.030 12.097  1.00 99.93  ? 251  GLU B N   1 
ATOM   6175 C CA  . GLU B 2 251 ? 6.759   -56.655 11.659  1.00 90.73  ? 251  GLU B CA  1 
ATOM   6176 C C   . GLU B 2 251 ? 7.849   -57.266 12.536  1.00 88.93  ? 251  GLU B C   1 
ATOM   6177 O O   . GLU B 2 251 ? 8.883   -57.685 12.032  1.00 87.12  ? 251  GLU B O   1 
ATOM   6178 C CB  . GLU B 2 251 ? 6.900   -55.134 11.611  1.00 84.03  ? 251  GLU B CB  1 
ATOM   6179 C CG  . GLU B 2 251 ? 6.158   -54.481 10.456  1.00 98.96  ? 251  GLU B CG  1 
ATOM   6180 C CD  . GLU B 2 251 ? 6.928   -53.323 9.829   1.00 120.74 ? 251  GLU B CD  1 
ATOM   6181 O OE1 . GLU B 2 251 ? 7.439   -52.460 10.586  1.00 133.87 ? 251  GLU B OE1 1 
ATOM   6182 O OE2 . GLU B 2 251 ? 7.019   -53.273 8.576   1.00 118.08 ? 251  GLU B OE2 1 
ATOM   6183 N N   . PHE B 2 252 ? 7.619   -57.332 13.843  1.00 91.46  ? 252  PHE B N   1 
ATOM   6184 C CA  . PHE B 2 252 ? 8.643   -57.851 14.740  1.00 103.07 ? 252  PHE B CA  1 
ATOM   6185 C C   . PHE B 2 252 ? 8.884   -59.332 14.516  1.00 104.69 ? 252  PHE B C   1 
ATOM   6186 O O   . PHE B 2 252 ? 10.034  -59.762 14.438  1.00 115.75 ? 252  PHE B O   1 
ATOM   6187 C CB  . PHE B 2 252 ? 8.318   -57.585 16.213  1.00 120.59 ? 252  PHE B CB  1 
ATOM   6188 C CG  . PHE B 2 252 ? 9.282   -58.242 17.171  1.00 138.04 ? 252  PHE B CG  1 
ATOM   6189 C CD1 . PHE B 2 252 ? 10.614  -57.845 17.221  1.00 137.78 ? 252  PHE B CD1 1 
ATOM   6190 C CD2 . PHE B 2 252 ? 8.859   -59.261 18.019  1.00 148.22 ? 252  PHE B CD2 1 
ATOM   6191 C CE1 . PHE B 2 252 ? 11.508  -58.451 18.099  1.00 137.40 ? 252  PHE B CE1 1 
ATOM   6192 C CE2 . PHE B 2 252 ? 9.748   -59.869 18.902  1.00 148.65 ? 252  PHE B CE2 1 
ATOM   6193 C CZ  . PHE B 2 252 ? 11.076  -59.460 18.941  1.00 142.20 ? 252  PHE B CZ  1 
ATOM   6194 N N   . SER B 2 253 ? 7.811   -60.113 14.421  1.00 95.30  ? 253  SER B N   1 
ATOM   6195 C CA  . SER B 2 253 ? 7.949   -61.551 14.184  1.00 96.90  ? 253  SER B CA  1 
ATOM   6196 C C   . SER B 2 253 ? 8.742   -61.838 12.900  1.00 95.92  ? 253  SER B C   1 
ATOM   6197 O O   . SER B 2 253 ? 9.793   -62.476 12.944  1.00 96.59  ? 253  SER B O   1 
ATOM   6198 C CB  . SER B 2 253 ? 6.578   -62.245 14.142  1.00 98.17  ? 253  SER B CB  1 
ATOM   6199 O OG  . SER B 2 253 ? 6.697   -63.643 13.902  1.00 90.48  ? 253  SER B OG  1 
ATOM   6200 N N   . VAL B 2 254 ? 8.249   -61.347 11.765  1.00 90.35  ? 254  VAL B N   1 
ATOM   6201 C CA  . VAL B 2 254 ? 8.865   -61.643 10.466  1.00 87.05  ? 254  VAL B CA  1 
ATOM   6202 C C   . VAL B 2 254 ? 10.283  -61.068 10.273  1.00 89.03  ? 254  VAL B C   1 
ATOM   6203 O O   . VAL B 2 254 ? 10.957  -61.387 9.299   1.00 87.87  ? 254  VAL B O   1 
ATOM   6204 C CB  . VAL B 2 254 ? 7.902   -61.303 9.286   1.00 85.67  ? 254  VAL B CB  1 
ATOM   6205 C CG1 . VAL B 2 254 ? 7.009   -60.144 9.644   1.00 90.79  ? 254  VAL B CG1 1 
ATOM   6206 C CG2 . VAL B 2 254 ? 8.654   -61.064 7.972   1.00 61.66  ? 254  VAL B CG2 1 
ATOM   6207 N N   . GLU B 2 255 ? 10.743  -60.249 11.215  1.00 100.52 ? 255  GLU B N   1 
ATOM   6208 C CA  . GLU B 2 255 ? 12.120  -59.763 11.199  1.00 105.61 ? 255  GLU B CA  1 
ATOM   6209 C C   . GLU B 2 255 ? 13.085  -60.829 11.725  1.00 101.98 ? 255  GLU B C   1 
ATOM   6210 O O   . GLU B 2 255 ? 14.228  -60.914 11.282  1.00 104.48 ? 255  GLU B O   1 
ATOM   6211 C CB  . GLU B 2 255 ? 12.260  -58.488 12.032  1.00 119.32 ? 255  GLU B CB  1 
ATOM   6212 C CG  . GLU B 2 255 ? 13.708  -58.033 12.235  1.00 133.36 ? 255  GLU B CG  1 
ATOM   6213 C CD  . GLU B 2 255 ? 13.943  -57.357 13.584  1.00 140.70 ? 255  GLU B CD  1 
ATOM   6214 O OE1 . GLU B 2 255 ? 13.033  -57.398 14.443  1.00 144.66 ? 255  GLU B OE1 1 
ATOM   6215 O OE2 . GLU B 2 255 ? 15.043  -56.793 13.787  1.00 139.11 ? 255  GLU B OE2 1 
ATOM   6216 N N   . GLN B 2 256 ? 12.625  -61.644 12.667  1.00 95.41  ? 256  GLN B N   1 
ATOM   6217 C CA  . GLN B 2 256 ? 13.471  -62.700 13.221  1.00 106.73 ? 256  GLN B CA  1 
ATOM   6218 C C   . GLN B 2 256 ? 13.315  -64.055 12.505  1.00 111.63 ? 256  GLN B C   1 
ATOM   6219 O O   . GLN B 2 256 ? 13.381  -65.111 13.137  1.00 119.84 ? 256  GLN B O   1 
ATOM   6220 C CB  . GLN B 2 256 ? 13.229  -62.848 14.729  1.00 110.78 ? 256  GLN B CB  1 
ATOM   6221 C CG  . GLN B 2 256 ? 11.762  -62.946 15.122  1.00 114.94 ? 256  GLN B CG  1 
ATOM   6222 C CD  . GLN B 2 256 ? 11.557  -63.103 16.616  1.00 119.49 ? 256  GLN B CD  1 
ATOM   6223 O OE1 . GLN B 2 256 ? 12.508  -63.292 17.369  1.00 121.55 ? 256  GLN B OE1 1 
ATOM   6224 N NE2 . GLN B 2 256 ? 10.305  -63.029 17.052  1.00 127.12 ? 256  GLN B NE2 1 
ATOM   6225 N N   . SER B 2 257 ? 13.121  -64.015 11.188  1.00 103.00 ? 257  SER B N   1 
ATOM   6226 C CA  . SER B 2 257 ? 12.972  -65.222 10.376  1.00 101.78 ? 257  SER B CA  1 
ATOM   6227 C C   . SER B 2 257 ? 14.323  -65.795 9.981   1.00 114.48 ? 257  SER B C   1 
ATOM   6228 O O   . SER B 2 257 ? 15.327  -65.085 10.009  1.00 120.43 ? 257  SER B O   1 
ATOM   6229 C CB  . SER B 2 257 ? 12.200  -64.898 9.106   1.00 92.54  ? 257  SER B CB  1 
ATOM   6230 O OG  . SER B 2 257 ? 11.236  -63.905 9.367   1.00 89.61  ? 257  SER B OG  1 
ATOM   6231 N N   . HIS B 2 258 ? 14.348  -67.070 9.595   1.00 119.47 ? 258  HIS B N   1 
ATOM   6232 C CA  . HIS B 2 258 ? 15.606  -67.710 9.225   1.00 132.39 ? 258  HIS B CA  1 
ATOM   6233 C C   . HIS B 2 258 ? 15.734  -67.903 7.721   1.00 146.88 ? 258  HIS B C   1 
ATOM   6234 O O   . HIS B 2 258 ? 14.985  -67.307 6.949   1.00 146.36 ? 258  HIS B O   1 
ATOM   6235 C CB  . HIS B 2 258 ? 15.787  -69.043 9.948   1.00 135.40 ? 258  HIS B CB  1 
ATOM   6236 C CG  . HIS B 2 258 ? 17.216  -69.368 10.245  1.00 141.21 ? 258  HIS B CG  1 
ATOM   6237 N ND1 . HIS B 2 258 ? 18.115  -69.734 9.268   1.00 144.54 ? 258  HIS B ND1 1 
ATOM   6238 C CD2 . HIS B 2 258 ? 17.905  -69.369 11.410  1.00 147.11 ? 258  HIS B CD2 1 
ATOM   6239 C CE1 . HIS B 2 258 ? 19.295  -69.954 9.819   1.00 149.98 ? 258  HIS B CE1 1 
ATOM   6240 N NE2 . HIS B 2 258 ? 19.195  -69.740 11.118  1.00 151.69 ? 258  HIS B NE2 1 
ATOM   6241 N N   . ASN B 2 259 ? 16.685  -68.738 7.313   1.00 162.32 ? 259  ASN B N   1 
ATOM   6242 C CA  . ASN B 2 259 ? 16.977  -68.918 5.899   1.00 177.28 ? 259  ASN B CA  1 
ATOM   6243 C C   . ASN B 2 259 ? 18.012  -70.013 5.635   1.00 198.34 ? 259  ASN B C   1 
ATOM   6244 O O   . ASN B 2 259 ? 18.341  -70.799 6.524   1.00 197.66 ? 259  ASN B O   1 
ATOM   6245 C CB  . ASN B 2 259 ? 17.467  -67.592 5.311   1.00 168.33 ? 259  ASN B CB  1 
ATOM   6246 C CG  . ASN B 2 259 ? 17.263  -67.507 3.818   1.00 165.22 ? 259  ASN B CG  1 
ATOM   6247 O OD1 . ASN B 2 259 ? 16.453  -68.241 3.248   1.00 176.14 ? 259  ASN B OD1 1 
ATOM   6248 N ND2 . ASN B 2 259 ? 17.994  -66.606 3.171   1.00 151.58 ? 259  ASN B ND2 1 
ATOM   6249 N N   . TYR B 2 260 ? 18.502  -70.059 4.397   1.00 217.65 ? 260  TYR B N   1 
ATOM   6250 C CA  . TYR B 2 260 ? 19.648  -70.888 4.008   1.00 226.92 ? 260  TYR B CA  1 
ATOM   6251 C C   . TYR B 2 260 ? 19.345  -72.384 3.941   1.00 220.43 ? 260  TYR B C   1 
ATOM   6252 O O   . TYR B 2 260 ? 20.260  -73.200 3.836   1.00 219.70 ? 260  TYR B O   1 
ATOM   6253 C CB  . TYR B 2 260 ? 20.845  -70.617 4.932   1.00 241.64 ? 260  TYR B CB  1 
ATOM   6254 C CG  . TYR B 2 260 ? 22.162  -71.213 4.468   1.00 255.00 ? 260  TYR B CG  1 
ATOM   6255 C CD1 . TYR B 2 260 ? 22.741  -72.280 5.145   1.00 260.17 ? 260  TYR B CD1 1 
ATOM   6256 C CD2 . TYR B 2 260 ? 22.829  -70.702 3.360   1.00 260.66 ? 260  TYR B CD2 1 
ATOM   6257 C CE1 . TYR B 2 260 ? 23.946  -72.824 4.729   1.00 264.15 ? 260  TYR B CE1 1 
ATOM   6258 C CE2 . TYR B 2 260 ? 24.035  -71.241 2.937   1.00 264.55 ? 260  TYR B CE2 1 
ATOM   6259 C CZ  . TYR B 2 260 ? 24.587  -72.301 3.626   1.00 265.46 ? 260  TYR B CZ  1 
ATOM   6260 O OH  . TYR B 2 260 ? 25.784  -72.840 3.210   1.00 265.04 ? 260  TYR B OH  1 
ATOM   6261 N N   . VAL B 2 261 ? 18.065  -72.739 3.987   1.00 214.26 ? 261  VAL B N   1 
ATOM   6262 C CA  . VAL B 2 261 ? 17.669  -74.141 3.957   1.00 214.22 ? 261  VAL B CA  1 
ATOM   6263 C C   . VAL B 2 261 ? 18.130  -74.855 5.223   1.00 217.08 ? 261  VAL B C   1 
ATOM   6264 O O   . VAL B 2 261 ? 19.312  -75.164 5.379   1.00 218.56 ? 261  VAL B O   1 
ATOM   6265 C CB  . VAL B 2 261 ? 18.249  -74.876 2.726   1.00 211.18 ? 261  VAL B CB  1 
ATOM   6266 C CG1 . VAL B 2 261 ? 17.914  -76.362 2.780   1.00 210.25 ? 261  VAL B CG1 1 
ATOM   6267 C CG2 . VAL B 2 261 ? 17.741  -74.246 1.436   1.00 209.01 ? 261  VAL B CG2 1 
HETATM 6268 O O   . HOH C 3 .   ? -17.130 -57.437 4.024   1.00 70.68  ? 2001 HOH A O   1 
HETATM 6269 O O   . HOH C 3 .   ? -7.283  -74.124 12.767  1.00 61.10  ? 2002 HOH A O   1 
HETATM 6270 O O   . HOH C 3 .   ? 1.279   -55.551 13.504  1.00 61.84  ? 2003 HOH A O   1 
HETATM 6271 O O   . HOH C 3 .   ? 0.176   -45.326 13.703  1.00 83.04  ? 2004 HOH A O   1 
HETATM 6272 O O   . HOH C 3 .   ? -4.085  -38.352 14.731  1.00 70.95  ? 2005 HOH A O   1 
HETATM 6273 O O   . HOH C 3 .   ? -5.420  -44.619 14.351  1.00 50.21  ? 2006 HOH A O   1 
HETATM 6274 O O   . HOH C 3 .   ? 9.970   -38.843 5.980   1.00 86.04  ? 2007 HOH A O   1 
HETATM 6275 O O   . HOH C 3 .   ? 15.835  -37.663 -14.287 1.00 96.47  ? 2008 HOH A O   1 
HETATM 6276 O O   . HOH C 3 .   ? 1.890   -53.827 -12.717 1.00 97.47  ? 2009 HOH A O   1 
HETATM 6277 O O   . HOH C 3 .   ? 6.274   -31.803 -10.497 1.00 79.31  ? 2010 HOH A O   1 
HETATM 6278 O O   . HOH C 3 .   ? -24.172 -36.321 -6.678  1.00 97.48  ? 2011 HOH A O   1 
HETATM 6279 O O   . HOH C 3 .   ? 3.624   -15.371 7.055   1.00 83.45  ? 2012 HOH A O   1 
HETATM 6280 O O   . HOH C 3 .   ? 12.472  -28.361 19.385  1.00 63.59  ? 2013 HOH A O   1 
HETATM 6281 O O   . HOH C 3 .   ? 0.770   -23.915 15.579  1.00 67.79  ? 2014 HOH A O   1 
HETATM 6282 O O   . HOH C 3 .   ? -1.942  -25.889 13.870  1.00 65.29  ? 2015 HOH A O   1 
HETATM 6283 O O   . HOH C 3 .   ? -0.246  -25.692 19.254  1.00 61.45  ? 2016 HOH A O   1 
HETATM 6284 O O   . HOH C 3 .   ? -1.839  -34.909 15.468  1.00 46.38  ? 2017 HOH A O   1 
HETATM 6285 O O   . HOH C 3 .   ? 4.586   -32.337 14.412  1.00 50.53  ? 2018 HOH A O   1 
HETATM 6286 O O   . HOH C 3 .   ? 6.333   -29.143 19.190  1.00 62.05  ? 2019 HOH A O   1 
HETATM 6287 O O   . HOH C 3 .   ? 5.359   -29.689 16.128  1.00 46.20  ? 2020 HOH A O   1 
HETATM 6288 O O   . HOH C 3 .   ? 10.568  -32.410 14.707  1.00 54.91  ? 2021 HOH A O   1 
HETATM 6289 O O   . HOH C 3 .   ? 10.518  -38.811 16.401  1.00 65.09  ? 2022 HOH A O   1 
HETATM 6290 O O   . HOH C 3 .   ? 6.281   -43.252 11.270  1.00 73.81  ? 2023 HOH A O   1 
HETATM 6291 O O   . HOH C 3 .   ? -1.507  -43.147 16.082  1.00 81.20  ? 2024 HOH A O   1 
HETATM 6292 O O   . HOH C 3 .   ? -1.985  -33.581 17.783  1.00 57.50  ? 2025 HOH A O   1 
HETATM 6293 O O   . HOH C 3 .   ? -7.922  -40.089 18.423  1.00 62.70  ? 2026 HOH A O   1 
HETATM 6294 O O   . HOH C 3 .   ? -7.656  -36.294 20.811  1.00 67.25  ? 2027 HOH A O   1 
HETATM 6295 O O   . HOH C 3 .   ? 1.918   -36.510 34.538  1.00 63.26  ? 2028 HOH A O   1 
HETATM 6296 O O   . HOH C 3 .   ? -6.211  -51.208 28.054  1.00 75.08  ? 2029 HOH A O   1 
HETATM 6297 O O   . HOH C 3 .   ? 1.225   -27.974 30.988  1.00 96.73  ? 2030 HOH A O   1 
HETATM 6298 O O   . HOH C 3 .   ? 3.928   -26.166 28.212  1.00 76.65  ? 2031 HOH A O   1 
HETATM 6299 O O   . HOH C 3 .   ? 4.935   -22.399 16.507  1.00 39.37  ? 2032 HOH A O   1 
HETATM 6300 O O   . HOH C 3 .   ? 25.451  -16.492 20.013  1.00 82.65  ? 2033 HOH A O   1 
HETATM 6301 O O   . HOH C 3 .   ? 19.972  -29.275 15.395  1.00 55.57  ? 2034 HOH A O   1 
HETATM 6302 O O   . HOH C 3 .   ? 15.917  -29.253 18.867  1.00 55.63  ? 2035 HOH A O   1 
HETATM 6303 O O   . HOH C 3 .   ? 23.801  -23.538 17.105  1.00 83.40  ? 2036 HOH A O   1 
HETATM 6304 O O   . HOH C 3 .   ? 9.435   -8.387  0.073   1.00 72.64  ? 2037 HOH A O   1 
HETATM 6305 O O   . HOH C 3 .   ? 9.357   -8.200  3.114   1.00 84.33  ? 2038 HOH A O   1 
HETATM 6306 O O   . HOH C 3 .   ? 10.480  -20.235 -6.230  1.00 104.97 ? 2039 HOH A O   1 
HETATM 6307 O O   . HOH C 3 .   ? 14.417  -17.262 -4.453  1.00 87.10  ? 2040 HOH A O   1 
HETATM 6308 O O   . HOH C 3 .   ? 3.529   -21.182 2.109   1.00 51.53  ? 2041 HOH A O   1 
HETATM 6309 O O   . HOH C 3 .   ? -6.122  -21.676 20.360  1.00 86.55  ? 2042 HOH A O   1 
HETATM 6310 O O   . HOH C 3 .   ? -15.885 -26.202 -3.645  1.00 81.85  ? 2043 HOH A O   1 
HETATM 6311 O O   . HOH C 3 .   ? -8.599  -31.549 17.688  1.00 70.94  ? 2044 HOH A O   1 
HETATM 6312 O O   . HOH C 3 .   ? 4.951   -42.211 8.437   1.00 56.12  ? 2045 HOH A O   1 
HETATM 6313 O O   . HOH C 3 .   ? 11.874  -36.665 13.668  1.00 56.38  ? 2046 HOH A O   1 
HETATM 6314 O O   . HOH D 3 .   ? -10.318 -66.350 -8.660  1.00 89.64  ? 2001 HOH B O   1 
HETATM 6315 O O   . HOH D 3 .   ? -4.531  -85.558 23.601  1.00 65.42  ? 2002 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . HIS A 1   ? 1.5749 1.5048 1.4002 -0.6397 -0.1058 0.0947  0   HIS A N   
2    C CA  . HIS A 1   ? 1.6731 1.5856 1.4908 -0.6300 -0.0855 0.0888  0   HIS A CA  
3    C C   . HIS A 1   ? 1.6776 1.6089 1.5193 -0.6080 -0.0723 0.0894  0   HIS A C   
4    O O   . HIS A 1   ? 1.7987 1.7170 1.6331 -0.5944 -0.0550 0.0870  0   HIS A O   
5    C CB  . HIS A 1   ? 1.7165 1.6011 1.4901 -0.6302 -0.0788 0.0741  0   HIS A CB  
6    C CG  . HIS A 1   ? 1.7171 1.5709 1.4635 -0.6485 -0.0825 0.0712  0   HIS A CG  
7    N ND1 . HIS A 1   ? 1.7160 1.5625 1.4458 -0.6676 -0.1005 0.0707  0   HIS A ND1 
8    C CD2 . HIS A 1   ? 1.6633 1.4908 1.3926 -0.6470 -0.0708 0.0682  0   HIS A CD2 
9    C CE1 . HIS A 1   ? 1.8357 1.6518 1.5434 -0.6811 -0.1010 0.0661  0   HIS A CE1 
10   N NE2 . HIS A 1   ? 1.8002 1.6052 1.5078 -0.6681 -0.0827 0.0649  0   HIS A NE2 
11   N N   . MET A 2   ? 1.4368 1.3972 1.3012 -0.5995 -0.0807 0.0924  1   MET A N   
12   C CA  . MET A 2   ? 1.3817 1.3600 1.2681 -0.5784 -0.0712 0.0903  1   MET A CA  
13   C C   . MET A 2   ? 1.1411 1.1118 1.0031 -0.5610 -0.0645 0.0746  1   MET A C   
14   O O   . MET A 2   ? 1.0959 1.0853 0.9717 -0.5539 -0.0710 0.0706  1   MET A O   
15   C CB  . MET A 2   ? 1.4472 1.4230 1.3516 -0.5703 -0.0555 0.0975  1   MET A CB  
16   C CG  . MET A 2   ? 1.4589 1.4554 1.4057 -0.5781 -0.0608 0.1134  1   MET A CG  
17   S SD  . MET A 2   ? 2.3400 2.3752 2.3240 -0.5653 -0.0713 0.1168  1   MET A SD  
18   C CE  . MET A 2   ? 1.5517 1.5866 1.5313 -0.5376 -0.0539 0.1056  1   MET A CE  
19   N N   . SER A 3   ? 1.0679 1.0114 0.8943 -0.5509 -0.0521 0.0659  2   SER A N   
20   C CA  . SER A 3   ? 1.0764 1.0106 0.8778 -0.5315 -0.0467 0.0506  2   SER A CA  
21   C C   . SER A 3   ? 1.1831 1.0938 0.9483 -0.5435 -0.0480 0.0426  2   SER A C   
22   O O   . SER A 3   ? 1.1731 1.0613 0.9170 -0.5576 -0.0456 0.0448  2   SER A O   
23   C CB  . SER A 3   ? 1.0804 1.0007 0.8668 -0.5058 -0.0313 0.0451  2   SER A CB  
24   O OG  . SER A 3   ? 1.0686 0.9660 0.8195 -0.4957 -0.0256 0.0314  2   SER A OG  
25   N N   . LEU A 4   ? 1.1049 1.0204 0.8652 -0.5369 -0.0511 0.0333  3   LEU A N   
26   C CA  . LEU A 4   ? 1.0795 0.9742 0.8066 -0.5458 -0.0506 0.0255  3   LEU A CA  
27   C C   . LEU A 4   ? 1.1358 1.0008 0.8286 -0.5341 -0.0373 0.0154  3   LEU A C   
28   O O   . LEU A 4   ? 1.2355 1.0760 0.8963 -0.5452 -0.0349 0.0110  3   LEU A O   
29   C CB  . LEU A 4   ? 1.1753 1.0838 0.9125 -0.5377 -0.0535 0.0189  3   LEU A CB  
30   C CG  . LEU A 4   ? 1.0845 1.0240 0.8587 -0.5454 -0.0657 0.0284  3   LEU A CG  
31   C CD1 . LEU A 4   ? 0.9852 0.9394 0.7786 -0.5288 -0.0648 0.0205  3   LEU A CD1 
32   C CD2 . LEU A 4   ? 1.1342 1.0689 0.8958 -0.5716 -0.0753 0.0369  3   LEU A CD2 
33   N N   . LYS A 5   ? 1.1481 1.0141 0.8462 -0.5107 -0.0290 0.0114  4   LYS A N   
34   C CA  . LYS A 5   ? 1.0907 0.9280 0.7571 -0.4983 -0.0164 0.0036  4   LYS A CA  
35   C C   . LYS A 5   ? 1.1792 0.9981 0.8331 -0.5135 -0.0117 0.0128  4   LYS A C   
36   O O   . LYS A 5   ? 1.2663 1.0572 0.8895 -0.5183 -0.0052 0.0078  4   LYS A O   
37   C CB  . LYS A 5   ? 0.8878 0.7290 0.5597 -0.4676 -0.0102 -0.0027 4   LYS A CB  
38   C CG  . LYS A 5   ? 0.9667 0.8107 0.6390 -0.4489 -0.0121 -0.0176 4   LYS A CG  
39   C CD  . LYS A 5   ? 1.0645 0.9163 0.7478 -0.4189 -0.0112 -0.0230 4   LYS A CD  
40   C CE  . LYS A 5   ? 1.0390 0.9030 0.7398 -0.4014 -0.0183 -0.0364 4   LYS A CE  
41   N NZ  . LYS A 5   ? 1.1424 0.9822 0.8178 -0.3874 -0.0125 -0.0500 4   LYS A NZ  
42   N N   . SER A 6   ? 1.1437 0.9784 0.8250 -0.5214 -0.0148 0.0262  5   SER A N   
43   C CA  . SER A 6   ? 1.1771 0.9971 0.8567 -0.5384 -0.0117 0.0363  5   SER A CA  
44   C C   . SER A 6   ? 1.2824 1.0894 0.9463 -0.5649 -0.0221 0.0350  5   SER A C   
45   O O   . SER A 6   ? 1.3516 1.1318 0.9933 -0.5743 -0.0178 0.0335  5   SER A O   
46   C CB  . SER A 6   ? 1.1021 0.9449 0.8217 -0.5442 -0.0147 0.0515  5   SER A CB  
47   O OG  . SER A 6   ? 1.2271 1.0821 0.9596 -0.5189 -0.0056 0.0528  5   SER A OG  
48   N N   . ALA A 7   ? 1.2127 1.0374 0.8870 -0.5760 -0.0360 0.0355  6   ALA A N   
49   C CA  . ALA A 7   ? 1.2225 1.0352 0.8792 -0.6000 -0.0477 0.0349  6   ALA A CA  
50   C C   . ALA A 7   ? 1.3243 1.1058 0.9364 -0.5979 -0.0403 0.0214  6   ALA A C   
51   O O   . ALA A 7   ? 1.3603 1.1173 0.9500 -0.6134 -0.0427 0.0198  6   ALA A O   
52   C CB  . ALA A 7   ? 1.1091 0.9456 0.7817 -0.6079 -0.0616 0.0382  6   ALA A CB  
53   N N   . VAL A 8   ? 1.2490 1.0311 0.8505 -0.5783 -0.0318 0.0112  7   VAL A N   
54   C CA  . VAL A 8   ? 1.2316 0.9853 0.7943 -0.5744 -0.0232 -0.0017 7   VAL A CA  
55   C C   . VAL A 8   ? 1.3137 1.0402 0.8574 -0.5690 -0.0115 -0.0047 7   VAL A C   
56   O O   . VAL A 8   ? 1.2788 0.9770 0.7911 -0.5780 -0.0087 -0.0114 7   VAL A O   
57   C CB  . VAL A 8   ? 1.0290 0.7916 0.5927 -0.5543 -0.0173 -0.0116 7   VAL A CB  
58   C CG1 . VAL A 8   ? 0.9210 0.6543 0.4498 -0.5460 -0.0056 -0.0249 7   VAL A CG1 
59   C CG2 . VAL A 8   ? 1.0859 0.8667 0.6603 -0.5640 -0.0271 -0.0086 7   VAL A CG2 
60   N N   . LYS A 9   ? 1.2130 0.9469 0.7749 -0.5542 -0.0041 0.0006  8   LYS A N   
61   C CA  . LYS A 9   ? 1.2883 0.9964 0.8335 -0.5477 0.0087  -0.0001 8   LYS A CA  
62   C C   . LYS A 9   ? 1.4635 1.1560 1.0071 -0.5725 0.0040  0.0071  8   LYS A C   
63   O O   . LYS A 9   ? 1.4572 1.1204 0.9778 -0.5755 0.0114  0.0029  8   LYS A O   
64   C CB  . LYS A 9   ? 1.1859 0.9038 0.7485 -0.5256 0.0185  0.0060  8   LYS A CB  
65   C CG  . LYS A 9   ? 1.1842 0.8729 0.7233 -0.5119 0.0345  0.0038  8   LYS A CG  
66   C CD  . LYS A 9   ? 1.3724 1.0673 0.9270 -0.4946 0.0450  0.0145  8   LYS A CD  
67   C CE  . LYS A 9   ? 1.5590 1.2800 1.1295 -0.4726 0.0417  0.0121  8   LYS A CE  
68   N NZ  . LYS A 9   ? 1.5103 1.2351 1.0897 -0.4519 0.0527  0.0212  8   LYS A NZ  
69   N N   . THR A 10  ? 1.4133 1.1253 0.9839 -0.5902 -0.0094 0.0174  9   THR A N   
70   C CA  . THR A 10  ? 1.3943 1.0944 0.9712 -0.6145 -0.0178 0.0242  9   THR A CA  
71   C C   . THR A 10  ? 1.2904 0.9635 0.8311 -0.6309 -0.0258 0.0136  9   THR A C   
72   O O   . THR A 10  ? 1.2719 0.9199 0.8026 -0.6423 -0.0253 0.0125  9   THR A O   
73   C CB  . THR A 10  ? 1.3438 1.0720 0.9603 -0.6290 -0.0327 0.0372  9   THR A CB  
74   O OG1 . THR A 10  ? 1.3222 1.0722 0.9712 -0.6132 -0.0233 0.0471  9   THR A OG1 
75   C CG2 . THR A 10  ? 1.3344 1.0493 0.9615 -0.6537 -0.0435 0.0434  9   THR A CG2 
76   N N   . VAL A 11  ? 1.2016 0.8787 0.7229 -0.6311 -0.0319 0.0057  10  VAL A N   
77   C CA  . VAL A 11  ? 1.3260 0.9762 0.8068 -0.6428 -0.0368 -0.0054 10  VAL A CA  
78   C C   . VAL A 11  ? 1.4724 1.0917 0.9220 -0.6318 -0.0208 -0.0168 10  VAL A C   
79   O O   . VAL A 11  ? 1.5175 1.1070 0.9387 -0.6439 -0.0231 -0.0241 10  VAL A O   
80   C CB  . VAL A 11  ? 1.3096 0.9706 0.7765 -0.6397 -0.0406 -0.0104 10  VAL A CB  
81   C CG1 . VAL A 11  ? 1.2805 0.9104 0.7010 -0.6499 -0.0429 -0.0216 10  VAL A CG1 
82   C CG2 . VAL A 11  ? 1.2559 0.9475 0.7526 -0.6496 -0.0566 0.0011  10  VAL A CG2 
83   N N   . LEU A 12  ? 1.3908 1.0165 0.8453 -0.6080 -0.0056 -0.0191 11  LEU A N   
84   C CA  . LEU A 12  ? 1.3277 0.9262 0.7564 -0.5946 0.0100  -0.0289 11  LEU A CA  
85   C C   . LEU A 12  ? 1.3718 0.9510 0.8046 -0.6005 0.0149  -0.0234 11  LEU A C   
86   O O   . LEU A 12  ? 1.3484 0.8966 0.7554 -0.6035 0.0210  -0.0311 11  LEU A O   
87   C CB  . LEU A 12  ? 1.2648 0.8765 0.7017 -0.5667 0.0217  -0.0317 11  LEU A CB  
88   C CG  . LEU A 12  ? 1.2707 0.8563 0.6843 -0.5494 0.0373  -0.0409 11  LEU A CG  
89   C CD1 . LEU A 12  ? 1.3154 0.8783 0.6956 -0.5528 0.0399  -0.0549 11  LEU A CD1 
90   C CD2 . LEU A 12  ? 1.2147 0.8152 0.6416 -0.5210 0.0449  -0.0417 11  LEU A CD2 
91   N N   . THR A 13  ? 1.3241 0.9218 0.7918 -0.6017 0.0136  -0.0094 12  THR A N   
92   C CA  . THR A 13  ? 1.4120 0.9943 0.8914 -0.6059 0.0208  -0.0013 12  THR A CA  
93   C C   . THR A 13  ? 1.5311 1.0962 1.0090 -0.6337 0.0070  -0.0017 12  THR A C   
94   O O   . THR A 13  ? 1.5496 1.0850 1.0133 -0.6390 0.0123  -0.0058 12  THR A O   
95   C CB  . THR A 13  ? 1.3950 1.0021 0.9147 -0.5992 0.0248  0.0149  12  THR A CB  
96   O OG1 . THR A 13  ? 1.3598 0.9775 0.8768 -0.5708 0.0377  0.0140  12  THR A OG1 
97   C CG2 . THR A 13  ? 1.2799 0.8703 0.8166 -0.6067 0.0331  0.0254  12  THR A CG2 
98   N N   . ASN A 14  ? 1.5327 1.1157 1.0256 -0.6509 -0.0119 0.0022  13  ASN A N   
99   C CA  . ASN A 14  ? 1.4692 1.0368 0.9596 -0.6771 -0.0300 0.0005  13  ASN A CA  
100  C C   . ASN A 14  ? 1.4515 0.9855 0.8936 -0.6819 -0.0315 -0.0162 13  ASN A C   
101  O O   . ASN A 14  ? 1.6984 1.2081 1.1322 -0.6991 -0.0415 -0.0205 13  ASN A O   
102  C CB  . ASN A 14  ? 1.4148 1.0073 0.9231 -0.6915 -0.0514 0.0063  13  ASN A CB  
103  C CG  . ASN A 14  ? 1.4171 1.0389 0.9783 -0.6927 -0.0530 0.0233  13  ASN A CG  
104  O OD1 . ASN A 14  ? 1.2675 0.8889 0.8519 -0.6843 -0.0379 0.0317  13  ASN A OD1 
105  N ND2 . ASN A 14  ? 1.4671 1.1139 1.0474 -0.7024 -0.0702 0.0293  13  ASN A ND2 
106  N N   . SER A 15  ? 1.4467 0.9788 0.8586 -0.6663 -0.0219 -0.0260 14  SER A N   
107  C CA  . SER A 15  ? 1.5505 1.0508 0.9163 -0.6692 -0.0207 -0.0418 14  SER A CA  
108  C C   . SER A 15  ? 1.6014 1.0740 0.9550 -0.6594 -0.0034 -0.0474 14  SER A C   
109  O O   . SER A 15  ? 1.6710 1.1116 0.9998 -0.6697 -0.0058 -0.0569 14  SER A O   
110  C CB  . SER A 15  ? 1.5529 1.0620 0.8948 -0.6576 -0.0167 -0.0494 14  SER A CB  
111  O OG  . SER A 15  ? 1.4969 1.0226 0.8410 -0.6703 -0.0341 -0.0455 14  SER A OG  
112  N N   . LEU A 16  ? 1.6506 1.1344 1.0206 -0.6387 0.0133  -0.0416 15  LEU A N   
113  C CA  . LEU A 16  ? 1.5842 1.0427 0.9427 -0.6265 0.0307  -0.0452 15  LEU A CA  
114  C C   . LEU A 16  ? 1.5833 1.0238 0.9586 -0.6422 0.0283  -0.0387 15  LEU A C   
115  O O   . LEU A 16  ? 1.6822 1.0910 1.0392 -0.6445 0.0346  -0.0460 15  LEU A O   
116  C CB  . LEU A 16  ? 1.4066 0.8812 0.7778 -0.5995 0.0468  -0.0394 15  LEU A CB  
117  C CG  . LEU A 16  ? 1.3884 0.8549 0.7332 -0.5769 0.0591  -0.0515 15  LEU A CG  
118  C CD1 . LEU A 16  ? 1.4446 0.8940 0.7562 -0.5850 0.0550  -0.0667 15  LEU A CD1 
119  C CD2 . LEU A 16  ? 1.3447 0.8423 0.7058 -0.5566 0.0611  -0.0483 15  LEU A CD2 
120  N N   . ARG A 17  ? 1.6254 1.0862 1.0389 -0.6536 0.0188  -0.0249 16  ARG A N   
121  C CA  . ARG A 17  ? 1.6828 1.1305 1.1233 -0.6690 0.0162  -0.0167 16  ARG A CA  
122  C C   . ARG A 17  ? 1.7584 1.1880 1.1909 -0.6957 -0.0062 -0.0251 16  ARG A C   
123  O O   . ARG A 17  ? 1.8523 1.2732 1.3135 -0.7119 -0.0140 -0.0191 16  ARG A O   
124  C CB  . ARG A 17  ? 1.6516 1.1285 1.1411 -0.6679 0.0180  0.0026  16  ARG A CB  
125  C CG  . ARG A 17  ? 1.7324 1.2191 1.2258 -0.6402 0.0412  0.0105  16  ARG A CG  
126  C CD  . ARG A 17  ? 1.8456 1.3636 1.3816 -0.6358 0.0438  0.0281  16  ARG A CD  
127  N NE  . ARG A 17  ? 2.0365 1.5567 1.5699 -0.6077 0.0666  0.0348  16  ARG A NE  
128  C CZ  . ARG A 17  ? 2.1514 1.6959 1.7118 -0.5953 0.0743  0.0486  16  ARG A CZ  
129  N NH1 . ARG A 17  ? 2.1697 1.7111 1.7196 -0.5679 0.0943  0.0530  16  ARG A NH1 
130  N NH2 . ARG A 17  ? 2.1869 1.7574 1.7833 -0.6094 0.0616  0.0576  16  ARG A NH2 
131  N N   . SER A 18  ? 1.8140 1.2361 1.2070 -0.6991 -0.0163 -0.0393 17  SER A N   
132  C CA  . SER A 18  ? 1.8824 1.2822 1.2554 -0.7211 -0.0378 -0.0501 17  SER A CA  
133  C C   . SER A 18  ? 1.8541 1.2162 1.1817 -0.7173 -0.0293 -0.0671 17  SER A C   
134  O O   . SER A 18  ? 1.8487 1.1835 1.1534 -0.7329 -0.0440 -0.0788 17  SER A O   
135  C CB  . SER A 18  ? 1.9488 1.3657 1.3058 -0.7276 -0.0555 -0.0528 17  SER A CB  
136  O OG  . SER A 18  ? 2.0462 1.4972 1.4468 -0.7329 -0.0654 -0.0374 17  SER A OG  
137  N N   . VAL A 19  ? 1.8244 1.1845 1.1385 -0.6955 -0.0064 -0.0693 18  VAL A N   
138  C CA  . VAL A 19  ? 1.7840 1.1097 1.0580 -0.6897 0.0039  -0.0849 18  VAL A CA  
139  C C   . VAL A 19  ? 1.7228 1.0203 1.0101 -0.6995 0.0052  -0.0849 18  VAL A C   
140  O O   . VAL A 19  ? 1.6593 0.9625 0.9805 -0.6933 0.0171  -0.0720 18  VAL A O   
141  C CB  . VAL A 19  ? 1.3777 0.7100 0.6378 -0.6631 0.0263  -0.0871 18  VAL A CB  
142  C CG1 . VAL A 19  ? 1.3732 0.6702 0.6059 -0.6548 0.0412  -0.0990 18  VAL A CG1 
143  C CG2 . VAL A 19  ? 1.4765 0.8254 0.7149 -0.6580 0.0224  -0.0930 18  VAL A CG2 
144  N N   . ALA A 20  ? 1.7601 1.0265 1.0214 -0.7150 -0.0079 -0.0991 19  ALA A N   
145  C CA  . ALA A 20  ? 1.7050 0.9424 0.9805 -0.7263 -0.0095 -0.1011 19  ALA A CA  
146  C C   . ALA A 20  ? 1.7333 0.9406 0.9785 -0.7126 0.0104  -0.1122 19  ALA A C   
147  O O   . ALA A 20  ? 1.7405 0.9187 0.9453 -0.7171 0.0059  -0.1299 19  ALA A O   
148  C CB  . ALA A 20  ? 1.6570 0.8755 0.9240 -0.7508 -0.0379 -0.1113 19  ALA A CB  
149  N N   . ASP A 21  ? 1.8391 1.0531 1.1025 -0.6946 0.0328  -0.1017 20  ASP A N   
150  C CA  . ASP A 21  ? 1.8916 1.0781 1.1324 -0.6803 0.0524  -0.1098 20  ASP A CA  
151  C C   . ASP A 21  ? 1.8035 0.9719 1.0758 -0.6836 0.0611  -0.1007 20  ASP A C   
152  O O   . ASP A 21  ? 1.6290 0.8053 0.9410 -0.6985 0.0511  -0.0894 20  ASP A O   
153  C CB  . ASP A 21  ? 1.9715 1.1764 1.2030 -0.6533 0.0717  -0.1060 20  ASP A CB  
154  C CG  . ASP A 21  ? 2.0246 1.2596 1.2950 -0.6419 0.0803  -0.0853 20  ASP A CG  
155  O OD1 . ASP A 21  ? 1.9887 1.2325 1.2957 -0.6550 0.0733  -0.0725 20  ASP A OD1 
156  O OD2 . ASP A 21  ? 2.0282 1.2775 1.2930 -0.6189 0.0939  -0.0823 20  ASP A OD2 
157  N N   . GLY A 22  ? 1.8519 0.9951 1.1078 -0.6698 0.0796  -0.1057 21  GLY A N   
158  C CA  . GLY A 22  ? 1.8511 0.9819 1.1356 -0.6638 0.0961  -0.0930 21  GLY A CA  
159  C C   . GLY A 22  ? 2.0192 1.1765 1.3131 -0.6393 0.1138  -0.0775 21  GLY A C   
160  O O   . GLY A 22  ? 2.0717 1.2409 1.3386 -0.6227 0.1182  -0.0840 21  GLY A O   
161  N N   . GLY A 23  ? 1.8655 1.0310 1.1978 -0.6361 0.1241  -0.0574 22  GLY A N   
162  C CA  . GLY A 23  ? 1.7751 0.9708 1.1209 -0.6164 0.1355  -0.0411 22  GLY A CA  
163  C C   . GLY A 23  ? 1.6442 0.8397 0.9643 -0.5854 0.1542  -0.0408 22  GLY A C   
164  O O   . GLY A 23  ? 1.5977 0.8033 0.9321 -0.5676 0.1691  -0.0242 22  GLY A O   
165  N N   . ASP A 24  ? 1.5239 0.7073 0.8066 -0.5779 0.1533  -0.0588 23  ASP A N   
166  C CA  . ASP A 24  ? 1.6721 0.8547 0.9324 -0.5486 0.1679  -0.0606 23  ASP A CA  
167  C C   . ASP A 24  ? 1.7577 0.9757 1.0146 -0.5379 0.1604  -0.0621 23  ASP A C   
168  O O   . ASP A 24  ? 1.7451 0.9860 1.0151 -0.5537 0.1454  -0.0613 23  ASP A O   
169  C CB  . ASP A 24  ? 1.7521 0.9035 0.9797 -0.5452 0.1720  -0.0790 23  ASP A CB  
170  C CG  . ASP A 24  ? 1.8993 1.0308 1.1163 -0.5195 0.1918  -0.0747 23  ASP A CG  
171  O OD1 . ASP A 24  ? 1.8997 1.0468 1.1211 -0.4969 0.2004  -0.0630 23  ASP A OD1 
172  O OD2 . ASP A 24  ? 1.8696 0.9684 1.0723 -0.5212 0.1982  -0.0837 23  ASP A OD2 
173  N N   . TRP A 25  ? 1.7384 0.9604 0.9799 -0.5108 0.1697  -0.0641 24  TRP A N   
174  C CA  . TRP A 25  ? 1.5670 0.8203 0.8071 -0.4993 0.1623  -0.0676 24  TRP A CA  
175  C C   . TRP A 25  ? 1.5207 0.7788 0.7479 -0.5154 0.1486  -0.0836 24  TRP A C   
176  O O   . TRP A 25  ? 1.5327 0.7646 0.7413 -0.5273 0.1481  -0.0955 24  TRP A O   
177  C CB  . TRP A 25  ? 1.4511 0.7018 0.6757 -0.4674 0.1725  -0.0709 24  TRP A CB  
178  C CG  . TRP A 25  ? 1.4824 0.7341 0.7155 -0.4470 0.1843  -0.0542 24  TRP A CG  
179  C CD1 . TRP A 25  ? 1.4278 0.6515 0.6519 -0.4340 0.1998  -0.0474 24  TRP A CD1 
180  C CD2 . TRP A 25  ? 1.4210 0.7015 0.6710 -0.4359 0.1828  -0.0416 24  TRP A CD2 
181  N NE1 . TRP A 25  ? 1.3304 0.5627 0.5621 -0.4147 0.2088  -0.0308 24  TRP A NE1 
182  C CE2 . TRP A 25  ? 1.3463 0.6131 0.5935 -0.4154 0.1987  -0.0275 24  TRP A CE2 
183  C CE3 . TRP A 25  ? 1.2596 0.5751 0.5261 -0.4406 0.1701  -0.0408 24  TRP A CE3 
184  C CZ2 . TRP A 25  ? 1.3634 0.6491 0.6210 -0.3988 0.2027  -0.0132 24  TRP A CZ2 
185  C CZ3 . TRP A 25  ? 1.2550 0.5906 0.5352 -0.4251 0.1731  -0.0273 24  TRP A CZ3 
186  C CH2 . TRP A 25  ? 1.4180 0.7382 0.6924 -0.4041 0.1896  -0.0139 24  TRP A CH2 
187  N N   . LYS A 26  ? 1.4466 0.7367 0.6826 -0.5151 0.1384  -0.0833 25  LYS A N   
188  C CA  . LYS A 26  ? 1.3658 0.6623 0.5883 -0.5266 0.1276  -0.0966 25  LYS A CA  
189  C C   . LYS A 26  ? 1.4666 0.7754 0.6814 -0.5043 0.1314  -0.1053 25  LYS A C   
190  O O   . LYS A 26  ? 1.4177 0.7408 0.6438 -0.4819 0.1360  -0.0997 25  LYS A O   
191  C CB  . LYS A 26  ? 1.3634 0.6860 0.6043 -0.5463 0.1116  -0.0897 25  LYS A CB  
192  C CG  . LYS A 26  ? 1.4560 0.7691 0.7110 -0.5702 0.1041  -0.0817 25  LYS A CG  
193  C CD  . LYS A 26  ? 1.4128 0.7540 0.6888 -0.5876 0.0868  -0.0745 25  LYS A CD  
194  C CE  . LYS A 26  ? 1.5316 0.8866 0.8455 -0.5928 0.0863  -0.0561 25  LYS A CE  
195  N NZ  . LYS A 26  ? 1.5441 0.8783 0.8690 -0.6162 0.0792  -0.0538 25  LYS A NZ  
196  N N   . VAL A 27  ? 1.3695 0.6709 0.5653 -0.5095 0.1297  -0.1194 26  VAL A N   
197  C CA  . VAL A 27  ? 1.3612 0.6766 0.5566 -0.4918 0.1321  -0.1277 26  VAL A CA  
198  C C   . VAL A 27  ? 1.5037 0.8455 0.7070 -0.5035 0.1209  -0.1274 26  VAL A C   
199  O O   . VAL A 27  ? 1.5019 0.8344 0.6890 -0.5235 0.1154  -0.1320 26  VAL A O   
200  C CB  . VAL A 27  ? 1.4552 0.7425 0.6264 -0.4852 0.1426  -0.1432 26  VAL A CB  
201  C CG1 . VAL A 27  ? 1.5309 0.8344 0.7065 -0.4731 0.1438  -0.1517 26  VAL A CG1 
202  C CG2 . VAL A 27  ? 1.4933 0.7587 0.6604 -0.4671 0.1540  -0.1433 26  VAL A CG2 
203  N N   . LEU A 28  ? 1.4968 0.8704 0.7241 -0.4903 0.1168  -0.1219 27  LEU A N   
204  C CA  . LEU A 28  ? 1.4097 0.8107 0.6491 -0.4996 0.1065  -0.1197 27  LEU A CA  
205  C C   . LEU A 28  ? 1.4131 0.8160 0.6478 -0.4896 0.1118  -0.1313 27  LEU A C   
206  O O   . LEU A 28  ? 1.3542 0.7714 0.6069 -0.4682 0.1146  -0.1338 27  LEU A O   
207  C CB  . LEU A 28  ? 1.2790 0.7136 0.5501 -0.4919 0.0991  -0.1074 27  LEU A CB  
208  C CG  . LEU A 28  ? 1.3600 0.8260 0.6491 -0.5001 0.0880  -0.1036 27  LEU A CG  
209  C CD1 . LEU A 28  ? 1.3806 0.8396 0.6546 -0.5276 0.0797  -0.1027 27  LEU A CD1 
210  C CD2 . LEU A 28  ? 1.2787 0.7751 0.5991 -0.4935 0.0809  -0.0912 27  LEU A CD2 
211  N N   . VAL A 29  ? 1.4968 0.8835 0.7075 -0.5043 0.1134  -0.1386 28  VAL A N   
212  C CA  . VAL A 29  ? 1.6144 1.0019 0.8213 -0.4966 0.1210  -0.1480 28  VAL A CA  
213  C C   . VAL A 29  ? 1.5254 0.9433 0.7493 -0.5027 0.1127  -0.1417 28  VAL A C   
214  O O   . VAL A 29  ? 1.4944 0.9156 0.7088 -0.5226 0.1028  -0.1358 28  VAL A O   
215  C CB  . VAL A 29  ? 1.7336 1.0862 0.9024 -0.5071 0.1297  -0.1589 28  VAL A CB  
216  C CG1 . VAL A 29  ? 1.8860 1.2386 1.0546 -0.4958 0.1417  -0.1675 28  VAL A CG1 
217  C CG2 . VAL A 29  ? 1.6172 0.9387 0.7701 -0.5034 0.1371  -0.1644 28  VAL A CG2 
218  N N   . VAL A 30  ? 1.5129 0.9524 0.7639 -0.4853 0.1157  -0.1433 29  VAL A N   
219  C CA  . VAL A 30  ? 1.4337 0.9072 0.7112 -0.4881 0.1064  -0.1349 29  VAL A CA  
220  C C   . VAL A 30  ? 1.4401 0.9229 0.7307 -0.4792 0.1146  -0.1400 29  VAL A C   
221  O O   . VAL A 30  ? 1.3963 0.8676 0.6900 -0.4636 0.1264  -0.1498 29  VAL A O   
222  C CB  . VAL A 30  ? 1.3748 0.8750 0.6857 -0.4761 0.0969  -0.1271 29  VAL A CB  
223  C CG1 . VAL A 30  ? 1.1923 0.7077 0.5329 -0.4507 0.0999  -0.1331 29  VAL A CG1 
224  C CG2 . VAL A 30  ? 1.4469 0.9739 0.7739 -0.4905 0.0832  -0.1147 29  VAL A CG2 
225  N N   . ASP A 31  ? 1.5877 1.0906 0.8874 -0.4897 0.1087  -0.1325 30  ASP A N   
226  C CA  . ASP A 31  ? 1.5483 1.0640 0.8657 -0.4834 0.1165  -0.1336 30  ASP A CA  
227  C C   . ASP A 31  ? 1.5903 1.1390 0.9597 -0.4645 0.1117  -0.1322 30  ASP A C   
228  O O   . ASP A 31  ? 1.6780 1.2401 1.0648 -0.4571 0.1013  -0.1297 30  ASP A O   
229  C CB  . ASP A 31  ? 1.5279 1.0517 0.8331 -0.5025 0.1103  -0.1239 30  ASP A CB  
230  C CG  . ASP A 31  ? 1.9014 1.4078 1.1830 -0.5054 0.1254  -0.1274 30  ASP A CG  
231  O OD1 . ASP A 31  ? 2.1484 1.6374 1.4266 -0.4930 0.1417  -0.1375 30  ASP A OD1 
232  O OD2 . ASP A 31  ? 2.0057 1.5148 1.2715 -0.5194 0.1214  -0.1196 30  ASP A OD2 
233  N N   . LYS A 32  ? 1.5991 1.1602 0.9939 -0.4563 0.1194  -0.1337 31  LYS A N   
234  C CA  . LYS A 32  ? 1.5774 1.1718 1.0254 -0.4406 0.1118  -0.1322 31  LYS A CA  
235  C C   . LYS A 32  ? 1.4454 1.0680 0.9087 -0.4517 0.0962  -0.1195 31  LYS A C   
236  O O   . LYS A 32  ? 1.3924 1.0357 0.8828 -0.4424 0.0840  -0.1176 31  LYS A O   
237  C CB  . LYS A 32  ? 1.5936 1.1946 1.0721 -0.4295 0.1243  -0.1364 31  LYS A CB  
238  C CG  . LYS A 32  ? 1.7541 1.3326 1.2317 -0.4140 0.1381  -0.1496 31  LYS A CG  
239  C CD  . LYS A 32  ? 1.7397 1.3386 1.2741 -0.3904 0.1345  -0.1564 31  LYS A CD  
240  C CE  . LYS A 32  ? 1.7290 1.3528 1.3061 -0.3899 0.1377  -0.1507 31  LYS A CE  
241  N NZ  . LYS A 32  ? 1.6272 1.2766 1.2662 -0.3685 0.1273  -0.1566 31  LYS A NZ  
242  N N   . PRO A 33  ? 1.3596 0.9816 0.8037 -0.4710 0.0964  -0.1107 32  PRO A N   
243  C CA  . PRO A 33  ? 1.2179 0.8643 0.6738 -0.4835 0.0807  -0.0981 32  PRO A CA  
244  C C   . PRO A 33  ? 1.3162 0.9586 0.7568 -0.4910 0.0690  -0.0950 32  PRO A C   
245  O O   . PRO A 33  ? 1.3915 1.0586 0.8572 -0.4919 0.0561  -0.0872 32  PRO A O   
246  C CB  . PRO A 33  ? 1.1539 0.7898 0.5793 -0.5025 0.0842  -0.0911 32  PRO A CB  
247  C CG  . PRO A 33  ? 1.2492 0.8657 0.6634 -0.4948 0.1041  -0.0988 32  PRO A CG  
248  C CD  . PRO A 33  ? 1.2985 0.8990 0.7128 -0.4795 0.1115  -0.1118 32  PRO A CD  
249  N N   . ALA A 34  ? 1.3754 0.9865 0.7772 -0.4965 0.0743  -0.1007 33  ALA A N   
250  C CA  . ALA A 34  ? 1.3566 0.9620 0.7471 -0.5039 0.0652  -0.0968 33  ALA A CA  
251  C C   . ALA A 34  ? 1.3482 0.9636 0.7638 -0.4829 0.0642  -0.0999 33  ALA A C   
252  O O   . ALA A 34  ? 1.3761 1.0070 0.8069 -0.4830 0.0547  -0.0922 33  ALA A O   
253  C CB  . ALA A 34  ? 1.2762 0.8448 0.6213 -0.5155 0.0710  -0.1022 33  ALA A CB  
254  N N   . LEU A 35  ? 1.3748 0.9805 0.7944 -0.4639 0.0740  -0.1109 34  LEU A N   
255  C CA  . LEU A 35  ? 1.3530 0.9657 0.7936 -0.4407 0.0719  -0.1155 34  LEU A CA  
256  C C   . LEU A 35  ? 1.3607 1.0083 0.8401 -0.4331 0.0595  -0.1090 34  LEU A C   
257  O O   . LEU A 35  ? 1.2939 0.9480 0.7798 -0.4237 0.0534  -0.1059 34  LEU A O   
258  C CB  . LEU A 35  ? 1.2444 0.8481 0.6946 -0.4211 0.0812  -0.1285 34  LEU A CB  
259  C CG  . LEU A 35  ? 1.2389 0.8282 0.6853 -0.3998 0.0826  -0.1363 34  LEU A CG  
260  C CD1 . LEU A 35  ? 1.0909 0.6871 0.5685 -0.3764 0.0836  -0.1476 34  LEU A CD1 
261  C CD2 . LEU A 35  ? 1.1317 0.7317 0.5821 -0.3938 0.0725  -0.1289 34  LEU A CD2 
262  N N   . ARG A 36  ? 1.3204 0.9894 0.8255 -0.4361 0.0570  -0.1069 35  ARG A N   
263  C CA  . ARG A 36  ? 1.2449 0.9476 0.7921 -0.4272 0.0454  -0.1027 35  ARG A CA  
264  C C   . ARG A 36  ? 1.2113 0.9274 0.7576 -0.4411 0.0354  -0.0898 35  ARG A C   
265  O O   . ARG A 36  ? 1.2011 0.9325 0.7662 -0.4294 0.0276  -0.0876 35  ARG A O   
266  C CB  . ARG A 36  ? 1.2633 0.9843 0.8397 -0.4291 0.0466  -0.1019 35  ARG A CB  
267  C CG  . ARG A 36  ? 1.4483 1.1826 1.0663 -0.4045 0.0455  -0.1123 35  ARG A CG  
268  C CD  . ARG A 36  ? 1.5526 1.3124 1.2034 -0.3901 0.0303  -0.1117 35  ARG A CD  
269  N NE  . ARG A 36  ? 1.7024 1.4491 1.3311 -0.3794 0.0270  -0.1143 35  ARG A NE  
270  C CZ  . ARG A 36  ? 1.7341 1.4958 1.3796 -0.3644 0.0159  -0.1144 35  ARG A CZ  
271  N NH1 . ARG A 36  ? 1.7685 1.5595 1.4554 -0.3589 0.0053  -0.1132 35  ARG A NH1 
272  N NH2 . ARG A 36  ? 1.6252 1.3713 1.2454 -0.3540 0.0160  -0.1153 35  ARG A NH2 
273  N N   . MET A 37  ? 1.1688 0.8774 0.6926 -0.4654 0.0354  -0.0818 36  MET A N   
274  C CA  . MET A 37  ? 1.1107 0.8298 0.6347 -0.4819 0.0254  -0.0692 36  MET A CA  
275  C C   . MET A 37  ? 1.1715 0.8785 0.6831 -0.4779 0.0260  -0.0673 36  MET A C   
276  O O   . MET A 37  ? 1.1459 0.8705 0.6774 -0.4747 0.0193  -0.0596 36  MET A O   
277  C CB  . MET A 37  ? 1.1611 0.8684 0.6588 -0.5074 0.0244  -0.0636 36  MET A CB  
278  C CG  . MET A 37  ? 1.2346 0.9436 0.7260 -0.5273 0.0138  -0.0523 36  MET A CG  
279  S SD  . MET A 37  ? 1.6472 1.3449 1.1103 -0.5541 0.0079  -0.0471 36  MET A SD  
280  C CE  . MET A 37  ? 2.1940 1.8510 1.6102 -0.5523 0.0232  -0.0610 36  MET A CE  
281  N N   . ILE A 38  ? 1.1353 0.8115 0.6152 -0.4766 0.0354  -0.0741 37  ILE A N   
282  C CA  . ILE A 38  ? 1.0344 0.6964 0.5020 -0.4730 0.0383  -0.0711 37  ILE A CA  
283  C C   . ILE A 38  ? 1.1728 0.8436 0.6570 -0.4452 0.0392  -0.0744 37  ILE A C   
284  O O   . ILE A 38  ? 1.1892 0.8631 0.6774 -0.4403 0.0386  -0.0668 37  ILE A O   
285  C CB  . ILE A 38  ? 1.1330 0.7581 0.5627 -0.4793 0.0482  -0.0775 37  ILE A CB  
286  C CG1 . ILE A 38  ? 1.2447 0.8592 0.6548 -0.5070 0.0443  -0.0741 37  ILE A CG1 
287  C CG2 . ILE A 38  ? 0.9621 0.5712 0.3818 -0.4730 0.0533  -0.0738 37  ILE A CG2 
288  C CD1 . ILE A 38  ? 1.3373 0.9169 0.7103 -0.5122 0.0538  -0.0842 37  ILE A CD1 
289  N N   . SER A 39  ? 1.3212 0.9955 0.8160 -0.4265 0.0404  -0.0856 38  SER A N   
290  C CA  . SER A 39  ? 1.2681 0.9471 0.7752 -0.3977 0.0387  -0.0916 38  SER A CA  
291  C C   . SER A 39  ? 1.2450 0.9538 0.7819 -0.3913 0.0285  -0.0844 38  SER A C   
292  O O   . SER A 39  ? 1.2417 0.9518 0.7810 -0.3703 0.0269  -0.0853 38  SER A O   
293  C CB  . SER A 39  ? 1.2717 0.9495 0.7905 -0.3805 0.0396  -0.1059 38  SER A CB  
294  O OG  . SER A 39  ? 1.4003 1.0749 0.9235 -0.3518 0.0367  -0.1137 38  SER A OG  
295  N N   . GLU A 40  ? 1.2903 1.0214 0.8476 -0.4091 0.0218  -0.0770 39  GLU A N   
296  C CA  . GLU A 40  ? 1.2227 0.9844 0.8131 -0.4043 0.0117  -0.0708 39  GLU A CA  
297  C C   . GLU A 40  ? 1.2169 0.9825 0.8044 -0.4174 0.0112  -0.0562 39  GLU A C   
298  O O   . GLU A 40  ? 1.1657 0.9535 0.7776 -0.4119 0.0049  -0.0500 39  GLU A O   
299  C CB  . GLU A 40  ? 1.1090 0.8938 0.7276 -0.4150 0.0049  -0.0700 39  GLU A CB  
300  C CG  . GLU A 40  ? 1.2375 1.0541 0.8978 -0.4021 -0.0060 -0.0696 39  GLU A CG  
301  C CD  . GLU A 40  ? 1.2641 1.0815 0.9386 -0.3716 -0.0092 -0.0838 39  GLU A CD  
302  O OE1 . GLU A 40  ? 1.2725 1.0812 0.9492 -0.3643 -0.0062 -0.0947 39  GLU A OE1 
303  O OE2 . GLU A 40  ? 1.3510 1.1774 1.0352 -0.3541 -0.0152 -0.0844 39  GLU A OE2 
304  N N   . CYS A 41  ? 1.3229 1.0663 0.8833 -0.4345 0.0180  -0.0509 40  CYS A N   
305  C CA  . CYS A 41  ? 1.2624 1.0086 0.8256 -0.4485 0.0177  -0.0366 40  CYS A CA  
306  C C   . CYS A 41  ? 1.2424 0.9644 0.7835 -0.4394 0.0291  -0.0337 40  CYS A C   
307  O O   . CYS A 41  ? 1.3322 1.0570 0.8809 -0.4457 0.0315  -0.0212 40  CYS A O   
308  C CB  . CYS A 41  ? 1.2603 1.0048 0.8192 -0.4796 0.0128  -0.0298 40  CYS A CB  
309  S SG  . CYS A 41  ? 1.5878 1.2926 1.1053 -0.4936 0.0214  -0.0339 40  CYS A SG  
310  N N   . ALA A 42  ? 1.1108 0.8093 0.6273 -0.4235 0.0369  -0.0445 41  ALA A N   
311  C CA  . ALA A 42  ? 1.0940 0.7659 0.5864 -0.4146 0.0490  -0.0417 41  ALA A CA  
312  C C   . ALA A 42  ? 1.0655 0.7216 0.5405 -0.3850 0.0538  -0.0536 41  ALA A C   
313  O O   . ALA A 42  ? 1.0942 0.7450 0.5644 -0.3806 0.0517  -0.0664 41  ALA A O   
314  C CB  . ALA A 42  ? 1.0696 0.7170 0.5409 -0.4382 0.0542  -0.0398 41  ALA A CB  
315  N N   . ARG A 43  ? 1.0778 0.7248 0.5431 -0.3643 0.0608  -0.0491 42  ARG A N   
316  C CA  . ARG A 43  ? 1.1339 0.7608 0.5772 -0.3357 0.0649  -0.0594 42  ARG A CA  
317  C C   . ARG A 43  ? 1.2587 0.8521 0.6730 -0.3430 0.0762  -0.0611 42  ARG A C   
318  O O   . ARG A 43  ? 1.5065 1.0928 0.9182 -0.3691 0.0804  -0.0540 42  ARG A O   
319  C CB  . ARG A 43  ? 1.3183 0.9435 0.7551 -0.3101 0.0693  -0.0527 42  ARG A CB  
320  C CG  . ARG A 43  ? 1.3751 1.0315 0.8398 -0.3047 0.0603  -0.0485 42  ARG A CG  
321  C CD  . ARG A 43  ? 1.4880 1.1629 0.9712 -0.2897 0.0447  -0.0642 42  ARG A CD  
322  N NE  . ARG A 43  ? 1.5377 1.2445 1.0567 -0.3086 0.0343  -0.0619 42  ARG A NE  
323  C CZ  . ARG A 43  ? 1.5025 1.2173 1.0345 -0.3293 0.0294  -0.0663 42  ARG A CZ  
324  N NH1 . ARG A 43  ? 1.5049 1.1982 1.0176 -0.3338 0.0344  -0.0740 42  ARG A NH1 
325  N NH2 . ARG A 43  ? 1.4259 1.1689 0.9889 -0.3446 0.0205  -0.0624 42  ARG A NH2 
326  N N   . MET A 44  ? 1.1832 0.7555 0.5767 -0.3201 0.0797  -0.0710 43  MET A N   
327  C CA  . MET A 44  ? 1.2552 0.7940 0.6211 -0.3244 0.0914  -0.0722 43  MET A CA  
328  C C   . MET A 44  ? 1.2126 0.7344 0.5649 -0.3275 0.1047  -0.0562 43  MET A C   
329  O O   . MET A 44  ? 1.2594 0.7621 0.6017 -0.3464 0.1129  -0.0518 43  MET A O   
330  C CB  . MET A 44  ? 1.3627 0.8830 0.7117 -0.2971 0.0914  -0.0859 43  MET A CB  
331  C CG  . MET A 44  ? 1.5005 1.0132 0.8496 -0.3056 0.0897  -0.1000 43  MET A CG  
332  S SD  . MET A 44  ? 1.6814 1.1680 1.0105 -0.3358 0.1018  -0.0968 43  MET A SD  
333  C CE  . MET A 44  ? 1.6874 1.1606 1.0118 -0.3317 0.1022  -0.1156 43  MET A CE  
334  N N   . SER A 45  ? 1.2061 0.7340 0.5590 -0.3077 0.1072  -0.0477 44  SER A N   
335  C CA  . SER A 45  ? 1.1798 0.6937 0.5239 -0.3072 0.1222  -0.0305 44  SER A CA  
336  C C   . SER A 45  ? 1.3050 0.8290 0.6713 -0.3412 0.1241  -0.0181 44  SER A C   
337  O O   . SER A 45  ? 1.2958 0.8011 0.6574 -0.3513 0.1369  -0.0064 44  SER A O   
338  C CB  . SER A 45  ? 1.2579 0.7812 0.6007 -0.2790 0.1235  -0.0244 44  SER A CB  
339  O OG  . SER A 45  ? 1.4765 0.9848 0.8103 -0.2753 0.1413  -0.0062 44  SER A OG  
340  N N   . GLU A 46  ? 1.3462 0.8990 0.7384 -0.3585 0.1107  -0.0204 45  GLU A N   
341  C CA  . GLU A 46  ? 1.3986 0.9625 0.8133 -0.3902 0.1086  -0.0096 45  GLU A CA  
342  C C   . GLU A 46  ? 1.4171 0.9642 0.8223 -0.4151 0.1063  -0.0162 45  GLU A C   
343  O O   . GLU A 46  ? 1.4236 0.9693 0.8405 -0.4408 0.1052  -0.0081 45  GLU A O   
344  C CB  . GLU A 46  ? 1.4808 1.0810 0.9255 -0.3984 0.0942  -0.0090 45  GLU A CB  
345  C CG  . GLU A 46  ? 1.6969 1.3154 1.1585 -0.3828 0.0972  0.0021  45  GLU A CG  
346  C CD  . GLU A 46  ? 1.8973 1.5516 1.3891 -0.3884 0.0822  0.0007  45  GLU A CD  
347  O OE1 . GLU A 46  ? 1.8643 1.5289 1.3586 -0.3902 0.0701  -0.0124 45  GLU A OE1 
348  O OE2 . GLU A 46  ? 2.0012 1.6730 1.5161 -0.3905 0.0836  0.0133  45  GLU A OE2 
349  N N   . ILE A 47  ? 1.4615 0.9955 0.8462 -0.4067 0.1048  -0.0315 46  ILE A N   
350  C CA  . ILE A 47  ? 1.4641 0.9796 0.8348 -0.4268 0.1036  -0.0400 46  ILE A CA  
351  C C   . ILE A 47  ? 1.4301 0.9106 0.7795 -0.4244 0.1178  -0.0372 46  ILE A C   
352  O O   . ILE A 47  ? 1.3813 0.8441 0.7249 -0.4463 0.1192  -0.0371 46  ILE A O   
353  C CB  . ILE A 47  ? 1.3371 0.8553 0.6994 -0.4182 0.0975  -0.0574 46  ILE A CB  
354  C CG1 . ILE A 47  ? 1.4015 0.9268 0.7673 -0.4443 0.0885  -0.0623 46  ILE A CG1 
355  C CG2 . ILE A 47  ? 1.4099 0.8977 0.7457 -0.4027 0.1069  -0.0674 46  ILE A CG2 
356  C CD1 . ILE A 47  ? 1.4952 1.0552 0.8887 -0.4524 0.0764  -0.0566 46  ILE A CD1 
357  N N   . LEU A 48  ? 1.4492 0.9187 0.7863 -0.3966 0.1276  -0.0350 47  LEU A N   
358  C CA  . LEU A 48  ? 1.4118 0.8478 0.7284 -0.3896 0.1425  -0.0311 47  LEU A CA  
359  C C   . LEU A 48  ? 1.4580 0.8880 0.7889 -0.4086 0.1503  -0.0144 47  LEU A C   
360  O O   . LEU A 48  ? 1.6092 1.0159 0.9344 -0.4251 0.1553  -0.0142 47  LEU A O   
361  C CB  . LEU A 48  ? 1.5006 0.9289 0.8017 -0.3541 0.1504  -0.0292 47  LEU A CB  
362  C CG  . LEU A 48  ? 1.5743 0.9751 0.8477 -0.3356 0.1549  -0.0410 47  LEU A CG  
363  C CD1 . LEU A 48  ? 1.5199 0.9160 0.7908 -0.3532 0.1480  -0.0566 47  LEU A CD1 
364  C CD2 . LEU A 48  ? 1.5238 0.9305 0.7878 -0.3005 0.1502  -0.0474 47  LEU A CD2 
365  N N   . ASP A 49  ? 1.4158 0.8662 0.7681 -0.4064 0.1515  -0.0006 48  ASP A N   
366  C CA  . ASP A 49  ? 1.6708 1.1158 1.0430 -0.4238 0.1600  0.0163  48  ASP A CA  
367  C C   . ASP A 49  ? 1.6258 1.0889 1.0247 -0.4570 0.1450  0.0166  48  ASP A C   
368  O O   . ASP A 49  ? 1.6514 1.1277 1.0800 -0.4700 0.1452  0.0306  48  ASP A O   
369  C CB  . ASP A 49  ? 1.7811 1.2307 1.1616 -0.4036 0.1745  0.0339  48  ASP A CB  
370  C CG  . ASP A 49  ? 1.5739 1.0568 0.9693 -0.3941 0.1654  0.0347  48  ASP A CG  
371  O OD1 . ASP A 49  ? 1.5222 1.0282 0.9349 -0.4127 0.1484  0.0277  48  ASP A OD1 
372  O OD2 . ASP A 49  ? 1.5278 1.0123 0.9166 -0.3676 0.1755  0.0426  48  ASP A OD2 
373  N N   . LEU A 50  ? 1.6542 1.1161 1.0410 -0.4696 0.1322  0.0008  49  LEU A N   
374  C CA  . LEU A 50  ? 1.5539 1.0231 0.9545 -0.5009 0.1175  -0.0016 49  LEU A CA  
375  C C   . LEU A 50  ? 1.4847 0.9215 0.8608 -0.5117 0.1189  -0.0129 49  LEU A C   
376  O O   . LEU A 50  ? 1.5185 0.9516 0.8919 -0.5349 0.1064  -0.0204 49  LEU A O   
377  C CB  . LEU A 50  ? 1.4154 0.9122 0.8193 -0.5032 0.1019  -0.0105 49  LEU A CB  
378  C CG  . LEU A 50  ? 1.4443 0.9649 0.8752 -0.5277 0.0862  -0.0044 49  LEU A CG  
379  C CD1 . LEU A 50  ? 1.2907 0.8238 0.7549 -0.5303 0.0908  0.0142  49  LEU A CD1 
380  C CD2 . LEU A 50  ? 1.4612 1.0103 0.8960 -0.5228 0.0743  -0.0113 49  LEU A CD2 
381  N N   . GLY A 51  ? 1.3387 0.7506 0.6948 -0.4932 0.1340  -0.0144 50  GLY A N   
382  C CA  . GLY A 51  ? 1.1367 0.5154 0.4698 -0.5000 0.1380  -0.0246 50  GLY A CA  
383  C C   . GLY A 51  ? 1.4871 0.8573 0.7922 -0.4956 0.1335  -0.0440 50  GLY A C   
384  O O   . GLY A 51  ? 1.4271 0.7692 0.7140 -0.5047 0.1361  -0.0531 50  GLY A O   
385  N N   . VAL A 52  ? 1.3525 0.7458 0.6566 -0.4825 0.1274  -0.0506 51  VAL A N   
386  C CA  . VAL A 52  ? 1.4165 0.8003 0.6979 -0.4723 0.1276  -0.0676 51  VAL A CA  
387  C C   . VAL A 52  ? 1.5034 0.8808 0.7757 -0.4402 0.1376  -0.0692 51  VAL A C   
388  O O   . VAL A 52  ? 1.3566 0.7513 0.6405 -0.4229 0.1383  -0.0606 51  VAL A O   
389  C CB  . VAL A 52  ? 1.2982 0.7069 0.5847 -0.4780 0.1152  -0.0759 51  VAL A CB  
390  C CG1 . VAL A 52  ? 1.4436 0.8639 0.7416 -0.5065 0.1029  -0.0707 51  VAL A CG1 
391  C CG2 . VAL A 52  ? 1.3345 0.7718 0.6376 -0.4560 0.1124  -0.0735 51  VAL A CG2 
392  N N   . THR A 53  ? 1.6115 0.9626 0.8618 -0.4319 0.1447  -0.0805 52  THR A N   
393  C CA  . THR A 53  ? 1.5253 0.8646 0.7641 -0.4015 0.1530  -0.0830 52  THR A CA  
394  C C   . THR A 53  ? 1.3777 0.7270 0.6149 -0.3847 0.1474  -0.0980 52  THR A C   
395  O O   . THR A 53  ? 1.4913 0.8417 0.7269 -0.3573 0.1482  -0.0997 52  THR A O   
396  C CB  . THR A 53  ? 1.4985 0.7994 0.7173 -0.3999 0.1659  -0.0838 52  THR A CB  
397  O OG1 . THR A 53  ? 1.5667 0.8565 0.7748 -0.3691 0.1736  -0.0818 52  THR A OG1 
398  C CG2 . THR A 53  ? 1.3565 0.6393 0.5601 -0.4107 0.1657  -0.1005 52  THR A CG2 
399  N N   . VAL A 54  ? 1.3247 0.6794 0.5627 -0.4002 0.1420  -0.1086 53  VAL A N   
400  C CA  . VAL A 54  ? 1.4902 0.8587 0.7355 -0.3870 0.1371  -0.1211 53  VAL A CA  
401  C C   . VAL A 54  ? 1.6094 1.0016 0.8677 -0.4062 0.1282  -0.1226 53  VAL A C   
402  O O   . VAL A 54  ? 1.6151 1.0041 0.8678 -0.4316 0.1262  -0.1184 53  VAL A O   
403  C CB  . VAL A 54  ? 1.4303 0.7730 0.6593 -0.3818 0.1449  -0.1358 53  VAL A CB  
404  C CG1 . VAL A 54  ? 1.2297 0.5682 0.4614 -0.3498 0.1461  -0.1423 53  VAL A CG1 
405  C CG2 . VAL A 54  ? 1.5614 0.8713 0.7679 -0.3979 0.1539  -0.1355 53  VAL A CG2 
406  N N   . VAL A 55  ? 1.4391 0.8538 0.7156 -0.3931 0.1223  -0.1287 54  VAL A N   
407  C CA  . VAL A 55  ? 1.3584 0.7917 0.6459 -0.4076 0.1168  -0.1322 54  VAL A CA  
408  C C   . VAL A 55  ? 1.4454 0.8695 0.7318 -0.3974 0.1229  -0.1467 54  VAL A C   
409  O O   . VAL A 55  ? 1.3951 0.8176 0.6907 -0.3731 0.1240  -0.1534 54  VAL A O   
410  C CB  . VAL A 55  ? 1.4840 0.9540 0.8010 -0.4026 0.1054  -0.1255 54  VAL A CB  
411  C CG1 . VAL A 55  ? 1.3512 0.8400 0.6785 -0.4220 0.0998  -0.1250 54  VAL A CG1 
412  C CG2 . VAL A 55  ? 1.0009 0.4773 0.3210 -0.4047 0.1025  -0.1114 54  VAL A CG2 
413  N N   . GLU A 56  ? 1.5097 0.9260 0.7844 -0.4152 0.1269  -0.1515 55  GLU A N   
414  C CA  . GLU A 56  ? 1.4789 0.8822 0.7506 -0.4076 0.1366  -0.1644 55  GLU A CA  
415  C C   . GLU A 56  ? 1.5321 0.9539 0.8158 -0.4172 0.1357  -0.1653 55  GLU A C   
416  O O   . GLU A 56  ? 1.4923 0.9277 0.7743 -0.4354 0.1284  -0.1568 55  GLU A O   
417  C CB  . GLU A 56  ? 1.6122 0.9778 0.8491 -0.4184 0.1476  -0.1705 55  GLU A CB  
418  C CG  . GLU A 56  ? 1.7153 1.0584 0.9391 -0.4101 0.1508  -0.1688 55  GLU A CG  
419  C CD  . GLU A 56  ? 1.8289 1.1633 1.0612 -0.3827 0.1562  -0.1771 55  GLU A CD  
420  O OE1 . GLU A 56  ? 1.7376 1.0415 0.9506 -0.3791 0.1655  -0.1827 55  GLU A OE1 
421  O OE2 . GLU A 56  ? 1.8881 1.2456 1.1476 -0.3646 0.1499  -0.1787 55  GLU A OE2 
422  N N   . ASP A 57  ? 1.5571 0.9790 0.8550 -0.4044 0.1434  -0.1748 56  ASP A N   
423  C CA  . ASP A 57  ? 1.5405 0.9757 0.8490 -0.4123 0.1470  -0.1752 56  ASP A CA  
424  C C   . ASP A 57  ? 1.5677 0.9732 0.8397 -0.4270 0.1606  -0.1805 56  ASP A C   
425  O O   . ASP A 57  ? 1.6502 1.0302 0.9098 -0.4190 0.1726  -0.1903 56  ASP A O   
426  C CB  . ASP A 57  ? 1.7919 1.2439 1.1413 -0.3907 0.1494  -0.1818 56  ASP A CB  
427  C CG  . ASP A 57  ? 1.8850 1.3479 1.2474 -0.3978 0.1575  -0.1812 56  ASP A CG  
428  O OD1 . ASP A 57  ? 1.8411 1.3177 1.1978 -0.4147 0.1523  -0.1718 56  ASP A OD1 
429  O OD2 . ASP A 57  ? 1.8944 1.3517 1.2741 -0.3858 0.1695  -0.1894 56  ASP A OD2 
430  N N   . VAL A 58  ? 1.6044 1.0121 0.8579 -0.4478 0.1579  -0.1744 57  VAL A N   
431  C CA  . VAL A 58  ? 1.6705 1.0483 0.8824 -0.4624 0.1686  -0.1794 57  VAL A CA  
432  C C   . VAL A 58  ? 1.7690 1.1296 0.9805 -0.4497 0.1883  -0.1904 57  VAL A C   
433  O O   . VAL A 58  ? 1.9847 1.3120 1.1604 -0.4551 0.1997  -0.1984 57  VAL A O   
434  C CB  . VAL A 58  ? 1.7334 1.1213 0.9323 -0.4811 0.1628  -0.1713 57  VAL A CB  
435  C CG1 . VAL A 58  ? 1.6229 1.0431 0.8606 -0.4722 0.1636  -0.1660 57  VAL A CG1 
436  C CG2 . VAL A 58  ? 1.8999 1.2539 1.0511 -0.4932 0.1739  -0.1778 57  VAL A CG2 
437  N N   . SER A 59  ? 1.7058 1.0885 0.9594 -0.4327 0.1921  -0.1912 58  SER A N   
438  C CA  . SER A 59  ? 1.8062 1.1757 1.0717 -0.4175 0.2102  -0.2014 58  SER A CA  
439  C C   . SER A 59  ? 2.0472 1.4045 1.3223 -0.4002 0.2098  -0.2097 58  SER A C   
440  O O   . SER A 59  ? 2.0234 1.3951 1.3149 -0.3924 0.1950  -0.2064 58  SER A O   
441  C CB  . SER A 59  ? 1.7401 1.1386 1.0535 -0.4063 0.2134  -0.1988 58  SER A CB  
442  O OG  . SER A 59  ? 1.8860 1.2734 1.2195 -0.3903 0.2305  -0.2083 58  SER A OG  
443  N N   . LYS A 60  ? 2.2149 1.5442 1.4780 -0.3936 0.2266  -0.2202 59  LYS A N   
444  C CA  . LYS A 60  ? 2.2045 1.5182 1.4748 -0.3766 0.2280  -0.2286 59  LYS A CA  
445  C C   . LYS A 60  ? 2.1150 1.3972 1.3405 -0.3871 0.2280  -0.2305 59  LYS A C   
446  O O   . LYS A 60  ? 2.0018 1.2533 1.2071 -0.3852 0.2417  -0.2396 59  LYS A O   
447  C CB  . LYS A 60  ? 2.2620 1.6020 1.5720 -0.3584 0.2111  -0.2261 59  LYS A CB  
448  C CG  . LYS A 60  ? 2.3375 1.7081 1.6995 -0.3451 0.2086  -0.2262 59  LYS A CG  
449  C CD  . LYS A 60  ? 2.3065 1.7002 1.7022 -0.3267 0.1892  -0.2253 59  LYS A CD  
450  C CE  . LYS A 60  ? 2.3004 1.7233 1.7520 -0.3133 0.1854  -0.2272 59  LYS A CE  
451  N NZ  . LYS A 60  ? 2.2673 1.7081 1.7514 -0.2914 0.1657  -0.2298 59  LYS A NZ  
452  N N   . GLN A 61  ? 2.2302 1.5208 1.4442 -0.3979 0.2128  -0.2215 60  GLN A N   
453  C CA  . GLN A 61  ? 2.3771 1.6416 1.5568 -0.4082 0.2106  -0.2212 60  GLN A CA  
454  C C   . GLN A 61  ? 2.4942 1.7287 1.6655 -0.3956 0.2213  -0.2310 60  GLN A C   
455  O O   . GLN A 61  ? 2.6785 1.8820 1.8187 -0.4047 0.2327  -0.2383 60  GLN A O   
456  C CB  . GLN A 61  ? 2.4085 1.6558 1.5484 -0.4333 0.2124  -0.2207 60  GLN A CB  
457  C CG  . GLN A 61  ? 2.2447 1.4961 1.3727 -0.4496 0.1969  -0.2110 60  GLN A CG  
458  C CD  . GLN A 61  ? 1.9775 1.2681 1.1365 -0.4481 0.1829  -0.1994 60  GLN A CD  
459  O OE1 . GLN A 61  ? 1.6098 0.9172 0.7962 -0.4318 0.1774  -0.1956 60  GLN A OE1 
460  N NE2 . GLN A 61  ? 1.9725 1.2771 1.1262 -0.4639 0.1768  -0.1938 60  GLN A NE2 
461  N N   . ARG A 62  ? 2.4097 1.6518 1.6069 -0.3739 0.2169  -0.2315 61  ARG A N   
462  C CA  . ARG A 62  ? 2.4254 1.6382 1.6113 -0.3629 0.2236  -0.2378 61  ARG A CA  
463  C C   . ARG A 62  ? 2.3187 1.5216 1.4841 -0.3712 0.2156  -0.2290 61  ARG A C   
464  O O   . ARG A 62  ? 2.1655 1.3832 1.3259 -0.3866 0.2060  -0.2193 61  ARG A O   
465  C CB  . ARG A 62  ? 2.3097 1.5299 1.5297 -0.3344 0.2225  -0.2432 61  ARG A CB  
466  C CG  . ARG A 62  ? 2.1707 1.4037 1.4027 -0.3187 0.2074  -0.2358 61  ARG A CG  
467  C CD  . ARG A 62  ? 2.0690 1.2746 1.2916 -0.3022 0.2109  -0.2397 61  ARG A CD  
468  N NE  . ARG A 62  ? 2.1127 1.3265 1.3380 -0.2874 0.1980  -0.2309 61  ARG A NE  
469  C CZ  . ARG A 62  ? 2.2380 1.4299 1.4521 -0.2715 0.1988  -0.2303 61  ARG A CZ  
470  N NH1 . ARG A 62  ? 2.2395 1.4386 1.4525 -0.2571 0.1882  -0.2212 61  ARG A NH1 
471  N NH2 . ARG A 62  ? 2.2768 1.4384 1.4794 -0.2693 0.2108  -0.2384 61  ARG A NH2 
472  N N   . LYS A 63  ? 2.2878 1.4654 1.4439 -0.3607 0.2205  -0.2319 62  LYS A N   
473  C CA  . LYS A 63  ? 2.0744 1.2373 1.2129 -0.3667 0.2169  -0.2234 62  LYS A CA  
474  C C   . LYS A 63  ? 2.0143 1.1675 1.1283 -0.3954 0.2157  -0.2198 62  LYS A C   
475  O O   . LYS A 63  ? 1.9695 1.1449 1.0880 -0.4085 0.2056  -0.2111 62  LYS A O   
476  C CB  . LYS A 63  ? 1.8336 1.0189 0.9896 -0.3524 0.2051  -0.2116 62  LYS A CB  
477  C CG  . LYS A 63  ? 1.9104 1.0737 1.0529 -0.3462 0.2072  -0.2043 62  LYS A CG  
478  C CD  . LYS A 63  ? 2.1132 1.2438 1.2458 -0.3342 0.2186  -0.2144 62  LYS A CD  
479  C CE  . LYS A 63  ? 2.2794 1.3836 1.3958 -0.3320 0.2232  -0.2064 62  LYS A CE  
480  N NZ  . LYS A 63  ? 2.3922 1.5079 1.5168 -0.3107 0.2164  -0.1948 62  LYS A NZ  
481  N N   . VAL A 64  ? 1.9258 1.0445 1.0151 -0.4045 0.2252  -0.2273 63  VAL A N   
482  C CA  . VAL A 64  ? 1.9869 1.0897 1.0519 -0.4305 0.2225  -0.2264 63  VAL A CA  
483  C C   . VAL A 64  ? 2.1063 1.2036 1.1731 -0.4354 0.2166  -0.2143 63  VAL A C   
484  O O   . VAL A 64  ? 2.1414 1.2229 1.2107 -0.4212 0.2225  -0.2122 63  VAL A O   
485  C CB  . VAL A 64  ? 1.9942 1.0605 1.0319 -0.4371 0.2348  -0.2412 63  VAL A CB  
486  C CG1 . VAL A 64  ? 1.9484 0.9873 0.9625 -0.4585 0.2315  -0.2415 63  VAL A CG1 
487  C CG2 . VAL A 64  ? 1.8350 0.9079 0.8648 -0.4413 0.2398  -0.2497 63  VAL A CG2 
488  N N   . LEU A 65  ? 2.0384 1.1485 1.1057 -0.4548 0.2055  -0.2055 64  LEU A N   
489  C CA  . LEU A 65  ? 2.0093 1.1197 1.0860 -0.4598 0.2005  -0.1916 64  LEU A CA  
490  C C   . LEU A 65  ? 2.0380 1.1334 1.1029 -0.4878 0.1935  -0.1911 64  LEU A C   
491  O O   . LEU A 65  ? 2.0314 1.1477 1.1060 -0.5022 0.1815  -0.1827 64  LEU A O   
492  C CB  . LEU A 65  ? 1.8718 1.0202 0.9733 -0.4519 0.1917  -0.1779 64  LEU A CB  
493  C CG  . LEU A 65  ? 1.7944 0.9584 0.9110 -0.4227 0.1945  -0.1768 64  LEU A CG  
494  C CD1 . LEU A 65  ? 1.4003 0.6035 0.5396 -0.4174 0.1837  -0.1663 64  LEU A CD1 
495  C CD2 . LEU A 65  ? 1.7158 0.8576 0.8293 -0.4059 0.2030  -0.1721 64  LEU A CD2 
496  N N   . PRO A 66  ? 2.0811 1.1398 1.1270 -0.4954 0.1997  -0.2004 65  PRO A N   
497  C CA  . PRO A 66  ? 2.1169 1.1586 1.1504 -0.5220 0.1904  -0.2035 65  PRO A CA  
498  C C   . PRO A 66  ? 2.1072 1.1520 1.1628 -0.5326 0.1836  -0.1882 65  PRO A C   
499  O O   . PRO A 66  ? 2.1674 1.2043 1.2211 -0.5552 0.1720  -0.1891 65  PRO A O   
500  C CB  . PRO A 66  ? 2.1021 1.1022 1.1108 -0.5230 0.2004  -0.2191 65  PRO A CB  
501  C CG  . PRO A 66  ? 2.0988 1.0976 1.1078 -0.4974 0.2152  -0.2241 65  PRO A CG  
502  C CD  . PRO A 66  ? 2.0796 1.1098 1.1157 -0.4801 0.2141  -0.2091 65  PRO A CD  
503  N N   . GLN A 67  ? 2.0145 1.0699 1.0911 -0.5156 0.1906  -0.1744 66  GLN A N   
504  C CA  . GLN A 67  ? 1.9501 1.0095 1.0508 -0.5225 0.1883  -0.1574 66  GLN A CA  
505  C C   . GLN A 67  ? 1.8568 0.9514 0.9768 -0.5331 0.1748  -0.1464 66  GLN A C   
506  O O   . GLN A 67  ? 1.8561 0.9540 0.9974 -0.5467 0.1694  -0.1344 66  GLN A O   
507  C CB  . GLN A 67  ? 2.0409 1.0987 1.1523 -0.4976 0.2021  -0.1453 66  GLN A CB  
508  C CG  . GLN A 67  ? 2.1924 1.2202 1.2862 -0.4813 0.2155  -0.1554 66  GLN A CG  
509  C CD  . GLN A 67  ? 2.3157 1.3520 1.3955 -0.4657 0.2171  -0.1690 66  GLN A CD  
510  O OE1 . GLN A 67  ? 2.2170 1.2816 1.3001 -0.4666 0.2088  -0.1707 66  GLN A OE1 
511  N NE2 . GLN A 67  ? 2.4062 1.4177 1.4736 -0.4511 0.2283  -0.1782 66  GLN A NE2 
512  N N   . PHE A 68  ? 1.8131 0.9337 0.9290 -0.5267 0.1699  -0.1503 67  PHE A N   
513  C CA  . PHE A 68  ? 1.8425 0.9994 0.9775 -0.5328 0.1580  -0.1401 67  PHE A CA  
514  C C   . PHE A 68  ? 1.8241 0.9874 0.9457 -0.5519 0.1444  -0.1495 67  PHE A C   
515  O O   . PHE A 68  ? 1.8320 0.9830 0.9283 -0.5501 0.1474  -0.1641 67  PHE A O   
516  C CB  . PHE A 68  ? 1.8407 1.0255 0.9850 -0.5082 0.1620  -0.1359 67  PHE A CB  
517  C CG  . PHE A 68  ? 1.9148 1.0951 1.0673 -0.4850 0.1739  -0.1266 67  PHE A CG  
518  C CD1 . PHE A 68  ? 1.9704 1.1463 1.1387 -0.4878 0.1776  -0.1110 67  PHE A CD1 
519  C CD2 . PHE A 68  ? 1.9172 1.0977 1.0627 -0.4594 0.1812  -0.1328 67  PHE A CD2 
520  C CE1 . PHE A 68  ? 2.0263 1.1962 1.1975 -0.4644 0.1898  -0.1012 67  PHE A CE1 
521  C CE2 . PHE A 68  ? 2.0133 1.1880 1.1620 -0.4361 0.1903  -0.1244 67  PHE A CE2 
522  C CZ  . PHE A 68  ? 2.0572 1.2259 1.2161 -0.4381 0.1953  -0.1082 67  PHE A CZ  
523  N N   . HIS A 69  ? 1.7416 0.9245 0.8801 -0.5688 0.1301  -0.1404 68  HIS A N   
524  C CA  . HIS A 69  ? 1.7541 0.9479 0.8802 -0.5840 0.1159  -0.1467 68  HIS A CA  
525  C C   . HIS A 69  ? 1.7066 0.9328 0.8376 -0.5703 0.1165  -0.1453 68  HIS A C   
526  O O   . HIS A 69  ? 1.6639 0.9186 0.8216 -0.5588 0.1170  -0.1332 68  HIS A O   
527  C CB  . HIS A 69  ? 1.7485 0.9525 0.8940 -0.6065 0.0984  -0.1373 68  HIS A CB  
528  C CG  . HIS A 69  ? 1.8652 1.0370 1.0064 -0.6246 0.0927  -0.1418 68  HIS A CG  
529  N ND1 . HIS A 69  ? 1.8723 1.0308 0.9973 -0.6467 0.0748  -0.1506 68  HIS A ND1 
530  C CD2 . HIS A 69  ? 2.0069 1.1561 1.1591 -0.6235 0.1016  -0.1387 68  HIS A CD2 
531  C CE1 . HIS A 69  ? 1.9964 1.1259 1.1247 -0.6589 0.0716  -0.1541 68  HIS A CE1 
532  N NE2 . HIS A 69  ? 2.0655 1.1892 1.2118 -0.6455 0.0886  -0.1464 68  HIS A NE2 
533  N N   . GLY A 70  ? 1.7095 0.9308 0.8154 -0.5713 0.1168  -0.1574 69  GLY A N   
534  C CA  . GLY A 70  ? 1.6360 0.8873 0.7499 -0.5611 0.1166  -0.1559 69  GLY A CA  
535  C C   . GLY A 70  ? 1.5990 0.8743 0.7220 -0.5777 0.0997  -0.1481 69  GLY A C   
536  O O   . GLY A 70  ? 1.6516 0.9121 0.7549 -0.5975 0.0887  -0.1521 69  GLY A O   
537  N N   . VAL A 71  ? 1.5065 0.8179 0.6590 -0.5691 0.0964  -0.1373 70  VAL A N   
538  C CA  . VAL A 71  ? 1.5976 0.9346 0.7608 -0.5825 0.0812  -0.1297 70  VAL A CA  
539  C C   . VAL A 71  ? 1.6062 0.9657 0.7732 -0.5706 0.0849  -0.1316 70  VAL A C   
540  O O   . VAL A 71  ? 1.5367 0.9139 0.7250 -0.5504 0.0926  -0.1299 70  VAL A O   
541  C CB  . VAL A 71  ? 1.5394 0.9019 0.7393 -0.5860 0.0722  -0.1137 70  VAL A CB  
542  C CG1 . VAL A 71  ? 1.4733 0.8598 0.6839 -0.6018 0.0551  -0.1065 70  VAL A CG1 
543  C CG2 . VAL A 71  ? 1.4894 0.8303 0.6928 -0.5960 0.0715  -0.1102 70  VAL A CG2 
544  N N   . TYR A 72  ? 1.6371 0.9944 0.7836 -0.5824 0.0790  -0.1351 71  TYR A N   
545  C CA  . TYR A 72  ? 1.6435 1.0195 0.7944 -0.5722 0.0845  -0.1362 71  TYR A CA  
546  C C   . TYR A 72  ? 1.6657 1.0753 0.8392 -0.5801 0.0704  -0.1242 71  TYR A C   
547  O O   . TYR A 72  ? 1.7475 1.1543 0.9093 -0.5995 0.0559  -0.1202 71  TYR A O   
548  C CB  . TYR A 72  ? 1.5946 0.9434 0.7046 -0.5761 0.0926  -0.1478 71  TYR A CB  
549  C CG  . TYR A 72  ? 1.6697 0.9857 0.7583 -0.5666 0.1085  -0.1608 71  TYR A CG  
550  C CD1 . TYR A 72  ? 1.6784 0.9638 0.7467 -0.5766 0.1060  -0.1661 71  TYR A CD1 
551  C CD2 . TYR A 72  ? 1.5571 0.8721 0.6490 -0.5479 0.1260  -0.1679 71  TYR A CD2 
552  C CE1 . TYR A 72  ? 1.6122 0.8672 0.6618 -0.5679 0.1206  -0.1779 71  TYR A CE1 
553  C CE2 . TYR A 72  ? 1.6145 0.8996 0.6888 -0.5390 0.1405  -0.1796 71  TYR A CE2 
554  C CZ  . TYR A 72  ? 1.7384 0.9935 0.7902 -0.5490 0.1379  -0.1845 71  TYR A CZ  
555  O OH  . TYR A 72  ? 1.8340 1.0592 0.8696 -0.5399 0.1525  -0.1961 71  TYR A OH  
556  N N   . PHE A 73  ? 1.5553 0.9960 0.7627 -0.5646 0.0732  -0.1189 72  PHE A N   
557  C CA  . PHE A 73  ? 1.6241 1.0965 0.8527 -0.5689 0.0633  -0.1093 72  PHE A CA  
558  C C   . PHE A 73  ? 1.6815 1.1574 0.9071 -0.5579 0.0751  -0.1148 72  PHE A C   
559  O O   . PHE A 73  ? 1.7090 1.1894 0.9513 -0.5382 0.0870  -0.1203 72  PHE A O   
560  C CB  . PHE A 73  ? 1.5634 1.0688 0.8356 -0.5599 0.0571  -0.0991 72  PHE A CB  
561  C CG  . PHE A 73  ? 1.6321 1.1400 0.9130 -0.5743 0.0448  -0.0897 72  PHE A CG  
562  C CD1 . PHE A 73  ? 1.5430 1.0250 0.8101 -0.5781 0.0479  -0.0925 72  PHE A CD1 
563  C CD2 . PHE A 73  ? 1.6948 1.2308 1.0013 -0.5839 0.0307  -0.0777 72  PHE A CD2 
564  C CE1 . PHE A 73  ? 1.5382 1.0224 0.8192 -0.5914 0.0378  -0.0829 72  PHE A CE1 
565  C CE2 . PHE A 73  ? 1.6617 1.2004 0.9815 -0.5970 0.0202  -0.0685 72  PHE A CE2 
566  C CZ  . PHE A 73  ? 1.5545 1.0672 0.8625 -0.6009 0.0241  -0.0710 72  PHE A CZ  
567  N N   . ILE A 74  ? 1.5594 1.0318 0.7640 -0.5700 0.0719  -0.1130 73  ILE A N   
568  C CA  . ILE A 74  ? 1.5021 0.9631 0.6899 -0.5619 0.0878  -0.1199 73  ILE A CA  
569  C C   . ILE A 74  ? 1.6291 1.0945 0.8004 -0.5735 0.0830  -0.1131 73  ILE A C   
570  O O   . ILE A 74  ? 1.6514 1.1181 0.8108 -0.5907 0.0657  -0.1063 73  ILE A O   
571  C CB  . ILE A 74  ? 1.5611 0.9811 0.7100 -0.5605 0.1005  -0.1335 73  ILE A CB  
572  C CG1 . ILE A 74  ? 1.6482 1.0646 0.8086 -0.5397 0.1211  -0.1420 73  ILE A CG1 
573  C CG2 . ILE A 74  ? 1.4799 0.8678 0.5749 -0.5780 0.0973  -0.1377 73  ILE A CG2 
574  C CD1 . ILE A 74  ? 1.8891 1.2650 1.0108 -0.5384 0.1349  -0.1553 73  ILE A CD1 
575  N N   . GLU A 75  ? 1.6733 1.1416 0.8469 -0.5633 0.0983  -0.1140 74  GLU A N   
576  C CA  . GLU A 75  ? 1.7922 1.2657 0.9521 -0.5711 0.0966  -0.1057 74  GLU A CA  
577  C C   . GLU A 75  ? 1.8684 1.3015 0.9664 -0.5785 0.1052  -0.1126 74  GLU A C   
578  O O   . GLU A 75  ? 1.9188 1.3249 0.9955 -0.5710 0.1212  -0.1245 74  GLU A O   
579  C CB  . GLU A 75  ? 1.8577 1.3572 1.0581 -0.5556 0.1098  -0.1009 74  GLU A CB  
580  C CG  . GLU A 75  ? 1.8917 1.4312 1.1353 -0.5578 0.0954  -0.0873 74  GLU A CG  
581  C CD  . GLU A 75  ? 1.9013 1.4665 1.1931 -0.5408 0.1078  -0.0846 74  GLU A CD  
582  O OE1 . GLU A 75  ? 1.7990 1.3584 1.1060 -0.5248 0.1227  -0.0944 74  GLU A OE1 
583  O OE2 . GLU A 75  ? 1.8853 1.4762 1.2025 -0.5432 0.1019  -0.0730 74  GLU A OE2 
584  N N   . PRO A 76  ? 1.8833 1.3109 0.9508 -0.5924 0.0940  -0.1054 75  PRO A N   
585  C CA  . PRO A 76  ? 1.9000 1.2879 0.9020 -0.5988 0.0999  -0.1113 75  PRO A CA  
586  C C   . PRO A 76  ? 1.9492 1.3268 0.9410 -0.5840 0.1288  -0.1130 75  PRO A C   
587  O O   . PRO A 76  ? 2.1192 1.4911 1.0850 -0.5859 0.1333  -0.1056 75  PRO A O   
588  C CB  . PRO A 76  ? 1.8624 1.2573 0.8475 -0.6138 0.0790  -0.0996 75  PRO A CB  
589  C CG  . PRO A 76  ? 1.8365 1.2698 0.8756 -0.6190 0.0593  -0.0901 75  PRO A CG  
590  C CD  . PRO A 76  ? 1.8198 1.2783 0.9130 -0.6024 0.0730  -0.0913 75  PRO A CD  
591  N N   . THR A 77  ? 1.8186 1.1928 0.8309 -0.5691 0.1483  -0.1220 76  THR A N   
592  C CA  . THR A 77  ? 1.7897 1.1588 0.8064 -0.5536 0.1771  -0.1229 76  THR A CA  
593  C C   . THR A 77  ? 1.8675 1.1984 0.8506 -0.5463 0.1972  -0.1382 76  THR A C   
594  O O   . THR A 77  ? 2.0303 1.3534 1.0196 -0.5450 0.1931  -0.1483 76  THR A O   
595  C CB  . THR A 77  ? 1.6872 1.0955 0.7776 -0.5385 0.1836  -0.1181 76  THR A CB  
596  O OG1 . THR A 77  ? 1.8011 1.2120 0.9171 -0.5311 0.1810  -0.1281 76  THR A OG1 
597  C CG2 . THR A 77  ? 1.3938 0.8410 0.5212 -0.5448 0.1639  -0.1036 76  THR A CG2 
598  N N   . GLU A 78  ? 1.9244 1.2307 0.8724 -0.5406 0.2202  -0.1393 77  GLU A N   
599  C CA  . GLU A 78  ? 2.0030 1.2714 0.9179 -0.5330 0.2416  -0.1538 77  GLU A CA  
600  C C   . GLU A 78  ? 1.9221 1.2000 0.8843 -0.5204 0.2485  -0.1629 77  GLU A C   
601  O O   . GLU A 78  ? 2.0335 1.2883 0.9750 -0.5227 0.2453  -0.1750 77  GLU A O   
602  C CB  . GLU A 78  ? 2.0971 1.3455 0.9852 -0.5233 0.2719  -0.1513 77  GLU A CB  
603  C CG  . GLU A 78  ? 2.2327 1.4340 1.0689 -0.5186 0.2921  -0.1666 77  GLU A CG  
604  C CD  . GLU A 78  ? 2.3889 1.5621 1.1774 -0.5125 0.3190  -0.1631 77  GLU A CD  
605  O OE1 . GLU A 78  ? 2.4654 1.6590 1.2738 -0.5084 0.3278  -0.1480 77  GLU A OE1 
606  O OE2 . GLU A 78  ? 2.3600 1.4896 1.0907 -0.5111 0.3322  -0.1753 77  GLU A OE2 
607  N N   . GLU A 79  ? 1.9064 1.2175 0.9324 -0.5069 0.2565  -0.1573 78  GLU A N   
608  C CA  . GLU A 79  ? 1.9476 1.2673 1.0185 -0.4929 0.2612  -0.1661 78  GLU A CA  
609  C C   . GLU A 79  ? 1.9833 1.2987 1.0474 -0.5002 0.2398  -0.1727 78  GLU A C   
610  O O   . GLU A 79  ? 1.9695 1.2664 1.0313 -0.4930 0.2469  -0.1842 78  GLU A O   
611  C CB  . GLU A 79  ? 2.0292 1.3910 1.1736 -0.4800 0.2612  -0.1585 78  GLU A CB  
612  C CG  . GLU A 79  ? 2.2192 1.6160 1.3883 -0.4890 0.2357  -0.1466 78  GLU A CG  
613  C CD  . GLU A 79  ? 2.2383 1.6750 1.4816 -0.4748 0.2312  -0.1431 78  GLU A CD  
614  O OE1 . GLU A 79  ? 2.1456 1.6000 1.4119 -0.4741 0.2116  -0.1441 78  GLU A OE1 
615  O OE2 . GLU A 79  ? 2.2066 1.6557 1.4851 -0.4639 0.2474  -0.1392 78  GLU A OE2 
616  N N   . ASN A 80  ? 1.9791 1.3110 1.0417 -0.5143 0.2149  -0.1647 79  ASN A N   
617  C CA  . ASN A 80  ? 1.8837 1.2126 0.9427 -0.5223 0.1954  -0.1683 79  ASN A CA  
618  C C   . ASN A 80  ? 1.9974 1.2832 0.9979 -0.5334 0.1950  -0.1789 79  ASN A C   
619  O O   . ASN A 80  ? 2.0561 1.3264 1.0557 -0.5301 0.1958  -0.1879 79  ASN A O   
620  C CB  . ASN A 80  ? 1.8153 1.1736 0.8922 -0.5346 0.1702  -0.1559 79  ASN A CB  
621  C CG  . ASN A 80  ? 1.7517 1.1515 0.8924 -0.5224 0.1647  -0.1491 79  ASN A CG  
622  O OD1 . ASN A 80  ? 1.7556 1.1601 0.9263 -0.5056 0.1738  -0.1552 79  ASN A OD1 
623  N ND2 . ASN A 80  ? 1.5679 0.9968 0.7288 -0.5303 0.1484  -0.1368 79  ASN A ND2 
624  N N   . LEU A 81  ? 1.9880 1.2533 0.9391 -0.5459 0.1927  -0.1780 80  LEU A N   
625  C CA  . LEU A 81  ? 2.0237 1.2460 0.9169 -0.5565 0.1899  -0.1895 80  LEU A CA  
626  C C   . LEU A 81  ? 2.0884 1.2814 0.9687 -0.5439 0.2136  -0.2034 80  LEU A C   
627  O O   . LEU A 81  ? 2.1816 1.3453 1.0354 -0.5489 0.2105  -0.2145 80  LEU A O   
628  C CB  . LEU A 81  ? 2.0428 1.2443 0.8803 -0.5681 0.1856  -0.1877 80  LEU A CB  
629  C CG  . LEU A 81  ? 2.1124 1.3240 0.9417 -0.5870 0.1546  -0.1799 80  LEU A CG  
630  C CD1 . LEU A 81  ? 2.1040 1.3651 0.9931 -0.5857 0.1442  -0.1644 80  LEU A CD1 
631  C CD2 . LEU A 81  ? 2.2057 1.3922 0.9742 -0.5957 0.1504  -0.1794 80  LEU A CD2 
632  N N   . ASP A 82  ? 2.0929 1.2936 0.9952 -0.5275 0.2373  -0.2027 81  ASP A N   
633  C CA  . ASP A 82  ? 2.2362 1.4117 1.1337 -0.5140 0.2611  -0.2152 81  ASP A CA  
634  C C   . ASP A 82  ? 2.1735 1.3566 1.1074 -0.5071 0.2550  -0.2204 81  ASP A C   
635  O O   . ASP A 82  ? 2.2378 1.3912 1.1531 -0.5038 0.2637  -0.2325 81  ASP A O   
636  C CB  . ASP A 82  ? 2.3408 1.5255 1.2625 -0.4977 0.2878  -0.2121 81  ASP A CB  
637  C CG  . ASP A 82  ? 2.4536 1.6157 1.3247 -0.5014 0.3024  -0.2096 81  ASP A CG  
638  O OD1 . ASP A 82  ? 2.4488 1.5854 1.2615 -0.5158 0.2902  -0.2124 81  ASP A OD1 
639  O OD2 . ASP A 82  ? 2.4724 1.6411 1.3623 -0.4890 0.3261  -0.2047 81  ASP A OD2 
640  N N   . TYR A 83  ? 2.0574 1.2786 1.0409 -0.5045 0.2401  -0.2111 82  TYR A N   
641  C CA  . TYR A 83  ? 2.0430 1.2716 1.0575 -0.4971 0.2327  -0.2140 82  TYR A CA  
642  C C   . TYR A 83  ? 2.1059 1.3131 1.0896 -0.5122 0.2171  -0.2174 82  TYR A C   
643  O O   . TYR A 83  ? 2.0606 1.2527 1.0472 -0.5069 0.2190  -0.2242 82  TYR A O   
644  C CB  . TYR A 83  ? 1.9334 1.2062 1.0034 -0.4899 0.2200  -0.2031 82  TYR A CB  
645  C CG  . TYR A 83  ? 1.9832 1.2782 1.0976 -0.4714 0.2337  -0.2019 82  TYR A CG  
646  C CD1 . TYR A 83  ? 2.0027 1.2860 1.1342 -0.4539 0.2504  -0.2117 82  TYR A CD1 
647  C CD2 . TYR A 83  ? 1.9693 1.2972 1.1130 -0.4715 0.2288  -0.1909 82  TYR A CD2 
648  C CE1 . TYR A 83  ? 2.0313 1.3350 1.2097 -0.4370 0.2615  -0.2111 82  TYR A CE1 
649  C CE2 . TYR A 83  ? 1.9393 1.2876 1.1296 -0.4548 0.2405  -0.1901 82  TYR A CE2 
650  C CZ  . TYR A 83  ? 1.9820 1.3182 1.1906 -0.4377 0.2564  -0.2003 82  TYR A CZ  
651  O OH  . TYR A 83  ? 1.9388 1.2951 1.1993 -0.4211 0.2666  -0.2000 82  TYR A OH  
652  N N   . VAL A 84  ? 2.1011 1.3070 1.0580 -0.5308 0.2011  -0.2121 83  VAL A N   
653  C CA  . VAL A 84  ? 1.9696 1.1550 0.9008 -0.5469 0.1846  -0.2152 83  VAL A CA  
654  C C   . VAL A 84  ? 2.1266 1.2647 1.0077 -0.5505 0.1949  -0.2304 83  VAL A C   
655  O O   . VAL A 84  ? 2.2815 1.4002 1.1610 -0.5500 0.1952  -0.2376 83  VAL A O   
656  C CB  . VAL A 84  ? 1.7759 0.9741 0.6973 -0.5658 0.1619  -0.2056 83  VAL A CB  
657  C CG1 . VAL A 84  ? 1.6497 0.8236 0.5468 -0.5831 0.1446  -0.2101 83  VAL A CG1 
658  C CG2 . VAL A 84  ? 1.6459 0.8902 0.6190 -0.5625 0.1512  -0.1910 83  VAL A CG2 
659  N N   . ILE A 85  ? 2.1080 1.2259 0.9473 -0.5532 0.2039  -0.2350 84  ILE A N   
660  C CA  . ILE A 85  ? 2.1885 1.2591 0.9764 -0.5554 0.2142  -0.2507 84  ILE A CA  
661  C C   . ILE A 85  ? 2.2615 1.3201 1.0668 -0.5386 0.2355  -0.2597 84  ILE A C   
662  O O   . ILE A 85  ? 2.3964 1.4176 1.1704 -0.5397 0.2421  -0.2730 84  ILE A O   
663  C CB  . ILE A 85  ? 2.1595 1.2078 0.8956 -0.5567 0.2253  -0.2542 84  ILE A CB  
664  C CG1 . ILE A 85  ? 2.3257 1.3857 1.0815 -0.5380 0.2535  -0.2513 84  ILE A CG1 
665  C CG2 . ILE A 85  ? 2.0857 1.1456 0.8035 -0.5718 0.2034  -0.2445 84  ILE A CG2 
666  C CD1 . ILE A 85  ? 2.4567 1.4971 1.1643 -0.5376 0.2674  -0.2513 84  ILE A CD1 
667  N N   . ARG A 86  ? 2.1244 1.2143 0.9808 -0.5227 0.2447  -0.2530 85  ARG A N   
668  C CA  . ARG A 86  ? 2.1585 1.2403 1.0372 -0.5049 0.2634  -0.2607 85  ARG A CA  
669  C C   . ARG A 86  ? 2.2889 1.3718 1.1908 -0.5032 0.2527  -0.2612 85  ARG A C   
670  O O   . ARG A 86  ? 2.3883 1.4462 1.2852 -0.4955 0.2637  -0.2713 85  ARG A O   
671  C CB  . ARG A 86  ? 2.2001 1.3120 1.1239 -0.4871 0.2774  -0.2547 85  ARG A CB  
672  C CG  . ARG A 86  ? 2.3807 1.4994 1.3476 -0.4677 0.2862  -0.2586 85  ARG A CG  
673  C CD  . ARG A 86  ? 2.5246 1.6757 1.5409 -0.4516 0.2956  -0.2527 85  ARG A CD  
674  N NE  . ARG A 86  ? 2.5917 1.7574 1.6562 -0.4330 0.2953  -0.2545 85  ARG A NE  
675  C CZ  . ARG A 86  ? 2.6061 1.8037 1.7085 -0.4279 0.2776  -0.2465 85  ARG A CZ  
676  N NH1 . ARG A 86  ? 2.6202 1.8400 1.7216 -0.4407 0.2599  -0.2358 85  ARG A NH1 
677  N NH2 . ARG A 86  ? 2.5731 1.7793 1.7134 -0.4090 0.2771  -0.2496 85  ARG A NH2 
678  N N   . ASP A 87  ? 2.2561 1.3670 1.1831 -0.5098 0.2325  -0.2498 86  ASP A N   
679  C CA  . ASP A 87  ? 2.1937 1.3060 1.1416 -0.5076 0.2235  -0.2476 86  ASP A CA  
680  C C   . ASP A 87  ? 2.2138 1.2878 1.1263 -0.5214 0.2189  -0.2561 86  ASP A C   
681  O O   . ASP A 87  ? 2.0417 1.1064 0.9658 -0.5183 0.2175  -0.2566 86  ASP A O   
682  C CB  . ASP A 87  ? 2.2177 1.3677 1.1983 -0.5118 0.2045  -0.2326 86  ASP A CB  
683  C CG  . ASP A 87  ? 2.3135 1.4999 1.3385 -0.4937 0.2079  -0.2258 86  ASP A CG  
684  O OD1 . ASP A 87  ? 2.4135 1.5968 1.4488 -0.4777 0.2243  -0.2324 86  ASP A OD1 
685  O OD2 . ASP A 87  ? 2.2927 1.5105 1.3446 -0.4952 0.1938  -0.2141 86  ASP A OD2 
686  N N   . PHE A 88  ? 2.3338 1.3840 1.2024 -0.5359 0.2165  -0.2630 87  PHE A N   
687  C CA  . PHE A 88  ? 2.4060 1.4183 1.2408 -0.5495 0.2100  -0.2730 87  PHE A CA  
688  C C   . PHE A 88  ? 2.5810 1.5528 1.3753 -0.5448 0.2286  -0.2898 87  PHE A C   
689  O O   . PHE A 88  ? 2.6983 1.6462 1.4921 -0.5384 0.2382  -0.2985 87  PHE A O   
690  C CB  . PHE A 88  ? 2.3615 1.3745 1.1771 -0.5715 0.1864  -0.2689 87  PHE A CB  
691  C CG  . PHE A 88  ? 2.3150 1.3616 1.1714 -0.5777 0.1683  -0.2535 87  PHE A CG  
692  C CD1 . PHE A 88  ? 2.3130 1.3538 1.1899 -0.5807 0.1622  -0.2509 87  PHE A CD1 
693  C CD2 . PHE A 88  ? 2.2721 1.3552 1.1473 -0.5798 0.1589  -0.2408 87  PHE A CD2 
694  C CE1 . PHE A 88  ? 2.2277 1.2982 1.1420 -0.5853 0.1485  -0.2358 87  PHE A CE1 
695  C CE2 . PHE A 88  ? 2.1884 1.3016 1.1014 -0.5848 0.1437  -0.2267 87  PHE A CE2 
696  C CZ  . PHE A 88  ? 2.1685 1.2752 1.1004 -0.5872 0.1392  -0.2242 87  PHE A CZ  
697  N N   . ALA A 89  ? 2.5600 1.5232 1.3195 -0.5473 0.2344  -0.2936 88  ALA A N   
698  C CA  . ALA A 89  ? 2.5690 1.4957 1.2887 -0.5402 0.2561  -0.3083 88  ALA A CA  
699  C C   . ALA A 89  ? 2.5824 1.4794 1.3022 -0.5320 0.2690  -0.3206 88  ALA A C   
700  O O   . ALA A 89  ? 2.5558 1.4133 1.2359 -0.5403 0.2674  -0.3339 88  ALA A O   
701  C CB  . ALA A 89  ? 2.4688 1.4137 1.2003 -0.5250 0.2771  -0.3037 88  ALA A CB  
702  N N   . ASP A 90  ? 2.6130 1.5283 1.3775 -0.5152 0.2809  -0.3165 89  ASP A N   
703  C CA  . ASP A 90  ? 2.7672 1.6572 1.5370 -0.5042 0.2951  -0.3268 89  ASP A CA  
704  C C   . ASP A 90  ? 2.7807 1.6463 1.5405 -0.5162 0.2813  -0.3316 89  ASP A C   
705  O O   . ASP A 90  ? 2.7270 1.5974 1.4812 -0.5331 0.2596  -0.3263 89  ASP A O   
706  C CB  . ASP A 90  ? 2.8586 1.7774 1.6825 -0.4841 0.3039  -0.3194 89  ASP A CB  
707  C CG  . ASP A 90  ? 3.0202 1.9132 1.8496 -0.4693 0.3224  -0.3303 89  ASP A CG  
708  O OD1 . ASP A 90  ? 3.0936 1.9598 1.8968 -0.4650 0.3417  -0.3421 89  ASP A OD1 
709  O OD2 . ASP A 90  ? 3.0346 1.9333 1.8939 -0.4612 0.3182  -0.3266 89  ASP A OD2 
710  N N   . ARG A 91  ? 2.8448 1.6840 1.6059 -0.5070 0.2944  -0.3413 90  ARG A N   
711  C CA  . ARG A 91  ? 2.8827 1.6951 1.6379 -0.5162 0.2852  -0.3464 90  ARG A CA  
712  C C   . ARG A 91  ? 2.7418 1.5799 1.5290 -0.5247 0.2644  -0.3311 90  ARG A C   
713  O O   . ARG A 91  ? 2.6132 1.4447 1.3871 -0.5436 0.2457  -0.3302 90  ARG A O   
714  C CB  . ARG A 91  ? 2.9687 1.7602 1.7364 -0.5000 0.3037  -0.3541 90  ARG A CB  
715  C CG  . ARG A 91  ? 3.0325 1.8064 1.8115 -0.5048 0.2956  -0.3536 90  ARG A CG  
716  C CD  . ARG A 91  ? 3.1155 1.8427 1.8543 -0.5181 0.2943  -0.3703 90  ARG A CD  
717  N NE  . ARG A 91  ? 3.1625 1.8590 1.8814 -0.5058 0.3171  -0.3859 90  ARG A NE  
718  C CZ  . ARG A 91  ? 3.2011 1.8533 1.8878 -0.5120 0.3208  -0.4026 90  ARG A CZ  
719  N NH1 . ARG A 91  ? 3.1937 1.8273 1.8666 -0.5306 0.3017  -0.4061 90  ARG A NH1 
720  N NH2 . ARG A 91  ? 3.2341 1.8604 1.9052 -0.4993 0.3434  -0.4160 90  ARG A NH2 
721  N N   . THR A 92  ? 2.7183 1.5843 1.5479 -0.5097 0.2676  -0.3194 91  THR A N   
722  C CA  . THR A 92  ? 2.6532 1.5446 1.5143 -0.5139 0.2518  -0.3035 91  THR A CA  
723  C C   . THR A 92  ? 2.5953 1.5273 1.4706 -0.5177 0.2402  -0.2911 91  THR A C   
724  O O   . THR A 92  ? 2.5232 1.4782 1.4119 -0.5044 0.2483  -0.2887 91  THR A O   
725  C CB  . THR A 92  ? 2.5829 1.4822 1.4784 -0.4940 0.2600  -0.2965 91  THR A CB  
726  O OG1 . THR A 92  ? 2.6817 1.5428 1.5656 -0.4902 0.2709  -0.3073 91  THR A OG1 
727  C CG2 . THR A 92  ? 2.3869 1.3092 1.3106 -0.4972 0.2459  -0.2793 91  THR A CG2 
728  N N   . PRO A 93  ? 2.5282 1.4691 1.4041 -0.5360 0.2208  -0.2833 92  PRO A N   
729  C CA  . PRO A 93  ? 2.4502 1.4289 1.3407 -0.5416 0.2079  -0.2709 92  PRO A CA  
730  C C   . PRO A 93  ? 2.3227 1.3369 1.2568 -0.5256 0.2087  -0.2565 92  PRO A C   
731  O O   . PRO A 93  ? 2.4104 1.4174 1.3606 -0.5137 0.2153  -0.2545 92  PRO A O   
732  C CB  . PRO A 93  ? 2.4372 1.4095 1.3216 -0.5646 0.1872  -0.2673 92  PRO A CB  
733  C CG  . PRO A 93  ? 2.3182 1.2621 1.2067 -0.5659 0.1900  -0.2707 92  PRO A CG  
734  C CD  . PRO A 93  ? 2.4191 1.3350 1.2883 -0.5519 0.2100  -0.2851 92  PRO A CD  
735  N N   . THR A 94  ? 2.1268 1.1772 1.0779 -0.5244 0.2017  -0.2469 93  THR A N   
736  C CA  . THR A 94  ? 1.9467 1.0305 0.9367 -0.5072 0.2019  -0.2353 93  THR A CA  
737  C C   . THR A 94  ? 1.8120 0.9142 0.8243 -0.5143 0.1878  -0.2203 93  THR A C   
738  O O   . THR A 94  ? 1.7182 0.8347 0.7560 -0.4991 0.1895  -0.2116 93  THR A O   
739  C CB  . THR A 94  ? 1.9528 1.0669 0.9560 -0.4985 0.2039  -0.2332 93  THR A CB  
740  O OG1 . THR A 94  ? 1.9980 1.0968 0.9918 -0.4858 0.2214  -0.2453 93  THR A OG1 
741  C CG2 . THR A 94  ? 1.9330 1.0824 0.9762 -0.4828 0.1991  -0.2215 93  THR A CG2 
742  N N   . TYR A 95  ? 1.8521 0.9526 0.8546 -0.5365 0.1738  -0.2172 94  TYR A N   
743  C CA  . TYR A 95  ? 1.8597 0.9721 0.8848 -0.5453 0.1620  -0.2034 94  TYR A CA  
744  C C   . TYR A 95  ? 1.9226 1.0042 0.9312 -0.5671 0.1536  -0.2079 94  TYR A C   
745  O O   . TYR A 95  ? 1.8060 0.8594 0.7820 -0.5755 0.1545  -0.2223 94  TYR A O   
746  C CB  . TYR A 95  ? 1.8056 0.9579 0.8514 -0.5493 0.1497  -0.1914 94  TYR A CB  
747  C CG  . TYR A 95  ? 1.8565 1.0379 0.9216 -0.5276 0.1566  -0.1885 94  TYR A CG  
748  C CD1 . TYR A 95  ? 1.7347 0.9245 0.8216 -0.5066 0.1636  -0.1830 94  TYR A CD1 
749  C CD2 . TYR A 95  ? 1.7736 0.9727 0.8355 -0.5274 0.1554  -0.1912 94  TYR A CD2 
750  C CE1 . TYR A 95  ? 1.7161 0.9306 0.8221 -0.4864 0.1669  -0.1820 94  TYR A CE1 
751  C CE2 . TYR A 95  ? 1.6703 0.8956 0.7554 -0.5079 0.1607  -0.1892 94  TYR A CE2 
752  C CZ  . TYR A 95  ? 1.7492 0.9824 0.8572 -0.4874 0.1652  -0.1854 94  TYR A CZ  
753  O OH  . TYR A 95  ? 1.5701 0.8282 0.7031 -0.4671 0.1674  -0.1849 94  TYR A OH  
754  N N   . GLU A 96  ? 1.9575 1.0425 0.9895 -0.5753 0.1461  -0.1962 95  GLU A N   
755  C CA  . GLU A 96  ? 1.9451 1.0033 0.9695 -0.5968 0.1356  -0.2003 95  GLU A CA  
756  C C   . GLU A 96  ? 1.9930 1.0529 0.9970 -0.6161 0.1179  -0.2064 95  GLU A C   
757  O O   . GLU A 96  ? 2.1463 1.1762 1.1265 -0.6316 0.1090  -0.2182 95  GLU A O   
758  C CB  . GLU A 96  ? 1.8747 0.9400 0.9355 -0.6026 0.1313  -0.1841 95  GLU A CB  
759  C CG  . GLU A 96  ? 2.2736 1.3061 1.3336 -0.6225 0.1228  -0.1893 95  GLU A CG  
760  C CD  . GLU A 96  ? 2.2882 1.3258 1.3899 -0.6275 0.1222  -0.1719 95  GLU A CD  
761  O OE1 . GLU A 96  ? 2.2373 1.2677 1.3530 -0.6490 0.1064  -0.1709 95  GLU A OE1 
762  O OE2 . GLU A 96  ? 2.2851 1.3325 1.4057 -0.6095 0.1374  -0.1593 95  GLU A OE2 
763  N N   . ALA A 97  ? 1.8692 0.9633 0.8818 -0.6140 0.1122  -0.1988 96  ALA A N   
764  C CA  . ALA A 97  ? 1.9287 1.0278 0.9217 -0.6296 0.0960  -0.2023 96  ALA A CA  
765  C C   . ALA A 97  ? 1.9646 1.1041 0.9724 -0.6212 0.0955  -0.1924 96  ALA A C   
766  O O   . ALA A 97  ? 1.9106 1.0753 0.9480 -0.6055 0.1042  -0.1824 96  ALA A O   
767  C CB  . ALA A 97  ? 1.8627 0.9574 0.8679 -0.6525 0.0741  -0.1979 96  ALA A CB  
768  N N   . ALA A 98  ? 2.0161 1.1600 1.0021 -0.6309 0.0849  -0.1955 97  ALA A N   
769  C CA  . ALA A 98  ? 1.9162 1.0969 0.9163 -0.6246 0.0836  -0.1862 97  ALA A CA  
770  C C   . ALA A 98  ? 1.9483 1.1495 0.9631 -0.6423 0.0608  -0.1756 97  ALA A C   
771  O O   . ALA A 98  ? 2.0125 1.1941 1.0045 -0.6604 0.0445  -0.1811 97  ALA A O   
772  C CB  . ALA A 98  ? 1.7596 0.9315 0.7249 -0.6177 0.0939  -0.1962 97  ALA A CB  
773  N N   . HIS A 99  ? 1.8571 1.0969 0.9106 -0.6366 0.0587  -0.1610 98  HIS A N   
774  C CA  . HIS A 99  ? 1.8660 1.1297 0.9382 -0.6514 0.0384  -0.1499 98  HIS A CA  
775  C C   . HIS A 99  ? 1.8199 1.1141 0.8975 -0.6427 0.0406  -0.1444 98  HIS A C   
776  O O   . HIS A 99  ? 1.9348 1.2557 1.0419 -0.6267 0.0503  -0.1372 98  HIS A O   
777  C CB  . HIS A 99  ? 1.8609 1.1431 0.9788 -0.6535 0.0339  -0.1360 98  HIS A CB  
778  C CG  . HIS A 99  ? 1.8951 1.1482 1.0141 -0.6626 0.0324  -0.1394 98  HIS A CG  
779  N ND1 . HIS A 99  ? 2.0346 1.2769 1.1589 -0.6846 0.0123  -0.1386 98  HIS A ND1 
780  C CD2 . HIS A 99  ? 1.8424 1.0739 0.9599 -0.6527 0.0481  -0.1438 98  HIS A CD2 
781  C CE1 . HIS A 99  ? 1.9644 1.1803 1.0930 -0.6882 0.0163  -0.1422 98  HIS A CE1 
782  N NE2 . HIS A 99  ? 1.8890 1.0977 1.0123 -0.6690 0.0386  -0.1449 98  HIS A NE2 
783  N N   . LEU A 100 ? 1.7928 1.0807 0.8404 -0.6525 0.0312  -0.1480 99  LEU A N   
784  C CA  . LEU A 100 ? 1.6744 0.9838 0.7201 -0.6438 0.0368  -0.1446 99  LEU A CA  
785  C C   . LEU A 100 ? 1.6089 0.9511 0.6798 -0.6534 0.0187  -0.1305 99  LEU A C   
786  O O   . LEU A 100 ? 1.7280 1.0619 0.7822 -0.6709 -0.0005 -0.1296 99  LEU A O   
787  C CB  . LEU A 100 ? 1.7511 1.0303 0.7435 -0.6450 0.0429  -0.1567 99  LEU A CB  
788  C CG  . LEU A 100 ? 1.7365 0.9817 0.7028 -0.6352 0.0619  -0.1714 99  LEU A CG  
789  C CD1 . LEU A 100 ? 1.7963 1.0100 0.7072 -0.6367 0.0683  -0.1830 99  LEU A CD1 
790  C CD2 . LEU A 100 ? 1.5735 0.8367 0.5703 -0.6133 0.0824  -0.1699 99  LEU A CD2 
791  N N   . PHE A 101 ? 1.5127 0.8914 0.6243 -0.6413 0.0239  -0.1203 100 PHE A N   
792  C CA  . PHE A 101 ? 1.6557 1.0683 0.7945 -0.6476 0.0095  -0.1068 100 PHE A CA  
793  C C   . PHE A 101 ? 1.7223 1.1527 0.8602 -0.6368 0.0183  -0.1048 100 PHE A C   
794  O O   . PHE A 101 ? 1.6530 1.0998 0.8140 -0.6185 0.0332  -0.1048 100 PHE A O   
795  C CB  . PHE A 101 ? 1.6401 1.0820 0.8294 -0.6418 0.0082  -0.0959 100 PHE A CB  
796  C CG  . PHE A 101 ? 1.7226 1.1512 0.9212 -0.6525 0.0007  -0.0942 100 PHE A CG  
797  C CD1 . PHE A 101 ? 1.6947 1.0976 0.8825 -0.6457 0.0135  -0.1023 100 PHE A CD1 
798  C CD2 . PHE A 101 ? 1.7604 1.2022 0.9822 -0.6692 -0.0186 -0.0838 100 PHE A CD2 
799  C CE1 . PHE A 101 ? 1.6476 1.0378 0.8475 -0.6555 0.0082  -0.0996 100 PHE A CE1 
800  C CE2 . PHE A 101 ? 1.5970 1.0267 0.8335 -0.6792 -0.0243 -0.0814 100 PHE A CE2 
801  C CZ  . PHE A 101 ? 1.6604 1.0641 0.8860 -0.6723 -0.0103 -0.0890 100 PHE A CZ  
802  N N   . PHE A 102 ? 1.7728 1.1996 0.8857 -0.6476 0.0084  -0.1026 101 PHE A N   
803  C CA  . PHE A 102 ? 1.7178 1.1588 0.8290 -0.6381 0.0184  -0.0993 101 PHE A CA  
804  C C   . PHE A 102 ? 1.7448 1.2282 0.9006 -0.6378 0.0087  -0.0845 101 PHE A C   
805  O O   . PHE A 102 ? 1.7798 1.2755 0.9491 -0.6520 -0.0116 -0.0758 101 PHE A O   
806  C CB  . PHE A 102 ? 1.6653 1.0768 0.7206 -0.6459 0.0177  -0.1045 101 PHE A CB  
807  C CG  . PHE A 102 ? 1.7806 1.1524 0.7935 -0.6404 0.0341  -0.1200 101 PHE A CG  
808  C CD1 . PHE A 102 ? 1.8417 1.2134 0.8641 -0.6217 0.0589  -0.1257 101 PHE A CD1 
809  C CD2 . PHE A 102 ? 1.8610 1.1950 0.8267 -0.6535 0.0239  -0.1296 101 PHE A CD2 
810  C CE1 . PHE A 102 ? 1.8612 1.1964 0.8466 -0.6163 0.0749  -0.1399 101 PHE A CE1 
811  C CE2 . PHE A 102 ? 1.8541 1.1507 0.7806 -0.6480 0.0396  -0.1446 101 PHE A CE2 
812  C CZ  . PHE A 102 ? 1.7938 1.0912 0.7302 -0.6295 0.0658  -0.1493 101 PHE A CZ  
813  N N   . LEU A 103 ? 1.7812 1.2865 0.9630 -0.6213 0.0230  -0.0821 102 LEU A N   
814  C CA  . LEU A 103 ? 1.7122 1.2590 0.9427 -0.6171 0.0165  -0.0697 102 LEU A CA  
815  C C   . LEU A 103 ? 1.7544 1.3119 0.9783 -0.6299 0.0026  -0.0588 102 LEU A C   
816  O O   . LEU A 103 ? 1.7359 1.3229 0.9950 -0.6350 -0.0117 -0.0475 102 LEU A O   
817  C CB  . LEU A 103 ? 1.7208 1.2841 0.9799 -0.5957 0.0346  -0.0722 102 LEU A CB  
818  C CG  . LEU A 103 ? 1.6862 1.2422 0.9564 -0.5805 0.0462  -0.0821 102 LEU A CG  
819  C CD1 . LEU A 103 ? 1.7703 1.3467 1.0763 -0.5592 0.0592  -0.0842 102 LEU A CD1 
820  C CD2 . LEU A 103 ? 1.6159 1.1836 0.9089 -0.5838 0.0340  -0.0774 102 LEU A CD2 
821  N N   . SER A 104 ? 1.7064 1.2390 0.8841 -0.6337 0.0078  -0.0620 103 SER A N   
822  C CA  . SER A 104 ? 1.7974 1.3285 0.9526 -0.6479 -0.0082 -0.0531 103 SER A CA  
823  C C   . SER A 104 ? 1.9638 1.4492 1.0501 -0.6557 -0.0077 -0.0629 103 SER A C   
824  O O   . SER A 104 ? 1.9586 1.4178 1.0208 -0.6488 0.0078  -0.0757 103 SER A O   
825  C CB  . SER A 104 ? 1.6726 1.2298 0.8503 -0.6401 -0.0013 -0.0418 103 SER A CB  
826  O OG  . SER A 104 ? 1.6604 1.2150 0.8425 -0.6225 0.0247  -0.0472 103 SER A OG  
827  N N   . PRO A 105 ? 2.0349 1.5096 1.0886 -0.6695 -0.0261 -0.0576 104 PRO A N   
828  C CA  . PRO A 105 ? 2.0025 1.4319 0.9861 -0.6768 -0.0298 -0.0674 104 PRO A CA  
829  C C   . PRO A 105 ? 2.0047 1.4037 0.9464 -0.6634 -0.0015 -0.0782 104 PRO A C   
830  O O   . PRO A 105 ? 2.0335 1.4443 0.9863 -0.6498 0.0201  -0.0731 104 PRO A O   
831  C CB  . PRO A 105 ? 1.9569 1.3895 0.9202 -0.6859 -0.0476 -0.0556 104 PRO A CB  
832  C CG  . PRO A 105 ? 1.9620 1.4360 0.9870 -0.6932 -0.0666 -0.0430 104 PRO A CG  
833  C CD  . PRO A 105 ? 2.0305 1.5344 1.1129 -0.6794 -0.0479 -0.0426 104 PRO A CD  
834  N N   . VAL A 106 ? 2.1089 1.4683 1.0049 -0.6676 -0.0020 -0.0931 105 VAL A N   
835  C CA  . VAL A 106 ? 2.2200 1.5457 1.0734 -0.6559 0.0241  -0.1053 105 VAL A CA  
836  C C   . VAL A 106 ? 2.3512 1.6401 1.1312 -0.6584 0.0239  -0.1078 105 VAL A C   
837  O O   . VAL A 106 ? 2.3533 1.6193 1.0944 -0.6723 -0.0010 -0.1119 105 VAL A O   
838  C CB  . VAL A 106 ? 2.0821 1.3834 0.9280 -0.6573 0.0259  -0.1214 105 VAL A CB  
839  C CG1 . VAL A 106 ? 1.9980 1.2964 0.8492 -0.6756 -0.0053 -0.1228 105 VAL A CG1 
840  C CG2 . VAL A 106 ? 2.0777 1.3317 0.8590 -0.6516 0.0432  -0.1361 105 VAL A CG2 
841  N N   . PRO A 107 ? 2.4234 1.7051 1.1846 -0.6441 0.0518  -0.1053 106 PRO A N   
842  C CA  . PRO A 107 ? 2.4632 1.7081 1.1511 -0.6424 0.0579  -0.1062 106 PRO A CA  
843  C C   . PRO A 107 ? 2.4559 1.6502 1.0790 -0.6466 0.0541  -0.1254 106 PRO A C   
844  O O   . PRO A 107 ? 2.3212 1.5089 0.9602 -0.6470 0.0566  -0.1378 106 PRO A O   
845  C CB  . PRO A 107 ? 2.4865 1.7363 1.1843 -0.6234 0.0961  -0.1014 106 PRO A CB  
846  C CG  . PRO A 107 ? 2.4388 1.7379 1.2212 -0.6179 0.1004  -0.0928 106 PRO A CG  
847  C CD  . PRO A 107 ? 2.4216 1.7300 1.2335 -0.6274 0.0799  -0.1011 106 PRO A CD  
848  N N   . ASP A 108 ? 2.6066 1.7641 1.1562 -0.6488 0.0482  -0.1277 107 ASP A N   
849  C CA  . ASP A 108 ? 2.7999 1.9062 1.2821 -0.6532 0.0404  -0.1469 107 ASP A CA  
850  C C   . ASP A 108 ? 2.7417 1.8186 1.1959 -0.6377 0.0769  -0.1591 107 ASP A C   
851  O O   . ASP A 108 ? 2.6400 1.6869 1.0715 -0.6399 0.0758  -0.1769 107 ASP A O   
852  C CB  . ASP A 108 ? 2.9862 2.0608 1.3947 -0.6590 0.0197  -0.1460 107 ASP A CB  
853  C CG  . ASP A 108 ? 3.0241 2.1251 1.4593 -0.6748 -0.0188 -0.1346 107 ASP A CG  
854  O OD1 . ASP A 108 ? 2.9807 2.1183 1.4862 -0.6835 -0.0320 -0.1308 107 ASP A OD1 
855  O OD2 . ASP A 108 ? 3.0688 2.1528 1.4537 -0.6777 -0.0356 -0.1292 107 ASP A OD2 
856  N N   . ALA A 109 ? 2.7158 1.8010 1.1743 -0.6221 0.1096  -0.1492 108 ALA A N   
857  C CA  . ALA A 109 ? 2.6956 1.7547 1.1324 -0.6062 0.1471  -0.1589 108 ALA A CA  
858  C C   . ALA A 109 ? 2.5997 1.6711 1.0890 -0.6043 0.1542  -0.1696 108 ALA A C   
859  O O   . ALA A 109 ? 2.5569 1.5953 1.0177 -0.5982 0.1704  -0.1853 108 ALA A O   
860  C CB  . ALA A 109 ? 2.6696 1.7441 1.1215 -0.5903 0.1805  -0.1436 108 ALA A CB  
861  N N   . LEU A 110 ? 2.5594 1.6772 1.1237 -0.6088 0.1419  -0.1609 109 LEU A N   
862  C CA  . LEU A 110 ? 2.5520 1.6847 1.1688 -0.6061 0.1463  -0.1687 109 LEU A CA  
863  C C   . LEU A 110 ? 2.5770 1.6888 1.1768 -0.6205 0.1205  -0.1820 109 LEU A C   
864  O O   . LEU A 110 ? 2.5322 1.6254 1.1318 -0.6169 0.1300  -0.1955 109 LEU A O   
865  C CB  . LEU A 110 ? 2.5029 1.6905 1.2015 -0.6041 0.1420  -0.1546 109 LEU A CB  
866  C CG  . LEU A 110 ? 2.5833 1.7962 1.3205 -0.5875 0.1702  -0.1440 109 LEU A CG  
867  C CD1 . LEU A 110 ? 2.6346 1.8282 1.3719 -0.5718 0.2019  -0.1555 109 LEU A CD1 
868  C CD2 . LEU A 110 ? 2.6037 1.8127 1.3084 -0.5861 0.1765  -0.1313 109 LEU A CD2 
869  N N   . MET A 111 ? 2.5772 1.6919 1.1657 -0.6366 0.0876  -0.1777 110 MET A N   
870  C CA  . MET A 111 ? 2.4921 1.5860 1.0662 -0.6518 0.0605  -0.1895 110 MET A CA  
871  C C   . MET A 111 ? 2.5020 1.5419 1.0111 -0.6485 0.0710  -0.2093 110 MET A C   
872  O O   . MET A 111 ? 2.4875 1.5117 1.0031 -0.6518 0.0683  -0.2221 110 MET A O   
873  C CB  . MET A 111 ? 2.5133 1.6113 1.0741 -0.6684 0.0244  -0.1825 110 MET A CB  
874  C CG  . MET A 111 ? 2.5725 1.6722 1.1588 -0.6856 -0.0069 -0.1876 110 MET A CG  
875  S SD  . MET A 111 ? 2.4501 1.6067 1.1150 -0.6963 -0.0301 -0.1677 110 MET A SD  
876  C CE  . MET A 111 ? 2.0982 1.2634 0.7332 -0.6969 -0.0394 -0.1535 110 MET A CE  
877  N N   . ALA A 112 ? 2.5543 1.5652 1.0009 -0.6408 0.0846  -0.2113 111 ALA A N   
878  C CA  . ALA A 112 ? 2.6666 1.6242 1.0464 -0.6352 0.0979  -0.2302 111 ALA A CA  
879  C C   . ALA A 112 ? 2.7514 1.7064 1.1578 -0.6222 0.1294  -0.2385 111 ALA A C   
880  O O   . ALA A 112 ? 2.8456 1.7706 1.2343 -0.6246 0.1278  -0.2553 111 ALA A O   
881  C CB  . ALA A 112 ? 2.6998 1.6294 1.0095 -0.6262 0.1119  -0.2279 111 ALA A CB  
882  N N   . LYS A 113 ? 2.7495 1.7355 1.2007 -0.6084 0.1567  -0.2270 112 LYS A N   
883  C CA  . LYS A 113 ? 2.7403 1.7253 1.2203 -0.5944 0.1862  -0.2342 112 LYS A CA  
884  C C   . LYS A 113 ? 2.7231 1.7121 1.2394 -0.6014 0.1725  -0.2430 112 LYS A C   
885  O O   . LYS A 113 ? 2.7407 1.7064 1.2512 -0.5943 0.1887  -0.2563 112 LYS A O   
886  C CB  . LYS A 113 ? 2.6277 1.6539 1.1669 -0.5805 0.2096  -0.2193 112 LYS A CB  
887  C CG  . LYS A 113 ? 2.5590 1.5839 1.1296 -0.5645 0.2397  -0.2266 112 LYS A CG  
888  C CD  . LYS A 113 ? 2.5253 1.5827 1.1444 -0.5493 0.2646  -0.2134 112 LYS A CD  
889  C CE  . LYS A 113 ? 2.5248 1.5748 1.1692 -0.5323 0.2953  -0.2220 112 LYS A CE  
890  N NZ  . LYS A 113 ? 2.5132 1.5855 1.1957 -0.5168 0.3227  -0.2107 112 LYS A NZ  
891  N N   . LEU A 114 ? 2.6428 1.6610 1.1973 -0.6147 0.1437  -0.2348 113 LEU A N   
892  C CA  . LEU A 114 ? 2.4709 1.4950 1.0625 -0.6218 0.1300  -0.2398 113 LEU A CA  
893  C C   . LEU A 114 ? 2.4379 1.4169 0.9805 -0.6339 0.1130  -0.2567 113 LEU A C   
894  O O   . LEU A 114 ? 2.3588 1.3215 0.9104 -0.6334 0.1168  -0.2676 113 LEU A O   
895  C CB  . LEU A 114 ? 2.3402 1.4081 0.9863 -0.6320 0.1058  -0.2246 113 LEU A CB  
896  C CG  . LEU A 114 ? 2.1329 1.2280 0.8430 -0.6299 0.1049  -0.2207 113 LEU A CG  
897  C CD1 . LEU A 114 ? 1.9211 1.0411 0.6638 -0.6457 0.0749  -0.2105 113 LEU A CD1 
898  C CD2 . LEU A 114 ? 2.1891 1.2526 0.8890 -0.6272 0.1137  -0.2360 113 LEU A CD2 
899  N N   . ALA A 115 ? 2.4651 1.4233 0.9565 -0.6442 0.0932  -0.2589 114 ALA A N   
900  C CA  . ALA A 115 ? 2.4361 1.3509 0.8804 -0.6566 0.0716  -0.2757 114 ALA A CA  
901  C C   . ALA A 115 ? 2.5914 1.4591 0.9867 -0.6467 0.0939  -0.2950 114 ALA A C   
902  O O   . ALA A 115 ? 2.6799 1.5165 1.0595 -0.6542 0.0821  -0.3106 114 ALA A O   
903  C CB  . ALA A 115 ? 2.3178 1.2198 0.7145 -0.6674 0.0446  -0.2741 114 ALA A CB  
904  N N   . SER A 116 ? 2.6138 1.4758 0.9881 -0.6296 0.1268  -0.2939 115 SER A N   
905  C CA  . SER A 116 ? 2.6915 1.5084 1.0178 -0.6186 0.1513  -0.3114 115 SER A CA  
906  C C   . SER A 116 ? 2.6488 1.4715 1.0215 -0.6102 0.1715  -0.3166 115 SER A C   
907  O O   . SER A 116 ? 2.7143 1.4988 1.0588 -0.6077 0.1796  -0.3339 115 SER A O   
908  C CB  . SER A 116 ? 2.7876 1.5931 1.0716 -0.6032 0.1805  -0.3074 115 SER A CB  
909  O OG  . SER A 116 ? 2.8312 1.6784 1.1730 -0.5909 0.2049  -0.2918 115 SER A OG  
910  N N   . ALA A 117 ? 2.5951 1.4645 1.0378 -0.6050 0.1788  -0.3018 116 ALA A N   
911  C CA  . ALA A 117 ? 2.5745 1.4524 1.0639 -0.5953 0.1963  -0.3049 116 ALA A CA  
912  C C   . ALA A 117 ? 2.5252 1.3975 1.0362 -0.6077 0.1743  -0.3110 116 ALA A C   
913  O O   . ALA A 117 ? 2.5139 1.3917 1.0263 -0.6242 0.1443  -0.3077 116 ALA A O   
914  C CB  . ALA A 117 ? 2.4847 1.4126 1.0394 -0.5843 0.2088  -0.2880 116 ALA A CB  
915  N N   . LYS A 118 ? 2.4791 1.3405 1.0098 -0.5994 0.1898  -0.3190 117 LYS A N   
916  C CA  . LYS A 118 ? 2.4826 1.3363 1.0356 -0.6092 0.1736  -0.3240 117 LYS A CA  
917  C C   . LYS A 118 ? 2.4872 1.3815 1.0922 -0.6198 0.1504  -0.3076 117 LYS A C   
918  O O   . LYS A 118 ? 2.4185 1.3047 1.0276 -0.6355 0.1264  -0.3095 117 LYS A O   
919  C CB  . LYS A 118 ? 2.4033 1.2492 0.9814 -0.5951 0.1968  -0.3300 117 LYS A CB  
920  C CG  . LYS A 118 ? 2.3009 1.1392 0.9058 -0.6033 0.1834  -0.3328 117 LYS A CG  
921  C CD  . LYS A 118 ? 2.2727 1.1017 0.8996 -0.5880 0.2064  -0.3381 117 LYS A CD  
922  C CE  . LYS A 118 ? 2.3430 1.1589 0.9909 -0.5965 0.1943  -0.3408 117 LYS A CE  
923  N NZ  . LYS A 118 ? 2.3966 1.1983 1.0609 -0.5817 0.2156  -0.3467 117 LYS A NZ  
924  N N   . ALA A 119 ? 2.4150 1.3524 1.0617 -0.6107 0.1580  -0.2919 118 ALA A N   
925  C CA  . ALA A 119 ? 2.2708 1.2489 0.9705 -0.6172 0.1405  -0.2758 118 ALA A CA  
926  C C   . ALA A 119 ? 2.3002 1.2767 0.9919 -0.6386 0.1085  -0.2732 118 ALA A C   
927  O O   . ALA A 119 ? 2.2290 1.2271 0.9631 -0.6464 0.0936  -0.2635 118 ALA A O   
928  C CB  . ALA A 119 ? 2.1001 1.1204 0.8317 -0.6062 0.1495  -0.2611 118 ALA A CB  
929  N N   . VAL A 120 ? 2.2791 1.2288 0.9165 -0.6473 0.0980  -0.2817 119 VAL A N   
930  C CA  . VAL A 120 ? 2.1898 1.1387 0.8192 -0.6669 0.0652  -0.2793 119 VAL A CA  
931  C C   . VAL A 120 ? 2.2608 1.2016 0.9190 -0.6800 0.0471  -0.2822 119 VAL A C   
932  O O   . VAL A 120 ? 2.2701 1.2334 0.9620 -0.6929 0.0244  -0.2714 119 VAL A O   
933  C CB  . VAL A 120 ? 2.3341 1.2455 0.8913 -0.6722 0.0560  -0.2917 119 VAL A CB  
934  C CG1 . VAL A 120 ? 2.4827 1.3450 0.9934 -0.6664 0.0705  -0.3125 119 VAL A CG1 
935  C CG2 . VAL A 120 ? 2.3726 1.2798 0.9234 -0.6926 0.0180  -0.2913 119 VAL A CG2 
936  N N   . LYS A 121 ? 2.3241 1.2333 0.9725 -0.6763 0.0584  -0.2957 120 LYS A N   
937  C CA  . LYS A 121 ? 2.3084 1.2042 0.9823 -0.6881 0.0439  -0.2994 120 LYS A CA  
938  C C   . LYS A 121 ? 2.2583 1.1935 1.0009 -0.6871 0.0447  -0.2811 120 LYS A C   
939  O O   . LYS A 121 ? 2.1542 1.0903 0.9275 -0.7006 0.0270  -0.2772 120 LYS A O   
940  C CB  . LYS A 121 ? 2.5059 1.3604 1.1566 -0.6817 0.0599  -0.3169 120 LYS A CB  
941  C CG  . LYS A 121 ? 2.6963 1.5359 1.3775 -0.6926 0.0482  -0.3199 120 LYS A CG  
942  C CD  . LYS A 121 ? 2.8066 1.6045 1.4648 -0.6858 0.0644  -0.3375 120 LYS A CD  
943  C CE  . LYS A 121 ? 2.8724 1.6569 1.5666 -0.6964 0.0539  -0.3384 120 LYS A CE  
944  N NZ  . LYS A 121 ? 2.9898 1.7287 1.6582 -0.6927 0.0650  -0.3576 120 LYS A NZ  
945  N N   . TYR A 122 ? 2.3857 1.3522 1.1524 -0.6705 0.0655  -0.2701 121 TYR A N   
946  C CA  . TYR A 122 ? 2.3138 1.3156 1.1396 -0.6645 0.0703  -0.2537 121 TYR A CA  
947  C C   . TYR A 122 ? 2.1549 1.1989 1.0135 -0.6708 0.0549  -0.2361 121 TYR A C   
948  O O   . TYR A 122 ? 2.0451 1.1153 0.9513 -0.6698 0.0535  -0.2223 121 TYR A O   
949  C CB  . TYR A 122 ? 2.2975 1.3104 1.1344 -0.6414 0.0984  -0.2522 121 TYR A CB  
950  C CG  . TYR A 122 ? 2.3330 1.3102 1.1519 -0.6324 0.1162  -0.2663 121 TYR A CG  
951  C CD1 . TYR A 122 ? 2.2659 1.2383 1.1149 -0.6283 0.1218  -0.2634 121 TYR A CD1 
952  C CD2 . TYR A 122 ? 2.4396 1.3874 1.2118 -0.6268 0.1289  -0.2818 121 TYR A CD2 
953  C CE1 . TYR A 122 ? 2.3136 1.2534 1.1477 -0.6196 0.1380  -0.2758 121 TYR A CE1 
954  C CE2 . TYR A 122 ? 2.5280 1.4434 1.2857 -0.6182 0.1457  -0.2948 121 TYR A CE2 
955  C CZ  . TYR A 122 ? 2.4704 1.3822 1.2599 -0.6150 0.1494  -0.2920 121 TYR A CZ  
956  O OH  . TYR A 122 ? 2.4981 1.3772 1.2740 -0.6062 0.1658  -0.3047 121 TYR A OH  
957  N N   . VAL A 123 ? 2.1420 1.1922 0.9748 -0.6762 0.0446  -0.2358 122 VAL A N   
958  C CA  . VAL A 123 ? 2.1566 1.2482 1.0217 -0.6807 0.0317  -0.2189 122 VAL A CA  
959  C C   . VAL A 123 ? 2.0563 1.1500 0.9421 -0.7015 0.0033  -0.2137 122 VAL A C   
960  O O   . VAL A 123 ? 2.1059 1.1780 0.9602 -0.7159 -0.0174 -0.2218 122 VAL A O   
961  C CB  . VAL A 123 ? 1.9844 1.0882 0.8221 -0.6757 0.0346  -0.2168 122 VAL A CB  
962  C CG1 . VAL A 123 ? 2.2039 1.2659 0.9764 -0.6778 0.0359  -0.2334 122 VAL A CG1 
963  C CG2 . VAL A 123 ? 1.8433 0.9790 0.7029 -0.6869 0.0126  -0.2025 122 VAL A CG2 
964  N N   . LYS A 124 ? 1.9323 1.0504 0.8716 -0.7016 0.0030  -0.2005 123 LYS A N   
965  C CA  . LYS A 124 ? 1.8835 1.0123 0.8580 -0.7192 -0.0203 -0.1914 123 LYS A CA  
966  C C   . LYS A 124 ? 2.1301 1.3041 1.1369 -0.7180 -0.0261 -0.1740 123 LYS A C   
967  O O   . LYS A 124 ? 2.2991 1.5001 1.3287 -0.7018 -0.0083 -0.1649 123 LYS A O   
968  C CB  . LYS A 124 ? 1.7899 0.9161 0.8047 -0.7177 -0.0119 -0.1860 123 LYS A CB  
969  C CG  . LYS A 124 ? 2.0163 1.0985 1.0137 -0.7262 -0.0149 -0.2008 123 LYS A CG  
970  C CD  . LYS A 124 ? 2.1360 1.1870 1.0878 -0.7132 0.0046  -0.2173 123 LYS A CD  
971  C CE  . LYS A 124 ? 2.3096 1.3155 1.2436 -0.7242 -0.0029 -0.2332 123 LYS A CE  
972  N NZ  . LYS A 124 ? 2.4002 1.3735 1.2936 -0.7117 0.0172  -0.2494 123 LYS A NZ  
973  N N   . THR A 125 ? 2.1647 1.3466 1.1742 -0.7344 -0.0517 -0.1699 124 THR A N   
974  C CA  . THR A 125 ? 2.2238 1.4473 1.2596 -0.7335 -0.0580 -0.1543 124 THR A CA  
975  C C   . THR A 125 ? 2.0344 1.2703 1.0429 -0.7190 -0.0439 -0.1547 124 THR A C   
976  O O   . THR A 125 ? 1.8801 1.1097 0.8751 -0.7023 -0.0201 -0.1604 124 THR A O   
977  C CB  . THR A 125 ? 2.4568 1.7154 1.5547 -0.7277 -0.0501 -0.1372 124 THR A CB  
978  O OG1 . THR A 125 ? 2.6579 1.9408 1.7907 -0.7420 -0.0721 -0.1246 124 THR A OG1 
979  C CG2 . THR A 125 ? 1.9978 1.2841 1.1046 -0.7061 -0.0281 -0.1308 124 THR A CG2 
980  N N   . LEU A 126 ? 2.0656 1.3191 1.0693 -0.7254 -0.0589 -0.1479 125 LEU A N   
981  C CA  . LEU A 126 ? 1.9547 1.2231 0.9398 -0.7130 -0.0468 -0.1453 125 LEU A CA  
982  C C   . LEU A 126 ? 1.8387 1.1379 0.8434 -0.7215 -0.0659 -0.1315 125 LEU A C   
983  O O   . LEU A 126 ? 1.8082 1.0935 0.7859 -0.7353 -0.0879 -0.1337 125 LEU A O   
984  C CB  . LEU A 126 ? 2.0366 1.2669 0.9558 -0.7106 -0.0406 -0.1606 125 LEU A CB  
985  C CG  . LEU A 126 ? 2.1636 1.4007 1.0568 -0.6975 -0.0243 -0.1591 125 LEU A CG  
986  C CD1 . LEU A 126 ? 2.1829 1.3782 1.0176 -0.6905 -0.0082 -0.1756 125 LEU A CD1 
987  C CD2 . LEU A 126 ? 2.2112 1.4629 1.0950 -0.7062 -0.0429 -0.1495 125 LEU A CD2 
988  N N   . LYS A 127 ? 1.8799 1.2197 0.9308 -0.7126 -0.0584 -0.1177 126 LYS A N   
989  C CA  . LYS A 127 ? 1.9093 1.2815 0.9868 -0.7199 -0.0755 -0.1034 126 LYS A CA  
990  C C   . LYS A 127 ? 1.9127 1.3116 0.9950 -0.7059 -0.0620 -0.0962 126 LYS A C   
991  O O   . LYS A 127 ? 1.8151 1.2104 0.8870 -0.6895 -0.0387 -0.1018 126 LYS A O   
992  C CB  . LYS A 127 ? 1.8400 1.2392 0.9774 -0.7251 -0.0834 -0.0914 126 LYS A CB  
993  C CG  . LYS A 127 ? 2.0715 1.4459 1.2140 -0.7377 -0.0933 -0.0970 126 LYS A CG  
994  C CD  . LYS A 127 ? 2.1512 1.5524 1.3551 -0.7406 -0.0961 -0.0832 126 LYS A CD  
995  C CE  . LYS A 127 ? 2.1686 1.5453 1.3835 -0.7523 -0.1029 -0.0874 126 LYS A CE  
996  N NZ  . LYS A 127 ? 2.1879 1.5905 1.4636 -0.7525 -0.1002 -0.0722 126 LYS A NZ  
997  N N   . GLU A 128 ? 1.8455 1.2710 0.9470 -0.7127 -0.0776 -0.0838 127 GLU A N   
998  C CA  . GLU A 128 ? 1.6979 1.1524 0.8135 -0.7012 -0.0678 -0.0748 127 GLU A CA  
999  C C   . GLU A 128 ? 1.8381 1.3356 1.0159 -0.7009 -0.0747 -0.0601 127 GLU A C   
1000 O O   . GLU A 128 ? 1.9643 1.4762 1.1588 -0.7142 -0.0962 -0.0505 127 GLU A O   
1001 C CB  . GLU A 128 ? 1.7257 1.1700 0.8009 -0.7080 -0.0786 -0.0728 127 GLU A CB  
1002 C CG  . GLU A 128 ? 1.8899 1.2924 0.8998 -0.7041 -0.0668 -0.0866 127 GLU A CG  
1003 C CD  . GLU A 128 ? 2.0065 1.3911 0.9677 -0.7130 -0.0822 -0.0851 127 GLU A CD  
1004 O OE1 . GLU A 128 ? 2.0356 1.4423 1.0168 -0.7220 -0.1024 -0.0727 127 GLU A OE1 
1005 O OE2 . GLU A 128 ? 2.0005 1.3475 0.9020 -0.7102 -0.0741 -0.0962 127 GLU A OE2 
1006 N N   . ILE A 129 ? 1.7914 1.3081 1.0024 -0.6846 -0.0567 -0.0589 128 ILE A N   
1007 C CA  . ILE A 129 ? 1.8194 1.3729 1.0871 -0.6806 -0.0595 -0.0471 128 ILE A CA  
1008 C C   . ILE A 129 ? 1.8937 1.4829 1.1904 -0.6805 -0.0678 -0.0343 128 ILE A C   
1009 O O   . ILE A 129 ? 1.9120 1.5281 1.2512 -0.6846 -0.0782 -0.0234 128 ILE A O   
1010 C CB  . ILE A 129 ? 1.9613 1.5212 1.2469 -0.6599 -0.0378 -0.0514 128 ILE A CB  
1011 C CG1 . ILE A 129 ? 2.0990 1.6304 1.3711 -0.6610 -0.0322 -0.0597 128 ILE A CG1 
1012 C CG2 . ILE A 129 ? 2.0173 1.6157 1.3556 -0.6509 -0.0382 -0.0403 128 ILE A CG2 
1013 C CD1 . ILE A 129 ? 2.2237 1.7577 1.5092 -0.6399 -0.0122 -0.0639 128 ILE A CD1 
1014 N N   . ASN A 130 ? 1.8143 1.4035 1.0902 -0.6750 -0.0615 -0.0350 129 ASN A N   
1015 C CA  . ASN A 130 ? 1.6905 1.3116 0.9927 -0.6741 -0.0677 -0.0228 129 ASN A CA  
1016 C C   . ASN A 130 ? 1.5066 1.1653 0.8644 -0.6597 -0.0605 -0.0164 129 ASN A C   
1017 O O   . ASN A 130 ? 1.4175 1.1056 0.8117 -0.6640 -0.0727 -0.0046 129 ASN A O   
1018 C CB  . ASN A 130 ? 1.6845 1.3103 0.9883 -0.6939 -0.0938 -0.0132 129 ASN A CB  
1019 C CG  . ASN A 130 ? 1.8386 1.4331 1.0854 -0.7043 -0.1024 -0.0173 129 ASN A CG  
1020 O OD1 . ASN A 130 ? 1.9643 1.5435 1.1767 -0.6953 -0.0870 -0.0225 129 ASN A OD1 
1021 N ND2 . ASN A 130 ? 1.9049 1.4881 1.1409 -0.7225 -0.1270 -0.0153 129 ASN A ND2 
1022 N N   . THR A 131 ? 1.5322 1.1255 1.1595 -0.5192 -0.0685 -0.0416 130 THR A N   
1023 C CA  . THR A 131 ? 1.4320 1.0425 1.0742 -0.4990 -0.0789 -0.0132 130 THR A CA  
1024 C C   . THR A 131 ? 1.4241 1.0153 1.0997 -0.4810 -0.0661 -0.0182 130 THR A C   
1025 O O   . THR A 131 ? 1.5699 1.1327 1.2878 -0.4779 -0.0618 -0.0220 130 THR A O   
1026 C CB  . THR A 131 ? 1.4560 1.0694 1.1193 -0.5001 -0.0945 0.0117  130 THR A CB  
1027 O OG1 . THR A 131 ? 1.6119 1.1895 1.3145 -0.5010 -0.0894 0.0076  130 THR A OG1 
1028 C CG2 . THR A 131 ? 1.3809 1.0125 1.0202 -0.5191 -0.1049 0.0124  130 THR A CG2 
1029 N N   . LEU A 132 ? 1.3085 0.9141 0.9692 -0.4695 -0.0601 -0.0193 131 LEU A N   
1030 C CA  . LEU A 132 ? 1.4309 1.0234 1.1275 -0.4508 -0.0495 -0.0227 131 LEU A CA  
1031 C C   . LEU A 132 ? 1.4114 1.0328 1.0975 -0.4340 -0.0553 -0.0050 131 LEU A C   
1032 O O   . LEU A 132 ? 1.2860 0.9101 0.9616 -0.4283 -0.0412 -0.0176 131 LEU A O   
1033 C CB  . LEU A 132 ? 1.4791 1.0448 1.1834 -0.4570 -0.0232 -0.0585 131 LEU A CB  
1034 C CG  . LEU A 132 ? 1.4384 1.0031 1.0908 -0.4787 -0.0098 -0.0835 131 LEU A CG  
1035 C CD1 . LEU A 132 ? 1.4772 1.0715 1.0795 -0.4773 -0.0166 -0.0713 131 LEU A CD1 
1036 C CD2 . LEU A 132 ? 1.3426 0.8778 1.0102 -0.4852 0.0206  -0.1208 131 LEU A CD2 
1037 N N   . PHE A 133 ? 1.3822 1.0245 1.0713 -0.4282 -0.0746 0.0232  132 PHE A N   
1038 C CA  . PHE A 133 ? 1.2814 0.9524 0.9673 -0.4131 -0.0815 0.0411  132 PHE A CA  
1039 C C   . PHE A 133 ? 1.2879 0.9602 1.0013 -0.4053 -0.0976 0.0661  132 PHE A C   
1040 O O   . PHE A 133 ? 1.2154 0.8810 0.9286 -0.4172 -0.1075 0.0760  132 PHE A O   
1041 C CB  . PHE A 133 ? 1.1028 0.8066 0.7481 -0.4212 -0.0889 0.0480  132 PHE A CB  
1042 C CG  . PHE A 133 ? 1.1678 0.8874 0.8076 -0.4322 -0.1055 0.0649  132 PHE A CG  
1043 C CD1 . PHE A 133 ? 1.1998 0.9384 0.8531 -0.4252 -0.1166 0.0875  132 PHE A CD1 
1044 C CD2 . PHE A 133 ? 1.2620 0.9785 0.8827 -0.4515 -0.1088 0.0563  132 PHE A CD2 
1045 C CE1 . PHE A 133 ? 1.1854 0.9381 0.8337 -0.4381 -0.1280 0.1006  132 PHE A CE1 
1046 C CE2 . PHE A 133 ? 1.1375 0.8690 0.7575 -0.4625 -0.1219 0.0695  132 PHE A CE2 
1047 C CZ  . PHE A 133 ? 1.1363 0.8857 0.7703 -0.4561 -0.1302 0.0913  132 PHE A CZ  
1048 N N   . ILE A 134 ? 1.1677 0.8470 0.9029 -0.3873 -0.1001 0.0760  133 ILE A N   
1049 C CA  . ILE A 134 ? 1.1019 0.7800 0.8576 -0.3816 -0.1172 0.1005  133 ILE A CA  
1050 C C   . ILE A 134 ? 1.0545 0.7666 0.7838 -0.3881 -0.1287 0.1210  133 ILE A C   
1051 O O   . ILE A 134 ? 1.0947 0.8372 0.8103 -0.3824 -0.1257 0.1214  133 ILE A O   
1052 C CB  . ILE A 134 ? 1.0567 0.7316 0.8462 -0.3609 -0.1184 0.1032  133 ILE A CB  
1053 C CG1 . ILE A 134 ? 1.0596 0.7057 0.8819 -0.3538 -0.1025 0.0774  133 ILE A CG1 
1054 C CG2 . ILE A 134 ? 1.0500 0.7150 0.8584 -0.3584 -0.1393 0.1286  133 ILE A CG2 
1055 C CD1 . ILE A 134 ? 1.2157 0.8242 1.0670 -0.3610 -0.1055 0.0732  133 ILE A CD1 
1056 N N   . PRO A 135 ? 1.1017 0.8077 0.8260 -0.4013 -0.1402 0.1370  134 PRO A N   
1057 C CA  . PRO A 135 ? 1.0584 0.7972 0.7620 -0.4090 -0.1478 0.1538  134 PRO A CA  
1058 C C   . PRO A 135 ? 1.1341 0.8780 0.8473 -0.4001 -0.1584 0.1739  134 PRO A C   
1059 O O   . PRO A 135 ? 1.1698 0.8948 0.8843 -0.4084 -0.1699 0.1913  134 PRO A O   
1060 C CB  . PRO A 135 ? 1.0960 0.8231 0.7891 -0.4302 -0.1522 0.1591  134 PRO A CB  
1061 C CG  . PRO A 135 ? 1.0698 0.7524 0.7856 -0.4296 -0.1538 0.1569  134 PRO A CG  
1062 C CD  . PRO A 135 ? 1.0969 0.7681 0.8324 -0.4131 -0.1435 0.1373  134 PRO A CD  
1063 N N   . LYS A 136 ? 1.1169 0.8848 0.8349 -0.3849 -0.1552 0.1716  135 LYS A N   
1064 C CA  . LYS A 136 ? 1.1510 0.9253 0.8794 -0.3749 -0.1652 0.1869  135 LYS A CA  
1065 C C   . LYS A 136 ? 1.1525 0.9494 0.8582 -0.3899 -0.1726 0.2050  135 LYS A C   
1066 O O   . LYS A 136 ? 1.1591 0.9457 0.8624 -0.3933 -0.1860 0.2238  135 LYS A O   
1067 C CB  . LYS A 136 ? 1.0280 0.8255 0.7686 -0.3560 -0.1568 0.1762  135 LYS A CB  
1068 C CG  . LYS A 136 ? 0.9238 0.6982 0.6966 -0.3377 -0.1523 0.1634  135 LYS A CG  
1069 C CD  . LYS A 136 ? 0.9639 0.7108 0.7636 -0.3316 -0.1691 0.1765  135 LYS A CD  
1070 C CE  . LYS A 136 ? 1.0688 0.8341 0.8601 -0.3321 -0.1851 0.1979  135 LYS A CE  
1071 N NZ  . LYS A 136 ? 1.1726 0.9058 0.9836 -0.3302 -0.2073 0.2156  135 LYS A NZ  
1072 N N   . GLU A 137 ? 1.0210 0.8490 0.7108 -0.3996 -0.1640 0.1986  136 GLU A N   
1073 C CA  . GLU A 137 ? 1.0580 0.9113 0.7303 -0.4165 -0.1656 0.2096  136 GLU A CA  
1074 C C   . GLU A 137 ? 1.1223 0.9875 0.7853 -0.4330 -0.1591 0.2010  136 GLU A C   
1075 O O   . GLU A 137 ? 1.2090 1.0709 0.8760 -0.4287 -0.1544 0.1864  136 GLU A O   
1076 C CB  . GLU A 137 ? 0.9704 0.8627 0.6471 -0.4077 -0.1611 0.2076  136 GLU A CB  
1077 C CG  . GLU A 137 ? 1.1694 1.0540 0.8568 -0.3923 -0.1689 0.2151  136 GLU A CG  
1078 C CD  . GLU A 137 ? 1.1363 1.0601 0.8269 -0.3874 -0.1643 0.2134  136 GLU A CD  
1079 O OE1 . GLU A 137 ? 1.0010 0.9561 0.6835 -0.4007 -0.1565 0.2104  136 GLU A OE1 
1080 O OE2 . GLU A 137 ? 1.1134 1.0370 0.8193 -0.3705 -0.1682 0.2133  136 GLU A OE2 
1081 N N   . HIS A 138 ? 1.0342 0.9131 0.6846 -0.4534 -0.1587 0.2089  137 HIS A N   
1082 C CA  . HIS A 138 ? 1.1194 1.0163 0.7689 -0.4688 -0.1528 0.1988  137 HIS A CA  
1083 C C   . HIS A 138 ? 1.1044 1.0267 0.7664 -0.4568 -0.1486 0.1822  137 HIS A C   
1084 O O   . HIS A 138 ? 1.2045 1.1228 0.8665 -0.4619 -0.1491 0.1719  137 HIS A O   
1085 C CB  . HIS A 138 ? 1.2317 1.1535 0.8738 -0.4898 -0.1480 0.2046  137 HIS A CB  
1086 C CG  . HIS A 138 ? 1.4453 1.3386 1.0666 -0.5070 -0.1523 0.2226  137 HIS A CG  
1087 N ND1 . HIS A 138 ? 1.4509 1.3101 1.0652 -0.5196 -0.1555 0.2272  137 HIS A ND1 
1088 C CD2 . HIS A 138 ? 1.5942 1.4862 1.1976 -0.5153 -0.1549 0.2382  137 HIS A CD2 
1089 C CE1 . HIS A 138 ? 1.4795 1.3157 1.0732 -0.5343 -0.1604 0.2467  137 HIS A CE1 
1090 N NE2 . HIS A 138 ? 1.5698 1.4251 1.1536 -0.5328 -0.1608 0.2542  137 HIS A NE2 
1091 N N   . ARG A 139 ? 1.0107 0.9575 0.6824 -0.4416 -0.1456 0.1802  138 ARG A N   
1092 C CA  . ARG A 139 ? 1.0466 1.0171 0.7292 -0.4317 -0.1428 0.1679  138 ARG A CA  
1093 C C   . ARG A 139 ? 0.9941 0.9511 0.6782 -0.4103 -0.1409 0.1628  138 ARG A C   
1094 O O   . ARG A 139 ? 0.9944 0.9681 0.6835 -0.4019 -0.1386 0.1552  138 ARG A O   
1095 C CB  . ARG A 139 ? 1.1187 1.1337 0.8183 -0.4335 -0.1384 0.1663  138 ARG A CB  
1096 C CG  . ARG A 139 ? 1.0648 1.0981 0.7688 -0.4566 -0.1362 0.1662  138 ARG A CG  
1097 C CD  . ARG A 139 ? 1.0533 1.1301 0.7855 -0.4580 -0.1326 0.1567  138 ARG A CD  
1098 N NE  . ARG A 139 ? 1.0407 1.1289 0.7845 -0.4771 -0.1341 0.1498  138 ARG A NE  
1099 C CZ  . ARG A 139 ? 1.1140 1.2214 0.8684 -0.4973 -0.1257 0.1472  138 ARG A CZ  
1100 N NH1 . ARG A 139 ? 1.2774 1.3938 1.0257 -0.5027 -0.1157 0.1520  138 ARG A NH1 
1101 N NH2 . ARG A 139 ? 1.0671 1.1847 0.8376 -0.5138 -0.1266 0.1386  138 ARG A NH2 
1102 N N   . VAL A 140 ? 0.9564 0.8823 0.6384 -0.4024 -0.1418 0.1670  139 VAL A N   
1103 C CA  . VAL A 140 ? 0.9820 0.8942 0.6707 -0.3832 -0.1369 0.1593  139 VAL A CA  
1104 C C   . VAL A 140 ? 1.0345 0.9060 0.7198 -0.3831 -0.1359 0.1519  139 VAL A C   
1105 O O   . VAL A 140 ? 1.0673 0.9128 0.7561 -0.3879 -0.1415 0.1590  139 VAL A O   
1106 C CB  . VAL A 140 ? 0.9944 0.9096 0.6976 -0.3690 -0.1375 0.1662  139 VAL A CB  
1107 C CG1 . VAL A 140 ? 0.8847 0.7903 0.6002 -0.3496 -0.1292 0.1546  139 VAL A CG1 
1108 C CG2 . VAL A 140 ? 0.7930 0.7480 0.5005 -0.3715 -0.1370 0.1720  139 VAL A CG2 
1109 N N   . PHE A 141 ? 1.0320 0.8968 0.7106 -0.3789 -0.1283 0.1373  140 PHE A N   
1110 C CA  . PHE A 141 ? 0.9299 0.7576 0.6073 -0.3792 -0.1226 0.1247  140 PHE A CA  
1111 C C   . PHE A 141 ? 1.0142 0.8313 0.7044 -0.3621 -0.1110 0.1137  140 PHE A C   
1112 O O   . PHE A 141 ? 1.1520 0.9908 0.8426 -0.3521 -0.1060 0.1131  140 PHE A O   
1113 C CB  . PHE A 141 ? 0.9891 0.8117 0.6432 -0.3942 -0.1215 0.1133  140 PHE A CB  
1114 C CG  . PHE A 141 ? 0.9792 0.8214 0.6160 -0.3924 -0.1183 0.1069  140 PHE A CG  
1115 C CD1 . PHE A 141 ? 0.9971 0.8749 0.6328 -0.3951 -0.1268 0.1161  140 PHE A CD1 
1116 C CD2 . PHE A 141 ? 0.9351 0.7586 0.5578 -0.3897 -0.1066 0.0913  140 PHE A CD2 
1117 C CE1 . PHE A 141 ? 1.0426 0.9362 0.6654 -0.3932 -0.1273 0.1131  140 PHE A CE1 
1118 C CE2 . PHE A 141 ? 1.0249 0.8626 0.6261 -0.3901 -0.1056 0.0887  140 PHE A CE2 
1119 C CZ  . PHE A 141 ? 1.0427 0.9151 0.6450 -0.3909 -0.1178 0.1011  140 PHE A CZ  
1120 N N   . THR A 142 ? 1.1186 0.9015 0.8237 -0.3595 -0.1054 0.1037  141 THR A N   
1121 C CA  . THR A 142 ? 1.0137 0.7837 0.7428 -0.3434 -0.0942 0.0923  141 THR A CA  
1122 C C   . THR A 142 ? 1.0910 0.8254 0.8251 -0.3487 -0.0806 0.0701  141 THR A C   
1123 O O   . THR A 142 ? 1.2834 0.9997 1.0117 -0.3622 -0.0839 0.0677  141 THR A O   
1124 C CB  . THR A 142 ? 1.1205 0.8884 0.8820 -0.3315 -0.1059 0.1066  141 THR A CB  
1125 O OG1 . THR A 142 ? 1.0871 0.8869 0.8511 -0.3203 -0.1070 0.1142  141 THR A OG1 
1126 C CG2 . THR A 142 ? 1.1983 0.9338 0.9986 -0.3207 -0.1001 0.0937  141 THR A CG2 
1127 N N   . LEU A 143 ? 1.0576 0.7819 0.8035 -0.3397 -0.0629 0.0516  142 LEU A N   
1128 C CA  . LEU A 143 ? 1.0112 0.7034 0.7608 -0.3474 -0.0446 0.0254  142 LEU A CA  
1129 C C   . LEU A 143 ? 1.0633 0.7302 0.8690 -0.3348 -0.0392 0.0148  142 LEU A C   
1130 O O   . LEU A 143 ? 1.0313 0.6709 0.8534 -0.3395 -0.0207 -0.0109 142 LEU A O   
1131 C CB  . LEU A 143 ? 0.9549 0.6504 0.6721 -0.3519 -0.0246 0.0081  142 LEU A CB  
1132 C CG  . LEU A 143 ? 0.9963 0.6958 0.6587 -0.3722 -0.0253 0.0054  142 LEU A CG  
1133 C CD1 . LEU A 143 ? 0.9162 0.6301 0.5679 -0.3805 -0.0480 0.0249  142 LEU A CD1 
1134 C CD2 . LEU A 143 ? 1.0911 0.8095 0.7194 -0.3715 -0.0198 0.0077  142 LEU A CD2 
1135 N N   . ASN A 144 ? 1.2248 0.9013 1.0616 -0.3198 -0.0559 0.0338  143 ASN A N   
1136 C CA  . ASN A 144 ? 1.2767 0.9309 1.1733 -0.3061 -0.0587 0.0288  143 ASN A CA  
1137 C C   . ASN A 144 ? 1.2697 0.9155 1.1971 -0.2958 -0.0345 0.0011  143 ASN A C   
1138 O O   . ASN A 144 ? 1.3343 0.9565 1.3181 -0.2873 -0.0309 -0.0127 143 ASN A O   
1139 C CB  . ASN A 144 ? 1.2531 0.8741 1.1728 -0.3152 -0.0642 0.0255  143 ASN A CB  
1140 C CG  . ASN A 144 ? 1.3020 0.9023 1.2865 -0.3004 -0.0784 0.0310  143 ASN A CG  
1141 O OD1 . ASN A 144 ? 1.0857 0.7009 1.0878 -0.2855 -0.0927 0.0463  143 ASN A OD1 
1142 N ND2 . ASN A 144 ? 1.4864 1.0524 1.5094 -0.3048 -0.0761 0.0186  143 ASN A ND2 
1143 N N   . GLU A 145 ? 1.2924 0.9567 1.1849 -0.2974 -0.0179 -0.0071 144 GLU A N   
1144 C CA  . GLU A 145 ? 1.2816 0.9405 1.1943 -0.2901 0.0082  -0.0325 144 GLU A CA  
1145 C C   . GLU A 145 ? 1.2259 0.9123 1.1569 -0.2711 0.0005  -0.0194 144 GLU A C   
1146 O O   . GLU A 145 ? 1.0298 0.7427 0.9227 -0.2718 0.0003  -0.0083 144 GLU A O   
1147 C CB  . GLU A 145 ? 1.3910 1.0504 1.2461 -0.3068 0.0306  -0.0472 144 GLU A CB  
1148 C CG  . GLU A 145 ? 1.6522 1.2860 1.5204 -0.3129 0.0645  -0.0835 144 GLU A CG  
1149 C CD  . GLU A 145 ? 1.7725 1.3749 1.6512 -0.3280 0.0732  -0.1039 144 GLU A CD  
1150 O OE1 . GLU A 145 ? 1.7719 1.3594 1.7103 -0.3190 0.0637  -0.1053 144 GLU A OE1 
1151 O OE2 . GLU A 145 ? 1.8980 1.4902 1.7261 -0.3496 0.0886  -0.1185 144 GLU A OE2 
1152 N N   . PRO A 146 ? 1.2954 0.9756 1.2883 -0.2542 -0.0076 -0.0208 145 PRO A N   
1153 C CA  . PRO A 146 ? 1.1594 0.8669 1.1706 -0.2371 -0.0190 -0.0073 145 PRO A CA  
1154 C C   . PRO A 146 ? 1.1643 0.8816 1.1803 -0.2304 0.0086  -0.0280 145 PRO A C   
1155 O O   . PRO A 146 ? 1.2075 0.9515 1.2289 -0.2186 0.0036  -0.0187 145 PRO A O   
1156 C CB  . PRO A 146 ? 1.1148 0.8072 1.1930 -0.2231 -0.0386 -0.0041 145 PRO A CB  
1157 C CG  . PRO A 146 ? 1.2635 0.9183 1.3683 -0.2313 -0.0308 -0.0218 145 PRO A CG  
1158 C CD  . PRO A 146 ? 1.3191 0.9669 1.3735 -0.2501 -0.0031 -0.0401 145 PRO A CD  
1159 N N   . HIS A 147 ? 1.1075 0.8021 1.1205 -0.2397 0.0387  -0.0568 146 HIS A N   
1160 C CA  . HIS A 147 ? 1.0725 0.7706 1.0843 -0.2376 0.0689  -0.0779 146 HIS A CA  
1161 C C   . HIS A 147 ? 1.0422 0.7402 0.9798 -0.2571 0.0860  -0.0799 146 HIS A C   
1162 O O   . HIS A 147 ? 0.9222 0.6119 0.8458 -0.2631 0.1156  -0.1003 146 HIS A O   
1163 C CB  . HIS A 147 ? 1.1683 0.8393 1.2409 -0.2338 0.0939  -0.1131 146 HIS A CB  
1164 C CG  . HIS A 147 ? 1.2713 0.9476 1.4229 -0.2113 0.0788  -0.1130 146 HIS A CG  
1165 N ND1 . HIS A 147 ? 1.3877 1.0430 1.6015 -0.2048 0.0643  -0.1180 146 HIS A ND1 
1166 C CD2 . HIS A 147 ? 1.1277 0.8276 1.3080 -0.1939 0.0738  -0.1083 146 HIS A CD2 
1167 C CE1 . HIS A 147 ? 1.3488 1.0143 1.6246 -0.1845 0.0485  -0.1149 146 HIS A CE1 
1168 N NE2 . HIS A 147 ? 1.0781 0.7715 1.3341 -0.1778 0.0547  -0.1101 146 HIS A NE2 
1169 N N   . GLY A 148 ? 1.0395 0.7463 0.9298 -0.2679 0.0660  -0.0578 147 GLY A N   
1170 C CA  . GLY A 148 ? 1.0591 0.7675 0.8800 -0.2863 0.0737  -0.0552 147 GLY A CA  
1171 C C   . GLY A 148 ? 1.0953 0.8175 0.8938 -0.2839 0.0897  -0.0560 147 GLY A C   
1172 O O   . GLY A 148 ? 1.0742 0.7796 0.8336 -0.2990 0.1128  -0.0713 147 GLY A O   
1173 N N   . LEU A 149 ? 0.9904 0.7420 0.8119 -0.2666 0.0774  -0.0394 148 LEU A N   
1174 C CA  . LEU A 149 ? 0.9161 0.6832 0.7256 -0.2619 0.0908  -0.0380 148 LEU A CA  
1175 C C   . LEU A 149 ? 1.0256 0.7680 0.8443 -0.2651 0.1270  -0.0678 148 LEU A C   
1176 O O   . LEU A 149 ? 1.1021 0.8377 0.8771 -0.2766 0.1452  -0.0715 148 LEU A O   
1177 C CB  . LEU A 149 ? 0.9505 0.7506 0.8009 -0.2412 0.0751  -0.0228 148 LEU A CB  
1178 C CG  . LEU A 149 ? 0.8717 0.7020 0.7102 -0.2352 0.0741  -0.0085 148 LEU A CG  
1179 C CD1 . LEU A 149 ? 0.9291 0.7597 0.8020 -0.2232 0.0977  -0.0252 148 LEU A CD1 
1180 C CD2 . LEU A 149 ? 0.8888 0.7193 0.6663 -0.2514 0.0737  0.0029  148 LEU A CD2 
1181 N N   . VAL A 150 ? 0.9376 0.6649 0.8140 -0.2563 0.1374  -0.0893 149 VAL A N   
1182 C CA  . VAL A 150 ? 0.9821 0.6854 0.8764 -0.2606 0.1750  -0.1226 149 VAL A CA  
1183 C C   . VAL A 150 ? 1.1249 0.7957 0.9675 -0.2876 0.1983  -0.1421 149 VAL A C   
1184 O O   . VAL A 150 ? 1.2280 0.8857 1.0318 -0.3015 0.2264  -0.1551 149 VAL A O   
1185 C CB  . VAL A 150 ? 0.9554 0.6511 0.9350 -0.2444 0.1785  -0.1428 149 VAL A CB  
1186 C CG1 . VAL A 150 ? 0.8866 0.5545 0.8870 -0.2532 0.2210  -0.1824 149 VAL A CG1 
1187 C CG2 . VAL A 150 ? 0.8796 0.6060 0.9072 -0.2200 0.1606  -0.1285 149 VAL A CG2 
1188 N N   . GLN A 151 ? 1.1344 0.7910 0.9746 -0.2966 0.1871  -0.1444 150 GLN A N   
1189 C CA  . GLN A 151 ? 1.1545 0.7809 0.9480 -0.3237 0.2080  -0.1654 150 GLN A CA  
1190 C C   . GLN A 151 ? 1.2219 0.8498 0.9250 -0.3434 0.2087  -0.1511 150 GLN A C   
1191 O O   . GLN A 151 ? 1.2990 0.9013 0.9522 -0.3683 0.2332  -0.1707 150 GLN A O   
1192 C CB  . GLN A 151 ? 1.0749 0.6913 0.8808 -0.3286 0.1892  -0.1642 150 GLN A CB  
1193 C CG  . GLN A 151 ? 1.1522 0.7655 1.0470 -0.3091 0.1798  -0.1713 150 GLN A CG  
1194 C CD  . GLN A 151 ? 1.4095 1.0199 1.3115 -0.3104 0.1501  -0.1554 150 GLN A CD  
1195 O OE1 . GLN A 151 ? 1.2563 0.8688 1.0996 -0.3259 0.1383  -0.1416 150 GLN A OE1 
1196 N NE2 . GLN A 151 ? 1.3796 0.9844 1.3556 -0.2944 0.1370  -0.1565 150 GLN A NE2 
1197 N N   . TYR A 152 ? 1.1321 0.7897 0.8159 -0.3334 0.1812  -0.1174 151 TYR A N   
1198 C CA  . TYR A 152 ? 1.2235 0.8844 0.8301 -0.3502 0.1726  -0.0990 151 TYR A CA  
1199 C C   . TYR A 152 ? 1.2858 0.9529 0.8701 -0.3484 0.1859  -0.0921 151 TYR A C   
1200 O O   . TYR A 152 ? 1.4250 1.0773 0.9421 -0.3691 0.1937  -0.0896 151 TYR A O   
1201 C CB  . TYR A 152 ? 1.1081 0.7962 0.7060 -0.3446 0.1325  -0.0670 151 TYR A CB  
1202 C CG  . TYR A 152 ? 1.1625 0.8523 0.6883 -0.3633 0.1185  -0.0497 151 TYR A CG  
1203 C CD1 . TYR A 152 ? 1.2837 0.9545 0.7643 -0.3863 0.1144  -0.0566 151 TYR A CD1 
1204 C CD2 . TYR A 152 ? 1.0961 0.8061 0.6024 -0.3583 0.1079  -0.0268 151 TYR A CD2 
1205 C CE1 . TYR A 152 ? 1.3346 1.0069 0.7508 -0.4037 0.0976  -0.0404 151 TYR A CE1 
1206 C CE2 . TYR A 152 ? 1.2581 0.9688 0.7040 -0.3748 0.0909  -0.0095 151 TYR A CE2 
1207 C CZ  . TYR A 152 ? 1.4078 1.0996 0.8078 -0.3976 0.0846  -0.0161 151 TYR A CZ  
1208 O OH  . TYR A 152 ? 1.4969 1.1894 0.8386 -0.4143 0.0638  0.0014  151 TYR A OH  
1209 N N   . TYR A 153 ? 1.1170 0.8051 0.7559 -0.3248 0.1866  -0.0878 152 TYR A N   
1210 C CA  . TYR A 153 ? 1.1293 0.8234 0.7553 -0.3218 0.2007  -0.0820 152 TYR A CA  
1211 C C   . TYR A 153 ? 1.1534 0.8333 0.8242 -0.3155 0.2376  -0.1123 152 TYR A C   
1212 O O   . TYR A 153 ? 1.0610 0.7380 0.7202 -0.3168 0.2580  -0.1142 152 TYR A O   
1213 C CB  . TYR A 153 ? 0.9594 0.6934 0.6091 -0.3014 0.1731  -0.0521 152 TYR A CB  
1214 C CG  . TYR A 153 ? 1.0373 0.7893 0.6527 -0.3065 0.1383  -0.0235 152 TYR A CG  
1215 C CD1 . TYR A 153 ? 1.0345 0.7808 0.5871 -0.3231 0.1316  -0.0078 152 TYR A CD1 
1216 C CD2 . TYR A 153 ? 1.0418 0.8166 0.6900 -0.2953 0.1111  -0.0115 152 TYR A CD2 
1217 C CE1 . TYR A 153 ? 1.0646 0.8294 0.5953 -0.3270 0.0985  0.0167  152 TYR A CE1 
1218 C CE2 . TYR A 153 ? 0.9592 0.7518 0.5821 -0.3007 0.0819  0.0118  152 TYR A CE2 
1219 C CZ  . TYR A 153 ? 1.1034 0.8922 0.6717 -0.3158 0.0756  0.0248  152 TYR A CZ  
1220 O OH  . TYR A 153 ? 1.1679 0.9758 0.7202 -0.3206 0.0456  0.0459  152 TYR A OH  
1221 N N   . GLY A 154 ? 1.1486 0.8191 0.8747 -0.3090 0.2458  -0.1360 153 GLY A N   
1222 C CA  . GLY A 154 ? 1.2413 0.9001 1.0241 -0.3017 0.2788  -0.1676 153 GLY A CA  
1223 C C   . GLY A 154 ? 1.2835 0.9072 1.0251 -0.3273 0.3227  -0.1965 153 GLY A C   
1224 O O   . GLY A 154 ? 1.3554 0.9623 1.0156 -0.3521 0.3260  -0.1897 153 GLY A O   
1225 N N   . SER A 155 ? 1.1338 0.7458 0.9318 -0.3227 0.3565  -0.2297 154 SER A N   
1226 C CA  . SER A 155 ? 1.3384 0.9167 1.1026 -0.3484 0.4046  -0.2614 154 SER A CA  
1227 C C   . SER A 155 ? 1.4016 0.9482 1.1489 -0.3729 0.4239  -0.2915 154 SER A C   
1228 O O   . SER A 155 ? 1.5578 1.0787 1.3235 -0.3876 0.4675  -0.3318 154 SER A O   
1229 C CB  . SER A 155 ? 1.4613 1.0400 1.2983 -0.3354 0.4370  -0.2892 154 SER A CB  
1230 O OG  . SER A 155 ? 1.4963 1.0716 1.4230 -0.3233 0.4432  -0.3191 154 SER A OG  
1231 N N   . ARG A 156 ? 1.4928 1.0420 1.2097 -0.3779 0.3931  -0.2741 155 ARG A N   
1232 C CA  . ARG A 156 ? 1.6409 1.1613 1.3292 -0.4043 0.4083  -0.2992 155 ARG A CA  
1233 C C   . ARG A 156 ? 1.5789 1.1041 1.1853 -0.4176 0.3744  -0.2670 155 ARG A C   
1234 O O   . ARG A 156 ? 1.4668 0.9734 1.0407 -0.4391 0.3770  -0.2801 155 ARG A O   
1235 C CB  . ARG A 156 ? 1.7622 1.2816 1.5419 -0.3898 0.4038  -0.3205 155 ARG A CB  
1236 C CG  . ARG A 156 ? 1.9338 1.4582 1.8175 -0.3667 0.4210  -0.3441 155 ARG A CG  
1237 C CD  . ARG A 156 ? 2.0585 1.5997 2.0292 -0.3384 0.3851  -0.3339 155 ARG A CD  
1238 N NE  . ARG A 156 ? 2.2236 1.7461 2.2019 -0.3504 0.3805  -0.3467 155 ARG A NE  
1239 C CZ  . ARG A 156 ? 2.2295 1.7614 2.2541 -0.3334 0.3436  -0.3293 155 ARG A CZ  
1240 N NH1 . ARG A 156 ? 2.1906 1.7505 2.2532 -0.3050 0.3075  -0.2982 155 ARG A NH1 
1241 N NH2 . ARG A 156 ? 2.2292 1.7413 2.2601 -0.3465 0.3435  -0.3432 155 ARG A NH2 
1242 N N   . SER A 157 ? 1.5465 1.0979 1.1261 -0.4046 0.3431  -0.2266 156 SER A N   
1243 C CA  . SER A 157 ? 1.4794 1.0420 0.9945 -0.4124 0.3059  -0.1925 156 SER A CA  
1244 C C   . SER A 157 ? 1.5319 1.0648 0.9552 -0.4499 0.3177  -0.2018 156 SER A C   
1245 O O   . SER A 157 ? 1.5641 1.0998 0.9504 -0.4597 0.2907  -0.1877 156 SER A O   
1246 C CB  . SER A 157 ? 1.4639 1.0537 0.9627 -0.3978 0.2825  -0.1552 156 SER A CB  
1247 O OG  . SER A 157 ? 1.6158 1.1894 1.0720 -0.4112 0.3099  -0.1594 156 SER A OG  
1248 N N   . SER A 158 ? 1.6248 1.1291 1.0099 -0.4723 0.3583  -0.2261 157 SER A N   
1249 C CA  . SER A 158 ? 1.7725 1.2446 1.0641 -0.5124 0.3743  -0.2390 157 SER A CA  
1250 C C   . SER A 158 ? 1.8407 1.3025 1.1329 -0.5264 0.3700  -0.2585 157 SER A C   
1251 O O   . SER A 158 ? 1.9298 1.3832 1.1476 -0.5499 0.3532  -0.2487 157 SER A O   
1252 C CB  . SER A 158 ? 1.8066 1.2461 1.0764 -0.5352 0.4288  -0.2741 157 SER A CB  
1253 O OG  . SER A 158 ? 1.8079 1.2368 1.1542 -0.5319 0.4631  -0.3186 157 SER A OG  
1254 N N   . SER A 159 ? 1.7320 1.1942 1.1114 -0.5118 0.3835  -0.2858 158 SER A N   
1255 C CA  . SER A 159 ? 1.7244 1.1732 1.1143 -0.5256 0.3854  -0.3094 158 SER A CA  
1256 C C   . SER A 159 ? 1.6690 1.1433 1.1094 -0.5009 0.3416  -0.2849 158 SER A C   
1257 O O   . SER A 159 ? 1.5143 0.9810 1.0093 -0.4988 0.3456  -0.3063 158 SER A O   
1258 C CB  . SER A 159 ? 1.7500 1.1752 1.2029 -0.5320 0.4332  -0.3613 158 SER A CB  
1259 O OG  . SER A 159 ? 1.7027 1.1442 1.2560 -0.4978 0.4344  -0.3630 158 SER A OG  
1260 N N   . TYR A 160 ? 1.6335 1.1364 1.0558 -0.4845 0.3008  -0.2409 159 TYR A N   
1261 C CA  . TYR A 160 ? 1.5505 1.0787 1.0236 -0.4607 0.2623  -0.2173 159 TYR A CA  
1262 C C   . TYR A 160 ? 1.5908 1.1106 1.0517 -0.4755 0.2481  -0.2230 159 TYR A C   
1263 O O   . TYR A 160 ? 1.6517 1.1787 1.1765 -0.4589 0.2331  -0.2210 159 TYR A O   
1264 C CB  . TYR A 160 ? 1.4760 1.0379 0.9358 -0.4421 0.2250  -0.1726 159 TYR A CB  
1265 C CG  . TYR A 160 ? 1.4137 0.9990 0.9127 -0.4246 0.1876  -0.1499 159 TYR A CG  
1266 C CD1 . TYR A 160 ? 1.3307 0.9260 0.9123 -0.3992 0.1824  -0.1507 159 TYR A CD1 
1267 C CD2 . TYR A 160 ? 1.3094 0.9047 0.7626 -0.4353 0.1576  -0.1285 159 TYR A CD2 
1268 C CE1 . TYR A 160 ? 1.2068 0.8195 0.8174 -0.3868 0.1499  -0.1294 159 TYR A CE1 
1269 C CE2 . TYR A 160 ? 1.2092 0.8237 0.6971 -0.4222 0.1274  -0.1098 159 TYR A CE2 
1270 C CZ  . TYR A 160 ? 1.2039 0.8261 0.7672 -0.3988 0.1245  -0.1097 159 TYR A CZ  
1271 O OH  . TYR A 160 ? 1.2146 0.8527 0.8062 -0.3885 0.0952  -0.0897 159 TYR A OH  
1272 N N   . ASN A 161 ? 1.5136 1.0175 0.8931 -0.5071 0.2516  -0.2293 160 ASN A N   
1273 C CA  . ASN A 161 ? 1.5449 1.0445 0.9041 -0.5226 0.2337  -0.2312 160 ASN A CA  
1274 C C   . ASN A 161 ? 1.4761 1.0058 0.8220 -0.5108 0.1862  -0.1893 160 ASN A C   
1275 O O   . ASN A 161 ? 1.3504 0.8941 0.7501 -0.4936 0.1652  -0.1782 160 ASN A O   
1276 C CB  . ASN A 161 ? 1.3370 0.8243 0.7725 -0.5171 0.2457  -0.2584 160 ASN A CB  
1277 C CG  . ASN A 161 ? 1.6100 1.0924 1.0247 -0.5344 0.2284  -0.2608 160 ASN A CG  
1278 O OD1 . ASN A 161 ? 1.5685 1.0549 0.9088 -0.5536 0.2108  -0.2475 160 ASN A OD1 
1279 N ND2 . ASN A 161 ? 1.5010 0.9745 0.9853 -0.5274 0.2321  -0.2774 160 ASN A ND2 
1280 N N   . ILE A 162 ? 1.5441 1.0824 0.8203 -0.5213 0.1689  -0.1663 161 ILE A N   
1281 C CA  . ILE A 162 ? 1.5835 1.1522 0.8557 -0.5100 0.1254  -0.1290 161 ILE A CA  
1282 C C   . ILE A 162 ? 1.6336 1.1996 0.8834 -0.5279 0.1066  -0.1320 161 ILE A C   
1283 O O   . ILE A 162 ? 1.5843 1.1747 0.8376 -0.5208 0.0720  -0.1058 161 ILE A O   
1284 C CB  . ILE A 162 ? 1.6077 1.1905 0.8303 -0.5100 0.1084  -0.1000 161 ILE A CB  
1285 C CG1 . ILE A 162 ? 1.7074 1.2775 0.8433 -0.5415 0.0954  -0.0970 161 ILE A CG1 
1286 C CG2 . ILE A 162 ? 1.4837 1.0582 0.7120 -0.5023 0.1372  -0.1063 161 ILE A CG2 
1287 C CD1 . ILE A 162 ? 1.8463 1.4342 0.9466 -0.5382 0.0669  -0.0616 161 ILE A CD1 
1288 N N   . ASP A 163 ? 1.7814 1.3182 1.0132 -0.5518 0.1316  -0.1668 162 ASP A N   
1289 C CA  . ASP A 163 ? 1.8252 1.3571 1.0442 -0.5694 0.1186  -0.1757 162 ASP A CA  
1290 C C   . ASP A 163 ? 1.7436 1.2912 1.0391 -0.5467 0.1014  -0.1655 162 ASP A C   
1291 O O   . ASP A 163 ? 1.7076 1.2770 1.0021 -0.5423 0.0683  -0.1407 162 ASP A O   
1292 C CB  . ASP A 163 ? 1.9671 1.4641 1.1612 -0.5994 0.1545  -0.2201 162 ASP A CB  
1293 C CG  . ASP A 163 ? 2.0853 1.5668 1.1776 -0.6345 0.1575  -0.2266 162 ASP A CG  
1294 O OD1 . ASP A 163 ? 2.1940 1.6907 1.2400 -0.6332 0.1302  -0.1944 162 ASP A OD1 
1295 O OD2 . ASP A 163 ? 1.9810 1.4343 1.0402 -0.6645 0.1867  -0.2638 162 ASP A OD2 
1296 N N   . HIS A 164 ? 1.6580 1.1933 1.0210 -0.5333 0.1237  -0.1844 163 HIS A N   
1297 C CA  . HIS A 164 ? 1.5650 1.1094 0.9992 -0.5130 0.1078  -0.1736 163 HIS A CA  
1298 C C   . HIS A 164 ? 1.5662 1.1448 1.0146 -0.4896 0.0749  -0.1325 163 HIS A C   
1299 O O   . HIS A 164 ? 1.5259 1.1162 1.0075 -0.4802 0.0531  -0.1159 163 HIS A O   
1300 C CB  . HIS A 164 ? 1.6111 1.1375 1.1193 -0.4990 0.1337  -0.1963 163 HIS A CB  
1301 C CG  . HIS A 164 ? 1.8173 1.3425 1.3938 -0.4850 0.1190  -0.1897 163 HIS A CG  
1302 N ND1 . HIS A 164 ? 1.9828 1.4917 1.5664 -0.5012 0.1191  -0.2052 163 HIS A ND1 
1303 C CD2 . HIS A 164 ? 1.8442 1.3805 1.4828 -0.4579 0.1031  -0.1687 163 HIS A CD2 
1304 C CE1 . HIS A 164 ? 1.9680 1.4765 1.6157 -0.4842 0.1039  -0.1921 163 HIS A CE1 
1305 N NE2 . HIS A 164 ? 1.9260 1.4506 1.6053 -0.4584 0.0931  -0.1693 163 HIS A NE2 
1306 N N   . LEU A 165 ? 1.4799 1.0734 0.9029 -0.4819 0.0731  -0.1172 164 LEU A N   
1307 C CA  . LEU A 165 ? 1.3785 1.0059 0.8143 -0.4620 0.0449  -0.0816 164 LEU A CA  
1308 C C   . LEU A 165 ? 1.4070 1.0526 0.8025 -0.4740 0.0150  -0.0621 164 LEU A C   
1309 O O   . LEU A 165 ? 1.3784 1.0469 0.8006 -0.4634 -0.0087 -0.0408 164 LEU A O   
1310 C CB  . LEU A 165 ? 1.4020 1.0391 0.8300 -0.4500 0.0538  -0.0733 164 LEU A CB  
1311 C CG  . LEU A 165 ? 1.1849 0.8581 0.6251 -0.4312 0.0283  -0.0397 164 LEU A CG  
1312 C CD1 . LEU A 165 ? 1.1006 0.7914 0.5958 -0.4143 0.0105  -0.0251 164 LEU A CD1 
1313 C CD2 . LEU A 165 ? 1.1403 0.8182 0.5888 -0.4174 0.0437  -0.0379 164 LEU A CD2 
1314 N N   . VAL A 166 ? 1.5125 1.1474 0.8437 -0.4977 0.0158  -0.0702 165 VAL A N   
1315 C CA  . VAL A 166 ? 1.5210 1.1713 0.8157 -0.5111 -0.0145 -0.0546 165 VAL A CA  
1316 C C   . VAL A 166 ? 1.5155 1.1651 0.8337 -0.5178 -0.0252 -0.0603 165 VAL A C   
1317 O O   . VAL A 166 ? 1.4157 1.0893 0.7440 -0.5150 -0.0524 -0.0405 165 VAL A O   
1318 C CB  . VAL A 166 ? 1.5439 1.1777 0.7608 -0.5384 -0.0130 -0.0638 165 VAL A CB  
1319 C CG1 . VAL A 166 ? 1.5188 1.1653 0.7052 -0.5546 -0.0457 -0.0532 165 VAL A CG1 
1320 C CG2 . VAL A 166 ? 1.5490 1.1873 0.7391 -0.5322 -0.0106 -0.0490 165 VAL A CG2 
1321 N N   . ARG A 167 ? 1.5983 1.2202 0.9296 -0.5273 -0.0024 -0.0885 166 ARG A N   
1322 C CA  . ARG A 167 ? 1.6600 1.2772 1.0160 -0.5347 -0.0100 -0.0954 166 ARG A CA  
1323 C C   . ARG A 167 ? 1.5798 1.2124 0.9997 -0.5112 -0.0219 -0.0750 166 ARG A C   
1324 O O   . ARG A 167 ? 1.4848 1.1302 0.9160 -0.5140 -0.0421 -0.0627 166 ARG A O   
1325 C CB  . ARG A 167 ? 1.8381 1.4206 1.1970 -0.5517 0.0188  -0.1328 166 ARG A CB  
1326 C CG  . ARG A 167 ? 2.0027 1.5691 1.4297 -0.5342 0.0403  -0.1446 166 ARG A CG  
1327 C CD  . ARG A 167 ? 2.1978 1.7304 1.6316 -0.5532 0.0705  -0.1854 166 ARG A CD  
1328 N NE  . ARG A 167 ? 2.3276 1.8458 1.7018 -0.5743 0.0937  -0.2090 166 ARG A NE  
1329 C CZ  . ARG A 167 ? 2.3922 1.8819 1.7557 -0.5975 0.1241  -0.2488 166 ARG A CZ  
1330 N NH1 . ARG A 167 ? 2.4709 1.9441 1.8863 -0.6007 0.1342  -0.2698 166 ARG A NH1 
1331 N NH2 . ARG A 167 ? 2.3425 1.8190 1.6431 -0.6192 0.1454  -0.2681 166 ARG A NH2 
1332 N N   . ARG A 168 ? 1.5209 1.1518 0.9808 -0.4899 -0.0095 -0.0718 167 ARG A N   
1333 C CA  . ARG A 168 ? 1.3722 1.0177 0.8850 -0.4687 -0.0227 -0.0498 167 ARG A CA  
1334 C C   . ARG A 168 ? 1.2117 0.8923 0.7118 -0.4649 -0.0498 -0.0209 167 ARG A C   
1335 O O   . ARG A 168 ? 1.2115 0.9024 0.7337 -0.4637 -0.0654 -0.0069 167 ARG A O   
1336 C CB  . ARG A 168 ? 1.3397 0.9826 0.8903 -0.4466 -0.0088 -0.0493 167 ARG A CB  
1337 C CG  . ARG A 168 ? 1.4081 1.0232 1.0127 -0.4404 0.0062  -0.0663 167 ARG A CG  
1338 C CD  . ARG A 168 ? 1.5627 1.1757 1.2040 -0.4201 0.0203  -0.0699 167 ARG A CD  
1339 N NE  . ARG A 168 ? 1.7743 1.3653 1.4803 -0.4098 0.0256  -0.0791 167 ARG A NE  
1340 C CZ  . ARG A 168 ? 1.8393 1.4369 1.5880 -0.3930 0.0061  -0.0563 167 ARG A CZ  
1341 N NH1 . ARG A 168 ? 1.7884 1.4153 1.5207 -0.3859 -0.0161 -0.0262 167 ARG A NH1 
1342 N NH2 . ARG A 168 ? 1.9022 1.4764 1.7108 -0.3845 0.0084  -0.0640 167 ARG A NH2 
1343 N N   . LEU A 169 ? 1.1925 0.8900 0.6588 -0.4646 -0.0544 -0.0130 168 LEU A N   
1344 C CA  . LEU A 169 ? 1.2065 0.9386 0.6685 -0.4604 -0.0788 0.0119  168 LEU A CA  
1345 C C   . LEU A 169 ? 1.3818 1.1218 0.8218 -0.4796 -0.0985 0.0133  168 LEU A C   
1346 O O   . LEU A 169 ? 1.4224 1.1874 0.8818 -0.4770 -0.1168 0.0298  168 LEU A O   
1347 C CB  . LEU A 169 ? 1.1881 0.9333 0.6261 -0.4541 -0.0785 0.0200  168 LEU A CB  
1348 C CG  . LEU A 169 ? 1.2018 0.9636 0.6741 -0.4302 -0.0731 0.0329  168 LEU A CG  
1349 C CD1 . LEU A 169 ? 1.1864 0.9331 0.7015 -0.4174 -0.0582 0.0251  168 LEU A CD1 
1350 C CD2 . LEU A 169 ? 1.2601 1.0197 0.7051 -0.4277 -0.0627 0.0316  168 LEU A CD2 
1351 N N   . SER A 170 ? 1.4243 1.1436 0.8247 -0.5002 -0.0940 -0.0059 169 SER A N   
1352 C CA  . SER A 170 ? 1.5300 1.2566 0.9118 -0.5192 -0.1140 -0.0068 169 SER A CA  
1353 C C   . SER A 170 ? 1.4880 1.2124 0.9101 -0.5198 -0.1157 -0.0076 169 SER A C   
1354 O O   . SER A 170 ? 1.5602 1.3029 0.9896 -0.5271 -0.1348 0.0009  169 SER A O   
1355 C CB  . SER A 170 ? 1.6704 1.3739 0.9974 -0.5438 -0.1087 -0.0290 169 SER A CB  
1356 O OG  . SER A 170 ? 1.6945 1.3676 1.0290 -0.5534 -0.0863 -0.0551 169 SER A OG  
1357 N N   . THR A 171 ? 1.4218 1.1224 0.8723 -0.5127 -0.0958 -0.0178 170 THR A N   
1358 C CA  . THR A 171 ? 1.3806 1.0748 0.8744 -0.5093 -0.0966 -0.0133 170 THR A CA  
1359 C C   . THR A 171 ? 1.4460 1.1714 0.9611 -0.5005 -0.1153 0.0134  170 THR A C   
1360 O O   . THR A 171 ? 1.5246 1.2534 1.0549 -0.5090 -0.1244 0.0182  170 THR A O   
1361 C CB  . THR A 171 ? 1.3753 1.0455 0.9048 -0.4945 -0.0773 -0.0191 170 THR A CB  
1362 O OG1 . THR A 171 ? 1.3486 0.9858 0.8816 -0.5073 -0.0602 -0.0464 170 THR A OG1 
1363 C CG2 . THR A 171 ? 1.3383 1.0137 0.9108 -0.4813 -0.0859 0.0020  170 THR A CG2 
1364 N N   . LEU A 172 ? 1.4285 1.1764 0.9452 -0.4851 -0.1189 0.0287  171 LEU A N   
1365 C CA  . LEU A 172 ? 1.3765 1.1566 0.9138 -0.4773 -0.1331 0.0509  171 LEU A CA  
1366 C C   . LEU A 172 ? 1.3094 1.1114 0.8380 -0.4928 -0.1514 0.0535  171 LEU A C   
1367 O O   . LEU A 172 ? 1.2437 1.0658 0.7952 -0.4940 -0.1600 0.0655  171 LEU A O   
1368 C CB  . LEU A 172 ? 1.4545 1.2547 0.9910 -0.4605 -0.1320 0.0612  171 LEU A CB  
1369 C CG  . LEU A 172 ? 1.4235 1.2486 0.9903 -0.4453 -0.1351 0.0800  171 LEU A CG  
1370 C CD1 . LEU A 172 ? 1.4367 1.2953 1.0124 -0.4525 -0.1512 0.0913  171 LEU A CD1 
1371 C CD2 . LEU A 172 ? 1.5311 1.3372 1.1233 -0.4400 -0.1285 0.0835  171 LEU A CD2 
1372 N N   . CYS A 173 ? 1.4266 1.2245 0.9219 -0.5059 -0.1573 0.0414  172 CYS A N   
1373 C CA  . CYS A 173 ? 1.3258 1.1460 0.8148 -0.5198 -0.1787 0.0433  172 CYS A CA  
1374 C C   . CYS A 173 ? 1.5078 1.3154 1.0001 -0.5385 -0.1812 0.0306  172 CYS A C   
1375 O O   . CYS A 173 ? 1.5111 1.3398 1.0200 -0.5475 -0.1960 0.0345  172 CYS A O   
1376 C CB  . CYS A 173 ? 1.1883 1.0108 0.6370 -0.5258 -0.1892 0.0396  172 CYS A CB  
1377 S SG  . CYS A 173 ? 1.5826 1.4188 1.0272 -0.5058 -0.1868 0.0547  172 CYS A SG  
1378 N N   . THR A 174 ? 1.5501 1.3237 1.0313 -0.5452 -0.1654 0.0133  173 THR A N   
1379 C CA  . THR A 174 ? 1.6022 1.3614 1.0918 -0.5624 -0.1651 0.0002  173 THR A CA  
1380 C C   . THR A 174 ? 1.5540 1.3143 1.0852 -0.5577 -0.1620 0.0133  173 THR A C   
1381 O O   . THR A 174 ? 1.4918 1.2650 1.0376 -0.5693 -0.1718 0.0155  173 THR A O   
1382 C CB  . THR A 174 ? 1.4303 1.1524 0.9009 -0.5730 -0.1475 -0.0253 173 THR A CB  
1383 O OG1 . THR A 174 ? 1.5057 1.2030 1.0098 -0.5642 -0.1299 -0.0261 173 THR A OG1 
1384 C CG2 . THR A 174 ? 1.4640 1.1786 0.8947 -0.5713 -0.1404 -0.0338 173 THR A CG2 
1385 N N   . THR A 175 ? 1.5907 1.3376 1.1404 -0.5418 -0.1494 0.0226  174 THR A N   
1386 C CA  . THR A 175 ? 1.5078 1.2512 1.0893 -0.5400 -0.1483 0.0374  174 THR A CA  
1387 C C   . THR A 175 ? 1.3950 1.1748 0.9872 -0.5390 -0.1600 0.0554  174 THR A C   
1388 O O   . THR A 175 ? 1.4117 1.1931 1.0222 -0.5468 -0.1610 0.0645  174 THR A O   
1389 C CB  . THR A 175 ? 1.3319 1.0515 0.9319 -0.5235 -0.1365 0.0450  174 THR A CB  
1390 O OG1 . THR A 175 ? 1.3080 1.0448 0.9234 -0.5141 -0.1417 0.0686  174 THR A OG1 
1391 C CG2 . THR A 175 ? 1.2011 0.9152 0.7874 -0.5109 -0.1274 0.0357  174 THR A CG2 
1392 N N   . MET A 176 ? 1.2938 1.1019 0.8759 -0.5310 -0.1676 0.0597  175 MET A N   
1393 C CA  . MET A 176 ? 1.3163 1.1614 0.9154 -0.5305 -0.1771 0.0729  175 MET A CA  
1394 C C   . MET A 176 ? 1.3442 1.2088 0.9451 -0.5474 -0.1916 0.0640  175 MET A C   
1395 O O   . MET A 176 ? 1.3284 1.2219 0.9527 -0.5525 -0.1983 0.0700  175 MET A O   
1396 C CB  . MET A 176 ? 1.4073 1.2743 1.0039 -0.5131 -0.1787 0.0817  175 MET A CB  
1397 C CG  . MET A 176 ? 1.3730 1.2674 0.9947 -0.5068 -0.1780 0.0970  175 MET A CG  
1398 S SD  . MET A 176 ? 1.3148 1.1852 0.9467 -0.5063 -0.1660 0.1083  175 MET A SD  
1399 C CE  . MET A 176 ? 1.3134 1.2232 0.9665 -0.5071 -0.1661 0.1218  175 MET A CE  
1400 N N   . ASN A 177 ? 1.4174 1.2661 0.9950 -0.5572 -0.1960 0.0479  176 ASN A N   
1401 C CA  . ASN A 177 ? 1.4000 1.2642 0.9760 -0.5741 -0.2133 0.0373  176 ASN A CA  
1402 C C   . ASN A 177 ? 1.3848 1.2863 0.9684 -0.5695 -0.2323 0.0451  176 ASN A C   
1403 O O   . ASN A 177 ? 1.2725 1.2025 0.8885 -0.5757 -0.2423 0.0476  176 ASN A O   
1404 C CB  . ASN A 177 ? 1.4765 1.3414 1.0794 -0.5899 -0.2120 0.0336  176 ASN A CB  
1405 C CG  . ASN A 177 ? 1.6418 1.5151 1.2428 -0.6089 -0.2283 0.0174  176 ASN A CG  
1406 O OD1 . ASN A 177 ? 1.5936 1.4605 1.1637 -0.6130 -0.2384 0.0066  176 ASN A OD1 
1407 N ND2 . ASN A 177 ? 1.6513 1.5385 1.2839 -0.6222 -0.2309 0.0148  176 ASN A ND2 
1408 N N   . VAL A 178 ? 1.4570 1.3571 1.0137 -0.5594 -0.2366 0.0480  177 VAL A N   
1409 C CA  . VAL A 178 ? 1.4283 1.3594 0.9924 -0.5533 -0.2557 0.0576  177 VAL A CA  
1410 C C   . VAL A 178 ? 1.4275 1.3434 0.9446 -0.5521 -0.2629 0.0557  177 VAL A C   
1411 O O   . VAL A 178 ? 1.3850 1.2719 0.8722 -0.5481 -0.2448 0.0505  177 VAL A O   
1412 C CB  . VAL A 178 ? 1.4027 1.3555 0.9979 -0.5357 -0.2468 0.0729  177 VAL A CB  
1413 C CG1 . VAL A 178 ? 1.4705 1.4005 1.0445 -0.5202 -0.2273 0.0772  177 VAL A CG1 
1414 C CG2 . VAL A 178 ? 1.4269 1.4140 1.0429 -0.5302 -0.2667 0.0815  177 VAL A CG2 
1415 N N   . ALA A 179 ? 1.5378 1.4717 1.0490 -0.5571 -0.2895 0.0596  178 ALA A N   
1416 C CA  . ALA A 179 ? 1.5756 1.4920 1.0331 -0.5614 -0.2992 0.0590  178 ALA A CA  
1417 C C   . ALA A 179 ? 1.4566 1.3929 0.9202 -0.5482 -0.3140 0.0776  178 ALA A C   
1418 O O   . ALA A 179 ? 1.4987 1.4522 0.9664 -0.5544 -0.3448 0.0842  178 ALA A O   
1419 C CB  . ALA A 179 ? 1.6225 1.5333 1.0534 -0.5842 -0.3221 0.0469  178 ALA A CB  
1420 N N   . PRO A 180 ? 1.3530 1.2859 0.8195 -0.5300 -0.2935 0.0860  179 PRO A N   
1421 C CA  . PRO A 180 ? 1.3395 1.2956 0.8291 -0.5140 -0.3017 0.1036  179 PRO A CA  
1422 C C   . PRO A 180 ? 1.3989 1.3423 0.8430 -0.5160 -0.3163 0.1126  179 PRO A C   
1423 O O   . PRO A 180 ? 1.3858 1.2966 0.7707 -0.5275 -0.3097 0.1040  179 PRO A O   
1424 C CB  . PRO A 180 ? 1.2134 1.1663 0.7197 -0.4960 -0.2710 0.1056  179 PRO A CB  
1425 C CG  . PRO A 180 ? 1.1369 1.0646 0.6323 -0.5026 -0.2502 0.0909  179 PRO A CG  
1426 C CD  . PRO A 180 ? 1.2921 1.1988 0.7465 -0.5231 -0.2610 0.0780  179 PRO A CD  
1427 N N   . ILE A 181 ? 1.4085 1.3766 0.8812 -0.5064 -0.3356 0.1294  180 ILE A N   
1428 C CA  . ILE A 181 ? 1.4695 1.4250 0.9040 -0.5050 -0.3472 0.1431  180 ILE A CA  
1429 C C   . ILE A 181 ? 1.4026 1.3464 0.8304 -0.4883 -0.3150 0.1453  180 ILE A C   
1430 O O   . ILE A 181 ? 1.1913 1.1562 0.6695 -0.4716 -0.2994 0.1471  180 ILE A O   
1431 C CB  . ILE A 181 ? 1.5687 1.5545 1.0455 -0.5000 -0.3818 0.1614  180 ILE A CB  
1432 C CG1 . ILE A 181 ? 1.7877 1.7758 1.2533 -0.5193 -0.4201 0.1611  180 ILE A CG1 
1433 C CG2 . ILE A 181 ? 1.5702 1.5452 1.0227 -0.4919 -0.3860 0.1793  180 ILE A CG2 
1434 C CD1 . ILE A 181 ? 1.9017 1.9026 1.3972 -0.5290 -0.4190 0.1433  180 ILE A CD1 
1435 N N   . VAL A 182 ? 1.4535 1.3633 0.8184 -0.4948 -0.3043 0.1433  181 VAL A N   
1436 C CA  . VAL A 182 ? 1.4040 1.2996 0.7610 -0.4810 -0.2725 0.1421  181 VAL A CA  
1437 C C   . VAL A 182 ? 1.4677 1.3750 0.8373 -0.4683 -0.2812 0.1624  181 VAL A C   
1438 O O   . VAL A 182 ? 1.5855 1.4855 0.9237 -0.4780 -0.3063 0.1759  181 VAL A O   
1439 C CB  . VAL A 182 ? 1.4973 1.3500 0.7850 -0.4957 -0.2514 0.1264  181 VAL A CB  
1440 C CG1 . VAL A 182 ? 1.5994 1.4377 0.8824 -0.4821 -0.2196 0.1245  181 VAL A CG1 
1441 C CG2 . VAL A 182 ? 1.4433 1.2841 0.7293 -0.5059 -0.2385 0.1047  181 VAL A CG2 
1442 N N   . ARG A 183 ? 1.3807 1.3056 0.7970 -0.4473 -0.2619 0.1651  182 ARG A N   
1443 C CA  . ARG A 183 ? 1.3427 1.2790 0.7781 -0.4337 -0.2651 0.1820  182 ARG A CA  
1444 C C   . ARG A 183 ? 1.3888 1.3049 0.8068 -0.4235 -0.2306 0.1759  182 ARG A C   
1445 O O   . ARG A 183 ? 1.3958 1.3056 0.8215 -0.4181 -0.2047 0.1603  182 ARG A O   
1446 C CB  . ARG A 183 ? 1.2678 1.2483 0.7834 -0.4180 -0.2728 0.1887  182 ARG A CB  
1447 C CG  . ARG A 183 ? 1.2434 1.2492 0.7927 -0.4266 -0.3041 0.1918  182 ARG A CG  
1448 C CD  . ARG A 183 ? 1.3355 1.3392 0.8715 -0.4345 -0.3405 0.2094  182 ARG A CD  
1449 N NE  . ARG A 183 ? 1.3289 1.3520 0.9092 -0.4197 -0.3485 0.2261  182 ARG A NE  
1450 C CZ  . ARG A 183 ? 1.2068 1.2703 0.8681 -0.4086 -0.3557 0.2279  182 ARG A CZ  
1451 N NH1 . ARG A 183 ? 1.1048 1.1930 0.8073 -0.4117 -0.3544 0.2145  182 ARG A NH1 
1452 N NH2 . ARG A 183 ? 1.1252 1.2040 0.8277 -0.3959 -0.3622 0.2419  182 ARG A NH2 
1453 N N   . TYR A 184 ? 1.3334 1.2387 0.7311 -0.4210 -0.2313 0.1888  183 TYR A N   
1454 C CA  . TYR A 184 ? 1.3758 1.2643 0.7636 -0.4111 -0.1984 0.1829  183 TYR A CA  
1455 C C   . TYR A 184 ? 1.3276 1.2259 0.7350 -0.3996 -0.2033 0.2019  183 TYR A C   
1456 O O   . TYR A 184 ? 1.2945 1.2019 0.7061 -0.4036 -0.2341 0.2209  183 TYR A O   
1457 C CB  . TYR A 184 ? 1.4567 1.3005 0.7696 -0.4294 -0.1803 0.1694  183 TYR A CB  
1458 C CG  . TYR A 184 ? 1.6220 1.4417 0.8688 -0.4508 -0.2025 0.1825  183 TYR A CG  
1459 C CD1 . TYR A 184 ? 1.6772 1.4954 0.8972 -0.4692 -0.2323 0.1845  183 TYR A CD1 
1460 C CD2 . TYR A 184 ? 1.5648 1.3619 0.7736 -0.4542 -0.1944 0.1932  183 TYR A CD2 
1461 C CE1 . TYR A 184 ? 1.7135 1.5087 0.8688 -0.4904 -0.2563 0.1977  183 TYR A CE1 
1462 C CE2 . TYR A 184 ? 1.6082 1.3799 0.7492 -0.4763 -0.2168 0.2077  183 TYR A CE2 
1463 C CZ  . TYR A 184 ? 1.7100 1.4810 0.8234 -0.4945 -0.2491 0.2104  183 TYR A CZ  
1464 O OH  . TYR A 184 ? 1.8416 1.5864 0.8836 -0.5181 -0.2752 0.2262  183 TYR A OH  
1465 N N   . SER A 185 ? 1.3412 1.2379 0.7661 -0.3849 -0.1741 0.1965  184 SER A N   
1466 C CA  . SER A 185 ? 1.4171 1.3210 0.8624 -0.3740 -0.1750 0.2129  184 SER A CA  
1467 C C   . SER A 185 ? 1.4513 1.3167 0.8266 -0.3901 -0.1786 0.2248  184 SER A C   
1468 O O   . SER A 185 ? 1.4809 1.3106 0.7949 -0.4047 -0.1588 0.2118  184 SER A O   
1469 C CB  . SER A 185 ? 1.4202 1.3348 0.9068 -0.3541 -0.1421 0.2017  184 SER A CB  
1470 O OG  . SER A 185 ? 1.3426 1.2538 0.8355 -0.3470 -0.1369 0.2146  184 SER A OG  
1471 N N   . SER A 186 ? 1.5254 1.3973 0.9112 -0.3888 -0.2037 0.2494  185 SER A N   
1472 C CA  . SER A 186 ? 1.6747 1.5088 0.9930 -0.4049 -0.2104 0.2660  185 SER A CA  
1473 C C   . SER A 186 ? 1.6686 1.4744 0.9561 -0.4044 -0.1672 0.2531  185 SER A C   
1474 O O   . SER A 186 ? 1.6224 1.3862 0.8311 -0.4255 -0.1576 0.2530  185 SER A O   
1475 C CB  . SER A 186 ? 1.6949 1.5439 1.0501 -0.3973 -0.2412 0.2957  185 SER A CB  
1476 O OG  . SER A 186 ? 1.6319 1.5077 1.0595 -0.3733 -0.2221 0.2944  185 SER A OG  
1477 N N   . THR A 187 ? 1.6578 1.4870 1.0082 -0.3817 -0.1409 0.2408  186 THR A N   
1478 C CA  . THR A 187 ? 1.5761 1.3850 0.9153 -0.3775 -0.0990 0.2255  186 THR A CA  
1479 C C   . THR A 187 ? 1.4866 1.2863 0.8187 -0.3787 -0.0691 0.1942  186 THR A C   
1480 O O   . THR A 187 ? 1.4374 1.2325 0.7886 -0.3687 -0.0354 0.1774  186 THR A O   
1481 C CB  . THR A 187 ? 1.4347 1.2719 0.8471 -0.3526 -0.0872 0.2300  186 THR A CB  
1482 O OG1 . THR A 187 ? 1.2800 1.1612 0.7663 -0.3338 -0.0910 0.2211  186 THR A OG1 
1483 C CG2 . THR A 187 ? 1.5759 1.4155 0.9959 -0.3525 -0.1134 0.2604  186 THR A CG2 
1484 N N   . SER A 188 ? 1.4226 1.2197 0.7323 -0.3908 -0.0827 0.1864  187 SER A N   
1485 C CA  . SER A 188 ? 1.3631 1.1441 0.6592 -0.3961 -0.0570 0.1578  187 SER A CA  
1486 C C   . SER A 188 ? 1.4214 1.1600 0.6627 -0.4110 -0.0223 0.1416  187 SER A C   
1487 O O   . SER A 188 ? 1.5196 1.2314 0.7013 -0.4287 -0.0249 0.1537  187 SER A O   
1488 C CB  . SER A 188 ? 1.3731 1.1502 0.6394 -0.4129 -0.0789 0.1544  187 SER A CB  
1489 O OG  . SER A 188 ? 1.5861 1.4012 0.9115 -0.3990 -0.0992 0.1586  187 SER A OG  
1490 N N   . THR A 189 ? 1.3325 1.0635 0.5944 -0.4054 0.0102  0.1139  188 THR A N   
1491 C CA  . THR A 189 ? 1.4746 1.1647 0.6881 -0.4229 0.0462  0.0917  188 THR A CA  
1492 C C   . THR A 189 ? 1.5725 1.2346 0.7110 -0.4535 0.0369  0.0865  188 THR A C   
1493 O O   . THR A 189 ? 1.6167 1.2935 0.7593 -0.4557 0.0093  0.0916  188 THR A O   
1494 C CB  . THR A 189 ? 1.4036 1.0927 0.6659 -0.4104 0.0800  0.0603  188 THR A CB  
1495 O OG1 . THR A 189 ? 1.4478 1.1374 0.7166 -0.4150 0.0730  0.0461  188 THR A OG1 
1496 C CG2 . THR A 189 ? 1.1431 0.8675 0.4855 -0.3792 0.0802  0.0658  188 THR A CG2 
1497 N N   . PRO A 190 ? 1.6182 1.2398 0.6865 -0.4791 0.0605  0.0756  189 PRO A N   
1498 C CA  . PRO A 190 ? 1.7225 1.3151 0.7133 -0.5119 0.0554  0.0665  189 PRO A CA  
1499 C C   . PRO A 190 ? 1.7637 1.3610 0.7826 -0.5115 0.0620  0.0397  189 PRO A C   
1500 O O   . PRO A 190 ? 1.7345 1.3326 0.7258 -0.5255 0.0370  0.0423  189 PRO A O   
1501 C CB  . PRO A 190 ? 1.7303 1.2792 0.6574 -0.5366 0.0953  0.0489  189 PRO A CB  
1502 C CG  . PRO A 190 ? 1.7602 1.3152 0.7102 -0.5204 0.1019  0.0677  189 PRO A CG  
1503 C CD  . PRO A 190 ? 1.6328 1.2333 0.6853 -0.4815 0.0918  0.0730  189 PRO A CD  
1504 N N   . GLY A 191 ? 1.8429 1.4427 0.9196 -0.4956 0.0940  0.0144  190 GLY A N   
1505 C CA  . GLY A 191 ? 1.8189 1.4215 0.9315 -0.4929 0.1000  -0.0093 190 GLY A CA  
1506 C C   . GLY A 191 ? 1.6281 1.2632 0.7720 -0.4808 0.0593  0.0105  190 GLY A C   
1507 O O   . GLY A 191 ? 1.6622 1.2928 0.7980 -0.4921 0.0514  -0.0007 190 GLY A O   
1508 N N   . THR A 192 ? 1.4356 1.1030 0.6169 -0.4591 0.0357  0.0383  191 THR A N   
1509 C CA  . THR A 192 ? 1.3116 1.0130 0.5307 -0.4468 0.0006  0.0561  191 THR A CA  
1510 C C   . THR A 192 ? 1.3348 1.0359 0.5026 -0.4663 -0.0337 0.0736  191 THR A C   
1511 O O   . THR A 192 ? 1.3364 1.0448 0.5070 -0.4728 -0.0514 0.0707  191 THR A O   
1512 C CB  . THR A 192 ? 1.3347 1.0725 0.6183 -0.4181 -0.0089 0.0750  191 THR A CB  
1513 O OG1 . THR A 192 ? 1.2752 1.0190 0.6155 -0.3994 0.0140  0.0583  191 THR A OG1 
1514 C CG2 . THR A 192 ? 1.3470 1.1193 0.6592 -0.4113 -0.0459 0.0952  191 THR A CG2 
1515 N N   . GLU A 193 ? 1.4522 1.1440 0.5748 -0.4760 -0.0442 0.0921  192 GLU A N   
1516 C CA  . GLU A 193 ? 1.5126 1.2005 0.5827 -0.4964 -0.0800 0.1098  192 GLU A CA  
1517 C C   . GLU A 193 ? 1.6016 1.2670 0.6237 -0.5222 -0.0780 0.0883  192 GLU A C   
1518 O O   . GLU A 193 ? 1.6072 1.2869 0.6322 -0.5279 -0.1079 0.0939  192 GLU A O   
1519 C CB  . GLU A 193 ? 1.6403 1.3054 0.6504 -0.5103 -0.0839 0.1279  192 GLU A CB  
1520 C CG  . GLU A 193 ? 1.8260 1.4953 0.8009 -0.5236 -0.1312 0.1559  192 GLU A CG  
1521 C CD  . GLU A 193 ? 2.0880 1.7277 0.9946 -0.5408 -0.1366 0.1758  192 GLU A CD  
1522 O OE1 . GLU A 193 ? 2.1426 1.7584 1.0279 -0.5433 -0.0998 0.1661  192 GLU A OE1 
1523 O OE2 . GLU A 193 ? 2.2206 1.8595 1.0954 -0.5528 -0.1784 0.2015  192 GLU A OE2 
1524 N N   . ARG A 194 ? 1.6984 1.3292 0.6807 -0.5386 -0.0409 0.0614  193 ARG A N   
1525 C CA  . ARG A 194 ? 1.8137 1.4206 0.7516 -0.5652 -0.0323 0.0355  193 ARG A CA  
1526 C C   . ARG A 194 ? 1.8268 1.4548 0.8253 -0.5528 -0.0384 0.0240  193 ARG A C   
1527 O O   . ARG A 194 ? 1.9142 1.5420 0.8911 -0.5689 -0.0582 0.0201  193 ARG A O   
1528 C CB  . ARG A 194 ? 2.0010 1.5705 0.9048 -0.5817 0.0162  0.0033  193 ARG A CB  
1529 C CG  . ARG A 194 ? 2.2811 1.8192 1.1139 -0.6189 0.0257  -0.0222 193 ARG A CG  
1530 C CD  . ARG A 194 ? 2.3850 1.9099 1.2538 -0.6203 0.0649  -0.0634 193 ARG A CD  
1531 N NE  . ARG A 194 ? 2.4364 1.9499 1.3379 -0.6087 0.1073  -0.0808 193 ARG A NE  
1532 C CZ  . ARG A 194 ? 2.4051 1.9015 1.3379 -0.6117 0.1471  -0.1191 193 ARG A CZ  
1533 N NH1 . ARG A 194 ? 2.3039 1.7922 1.2719 -0.6001 0.1829  -0.1339 193 ARG A NH1 
1534 N NH2 . ARG A 194 ? 2.4278 1.9152 1.3618 -0.6265 0.1512  -0.1437 193 ARG A NH2 
1535 N N   . MET A 195 ? 1.6473 1.2922 0.7203 -0.5253 -0.0224 0.0191  194 MET A N   
1536 C CA  . MET A 195 ? 1.5863 1.2493 0.7168 -0.5131 -0.0291 0.0123  194 MET A CA  
1537 C C   . MET A 195 ? 1.6142 1.3060 0.7544 -0.5117 -0.0713 0.0353  194 MET A C   
1538 O O   . MET A 195 ? 1.7517 1.4457 0.8988 -0.5199 -0.0814 0.0267  194 MET A O   
1539 C CB  . MET A 195 ? 1.6123 1.2918 0.8179 -0.4830 -0.0132 0.0115  194 MET A CB  
1540 C CG  . MET A 195 ? 1.6165 1.3170 0.8803 -0.4694 -0.0261 0.0131  194 MET A CG  
1541 S SD  . MET A 195 ? 2.0110 1.7458 1.3504 -0.4348 -0.0289 0.0308  194 MET A SD  
1542 C CE  . MET A 195 ? 1.4463 1.1585 0.7964 -0.4264 0.0110  0.0109  194 MET A CE  
1543 N N   . ALA A 196 ? 1.5384 1.2521 0.6843 -0.5018 -0.0949 0.0630  195 ALA A N   
1544 C CA  . ALA A 196 ? 1.4798 1.2227 0.6430 -0.5004 -0.1347 0.0837  195 ALA A CA  
1545 C C   . ALA A 196 ? 1.6554 1.3830 0.7557 -0.5291 -0.1577 0.0828  195 ALA A C   
1546 O O   . ALA A 196 ? 1.5940 1.3375 0.7091 -0.5342 -0.1819 0.0843  195 ALA A O   
1547 C CB  . ALA A 196 ? 1.2709 1.0391 0.4607 -0.4836 -0.1524 0.1111  195 ALA A CB  
1548 N N   . MET A 197 ? 1.7159 1.4125 0.7443 -0.5494 -0.1506 0.0802  196 MET A N   
1549 C CA  . MET A 197 ? 1.8801 1.5591 0.8397 -0.5800 -0.1723 0.0780  196 MET A CA  
1550 C C   . MET A 197 ? 1.8864 1.5570 0.8485 -0.5924 -0.1599 0.0491  196 MET A C   
1551 O O   . MET A 197 ? 1.8806 1.5629 0.8432 -0.6024 -0.1874 0.0499  196 MET A O   
1552 C CB  . MET A 197 ? 1.9469 1.5875 0.8197 -0.6043 -0.1587 0.0755  196 MET A CB  
1553 C CG  . MET A 197 ? 1.8681 1.5101 0.7259 -0.5976 -0.1747 0.1068  196 MET A CG  
1554 S SD  . MET A 197 ? 2.2415 1.9138 1.1160 -0.5940 -0.2380 0.1441  196 MET A SD  
1555 C CE  . MET A 197 ? 2.2853 1.9351 1.1048 -0.6009 -0.2481 0.1740  196 MET A CE  
1556 N N   . GLN A 198 ? 1.8354 1.4863 0.8061 -0.5908 -0.1182 0.0227  197 GLN A N   
1557 C CA  . GLN A 198 ? 1.8460 1.4809 0.8147 -0.6056 -0.1005 -0.0084 197 GLN A CA  
1558 C C   . GLN A 198 ? 1.7621 1.4243 0.7987 -0.5905 -0.1161 -0.0059 197 GLN A C   
1559 O O   . GLN A 198 ? 1.6764 1.3328 0.7061 -0.6065 -0.1206 -0.0221 197 GLN A O   
1560 C CB  . GLN A 198 ? 1.8776 1.4868 0.8548 -0.6040 -0.0524 -0.0364 197 GLN A CB  
1561 C CG  . GLN A 198 ? 2.0446 1.6235 0.9890 -0.6314 -0.0279 -0.0734 197 GLN A CG  
1562 C CD  . GLN A 198 ? 2.1620 1.7149 1.1186 -0.6310 0.0210  -0.1028 197 GLN A CD  
1563 O OE1 . GLN A 198 ? 2.0453 1.5889 0.9844 -0.6277 0.0386  -0.0990 197 GLN A OE1 
1564 N NE2 . GLN A 198 ? 2.2576 1.7984 1.2495 -0.6346 0.0436  -0.1333 197 GLN A NE2 
1565 N N   . LEU A 199 ? 1.6101 1.3010 0.7102 -0.5615 -0.1230 0.0138  198 LEU A N   
1566 C CA  . LEU A 199 ? 1.4898 1.2065 0.6523 -0.5478 -0.1362 0.0188  198 LEU A CA  
1567 C C   . LEU A 199 ? 1.6306 1.3654 0.7821 -0.5606 -0.1742 0.0300  198 LEU A C   
1568 O O   . LEU A 199 ? 1.7659 1.5093 0.9447 -0.5642 -0.1819 0.0230  198 LEU A O   
1569 C CB  . LEU A 199 ? 1.3400 1.0845 0.5630 -0.5179 -0.1366 0.0382  198 LEU A CB  
1570 C CG  . LEU A 199 ? 1.2982 1.0551 0.5855 -0.5013 -0.1282 0.0354  198 LEU A CG  
1571 C CD1 . LEU A 199 ? 1.2700 1.0654 0.6045 -0.4834 -0.1483 0.0592  198 LEU A CD1 
1572 C CD2 . LEU A 199 ? 1.2842 1.0304 0.5731 -0.5165 -0.1300 0.0194  198 LEU A CD2 
1573 N N   . GLN A 200 ? 1.5791 1.3188 0.6934 -0.5678 -0.1989 0.0477  199 GLN A N   
1574 C CA  . GLN A 200 ? 1.5721 1.3303 0.6817 -0.5790 -0.2391 0.0594  199 GLN A CA  
1575 C C   . GLN A 200 ? 1.6632 1.4004 0.7255 -0.6080 -0.2424 0.0375  199 GLN A C   
1576 O O   . GLN A 200 ? 1.6957 1.4482 0.7831 -0.6135 -0.2606 0.0335  199 GLN A O   
1577 C CB  . GLN A 200 ? 1.6331 1.3979 0.7155 -0.5802 -0.2675 0.0850  199 GLN A CB  
1578 C CG  . GLN A 200 ? 1.6908 1.4828 0.7936 -0.5845 -0.3129 0.1006  199 GLN A CG  
1579 C CD  . GLN A 200 ? 1.5913 1.4230 0.7821 -0.5614 -0.3193 0.1094  199 GLN A CD  
1580 O OE1 . GLN A 200 ? 1.6123 1.4640 0.8417 -0.5417 -0.3223 0.1274  199 GLN A OE1 
1581 N NE2 . GLN A 200 ? 1.4796 1.3221 0.7018 -0.5656 -0.3201 0.0958  199 GLN A NE2 
1582 N N   . LYS A 201 ? 1.7865 1.4887 0.7817 -0.6279 -0.2224 0.0210  200 LYS A N   
1583 C CA  . LYS A 201 ? 1.8649 1.5442 0.8114 -0.6582 -0.2191 -0.0053 200 LYS A CA  
1584 C C   . LYS A 201 ? 1.8589 1.5362 0.8530 -0.6550 -0.1959 -0.0299 200 LYS A C   
1585 O O   . LYS A 201 ? 1.8946 1.5671 0.8760 -0.6749 -0.2035 -0.0472 200 LYS A O   
1586 C CB  . LYS A 201 ? 1.8662 1.5070 0.7328 -0.6813 -0.1942 -0.0215 200 LYS A CB  
1587 C CG  . LYS A 201 ? 1.9844 1.6180 0.7825 -0.6958 -0.2217 0.0009  200 LYS A CG  
1588 C CD  . LYS A 201 ? 2.1532 1.7451 0.8609 -0.7276 -0.1961 -0.0202 200 LYS A CD  
1589 C CE  . LYS A 201 ? 2.2888 1.8692 0.9163 -0.7481 -0.2294 0.0041  200 LYS A CE  
1590 N NZ  . LYS A 201 ? 2.3991 1.9364 0.9265 -0.7855 -0.2043 -0.0175 200 LYS A NZ  
1591 N N   . GLU A 202 ? 1.7339 1.4138 0.7830 -0.6308 -0.1691 -0.0311 201 GLU A N   
1592 C CA  . GLU A 202 ? 1.6720 1.3463 0.7693 -0.6261 -0.1481 -0.0507 201 GLU A CA  
1593 C C   . GLU A 202 ? 1.6328 1.3351 0.7789 -0.6199 -0.1736 -0.0397 201 GLU A C   
1594 O O   . GLU A 202 ? 1.6657 1.3614 0.8166 -0.6348 -0.1739 -0.0573 201 GLU A O   
1595 C CB  . GLU A 202 ? 1.7432 1.4119 0.8862 -0.6018 -0.1171 -0.0521 201 GLU A CB  
1596 C CG  . GLU A 202 ? 1.9567 1.5898 1.0743 -0.6122 -0.0784 -0.0808 201 GLU A CG  
1597 C CD  . GLU A 202 ? 2.1774 1.7901 1.3192 -0.6225 -0.0572 -0.1112 201 GLU A CD  
1598 O OE1 . GLU A 202 ? 2.3701 1.9906 1.5225 -0.6315 -0.0745 -0.1132 201 GLU A OE1 
1599 O OE2 . GLU A 202 ? 2.1448 1.7334 1.2998 -0.6217 -0.0227 -0.1341 201 GLU A OE2 
1600 N N   . ILE A 203 ? 1.4719 1.2055 0.6562 -0.5996 -0.1931 -0.0126 202 ILE A N   
1601 C CA  . ILE A 203 ? 1.5390 1.2999 0.7713 -0.5956 -0.2142 -0.0038 202 ILE A CA  
1602 C C   . ILE A 203 ? 1.6573 1.4238 0.8591 -0.6193 -0.2441 -0.0083 202 ILE A C   
1603 O O   . ILE A 203 ? 1.6804 1.4548 0.9081 -0.6273 -0.2522 -0.0165 202 ILE A O   
1604 C CB  . ILE A 203 ? 1.6991 1.4943 0.9785 -0.5723 -0.2280 0.0232  202 ILE A CB  
1605 C CG1 . ILE A 203 ? 1.8650 1.6832 1.1324 -0.5780 -0.2647 0.0395  202 ILE A CG1 
1606 C CG2 . ILE A 203 ? 1.7045 1.4948 0.9913 -0.5517 -0.2060 0.0311  202 ILE A CG2 
1607 C CD1 . ILE A 203 ? 1.9144 1.7654 1.2299 -0.5563 -0.2755 0.0627  202 ILE A CD1 
1608 N N   . ASP A 204 ? 1.7445 1.5052 0.8901 -0.6315 -0.2614 -0.0025 203 ASP A N   
1609 C CA  . ASP A 204 ? 1.7436 1.5081 0.8542 -0.6553 -0.2944 -0.0053 203 ASP A CA  
1610 C C   . ASP A 204 ? 1.8227 1.5607 0.8977 -0.6814 -0.2802 -0.0370 203 ASP A C   
1611 O O   . ASP A 204 ? 1.8736 1.6207 0.9548 -0.6965 -0.3001 -0.0461 203 ASP A O   
1612 C CB  . ASP A 204 ? 1.8637 1.6240 0.9175 -0.6629 -0.3178 0.0119  203 ASP A CB  
1613 C CG  . ASP A 204 ? 1.9131 1.7058 1.0112 -0.6411 -0.3438 0.0431  203 ASP A CG  
1614 O OD1 . ASP A 204 ? 1.8509 1.6721 1.0206 -0.6243 -0.3462 0.0485  203 ASP A OD1 
1615 O OD2 . ASP A 204 ? 1.9411 1.7296 1.0029 -0.6422 -0.3607 0.0615  203 ASP A OD2 
1616 N N   . MET A 205 ? 1.8526 1.5586 0.8948 -0.6873 -0.2444 -0.0561 204 MET A N   
1617 C CA  . MET A 205 ? 1.9807 1.6603 0.9962 -0.7118 -0.2242 -0.0903 204 MET A CA  
1618 C C   . MET A 205 ? 1.9524 1.6385 1.0370 -0.7028 -0.2123 -0.1009 204 MET A C   
1619 O O   . MET A 205 ? 1.9668 1.6371 1.0471 -0.7216 -0.2008 -0.1279 204 MET A O   
1620 C CB  . MET A 205 ? 2.1136 1.7587 1.0892 -0.7188 -0.1848 -0.1101 204 MET A CB  
1621 C CG  . MET A 205 ? 2.2381 1.8537 1.1722 -0.7505 -0.1634 -0.1489 204 MET A CG  
1622 S SD  . MET A 205 ? 2.9351 2.5301 1.9326 -0.7410 -0.1156 -0.1788 204 MET A SD  
1623 C CE  . MET A 205 ? 2.3810 1.9769 1.4134 -0.7070 -0.0949 -0.1590 204 MET A CE  
1624 N N   . SER A 206 ? 1.9295 1.6377 1.0766 -0.6755 -0.2146 -0.0793 205 SER A N   
1625 C CA  . SER A 206 ? 1.7921 1.5076 1.0023 -0.6675 -0.2079 -0.0827 205 SER A CA  
1626 C C   . SER A 206 ? 1.8070 1.5515 1.0392 -0.6740 -0.2414 -0.0740 205 SER A C   
1627 O O   . SER A 206 ? 1.8901 1.6343 1.1531 -0.6819 -0.2390 -0.0862 205 SER A O   
1628 C CB  . SER A 206 ? 1.7005 1.4235 0.9633 -0.6379 -0.1925 -0.0648 205 SER A CB  
1629 O OG  . SER A 206 ? 1.6884 1.3824 0.9545 -0.6321 -0.1584 -0.0793 205 SER A OG  
1630 N N   . VAL A 207 ? 1.7450 1.5140 0.9664 -0.6710 -0.2724 -0.0536 206 VAL A N   
1631 C CA  . VAL A 207 ? 1.7940 1.5941 1.0478 -0.6752 -0.3052 -0.0455 206 VAL A CA  
1632 C C   . VAL A 207 ? 1.9982 1.7922 1.2137 -0.7044 -0.3258 -0.0646 206 VAL A C   
1633 O O   . VAL A 207 ? 2.0032 1.8092 1.2515 -0.7139 -0.3359 -0.0745 206 VAL A O   
1634 C CB  . VAL A 207 ? 1.6956 1.5263 0.9659 -0.6602 -0.3329 -0.0173 206 VAL A CB  
1635 C CG1 . VAL A 207 ? 1.5823 1.4471 0.9045 -0.6624 -0.3614 -0.0122 206 VAL A CG1 
1636 C CG2 . VAL A 207 ? 1.6034 1.4396 0.9053 -0.6333 -0.3116 -0.0009 206 VAL A CG2 
1637 N N   . SER A 208 ? 2.0675 1.8421 1.2118 -0.7205 -0.3314 -0.0705 207 SER A N   
1638 C CA  . SER A 208 ? 2.1996 1.9652 1.2984 -0.7513 -0.3493 -0.0910 207 SER A CA  
1639 C C   . SER A 208 ? 2.1928 1.9325 1.2914 -0.7653 -0.3150 -0.1241 207 SER A C   
1640 O O   . SER A 208 ? 2.2883 2.0159 1.3487 -0.7931 -0.3205 -0.1483 207 SER A O   
1641 C CB  . SER A 208 ? 2.3056 2.0550 1.3199 -0.7681 -0.3648 -0.0871 207 SER A CB  
1642 O OG  . SER A 208 ? 2.3955 2.1137 1.3708 -0.7677 -0.3264 -0.0966 207 SER A OG  
1643 N N   . GLN A 209 ? 2.0097 1.7409 1.1535 -0.7463 -0.2810 -0.1252 208 GLN A N   
1644 C CA  . GLN A 209 ? 1.9853 1.6911 1.1433 -0.7557 -0.2482 -0.1541 208 GLN A CA  
1645 C C   . GLN A 209 ? 1.8964 1.6152 1.1297 -0.7439 -0.2444 -0.1499 208 GLN A C   
1646 O O   . GLN A 209 ? 1.8751 1.5737 1.1336 -0.7486 -0.2192 -0.1693 208 GLN A O   
1647 C CB  . GLN A 209 ? 1.9915 1.6682 1.1369 -0.7471 -0.2096 -0.1624 208 GLN A CB  
1648 C CG  . GLN A 209 ? 2.1050 1.7512 1.2579 -0.7618 -0.1762 -0.1975 208 GLN A CG  
1649 C CD  . GLN A 209 ? 2.1956 1.8136 1.3410 -0.7548 -0.1386 -0.2092 208 GLN A CD  
1650 O OE1 . GLN A 209 ? 2.1707 1.7932 1.3216 -0.7328 -0.1345 -0.1880 208 GLN A OE1 
1651 N NE2 . GLN A 209 ? 2.2561 1.8454 1.3937 -0.7740 -0.1098 -0.2454 208 GLN A NE2 
1652 N N   . GLY A 210 ? 1.8100 1.5615 1.0801 -0.7300 -0.2687 -0.1249 209 GLY A N   
1653 C CA  . GLY A 210 ? 1.7989 1.5642 1.1350 -0.7224 -0.2663 -0.1198 209 GLY A CA  
1654 C C   . GLY A 210 ? 1.8145 1.5639 1.1880 -0.7033 -0.2349 -0.1129 209 GLY A C   
1655 O O   . GLY A 210 ? 1.7461 1.4877 1.1597 -0.7054 -0.2225 -0.1187 209 GLY A O   
1656 N N   . LEU A 211 ? 1.7763 1.5195 1.1366 -0.6852 -0.2233 -0.0997 210 LEU A N   
1657 C CA  . LEU A 211 ? 1.5517 1.2825 0.9479 -0.6650 -0.1988 -0.0897 210 LEU A CA  
1658 C C   . LEU A 211 ? 1.5194 1.2805 0.9503 -0.6459 -0.2107 -0.0608 210 LEU A C   
1659 O O   . LEU A 211 ? 1.4735 1.2306 0.9389 -0.6310 -0.1966 -0.0486 210 LEU A O   
1660 C CB  . LEU A 211 ? 1.5467 1.2536 0.9150 -0.6568 -0.1771 -0.0954 210 LEU A CB  
1661 C CG  . LEU A 211 ? 1.5818 1.2523 0.9361 -0.6718 -0.1516 -0.1267 210 LEU A CG  
1662 C CD1 . LEU A 211 ? 1.6091 1.2594 0.9476 -0.6607 -0.1279 -0.1310 210 LEU A CD1 
1663 C CD2 . LEU A 211 ? 1.3223 0.9773 0.7286 -0.6727 -0.1383 -0.1342 210 LEU A CD2 
1664 N N   . ILE A 212 ? 1.6236 1.4148 1.0461 -0.6476 -0.2376 -0.0506 211 ILE A N   
1665 C CA  . ILE A 212 ? 1.6850 1.5098 1.1468 -0.6340 -0.2502 -0.0281 211 ILE A CA  
1666 C C   . ILE A 212 ? 1.7955 1.6514 1.2660 -0.6453 -0.2820 -0.0273 211 ILE A C   
1667 O O   . ILE A 212 ? 1.8875 1.7464 1.3217 -0.6535 -0.3026 -0.0303 211 ILE A O   
1668 C CB  . ILE A 212 ? 1.9175 1.7503 1.3756 -0.6115 -0.2456 -0.0085 211 ILE A CB  
1669 C CG1 . ILE A 212 ? 1.7499 1.5730 1.1551 -0.6136 -0.2518 -0.0114 211 ILE A CG1 
1670 C CG2 . ILE A 212 ? 2.0807 1.8926 1.5544 -0.5971 -0.2178 -0.0047 211 ILE A CG2 
1671 C CD1 . ILE A 212 ? 1.6107 1.4250 1.0079 -0.5938 -0.2340 -0.0009 211 ILE A CD1 
1672 N N   . ASN A 213 ? 1.7583 1.6359 1.2779 -0.6469 -0.2862 -0.0235 212 ASN A N   
1673 C CA  . ASN A 213 ? 1.7476 1.6579 1.2923 -0.6564 -0.3152 -0.0242 212 ASN A CA  
1674 C C   . ASN A 213 ? 1.6780 1.6228 1.2732 -0.6429 -0.3190 -0.0068 212 ASN A C   
1675 O O   . ASN A 213 ? 1.7087 1.6549 1.3351 -0.6388 -0.2989 -0.0021 212 ASN A O   
1676 C CB  . ASN A 213 ? 1.8250 1.7312 1.3868 -0.6776 -0.3166 -0.0441 212 ASN A CB  
1677 C CG  . ASN A 213 ? 1.9907 1.8814 1.5819 -0.6775 -0.2878 -0.0451 212 ASN A CG  
1678 O OD1 . ASN A 213 ? 2.0272 1.9089 1.6229 -0.6620 -0.2683 -0.0308 212 ASN A OD1 
1679 N ND2 . ASN A 213 ? 2.0897 1.9761 1.7004 -0.6957 -0.2865 -0.0613 212 ASN A ND2 
1680 N N   . ALA A 214 ? 1.7410 1.7125 1.3438 -0.6374 -0.3446 0.0027  213 ALA A N   
1681 C CA  . ALA A 214 ? 1.9703 1.9762 1.6255 -0.6252 -0.3472 0.0162  213 ALA A CA  
1682 C C   . ALA A 214 ? 2.1990 2.2391 1.8939 -0.6331 -0.3805 0.0131  213 ALA A C   
1683 O O   . ALA A 214 ? 2.3229 2.3587 1.9954 -0.6457 -0.4059 0.0048  213 ALA A O   
1684 C CB  . ALA A 214 ? 2.0280 2.0343 1.6672 -0.6046 -0.3419 0.0337  213 ALA A CB  
1685 N N   . ARG A 215 ? 2.3426 2.4166 2.0984 -0.6268 -0.3810 0.0185  214 ARG A N   
1686 C CA  . ARG A 215 ? 2.5355 2.6445 2.3440 -0.6335 -0.4124 0.0138  214 ARG A CA  
1687 C C   . ARG A 215 ? 2.4871 2.6128 2.3005 -0.6200 -0.4401 0.0296  214 ARG A C   
1688 O O   . ARG A 215 ? 2.5761 2.7183 2.4092 -0.6260 -0.4772 0.0285  214 ARG A O   
1689 C CB  . ARG A 215 ? 2.6378 2.7762 2.5192 -0.6385 -0.3977 0.0057  214 ARG A CB  
1690 C CG  . ARG A 215 ? 2.6956 2.8713 2.6445 -0.6472 -0.4282 -0.0044 214 ARG A CG  
1691 C CD  . ARG A 215 ? 2.7757 2.9419 2.7049 -0.6635 -0.4572 -0.0170 214 ARG A CD  
1692 N NE  . ARG A 215 ? 2.8410 3.0436 2.8404 -0.6708 -0.4903 -0.0264 214 ARG A NE  
1693 C CZ  . ARG A 215 ? 2.9515 3.1552 2.9492 -0.6852 -0.5232 -0.0378 214 ARG A CZ  
1694 N NH1 . ARG A 215 ? 3.0211 3.1911 2.9467 -0.6953 -0.5250 -0.0426 214 ARG A NH1 
1695 N NH2 . ARG A 215 ? 2.9646 3.2035 3.0359 -0.6902 -0.5545 -0.0461 214 ARG A NH2 
1696 N N   . GLU A 216 ? 2.2786 2.3990 2.0758 -0.6021 -0.4237 0.0448  215 GLU A N   
1697 C CA  . GLU A 216 ? 2.2278 2.3588 2.0250 -0.5886 -0.4467 0.0617  215 GLU A CA  
1698 C C   . GLU A 216 ? 2.0371 2.2121 1.9201 -0.5832 -0.4632 0.0638  215 GLU A C   
1699 O O   . GLU A 216 ? 2.0924 2.2819 1.9969 -0.5842 -0.5015 0.0690  215 GLU A O   
1700 C CB  . GLU A 216 ? 2.4102 2.5225 2.1538 -0.5979 -0.4811 0.0647  215 GLU A CB  
1701 C CG  . GLU A 216 ? 2.5075 2.5759 2.1637 -0.6029 -0.4647 0.0623  215 GLU A CG  
1702 C CD  . GLU A 216 ? 2.5357 2.5877 2.1498 -0.5878 -0.4568 0.0794  215 GLU A CD  
1703 O OE1 . GLU A 216 ? 2.5091 2.5825 2.1642 -0.5708 -0.4537 0.0925  215 GLU A OE1 
1704 O OE2 . GLU A 216 ? 2.5873 2.6052 2.1291 -0.5943 -0.4520 0.0780  215 GLU A OE2 
1705 N N   . GLY A 217 ? 1.8205 2.0159 1.7533 -0.5786 -0.4348 0.0592  216 GLY A N   
1706 C CA  . GLY A 217 ? 1.7359 1.9742 1.7561 -0.5746 -0.4433 0.0569  216 GLY A CA  
1707 C C   . GLY A 217 ? 1.7948 2.0458 1.8326 -0.5587 -0.4688 0.0739  216 GLY A C   
1708 O O   . GLY A 217 ? 1.8621 2.0871 1.8376 -0.5519 -0.4813 0.0891  216 GLY A O   
1709 N N   . LYS A 218 ? 1.7488 2.0391 1.8738 -0.5539 -0.4752 0.0706  217 LYS A N   
1710 C CA  . LYS A 218 ? 1.7125 2.0174 1.8693 -0.5386 -0.5006 0.0867  217 LYS A CA  
1711 C C   . LYS A 218 ? 1.6286 1.9121 1.7303 -0.5221 -0.4807 0.1040  217 LYS A C   
1712 O O   . LYS A 218 ? 1.5636 1.8321 1.6327 -0.5134 -0.5042 0.1226  217 LYS A O   
1713 C CB  . LYS A 218 ? 1.7200 2.0720 1.9896 -0.5362 -0.5001 0.0756  217 LYS A CB  
1714 C CG  . LYS A 218 ? 1.7773 2.1470 2.0981 -0.5219 -0.5341 0.0909  217 LYS A CG  
1715 C CD  . LYS A 218 ? 1.7806 2.1985 2.2248 -0.5212 -0.5325 0.0749  217 LYS A CD  
1716 C CE  . LYS A 218 ? 1.7889 2.2231 2.2941 -0.5076 -0.5731 0.0905  217 LYS A CE  
1717 N NZ  . LYS A 218 ? 1.7320 2.1528 2.2039 -0.4891 -0.5632 0.1116  217 LYS A NZ  
1718 N N   . LEU A 219 ? 1.5477 1.8290 1.6389 -0.5190 -0.4380 0.0979  218 LEU A N   
1719 C CA  . LEU A 219 ? 1.3753 1.6371 1.4178 -0.5039 -0.4158 0.1109  218 LEU A CA  
1720 C C   . LEU A 219 ? 1.4091 1.6264 1.3581 -0.5082 -0.4056 0.1136  218 LEU A C   
1721 O O   . LEU A 219 ? 1.4345 1.6397 1.3640 -0.5225 -0.3988 0.1016  218 LEU A O   
1722 C CB  . LEU A 219 ? 1.2221 1.5047 1.3022 -0.4991 -0.3779 0.1029  218 LEU A CB  
1723 C CG  . LEU A 219 ? 1.1880 1.5116 1.3546 -0.4906 -0.3801 0.1011  218 LEU A CG  
1724 C CD1 . LEU A 219 ? 1.3040 1.6531 1.5396 -0.4971 -0.4161 0.0958  218 LEU A CD1 
1725 C CD2 . LEU A 219 ? 0.9465 1.2937 1.1518 -0.4945 -0.3412 0.0863  218 LEU A CD2 
1726 N N   . LYS A 220 ? 1.3853 1.5780 1.2805 -0.4966 -0.4032 0.1277  219 LYS A N   
1727 C CA  . LYS A 220 ? 1.3826 1.5329 1.1936 -0.5017 -0.3949 0.1280  219 LYS A CA  
1728 C C   . LYS A 220 ? 1.3146 1.4451 1.0912 -0.4911 -0.3579 0.1289  219 LYS A C   
1729 O O   . LYS A 220 ? 1.1379 1.2796 0.9335 -0.4758 -0.3449 0.1366  219 LYS A O   
1730 C CB  . LYS A 220 ? 1.3644 1.4932 1.1258 -0.5040 -0.4250 0.1402  219 LYS A CB  
1731 C CG  . LYS A 220 ? 1.5319 1.6465 1.2617 -0.5240 -0.4488 0.1319  219 LYS A CG  
1732 C CD  . LYS A 220 ? 1.6897 1.7786 1.3565 -0.5296 -0.4766 0.1445  219 LYS A CD  
1733 C CE  . LYS A 220 ? 1.6332 1.7085 1.2646 -0.5518 -0.5016 0.1345  219 LYS A CE  
1734 N NZ  . LYS A 220 ? 1.5978 1.6381 1.1440 -0.5619 -0.5182 0.1435  219 LYS A NZ  
1735 N N   . SER A 221 ? 1.2881 1.3894 1.0184 -0.4999 -0.3425 0.1201  220 SER A N   
1736 C CA  . SER A 221 ? 1.3119 1.3888 1.0079 -0.4913 -0.3117 0.1200  220 SER A CA  
1737 C C   . SER A 221 ? 1.3362 1.3885 0.9826 -0.4828 -0.3119 0.1284  220 SER A C   
1738 O O   . SER A 221 ? 1.3569 1.3882 0.9586 -0.4928 -0.3279 0.1279  220 SER A O   
1739 C CB  . SER A 221 ? 1.3227 1.3736 0.9903 -0.5041 -0.2986 0.1077  220 SER A CB  
1740 O OG  . SER A 221 ? 1.2551 1.3226 0.9629 -0.5091 -0.2860 0.1023  220 SER A OG  
1741 N N   . GLN A 222 ? 1.2529 1.3074 0.9059 -0.4661 -0.2930 0.1351  221 GLN A N   
1742 C CA  . GLN A 222 ? 1.2542 1.2871 0.8662 -0.4577 -0.2896 0.1426  221 GLN A CA  
1743 C C   . GLN A 222 ? 1.2471 1.2572 0.8374 -0.4486 -0.2577 0.1372  221 GLN A C   
1744 O O   . GLN A 222 ? 1.1981 1.2168 0.8153 -0.4440 -0.2414 0.1334  221 GLN A O   
1745 C CB  . GLN A 222 ? 1.1483 1.2064 0.7953 -0.4451 -0.3014 0.1567  221 GLN A CB  
1746 C CG  . GLN A 222 ? 1.1737 1.2603 0.8634 -0.4518 -0.3343 0.1616  221 GLN A CG  
1747 C CD  . GLN A 222 ? 1.2018 1.3154 0.9408 -0.4380 -0.3444 0.1745  221 GLN A CD  
1748 O OE1 . GLN A 222 ? 1.2437 1.3442 0.9605 -0.4278 -0.3392 0.1849  221 GLN A OE1 
1749 N NE2 . GLN A 222 ? 1.0181 1.1692 0.8282 -0.4384 -0.3572 0.1724  221 GLN A NE2 
1750 N N   . PHE A 223 ? 1.3136 1.2932 0.8548 -0.4479 -0.2495 0.1363  222 PHE A N   
1751 C CA  . PHE A 223 ? 1.2450 1.2005 0.7692 -0.4401 -0.2205 0.1283  222 PHE A CA  
1752 C C   . PHE A 223 ? 1.3144 1.2635 0.8257 -0.4276 -0.2109 0.1352  222 PHE A C   
1753 O O   . PHE A 223 ? 1.3621 1.2858 0.8254 -0.4349 -0.2111 0.1340  222 PHE A O   
1754 C CB  . PHE A 223 ? 1.3039 1.2235 0.7825 -0.4554 -0.2136 0.1133  222 PHE A CB  
1755 C CG  . PHE A 223 ? 1.3527 1.2496 0.8311 -0.4488 -0.1860 0.1024  222 PHE A CG  
1756 C CD1 . PHE A 223 ? 1.4261 1.3283 0.9277 -0.4300 -0.1691 0.1066  222 PHE A CD1 
1757 C CD2 . PHE A 223 ? 1.2914 1.1614 0.7505 -0.4615 -0.1780 0.0869  222 PHE A CD2 
1758 C CE1 . PHE A 223 ? 1.3409 1.2220 0.8481 -0.4235 -0.1476 0.0970  222 PHE A CE1 
1759 C CE2 . PHE A 223 ? 1.2793 1.1273 0.7464 -0.4549 -0.1551 0.0770  222 PHE A CE2 
1760 C CZ  . PHE A 223 ? 1.3041 1.1576 0.7958 -0.4356 -0.1412 0.0827  222 PHE A CZ  
1761 N N   . LEU A 224 ? 1.2678 1.2397 0.8208 -0.4104 -0.2015 0.1416  223 LEU A N   
1762 C CA  . LEU A 224 ? 1.2349 1.2075 0.7879 -0.3972 -0.1933 0.1490  223 LEU A CA  
1763 C C   . LEU A 224 ? 1.1883 1.1318 0.7176 -0.3909 -0.1656 0.1386  223 LEU A C   
1764 O O   . LEU A 224 ? 1.2450 1.1881 0.7953 -0.3832 -0.1500 0.1313  223 LEU A O   
1765 C CB  . LEU A 224 ? 1.1550 1.1663 0.7674 -0.3826 -0.1933 0.1567  223 LEU A CB  
1766 C CG  . LEU A 224 ? 1.0898 1.1072 0.7147 -0.3675 -0.1841 0.1639  223 LEU A CG  
1767 C CD1 . LEU A 224 ? 1.0790 1.0798 0.6679 -0.3740 -0.1987 0.1740  223 LEU A CD1 
1768 C CD2 . LEU A 224 ? 0.9949 1.0544 0.6829 -0.3569 -0.1865 0.1689  223 LEU A CD2 
1769 N N   . ILE A 225 ? 1.1662 1.0843 0.6527 -0.3951 -0.1600 0.1380  224 ILE A N   
1770 C CA  . ILE A 225 ? 1.1623 1.0521 0.6296 -0.3909 -0.1313 0.1248  224 ILE A CA  
1771 C C   . ILE A 225 ? 1.1110 1.0048 0.5899 -0.3762 -0.1176 0.1304  224 ILE A C   
1772 O O   . ILE A 225 ? 1.1387 1.0308 0.5976 -0.3793 -0.1262 0.1420  224 ILE A O   
1773 C CB  . ILE A 225 ? 1.1616 1.0131 0.5689 -0.4106 -0.1250 0.1117  224 ILE A CB  
1774 C CG1 . ILE A 225 ? 1.2759 1.1212 0.6836 -0.4216 -0.1296 0.1004  224 ILE A CG1 
1775 C CG2 . ILE A 225 ? 1.1031 0.9271 0.4963 -0.4067 -0.0931 0.0967  224 ILE A CG2 
1776 C CD1 . ILE A 225 ? 1.5215 1.3301 0.8764 -0.4419 -0.1198 0.0824  224 ILE A CD1 
1777 N N   . LEU A 226 ? 1.1838 1.0817 0.6963 -0.3606 -0.0972 0.1226  225 LEU A N   
1778 C CA  . LEU A 226 ? 1.1218 1.0321 0.6607 -0.3440 -0.0848 0.1270  225 LEU A CA  
1779 C C   . LEU A 226 ? 1.1760 1.0623 0.7128 -0.3371 -0.0552 0.1106  225 LEU A C   
1780 O O   . LEU A 226 ? 1.1194 0.9929 0.6652 -0.3361 -0.0446 0.0966  225 LEU A O   
1781 C CB  . LEU A 226 ? 0.9946 0.9448 0.5916 -0.3296 -0.0918 0.1341  225 LEU A CB  
1782 C CG  . LEU A 226 ? 0.9839 0.9637 0.5984 -0.3340 -0.1173 0.1486  225 LEU A CG  
1783 C CD1 . LEU A 226 ? 0.8527 0.8709 0.5226 -0.3244 -0.1198 0.1507  225 LEU A CD1 
1784 C CD2 . LEU A 226 ? 1.0170 0.9978 0.6234 -0.3329 -0.1240 0.1608  225 LEU A CD2 
1785 N N   . ASP A 227 ? 1.1877 1.0675 0.7166 -0.3326 -0.0422 0.1124  226 ASP A N   
1786 C CA  . ASP A 227 ? 1.1016 0.9676 0.6453 -0.3221 -0.0131 0.0970  226 ASP A CA  
1787 C C   . ASP A 227 ? 1.0841 0.9817 0.6904 -0.3006 -0.0110 0.0981  226 ASP A C   
1788 O O   . ASP A 227 ? 0.9861 0.9169 0.6198 -0.2940 -0.0275 0.1125  226 ASP A O   
1789 C CB  . ASP A 227 ? 1.0132 0.8620 0.5271 -0.3264 0.0007  0.0994  226 ASP A CB  
1790 C CG  . ASP A 227 ? 1.1791 0.9863 0.6283 -0.3488 0.0126  0.0880  226 ASP A CG  
1791 O OD1 . ASP A 227 ? 1.2239 1.0102 0.6720 -0.3526 0.0320  0.0657  226 ASP A OD1 
1792 O OD2 . ASP A 227 ? 1.2577 1.0525 0.6583 -0.3636 0.0023  0.1010  226 ASP A OD2 
1793 N N   . ARG A 228 ? 0.9602 0.8479 0.5911 -0.2907 0.0088  0.0817  227 ARG A N   
1794 C CA  . ARG A 228 ? 0.8852 0.8007 0.5711 -0.2718 0.0094  0.0819  227 ARG A CA  
1795 C C   . ARG A 228 ? 0.9627 0.9033 0.6673 -0.2626 0.0103  0.0924  227 ARG A C   
1796 O O   . ARG A 228 ? 0.8870 0.8612 0.6307 -0.2520 0.0018  0.0989  227 ARG A O   
1797 C CB  . ARG A 228 ? 0.9417 0.8401 0.6537 -0.2621 0.0301  0.0621  227 ARG A CB  
1798 C CG  . ARG A 228 ? 0.7937 0.7146 0.5541 -0.2478 0.0210  0.0630  227 ARG A CG  
1799 C CD  . ARG A 228 ? 0.7373 0.6972 0.5108 -0.2450 0.0028  0.0809  227 ARG A CD  
1800 N NE  . ARG A 228 ? 0.7861 0.7591 0.5715 -0.2467 -0.0152 0.0877  227 ARG A NE  
1801 C CZ  . ARG A 228 ? 0.8759 0.8792 0.6672 -0.2503 -0.0307 0.1008  227 ARG A CZ  
1802 N NH1 . ARG A 228 ? 0.7002 0.7250 0.4934 -0.2508 -0.0324 0.1082  227 ARG A NH1 
1803 N NH2 . ARG A 228 ? 0.9721 0.9829 0.7695 -0.2546 -0.0441 0.1060  227 ARG A NH2 
1804 N N   . ALA A 229 ? 1.0932 1.0158 0.7682 -0.2686 0.0211  0.0937  228 ALA A N   
1805 C CA  . ALA A 229 ? 0.9129 0.8527 0.6044 -0.2609 0.0235  0.1042  228 ALA A CA  
1806 C C   . ALA A 229 ? 0.9036 0.8764 0.6116 -0.2607 -0.0020 0.1239  228 ALA A C   
1807 O O   . ALA A 229 ? 0.9453 0.9368 0.6790 -0.2530 -0.0017 0.1325  228 ALA A O   
1808 C CB  . ALA A 229 ? 0.9246 0.8316 0.5704 -0.2720 0.0377  0.1045  228 ALA A CB  
1809 N N   . VAL A 230 ? 0.8255 0.8054 0.5235 -0.2698 -0.0230 0.1296  229 VAL A N   
1810 C CA  . VAL A 230 ? 0.8320 0.8445 0.5538 -0.2705 -0.0457 0.1444  229 VAL A CA  
1811 C C   . VAL A 230 ? 0.9038 0.9551 0.6860 -0.2551 -0.0409 0.1425  229 VAL A C   
1812 O O   . VAL A 230 ? 0.9790 1.0577 0.7927 -0.2522 -0.0504 0.1520  229 VAL A O   
1813 C CB  . VAL A 230 ? 0.9164 0.9320 0.6258 -0.2822 -0.0646 0.1460  229 VAL A CB  
1814 C CG1 . VAL A 230 ? 0.7721 0.7935 0.5012 -0.2771 -0.0576 0.1346  229 VAL A CG1 
1815 C CG2 . VAL A 230 ? 0.9089 0.9564 0.6448 -0.2854 -0.0873 0.1591  229 VAL A CG2 
1816 N N   . ASP A 231 ? 0.8220 0.8747 0.6216 -0.2462 -0.0267 0.1293  230 ASP A N   
1817 C CA  . ASP A 231 ? 0.7799 0.8674 0.6302 -0.2341 -0.0222 0.1245  230 ASP A CA  
1818 C C   . ASP A 231 ? 0.8215 0.8973 0.6808 -0.2245 -0.0067 0.1099  230 ASP A C   
1819 O O   . ASP A 231 ? 0.9580 1.0225 0.8073 -0.2278 -0.0114 0.1057  230 ASP A O   
1820 C CB  . ASP A 231 ? 0.6877 0.8044 0.5547 -0.2410 -0.0392 0.1293  230 ASP A CB  
1821 C CG  . ASP A 231 ? 0.7914 0.9417 0.7012 -0.2331 -0.0338 0.1223  230 ASP A CG  
1822 O OD1 . ASP A 231 ? 0.7504 0.9016 0.6786 -0.2209 -0.0194 0.1136  230 ASP A OD1 
1823 O OD2 . ASP A 231 ? 0.8071 0.9828 0.7312 -0.2410 -0.0438 0.1245  230 ASP A OD2 
1824 N N   . LEU A 232 ? 0.7057 0.7836 0.5880 -0.2125 0.0110  0.1023  231 LEU A N   
1825 C CA  . LEU A 232 ? 0.7253 0.7918 0.6233 -0.2024 0.0257  0.0869  231 LEU A CA  
1826 C C   . LEU A 232 ? 0.7530 0.8540 0.6962 -0.1920 0.0235  0.0822  231 LEU A C   
1827 O O   . LEU A 232 ? 0.7378 0.8347 0.7019 -0.1824 0.0312  0.0701  231 LEU A O   
1828 C CB  . LEU A 232 ? 0.7108 0.7565 0.6068 -0.1972 0.0487  0.0786  231 LEU A CB  
1829 C CG  . LEU A 232 ? 0.7747 0.7761 0.6325 -0.2051 0.0615  0.0693  231 LEU A CG  
1830 C CD1 . LEU A 232 ? 0.7802 0.7652 0.5997 -0.2193 0.0454  0.0749  231 LEU A CD1 
1831 C CD2 . LEU A 232 ? 0.8284 0.8089 0.6602 -0.2106 0.0780  0.0710  231 LEU A CD2 
1832 N N   . LYS A 233 ? 0.6925 0.8275 0.6516 -0.1954 0.0125  0.0904  232 LYS A N   
1833 C CA  . LYS A 233 ? 0.6639 0.8345 0.6610 -0.1897 0.0114  0.0850  232 LYS A CA  
1834 C C   . LYS A 233 ? 0.7056 0.8820 0.6924 -0.1982 -0.0046 0.0880  232 LYS A C   
1835 O O   . LYS A 233 ? 0.7823 0.9667 0.7848 -0.1934 -0.0063 0.0818  232 LYS A O   
1836 C CB  . LYS A 233 ? 0.8498 1.0557 0.8763 -0.1903 0.0127  0.0884  232 LYS A CB  
1837 C CG  . LYS A 233 ? 0.8583 1.0630 0.9054 -0.1803 0.0289  0.0857  232 LYS A CG  
1838 C CD  . LYS A 233 ? 0.8252 1.0568 0.8986 -0.1829 0.0258  0.0932  232 LYS A CD  
1839 C CE  . LYS A 233 ? 0.9366 1.1606 1.0269 -0.1740 0.0406  0.0939  232 LYS A CE  
1840 N NZ  . LYS A 233 ? 0.9399 1.1820 1.0547 -0.1770 0.0334  0.1051  232 LYS A NZ  
1841 N N   . SER A 234 ? 0.7195 0.8906 0.6794 -0.2118 -0.0173 0.0982  233 SER A N   
1842 C CA  . SER A 234 ? 0.6262 0.7998 0.5719 -0.2230 -0.0317 0.1030  233 SER A CA  
1843 C C   . SER A 234 ? 0.6919 0.8401 0.6286 -0.2192 -0.0363 0.1004  233 SER A C   
1844 O O   . SER A 234 ? 0.7075 0.8666 0.6475 -0.2232 -0.0457 0.1025  233 SER A O   
1845 C CB  . SER A 234 ? 0.5424 0.7068 0.4602 -0.2377 -0.0425 0.1126  233 SER A CB  
1846 O OG  . SER A 234 ? 0.6824 0.8783 0.6192 -0.2435 -0.0439 0.1152  233 SER A OG  
1847 N N   . PRO A 235 ? 0.7010 0.8143 0.6269 -0.2129 -0.0300 0.0956  234 PRO A N   
1848 C CA  . PRO A 235 ? 0.6268 0.7142 0.5567 -0.2068 -0.0329 0.0904  234 PRO A CA  
1849 C C   . PRO A 235 ? 0.7077 0.8111 0.6731 -0.1943 -0.0319 0.0828  234 PRO A C   
1850 O O   . PRO A 235 ? 0.9260 1.0133 0.8995 -0.1907 -0.0419 0.0819  234 PRO A O   
1851 C CB  . PRO A 235 ? 0.5785 0.6333 0.4999 -0.2024 -0.0176 0.0807  234 PRO A CB  
1852 C CG  . PRO A 235 ? 0.7200 0.7740 0.6121 -0.2130 -0.0163 0.0876  234 PRO A CG  
1853 C CD  . PRO A 235 ? 0.7381 0.8321 0.6442 -0.2147 -0.0210 0.0953  234 PRO A CD  
1854 N N   . LEU A 236 ? 0.5661 0.7001 0.5554 -0.1880 -0.0217 0.0776  235 LEU A N   
1855 C CA  . LEU A 236 ? 0.6194 0.7680 0.6453 -0.1752 -0.0186 0.0670  235 LEU A CA  
1856 C C   . LEU A 236 ? 0.5692 0.7544 0.6053 -0.1805 -0.0291 0.0698  235 LEU A C   
1857 O O   . LEU A 236 ? 0.5537 0.7451 0.6093 -0.1743 -0.0367 0.0649  235 LEU A O   
1858 C CB  . LEU A 236 ? 0.4681 0.6207 0.5197 -0.1628 0.0042  0.0542  235 LEU A CB  
1859 C CG  . LEU A 236 ? 0.5338 0.6478 0.5778 -0.1581 0.0185  0.0463  235 LEU A CG  
1860 C CD1 . LEU A 236 ? 0.5300 0.6470 0.5835 -0.1528 0.0416  0.0396  235 LEU A CD1 
1861 C CD2 . LEU A 236 ? 0.3536 0.4470 0.4227 -0.1482 0.0164  0.0344  235 LEU A CD2 
1862 N N   . VAL A 237 ? 0.5111 0.7200 0.5349 -0.1932 -0.0298 0.0765  236 VAL A N   
1863 C CA  . VAL A 237 ? 0.6475 0.8952 0.6830 -0.2011 -0.0327 0.0745  236 VAL A CA  
1864 C C   . VAL A 237 ? 0.7325 0.9776 0.7453 -0.2134 -0.0525 0.0828  236 VAL A C   
1865 O O   . VAL A 237 ? 0.7503 0.9749 0.7309 -0.2252 -0.0641 0.0952  236 VAL A O   
1866 C CB  . VAL A 237 ? 0.6351 0.9096 0.6711 -0.2131 -0.0258 0.0766  236 VAL A CB  
1867 C CG1 . VAL A 237 ? 0.6260 0.9057 0.6867 -0.2023 -0.0095 0.0712  236 VAL A CG1 
1868 C CG2 . VAL A 237 ? 0.5645 0.8217 0.5650 -0.2279 -0.0365 0.0894  236 VAL A CG2 
1869 N N   . HIS A 238 ? 0.6153 0.8805 0.6436 -0.2119 -0.0571 0.0764  237 HIS A N   
1870 C CA  . HIS A 238 ? 0.5998 0.8704 0.6019 -0.2288 -0.0752 0.0852  237 HIS A CA  
1871 C C   . HIS A 238 ? 0.6441 0.9323 0.6222 -0.2511 -0.0713 0.0903  237 HIS A C   
1872 O O   . HIS A 238 ? 0.8919 1.2100 0.8895 -0.2542 -0.0545 0.0806  237 HIS A O   
1873 C CB  . HIS A 238 ? 0.4887 0.7872 0.5103 -0.2274 -0.0776 0.0747  237 HIS A CB  
1874 C CG  . HIS A 238 ? 0.4838 0.7622 0.5223 -0.2115 -0.0924 0.0736  237 HIS A CG  
1875 N ND1 . HIS A 238 ? 0.5812 0.8606 0.6632 -0.1897 -0.0802 0.0585  237 HIS A ND1 
1876 C CD2 . HIS A 238 ? 0.6039 0.8608 0.6260 -0.2147 -0.1193 0.0854  237 HIS A CD2 
1877 C CE1 . HIS A 238 ? 0.6576 0.9188 0.7537 -0.1796 -0.0981 0.0588  237 HIS A CE1 
1878 N NE2 . HIS A 238 ? 0.6433 0.8904 0.7045 -0.1939 -0.1238 0.0761  237 HIS A NE2 
1879 N N   . GLU A 239 ? 0.7371 0.6478 0.7453 -0.0929 0.0488  -0.0542 238 GLU A N   
1880 C CA  . GLU A 239 ? 0.6881 0.6128 0.7091 -0.0943 0.0464  -0.0466 238 GLU A CA  
1881 C C   . GLU A 239 ? 0.6973 0.6209 0.7149 -0.0949 0.0515  -0.0563 238 GLU A C   
1882 O O   . GLU A 239 ? 0.8098 0.7233 0.8078 -0.0974 0.0512  -0.0647 238 GLU A O   
1883 C CB  . GLU A 239 ? 0.4269 0.3578 0.4341 -0.1046 0.0353  -0.0376 238 GLU A CB  
1884 C CG  . GLU A 239 ? 0.8813 0.8339 0.9045 -0.1088 0.0300  -0.0258 238 GLU A CG  
1885 C CD  . GLU A 239 ? 0.9749 0.9451 1.0219 -0.1061 0.0249  -0.0075 238 GLU A CD  
1886 O OE1 . GLU A 239 ? 0.6947 0.6578 0.7320 -0.1080 0.0211  -0.0034 238 GLU A OE1 
1887 O OE2 . GLU A 239 ? 0.9407 0.9330 1.0173 -0.1020 0.0253  0.0040  238 GLU A OE2 
1888 N N   . LEU A 240 ? 0.5828 0.5170 0.6208 -0.0919 0.0573  -0.0540 239 LEU A N   
1889 C CA  . LEU A 240 ? 0.7307 0.6631 0.7655 -0.0935 0.0647  -0.0637 239 LEU A CA  
1890 C C   . LEU A 240 ? 0.8219 0.7670 0.8568 -0.0999 0.0613  -0.0597 239 LEU A C   
1891 O O   . LEU A 240 ? 0.8698 0.8171 0.9073 -0.1013 0.0690  -0.0654 239 LEU A O   
1892 C CB  . LEU A 240 ? 0.6840 0.6136 0.7379 -0.0870 0.0795  -0.0684 239 LEU A CB  
1893 C CG  . LEU A 240 ? 0.7431 0.6560 0.7888 -0.0859 0.0856  -0.0777 239 LEU A CG  
1894 C CD1 . LEU A 240 ? 0.7576 0.6681 0.8145 -0.0802 0.0835  -0.0690 239 LEU A CD1 
1895 C CD2 . LEU A 240 ? 0.7497 0.6535 0.8011 -0.0860 0.1029  -0.0881 239 LEU A CD2 
1896 N N   . THR A 241 ? 0.6800 0.6334 0.7097 -0.1064 0.0504  -0.0503 240 THR A N   
1897 C CA  . THR A 241 ? 0.6186 0.5813 0.6417 -0.1166 0.0465  -0.0478 240 THR A CA  
1898 C C   . THR A 241 ? 0.6880 0.6289 0.6763 -0.1234 0.0437  -0.0568 240 THR A C   
1899 O O   . THR A 241 ? 0.7207 0.6458 0.6944 -0.1206 0.0424  -0.0604 240 THR A O   
1900 C CB  . THR A 241 ? 0.6848 0.6704 0.7199 -0.1241 0.0364  -0.0320 240 THR A CB  
1901 O OG1 . THR A 241 ? 0.8110 0.7883 0.8294 -0.1285 0.0277  -0.0282 240 THR A OG1 
1902 C CG2 . THR A 241 ? 0.5803 0.5897 0.6577 -0.1132 0.0415  -0.0200 240 THR A CG2 
1903 N N   . TYR A 242 ? 0.7448 0.6849 0.7219 -0.1315 0.0443  -0.0592 241 TYR A N   
1904 C CA  . TYR A 242 ? 0.6274 0.5452 0.5764 -0.1345 0.0456  -0.0669 241 TYR A CA  
1905 C C   . TYR A 242 ? 0.6989 0.5959 0.6231 -0.1375 0.0418  -0.0674 241 TYR A C   
1906 O O   . TYR A 242 ? 0.5921 0.4741 0.5078 -0.1296 0.0444  -0.0715 241 TYR A O   
1907 C CB  . TYR A 242 ? 0.6986 0.6194 0.6402 -0.1448 0.0468  -0.0671 241 TYR A CB  
1908 C CG  . TYR A 242 ? 0.7282 0.6267 0.6439 -0.1470 0.0492  -0.0723 241 TYR A CG  
1909 C CD1 . TYR A 242 ? 0.6147 0.5040 0.5267 -0.1379 0.0520  -0.0766 241 TYR A CD1 
1910 C CD2 . TYR A 242 ? 0.8136 0.7019 0.7091 -0.1594 0.0483  -0.0713 241 TYR A CD2 
1911 C CE1 . TYR A 242 ? 0.7136 0.5864 0.6052 -0.1392 0.0528  -0.0770 241 TYR A CE1 
1912 C CE2 . TYR A 242 ? 0.8916 0.7581 0.7650 -0.1603 0.0510  -0.0734 241 TYR A CE2 
1913 C CZ  . TYR A 242 ? 0.8379 0.6978 0.7106 -0.1492 0.0527  -0.0750 241 TYR A CZ  
1914 O OH  . TYR A 242 ? 0.7962 0.6372 0.6490 -0.1497 0.0541  -0.0729 241 TYR A OH  
1915 N N   . GLN A 243 ? 0.7001 0.5966 0.6122 -0.1503 0.0368  -0.0629 242 GLN A N   
1916 C CA  . GLN A 243 ? 0.7615 0.6340 0.6459 -0.1561 0.0366  -0.0650 242 GLN A CA  
1917 C C   . GLN A 243 ? 0.8737 0.7432 0.7643 -0.1453 0.0376  -0.0656 242 GLN A C   
1918 O O   . GLN A 243 ? 0.7312 0.5805 0.6099 -0.1381 0.0433  -0.0705 242 GLN A O   
1919 C CB  . GLN A 243 ? 0.6693 0.5461 0.5392 -0.1762 0.0302  -0.0599 242 GLN A CB  
1920 C CG  . GLN A 243 ? 0.7538 0.5960 0.5851 -0.1867 0.0348  -0.0657 242 GLN A CG  
1921 C CD  . GLN A 243 ? 0.9492 0.7939 0.7590 -0.2115 0.0282  -0.0618 242 GLN A CD  
1922 O OE1 . GLN A 243 ? 0.9917 0.8674 0.8189 -0.2173 0.0177  -0.0517 242 GLN A OE1 
1923 N NE2 . GLN A 243 ? 0.9929 0.8038 0.7636 -0.2272 0.0350  -0.0690 242 GLN A NE2 
1924 N N   . ALA A 244 ? 0.9233 0.8143 0.8352 -0.1437 0.0326  -0.0590 243 ALA A N   
1925 C CA  . ALA A 244 ? 0.7566 0.6457 0.6734 -0.1364 0.0330  -0.0583 243 ALA A CA  
1926 C C   . ALA A 244 ? 0.7240 0.6060 0.6487 -0.1217 0.0397  -0.0651 243 ALA A C   
1927 O O   . ALA A 244 ? 0.6520 0.5224 0.5689 -0.1174 0.0428  -0.0678 243 ALA A O   
1928 C CB  . ALA A 244 ? 0.6142 0.5280 0.5556 -0.1363 0.0266  -0.0471 243 ALA A CB  
1929 N N   . ALA A 245 ? 0.5807 0.4711 0.5196 -0.1162 0.0422  -0.0676 244 ALA A N   
1930 C CA  . ALA A 245 ? 0.6029 0.4904 0.5466 -0.1072 0.0468  -0.0731 244 ALA A CA  
1931 C C   . ALA A 245 ? 0.7233 0.5957 0.6492 -0.1054 0.0487  -0.0757 244 ALA A C   
1932 O O   . ALA A 245 ? 0.8642 0.7355 0.7924 -0.0986 0.0507  -0.0769 244 ALA A O   
1933 C CB  . ALA A 245 ? 0.5316 0.4301 0.4904 -0.1055 0.0504  -0.0761 244 ALA A CB  
1934 N N   . ALA A 246 ? 0.7418 0.6037 0.6517 -0.1116 0.0486  -0.0751 245 ALA A N   
1935 C CA  . ALA A 246 ? 0.7063 0.5506 0.6009 -0.1081 0.0523  -0.0751 245 ALA A CA  
1936 C C   . ALA A 246 ? 0.8362 0.6654 0.7225 -0.1038 0.0570  -0.0751 245 ALA A C   
1937 O O   . ALA A 246 ? 0.7324 0.5583 0.6225 -0.0936 0.0610  -0.0734 245 ALA A O   
1938 C CB  . ALA A 246 ? 0.6269 0.4579 0.5036 -0.1173 0.0530  -0.0746 245 ALA A CB  
1939 N N   . TYR A 247 ? 0.6411 0.4630 0.5163 -0.1126 0.0570  -0.0761 246 TYR A N   
1940 C CA  . TYR A 247 ? 0.7675 0.5696 0.6279 -0.1119 0.0647  -0.0780 246 TYR A CA  
1941 C C   . TYR A 247 ? 0.8085 0.6218 0.6854 -0.1020 0.0662  -0.0776 246 TYR A C   
1942 O O   . TYR A 247 ? 0.7669 0.5670 0.6388 -0.0958 0.0754  -0.0787 246 TYR A O   
1943 C CB  . TYR A 247 ? 0.6669 0.4588 0.5053 -0.1291 0.0634  -0.0793 246 TYR A CB  
1944 C CG  . TYR A 247 ? 0.7726 0.5394 0.5841 -0.1400 0.0684  -0.0820 246 TYR A CG  
1945 C CD1 . TYR A 247 ? 0.7787 0.5546 0.5914 -0.1476 0.0620  -0.0799 246 TYR A CD1 
1946 C CD2 . TYR A 247 ? 0.7721 0.5036 0.5561 -0.1435 0.0818  -0.0871 246 TYR A CD2 
1947 C CE1 . TYR A 247 ? 0.8306 0.5820 0.6169 -0.1596 0.0669  -0.0824 246 TYR A CE1 
1948 C CE2 . TYR A 247 ? 0.7385 0.4409 0.4946 -0.1549 0.0887  -0.0904 246 TYR A CE2 
1949 C CZ  . TYR A 247 ? 0.8090 0.5216 0.5657 -0.1637 0.0803  -0.0878 246 TYR A CZ  
1950 O OH  . TYR A 247 ? 0.8371 0.5192 0.5639 -0.1775 0.0874  -0.0912 246 TYR A OH  
1951 N N   . ASP A 248 ? 0.7359 0.5721 0.6327 -0.1009 0.0589  -0.0761 247 ASP A N   
1952 C CA  . ASP A 248 ? 0.6862 0.5342 0.5988 -0.0942 0.0595  -0.0759 247 ASP A CA  
1953 C C   . ASP A 248 ? 0.7137 0.5698 0.6383 -0.0845 0.0614  -0.0754 247 ASP A C   
1954 O O   . ASP A 248 ? 0.8452 0.6987 0.7720 -0.0775 0.0673  -0.0740 247 ASP A O   
1955 C CB  . ASP A 248 ? 0.6662 0.5308 0.5944 -0.0971 0.0532  -0.0742 247 ASP A CB  
1956 C CG  . ASP A 248 ? 0.7652 0.6358 0.7037 -0.0946 0.0544  -0.0736 247 ASP A CG  
1957 O OD1 . ASP A 248 ? 0.7969 0.6629 0.7321 -0.0910 0.0594  -0.0750 247 ASP A OD1 
1958 O OD2 . ASP A 248 ? 0.6802 0.5596 0.6317 -0.0957 0.0515  -0.0709 247 ASP A OD2 
1959 N N   . LEU A 249 ? 0.6227 0.4902 0.5550 -0.0853 0.0568  -0.0755 248 LEU A N   
1960 C CA  . LEU A 249 ? 0.5607 0.4414 0.5028 -0.0810 0.0555  -0.0738 248 LEU A CA  
1961 C C   . LEU A 249 ? 0.6772 0.5532 0.6152 -0.0743 0.0573  -0.0675 248 LEU A C   
1962 O O   . LEU A 249 ? 0.7496 0.6406 0.6984 -0.0697 0.0557  -0.0621 248 LEU A O   
1963 C CB  . LEU A 249 ? 0.6386 0.5299 0.5851 -0.0873 0.0519  -0.0773 248 LEU A CB  
1964 C CG  . LEU A 249 ? 0.6174 0.5121 0.5732 -0.0907 0.0531  -0.0814 248 LEU A CG  
1965 C CD1 . LEU A 249 ? 0.5945 0.4935 0.5547 -0.0959 0.0547  -0.0856 248 LEU A CD1 
1966 C CD2 . LEU A 249 ? 0.5407 0.4423 0.5051 -0.0897 0.0545  -0.0824 248 LEU A CD2 
1967 N N   . LEU A 250 ? 0.7360 0.5919 0.6589 -0.0746 0.0605  -0.0667 249 LEU A N   
1968 C CA  . LEU A 250 ? 0.6337 0.4804 0.5528 -0.0671 0.0638  -0.0590 249 LEU A CA  
1969 C C   . LEU A 250 ? 0.7365 0.5598 0.6486 -0.0594 0.0758  -0.0576 249 LEU A C   
1970 O O   . LEU A 250 ? 0.7900 0.6023 0.6941 -0.0634 0.0809  -0.0641 249 LEU A O   
1971 C CB  . LEU A 250 ? 0.6018 0.4381 0.5064 -0.0736 0.0612  -0.0586 249 LEU A CB  
1972 C CG  . LEU A 250 ? 0.7235 0.5769 0.6304 -0.0832 0.0535  -0.0620 249 LEU A CG  
1973 C CD1 . LEU A 250 ? 0.7679 0.6086 0.6591 -0.0894 0.0533  -0.0606 249 LEU A CD1 
1974 C CD2 . LEU A 250 ? 0.5382 0.4161 0.4579 -0.0825 0.0479  -0.0588 249 LEU A CD2 
1975 N N   . ASN A 251 ? 0.5758 0.3905 0.4903 -0.0486 0.0814  -0.0482 250 ASN A N   
1976 C CA  . ASN A 251 ? 0.8848 0.6730 0.7941 -0.0390 0.0975  -0.0466 250 ASN A CA  
1977 C C   . ASN A 251 ? 0.9868 0.7361 0.8669 -0.0460 0.1058  -0.0513 250 ASN A C   
1978 O O   . ASN A 251 ? 0.8957 0.6312 0.7711 -0.0414 0.1082  -0.0436 250 ASN A O   
1979 C CB  . ASN A 251 ? 1.1552 0.9547 1.0878 -0.0209 0.1020  -0.0312 250 ASN A CB  
1980 C CG  . ASN A 251 ? 1.4859 1.2775 1.4291 -0.0089 0.1184  -0.0302 250 ASN A CG  
1981 O OD1 . ASN A 251 ? 1.4098 1.1638 1.3375 -0.0046 0.1367  -0.0336 250 ASN A OD1 
1982 N ND2 . ASN A 251 ? 1.6769 1.5024 1.6448 -0.0051 0.1139  -0.0269 250 ASN A ND2 
1983 N N   . ILE A 252 ? 0.9433 0.6758 0.8024 -0.0594 0.1093  -0.0629 251 ILE A N   
1984 C CA  . ILE A 252 ? 0.9651 0.6624 0.7921 -0.0724 0.1160  -0.0691 251 ILE A CA  
1985 C C   . ILE A 252 ? 1.1067 0.7704 0.9126 -0.0755 0.1343  -0.0768 251 ILE A C   
1986 O O   . ILE A 252 ? 1.2636 0.9276 1.0556 -0.0898 0.1323  -0.0850 251 ILE A O   
1987 C CB  . ILE A 252 ? 0.8736 0.5849 0.6910 -0.0917 0.1016  -0.0747 251 ILE A CB  
1988 C CG1 . ILE A 252 ? 0.7971 0.5382 0.6338 -0.0889 0.0879  -0.0690 251 ILE A CG1 
1989 C CG2 . ILE A 252 ? 0.9269 0.6061 0.7107 -0.1088 0.1072  -0.0802 251 ILE A CG2 
1990 C CD1 . ILE A 252 ? 0.8652 0.6196 0.6972 -0.1047 0.0775  -0.0728 251 ILE A CD1 
1991 N N   . GLU A 253 ? 1.0914 0.7255 0.8950 -0.0619 0.1532  -0.0730 252 GLU A N   
1992 C CA  . GLU A 253 ? 1.2609 0.8561 1.0422 -0.0639 0.1762  -0.0816 252 GLU A CA  
1993 C C   . GLU A 253 ? 1.2340 0.7821 0.9722 -0.0825 0.1865  -0.0903 252 GLU A C   
1994 O O   . GLU A 253 ? 1.2827 0.8156 1.0170 -0.0795 0.1874  -0.0846 252 GLU A O   
1995 C CB  . GLU A 253 ? 1.5121 1.0999 1.3183 -0.0372 0.1950  -0.0719 252 GLU A CB  
1996 C CG  . GLU A 253 ? 1.7742 1.3490 1.5786 -0.0334 0.2153  -0.0791 252 GLU A CG  
1997 C CD  . GLU A 253 ? 1.8450 1.4667 1.6761 -0.0314 0.2017  -0.0777 252 GLU A CD  
1998 O OE1 . GLU A 253 ? 1.8582 1.5137 1.6961 -0.0411 0.1772  -0.0771 252 GLU A OE1 
1999 O OE2 . GLU A 253 ? 1.7986 1.4210 1.6433 -0.0203 0.2177  -0.0774 252 GLU A OE2 
2000 N N   . ASN A 254 ? 1.1813 0.7076 0.8850 -0.1045 0.1931  -0.1036 253 ASN A N   
2001 C CA  . ASN A 254 ? 1.1748 0.6573 0.8316 -0.1291 0.2022  -0.1137 253 ASN A CA  
2002 C C   . ASN A 254 ? 1.0835 0.5772 0.7374 -0.1398 0.1849  -0.1093 253 ASN A C   
2003 O O   . ASN A 254 ? 1.1652 0.6196 0.7910 -0.1495 0.1960  -0.1123 253 ASN A O   
2004 C CB  . ASN A 254 ? 1.2993 0.7211 0.9344 -0.1212 0.2355  -0.1181 253 ASN A CB  
2005 C CG  . ASN A 254 ? 1.5065 0.9162 1.1470 -0.1089 0.2570  -0.1225 253 ASN A CG  
2006 O OD1 . ASN A 254 ? 1.5270 0.9332 1.1434 -0.1282 0.2593  -0.1340 253 ASN A OD1 
2007 N ND2 . ASN A 254 ? 1.4596 0.8656 1.1333 -0.0771 0.2728  -0.1118 253 ASN A ND2 
2008 N N   . ASP A 255 ? 1.1616 0.7069 0.8437 -0.1386 0.1599  -0.1026 254 ASP A N   
2009 C CA  . ASP A 255 ? 1.0281 0.5904 0.7098 -0.1504 0.1435  -0.0992 254 ASP A CA  
2010 C C   . ASP A 255 ? 1.1343 0.6905 0.8292 -0.1342 0.1454  -0.0897 254 ASP A C   
2011 O O   . ASP A 255 ? 1.1680 0.7323 0.8591 -0.1441 0.1354  -0.0871 254 ASP A O   
2012 C CB  . ASP A 255 ? 0.8858 0.4242 0.5250 -0.1827 0.1450  -0.1082 254 ASP A CB  
2013 C CG  . ASP A 255 ? 1.1166 0.6736 0.7459 -0.2017 0.1363  -0.1132 254 ASP A CG  
2014 O OD1 . ASP A 255 ? 0.9939 0.5993 0.6518 -0.2000 0.1164  -0.1069 254 ASP A OD1 
2015 O OD2 . ASP A 255 ? 1.2130 0.7342 0.8048 -0.2186 0.1506  -0.1229 254 ASP A OD2 
2016 N N   . ILE A 256 ? 1.1402 0.6854 0.8523 -0.1095 0.1578  -0.0826 255 ILE A N   
2017 C CA  . ILE A 256 ? 0.9970 0.5401 0.7245 -0.0924 0.1584  -0.0693 255 ILE A CA  
2018 C C   . ILE A 256 ? 0.9709 0.5663 0.7385 -0.0771 0.1402  -0.0581 255 ILE A C   
2019 O O   . ILE A 256 ? 1.0218 0.6412 0.8135 -0.0649 0.1388  -0.0561 255 ILE A O   
2020 C CB  . ILE A 256 ? 0.9998 0.5017 0.7264 -0.0729 0.1833  -0.0635 255 ILE A CB  
2021 C CG1 . ILE A 256 ? 1.1769 0.6176 0.8578 -0.0898 0.2059  -0.0767 255 ILE A CG1 
2022 C CG2 . ILE A 256 ? 0.9703 0.4748 0.7154 -0.0551 0.1811  -0.0453 255 ILE A CG2 
2023 C CD1 . ILE A 256 ? 1.1802 0.5729 0.8593 -0.0698 0.2363  -0.0727 255 ILE A CD1 
2024 N N   . TYR A 257 ? 0.9347 0.5467 0.7066 -0.0805 0.1273  -0.0516 256 TYR A N   
2025 C CA  . TYR A 257 ? 0.9097 0.5664 0.7123 -0.0704 0.1117  -0.0420 256 TYR A CA  
2026 C C   . TYR A 257 ? 0.9369 0.5867 0.7473 -0.0559 0.1139  -0.0248 256 TYR A C   
2027 O O   . TYR A 257 ? 1.0415 0.6574 0.8305 -0.0601 0.1217  -0.0220 256 TYR A O   
2028 C CB  . TYR A 257 ? 0.7681 0.4528 0.5695 -0.0874 0.0955  -0.0480 256 TYR A CB  
2029 C CG  . TYR A 257 ? 0.8455 0.5712 0.6713 -0.0819 0.0817  -0.0416 256 TYR A CG  
2030 C CD1 . TYR A 257 ? 0.8159 0.5703 0.6647 -0.0745 0.0768  -0.0422 256 TYR A CD1 
2031 C CD2 . TYR A 257 ? 0.8465 0.5804 0.6688 -0.0870 0.0747  -0.0356 256 TYR A CD2 
2032 C CE1 . TYR A 257 ? 0.6240 0.4121 0.4896 -0.0737 0.0656  -0.0381 256 TYR A CE1 
2033 C CE2 . TYR A 257 ? 0.8919 0.6600 0.7302 -0.0863 0.0636  -0.0315 256 TYR A CE2 
2034 C CZ  . TYR A 257 ? 0.8660 0.6603 0.7250 -0.0803 0.0593  -0.0332 256 TYR A CZ  
2035 O OH  . TYR A 257 ? 1.0021 0.8268 0.8716 -0.0836 0.0495  -0.0304 256 TYR A OH  
2036 N N   . SER A 258 ? 1.0415 0.7233 0.8817 -0.0401 0.1071  -0.0117 257 SER A N   
2037 C CA  . SER A 258 ? 1.1068 0.7919 0.9582 -0.0272 0.1049  0.0093  257 SER A CA  
2038 C C   . SER A 258 ? 1.1386 0.8674 1.0008 -0.0343 0.0843  0.0160  257 SER A C   
2039 O O   . SER A 258 ? 1.2602 1.0250 1.1382 -0.0372 0.0741  0.0111  257 SER A O   
2040 C CB  . SER A 258 ? 1.0815 0.7693 0.9606 -0.0025 0.1151  0.0250  257 SER A CB  
2041 O OG  . SER A 258 ? 1.2662 0.9092 1.1342 0.0049  0.1387  0.0185  257 SER A OG  
2042 N N   . TYR A 259 ? 1.1025 0.8251 0.9531 -0.0385 0.0795  0.0268  258 TYR A N   
2043 C CA  . TYR A 259 ? 1.2279 0.9882 1.0838 -0.0469 0.0618  0.0345  258 TYR A CA  
2044 C C   . TYR A 259 ? 1.5854 1.3426 1.4418 -0.0392 0.0586  0.0598  258 TYR A C   
2045 O O   . TYR A 259 ? 1.6867 1.4136 1.5456 -0.0230 0.0711  0.0727  258 TYR A O   
2046 C CB  . TYR A 259 ? 1.0063 0.7701 0.8420 -0.0693 0.0562  0.0170  258 TYR A CB  
2047 C CG  . TYR A 259 ? 1.0336 0.7620 0.8423 -0.0789 0.0632  0.0146  258 TYR A CG  
2048 C CD1 . TYR A 259 ? 1.1516 0.8422 0.9461 -0.0793 0.0770  0.0053  258 TYR A CD1 
2049 C CD2 . TYR A 259 ? 1.1638 0.8958 0.9576 -0.0908 0.0565  0.0209  258 TYR A CD2 
2050 C CE1 . TYR A 259 ? 1.2794 0.9371 1.0466 -0.0917 0.0836  0.0025  258 TYR A CE1 
2051 C CE2 . TYR A 259 ? 1.1238 0.8234 0.8920 -0.1015 0.0633  0.0186  258 TYR A CE2 
2052 C CZ  . TYR A 259 ? 1.1697 0.8325 0.9252 -0.1021 0.0766  0.0095  258 TYR A CZ  
2053 O OH  . TYR A 259 ? 1.2520 0.8819 0.9800 -0.1157 0.0837  0.0068  258 TYR A OH  
2054 N N   . SER A 260 ? 1.6993 1.4861 1.5522 -0.0511 0.0429  0.0674  259 SER A N   
2055 C CA  . SER A 260 ? 1.6929 1.4827 1.5453 -0.0464 0.0364  0.0944  259 SER A CA  
2056 C C   . SER A 260 ? 1.6542 1.4438 1.4777 -0.0688 0.0283  0.0912  259 SER A C   
2057 O O   . SER A 260 ? 1.6324 1.4476 1.4487 -0.0870 0.0198  0.0769  259 SER A O   
2058 C CB  . SER A 260 ? 1.6848 1.5220 1.5660 -0.0384 0.0226  0.1154  259 SER A CB  
2059 O OG  . SER A 260 ? 1.6131 1.4555 1.5237 -0.0188 0.0308  0.1170  259 SER A OG  
2060 N N   . THR A 261 ? 1.6870 1.4445 1.4931 -0.0678 0.0335  0.1039  260 THR A N   
2061 C CA  . THR A 261 ? 1.7138 1.4713 1.4922 -0.0886 0.0262  0.1054  260 THR A CA  
2062 C C   . THR A 261 ? 1.8408 1.5852 1.6151 -0.0802 0.0236  0.1370  260 THR A C   
2063 O O   . THR A 261 ? 1.8363 1.5816 1.6350 -0.0574 0.0249  0.1599  260 THR A O   
2064 C CB  . THR A 261 ? 1.6038 1.3287 1.3554 -0.1043 0.0372  0.0827  260 THR A CB  
2065 O OG1 . THR A 261 ? 1.5807 1.2593 1.3283 -0.0922 0.0536  0.0823  260 THR A OG1 
2066 C CG2 . THR A 261 ? 1.5327 1.2782 1.2878 -0.1165 0.0368  0.0550  260 THR A CG2 
2067 N N   . VAL A 262 ? 1.9886 1.7211 1.7334 -0.0982 0.0208  0.1392  261 VAL A N   
2068 C CA  . VAL A 262 ? 2.0786 1.7963 1.8149 -0.0931 0.0177  0.1704  261 VAL A CA  
2069 C C   . VAL A 262 ? 2.1633 1.8276 1.8692 -0.1006 0.0322  0.1646  261 VAL A C   
2070 O O   . VAL A 262 ? 2.0726 1.7258 1.7590 -0.1190 0.0385  0.1373  261 VAL A O   
2071 C CB  . VAL A 262 ? 2.0413 1.7991 1.7654 -0.1124 -0.0025 0.1849  261 VAL A CB  
2072 C CG1 . VAL A 262 ? 2.0053 1.8167 1.7555 -0.1098 -0.0176 0.1909  261 VAL A CG1 
2073 C CG2 . VAL A 262 ? 2.0052 1.7622 1.6963 -0.1425 -0.0016 0.1591  261 VAL A CG2 
2074 N N   . ASP A 263 ? 2.3409 1.9727 2.0446 -0.0864 0.0381  0.1917  262 ASP A N   
2075 C CA  . ASP A 263 ? 2.4452 2.0247 2.1158 -0.0963 0.0508  0.1908  262 ASP A CA  
2076 C C   . ASP A 263 ? 2.5009 2.0900 2.1510 -0.1103 0.0376  0.2147  262 ASP A C   
2077 O O   . ASP A 263 ? 2.4387 2.0761 2.0885 -0.1243 0.0192  0.2178  262 ASP A O   
2078 C CB  . ASP A 263 ? 2.4744 1.9969 2.1504 -0.0724 0.0724  0.2014  262 ASP A CB  
2079 C CG  . ASP A 263 ? 2.4480 1.9783 2.1560 -0.0423 0.0697  0.2401  262 ASP A CG  
2080 O OD1 . ASP A 263 ? 2.4933 2.0782 2.2196 -0.0418 0.0482  0.2596  262 ASP A OD1 
2081 O OD2 . ASP A 263 ? 2.3679 1.8501 2.0834 -0.0198 0.0903  0.2517  262 ASP A OD2 
2082 N N   . ALA A 264 ? 2.6209 2.1613 2.2505 -0.1085 0.0480  0.2309  263 ALA A N   
2083 C CA  . ALA A 264 ? 2.6410 2.1857 2.2500 -0.1202 0.0361  0.2582  263 ALA A CA  
2084 C C   . ALA A 264 ? 2.6339 2.2347 2.2682 -0.1114 0.0135  0.2878  263 ALA A C   
2085 O O   . ALA A 264 ? 2.6093 2.2486 2.2274 -0.1344 -0.0044 0.2915  263 ALA A O   
2086 C CB  . ALA A 264 ? 2.6547 2.1365 2.2494 -0.1087 0.0518  0.2806  263 ALA A CB  
2087 N N   . GLY A 265 ? 2.6112 2.2176 2.2848 -0.0798 0.0153  0.3084  264 GLY A N   
2088 C CA  . GLY A 265 ? 2.5335 2.1983 2.2373 -0.0705 -0.0064 0.3385  264 GLY A CA  
2089 C C   . GLY A 265 ? 2.4169 2.1127 2.1618 -0.0517 -0.0058 0.3288  264 GLY A C   
2090 O O   . GLY A 265 ? 2.2893 2.0232 2.0342 -0.0680 -0.0150 0.3035  264 GLY A O   
2091 N N   . GLY A 266 ? 2.4397 2.1167 2.2196 -0.0173 0.0071  0.3492  265 GLY A N   
2092 C CA  . GLY A 266 ? 2.4223 2.1258 2.2441 0.0035  0.0105  0.3440  265 GLY A CA  
2093 C C   . GLY A 266 ? 2.4202 2.1517 2.2355 -0.0163 0.0056  0.3033  265 GLY A C   
2094 O O   . GLY A 266 ? 2.3888 2.0867 2.1797 -0.0283 0.0193  0.2678  265 GLY A O   
2095 N N   . ARG A 267 ? 2.4747 2.2688 2.3120 -0.0208 -0.0141 0.3100  266 ARG A N   
2096 C CA  . ARG A 267 ? 2.4700 2.2916 2.3022 -0.0395 -0.0189 0.2743  266 ARG A CA  
2097 C C   . ARG A 267 ? 2.5256 2.3430 2.3896 -0.0177 -0.0045 0.2598  266 ARG A C   
2098 O O   . ARG A 267 ? 2.5009 2.2866 2.3852 0.0099  0.0129  0.2724  266 ARG A O   
2099 C CB  . ARG A 267 ? 2.4007 2.2871 2.2348 -0.0597 -0.0453 0.2852  266 ARG A CB  
2100 C CG  . ARG A 267 ? 2.3717 2.2671 2.1736 -0.0827 -0.0610 0.3041  266 ARG A CG  
2101 C CD  . ARG A 267 ? 2.3718 2.2730 2.1941 -0.0628 -0.0687 0.3541  266 ARG A CD  
2102 N NE  . ARG A 267 ? 2.3516 2.2536 2.1387 -0.0850 -0.0821 0.3730  266 ARG A NE  
2103 C CZ  . ARG A 267 ? 2.2985 2.2077 2.0957 -0.0738 -0.0924 0.4195  266 ARG A CZ  
2104 N NH1 . ARG A 267 ? 2.2725 2.1896 2.1182 -0.0384 -0.0895 0.4522  266 ARG A NH1 
2105 N NH2 . ARG A 267 ? 2.2834 2.1922 2.0433 -0.0977 -0.1047 0.4345  266 ARG A NH2 
2106 N N   . GLU A 268 ? 2.6057 2.4528 2.4724 -0.0307 -0.0099 0.2334  267 GLU A N   
2107 C CA  . GLU A 268 ? 2.6283 2.4735 2.5201 -0.0150 0.0027  0.2162  267 GLU A CA  
2108 C C   . GLU A 268 ? 2.6324 2.4204 2.5284 0.0082  0.0286  0.2138  267 GLU A C   
2109 O O   . GLU A 268 ? 2.6448 2.4329 2.5737 0.0335  0.0394  0.2252  267 GLU A O   
2110 C CB  . GLU A 268 ? 2.6338 2.5340 2.5667 -0.0034 -0.0094 0.2367  267 GLU A CB  
2111 C CG  . GLU A 268 ? 2.6303 2.5836 2.5565 -0.0302 -0.0310 0.2286  267 GLU A CG  
2112 C CD  . GLU A 268 ? 2.7008 2.6846 2.6131 -0.0475 -0.0525 0.2549  267 GLU A CD  
2113 O OE1 . GLU A 268 ? 2.7984 2.7734 2.7184 -0.0330 -0.0538 0.2876  267 GLU A OE1 
2114 O OE2 . GLU A 268 ? 2.6718 2.6866 2.5638 -0.0764 -0.0672 0.2434  267 GLU A OE2 
2115 N N   . GLN A 269 ? 2.5611 2.2998 2.4220 -0.0021 0.0400  0.1990  268 GLN A N   
2116 C CA  . GLN A 269 ? 2.4104 2.0889 2.2640 0.0115  0.0662  0.1890  268 GLN A CA  
2117 C C   . GLN A 269 ? 2.2902 1.9660 2.1425 0.0057  0.0745  0.1550  268 GLN A C   
2118 O O   . GLN A 269 ? 2.2935 1.9749 2.1235 -0.0176 0.0685  0.1298  268 GLN A O   
2119 C CB  . GLN A 269 ? 2.3391 1.9692 2.1524 -0.0033 0.0738  0.1837  268 GLN A CB  
2120 C CG  . GLN A 269 ? 2.3063 1.9326 2.1160 0.0009  0.0665  0.2181  268 GLN A CG  
2121 C CD  . GLN A 269 ? 2.2509 1.8503 2.0871 0.0342  0.0822  0.2486  268 GLN A CD  
2122 O OE1 . GLN A 269 ? 2.2032 1.7863 2.0603 0.0539  0.1003  0.2422  268 GLN A OE1 
2123 N NE2 . GLN A 269 ? 2.2457 1.8395 2.0818 0.0408  0.0768  0.2829  268 GLN A NE2 
2124 N N   . GLN A 270 ? 2.1575 1.8263 2.0351 0.0271  0.0888  0.1558  269 GLN A N   
2125 C CA  . GLN A 270 ? 1.9704 1.6385 1.8475 0.0221  0.0962  0.1266  269 GLN A CA  
2126 C C   . GLN A 270 ? 1.7248 1.3331 1.5684 0.0135  0.1167  0.1037  269 GLN A C   
2127 O O   . GLN A 270 ? 1.6815 1.2438 1.5235 0.0289  0.1397  0.1077  269 GLN A O   
2128 C CB  . GLN A 270 ? 2.0276 1.7155 1.9439 0.0457  0.1036  0.1357  269 GLN A CB  
2129 C CG  . GLN A 270 ? 2.0789 1.8298 2.0311 0.0532  0.0832  0.1611  269 GLN A CG  
2130 C CD  . GLN A 270 ? 2.1844 1.9366 2.1546 0.0715  0.0818  0.1994  269 GLN A CD  
2131 O OE1 . GLN A 270 ? 2.1996 1.9000 2.1596 0.0839  0.1006  0.2076  269 GLN A OE1 
2132 N NE2 . GLN A 270 ? 2.1942 2.0053 2.1902 0.0720  0.0597  0.2244  269 GLN A NE2 
2133 N N   . ARG A 271 ? 1.5234 1.1329 1.3403 -0.0123 0.1093  0.0804  270 ARG A N   
2134 C CA  . ARG A 271 ? 1.4165 0.9793 1.2010 -0.0264 0.1246  0.0580  270 ARG A CA  
2135 C C   . ARG A 271 ? 1.3402 0.9063 1.1296 -0.0274 0.1312  0.0376  270 ARG A C   
2136 O O   . ARG A 271 ? 1.3643 0.9747 1.1736 -0.0284 0.1181  0.0324  270 ARG A O   
2137 C CB  . ARG A 271 ? 1.3587 0.9258 1.1158 -0.0541 0.1136  0.0451  270 ARG A CB  
2138 C CG  . ARG A 271 ? 1.5233 1.0731 1.2630 -0.0594 0.1115  0.0607  270 ARG A CG  
2139 C CD  . ARG A 271 ? 1.7387 1.2818 1.4479 -0.0882 0.1078  0.0439  270 ARG A CD  
2140 N NE  . ARG A 271 ? 1.9483 1.4417 1.6291 -0.0995 0.1253  0.0290  270 ARG A NE  
2141 C CZ  . ARG A 271 ? 1.8846 1.3819 1.5532 -0.1190 0.1251  0.0068  270 ARG A CZ  
2142 N NH1 . ARG A 271 ? 1.6518 1.1984 1.3373 -0.1261 0.1101  -0.0030 270 ARG A NH1 
2143 N NH2 . ARG A 271 ? 1.9050 1.3561 1.5439 -0.1323 0.1406  -0.0047 270 ARG A NH2 
2144 N N   . GLN A 272 ? 1.3112 0.8273 1.0796 -0.0287 0.1528  0.0264  271 GLN A N   
2145 C CA  . GLN A 272 ? 1.1184 0.6310 0.8787 -0.0382 0.1588  0.0046  271 GLN A CA  
2146 C C   . GLN A 272 ? 1.1670 0.6497 0.8868 -0.0662 0.1616  -0.0130 271 GLN A C   
2147 O O   . GLN A 272 ? 1.2749 0.7075 0.9674 -0.0712 0.1771  -0.0124 271 GLN A O   
2148 C CB  . GLN A 272 ? 1.0786 0.5552 0.8427 -0.0204 0.1841  0.0050  271 GLN A CB  
2149 C CG  . GLN A 272 ? 1.2364 0.7487 1.0441 0.0056  0.1825  0.0201  271 GLN A CG  
2150 C CD  . GLN A 272 ? 1.3973 0.8721 1.2100 0.0238  0.2116  0.0199  271 GLN A CD  
2151 O OE1 . GLN A 272 ? 1.4309 0.8533 1.2307 0.0331  0.2344  0.0264  271 GLN A OE1 
2152 N NE2 . GLN A 272 ? 1.3610 0.8594 1.1914 0.0286  0.2134  0.0122  271 GLN A NE2 
2153 N N   . VAL A 273 ? 1.1172 0.6309 0.8341 -0.0851 0.1473  -0.0274 272 VAL A N   
2154 C CA  . VAL A 273 ? 1.1091 0.6027 0.7919 -0.1131 0.1485  -0.0423 272 VAL A CA  
2155 C C   . VAL A 273 ? 1.1405 0.6429 0.8190 -0.1239 0.1486  -0.0578 272 VAL A C   
2156 O O   . VAL A 273 ? 1.0960 0.6294 0.8010 -0.1112 0.1428  -0.0571 272 VAL A O   
2157 C CB  . VAL A 273 ? 1.0418 0.5690 0.7265 -0.1281 0.1300  -0.0411 272 VAL A CB  
2158 C CG1 . VAL A 273 ? 1.0097 0.5934 0.7246 -0.1249 0.1125  -0.0432 272 VAL A CG1 
2159 C CG2 . VAL A 273 ? 1.2323 0.7422 0.8851 -0.1574 0.1315  -0.0533 272 VAL A CG2 
2160 N N   . VAL A 274 ? 1.2434 0.7182 0.8870 -0.1491 0.1551  -0.0707 273 VAL A N   
2161 C CA  . VAL A 274 ? 1.1036 0.5923 0.7397 -0.1653 0.1509  -0.0833 273 VAL A CA  
2162 C C   . VAL A 274 ? 1.1469 0.6834 0.7928 -0.1831 0.1288  -0.0849 273 VAL A C   
2163 O O   . VAL A 274 ? 1.1759 0.7133 0.8114 -0.1976 0.1239  -0.0835 273 VAL A O   
2164 C CB  . VAL A 274 ? 1.0982 0.5333 0.6881 -0.1872 0.1695  -0.0959 273 VAL A CB  
2165 C CG1 . VAL A 274 ? 1.2460 0.7008 0.8259 -0.2078 0.1616  -0.1062 273 VAL A CG1 
2166 C CG2 . VAL A 274 ? 1.0795 0.4648 0.6618 -0.1679 0.1959  -0.0955 273 VAL A CG2 
2167 N N   . LEU A 275 ? 1.0524 0.6285 0.7206 -0.1809 0.1171  -0.0866 274 LEU A N   
2168 C CA  . LEU A 275 ? 1.0067 0.6267 0.6877 -0.1957 0.0994  -0.0869 274 LEU A CA  
2169 C C   . LEU A 275 ? 1.1547 0.7645 0.8050 -0.2259 0.0991  -0.0940 274 LEU A C   
2170 O O   . LEU A 275 ? 1.2207 0.8141 0.8540 -0.2324 0.1053  -0.0999 274 LEU A O   
2171 C CB  . LEU A 275 ? 1.0389 0.6996 0.7543 -0.1812 0.0892  -0.0846 274 LEU A CB  
2172 C CG  . LEU A 275 ? 0.9991 0.6924 0.7487 -0.1627 0.0810  -0.0780 274 LEU A CG  
2173 C CD1 . LEU A 275 ? 0.9046 0.5812 0.6487 -0.1562 0.0854  -0.0724 274 LEU A CD1 
2174 C CD2 . LEU A 275 ? 0.9000 0.6050 0.6711 -0.1435 0.0815  -0.0767 274 LEU A CD2 
2175 N N   . GLY A 276 ? 1.1062 0.7276 0.7483 -0.2467 0.0918  -0.0930 275 GLY A N   
2176 C CA  . GLY A 276 ? 1.1328 0.7454 0.7427 -0.2797 0.0907  -0.0982 275 GLY A CA  
2177 C C   . GLY A 276 ? 1.2022 0.8460 0.8152 -0.3024 0.0785  -0.0940 275 GLY A C   
2178 O O   . GLY A 276 ? 1.2115 0.8830 0.8520 -0.2923 0.0724  -0.0880 275 GLY A O   
2179 N N   . GLU A 277 ? 1.3553 0.9947 0.9382 -0.3355 0.0760  -0.0972 276 GLU A N   
2180 C CA  . GLU A 277 ? 1.3689 1.0448 0.9556 -0.3619 0.0631  -0.0915 276 GLU A CA  
2181 C C   . GLU A 277 ? 1.3505 1.0119 0.9273 -0.3694 0.0687  -0.0917 276 GLU A C   
2182 O O   . GLU A 277 ? 1.3369 1.0379 0.9291 -0.3848 0.0582  -0.0853 276 GLU A O   
2183 C CB  . GLU A 277 ? 1.5329 1.2012 1.0807 -0.4003 0.0601  -0.0950 276 GLU A CB  
2184 C CG  . GLU A 277 ? 1.6113 1.2141 1.1001 -0.4255 0.0777  -0.1071 276 GLU A CG  
2185 C CD  . GLU A 277 ? 1.7435 1.2836 1.1981 -0.4171 0.0984  -0.1192 276 GLU A CD  
2186 O OE1 . GLU A 277 ? 1.6611 1.2019 1.1426 -0.3826 0.1022  -0.1179 276 GLU A OE1 
2187 O OE2 . GLU A 277 ? 1.9016 1.3908 1.3017 -0.4464 0.1125  -0.1304 276 GLU A OE2 
2188 N N   . ASP A 278 ? 1.3010 0.9068 0.8530 -0.3595 0.0856  -0.0975 277 ASP A N   
2189 C CA  . ASP A 278 ? 1.3574 0.9451 0.8946 -0.3698 0.0911  -0.0966 277 ASP A CA  
2190 C C   . ASP A 278 ? 1.2856 0.8942 0.8581 -0.3420 0.0886  -0.0891 277 ASP A C   
2191 O O   . ASP A 278 ? 1.4549 1.0380 1.0138 -0.3423 0.0961  -0.0875 277 ASP A O   
2192 C CB  . ASP A 278 ? 1.5716 1.0834 1.0556 -0.3823 0.1118  -0.1053 277 ASP A CB  
2193 C CG  . ASP A 278 ? 1.7998 1.2680 1.2798 -0.3534 0.1275  -0.1083 277 ASP A CG  
2194 O OD1 . ASP A 278 ? 1.8704 1.3692 1.3874 -0.3255 0.1207  -0.1039 277 ASP A OD1 
2195 O OD2 . ASP A 278 ? 1.6291 1.0315 1.0691 -0.3592 0.1483  -0.1147 277 ASP A OD2 
2196 N N   . ASP A 279 ? 1.1439 0.7980 0.7591 -0.3203 0.0782  -0.0845 278 ASP A N   
2197 C CA  . ASP A 279 ? 0.9553 0.6330 0.6030 -0.2964 0.0755  -0.0789 278 ASP A CA  
2198 C C   . ASP A 279 ? 0.9799 0.7198 0.6658 -0.2996 0.0630  -0.0745 278 ASP A C   
2199 O O   . ASP A 279 ? 1.0705 0.8398 0.7803 -0.2926 0.0556  -0.0730 278 ASP A O   
2200 C CB  . ASP A 279 ? 1.0531 0.7191 0.7140 -0.2659 0.0790  -0.0783 278 ASP A CB  
2201 C CG  . ASP A 279 ? 1.1390 0.8364 0.8337 -0.2446 0.0738  -0.0732 278 ASP A CG  
2202 O OD1 . ASP A 279 ? 1.1014 0.8310 0.8120 -0.2514 0.0687  -0.0713 278 ASP A OD1 
2203 O OD2 . ASP A 279 ? 1.0262 0.7161 0.7308 -0.2221 0.0758  -0.0714 278 ASP A OD2 
2204 N N   . ASP A 280 ? 0.9918 0.7503 0.6838 -0.3104 0.0623  -0.0718 279 ASP A N   
2205 C CA  . ASP A 280 ? 0.8982 0.7133 0.6246 -0.3182 0.0542  -0.0667 279 ASP A CA  
2206 C C   . ASP A 280 ? 0.9280 0.7765 0.6964 -0.2923 0.0524  -0.0646 279 ASP A C   
2207 O O   . ASP A 280 ? 1.0115 0.9044 0.8143 -0.2914 0.0468  -0.0595 279 ASP A O   
2208 C CB  . ASP A 280 ? 0.9444 0.7677 0.6635 -0.3388 0.0570  -0.0650 279 ASP A CB  
2209 C CG  . ASP A 280 ? 1.4206 1.2055 1.1170 -0.3321 0.0666  -0.0673 279 ASP A CG  
2210 O OD1 . ASP A 280 ? 1.5400 1.2739 1.1968 -0.3397 0.0730  -0.0699 279 ASP A OD1 
2211 O OD2 . ASP A 280 ? 1.5026 1.3069 1.2196 -0.3198 0.0687  -0.0658 279 ASP A OD2 
2212 N N   . ILE A 281 ? 0.8792 0.7065 0.6448 -0.2724 0.0578  -0.0673 280 ILE A N   
2213 C CA  . ILE A 281 ? 0.8808 0.7333 0.6796 -0.2505 0.0572  -0.0673 280 ILE A CA  
2214 C C   . ILE A 281 ? 0.9288 0.7860 0.7402 -0.2385 0.0522  -0.0671 280 ILE A C   
2215 O O   . ILE A 281 ? 0.9734 0.8628 0.8176 -0.2292 0.0496  -0.0650 280 ILE A O   
2216 C CB  . ILE A 281 ? 0.9221 0.7541 0.7118 -0.2365 0.0623  -0.0689 280 ILE A CB  
2217 C CG1 . ILE A 281 ? 1.0330 0.8702 0.8168 -0.2474 0.0673  -0.0685 280 ILE A CG1 
2218 C CG2 . ILE A 281 ? 0.9398 0.7905 0.7561 -0.2167 0.0616  -0.0706 280 ILE A CG2 
2219 C CD1 . ILE A 281 ? 1.2361 1.0383 0.9913 -0.2445 0.0704  -0.0661 280 ILE A CD1 
2220 N N   . TRP A 282 ? 0.8321 0.6550 0.6172 -0.2389 0.0527  -0.0692 281 TRP A N   
2221 C CA  . TRP A 282 ? 0.8522 0.6771 0.6444 -0.2307 0.0489  -0.0695 281 TRP A CA  
2222 C C   . TRP A 282 ? 0.9386 0.8010 0.7506 -0.2424 0.0404  -0.0640 281 TRP A C   
2223 O O   . TRP A 282 ? 0.7939 0.6838 0.6370 -0.2296 0.0366  -0.0604 281 TRP A O   
2224 C CB  . TRP A 282 ? 0.8659 0.6468 0.6224 -0.2356 0.0540  -0.0734 281 TRP A CB  
2225 C CG  . TRP A 282 ? 0.8852 0.6644 0.6441 -0.2288 0.0522  -0.0746 281 TRP A CG  
2226 C CD1 . TRP A 282 ? 0.9878 0.7502 0.7216 -0.2450 0.0526  -0.0771 281 TRP A CD1 
2227 C CD2 . TRP A 282 ? 0.7855 0.5779 0.5694 -0.2069 0.0508  -0.0739 281 TRP A CD2 
2228 N NE1 . TRP A 282 ? 0.8928 0.6574 0.6348 -0.2336 0.0517  -0.0777 281 TRP A NE1 
2229 C CE2 . TRP A 282 ? 0.7347 0.5179 0.5085 -0.2097 0.0505  -0.0755 281 TRP A CE2 
2230 C CE3 . TRP A 282 ? 0.7331 0.5427 0.5434 -0.1880 0.0504  -0.0728 281 TRP A CE3 
2231 C CZ2 . TRP A 282 ? 0.6782 0.4698 0.4700 -0.1928 0.0497  -0.0752 281 TRP A CZ2 
2232 C CZ3 . TRP A 282 ? 0.7904 0.6079 0.6176 -0.1726 0.0494  -0.0730 281 TRP A CZ3 
2233 C CH2 . TRP A 282 ? 0.7338 0.5426 0.5528 -0.1744 0.0490  -0.0738 281 TRP A CH2 
2234 N N   . LEU A 283 ? 0.9516 0.8152 0.7455 -0.2677 0.0372  -0.0620 282 LEU A N   
2235 C CA  . LEU A 283 ? 0.9313 0.8405 0.7488 -0.2815 0.0273  -0.0525 282 LEU A CA  
2236 C C   . LEU A 283 ? 1.0317 0.9789 0.8924 -0.2675 0.0293  -0.0478 282 LEU A C   
2237 O O   . LEU A 283 ? 1.2119 1.1462 1.0709 -0.2585 0.0378  -0.0535 282 LEU A O   
2238 C CB  . LEU A 283 ? 0.9678 0.8746 0.7588 -0.3134 0.0247  -0.0512 282 LEU A CB  
2239 C CG  . LEU A 283 ? 1.0805 0.9609 0.8293 -0.3381 0.0217  -0.0541 282 LEU A CG  
2240 C CD1 . LEU A 283 ? 1.0502 0.8764 0.7678 -0.3261 0.0315  -0.0648 282 LEU A CD1 
2241 C CD2 . LEU A 283 ? 1.0443 0.9129 0.7622 -0.3694 0.0234  -0.0560 282 LEU A CD2 
2242 N N   . GLN A 284 ? 0.9063 0.8989 0.8054 -0.2656 0.0229  -0.0367 283 GLN A N   
2243 C CA  . GLN A 284 ? 1.0839 1.1104 1.0253 -0.2528 0.0294  -0.0327 283 GLN A CA  
2244 C C   . GLN A 284 ? 1.0136 1.0299 0.9710 -0.2260 0.0377  -0.0390 283 GLN A C   
2245 O O   . GLN A 284 ? 1.0444 1.0888 1.0415 -0.2123 0.0423  -0.0337 283 GLN A O   
2246 C CB  . GLN A 284 ? 1.1113 1.1360 1.0432 -0.2646 0.0369  -0.0368 283 GLN A CB  
2247 C CG  . GLN A 284 ? 0.9887 0.9965 0.9215 -0.2481 0.0497  -0.0466 283 GLN A CG  
2248 C CD  . GLN A 284 ? 1.3320 1.3535 1.2691 -0.2590 0.0583  -0.0474 283 GLN A CD  
2249 O OE1 . GLN A 284 ? 1.2815 1.3097 1.2353 -0.2477 0.0699  -0.0518 283 GLN A OE1 
2250 N NE2 . GLN A 284 ? 1.4051 1.4295 1.3244 -0.2834 0.0538  -0.0439 283 GLN A NE2 
2251 N N   . MET A 285 ? 0.9384 0.9147 0.8658 -0.2191 0.0408  -0.0495 284 MET A N   
2252 C CA  . MET A 285 ? 0.9000 0.8675 0.8386 -0.1978 0.0469  -0.0552 284 MET A CA  
2253 C C   . MET A 285 ? 0.8466 0.8072 0.7873 -0.1875 0.0414  -0.0538 284 MET A C   
2254 O O   . MET A 285 ? 0.6831 0.6484 0.6439 -0.1715 0.0454  -0.0552 284 MET A O   
2255 C CB  . MET A 285 ? 0.7633 0.6996 0.6746 -0.1954 0.0529  -0.0644 284 MET A CB  
2256 C CG  . MET A 285 ? 0.8501 0.7929 0.7769 -0.1840 0.0621  -0.0696 284 MET A CG  
2257 S SD  . MET A 285 ? 0.9383 0.8992 0.8736 -0.1945 0.0720  -0.0708 284 MET A SD  
2258 C CE  . MET A 285 ? 1.9803 1.9820 1.9507 -0.2013 0.0693  -0.0595 284 MET A CE  
2259 N N   . ARG A 286 ? 0.7266 0.6752 0.6447 -0.1989 0.0337  -0.0514 285 ARG A N   
2260 C CA  . ARG A 286 ? 0.7823 0.7164 0.6926 -0.1916 0.0305  -0.0522 285 ARG A CA  
2261 C C   . ARG A 286 ? 0.6928 0.6544 0.6346 -0.1835 0.0256  -0.0430 285 ARG A C   
2262 O O   . ARG A 286 ? 0.7110 0.6613 0.6506 -0.1742 0.0252  -0.0446 285 ARG A O   
2263 C CB  . ARG A 286 ? 0.7650 0.6743 0.6375 -0.2089 0.0269  -0.0539 285 ARG A CB  
2264 C CG  . ARG A 286 ? 0.6262 0.5574 0.4953 -0.2327 0.0180  -0.0453 285 ARG A CG  
2265 C CD  . ARG A 286 ? 0.7767 0.6734 0.5999 -0.2520 0.0182  -0.0509 285 ARG A CD  
2266 N NE  . ARG A 286 ? 0.8767 0.7903 0.6864 -0.2812 0.0088  -0.0438 285 ARG A NE  
2267 C CZ  . ARG A 286 ? 1.0172 0.9008 0.7827 -0.3036 0.0097  -0.0493 285 ARG A CZ  
2268 N NH1 . ARG A 286 ? 0.9337 0.8361 0.6850 -0.3343 -0.0003 -0.0424 285 ARG A NH1 
2269 N NH2 . ARG A 286 ? 0.9972 0.8322 0.7325 -0.2961 0.0216  -0.0614 285 ARG A NH2 
2270 N N   . HIS A 287 ? 0.6888 0.6866 0.6611 -0.1867 0.0225  -0.0319 286 HIS A N   
2271 C CA  . HIS A 287 ? 0.6534 0.6781 0.6601 -0.1771 0.0187  -0.0194 286 HIS A CA  
2272 C C   . HIS A 287 ? 0.7303 0.7695 0.7753 -0.1583 0.0304  -0.0190 286 HIS A C   
2273 O O   . HIS A 287 ? 0.8096 0.8709 0.8892 -0.1479 0.0306  -0.0070 286 HIS A O   
2274 C CB  . HIS A 287 ? 0.5233 0.5831 0.5421 -0.1936 0.0063  -0.0021 286 HIS A CB  
2275 C CG  . HIS A 287 ? 0.6577 0.7021 0.6342 -0.2175 -0.0035 -0.0036 286 HIS A CG  
2276 N ND1 . HIS A 287 ? 0.6732 0.6815 0.6153 -0.2180 -0.0029 -0.0133 286 HIS A ND1 
2277 C CD2 . HIS A 287 ? 0.8685 0.9272 0.8296 -0.2436 -0.0125 0.0028  286 HIS A CD2 
2278 C CE1 . HIS A 287 ? 0.7028 0.6997 0.6083 -0.2428 -0.0091 -0.0141 286 HIS A CE1 
2279 N NE2 . HIS A 287 ? 0.9317 0.9584 0.8461 -0.2602 -0.0158 -0.0047 286 HIS A NE2 
2280 N N   . LEU A 288 ? 0.6668 0.6913 0.7041 -0.1549 0.0413  -0.0316 287 LEU A N   
2281 C CA  . LEU A 288 ? 0.6672 0.6979 0.7319 -0.1407 0.0560  -0.0354 287 LEU A CA  
2282 C C   . LEU A 288 ? 0.6622 0.6691 0.7215 -0.1274 0.0622  -0.0450 287 LEU A C   
2283 O O   . LEU A 288 ? 0.6632 0.6475 0.6945 -0.1291 0.0564  -0.0512 287 LEU A O   
2284 C CB  . LEU A 288 ? 0.6575 0.6842 0.7117 -0.1476 0.0649  -0.0446 287 LEU A CB  
2285 C CG  . LEU A 288 ? 0.6569 0.7163 0.7344 -0.1561 0.0670  -0.0352 287 LEU A CG  
2286 C CD1 . LEU A 288 ? 0.4689 0.5564 0.5586 -0.1661 0.0519  -0.0179 287 LEU A CD1 
2287 C CD2 . LEU A 288 ? 0.4873 0.5350 0.5376 -0.1697 0.0701  -0.0441 287 LEU A CD2 
2288 N N   . HIS A 289 ? 0.7494 0.7611 0.8361 -0.1149 0.0755  -0.0459 288 HIS A N   
2289 C CA  . HIS A 289 ? 0.6978 0.6867 0.7780 -0.1059 0.0839  -0.0568 288 HIS A CA  
2290 C C   . HIS A 289 ? 0.7080 0.6758 0.7552 -0.1128 0.0867  -0.0719 288 HIS A C   
2291 O O   . HIS A 289 ? 0.7871 0.7578 0.8289 -0.1195 0.0925  -0.0763 288 HIS A O   
2292 C CB  . HIS A 289 ? 0.8155 0.8098 0.9292 -0.0941 0.1024  -0.0563 288 HIS A CB  
2293 C CG  . HIS A 289 ? 0.8531 0.8255 0.9645 -0.0861 0.1105  -0.0639 288 HIS A CG  
2294 N ND1 . HIS A 289 ? 0.7436 0.6935 0.8318 -0.0904 0.1200  -0.0811 288 HIS A ND1 
2295 C CD2 . HIS A 289 ? 0.7885 0.7583 0.9158 -0.0766 0.1098  -0.0559 288 HIS A CD2 
2296 C CE1 . HIS A 289 ? 0.8377 0.7722 0.9276 -0.0848 0.1254  -0.0844 288 HIS A CE1 
2297 N NE2 . HIS A 289 ? 0.9675 0.9120 1.0810 -0.0755 0.1199  -0.0696 288 HIS A NE2 
2298 N N   . ILE A 290 ? 0.7121 0.6613 0.7389 -0.1116 0.0826  -0.0783 289 ILE A N   
2299 C CA  . ILE A 290 ? 0.7947 0.7292 0.7929 -0.1181 0.0822  -0.0879 289 ILE A CA  
2300 C C   . ILE A 290 ? 0.8431 0.7748 0.8381 -0.1226 0.0960  -0.0979 289 ILE A C   
2301 O O   . ILE A 290 ? 0.9539 0.8804 0.9266 -0.1313 0.0944  -0.1016 289 ILE A O   
2302 C CB  . ILE A 290 ? 0.7710 0.6923 0.7543 -0.1154 0.0764  -0.0908 289 ILE A CB  
2303 C CG1 . ILE A 290 ? 0.6538 0.5719 0.6502 -0.1100 0.0854  -0.0957 289 ILE A CG1 
2304 C CG2 . ILE A 290 ? 0.9521 0.8710 0.9299 -0.1135 0.0650  -0.0833 289 ILE A CG2 
2305 C CD1 . ILE A 290 ? 0.8717 0.7812 0.8550 -0.1097 0.0802  -0.0987 289 ILE A CD1 
2306 N N   . SER A 291 ? 0.7790 0.7110 0.7933 -0.1175 0.1107  -0.1023 290 SER A N   
2307 C CA  . SER A 291 ? 0.9763 0.9013 0.9833 -0.1243 0.1276  -0.1143 290 SER A CA  
2308 C C   . SER A 291 ? 0.9962 0.9330 1.0060 -0.1303 0.1327  -0.1129 290 SER A C   
2309 O O   . SER A 291 ? 1.0921 1.0229 1.0805 -0.1417 0.1389  -0.1213 290 SER A O   
2310 C CB  . SER A 291 ? 0.8884 0.8069 0.9177 -0.1167 0.1469  -0.1192 290 SER A CB  
2311 O OG  . SER A 291 ? 0.9208 0.8563 0.9870 -0.1058 0.1526  -0.1080 290 SER A OG  
2312 N N   . GLU A 292 ? 0.7473 0.7030 0.7831 -0.1246 0.1291  -0.1011 291 GLU A N   
2313 C CA  . GLU A 292 ? 0.7124 0.6846 0.7559 -0.1308 0.1327  -0.0974 291 GLU A CA  
2314 C C   . GLU A 292 ? 0.8280 0.7959 0.8401 -0.1431 0.1172  -0.0956 291 GLU A C   
2315 O O   . GLU A 292 ? 0.7586 0.7292 0.7602 -0.1534 0.1221  -0.0982 291 GLU A O   
2316 C CB  . GLU A 292 ? 0.6529 0.6516 0.7372 -0.1219 0.1320  -0.0824 291 GLU A CB  
2317 C CG  . GLU A 292 ? 1.0464 1.0704 1.1443 -0.1293 0.1318  -0.0744 291 GLU A CG  
2318 C CD  . GLU A 292 ? 1.2614 1.3172 1.4008 -0.1216 0.1266  -0.0555 291 GLU A CD  
2319 O OE1 . GLU A 292 ? 1.2844 1.3384 1.4394 -0.1096 0.1240  -0.0493 291 GLU A OE1 
2320 O OE2 . GLU A 292 ? 1.2977 1.3818 1.4538 -0.1288 0.1245  -0.0456 291 GLU A OE2 
2321 N N   . VAL A 293 ? 0.8295 0.7881 0.8262 -0.1420 0.1009  -0.0912 292 VAL A N   
2322 C CA  . VAL A 293 ? 0.7599 0.7075 0.7267 -0.1514 0.0894  -0.0893 292 VAL A CA  
2323 C C   . VAL A 293 ? 0.7879 0.7195 0.7265 -0.1575 0.0918  -0.0967 292 VAL A C   
2324 O O   . VAL A 293 ? 0.7902 0.7180 0.7110 -0.1677 0.0918  -0.0964 292 VAL A O   
2325 C CB  . VAL A 293 ? 0.7372 0.6748 0.6944 -0.1475 0.0757  -0.0839 292 VAL A CB  
2326 C CG1 . VAL A 293 ? 0.6523 0.5698 0.5771 -0.1538 0.0690  -0.0837 292 VAL A CG1 
2327 C CG2 . VAL A 293 ? 0.7581 0.7116 0.7321 -0.1490 0.0694  -0.0743 292 VAL A CG2 
2328 N N   . PHE A 294 ? 0.9663 0.8897 0.9003 -0.1529 0.0929  -0.1020 293 PHE A N   
2329 C CA  . PHE A 294 ? 1.1310 1.0453 1.0406 -0.1610 0.0950  -0.1079 293 PHE A CA  
2330 C C   . PHE A 294 ? 1.0743 0.9911 0.9737 -0.1734 0.1047  -0.1117 293 PHE A C   
2331 O O   . PHE A 294 ? 1.0432 0.9527 0.9172 -0.1824 0.0990  -0.1086 293 PHE A O   
2332 C CB  . PHE A 294 ? 1.2719 1.1840 1.1864 -0.1589 0.1029  -0.1165 293 PHE A CB  
2333 C CG  . PHE A 294 ? 1.5811 1.4869 1.4682 -0.1700 0.1010  -0.1209 293 PHE A CG  
2334 C CD1 . PHE A 294 ? 1.6541 1.5585 1.5287 -0.1684 0.0858  -0.1130 293 PHE A CD1 
2335 C CD2 . PHE A 294 ? 1.7897 1.6925 1.6640 -0.1831 0.1152  -0.1319 293 PHE A CD2 
2336 C CE1 . PHE A 294 ? 1.7326 1.6379 1.5846 -0.1799 0.0815  -0.1133 293 PHE A CE1 
2337 C CE2 . PHE A 294 ? 1.8900 1.7896 1.7353 -0.1977 0.1115  -0.1348 293 PHE A CE2 
2338 C CZ  . PHE A 294 ? 1.8357 1.7392 1.6710 -0.1962 0.0930  -0.1240 293 PHE A CZ  
2339 N N   . ARG A 295 ? 1.0106 0.9377 0.9314 -0.1731 0.1202  -0.1170 294 ARG A N   
2340 C CA  . ARG A 295 ? 0.9118 0.8414 0.8240 -0.1854 0.1340  -0.1230 294 ARG A CA  
2341 C C   . ARG A 295 ? 0.9701 0.9117 0.8884 -0.1909 0.1333  -0.1162 294 ARG A C   
2342 O O   . ARG A 295 ? 1.0647 1.0056 0.9672 -0.2037 0.1412  -0.1197 294 ARG A O   
2343 C CB  . ARG A 295 ? 0.9584 0.8891 0.8869 -0.1839 0.1571  -0.1346 294 ARG A CB  
2344 C CG  . ARG A 295 ? 1.0506 0.9966 1.0237 -0.1688 0.1658  -0.1300 294 ARG A CG  
2345 C CD  . ARG A 295 ? 0.9328 0.8728 0.9224 -0.1647 0.1923  -0.1412 294 ARG A CD  
2346 N NE  . ARG A 295 ? 1.0274 0.9816 1.0629 -0.1465 0.1980  -0.1322 294 ARG A NE  
2347 C CZ  . ARG A 295 ? 1.2227 1.2023 1.2935 -0.1405 0.2038  -0.1219 294 ARG A CZ  
2348 N NH1 . ARG A 295 ? 1.1109 1.1024 1.1745 -0.1522 0.2061  -0.1218 294 ARG A NH1 
2349 N NH2 . ARG A 295 ? 1.2899 1.2853 1.4043 -0.1236 0.2071  -0.1101 294 ARG A NH2 
2350 N N   . LYS A 296 ? 0.8256 0.7785 0.7641 -0.1841 0.1239  -0.1064 295 LYS A N   
2351 C CA  . LYS A 296 ? 0.7728 0.7378 0.7139 -0.1932 0.1213  -0.0994 295 LYS A CA  
2352 C C   . LYS A 296 ? 0.8677 0.8128 0.7716 -0.2037 0.1088  -0.0957 295 LYS A C   
2353 O O   . LYS A 296 ? 1.0205 0.9661 0.9116 -0.2170 0.1114  -0.0944 295 LYS A O   
2354 C CB  . LYS A 296 ? 0.7365 0.7226 0.7089 -0.1870 0.1146  -0.0892 295 LYS A CB  
2355 C CG  . LYS A 296 ? 0.9135 0.9223 0.9296 -0.1745 0.1271  -0.0876 295 LYS A CG  
2356 C CD  . LYS A 296 ? 1.1515 1.1874 1.1947 -0.1791 0.1415  -0.0848 295 LYS A CD  
2357 C CE  . LYS A 296 ? 1.2233 1.2859 1.3179 -0.1635 0.1506  -0.0761 295 LYS A CE  
2358 N NZ  . LYS A 296 ? 1.2153 1.2957 1.3254 -0.1610 0.1310  -0.0603 295 LYS A NZ  
2359 N N   . VAL A 297 ? 0.9094 0.8364 0.7976 -0.1972 0.0967  -0.0931 296 VAL A N   
2360 C CA  . VAL A 297 ? 0.8739 0.7780 0.7293 -0.2033 0.0875  -0.0880 296 VAL A CA  
2361 C C   . VAL A 297 ? 0.8514 0.7482 0.6832 -0.2132 0.0926  -0.0905 296 VAL A C   
2362 O O   . VAL A 297 ? 0.7583 0.6440 0.5681 -0.2242 0.0913  -0.0860 296 VAL A O   
2363 C CB  . VAL A 297 ? 0.8068 0.6951 0.6553 -0.1915 0.0773  -0.0844 296 VAL A CB  
2364 C CG1 . VAL A 297 ? 0.8205 0.6844 0.6389 -0.1945 0.0712  -0.0772 296 VAL A CG1 
2365 C CG2 . VAL A 297 ? 0.7734 0.6652 0.6372 -0.1857 0.0722  -0.0816 296 VAL A CG2 
2366 N N   . LYS A 298 ? 0.8343 0.7359 0.6679 -0.2114 0.0987  -0.0976 297 LYS A N   
2367 C CA  . LYS A 298 ? 0.8218 0.7191 0.6306 -0.2248 0.1045  -0.1011 297 LYS A CA  
2368 C C   . LYS A 298 ? 0.8443 0.7502 0.6534 -0.2381 0.1179  -0.1052 297 LYS A C   
2369 O O   . LYS A 298 ? 0.8293 0.7265 0.6120 -0.2514 0.1171  -0.1015 297 LYS A O   
2370 C CB  . LYS A 298 ? 0.9602 0.8605 0.7691 -0.2239 0.1104  -0.1103 297 LYS A CB  
2371 C CG  . LYS A 298 ? 1.2035 1.0991 0.9803 -0.2416 0.1148  -0.1141 297 LYS A CG  
2372 C CD  . LYS A 298 ? 1.2484 1.1337 0.9961 -0.2480 0.0997  -0.0998 297 LYS A CD  
2373 C CE  . LYS A 298 ? 1.2759 1.1596 0.9895 -0.2685 0.1026  -0.1013 297 LYS A CE  
2374 N NZ  . LYS A 298 ? 1.2952 1.1694 0.9827 -0.2746 0.0888  -0.0840 297 LYS A NZ  
2375 N N   . SER A 299 ? 0.9723 0.8968 0.8136 -0.2338 0.1303  -0.1109 298 SER A N   
2376 C CA  . SER A 299 ? 0.8992 0.8384 0.7503 -0.2443 0.1444  -0.1133 298 SER A CA  
2377 C C   . SER A 299 ? 0.9294 0.8668 0.7696 -0.2540 0.1352  -0.1037 298 SER A C   
2378 O O   . SER A 299 ? 0.9236 0.8595 0.7461 -0.2695 0.1413  -0.1038 298 SER A O   
2379 C CB  . SER A 299 ? 0.9007 0.8646 0.7981 -0.2330 0.1566  -0.1154 298 SER A CB  
2380 O OG  . SER A 299 ? 1.1505 1.1153 1.0562 -0.2313 0.1773  -0.1274 298 SER A OG  
2381 N N   . SER A 300 ? 0.9343 0.8708 0.7839 -0.2465 0.1218  -0.0960 299 SER A N   
2382 C CA  . SER A 300 ? 0.8190 0.7502 0.6570 -0.2572 0.1139  -0.0882 299 SER A CA  
2383 C C   . SER A 300 ? 0.9524 0.8521 0.7475 -0.2663 0.1082  -0.0843 299 SER A C   
2384 O O   . SER A 300 ? 0.8580 0.7505 0.6351 -0.2819 0.1095  -0.0808 299 SER A O   
2385 C CB  . SER A 300 ? 0.7811 0.7125 0.6320 -0.2482 0.1018  -0.0828 299 SER A CB  
2386 O OG  . SER A 300 ? 0.9734 0.8979 0.8108 -0.2617 0.0954  -0.0768 299 SER A OG  
2387 N N   . PHE A 301 ? 1.0317 0.9144 0.8119 -0.2569 0.1020  -0.0833 300 PHE A N   
2388 C CA  . PHE A 301 ? 1.0930 0.9493 0.8374 -0.2624 0.0959  -0.0755 300 PHE A CA  
2389 C C   . PHE A 301 ? 1.0553 0.9137 0.7795 -0.2793 0.1046  -0.0775 300 PHE A C   
2390 O O   . PHE A 301 ? 1.0582 0.8995 0.7564 -0.2914 0.1033  -0.0702 300 PHE A O   
2391 C CB  . PHE A 301 ? 1.1602 1.0073 0.9005 -0.2482 0.0867  -0.0715 300 PHE A CB  
2392 C CG  . PHE A 301 ? 1.1680 0.9942 0.8774 -0.2516 0.0796  -0.0593 300 PHE A CG  
2393 C CD1 . PHE A 301 ? 0.9967 0.7957 0.6905 -0.2497 0.0745  -0.0478 300 PHE A CD1 
2394 C CD2 . PHE A 301 ? 1.1428 0.9756 0.8375 -0.2579 0.0786  -0.0582 300 PHE A CD2 
2395 C CE1 . PHE A 301 ? 1.0768 0.8568 0.7461 -0.2505 0.0687  -0.0330 300 PHE A CE1 
2396 C CE2 . PHE A 301 ? 1.0865 0.9047 0.7548 -0.2615 0.0700  -0.0428 300 PHE A CE2 
2397 C CZ  . PHE A 301 ? 1.0682 0.8605 0.7262 -0.2560 0.0650  -0.0289 300 PHE A CZ  
2398 N N   . ASP A 302 ? 0.9753 0.8513 0.7088 -0.2812 0.1151  -0.0878 301 ASP A N   
2399 C CA  . ASP A 302 ? 1.0692 0.9475 0.7816 -0.2994 0.1267  -0.0924 301 ASP A CA  
2400 C C   . ASP A 302 ? 1.1477 1.0365 0.8663 -0.3129 0.1382  -0.0944 301 ASP A C   
2401 O O   . ASP A 302 ? 1.1789 1.0588 0.8694 -0.3304 0.1420  -0.0916 301 ASP A O   
2402 C CB  . ASP A 302 ? 1.0960 0.9866 0.8155 -0.2997 0.1396  -0.1059 301 ASP A CB  
2403 C CG  . ASP A 302 ? 1.2835 1.1648 0.9852 -0.2959 0.1284  -0.1034 301 ASP A CG  
2404 O OD1 . ASP A 302 ? 1.3782 1.2461 1.0610 -0.2938 0.1114  -0.0891 301 ASP A OD1 
2405 O OD2 . ASP A 302 ? 1.2774 1.1653 0.9848 -0.2956 0.1376  -0.1151 301 ASP A OD2 
2406 N N   . GLU A 303 ? 1.1133 1.0233 0.8691 -0.3059 0.1431  -0.0975 302 GLU A N   
2407 C CA  . GLU A 303 ? 1.0944 1.0213 0.8616 -0.3191 0.1520  -0.0969 302 GLU A CA  
2408 C C   . GLU A 303 ? 1.1276 1.0325 0.8667 -0.3307 0.1405  -0.0865 302 GLU A C   
2409 O O   . GLU A 303 ? 1.2607 1.1659 0.9853 -0.3493 0.1472  -0.0851 302 GLU A O   
2410 C CB  . GLU A 303 ? 1.2037 1.1630 1.0198 -0.3091 0.1564  -0.0977 302 GLU A CB  
2411 C CG  . GLU A 303 ? 1.5918 1.5717 1.4394 -0.2983 0.1743  -0.1077 302 GLU A CG  
2412 C CD  . GLU A 303 ? 1.7962 1.8102 1.6970 -0.2857 0.1780  -0.1040 302 GLU A CD  
2413 O OE1 . GLU A 303 ? 1.8534 1.8966 1.7800 -0.2931 0.1894  -0.1013 302 GLU A OE1 
2414 O OE2 . GLU A 303 ? 1.7865 1.8005 1.7048 -0.2687 0.1697  -0.1021 302 GLU A OE2 
2415 N N   . PHE A 304 ? 1.2087 1.0916 0.9388 -0.3203 0.1252  -0.0796 303 PHE A N   
2416 C CA  . PHE A 304 ? 1.1492 1.0037 0.8515 -0.3303 0.1174  -0.0706 303 PHE A CA  
2417 C C   . PHE A 304 ? 1.0971 0.9260 0.7597 -0.3422 0.1184  -0.0646 303 PHE A C   
2418 O O   . PHE A 304 ? 1.1370 0.9534 0.7789 -0.3600 0.1215  -0.0604 303 PHE A O   
2419 C CB  . PHE A 304 ? 1.0993 0.9306 0.7985 -0.3155 0.1049  -0.0654 303 PHE A CB  
2420 C CG  . PHE A 304 ? 1.1477 0.9425 0.8160 -0.3255 0.1012  -0.0575 303 PHE A CG  
2421 C CD1 . PHE A 304 ? 1.1022 0.8617 0.7373 -0.3256 0.0991  -0.0481 303 PHE A CD1 
2422 C CD2 . PHE A 304 ? 1.2096 1.0045 0.8809 -0.3366 0.1006  -0.0586 303 PHE A CD2 
2423 C CE1 . PHE A 304 ? 1.1572 0.8772 0.7636 -0.3340 0.0991  -0.0407 303 PHE A CE1 
2424 C CE2 . PHE A 304 ? 1.1514 0.9065 0.7895 -0.3488 0.1003  -0.0535 303 PHE A CE2 
2425 C CZ  . PHE A 304 ? 1.1539 0.8688 0.7598 -0.3463 0.1010  -0.0449 303 PHE A CZ  
2426 N N   . CYS A 305 ? 1.0902 0.9122 0.7410 -0.3340 0.1151  -0.0628 304 CYS A N   
2427 C CA  . CYS A 305 ? 1.2777 1.0787 0.8906 -0.3454 0.1136  -0.0536 304 CYS A CA  
2428 C C   . CYS A 305 ? 1.3503 1.1643 0.9521 -0.3679 0.1275  -0.0595 304 CYS A C   
2429 O O   . CYS A 305 ? 1.4876 1.2829 1.0612 -0.3841 0.1286  -0.0517 304 CYS A O   
2430 C CB  . CYS A 305 ? 1.3064 1.1073 0.9119 -0.3353 0.1061  -0.0499 304 CYS A CB  
2431 S SG  . CYS A 305 ? 1.3469 1.1299 0.9607 -0.3102 0.0902  -0.0385 304 CYS A SG  
2432 N N   . VAL A 306 ? 1.3213 1.1651 0.9451 -0.3689 0.1401  -0.0733 305 VAL A N   
2433 C CA  . VAL A 306 ? 1.3194 1.1780 0.9370 -0.3890 0.1577  -0.0809 305 VAL A CA  
2434 C C   . VAL A 306 ? 1.3325 1.1951 0.9542 -0.4030 0.1623  -0.0781 305 VAL A C   
2435 O O   . VAL A 306 ? 1.3710 1.2268 0.9667 -0.4239 0.1695  -0.0758 305 VAL A O   
2436 C CB  . VAL A 306 ? 1.2014 1.0903 0.8512 -0.3836 0.1749  -0.0971 305 VAL A CB  
2437 C CG1 . VAL A 306 ? 1.1032 1.0161 0.7693 -0.3984 0.1956  -0.1042 305 VAL A CG1 
2438 C CG2 . VAL A 306 ? 1.0311 0.9129 0.6571 -0.3868 0.1783  -0.1029 305 VAL A CG2 
2439 N N   . SER A 307 ? 1.2912 1.1653 0.9434 -0.3938 0.1575  -0.0778 306 SER A N   
2440 C CA  . SER A 307 ? 1.2675 1.1486 0.9242 -0.4097 0.1596  -0.0746 306 SER A CA  
2441 C C   . SER A 307 ? 1.2833 1.1220 0.8969 -0.4220 0.1504  -0.0635 306 SER A C   
2442 O O   . SER A 307 ? 1.3167 1.1516 0.9133 -0.4444 0.1565  -0.0610 306 SER A O   
2443 C CB  . SER A 307 ? 1.3573 1.2627 1.0546 -0.3988 0.1542  -0.0755 306 SER A CB  
2444 O OG  . SER A 307 ? 1.5220 1.4190 1.2092 -0.4146 0.1482  -0.0693 306 SER A OG  
2445 N N   . ALA A 308 ? 1.2025 1.0082 0.7995 -0.4070 0.1373  -0.0561 307 ALA A N   
2446 C CA  . ALA A 308 ? 1.2035 0.9643 0.7641 -0.4146 0.1311  -0.0446 307 ALA A CA  
2447 C C   . ALA A 308 ? 1.3399 1.0793 0.8622 -0.4293 0.1346  -0.0363 307 ALA A C   
2448 O O   . ALA A 308 ? 1.4916 1.1948 0.9823 -0.4412 0.1339  -0.0264 307 ALA A O   
2449 C CB  . ALA A 308 ? 1.0604 0.7930 0.6182 -0.3925 0.1195  -0.0380 307 ALA A CB  
2450 N N   . ARG A 309 ? 1.3294 1.0890 0.8518 -0.4301 0.1392  -0.0401 308 ARG A N   
2451 C CA  . ARG A 309 ? 1.4186 1.1638 0.9030 -0.4485 0.1432  -0.0327 308 ARG A CA  
2452 C C   . ARG A 309 ? 1.4840 1.2475 0.9665 -0.4745 0.1591  -0.0404 308 ARG A C   
2453 O O   . ARG A 309 ? 1.4950 1.2370 0.9421 -0.4946 0.1623  -0.0321 308 ARG A O   
2454 C CB  . ARG A 309 ? 1.3730 1.1285 0.8498 -0.4429 0.1410  -0.0330 308 ARG A CB  
2455 C CG  . ARG A 309 ? 1.3406 1.0737 0.8086 -0.4233 0.1238  -0.0181 308 ARG A CG  
2456 C CD  . ARG A 309 ? 1.1685 0.9140 0.6245 -0.4232 0.1194  -0.0163 308 ARG A CD  
2457 N NE  . ARG A 309 ? 1.3323 1.0532 0.7659 -0.4149 0.1028  0.0072  308 ARG A NE  
2458 C CZ  . ARG A 309 ? 1.5574 1.2645 0.9529 -0.4309 0.0987  0.0236  308 ARG A CZ  
2459 N NH1 . ARG A 309 ? 1.4656 1.1795 0.8379 -0.4574 0.1109  0.0162  308 ARG A NH1 
2460 N NH2 . ARG A 309 ? 1.6560 1.3442 1.0377 -0.4203 0.0828  0.0488  308 ARG A NH2 
2461 N N   . ARG A 310 ? 1.5424 1.3467 1.0649 -0.4738 0.1694  -0.0545 309 ARG A N   
2462 C CA  . ARG A 310 ? 1.6107 1.4401 1.1402 -0.4968 0.1859  -0.0608 309 ARG A CA  
2463 C C   . ARG A 310 ? 1.6591 1.4779 1.1835 -0.5122 0.1829  -0.0550 309 ARG A C   
2464 O O   . ARG A 310 ? 1.8547 1.6861 1.3741 -0.5363 0.1942  -0.0562 309 ARG A O   
2465 C CB  . ARG A 310 ? 1.6417 1.5211 1.2212 -0.4890 0.2000  -0.0749 309 ARG A CB  
2466 C CG  . ARG A 310 ? 1.7466 1.6353 1.3243 -0.4838 0.2116  -0.0846 309 ARG A CG  
2467 C CD  . ARG A 310 ? 1.8989 1.8312 1.5303 -0.4721 0.2281  -0.0976 309 ARG A CD  
2468 N NE  . ARG A 310 ? 1.9754 1.9089 1.6059 -0.4630 0.2384  -0.1088 309 ARG A NE  
2469 C CZ  . ARG A 310 ? 1.9160 1.8741 1.5896 -0.4448 0.2492  -0.1188 309 ARG A CZ  
2470 N NH1 . ARG A 310 ? 1.8113 1.7991 1.5351 -0.4325 0.2491  -0.1165 309 ARG A NH1 
2471 N NH2 . ARG A 310 ? 1.9069 1.8590 1.5719 -0.4404 0.2602  -0.1302 309 ARG A NH2 
2472 N N   . LEU A 311 ? 1.6669 1.4618 1.1905 -0.5005 0.1690  -0.0495 310 LEU A N   
2473 C CA  . LEU A 311 ? 1.6575 1.4309 1.1649 -0.5184 0.1664  -0.0445 310 LEU A CA  
2474 C C   . LEU A 311 ? 1.5318 1.2552 0.9863 -0.5342 0.1672  -0.0333 310 LEU A C   
2475 O O   . LEU A 311 ? 1.7065 1.4166 1.1411 -0.5595 0.1723  -0.0310 310 LEU A O   
2476 C CB  . LEU A 311 ? 1.9393 1.6959 1.4557 -0.5031 0.1543  -0.0434 310 LEU A CB  
2477 C CG  . LEU A 311 ? 2.0969 1.9025 1.6634 -0.4945 0.1523  -0.0514 310 LEU A CG  
2478 C CD1 . LEU A 311 ? 2.2648 2.0469 1.8290 -0.4856 0.1408  -0.0499 310 LEU A CD1 
2479 C CD2 . LEU A 311 ? 2.0160 1.8656 1.6042 -0.5191 0.1611  -0.0544 310 LEU A CD2 
2480 N N   . GLN A 312 ? 1.5165 1.2131 0.9483 -0.5204 0.1617  -0.0247 311 GLN A N   
2481 C CA  . GLN A 312 ? 1.7687 1.4263 1.1532 -0.5357 0.1633  -0.0114 311 GLN A CA  
2482 C C   . GLN A 312 ? 1.8876 1.5736 1.2654 -0.5515 0.1739  -0.0157 311 GLN A C   
2483 O O   . GLN A 312 ? 1.8766 1.6007 1.2749 -0.5671 0.1868  -0.0277 311 GLN A O   
2484 C CB  . GLN A 312 ? 1.7668 1.3828 1.1301 -0.5144 0.1510  0.0049  311 GLN A CB  
2485 C CG  . GLN A 312 ? 1.7643 1.3205 1.0930 -0.5193 0.1499  0.0196  311 GLN A CG  
2486 C CD  . GLN A 312 ? 1.7051 1.2382 1.0476 -0.4975 0.1441  0.0195  311 GLN A CD  
2487 O OE1 . GLN A 312 ? 1.8518 1.4166 1.2298 -0.4798 0.1392  0.0091  311 GLN A OE1 
2488 N NE2 . GLN A 312 ? 1.5774 1.0525 0.8908 -0.4990 0.1464  0.0308  311 GLN A NE2 
2489 N N   . GLY A 313 ? 1.9200 1.5895 1.2699 -0.5483 0.1692  -0.0051 312 GLY A N   
2490 C CA  . GLY A 313 ? 1.9534 1.6450 1.2893 -0.5653 0.1798  -0.0099 312 GLY A CA  
2491 C C   . GLY A 313 ? 2.0830 1.7690 1.4013 -0.5542 0.1697  -0.0013 312 GLY A C   
2492 O O   . GLY A 313 ? 2.2850 1.9404 1.5632 -0.5615 0.1618  0.0178  312 GLY A O   
2493 N N   . LEU A 314 ? 1.9625 1.6791 1.3104 -0.5380 0.1696  -0.0140 313 LEU A N   
2494 C CA  . LEU A 314 ? 2.0407 1.7563 1.3751 -0.5282 0.1583  -0.0068 313 LEU A CA  
2495 C C   . LEU A 314 ? 2.1324 1.8863 1.4920 -0.5250 0.1699  -0.0288 313 LEU A C   
2496 O O   . LEU A 314 ? 2.2058 1.9847 1.5887 -0.5326 0.1888  -0.0464 313 LEU A O   
2497 C CB  . LEU A 314 ? 2.0757 1.7694 1.4205 -0.5004 0.1387  0.0081  313 LEU A CB  
2498 C CG  . LEU A 314 ? 2.0258 1.6746 1.3502 -0.4985 0.1310  0.0288  313 LEU A CG  
2499 C CD1 . LEU A 314 ? 1.8951 1.5294 1.2476 -0.4728 0.1241  0.0295  313 LEU A CD1 
2500 C CD2 . LEU A 314 ? 2.1123 1.7360 1.3990 -0.5007 0.1184  0.0556  313 LEU A CD2 
2501 N N   . ARG A 315 ? 2.0911 1.8497 1.4468 -0.5148 0.1600  -0.0269 314 ARG A N   
2502 C CA  . ARG A 315 ? 2.1078 1.8955 1.4886 -0.5087 0.1712  -0.0482 314 ARG A CA  
2503 C C   . ARG A 315 ? 2.1505 1.9388 1.5238 -0.4979 0.1557  -0.0427 314 ARG A C   
2504 O O   . ARG A 315 ? 2.2458 2.0218 1.5812 -0.5084 0.1422  -0.0253 314 ARG A O   
2505 C CB  . ARG A 315 ? 2.2103 2.0139 1.5776 -0.5340 0.1967  -0.0657 314 ARG A CB  
2506 C CG  . ARG A 315 ? 2.2792 2.1072 1.6743 -0.5269 0.2139  -0.0890 314 ARG A CG  
2507 C CD  . ARG A 315 ? 2.3665 2.2190 1.8108 -0.5193 0.2352  -0.1047 314 ARG A CD  
2508 N NE  . ARG A 315 ? 2.5156 2.3758 1.9477 -0.5440 0.2580  -0.1116 314 ARG A NE  
2509 C CZ  . ARG A 315 ? 2.4777 2.3652 1.9504 -0.5429 0.2812  -0.1244 314 ARG A CZ  
2510 N NH1 . ARG A 315 ? 2.4276 2.3368 1.9550 -0.5181 0.2833  -0.1305 314 ARG A NH1 
2511 N NH2 . ARG A 315 ? 2.4202 2.3155 1.8802 -0.5666 0.3023  -0.1293 314 ARG A NH2 
2512 N N   . ASP A 316 ? 2.0838 1.8889 1.4937 -0.4784 0.1575  -0.0562 315 ASP A N   
2513 C CA  . ASP A 316 ? 2.1015 1.9087 1.5118 -0.4654 0.1410  -0.0503 315 ASP A CA  
2514 C C   . ASP A 316 ? 2.1382 1.9550 1.5191 -0.4855 0.1473  -0.0597 315 ASP A C   
2515 O O   . ASP A 316 ? 1.9702 1.8004 1.3692 -0.4816 0.1598  -0.0797 315 ASP A O   
2516 C CB  . ASP A 316 ? 2.1384 1.9579 1.5973 -0.4382 0.1410  -0.0614 315 ASP A CB  
2517 C CG  . ASP A 316 ? 2.1731 1.9838 1.6593 -0.4204 0.1349  -0.0543 315 ASP A CG  
2518 O OD1 . ASP A 316 ? 2.2378 2.0416 1.7179 -0.4316 0.1422  -0.0527 315 ASP A OD1 
2519 O OD2 . ASP A 316 ? 2.1288 1.9395 1.6409 -0.3974 0.1238  -0.0513 315 ASP A OD2 
2520 N N   . SER A 317 ? 2.3850 2.1931 1.7184 -0.5082 0.1388  -0.0448 316 SER A N   
2521 C CA  . SER A 317 ? 2.5695 2.3857 1.8671 -0.5320 0.1420  -0.0519 316 SER A CA  
2522 C C   . SER A 317 ? 2.6263 2.4479 1.9172 -0.5245 0.1144  -0.0324 316 SER A C   
2523 O O   . SER A 317 ? 2.6287 2.4603 1.8930 -0.5433 0.1125  -0.0373 316 SER A O   
2524 C CB  . SER A 317 ? 2.6600 2.4683 1.9054 -0.5669 0.1498  -0.0479 316 SER A CB  
2525 O OG  . SER A 317 ? 2.7092 2.5028 1.9350 -0.5675 0.1293  -0.0172 316 SER A OG  
2526 N N   . GLN A 318 ? 2.6550 2.4705 1.9706 -0.4981 0.0943  -0.0106 317 GLN A N   
2527 C CA  . GLN A 318 ? 2.7035 2.5270 2.0201 -0.4874 0.0680  0.0123  317 GLN A CA  
2528 C C   . GLN A 318 ? 2.6866 2.5198 2.0494 -0.4586 0.0652  0.0030  317 GLN A C   
2529 O O   . GLN A 318 ? 2.6382 2.4617 2.0359 -0.4329 0.0657  0.0037  317 GLN A O   
2530 C CB  . GLN A 318 ? 2.7681 2.5757 2.0787 -0.4772 0.0487  0.0472  317 GLN A CB  
2531 C CG  . GLN A 318 ? 2.8609 2.6569 2.1242 -0.5052 0.0489  0.0613  317 GLN A CG  
2532 C CD  . GLN A 318 ? 2.8806 2.6565 2.1400 -0.4925 0.0314  0.0978  317 GLN A CD  
2533 O OE1 . GLN A 318 ? 2.8497 2.6219 2.1407 -0.4630 0.0187  0.1137  317 GLN A OE1 
2534 N NE2 . GLN A 318 ? 2.9228 2.6833 2.1431 -0.5146 0.0326  0.1116  317 GLN A NE2 
2535 N N   . GLN A 319 ? 2.7536 2.6046 2.1129 -0.4658 0.0624  -0.0060 318 GLN A N   
2536 C CA  . GLN A 319 ? 2.7679 2.6288 2.1672 -0.4412 0.0586  -0.0133 318 GLN A CA  
2537 C C   . GLN A 319 ? 2.7221 2.6022 2.1134 -0.4442 0.0354  0.0052  318 GLN A C   
2538 O O   . GLN A 319 ? 2.6825 2.5757 2.0472 -0.4690 0.0365  -0.0041 318 GLN A O   
2539 C CB  . GLN A 319 ? 2.8243 2.6881 2.2381 -0.4439 0.0839  -0.0480 318 GLN A CB  
2540 C CG  . GLN A 319 ? 2.8329 2.6862 2.2689 -0.4352 0.1050  -0.0630 318 GLN A CG  
2541 C CD  . GLN A 319 ? 2.8051 2.6629 2.2576 -0.4375 0.1322  -0.0937 318 GLN A CD  
2542 O OE1 . GLN A 319 ? 2.8005 2.6626 2.2393 -0.4499 0.1391  -0.1071 318 GLN A OE1 
2543 N NE2 . GLN A 319 ? 2.7691 2.6258 2.2515 -0.4262 0.1485  -0.1039 318 GLN A NE2 
2544 N N   . GLY A 320 ? 2.7015 2.5831 2.1152 -0.4202 0.0154  0.0322  319 GLY A N   
2545 C CA  . GLY A 320 ? 2.7419 2.6472 2.1600 -0.4175 -0.0073 0.0531  319 GLY A CA  
2546 C C   . GLY A 320 ? 2.7527 2.6616 2.2188 -0.3853 -0.0086 0.0485  319 GLY A C   
2547 O O   . GLY A 320 ? 2.7490 2.6388 2.2422 -0.3619 0.0007  0.0425  319 GLY A O   
2548 N N   . GLU A 321 ? 2.8997 2.8337 2.3741 -0.3871 -0.0199 0.0508  320 GLU A N   
2549 C CA  . GLU A 321 ? 2.9740 2.9141 2.4919 -0.3591 -0.0215 0.0470  320 GLU A CA  
2550 C C   . GLU A 321 ? 2.8822 2.8015 2.4242 -0.3431 0.0004  0.0182  320 GLU A C   
2551 O O   . GLU A 321 ? 2.8866 2.8005 2.4638 -0.3154 0.0001  0.0196  320 GLU A O   
2552 C CB  . GLU A 321 ? 3.1333 3.0765 2.6779 -0.3317 -0.0388 0.0805  320 GLU A CB  
2553 C CG  . GLU A 321 ? 3.3035 3.2745 2.8340 -0.3433 -0.0630 0.1154  320 GLU A CG  
2554 C CD  . GLU A 321 ? 3.4371 3.4454 2.9722 -0.3550 -0.0754 0.1159  320 GLU A CD  
2555 O OE1 . GLU A 321 ? 3.4674 3.4761 3.0204 -0.3493 -0.0649 0.0905  320 GLU A OE1 
2556 O OE2 . GLU A 321 ? 3.5151 3.5535 3.0356 -0.3714 -0.0964 0.1432  320 GLU A OE2 
2557 N N   . GLY A 322 ? 2.6322 2.5415 2.1552 -0.3614 0.0198  -0.0065 321 GLY A N   
2558 C CA  . GLY A 322 ? 2.3396 2.2365 1.8872 -0.3490 0.0404  -0.0320 321 GLY A CA  
2559 C C   . GLY A 322 ? 2.0619 1.9409 1.6294 -0.3289 0.0434  -0.0263 321 GLY A C   
2560 O O   . GLY A 322 ? 2.0441 1.9108 1.5922 -0.3374 0.0448  -0.0180 321 GLY A O   
2561 N N   . GLY A 323 ? 1.8863 1.7628 1.4895 -0.3046 0.0449  -0.0313 322 GLY A N   
2562 C CA  . GLY A 323 ? 1.8455 1.7045 1.4655 -0.2884 0.0484  -0.0283 322 GLY A CA  
2563 C C   . GLY A 323 ? 1.8290 1.6759 1.4514 -0.2728 0.0339  -0.0030 322 GLY A C   
2564 O O   . GLY A 323 ? 1.8058 1.6314 1.4316 -0.2642 0.0374  0.0014  322 GLY A O   
2565 N N   . ALA A 324 ? 1.8063 1.6667 1.4277 -0.2695 0.0189  0.0143  323 ALA A N   
2566 C CA  . ALA A 324 ? 1.7193 1.5698 1.3459 -0.2531 0.0070  0.0421  323 ALA A CA  
2567 C C   . ALA A 324 ? 1.6868 1.5216 1.2831 -0.2658 0.0046  0.0592  323 ALA A C   
2568 O O   . ALA A 324 ? 1.6066 1.4168 1.2043 -0.2525 0.0040  0.0762  323 ALA A O   
2569 C CB  . ALA A 324 ? 1.5293 1.4062 1.1677 -0.2468 -0.0090 0.0590  323 ALA A CB  
2570 N N   . GLY A 325 ? 1.5952 1.4416 1.1621 -0.2926 0.0051  0.0539  324 GLY A N   
2571 C CA  . GLY A 325 ? 1.5724 1.4065 1.1061 -0.3092 0.0028  0.0694  324 GLY A CA  
2572 C C   . GLY A 325 ? 1.6369 1.4449 1.1637 -0.3135 0.0195  0.0551  324 GLY A C   
2573 O O   . GLY A 325 ? 1.6717 1.4589 1.1767 -0.3204 0.0197  0.0692  324 GLY A O   
2574 N N   . ALA A 326 ? 1.5761 1.3868 1.1222 -0.3103 0.0332  0.0283  325 ALA A N   
2575 C CA  . ALA A 326 ? 1.4592 1.2521 1.0071 -0.3128 0.0477  0.0153  325 ALA A CA  
2576 C C   . ALA A 326 ? 1.5384 1.3044 1.0989 -0.2925 0.0451  0.0277  325 ALA A C   
2577 O O   . ALA A 326 ? 1.7119 1.4525 1.2577 -0.2982 0.0508  0.0323  325 ALA A O   
2578 C CB  . ALA A 326 ? 1.2636 1.0723 0.8345 -0.3127 0.0612  -0.0121 325 ALA A CB  
2579 N N   . LEU A 327 ? 1.3223 1.0917 0.9078 -0.2703 0.0381  0.0325  326 LEU A N   
2580 C CA  . LEU A 327 ? 1.2407 0.9821 0.8379 -0.2502 0.0387  0.0423  326 LEU A CA  
2581 C C   . LEU A 327 ? 1.3778 1.0949 0.9570 -0.2461 0.0326  0.0711  326 LEU A C   
2582 O O   . LEU A 327 ? 1.4932 1.1740 1.0668 -0.2392 0.0395  0.0778  326 LEU A O   
2583 C CB  . LEU A 327 ? 1.0202 0.7735 0.6486 -0.2283 0.0345  0.0399  326 LEU A CB  
2584 C CG  . LEU A 327 ? 1.1579 0.8842 0.8012 -0.2091 0.0405  0.0401  326 LEU A CG  
2585 C CD1 . LEU A 327 ? 1.3267 1.0714 0.9975 -0.1991 0.0419  0.0228  326 LEU A CD1 
2586 C CD2 . LEU A 327 ? 1.2430 0.9507 0.8892 -0.1901 0.0357  0.0666  326 LEU A CD2 
2587 N N   . LYS A 328 ? 1.3654 1.1017 0.9345 -0.2517 0.0202  0.0890  327 LYS A N   
2588 C CA  . LYS A 328 ? 1.3469 1.0645 0.9007 -0.2480 0.0131  0.1205  327 LYS A CA  
2589 C C   . LYS A 328 ? 1.3126 1.0055 0.8322 -0.2694 0.0209  0.1199  327 LYS A C   
2590 O O   . LYS A 328 ? 1.3769 1.0328 0.8854 -0.2636 0.0250  0.1365  327 LYS A O   
2591 C CB  . LYS A 328 ? 1.4651 1.2174 1.0170 -0.2518 -0.0052 0.1421  327 LYS A CB  
2592 C CG  . LYS A 328 ? 1.7139 1.4541 1.2543 -0.2468 -0.0155 0.1811  327 LYS A CG  
2593 C CD  . LYS A 328 ? 1.7871 1.5572 1.3539 -0.2287 -0.0324 0.2090  327 LYS A CD  
2594 C CE  . LYS A 328 ? 1.9231 1.6676 1.5230 -0.1932 -0.0255 0.2233  327 LYS A CE  
2595 N NZ  . LYS A 328 ? 1.9666 1.6972 1.5857 -0.1815 -0.0103 0.1917  327 LYS A NZ  
2596 N N   . GLN A 329 ? 1.2982 1.0097 0.8014 -0.2942 0.0253  0.1004  328 GLN A N   
2597 C CA  . GLN A 329 ? 1.3741 1.0685 0.8442 -0.3176 0.0328  0.0999  328 GLN A CA  
2598 C C   . GLN A 329 ? 1.4816 1.1461 0.9542 -0.3171 0.0479  0.0856  328 GLN A C   
2599 O O   . GLN A 329 ? 1.5519 1.1888 0.9992 -0.3303 0.0541  0.0921  328 GLN A O   
2600 C CB  . GLN A 329 ? 1.3854 1.1094 0.8394 -0.3442 0.0367  0.0813  328 GLN A CB  
2601 C CG  . GLN A 329 ? 1.4889 1.1995 0.9078 -0.3707 0.0454  0.0806  328 GLN A CG  
2602 C CD  . GLN A 329 ? 1.6285 1.3659 1.0341 -0.3958 0.0551  0.0582  328 GLN A CD  
2603 O OE1 . GLN A 329 ? 1.7254 1.4822 1.1548 -0.3923 0.0642  0.0338  328 GLN A OE1 
2604 N NE2 . GLN A 329 ? 1.6561 1.3926 1.0228 -0.4214 0.0548  0.0669  328 GLN A NE2 
2605 N N   . MET A 330 ? 1.4486 1.1190 0.9499 -0.3042 0.0532  0.0668  329 MET A N   
2606 C CA  . MET A 330 ? 1.4526 1.0996 0.9557 -0.3069 0.0656  0.0533  329 MET A CA  
2607 C C   . MET A 330 ? 1.3656 0.9661 0.8624 -0.2923 0.0677  0.0701  329 MET A C   
2608 O O   . MET A 330 ? 1.3678 0.9351 0.8438 -0.3040 0.0770  0.0702  329 MET A O   
2609 C CB  . MET A 330 ? 1.4460 1.1167 0.9803 -0.3002 0.0698  0.0296  329 MET A CB  
2610 C CG  . MET A 330 ? 1.4333 1.0946 0.9684 -0.3120 0.0810  0.0142  329 MET A CG  
2611 S SD  . MET A 330 ? 1.7430 1.4428 1.2835 -0.3353 0.0903  -0.0058 329 MET A SD  
2612 C CE  . MET A 330 ? 1.8543 1.5542 1.3605 -0.3525 0.0887  0.0063  329 MET A CE  
2613 N N   . LEU A 331 ? 1.3102 0.9075 0.8249 -0.2673 0.0609  0.0840  330 LEU A N   
2614 C CA  . LEU A 331 ? 1.2782 0.8293 0.7901 -0.2496 0.0663  0.1010  330 LEU A CA  
2615 C C   . LEU A 331 ? 1.4637 0.9850 0.9476 -0.2550 0.0656  0.1276  330 LEU A C   
2616 O O   . LEU A 331 ? 1.5790 1.0505 1.0513 -0.2471 0.0758  0.1394  330 LEU A O   
2617 C CB  . LEU A 331 ? 1.0612 0.6226 0.6039 -0.2205 0.0603  0.1111  330 LEU A CB  
2618 C CG  . LEU A 331 ? 1.2226 0.7977 0.7895 -0.2132 0.0647  0.0865  330 LEU A CG  
2619 C CD1 . LEU A 331 ? 1.0205 0.6134 0.6188 -0.1871 0.0583  0.0952  330 LEU A CD1 
2620 C CD2 . LEU A 331 ? 1.3904 0.9217 0.9452 -0.2172 0.0804  0.0737  330 LEU A CD2 
2621 N N   . LYS A 332 ? 1.3872 0.9364 0.8578 -0.2695 0.0548  0.1372  331 LYS A N   
2622 C CA  . LYS A 332 ? 1.4432 0.9684 0.8849 -0.2778 0.0524  0.1639  331 LYS A CA  
2623 C C   . LYS A 332 ? 1.5842 1.0888 0.9932 -0.3069 0.0636  0.1510  331 LYS A C   
2624 O O   . LYS A 332 ? 1.6341 1.0919 1.0196 -0.3105 0.0716  0.1649  331 LYS A O   
2625 C CB  . LYS A 332 ? 1.3973 0.9622 0.8356 -0.2828 0.0342  0.1834  331 LYS A CB  
2626 C CG  . LYS A 332 ? 1.6667 1.2123 1.0711 -0.2963 0.0297  0.2120  331 LYS A CG  
2627 C CD  . LYS A 332 ? 1.8506 1.4350 1.2534 -0.2983 0.0087  0.2388  331 LYS A CD  
2628 C CE  . LYS A 332 ? 1.9788 1.5423 1.3476 -0.3109 0.0031  0.2717  331 LYS A CE  
2629 N NZ  . LYS A 332 ? 2.0187 1.6190 1.3890 -0.3097 -0.0200 0.3060  331 LYS A NZ  
2630 N N   . ASP A 333 ? 1.5742 1.1130 0.9833 -0.3271 0.0657  0.1248  332 ASP A N   
2631 C CA  . ASP A 333 ? 1.6079 1.1390 0.9903 -0.3567 0.0761  0.1125  332 ASP A CA  
2632 C C   . ASP A 333 ? 1.5605 1.0657 0.9446 -0.3620 0.0904  0.0940  332 ASP A C   
2633 O O   . ASP A 333 ? 1.6651 1.1386 1.0218 -0.3806 0.0996  0.0960  332 ASP A O   
2634 C CB  . ASP A 333 ? 1.6952 1.2748 1.0783 -0.3763 0.0753  0.0942  332 ASP A CB  
2635 C CG  . ASP A 333 ? 1.8148 1.4129 1.1783 -0.3845 0.0632  0.1127  332 ASP A CG  
2636 O OD1 . ASP A 333 ? 1.8805 1.4640 1.2394 -0.3705 0.0516  0.1418  332 ASP A OD1 
2637 O OD2 . ASP A 333 ? 1.7090 1.3369 1.0616 -0.4058 0.0661  0.0991  332 ASP A OD2 
2638 N N   . LEU A 334 ? 1.3947 0.9134 0.8088 -0.3479 0.0915  0.0772  333 LEU A N   
2639 C CA  . LEU A 334 ? 1.3235 0.8247 0.7400 -0.3551 0.1025  0.0596  333 LEU A CA  
2640 C C   . LEU A 334 ? 1.3499 0.8206 0.7789 -0.3313 0.1048  0.0620  333 LEU A C   
2641 O O   . LEU A 334 ? 1.3156 0.8053 0.7687 -0.3242 0.1049  0.0454  333 LEU A O   
2642 C CB  . LEU A 334 ? 1.4481 0.9991 0.8891 -0.3652 0.1036  0.0347  333 LEU A CB  
2643 C CG  . LEU A 334 ? 1.3476 0.9221 0.7786 -0.3941 0.1103  0.0242  333 LEU A CG  
2644 C CD1 . LEU A 334 ? 1.2247 0.7696 0.6168 -0.4109 0.1130  0.0403  333 LEU A CD1 
2645 C CD2 . LEU A 334 ? 1.1875 0.8156 0.6421 -0.3940 0.1083  0.0120  333 LEU A CD2 
2646 N N   . PRO A 335 ? 1.3334 0.7552 0.7461 -0.3188 0.1085  0.0833  334 PRO A N   
2647 C CA  . PRO A 335 ? 1.3463 0.7331 0.7693 -0.2951 0.1151  0.0866  334 PRO A CA  
2648 C C   . PRO A 335 ? 1.3277 0.7000 0.7481 -0.3066 0.1258  0.0624  334 PRO A C   
2649 O O   . PRO A 335 ? 1.2972 0.6654 0.7351 -0.2898 0.1283  0.0557  334 PRO A O   
2650 C CB  . PRO A 335 ? 1.4456 0.7724 0.8420 -0.2899 0.1239  0.1114  334 PRO A CB  
2651 C CG  . PRO A 335 ? 1.5244 0.8695 0.9066 -0.3014 0.1139  0.1284  334 PRO A CG  
2652 C CD  . PRO A 335 ? 1.4560 0.8482 0.8379 -0.3278 0.1095  0.1057  334 PRO A CD  
2653 N N   . GLN A 336 ? 1.3998 0.7652 0.7971 -0.3371 0.1320  0.0509  335 GLN A N   
2654 C CA  . GLN A 336 ? 1.3204 0.6843 0.7145 -0.3555 0.1387  0.0288  335 GLN A CA  
2655 C C   . GLN A 336 ? 1.3209 0.7304 0.7514 -0.3429 0.1308  0.0143  335 GLN A C   
2656 O O   . GLN A 336 ? 1.3669 0.7624 0.7973 -0.3446 0.1361  0.0026  335 GLN A O   
2657 C CB  . GLN A 336 ? 1.1692 0.5557 0.5502 -0.3893 0.1392  0.0198  335 GLN A CB  
2658 C CG  . GLN A 336 ? 1.2286 0.6384 0.6073 -0.3918 0.1329  0.0320  335 GLN A CG  
2659 C CD  . GLN A 336 ? 1.4971 0.9415 0.8723 -0.4220 0.1343  0.0210  335 GLN A CD  
2660 O OE1 . GLN A 336 ? 1.5594 1.0119 0.9215 -0.4324 0.1337  0.0292  335 GLN A OE1 
2661 N NE2 . GLN A 336 ? 1.6190 1.0862 1.0065 -0.4374 0.1366  0.0035  335 GLN A NE2 
2662 N N   . HIS A 337 ? 1.2127 0.6751 0.6715 -0.3323 0.1189  0.0149  336 HIS A N   
2663 C CA  . HIS A 337 ? 1.1133 0.6207 0.6063 -0.3236 0.1122  0.0009  336 HIS A CA  
2664 C C   . HIS A 337 ? 1.1444 0.6506 0.6586 -0.2925 0.1080  0.0066  336 HIS A C   
2665 O O   . HIS A 337 ? 0.9823 0.5270 0.5253 -0.2829 0.1013  -0.0024 336 HIS A O   
2666 C CB  . HIS A 337 ? 1.0124 0.5769 0.5251 -0.3317 0.1054  -0.0055 336 HIS A CB  
2667 C CG  . HIS A 337 ? 1.1921 0.7683 0.6932 -0.3614 0.1107  -0.0130 336 HIS A CG  
2668 N ND1 . HIS A 337 ? 1.2641 0.8359 0.7606 -0.3800 0.1154  -0.0230 336 HIS A ND1 
2669 C CD2 . HIS A 337 ? 1.1607 0.7564 0.6547 -0.3773 0.1124  -0.0117 336 HIS A CD2 
2670 C CE1 . HIS A 337 ? 1.2904 0.8811 0.7808 -0.4052 0.1192  -0.0264 336 HIS A CE1 
2671 N NE2 . HIS A 337 ? 1.2806 0.8847 0.7695 -0.4032 0.1186  -0.0204 336 HIS A NE2 
2672 N N   . ARG A 338 ? 1.1902 0.6520 0.6915 -0.2767 0.1131  0.0226  337 ARG A N   
2673 C CA  . ARG A 338 ? 1.1417 0.6018 0.6649 -0.2467 0.1111  0.0308  337 ARG A CA  
2674 C C   . ARG A 338 ? 1.0821 0.5583 0.6261 -0.2399 0.1113  0.0140  337 ARG A C   
2675 O O   . ARG A 338 ? 1.2229 0.7265 0.7945 -0.2199 0.1041  0.0160  337 ARG A O   
2676 C CB  . ARG A 338 ? 1.1766 0.5767 0.6828 -0.2323 0.1232  0.0483  337 ARG A CB  
2677 C CG  . ARG A 338 ? 1.3517 0.7492 0.8835 -0.2008 0.1243  0.0575  337 ARG A CG  
2678 C CD  . ARG A 338 ? 1.7376 1.0679 1.2536 -0.1886 0.1446  0.0654  337 ARG A CD  
2679 N NE  . ARG A 338 ? 1.9929 1.3225 1.5332 -0.1645 0.1504  0.0630  337 ARG A NE  
2680 C CZ  . ARG A 338 ? 2.1721 1.4769 1.7031 -0.1698 0.1635  0.0435  337 ARG A CZ  
2681 N NH1 . ARG A 338 ? 2.2882 1.5680 1.7862 -0.1993 0.1709  0.0258  337 ARG A NH1 
2682 N NH2 . ARG A 338 ? 2.1457 1.4514 1.6990 -0.1476 0.1694  0.0424  337 ARG A NH2 
2683 N N   . GLU A 339 ? 1.1551 0.6156 0.6845 -0.2583 0.1188  -0.0016 338 GLU A N   
2684 C CA  . GLU A 339 ? 1.1826 0.6546 0.7268 -0.2542 0.1190  -0.0155 338 GLU A CA  
2685 C C   . GLU A 339 ? 1.1644 0.6987 0.7382 -0.2583 0.1062  -0.0260 338 GLU A C   
2686 O O   . GLU A 339 ? 1.2782 0.8333 0.8754 -0.2437 0.1019  -0.0306 338 GLU A O   
2687 C CB  . GLU A 339 ? 1.3183 0.7493 0.8323 -0.2752 0.1313  -0.0270 338 GLU A CB  
2688 C CG  . GLU A 339 ? 1.5631 0.9295 1.0560 -0.2629 0.1487  -0.0223 338 GLU A CG  
2689 C CD  . GLU A 339 ? 1.7642 1.0941 1.2268 -0.2853 0.1611  -0.0383 338 GLU A CD  
2690 O OE1 . GLU A 339 ? 1.8193 1.1825 1.2817 -0.3096 0.1525  -0.0508 338 GLU A OE1 
2691 O OE2 . GLU A 339 ? 1.7376 1.0062 1.1769 -0.2792 0.1803  -0.0377 338 GLU A OE2 
2692 N N   . GLN A 340 ? 1.1227 0.6847 0.6960 -0.2777 0.1021  -0.0297 339 GLN A N   
2693 C CA  . GLN A 340 ? 1.1334 0.7525 0.7379 -0.2786 0.0933  -0.0376 339 GLN A CA  
2694 C C   . GLN A 340 ? 1.0503 0.6907 0.6761 -0.2559 0.0867  -0.0313 339 GLN A C   
2695 O O   . GLN A 340 ? 1.1777 0.8510 0.8306 -0.2462 0.0815  -0.0375 339 GLN A O   
2696 C CB  . GLN A 340 ? 1.1227 0.7662 0.7245 -0.3012 0.0937  -0.0405 339 GLN A CB  
2697 C CG  . GLN A 340 ? 1.3796 1.0409 0.9849 -0.3233 0.0944  -0.0499 339 GLN A CG  
2698 C CD  . GLN A 340 ? 1.5484 1.2548 1.1908 -0.3152 0.0879  -0.0566 339 GLN A CD  
2699 O OE1 . GLN A 340 ? 1.5172 1.2251 1.1741 -0.2942 0.0844  -0.0569 339 GLN A OE1 
2700 N NE2 . GLN A 340 ? 1.6847 1.4291 1.3440 -0.3319 0.0866  -0.0604 339 GLN A NE2 
2701 N N   . MET A 341 ? 1.0257 0.6463 0.6377 -0.2491 0.0867  -0.0176 340 MET A N   
2702 C CA  . MET A 341 ? 1.0520 0.6934 0.6791 -0.2324 0.0789  -0.0088 340 MET A CA  
2703 C C   . MET A 341 ? 1.0545 0.6965 0.7018 -0.2097 0.0767  -0.0074 340 MET A C   
2704 O O   . MET A 341 ? 1.0901 0.7660 0.7603 -0.2010 0.0698  -0.0108 340 MET A O   
2705 C CB  . MET A 341 ? 1.2176 0.8369 0.8239 -0.2316 0.0780  0.0101  340 MET A CB  
2706 C CG  . MET A 341 ? 1.3482 0.9983 0.9515 -0.2431 0.0720  0.0120  340 MET A CG  
2707 S SD  . MET A 341 ? 1.2686 0.9445 0.8736 -0.2676 0.0780  -0.0085 340 MET A SD  
2708 C CE  . MET A 341 ? 1.7716 1.4866 1.3809 -0.2736 0.0738  -0.0103 340 MET A CE  
2709 N N   . GLN A 342 ? 1.0799 0.6819 0.7173 -0.2011 0.0845  -0.0030 341 GLN A N   
2710 C CA  . GLN A 342 ? 1.0622 0.6614 0.7175 -0.1805 0.0858  -0.0027 341 GLN A CA  
2711 C C   . GLN A 342 ? 1.0183 0.6475 0.6914 -0.1848 0.0824  -0.0199 341 GLN A C   
2712 O O   . GLN A 342 ? 0.9542 0.6054 0.6503 -0.1703 0.0778  -0.0208 341 GLN A O   
2713 C CB  . GLN A 342 ? 1.2002 0.7453 0.8371 -0.1751 0.1002  0.0005  341 GLN A CB  
2714 C CG  . GLN A 342 ? 1.3229 0.8346 0.9502 -0.1619 0.1058  0.0218  341 GLN A CG  
2715 C CD  . GLN A 342 ? 1.6105 1.0644 1.2225 -0.1534 0.1250  0.0230  341 GLN A CD  
2716 O OE1 . GLN A 342 ? 1.8192 1.2527 1.4409 -0.1302 0.1319  0.0403  341 GLN A OE1 
2717 N NE2 . GLN A 342 ? 1.5823 1.0103 1.1708 -0.1730 0.1347  0.0051  341 GLN A NE2 
2718 N N   . LYS A 343 ? 1.0357 0.6677 0.6993 -0.2053 0.0843  -0.0316 342 LYS A N   
2719 C CA  . LYS A 343 ? 0.9856 0.6484 0.6682 -0.2097 0.0804  -0.0441 342 LYS A CA  
2720 C C   . LYS A 343 ? 0.9550 0.6638 0.6657 -0.2034 0.0723  -0.0463 342 LYS A C   
2721 O O   . LYS A 343 ? 1.0570 0.7861 0.7893 -0.1937 0.0689  -0.0511 342 LYS A O   
2722 C CB  . LYS A 343 ? 1.0514 0.7143 0.7211 -0.2344 0.0826  -0.0521 342 LYS A CB  
2723 C CG  . LYS A 343 ? 1.2926 0.9392 0.9537 -0.2404 0.0857  -0.0590 342 LYS A CG  
2724 C CD  . LYS A 343 ? 1.5631 1.2088 1.2064 -0.2695 0.0868  -0.0643 342 LYS A CD  
2725 C CE  . LYS A 343 ? 1.6567 1.2459 1.2582 -0.2830 0.0984  -0.0637 342 LYS A CE  
2726 N NZ  . LYS A 343 ? 1.5960 1.1477 1.1749 -0.2875 0.1067  -0.0701 342 LYS A NZ  
2727 N N   . TYR A 344 ? 0.8242 0.5462 0.5318 -0.2103 0.0708  -0.0433 343 TYR A N   
2728 C CA  . TYR A 344 ? 0.7810 0.5395 0.5092 -0.2069 0.0667  -0.0471 343 TYR A CA  
2729 C C   . TYR A 344 ? 0.9382 0.7009 0.6751 -0.1897 0.0613  -0.0403 343 TYR A C   
2730 O O   . TYR A 344 ? 1.0919 0.8802 0.8478 -0.1843 0.0585  -0.0458 343 TYR A O   
2731 C CB  . TYR A 344 ? 0.7798 0.5488 0.4977 -0.2217 0.0689  -0.0470 343 TYR A CB  
2732 C CG  . TYR A 344 ? 0.9932 0.7788 0.7170 -0.2380 0.0744  -0.0558 343 TYR A CG  
2733 C CD1 . TYR A 344 ? 0.8743 0.6932 0.6271 -0.2364 0.0763  -0.0648 343 TYR A CD1 
2734 C CD2 . TYR A 344 ? 0.9942 0.7635 0.6965 -0.2552 0.0784  -0.0534 343 TYR A CD2 
2735 C CE1 . TYR A 344 ? 0.8955 0.7355 0.6603 -0.2498 0.0816  -0.0694 343 TYR A CE1 
2736 C CE2 . TYR A 344 ? 1.0116 0.8022 0.7227 -0.2714 0.0830  -0.0595 343 TYR A CE2 
2737 C CZ  . TYR A 344 ? 0.9876 0.8157 0.7320 -0.2678 0.0844  -0.0665 343 TYR A CZ  
2738 O OH  . TYR A 344 ? 0.9130 0.7669 0.6718 -0.2824 0.0892  -0.0692 343 TYR A OH  
2739 N N   . SER A 345 ? 0.9832 0.7215 0.7070 -0.1815 0.0604  -0.0269 344 SER A N   
2740 C CA  . SER A 345 ? 1.0083 0.7584 0.7431 -0.1672 0.0537  -0.0169 344 SER A CA  
2741 C C   . SER A 345 ? 1.0321 0.7865 0.7877 -0.1522 0.0540  -0.0215 344 SER A C   
2742 O O   . SER A 345 ? 0.9832 0.7617 0.7559 -0.1447 0.0484  -0.0211 344 SER A O   
2743 C CB  . SER A 345 ? 0.8900 0.6177 0.6104 -0.1609 0.0524  0.0031  344 SER A CB  
2744 O OG  . SER A 345 ? 1.1232 0.8167 0.8414 -0.1488 0.0602  0.0080  344 SER A OG  
2745 N N   . LEU A 346 ? 0.8577 0.5884 0.6087 -0.1511 0.0610  -0.0267 345 LEU A N   
2746 C CA  . LEU A 346 ? 0.8218 0.5538 0.5878 -0.1405 0.0628  -0.0325 345 LEU A CA  
2747 C C   . LEU A 346 ? 0.8950 0.6611 0.6809 -0.1437 0.0581  -0.0440 345 LEU A C   
2748 O O   . LEU A 346 ? 1.0106 0.7917 0.8139 -0.1328 0.0553  -0.0442 345 LEU A O   
2749 C CB  . LEU A 346 ? 0.7621 0.4603 0.5116 -0.1453 0.0721  -0.0377 345 LEU A CB  
2750 C CG  . LEU A 346 ? 0.8672 0.5718 0.6261 -0.1451 0.0731  -0.0483 345 LEU A CG  
2751 C CD1 . LEU A 346 ? 0.7398 0.4420 0.5125 -0.1260 0.0756  -0.0445 345 LEU A CD1 
2752 C CD2 . LEU A 346 ? 0.8315 0.5071 0.5663 -0.1605 0.0805  -0.0551 345 LEU A CD2 
2753 N N   . HIS A 347 ? 0.9088 0.6873 0.6939 -0.1581 0.0585  -0.0522 346 HIS A N   
2754 C CA  . HIS A 347 ? 0.8286 0.6370 0.6357 -0.1593 0.0568  -0.0613 346 HIS A CA  
2755 C C   . HIS A 347 ? 0.7744 0.6054 0.5908 -0.1589 0.0552  -0.0630 346 HIS A C   
2756 O O   . HIS A 347 ? 0.8956 0.7442 0.7301 -0.1545 0.0552  -0.0689 346 HIS A O   
2757 C CB  . HIS A 347 ? 0.7375 0.5546 0.5474 -0.1727 0.0592  -0.0671 346 HIS A CB  
2758 C CG  . HIS A 347 ? 0.8559 0.6541 0.6545 -0.1775 0.0598  -0.0671 346 HIS A CG  
2759 N ND1 . HIS A 347 ? 0.8977 0.6985 0.7058 -0.1721 0.0581  -0.0693 346 HIS A ND1 
2760 C CD2 . HIS A 347 ? 0.7632 0.5367 0.5376 -0.1900 0.0630  -0.0657 346 HIS A CD2 
2761 C CE1 . HIS A 347 ? 0.8771 0.6566 0.6658 -0.1822 0.0601  -0.0699 346 HIS A CE1 
2762 N NE2 . HIS A 347 ? 0.8408 0.6020 0.6085 -0.1933 0.0636  -0.0682 346 HIS A NE2 
2763 N N   . LEU A 348 ? 0.7436 0.5719 0.5446 -0.1655 0.0545  -0.0579 347 LEU A N   
2764 C CA  . LEU A 348 ? 0.6535 0.4989 0.4551 -0.1680 0.0523  -0.0584 347 LEU A CA  
2765 C C   . LEU A 348 ? 0.8500 0.7016 0.6630 -0.1551 0.0462  -0.0536 347 LEU A C   
2766 O O   . LEU A 348 ? 0.9699 0.8384 0.7942 -0.1551 0.0461  -0.0603 347 LEU A O   
2767 C CB  . LEU A 348 ? 0.6736 0.5120 0.4520 -0.1771 0.0499  -0.0490 347 LEU A CB  
2768 C CG  . LEU A 348 ? 0.8044 0.6502 0.5699 -0.1948 0.0557  -0.0554 347 LEU A CG  
2769 C CD1 . LEU A 348 ? 0.7057 0.5645 0.4884 -0.1989 0.0657  -0.0705 347 LEU A CD1 
2770 C CD2 . LEU A 348 ? 0.7367 0.5630 0.4794 -0.2029 0.0558  -0.0461 347 LEU A CD2 
2771 N N   . ASP A 349 ? 0.8333 0.6693 0.6436 -0.1442 0.0432  -0.0419 348 ASP A N   
2772 C CA  . ASP A 349 ? 0.7653 0.6077 0.5892 -0.1304 0.0388  -0.0346 348 ASP A CA  
2773 C C   . ASP A 349 ? 0.8258 0.6744 0.6677 -0.1239 0.0414  -0.0447 348 ASP A C   
2774 O O   . ASP A 349 ? 0.9281 0.7948 0.7826 -0.1210 0.0381  -0.0460 348 ASP A O   
2775 C CB  . ASP A 349 ? 0.8272 0.6459 0.6465 -0.1183 0.0403  -0.0204 348 ASP A CB  
2776 C CG  . ASP A 349 ? 0.9458 0.7767 0.7811 -0.1039 0.0356  -0.0069 348 ASP A CG  
2777 O OD1 . ASP A 349 ? 0.9957 0.8341 0.8282 -0.1029 0.0291  0.0098  348 ASP A OD1 
2778 O OD2 . ASP A 349 ? 0.9706 0.8060 0.8222 -0.0945 0.0381  -0.0113 348 ASP A OD2 
2779 N N   . MET A 350 ? 0.8989 0.7324 0.7399 -0.1235 0.0467  -0.0508 349 MET A N   
2780 C CA  . MET A 350 ? 0.8652 0.7023 0.7203 -0.1178 0.0484  -0.0575 349 MET A CA  
2781 C C   . MET A 350 ? 0.8382 0.6970 0.7066 -0.1233 0.0483  -0.0669 349 MET A C   
2782 O O   . MET A 350 ? 0.8029 0.6726 0.6848 -0.1181 0.0474  -0.0696 349 MET A O   
2783 C CB  . MET A 350 ? 0.8069 0.6240 0.6531 -0.1208 0.0530  -0.0606 349 MET A CB  
2784 C CG  . MET A 350 ? 0.7816 0.5936 0.6347 -0.1134 0.0551  -0.0628 349 MET A CG  
2785 S SD  . MET A 350 ? 0.9930 0.7718 0.8234 -0.1199 0.0621  -0.0646 349 MET A SD  
2786 C CE  . MET A 350 ? 0.7991 0.5958 0.6331 -0.1359 0.0575  -0.0710 349 MET A CE  
2787 N N   . SER A 351 ? 0.9096 0.7729 0.7744 -0.1338 0.0510  -0.0717 350 SER A N   
2788 C CA  . SER A 351 ? 0.8298 0.7101 0.7071 -0.1383 0.0552  -0.0803 350 SER A CA  
2789 C C   . SER A 351 ? 0.8108 0.7005 0.6892 -0.1381 0.0538  -0.0820 350 SER A C   
2790 O O   . SER A 351 ? 0.6841 0.5811 0.5759 -0.1354 0.0564  -0.0877 350 SER A O   
2791 C CB  . SER A 351 ? 0.7044 0.5874 0.5744 -0.1499 0.0605  -0.0835 350 SER A CB  
2792 O OG  . SER A 351 ? 1.0512 0.9428 0.9378 -0.1510 0.0657  -0.0874 350 SER A OG  
2793 N N   . ASN A 352 ? 0.7135 0.6036 0.5766 -0.1429 0.0492  -0.0757 351 ASN A N   
2794 C CA  . ASN A 352 ? 0.7380 0.6408 0.5988 -0.1474 0.0458  -0.0757 351 ASN A CA  
2795 C C   . ASN A 352 ? 0.7912 0.7002 0.6664 -0.1368 0.0410  -0.0717 351 ASN A C   
2796 O O   . ASN A 352 ? 0.7940 0.7128 0.6753 -0.1405 0.0423  -0.0781 351 ASN A O   
2797 C CB  . ASN A 352 ? 0.6958 0.6018 0.5374 -0.1557 0.0390  -0.0654 351 ASN A CB  
2798 C CG  . ASN A 352 ? 0.9684 0.8904 0.8015 -0.1688 0.0359  -0.0676 351 ASN A CG  
2799 O OD1 . ASN A 352 ? 1.1370 1.0726 0.9711 -0.1679 0.0256  -0.0557 351 ASN A OD1 
2800 N ND2 . ASN A 352 ? 1.0540 0.9754 0.8797 -0.1821 0.0462  -0.0827 351 ASN A ND2 
2801 N N   . ALA A 353 ? 0.5759 0.4767 0.4552 -0.1246 0.0377  -0.0619 352 ALA A N   
2802 C CA  . ALA A 353 ? 0.6319 0.5382 0.5257 -0.1138 0.0355  -0.0577 352 ALA A CA  
2803 C C   . ALA A 353 ? 0.6891 0.5968 0.5954 -0.1127 0.0404  -0.0689 352 ALA A C   
2804 O O   . ALA A 353 ? 0.6628 0.5823 0.5782 -0.1126 0.0391  -0.0702 352 ALA A O   
2805 C CB  . ALA A 353 ? 0.5511 0.4413 0.4455 -0.1008 0.0366  -0.0478 352 ALA A CB  
2806 N N   . ILE A 354 ? 0.6203 0.5175 0.5276 -0.1129 0.0455  -0.0753 353 ILE A N   
2807 C CA  . ILE A 354 ? 0.6700 0.5694 0.5904 -0.1118 0.0498  -0.0828 353 ILE A CA  
2808 C C   . ILE A 354 ? 0.7799 0.6883 0.7034 -0.1195 0.0538  -0.0907 353 ILE A C   
2809 O O   . ILE A 354 ? 0.8229 0.7349 0.7551 -0.1183 0.0552  -0.0937 353 ILE A O   
2810 C CB  . ILE A 354 ? 0.6256 0.5190 0.5488 -0.1128 0.0531  -0.0848 353 ILE A CB  
2811 C CG1 . ILE A 354 ? 0.7634 0.6442 0.6793 -0.1090 0.0506  -0.0794 353 ILE A CG1 
2812 C CG2 . ILE A 354 ? 0.6793 0.5780 0.6194 -0.1108 0.0570  -0.0887 353 ILE A CG2 
2813 C CD1 . ILE A 354 ? 0.8580 0.7374 0.7745 -0.1144 0.0513  -0.0797 353 ILE A CD1 
2814 N N   . ASN A 355 ? 0.7393 0.6486 0.6530 -0.1293 0.0575  -0.0951 354 ASN A N   
2815 C CA  . ASN A 355 ? 0.7492 0.6610 0.6605 -0.1394 0.0652  -0.1052 354 ASN A CA  
2816 C C   . ASN A 355 ? 0.7983 0.7189 0.7046 -0.1451 0.0599  -0.1045 354 ASN A C   
2817 O O   . ASN A 355 ? 0.9258 0.8446 0.8347 -0.1505 0.0666  -0.1129 354 ASN A O   
2818 C CB  . ASN A 355 ? 0.9243 0.8345 0.8203 -0.1515 0.0711  -0.1103 354 ASN A CB  
2819 C CG  . ASN A 355 ? 1.1966 1.1011 1.1041 -0.1513 0.0862  -0.1193 354 ASN A CG  
2820 O OD1 . ASN A 355 ? 0.9952 0.8999 0.9222 -0.1405 0.0876  -0.1160 354 ASN A OD1 
2821 N ND2 . ASN A 355 ? 1.4833 1.3839 1.3791 -0.1639 0.0983  -0.1298 354 ASN A ND2 
2822 N N   . MET A 356 ? 0.8024 0.7328 0.7030 -0.1440 0.0485  -0.0931 355 MET A N   
2823 C CA  . MET A 356 ? 0.8208 0.7675 0.7203 -0.1501 0.0412  -0.0884 355 MET A CA  
2824 C C   . MET A 356 ? 0.8738 0.8235 0.7912 -0.1399 0.0407  -0.0868 355 MET A C   
2825 O O   . MET A 356 ? 1.0203 0.9798 0.9390 -0.1483 0.0402  -0.0898 355 MET A O   
2826 C CB  . MET A 356 ? 0.9527 0.9130 0.8462 -0.1498 0.0292  -0.0723 355 MET A CB  
2827 C CG  . MET A 356 ? 1.0455 1.0105 0.9162 -0.1676 0.0268  -0.0724 355 MET A CG  
2828 S SD  . MET A 356 ? 1.8823 1.8674 1.7504 -0.1657 0.0105  -0.0475 355 MET A SD  
2829 C CE  . MET A 356 ? 2.3910 2.3741 2.2268 -0.1881 0.0099  -0.0500 355 MET A CE  
2830 N N   . ALA A 357 ? 0.7432 0.6836 0.6714 -0.1245 0.0415  -0.0826 356 ALA A N   
2831 C CA  . ALA A 357 ? 0.6445 0.5857 0.5869 -0.1158 0.0424  -0.0814 356 ALA A CA  
2832 C C   . ALA A 357 ? 0.7815 0.7142 0.7286 -0.1195 0.0505  -0.0926 356 ALA A C   
2833 O O   . ALA A 357 ? 0.7878 0.7229 0.7435 -0.1178 0.0516  -0.0931 356 ALA A O   
2834 C CB  . ALA A 357 ? 0.3815 0.3112 0.3278 -0.1018 0.0429  -0.0752 356 ALA A CB  
2835 N N   . PHE A 358 ? 0.7620 0.6844 0.7053 -0.1238 0.0576  -0.1004 357 PHE A N   
2836 C CA  . PHE A 358 ? 0.7832 0.6957 0.7344 -0.1248 0.0675  -0.1085 357 PHE A CA  
2837 C C   . PHE A 358 ? 0.8020 0.7149 0.7435 -0.1397 0.0728  -0.1174 357 PHE A C   
2838 O O   . PHE A 358 ? 0.8215 0.7242 0.7557 -0.1481 0.0835  -0.1270 357 PHE A O   
2839 C CB  . PHE A 358 ? 0.8258 0.7289 0.7829 -0.1213 0.0755  -0.1113 357 PHE A CB  
2840 C CG  . PHE A 358 ? 0.7881 0.6840 0.7625 -0.1135 0.0817  -0.1104 357 PHE A CG  
2841 C CD1 . PHE A 358 ? 0.7937 0.6916 0.7769 -0.1043 0.0753  -0.1013 357 PHE A CD1 
2842 C CD2 . PHE A 358 ? 1.0330 0.9182 1.0131 -0.1165 0.0948  -0.1178 357 PHE A CD2 
2843 C CE1 . PHE A 358 ? 0.8236 0.7179 0.8225 -0.0982 0.0789  -0.0971 357 PHE A CE1 
2844 C CE2 . PHE A 358 ? 0.9636 0.8417 0.9621 -0.1076 0.1006  -0.1135 357 PHE A CE2 
2845 C CZ  . PHE A 358 ? 0.7851 0.6703 0.7937 -0.0984 0.0911  -0.1018 357 PHE A CZ  
2846 N N   . SER A 359 ? 0.7651 0.6901 0.7058 -0.1444 0.0662  -0.1143 358 SER A N   
2847 C CA  . SER A 359 ? 0.7636 0.6913 0.6926 -0.1627 0.0694  -0.1220 358 SER A CA  
2848 C C   . SER A 359 ? 0.8313 0.7372 0.7631 -0.1655 0.0843  -0.1329 358 SER A C   
2849 O O   . SER A 359 ? 0.8162 0.7105 0.7636 -0.1511 0.0891  -0.1306 358 SER A O   
2850 C CB  . SER A 359 ? 0.7142 0.6653 0.6482 -0.1652 0.0579  -0.1128 358 SER A CB  
2851 O OG  . SER A 359 ? 0.7576 0.7055 0.7079 -0.1524 0.0590  -0.1092 358 SER A OG  
2852 N N   . SER A 360 ? 0.9199 0.8191 0.8351 -0.1855 0.0920  -0.1439 359 SER A N   
2853 C CA  . SER A 360 ? 0.9309 0.8057 0.8471 -0.1894 0.1077  -0.1537 359 SER A CA  
2854 C C   . SER A 360 ? 0.8310 0.7094 0.7650 -0.1778 0.1027  -0.1453 359 SER A C   
2855 O O   . SER A 360 ? 0.7116 0.5698 0.6570 -0.1683 0.1131  -0.1459 359 SER A O   
2856 C CB  . SER A 360 ? 0.9619 0.8299 0.8521 -0.2175 0.1151  -0.1668 359 SER A CB  
2857 O OG  . SER A 360 ? 1.1640 1.0612 1.0496 -0.2297 0.0987  -0.1596 359 SER A OG  
2858 N N   . THR A 361 ? 0.6036 0.5082 0.5412 -0.1783 0.0878  -0.1359 360 THR A N   
2859 C CA  . THR A 361 ? 0.6819 0.5898 0.6348 -0.1678 0.0848  -0.1285 360 THR A CA  
2860 C C   . THR A 361 ? 0.7698 0.6655 0.7373 -0.1470 0.0866  -0.1224 360 THR A C   
2861 O O   . THR A 361 ? 0.7648 0.6443 0.7396 -0.1422 0.0939  -0.1220 360 THR A O   
2862 C CB  . THR A 361 ? 0.7817 0.7209 0.7414 -0.1664 0.0707  -0.1176 360 THR A CB  
2863 O OG1 . THR A 361 ? 0.9936 0.9513 0.9423 -0.1876 0.0663  -0.1198 360 THR A OG1 
2864 C CG2 . THR A 361 ? 0.6726 0.6127 0.6458 -0.1571 0.0709  -0.1117 360 THR A CG2 
2865 N N   . ILE A 362 ? 0.6734 0.5777 0.6438 -0.1366 0.0794  -0.1162 361 ILE A N   
2866 C CA  . ILE A 362 ? 0.7483 0.6454 0.7290 -0.1212 0.0788  -0.1096 361 ILE A CA  
2867 C C   . ILE A 362 ? 0.7611 0.6394 0.7492 -0.1177 0.0901  -0.1125 361 ILE A C   
2868 O O   . ILE A 362 ? 0.8042 0.6768 0.8038 -0.1083 0.0906  -0.1052 361 ILE A O   
2869 C CB  . ILE A 362 ? 0.7788 0.6851 0.7565 -0.1152 0.0709  -0.1046 361 ILE A CB  
2870 C CG1 . ILE A 362 ? 0.5947 0.5182 0.5702 -0.1149 0.0621  -0.0987 361 ILE A CG1 
2871 C CG2 . ILE A 362 ? 0.6271 0.5270 0.6117 -0.1042 0.0696  -0.0983 361 ILE A CG2 
2872 C CD1 . ILE A 362 ? 0.4122 0.3378 0.3951 -0.1078 0.0609  -0.0929 361 ILE A CD1 
2873 N N   . ASP A 363 ? 0.7175 0.5869 0.6991 -0.1257 0.0999  -0.1221 362 ASP A N   
2874 C CA  . ASP A 363 ? 0.7825 0.6315 0.7734 -0.1222 0.1160  -0.1259 362 ASP A CA  
2875 C C   . ASP A 363 ? 0.8167 0.6490 0.8146 -0.1211 0.1242  -0.1247 362 ASP A C   
2876 O O   . ASP A 363 ? 0.8788 0.7033 0.8949 -0.1086 0.1286  -0.1157 362 ASP A O   
2877 C CB  . ASP A 363 ? 0.9754 0.8143 0.9516 -0.1351 0.1284  -0.1396 362 ASP A CB  
2878 C CG  . ASP A 363 ? 1.3460 1.1658 1.3354 -0.1279 0.1477  -0.1428 362 ASP A CG  
2879 O OD1 . ASP A 363 ? 1.5465 1.3548 1.5551 -0.1164 0.1551  -0.1359 362 ASP A OD1 
2880 O OD2 . ASP A 363 ? 1.5079 1.3246 1.4892 -0.1336 0.1566  -0.1510 362 ASP A OD2 
2881 N N   . SER A 364 ? 0.9035 0.7321 0.8875 -0.1352 0.1255  -0.1320 363 SER A N   
2882 C CA  . SER A 364 ? 0.7391 0.5535 0.7265 -0.1364 0.1310  -0.1301 363 SER A CA  
2883 C C   . SER A 364 ? 0.8503 0.6730 0.8527 -0.1220 0.1209  -0.1148 363 SER A C   
2884 O O   . SER A 364 ? 0.9114 0.7183 0.9259 -0.1141 0.1281  -0.1077 363 SER A O   
2885 C CB  . SER A 364 ? 0.8009 0.6230 0.7715 -0.1552 0.1271  -0.1370 363 SER A CB  
2886 O OG  . SER A 364 ? 1.0171 0.8290 0.9683 -0.1742 0.1369  -0.1515 363 SER A OG  
2887 N N   . CYS A 365 ? 0.7701 0.6159 0.7705 -0.1196 0.1056  -0.1091 364 CYS A N   
2888 C CA  . CYS A 365 ? 0.7506 0.6027 0.7588 -0.1095 0.0971  -0.0964 364 CYS A CA  
2889 C C   . CYS A 365 ? 0.7351 0.5829 0.7570 -0.0978 0.0977  -0.0868 364 CYS A C   
2890 O O   . CYS A 365 ? 0.7707 0.6141 0.8009 -0.0923 0.0965  -0.0756 364 CYS A O   
2891 C CB  . CYS A 365 ? 0.5507 0.4229 0.5529 -0.1081 0.0849  -0.0936 364 CYS A CB  
2892 S SG  . CYS A 365 ? 0.9125 0.8010 0.9076 -0.1180 0.0816  -0.0979 364 CYS A SG  
2893 N N   . THR A 366 ? 0.7245 0.5768 0.7492 -0.0951 0.0986  -0.0896 365 THR A N   
2894 C CA  . THR A 366 ? 0.6778 0.5327 0.7190 -0.0850 0.0987  -0.0793 365 THR A CA  
2895 C C   . THR A 366 ? 0.7217 0.5601 0.7816 -0.0782 0.1125  -0.0739 365 THR A C   
2896 O O   . THR A 366 ? 0.7312 0.5738 0.8075 -0.0697 0.1089  -0.0577 365 THR A O   
2897 C CB  . THR A 366 ? 0.7398 0.6042 0.7798 -0.0850 0.0979  -0.0839 365 THR A CB  
2898 O OG1 . THR A 366 ? 0.7363 0.6124 0.7600 -0.0894 0.0859  -0.0860 365 THR A OG1 
2899 C CG2 . THR A 366 ? 0.8238 0.6975 0.8834 -0.0761 0.0964  -0.0712 365 THR A CG2 
2900 N N   . LYS A 367 ? 0.7473 0.5661 0.8040 -0.0829 0.1289  -0.0863 366 LYS A N   
2901 C CA  . LYS A 367 ? 0.7809 0.5763 0.8542 -0.0758 0.1465  -0.0822 366 LYS A CA  
2902 C C   . LYS A 367 ? 0.7731 0.5626 0.8516 -0.0725 0.1422  -0.0689 366 LYS A C   
2903 O O   . LYS A 367 ? 0.7871 0.5736 0.8886 -0.0599 0.1454  -0.0519 366 LYS A O   
2904 C CB  . LYS A 367 ? 0.8679 0.6364 0.9269 -0.0868 0.1665  -0.1012 366 LYS A CB  
2905 C CG  . LYS A 367 ? 1.1934 0.9620 1.2474 -0.0907 0.1760  -0.1137 366 LYS A CG  
2906 C CD  . LYS A 367 ? 1.4945 1.2342 1.5258 -0.1075 0.1955  -0.1341 366 LYS A CD  
2907 C CE  . LYS A 367 ? 1.6008 1.3056 1.6393 -0.1043 0.2152  -0.1330 366 LYS A CE  
2908 N NZ  . LYS A 367 ? 1.6278 1.3071 1.6346 -0.1280 0.2269  -0.1524 366 LYS A NZ  
2909 N N   . ALA A 368 ? 0.6987 0.4888 0.7570 -0.0840 0.1348  -0.0750 367 ALA A N   
2910 C CA  . ALA A 368 ? 0.6747 0.4594 0.7327 -0.0842 0.1306  -0.0641 367 ALA A CA  
2911 C C   . ALA A 368 ? 0.7582 0.5628 0.8260 -0.0758 0.1149  -0.0448 367 ALA A C   
2912 O O   . ALA A 368 ? 0.7928 0.5914 0.8729 -0.0695 0.1150  -0.0281 367 ALA A O   
2913 C CB  . ALA A 368 ? 0.6874 0.4757 0.7235 -0.0989 0.1256  -0.0748 367 ALA A CB  
2914 N N   . GLU A 369 ? 0.6700 0.4969 0.7301 -0.0776 0.1018  -0.0466 368 GLU A N   
2915 C CA  . GLU A 369 ? 0.6715 0.5165 0.7345 -0.0745 0.0872  -0.0309 368 GLU A CA  
2916 C C   . GLU A 369 ? 0.8114 0.6624 0.9015 -0.0633 0.0880  -0.0128 368 GLU A C   
2917 O O   . GLU A 369 ? 0.7966 0.6553 0.8937 -0.0616 0.0794  0.0065  368 GLU A O   
2918 C CB  . GLU A 369 ? 0.6150 0.4764 0.6634 -0.0792 0.0772  -0.0385 368 GLU A CB  
2919 C CG  . GLU A 369 ? 0.7573 0.6193 0.7839 -0.0875 0.0737  -0.0485 368 GLU A CG  
2920 C CD  . GLU A 369 ? 0.8923 0.7652 0.9076 -0.0893 0.0681  -0.0563 368 GLU A CD  
2921 O OE1 . GLU A 369 ? 0.7739 0.6535 0.7943 -0.0865 0.0650  -0.0536 368 GLU A OE1 
2922 O OE2 . GLU A 369 ? 1.1080 0.9830 1.1110 -0.0931 0.0677  -0.0637 368 GLU A OE2 
2923 N N   . GLN A 370 ? 0.6527 0.5022 0.7589 -0.0564 0.0987  -0.0177 369 GLN A N   
2924 C CA  . GLN A 370 ? 0.7359 0.5944 0.8747 -0.0436 0.1023  0.0006  369 GLN A CA  
2925 C C   . GLN A 370 ? 0.8612 0.7029 1.0199 -0.0340 0.1121  0.0163  369 GLN A C   
2926 O O   . GLN A 370 ? 0.7917 0.6492 0.9738 -0.0258 0.1049  0.0416  369 GLN A O   
2927 C CB  . GLN A 370 ? 0.7463 0.6039 0.8980 -0.0383 0.1163  -0.0100 369 GLN A CB  
2928 C CG  . GLN A 370 ? 0.6972 0.5743 0.8348 -0.0458 0.1057  -0.0192 369 GLN A CG  
2929 C CD  . GLN A 370 ? 0.6566 0.5621 0.7981 -0.0478 0.0860  -0.0015 369 GLN A CD  
2930 O OE1 . GLN A 370 ? 0.6666 0.5913 0.8364 -0.0402 0.0844  0.0164  369 GLN A OE1 
2931 N NE2 . GLN A 370 ? 0.5701 0.4789 0.6834 -0.0590 0.0721  -0.0060 369 GLN A NE2 
2932 N N   . ASN A 371 ? 0.8174 0.6276 0.9665 -0.0364 0.1284  0.0027  370 ASN A N   
2933 C CA  . ASN A 371 ? 0.7606 0.5467 0.9243 -0.0284 0.1406  0.0156  370 ASN A CA  
2934 C C   . ASN A 371 ? 0.8162 0.6117 0.9749 -0.0315 0.1237  0.0355  370 ASN A C   
2935 O O   . ASN A 371 ? 0.9999 0.7968 1.1824 -0.0208 0.1232  0.0609  370 ASN A O   
2936 C CB  . ASN A 371 ? 0.8402 0.5891 0.9849 -0.0369 0.1600  -0.0062 370 ASN A CB  
2937 C CG  . ASN A 371 ? 1.0010 0.7314 1.1508 -0.0344 0.1826  -0.0234 370 ASN A CG  
2938 O OD1 . ASN A 371 ? 1.0970 0.8394 1.2716 -0.0220 0.1877  -0.0165 370 ASN A OD1 
2939 N ND2 . ASN A 371 ? 0.9592 0.6608 1.0839 -0.0484 0.1970  -0.0460 370 ASN A ND2 
2940 N N   . ILE A 372 ? 0.7947 0.5968 0.9225 -0.0465 0.1108  0.0249  371 ILE A N   
2941 C CA  . ILE A 372 ? 0.8647 0.6738 0.9805 -0.0532 0.0964  0.0400  371 ILE A CA  
2942 C C   . ILE A 372 ? 0.8330 0.6727 0.9606 -0.0506 0.0783  0.0641  371 ILE A C   
2943 O O   . ILE A 372 ? 0.8540 0.6986 0.9865 -0.0506 0.0698  0.0876  371 ILE A O   
2944 C CB  . ILE A 372 ? 0.7692 0.5821 0.8513 -0.0690 0.0888  0.0220  371 ILE A CB  
2945 C CG1 . ILE A 372 ? 0.7273 0.5166 0.7972 -0.0755 0.1035  0.0014  371 ILE A CG1 
2946 C CG2 . ILE A 372 ? 0.6986 0.5200 0.7651 -0.0776 0.0752  0.0362  371 ILE A CG2 
2947 C CD1 . ILE A 372 ? 0.8658 0.6662 0.9114 -0.0877 0.0974  -0.0163 371 ILE A CD1 
2948 N N   . VAL A 373 ? 0.8653 0.7265 0.9956 -0.0507 0.0718  0.0588  372 VAL A N   
2949 C CA  . VAL A 373 ? 0.7991 0.6919 0.9312 -0.0554 0.0526  0.0767  372 VAL A CA  
2950 C C   . VAL A 373 ? 0.8447 0.7569 1.0185 -0.0414 0.0512  0.1047  372 VAL A C   
2951 O O   . VAL A 373 ? 0.8990 0.8365 1.0785 -0.0460 0.0342  0.1300  372 VAL A O   
2952 C CB  . VAL A 373 ? 0.6106 0.5156 0.7213 -0.0652 0.0460  0.0575  372 VAL A CB  
2953 C CG1 . VAL A 373 ? 0.6680 0.5982 0.8005 -0.0606 0.0413  0.0661  372 VAL A CG1 
2954 C CG2 . VAL A 373 ? 0.5505 0.4595 0.6262 -0.0819 0.0328  0.0553  372 VAL A CG2 
2955 N N   . THR A 374 ? 0.7062 0.6072 0.9095 -0.0253 0.0701  0.1015  373 THR A N   
2956 C CA  . THR A 374 ? 0.6165 0.5348 0.8664 -0.0082 0.0735  0.1294  373 THR A CA  
2957 C C   . THR A 374 ? 0.8261 0.7182 1.0951 0.0049  0.0871  0.1452  373 THR A C   
2958 O O   . THR A 374 ? 0.8745 0.7800 1.1843 0.0207  0.0887  0.1757  373 THR A O   
2959 C CB  . THR A 374 ? 0.7238 0.6431 0.9983 0.0037  0.0909  0.1180  373 THR A CB  
2960 O OG1 . THR A 374 ? 0.7875 0.6645 1.0589 0.0103  0.1173  0.0971  373 THR A OG1 
2961 C CG2 . THR A 374 ? 0.7440 0.6807 0.9950 -0.0099 0.0808  0.0984  373 THR A CG2 
2962 N N   . GLU A 375 ? 0.8642 0.7194 1.1053 -0.0016 0.0977  0.1254  374 GLU A N   
2963 C CA  . GLU A 375 ? 0.9182 0.7414 1.1693 0.0071  0.1117  0.1373  374 GLU A CA  
2964 C C   . GLU A 375 ? 1.0696 0.8676 1.3574 0.0283  0.1409  0.1392  374 GLU A C   
2965 O O   . GLU A 375 ? 1.1951 0.9686 1.5019 0.0405  0.1541  0.1569  374 GLU A O   
2966 C CB  . GLU A 375 ? 0.8214 0.6638 1.0800 0.0063  0.0924  0.1732  374 GLU A CB  
2967 C CG  . GLU A 375 ? 1.0387 0.8959 1.2541 -0.0174 0.0689  0.1684  374 GLU A CG  
2968 C CD  . GLU A 375 ? 1.1867 1.0519 1.3991 -0.0227 0.0535  0.2004  374 GLU A CD  
2969 O OE1 . GLU A 375 ? 1.2193 1.0796 1.4653 -0.0067 0.0591  0.2294  374 GLU A OE1 
2970 O OE2 . GLU A 375 ? 1.2242 1.0994 1.3995 -0.0432 0.0367  0.1969  374 GLU A OE2 
2971 N N   . GLU A 376 ? 0.9803 0.7809 1.2760 0.0322  0.1531  0.1205  375 GLU A N   
2972 C CA  . GLU A 376 ? 1.0864 0.8530 1.4041 0.0472  0.1866  0.1114  375 GLU A CA  
2973 C C   . GLU A 376 ? 1.1475 0.9037 1.4391 0.0355  0.1972  0.0740  375 GLU A C   
2974 O O   . GLU A 376 ? 1.1620 0.9439 1.4294 0.0211  0.1772  0.0620  375 GLU A O   
2975 C CB  . GLU A 376 ? 1.2092 0.9977 1.5842 0.0719  0.1944  0.1416  375 GLU A CB  
2976 C CG  . GLU A 376 ? 1.3057 1.1408 1.6960 0.0719  0.1819  0.1430  375 GLU A CG  
2977 C CD  . GLU A 376 ? 1.4605 1.3221 1.9131 0.0967  0.1907  0.1752  375 GLU A CD  
2978 O OE1 . GLU A 376 ? 1.5081 1.3615 1.9934 0.1141  0.1979  0.2046  375 GLU A OE1 
2979 O OE2 . GLU A 376 ? 1.5088 1.4008 1.9796 0.0992  0.1907  0.1728  375 GLU A OE2 
2980 N N   . GLU A 377 ? 1.2297 0.9463 1.5238 0.0404  0.2292  0.0562  376 GLU A N   
2981 C CA  . GLU A 377 ? 1.3229 1.0285 1.5905 0.0272  0.2405  0.0221  376 GLU A CA  
2982 C C   . GLU A 377 ? 1.4012 1.1299 1.6988 0.0393  0.2486  0.0250  376 GLU A C   
2983 O O   . GLU A 377 ? 1.5606 1.3169 1.9014 0.0577  0.2443  0.0541  376 GLU A O   
2984 C CB  . GLU A 377 ? 1.3749 1.0239 1.6225 0.0206  0.2723  -0.0012 376 GLU A CB  
2985 C CG  . GLU A 377 ? 1.4900 1.1135 1.7073 0.0062  0.2680  -0.0062 376 GLU A CG  
2986 C CD  . GLU A 377 ? 1.7315 1.2967 1.9283 -0.0030 0.3014  -0.0288 376 GLU A CD  
2987 O OE1 . GLU A 377 ? 1.7871 1.3333 1.9827 -0.0034 0.3257  -0.0469 376 GLU A OE1 
2988 O OE2 . GLU A 377 ? 1.8073 1.3445 1.9866 -0.0118 0.3046  -0.0291 376 GLU A OE2 
2989 N N   . GLN A 378 ? 1.2761 0.9964 1.5515 0.0279  0.2596  -0.0034 377 GLN A N   
2990 C CA  . GLN A 378 ? 1.1964 0.9306 1.4992 0.0388  0.2745  -0.0035 377 GLN A CA  
2991 C C   . GLN A 378 ? 1.2995 1.0123 1.6484 0.0637  0.3050  0.0141  377 GLN A C   
2992 O O   . GLN A 378 ? 1.2479 0.9929 1.6443 0.0830  0.3048  0.0391  377 GLN A O   
2993 C CB  . GLN A 378 ? 1.2347 0.9469 1.5029 0.0219  0.2914  -0.0384 377 GLN A CB  
2994 C CG  . GLN A 378 ? 1.4822 1.1985 1.7002 -0.0035 0.2696  -0.0589 377 GLN A CG  
2995 C CD  . GLN A 378 ? 1.6465 1.3457 1.8320 -0.0212 0.2847  -0.0892 377 GLN A CD  
2996 O OE1 . GLN A 378 ? 1.6291 1.3079 1.8252 -0.0162 0.3142  -0.0981 377 GLN A OE1 
2997 N NE2 . GLN A 378 ? 1.7037 1.4117 1.8496 -0.0424 0.2652  -0.1042 377 GLN A NE2 
2998 N N   . ASP A 379 ? 1.4318 1.0900 1.7666 0.0624  0.3319  0.0016  378 ASP A N   
2999 C CA  . ASP A 379 ? 1.4898 1.1133 1.8633 0.0860  0.3666  0.0159  378 ASP A CA  
3000 C C   . ASP A 379 ? 1.4136 1.0717 1.8427 0.1118  0.3532  0.0608  378 ASP A C   
3001 O O   . ASP A 379 ? 1.4785 1.1441 1.9604 0.1372  0.3735  0.0811  378 ASP A O   
3002 C CB  . ASP A 379 ? 1.6224 1.1850 1.9645 0.0761  0.3858  0.0014  378 ASP A CB  
3003 C CG  . ASP A 379 ? 1.7746 1.2989 2.0629 0.0487  0.4037  -0.0413 378 ASP A CG  
3004 O OD1 . ASP A 379 ? 1.8208 1.3704 2.0722 0.0260  0.3779  -0.0581 378 ASP A OD1 
3005 O OD2 . ASP A 379 ? 1.7444 1.2126 2.0266 0.0492  0.4441  -0.0570 378 ASP A OD2 
3006 N N   . GLY A 380 ? 1.2358 0.9159 1.6528 0.1044  0.3194  0.0770  379 GLY A N   
3007 C CA  . GLY A 380 ? 1.0988 0.8089 1.5594 0.1234  0.3034  0.1206  379 GLY A CA  
3008 C C   . GLY A 380 ? 1.1277 0.7988 1.5733 0.1220  0.3062  0.1282  379 GLY A C   
3009 O O   . GLY A 380 ? 1.0251 0.7157 1.4961 0.1330  0.2899  0.1642  379 GLY A O   
3010 N N   . ASN A 381 ? 1.2590 0.8758 1.6613 0.1062  0.3263  0.0950  380 ASN A N   
3011 C CA  . ASN A 381 ? 1.4417 1.0186 1.8222 0.0996  0.3294  0.0974  380 ASN A CA  
3012 C C   . ASN A 381 ? 1.4553 1.0664 1.8122 0.0841  0.2886  0.1087  380 ASN A C   
3013 O O   . ASN A 381 ? 1.4808 1.1069 1.7972 0.0611  0.2698  0.0851  380 ASN A O   
3014 C CB  . ASN A 381 ? 1.5491 1.0668 1.8830 0.0794  0.3565  0.0570  380 ASN A CB  
3015 C CG  . ASN A 381 ? 1.7864 1.2427 2.1395 0.0955  0.4032  0.0559  380 ASN A CG  
3016 O OD1 . ASN A 381 ? 1.7845 1.2452 2.1882 0.1233  0.4223  0.0759  380 ASN A OD1 
3017 N ND2 . ASN A 381 ? 1.8680 1.2657 2.1813 0.0777  0.4237  0.0330  380 ASN A ND2 
3018 N N   . LYS A 382 ? 1.4100 1.0332 1.7928 0.0969  0.2763  0.1461  381 LYS A N   
3019 C CA  . LYS A 382 ? 1.3038 0.9587 1.6643 0.0819  0.2397  0.1592  381 LYS A CA  
3020 C C   . LYS A 382 ? 1.2911 0.9179 1.5944 0.0546  0.2378  0.1259  381 LYS A C   
3021 O O   . LYS A 382 ? 1.3388 0.9137 1.6259 0.0502  0.2645  0.1073  381 LYS A O   
3022 C CB  . LYS A 382 ? 1.2560 0.9128 1.6464 0.0972  0.2335  0.2028  381 LYS A CB  
3023 C CG  . LYS A 382 ? 1.3371 1.0454 1.7207 0.0867  0.1928  0.2282  381 LYS A CG  
3024 C CD  . LYS A 382 ? 1.4612 1.1639 1.8637 0.0965  0.1871  0.2691  381 LYS A CD  
3025 C CE  . LYS A 382 ? 1.5313 1.2751 1.9092 0.0771  0.1484  0.2866  381 LYS A CE  
3026 N NZ  . LYS A 382 ? 1.6103 1.3396 1.9910 0.0795  0.1434  0.3200  381 LYS A NZ  
3027 N N   . VAL A 383 ? 1.2026 0.8639 1.4760 0.0356  0.2081  0.1182  382 VAL A N   
3028 C CA  . VAL A 383 ? 1.2038 0.8484 1.4290 0.0109  0.2035  0.0917  382 VAL A CA  
3029 C C   . VAL A 383 ? 1.1670 0.8199 1.3792 0.0030  0.1837  0.1119  382 VAL A C   
3030 O O   . VAL A 383 ? 1.1586 0.8511 1.3792 0.0045  0.1590  0.1346  382 VAL A O   
3031 C CB  . VAL A 383 ? 0.9936 0.6649 1.1916 -0.0054 0.1900  0.0635  382 VAL A CB  
3032 C CG1 . VAL A 383 ? 0.9848 0.6931 1.2076 0.0056  0.1813  0.0711  382 VAL A CG1 
3033 C CG2 . VAL A 383 ? 0.9506 0.6421 1.1162 -0.0242 0.1655  0.0603  382 VAL A CG2 
3034 N N   . ARG A 384 ? 1.1730 0.7879 1.3619 -0.0079 0.1952  0.1032  383 ARG A N   
3035 C CA  . ARG A 384 ? 1.3213 0.9357 1.4991 -0.0146 0.1819  0.1242  383 ARG A CA  
3036 C C   . ARG A 384 ? 1.2695 0.8800 1.4034 -0.0404 0.1755  0.1001  383 ARG A C   
3037 O O   . ARG A 384 ? 1.2922 0.9227 1.4095 -0.0511 0.1560  0.1107  383 ARG A O   
3038 C CB  . ARG A 384 ? 1.4688 1.0396 1.6660 -0.0010 0.2030  0.1454  383 ARG A CB  
3039 C CG  . ARG A 384 ? 1.6350 1.2142 1.8838 0.0280  0.2089  0.1778  383 ARG A CG  
3040 C CD  . ARG A 384 ? 1.8946 1.4197 2.1634 0.0438  0.2383  0.1935  383 ARG A CD  
3041 N NE  . ARG A 384 ? 2.0687 1.5447 2.3311 0.0440  0.2737  0.1619  383 ARG A NE  
3042 C CZ  . ARG A 384 ? 2.1086 1.5659 2.4071 0.0667  0.3003  0.1656  383 ARG A CZ  
3043 N NH1 . ARG A 384 ? 2.0602 1.5480 2.4099 0.0936  0.2947  0.2022  383 ARG A NH1 
3044 N NH2 . ARG A 384 ? 2.1123 1.5211 2.3953 0.0613  0.3335  0.1331  383 ARG A NH2 
3045 N N   . ASP A 385 ? 1.1827 0.7689 1.2978 -0.0518 0.1925  0.0685  384 ASP A N   
3046 C CA  . ASP A 385 ? 1.2132 0.8033 1.2924 -0.0760 0.1865  0.0460  384 ASP A CA  
3047 C C   . ASP A 385 ? 1.1635 0.7955 1.2336 -0.0821 0.1691  0.0302  384 ASP A C   
3048 O O   . ASP A 385 ? 1.0972 0.7291 1.1602 -0.0877 0.1763  0.0063  384 ASP A O   
3049 C CB  . ASP A 385 ? 1.2745 0.8226 1.3359 -0.0896 0.2109  0.0215  384 ASP A CB  
3050 C CG  . ASP A 385 ? 1.4056 0.9614 1.4347 -0.1153 0.2046  0.0032  384 ASP A CG  
3051 O OD1 . ASP A 385 ? 1.4500 1.0372 1.4713 -0.1203 0.1848  0.0109  384 ASP A OD1 
3052 O OD2 . ASP A 385 ? 1.4772 1.0082 1.4884 -0.1318 0.2206  -0.0189 384 ASP A OD2 
3053 N N   . PHE A 386 ? 1.1112 0.7769 1.1793 -0.0820 0.1470  0.0444  385 PHE A N   
3054 C CA  . PHE A 386 ? 0.9664 0.6676 1.0251 -0.0869 0.1318  0.0318  385 PHE A CA  
3055 C C   . PHE A 386 ? 0.9404 0.6436 0.9744 -0.1044 0.1339  0.0066  385 PHE A C   
3056 O O   . PHE A 386 ? 1.0406 0.7599 1.0708 -0.1069 0.1315  -0.0104 385 PHE A O   
3057 C CB  . PHE A 386 ? 0.9312 0.6614 0.9869 -0.0872 0.1106  0.0514  385 PHE A CB  
3058 C CG  . PHE A 386 ? 0.9790 0.7181 1.0623 -0.0716 0.1046  0.0794  385 PHE A CG  
3059 C CD1 . PHE A 386 ? 0.9690 0.7224 1.0748 -0.0591 0.1049  0.0792  385 PHE A CD1 
3060 C CD2 . PHE A 386 ? 0.9427 0.6779 1.0310 -0.0698 0.0988  0.1078  385 PHE A CD2 
3061 C CE1 . PHE A 386 ? 0.9988 0.7661 1.1353 -0.0445 0.0996  0.1073  385 PHE A CE1 
3062 C CE2 . PHE A 386 ? 0.7698 0.5189 0.8879 -0.0552 0.0920  0.1375  385 PHE A CE2 
3063 C CZ  . PHE A 386 ? 0.8843 0.6512 1.0284 -0.0422 0.0924  0.1375  385 PHE A CZ  
3064 N N   . ILE A 387 ? 1.1465 0.8344 1.1653 -0.1168 0.1387  0.0058  386 ILE A N   
3065 C CA  . ILE A 387 ? 1.1173 0.8120 1.1169 -0.1342 0.1408  -0.0152 386 ILE A CA  
3066 C C   . ILE A 387 ? 1.0746 0.7545 1.0728 -0.1405 0.1548  -0.0359 386 ILE A C   
3067 O O   . ILE A 387 ? 1.1544 0.8537 1.1436 -0.1510 0.1517  -0.0527 386 ILE A O   
3068 C CB  . ILE A 387 ? 1.0708 0.7550 1.0553 -0.1478 0.1432  -0.0102 386 ILE A CB  
3069 C CG1 . ILE A 387 ? 1.1061 0.8063 1.0867 -0.1447 0.1288  0.0093  386 ILE A CG1 
3070 C CG2 . ILE A 387 ? 1.1075 0.8069 1.0777 -0.1655 0.1446  -0.0298 386 ILE A CG2 
3071 C CD1 . ILE A 387 ? 1.1423 0.8486 1.1029 -0.1608 0.1277  0.0078  386 ILE A CD1 
3072 N N   . GLY A 388 ? 0.9414 0.5867 0.9481 -0.1344 0.1711  -0.0339 387 GLY A N   
3073 C CA  . GLY A 388 ? 0.8146 0.4409 0.8156 -0.1422 0.1869  -0.0545 387 GLY A CA  
3074 C C   . GLY A 388 ? 0.9976 0.6471 1.0057 -0.1353 0.1812  -0.0638 387 GLY A C   
3075 O O   . GLY A 388 ? 1.2213 0.8742 1.2162 -0.1489 0.1851  -0.0836 387 GLY A O   
3076 N N   . GLU A 389 ? 0.8222 0.4888 0.8495 -0.1163 0.1712  -0.0485 388 GLU A N   
3077 C CA  . GLU A 389 ? 0.9132 0.6026 0.9479 -0.1092 0.1649  -0.0549 388 GLU A CA  
3078 C C   . GLU A 389 ? 0.9443 0.6645 0.9633 -0.1211 0.1512  -0.0678 388 GLU A C   
3079 O O   . GLU A 389 ? 1.0905 0.8205 1.1051 -0.1249 0.1514  -0.0813 388 GLU A O   
3080 C CB  . GLU A 389 ? 1.0021 0.7106 1.0580 -0.0908 0.1529  -0.0338 388 GLU A CB  
3081 C CG  . GLU A 389 ? 1.2488 0.9391 1.3308 -0.0739 0.1668  -0.0227 388 GLU A CG  
3082 C CD  . GLU A 389 ? 1.3440 1.0209 1.4260 -0.0748 0.1837  -0.0422 388 GLU A CD  
3083 O OE1 . GLU A 389 ? 1.3011 0.9975 1.3692 -0.0838 0.1761  -0.0581 388 GLU A OE1 
3084 O OE2 . GLU A 389 ? 1.4932 1.1381 1.5883 -0.0667 0.2059  -0.0410 388 GLU A OE2 
3085 N N   . VAL A 390 ? 0.9048 0.6398 0.9161 -0.1265 0.1403  -0.0620 389 VAL A N   
3086 C CA  . VAL A 390 ? 0.7728 0.5382 0.7746 -0.1337 0.1283  -0.0693 389 VAL A CA  
3087 C C   . VAL A 390 ? 0.8039 0.5712 0.7931 -0.1522 0.1338  -0.0852 389 VAL A C   
3088 O O   . VAL A 390 ? 0.9706 0.7631 0.9566 -0.1572 0.1267  -0.0931 389 VAL A O   
3089 C CB  . VAL A 390 ? 0.7992 0.5770 0.7977 -0.1324 0.1182  -0.0566 389 VAL A CB  
3090 C CG1 . VAL A 390 ? 0.8447 0.6410 0.8324 -0.1448 0.1156  -0.0646 389 VAL A CG1 
3091 C CG2 . VAL A 390 ? 0.8234 0.6172 0.8276 -0.1203 0.1064  -0.0469 389 VAL A CG2 
3092 N N   . ALA A 391 ? 0.9185 0.6596 0.9005 -0.1635 0.1464  -0.0886 390 ALA A N   
3093 C CA  . ALA A 391 ? 1.0283 0.7739 0.9964 -0.1858 0.1505  -0.1025 390 ALA A CA  
3094 C C   . ALA A 391 ? 0.8989 0.6589 0.8618 -0.1936 0.1490  -0.1162 390 ALA A C   
3095 O O   . ALA A 391 ? 0.9020 0.6935 0.8615 -0.2048 0.1400  -0.1206 390 ALA A O   
3096 C CB  . ALA A 391 ? 1.0598 0.7663 1.0174 -0.1988 0.1675  -0.1061 390 ALA A CB  
3097 N N   . SER A 392 ? 0.7882 0.5267 0.7518 -0.1875 0.1582  -0.1213 391 SER A N   
3098 C CA  . SER A 392 ? 0.9376 0.6867 0.8934 -0.1950 0.1574  -0.1336 391 SER A CA  
3099 C C   . SER A 392 ? 1.0302 0.8231 0.9924 -0.1894 0.1382  -0.1293 391 SER A C   
3100 O O   . SER A 392 ? 1.1481 0.9642 1.1018 -0.2041 0.1319  -0.1360 391 SER A O   
3101 C CB  . SER A 392 ? 1.1029 0.8267 1.0649 -0.1819 0.1695  -0.1354 391 SER A CB  
3102 O OG  . SER A 392 ? 1.4021 1.0824 1.3635 -0.1815 0.1899  -0.1362 391 SER A OG  
3103 N N   . VAL A 393 ? 0.7720 0.5753 0.7486 -0.1691 0.1294  -0.1171 392 VAL A N   
3104 C CA  . VAL A 393 ? 0.7291 0.5659 0.7109 -0.1619 0.1145  -0.1125 392 VAL A CA  
3105 C C   . VAL A 393 ? 0.7713 0.6344 0.7531 -0.1708 0.1078  -0.1105 392 VAL A C   
3106 O O   . VAL A 393 ? 0.8833 0.7735 0.8651 -0.1772 0.1006  -0.1125 392 VAL A O   
3107 C CB  . VAL A 393 ? 0.6198 0.4570 0.6124 -0.1420 0.1086  -0.1007 392 VAL A CB  
3108 C CG1 . VAL A 393 ? 0.6099 0.4751 0.6044 -0.1360 0.0964  -0.0964 392 VAL A CG1 
3109 C CG2 . VAL A 393 ? 0.6760 0.4992 0.6739 -0.1329 0.1133  -0.1013 392 VAL A CG2 
3110 N N   . VAL A 394 ? 0.7900 0.6462 0.7732 -0.1711 0.1105  -0.1048 393 VAL A N   
3111 C CA  . VAL A 394 ? 0.8448 0.7256 0.8311 -0.1771 0.1067  -0.1014 393 VAL A CA  
3112 C C   . VAL A 394 ? 0.8706 0.7725 0.8543 -0.1982 0.1066  -0.1077 393 VAL A C   
3113 O O   . VAL A 394 ? 0.8826 0.8181 0.8764 -0.1995 0.1009  -0.1029 393 VAL A O   
3114 C CB  . VAL A 394 ? 0.9847 0.8499 0.9698 -0.1744 0.1111  -0.0939 393 VAL A CB  
3115 C CG1 . VAL A 394 ? 1.0040 0.8786 0.9867 -0.1912 0.1152  -0.0955 393 VAL A CG1 
3116 C CG2 . VAL A 394 ? 1.0585 0.9331 1.0475 -0.1590 0.1049  -0.0851 393 VAL A CG2 
3117 N N   . VAL A 395 ? 0.6877 0.5710 0.6583 -0.2154 0.1137  -0.1177 394 VAL A N   
3118 C CA  . VAL A 395 ? 0.9119 0.8182 0.8760 -0.2403 0.1115  -0.1239 394 VAL A CA  
3119 C C   . VAL A 395 ? 1.0227 0.9608 0.9905 -0.2405 0.1001  -0.1231 394 VAL A C   
3120 O O   . VAL A 395 ? 1.0846 1.0633 1.0601 -0.2513 0.0911  -0.1183 394 VAL A O   
3121 C CB  . VAL A 395 ? 1.0049 0.8781 0.9462 -0.2639 0.1241  -0.1378 394 VAL A CB  
3122 C CG1 . VAL A 395 ? 1.0479 0.9096 0.9817 -0.2824 0.1324  -0.1397 394 VAL A CG1 
3123 C CG2 . VAL A 395 ? 0.9345 0.7641 0.8692 -0.2518 0.1355  -0.1432 394 VAL A CG2 
3124 N N   . ASP A 396 ? 0.9750 0.8951 0.9379 -0.2296 0.1011  -0.1266 395 ASP A N   
3125 C CA  . ASP A 396 ? 0.9038 0.8460 0.8665 -0.2286 0.0915  -0.1259 395 ASP A CA  
3126 C C   . ASP A 396 ? 0.7850 0.7693 0.7680 -0.2167 0.0787  -0.1122 395 ASP A C   
3127 O O   . ASP A 396 ? 0.8947 0.8768 0.8899 -0.1951 0.0783  -0.1050 395 ASP A O   
3128 C CB  . ASP A 396 ? 0.9606 0.8758 0.9203 -0.2124 0.0960  -0.1290 395 ASP A CB  
3129 C CG  . ASP A 396 ? 1.0362 0.9610 0.9857 -0.2198 0.0913  -0.1333 395 ASP A CG  
3130 O OD1 . ASP A 396 ? 0.9807 0.9339 0.9241 -0.2384 0.0832  -0.1328 395 ASP A OD1 
3131 O OD2 . ASP A 396 ? 1.1557 1.0619 1.1035 -0.2079 0.0954  -0.1360 395 ASP A OD2 
3132 N N   . ARG A 397 ? 0.8298 0.8522 0.8162 -0.2320 0.0695  -0.1077 396 ARG A N   
3133 C CA  . ARG A 397 ? 0.9282 0.9935 0.9394 -0.2212 0.0602  -0.0924 396 ARG A CA  
3134 C C   . ARG A 397 ? 0.9063 0.9841 0.9238 -0.2057 0.0517  -0.0846 396 ARG A C   
3135 O O   . ARG A 397 ? 0.9483 1.0534 0.9874 -0.1905 0.0469  -0.0710 396 ARG A O   
3136 C CB  . ARG A 397 ? 0.9024 1.0095 0.9206 -0.2445 0.0536  -0.0869 396 ARG A CB  
3137 C CG  . ARG A 397 ? 1.0386 1.1496 1.0336 -0.2750 0.0490  -0.0948 396 ARG A CG  
3138 C CD  . ARG A 397 ? 1.2154 1.3797 1.2217 -0.2978 0.0383  -0.0843 396 ARG A CD  
3139 N NE  . ARG A 397 ? 1.3568 1.5325 1.3810 -0.2964 0.0440  -0.0803 396 ARG A NE  
3140 C CZ  . ARG A 397 ? 1.3666 1.5930 1.4237 -0.2899 0.0375  -0.0629 396 ARG A CZ  
3141 N NH1 . ARG A 397 ? 1.2517 1.5232 1.3299 -0.2829 0.0241  -0.0456 396 ARG A NH1 
3142 N NH2 . ARG A 397 ? 1.3780 1.6099 1.4482 -0.2900 0.0456  -0.0616 396 ARG A NH2 
3143 N N   . ARG A 398 ? 0.9144 0.9692 0.9128 -0.2096 0.0522  -0.0932 397 ARG A N   
3144 C CA  . ARG A 398 ? 0.8134 0.8695 0.8132 -0.1945 0.0465  -0.0879 397 ARG A CA  
3145 C C   . ARG A 398 ? 0.8429 0.8747 0.8495 -0.1687 0.0521  -0.0867 397 ARG A C   
3146 O O   . ARG A 398 ? 1.0253 1.0556 1.0331 -0.1554 0.0486  -0.0820 397 ARG A O   
3147 C CB  . ARG A 398 ? 0.8361 0.8728 0.8113 -0.2087 0.0480  -0.0993 397 ARG A CB  
3148 C CG  . ARG A 398 ? 0.9830 1.0450 0.9446 -0.2375 0.0402  -0.0998 397 ARG A CG  
3149 C CD  . ARG A 398 ? 1.2420 1.2696 1.1728 -0.2596 0.0517  -0.1192 397 ARG A CD  
3150 N NE  . ARG A 398 ? 1.3718 1.3849 1.2869 -0.2590 0.0530  -0.1243 397 ARG A NE  
3151 C CZ  . ARG A 398 ? 1.4895 1.5211 1.3864 -0.2795 0.0446  -0.1234 397 ARG A CZ  
3152 N NH1 . ARG A 398 ? 1.4852 1.5539 1.3788 -0.3029 0.0326  -0.1159 397 ARG A NH1 
3153 N NH2 . ARG A 398 ? 1.5239 1.5395 1.4057 -0.2784 0.0477  -0.1286 397 ARG A NH2 
3154 N N   . VAL A 399 ? 0.6842 0.6972 0.6929 -0.1639 0.0605  -0.0901 398 VAL A N   
3155 C CA  . VAL A 399 ? 0.6762 0.6649 0.6855 -0.1452 0.0651  -0.0895 398 VAL A CA  
3156 C C   . VAL A 399 ? 0.6641 0.6646 0.6870 -0.1308 0.0659  -0.0804 398 VAL A C   
3157 O O   . VAL A 399 ? 0.8164 0.8295 0.8479 -0.1340 0.0691  -0.0776 398 VAL A O   
3158 C CB  . VAL A 399 ? 0.7873 0.7449 0.7886 -0.1478 0.0737  -0.0966 398 VAL A CB  
3159 C CG1 . VAL A 399 ? 0.6405 0.5814 0.6432 -0.1315 0.0756  -0.0922 398 VAL A CG1 
3160 C CG2 . VAL A 399 ? 0.6775 0.6149 0.6665 -0.1568 0.0779  -0.1062 398 VAL A CG2 
3161 N N   . SER A 400 ? 0.7786 0.7727 0.8015 -0.1161 0.0649  -0.0764 399 SER A N   
3162 C CA  . SER A 400 ? 0.6733 0.6696 0.7042 -0.1021 0.0695  -0.0698 399 SER A CA  
3163 C C   . SER A 400 ? 0.7216 0.7066 0.7502 -0.1035 0.0775  -0.0721 399 SER A C   
3164 O O   . SER A 400 ? 0.6363 0.6020 0.6543 -0.1101 0.0784  -0.0775 399 SER A O   
3165 C CB  . SER A 400 ? 0.4496 0.4251 0.4704 -0.0909 0.0697  -0.0699 399 SER A CB  
3166 O OG  . SER A 400 ? 0.9206 0.8797 0.9359 -0.0835 0.0776  -0.0697 399 SER A OG  
3167 N N   . THR A 401 ? 0.6188 0.6149 0.6578 -0.0966 0.0844  -0.0669 400 THR A N   
3168 C CA  . THR A 401 ? 0.7016 0.6839 0.7339 -0.0979 0.0934  -0.0691 400 THR A CA  
3169 C C   . THR A 401 ? 0.7215 0.6716 0.7326 -0.0954 0.0939  -0.0726 400 THR A C   
3170 O O   . THR A 401 ? 0.7895 0.7244 0.7898 -0.1026 0.0935  -0.0746 400 THR A O   
3171 C CB  . THR A 401 ? 0.7201 0.7175 0.7666 -0.0895 0.1045  -0.0637 400 THR A CB  
3172 O OG1 . THR A 401 ? 0.7232 0.7497 0.7872 -0.0981 0.1052  -0.0606 400 THR A OG1 
3173 C CG2 . THR A 401 ? 0.5880 0.5588 0.6167 -0.0878 0.1159  -0.0674 400 THR A CG2 
3174 N N   . GLU A 402 ? 0.7265 0.6675 0.7321 -0.0861 0.0942  -0.0718 401 GLU A N   
3175 C CA  . GLU A 402 ? 0.7344 0.6497 0.7198 -0.0864 0.0927  -0.0741 401 GLU A CA  
3176 C C   . GLU A 402 ? 0.7326 0.6412 0.7143 -0.0930 0.0836  -0.0753 401 GLU A C   
3177 O O   . GLU A 402 ? 0.7532 0.6475 0.7236 -0.0973 0.0823  -0.0740 401 GLU A O   
3178 C CB  . GLU A 402 ? 0.8082 0.7162 0.7891 -0.0777 0.0939  -0.0734 401 GLU A CB  
3179 C CG  . GLU A 402 ? 1.0839 0.9690 1.0433 -0.0813 0.0908  -0.0755 401 GLU A CG  
3180 C CD  . GLU A 402 ? 1.2804 1.1633 1.2391 -0.0767 0.0858  -0.0751 401 GLU A CD  
3181 O OE1 . GLU A 402 ? 1.4025 1.2806 1.3607 -0.0688 0.0924  -0.0737 401 GLU A OE1 
3182 O OE2 . GLU A 402 ? 1.2621 1.1469 1.2214 -0.0805 0.0768  -0.0755 401 GLU A OE2 
3183 N N   . ASP A 403 ? 0.6938 0.6131 0.6852 -0.0943 0.0783  -0.0768 402 ASP A N   
3184 C CA  . ASP A 403 ? 0.8011 0.7112 0.7910 -0.0992 0.0745  -0.0788 402 ASP A CA  
3185 C C   . ASP A 403 ? 0.7308 0.6342 0.7213 -0.1061 0.0778  -0.0782 402 ASP A C   
3186 O O   . ASP A 403 ? 0.6681 0.5574 0.6553 -0.1065 0.0770  -0.0750 402 ASP A O   
3187 C CB  . ASP A 403 ? 0.8765 0.7954 0.8718 -0.1018 0.0713  -0.0826 402 ASP A CB  
3188 C CG  . ASP A 403 ? 1.0359 0.9555 1.0279 -0.0957 0.0674  -0.0818 402 ASP A CG  
3189 O OD1 . ASP A 403 ? 0.8430 0.7509 0.8275 -0.0911 0.0669  -0.0796 402 ASP A OD1 
3190 O OD2 . ASP A 403 ? 1.2520 1.1840 1.2468 -0.0978 0.0644  -0.0828 402 ASP A OD2 
3191 N N   . LYS A 404 ? 0.6939 0.6089 0.6898 -0.1117 0.0815  -0.0795 403 LYS A N   
3192 C CA  . LYS A 404 ? 0.5845 0.4913 0.5787 -0.1195 0.0858  -0.0787 403 LYS A CA  
3193 C C   . LYS A 404 ? 0.6913 0.5849 0.6751 -0.1175 0.0870  -0.0729 403 LYS A C   
3194 O O   . LYS A 404 ? 0.6720 0.5504 0.6519 -0.1198 0.0863  -0.0681 403 LYS A O   
3195 C CB  . LYS A 404 ? 0.6309 0.5568 0.6326 -0.1273 0.0896  -0.0803 403 LYS A CB  
3196 C CG  . LYS A 404 ? 0.6167 0.5559 0.6242 -0.1368 0.0874  -0.0852 403 LYS A CG  
3197 C CD  . LYS A 404 ? 0.7988 0.7662 0.8168 -0.1450 0.0888  -0.0836 403 LYS A CD  
3198 C CE  . LYS A 404 ? 1.1125 1.0950 1.1318 -0.1605 0.0850  -0.0880 403 LYS A CE  
3199 N NZ  . LYS A 404 ? 1.2618 1.2856 1.2977 -0.1650 0.0813  -0.0817 403 LYS A NZ  
3200 N N   . LEU A 405 ? 0.6227 0.5210 0.6012 -0.1137 0.0897  -0.0722 404 LEU A N   
3201 C CA  . LEU A 405 ? 0.7727 0.6568 0.7343 -0.1158 0.0910  -0.0679 404 LEU A CA  
3202 C C   . LEU A 405 ? 0.8076 0.6795 0.7623 -0.1157 0.0827  -0.0621 404 LEU A C   
3203 O O   . LEU A 405 ? 0.8060 0.6688 0.7525 -0.1213 0.0805  -0.0544 404 LEU A O   
3204 C CB  . LEU A 405 ? 0.7956 0.6802 0.7489 -0.1117 0.0975  -0.0705 404 LEU A CB  
3205 C CG  . LEU A 405 ? 0.8812 0.7733 0.8368 -0.1142 0.1091  -0.0719 404 LEU A CG  
3206 C CD1 . LEU A 405 ? 0.7134 0.6035 0.6648 -0.1072 0.1202  -0.0750 404 LEU A CD1 
3207 C CD2 . LEU A 405 ? 0.7702 0.6500 0.7100 -0.1254 0.1108  -0.0683 404 LEU A CD2 
3208 N N   . ARG A 406 ? 0.7102 0.5844 0.6697 -0.1098 0.0777  -0.0638 405 ARG A N   
3209 C CA  . ARG A 406 ? 0.7226 0.5911 0.6804 -0.1094 0.0701  -0.0570 405 ARG A CA  
3210 C C   . ARG A 406 ? 0.7304 0.5943 0.6999 -0.1097 0.0688  -0.0499 405 ARG A C   
3211 O O   . ARG A 406 ? 0.8560 0.7160 0.8230 -0.1119 0.0639  -0.0382 405 ARG A O   
3212 C CB  . ARG A 406 ? 0.7989 0.6720 0.7616 -0.1037 0.0668  -0.0609 405 ARG A CB  
3213 C CG  . ARG A 406 ? 0.7322 0.6036 0.6812 -0.1029 0.0684  -0.0650 405 ARG A CG  
3214 C CD  . ARG A 406 ? 0.7247 0.5962 0.6730 -0.1012 0.0627  -0.0644 405 ARG A CD  
3215 N NE  . ARG A 406 ? 0.8166 0.6924 0.7700 -0.0952 0.0646  -0.0704 405 ARG A NE  
3216 C CZ  . ARG A 406 ? 0.8569 0.7348 0.8132 -0.0936 0.0605  -0.0710 405 ARG A CZ  
3217 N NH1 . ARG A 406 ? 0.5550 0.4336 0.5136 -0.0964 0.0553  -0.0660 405 ARG A NH1 
3218 N NH2 . ARG A 406 ? 1.0966 0.9783 1.0552 -0.0893 0.0617  -0.0748 405 ARG A NH2 
3219 N N   . CYS A 407 ? 0.6366 0.5002 0.6182 -0.1084 0.0738  -0.0559 406 CYS A N   
3220 C CA  . CYS A 407 ? 0.8000 0.6520 0.7911 -0.1086 0.0775  -0.0508 406 CYS A CA  
3221 C C   . CYS A 407 ? 0.8076 0.6516 0.7917 -0.1147 0.0791  -0.0427 406 CYS A C   
3222 O O   . CYS A 407 ? 0.7339 0.5686 0.7229 -0.1131 0.0778  -0.0301 406 CYS A O   
3223 C CB  . CYS A 407 ? 0.7786 0.6276 0.7771 -0.1107 0.0851  -0.0619 406 CYS A CB  
3224 S SG  . CYS A 407 ? 1.0903 0.9423 1.0968 -0.1049 0.0851  -0.0683 406 CYS A SG  
3225 N N   . LEU A 408 ? 0.8172 0.6661 0.7916 -0.1213 0.0825  -0.0483 407 LEU A N   
3226 C CA  . LEU A 408 ? 0.7200 0.5614 0.6848 -0.1289 0.0850  -0.0413 407 LEU A CA  
3227 C C   . LEU A 408 ? 0.8962 0.7348 0.8486 -0.1307 0.0775  -0.0281 407 LEU A C   
3228 O O   . LEU A 408 ? 0.8937 0.7230 0.8433 -0.1346 0.0759  -0.0153 407 LEU A O   
3229 C CB  . LEU A 408 ? 0.6061 0.4574 0.5642 -0.1353 0.0914  -0.0496 407 LEU A CB  
3230 C CG  . LEU A 408 ? 0.6934 0.5481 0.6592 -0.1421 0.0988  -0.0564 407 LEU A CG  
3231 C CD1 . LEU A 408 ? 0.6640 0.5029 0.6372 -0.1436 0.1010  -0.0562 407 LEU A CD1 
3232 C CD2 . LEU A 408 ? 0.7410 0.6176 0.7154 -0.1402 0.1000  -0.0660 407 LEU A CD2 
3233 N N   . MET A 409 ? 0.7880 0.6340 0.7308 -0.1299 0.0728  -0.0304 408 MET A N   
3234 C CA  . MET A 409 ? 0.6338 0.4787 0.5587 -0.1370 0.0651  -0.0193 408 MET A CA  
3235 C C   . MET A 409 ? 0.7375 0.5841 0.6757 -0.1332 0.0552  -0.0024 408 MET A C   
3236 O O   . MET A 409 ? 0.8376 0.6838 0.7677 -0.1402 0.0481  0.0140  408 MET A O   
3237 C CB  . MET A 409 ? 0.6506 0.4990 0.5608 -0.1385 0.0644  -0.0275 408 MET A CB  
3238 C CG  . MET A 409 ? 0.6668 0.5124 0.5644 -0.1408 0.0763  -0.0405 408 MET A CG  
3239 S SD  . MET A 409 ? 0.8931 0.7362 0.7788 -0.1379 0.0807  -0.0516 408 MET A SD  
3240 C CE  . MET A 409 ? 0.8446 0.6772 0.6961 -0.1547 0.0742  -0.0445 408 MET A CE  
3241 N N   . LEU A 410 ? 0.7346 0.5849 0.6944 -0.1223 0.0553  -0.0051 409 LEU A N   
3242 C CA  . LEU A 410 ? 0.6478 0.5017 0.6273 -0.1155 0.0493  0.0110  409 LEU A CA  
3243 C C   . LEU A 410 ? 0.8367 0.6779 0.8264 -0.1136 0.0537  0.0229  409 LEU A C   
3244 O O   . LEU A 410 ? 0.9612 0.8054 0.9590 -0.1125 0.0467  0.0445  409 LEU A O   
3245 C CB  . LEU A 410 ? 0.5536 0.4104 0.5532 -0.1045 0.0535  0.0021  409 LEU A CB  
3246 C CG  . LEU A 410 ? 0.6835 0.5555 0.6857 -0.1032 0.0451  0.0048  409 LEU A CG  
3247 C CD1 . LEU A 410 ? 0.6646 0.5454 0.6453 -0.1156 0.0334  0.0145  409 LEU A CD1 
3248 C CD2 . LEU A 410 ? 0.6438 0.5162 0.6423 -0.1009 0.0500  -0.0144 409 LEU A CD2 
3249 N N   . CYS A 411 ? 0.8565 0.6843 0.8455 -0.1143 0.0653  0.0101  410 CYS A N   
3250 C CA  . CYS A 411 ? 0.8870 0.6969 0.8811 -0.1149 0.0724  0.0182  410 CYS A CA  
3251 C C   . CYS A 411 ? 0.8817 0.6899 0.8605 -0.1242 0.0658  0.0357  410 CYS A C   
3252 O O   . CYS A 411 ? 0.8593 0.6589 0.8492 -0.1203 0.0646  0.0555  410 CYS A O   
3253 C CB  . CYS A 411 ? 0.9511 0.7509 0.9407 -0.1200 0.0847  -0.0009 410 CYS A CB  
3254 S SG  . CYS A 411 ? 1.0639 0.8349 1.0599 -0.1218 0.0978  0.0035  410 CYS A SG  
3255 N N   . VAL A 412 ? 0.7891 0.6042 0.7423 -0.1364 0.0628  0.0298  411 VAL A N   
3256 C CA  . VAL A 412 ? 0.8343 0.6465 0.7677 -0.1485 0.0575  0.0453  411 VAL A CA  
3257 C C   . VAL A 412 ? 0.8834 0.7090 0.8143 -0.1511 0.0416  0.0672  411 VAL A C   
3258 O O   . VAL A 412 ? 1.1341 0.9587 1.0556 -0.1593 0.0343  0.0879  411 VAL A O   
3259 C CB  . VAL A 412 ? 0.8355 0.6473 0.7398 -0.1630 0.0636  0.0316  411 VAL A CB  
3260 C CG1 . VAL A 412 ? 0.7522 0.5626 0.6642 -0.1599 0.0768  0.0101  411 VAL A CG1 
3261 C CG2 . VAL A 412 ? 0.7675 0.5898 0.6501 -0.1707 0.0578  0.0277  411 VAL A CG2 
3262 N N   . LEU A 413 ? 0.8454 0.6856 0.7842 -0.1459 0.0353  0.0638  412 LEU A N   
3263 C CA  . LEU A 413 ? 0.8755 0.7338 0.8170 -0.1490 0.0192  0.0855  412 LEU A CA  
3264 C C   . LEU A 413 ? 1.0256 0.8863 1.0014 -0.1355 0.0158  0.1110  412 LEU A C   
3265 O O   . LEU A 413 ? 1.1666 1.0400 1.1436 -0.1409 0.0025  0.1384  412 LEU A O   
3266 C CB  . LEU A 413 ? 0.9212 0.7933 0.8662 -0.1462 0.0157  0.0743  412 LEU A CB  
3267 C CG  . LEU A 413 ? 0.8718 0.7505 0.7817 -0.1642 0.0089  0.0677  412 LEU A CG  
3268 C CD1 . LEU A 413 ? 0.6830 0.5490 0.5564 -0.1815 0.0130  0.0636  412 LEU A CD1 
3269 C CD2 . LEU A 413 ? 0.6415 0.5186 0.5512 -0.1585 0.0161  0.0444  412 LEU A CD2 
3270 N N   . ALA A 414 ? 0.9278 0.7757 0.9311 -0.1186 0.0290  0.1025  413 ALA A N   
3271 C CA  . ALA A 414 ? 0.8501 0.6924 0.8884 -0.1026 0.0328  0.1233  413 ALA A CA  
3272 C C   . ALA A 414 ? 0.9962 0.8197 1.0301 -0.1055 0.0358  0.1400  413 ALA A C   
3273 O O   . ALA A 414 ? 1.0316 0.8628 1.0808 -0.1016 0.0269  0.1713  413 ALA A O   
3274 C CB  . ALA A 414 ? 0.7978 0.6244 0.8577 -0.0878 0.0503  0.1046  413 ALA A CB  
3275 N N   . LYS A 415 ? 0.9909 0.7916 1.0057 -0.1126 0.0481  0.1207  414 LYS A N   
3276 C CA  . LYS A 415 ? 0.9286 0.7084 0.9335 -0.1188 0.0525  0.1328  414 LYS A CA  
3277 C C   . LYS A 415 ? 1.0927 0.8867 1.0781 -0.1325 0.0355  0.1581  414 LYS A C   
3278 O O   . LYS A 415 ? 1.3236 1.1064 1.3126 -0.1325 0.0343  0.1822  414 LYS A O   
3279 C CB  . LYS A 415 ? 0.8922 0.6552 0.8742 -0.1301 0.0654  0.1060  414 LYS A CB  
3280 C CG  . LYS A 415 ? 0.8898 0.6325 0.8868 -0.1217 0.0832  0.0859  414 LYS A CG  
3281 C CD  . LYS A 415 ? 0.9122 0.6392 0.8891 -0.1358 0.0945  0.0689  414 LYS A CD  
3282 C CE  . LYS A 415 ? 1.0130 0.7174 0.9831 -0.1416 0.0978  0.0886  414 LYS A CE  
3283 N NZ  . LYS A 415 ? 1.1502 0.8288 1.1461 -0.1264 0.1070  0.1049  414 LYS A NZ  
3284 N N   . ASN A 416 ? 1.1771 0.9934 1.1390 -0.1461 0.0232  0.1526  415 ASN A N   
3285 C CA  . ASN A 416 ? 1.2584 1.0889 1.1958 -0.1637 0.0064  0.1753  415 ASN A CA  
3286 C C   . ASN A 416 ? 1.2671 1.0773 1.1809 -0.1763 0.0116  0.1813  415 ASN A C   
3287 O O   . ASN A 416 ? 1.3642 1.1771 1.2754 -0.1820 0.0010  0.2119  415 ASN A O   
3288 C CB  . ASN A 416 ? 1.4370 1.2890 1.4044 -0.1543 -0.0091 0.2114  415 ASN A CB  
3289 C CG  . ASN A 416 ? 1.5966 1.4678 1.5390 -0.1753 -0.0295 0.2398  415 ASN A CG  
3290 O OD1 . ASN A 416 ? 1.7062 1.5800 1.6047 -0.1991 -0.0340 0.2277  415 ASN A OD1 
3291 N ND2 . ASN A 416 ? 1.5683 1.4526 1.5384 -0.1671 -0.0411 0.2790  415 ASN A ND2 
3292 N N   . GLY A 417 ? 1.1904 0.9827 1.0883 -0.1813 0.0276  0.1537  416 GLY A N   
3293 C CA  . GLY A 417 ? 1.1276 0.9006 1.0044 -0.1938 0.0351  0.1566  416 GLY A CA  
3294 C C   . GLY A 417 ? 1.0873 0.8359 0.9782 -0.1856 0.0545  0.1391  416 GLY A C   
3295 O O   . GLY A 417 ? 0.9820 0.7149 0.9010 -0.1704 0.0604  0.1482  416 GLY A O   
3296 N N   . THR A 418 ? 1.0026 0.7483 0.8735 -0.1970 0.0656  0.1141  417 THR A N   
3297 C CA  . THR A 418 ? 0.9576 0.6887 0.8392 -0.1937 0.0825  0.0934  417 THR A CA  
3298 C C   . THR A 418 ? 0.9690 0.6961 0.8236 -0.2128 0.0912  0.0846  417 THR A C   
3299 O O   . THR A 418 ? 1.0996 0.8411 0.9317 -0.2237 0.0896  0.0770  417 THR A O   
3300 C CB  . THR A 418 ? 1.0511 0.7969 0.9459 -0.1848 0.0861  0.0679  417 THR A CB  
3301 O OG1 . THR A 418 ? 1.2550 1.0080 1.1715 -0.1692 0.0775  0.0760  417 THR A OG1 
3302 C CG2 . THR A 418 ? 0.9884 0.7230 0.8944 -0.1839 0.1011  0.0487  417 THR A CG2 
3303 N N   . SER A 419 ? 1.0006 0.7065 0.8562 -0.2178 0.1023  0.0854  418 SER A N   
3304 C CA  . SER A 419 ? 1.2114 0.9141 1.0420 -0.2374 0.1108  0.0805  418 SER A CA  
3305 C C   . SER A 419 ? 1.1895 0.9142 1.0155 -0.2429 0.1192  0.0537  418 SER A C   
3306 O O   . SER A 419 ? 1.1206 0.8559 0.9667 -0.2328 0.1222  0.0369  418 SER A O   
3307 C CB  . SER A 419 ? 1.2415 0.9168 1.0757 -0.2428 0.1228  0.0836  418 SER A CB  
3308 O OG  . SER A 419 ? 1.2694 0.9433 1.1222 -0.2382 0.1334  0.0621  418 SER A OG  
3309 N N   . SER A 420 ? 1.2043 0.9358 1.0046 -0.2589 0.1241  0.0509  419 SER A N   
3310 C CA  . SER A 420 ? 1.1937 0.9457 0.9934 -0.2625 0.1356  0.0282  419 SER A CA  
3311 C C   . SER A 420 ? 1.2417 0.9999 1.0663 -0.2593 0.1452  0.0130  419 SER A C   
3312 O O   . SER A 420 ? 1.3536 1.1335 1.1936 -0.2525 0.1491  -0.0032 419 SER A O   
3313 C CB  . SER A 420 ? 1.3725 1.1247 1.1431 -0.2820 0.1456  0.0279  419 SER A CB  
3314 O OG  . SER A 420 ? 1.6413 1.3917 1.3832 -0.2889 0.1383  0.0369  419 SER A OG  
3315 N N   . HIS A 421 ? 1.2975 1.0362 1.1245 -0.2660 0.1491  0.0195  420 HIS A N   
3316 C CA  . HIS A 421 ? 1.3914 1.1352 1.2350 -0.2706 0.1590  0.0051  420 HIS A CA  
3317 C C   . HIS A 421 ? 1.2011 0.9462 1.0678 -0.2561 0.1546  -0.0031 420 HIS A C   
3318 O O   . HIS A 421 ? 1.1189 0.8872 1.0006 -0.2555 0.1576  -0.0188 420 HIS A O   
3319 C CB  . HIS A 421 ? 1.5735 1.2909 1.4069 -0.2861 0.1670  0.0130  420 HIS A CB  
3320 C CG  . HIS A 421 ? 1.6996 1.4259 1.5433 -0.2987 0.1781  -0.0023 420 HIS A CG  
3321 N ND1 . HIS A 421 ? 1.7443 1.5027 1.5908 -0.3100 0.1862  -0.0137 420 HIS A ND1 
3322 C CD2 . HIS A 421 ? 1.7567 1.4651 1.6082 -0.3036 0.1830  -0.0078 420 HIS A CD2 
3323 C CE1 . HIS A 421 ? 1.7992 1.5641 1.6563 -0.3222 0.1929  -0.0238 420 HIS A CE1 
3324 N NE2 . HIS A 421 ? 1.8119 1.5445 1.6689 -0.3203 0.1913  -0.0217 420 HIS A NE2 
3325 N N   . GLU A 422 ? 1.0453 0.7672 0.9158 -0.2448 0.1477  0.0092  421 GLU A N   
3326 C CA  . GLU A 422 ? 1.1164 0.8351 1.0065 -0.2317 0.1458  0.0019  421 GLU A CA  
3327 C C   . GLU A 422 ? 1.0414 0.7900 0.9412 -0.2202 0.1383  -0.0082 421 GLU A C   
3328 O O   . GLU A 422 ? 0.9830 0.7411 0.8972 -0.2153 0.1390  -0.0211 421 GLU A O   
3329 C CB  . GLU A 422 ? 1.2539 0.9433 1.1493 -0.2197 0.1421  0.0201  421 GLU A CB  
3330 C CG  . GLU A 422 ? 1.3689 1.0489 1.2836 -0.2071 0.1447  0.0125  421 GLU A CG  
3331 C CD  . GLU A 422 ? 1.5696 1.2225 1.4952 -0.1926 0.1438  0.0328  421 GLU A CD  
3332 O OE1 . GLU A 422 ? 1.5265 1.1783 1.4471 -0.1897 0.1351  0.0553  421 GLU A OE1 
3333 O OE2 . GLU A 422 ? 1.6655 1.2992 1.6050 -0.1845 0.1526  0.0273  421 GLU A OE2 
3334 N N   . LEU A 423 ? 0.9991 0.7601 0.8878 -0.2181 0.1318  -0.0024 422 LEU A N   
3335 C CA  . LEU A 423 ? 0.8801 0.6642 0.7739 -0.2084 0.1267  -0.0114 422 LEU A CA  
3336 C C   . LEU A 423 ? 0.9816 0.7915 0.8818 -0.2125 0.1351  -0.0277 422 LEU A C   
3337 O O   . LEU A 423 ? 0.9936 0.8206 0.9090 -0.2034 0.1332  -0.0376 422 LEU A O   
3338 C CB  . LEU A 423 ? 0.8853 0.6698 0.7603 -0.2085 0.1190  -0.0006 422 LEU A CB  
3339 C CG  . LEU A 423 ? 0.8749 0.6757 0.7515 -0.1991 0.1143  -0.0088 422 LEU A CG  
3340 C CD1 . LEU A 423 ? 0.8249 0.6286 0.7246 -0.1848 0.1089  -0.0130 422 LEU A CD1 
3341 C CD2 . LEU A 423 ? 0.8001 0.5966 0.6544 -0.2035 0.1054  0.0036  422 LEU A CD2 
3342 N N   . ASN A 424 ? 1.0230 0.8376 0.9134 -0.2259 0.1446  -0.0287 423 ASN A N   
3343 C CA  . ASN A 424 ? 1.0268 0.8702 0.9295 -0.2291 0.1540  -0.0409 423 ASN A CA  
3344 C C   . ASN A 424 ? 1.0367 0.8919 0.9604 -0.2312 0.1540  -0.0488 423 ASN A C   
3345 O O   . ASN A 424 ? 1.0683 0.9536 1.0100 -0.2281 0.1558  -0.0568 423 ASN A O   
3346 C CB  . ASN A 424 ? 1.0116 0.8588 0.9013 -0.2442 0.1662  -0.0397 423 ASN A CB  
3347 C CG  . ASN A 424 ? 1.2171 1.0987 1.1229 -0.2430 0.1778  -0.0497 423 ASN A CG  
3348 O OD1 . ASN A 424 ? 1.3656 1.2523 1.2646 -0.2368 0.1840  -0.0523 423 ASN A OD1 
3349 N ND2 . ASN A 424 ? 1.0956 1.0005 1.0229 -0.2495 0.1819  -0.0545 423 ASN A ND2 
3350 N N   . ASN A 425 ? 1.0020 0.8327 0.9227 -0.2369 0.1525  -0.0458 424 ASN A N   
3351 C CA  . ASN A 425 ? 1.0154 0.8515 0.9485 -0.2440 0.1539  -0.0549 424 ASN A CA  
3352 C C   . ASN A 425 ? 1.0395 0.8789 0.9838 -0.2307 0.1461  -0.0602 424 ASN A C   
3353 O O   . ASN A 425 ? 1.0187 0.8787 0.9746 -0.2350 0.1451  -0.0692 424 ASN A O   
3354 C CB  . ASN A 425 ? 1.0423 0.8442 0.9643 -0.2576 0.1599  -0.0520 424 ASN A CB  
3355 C CG  . ASN A 425 ? 1.2213 1.0324 1.1388 -0.2793 0.1692  -0.0545 424 ASN A CG  
3356 O OD1 . ASN A 425 ? 1.3652 1.1501 1.2673 -0.2892 0.1751  -0.0468 424 ASN A OD1 
3357 N ND2 . ASN A 425 ? 1.2044 1.0554 1.1368 -0.2871 0.1703  -0.0635 424 ASN A ND2 
3358 N N   . LEU A 426 ? 0.9767 0.7972 0.9169 -0.2163 0.1399  -0.0531 425 LEU A N   
3359 C CA  . LEU A 426 ? 0.8354 0.6587 0.7855 -0.2029 0.1331  -0.0572 425 LEU A CA  
3360 C C   . LEU A 426 ? 0.8373 0.6949 0.7972 -0.1961 0.1293  -0.0632 425 LEU A C   
3361 O O   . LEU A 426 ? 0.8357 0.7087 0.8066 -0.1937 0.1262  -0.0704 425 LEU A O   
3362 C CB  . LEU A 426 ? 0.6215 0.4237 0.5674 -0.1897 0.1271  -0.0456 425 LEU A CB  
3363 C CG  . LEU A 426 ? 0.8123 0.6161 0.7684 -0.1756 0.1206  -0.0479 425 LEU A CG  
3364 C CD1 . LEU A 426 ? 0.6322 0.4303 0.5955 -0.1798 0.1258  -0.0592 425 LEU A CD1 
3365 C CD2 . LEU A 426 ? 0.9167 0.7019 0.8719 -0.1657 0.1156  -0.0327 425 LEU A CD2 
3366 N N   . LEU A 427 ? 0.7466 0.6143 0.7013 -0.1936 0.1310  -0.0596 426 LEU A N   
3367 C CA  . LEU A 427 ? 0.6900 0.5853 0.6549 -0.1855 0.1314  -0.0641 426 LEU A CA  
3368 C C   . LEU A 427 ? 0.8148 0.7419 0.7979 -0.1931 0.1356  -0.0694 426 LEU A C   
3369 O O   . LEU A 427 ? 0.8953 0.8468 0.8944 -0.1857 0.1323  -0.0720 426 LEU A O   
3370 C CB  . LEU A 427 ? 0.6284 0.5207 0.5797 -0.1834 0.1367  -0.0606 426 LEU A CB  
3371 C CG  . LEU A 427 ? 0.6920 0.5708 0.6316 -0.1727 0.1299  -0.0577 426 LEU A CG  
3372 C CD1 . LEU A 427 ? 0.6587 0.5239 0.6015 -0.1666 0.1187  -0.0546 426 LEU A CD1 
3373 C CD2 . LEU A 427 ? 0.6251 0.4878 0.5394 -0.1798 0.1329  -0.0515 426 LEU A CD2 
3374 N N   . ASP A 428 ? 0.9515 0.8801 0.9328 -0.2092 0.1420  -0.0692 427 ASP A N   
3375 C CA  . ASP A 428 ? 0.9962 0.9589 0.9954 -0.2206 0.1443  -0.0726 427 ASP A CA  
3376 C C   . ASP A 428 ? 0.9084 0.8752 0.9126 -0.2267 0.1363  -0.0779 427 ASP A C   
3377 O O   . ASP A 428 ? 0.9169 0.9195 0.9389 -0.2280 0.1321  -0.0786 427 ASP A O   
3378 C CB  . ASP A 428 ? 1.0459 1.0083 1.0395 -0.2395 0.1534  -0.0714 427 ASP A CB  
3379 C CG  . ASP A 428 ? 1.2959 1.2698 1.2902 -0.2363 0.1638  -0.0677 427 ASP A CG  
3380 O OD1 . ASP A 428 ? 1.2541 1.2447 1.2593 -0.2205 0.1658  -0.0672 427 ASP A OD1 
3381 O OD2 . ASP A 428 ? 1.3755 1.3393 1.3579 -0.2503 0.1720  -0.0656 427 ASP A OD2 
3382 N N   . ASN A 429 ? 0.7985 0.7289 0.7871 -0.2304 0.1351  -0.0806 428 ASN A N   
3383 C CA  . ASN A 429 ? 0.8484 0.7772 0.8366 -0.2385 0.1311  -0.0878 428 ASN A CA  
3384 C C   . ASN A 429 ? 0.8725 0.8160 0.8699 -0.2232 0.1223  -0.0887 428 ASN A C   
3385 O O   . ASN A 429 ? 0.9894 0.9493 0.9904 -0.2312 0.1175  -0.0935 428 ASN A O   
3386 C CB  . ASN A 429 ? 1.0002 0.8815 0.9706 -0.2441 0.1367  -0.0908 428 ASN A CB  
3387 C CG  . ASN A 429 ? 0.9881 0.8524 0.9475 -0.2635 0.1462  -0.0907 428 ASN A CG  
3388 O OD1 . ASN A 429 ? 0.9587 0.8493 0.9217 -0.2818 0.1480  -0.0935 428 ASN A OD1 
3389 N ND2 . ASN A 429 ? 1.0147 0.8366 0.9618 -0.2600 0.1523  -0.0857 428 ASN A ND2 
3390 N N   . ALA A 430 ? 0.9043 0.8414 0.9027 -0.2035 0.1202  -0.0838 429 ALA A N   
3391 C CA  . ALA A 430 ? 0.8137 0.7601 0.8187 -0.1883 0.1128  -0.0839 429 ALA A CA  
3392 C C   . ALA A 430 ? 0.9003 0.8875 0.9242 -0.1821 0.1106  -0.0803 429 ALA A C   
3393 O O   . ALA A 430 ? 0.9582 0.9554 0.9886 -0.1706 0.1046  -0.0793 429 ALA A O   
3394 C CB  . ALA A 430 ? 0.7103 0.6315 0.7065 -0.1731 0.1117  -0.0799 429 ALA A CB  
3395 N N   . ASN A 431 ? 0.8707 0.8817 0.9052 -0.1895 0.1163  -0.0772 430 ASN A N   
3396 C CA  . ASN A 431 ? 0.8722 0.9233 0.9307 -0.1809 0.1175  -0.0708 430 ASN A CA  
3397 C C   . ASN A 431 ? 0.9119 0.9515 0.9693 -0.1591 0.1206  -0.0685 430 ASN A C   
3398 O O   . ASN A 431 ? 0.9723 1.0268 1.0419 -0.1467 0.1165  -0.0651 430 ASN A O   
3399 C CB  . ASN A 431 ? 0.9509 1.0373 1.0257 -0.1862 0.1075  -0.0680 430 ASN A CB  
3400 C CG  . ASN A 431 ? 1.3964 1.5007 1.4715 -0.2123 0.1053  -0.0701 430 ASN A CG  
3401 O OD1 . ASN A 431 ? 1.5121 1.6099 1.5750 -0.2265 0.0984  -0.0758 430 ASN A OD1 
3402 N ND2 . ASN A 431 ? 1.5773 1.7031 1.6642 -0.2210 0.1126  -0.0663 430 ASN A ND2 
3403 N N   . ILE A 432 ? 0.7678 0.7788 0.8076 -0.1565 0.1276  -0.0700 431 ILE A N   
3404 C CA  . ILE A 432 ? 0.7114 0.7081 0.7439 -0.1411 0.1322  -0.0694 431 ILE A CA  
3405 C C   . ILE A 432 ? 0.7968 0.8039 0.8354 -0.1383 0.1478  -0.0676 431 ILE A C   
3406 O O   . ILE A 432 ? 0.8071 0.8052 0.8344 -0.1489 0.1552  -0.0684 431 ILE A O   
3407 C CB  . ILE A 432 ? 0.6988 0.6575 0.7047 -0.1418 0.1278  -0.0713 431 ILE A CB  
3408 C CG1 . ILE A 432 ? 0.6960 0.6485 0.7023 -0.1383 0.1158  -0.0729 431 ILE A CG1 
3409 C CG2 . ILE A 432 ? 0.5997 0.5416 0.5903 -0.1334 0.1346  -0.0714 431 ILE A CG2 
3410 C CD1 . ILE A 432 ? 0.7942 0.7176 0.7840 -0.1413 0.1109  -0.0722 431 ILE A CD1 
3411 N N   . ALA A 433 ? 0.8281 0.8538 0.8857 -0.1238 0.1545  -0.0644 432 ALA A N   
3412 C CA  . ALA A 433 ? 0.8315 0.8693 0.9008 -0.1185 0.1736  -0.0625 432 ALA A CA  
3413 C C   . ALA A 433 ? 0.9601 0.9612 0.9966 -0.1228 0.1854  -0.0687 432 ALA A C   
3414 O O   . ALA A 433 ? 1.0081 0.9776 1.0183 -0.1213 0.1806  -0.0723 432 ALA A O   
3415 C CB  . ALA A 433 ? 0.7050 0.7610 0.7998 -0.0984 0.1808  -0.0567 432 ALA A CB  
3416 N N   . THR A 434 ? 0.9126 0.9200 0.9497 -0.1302 0.2006  -0.0692 433 THR A N   
3417 C CA  . THR A 434 ? 0.9233 0.8973 0.9245 -0.1403 0.2105  -0.0743 433 THR A CA  
3418 C C   . THR A 434 ? 0.9827 0.9257 0.9594 -0.1324 0.2202  -0.0797 433 THR A C   
3419 O O   . THR A 434 ? 1.0263 0.9377 0.9658 -0.1431 0.2165  -0.0827 433 THR A O   
3420 C CB  . THR A 434 ? 0.9148 0.9029 0.9211 -0.1509 0.2275  -0.0742 433 THR A CB  
3421 O OG1 . THR A 434 ? 0.9777 0.9957 1.0181 -0.1374 0.2455  -0.0720 433 THR A OG1 
3422 C CG2 . THR A 434 ? 0.8432 0.8498 0.8600 -0.1654 0.2154  -0.0702 433 THR A CG2 
3423 N N   . PRO A 435 ? 1.0012 0.9528 0.9979 -0.1149 0.2328  -0.0799 434 PRO A N   
3424 C CA  . PRO A 435 ? 0.9472 0.8639 0.9173 -0.1092 0.2422  -0.0862 434 PRO A CA  
3425 C C   . PRO A 435 ? 0.9957 0.8928 0.9454 -0.1114 0.2203  -0.0866 434 PRO A C   
3426 O O   . PRO A 435 ? 1.0783 0.9425 0.9918 -0.1187 0.2230  -0.0921 434 PRO A O   
3427 C CB  . PRO A 435 ? 1.1095 1.0429 1.1141 -0.0871 0.2579  -0.0830 434 PRO A CB  
3428 C CG  . PRO A 435 ? 1.1371 1.1116 1.1793 -0.0854 0.2671  -0.0764 434 PRO A CG  
3429 C CD  . PRO A 435 ? 1.0074 0.9990 1.0499 -0.1012 0.2433  -0.0732 434 PRO A CD  
3430 N N   . SER A 436 ? 0.9648 0.8823 0.9358 -0.1075 0.1998  -0.0810 435 SER A N   
3431 C CA  . SER A 436 ? 0.8691 0.7709 0.8248 -0.1089 0.1808  -0.0809 435 SER A CA  
3432 C C   . SER A 436 ? 0.9153 0.8005 0.8448 -0.1253 0.1681  -0.0799 435 SER A C   
3433 O O   . SER A 436 ? 0.9587 0.8314 0.8760 -0.1269 0.1539  -0.0784 435 SER A O   
3434 C CB  . SER A 436 ? 0.7927 0.7192 0.7775 -0.0998 0.1659  -0.0761 435 SER A CB  
3435 O OG  . SER A 436 ? 0.8615 0.8096 0.8749 -0.0847 0.1755  -0.0723 435 SER A OG  
3436 N N   . ARG A 437 ? 0.8097 0.6956 0.7320 -0.1371 0.1737  -0.0788 436 ARG A N   
3437 C CA  . ARG A 437 ? 0.7565 0.6281 0.6579 -0.1512 0.1613  -0.0739 436 ARG A CA  
3438 C C   . ARG A 437 ? 0.8168 0.6616 0.6794 -0.1622 0.1618  -0.0737 436 ARG A C   
3439 O O   . ARG A 437 ? 0.8761 0.7113 0.7226 -0.1727 0.1493  -0.0658 436 ARG A O   
3440 C CB  . ARG A 437 ? 0.7180 0.5991 0.6251 -0.1615 0.1651  -0.0710 436 ARG A CB  
3441 C CG  . ARG A 437 ? 0.7404 0.6499 0.6820 -0.1562 0.1640  -0.0711 436 ARG A CG  
3442 C CD  . ARG A 437 ? 0.7882 0.7031 0.7316 -0.1699 0.1659  -0.0682 436 ARG A CD  
3443 N NE  . ARG A 437 ? 0.8256 0.7687 0.7987 -0.1693 0.1633  -0.0686 436 ARG A NE  
3444 C CZ  . ARG A 437 ? 0.8400 0.7923 0.8189 -0.1826 0.1649  -0.0673 436 ARG A CZ  
3445 N NH1 . ARG A 437 ? 0.9659 0.8997 0.9242 -0.1955 0.1696  -0.0647 436 ARG A NH1 
3446 N NH2 . ARG A 437 ? 0.6877 0.6674 0.6908 -0.1851 0.1614  -0.0679 436 ARG A NH2 
3447 N N   . SER A 438 ? 0.8970 0.7295 0.7441 -0.1607 0.1766  -0.0812 437 SER A N   
3448 C CA  . SER A 438 ? 0.9580 0.7642 0.7625 -0.1759 0.1774  -0.0825 437 SER A CA  
3449 C C   . SER A 438 ? 0.8872 0.6889 0.6857 -0.1761 0.1568  -0.0770 437 SER A C   
3450 O O   . SER A 438 ? 0.8064 0.5943 0.5731 -0.1919 0.1488  -0.0725 437 SER A O   
3451 C CB  . SER A 438 ? 0.9624 0.7507 0.7490 -0.1755 0.2024  -0.0943 437 SER A CB  
3452 O OG  . SER A 438 ? 1.0935 0.8921 0.9116 -0.1543 0.2098  -0.0980 437 SER A OG  
3453 N N   . ALA A 439 ? 0.8691 0.6851 0.6983 -0.1601 0.1477  -0.0761 438 ALA A N   
3454 C CA  . ALA A 439 ? 0.7864 0.6026 0.6166 -0.1590 0.1287  -0.0701 438 ALA A CA  
3455 C C   . ALA A 439 ? 0.8475 0.6673 0.6765 -0.1675 0.1126  -0.0572 438 ALA A C   
3456 O O   . ALA A 439 ? 1.1075 0.9254 0.9282 -0.1723 0.0987  -0.0492 438 ALA A O   
3457 C CB  . ALA A 439 ? 0.8707 0.7018 0.7332 -0.1417 0.1241  -0.0720 438 ALA A CB  
3458 N N   . ILE A 440 ? 0.8020 0.6277 0.6413 -0.1692 0.1151  -0.0537 439 ILE A N   
3459 C CA  . ILE A 440 ? 0.8179 0.6431 0.6576 -0.1758 0.1031  -0.0398 439 ILE A CA  
3460 C C   . ILE A 440 ? 0.9359 0.7496 0.7415 -0.1947 0.1033  -0.0322 439 ILE A C   
3461 O O   . ILE A 440 ? 0.8386 0.6503 0.6316 -0.2030 0.0893  -0.0186 439 ILE A O   
3462 C CB  . ILE A 440 ? 0.8148 0.6472 0.6778 -0.1716 0.1069  -0.0397 439 ILE A CB  
3463 C CG1 . ILE A 440 ? 0.8141 0.6595 0.7062 -0.1574 0.1074  -0.0480 439 ILE A CG1 
3464 C CG2 . ILE A 440 ? 0.6696 0.4957 0.5351 -0.1756 0.0965  -0.0246 439 ILE A CG2 
3465 C CD1 . ILE A 440 ? 0.7759 0.6212 0.6814 -0.1498 0.0950  -0.0429 439 ILE A CD1 
3466 N N   . TYR A 441 ? 0.9816 0.7902 0.7727 -0.2025 0.1194  -0.0398 440 TYR A N   
3467 C CA  . TYR A 441 ? 0.9069 0.7038 0.6624 -0.2231 0.1214  -0.0331 440 TYR A CA  
3468 C C   . TYR A 441 ? 1.0100 0.7950 0.7274 -0.2384 0.1181  -0.0329 440 TYR A C   
3469 O O   . TYR A 441 ? 1.0035 0.7834 0.6920 -0.2575 0.1088  -0.0203 440 TYR A O   
3470 C CB  . TYR A 441 ? 0.7950 0.5897 0.5446 -0.2282 0.1425  -0.0429 440 TYR A CB  
3471 C CG  . TYR A 441 ? 0.9119 0.7186 0.6920 -0.2211 0.1434  -0.0400 440 TYR A CG  
3472 C CD1 . TYR A 441 ? 0.7938 0.5961 0.5704 -0.2299 0.1342  -0.0254 440 TYR A CD1 
3473 C CD2 . TYR A 441 ? 0.8514 0.6738 0.6635 -0.2068 0.1530  -0.0505 440 TYR A CD2 
3474 C CE1 . TYR A 441 ? 0.7887 0.5972 0.5892 -0.2260 0.1365  -0.0242 440 TYR A CE1 
3475 C CE2 . TYR A 441 ? 0.8205 0.6544 0.6568 -0.2047 0.1531  -0.0486 440 TYR A CE2 
3476 C CZ  . TYR A 441 ? 0.8813 0.7058 0.7101 -0.2150 0.1459  -0.0368 440 TYR A CZ  
3477 O OH  . TYR A 441 ? 0.9616 0.7930 0.8108 -0.2157 0.1482  -0.0365 440 TYR A OH  
3478 N N   . ASN A 442 ? 0.9946 0.7748 0.7099 -0.2321 0.1253  -0.0459 441 ASN A N   
3479 C CA  . ASN A 442 ? 0.9869 0.7517 0.6607 -0.2505 0.1248  -0.0483 441 ASN A CA  
3480 C C   . ASN A 442 ? 0.9855 0.7600 0.6559 -0.2579 0.0992  -0.0315 441 ASN A C   
3481 O O   . ASN A 442 ? 1.0152 0.7811 0.6477 -0.2793 0.0943  -0.0294 441 ASN A O   
3482 C CB  . ASN A 442 ? 0.9837 0.7344 0.6524 -0.2431 0.1437  -0.0673 441 ASN A CB  
3483 C CG  . ASN A 442 ? 1.0042 0.7436 0.6671 -0.2416 0.1720  -0.0811 441 ASN A CG  
3484 O OD1 . ASN A 442 ? 1.0967 0.8392 0.7556 -0.2491 0.1773  -0.0778 441 ASN A OD1 
3485 N ND2 . ASN A 442 ? 0.9536 0.6799 0.6179 -0.2313 0.1917  -0.0957 441 ASN A ND2 
3486 N N   . LEU A 443 ? 0.9369 0.7295 0.6462 -0.2419 0.0838  -0.0190 442 LEU A N   
3487 C CA  . LEU A 443 ? 0.9347 0.7409 0.6482 -0.2468 0.0607  0.0008  442 LEU A CA  
3488 C C   . LEU A 443 ? 1.0786 0.8848 0.7586 -0.2720 0.0502  0.0187  442 LEU A C   
3489 O O   . LEU A 443 ? 1.0046 0.8227 0.6744 -0.2847 0.0319  0.0350  442 LEU A O   
3490 C CB  . LEU A 443 ? 0.8913 0.7124 0.6523 -0.2248 0.0515  0.0112  442 LEU A CB  
3491 C CG  . LEU A 443 ? 0.8857 0.7115 0.6783 -0.2033 0.0558  -0.0018 442 LEU A CG  
3492 C CD1 . LEU A 443 ? 0.7156 0.5503 0.5484 -0.1859 0.0510  0.0067  442 LEU A CD1 
3493 C CD2 . LEU A 443 ? 0.7313 0.5617 0.5174 -0.2061 0.0475  -0.0028 442 LEU A CD2 
3494 N N   . GLU A 444 ? 1.2115 1.0071 0.8749 -0.2805 0.0614  0.0169  443 GLU A N   
3495 C CA  . GLU A 444 ? 1.3185 1.1107 0.9423 -0.3079 0.0545  0.0317  443 GLU A CA  
3496 C C   . GLU A 444 ? 1.2291 1.0145 0.8049 -0.3349 0.0516  0.0279  443 GLU A C   
3497 O O   . GLU A 444 ? 1.2815 1.0773 0.8336 -0.3571 0.0328  0.0486  443 GLU A O   
3498 C CB  . GLU A 444 ? 1.4794 1.2562 1.0852 -0.3152 0.0742  0.0222  443 GLU A CB  
3499 C CG  . GLU A 444 ? 1.7221 1.5039 1.3661 -0.2968 0.0765  0.0280  443 GLU A CG  
3500 C CD  . GLU A 444 ? 1.7905 1.5600 1.4197 -0.3039 0.0984  0.0158  443 GLU A CD  
3501 O OE1 . GLU A 444 ? 1.5352 1.3082 1.1974 -0.2869 0.1082  0.0087  443 GLU A OE1 
3502 O OE2 . GLU A 444 ? 1.9066 1.6639 1.4903 -0.3283 0.1064  0.0131  443 GLU A OE2 
3503 N N   . MET A 445 ? 1.0839 0.8514 0.6448 -0.3340 0.0708  0.0025  444 MET A N   
3504 C CA  . MET A 445 ? 1.1812 0.9336 0.6911 -0.3615 0.0738  -0.0062 444 MET A CA  
3505 C C   . MET A 445 ? 1.2149 0.9847 0.7302 -0.3661 0.0514  0.0053  444 MET A C   
3506 O O   . MET A 445 ? 1.3328 1.0920 0.8035 -0.3933 0.0506  0.0002  444 MET A O   
3507 C CB  . MET A 445 ? 1.1637 0.8871 0.6594 -0.3561 0.1049  -0.0365 444 MET A CB  
3508 C CG  . MET A 445 ? 1.0952 0.8079 0.5978 -0.3464 0.1287  -0.0478 444 MET A CG  
3509 S SD  . MET A 445 ? 1.3089 0.9824 0.7725 -0.3547 0.1684  -0.0785 444 MET A SD  
3510 C CE  . MET A 445 ? 1.2946 0.9791 0.8181 -0.3164 0.1868  -0.0870 444 MET A CE  
3511 N N   . LEU A 446 ? 1.0550 0.8500 0.6234 -0.3410 0.0354  0.0195  445 LEU A N   
3512 C CA  . LEU A 446 ? 1.0347 0.8536 0.6165 -0.3438 0.0126  0.0354  445 LEU A CA  
3513 C C   . LEU A 446 ? 1.1887 1.0377 0.7959 -0.3427 -0.0118 0.0693  445 LEU A C   
3514 O O   . LEU A 446 ? 1.2772 1.1526 0.9194 -0.3320 -0.0293 0.0867  445 LEU A O   
3515 C CB  . LEU A 446 ? 0.9227 0.7454 0.5462 -0.3152 0.0166  0.0240  445 LEU A CB  
3516 C CG  . LEU A 446 ? 0.9363 0.7303 0.5437 -0.3106 0.0407  -0.0059 445 LEU A CG  
3517 C CD1 . LEU A 446 ? 0.8313 0.6326 0.4848 -0.2801 0.0429  -0.0129 445 LEU A CD1 
3518 C CD2 . LEU A 446 ? 0.9197 0.6966 0.4739 -0.3413 0.0433  -0.0148 445 LEU A CD2 
3519 N N   . GLY A 447 ? 1.3072 1.1513 0.8980 -0.3529 -0.0112 0.0794  446 GLY A N   
3520 C CA  . GLY A 447 ? 1.3579 1.2261 0.9656 -0.3551 -0.0329 0.1143  446 GLY A CA  
3521 C C   . GLY A 447 ? 1.4447 1.3255 1.1159 -0.3198 -0.0363 0.1269  446 GLY A C   
3522 O O   . GLY A 447 ? 1.6515 1.5594 1.3540 -0.3129 -0.0557 0.1543  446 GLY A O   
3523 N N   . ALA A 448 ? 1.2820 1.1437 0.9723 -0.2985 -0.0167 0.1077  447 ALA A N   
3524 C CA  . ALA A 448 ? 1.1960 1.0636 0.9414 -0.2672 -0.0159 0.1133  447 ALA A CA  
3525 C C   . ALA A 448 ? 1.1891 1.0487 0.9476 -0.2605 -0.0130 0.1271  447 ALA A C   
3526 O O   . ALA A 448 ? 1.3387 1.2068 1.1363 -0.2429 -0.0200 0.1472  447 ALA A O   
3527 C CB  . ALA A 448 ? 1.2253 1.0812 0.9878 -0.2481 0.0017  0.0835  447 ALA A CB  
3528 N N   . THR A 449 ? 0.9885 0.8299 0.7143 -0.2746 -0.0009 0.1166  448 THR A N   
3529 C CA  . THR A 449 ? 1.2899 1.1186 1.0258 -0.2689 0.0065  0.1238  448 THR A CA  
3530 C C   . THR A 449 ? 1.1195 0.9406 0.8973 -0.2419 0.0196  0.1095  448 THR A C   
3531 O O   . THR A 449 ? 0.9324 0.7608 0.7480 -0.2227 0.0139  0.1190  448 THR A O   
3532 C CB  . THR A 449 ? 1.5060 1.3431 1.2458 -0.2750 -0.0111 0.1621  448 THR A CB  
3533 O OG1 . THR A 449 ? 1.3078 1.1479 1.0982 -0.2486 -0.0138 0.1772  448 THR A OG1 
3534 C CG2 . THR A 449 ? 1.6032 1.4622 1.3184 -0.2968 -0.0328 0.1832  448 THR A CG2 
3535 N N   . VAL A 450 ? 1.0136 0.8211 0.7834 -0.2420 0.0382  0.0862  449 VAL A N   
3536 C CA  . VAL A 450 ? 1.0787 0.8824 0.8815 -0.2219 0.0500  0.0696  449 VAL A CA  
3537 C C   . VAL A 450 ? 0.9914 0.7811 0.7991 -0.2226 0.0595  0.0726  449 VAL A C   
3538 O O   . VAL A 450 ? 1.0372 0.8204 0.8740 -0.2088 0.0611  0.0776  449 VAL A O   
3539 C CB  . VAL A 450 ? 1.1148 0.9208 0.9132 -0.2187 0.0625  0.0410  449 VAL A CB  
3540 C CG1 . VAL A 450 ? 0.9472 0.7572 0.7164 -0.2311 0.0573  0.0381  449 VAL A CG1 
3541 C CG2 . VAL A 450 ? 1.0737 0.8724 0.8629 -0.2240 0.0807  0.0251  449 VAL A CG2 
3542 N N   . VAL A 451 ? 0.9825 0.7654 0.7591 -0.2406 0.0669  0.0698  450 VAL A N   
3543 C CA  . VAL A 451 ? 1.1480 0.9174 0.9227 -0.2466 0.0756  0.0747  450 VAL A CA  
3544 C C   . VAL A 451 ? 1.2381 1.0003 1.0053 -0.2537 0.0624  0.1065  450 VAL A C   
3545 O O   . VAL A 451 ? 1.2067 0.9762 0.9495 -0.2670 0.0494  0.1220  450 VAL A O   
3546 C CB  . VAL A 451 ? 1.1487 0.9153 0.8945 -0.2632 0.0911  0.0589  450 VAL A CB  
3547 C CG1 . VAL A 451 ? 1.3293 1.0838 1.0765 -0.2694 0.1011  0.0621  450 VAL A CG1 
3548 C CG2 . VAL A 451 ? 1.0097 0.7862 0.7661 -0.2545 0.1038  0.0322  450 VAL A CG2 
3549 N N   . ALA A 452 ? 1.3679 1.1149 1.1546 -0.2462 0.0662  0.1170  451 ALA A N   
3550 C CA  . ALA A 452 ? 1.4057 1.1445 1.1952 -0.2468 0.0546  0.1507  451 ALA A CA  
3551 C C   . ALA A 452 ? 1.4288 1.1643 1.1778 -0.2716 0.0502  0.1661  451 ALA A C   
3552 O O   . ALA A 452 ? 1.5020 1.2403 1.2458 -0.2764 0.0344  0.1979  451 ALA A O   
3553 C CB  . ALA A 452 ? 1.3812 1.0969 1.1986 -0.2332 0.0647  0.1553  451 ALA A CB  
3554 N N   . ASP A 453 ? 1.2709 1.0026 0.9919 -0.2877 0.0643  0.1448  452 ASP A N   
3555 C CA  . ASP A 453 ? 1.2752 1.0009 0.9542 -0.3136 0.0638  0.1565  452 ASP A CA  
3556 C C   . ASP A 453 ? 1.2510 0.9911 0.8932 -0.3322 0.0527  0.1599  452 ASP A C   
3557 O O   . ASP A 453 ? 1.2518 0.9884 0.8538 -0.3569 0.0489  0.1729  452 ASP A O   
3558 C CB  . ASP A 453 ? 1.8557 1.5700 1.5208 -0.3248 0.0860  0.1356  452 ASP A CB  
3559 C CG  . ASP A 453 ? 1.5259 1.2518 1.1832 -0.3271 0.1013  0.1026  452 ASP A CG  
3560 O OD1 . ASP A 453 ? 1.2058 0.9414 0.8449 -0.3321 0.0962  0.0975  452 ASP A OD1 
3561 O OD2 . ASP A 453 ? 1.4769 1.2020 1.1460 -0.3249 0.1193  0.0830  452 ASP A OD2 
3562 N N   . ARG A 454 ? 1.4807 1.2355 1.1340 -0.3225 0.0473  0.1486  453 ARG A N   
3563 C CA  . ARG A 454 ? 1.6117 1.3777 1.2286 -0.3420 0.0373  0.1502  453 ARG A CA  
3564 C C   . ARG A 454 ? 1.6078 1.3899 1.2294 -0.3446 0.0099  0.1864  453 ARG A C   
3565 O O   . ARG A 454 ? 1.7327 1.5270 1.3217 -0.3656 -0.0027 0.1935  453 ARG A O   
3566 C CB  . ARG A 454 ? 1.5892 1.3613 1.2115 -0.3333 0.0459  0.1207  453 ARG A CB  
3567 C CG  . ARG A 454 ? 1.7316 1.5042 1.3049 -0.3587 0.0464  0.1116  453 ARG A CG  
3568 C CD  . ARG A 454 ? 1.8617 1.6382 1.4446 -0.3474 0.0526  0.0876  453 ARG A CD  
3569 N NE  . ARG A 454 ? 1.9090 1.6820 1.4429 -0.3735 0.0520  0.0811  453 ARG A NE  
3570 C CZ  . ARG A 454 ? 1.9362 1.6912 1.4253 -0.3947 0.0720  0.0631  453 ARG A CZ  
3571 N NH1 . ARG A 454 ? 1.9216 1.6658 1.4137 -0.3913 0.0925  0.0517  453 ARG A NH1 
3572 N NH2 . ARG A 454 ? 1.9630 1.7103 1.4038 -0.4207 0.0730  0.0560  453 ARG A NH2 
3573 N N   . ARG A 455 ? 1.4782 1.2606 1.1408 -0.3243 0.0019  0.2097  454 ARG A N   
3574 C CA  . ARG A 455 ? 1.7096 1.5106 1.3878 -0.3220 -0.0230 0.2496  454 ARG A CA  
3575 C C   . ARG A 455 ? 1.8420 1.6670 1.5510 -0.3065 -0.0349 0.2509  454 ARG A C   
3576 O O   . ARG A 455 ? 1.7758 1.6115 1.4630 -0.3181 -0.0365 0.2325  454 ARG A O   
3577 C CB  . ARG A 455 ? 1.6653 1.4755 1.2946 -0.3558 -0.0391 0.2740  454 ARG A CB  
3578 C CG  . ARG A 455 ? 1.6802 1.5197 1.3266 -0.3559 -0.0681 0.3173  454 ARG A CG  
3579 C CD  . ARG A 455 ? 1.8752 1.7267 1.4686 -0.3938 -0.0860 0.3420  454 ARG A CD  
3580 N NE  . ARG A 455 ? 2.0938 1.9814 1.7077 -0.3946 -0.1161 0.3863  454 ARG A NE  
3581 C CZ  . ARG A 455 ? 2.3137 2.2213 1.8908 -0.4263 -0.1388 0.4191  454 ARG A CZ  
3582 N NH1 . ARG A 455 ? 2.3728 2.2630 1.8865 -0.4606 -0.1329 0.4102  454 ARG A NH1 
3583 N NH2 . ARG A 455 ? 2.3761 2.3231 1.9800 -0.4247 -0.1673 0.4620  454 ARG A NH2 
3584 N N   . GLY A 456 ? 1.8938 1.7253 1.6532 -0.2807 -0.0414 0.2731  455 GLY A N   
3585 C CA  . GLY A 456 ? 1.8517 1.7054 1.6478 -0.2626 -0.0497 0.2750  455 GLY A CA  
3586 C C   . GLY A 456 ? 1.9706 1.8594 1.7537 -0.2803 -0.0752 0.2994  455 GLY A C   
3587 O O   . GLY A 456 ? 1.9724 1.8730 1.7340 -0.3000 -0.0919 0.3306  455 GLY A O   
3588 N N   . ARG A 457 ? 2.0802 1.9871 1.8752 -0.2752 -0.0788 0.2860  456 ARG A N   
3589 C CA  . ARG A 457 ? 2.1605 2.1028 1.9423 -0.2949 -0.1024 0.3054  456 ARG A CA  
3590 C C   . ARG A 457 ? 2.1125 2.0874 1.9520 -0.2736 -0.1187 0.3424  456 ARG A C   
3591 O O   . ARG A 457 ? 1.9927 1.9642 1.8801 -0.2428 -0.1077 0.3347  456 ARG A O   
3592 C CB  . ARG A 457 ? 2.2033 2.1456 1.9604 -0.3054 -0.0963 0.2701  456 ARG A CB  
3593 C CG  . ARG A 457 ? 2.3038 2.2617 2.0063 -0.3451 -0.1120 0.2751  456 ARG A CG  
3594 C CD  . ARG A 457 ? 2.3934 2.3289 2.0394 -0.3730 -0.1058 0.2707  456 ARG A CD  
3595 N NE  . ARG A 457 ? 2.4787 2.4350 2.0775 -0.4129 -0.1275 0.2929  456 ARG A NE  
3596 C CZ  . ARG A 457 ? 2.5290 2.5024 2.1216 -0.4268 -0.1469 0.3326  456 ARG A CZ  
3597 N NH1 . ARG A 457 ? 2.5245 2.5190 2.0695 -0.4673 -0.1677 0.3515  456 ARG A NH1 
3598 N NH2 . ARG A 457 ? 2.5597 2.5274 2.1911 -0.4021 -0.1453 0.3539  456 ARG A NH2 
3599 N N   . LYS A 458 ? 2.1891 2.1971 2.0240 -0.2910 -0.1444 0.3836  457 LYS A N   
3600 C CA  . LYS A 458 ? 2.1982 2.2413 2.0930 -0.2699 -0.1602 0.4268  457 LYS A CA  
3601 C C   . LYS A 458 ? 2.0915 2.1537 2.0298 -0.2486 -0.1571 0.4156  457 LYS A C   
3602 O O   . LYS A 458 ? 1.9941 2.0699 1.9078 -0.2664 -0.1623 0.3957  457 LYS A O   
3603 C CB  . LYS A 458 ? 2.2531 2.3382 2.1320 -0.2979 -0.1922 0.4735  457 LYS A CB  
3604 C CG  . LYS A 458 ? 2.2676 2.3361 2.1201 -0.3107 -0.1960 0.4970  457 LYS A CG  
3605 C CD  . LYS A 458 ? 2.2540 2.3686 2.0961 -0.3370 -0.2301 0.5497  457 LYS A CD  
3606 C CE  . LYS A 458 ? 2.2502 2.3445 2.0628 -0.3502 -0.2325 0.5722  457 LYS A CE  
3607 N NZ  . LYS A 458 ? 2.2449 2.3853 2.0452 -0.3778 -0.2675 0.6271  457 LYS A NZ  
3608 N N   . PRO A 459 ? 2.0955 2.1552 2.0970 -0.2109 -0.1464 0.4278  458 PRO A N   
3609 C CA  . PRO A 459 ? 2.0193 2.0888 2.0667 -0.1855 -0.1367 0.4148  458 PRO A CA  
3610 C C   . PRO A 459 ? 2.0149 2.1340 2.0664 -0.2006 -0.1581 0.4263  458 PRO A C   
3611 O O   . PRO A 459 ? 2.0569 2.2176 2.1092 -0.2180 -0.1841 0.4657  458 PRO A O   
3612 C CB  . PRO A 459 ? 1.9933 2.0621 2.1059 -0.1498 -0.1289 0.4466  458 PRO A CB  
3613 C CG  . PRO A 459 ? 2.0674 2.0999 2.1605 -0.1511 -0.1210 0.4528  458 PRO A CG  
3614 C CD  . PRO A 459 ? 2.1407 2.1838 2.1714 -0.1912 -0.1409 0.4572  458 PRO A CD  
3615 N N   . LYS A 460 ? 1.9301 2.0456 1.9835 -0.1955 -0.1474 0.3927  459 LYS A N   
3616 C CA  . LYS A 460 ? 1.8816 2.0405 1.9410 -0.2086 -0.1641 0.3994  459 LYS A CA  
3617 C C   . LYS A 460 ? 1.6991 1.9016 1.8309 -0.1844 -0.1731 0.4413  459 LYS A C   
3618 O O   . LYS A 460 ? 1.5282 1.7184 1.7101 -0.1495 -0.1535 0.4371  459 LYS A O   
3619 C CB  . LYS A 460 ? 1.9420 2.0806 1.9872 -0.2064 -0.1476 0.3530  459 LYS A CB  
3620 C CG  . LYS A 460 ? 2.0095 2.1048 1.9917 -0.2248 -0.1349 0.3126  459 LYS A CG  
3621 C CD  . LYS A 460 ? 2.0163 2.0931 1.9891 -0.2201 -0.1190 0.2714  459 LYS A CD  
3622 C CE  . LYS A 460 ? 2.0594 2.0957 1.9764 -0.2353 -0.1049 0.2353  459 LYS A CE  
3623 N NZ  . LYS A 460 ? 2.0546 2.0738 1.9646 -0.2294 -0.0900 0.1987  459 LYS A NZ  
3624 N N   . THR A 461 ? 1.7001 1.9544 1.8367 -0.2043 -0.2020 0.4826  460 THR A N   
3625 C CA  . THR A 461 ? 1.6747 1.9786 1.8839 -0.1823 -0.2130 0.5305  460 THR A CA  
3626 C C   . THR A 461 ? 1.5741 1.9239 1.8104 -0.1852 -0.2213 0.5313  460 THR A C   
3627 O O   . THR A 461 ? 1.5780 1.9813 1.8077 -0.2133 -0.2498 0.5590  460 THR A O   
3628 C CB  . THR A 461 ? 1.7195 2.0623 1.9273 -0.2008 -0.2424 0.5839  460 THR A CB  
3629 O OG1 . THR A 461 ? 1.7938 2.2009 2.0703 -0.1871 -0.2591 0.6328  460 THR A OG1 
3630 C CG2 . THR A 461 ? 1.6601 2.0133 1.7895 -0.2535 -0.2649 0.5755  460 THR A CG2 
3631 N N   . MET A 462 ? 1.3828 1.7124 1.6474 -0.1588 -0.1968 0.5014  461 MET A N   
3632 C CA  . MET A 462 ? 1.2235 1.5940 1.5166 -0.1594 -0.2015 0.5011  461 MET A CA  
3633 C C   . MET A 462 ? 1.0888 1.4460 1.4424 -0.1172 -0.1730 0.4896  461 MET A C   
3634 O O   . MET A 462 ? 1.0733 1.3767 1.4102 -0.1036 -0.1469 0.4482  461 MET A O   
3635 C CB  . MET A 462 ? 1.1760 1.5342 1.4024 -0.1945 -0.2056 0.4608  461 MET A CB  
3636 C CG  . MET A 462 ? 1.1575 1.5692 1.3974 -0.2120 -0.2218 0.4702  461 MET A CG  
3637 S SD  . MET A 462 ? 1.3172 1.6936 1.5089 -0.2264 -0.2060 0.4116  461 MET A SD  
3638 C CE  . MET A 462 ? 1.0495 1.3704 1.1487 -0.2579 -0.2043 0.3788  461 MET A CE  
3639 N N   . LYS A 463 ? 0.9985 1.4068 1.4222 -0.0980 -0.1777 0.5278  462 LYS A N   
3640 C CA  . LYS A 463 ? 0.9619 1.3638 1.4462 -0.0599 -0.1499 0.5206  462 LYS A CA  
3641 C C   . LYS A 463 ? 0.9978 1.3852 1.4577 -0.0678 -0.1376 0.4741  462 LYS A C   
3642 O O   . LYS A 463 ? 1.0738 1.4858 1.4972 -0.1002 -0.1569 0.4660  462 LYS A O   
3643 C CB  . LYS A 463 ? 0.9280 1.3978 1.4928 -0.0419 -0.1602 0.5752  462 LYS A CB  
3644 C CG  . LYS A 463 ? 1.3987 1.9351 1.9590 -0.0729 -0.2015 0.6227  462 LYS A CG  
3645 C CD  . LYS A 463 ? 1.3653 1.9447 1.8926 -0.1126 -0.2245 0.6126  462 LYS A CD  
3646 C CE  . LYS A 463 ? 1.2187 1.8743 1.7525 -0.1432 -0.2654 0.6656  462 LYS A CE  
3647 N NZ  . LYS A 463 ? 1.0179 1.7112 1.5113 -0.1878 -0.2878 0.6547  462 LYS A NZ  
3648 N N   . ARG A 464 ? 0.9311 1.2777 1.4092 -0.0402 -0.1054 0.4445  463 ARG A N   
3649 C CA  . ARG A 464 ? 0.9196 1.2396 1.3627 -0.0488 -0.0925 0.3965  463 ARG A CA  
3650 C C   . ARG A 464 ? 1.1422 1.4963 1.6246 -0.0413 -0.0858 0.3951  463 ARG A C   
3651 O O   . ARG A 464 ? 1.3987 1.7271 1.8577 -0.0439 -0.0715 0.3567  463 ARG A O   
3652 C CB  . ARG A 464 ? 0.8153 1.0662 1.2374 -0.0321 -0.0630 0.3575  463 ARG A CB  
3653 C CG  . ARG A 464 ? 0.7146 0.9238 1.0745 -0.0498 -0.0674 0.3377  463 ARG A CG  
3654 C CD  . ARG A 464 ? 0.6663 0.8799 0.9646 -0.0856 -0.0860 0.3181  463 ARG A CD  
3655 N NE  . ARG A 464 ? 0.7872 1.0125 1.0800 -0.0933 -0.0840 0.2967  463 ARG A NE  
3656 C CZ  . ARG A 464 ? 0.7746 0.9641 1.0284 -0.0994 -0.0719 0.2556  463 ARG A CZ  
3657 N NH1 . ARG A 464 ? 0.6692 0.8123 0.8893 -0.0981 -0.0605 0.2313  463 ARG A NH1 
3658 N NH2 . ARG A 464 ? 0.7644 0.9666 1.0148 -0.1069 -0.0715 0.2406  463 ARG A NH2 
3659 N N   . ILE A 465 ? 1.1185 1.5323 1.6610 -0.0326 -0.0963 0.4379  464 ILE A N   
3660 C CA  . ILE A 465 ? 1.3151 1.7667 1.8991 -0.0261 -0.0895 0.4394  464 ILE A CA  
3661 C C   . ILE A 465 ? 1.4181 1.8384 2.0455 0.0115  -0.0510 0.4239  464 ILE A C   
3662 O O   . ILE A 465 ? 1.5388 1.9972 2.2337 0.0330  -0.0407 0.4486  464 ILE A O   
3663 C CB  . ILE A 465 ? 0.6384 1.0932 1.1691 -0.0596 -0.1005 0.4076  464 ILE A CB  
3664 C CG1 . ILE A 465 ? 0.7017 1.1999 1.1999 -0.0990 -0.1378 0.4298  464 ILE A CG1 
3665 C CG2 . ILE A 465 ? 0.4686 0.9521 1.0401 -0.0504 -0.0874 0.4030  464 ILE A CG2 
3666 C CD1 . ILE A 465 ? 0.4870 1.0128 0.9603 -0.1297 -0.1500 0.4166  464 ILE A CD1 
3667 N N   . GLU A 466 ? 1.3567 1.7089 1.9461 0.0183  -0.0287 0.3839  465 GLU A N   
3668 C CA  . GLU A 466 ? 1.4592 1.7751 2.0799 0.0490  0.0092  0.3658  465 GLU A CA  
3669 C C   . GLU A 466 ? 1.2799 1.6141 1.9127 0.0473  0.0198  0.3477  465 GLU A C   
3670 O O   . GLU A 466 ? 1.0600 1.4541 1.7307 0.0436  0.0073  0.3736  465 GLU A O   
3671 C CB  . GLU A 466 ? 1.6519 1.9807 2.3450 0.0829  0.0242  0.4054  465 GLU A CB  
3672 C CG  . GLU A 466 ? 1.8482 2.1420 2.5314 0.0910  0.0243  0.4183  465 GLU A CG  
3673 C CD  . GLU A 466 ? 2.0055 2.3077 2.7633 0.1273  0.0427  0.4586  465 GLU A CD  
3674 O OE1 . GLU A 466 ? 2.0097 2.3414 2.8279 0.1483  0.0594  0.4727  465 GLU A OE1 
3675 O OE2 . GLU A 466 ? 2.0810 2.3595 2.8381 0.1354  0.0419  0.4769  465 GLU A OE2 
3676 N N   . ARG A 467 ? 1.2353 1.5194 1.8352 0.0483  0.0425  0.3041  466 ARG A N   
3677 C CA  . ARG A 467 ? 1.0420 1.3369 1.6391 0.0413  0.0507  0.2824  466 ARG A CA  
3678 C C   . ARG A 467 ? 1.1019 1.3510 1.7086 0.0623  0.0897  0.2546  466 ARG A C   
3679 O O   . ARG A 467 ? 1.0270 1.2294 1.6292 0.0768  0.1084  0.2459  466 ARG A O   
3680 C CB  . ARG A 467 ? 0.8251 1.1077 1.3516 0.0086  0.0308  0.2536  466 ARG A CB  
3681 C CG  . ARG A 467 ? 0.7117 1.0156 1.2095 -0.0147 -0.0029 0.2725  466 ARG A CG  
3682 C CD  . ARG A 467 ? 0.8059 1.0913 1.2349 -0.0451 -0.0173 0.2434  466 ARG A CD  
3683 N NE  . ARG A 467 ? 0.9150 1.2321 1.3212 -0.0720 -0.0485 0.2641  466 ARG A NE  
3684 C CZ  . ARG A 467 ? 0.8533 1.2210 1.2682 -0.0916 -0.0671 0.2818  466 ARG A CZ  
3685 N NH1 . ARG A 467 ? 0.7893 1.1814 1.1760 -0.1201 -0.0948 0.2988  466 ARG A NH1 
3686 N NH2 . ARG A 467 ? 0.8631 1.2570 1.3126 -0.0852 -0.0575 0.2820  466 ARG A NH2 
3687 N N   . ASP A 468 ? 1.2254 1.4873 1.8435 0.0617  0.1028  0.2409  467 ASP A N   
3688 C CA  . ASP A 468 ? 1.3105 1.5260 1.9227 0.0736  0.1385  0.2086  467 ASP A CA  
3689 C C   . ASP A 468 ? 1.0788 1.2554 1.6180 0.0502  0.1324  0.1681  467 ASP A C   
3690 O O   . ASP A 468 ? 0.9080 1.1034 1.4219 0.0302  0.1175  0.1579  467 ASP A O   
3691 C CB  . ASP A 468 ? 1.4425 1.6889 2.1000 0.0833  0.1579  0.2125  467 ASP A CB  
3692 C CG  . ASP A 468 ? 1.5110 1.7081 2.1526 0.0896  0.1947  0.1759  467 ASP A CG  
3693 O OD1 . ASP A 468 ? 1.5338 1.6823 2.1738 0.1045  0.2192  0.1656  467 ASP A OD1 
3694 O OD2 . ASP A 468 ? 1.4111 1.6168 2.0384 0.0772  0.1989  0.1573  467 ASP A OD2 
3695 N N   . MET A 469 ? 1.0281 1.1516 1.5348 0.0524  0.1436  0.1471  468 MET A N   
3696 C CA  . MET A 469 ? 1.0525 1.1408 1.4954 0.0328  0.1392  0.1115  468 MET A CA  
3697 C C   . MET A 469 ? 1.0414 1.0851 1.4734 0.0391  0.1721  0.0817  468 MET A C   
3698 O O   . MET A 469 ? 0.9288 0.9323 1.3540 0.0470  0.1885  0.0732  468 MET A O   
3699 C CB  . MET A 469 ? 1.0019 1.0705 1.4081 0.0233  0.1204  0.1108  468 MET A CB  
3700 C CG  . MET A 469 ? 0.8071 0.9152 1.2152 0.0126  0.0884  0.1385  468 MET A CG  
3701 S SD  . MET A 469 ? 1.1029 1.2477 1.4857 -0.0133 0.0635  0.1356  468 MET A SD  
3702 C CE  . MET A 469 ? 0.7855 0.8871 1.0968 -0.0323 0.0583  0.0990  468 MET A CE  
3703 N N   . PRO A 470 ? 1.0055 1.0558 1.4333 0.0330  0.1821  0.0659  469 PRO A N   
3704 C CA  . PRO A 470 ? 1.0942 1.1081 1.5080 0.0338  0.2129  0.0373  469 PRO A CA  
3705 C C   . PRO A 470 ? 0.9963 0.9658 1.3518 0.0187  0.2120  0.0077  469 PRO A C   
3706 O O   . PRO A 470 ? 1.0787 1.0088 1.4278 0.0241  0.2331  -0.0039 469 PRO A O   
3707 C CB  . PRO A 470 ? 1.1316 1.1737 1.5455 0.0238  0.2113  0.0316  469 PRO A CB  
3708 C CG  . PRO A 470 ? 0.8988 0.9769 1.2998 0.0091  0.1747  0.0456  469 PRO A CG  
3709 C CD  . PRO A 470 ? 0.8927 0.9877 1.3224 0.0200  0.1612  0.0749  469 PRO A CD  
3710 N N   . TYR A 471 ? 0.8457 0.8219 1.1604 -0.0004 0.1888  -0.0033 470 TYR A N   
3711 C CA  . TYR A 471 ? 0.9671 0.9107 1.2307 -0.0150 0.1847  -0.0274 470 TYR A CA  
3712 C C   . TYR A 471 ? 0.9434 0.8623 1.2000 -0.0110 0.1837  -0.0254 470 TYR A C   
3713 O O   . TYR A 471 ? 0.9556 0.8902 1.2245 -0.0065 0.1666  -0.0051 470 TYR A O   
3714 C CB  . TYR A 471 ? 0.8490 0.8091 1.0799 -0.0315 0.1573  -0.0305 470 TYR A CB  
3715 C CG  . TYR A 471 ? 0.9834 0.9616 1.2105 -0.0399 0.1571  -0.0357 470 TYR A CG  
3716 C CD1 . TYR A 471 ? 0.9352 0.8940 1.1325 -0.0503 0.1679  -0.0584 470 TYR A CD1 
3717 C CD2 . TYR A 471 ? 1.0752 1.0913 1.3258 -0.0401 0.1447  -0.0170 470 TYR A CD2 
3718 C CE1 . TYR A 471 ? 1.0711 1.0448 1.2623 -0.0592 0.1676  -0.0624 470 TYR A CE1 
3719 C CE2 . TYR A 471 ? 1.0341 1.0658 1.2794 -0.0498 0.1446  -0.0219 470 TYR A CE2 
3720 C CZ  . TYR A 471 ? 1.2005 1.2095 1.4161 -0.0585 0.1568  -0.0447 470 TYR A CZ  
3721 O OH  . TYR A 471 ? 1.3645 1.3871 1.5729 -0.0689 0.1575  -0.0491 470 TYR A OH  
3722 N N   . VAL A 472 ? 0.8110 0.6919 1.0444 -0.0155 0.2014  -0.0462 471 VAL A N   
3723 C CA  . VAL A 472 ? 0.9120 0.7677 1.1403 -0.0126 0.2035  -0.0443 471 VAL A CA  
3724 C C   . VAL A 472 ? 0.7485 0.6074 0.9455 -0.0246 0.1776  -0.0453 471 VAL A C   
3725 O O   . VAL A 472 ? 0.8913 0.7393 1.0903 -0.0211 0.1747  -0.0368 471 VAL A O   
3726 C CB  . VAL A 472 ? 1.0173 0.8282 1.2330 -0.0150 0.2339  -0.0647 471 VAL A CB  
3727 C CG1 . VAL A 472 ? 1.0635 0.8645 1.3195 0.0032  0.2644  -0.0576 471 VAL A CG1 
3728 C CG2 . VAL A 472 ? 1.0981 0.8967 1.2713 -0.0356 0.2368  -0.0921 471 VAL A CG2 
3729 N N   . LEU A 473 ? 0.5848 0.4571 0.7542 -0.0378 0.1610  -0.0547 472 LEU A N   
3730 C CA  . LEU A 473 ? 0.6279 0.5060 0.7717 -0.0471 0.1384  -0.0541 472 LEU A CA  
3731 C C   . LEU A 473 ? 0.6660 0.5739 0.8178 -0.0464 0.1170  -0.0359 472 LEU A C   
3732 O O   . LEU A 473 ? 0.7721 0.6843 0.9010 -0.0548 0.1002  -0.0362 472 LEU A O   
3733 C CB  . LEU A 473 ? 0.6036 0.4751 0.7119 -0.0616 0.1345  -0.0740 472 LEU A CB  
3734 C CG  . LEU A 473 ? 0.7312 0.5755 0.8241 -0.0689 0.1530  -0.0926 472 LEU A CG  
3735 C CD1 . LEU A 473 ? 0.7345 0.5804 0.7954 -0.0842 0.1468  -0.1080 472 LEU A CD1 
3736 C CD2 . LEU A 473 ? 0.6484 0.4741 0.7383 -0.0691 0.1559  -0.0920 472 LEU A CD2 
3737 N N   . SER A 474 ? 0.5860 0.5146 0.7702 -0.0375 0.1188  -0.0196 473 SER A N   
3738 C CA  . SER A 474 ? 0.7187 0.6784 0.9092 -0.0411 0.0984  -0.0018 473 SER A CA  
3739 C C   . SER A 474 ? 0.8756 0.8549 1.1070 -0.0288 0.0979  0.0252  473 SER A C   
3740 O O   . SER A 474 ? 0.8542 0.8636 1.1128 -0.0259 0.0952  0.0399  473 SER A O   
3741 C CB  . SER A 474 ? 0.6362 0.6134 0.8239 -0.0479 0.0961  -0.0068 473 SER A CB  
3742 O OG  . SER A 474 ? 0.7328 0.6920 0.8858 -0.0577 0.0978  -0.0290 473 SER A OG  
3743 N N   . ARG A 475 ? 0.8309 0.7953 1.0682 -0.0219 0.1005  0.0336  474 ARG A N   
3744 C CA  . ARG A 475 ? 0.7000 0.6810 0.9790 -0.0079 0.1011  0.0626  474 ARG A CA  
3745 C C   . ARG A 475 ? 0.7186 0.7232 0.9911 -0.0169 0.0751  0.0843  474 ARG A C   
3746 O O   . ARG A 475 ? 0.7478 0.7795 1.0541 -0.0095 0.0680  0.1137  474 ARG A O   
3747 C CB  . ARG A 475 ? 0.7124 0.6591 1.0035 0.0054  0.1226  0.0609  474 ARG A CB  
3748 C CG  . ARG A 475 ? 0.6217 0.5344 0.8971 0.0046  0.1465  0.0314  474 ARG A CG  
3749 C CD  . ARG A 475 ? 0.6953 0.5752 0.9910 0.0189  0.1735  0.0322  474 ARG A CD  
3750 N NE  . ARG A 475 ? 0.6957 0.5572 0.9852 0.0200  0.1694  0.0418  474 ARG A NE  
3751 C CZ  . ARG A 475 ? 0.8580 0.6924 1.1097 0.0069  0.1686  0.0232  474 ARG A CZ  
3752 N NH1 . ARG A 475 ? 0.8272 0.6523 1.0445 -0.0081 0.1694  -0.0043 474 ARG A NH1 
3753 N NH2 . ARG A 475 ? 0.9722 0.7917 1.2212 0.0080  0.1658  0.0342  474 ARG A NH2 
3754 N N   . TRP A 476 ? 0.7540 0.7489 0.9827 -0.0334 0.0616  0.0707  475 TRP A N   
3755 C CA  . TRP A 476 ? 0.6798 0.6914 0.8921 -0.0465 0.0391  0.0865  475 TRP A CA  
3756 C C   . TRP A 476 ? 0.7266 0.7724 0.9353 -0.0603 0.0221  0.0952  475 TRP A C   
3757 O O   . TRP A 476 ? 0.7056 0.7505 0.8994 -0.0670 0.0241  0.0779  475 TRP A O   
3758 C CB  . TRP A 476 ? 0.6667 0.6512 0.8343 -0.0581 0.0358  0.0679  475 TRP A CB  
3759 C CG  . TRP A 476 ? 0.5395 0.5364 0.6810 -0.0754 0.0159  0.0780  475 TRP A CG  
3760 C CD1 . TRP A 476 ? 0.5249 0.5233 0.6319 -0.0924 0.0066  0.0665  475 TRP A CD1 
3761 C CD2 . TRP A 476 ? 0.6990 0.7054 0.8433 -0.0791 0.0045  0.1018  475 TRP A CD2 
3762 N NE1 . TRP A 476 ? 0.6530 0.6599 0.7388 -0.1081 -0.0085 0.0793  475 TRP A NE1 
3763 C CE2 . TRP A 476 ? 0.7090 0.7229 0.8164 -0.1012 -0.0114 0.1017  475 TRP A CE2 
3764 C CE3 . TRP A 476 ? 0.7104 0.7179 0.8836 -0.0667 0.0072  0.1240  475 TRP A CE3 
3765 C CZ2 . TRP A 476 ? 0.6831 0.7076 0.7789 -0.1135 -0.0259 0.1223  475 TRP A CZ2 
3766 C CZ3 . TRP A 476 ? 0.6403 0.6601 0.8054 -0.0768 -0.0087 0.1470  475 TRP A CZ3 
3767 C CH2 . TRP A 476 ? 0.7349 0.7642 0.8601 -0.1012 -0.0257 0.1456  475 TRP A CH2 
3768 N N   . THR A 477 ? 0.7576 0.8335 0.9786 -0.0665 0.0050  0.1233  476 THR A N   
3769 C CA  . THR A 477 ? 0.7293 0.8394 0.9425 -0.0853 -0.0138 0.1344  476 THR A CA  
3770 C C   . THR A 477 ? 0.8473 0.9557 1.0210 -0.1066 -0.0319 0.1402  476 THR A C   
3771 O O   . THR A 477 ? 0.8766 0.9882 1.0584 -0.1039 -0.0377 0.1594  476 THR A O   
3772 C CB  . THR A 477 ? 0.6689 0.8257 0.9352 -0.0773 -0.0201 0.1685  476 THR A CB  
3773 O OG1 . THR A 477 ? 0.8220 0.9781 1.1294 -0.0549 0.0013  0.1647  476 THR A OG1 
3774 C CG2 . THR A 477 ? 0.5292 0.7247 0.7862 -0.1008 -0.0404 0.1799  476 THR A CG2 
3775 N N   . PRO A 478 ? 0.8302 0.9304 0.7984 -0.1833 -0.0718 0.0953  477 PRO A N   
3776 C CA  . PRO A 478 ? 0.8660 0.9615 0.8223 -0.1949 -0.0760 0.0993  477 PRO A CA  
3777 C C   . PRO A 478 ? 0.9442 1.0549 0.9126 -0.2063 -0.0832 0.1110  477 PRO A C   
3778 O O   . PRO A 478 ? 0.9279 1.0528 0.9072 -0.2111 -0.0841 0.1166  477 PRO A O   
3779 C CB  . PRO A 478 ? 0.8489 0.9289 0.7751 -0.2014 -0.0708 0.0953  477 PRO A CB  
3780 C CG  . PRO A 478 ? 0.7574 0.8283 0.6777 -0.1895 -0.0650 0.0866  477 PRO A CG  
3781 C CD  . PRO A 478 ? 0.7580 0.8445 0.7034 -0.1819 -0.0644 0.0888  477 PRO A CD  
3782 N N   . ILE A 479 ? 0.8566 0.9633 0.8231 -0.2109 -0.0885 0.1150  478 ILE A N   
3783 C CA  . ILE A 479 ? 0.7284 0.8441 0.7017 -0.2212 -0.0981 0.1263  478 ILE A CA  
3784 C C   . ILE A 479 ? 0.8859 1.0022 0.8443 -0.2359 -0.1011 0.1312  478 ILE A C   
3785 O O   . ILE A 479 ? 1.0714 1.2033 1.0454 -0.2429 -0.1101 0.1404  478 ILE A O   
3786 C CB  . ILE A 479 ? 0.7508 0.8532 0.7126 -0.2253 -0.1008 0.1288  478 ILE A CB  
3787 C CG1 . ILE A 479 ? 0.6304 0.7380 0.6159 -0.2140 -0.1023 0.1286  478 ILE A CG1 
3788 C CG2 . ILE A 479 ? 0.7320 0.8326 0.6829 -0.2399 -0.1112 0.1400  478 ILE A CG2 
3789 C CD1 . ILE A 479 ? 0.7635 0.8584 0.7392 -0.2192 -0.1036 0.1323  478 ILE A CD1 
3790 N N   . VAL A 480 ? 0.9377 1.0363 0.8669 -0.2406 -0.0945 0.1252  479 VAL A N   
3791 C CA  . VAL A 480 ? 0.9284 1.0219 0.8378 -0.2561 -0.0974 0.1291  479 VAL A CA  
3792 C C   . VAL A 480 ? 0.8513 0.9665 0.7838 -0.2584 -0.0984 0.1330  479 VAL A C   
3793 O O   . VAL A 480 ? 0.7500 0.8701 0.6800 -0.2731 -0.1054 0.1398  479 VAL A O   
3794 C CB  . VAL A 480 ? 0.9164 0.9835 0.7886 -0.2586 -0.0887 0.1209  479 VAL A CB  
3795 C CG1 . VAL A 480 ? 0.8877 0.9544 0.7567 -0.2553 -0.0809 0.1151  479 VAL A CG1 
3796 C CG2 . VAL A 480 ? 0.9265 0.9757 0.7670 -0.2758 -0.0942 0.1258  479 VAL A CG2 
3797 N N   . LYS A 481 ? 0.8007 0.9284 0.7563 -0.2443 -0.0912 0.1288  480 LYS A N   
3798 C CA  . LYS A 481 ? 0.9070 1.0553 0.8861 -0.2455 -0.0883 0.1325  480 LYS A CA  
3799 C C   . LYS A 481 ? 0.8693 1.0432 0.8823 -0.2497 -0.1001 0.1440  480 LYS A C   
3800 O O   . LYS A 481 ? 0.8175 1.0084 0.8464 -0.2604 -0.1039 0.1511  480 LYS A O   
3801 C CB  . LYS A 481 ? 0.8602 1.0109 0.8509 -0.2285 -0.0761 0.1249  480 LYS A CB  
3802 C CG  . LYS A 481 ? 0.6662 0.8312 0.6717 -0.2306 -0.0673 0.1270  480 LYS A CG  
3803 C CD  . LYS A 481 ? 0.6996 0.8668 0.7182 -0.2129 -0.0556 0.1212  480 LYS A CD  
3804 C CE  . LYS A 481 ? 0.7520 0.9199 0.7674 -0.2152 -0.0413 0.1197  480 LYS A CE  
3805 N NZ  . LYS A 481 ? 0.8025 0.9702 0.8282 -0.1979 -0.0285 0.1147  480 LYS A NZ  
3806 N N   . ASP A 482 ? 0.8038 0.9802 0.8292 -0.2414 -0.1064 0.1461  481 ASP A N   
3807 C CA  . ASP A 482 ? 0.8666 1.0632 0.9216 -0.2436 -0.1199 0.1574  481 ASP A CA  
3808 C C   . ASP A 482 ? 0.8576 1.0500 0.8972 -0.2631 -0.1350 0.1662  481 ASP A C   
3809 O O   . ASP A 482 ? 0.8160 1.0291 0.8805 -0.2707 -0.1464 0.1760  481 ASP A O   
3810 C CB  . ASP A 482 ? 0.7843 0.9779 0.8491 -0.2306 -0.1229 0.1573  481 ASP A CB  
3811 C CG  . ASP A 482 ? 1.0156 1.2138 1.0980 -0.2120 -0.1107 0.1497  481 ASP A CG  
3812 O OD1 . ASP A 482 ? 1.2462 1.4460 1.3274 -0.2087 -0.0989 0.1438  481 ASP A OD1 
3813 O OD2 . ASP A 482 ? 0.9539 1.1506 1.0480 -0.2009 -0.1129 0.1495  481 ASP A OD2 
3814 N N   . LEU A 483 ? 0.8670 1.0314 0.8654 -0.2712 -0.1352 0.1627  482 LEU A N   
3815 C CA  . LEU A 483 ? 1.0276 1.1802 1.0012 -0.2906 -0.1478 0.1693  482 LEU A CA  
3816 C C   . LEU A 483 ? 1.1092 1.2740 1.0898 -0.3032 -0.1495 0.1719  482 LEU A C   
3817 O O   . LEU A 483 ? 1.2797 1.4546 1.2697 -0.3170 -0.1657 0.1818  482 LEU A O   
3818 C CB  . LEU A 483 ? 1.0736 1.1910 0.9985 -0.2955 -0.1421 0.1628  482 LEU A CB  
3819 C CG  . LEU A 483 ? 1.0038 1.1047 0.9124 -0.2964 -0.1491 0.1669  482 LEU A CG  
3820 C CD1 . LEU A 483 ? 0.9972 1.1179 0.9430 -0.2828 -0.1521 0.1704  482 LEU A CD1 
3821 C CD2 . LEU A 483 ? 1.0358 1.1080 0.9095 -0.2932 -0.1354 0.1578  482 LEU A CD2 
3822 N N   . MET A 484 ? 0.9485 1.1107 0.9236 -0.2992 -0.1336 0.1634  483 MET A N   
3823 C CA  . MET A 484 ? 0.9678 1.1397 0.9487 -0.3114 -0.1318 0.1653  483 MET A CA  
3824 C C   . MET A 484 ? 0.9972 1.2075 1.0307 -0.3122 -0.1383 0.1748  483 MET A C   
3825 O O   . MET A 484 ? 0.9649 1.1863 1.0087 -0.3290 -0.1520 0.1836  483 MET A O   
3826 C CB  . MET A 484 ? 1.0011 1.1618 0.9673 -0.3038 -0.1120 0.1546  483 MET A CB  
3827 C CG  . MET A 484 ? 1.0311 1.1548 0.9461 -0.3074 -0.1069 0.1464  483 MET A CG  
3828 S SD  . MET A 484 ? 0.9997 1.1079 0.8989 -0.2916 -0.0866 0.1333  483 MET A SD  
3829 C CE  . MET A 484 ? 0.9174 0.9854 0.7639 -0.2942 -0.0852 0.1260  483 MET A CE  
3830 N N   . GLU A 485 ? 1.0319 1.2615 1.0991 -0.2938 -0.1287 0.1731  484 GLU A N   
3831 C CA  . GLU A 485 ? 0.8992 1.1663 1.0205 -0.2906 -0.1304 0.1811  484 GLU A CA  
3832 C C   . GLU A 485 ? 1.0231 1.3073 1.1693 -0.2971 -0.1539 0.1937  484 GLU A C   
3833 O O   . GLU A 485 ? 1.1084 1.4207 1.2916 -0.3061 -0.1628 0.2030  484 GLU A O   
3834 C CB  . GLU A 485 ? 0.7812 1.0583 0.9260 -0.2677 -0.1145 0.1756  484 GLU A CB  
3835 C CG  . GLU A 485 ? 0.9479 1.2142 1.0774 -0.2617 -0.0921 0.1655  484 GLU A CG  
3836 C CD  . GLU A 485 ? 1.1230 1.3932 1.2693 -0.2392 -0.0778 0.1596  484 GLU A CD  
3837 O OE1 . GLU A 485 ? 1.2486 1.5339 1.4241 -0.2287 -0.0844 0.1643  484 GLU A OE1 
3838 O OE2 . GLU A 485 ? 1.1598 1.4149 1.2871 -0.2320 -0.0605 0.1505  484 GLU A OE2 
3839 N N   . TYR A 486 ? 0.9989 1.2658 1.1259 -0.2931 -0.1644 0.1945  485 TYR A N   
3840 C CA  . TYR A 486 ? 0.9628 1.2381 1.1036 -0.3001 -0.1887 0.2067  485 TYR A CA  
3841 C C   . TYR A 486 ? 1.0171 1.2897 1.1451 -0.3244 -0.2055 0.2136  485 TYR A C   
3842 O O   . TYR A 486 ? 1.0591 1.3569 1.2227 -0.3318 -0.2232 0.2247  485 TYR A O   
3843 C CB  . TYR A 486 ? 0.9405 1.1890 1.0509 -0.2947 -0.1951 0.2059  485 TYR A CB  
3844 C CG  . TYR A 486 ? 1.0136 1.2695 1.1471 -0.2728 -0.1870 0.2033  485 TYR A CG  
3845 C CD1 . TYR A 486 ? 0.9895 1.2779 1.1751 -0.2605 -0.1859 0.2078  485 TYR A CD1 
3846 C CD2 . TYR A 486 ? 0.9575 1.1873 1.0619 -0.2646 -0.1801 0.1965  485 TYR A CD2 
3847 C CE1 . TYR A 486 ? 0.9419 1.2326 1.1448 -0.2404 -0.1788 0.2051  485 TYR A CE1 
3848 C CE2 . TYR A 486 ? 0.9642 1.1982 1.0881 -0.2462 -0.1742 0.1942  485 TYR A CE2 
3849 C CZ  . TYR A 486 ? 1.0390 1.3015 1.2098 -0.2341 -0.1740 0.1983  485 TYR A CZ  
3850 O OH  . TYR A 486 ? 1.0254 1.2878 1.2119 -0.2157 -0.1683 0.1956  485 TYR A OH  
3851 N N   . ILE A 487 ? 1.0623 1.3036 1.1400 -0.3364 -0.2007 0.2070  486 ILE A N   
3852 C CA  . ILE A 487 ? 1.0523 1.2830 1.1082 -0.3605 -0.2158 0.2121  486 ILE A CA  
3853 C C   . ILE A 487 ? 1.1554 1.4167 1.2499 -0.3702 -0.2141 0.2158  486 ILE A C   
3854 O O   . ILE A 487 ? 1.2692 1.5399 1.3745 -0.3889 -0.2340 0.2249  486 ILE A O   
3855 C CB  . ILE A 487 ? 1.0129 1.2001 1.0045 -0.3687 -0.2070 0.2027  486 ILE A CB  
3856 C CG1 . ILE A 487 ? 1.0441 1.1996 0.9960 -0.3655 -0.2125 0.2019  486 ILE A CG1 
3857 C CG2 . ILE A 487 ? 0.9711 1.1469 0.9412 -0.3934 -0.2185 0.2062  486 ILE A CG2 
3858 C CD1 . ILE A 487 ? 1.0208 1.1344 0.9132 -0.3700 -0.2008 0.1923  486 ILE A CD1 
3859 N N   . ALA A 488 ? 1.2002 1.4758 1.3150 -0.3580 -0.1903 0.2089  487 ALA A N   
3860 C CA  . ALA A 488 ? 1.3407 1.6462 1.4949 -0.3654 -0.1834 0.2122  487 ALA A CA  
3861 C C   . ALA A 488 ? 1.3530 1.7041 1.5759 -0.3599 -0.1934 0.2234  487 ALA A C   
3862 O O   . ALA A 488 ? 1.3003 1.6831 1.5684 -0.3592 -0.1820 0.2258  487 ALA A O   
3863 C CB  . ALA A 488 ? 1.3074 1.6086 1.4559 -0.3532 -0.1535 0.2013  487 ALA A CB  
3864 N N   . THR A 489 ? 1.3829 1.7356 1.6126 -0.3557 -0.2142 0.2303  488 THR A N   
3865 C CA  . THR A 489 ? 1.3067 1.6989 1.5994 -0.3461 -0.2250 0.2407  488 THR A CA  
3866 C C   . THR A 489 ? 1.3050 1.6871 1.5869 -0.3529 -0.2569 0.2503  488 THR A C   
3867 O O   . THR A 489 ? 1.3361 1.7388 1.6559 -0.3411 -0.2690 0.2583  488 THR A O   
3868 C CB  . THR A 489 ? 1.2713 1.6728 1.5853 -0.3181 -0.2039 0.2347  488 THR A CB  
3869 O OG1 . THR A 489 ? 1.0315 1.4369 1.3486 -0.3127 -0.1750 0.2258  488 THR A OG1 
3870 C CG2 . THR A 489 ? 1.4266 1.8669 1.8055 -0.3059 -0.2137 0.2453  488 THR A CG2 
3871 N N   . GLY A 490 ? 1.3139 1.6605 1.5402 -0.3716 -0.2701 0.2495  489 GLY A N   
3872 C CA  . GLY A 490 ? 1.3980 1.7231 1.5973 -0.3796 -0.2985 0.2573  489 GLY A CA  
3873 C C   . GLY A 490 ? 1.4874 1.8088 1.6913 -0.3592 -0.3004 0.2589  489 GLY A C   
3874 O O   . GLY A 490 ? 1.6863 1.9987 1.8834 -0.3628 -0.3257 0.2683  489 GLY A O   
3875 N N   . GLN A 491 ? 1.3471 1.6717 1.5588 -0.3383 -0.2745 0.2498  490 GLN A N   
3876 C CA  . GLN A 491 ? 1.3165 1.6428 1.5425 -0.3179 -0.2744 0.2513  490 GLN A CA  
3877 C C   . GLN A 491 ? 1.3002 1.5828 1.4677 -0.3148 -0.2701 0.2450  490 GLN A C   
3878 O O   . GLN A 491 ? 1.3794 1.6581 1.5520 -0.2975 -0.2636 0.2431  490 GLN A O   
3879 C CB  . GLN A 491 ? 1.4055 1.7590 1.6749 -0.2966 -0.2498 0.2453  490 GLN A CB  
3880 C CG  . GLN A 491 ? 1.5291 1.9025 1.8415 -0.2773 -0.2560 0.2519  490 GLN A CG  
3881 C CD  . GLN A 491 ? 1.6488 2.0546 2.0106 -0.2831 -0.2813 0.2669  490 GLN A CD  
3882 O OE1 . GLN A 491 ? 1.5786 2.0060 1.9626 -0.2980 -0.2869 0.2710  490 GLN A OE1 
3883 N NE2 . GLN A 491 ? 1.6984 2.1075 2.0789 -0.2715 -0.2978 0.2753  490 GLN A NE2 
3884 N N   . LEU A 492 ? 1.2154 1.4646 1.3282 -0.3317 -0.2729 0.2418  491 LEU A N   
3885 C CA  . LEU A 492 ? 1.1775 1.3857 1.2357 -0.3298 -0.2655 0.2355  491 LEU A CA  
3886 C C   . LEU A 492 ? 1.2145 1.3952 1.2382 -0.3416 -0.2899 0.2452  491 LEU A C   
3887 O O   . LEU A 492 ? 1.1656 1.3256 1.1539 -0.3610 -0.3024 0.2478  491 LEU A O   
3888 C CB  . LEU A 492 ? 1.1467 1.3311 1.1627 -0.3373 -0.2472 0.2239  491 LEU A CB  
3889 C CG  . LEU A 492 ? 1.0377 1.1824 1.0014 -0.3345 -0.2344 0.2157  491 LEU A CG  
3890 C CD1 . LEU A 492 ? 0.8504 1.0024 0.8320 -0.3134 -0.2144 0.2074  491 LEU A CD1 
3891 C CD2 . LEU A 492 ? 1.0840 1.2031 1.0037 -0.3468 -0.2246 0.2078  491 LEU A CD2 
3892 N N   . ASP A 493 ? 1.3222 1.4991 1.3526 -0.3302 -0.2965 0.2504  492 ASP A N   
3893 C CA  . ASP A 493 ? 1.4850 1.6316 1.4796 -0.3391 -0.3187 0.2601  492 ASP A CA  
3894 C C   . ASP A 493 ? 1.5625 1.6675 1.4917 -0.3594 -0.3230 0.2585  492 ASP A C   
3895 O O   . ASP A 493 ? 1.5872 1.6725 1.4835 -0.3607 -0.3011 0.2474  492 ASP A O   
3896 C CB  . ASP A 493 ? 1.5704 1.6980 1.5520 -0.3250 -0.3098 0.2589  492 ASP A CB  
3897 C CG  . ASP A 493 ? 1.6559 1.8155 1.6942 -0.3055 -0.3110 0.2628  492 ASP A CG  
3898 O OD1 . ASP A 493 ? 1.7869 1.9856 1.8770 -0.3011 -0.3152 0.2654  492 ASP A OD1 
3899 O OD2 . ASP A 493 ? 1.5757 1.7203 1.6065 -0.2946 -0.3066 0.2631  492 ASP A OD2 
3900 N N   . LEU A 494 ? 1.6001 1.6892 1.5084 -0.3746 -0.3519 0.2697  493 LEU A N   
3901 C CA  . LEU A 494 ? 1.5588 1.5997 1.3961 -0.3936 -0.3573 0.2689  493 LEU A CA  
3902 C C   . LEU A 494 ? 1.6530 1.6498 1.4378 -0.3898 -0.3479 0.2676  493 LEU A C   
3903 O O   . LEU A 494 ? 1.6582 1.6118 1.3808 -0.4008 -0.3405 0.2633  493 LEU A O   
3904 C CB  . LEU A 494 ? 1.4155 1.4509 1.2446 -0.4127 -0.3935 0.2811  493 LEU A CB  
3905 C CG  . LEU A 494 ? 1.4952 1.5621 1.3586 -0.4242 -0.4005 0.2808  493 LEU A CG  
3906 C CD1 . LEU A 494 ? 1.5275 1.6542 1.4746 -0.4083 -0.3946 0.2821  493 LEU A CD1 
3907 C CD2 . LEU A 494 ? 1.6112 1.6650 1.4576 -0.4461 -0.4383 0.2925  493 LEU A CD2 
3908 N N   . GLU A 495 ? 1.6921 1.6988 1.5021 -0.3741 -0.3468 0.2715  494 GLU A N   
3909 C CA  . GLU A 495 ? 1.7350 1.7026 1.5013 -0.3703 -0.3361 0.2711  494 GLU A CA  
3910 C C   . GLU A 495 ? 1.6123 1.5785 1.3756 -0.3600 -0.3005 0.2568  494 GLU A C   
3911 O O   . GLU A 495 ? 1.5627 1.4916 1.2787 -0.3624 -0.2849 0.2527  494 GLU A O   
3912 C CB  . GLU A 495 ? 1.8935 1.8691 1.6863 -0.3583 -0.3496 0.2811  494 GLU A CB  
3913 C CG  . GLU A 495 ? 1.9831 2.0128 1.8534 -0.3429 -0.3546 0.2832  494 GLU A CG  
3914 C CD  . GLU A 495 ? 2.0722 2.1226 1.9717 -0.3493 -0.3893 0.2965  494 GLU A CD  
3915 O OE1 . GLU A 495 ? 2.1269 2.1513 1.9864 -0.3678 -0.4109 0.3030  494 GLU A OE1 
3916 O OE2 . GLU A 495 ? 2.0102 2.1021 1.9730 -0.3357 -0.3953 0.3006  494 GLU A OE2 
3917 N N   . SER A 496 ? 1.5469 1.5535 1.3613 -0.3484 -0.2879 0.2494  495 SER A N   
3918 C CA  . SER A 496 ? 1.3030 1.3123 1.1209 -0.3376 -0.2575 0.2359  495 SER A CA  
3919 C C   . SER A 496 ? 1.2529 1.2468 1.0376 -0.3479 -0.2451 0.2268  495 SER A C   
3920 O O   . SER A 496 ? 1.2325 1.2048 0.9893 -0.3454 -0.2234 0.2179  495 SER A O   
3921 C CB  . SER A 496 ? 1.1552 1.2088 1.0360 -0.3206 -0.2504 0.2320  495 SER A CB  
3922 O OG  . SER A 496 ? 1.1506 1.2022 1.0356 -0.3075 -0.2266 0.2218  495 SER A OG  
3923 N N   . TYR A 497 ? 1.2134 1.2184 1.0030 -0.3594 -0.2590 0.2295  496 TYR A N   
3924 C CA  . TYR A 497 ? 1.1949 1.1826 0.9509 -0.3708 -0.2503 0.2220  496 TYR A CA  
3925 C C   . TYR A 497 ? 1.2515 1.2244 0.9815 -0.3918 -0.2761 0.2306  496 TYR A C   
3926 O O   . TYR A 497 ? 1.2114 1.2121 0.9733 -0.3982 -0.2883 0.2336  496 TYR A O   
3927 C CB  . TYR A 497 ? 1.1515 1.1716 0.9459 -0.3621 -0.2347 0.2128  496 TYR A CB  
3928 C CG  . TYR A 497 ? 1.1402 1.1651 0.9469 -0.3439 -0.2091 0.2021  496 TYR A CG  
3929 C CD1 . TYR A 497 ? 1.1516 1.2012 1.0008 -0.3278 -0.2068 0.2032  496 TYR A CD1 
3930 C CD2 . TYR A 497 ? 1.1888 1.1921 0.9647 -0.3427 -0.1886 0.1910  496 TYR A CD2 
3931 C CE1 . TYR A 497 ? 1.1702 1.2224 1.0300 -0.3125 -0.1862 0.1936  496 TYR A CE1 
3932 C CE2 . TYR A 497 ? 1.2006 1.2092 0.9907 -0.3265 -0.1682 0.1817  496 TYR A CE2 
3933 C CZ  . TYR A 497 ? 1.1896 1.2225 1.0213 -0.3121 -0.1677 0.1829  496 TYR A CZ  
3934 O OH  . TYR A 497 ? 1.0265 1.0634 0.8723 -0.2972 -0.1500 0.1737  496 TYR A OH  
3935 N N   . PRO A 498 ? 1.3524 1.2795 1.0231 -0.4035 -0.2843 0.2347  497 PRO A N   
3936 C CA  . PRO A 498 ? 1.4480 1.3532 1.0858 -0.4245 -0.3124 0.2434  497 PRO A CA  
3937 C C   . PRO A 498 ? 1.5102 1.4049 1.1250 -0.4385 -0.3097 0.2371  497 PRO A C   
3938 O O   . PRO A 498 ? 1.5574 1.4415 1.1554 -0.4334 -0.2836 0.2255  497 PRO A O   
3939 C CB  . PRO A 498 ? 1.5144 1.3642 1.0838 -0.4306 -0.3133 0.2465  497 PRO A CB  
3940 C CG  . PRO A 498 ? 1.4932 1.3455 1.0738 -0.4123 -0.2891 0.2420  497 PRO A CG  
3941 C CD  . PRO A 498 ? 1.3954 1.2868 1.0252 -0.3978 -0.2665 0.2312  497 PRO A CD  
3942 N N   . ALA A 499 ? 1.5440 1.4404 1.1581 -0.4564 -0.3379 0.2451  498 ALA A N   
3943 C CA  . ALA A 499 ? 1.4096 1.2867 0.9917 -0.4737 -0.3392 0.2404  498 ALA A CA  
3944 C C   . ALA A 499 ? 1.4791 1.2909 0.9756 -0.4894 -0.3470 0.2412  498 ALA A C   
3945 O O   . ALA A 499 ? 1.5349 1.3223 1.0042 -0.4923 -0.3629 0.2495  498 ALA A O   
3946 C CB  . ALA A 499 ? 1.3339 1.2466 0.9613 -0.4866 -0.3651 0.2484  498 ALA A CB  
3947 N N   . VAL A 500 ? 1.4581 1.2379 0.9088 -0.4992 -0.3351 0.2325  499 VAL A N   
3948 C CA  . VAL A 500 ? 1.6471 1.3617 1.0131 -0.5161 -0.3435 0.2330  499 VAL A CA  
3949 C C   . VAL A 500 ? 1.7622 1.4720 1.1227 -0.5378 -0.3856 0.2454  499 VAL A C   
3950 O O   . VAL A 500 ? 1.8800 1.5500 1.1922 -0.5468 -0.4049 0.2528  499 VAL A O   
3951 C CB  . VAL A 500 ? 1.6856 1.3677 1.0065 -0.5225 -0.3240 0.2213  499 VAL A CB  
3952 C CG1 . VAL A 500 ? 1.7240 1.3341 0.9531 -0.5402 -0.3334 0.2219  499 VAL A CG1 
3953 C CG2 . VAL A 500 ? 1.6803 1.3681 1.0095 -0.5006 -0.2845 0.2091  499 VAL A CG2 
3954 N N   . ARG A 501 ? 1.6966 1.4468 1.1077 -0.5465 -0.4000 0.2479  500 ARG A N   
3955 C CA  . ARG A 501 ? 1.7127 1.4672 1.1319 -0.5676 -0.4416 0.2599  500 ARG A CA  
3956 C C   . ARG A 501 ? 1.6927 1.5212 1.2096 -0.5625 -0.4528 0.2666  500 ARG A C   
3957 O O   . ARG A 501 ? 1.6033 1.4737 1.1729 -0.5444 -0.4268 0.2606  500 ARG A O   
3958 C CB  . ARG A 501 ? 1.6920 1.4082 1.0598 -0.5919 -0.4508 0.2562  500 ARG A CB  
3959 C CG  . ARG A 501 ? 1.6296 1.3813 1.0406 -0.5929 -0.4350 0.2492  500 ARG A CG  
3960 C CD  . ARG A 501 ? 1.6355 1.3799 1.0391 -0.6214 -0.4638 0.2540  500 ARG A CD  
3961 N NE  . ARG A 501 ? 1.6360 1.4221 1.0925 -0.6231 -0.4507 0.2497  500 ARG A NE  
3962 C CZ  . ARG A 501 ? 1.6830 1.4431 1.1041 -0.6269 -0.4283 0.2387  500 ARG A CZ  
3963 N NH1 . ARG A 501 ? 1.6300 1.3247 0.9661 -0.6282 -0.4160 0.2306  500 ARG A NH1 
3964 N NH2 . ARG A 501 ? 1.6866 1.4841 1.1560 -0.6289 -0.4173 0.2360  500 ARG A NH2 
3965 N N   . ASP A 502 ? 1.8070 1.6499 1.3472 -0.5784 -0.4918 0.2791  501 ASP A N   
3966 C CA  . ASP A 502 ? 1.7939 1.7067 1.4285 -0.5762 -0.5047 0.2867  501 ASP A CA  
3967 C C   . ASP A 502 ? 1.6269 1.5874 1.3254 -0.5477 -0.4836 0.2860  501 ASP A C   
3968 O O   . ASP A 502 ? 1.5746 1.5886 1.3429 -0.5393 -0.4713 0.2847  501 ASP A O   
3969 C CB  . ASP A 502 ? 1.8426 1.7770 1.5021 -0.5886 -0.4957 0.2813  501 ASP A CB  
3970 C CG  . ASP A 502 ? 1.8770 1.7855 1.5058 -0.6202 -0.5296 0.2871  501 ASP A CG  
3971 O OD1 . ASP A 502 ? 1.8697 1.7249 1.4311 -0.6331 -0.5531 0.2910  501 ASP A OD1 
3972 O OD2 . ASP A 502 ? 1.9187 1.8584 1.5893 -0.6330 -0.5326 0.2877  501 ASP A OD2 
3973 N N   . GLY A 503 ? 1.6255 1.5638 1.2976 -0.5335 -0.4790 0.2870  502 GLY A N   
3974 C CA  . GLY A 503 ? 1.6052 1.5816 1.3308 -0.5072 -0.4612 0.2866  502 GLY A CA  
3975 C C   . GLY A 503 ? 1.6003 1.6424 1.4183 -0.5001 -0.4754 0.2955  502 GLY A C   
3976 O O   . GLY A 503 ? 1.3776 1.4614 1.2502 -0.4826 -0.4511 0.2903  502 GLY A O   
3977 N N   . PRO A 504 ? 1.7821 1.8330 1.6184 -0.5129 -0.5151 0.3093  503 PRO A N   
3978 C CA  . PRO A 504 ? 1.7454 1.8607 1.6747 -0.5053 -0.5295 0.3188  503 PRO A CA  
3979 C C   . PRO A 504 ? 1.7967 1.9566 1.7809 -0.5120 -0.5179 0.3153  503 PRO A C   
3980 O O   . PRO A 504 ? 1.8785 2.0938 1.9428 -0.5077 -0.5275 0.3230  503 PRO A O   
3981 C CB  . PRO A 504 ? 1.6243 1.7286 1.5476 -0.5216 -0.5780 0.3340  503 PRO A CB  
3982 C CG  . PRO A 504 ? 1.6504 1.6811 1.4744 -0.5304 -0.5847 0.3325  503 PRO A CG  
3983 C CD  . PRO A 504 ? 1.7394 1.7389 1.5107 -0.5330 -0.5490 0.3170  503 PRO A CD  
3984 N N   . SER A 505 ? 1.7309 1.8658 1.6724 -0.5220 -0.4966 0.3039  504 SER A N   
3985 C CA  . SER A 505 ? 1.6948 1.8633 1.6774 -0.5308 -0.4845 0.3003  504 SER A CA  
3986 C C   . SER A 505 ? 1.6890 1.8937 1.7171 -0.5071 -0.4454 0.2914  504 SER A C   
3987 O O   . SER A 505 ? 1.5876 1.8180 1.6471 -0.5111 -0.4289 0.2872  504 SER A O   
3988 C CB  . SER A 505 ? 1.6936 1.8145 1.6062 -0.5528 -0.4809 0.2925  504 SER A CB  
3989 O OG  . SER A 505 ? 1.7336 1.8839 1.6836 -0.5641 -0.4721 0.2904  504 SER A OG  
3990 N N   . VAL A 506 ? 1.7109 1.9139 1.7389 -0.4833 -0.4313 0.2887  505 VAL A N   
3991 C CA  . VAL A 506 ? 1.5286 1.7629 1.5984 -0.4591 -0.3980 0.2810  505 VAL A CA  
3992 C C   . VAL A 506 ? 1.6093 1.8757 1.7326 -0.4390 -0.4066 0.2894  505 VAL A C   
3993 O O   . VAL A 506 ? 1.3939 1.6495 1.5059 -0.4193 -0.3917 0.2849  505 VAL A O   
3994 C CB  . VAL A 506 ? 1.2755 1.4714 1.2881 -0.4481 -0.3673 0.2668  505 VAL A CB  
3995 C CG1 . VAL A 506 ? 1.2508 1.4768 1.3033 -0.4274 -0.3347 0.2580  505 VAL A CG1 
3996 C CG2 . VAL A 506 ? 1.1449 1.2985 1.0932 -0.4679 -0.3638 0.2598  505 VAL A CG2 
3997 N N   . VAL A 507 ? 1.7902 2.0951 1.9723 -0.4449 -0.4319 0.3019  506 VAL A N   
3998 C CA  . VAL A 507 ? 1.8336 2.1706 2.0713 -0.4266 -0.4438 0.3114  506 VAL A CA  
3999 C C   . VAL A 507 ? 1.7538 2.1312 2.0492 -0.4029 -0.4120 0.3056  506 VAL A C   
4000 O O   . VAL A 507 ? 1.5623 1.9520 1.8672 -0.4040 -0.3861 0.2970  506 VAL A O   
4001 C CB  . VAL A 507 ? 1.5348 1.9037 1.8241 -0.4398 -0.4826 0.3273  506 VAL A CB  
4002 C CG1 . VAL A 507 ? 1.5162 1.8424 1.7513 -0.4545 -0.5205 0.3360  506 VAL A CG1 
4003 C CG2 . VAL A 507 ? 1.4518 1.8481 1.7731 -0.4597 -0.4819 0.3275  506 VAL A CG2 
4004 N N   . GLN A 508 ? 1.9521 2.3469 2.2828 -0.3814 -0.4144 0.3105  507 GLN A N   
4005 C CA  . GLN A 508 ? 2.1707 2.5994 2.5525 -0.3577 -0.3853 0.3052  507 GLN A CA  
4006 C C   . GLN A 508 ? 2.2646 2.7356 2.7199 -0.3427 -0.4004 0.3172  507 GLN A C   
4007 O O   . GLN A 508 ? 2.2543 2.7138 2.7040 -0.3391 -0.4266 0.3264  507 GLN A O   
4008 C CB  . GLN A 508 ? 2.2962 2.6928 2.6339 -0.3402 -0.3593 0.2931  507 GLN A CB  
4009 C CG  . GLN A 508 ? 2.3499 2.7178 2.6586 -0.3311 -0.3748 0.2978  507 GLN A CG  
4010 C CD  . GLN A 508 ? 2.3640 2.6770 2.5903 -0.3455 -0.3798 0.2937  507 GLN A CD  
4011 O OE1 . GLN A 508 ? 2.4407 2.7369 2.6327 -0.3657 -0.3830 0.2912  507 GLN A OE1 
4012 N NE2 . GLN A 508 ? 2.2832 2.5665 2.4769 -0.3350 -0.3793 0.2932  507 GLN A NE2 
4013 N N   . PRO A 509 ? 2.3331 2.8519 2.8573 -0.3339 -0.3835 0.3175  508 PRO A N   
4014 C CA  . PRO A 509 ? 2.3387 2.8981 2.9357 -0.3130 -0.3884 0.3264  508 PRO A CA  
4015 C C   . PRO A 509 ? 2.3111 2.8508 2.8902 -0.2867 -0.3704 0.3197  508 PRO A C   
4016 O O   . PRO A 509 ? 2.3189 2.8460 2.8753 -0.2777 -0.3377 0.3064  508 PRO A O   
4017 C CB  . PRO A 509 ? 2.3249 2.9315 2.9856 -0.3106 -0.3634 0.3243  508 PRO A CB  
4018 C CG  . PRO A 509 ? 2.3315 2.9268 2.9604 -0.3379 -0.3610 0.3200  508 PRO A CG  
4019 C CD  . PRO A 509 ? 2.3339 2.8703 2.8716 -0.3447 -0.3606 0.3108  508 PRO A CD  
4020 N N   . LYS A 510 ? 2.2454 2.7799 2.8323 -0.2752 -0.3929 0.3288  509 LYS A N   
4021 C CA  . LYS A 510 ? 2.1297 2.6407 2.6959 -0.2523 -0.3799 0.3236  509 LYS A CA  
4022 C C   . LYS A 510 ? 2.0698 2.5883 2.6462 -0.2344 -0.3388 0.3100  509 LYS A C   
4023 O O   . LYS A 510 ? 1.9820 2.4658 2.5051 -0.2320 -0.3198 0.2981  509 LYS A O   
4024 C CB  . LYS A 510 ? 2.0124 2.5399 2.6233 -0.2357 -0.4031 0.3368  509 LYS A CB  
4025 C CG  . LYS A 510 ? 1.9464 2.4559 2.5357 -0.2509 -0.4461 0.3502  509 LYS A CG  
4026 C CD  . LYS A 510 ? 1.8573 2.3852 2.4957 -0.2329 -0.4699 0.3639  509 LYS A CD  
4027 C CE  . LYS A 510 ? 1.7917 2.2992 2.4060 -0.2488 -0.5156 0.3779  509 LYS A CE  
4028 N NZ  . LYS A 510 ? 1.7368 2.2673 2.4071 -0.2317 -0.5423 0.3927  509 LYS A NZ  
4029 N N   . GLU A 562 ? 2.1903 2.4396 2.2833 -0.5386 -0.0131 0.2052  561 GLU A N   
4030 C CA  . GLU A 562 ? 2.1847 2.3733 2.1946 -0.5307 -0.0099 0.1935  561 GLU A CA  
4031 C C   . GLU A 562 ? 2.2143 2.3755 2.1840 -0.5433 -0.0401 0.1928  561 GLU A C   
4032 O O   . GLU A 562 ? 2.1359 2.2899 2.0902 -0.5271 -0.0535 0.1888  561 GLU A O   
4033 C CB  . GLU A 562 ? 2.1467 2.3016 2.1186 -0.5414 0.0143  0.1902  561 GLU A CB  
4034 C CG  . GLU A 562 ? 2.0969 2.2550 2.0800 -0.5773 0.0086  0.1987  561 GLU A CG  
4035 C CD  . GLU A 562 ? 1.9924 2.2133 2.0631 -0.5892 0.0125  0.2108  561 GLU A CD  
4036 O OE1 . GLU A 562 ? 1.9652 2.2101 2.0704 -0.5744 0.0397  0.2112  561 GLU A OE1 
4037 O OE2 . GLU A 562 ? 1.9055 2.1504 2.0103 -0.6133 -0.0117 0.2200  561 GLU A OE2 
4038 N N   . SER A 563 ? 2.2618 2.4059 2.2136 -0.5728 -0.0497 0.1968  562 SER A N   
4039 C CA  . SER A 563 ? 2.1751 2.2857 2.0811 -0.5877 -0.0768 0.1960  562 SER A CA  
4040 C C   . SER A 563 ? 1.9489 2.0943 1.8969 -0.5926 -0.1065 0.2043  562 SER A C   
4041 O O   . SER A 563 ? 1.7496 1.8676 1.6590 -0.5991 -0.1295 0.2032  562 SER A O   
4042 C CB  . SER A 563 ? 2.2015 2.2831 2.0776 -0.6195 -0.0793 0.1984  562 SER A CB  
4043 O OG  . SER A 563 ? 2.1861 2.2281 2.0148 -0.6145 -0.0534 0.1907  562 SER A OG  
4044 N N   . ALA A 564 ? 1.9136 2.1170 1.9390 -0.5889 -0.1053 0.2128  563 ALA A N   
4045 C CA  . ALA A 564 ? 1.7934 2.0324 1.8636 -0.5891 -0.1329 0.2211  563 ALA A CA  
4046 C C   . ALA A 564 ? 1.8436 2.0753 1.8970 -0.5587 -0.1334 0.2146  563 ALA A C   
4047 O O   . ALA A 564 ? 1.9202 2.1137 1.9199 -0.5422 -0.1181 0.2035  563 ALA A O   
4048 C CB  . ALA A 564 ? 1.6139 1.9177 1.7755 -0.5927 -0.1298 0.2323  563 ALA A CB  
4049 N N   . LYS A 565 ? 1.6622 1.9308 1.7633 -0.5517 -0.1516 0.2219  564 LYS A N   
4050 C CA  . LYS A 565 ? 1.3451 1.6088 1.4347 -0.5253 -0.1547 0.2173  564 LYS A CA  
4051 C C   . LYS A 565 ? 1.1573 1.3719 1.1774 -0.5290 -0.1725 0.2123  564 LYS A C   
4052 O O   . LYS A 565 ? 1.1544 1.3242 1.1149 -0.5388 -0.1675 0.2055  564 LYS A O   
4053 C CB  . LYS A 565 ? 1.2164 1.4775 1.3019 -0.4970 -0.1235 0.2078  564 LYS A CB  
4054 C CG  . LYS A 565 ? 1.2789 1.5859 1.4305 -0.4896 -0.1031 0.2122  564 LYS A CG  
4055 C CD  . LYS A 565 ? 1.2472 1.5594 1.4060 -0.4574 -0.0827 0.2052  564 LYS A CD  
4056 C CE  . LYS A 565 ? 1.2241 1.4908 1.3207 -0.4455 -0.0613 0.1922  564 LYS A CE  
4057 N NZ  . LYS A 565 ? 1.1638 1.4289 1.2587 -0.4153 -0.0518 0.1851  564 LYS A NZ  
4058 N N   . PRO A 566 ? 1.0843 1.3056 1.1111 -0.5210 -0.1925 0.2159  565 PRO A N   
4059 C CA  . PRO A 566 ? 1.2424 1.4200 1.2076 -0.5203 -0.2069 0.2116  565 PRO A CA  
4060 C C   . PRO A 566 ? 1.1825 1.3266 1.1007 -0.4972 -0.1848 0.1986  565 PRO A C   
4061 O O   . PRO A 566 ? 0.9147 1.0772 0.8576 -0.4753 -0.1647 0.1942  565 PRO A O   
4062 C CB  . PRO A 566 ? 1.1683 1.3721 1.1685 -0.5140 -0.2296 0.2204  565 PRO A CB  
4063 C CG  . PRO A 566 ? 1.0612 1.3236 1.1434 -0.5098 -0.2272 0.2288  565 PRO A CG  
4064 C CD  . PRO A 566 ? 0.9769 1.2502 1.0751 -0.5091 -0.1988 0.2243  565 PRO A CD  
4065 N N   . LYS A 567 ? 1.1747 1.2694 1.0261 -0.5020 -0.1889 0.1925  566 LYS A N   
4066 C CA  . LYS A 567 ? 1.1223 1.1860 0.9320 -0.4811 -0.1704 0.1807  566 LYS A CA  
4067 C C   . LYS A 567 ? 1.0992 1.1651 0.9103 -0.4649 -0.1778 0.1810  566 LYS A C   
4068 O O   . LYS A 567 ? 1.1031 1.1697 0.9144 -0.4749 -0.2001 0.1886  566 LYS A O   
4069 C CB  . LYS A 567 ? 1.0728 1.0814 0.8112 -0.4918 -0.1679 0.1735  566 LYS A CB  
4070 C CG  . LYS A 567 ? 1.0692 1.0665 0.7959 -0.5153 -0.1680 0.1752  566 LYS A CG  
4071 C CD  . LYS A 567 ? 1.0811 1.0894 0.8247 -0.5075 -0.1437 0.1709  566 LYS A CD  
4072 C CE  . LYS A 567 ? 1.2883 1.2887 1.0260 -0.5342 -0.1451 0.1747  566 LYS A CE  
4073 N NZ  . LYS A 567 ? 1.3798 1.3984 1.1443 -0.5303 -0.1222 0.1736  566 LYS A NZ  
4074 N N   . LEU A 568 ? 1.0889 1.1549 0.9011 -0.4404 -0.1599 0.1731  567 LEU A N   
4075 C CA  . LEU A 568 ? 1.0877 1.1446 0.8884 -0.4258 -0.1630 0.1712  567 LEU A CA  
4076 C C   . LEU A 568 ? 1.1604 1.1795 0.9132 -0.4133 -0.1459 0.1591  567 LEU A C   
4077 O O   . LEU A 568 ? 1.1398 1.1626 0.9000 -0.3973 -0.1280 0.1516  567 LEU A O   
4078 C CB  . LEU A 568 ? 0.9528 1.0493 0.8079 -0.4070 -0.1603 0.1740  567 LEU A CB  
4079 C CG  . LEU A 568 ? 0.9958 1.0808 0.8382 -0.3901 -0.1588 0.1704  567 LEU A CG  
4080 C CD1 . LEU A 568 ? 0.9649 1.0246 0.7727 -0.4025 -0.1766 0.1753  567 LEU A CD1 
4081 C CD2 . LEU A 568 ? 1.0044 1.1258 0.8990 -0.3727 -0.1575 0.1735  567 LEU A CD2 
4082 N N   . PHE A 569 ? 1.1504 1.1316 0.8535 -0.4205 -0.1518 0.1573  568 PHE A N   
4083 C CA  . PHE A 569 ? 1.2251 1.1726 0.8878 -0.4070 -0.1362 0.1467  568 PHE A CA  
4084 C C   . PHE A 569 ? 1.2155 1.1700 0.8900 -0.3896 -0.1339 0.1457  568 PHE A C   
4085 O O   . PHE A 569 ? 1.2261 1.1841 0.9039 -0.3951 -0.1478 0.1530  568 PHE A O   
4086 C CB  . PHE A 569 ? 1.2985 1.1983 0.8995 -0.4220 -0.1400 0.1446  568 PHE A CB  
4087 C CG  . PHE A 569 ? 1.3475 1.2347 0.9313 -0.4417 -0.1439 0.1458  568 PHE A CG  
4088 C CD1 . PHE A 569 ? 1.3021 1.2017 0.9034 -0.4382 -0.1317 0.1425  568 PHE A CD1 
4089 C CD2 . PHE A 569 ? 1.4123 1.2707 0.9580 -0.4646 -0.1596 0.1501  568 PHE A CD2 
4090 C CE1 . PHE A 569 ? 1.2422 1.1282 0.8267 -0.4577 -0.1342 0.1439  568 PHE A CE1 
4091 C CE2 . PHE A 569 ? 1.3070 1.1518 0.8362 -0.4843 -0.1638 0.1512  568 PHE A CE2 
4092 C CZ  . PHE A 569 ? 1.1823 1.0419 0.7325 -0.4811 -0.1505 0.1483  568 PHE A CZ  
4093 N N   . VAL A 570 ? 1.1360 1.0912 0.8163 -0.3692 -0.1173 0.1370  569 VAL A N   
4094 C CA  . VAL A 570 ? 1.0964 1.0523 0.7825 -0.3542 -0.1133 0.1350  569 VAL A CA  
4095 C C   . VAL A 570 ? 1.0605 0.9822 0.7079 -0.3455 -0.0989 0.1253  569 VAL A C   
4096 O O   . VAL A 570 ? 1.1163 1.0313 0.7585 -0.3365 -0.0873 0.1174  569 VAL A O   
4097 C CB  . VAL A 570 ? 0.9226 0.9126 0.6571 -0.3360 -0.1079 0.1336  569 VAL A CB  
4098 C CG1 . VAL A 570 ? 0.9191 0.9077 0.6585 -0.3236 -0.1052 0.1322  569 VAL A CG1 
4099 C CG2 . VAL A 570 ? 0.8146 0.8400 0.5916 -0.3419 -0.1195 0.1430  569 VAL A CG2 
4100 N N   . PHE A 571 ? 0.8684 0.7669 0.4877 -0.3481 -0.0993 0.1261  570 PHE A N   
4101 C CA  . PHE A 571 ? 0.8852 0.7540 0.4736 -0.3380 -0.0835 0.1172  570 PHE A CA  
4102 C C   . PHE A 571 ? 1.0514 0.9273 0.6563 -0.3251 -0.0771 0.1165  570 PHE A C   
4103 O O   . PHE A 571 ? 1.0775 0.9521 0.6793 -0.3319 -0.0846 0.1236  570 PHE A O   
4104 C CB  . PHE A 571 ? 0.9043 0.7301 0.4358 -0.3527 -0.0841 0.1172  570 PHE A CB  
4105 C CG  . PHE A 571 ? 1.0182 0.8124 0.5183 -0.3417 -0.0662 0.1087  570 PHE A CG  
4106 C CD1 . PHE A 571 ? 1.0565 0.8395 0.5486 -0.3308 -0.0539 0.0995  570 PHE A CD1 
4107 C CD2 . PHE A 571 ? 1.1081 0.8823 0.5861 -0.3421 -0.0610 0.1101  570 PHE A CD2 
4108 C CE1 . PHE A 571 ? 0.9394 0.6950 0.4069 -0.3195 -0.0375 0.0919  570 PHE A CE1 
4109 C CE2 . PHE A 571 ? 1.1484 0.8952 0.6013 -0.3314 -0.0419 0.1024  570 PHE A CE2 
4110 C CZ  . PHE A 571 ? 1.0680 0.8069 0.5179 -0.3197 -0.0305 0.0933  570 PHE A CZ  
4111 N N   . ILE A 572 ? 1.1417 1.0236 0.7635 -0.3069 -0.0640 0.1083  571 ILE A N   
4112 C CA  . ILE A 572 ? 1.0825 0.9719 0.7236 -0.2943 -0.0563 0.1066  571 ILE A CA  
4113 C C   . ILE A 572 ? 1.0192 0.8781 0.6299 -0.2886 -0.0401 0.0996  571 ILE A C   
4114 O O   . ILE A 572 ? 0.9616 0.8078 0.5598 -0.2821 -0.0326 0.0922  571 ILE A O   
4115 C CB  . ILE A 572 ? 0.9302 0.8487 0.6158 -0.2775 -0.0540 0.1019  571 ILE A CB  
4116 C CG1 . ILE A 572 ? 0.9190 0.8666 0.6348 -0.2809 -0.0666 0.1077  571 ILE A CG1 
4117 C CG2 . ILE A 572 ? 0.8800 0.8063 0.5876 -0.2663 -0.0472 0.1003  571 ILE A CG2 
4118 C CD1 . ILE A 572 ? 0.7544 0.7265 0.5094 -0.2645 -0.0645 0.1031  571 ILE A CD1 
4119 N N   . ASN A 573 ? 0.9456 0.7912 0.5437 -0.2904 -0.0338 0.1022  572 ASN A N   
4120 C CA  . ASN A 573 ? 0.9583 0.7763 0.5313 -0.2836 -0.0152 0.0956  572 ASN A CA  
4121 C C   . ASN A 573 ? 1.0264 0.8612 0.6351 -0.2635 -0.0042 0.0871  572 ASN A C   
4122 O O   . ASN A 573 ? 1.0462 0.9113 0.6986 -0.2553 -0.0082 0.0875  572 ASN A O   
4123 C CB  . ASN A 573 ? 1.0576 0.8571 0.6099 -0.2898 -0.0082 0.1005  572 ASN A CB  
4124 C CG  . ASN A 573 ? 1.2850 1.0510 0.7837 -0.3089 -0.0160 0.1064  572 ASN A CG  
4125 O OD1 . ASN A 573 ? 1.3455 1.0788 0.8017 -0.3132 -0.0100 0.1023  572 ASN A OD1 
4126 N ND2 . ASN A 573 ? 1.3375 1.1090 0.8363 -0.3204 -0.0306 0.1161  572 ASN A ND2 
4127 N N   . GLY A 574 ? 1.0659 0.8794 0.6555 -0.2554 0.0086  0.0793  573 GLY A N   
4128 C CA  . GLY A 574 ? 1.0539 0.8809 0.6766 -0.2362 0.0177  0.0714  573 GLY A CA  
4129 C C   . GLY A 574 ? 1.0593 0.9008 0.7010 -0.2267 0.0088  0.0663  573 GLY A C   
4130 O O   . GLY A 574 ? 1.0497 0.8738 0.6757 -0.2186 0.0142  0.0597  573 GLY A O   
4131 N N   . THR A 575 ? 0.9519 0.8217 0.6242 -0.2273 -0.0041 0.0694  574 THR A N   
4132 C CA  . THR A 575 ? 0.8706 0.7559 0.5667 -0.2156 -0.0109 0.0643  574 THR A CA  
4133 C C   . THR A 575 ? 0.8880 0.7901 0.5923 -0.2237 -0.0239 0.0694  574 THR A C   
4134 O O   . THR A 575 ? 0.9496 0.8650 0.6635 -0.2333 -0.0296 0.0769  574 THR A O   
4135 C CB  . THR A 575 ? 0.8584 0.7656 0.5991 -0.2003 -0.0095 0.0602  574 THR A CB  
4136 O OG1 . THR A 575 ? 0.9846 0.8807 0.7261 -0.1862 -0.0021 0.0521  574 THR A OG1 
4137 C CG2 . THR A 575 ? 0.7051 0.6369 0.4764 -0.1953 -0.0220 0.0602  574 THR A CG2 
4138 N N   . VAL A 576 ? 0.6995 0.5998 0.3995 -0.2197 -0.0278 0.0657  575 VAL A N   
4139 C CA  . VAL A 576 ? 0.5823 0.5018 0.2974 -0.2243 -0.0369 0.0698  575 VAL A CA  
4140 C C   . VAL A 576 ? 0.6721 0.5993 0.4061 -0.2086 -0.0388 0.0632  575 VAL A C   
4141 O O   . VAL A 576 ? 0.7479 0.6588 0.4707 -0.1980 -0.0354 0.0560  575 VAL A O   
4142 C CB  . VAL A 576 ? 0.8278 0.7361 0.5146 -0.2401 -0.0399 0.0741  575 VAL A CB  
4143 C CG1 . VAL A 576 ? 0.7960 0.6801 0.4548 -0.2359 -0.0356 0.0677  575 VAL A CG1 
4144 C CG2 . VAL A 576 ? 0.8203 0.7549 0.5323 -0.2455 -0.0475 0.0801  575 VAL A CG2 
4145 N N   . SER A 577 ? 0.7505 0.7001 0.5114 -0.2066 -0.0446 0.0656  576 SER A N   
4146 C CA  . SER A 577 ? 0.7486 0.7037 0.5266 -0.1915 -0.0474 0.0594  576 SER A CA  
4147 C C   . SER A 577 ? 0.7633 0.7143 0.5286 -0.1933 -0.0478 0.0594  576 SER A C   
4148 O O   . SER A 577 ? 0.9054 0.8634 0.6672 -0.2063 -0.0475 0.0660  576 SER A O   
4149 C CB  . SER A 577 ? 0.7011 0.6800 0.5162 -0.1866 -0.0522 0.0614  576 SER A CB  
4150 O OG  . SER A 577 ? 0.8865 0.8687 0.7146 -0.1854 -0.0504 0.0617  576 SER A OG  
4151 N N   . TYR A 578 ? 0.8369 0.7762 0.5959 -0.1808 -0.0487 0.0523  577 TYR A N   
4152 C CA  . TYR A 578 ? 0.7926 0.7238 0.5353 -0.1822 -0.0465 0.0521  577 TYR A CA  
4153 C C   . TYR A 578 ? 0.7974 0.7522 0.5644 -0.1854 -0.0464 0.0574  577 TYR A C   
4154 O O   . TYR A 578 ? 0.9144 0.8699 0.6733 -0.1933 -0.0416 0.0610  577 TYR A O   
4155 C CB  . TYR A 578 ? 0.7044 0.6132 0.4303 -0.1673 -0.0484 0.0435  577 TYR A CB  
4156 C CG  . TYR A 578 ? 0.8661 0.7472 0.5611 -0.1652 -0.0470 0.0393  577 TYR A CG  
4157 C CD1 . TYR A 578 ? 1.0467 0.9088 0.7082 -0.1765 -0.0411 0.0417  577 TYR A CD1 
4158 C CD2 . TYR A 578 ? 0.8181 0.6915 0.5186 -0.1518 -0.0517 0.0330  577 TYR A CD2 
4159 C CE1 . TYR A 578 ? 0.8079 0.6409 0.4383 -0.1738 -0.0396 0.0378  577 TYR A CE1 
4160 C CE2 . TYR A 578 ? 1.0059 0.8537 0.6799 -0.1481 -0.0499 0.0293  577 TYR A CE2 
4161 C CZ  . TYR A 578 ? 0.9286 0.7547 0.5654 -0.1587 -0.0438 0.0316  577 TYR A CZ  
4162 O OH  . TYR A 578 ? 0.9767 0.7739 0.5847 -0.1540 -0.0419 0.0278  577 TYR A OH  
4163 N N   . ASN A 579 ? 0.8172 0.7913 0.6153 -0.1794 -0.0510 0.0581  578 ASN A N   
4164 C CA  . ASN A 579 ? 0.8409 0.8372 0.6640 -0.1811 -0.0509 0.0635  578 ASN A CA  
4165 C C   . ASN A 579 ? 0.8239 0.8378 0.6567 -0.1972 -0.0511 0.0736  578 ASN A C   
4166 O O   . ASN A 579 ? 0.9425 0.9727 0.7907 -0.2014 -0.0493 0.0791  578 ASN A O   
4167 C CB  . ASN A 579 ? 0.9375 0.9450 0.7882 -0.1693 -0.0565 0.0610  578 ASN A CB  
4168 C CG  . ASN A 579 ? 0.8908 0.9056 0.7562 -0.1712 -0.0610 0.0626  578 ASN A CG  
4169 O OD1 . ASN A 579 ? 0.7791 0.7872 0.6310 -0.1790 -0.0593 0.0642  578 ASN A OD1 
4170 N ND2 . ASN A 579 ? 0.7795 0.8053 0.6707 -0.1641 -0.0658 0.0621  578 ASN A ND2 
4171 N N   . GLU A 580 ? 0.7431 0.7523 0.5663 -0.2059 -0.0533 0.0760  579 GLU A N   
4172 C CA  . GLU A 580 ? 0.7899 0.8096 0.6152 -0.2223 -0.0563 0.0854  579 GLU A CA  
4173 C C   . GLU A 580 ? 0.9242 0.9331 0.7255 -0.2345 -0.0526 0.0872  579 GLU A C   
4174 O O   . GLU A 580 ? 0.9708 0.9934 0.7808 -0.2476 -0.0553 0.0951  579 GLU A O   
4175 C CB  . GLU A 580 ? 0.7215 0.7340 0.5383 -0.2274 -0.0591 0.0871  579 GLU A CB  
4176 C CG  . GLU A 580 ? 0.8617 0.8857 0.7038 -0.2187 -0.0620 0.0871  579 GLU A CG  
4177 C CD  . GLU A 580 ? 0.9502 0.9616 0.7801 -0.2213 -0.0601 0.0867  579 GLU A CD  
4178 O OE1 . GLU A 580 ? 0.8466 0.8387 0.6554 -0.2178 -0.0543 0.0803  579 GLU A OE1 
4179 O OE2 . GLU A 580 ? 0.9153 0.9350 0.7566 -0.2261 -0.0637 0.0929  579 GLU A OE2 
4180 N N   . ILE A 581 ? 0.9895 0.9730 0.7612 -0.2302 -0.0474 0.0800  580 ILE A N   
4181 C CA  . ILE A 581 ? 0.9462 0.9139 0.6910 -0.2405 -0.0428 0.0805  580 ILE A CA  
4182 C C   . ILE A 581 ? 0.9780 0.9601 0.7389 -0.2404 -0.0378 0.0829  580 ILE A C   
4183 O O   . ILE A 581 ? 0.9392 0.9298 0.7029 -0.2551 -0.0363 0.0895  580 ILE A O   
4184 C CB  . ILE A 581 ? 0.7644 0.6986 0.4736 -0.2323 -0.0386 0.0718  580 ILE A CB  
4185 C CG1 . ILE A 581 ? 0.7655 0.6840 0.4562 -0.2356 -0.0403 0.0707  580 ILE A CG1 
4186 C CG2 . ILE A 581 ? 0.6617 0.5767 0.3428 -0.2394 -0.0324 0.0713  580 ILE A CG2 
4187 C CD1 . ILE A 581 ? 0.6533 0.5417 0.3158 -0.2246 -0.0368 0.0622  580 ILE A CD1 
4188 N N   . ARG A 582 ? 0.9303 0.9148 0.7026 -0.2241 -0.0350 0.0777  581 ARG A N   
4189 C CA  . ARG A 582 ? 0.8868 0.8826 0.6730 -0.2216 -0.0276 0.0793  581 ARG A CA  
4190 C C   . ARG A 582 ? 0.9369 0.9661 0.7594 -0.2319 -0.0297 0.0893  581 ARG A C   
4191 O O   . ARG A 582 ? 0.9980 1.0391 0.8318 -0.2385 -0.0223 0.0939  581 ARG A O   
4192 C CB  . ARG A 582 ? 0.8184 0.8115 0.6127 -0.2021 -0.0269 0.0725  581 ARG A CB  
4193 C CG  . ARG A 582 ? 0.8671 0.8589 0.6616 -0.1967 -0.0159 0.0716  581 ARG A CG  
4194 C CD  . ARG A 582 ? 0.9358 0.9234 0.7373 -0.1781 -0.0172 0.0651  581 ARG A CD  
4195 N NE  . ARG A 582 ? 0.9586 0.9732 0.7980 -0.1751 -0.0239 0.0689  581 ARG A NE  
4196 C CZ  . ARG A 582 ? 0.9437 0.9569 0.7914 -0.1656 -0.0336 0.0647  581 ARG A CZ  
4197 N NH1 . ARG A 582 ? 0.7803 0.7693 0.6050 -0.1574 -0.0386 0.0563  581 ARG A NH1 
4198 N NH2 . ARG A 582 ? 0.8761 0.9121 0.7564 -0.1644 -0.0388 0.0692  581 ARG A NH2 
4199 N N   . CYS A 583 ? 0.8736 0.9177 0.7150 -0.2334 -0.0397 0.0932  582 CYS A N   
4200 C CA  . CYS A 583 ? 0.8891 0.9644 0.7670 -0.2404 -0.0448 0.1029  582 CYS A CA  
4201 C C   . CYS A 583 ? 0.8995 0.9819 0.7762 -0.2608 -0.0469 0.1109  582 CYS A C   
4202 O O   . CYS A 583 ? 0.9633 1.0712 0.8706 -0.2665 -0.0461 0.1182  582 CYS A O   
4203 C CB  . CYS A 583 ? 0.8000 0.8841 0.6926 -0.2375 -0.0557 0.1054  582 CYS A CB  
4204 S SG  . CYS A 583 ? 1.1207 1.2090 1.0334 -0.2156 -0.0548 0.0994  582 CYS A SG  
4205 N N   . ALA A 584 ? 0.9315 0.9907 0.7737 -0.2718 -0.0497 0.1095  583 ALA A N   
4206 C CA  . ALA A 584 ? 0.8003 0.8601 0.6350 -0.2930 -0.0535 0.1163  583 ALA A CA  
4207 C C   . ALA A 584 ? 0.8886 0.9529 0.7283 -0.2974 -0.0418 0.1172  583 ALA A C   
4208 O O   . ALA A 584 ? 1.0227 1.1059 0.8824 -0.3128 -0.0440 0.1254  583 ALA A O   
4209 C CB  . ALA A 584 ? 0.6542 0.6806 0.4438 -0.3011 -0.0563 0.1127  583 ALA A CB  
4210 N N   . TYR A 585 ? 0.8358 0.8822 0.6577 -0.2842 -0.0293 0.1090  584 TYR A N   
4211 C CA  . TYR A 585 ? 0.8519 0.8987 0.6748 -0.2870 -0.0152 0.1095  584 TYR A CA  
4212 C C   . TYR A 585 ? 0.9115 0.9935 0.7822 -0.2804 -0.0096 0.1143  584 TYR A C   
4213 O O   . TYR A 585 ? 0.8780 0.9804 0.7729 -0.2918 -0.0037 0.1214  584 TYR A O   
4214 C CB  . TYR A 585 ? 0.8018 0.8135 0.5854 -0.2743 -0.0046 0.0994  584 TYR A CB  
4215 C CG  . TYR A 585 ? 0.8788 0.8544 0.6154 -0.2810 -0.0076 0.0951  584 TYR A CG  
4216 C CD1 . TYR A 585 ? 0.8449 0.8063 0.5656 -0.2742 -0.0173 0.0905  584 TYR A CD1 
4217 C CD2 . TYR A 585 ? 0.7986 0.7531 0.5068 -0.2940 0.0005  0.0959  584 TYR A CD2 
4218 C CE1 . TYR A 585 ? 0.8547 0.7824 0.5335 -0.2785 -0.0186 0.0864  584 TYR A CE1 
4219 C CE2 . TYR A 585 ? 0.6958 0.6141 0.3590 -0.2993 -0.0022 0.0920  584 TYR A CE2 
4220 C CZ  . TYR A 585 ? 0.9338 0.8389 0.5827 -0.2905 -0.0116 0.0870  584 TYR A CZ  
4221 O OH  . TYR A 585 ? 1.0065 0.8751 0.6118 -0.2935 -0.0130 0.0828  584 TYR A OH  
4222 N N   . GLU A 586 ? 0.9289 1.0179 0.8149 -0.2620 -0.0111 0.1107  585 GLU A N   
4223 C CA  . GLU A 586 ? 0.8433 0.9618 0.7719 -0.2534 -0.0048 0.1147  585 GLU A CA  
4224 C C   . GLU A 586 ? 0.9490 1.1036 0.9199 -0.2677 -0.0134 0.1266  585 GLU A C   
4225 O O   . GLU A 586 ? 0.9136 1.0935 0.9192 -0.2691 -0.0040 0.1322  585 GLU A O   
4226 C CB  . GLU A 586 ? 0.7215 0.8404 0.6593 -0.2336 -0.0092 0.1097  585 GLU A CB  
4227 C CG  . GLU A 586 ? 0.9312 1.0164 0.8323 -0.2187 -0.0041 0.0981  585 GLU A CG  
4228 C CD  . GLU A 586 ? 1.1590 1.2445 1.0702 -0.2023 -0.0120 0.0936  585 GLU A CD  
4229 O OE1 . GLU A 586 ? 1.1707 1.2768 1.1084 -0.2044 -0.0228 0.0991  585 GLU A OE1 
4230 O OE2 . GLU A 586 ? 1.2976 1.3607 1.1887 -0.1880 -0.0083 0.0847  585 GLU A OE2 
4231 N N   . VAL A 587 ? 0.9332 1.0891 0.9007 -0.2781 -0.0311 0.1306  586 VAL A N   
4232 C CA  . VAL A 587 ? 0.9396 1.1272 0.9453 -0.2902 -0.0446 0.1421  586 VAL A CA  
4233 C C   . VAL A 587 ? 1.0086 1.2036 1.0179 -0.3128 -0.0456 0.1490  586 VAL A C   
4234 O O   . VAL A 587 ? 1.0826 1.3100 1.1340 -0.3224 -0.0529 0.1590  586 VAL A O   
4235 C CB  . VAL A 587 ? 0.8652 1.0477 0.8627 -0.2918 -0.0637 0.1442  586 VAL A CB  
4236 C CG1 . VAL A 587 ? 0.6974 0.8989 0.7145 -0.3110 -0.0816 0.1559  586 VAL A CG1 
4237 C CG2 . VAL A 587 ? 0.8164 1.0077 0.8340 -0.2720 -0.0647 0.1422  586 VAL A CG2 
4238 N N   . SER A 588 ? 1.0076 1.1723 0.9743 -0.3215 -0.0389 0.1437  587 SER A N   
4239 C CA  . SER A 588 ? 0.9935 1.1616 0.9611 -0.3433 -0.0369 0.1493  587 SER A CA  
4240 C C   . SER A 588 ? 1.0729 1.2648 1.0760 -0.3410 -0.0180 0.1521  587 SER A C   
4241 O O   . SER A 588 ? 1.1342 1.3573 1.1782 -0.3548 -0.0202 0.1617  587 SER A O   
4242 C CB  . SER A 588 ? 0.9418 1.0667 0.8510 -0.3515 -0.0329 0.1424  587 SER A CB  
4243 O OG  . SER A 588 ? 1.0188 1.1247 0.8994 -0.3603 -0.0501 0.1424  587 SER A OG  
4244 N N   . GLN A 589 ? 1.2290 1.4054 1.2166 -0.3232 0.0007  0.1439  588 GLN A N   
4245 C CA  . GLN A 589 ? 1.2927 1.4832 1.3038 -0.3200 0.0230  0.1454  588 GLN A CA  
4246 C C   . GLN A 589 ? 1.2994 1.5314 1.3701 -0.3082 0.0253  0.1511  588 GLN A C   
4247 O O   . GLN A 589 ? 1.4624 1.7110 1.5604 -0.3046 0.0453  0.1533  588 GLN A O   
4248 C CB  . GLN A 589 ? 1.3757 1.5281 1.3411 -0.3052 0.0413  0.1344  588 GLN A CB  
4249 C CG  . GLN A 589 ? 1.5769 1.6871 1.4843 -0.3159 0.0406  0.1292  588 GLN A CG  
4250 C CD  . GLN A 589 ? 1.7128 1.7819 1.5712 -0.2973 0.0471  0.1174  588 GLN A CD  
4251 O OE1 . GLN A 589 ? 1.7336 1.7665 1.5444 -0.3011 0.0440  0.1123  588 GLN A OE1 
4252 N NE2 . GLN A 589 ? 1.7117 1.7846 1.5812 -0.2767 0.0551  0.1131  588 GLN A NE2 
4253 N N   . SER A 590 ? 1.2103 1.4574 1.3006 -0.3020 0.0062  0.1538  589 SER A N   
4254 C CA  . SER A 590 ? 1.2563 1.5405 1.4023 -0.2897 0.0065  0.1596  589 SER A CA  
4255 C C   . SER A 590 ? 1.4052 1.7284 1.6008 -0.3058 -0.0104 0.1726  589 SER A C   
4256 O O   . SER A 590 ? 1.6211 1.9746 1.8600 -0.3129 -0.0006 0.1798  589 SER A O   
4257 C CB  . SER A 590 ? 1.1908 1.4659 1.3296 -0.2689 -0.0017 0.1541  589 SER A CB  
4258 O OG  . SER A 590 ? 1.2342 1.4974 1.3518 -0.2756 -0.0241 0.1546  589 SER A OG  
4259 N N   . SER A 591 ? 1.3325 1.6542 1.5219 -0.3122 -0.0359 0.1761  590 SER A N   
4260 C CA  . SER A 591 ? 1.3187 1.6741 1.5521 -0.3269 -0.0560 0.1887  590 SER A CA  
4261 C C   . SER A 591 ? 1.1210 1.4598 1.3239 -0.3510 -0.0773 0.1920  590 SER A C   
4262 O O   . SER A 591 ? 0.8449 1.1498 0.9984 -0.3507 -0.0869 0.1863  590 SER A O   
4263 C CB  . SER A 591 ? 1.4830 1.8590 1.7501 -0.3115 -0.0700 0.1934  590 SER A CB  
4264 O OG  . SER A 591 ? 1.4879 1.8988 1.8030 -0.3238 -0.0904 0.2066  590 SER A OG  
4265 N N   . GLY A 592 ? 0.9623 1.3242 1.1953 -0.3718 -0.0832 0.2010  591 GLY A N   
4266 C CA  . GLY A 592 ? 0.9050 1.2696 1.1380 -0.3939 -0.1122 0.2096  591 GLY A CA  
4267 C C   . GLY A 592 ? 0.9907 1.3135 1.1609 -0.4131 -0.1214 0.2056  591 GLY A C   
4268 O O   . GLY A 592 ? 0.9997 1.3235 1.1704 -0.4359 -0.1254 0.2098  591 GLY A O   
4269 N N   . TYR A 593 ? 1.1143 1.4001 1.2319 -0.4042 -0.1247 0.1977  592 TYR A N   
4270 C CA  . TYR A 593 ? 1.0667 1.3091 1.1217 -0.4194 -0.1321 0.1932  592 TYR A CA  
4271 C C   . TYR A 593 ? 1.1379 1.3471 1.1483 -0.4136 -0.1086 0.1815  592 TYR A C   
4272 O O   . TYR A 593 ? 1.2167 1.4323 1.2385 -0.3960 -0.0879 0.1761  592 TYR A O   
4273 C CB  . TYR A 593 ? 1.0331 1.2527 1.0558 -0.4135 -0.1480 0.1916  592 TYR A CB  
4274 C CG  . TYR A 593 ? 1.0573 1.2917 1.0996 -0.4259 -0.1768 0.2030  592 TYR A CG  
4275 C CD1 . TYR A 593 ? 1.1160 1.3923 1.2186 -0.4177 -0.1854 0.2118  592 TYR A CD1 
4276 C CD2 . TYR A 593 ? 1.1084 1.3113 1.1059 -0.4451 -0.1960 0.2049  592 TYR A CD2 
4277 C CE1 . TYR A 593 ? 1.1654 1.4533 1.2849 -0.4286 -0.2144 0.2228  592 TYR A CE1 
4278 C CE2 . TYR A 593 ? 1.2607 1.4725 1.2708 -0.4569 -0.2245 0.2156  592 TYR A CE2 
4279 C CZ  . TYR A 593 ? 1.2541 1.5088 1.3258 -0.4487 -0.2346 0.2247  592 TYR A CZ  
4280 O OH  . TYR A 593 ? 1.2685 1.5298 1.3513 -0.4599 -0.2654 0.2358  592 TYR A OH  
4281 N N   . GLU A 594 ? 1.0611 1.2320 1.0183 -0.4285 -0.1128 0.1779  593 GLU A N   
4282 C CA  . GLU A 594 ? 1.0660 1.1967 0.9707 -0.4203 -0.0956 0.1663  593 GLU A CA  
4283 C C   . GLU A 594 ? 1.1834 1.2854 1.0489 -0.4100 -0.1033 0.1605  593 GLU A C   
4284 O O   . GLU A 594 ? 1.1705 1.2592 1.0162 -0.4229 -0.1212 0.1642  593 GLU A O   
4285 C CB  . GLU A 594 ? 1.0997 1.2026 0.9682 -0.4422 -0.0938 0.1657  593 GLU A CB  
4286 C CG  . GLU A 594 ? 1.0692 1.1948 0.9705 -0.4543 -0.0821 0.1707  593 GLU A CG  
4287 C CD  . GLU A 594 ? 1.1280 1.2573 1.0373 -0.4349 -0.0557 0.1646  593 GLU A CD  
4288 O OE1 . GLU A 594 ? 1.1914 1.3547 1.1466 -0.4194 -0.0499 0.1667  593 GLU A OE1 
4289 O OE2 . GLU A 594 ? 1.1550 1.2502 1.0219 -0.4351 -0.0412 0.1578  593 GLU A OE2 
4290 N N   . VAL A 595 ? 1.2034 1.2945 1.0571 -0.3873 -0.0897 0.1515  594 VAL A N   
4291 C CA  . VAL A 595 ? 1.1419 1.2118 0.9682 -0.3758 -0.0945 0.1462  594 VAL A CA  
4292 C C   . VAL A 595 ? 1.0428 1.0683 0.8131 -0.3726 -0.0852 0.1361  594 VAL A C   
4293 O O   . VAL A 595 ? 0.9682 0.9817 0.7259 -0.3670 -0.0709 0.1302  594 VAL A O   
4294 C CB  . VAL A 595 ? 1.1131 1.2042 0.9711 -0.3524 -0.0893 0.1439  594 VAL A CB  
4295 C CG1 . VAL A 595 ? 0.9860 1.0615 0.8250 -0.3441 -0.0962 0.1412  594 VAL A CG1 
4296 C CG2 . VAL A 595 ? 1.1474 1.2818 1.0623 -0.3535 -0.0959 0.1537  594 VAL A CG2 
4297 N N   . TYR A 596 ? 1.0116 1.0107 0.7470 -0.3760 -0.0931 0.1344  595 TYR A N   
4298 C CA  . TYR A 596 ? 1.0246 0.9831 0.7112 -0.3694 -0.0840 0.1248  595 TYR A CA  
4299 C C   . TYR A 596 ? 1.1660 1.1165 0.8453 -0.3548 -0.0844 0.1208  595 TYR A C   
4300 O O   . TYR A 596 ? 1.1949 1.1517 0.8799 -0.3604 -0.0958 0.1266  595 TYR A O   
4301 C CB  . TYR A 596 ? 0.9929 0.9181 0.6352 -0.3902 -0.0893 0.1258  595 TYR A CB  
4302 C CG  . TYR A 596 ? 1.1666 1.1004 0.8185 -0.4077 -0.0896 0.1306  595 TYR A CG  
4303 C CD1 . TYR A 596 ? 1.2020 1.1644 0.8869 -0.4254 -0.1036 0.1412  595 TYR A CD1 
4304 C CD2 . TYR A 596 ? 1.2032 1.1166 0.8328 -0.4067 -0.0759 0.1251  595 TYR A CD2 
4305 C CE1 . TYR A 596 ? 1.2598 1.2337 0.9598 -0.4423 -0.1028 0.1462  595 TYR A CE1 
4306 C CE2 . TYR A 596 ? 1.2640 1.1850 0.9033 -0.4238 -0.0740 0.1299  595 TYR A CE2 
4307 C CZ  . TYR A 596 ? 1.3244 1.2774 1.0013 -0.4420 -0.0869 0.1406  595 TYR A CZ  
4308 O OH  . TYR A 596 ? 1.2953 1.2594 0.9879 -0.4605 -0.0844 0.1461  595 TYR A OH  
4309 N N   . ILE A 597 ? 1.0844 1.0206 0.7518 -0.3364 -0.0725 0.1114  596 ILE A N   
4310 C CA  . ILE A 597 ? 0.9947 0.9272 0.6624 -0.3220 -0.0709 0.1076  596 ILE A CA  
4311 C C   . ILE A 597 ? 0.9802 0.8752 0.6062 -0.3154 -0.0623 0.0991  596 ILE A C   
4312 O O   . ILE A 597 ? 0.9468 0.8224 0.5513 -0.3125 -0.0552 0.0934  596 ILE A O   
4313 C CB  . ILE A 597 ? 0.9283 0.8882 0.6363 -0.3028 -0.0669 0.1051  596 ILE A CB  
4314 C CG1 . ILE A 597 ? 0.7965 0.7603 0.5147 -0.2929 -0.0685 0.1044  596 ILE A CG1 
4315 C CG2 . ILE A 597 ? 0.8673 0.8162 0.5674 -0.2891 -0.0560 0.0963  596 ILE A CG2 
4316 C CD1 . ILE A 597 ? 0.8395 0.8330 0.6005 -0.2795 -0.0693 0.1051  596 ILE A CD1 
4317 N N   . GLY A 598 ? 0.9461 0.8297 0.5604 -0.3128 -0.0623 0.0984  597 GLY A N   
4318 C CA  . GLY A 598 ? 1.0058 0.8557 0.5848 -0.3053 -0.0525 0.0907  597 GLY A CA  
4319 C C   . GLY A 598 ? 1.0444 0.8891 0.6228 -0.2974 -0.0479 0.0894  597 GLY A C   
4320 O O   . GLY A 598 ? 1.0342 0.8978 0.6343 -0.2996 -0.0535 0.0952  597 GLY A O   
4321 N N   . ALA A 599 ? 1.0391 0.8563 0.5917 -0.2882 -0.0367 0.0820  598 ALA A N   
4322 C CA  . ALA A 599 ? 0.9755 0.7884 0.5318 -0.2777 -0.0276 0.0793  598 ALA A CA  
4323 C C   . ALA A 599 ? 0.9778 0.7540 0.4970 -0.2713 -0.0150 0.0718  598 ALA A C   
4324 O O   . ALA A 599 ? 1.1906 0.9471 0.6849 -0.2732 -0.0149 0.0686  598 ALA A O   
4325 C CB  . ALA A 599 ? 0.8689 0.7122 0.4723 -0.2600 -0.0261 0.0761  598 ALA A CB  
4326 N N   . HIS A 600 ? 0.9176 0.6836 0.4333 -0.2634 -0.0034 0.0693  599 HIS A N   
4327 C CA  . HIS A 600 ? 0.9346 0.6684 0.4217 -0.2536 0.0108  0.0618  599 HIS A CA  
4328 C C   . HIS A 600 ? 1.0185 0.7563 0.5197 -0.2379 0.0109  0.0547  599 HIS A C   
4329 O O   . HIS A 600 ? 1.2164 0.9240 0.6845 -0.2354 0.0154  0.0500  599 HIS A O   
4330 C CB  . HIS A 600 ? 1.0512 0.7841 0.5491 -0.2436 0.0256  0.0599  599 HIS A CB  
4331 C CG  . HIS A 600 ? 1.0432 0.7589 0.5127 -0.2585 0.0285  0.0661  599 HIS A CG  
4332 N ND1 . HIS A 600 ? 1.1421 0.8771 0.6245 -0.2712 0.0161  0.0747  599 HIS A ND1 
4333 C CD2 . HIS A 600 ? 1.0858 0.7634 0.5113 -0.2622 0.0423  0.0651  599 HIS A CD2 
4334 C CE1 . HIS A 600 ? 1.2173 0.9261 0.6635 -0.2827 0.0203  0.0790  599 HIS A CE1 
4335 N NE2 . HIS A 600 ? 1.1842 0.8569 0.5939 -0.2778 0.0370  0.0731  599 HIS A NE2 
4336 N N   . ASN A 601 ? 0.9675 0.7394 0.5147 -0.2273 0.0052  0.0539  600 ASN A N   
4337 C CA  . ASN A 601 ? 0.9505 0.7241 0.5075 -0.2135 0.0023  0.0479  600 ASN A CA  
4338 C C   . ASN A 601 ? 0.9584 0.7670 0.5566 -0.2097 -0.0081 0.0495  600 ASN A C   
4339 O O   . ASN A 601 ? 1.0092 0.8423 0.6331 -0.2149 -0.0117 0.0547  600 ASN A O   
4340 C CB  . ASN A 601 ? 1.0835 0.8467 0.6473 -0.1937 0.0123  0.0401  600 ASN A CB  
4341 C CG  . ASN A 601 ? 1.2757 1.0146 0.8170 -0.1837 0.0114  0.0339  600 ASN A CG  
4342 O OD1 . ASN A 601 ? 1.4161 1.1455 0.9363 -0.1918 0.0042  0.0353  600 ASN A OD1 
4343 N ND2 . ASN A 601 ? 1.3203 1.0484 0.8668 -0.1658 0.0190  0.0275  600 ASN A ND2 
4344 N N   . ILE A 602 ? 0.9717 0.7788 0.5715 -0.2009 -0.0129 0.0454  601 ILE A N   
4345 C CA  . ILE A 602 ? 0.9832 0.8176 0.6193 -0.1925 -0.0208 0.0447  601 ILE A CA  
4346 C C   . ILE A 602 ? 0.8954 0.7392 0.5618 -0.1737 -0.0198 0.0387  601 ILE A C   
4347 O O   . ILE A 602 ? 0.9797 0.8050 0.6360 -0.1622 -0.0155 0.0329  601 ILE A O   
4348 C CB  . ILE A 602 ? 0.9344 0.7581 0.5545 -0.1907 -0.0256 0.0425  601 ILE A CB  
4349 C CG1 . ILE A 602 ? 0.8343 0.6584 0.4378 -0.2103 -0.0271 0.0495  601 ILE A CG1 
4350 C CG2 . ILE A 602 ? 0.8707 0.7129 0.5216 -0.1769 -0.0326 0.0392  601 ILE A CG2 
4351 C CD1 . ILE A 602 ? 0.8775 0.6838 0.4570 -0.2110 -0.0275 0.0477  601 ILE A CD1 
4352 N N   . ALA A 603 ? 0.8425 0.7148 0.5477 -0.1707 -0.0243 0.0403  602 ALA A N   
4353 C CA  . ALA A 603 ? 0.8300 0.7139 0.5690 -0.1542 -0.0260 0.0348  602 ALA A CA  
4354 C C   . ALA A 603 ? 0.6954 0.5971 0.4597 -0.1480 -0.0376 0.0335  602 ALA A C   
4355 O O   . ALA A 603 ? 0.7788 0.6975 0.5547 -0.1563 -0.0406 0.0387  602 ALA A O   
4356 C CB  . ALA A 603 ? 0.7179 0.6153 0.4805 -0.1560 -0.0180 0.0373  602 ALA A CB  
4357 N N   . THR A 604 ? 0.5862 0.4813 0.3563 -0.1329 -0.0446 0.0267  603 THR A N   
4358 C CA  . THR A 604 ? 0.7379 0.6472 0.5339 -0.1248 -0.0561 0.0241  603 THR A CA  
4359 C C   . THR A 604 ? 0.7696 0.7045 0.6095 -0.1231 -0.0572 0.0251  603 THR A C   
4360 O O   . THR A 604 ? 0.6192 0.5597 0.4694 -0.1266 -0.0478 0.0272  603 THR A O   
4361 C CB  . THR A 604 ? 0.7025 0.5952 0.4928 -0.1090 -0.0655 0.0165  603 THR A CB  
4362 O OG1 . THR A 604 ? 0.6472 0.5403 0.4558 -0.0991 -0.0638 0.0128  603 THR A OG1 
4363 C CG2 . THR A 604 ? 0.6612 0.5250 0.4055 -0.1108 -0.0638 0.0158  603 THR A CG2 
4364 N N   . PRO A 605 ? 0.8553 0.8028 0.7185 -0.1181 -0.0678 0.0234  604 PRO A N   
4365 C CA  . PRO A 605 ? 0.7097 0.6792 0.6148 -0.1169 -0.0698 0.0241  604 PRO A CA  
4366 C C   . PRO A 605 ? 0.6071 0.5802 0.5379 -0.1078 -0.0684 0.0197  604 PRO A C   
4367 O O   . PRO A 605 ? 0.6279 0.6147 0.5817 -0.1124 -0.0593 0.0228  604 PRO A O   
4368 C CB  . PRO A 605 ? 0.5787 0.5525 0.4953 -0.1115 -0.0832 0.0214  604 PRO A CB  
4369 C CG  . PRO A 605 ? 0.5481 0.5091 0.4293 -0.1160 -0.0820 0.0234  604 PRO A CG  
4370 C CD  . PRO A 605 ? 0.7119 0.6526 0.5611 -0.1158 -0.0762 0.0220  604 PRO A CD  
4371 N N   . ALA A 606 ? 0.5935 0.5539 0.5206 -0.0949 -0.0766 0.0131  605 ALA A N   
4372 C CA  . ALA A 606 ? 0.5536 0.5171 0.5050 -0.0852 -0.0742 0.0093  605 ALA A CA  
4373 C C   . ALA A 606 ? 0.7136 0.6724 0.6531 -0.0906 -0.0543 0.0126  605 ALA A C   
4374 O O   . ALA A 606 ? 0.7243 0.6961 0.6938 -0.0892 -0.0446 0.0130  605 ALA A O   
4375 C CB  . ALA A 606 ? 0.4758 0.4209 0.4160 -0.0704 -0.0873 0.0025  605 ALA A CB  
4376 N N   . GLU A 607 ? 0.6588 0.5971 0.5531 -0.0974 -0.0473 0.0148  606 GLU A N   
4377 C CA  . GLU A 607 ? 0.7644 0.6921 0.6413 -0.1021 -0.0296 0.0170  606 GLU A CA  
4378 C C   . GLU A 607 ? 0.7213 0.6629 0.6083 -0.1157 -0.0178 0.0237  606 GLU A C   
4379 O O   . GLU A 607 ? 0.7059 0.6456 0.5967 -0.1168 -0.0022 0.0248  606 GLU A O   
4380 C CB  . GLU A 607 ? 0.7902 0.6888 0.6143 -0.1067 -0.0268 0.0174  606 GLU A CB  
4381 C CG  . GLU A 607 ? 0.8989 0.7779 0.7100 -0.0917 -0.0353 0.0108  606 GLU A CG  
4382 C CD  . GLU A 607 ? 1.0865 0.9347 0.8436 -0.0975 -0.0341 0.0114  606 GLU A CD  
4383 O OE1 . GLU A 607 ? 0.8830 0.7311 0.6194 -0.1126 -0.0335 0.0165  606 GLU A OE1 
4384 O OE2 . GLU A 607 ? 1.1422 0.9667 0.8799 -0.0866 -0.0341 0.0070  606 GLU A OE2 
4385 N N   . PHE A 608 ? 0.6453 0.5986 0.5346 -0.1255 -0.0248 0.0283  607 PHE A N   
4386 C CA  . PHE A 608 ? 0.7389 0.7041 0.6369 -0.1380 -0.0171 0.0354  607 PHE A CA  
4387 C C   . PHE A 608 ? 0.7936 0.7785 0.7377 -0.1335 -0.0131 0.0347  607 PHE A C   
4388 O O   . PHE A 608 ? 0.8188 0.8051 0.7662 -0.1405 0.0010  0.0389  607 PHE A O   
4389 C CB  . PHE A 608 ? 0.6551 0.6287 0.5483 -0.1469 -0.0273 0.0403  607 PHE A CB  
4390 C CG  . PHE A 608 ? 0.6956 0.6786 0.5944 -0.1593 -0.0223 0.0481  607 PHE A CG  
4391 C CD1 . PHE A 608 ? 0.6962 0.6659 0.5622 -0.1720 -0.0146 0.0541  607 PHE A CD1 
4392 C CD2 . PHE A 608 ? 0.8392 0.8415 0.7737 -0.1586 -0.0267 0.0498  607 PHE A CD2 
4393 C CE1 . PHE A 608 ? 0.7614 0.7366 0.6294 -0.1833 -0.0121 0.0619  607 PHE A CE1 
4394 C CE2 . PHE A 608 ? 0.7422 0.7501 0.6793 -0.1697 -0.0228 0.0576  607 PHE A CE2 
4395 C CZ  . PHE A 608 ? 0.6520 0.6463 0.5556 -0.1816 -0.0158 0.0638  607 PHE A CZ  
4396 N N   . VAL A 609 ? 0.6662 0.6642 0.6441 -0.1225 -0.0256 0.0295  608 VAL A N   
4397 C CA  . VAL A 609 ? 0.6740 0.6914 0.7005 -0.1180 -0.0231 0.0281  608 VAL A CA  
4398 C C   . VAL A 609 ? 0.7347 0.7488 0.7706 -0.1123 -0.0055 0.0262  608 VAL A C   
4399 O O   . VAL A 609 ? 0.9478 0.9735 1.0101 -0.1160 0.0081  0.0289  608 VAL A O   
4400 C CB  . VAL A 609 ? 0.5393 0.5679 0.5983 -0.1069 -0.0436 0.0220  608 VAL A CB  
4401 C CG1 . VAL A 609 ? 0.4173 0.4642 0.5274 -0.1006 -0.0415 0.0194  608 VAL A CG1 
4402 C CG2 . VAL A 609 ? 0.5543 0.5900 0.6162 -0.1129 -0.0563 0.0244  608 VAL A CG2 
4403 N N   . GLU A 610 ? 0.7450 0.7417 0.7585 -0.1030 -0.0046 0.0217  609 GLU A N   
4404 C CA  . GLU A 610 ? 0.6863 0.6761 0.7044 -0.0952 0.0126  0.0192  609 GLU A CA  
4405 C C   . GLU A 610 ? 0.6831 0.6580 0.6695 -0.1070 0.0355  0.0247  609 GLU A C   
4406 O O   . GLU A 610 ? 0.6824 0.6585 0.6839 -0.1047 0.0551  0.0249  609 GLU A O   
4407 C CB  . GLU A 610 ? 0.6600 0.6290 0.6531 -0.0825 0.0060  0.0134  609 GLU A CB  
4408 C CG  . GLU A 610 ? 0.9948 0.9590 1.0025 -0.0691 0.0200  0.0095  609 GLU A CG  
4409 C CD  . GLU A 610 ? 1.4453 1.4404 1.5209 -0.0609 0.0206  0.0078  609 GLU A CD  
4410 O OE1 . GLU A 610 ? 1.3528 1.3680 1.4614 -0.0607 0.0015  0.0070  609 GLU A OE1 
4411 O OE2 . GLU A 610 ? 1.6753 1.6737 1.7713 -0.0550 0.0409  0.0073  609 GLU A OE2 
4412 N N   . LEU A 611 ? 0.6493 0.6089 0.5910 -0.1199 0.0328  0.0292  610 LEU A N   
4413 C CA  . LEU A 611 ? 0.6935 0.6333 0.5963 -0.1323 0.0498  0.0344  610 LEU A CA  
4414 C C   . LEU A 611 ? 0.7696 0.7233 0.6944 -0.1415 0.0598  0.0402  610 LEU A C   
4415 O O   . LEU A 611 ? 0.9058 0.8469 0.8177 -0.1457 0.0804  0.0426  610 LEU A O   
4416 C CB  . LEU A 611 ? 0.7708 0.6948 0.6269 -0.1448 0.0396  0.0383  610 LEU A CB  
4417 C CG  . LEU A 611 ? 0.7658 0.6596 0.5723 -0.1455 0.0404  0.0361  610 LEU A CG  
4418 C CD1 . LEU A 611 ? 0.6333 0.5144 0.4423 -0.1293 0.0497  0.0289  610 LEU A CD1 
4419 C CD2 . LEU A 611 ? 0.6177 0.5131 0.4118 -0.1483 0.0210  0.0362  610 LEU A CD2 
4420 N N   . VAL A 612 ? 0.8250 0.8009 0.7785 -0.1449 0.0455  0.0426  611 VAL A N   
4421 C CA  . VAL A 612 ? 0.7337 0.7207 0.7050 -0.1549 0.0524  0.0489  611 VAL A CA  
4422 C C   . VAL A 612 ? 0.7048 0.7055 0.7201 -0.1478 0.0678  0.0466  611 VAL A C   
4423 O O   . VAL A 612 ? 0.7408 0.7384 0.7573 -0.1555 0.0859  0.0514  611 VAL A O   
4424 C CB  . VAL A 612 ? 0.6462 0.6516 0.6379 -0.1586 0.0328  0.0514  611 VAL A CB  
4425 C CG1 . VAL A 612 ? 0.6929 0.7104 0.7113 -0.1661 0.0397  0.0569  611 VAL A CG1 
4426 C CG2 . VAL A 612 ? 0.6544 0.6482 0.6055 -0.1678 0.0221  0.0559  611 VAL A CG2 
4427 N N   . SER A 613 ? 0.6733 0.6880 0.7245 -0.1332 0.0606  0.0394  612 SER A N   
4428 C CA  . SER A 613 ? 0.7345 0.7662 0.8354 -0.1253 0.0738  0.0369  612 SER A CA  
4429 C C   . SER A 613 ? 0.8719 0.8856 0.9542 -0.1224 0.1019  0.0365  612 SER A C   
4430 O O   . SER A 613 ? 1.0672 1.0924 1.1857 -0.1196 0.1213  0.0367  612 SER A O   
4431 C CB  . SER A 613 ? 0.7023 0.7524 0.8455 -0.1100 0.0550  0.0294  612 SER A CB  
4432 O OG  . SER A 613 ? 0.9048 0.9389 1.0270 -0.0975 0.0552  0.0240  612 SER A OG  
4433 N N   . LEU A 614 ? 0.8761 0.8601 0.9016 -0.1235 0.1051  0.0360  613 LEU A N   
4434 C CA  . LEU A 614 ? 0.8809 0.8398 0.8779 -0.1201 0.1309  0.0348  613 LEU A CA  
4435 C C   . LEU A 614 ? 0.9005 0.8350 0.8527 -0.1361 0.1504  0.0419  613 LEU A C   
4436 O O   . LEU A 614 ? 1.0158 0.9266 0.9426 -0.1344 0.1750  0.0412  613 LEU A O   
4437 C CB  . LEU A 614 ? 0.7914 0.7259 0.7480 -0.1119 0.1239  0.0297  613 LEU A CB  
4438 C CG  . LEU A 614 ? 0.8508 0.7989 0.8434 -0.0925 0.1115  0.0222  613 LEU A CG  
4439 C CD1 . LEU A 614 ? 0.7865 0.7055 0.7308 -0.0869 0.1031  0.0183  613 LEU A CD1 
4440 C CD2 . LEU A 614 ? 0.9850 0.9455 1.0230 -0.0793 0.1321  0.0192  613 LEU A CD2 
4441 N N   . LEU A 615 ? 0.7986 0.7365 0.7398 -0.1509 0.1392  0.0485  614 LEU A N   
4442 C CA  . LEU A 615 ? 0.8520 0.7638 0.7452 -0.1670 0.1515  0.0559  614 LEU A CA  
4443 C C   . LEU A 615 ? 0.9911 0.8935 0.8885 -0.1688 0.1834  0.0583  614 LEU A C   
4444 O O   . LEU A 615 ? 1.1759 1.0449 1.0206 -0.1793 0.1982  0.0628  614 LEU A O   
4445 C CB  . LEU A 615 ? 0.7604 0.6821 0.6513 -0.1803 0.1318  0.0630  614 LEU A CB  
4446 C CG  . LEU A 615 ? 0.8237 0.7453 0.6942 -0.1814 0.1055  0.0620  614 LEU A CG  
4447 C CD1 . LEU A 615 ? 0.9237 0.8642 0.8101 -0.1892 0.0851  0.0674  614 LEU A CD1 
4448 C CD2 . LEU A 615 ? 0.7697 0.6554 0.5747 -0.1897 0.1080  0.0636  614 LEU A CD2 
4449 N N   . ASP A 616 ? 0.9688 0.8988 0.9277 -0.1589 0.1941  0.0554  615 ASP A N   
4450 C CA  . ASP A 616 ? 0.9459 0.8711 0.9170 -0.1607 0.2269  0.0579  615 ASP A CA  
4451 C C   . ASP A 616 ? 0.9383 0.8641 0.9318 -0.1438 0.2494  0.0510  615 ASP A C   
4452 O O   . ASP A 616 ? 1.0257 0.9526 1.0405 -0.1421 0.2791  0.0520  615 ASP A O   
4453 C CB  . ASP A 616 ? 0.9410 0.8973 0.9675 -0.1668 0.2262  0.0624  615 ASP A CB  
4454 C CG  . ASP A 616 ? 1.0098 1.0088 1.1120 -0.1544 0.2101  0.0567  615 ASP A CG  
4455 O OD1 . ASP A 616 ? 1.0087 1.0143 1.1175 -0.1417 0.1926  0.0500  615 ASP A OD1 
4456 O OD2 . ASP A 616 ? 1.0417 1.0658 1.1957 -0.1581 0.2143  0.0593  615 ASP A OD2 
4457 N N   . LYS A 617 ? 1.0168 0.9405 1.0052 -0.1308 0.2358  0.0441  616 LYS A N   
4458 C CA  . LYS A 617 ? 1.1378 1.0628 1.1500 -0.1121 0.2528  0.0372  616 LYS A CA  
4459 C C   . LYS A 617 ? 1.4603 1.3404 1.4029 -0.1085 0.2621  0.0340  616 LYS A C   
4460 O O   . LYS A 617 ? 1.5725 1.4402 1.5168 -0.0947 0.2850  0.0294  616 LYS A O   
4461 C CB  . LYS A 617 ? 1.0484 1.0103 1.1224 -0.0972 0.2278  0.0315  616 LYS A CB  
4462 C CG  . LYS A 617 ? 1.1654 1.1684 1.3062 -0.1017 0.2176  0.0342  616 LYS A CG  
4463 C CD  . LYS A 617 ? 1.2963 1.3303 1.4881 -0.0900 0.1864  0.0289  616 LYS A CD  
4464 C CE  . LYS A 617 ? 1.3437 1.4100 1.5853 -0.0993 0.1722  0.0324  616 LYS A CE  
4465 N NZ  . LYS A 617 ? 1.3543 1.4503 1.6511 -0.0879 0.1440  0.0271  616 LYS A NZ  
4466 N N   . ALA A 618 ? 1.4837 1.3377 1.3668 -0.1197 0.2471  0.0361  617 ALA A N   
4467 N N   . ASP B 2   ? 2.5383 2.4337 2.2548 -0.3587 -0.4899 0.0643  2   ASP B N   
4468 C CA  . ASP B 2   ? 2.5712 2.4639 2.2735 -0.3589 -0.5141 0.0839  2   ASP B CA  
4469 C C   . ASP B 2   ? 2.4739 2.3365 2.1340 -0.3591 -0.4992 0.1078  2   ASP B C   
4470 O O   . ASP B 2   ? 2.4704 2.3196 2.0885 -0.3715 -0.4879 0.1109  2   ASP B O   
4471 C CB  . ASP B 2   ? 2.6316 2.5405 2.3773 -0.3448 -0.5477 0.0921  2   ASP B CB  
4472 C CG  . ASP B 2   ? 2.6436 2.5813 2.4182 -0.3483 -0.5748 0.0778  2   ASP B CG  
4473 O OD1 . ASP B 2   ? 2.6402 2.5863 2.4020 -0.3622 -0.5674 0.0606  2   ASP B OD1 
4474 O OD2 . ASP B 2   ? 2.6052 2.5569 2.4161 -0.3373 -0.6036 0.0839  2   ASP B OD2 
4475 N N   . ARG B 3   ? 2.3317 2.1835 2.0037 -0.3456 -0.4989 0.1241  3   ARG B N   
4476 C CA  . ARG B 3   ? 2.2648 2.0897 1.9033 -0.3441 -0.4874 0.1485  3   ARG B CA  
4477 C C   . ARG B 3   ? 2.1729 1.9773 1.7759 -0.3526 -0.4497 0.1447  3   ARG B C   
4478 O O   . ARG B 3   ? 2.2266 2.0079 1.7989 -0.3533 -0.4358 0.1630  3   ARG B O   
4479 C CB  . ARG B 3   ? 2.3085 2.1282 1.9720 -0.3276 -0.4968 0.1662  3   ARG B CB  
4480 C CG  . ARG B 3   ? 2.3631 2.2036 2.0689 -0.3174 -0.5321 0.1674  3   ARG B CG  
4481 C CD  . ARG B 3   ? 2.3721 2.2309 2.1209 -0.3107 -0.5328 0.1468  3   ARG B CD  
4482 N NE  . ARG B 3   ? 2.3055 2.1862 2.0969 -0.3021 -0.5655 0.1442  3   ARG B NE  
4483 C CZ  . ARG B 3   ? 2.1473 2.0435 1.9812 -0.2937 -0.5711 0.1298  3   ARG B CZ  
4484 N NH1 . ARG B 3   ? 2.0493 1.9411 1.8870 -0.2932 -0.5468 0.1170  3   ARG B NH1 
4485 N NH2 . ARG B 3   ? 2.0951 2.0104 1.9677 -0.2859 -0.6008 0.1284  3   ARG B NH2 
4486 N N   . LEU B 4   ? 2.0683 1.8806 1.6763 -0.3589 -0.4328 0.1211  4   LEU B N   
4487 C CA  . LEU B 4   ? 1.9339 1.7274 1.5085 -0.3680 -0.3970 0.1153  4   LEU B CA  
4488 C C   . LEU B 4   ? 1.9799 1.7676 1.5150 -0.3846 -0.3902 0.1107  4   LEU B C   
4489 O O   . LEU B 4   ? 1.9915 1.7558 1.4883 -0.3910 -0.3664 0.1192  4   LEU B O   
4490 C CB  . LEU B 4   ? 1.7540 1.5561 1.3483 -0.3685 -0.3803 0.0923  4   LEU B CB  
4491 C CG  . LEU B 4   ? 1.5404 1.3240 1.1056 -0.3770 -0.3427 0.0839  4   LEU B CG  
4492 C CD1 . LEU B 4   ? 1.6291 1.4176 1.1721 -0.3941 -0.3330 0.0643  4   LEU B CD1 
4493 C CD2 . LEU B 4   ? 1.2294 0.9840 0.7638 -0.3745 -0.3231 0.1065  4   LEU B CD2 
4494 N N   . SER B 5   ? 1.9804 1.7895 1.5256 -0.3918 -0.4110 0.0970  5   SER B N   
4495 C CA  . SER B 5   ? 2.0007 1.8058 1.5089 -0.4081 -0.4100 0.0932  5   SER B CA  
4496 C C   . SER B 5   ? 2.0518 1.8357 1.5259 -0.4086 -0.4136 0.1188  5   SER B C   
4497 O O   . SER B 5   ? 2.0428 1.8051 1.4733 -0.4194 -0.3913 0.1225  5   SER B O   
4498 C CB  . SER B 5   ? 2.0092 1.8427 1.5397 -0.4135 -0.4394 0.0787  5   SER B CB  
4499 O OG  . SER B 5   ? 2.0154 1.8659 1.5658 -0.4190 -0.4299 0.0518  5   SER B OG  
4500 N N   . ARG B 6   ? 2.1067 1.8960 1.6012 -0.3970 -0.4407 0.1362  6   ARG B N   
4501 C CA  . ARG B 6   ? 2.1982 1.9692 1.6642 -0.3969 -0.4481 0.1613  6   ARG B CA  
4502 C C   . ARG B 6   ? 2.0569 1.7983 1.4938 -0.3956 -0.4165 0.1761  6   ARG B C   
4503 O O   . ARG B 6   ? 2.0342 1.7558 1.4346 -0.4011 -0.4115 0.1921  6   ARG B O   
4504 C CB  . ARG B 6   ? 2.4231 2.2053 1.9225 -0.3826 -0.4814 0.1770  6   ARG B CB  
4505 C CG  . ARG B 6   ? 2.6032 2.4149 2.1358 -0.3821 -0.5152 0.1648  6   ARG B CG  
4506 C CD  . ARG B 6   ? 2.7043 2.5265 2.2773 -0.3654 -0.5441 0.1785  6   ARG B CD  
4507 N NE  . ARG B 6   ? 2.7274 2.5788 2.3386 -0.3632 -0.5752 0.1662  6   ARG B NE  
4508 C CZ  . ARG B 6   ? 2.6931 2.5584 2.3474 -0.3489 -0.6007 0.1720  6   ARG B CZ  
4509 N NH1 . ARG B 6   ? 2.6839 2.5366 2.3478 -0.3359 -0.5993 0.1898  6   ARG B NH1 
4510 N NH2 . ARG B 6   ? 2.6460 2.5378 2.3353 -0.3476 -0.6275 0.1598  6   ARG B NH2 
4511 N N   . LEU B 7   ? 2.0144 1.7525 1.4677 -0.3883 -0.3953 0.1708  7   LEU B N   
4512 C CA  . LEU B 7   ? 1.9524 1.6639 1.3834 -0.3862 -0.3646 0.1839  7   LEU B CA  
4513 C C   . LEU B 7   ? 1.9399 1.6355 1.3302 -0.4016 -0.3333 0.1728  7   LEU B C   
4514 O O   . LEU B 7   ? 1.9074 1.5791 1.2624 -0.4064 -0.3149 0.1863  7   LEU B O   
4515 C CB  . LEU B 7   ? 1.7818 1.4952 1.2458 -0.3727 -0.3555 0.1834  7   LEU B CB  
4516 C CG  . LEU B 7   ? 1.6677 1.3574 1.1227 -0.3651 -0.3338 0.2030  7   LEU B CG  
4517 C CD1 . LEU B 7   ? 1.5360 1.2102 0.9714 -0.3710 -0.2972 0.1939  7   LEU B CD1 
4518 C CD2 . LEU B 7   ? 1.7777 1.4500 1.2062 -0.3662 -0.3366 0.2269  7   LEU B CD2 
4519 N N   . ARG B 8   ? 1.9595 1.6679 1.3553 -0.4094 -0.3266 0.1480  8   ARG B N   
4520 C CA  . ARG B 8   ? 2.0387 1.7329 1.3983 -0.4243 -0.2967 0.1351  8   ARG B CA  
4521 C C   . ARG B 8   ? 2.1147 1.8022 1.4348 -0.4396 -0.3022 0.1362  8   ARG B C   
4522 O O   . ARG B 8   ? 2.1621 1.8293 1.4427 -0.4516 -0.2759 0.1334  8   ARG B O   
4523 C CB  . ARG B 8   ? 2.0208 1.7311 1.3989 -0.4288 -0.2887 0.1079  8   ARG B CB  
4524 C CG  . ARG B 8   ? 1.9550 1.6565 1.3463 -0.4208 -0.2634 0.1052  8   ARG B CG  
4525 C CD  . ARG B 8   ? 1.8779 1.6001 1.2987 -0.4215 -0.2641 0.0804  8   ARG B CD  
4526 N NE  . ARG B 8   ? 1.8609 1.5724 1.2897 -0.4152 -0.2394 0.0781  8   ARG B NE  
4527 C CZ  . ARG B 8   ? 1.8788 1.6036 1.3330 -0.4138 -0.2360 0.0593  8   ARG B CZ  
4528 N NH1 . ARG B 8   ? 1.8817 1.6324 1.3589 -0.4178 -0.2551 0.0407  8   ARG B NH1 
4529 N NH2 . ARG B 8   ? 1.8568 1.5688 1.3138 -0.4085 -0.2135 0.0592  8   ARG B NH2 
4530 N N   . GLN B 9   ? 2.1087 1.8123 1.4390 -0.4392 -0.3364 0.1403  9   GLN B N   
4531 C CA  . GLN B 9   ? 2.1590 1.8545 1.4507 -0.4526 -0.3457 0.1456  9   GLN B CA  
4532 C C   . GLN B 9   ? 2.3509 2.0187 1.6128 -0.4500 -0.3347 0.1713  9   GLN B C   
4533 O O   . GLN B 9   ? 2.4589 2.1052 1.6751 -0.4629 -0.3168 0.1739  9   GLN B O   
4534 C CB  . GLN B 9   ? 2.1071 1.8273 1.4206 -0.4515 -0.3875 0.1452  9   GLN B CB  
4535 C CG  . GLN B 9   ? 2.1818 1.8916 1.4557 -0.4630 -0.4020 0.1565  9   GLN B CG  
4536 C CD  . GLN B 9   ? 2.2221 1.9531 1.5212 -0.4577 -0.4453 0.1633  9   GLN B CD  
4537 O OE1 . GLN B 9   ? 2.2436 1.9991 1.5914 -0.4463 -0.4644 0.1567  9   GLN B OE1 
4538 N NE2 . GLN B 9   ? 2.1935 1.9141 1.4589 -0.4661 -0.4607 0.1767  9   GLN B NE2 
4539 N N   . MET B 10  ? 2.4219 2.0898 1.7105 -0.4335 -0.3446 0.1896  10  MET B N   
4540 C CA  . MET B 10  ? 2.4528 2.0972 1.7205 -0.4293 -0.3374 0.2155  10  MET B CA  
4541 C C   . MET B 10  ? 2.3891 2.0091 1.6408 -0.4281 -0.2977 0.2206  10  MET B C   
4542 O O   . MET B 10  ? 2.3492 1.9495 1.5882 -0.4234 -0.2877 0.2417  10  MET B O   
4543 C CB  . MET B 10  ? 2.5130 2.1677 1.8175 -0.4125 -0.3647 0.2331  10  MET B CB  
4544 C CG  . MET B 10  ? 2.5637 2.2391 1.8822 -0.4129 -0.4050 0.2328  10  MET B CG  
4545 S SD  . MET B 10  ? 2.3460 2.0380 1.7178 -0.3920 -0.4368 0.2473  10  MET B SD  
4546 C CE  . MET B 10  ? 2.2738 1.9858 1.6506 -0.3969 -0.4800 0.2457  10  MET B CE  
4547 N N   . ALA B 11  ? 2.3934 2.0145 1.6467 -0.4322 -0.2750 0.2014  11  ALA B N   
4548 C CA  . ALA B 11  ? 2.4238 2.0222 1.6633 -0.4312 -0.2373 0.2049  11  ALA B CA  
4549 C C   . ALA B 11  ? 2.5711 2.1542 1.7683 -0.4490 -0.2104 0.1904  11  ALA B C   
4550 O O   . ALA B 11  ? 2.5891 2.1485 1.7649 -0.4511 -0.1775 0.1950  11  ALA B O   
4551 C CB  . ALA B 11  ? 2.3236 1.9321 1.6013 -0.4194 -0.2305 0.1975  11  ALA B CB  
4552 N N   . ALA B 12  ? 2.6605 2.2574 1.8474 -0.4617 -0.2248 0.1727  12  ALA B N   
4553 C CA  . ALA B 12  ? 2.7395 2.3233 1.8853 -0.4803 -0.2028 0.1573  12  ALA B CA  
4554 C C   . ALA B 12  ? 2.8692 2.4351 1.9695 -0.4922 -0.2050 0.1685  12  ALA B C   
4555 O O   . ALA B 12  ? 2.9239 2.4745 1.9838 -0.5088 -0.1861 0.1583  12  ALA B O   
4556 C CB  . ALA B 12  ? 2.7049 2.3128 1.8633 -0.4891 -0.2156 0.1310  12  ALA B CB  
4557 N N   . GLU B 13  ? 2.9244 2.4911 2.0305 -0.4843 -0.2278 0.1894  13  GLU B N   
4558 C CA  . GLU B 13  ? 2.9298 2.4774 1.9929 -0.4943 -0.2306 0.2033  13  GLU B CA  
4559 C C   . GLU B 13  ? 2.9186 2.4362 1.9624 -0.4901 -0.2004 0.2227  13  GLU B C   
4560 O O   . GLU B 13  ? 2.8658 2.3690 1.8885 -0.4909 -0.2057 0.2417  13  GLU B O   
4561 C CB  . GLU B 13  ? 2.8891 2.4525 1.9676 -0.4886 -0.2721 0.2163  13  GLU B CB  
4562 C CG  . GLU B 13  ? 2.8497 2.4434 1.9487 -0.4926 -0.3049 0.1991  13  GLU B CG  
4563 C CD  . GLU B 13  ? 2.8088 2.4176 1.9282 -0.4845 -0.3457 0.2137  13  GLU B CD  
4564 O OE1 . GLU B 13  ? 2.7669 2.3622 1.8835 -0.4759 -0.3478 0.2370  13  GLU B OE1 
4565 O OE2 . GLU B 13  ? 2.7961 2.4303 1.9356 -0.4865 -0.3753 0.2020  13  GLU B OE2 
4566 N N   . ASN B 14  ? 2.9473 2.4555 1.9996 -0.4855 -0.1689 0.2180  14  ASN B N   
4567 C CA  . ASN B 14  ? 2.9385 2.4196 1.9782 -0.4806 -0.1378 0.2349  14  ASN B CA  
4568 C C   . ASN B 14  ? 2.8754 2.3353 1.8835 -0.4927 -0.0983 0.2215  14  ASN B C   
4569 O O   . ASN B 14  ? 2.8523 2.2846 1.8300 -0.4972 -0.0709 0.2318  14  ASN B O   
4570 C CB  . ASN B 14  ? 2.9416 2.4307 2.0283 -0.4604 -0.1379 0.2461  14  ASN B CB  
4571 C CG  . ASN B 14  ? 2.8835 2.3952 2.0059 -0.4480 -0.1770 0.2566  14  ASN B CG  
4572 O OD1 . ASN B 14  ? 2.8028 2.3330 1.9676 -0.4352 -0.1884 0.2536  14  ASN B OD1 
4573 N ND2 . ASN B 14  ? 2.9046 2.4138 2.0090 -0.4521 -0.1975 0.2688  14  ASN B ND2 
4574 N N   . GLN B 15  ? 2.8257 2.2987 1.8421 -0.4979 -0.0953 0.1982  15  GLN B N   
4575 C CA  . GLN B 15  ? 2.7728 2.2278 1.7618 -0.5098 -0.0595 0.1826  15  GLN B CA  
4576 C C   . GLN B 15  ? 2.6480 2.0986 1.5937 -0.5314 -0.0617 0.1669  15  GLN B C   
4577 O O   . GLN B 15  ? 2.4929 1.9631 1.4452 -0.5389 -0.0760 0.1465  15  GLN B O   
4578 C CB  . GLN B 15  ? 2.7738 2.2437 1.7955 -0.5039 -0.0528 0.1658  15  GLN B CB  
4579 C CG  . GLN B 15  ? 2.7395 2.2163 1.8053 -0.4832 -0.0543 0.1793  15  GLN B CG  
4580 C CD  . GLN B 15  ? 2.7091 2.2031 1.8064 -0.4785 -0.0534 0.1617  15  GLN B CD  
4581 O OE1 . GLN B 15  ? 2.7149 2.2154 1.8021 -0.4905 -0.0495 0.1392  15  GLN B OE1 
4582 N NE2 . GLN B 15  ? 2.6218 2.1226 1.7568 -0.4614 -0.0571 0.1717  15  GLN B NE2 
4583 N N   . PRO B 39  ? 2.3903 1.7936 1.7334 -0.3691 0.1288  0.1345  39  PRO B N   
4584 C CA  . PRO B 39  ? 2.3991 1.8111 1.7664 -0.3571 0.1037  0.1488  39  PRO B CA  
4585 C C   . PRO B 39  ? 2.5174 1.9175 1.8848 -0.3551 0.1075  0.1481  39  PRO B C   
4586 O O   . PRO B 39  ? 2.5035 1.8952 1.8547 -0.3643 0.1250  0.1307  39  PRO B O   
4587 C CB  . PRO B 39  ? 2.2739 1.7144 1.6561 -0.3592 0.0784  0.1333  39  PRO B CB  
4588 C CG  . PRO B 39  ? 2.2891 1.7359 1.6578 -0.3686 0.0860  0.1224  39  PRO B CG  
4589 C CD  . PRO B 39  ? 2.3508 1.7756 1.6931 -0.3776 0.1189  0.1156  39  PRO B CD  
4590 N N   . GLU B 40  ? 2.6304 2.0290 2.0147 -0.3439 0.0912  0.1668  40  GLU B N   
4591 C CA  . GLU B 40  ? 2.6787 2.0646 2.0618 -0.3417 0.0924  0.1687  40  GLU B CA  
4592 C C   . GLU B 40  ? 2.5969 2.0001 1.9917 -0.3430 0.0718  0.1524  40  GLU B C   
4593 O O   . GLU B 40  ? 2.6072 2.0325 2.0192 -0.3407 0.0503  0.1481  40  GLU B O   
4594 C CB  . GLU B 40  ? 2.7170 2.0897 2.1111 -0.3295 0.0868  0.1986  40  GLU B CB  
4595 C CG  . GLU B 40  ? 2.7540 2.1067 2.1384 -0.3275 0.1098  0.2157  40  GLU B CG  
4596 C CD  . GLU B 40  ? 2.7844 2.1145 2.1450 -0.3350 0.1385  0.2074  40  GLU B CD  
4597 O OE1 . GLU B 40  ? 2.7803 2.1070 2.1327 -0.3400 0.1392  0.1936  40  GLU B OE1 
4598 O OE2 . GLU B 40  ? 2.8030 2.1178 2.1527 -0.3361 0.1611  0.2146  40  GLU B OE2 
4599 N N   . PRO B 41  ? 2.4633 1.8553 1.8485 -0.3468 0.0787  0.1432  41  PRO B N   
4600 C CA  . PRO B 41  ? 2.3642 1.7696 1.7578 -0.3495 0.0637  0.1251  41  PRO B CA  
4601 C C   . PRO B 41  ? 2.2192 1.6395 1.6381 -0.3393 0.0332  0.1364  41  PRO B C   
4602 O O   . PRO B 41  ? 2.1517 1.5950 1.5867 -0.3393 0.0162  0.1255  41  PRO B O   
4603 C CB  . PRO B 41  ? 2.4125 1.7952 1.7888 -0.3527 0.0775  0.1238  41  PRO B CB  
4604 C CG  . PRO B 41  ? 2.4283 1.7897 1.7838 -0.3565 0.1053  0.1298  41  PRO B CG  
4605 C CD  . PRO B 41  ? 2.4412 1.8055 1.8061 -0.3490 0.1025  0.1498  41  PRO B CD  
4606 N N   . PHE B 42  ? 2.1142 1.5209 1.5369 -0.3309 0.0261  0.1580  42  PHE B N   
4607 C CA  . PHE B 42  ? 2.0080 1.4253 1.4534 -0.3215 -0.0021 0.1701  42  PHE B CA  
4608 C C   . PHE B 42  ? 1.8109 1.2314 1.2587 -0.3242 -0.0133 0.1548  42  PHE B C   
4609 O O   . PHE B 42  ? 1.4892 0.9285 0.9462 -0.3280 -0.0221 0.1341  42  PHE B O   
4610 C CB  . PHE B 42  ? 1.9655 1.4057 1.4310 -0.3172 -0.0196 0.1720  42  PHE B CB  
4611 C CG  . PHE B 42  ? 1.9331 1.3843 1.4226 -0.3080 -0.0483 0.1832  42  PHE B CG  
4612 C CD1 . PHE B 42  ? 1.8491 1.2895 1.3465 -0.2987 -0.0565 0.2100  42  PHE B CD1 
4613 C CD2 . PHE B 42  ? 1.9559 1.4279 1.4611 -0.3086 -0.0670 0.1669  42  PHE B CD2 
4614 C CE1 . PHE B 42  ? 1.7359 1.1856 1.2548 -0.2909 -0.0828 0.2200  42  PHE B CE1 
4615 C CE2 . PHE B 42  ? 1.9153 1.3960 1.4423 -0.3003 -0.0928 0.1769  42  PHE B CE2 
4616 C CZ  . PHE B 42  ? 1.8131 1.2824 1.3461 -0.2917 -0.1007 0.2033  42  PHE B CZ  
4617 N N   . MET B 43  ? 1.8924 1.2937 1.3314 -0.3223 -0.0126 0.1652  43  MET B N   
4618 C CA  . MET B 43  ? 1.8515 1.2514 1.2897 -0.3247 -0.0230 0.1537  43  MET B CA  
4619 C C   . MET B 43  ? 1.6704 1.0753 1.0972 -0.3364 -0.0099 0.1223  43  MET B C   
4620 O O   . MET B 43  ? 1.5426 0.9610 0.9800 -0.3384 -0.0223 0.1054  43  MET B O   
4621 C CB  . MET B 43  ? 1.9418 1.3592 1.4063 -0.3168 -0.0525 0.1591  43  MET B CB  
4622 C CG  . MET B 43  ? 1.9711 1.3859 1.4495 -0.3058 -0.0653 0.1896  43  MET B CG  
4623 S SD  . MET B 43  ? 2.0550 1.4719 1.5518 -0.2980 -0.0957 0.2015  43  MET B SD  
4624 C CE  . MET B 43  ? 0.9163 0.3626 0.4358 -0.2980 -0.1137 0.1811  43  MET B CE  
4625 N N   . ALA B 44  ? 1.6438 1.0372 1.0497 -0.3442 0.0159  0.1146  44  ALA B N   
4626 C CA  . ALA B 44  ? 1.7290 1.1269 1.1240 -0.3562 0.0312  0.0850  44  ALA B CA  
4627 C C   . ALA B 44  ? 1.7194 1.1100 1.1065 -0.3613 0.0296  0.0708  44  ALA B C   
4628 O O   . ALA B 44  ? 1.7449 1.1515 1.1409 -0.3667 0.0260  0.0470  44  ALA B O   
4629 C CB  . ALA B 44  ? 1.7733 1.1555 1.1449 -0.3636 0.0602  0.0822  44  ALA B CB  
4630 N N   . ASP B 45  ? 1.6324 0.9985 1.0032 -0.3599 0.0324  0.0850  45  ASP B N   
4631 C CA  . ASP B 45  ? 1.5581 0.9143 0.9173 -0.3657 0.0317  0.0721  45  ASP B CA  
4632 C C   . ASP B 45  ? 1.5908 0.9648 0.9729 -0.3610 0.0058  0.0669  45  ASP B C   
4633 O O   . ASP B 45  ? 1.5626 0.9416 0.9443 -0.3677 0.0062  0.0442  45  ASP B O   
4634 C CB  . ASP B 45  ? 1.6860 1.0115 1.0220 -0.3651 0.0370  0.0906  45  ASP B CB  
4635 C CG  . ASP B 45  ? 2.0100 1.3200 1.3239 -0.3750 0.0452  0.0733  45  ASP B CG  
4636 O OD1 . ASP B 45  ? 2.0050 1.3285 1.3228 -0.3825 0.0489  0.0462  45  ASP B OD1 
4637 O OD2 . ASP B 45  ? 2.2275 1.5114 1.5200 -0.3757 0.0484  0.0869  45  ASP B OD2 
4638 N N   . PHE B 46  ? 1.6419 1.0248 1.0446 -0.3497 -0.0158 0.0877  46  PHE B N   
4639 C CA  . PHE B 46  ? 1.5888 0.9878 1.0148 -0.3444 -0.0414 0.0850  46  PHE B CA  
4640 C C   . PHE B 46  ? 1.5019 0.9279 0.9475 -0.3477 -0.0452 0.0591  46  PHE B C   
4641 O O   . PHE B 46  ? 1.4344 0.8658 0.8854 -0.3513 -0.0508 0.0407  46  PHE B O   
4642 C CB  . PHE B 46  ? 1.6008 1.0046 1.0459 -0.3319 -0.0625 0.1128  46  PHE B CB  
4643 C CG  . PHE B 46  ? 1.5639 0.9873 1.0362 -0.3260 -0.0886 0.1098  46  PHE B CG  
4644 C CD1 . PHE B 46  ? 1.5809 0.9965 1.0535 -0.3250 -0.1031 0.1106  46  PHE B CD1 
4645 C CD2 . PHE B 46  ? 1.5140 0.9623 1.0105 -0.3218 -0.0985 0.1060  46  PHE B CD2 
4646 C CE1 . PHE B 46  ? 1.5218 0.9542 1.0197 -0.3196 -0.1263 0.1074  46  PHE B CE1 
4647 C CE2 . PHE B 46  ? 1.4945 0.9598 1.0166 -0.3161 -0.1223 0.1036  46  PHE B CE2 
4648 C CZ  . PHE B 46  ? 1.5124 0.9698 1.0359 -0.3148 -0.1358 0.1041  46  PHE B CZ  
4649 N N   . PHE B 47  ? 1.3999 0.8425 0.8565 -0.3467 -0.0420 0.0575  47  PHE B N   
4650 C CA  . PHE B 47  ? 1.4700 0.9391 0.9468 -0.3497 -0.0471 0.0343  47  PHE B CA  
4651 C C   . PHE B 47  ? 1.4817 0.9496 0.9471 -0.3619 -0.0289 0.0050  47  PHE B C   
4652 O O   . PHE B 47  ? 1.4427 0.9307 0.9268 -0.3647 -0.0346 -0.0169 47  PHE B O   
4653 C CB  . PHE B 47  ? 1.3406 0.8255 0.8271 -0.3477 -0.0465 0.0385  47  PHE B CB  
4654 C CG  . PHE B 47  ? 1.3722 0.8653 0.8775 -0.3359 -0.0684 0.0620  47  PHE B CG  
4655 C CD1 . PHE B 47  ? 1.3455 0.8615 0.8791 -0.3305 -0.0915 0.0575  47  PHE B CD1 
4656 C CD2 . PHE B 47  ? 1.3558 0.8332 0.8517 -0.3301 -0.0659 0.0889  47  PHE B CD2 
4657 C CE1 . PHE B 47  ? 1.2932 0.8158 0.8435 -0.3201 -0.1113 0.0792  47  PHE B CE1 
4658 C CE2 . PHE B 47  ? 1.3383 0.8232 0.8523 -0.3197 -0.0851 0.1104  47  PHE B CE2 
4659 C CZ  . PHE B 47  ? 1.3592 0.8663 0.8994 -0.3150 -0.1079 0.1055  47  PHE B CZ  
4660 N N   . ASN B 48  ? 1.3182 0.7619 0.7538 -0.3689 -0.0068 0.0054  48  ASN B N   
4661 C CA  . ASN B 48  ? 1.2221 0.6577 0.6413 -0.3809 0.0124  -0.0191 48  ASN B CA  
4662 C C   . ASN B 48  ? 1.3822 0.8152 0.8051 -0.3818 0.0021  -0.0294 48  ASN B C   
4663 O O   . ASN B 48  ? 1.3329 0.7784 0.7652 -0.3883 0.0057  -0.0555 48  ASN B O   
4664 C CB  . ASN B 48  ? 1.4811 0.8869 0.8663 -0.3862 0.0348  -0.0097 48  ASN B CB  
4665 C CG  . ASN B 48  ? 1.6694 1.0743 1.0407 -0.3975 0.0609  -0.0285 48  ASN B CG  
4666 O OD1 . ASN B 48  ? 1.6764 1.1000 1.0603 -0.3985 0.0629  -0.0351 48  ASN B OD1 
4667 N ND2 . ASN B 48  ? 1.7080 1.0901 1.0518 -0.4069 0.0812  -0.0368 48  ASN B ND2 
4668 N N   . ARG B 49  ? 1.4389 0.8551 0.8544 -0.3755 -0.0103 -0.0092 49  ARG B N   
4669 C CA  . ARG B 49  ? 1.4945 0.9045 0.9096 -0.3768 -0.0201 -0.0174 49  ARG B CA  
4670 C C   . ARG B 49  ? 1.5726 1.0105 1.0226 -0.3723 -0.0393 -0.0307 49  ARG B C   
4671 O O   . ARG B 49  ? 1.6251 1.0668 1.0797 -0.3778 -0.0379 -0.0529 49  ARG B O   
4672 C CB  . ARG B 49  ? 1.5855 0.9747 0.9893 -0.3703 -0.0339 0.0088  49  ARG B CB  
4673 C CG  . ARG B 49  ? 1.6355 1.0027 1.0167 -0.3688 -0.0238 0.0329  49  ARG B CG  
4674 C CD  . ARG B 49  ? 1.5965 0.9402 0.9625 -0.3660 -0.0352 0.0520  49  ARG B CD  
4675 N NE  . ARG B 49  ? 1.6429 0.9648 0.9792 -0.3772 -0.0209 0.0374  49  ARG B NE  
4676 C CZ  . ARG B 49  ? 1.8125 1.1090 1.1176 -0.3832 -0.0021 0.0438  49  ARG B CZ  
4677 N NH1 . ARG B 49  ? 1.7916 1.0822 1.0940 -0.3782 0.0041  0.0644  49  ARG B NH1 
4678 N NH2 . ARG B 49  ? 1.8255 1.1014 1.1022 -0.3941 0.0109  0.0299  49  ARG B NH2 
4679 N N   . VAL B 50  ? 1.4165 0.8732 0.8916 -0.3623 -0.0572 -0.0172 50  VAL B N   
4680 C CA  . VAL B 50  ? 1.4164 0.8978 0.9250 -0.3573 -0.0771 -0.0279 50  VAL B CA  
4681 C C   . VAL B 50  ? 1.2940 0.7982 0.8187 -0.3638 -0.0679 -0.0564 50  VAL B C   
4682 O O   . VAL B 50  ? 1.1497 0.6675 0.6948 -0.3646 -0.0753 -0.0754 50  VAL B O   
4683 C CB  . VAL B 50  ? 1.6289 1.1217 1.1605 -0.3441 -0.1031 -0.0041 50  VAL B CB  
4684 C CG1 . VAL B 50  ? 1.5541 1.0246 1.0722 -0.3389 -0.1128 0.0206  50  VAL B CG1 
4685 C CG2 . VAL B 50  ? 0.8957 0.3996 0.4325 -0.3408 -0.1009 0.0072  50  VAL B CG2 
4686 N N   . LYS B 51  ? 1.3190 0.8264 0.8347 -0.3691 -0.0511 -0.0600 51  LYS B N   
4687 C CA  . LYS B 51  ? 1.2468 0.7712 0.7716 -0.3782 -0.0377 -0.0886 51  LYS B CA  
4688 C C   . LYS B 51  ? 1.3444 0.8568 0.8568 -0.3879 -0.0230 -0.1107 51  LYS B C   
4689 O O   . LYS B 51  ? 1.3015 0.8309 0.8360 -0.3905 -0.0258 -0.1335 51  LYS B O   
4690 C CB  . LYS B 51  ? 1.1472 0.6695 0.6555 -0.3846 -0.0180 -0.0886 51  LYS B CB  
4691 C CG  . LYS B 51  ? 1.2168 0.7683 0.7493 -0.3854 -0.0228 -0.1001 51  LYS B CG  
4692 C CD  . LYS B 51  ? 1.3039 0.8768 0.8616 -0.3902 -0.0248 -0.1291 51  LYS B CD  
4693 C CE  . LYS B 51  ? 1.4163 1.0201 1.0030 -0.3884 -0.0371 -0.1362 51  LYS B CE  
4694 N NZ  . LYS B 51  ? 1.5525 1.1764 1.1600 -0.3966 -0.0309 -0.1675 51  LYS B NZ  
4695 N N   . ARG B 52  ? 1.2968 0.7795 0.7743 -0.3931 -0.0073 -0.1035 52  ARG B N   
4696 C CA  . ARG B 52  ? 1.2217 0.6882 0.6815 -0.4029 0.0074  -0.1218 52  ARG B CA  
4697 C C   . ARG B 52  ? 1.3091 0.7818 0.7879 -0.3991 -0.0098 -0.1301 52  ARG B C   
4698 O O   . ARG B 52  ? 1.2441 0.7245 0.7320 -0.4062 -0.0015 -0.1567 52  ARG B O   
4699 C CB  . ARG B 52  ? 1.4353 0.8663 0.8541 -0.4067 0.0207  -0.1063 52  ARG B CB  
4700 C CG  . ARG B 52  ? 1.5633 0.9774 0.9543 -0.4213 0.0498  -0.1263 52  ARG B CG  
4701 C CD  . ARG B 52  ? 1.5808 0.9598 0.9352 -0.4257 0.0568  -0.1175 52  ARG B CD  
4702 N NE  . ARG B 52  ? 1.6316 0.9933 0.9726 -0.4170 0.0452  -0.0847 52  ARG B NE  
4703 C CZ  . ARG B 52  ? 1.7677 1.1237 1.1000 -0.4139 0.0516  -0.0665 52  ARG B CZ  
4704 N NH1 . ARG B 52  ? 1.7409 1.0817 1.0643 -0.4057 0.0405  -0.0371 52  ARG B NH1 
4705 N NH2 . ARG B 52  ? 1.7749 1.1406 1.1086 -0.4193 0.0693  -0.0779 52  ARG B NH2 
4706 N N   . ILE B 53  ? 1.1811 0.6500 0.6661 -0.3884 -0.0326 -0.1078 53  ILE B N   
4707 C CA  . ILE B 53  ? 1.1879 0.6606 0.6902 -0.3841 -0.0505 -0.1131 53  ILE B CA  
4708 C C   . ILE B 53  ? 1.2441 0.7496 0.7879 -0.3811 -0.0604 -0.1326 53  ILE B C   
4709 O O   . ILE B 53  ? 1.2245 0.7346 0.7794 -0.3855 -0.0575 -0.1555 53  ILE B O   
4710 C CB  . ILE B 53  ? 1.3137 0.7770 0.8164 -0.3729 -0.0744 -0.0835 53  ILE B CB  
4711 C CG1 . ILE B 53  ? 1.3324 0.7632 0.7962 -0.3758 -0.0661 -0.0641 53  ILE B CG1 
4712 C CG2 . ILE B 53  ? 1.0304 0.4970 0.5510 -0.3691 -0.0927 -0.0900 53  ILE B CG2 
4713 C CD1 . ILE B 53  ? 1.1718 0.5977 0.6384 -0.3648 -0.0856 -0.0321 53  ILE B CD1 
4714 N N   . ARG B 54  ? 1.2650 1.0797 0.6796 -0.5007 -0.1225 -0.0827 54  ARG B N   
4715 C CA  . ARG B 54  ? 1.2245 1.0975 0.6488 -0.5027 -0.1265 -0.0738 54  ARG B CA  
4716 C C   . ARG B 54  ? 1.3130 1.1944 0.7412 -0.5207 -0.1256 -0.0828 54  ARG B C   
4717 O O   . ARG B 54  ? 1.3600 1.2587 0.7996 -0.5189 -0.1263 -0.0670 54  ARG B O   
4718 C CB  . ARG B 54  ? 1.0669 0.9874 0.4861 -0.5025 -0.1297 -0.0815 54  ARG B CB  
4719 C CG  . ARG B 54  ? 1.0034 0.9191 0.4207 -0.4841 -0.1286 -0.0721 54  ARG B CG  
4720 C CD  . ARG B 54  ? 1.0384 1.0147 0.4552 -0.4758 -0.1304 -0.0660 54  ARG B CD  
4721 N NE  . ARG B 54  ? 1.2312 1.2055 0.6560 -0.4529 -0.1249 -0.0449 54  ARG B NE  
4722 C CZ  . ARG B 54  ? 1.3499 1.2889 0.7720 -0.4446 -0.1217 -0.0483 54  ARG B CZ  
4723 N NH1 . ARG B 54  ? 1.2990 1.2028 0.7083 -0.4561 -0.1236 -0.0695 54  ARG B NH1 
4724 N NH2 . ARG B 54  ? 1.2950 1.2336 0.7291 -0.4247 -0.1140 -0.0306 54  ARG B NH2 
4725 N N   . ASP B 55  ? 1.3815 1.2483 0.8024 -0.5382 -0.1213 -0.1088 55  ASP B N   
4726 C CA  . ASP B 55  ? 1.4031 1.2757 0.8308 -0.5578 -0.1171 -0.1228 55  ASP B CA  
4727 C C   . ASP B 55  ? 1.3303 1.1620 0.7635 -0.5549 -0.1124 -0.1090 55  ASP B C   
4728 O O   . ASP B 55  ? 1.1090 0.9643 0.5542 -0.5615 -0.1134 -0.1034 55  ASP B O   
4729 C CB  . ASP B 55  ? 1.4789 1.3325 0.9000 -0.5773 -0.1070 -0.1553 55  ASP B CB  
4730 C CG  . ASP B 55  ? 1.6404 1.5522 1.0596 -0.5888 -0.1116 -0.1756 55  ASP B CG  
4731 O OD1 . ASP B 55  ? 1.6672 1.6410 1.0911 -0.5823 -0.1232 -0.1640 55  ASP B OD1 
4732 O OD2 . ASP B 55  ? 1.7011 1.5971 1.1138 -0.6035 -0.1017 -0.2026 55  ASP B OD2 
4733 N N   . ASN B 56  ? 1.3101 1.0835 0.7342 -0.5440 -0.1072 -0.1032 56  ASN B N   
4734 C CA  . ASN B 56  ? 1.2808 1.0156 0.7065 -0.5383 -0.1029 -0.0895 56  ASN B CA  
4735 C C   . ASN B 56  ? 1.4345 1.1965 0.8717 -0.5288 -0.1098 -0.0648 56  ASN B C   
4736 O O   . ASN B 56  ? 1.5323 1.2908 0.9773 -0.5332 -0.1069 -0.0567 56  ASN B O   
4737 C CB  . ASN B 56  ? 1.3932 1.0724 0.8056 -0.5238 -0.0983 -0.0859 56  ASN B CB  
4738 C CG  . ASN B 56  ? 1.4840 1.1243 0.8860 -0.5311 -0.0846 -0.1056 56  ASN B CG  
4739 O OD1 . ASN B 56  ? 1.5784 1.2289 0.9849 -0.5499 -0.0766 -0.1250 56  ASN B OD1 
4740 N ND2 . ASN B 56  ? 1.4983 1.0956 0.8878 -0.5159 -0.0798 -0.1011 56  ASN B ND2 
4741 N N   . ILE B 57  ? 1.3460 1.1316 0.7854 -0.5153 -0.1158 -0.0525 57  ILE B N   
4742 C CA  . ILE B 57  ? 1.2740 1.0849 0.7265 -0.5049 -0.1169 -0.0283 57  ILE B CA  
4743 C C   . ILE B 57  ? 1.2261 1.0850 0.6909 -0.5144 -0.1175 -0.0228 57  ILE B C   
4744 O O   . ILE B 57  ? 1.1838 1.0395 0.6581 -0.5143 -0.1138 -0.0077 57  ILE B O   
4745 C CB  . ILE B 57  ? 1.2633 1.0959 0.7193 -0.4894 -0.1183 -0.0183 57  ILE B CB  
4746 C CG1 . ILE B 57  ? 1.2153 1.0041 0.6663 -0.4779 -0.1171 -0.0184 57  ILE B CG1 
4747 C CG2 . ILE B 57  ? 1.1312 1.0006 0.6040 -0.4801 -0.1139 0.0062  57  ILE B CG2 
4748 C CD1 . ILE B 57  ? 1.1696 0.9759 0.6264 -0.4643 -0.1164 -0.0130 57  ILE B CD1 
4749 N N   . GLU B 58  ? 1.1915 1.0972 0.6560 -0.5224 -0.1221 -0.0356 58  GLU B N   
4750 C CA  . GLU B 58  ? 1.3074 1.2677 0.7838 -0.5322 -0.1243 -0.0345 58  GLU B CA  
4751 C C   . GLU B 58  ? 1.4006 1.3345 0.8827 -0.5480 -0.1197 -0.0428 58  GLU B C   
4752 O O   . GLU B 58  ? 1.3964 1.3522 0.8922 -0.5492 -0.1183 -0.0280 58  GLU B O   
4753 C CB  . GLU B 58  ? 1.3441 1.3593 0.8167 -0.5409 -0.1306 -0.0546 58  GLU B CB  
4754 C CG  . GLU B 58  ? 1.6330 1.6834 1.1006 -0.5235 -0.1339 -0.0437 58  GLU B CG  
4755 C CD  . GLU B 58  ? 1.9308 2.0449 1.3935 -0.5314 -0.1409 -0.0627 58  GLU B CD  
4756 O OE1 . GLU B 58  ? 1.9580 2.1033 1.4262 -0.5504 -0.1438 -0.0819 58  GLU B OE1 
4757 O OE2 . GLU B 58  ? 2.0724 2.2070 1.5262 -0.5187 -0.1426 -0.0597 58  GLU B OE2 
4758 N N   . ASP B 59  ? 1.4232 1.3085 0.8959 -0.5589 -0.1146 -0.0650 59  ASP B N   
4759 C CA  . ASP B 59  ? 1.3759 1.2257 0.8535 -0.5712 -0.1059 -0.0723 59  ASP B CA  
4760 C C   . ASP B 59  ? 1.3474 1.1671 0.8283 -0.5594 -0.1028 -0.0455 59  ASP B C   
4761 O O   . ASP B 59  ? 1.2057 1.0388 0.7000 -0.5653 -0.1003 -0.0369 59  ASP B O   
4762 C CB  . ASP B 59  ? 1.5194 1.3114 0.9843 -0.5777 -0.0955 -0.0944 59  ASP B CB  
4763 C CG  . ASP B 59  ? 1.7652 1.5823 1.2320 -0.5974 -0.0921 -0.1269 59  ASP B CG  
4764 O OD1 . ASP B 59  ? 1.7698 1.6515 1.2491 -0.6089 -0.0989 -0.1352 59  ASP B OD1 
4765 O OD2 . ASP B 59  ? 1.8185 1.5931 1.2748 -0.6011 -0.0812 -0.1444 59  ASP B OD2 
4766 N N   . ILE B 60  ? 1.3031 1.0846 0.7728 -0.5433 -0.1027 -0.0338 60  ILE B N   
4767 C CA  . ILE B 60  ? 1.2916 1.0468 0.7636 -0.5325 -0.0992 -0.0111 60  ILE B CA  
4768 C C   . ILE B 60  ? 1.3646 1.1669 0.8545 -0.5302 -0.0997 0.0109  60  ILE B C   
4769 O O   . ILE B 60  ? 1.2965 1.0862 0.7942 -0.5316 -0.0938 0.0244  60  ILE B O   
4770 C CB  . ILE B 60  ? 1.3328 1.0581 0.7939 -0.5159 -0.1007 -0.0046 60  ILE B CB  
4771 C CG1 . ILE B 60  ? 1.3818 1.0612 0.8250 -0.5145 -0.0985 -0.0220 60  ILE B CG1 
4772 C CG2 . ILE B 60  ? 1.2543 0.9574 0.7190 -0.5071 -0.0960 0.0150  60  ILE B CG2 
4773 C CD1 . ILE B 60  ? 1.3073 0.9561 0.7404 -0.4975 -0.1000 -0.0154 60  ILE B CD1 
4774 N N   . GLU B 61  ? 1.4296 1.2853 0.9256 -0.5250 -0.1046 0.0160  61  GLU B N   
4775 C CA  . GLU B 61  ? 1.4005 1.3053 0.9133 -0.5187 -0.1018 0.0402  61  GLU B CA  
4776 C C   . GLU B 61  ? 1.5548 1.4841 1.0804 -0.5316 -0.1006 0.0414  61  GLU B C   
4777 O O   . GLU B 61  ? 1.6486 1.5834 1.1869 -0.5274 -0.0933 0.0644  61  GLU B O   
4778 C CB  . GLU B 61  ? 1.3230 1.2862 0.8380 -0.5096 -0.1060 0.0438  61  GLU B CB  
4779 C CG  . GLU B 61  ? 1.5421 1.4900 1.0541 -0.4925 -0.1018 0.0538  61  GLU B CG  
4780 C CD  . GLU B 61  ? 1.6707 1.6776 1.1896 -0.4783 -0.0994 0.0684  61  GLU B CD  
4781 O OE1 . GLU B 61  ? 1.6583 1.6869 1.1921 -0.4662 -0.0875 0.0957  61  GLU B OE1 
4782 O OE2 . GLU B 61  ? 1.7223 1.7526 1.2314 -0.4781 -0.1071 0.0536  61  GLU B OE2 
4783 N N   . GLN B 62  ? 1.5834 1.5282 1.1077 -0.5480 -0.1060 0.0155  62  GLN B N   
4784 C CA  . GLN B 62  ? 1.5137 1.4838 1.0531 -0.5631 -0.1048 0.0101  62  GLN B CA  
4785 C C   . GLN B 62  ? 1.5064 1.4117 1.0463 -0.5682 -0.0950 0.0131  62  GLN B C   
4786 O O   . GLN B 62  ? 1.5415 1.4547 1.0958 -0.5702 -0.0899 0.0290  62  GLN B O   
4787 C CB  . GLN B 62  ? 1.7074 1.7066 1.2468 -0.5818 -0.1101 -0.0248 62  GLN B CB  
4788 C CG  . GLN B 62  ? 1.9314 2.0209 1.4867 -0.5879 -0.1177 -0.0276 62  GLN B CG  
4789 C CD  . GLN B 62  ? 2.0615 2.2097 1.6118 -0.5700 -0.1253 -0.0122 62  GLN B CD  
4790 O OE1 . GLN B 62  ? 2.1550 2.2779 1.6898 -0.5589 -0.1259 -0.0109 62  GLN B OE1 
4791 N NE2 . GLN B 62  ? 2.0201 2.2484 1.5841 -0.5656 -0.1298 0.0004  62  GLN B NE2 
4792 N N   . ALA B 63  ? 1.4187 1.2604 0.9420 -0.5685 -0.0913 -0.0008 63  ALA B N   
4793 C CA  . ALA B 63  ? 1.3913 1.1673 0.9097 -0.5691 -0.0810 0.0025  63  ALA B CA  
4794 C C   . ALA B 63  ? 1.4893 1.2502 1.0110 -0.5567 -0.0767 0.0329  63  ALA B C   
4795 O O   . ALA B 63  ? 1.6519 1.3893 1.1803 -0.5607 -0.0685 0.0416  63  ALA B O   
4796 C CB  . ALA B 63  ? 1.2621 0.9797 0.7590 -0.5642 -0.0776 -0.0122 63  ALA B CB  
4797 N N   . ILE B 64  ? 1.3526 1.1251 0.8709 -0.5424 -0.0799 0.0478  64  ILE B N   
4798 C CA  . ILE B 64  ? 1.4979 1.2580 1.0216 -0.5320 -0.0724 0.0739  64  ILE B CA  
4799 C C   . ILE B 64  ? 1.5276 1.3236 1.0725 -0.5363 -0.0663 0.0935  64  ILE B C   
4800 O O   . ILE B 64  ? 1.4854 1.2518 1.0346 -0.5365 -0.0565 0.1081  64  ILE B O   
4801 C CB  . ILE B 64  ? 1.5633 1.3392 1.0862 -0.5175 -0.0732 0.0838  64  ILE B CB  
4802 C CG1 . ILE B 64  ? 1.4848 1.2128 0.9887 -0.5107 -0.0761 0.0709  64  ILE B CG1 
4803 C CG2 . ILE B 64  ? 1.4865 1.2719 1.0246 -0.5096 -0.0608 0.1117  64  ILE B CG2 
4804 C CD1 . ILE B 64  ? 1.4581 1.2069 0.9611 -0.5004 -0.0801 0.0686  64  ILE B CD1 
4805 N N   . GLU B 65  ? 1.6186 1.4806 1.1762 -0.5387 -0.0717 0.0943  65  GLU B N   
4806 C CA  . GLU B 65  ? 1.6925 1.6002 1.2716 -0.5393 -0.0661 0.1158  65  GLU B CA  
4807 C C   . GLU B 65  ? 1.7054 1.6048 1.2937 -0.5559 -0.0648 0.1056  65  GLU B C   
4808 O O   . GLU B 65  ? 1.7506 1.6860 1.3583 -0.5580 -0.0604 0.1217  65  GLU B O   
4809 C CB  . GLU B 65  ? 1.7297 1.7188 1.3182 -0.5327 -0.0723 0.1217  65  GLU B CB  
4810 C CG  . GLU B 65  ? 1.8308 1.8284 1.4122 -0.5151 -0.0704 0.1319  65  GLU B CG  
4811 C CD  . GLU B 65  ? 1.8804 1.8488 1.4685 -0.5018 -0.0531 0.1601  65  GLU B CD  
4812 O OE1 . GLU B 65  ? 1.8705 1.8363 1.4722 -0.5026 -0.0415 0.1808  65  GLU B OE1 
4813 O OE2 . GLU B 65  ? 1.8800 1.8283 1.4613 -0.4916 -0.0494 0.1604  65  GLU B OE2 
4814 N N   . GLN B 66  ? 1.6549 1.5059 1.2308 -0.5664 -0.0663 0.0795  66  GLN B N   
4815 C CA  . GLN B 66  ? 1.6595 1.4891 1.2447 -0.5816 -0.0602 0.0680  66  GLN B CA  
4816 C C   . GLN B 66  ? 1.7267 1.4796 1.3017 -0.5769 -0.0483 0.0792  66  GLN B C   
4817 O O   . GLN B 66  ? 1.8048 1.5407 1.3915 -0.5834 -0.0390 0.0863  66  GLN B O   
4818 C CB  . GLN B 66  ? 1.7650 1.5912 1.3461 -0.5964 -0.0635 0.0311  66  GLN B CB  
4819 C CG  . GLN B 66  ? 1.7967 1.7047 1.3902 -0.6055 -0.0747 0.0149  66  GLN B CG  
4820 C CD  . GLN B 66  ? 1.7996 1.6989 1.3826 -0.6166 -0.0770 -0.0211 66  GLN B CD  
4821 O OE1 . GLN B 66  ? 1.8679 1.7004 1.4394 -0.6201 -0.0670 -0.0354 66  GLN B OE1 
4822 N NE2 . GLN B 66  ? 1.6619 1.6287 1.2477 -0.6206 -0.0882 -0.0348 66  GLN B NE2 
4823 N N   . VAL B 67  ? 1.7704 1.4794 1.3236 -0.5651 -0.0485 0.0801  67  VAL B N   
4824 C CA  . VAL B 67  ? 1.7449 1.3907 1.2860 -0.5575 -0.0386 0.0927  67  VAL B CA  
4825 C C   . VAL B 67  ? 1.6519 1.3140 1.2078 -0.5529 -0.0311 0.1228  67  VAL B C   
4826 O O   . VAL B 67  ? 1.6289 1.2500 1.1835 -0.5522 -0.0201 0.1353  67  VAL B O   
4827 C CB  . VAL B 67  ? 1.6841 1.2938 1.2006 -0.5445 -0.0423 0.0871  67  VAL B CB  
4828 C CG1 . VAL B 67  ? 1.6594 1.2107 1.1619 -0.5364 -0.0329 0.0977  67  VAL B CG1 
4829 C CG2 . VAL B 67  ? 1.6580 1.2531 1.1609 -0.5473 -0.0469 0.0604  67  VAL B CG2 
4830 N N   . ALA B 68  ? 1.7361 1.4578 1.3060 -0.5489 -0.0344 0.1354  68  ALA B N   
4831 C CA  . ALA B 68  ? 1.7480 1.4892 1.3348 -0.5432 -0.0226 0.1663  68  ALA B CA  
4832 C C   . ALA B 68  ? 1.8655 1.6081 1.4694 -0.5528 -0.0148 0.1763  68  ALA B C   
4833 O O   . ALA B 68  ? 1.9133 1.6174 1.5189 -0.5516 -0.0012 0.1935  68  ALA B O   
4834 C CB  . ALA B 68  ? 1.4758 1.2861 1.0757 -0.5347 -0.0249 0.1789  68  ALA B CB  
4835 N N   . GLN B 69  ? 1.8800 1.6680 1.4975 -0.5633 -0.0226 0.1637  69  GLN B N   
4836 C CA  . GLN B 69  ? 1.9105 1.7059 1.5480 -0.5740 -0.0160 0.1693  69  GLN B CA  
4837 C C   . GLN B 69  ? 1.9022 1.6198 1.5297 -0.5809 -0.0071 0.1596  69  GLN B C   
4838 O O   . GLN B 69  ? 1.9240 1.6136 1.5594 -0.5811 0.0060  0.1788  69  GLN B O   
4839 C CB  . GLN B 69  ? 1.8933 1.7563 1.5478 -0.5860 -0.0273 0.1496  69  GLN B CB  
4840 C CG  . GLN B 69  ? 1.9765 1.9242 1.6405 -0.5768 -0.0356 0.1613  69  GLN B CG  
4841 C CD  . GLN B 69  ? 2.0584 2.0794 1.7381 -0.5893 -0.0479 0.1385  69  GLN B CD  
4842 O OE1 . GLN B 69  ? 2.0261 2.0333 1.7135 -0.6073 -0.0483 0.1124  69  GLN B OE1 
4843 N NE2 . GLN B 69  ? 2.0742 2.1754 1.7594 -0.5795 -0.0563 0.1472  69  GLN B NE2 
4844 N N   . LEU B 70  ? 1.8425 1.5245 1.4525 -0.5850 -0.0118 0.1313  70  LEU B N   
4845 C CA  . LEU B 70  ? 1.8886 1.4968 1.4872 -0.5881 -0.0008 0.1220  70  LEU B CA  
4846 C C   . LEU B 70  ? 2.0064 1.5590 1.5914 -0.5769 0.0104  0.1456  70  LEU B C   
4847 O O   . LEU B 70  ? 2.1521 1.6520 1.7338 -0.5785 0.0229  0.1478  70  LEU B O   
4848 C CB  . LEU B 70  ? 1.8313 1.4070 1.4085 -0.5876 -0.0044 0.0937  70  LEU B CB  
4849 C CG  . LEU B 70  ? 1.7383 1.3535 1.3278 -0.6023 -0.0101 0.0638  70  LEU B CG  
4850 C CD1 . LEU B 70  ? 1.6507 1.2174 1.2185 -0.6002 -0.0062 0.0398  70  LEU B CD1 
4851 C CD2 . LEU B 70  ? 1.7883 1.4201 1.4065 -0.6193 -0.0015 0.0561  70  LEU B CD2 
4852 N N   . HIS B 71  ? 1.9667 1.5312 1.5448 -0.5658 0.0079  0.1618  71  HIS B N   
4853 C CA  . HIS B 71  ? 1.9992 1.5180 1.5659 -0.5572 0.0194  0.1808  71  HIS B CA  
4854 C C   . HIS B 71  ? 2.0599 1.5899 1.6490 -0.5604 0.0333  0.2087  71  HIS B C   
4855 O O   . HIS B 71  ? 2.1019 1.5911 1.6851 -0.5533 0.0426  0.2120  71  HIS B O   
4856 C CB  . HIS B 71  ? 1.9870 1.5139 1.5414 -0.5461 0.0147  0.1833  71  HIS B CB  
4857 C CG  . HIS B 71  ? 1.9809 1.4676 1.5062 -0.5385 0.0075  0.1633  71  HIS B CG  
4858 N ND1 . HIS B 71  ? 2.0608 1.4862 1.5649 -0.5338 0.0142  0.1599  71  HIS B ND1 
4859 C CD2 . HIS B 71  ? 1.9220 1.4228 1.4355 -0.5327 -0.0048 0.1475  71  HIS B CD2 
4860 C CE1 . HIS B 71  ? 2.0540 1.4612 1.5347 -0.5244 0.0059  0.1436  71  HIS B CE1 
4861 N NE2 . HIS B 71  ? 1.9661 1.4173 1.4529 -0.5244 -0.0057 0.1355  71  HIS B NE2 
4862 N N   . THR B 72  ? 2.0487 1.6434 1.6604 -0.5603 0.0322  0.2236  72  THR B N   
4863 C CA  . THR B 72  ? 2.1226 1.7360 1.7580 -0.5608 0.0476  0.2540  72  THR B CA  
4864 C C   . THR B 72  ? 2.1942 1.8121 1.8478 -0.5724 0.0498  0.2523  72  THR B C   
4865 O O   . THR B 72  ? 2.2247 1.8535 1.8969 -0.5686 0.0606  0.2725  72  THR B O   
4866 C CB  . THR B 72  ? 2.0998 1.7870 1.7547 -0.5533 0.0482  0.2731  72  THR B CB  
4867 O OG1 . THR B 72  ? 1.9984 1.7476 1.6623 -0.5575 0.0311  0.2571  72  THR B OG1 
4868 C CG2 . THR B 72  ? 2.0741 1.7548 1.7162 -0.5421 0.0510  0.2754  72  THR B CG2 
4869 N N   . GLU B 73  ? 2.2088 1.8223 1.8575 -0.5811 0.0386  0.2226  73  GLU B N   
4870 C CA  . GLU B 73  ? 2.1951 1.8109 1.8634 -0.5943 0.0420  0.2135  73  GLU B CA  
4871 C C   . GLU B 73  ? 2.2829 1.8126 1.9375 -0.5955 0.0563  0.2115  73  GLU B C   
4872 O O   . GLU B 73  ? 2.4090 1.9284 2.0810 -0.6013 0.0659  0.2135  73  GLU B O   
4873 C CB  . GLU B 73  ? 2.1768 1.8318 1.8503 -0.6048 0.0276  0.1796  73  GLU B CB  
4874 C CG  . GLU B 73  ? 2.2107 1.8940 1.9142 -0.6213 0.0304  0.1666  73  GLU B CG  
4875 C CD  . GLU B 73  ? 2.2122 1.9399 1.9225 -0.6339 0.0180  0.1294  73  GLU B CD  
4876 O OE1 . GLU B 73  ? 2.0980 1.8726 1.7997 -0.6290 0.0035  0.1238  73  GLU B OE1 
4877 O OE2 . GLU B 73  ? 2.2720 1.9866 1.9973 -0.6493 0.0249  0.1047  73  GLU B OE2 
4878 N N   . SER B 74  ? 2.2233 1.7017 1.8439 -0.5802 0.0548  0.2025  74  SER B N   
4879 C CA  . SER B 74  ? 2.1948 1.6071 1.7931 -0.5641 0.0641  0.1954  74  SER B CA  
4880 C C   . SER B 74  ? 2.2566 1.6622 1.8544 -0.5455 0.0721  0.2140  74  SER B C   
4881 O O   . SER B 74  ? 2.2970 1.6529 1.8743 -0.5301 0.0801  0.2102  74  SER B O   
4882 C CB  . SER B 74  ? 2.0778 1.4454 1.6402 -0.5535 0.0601  0.1800  74  SER B CB  
4883 O OG  . SER B 74  ? 1.9684 1.3217 1.5310 -0.5676 0.0597  0.1593  74  SER B OG  
4884 N N   . LEU B 75  ? 2.2658 1.7226 1.8872 -0.5467 0.0721  0.2341  75  LEU B N   
4885 C CA  . LEU B 75  ? 2.3844 1.8388 2.0149 -0.5318 0.0833  0.2513  75  LEU B CA  
4886 C C   . LEU B 75  ? 2.5407 1.9956 2.1955 -0.5390 0.0920  0.2572  75  LEU B C   
4887 O O   . LEU B 75  ? 2.4742 1.9706 2.1551 -0.5582 0.0891  0.2606  75  LEU B O   
4888 C CB  . LEU B 75  ? 2.3662 1.8731 2.0150 -0.5273 0.0845  0.2722  75  LEU B CB  
4889 C CG  . LEU B 75  ? 2.3396 1.8460 2.0029 -0.5117 0.0997  0.2900  75  LEU B CG  
4890 C CD1 . LEU B 75  ? 2.2289 1.7565 1.8946 -0.5005 0.1051  0.2992  75  LEU B CD1 
4891 C CD2 . LEU B 75  ? 2.3328 1.8770 2.0317 -0.5177 0.1064  0.3111  75  LEU B CD2 
4892 N N   . VAL B 76  ? 2.7510 2.1622 2.3986 -0.5251 0.1036  0.2575  76  VAL B N   
4893 C CA  . VAL B 76  ? 2.8762 2.2742 2.5435 -0.5298 0.1141  0.2594  76  VAL B CA  
4894 C C   . VAL B 76  ? 2.9374 2.3326 2.6125 -0.5508 0.1114  0.2414  76  VAL B C   
4895 O O   . VAL B 76  ? 2.9131 2.2652 2.5628 -0.5491 0.1111  0.2213  76  VAL B O   
4896 C CB  . VAL B 76  ? 3.0606 2.5039 2.7649 -0.5299 0.1212  0.2858  76  VAL B CB  
4897 C CG1 . VAL B 76  ? 3.0191 2.5361 2.7499 -0.5468 0.1125  0.2994  76  VAL B CG1 
4898 C CG2 . VAL B 76  ? 3.0765 2.4983 2.7997 -0.5319 0.1338  0.2873  76  VAL B CG2 
4899 N N   . ALA B 77  ? 2.9505 2.3933 2.6629 -0.5712 0.1114  0.2479  77  ALA B N   
4900 C CA  . ALA B 77  ? 2.9344 2.3851 2.6632 -0.5972 0.1104  0.2262  77  ALA B CA  
4901 C C   . ALA B 77  ? 3.0009 2.3869 2.7245 -0.5946 0.1258  0.2068  77  ALA B C   
4902 O O   . ALA B 77  ? 3.0834 2.4361 2.7926 -0.5997 0.1278  0.1830  77  ALA B O   
4903 C CB  . ALA B 77  ? 2.8858 2.3489 2.5983 -0.6066 0.0971  0.2103  77  ALA B CB  
4904 N N   . VAL B 78  ? 2.9781 2.3457 2.7146 -0.5855 0.1391  0.2180  78  VAL B N   
4905 C CA  . VAL B 78  ? 3.0218 2.3326 2.7604 -0.5833 0.1580  0.2023  78  VAL B CA  
4906 C C   . VAL B 78  ? 3.1176 2.3597 2.8132 -0.5648 0.1649  0.1866  78  VAL B C   
4907 O O   . VAL B 78  ? 3.1116 2.3210 2.8083 -0.5727 0.1765  0.1646  78  VAL B O   
4908 C CB  . VAL B 78  ? 2.9404 2.2768 2.7208 -0.6160 0.1635  0.1821  78  VAL B CB  
4909 C CG1 . VAL B 78  ? 2.9554 2.2379 2.7480 -0.6128 0.1880  0.1705  78  VAL B CG1 
4910 C CG2 . VAL B 78  ? 2.8662 2.2867 2.6894 -0.6380 0.1536  0.1979  78  VAL B CG2 
4911 N N   . SER B 79  ? 3.1805 2.4035 2.8409 -0.5408 0.1598  0.1974  79  SER B N   
4912 C CA  . SER B 79  ? 3.2199 2.3816 2.8383 -0.5206 0.1671  0.1877  79  SER B CA  
4913 C C   . SER B 79  ? 3.2173 2.3586 2.8239 -0.5290 0.1679  0.1665  79  SER B C   
4914 O O   . SER B 79  ? 3.2759 2.4561 2.8900 -0.5459 0.1527  0.1602  79  SER B O   
4915 C CB  . SER B 79  ? 3.2545 2.3633 2.8680 -0.5037 0.1898  0.1895  79  SER B CB  
4916 O OG  . SER B 79  ? 3.2686 2.3253 2.8389 -0.4815 0.1966  0.1858  79  SER B OG  
4917 N N   . LYS B 80  ? 3.1074 2.1870 2.6962 -0.5162 0.1879  0.1564  80  LYS B N   
4918 C CA  . LYS B 80  ? 3.0067 2.0555 2.5784 -0.5171 0.1935  0.1389  80  LYS B CA  
4919 C C   . LYS B 80  ? 2.9804 2.0435 2.5887 -0.5453 0.2014  0.1172  80  LYS B C   
4920 O O   . LYS B 80  ? 2.9567 2.0025 2.5573 -0.5506 0.2059  0.1001  80  LYS B O   
4921 C CB  . LYS B 80  ? 2.9614 1.9381 2.5010 -0.4905 0.2164  0.1388  80  LYS B CB  
4922 C CG  . LYS B 80  ? 2.9616 1.9023 2.4786 -0.4855 0.2243  0.1259  80  LYS B CG  
4923 C CD  . LYS B 80  ? 3.0139 1.8827 2.5071 -0.4601 0.2544  0.1274  80  LYS B CD  
4924 C CE  . LYS B 80  ? 2.9940 1.8452 2.4519 -0.4338 0.2505  0.1458  80  LYS B CE  
4925 N NZ  . LYS B 80  ? 3.0436 1.8263 2.4787 -0.4082 0.2819  0.1492  80  LYS B NZ  
4926 N N   . GLU B 81  ? 2.9864 2.0824 2.6364 -0.5645 0.2042  0.1165  81  GLU B N   
4927 C CA  . GLU B 81  ? 2.9878 2.1094 2.6795 -0.5971 0.2103  0.0918  81  GLU B CA  
4928 C C   . GLU B 81  ? 2.9186 2.0829 2.6091 -0.6152 0.1896  0.0795  81  GLU B C   
4929 O O   . GLU B 81  ? 2.8788 2.0292 2.5755 -0.6287 0.1991  0.0531  81  GLU B O   
4930 C CB  . GLU B 81  ? 2.9823 2.1544 2.7202 -0.6175 0.2076  0.0973  81  GLU B CB  
4931 C CG  . GLU B 81  ? 2.9891 2.1200 2.7396 -0.6060 0.2320  0.1028  81  GLU B CG  
4932 C CD  . GLU B 81  ? 3.0183 2.1011 2.7867 -0.6143 0.2632  0.0744  81  GLU B CD  
4933 O OE1 . GLU B 81  ? 3.0405 2.0833 2.8199 -0.6041 0.2876  0.0766  81  GLU B OE1 
4934 O OE2 . GLU B 81  ? 3.0204 2.1046 2.7936 -0.6309 0.2657  0.0489  81  GLU B OE2 
4935 N N   . ASP B 82  ? 2.8928 2.1079 2.5762 -0.6146 0.1639  0.0985  82  ASP B N   
4936 C CA  . ASP B 82  ? 2.8428 2.1069 2.5279 -0.6316 0.1432  0.0900  82  ASP B CA  
4937 C C   . ASP B 82  ? 2.8633 2.1055 2.5024 -0.6084 0.1315  0.1000  82  ASP B C   
4938 O O   . ASP B 82  ? 2.8999 2.1622 2.5340 -0.6184 0.1196  0.0882  82  ASP B O   
4939 C CB  . ASP B 82  ? 2.7132 2.0606 2.4308 -0.6511 0.1252  0.1034  82  ASP B CB  
4940 C CG  . ASP B 82  ? 2.5948 1.9810 2.3603 -0.6729 0.1332  0.0906  82  ASP B CG  
4941 O OD1 . ASP B 82  ? 2.4955 1.9712 2.2867 -0.6855 0.1166  0.0807  82  ASP B OD1 
4942 O OD2 . ASP B 82  ? 2.5837 1.9185 2.3585 -0.6713 0.1552  0.0883  82  ASP B OD2 
4943 N N   . ARG B 83  ? 2.8216 2.0260 2.4297 -0.5791 0.1349  0.1192  83  ARG B N   
4944 C CA  . ARG B 83  ? 2.7904 1.9770 2.3579 -0.5586 0.1244  0.1265  83  ARG B CA  
4945 C C   . ARG B 83  ? 2.8217 1.9734 2.3706 -0.5580 0.1295  0.1077  83  ARG B C   
4946 O O   . ARG B 83  ? 2.8831 2.0527 2.4186 -0.5596 0.1141  0.1053  83  ARG B O   
4947 C CB  . ARG B 83  ? 2.8114 1.9568 2.3508 -0.5300 0.1321  0.1419  83  ARG B CB  
4948 C CG  . ARG B 83  ? 2.8034 1.9838 2.3481 -0.5240 0.1222  0.1621  83  ARG B CG  
4949 C CD  . ARG B 83  ? 2.8648 2.0057 2.3756 -0.4979 0.1271  0.1705  83  ARG B CD  
4950 N NE  . ARG B 83  ? 2.9545 2.0339 2.4492 -0.4843 0.1477  0.1646  83  ARG B NE  
4951 C CZ  . ARG B 83  ? 2.9900 2.0260 2.4548 -0.4728 0.1539  0.1567  83  ARG B CZ  
4952 N NH1 . ARG B 83  ? 2.9531 2.0008 2.4013 -0.4744 0.1391  0.1525  83  ARG B NH1 
4953 N NH2 . ARG B 83  ? 3.0341 2.0143 2.4862 -0.4582 0.1768  0.1546  83  ARG B NH2 
4954 N N   . ASP B 84  ? 2.7711 1.8710 2.3203 -0.5543 0.1538  0.0953  84  ASP B N   
4955 C CA  . ASP B 84  ? 2.7623 1.8232 2.2964 -0.5520 0.1650  0.0785  84  ASP B CA  
4956 C C   . ASP B 84  ? 2.6589 1.7629 2.2215 -0.5826 0.1572  0.0546  84  ASP B C   
4957 O O   . ASP B 84  ? 2.6497 1.7547 2.1952 -0.5759 0.1536  0.0409  84  ASP B O   
4958 C CB  . ASP B 84  ? 2.8714 1.8660 2.4036 -0.5400 0.1992  0.0717  84  ASP B CB  
4959 C CG  . ASP B 84  ? 2.9242 1.8714 2.4196 -0.5059 0.2079  0.0926  84  ASP B CG  
4960 O OD1 . ASP B 84  ? 2.9169 1.8766 2.3839 -0.4918 0.1878  0.1078  84  ASP B OD1 
4961 O OD2 . ASP B 84  ? 2.9337 1.8321 2.4299 -0.4940 0.2362  0.0921  84  ASP B OD2 
4962 N N   . ARG B 85  ? 2.5849 1.7418 2.1873 -0.6065 0.1528  0.0456  85  ARG B N   
4963 C CA  . ARG B 85  ? 2.5434 1.7671 2.1707 -0.6272 0.1421  0.0168  85  ARG B CA  
4964 C C   . ARG B 85  ? 2.4470 1.7288 2.0588 -0.6226 0.1119  0.0229  85  ARG B C   
4965 O O   . ARG B 85  ? 2.4222 1.7379 2.0350 -0.6296 0.1038  0.0003  85  ARG B O   
4966 C CB  . ARG B 85  ? 2.5537 1.8290 2.2272 -0.6519 0.1429  0.0072  85  ARG B CB  
4967 C CG  . ARG B 85  ? 2.6298 1.8571 2.3288 -0.6624 0.1752  -0.0090 85  ARG B CG  
4968 C CD  . ARG B 85  ? 2.7037 1.9463 2.4261 -0.6821 0.1892  -0.0529 85  ARG B CD  
4969 N NE  . ARG B 85  ? 2.7644 1.9585 2.5152 -0.6928 0.2248  -0.0709 85  ARG B NE  
4970 C CZ  . ARG B 85  ? 2.7397 1.9312 2.5160 -0.7111 0.2478  -0.1109 85  ARG B CZ  
4971 N NH1 . ARG B 85  ? 2.6819 1.9169 2.4568 -0.7213 0.2377  -0.1373 85  ARG B NH1 
4972 N NH2 . ARG B 85  ? 2.7355 1.8787 2.5399 -0.7198 0.2836  -0.1257 85  ARG B NH2 
4973 N N   . LEU B 86  ? 2.4033 1.6941 2.0020 -0.6111 0.0979  0.0530  86  LEU B N   
4974 C CA  . LEU B 86  ? 2.3029 1.6441 1.8891 -0.6051 0.0733  0.0614  86  LEU B CA  
4975 C C   . LEU B 86  ? 2.3595 1.6605 1.9069 -0.5847 0.0703  0.0632  86  LEU B C   
4976 O O   . LEU B 86  ? 2.4410 1.7702 1.9804 -0.5840 0.0581  0.0497  86  LEU B O   
4977 C CB  . LEU B 86  ? 2.1181 1.4891 1.7122 -0.6027 0.0644  0.0918  86  LEU B CB  
4978 C CG  . LEU B 86  ? 1.9243 1.3548 1.5577 -0.6200 0.0627  0.0946  86  LEU B CG  
4979 C CD1 . LEU B 86  ? 1.8513 1.3091 1.4894 -0.6134 0.0572  0.1286  86  LEU B CD1 
4980 C CD2 . LEU B 86  ? 1.7938 1.2982 1.4463 -0.6345 0.0493  0.0687  86  LEU B CD2 
4981 N N   . ASN B 87  ? 2.2686 1.5066 1.7917 -0.5676 0.0814  0.0796  87  ASN B N   
4982 C CA  . ASN B 87  ? 2.2036 1.4068 1.6895 -0.5461 0.0790  0.0813  87  ASN B CA  
4983 C C   . ASN B 87  ? 2.2381 1.4278 1.7169 -0.5444 0.0862  0.0569  87  ASN B C   
4984 O O   . ASN B 87  ? 2.2715 1.4462 1.7228 -0.5274 0.0818  0.0561  87  ASN B O   
4985 C CB  . ASN B 87  ? 2.2211 1.3585 1.6825 -0.5277 0.0935  0.0994  87  ASN B CB  
4986 C CG  . ASN B 87  ? 2.2877 1.4157 1.7142 -0.5065 0.0821  0.1091  87  ASN B CG  
4987 O OD1 . ASN B 87  ? 2.2523 1.4254 1.6779 -0.5076 0.0627  0.1071  87  ASN B OD1 
4988 N ND2 . ASN B 87  ? 2.3220 1.3938 1.7203 -0.4867 0.0948  0.1191  87  ASN B ND2 
4989 N N   . GLU B 88  ? 2.2588 1.4557 1.7644 -0.5628 0.0990  0.0361  88  GLU B N   
4990 C CA  . GLU B 88  ? 2.2827 1.4669 1.7875 -0.5653 0.1114  0.0102  88  GLU B CA  
4991 C C   . GLU B 88  ? 2.1608 1.4101 1.6717 -0.5761 0.0895  -0.0049 88  GLU B C   
4992 O O   . GLU B 88  ? 2.0656 1.3059 1.5610 -0.5691 0.0911  -0.0171 88  GLU B O   
4993 C CB  . GLU B 88  ? 2.3802 1.5474 1.9158 -0.5838 0.1374  -0.0102 88  GLU B CB  
4994 C CG  . GLU B 88  ? 2.4617 1.5899 1.9949 -0.5828 0.1636  -0.0345 88  GLU B CG  
4995 C CD  . GLU B 88  ? 2.6323 1.6758 2.1394 -0.5563 0.1918  -0.0204 88  GLU B CD  
4996 O OE1 . GLU B 88  ? 2.7244 1.7440 2.2076 -0.5365 0.1847  0.0074  88  GLU B OE1 
4997 O OE2 . GLU B 88  ? 2.6621 1.6635 2.1725 -0.5544 0.2231  -0.0372 88  GLU B OE2 
4998 N N   . LYS B 89  ? 2.1469 1.4618 1.6802 -0.5915 0.0709  -0.0024 89  LYS B N   
4999 C CA  . LYS B 89  ? 2.1689 1.5505 1.7068 -0.5990 0.0491  -0.0122 89  LYS B CA  
5000 C C   . LYS B 89  ? 2.1126 1.4970 1.6236 -0.5792 0.0315  0.0072  89  LYS B C   
5001 O O   . LYS B 89  ? 2.0541 1.4502 1.5520 -0.5743 0.0231  -0.0027 89  LYS B O   
5002 C CB  . LYS B 89  ? 2.1923 1.6468 1.7619 -0.6173 0.0366  -0.0118 89  LYS B CB  
5003 C CG  . LYS B 89  ? 2.2361 1.7070 1.8387 -0.6407 0.0503  -0.0363 89  LYS B CG  
5004 C CD  . LYS B 89  ? 2.2130 1.7706 1.8451 -0.6556 0.0341  -0.0349 89  LYS B CD  
5005 C CE  . LYS B 89  ? 2.2625 1.8473 1.9305 -0.6810 0.0460  -0.0651 89  LYS B CE  
5006 N NZ  . LYS B 89  ? 2.1981 1.8786 1.8946 -0.6940 0.0288  -0.0655 89  LYS B NZ  
5007 N N   . LEU B 90  ? 2.0596 1.4334 1.5644 -0.5691 0.0280  0.0335  90  LEU B N   
5008 C CA  . LEU B 90  ? 1.9988 1.3766 1.4830 -0.5526 0.0142  0.0499  90  LEU B CA  
5009 C C   . LEU B 90  ? 2.0855 1.4297 1.5410 -0.5363 0.0146  0.0414  90  LEU B C   
5010 O O   . LEU B 90  ? 2.1918 1.5654 1.6412 -0.5328 0.0008  0.0359  90  LEU B O   
5011 C CB  . LEU B 90  ? 1.9990 1.3491 1.4769 -0.5437 0.0190  0.0748  90  LEU B CB  
5012 C CG  . LEU B 90  ? 1.9902 1.3803 1.4914 -0.5526 0.0152  0.0935  90  LEU B CG  
5013 C CD1 . LEU B 90  ? 1.9911 1.3398 1.4815 -0.5431 0.0244  0.1153  90  LEU B CD1 
5014 C CD2 . LEU B 90  ? 1.9998 1.4498 1.5078 -0.5523 -0.0009 0.0973  90  LEU B CD2 
5015 N N   . GLN B 91  ? 2.0441 1.3272 1.4818 -0.5242 0.0315  0.0422  91  GLN B N   
5016 C CA  . GLN B 91  ? 2.0551 1.3079 1.4637 -0.5040 0.0330  0.0390  91  GLN B CA  
5017 C C   . GLN B 91  ? 1.9497 1.2074 1.3623 -0.5105 0.0388  0.0163  91  GLN B C   
5018 O O   . GLN B 91  ? 1.9012 1.1361 1.2925 -0.4944 0.0427  0.0126  91  GLN B O   
5019 C CB  . GLN B 91  ? 2.1958 1.3848 1.5811 -0.4842 0.0507  0.0503  91  GLN B CB  
5020 C CG  . GLN B 91  ? 2.3398 1.4866 1.7354 -0.4901 0.0775  0.0436  91  GLN B CG  
5021 C CD  . GLN B 91  ? 2.4424 1.5313 1.8172 -0.4706 0.0940  0.0608  91  GLN B CD  
5022 O OE1 . GLN B 91  ? 2.3727 1.4618 1.7315 -0.4593 0.0830  0.0776  91  GLN B OE1 
5023 N NE2 . GLN B 91  ? 2.4848 1.5233 1.8603 -0.4664 0.1229  0.0558  91  GLN B NE2 
5024 N N   . ASP B 92  ? 1.9644 1.2552 1.4049 -0.5341 0.0402  0.0006  92  ASP B N   
5025 C CA  . ASP B 92  ? 2.0444 1.3467 1.4922 -0.5451 0.0462  -0.0247 92  ASP B CA  
5026 C C   . ASP B 92  ? 1.9198 1.2834 1.3713 -0.5511 0.0222  -0.0297 92  ASP B C   
5027 O O   . ASP B 92  ? 1.9317 1.2949 1.3707 -0.5450 0.0199  -0.0392 92  ASP B O   
5028 C CB  . ASP B 92  ? 2.1820 1.4884 1.6591 -0.5689 0.0633  -0.0446 92  ASP B CB  
5029 C CG  . ASP B 92  ? 2.3366 1.6430 1.8207 -0.5809 0.0774  -0.0744 92  ASP B CG  
5030 O OD1 . ASP B 92  ? 2.3413 1.6887 1.8232 -0.5853 0.0617  -0.0842 92  ASP B OD1 
5031 O OD2 . ASP B 92  ? 2.4136 1.6771 1.9065 -0.5861 0.1069  -0.0886 92  ASP B OD2 
5032 N N   . THR B 93  ? 1.8908 1.3061 1.3595 -0.5611 0.0062  -0.0213 93  THR B N   
5033 C CA  . THR B 93  ? 1.8554 1.3277 1.3264 -0.5621 -0.0149 -0.0203 93  THR B CA  
5034 C C   . THR B 93  ? 1.7923 1.2496 1.2405 -0.5405 -0.0246 -0.0047 93  THR B C   
5035 O O   . THR B 93  ? 1.9338 1.4104 1.3748 -0.5360 -0.0345 -0.0111 93  THR B O   
5036 C CB  . THR B 93  ? 1.8042 1.3350 1.2985 -0.5732 -0.0257 -0.0097 93  THR B CB  
5037 O OG1 . THR B 93  ? 1.9225 1.4325 1.4156 -0.5645 -0.0234 0.0152  93  THR B OG1 
5038 C CG2 . THR B 93  ? 1.7695 1.3272 1.2890 -0.5954 -0.0186 -0.0284 93  THR B CG2 
5039 N N   . MET B 94  ? 1.5748 0.9989 1.0126 -0.5281 -0.0211 0.0138  94  MET B N   
5040 C CA  . MET B 94  ? 1.6349 1.0459 1.0526 -0.5086 -0.0289 0.0252  94  MET B CA  
5041 C C   . MET B 94  ? 1.6518 1.0394 1.0487 -0.4954 -0.0275 0.0141  94  MET B C   
5042 O O   . MET B 94  ? 1.8360 1.2392 1.2244 -0.4852 -0.0394 0.0150  94  MET B O   
5043 C CB  . MET B 94  ? 1.7157 1.0872 1.1223 -0.4980 -0.0211 0.0417  94  MET B CB  
5044 C CG  . MET B 94  ? 1.6357 1.0306 1.0574 -0.5039 -0.0249 0.0590  94  MET B CG  
5045 S SD  . MET B 94  ? 2.0039 1.3520 1.4063 -0.4891 -0.0170 0.0755  94  MET B SD  
5046 C CE  . MET B 94  ? 1.8866 1.2610 1.3153 -0.5028 -0.0142 0.0943  94  MET B CE  
5047 N N   . ALA B 95  ? 1.6151 0.9638 1.0055 -0.4948 -0.0102 0.0043  95  ALA B N   
5048 C CA  . ALA B 95  ? 1.6190 0.9405 0.9900 -0.4802 -0.0030 -0.0035 95  ALA B CA  
5049 C C   . ALA B 95  ? 1.5516 0.9063 0.9313 -0.4914 -0.0094 -0.0207 95  ALA B C   
5050 O O   . ALA B 95  ? 1.5534 0.9029 0.9191 -0.4789 -0.0117 -0.0240 95  ALA B O   
5051 C CB  . ALA B 95  ? 1.6131 0.8806 0.9775 -0.4757 0.0238  -0.0073 95  ALA B CB  
5052 N N   . ARG B 96  ? 1.5774 0.9684 0.9802 -0.5144 -0.0119 -0.0319 96  ARG B N   
5053 C CA  . ARG B 96  ? 1.7007 1.1289 1.1111 -0.5259 -0.0189 -0.0491 96  ARG B CA  
5054 C C   . ARG B 96  ? 1.6951 1.1637 1.1037 -0.5185 -0.0410 -0.0394 96  ARG B C   
5055 O O   . ARG B 96  ? 1.7353 1.2091 1.1351 -0.5119 -0.0461 -0.0456 96  ARG B O   
5056 C CB  . ARG B 96  ? 1.6555 1.1190 1.0904 -0.5519 -0.0159 -0.0659 96  ARG B CB  
5057 C CG  . ARG B 96  ? 1.8102 1.3083 1.2501 -0.5645 -0.0195 -0.0881 96  ARG B CG  
5058 C CD  . ARG B 96  ? 1.8575 1.3585 1.3147 -0.5881 -0.0021 -0.1156 96  ARG B CD  
5059 N NE  . ARG B 96  ? 1.8642 1.3763 1.3409 -0.6001 0.0011  -0.1133 96  ARG B NE  
5060 C CZ  . ARG B 96  ? 1.7554 1.3268 1.2480 -0.6085 -0.0160 -0.1065 96  ARG B CZ  
5061 N NH1 . ARG B 96  ? 1.3951 1.0190 0.8856 -0.6051 -0.0363 -0.1011 96  ARG B NH1 
5062 N NH2 . ARG B 96  ? 1.7070 1.2846 1.2182 -0.6184 -0.0107 -0.1035 96  ARG B NH2 
5063 N N   . ILE B 97  ? 1.5261 1.0207 0.9447 -0.5192 -0.0511 -0.0236 97  ILE B N   
5064 C CA  . ILE B 97  ? 1.3549 0.8836 0.7755 -0.5115 -0.0664 -0.0128 97  ILE B CA  
5065 C C   . ILE B 97  ? 1.3940 0.8961 0.7955 -0.4919 -0.0692 -0.0101 97  ILE B C   
5066 O O   . ILE B 97  ? 1.5295 1.0537 0.9307 -0.4861 -0.0788 -0.0117 97  ILE B O   
5067 C CB  . ILE B 97  ? 1.3113 0.8573 0.7445 -0.5123 -0.0689 0.0065  97  ILE B CB  
5068 C CG1 . ILE B 97  ? 1.2267 0.8100 0.6808 -0.5300 -0.0677 0.0050  97  ILE B CG1 
5069 C CG2 . ILE B 97  ? 1.2561 0.8292 0.6927 -0.5023 -0.0785 0.0177  97  ILE B CG2 
5070 C CD1 . ILE B 97  ? 1.3192 0.9249 0.7884 -0.5307 -0.0678 0.0262  97  ILE B CD1 
5071 N N   . SER B 98  ? 1.3765 0.8328 0.7622 -0.4807 -0.0600 -0.0061 98  SER B N   
5072 C CA  . SER B 98  ? 1.3925 0.8268 0.7584 -0.4600 -0.0621 -0.0039 98  SER B CA  
5073 C C   . SER B 98  ? 1.4866 0.9114 0.8433 -0.4556 -0.0580 -0.0170 98  SER B C   
5074 O O   . SER B 98  ? 1.3788 0.8166 0.7307 -0.4454 -0.0673 -0.0186 98  SER B O   
5075 C CB  . SER B 98  ? 1.3988 0.7905 0.7483 -0.4468 -0.0521 0.0059  98  SER B CB  
5076 O OG  . SER B 98  ? 1.5552 0.9260 0.8829 -0.4246 -0.0512 0.0065  98  SER B OG  
5077 N N   . ALA B 99  ? 1.5613 0.9627 0.9177 -0.4641 -0.0418 -0.0272 99  ALA B N   
5078 C CA  . ALA B 99  ? 1.5029 0.8915 0.8527 -0.4624 -0.0324 -0.0404 99  ALA B CA  
5079 C C   . ALA B 99  ? 1.4557 0.8875 0.8161 -0.4732 -0.0458 -0.0506 99  ALA B C   
5080 O O   . ALA B 99  ? 1.3749 0.8038 0.7270 -0.4643 -0.0465 -0.0552 99  ALA B O   
5081 C CB  . ALA B 99  ? 1.4089 0.7668 0.7626 -0.4743 -0.0082 -0.0525 99  ALA B CB  
5082 N N   . LEU B 100 ? 1.3706 0.8430 0.7489 -0.4906 -0.0552 -0.0528 100 LEU B N   
5083 C CA  . LEU B 100 ? 1.3651 0.8834 0.7528 -0.4980 -0.0682 -0.0589 100 LEU B CA  
5084 C C   . LEU B 100 ? 1.4748 1.0074 0.8600 -0.4818 -0.0822 -0.0467 100 LEU B C   
5085 O O   . LEU B 100 ? 1.5093 1.0565 0.8934 -0.4780 -0.0879 -0.0520 100 LEU B O   
5086 C CB  . LEU B 100 ? 1.3119 0.8742 0.7185 -0.5160 -0.0734 -0.0602 100 LEU B CB  
5087 C CG  . LEU B 100 ? 1.4266 0.9956 0.8413 -0.5371 -0.0626 -0.0815 100 LEU B CG  
5088 C CD1 . LEU B 100 ? 1.0455 0.6657 0.4795 -0.5525 -0.0695 -0.0812 100 LEU B CD1 
5089 C CD2 . LEU B 100 ? 1.4654 1.0428 0.8749 -0.5413 -0.0614 -0.0992 100 LEU B CD2 
5090 N N   . GLY B 101 ? 1.4473 0.9747 0.8329 -0.4731 -0.0858 -0.0319 101 GLY B N   
5091 C CA  . GLY B 101 ? 1.4501 0.9880 0.8359 -0.4590 -0.0955 -0.0237 101 GLY B CA  
5092 C C   . GLY B 101 ? 1.4501 0.9683 0.8211 -0.4428 -0.0963 -0.0287 101 GLY B C   
5093 O O   . GLY B 101 ? 1.4695 1.0077 0.8454 -0.4378 -0.1038 -0.0318 101 GLY B O   
5094 N N   . ASN B 102 ? 1.4316 0.9114 0.7853 -0.4329 -0.0869 -0.0283 102 ASN B N   
5095 C CA  . ASN B 102 ? 1.4476 0.9106 0.7862 -0.4138 -0.0860 -0.0298 102 ASN B CA  
5096 C C   . ASN B 102 ? 1.3956 0.8623 0.7349 -0.4173 -0.0834 -0.0407 102 ASN B C   
5097 O O   . ASN B 102 ? 1.3667 0.8377 0.7020 -0.4038 -0.0884 -0.0414 102 ASN B O   
5098 C CB  . ASN B 102 ? 1.5881 1.0094 0.9069 -0.3993 -0.0723 -0.0238 102 ASN B CB  
5099 C CG  . ASN B 102 ? 1.7844 1.2028 1.0975 -0.3897 -0.0770 -0.0129 102 ASN B CG  
5100 O OD1 . ASN B 102 ? 1.8675 1.2614 1.1753 -0.3918 -0.0667 -0.0072 102 ASN B OD1 
5101 N ND2 . ASN B 102 ? 1.7759 1.2197 1.0917 -0.3804 -0.0912 -0.0117 102 ASN B ND2 
5102 N N   . LYS B 103 ? 1.4487 0.9161 0.7941 -0.4359 -0.0751 -0.0504 103 LYS B N   
5103 C CA  . LYS B 103 ? 1.5139 0.9857 0.8597 -0.4418 -0.0713 -0.0627 103 LYS B CA  
5104 C C   . LYS B 103 ? 1.4626 0.9743 0.8199 -0.4425 -0.0877 -0.0627 103 LYS B C   
5105 O O   . LYS B 103 ? 1.4581 0.9704 0.8125 -0.4332 -0.0900 -0.0653 103 LYS B O   
5106 C CB  . LYS B 103 ? 1.5562 1.0267 0.9079 -0.4644 -0.0587 -0.0774 103 LYS B CB  
5107 C CG  . LYS B 103 ? 1.5808 1.0189 0.9238 -0.4658 -0.0380 -0.0899 103 LYS B CG  
5108 C CD  . LYS B 103 ? 1.6375 1.0890 0.9792 -0.4638 -0.0428 -0.0963 103 LYS B CD  
5109 C CE  . LYS B 103 ? 1.7645 1.1757 1.0922 -0.4468 -0.0258 -0.0941 103 LYS B CE  
5110 N NZ  . LYS B 103 ? 1.9067 1.2819 1.2318 -0.4574 0.0037  -0.1068 103 LYS B NZ  
5111 N N   . ILE B 104 ? 1.3641 0.9081 0.7355 -0.4522 -0.0964 -0.0585 104 ILE B N   
5112 C CA  . ILE B 104 ? 1.3508 0.9320 0.7352 -0.4508 -0.1075 -0.0556 104 ILE B CA  
5113 C C   . ILE B 104 ? 1.3301 0.9069 0.7143 -0.4325 -0.1135 -0.0508 104 ILE B C   
5114 O O   . ILE B 104 ? 1.2412 0.8319 0.6309 -0.4274 -0.1174 -0.0542 104 ILE B O   
5115 C CB  . ILE B 104 ? 1.2788 0.8909 0.6784 -0.4584 -0.1116 -0.0459 104 ILE B CB  
5116 C CG1 . ILE B 104 ? 1.2477 0.8857 0.6526 -0.4760 -0.1097 -0.0524 104 ILE B CG1 
5117 C CG2 . ILE B 104 ? 1.2300 0.8695 0.6436 -0.4500 -0.1176 -0.0386 104 ILE B CG2 
5118 C CD1 . ILE B 104 ? 1.1765 0.8355 0.5932 -0.4837 -0.1099 -0.0418 104 ILE B CD1 
5119 N N   . ARG B 105 ? 1.3012 0.8607 0.6795 -0.4225 -0.1137 -0.0441 105 ARG B N   
5120 C CA  . ARG B 105 ? 1.3348 0.8974 0.7143 -0.4059 -0.1202 -0.0428 105 ARG B CA  
5121 C C   . ARG B 105 ? 1.3903 0.9375 0.7581 -0.3933 -0.1187 -0.0482 105 ARG B C   
5122 O O   . ARG B 105 ? 1.5431 1.1046 0.9183 -0.3835 -0.1250 -0.0512 105 ARG B O   
5123 C CB  . ARG B 105 ? 1.1689 0.7222 0.5432 -0.3982 -0.1212 -0.0360 105 ARG B CB  
5124 C CG  . ARG B 105 ? 1.3697 0.9308 0.7435 -0.3808 -0.1283 -0.0389 105 ARG B CG  
5125 C CD  . ARG B 105 ? 1.4890 1.0613 0.8698 -0.3795 -0.1313 -0.0364 105 ARG B CD  
5126 N NE  . ARG B 105 ? 1.5670 1.1156 0.9328 -0.3807 -0.1259 -0.0283 105 ARG B NE  
5127 C CZ  . ARG B 105 ? 1.7157 1.2609 1.0731 -0.3715 -0.1274 -0.0263 105 ARG B CZ  
5128 N NH1 . ARG B 105 ? 1.6087 1.1773 0.9725 -0.3620 -0.1351 -0.0343 105 ARG B NH1 
5129 N NH2 . ARG B 105 ? 1.8105 1.3305 1.1539 -0.3722 -0.1207 -0.0178 105 ARG B NH2 
5130 N N   . ALA B 106 ? 1.3584 0.8759 0.7102 -0.3935 -0.1077 -0.0496 106 ALA B N   
5131 C CA  . ALA B 106 ? 1.4361 0.9353 0.7764 -0.3801 -0.1017 -0.0518 106 ALA B CA  
5132 C C   . ALA B 106 ? 1.5158 1.0254 0.8636 -0.3889 -0.1011 -0.0607 106 ALA B C   
5133 O O   . ALA B 106 ? 1.5468 1.0554 0.8935 -0.3769 -0.1019 -0.0618 106 ALA B O   
5134 C CB  . ALA B 106 ? 1.2262 0.6862 0.5484 -0.3758 -0.0840 -0.0492 106 ALA B CB  
5135 N N   . ASP B 107 ? 1.4784 1.0005 0.8333 -0.4090 -0.0997 -0.0668 107 ASP B N   
5136 C CA  . ASP B 107 ? 1.5209 1.0576 0.8813 -0.4174 -0.0998 -0.0755 107 ASP B CA  
5137 C C   . ASP B 107 ? 1.5115 1.0770 0.8869 -0.4094 -0.1121 -0.0722 107 ASP B C   
5138 O O   . ASP B 107 ? 1.5654 1.1327 0.9429 -0.4041 -0.1121 -0.0761 107 ASP B O   
5139 C CB  . ASP B 107 ? 1.5584 1.1114 0.9225 -0.4396 -0.0967 -0.0838 107 ASP B CB  
5140 C CG  . ASP B 107 ? 1.6464 1.1707 0.9998 -0.4512 -0.0796 -0.0947 107 ASP B CG  
5141 O OD1 . ASP B 107 ? 1.6977 1.1887 1.0404 -0.4424 -0.0669 -0.0964 107 ASP B OD1 
5142 O OD2 . ASP B 107 ? 1.6138 1.1504 0.9716 -0.4691 -0.0766 -0.1019 107 ASP B OD2 
5143 N N   . LEU B 108 ? 1.4085 0.9942 0.7961 -0.4086 -0.1195 -0.0653 108 LEU B N   
5144 C CA  . LEU B 108 ? 1.3972 1.0074 0.8031 -0.4009 -0.1261 -0.0635 108 LEU B CA  
5145 C C   . LEU B 108 ? 1.5345 1.1361 0.9403 -0.3838 -0.1293 -0.0660 108 LEU B C   
5146 O O   . LEU B 108 ? 1.5670 1.1755 0.9810 -0.3786 -0.1299 -0.0702 108 LEU B O   
5147 C CB  . LEU B 108 ? 1.2924 0.9217 0.7128 -0.4035 -0.1284 -0.0561 108 LEU B CB  
5148 C CG  . LEU B 108 ? 1.2540 0.9051 0.6814 -0.4167 -0.1255 -0.0509 108 LEU B CG  
5149 C CD1 . LEU B 108 ? 1.1471 0.8128 0.5894 -0.4176 -0.1239 -0.0411 108 LEU B CD1 
5150 C CD2 . LEU B 108 ? 1.1235 0.7964 0.5587 -0.4174 -0.1241 -0.0530 108 LEU B CD2 
5151 N N   . LYS B 109 ? 1.5298 1.1186 0.9260 -0.3740 -0.1310 -0.0631 109 LYS B N   
5152 C CA  . LYS B 109 ? 1.4353 1.0233 0.8300 -0.3555 -0.1350 -0.0651 109 LYS B CA  
5153 C C   . LYS B 109 ? 1.4278 1.0011 0.8150 -0.3497 -0.1297 -0.0675 109 LYS B C   
5154 O O   . LYS B 109 ? 1.4424 1.0273 0.8402 -0.3394 -0.1336 -0.0712 109 LYS B O   
5155 C CB  . LYS B 109 ? 1.5129 1.0887 0.8912 -0.3434 -0.1358 -0.0599 109 LYS B CB  
5156 C CG  . LYS B 109 ? 1.7370 1.3354 1.1271 -0.3421 -0.1436 -0.0613 109 LYS B CG  
5157 C CD  . LYS B 109 ? 1.9053 1.4927 1.2758 -0.3294 -0.1443 -0.0558 109 LYS B CD  
5158 C CE  . LYS B 109 ? 1.9536 1.5626 1.3355 -0.3324 -0.1503 -0.0592 109 LYS B CE  
5159 N NZ  . LYS B 109 ? 1.9888 1.5869 1.3488 -0.3200 -0.1505 -0.0533 109 LYS B NZ  
5160 N N   . GLN B 110 ? 1.4750 1.0225 0.8461 -0.3574 -0.1189 -0.0666 110 GLN B N   
5161 C CA  . GLN B 110 ? 1.5022 1.0314 0.8657 -0.3542 -0.1095 -0.0693 110 GLN B CA  
5162 C C   . GLN B 110 ? 1.4975 1.0454 0.8768 -0.3593 -0.1136 -0.0755 110 GLN B C   
5163 O O   . GLN B 110 ? 1.4798 1.0237 0.8616 -0.3487 -0.1120 -0.0765 110 GLN B O   
5164 C CB  . GLN B 110 ? 1.7217 1.2218 1.0695 -0.3670 -0.0934 -0.0716 110 GLN B CB  
5165 C CG  . GLN B 110 ? 1.9002 1.3782 1.2409 -0.3679 -0.0788 -0.0766 110 GLN B CG  
5166 C CD  . GLN B 110 ? 1.9707 1.4369 1.3069 -0.3439 -0.0752 -0.0688 110 GLN B CD  
5167 O OE1 . GLN B 110 ? 1.9821 1.4500 1.3137 -0.3252 -0.0793 -0.0596 110 GLN B OE1 
5168 N NE2 . GLN B 110 ? 1.8556 1.3124 1.1926 -0.3434 -0.0673 -0.0722 110 GLN B NE2 
5169 N N   . ILE B 111 ? 1.4896 1.0586 0.8800 -0.3734 -0.1176 -0.0779 111 ILE B N   
5170 C CA  . ILE B 111 ? 1.4734 1.0601 0.8775 -0.3762 -0.1188 -0.0817 111 ILE B CA  
5171 C C   . ILE B 111 ? 1.4898 1.0943 0.9152 -0.3628 -0.1254 -0.0817 111 ILE B C   
5172 O O   . ILE B 111 ? 1.3798 0.9878 0.8153 -0.3577 -0.1237 -0.0849 111 ILE B O   
5173 C CB  . ILE B 111 ? 1.4039 1.0131 0.8134 -0.3911 -0.1191 -0.0815 111 ILE B CB  
5174 C CG1 . ILE B 111 ? 1.3797 0.9781 0.7719 -0.4066 -0.1132 -0.0856 111 ILE B CG1 
5175 C CG2 . ILE B 111 ? 1.4292 1.0541 0.8484 -0.3905 -0.1173 -0.0839 111 ILE B CG2 
5176 C CD1 . ILE B 111 ? 1.2890 0.9175 0.6854 -0.4204 -0.1145 -0.0862 111 ILE B CD1 
5177 N N   . GLU B 112 ? 1.5416 1.1572 0.9748 -0.3579 -0.1314 -0.0797 112 GLU B N   
5178 C CA  . GLU B 112 ? 1.5884 1.2243 1.0445 -0.3474 -0.1363 -0.0843 112 GLU B CA  
5179 C C   . GLU B 112 ? 1.6335 1.2623 1.0875 -0.3324 -0.1380 -0.0875 112 GLU B C   
5180 O O   . GLU B 112 ? 1.6278 1.2645 1.0986 -0.3279 -0.1367 -0.0925 112 GLU B O   
5181 C CB  . GLU B 112 ? 1.7095 1.3572 1.1699 -0.3459 -0.1415 -0.0841 112 GLU B CB  
5182 C CG  . GLU B 112 ? 1.9287 1.6022 1.4162 -0.3385 -0.1449 -0.0939 112 GLU B CG  
5183 C CD  . GLU B 112 ? 2.0799 1.7642 1.5655 -0.3343 -0.1511 -0.0968 112 GLU B CD  
5184 O OE1 . GLU B 112 ? 2.1071 1.7746 1.5682 -0.3349 -0.1525 -0.0886 112 GLU B OE1 
5185 O OE2 . GLU B 112 ? 2.0686 1.7785 1.5778 -0.3309 -0.1533 -0.1087 112 GLU B OE2 
5186 N N   . LYS B 113 ? 1.7311 1.3450 1.1647 -0.3230 -0.1391 -0.0831 113 LYS B N   
5187 C CA  . LYS B 113 ? 1.7908 1.3976 1.2190 -0.3060 -0.1382 -0.0821 113 LYS B CA  
5188 C C   . LYS B 113 ? 1.7061 1.2959 1.1338 -0.3097 -0.1294 -0.0826 113 LYS B C   
5189 O O   . LYS B 113 ? 1.6477 1.2439 1.0879 -0.2993 -0.1301 -0.0854 113 LYS B O   
5190 C CB  . LYS B 113 ? 1.9438 1.5302 1.3452 -0.2948 -0.1340 -0.0726 113 LYS B CB  
5191 C CG  . LYS B 113 ? 2.0772 1.6819 1.4763 -0.2860 -0.1433 -0.0717 113 LYS B CG  
5192 C CD  . LYS B 113 ? 2.1646 1.7465 1.5351 -0.2714 -0.1357 -0.0596 113 LYS B CD  
5193 C CE  . LYS B 113 ? 2.1063 1.7077 1.4717 -0.2616 -0.1451 -0.0586 113 LYS B CE  
5194 N NZ  . LYS B 113 ? 2.1011 1.6779 1.4373 -0.2453 -0.1350 -0.0445 113 LYS B NZ  
5195 N N   . GLU B 114 ? 1.7599 1.3301 1.1739 -0.3250 -0.1209 -0.0814 114 GLU B N   
5196 C CA  . GLU B 114 ? 1.8354 1.3907 1.2467 -0.3309 -0.1117 -0.0841 114 GLU B CA  
5197 C C   . GLU B 114 ? 1.7517 1.3274 1.1873 -0.3299 -0.1155 -0.0891 114 GLU B C   
5198 O O   . GLU B 114 ? 1.7165 1.2837 1.1565 -0.3233 -0.1108 -0.0904 114 GLU B O   
5199 C CB  . GLU B 114 ? 1.8777 1.4204 1.2737 -0.3506 -0.1038 -0.0866 114 GLU B CB  
5200 C CG  . GLU B 114 ? 1.9172 1.4252 1.2914 -0.3535 -0.0882 -0.0864 114 GLU B CG  
5201 C CD  . GLU B 114 ? 2.0589 1.5615 1.4223 -0.3760 -0.0806 -0.0941 114 GLU B CD  
5202 O OE1 . GLU B 114 ? 2.0547 1.5815 1.4243 -0.3862 -0.0896 -0.0956 114 GLU B OE1 
5203 O OE2 . GLU B 114 ? 2.1501 1.6263 1.5004 -0.3837 -0.0641 -0.0996 114 GLU B OE2 
5204 N N   . ASN B 115 ? 1.6682 1.2685 1.1204 -0.3355 -0.1210 -0.0909 115 ASN B N   
5205 C CA  . ASN B 115 ? 1.5839 1.2024 1.0621 -0.3335 -0.1197 -0.0948 115 ASN B CA  
5206 C C   . ASN B 115 ? 1.6245 1.2555 1.1258 -0.3191 -0.1237 -0.1006 115 ASN B C   
5207 O O   . ASN B 115 ? 1.6579 1.2879 1.1736 -0.3129 -0.1195 -0.1040 115 ASN B O   
5208 C CB  . ASN B 115 ? 1.4849 1.1251 0.9757 -0.3420 -0.1193 -0.0930 115 ASN B CB  
5209 C CG  . ASN B 115 ? 1.5404 1.1788 1.0133 -0.3552 -0.1155 -0.0883 115 ASN B CG  
5210 O OD1 . ASN B 115 ? 1.5879 1.2085 1.0391 -0.3609 -0.1130 -0.0896 115 ASN B OD1 
5211 N ND2 . ASN B 115 ? 1.4906 1.1502 0.9738 -0.3601 -0.1135 -0.0835 115 ASN B ND2 
5212 N N   . LYS B 116 ? 1.6502 1.2955 1.1555 -0.3140 -0.1318 -0.1028 116 LYS B N   
5213 C CA  . LYS B 116 ? 1.5680 1.2347 1.0956 -0.3010 -0.1377 -0.1116 116 LYS B CA  
5214 C C   . LYS B 116 ? 1.6288 1.2839 1.1514 -0.2879 -0.1367 -0.1098 116 LYS B C   
5215 O O   . LYS B 116 ? 1.7457 1.4141 1.2935 -0.2806 -0.1362 -0.1176 116 LYS B O   
5216 C CB  . LYS B 116 ? 1.5431 1.2259 1.0650 -0.2968 -0.1473 -0.1132 116 LYS B CB  
5217 C CG  . LYS B 116 ? 1.7394 1.4583 1.2909 -0.2890 -0.1538 -0.1281 116 LYS B CG  
5218 C CD  . LYS B 116 ? 1.8315 1.5696 1.3823 -0.2923 -0.1601 -0.1326 116 LYS B CD  
5219 C CE  . LYS B 116 ? 1.8719 1.6512 1.4572 -0.2888 -0.1644 -0.1531 116 LYS B CE  
5220 N NZ  . LYS B 116 ? 1.8233 1.6218 1.4122 -0.2958 -0.1672 -0.1608 116 LYS B NZ  
5221 N N   . ARG B 117 ? 1.6498 1.2787 1.1418 -0.2850 -0.1337 -0.0994 117 ARG B N   
5222 C CA  . ARG B 117 ? 1.8398 1.4525 1.3242 -0.2720 -0.1283 -0.0942 117 ARG B CA  
5223 C C   . ARG B 117 ? 1.8196 1.4091 1.3038 -0.2802 -0.1170 -0.0940 117 ARG B C   
5224 O O   . ARG B 117 ? 1.9019 1.4637 1.3688 -0.2769 -0.1069 -0.0873 117 ARG B O   
5225 C CB  . ARG B 117 ? 2.1478 1.7374 1.6004 -0.2648 -0.1230 -0.0823 117 ARG B CB  
5226 C CG  . ARG B 117 ? 2.3460 1.9575 1.7938 -0.2490 -0.1326 -0.0793 117 ARG B CG  
5227 C CD  . ARG B 117 ? 2.5226 2.1070 1.9406 -0.2352 -0.1212 -0.0640 117 ARG B CD  
5228 N NE  . ARG B 117 ? 2.6408 2.2150 2.0591 -0.2194 -0.1118 -0.0567 117 ARG B NE  
5229 C CZ  . ARG B 117 ? 2.6659 2.2099 2.0618 -0.2070 -0.0943 -0.0418 117 ARG B CZ  
5230 N NH1 . ARG B 117 ? 2.6805 2.2001 2.0523 -0.2089 -0.0836 -0.0340 117 ARG B NH1 
5231 N NH2 . ARG B 117 ? 2.6378 2.1740 2.0369 -0.1923 -0.0845 -0.0342 117 ARG B NH2 
5232 N N   . ALA B 118 ? 1.6992 1.2994 1.2020 -0.2900 -0.1164 -0.1006 118 ALA B N   
5233 C CA  . ALA B 118 ? 1.6832 1.2655 1.1846 -0.2965 -0.1059 -0.1004 118 ALA B CA  
5234 C C   . ALA B 118 ? 1.8214 1.4218 1.3551 -0.2951 -0.1037 -0.1072 118 ALA B C   
5235 O O   . ALA B 118 ? 1.8337 1.4216 1.3690 -0.2968 -0.0944 -0.1067 118 ALA B O   
5236 C CB  . ALA B 118 ? 1.5799 1.1485 1.0564 -0.3130 -0.1011 -0.0975 118 ALA B CB  
5237 N N   . GLN B 119 ? 1.8747 1.5034 1.4342 -0.2919 -0.1098 -0.1142 119 GLN B N   
5238 C CA  . GLN B 119 ? 1.8891 1.5346 1.4852 -0.2900 -0.1030 -0.1226 119 GLN B CA  
5239 C C   . GLN B 119 ? 1.9824 1.6187 1.5947 -0.2799 -0.0968 -0.1258 119 GLN B C   
5240 O O   . GLN B 119 ? 1.9612 1.5825 1.5759 -0.2808 -0.0853 -0.1230 119 GLN B O   
5241 C CB  . GLN B 119 ? 1.9178 1.5953 1.5413 -0.2885 -0.1090 -0.1340 119 GLN B CB  
5242 C CG  . GLN B 119 ? 1.9634 1.6499 1.5748 -0.2982 -0.1135 -0.1309 119 GLN B CG  
5243 C CD  . GLN B 119 ? 2.0143 1.7033 1.6362 -0.3068 -0.1010 -0.1272 119 GLN B CD  
5244 O OE1 . GLN B 119 ? 1.9348 1.6266 1.5831 -0.3037 -0.0876 -0.1306 119 GLN B OE1 
5245 N NE2 . GLN B 119 ? 2.0653 1.7538 1.6672 -0.3159 -0.1035 -0.1188 119 GLN B NE2 
5246 N N   . GLN B 120 ? 2.1198 1.7670 1.7423 -0.2691 -0.1044 -0.1309 120 GLN B N   
5247 C CA  . GLN B 120 ? 2.2056 1.8503 1.8498 -0.2582 -0.0994 -0.1351 120 GLN B CA  
5248 C C   . GLN B 120 ? 2.1236 1.7301 1.7458 -0.2584 -0.0889 -0.1242 120 GLN B C   
5249 O O   . GLN B 120 ? 2.1109 1.7081 1.7520 -0.2531 -0.0793 -0.1265 120 GLN B O   
5250 C CB  . GLN B 120 ? 2.3122 1.9785 1.9622 -0.2446 -0.1111 -0.1385 120 GLN B CB  
5251 C CG  . GLN B 120 ? 2.3637 2.0680 2.0228 -0.2449 -0.1240 -0.1485 120 GLN B CG  
5252 C CD  . GLN B 120 ? 2.3998 2.0944 2.0191 -0.2477 -0.1312 -0.1364 120 GLN B CD  
5253 O OE1 . GLN B 120 ? 2.3806 2.0691 1.9893 -0.2606 -0.1299 -0.1347 120 GLN B OE1 
5254 N NE2 . GLN B 120 ? 2.4172 2.1102 2.0153 -0.2339 -0.1367 -0.1270 120 GLN B NE2 
5255 N N   . GLU B 121 ? 2.1002 1.6843 1.6835 -0.2653 -0.0889 -0.1138 121 GLU B N   
5256 C CA  . GLU B 121 ? 2.2644 1.8130 1.8242 -0.2683 -0.0776 -0.1063 121 GLU B CA  
5257 C C   . GLU B 121 ? 2.2789 1.8203 1.8334 -0.2790 -0.0692 -0.1066 121 GLU B C   
5258 O O   . GLU B 121 ? 2.3284 1.8481 1.8767 -0.2791 -0.0581 -0.1047 121 GLU B O   
5259 C CB  . GLU B 121 ? 2.4031 1.9312 1.9263 -0.2723 -0.0772 -0.0981 121 GLU B CB  
5260 C CG  . GLU B 121 ? 2.5233 2.0515 2.0453 -0.2565 -0.0796 -0.0921 121 GLU B CG  
5261 C CD  . GLU B 121 ? 2.6224 2.1881 2.1591 -0.2480 -0.0951 -0.0961 121 GLU B CD  
5262 O OE1 . GLU B 121 ? 2.6775 2.2604 2.2167 -0.2577 -0.1024 -0.1016 121 GLU B OE1 
5263 O OE2 . GLU B 121 ? 2.6172 2.1977 2.1625 -0.2308 -0.0994 -0.0935 121 GLU B OE2 
5264 N N   . GLY B 122 ? 2.2229 1.7845 1.7791 -0.2866 -0.0735 -0.1081 122 GLY B N   
5265 C CA  . GLY B 122 ? 2.1634 1.7260 1.7119 -0.2941 -0.0660 -0.1056 122 GLY B CA  
5266 C C   . GLY B 122 ? 2.1030 1.6791 1.6851 -0.2862 -0.0563 -0.1079 122 GLY B C   
5267 O O   . GLY B 122 ? 2.0261 1.6088 1.6045 -0.2881 -0.0483 -0.1032 122 GLY B O   
5268 N N   . THR B 123 ? 2.1063 1.6888 1.7224 -0.2764 -0.0553 -0.1152 123 THR B N   
5269 C CA  . THR B 123 ? 2.0837 1.6742 1.7377 -0.2685 -0.0410 -0.1199 123 THR B CA  
5270 C C   . THR B 123 ? 2.2023 1.7734 1.8708 -0.2586 -0.0327 -0.1225 123 THR B C   
5271 O O   . THR B 123 ? 2.2044 1.7753 1.8814 -0.2540 -0.0404 -0.1275 123 THR B O   
5272 C CB  . THR B 123 ? 1.9489 1.5683 1.6408 -0.2674 -0.0428 -0.1316 123 THR B CB  
5273 O OG1 . THR B 123 ? 1.9669 1.5946 1.6702 -0.2631 -0.0548 -0.1410 123 THR B OG1 
5274 C CG2 . THR B 123 ? 1.8680 1.5045 1.5465 -0.2771 -0.0499 -0.1284 123 THR B CG2 
5275 N N   . PHE B 124 ? 2.3200 1.8763 1.9910 -0.2537 -0.0161 -0.1176 124 PHE B N   
5276 C CA  . PHE B 124 ? 2.4432 1.9760 2.1251 -0.2445 -0.0058 -0.1183 124 PHE B CA  
5277 C C   . PHE B 124 ? 2.4309 1.9708 2.1623 -0.2342 0.0113  -0.1262 124 PHE B C   
5278 O O   . PHE B 124 ? 2.4417 1.9615 2.1805 -0.2256 0.0289  -0.1224 124 PHE B O   
5279 C CB  . PHE B 124 ? 2.5845 2.0917 2.2304 -0.2459 0.0026  -0.1079 124 PHE B CB  
5280 C CG  . PHE B 124 ? 2.7355 2.2376 2.3354 -0.2590 -0.0095 -0.1035 124 PHE B CG  
5281 C CD1 . PHE B 124 ? 2.7688 2.2879 2.3469 -0.2674 -0.0130 -0.0995 124 PHE B CD1 
5282 C CD2 . PHE B 124 ? 2.8299 2.3107 2.4111 -0.2626 -0.0148 -0.1034 124 PHE B CD2 
5283 C CE1 . PHE B 124 ? 2.8371 2.3527 2.3772 -0.2812 -0.0224 -0.0987 124 PHE B CE1 
5284 C CE2 . PHE B 124 ? 2.8641 2.3375 2.4068 -0.2756 -0.0210 -0.1014 124 PHE B CE2 
5285 C CZ  . PHE B 124 ? 2.8686 2.3597 2.3917 -0.2859 -0.0252 -0.1006 124 PHE B CZ  
5286 N N   . GLU B 125 ? 2.3876 1.9555 2.1536 -0.2355 0.0081  -0.1386 125 GLU B N   
5287 C CA  . GLU B 125 ? 2.3588 1.9366 2.1762 -0.2289 0.0286  -0.1496 125 GLU B CA  
5288 C C   . GLU B 125 ? 2.3240 1.8945 2.1361 -0.2247 0.0497  -0.1374 125 GLU B C   
5289 O O   . GLU B 125 ? 2.3789 1.9526 2.1539 -0.2300 0.0429  -0.1248 125 GLU B O   
5290 C CB  . GLU B 125 ? 2.3904 1.9529 2.2374 -0.2190 0.0389  -0.1569 125 GLU B CB  
5291 C CG  . GLU B 125 ? 2.4656 2.0414 2.3219 -0.2193 0.0199  -0.1674 125 GLU B CG  
5292 C CD  . GLU B 125 ? 2.5084 2.0662 2.3883 -0.2090 0.0298  -0.1707 125 GLU B CD  
5293 O OE1 . GLU B 125 ? 2.5270 2.0639 2.4254 -0.2023 0.0534  -0.1690 125 GLU B OE1 
5294 O OE2 . GLU B 125 ? 2.5097 2.0741 2.3895 -0.2061 0.0154  -0.1733 125 GLU B OE2 
5295 N N   . ASP B 126 ? 2.2165 1.7787 2.0665 -0.2138 0.0767  -0.1406 126 ASP B N   
5296 C CA  . ASP B 126 ? 2.1636 1.7192 2.0108 -0.2042 0.1018  -0.1260 126 ASP B CA  
5297 C C   . ASP B 126 ? 2.1437 1.7251 1.9938 -0.2100 0.1043  -0.1233 126 ASP B C   
5298 O O   . ASP B 126 ? 2.1358 1.7188 1.9910 -0.2003 0.1284  -0.1106 126 ASP B O   
5299 C CB  . ASP B 126 ? 2.2046 1.7419 1.9984 -0.2006 0.0970  -0.1071 126 ASP B CB  
5300 C CG  . ASP B 126 ? 2.2789 1.7887 2.0602 -0.1991 0.0901  -0.1092 126 ASP B CG  
5301 O OD1 . ASP B 126 ? 2.3378 1.8426 2.1550 -0.1972 0.0917  -0.1227 126 ASP B OD1 
5302 O OD2 . ASP B 126 ? 2.2623 1.7575 1.9988 -0.2002 0.0841  -0.0982 126 ASP B OD2 
5303 N N   . GLY B 127 ? 2.1427 1.7445 1.9890 -0.2241 0.0809  -0.1334 127 GLY B N   
5304 C CA  . GLY B 127 ? 2.0704 1.6948 1.9145 -0.2317 0.0798  -0.1305 127 GLY B CA  
5305 C C   . GLY B 127 ? 1.9919 1.6182 1.7814 -0.2365 0.0634  -0.1118 127 GLY B C   
5306 O O   . GLY B 127 ? 1.9702 1.6147 1.7502 -0.2450 0.0556  -0.1086 127 GLY B O   
5307 N N   . THR B 128 ? 1.8682 1.4766 1.6232 -0.2320 0.0590  -0.1011 128 THR B N   
5308 C CA  . THR B 128 ? 1.7241 1.3370 1.4295 -0.2370 0.0465  -0.0866 128 THR B CA  
5309 C C   . THR B 128 ? 1.6775 1.2916 1.3536 -0.2530 0.0173  -0.0925 128 THR B C   
5310 O O   . THR B 128 ? 1.7043 1.3125 1.3925 -0.2566 0.0062  -0.1048 128 THR B O   
5311 C CB  . THR B 128 ? 1.7138 1.3093 1.3928 -0.2279 0.0541  -0.0766 128 THR B CB  
5312 O OG1 . THR B 128 ? 1.8226 1.3948 1.4880 -0.2332 0.0409  -0.0850 128 THR B OG1 
5313 C CG2 . THR B 128 ? 1.5664 1.1541 1.2766 -0.2085 0.0856  -0.0710 128 THR B CG2 
5314 N N   . VAL B 129 ? 1.5946 1.2185 1.2334 -0.2611 0.0066  -0.0835 129 VAL B N   
5315 C CA  . VAL B 129 ? 1.5942 1.2162 1.2044 -0.2757 -0.0165 -0.0879 129 VAL B CA  
5316 C C   . VAL B 129 ? 1.7642 1.3724 1.3332 -0.2815 -0.0221 -0.0850 129 VAL B C   
5317 O O   . VAL B 129 ? 1.9791 1.5666 1.5449 -0.2759 -0.0152 -0.0863 129 VAL B O   
5318 C CB  . VAL B 129 ? 1.5313 1.1763 1.1372 -0.2846 -0.0245 -0.0847 129 VAL B CB  
5319 C CG1 . VAL B 129 ? 1.5664 1.2057 1.1504 -0.2972 -0.0452 -0.0906 129 VAL B CG1 
5320 C CG2 . VAL B 129 ? 1.4223 1.0810 1.0701 -0.2797 -0.0133 -0.0885 129 VAL B CG2 
5321 N N   . SER B 130 ? 1.6665 1.2861 1.2055 -0.2937 -0.0329 -0.0826 130 SER B N   
5322 C CA  . SER B 130 ? 1.6438 1.2519 1.1462 -0.3035 -0.0375 -0.0853 130 SER B CA  
5323 C C   . SER B 130 ? 1.6503 1.2831 1.1288 -0.3156 -0.0455 -0.0830 130 SER B C   
5324 O O   . SER B 130 ? 1.6475 1.2887 1.1284 -0.3230 -0.0549 -0.0835 130 SER B O   
5325 C CB  . SER B 130 ? 1.6710 1.2510 1.1659 -0.3101 -0.0452 -0.0935 130 SER B CB  
5326 O OG  . SER B 130 ? 1.6525 1.2373 1.1338 -0.3222 -0.0571 -0.0958 130 SER B OG  
5327 N N   . THR B 131 ? 1.5778 1.2246 1.0335 -0.3173 -0.0416 -0.0814 131 THR B N   
5328 C CA  . THR B 131 ? 1.5337 1.2141 0.9703 -0.3268 -0.0481 -0.0793 131 THR B CA  
5329 C C   . THR B 131 ? 1.5509 1.2258 0.9782 -0.3448 -0.0612 -0.0873 131 THR B C   
5330 O O   . THR B 131 ? 1.5122 1.2119 0.9401 -0.3497 -0.0671 -0.0828 131 THR B O   
5331 C CB  . THR B 131 ? 1.4765 1.1735 0.8843 -0.3297 -0.0448 -0.0828 131 THR B CB  
5332 O OG1 . THR B 131 ? 1.5358 1.2287 0.9514 -0.3106 -0.0307 -0.0750 131 THR B OG1 
5333 C CG2 . THR B 131 ? 1.3340 1.0795 0.7288 -0.3335 -0.0500 -0.0780 131 THR B CG2 
5334 N N   . ASP B 132 ? 1.6869 1.3279 1.1066 -0.3526 -0.0632 -0.0972 132 ASP B N   
5335 C CA  . ASP B 132 ? 1.6582 1.2876 1.0702 -0.3657 -0.0713 -0.1029 132 ASP B CA  
5336 C C   . ASP B 132 ? 1.5564 1.1953 0.9902 -0.3597 -0.0778 -0.0953 132 ASP B C   
5337 O O   . ASP B 132 ? 1.4839 1.1401 0.9135 -0.3678 -0.0839 -0.0935 132 ASP B O   
5338 C CB  . ASP B 132 ? 1.7253 1.3141 1.1314 -0.3676 -0.0674 -0.1097 132 ASP B CB  
5339 C CG  . ASP B 132 ? 1.8707 1.4439 1.2588 -0.3727 -0.0571 -0.1176 132 ASP B CG  
5340 O OD1 . ASP B 132 ? 1.9022 1.4698 1.2992 -0.3605 -0.0508 -0.1139 132 ASP B OD1 
5341 O OD2 . ASP B 132 ? 1.9158 1.4811 1.2820 -0.3897 -0.0534 -0.1287 132 ASP B OD2 
5342 N N   . LEU B 133 ? 1.5134 1.1420 0.9716 -0.3461 -0.0756 -0.0924 133 LEU B N   
5343 C CA  . LEU B 133 ? 1.4531 1.0903 0.9337 -0.3412 -0.0805 -0.0893 133 LEU B CA  
5344 C C   . LEU B 133 ? 1.4173 1.0850 0.9124 -0.3383 -0.0765 -0.0806 133 LEU B C   
5345 O O   . LEU B 133 ? 1.3993 1.0780 0.9018 -0.3417 -0.0812 -0.0780 133 LEU B O   
5346 C CB  . LEU B 133 ? 1.3725 0.9966 0.8780 -0.3288 -0.0785 -0.0928 133 LEU B CB  
5347 C CG  . LEU B 133 ? 1.4216 1.0589 0.9535 -0.3241 -0.0827 -0.0945 133 LEU B CG  
5348 C CD1 . LEU B 133 ? 1.4482 1.0850 0.9641 -0.3321 -0.0941 -0.0946 133 LEU B CD1 
5349 C CD2 . LEU B 133 ? 1.5690 1.1991 1.1248 -0.3130 -0.0815 -0.1016 133 LEU B CD2 
5350 N N   . ARG B 134 ? 1.2982 0.9790 0.7967 -0.3305 -0.0657 -0.0745 134 ARG B N   
5351 C CA  . ARG B 134 ? 1.2356 0.9464 0.7458 -0.3245 -0.0575 -0.0624 134 ARG B CA  
5352 C C   . ARG B 134 ? 1.2901 1.0227 0.7803 -0.3369 -0.0665 -0.0587 134 ARG B C   
5353 O O   . ARG B 134 ? 1.1994 0.9469 0.7022 -0.3374 -0.0657 -0.0514 134 ARG B O   
5354 C CB  . ARG B 134 ? 1.2900 1.0117 0.8012 -0.3109 -0.0428 -0.0544 134 ARG B CB  
5355 C CG  . ARG B 134 ? 1.3918 1.0964 0.9329 -0.2959 -0.0279 -0.0552 134 ARG B CG  
5356 C CD  . ARG B 134 ? 1.3754 1.0869 0.9125 -0.2809 -0.0119 -0.0461 134 ARG B CD  
5357 N NE  . ARG B 134 ? 1.2814 1.0288 0.8128 -0.2737 -0.0039 -0.0300 134 ARG B NE  
5358 C CZ  . ARG B 134 ? 1.2316 0.9999 0.7408 -0.2652 0.0013  -0.0214 134 ARG B CZ  
5359 N NH1 . ARG B 134 ? 1.2689 1.0220 0.7591 -0.2650 -0.0003 -0.0290 134 ARG B NH1 
5360 N NH2 . ARG B 134 ? 1.1124 0.9192 0.6176 -0.2561 0.0085  -0.0048 134 ARG B NH2 
5361 N N   . ILE B 135 ? 1.2544 0.9887 0.7153 -0.3479 -0.0733 -0.0652 135 ILE B N   
5362 C CA  . ILE B 135 ? 1.1800 0.9356 0.6227 -0.3622 -0.0819 -0.0662 135 ILE B CA  
5363 C C   . ILE B 135 ? 1.2673 1.0071 0.7131 -0.3719 -0.0905 -0.0695 135 ILE B C   
5364 O O   . ILE B 135 ? 1.3422 1.1013 0.7914 -0.3760 -0.0931 -0.0626 135 ILE B O   
5365 C CB  . ILE B 135 ? 1.2453 1.0010 0.6594 -0.3754 -0.0856 -0.0796 135 ILE B CB  
5366 C CG1 . ILE B 135 ? 1.2188 1.0056 0.6243 -0.3666 -0.0790 -0.0750 135 ILE B CG1 
5367 C CG2 . ILE B 135 ? 1.1938 0.9617 0.5934 -0.3944 -0.0941 -0.0871 135 ILE B CG2 
5368 C CD1 . ILE B 135 ? 1.1120 0.8918 0.4928 -0.3770 -0.0789 -0.0911 135 ILE B CD1 
5369 N N   . ARG B 136 ? 1.2819 0.9874 0.7262 -0.3738 -0.0936 -0.0784 136 ARG B N   
5370 C CA  . ARG B 136 ? 1.4052 1.0952 0.8504 -0.3790 -0.1005 -0.0803 136 ARG B CA  
5371 C C   . ARG B 136 ? 1.3608 1.0647 0.8296 -0.3721 -0.0999 -0.0713 136 ARG B C   
5372 O O   . ARG B 136 ? 1.3071 1.0158 0.7740 -0.3788 -0.1045 -0.0683 136 ARG B O   
5373 C CB  . ARG B 136 ? 1.5744 1.2303 1.0172 -0.3751 -0.1014 -0.0876 136 ARG B CB  
5374 C CG  . ARG B 136 ? 1.5441 1.1790 0.9642 -0.3833 -0.0977 -0.0967 136 ARG B CG  
5375 C CD  . ARG B 136 ? 1.5257 1.1284 0.9463 -0.3751 -0.0955 -0.0995 136 ARG B CD  
5376 N NE  . ARG B 136 ? 1.6252 1.2020 1.0239 -0.3851 -0.0901 -0.1058 136 ARG B NE  
5377 C CZ  . ARG B 136 ? 1.5440 1.1089 0.9355 -0.3878 -0.0913 -0.1048 136 ARG B CZ  
5378 N NH1 . ARG B 136 ? 1.4589 1.0369 0.8614 -0.3818 -0.1002 -0.0982 136 ARG B NH1 
5379 N NH2 . ARG B 136 ? 1.5168 1.0551 0.8905 -0.3963 -0.0807 -0.1106 136 ARG B NH2 
5380 N N   . GLN B 137 ? 1.3800 1.0887 0.8724 -0.3593 -0.0918 -0.0681 137 GLN B N   
5381 C CA  . GLN B 137 ? 1.2914 1.0114 0.8107 -0.3537 -0.0864 -0.0630 137 GLN B CA  
5382 C C   . GLN B 137 ? 1.2337 0.9810 0.7570 -0.3551 -0.0796 -0.0495 137 GLN B C   
5383 O O   . GLN B 137 ? 1.2684 1.0205 0.8014 -0.3585 -0.0794 -0.0458 137 GLN B O   
5384 C CB  . GLN B 137 ? 1.3385 1.0558 0.8864 -0.3409 -0.0753 -0.0661 137 GLN B CB  
5385 C CG  . GLN B 137 ? 1.4166 1.1141 0.9698 -0.3383 -0.0828 -0.0790 137 GLN B CG  
5386 C CD  . GLN B 137 ? 1.3859 1.0820 0.9688 -0.3268 -0.0716 -0.0847 137 GLN B CD  
5387 O OE1 . GLN B 137 ? 1.4008 1.1045 0.9972 -0.3197 -0.0562 -0.0784 137 GLN B OE1 
5388 N NE2 . GLN B 137 ? 1.2615 0.9494 0.8552 -0.3233 -0.0781 -0.0963 137 GLN B NE2 
5389 N N   . SER B 138 ? 1.1050 0.8722 0.6199 -0.3515 -0.0736 -0.0414 138 SER B N   
5390 C CA  . SER B 138 ? 1.0847 0.8836 0.6020 -0.3503 -0.0669 -0.0260 138 SER B CA  
5391 C C   . SER B 138 ? 1.2320 1.0384 0.7298 -0.3657 -0.0800 -0.0269 138 SER B C   
5392 O O   . SER B 138 ? 1.3387 1.1614 0.8447 -0.3671 -0.0765 -0.0158 138 SER B O   
5393 C CB  . SER B 138 ? 1.0403 0.8661 0.5536 -0.3382 -0.0561 -0.0152 138 SER B CB  
5394 O OG  . SER B 138 ? 1.2356 1.0572 0.7242 -0.3432 -0.0652 -0.0260 138 SER B OG  
5395 N N   . GLN B 139 ? 1.2325 1.0248 0.7066 -0.3775 -0.0922 -0.0404 139 GLN B N   
5396 C CA  . GLN B 139 ? 1.2122 1.0044 0.6707 -0.3933 -0.1020 -0.0449 139 GLN B CA  
5397 C C   . GLN B 139 ? 1.2118 0.9821 0.6793 -0.3956 -0.1048 -0.0442 139 GLN B C   
5398 O O   . GLN B 139 ? 1.2150 0.9951 0.6838 -0.4019 -0.1061 -0.0375 139 GLN B O   
5399 C CB  . GLN B 139 ? 1.1697 0.9434 0.6049 -0.4054 -0.1085 -0.0619 139 GLN B CB  
5400 C CG  . GLN B 139 ? 1.1804 0.9786 0.6012 -0.4085 -0.1073 -0.0676 139 GLN B CG  
5401 C CD  . GLN B 139 ? 1.1817 1.0241 0.5962 -0.4169 -0.1103 -0.0647 139 GLN B CD  
5402 O OE1 . GLN B 139 ? 1.1362 0.9863 0.5564 -0.4224 -0.1131 -0.0587 139 GLN B OE1 
5403 N NE2 . GLN B 139 ? 1.1855 1.0600 0.5882 -0.4174 -0.1099 -0.0693 139 GLN B NE2 
5404 N N   . HIS B 140 ? 1.0398 0.7826 0.5132 -0.3900 -0.1059 -0.0515 140 HIS B N   
5405 C CA  . HIS B 140 ? 1.0982 0.8232 0.5768 -0.3905 -0.1098 -0.0531 140 HIS B CA  
5406 C C   . HIS B 140 ? 1.2488 0.9908 0.7494 -0.3875 -0.1023 -0.0425 140 HIS B C   
5407 O O   . HIS B 140 ? 1.1691 0.9075 0.6677 -0.3935 -0.1050 -0.0393 140 HIS B O   
5408 C CB  . HIS B 140 ? 1.2064 0.9099 0.6901 -0.3818 -0.1121 -0.0626 140 HIS B CB  
5409 C CG  . HIS B 140 ? 1.4204 1.1107 0.9050 -0.3804 -0.1178 -0.0658 140 HIS B CG  
5410 N ND1 . HIS B 140 ? 1.5008 1.1919 0.9806 -0.3872 -0.1198 -0.0605 140 HIS B ND1 
5411 C CD2 . HIS B 140 ? 1.5771 1.2565 1.0662 -0.3716 -0.1220 -0.0734 140 HIS B CD2 
5412 C CE1 . HIS B 140 ? 1.5899 1.2696 1.0693 -0.3823 -0.1247 -0.0649 140 HIS B CE1 
5413 N NE2 . HIS B 140 ? 1.6574 1.3328 1.1423 -0.3725 -0.1268 -0.0729 140 HIS B NE2 
5414 N N   . SER B 141 ? 1.2869 1.0449 0.8090 -0.3778 -0.0899 -0.0366 141 SER B N   
5415 C CA  . SER B 141 ? 1.1809 0.9530 0.7277 -0.3742 -0.0761 -0.0264 141 SER B CA  
5416 C C   . SER B 141 ? 1.2147 1.0080 0.7554 -0.3793 -0.0733 -0.0109 141 SER B C   
5417 O O   . SER B 141 ? 1.2293 1.0208 0.7744 -0.3851 -0.0721 -0.0060 141 SER B O   
5418 C CB  . SER B 141 ? 1.3421 1.1245 0.9141 -0.3612 -0.0580 -0.0227 141 SER B CB  
5419 O OG  . SER B 141 ? 1.6243 1.3898 1.2091 -0.3572 -0.0591 -0.0382 141 SER B OG  
5420 N N   . SER B 142 ? 1.1556 0.9717 0.6860 -0.3767 -0.0721 -0.0034 142 SER B N   
5421 C CA  . SER B 142 ? 1.1034 0.9497 0.6297 -0.3793 -0.0695 0.0120  142 SER B CA  
5422 C C   . SER B 142 ? 1.1917 1.0285 0.7053 -0.3945 -0.0815 0.0087  142 SER B C   
5423 O O   . SER B 142 ? 1.1950 1.0434 0.7176 -0.3963 -0.0752 0.0219  142 SER B O   
5424 C CB  . SER B 142 ? 1.0776 0.9534 0.5883 -0.3761 -0.0724 0.0141  142 SER B CB  
5425 O OG  . SER B 142 ? 1.2966 1.2111 0.8051 -0.3764 -0.0702 0.0293  142 SER B OG  
5426 N N   . LEU B 143 ? 1.0666 0.8800 0.5604 -0.4045 -0.0958 -0.0078 143 LEU B N   
5427 C CA  . LEU B 143 ? 1.1864 0.9890 0.6670 -0.4181 -0.1045 -0.0116 143 LEU B CA  
5428 C C   . LEU B 143 ? 1.1367 0.9137 0.6245 -0.4187 -0.1034 -0.0099 143 LEU B C   
5429 O O   . LEU B 143 ? 1.0016 0.7779 0.4877 -0.4262 -0.1038 -0.0038 143 LEU B O   
5430 C CB  . LEU B 143 ? 1.2743 1.0575 0.7327 -0.4274 -0.1141 -0.0294 143 LEU B CB  
5431 C CG  . LEU B 143 ? 1.3242 1.1353 0.7717 -0.4326 -0.1160 -0.0353 143 LEU B CG  
5432 C CD1 . LEU B 143 ? 1.3059 1.0905 0.7353 -0.4414 -0.1200 -0.0548 143 LEU B CD1 
5433 C CD2 . LEU B 143 ? 1.3879 1.2351 0.8351 -0.4419 -0.1172 -0.0294 143 LEU B CD2 
5434 N N   . SER B 144 ? 1.0744 0.8329 0.5706 -0.4109 -0.1021 -0.0165 144 SER B N   
5435 C CA  . SER B 144 ? 1.1714 0.9130 0.6752 -0.4105 -0.1008 -0.0172 144 SER B CA  
5436 C C   . SER B 144 ? 1.1106 0.8699 0.6336 -0.4111 -0.0875 -0.0018 144 SER B C   
5437 O O   . SER B 144 ? 1.0768 0.8265 0.5984 -0.4169 -0.0871 0.0023  144 SER B O   
5438 C CB  . SER B 144 ? 1.1709 0.9022 0.6856 -0.4016 -0.1006 -0.0286 144 SER B CB  
5439 O OG  . SER B 144 ? 1.2200 0.9344 0.7168 -0.3996 -0.1112 -0.0398 144 SER B OG  
5440 N N   . ARG B 145 ? 1.0374 0.8211 0.5780 -0.4038 -0.0741 0.0083  145 ARG B N   
5441 C CA  . ARG B 145 ? 1.0132 0.8148 0.5730 -0.4020 -0.0565 0.0265  145 ARG B CA  
5442 C C   . ARG B 145 ? 0.9822 0.7976 0.5292 -0.4099 -0.0617 0.0384  145 ARG B C   
5443 O O   . ARG B 145 ? 1.1705 0.9788 0.7214 -0.4157 -0.0574 0.0459  145 ARG B O   
5444 C CB  . ARG B 145 ? 1.1185 0.9436 0.6995 -0.3887 -0.0368 0.0377  145 ARG B CB  
5445 C CG  . ARG B 145 ? 1.0752 0.8871 0.6801 -0.3820 -0.0240 0.0265  145 ARG B CG  
5446 C CD  . ARG B 145 ? 1.5178 1.3487 1.1489 -0.3675 0.0039  0.0404  145 ARG B CD  
5447 N NE  . ARG B 145 ? 1.6833 1.5299 1.3031 -0.3574 0.0003  0.0441  145 ARG B NE  
5448 C CZ  . ARG B 145 ? 1.7880 1.6223 1.4020 -0.3551 -0.0096 0.0278  145 ARG B CZ  
5449 N NH1 . ARG B 145 ? 1.7360 1.5456 1.3550 -0.3609 -0.0180 0.0073  145 ARG B NH1 
5450 N NH2 . ARG B 145 ? 1.7560 1.6049 1.3584 -0.3461 -0.0111 0.0323  145 ARG B NH2 
5451 N N   . LYS B 146 ? 0.9990 0.8353 0.5314 -0.4110 -0.0705 0.0384  146 LYS B N   
5452 C CA  . LYS B 146 ? 1.0643 0.9199 0.5864 -0.4202 -0.0766 0.0454  146 LYS B CA  
5453 C C   . LYS B 146 ? 1.1538 0.9773 0.6666 -0.4324 -0.0844 0.0383  146 LYS B C   
5454 O O   . LYS B 146 ? 1.2436 1.0741 0.7608 -0.4377 -0.0805 0.0501  146 LYS B O   
5455 C CB  . LYS B 146 ? 1.1731 1.0519 0.6782 -0.4238 -0.0881 0.0360  146 LYS B CB  
5456 C CG  . LYS B 146 ? 1.5258 1.4390 1.0257 -0.4329 -0.0929 0.0412  146 LYS B CG  
5457 C CD  . LYS B 146 ? 1.8034 1.7616 1.3195 -0.4214 -0.0796 0.0674  146 LYS B CD  
5458 C CE  . LYS B 146 ? 1.9124 1.8620 1.4408 -0.4255 -0.0716 0.0825  146 LYS B CE  
5459 N NZ  . LYS B 146 ? 1.9445 1.9326 1.4917 -0.4111 -0.0529 0.1118  146 LYS B NZ  
5460 N N   . PHE B 147 ? 1.0891 0.8774 0.5894 -0.4347 -0.0936 0.0210  147 PHE B N   
5461 C CA  . PHE B 147 ? 1.1504 0.9055 0.6394 -0.4421 -0.0989 0.0152  147 PHE B CA  
5462 C C   . PHE B 147 ? 1.2430 0.9864 0.7442 -0.4409 -0.0899 0.0250  147 PHE B C   
5463 O O   . PHE B 147 ? 1.2428 0.9784 0.7409 -0.4481 -0.0887 0.0319  147 PHE B O   
5464 C CB  . PHE B 147 ? 1.1332 0.8568 0.6055 -0.4401 -0.1081 -0.0023 147 PHE B CB  
5465 C CG  . PHE B 147 ? 1.1960 0.8862 0.6535 -0.4440 -0.1114 -0.0064 147 PHE B CG  
5466 C CD1 . PHE B 147 ? 1.2705 0.9573 0.7212 -0.4548 -0.1109 -0.0038 147 PHE B CD1 
5467 C CD2 . PHE B 147 ? 1.1546 0.8194 0.6056 -0.4357 -0.1140 -0.0128 147 PHE B CD2 
5468 C CE1 . PHE B 147 ? 1.2305 0.8830 0.6679 -0.4565 -0.1106 -0.0062 147 PHE B CE1 
5469 C CE2 . PHE B 147 ? 1.0906 0.7255 0.5257 -0.4356 -0.1153 -0.0140 147 PHE B CE2 
5470 C CZ  . PHE B 147 ? 1.1935 0.8193 0.6216 -0.4456 -0.1124 -0.0101 147 PHE B CZ  
5471 N N   . VAL B 148 ? 1.2415 0.9834 0.7580 -0.4330 -0.0821 0.0238  148 VAL B N   
5472 C CA  . VAL B 148 ? 1.1709 0.9034 0.7012 -0.4335 -0.0706 0.0292  148 VAL B CA  
5473 C C   . VAL B 148 ? 1.2233 0.9748 0.7678 -0.4366 -0.0560 0.0508  148 VAL B C   
5474 O O   . VAL B 148 ? 1.2234 0.9616 0.7700 -0.4420 -0.0498 0.0577  148 VAL B O   
5475 C CB  . VAL B 148 ? 1.0409 0.7754 0.5915 -0.4263 -0.0611 0.0201  148 VAL B CB  
5476 C CG1 . VAL B 148 ? 0.9554 0.6864 0.5260 -0.4292 -0.0433 0.0246  148 VAL B CG1 
5477 C CG2 . VAL B 148 ? 1.0250 0.7425 0.5624 -0.4224 -0.0760 -0.0005 148 VAL B CG2 
5478 N N   . LYS B 149 ? 1.1490 0.9329 0.7020 -0.4318 -0.0500 0.0626  149 LYS B N   
5479 C CA  . LYS B 149 ? 1.1375 0.9470 0.7046 -0.4309 -0.0349 0.0863  149 LYS B CA  
5480 C C   . LYS B 149 ? 1.2595 1.0704 0.8133 -0.4413 -0.0450 0.0914  149 LYS B C   
5481 O O   . LYS B 149 ? 1.3638 1.1774 0.9275 -0.4439 -0.0336 0.1078  149 LYS B O   
5482 C CB  . LYS B 149 ? 1.2594 1.1087 0.8370 -0.4189 -0.0254 0.0990  149 LYS B CB  
5483 C CG  . LYS B 149 ? 1.4610 1.3448 1.0522 -0.4137 -0.0091 0.1271  149 LYS B CG  
5484 C CD  . LYS B 149 ? 1.6351 1.5638 1.2311 -0.3983 -0.0018 0.1403  149 LYS B CD  
5485 C CE  . LYS B 149 ? 1.7020 1.6267 1.3191 -0.3835 0.0222  0.1450  149 LYS B CE  
5486 N NZ  . LYS B 149 ? 1.6587 1.5608 1.2694 -0.3839 0.0112  0.1201  149 LYS B NZ  
5487 N N   . VAL B 150 ? 1.3847 1.1926 0.9182 -0.4477 -0.0637 0.0765  150 VAL B N   
5488 C CA  . VAL B 150 ? 1.3890 1.1959 0.9124 -0.4593 -0.0716 0.0763  150 VAL B CA  
5489 C C   . VAL B 150 ? 1.2438 1.0073 0.7609 -0.4650 -0.0709 0.0735  150 VAL B C   
5490 O O   . VAL B 150 ? 1.2721 1.0334 0.7932 -0.4712 -0.0659 0.0848  150 VAL B O   
5491 C CB  . VAL B 150 ? 1.1874 0.9972 0.6927 -0.4669 -0.0873 0.0567  150 VAL B CB  
5492 C CG1 . VAL B 150 ? 1.2227 1.0287 0.7230 -0.4803 -0.0911 0.0540  150 VAL B CG1 
5493 C CG2 . VAL B 150 ? 1.2776 1.1346 0.7860 -0.4622 -0.0893 0.0580  150 VAL B CG2 
5494 N N   . MET B 151 ? 1.1903 0.9212 0.6971 -0.4617 -0.0757 0.0590  151 MET B N   
5495 C CA  . MET B 151 ? 1.2598 0.9517 0.7566 -0.4641 -0.0758 0.0557  151 MET B CA  
5496 C C   . MET B 151 ? 1.3355 1.0258 0.8487 -0.4637 -0.0605 0.0701  151 MET B C   
5497 O O   . MET B 151 ? 1.4349 1.0999 0.9423 -0.4678 -0.0574 0.0735  151 MET B O   
5498 C CB  . MET B 151 ? 1.1806 0.8469 0.6626 -0.4573 -0.0844 0.0380  151 MET B CB  
5499 C CG  . MET B 151 ? 1.3021 0.9601 0.7660 -0.4582 -0.0956 0.0246  151 MET B CG  
5500 S SD  . MET B 151 ? 1.5729 1.2200 1.0270 -0.4707 -0.0957 0.0254  151 MET B SD  
5501 C CE  . MET B 151 ? 1.1678 0.7631 0.6015 -0.4652 -0.0945 0.0216  151 MET B CE  
5502 N N   . THR B 152 ? 1.3032 1.0190 0.8376 -0.4585 -0.0478 0.0791  152 THR B N   
5503 C CA  . THR B 152 ? 1.3475 1.0610 0.9011 -0.4587 -0.0276 0.0923  152 THR B CA  
5504 C C   . THR B 152 ? 1.3512 1.0750 0.9106 -0.4640 -0.0196 0.1137  152 THR B C   
5505 O O   . THR B 152 ? 1.3639 1.0711 0.9300 -0.4680 -0.0065 0.1237  152 THR B O   
5506 C CB  . THR B 152 ? 1.3325 1.0687 0.9107 -0.4506 -0.0101 0.0968  152 THR B CB  
5507 O OG1 . THR B 152 ? 1.4185 1.1434 0.9942 -0.4470 -0.0168 0.0747  152 THR B OG1 
5508 C CG2 . THR B 152 ? 1.2442 0.9783 0.8458 -0.4519 0.0173  0.1123  152 THR B CG2 
5509 N N   . ARG B 153 ? 1.3579 1.1113 0.9151 -0.4643 -0.0275 0.1195  153 ARG B N   
5510 C CA  . ARG B 153 ? 1.3764 1.1471 0.9399 -0.4694 -0.0228 0.1379  153 ARG B CA  
5511 C C   . ARG B 153 ? 1.4141 1.1460 0.9623 -0.4797 -0.0305 0.1305  153 ARG B C   
5512 O O   . ARG B 153 ? 1.3888 1.1113 0.9443 -0.4840 -0.0196 0.1455  153 ARG B O   
5513 C CB  . ARG B 153 ? 1.3521 1.1695 0.9154 -0.4683 -0.0324 0.1400  153 ARG B CB  
5514 C CG  . ARG B 153 ? 1.5532 1.3972 1.1246 -0.4738 -0.0300 0.1562  153 ARG B CG  
5515 C CD  . ARG B 153 ? 1.7082 1.5545 1.2998 -0.4690 -0.0063 0.1843  153 ARG B CD  
5516 N NE  . ARG B 153 ? 1.7997 1.6728 1.4003 -0.4736 -0.0042 0.2010  153 ARG B NE  
5517 C CZ  . ARG B 153 ? 1.8024 1.6647 1.4165 -0.4745 0.0136  0.2228  153 ARG B CZ  
5518 N NH1 . ARG B 153 ? 1.7794 1.6037 1.3991 -0.4726 0.0318  0.2287  153 ARG B NH1 
5519 N NH2 . ARG B 153 ? 1.7766 1.6677 1.4000 -0.4783 0.0140  0.2372  153 ARG B NH2 
5520 N N   . TYR B 154 ? 1.4465 1.1539 0.9736 -0.4821 -0.0465 0.1086  154 TYR B N   
5521 C CA  . TYR B 154 ? 1.4795 1.1449 0.9897 -0.4880 -0.0511 0.1008  154 TYR B CA  
5522 C C   . TYR B 154 ? 1.4983 1.1307 1.0073 -0.4857 -0.0409 0.1055  154 TYR B C   
5523 O O   . TYR B 154 ? 1.4782 1.0921 0.9883 -0.4907 -0.0327 0.1164  154 TYR B O   
5524 C CB  . TYR B 154 ? 1.4469 1.0927 0.9357 -0.4866 -0.0653 0.0784  154 TYR B CB  
5525 C CG  . TYR B 154 ? 1.4295 1.0328 0.9001 -0.4899 -0.0670 0.0710  154 TYR B CG  
5526 C CD1 . TYR B 154 ? 1.4370 1.0376 0.9120 -0.4999 -0.0629 0.0762  154 TYR B CD1 
5527 C CD2 . TYR B 154 ? 1.5032 1.0711 0.9531 -0.4813 -0.0712 0.0591  154 TYR B CD2 
5528 C CE1 . TYR B 154 ? 1.5448 1.1025 1.0048 -0.5017 -0.0603 0.0695  154 TYR B CE1 
5529 C CE2 . TYR B 154 ? 1.5936 1.1213 1.0258 -0.4805 -0.0689 0.0548  154 TYR B CE2 
5530 C CZ  . TYR B 154 ? 1.6149 1.1347 1.0525 -0.4909 -0.0623 0.0599  154 TYR B CZ  
5531 O OH  . TYR B 154 ? 1.5591 1.0350 0.9808 -0.4888 -0.0560 0.0560  154 TYR B OH  
5532 N N   . ASN B 155 ? 1.5392 1.1664 1.0470 -0.4788 -0.0408 0.0958  155 ASN B N   
5533 C CA  . ASN B 155 ? 1.4918 1.0954 0.9999 -0.4777 -0.0309 0.0954  155 ASN B CA  
5534 C C   . ASN B 155 ? 1.5118 1.1198 1.0400 -0.4832 -0.0102 0.1167  155 ASN B C   
5535 O O   . ASN B 155 ? 1.4684 1.0488 0.9923 -0.4864 -0.0017 0.1196  155 ASN B O   
5536 C CB  . ASN B 155 ? 1.4019 1.0149 0.9160 -0.4712 -0.0308 0.0810  155 ASN B CB  
5537 C CG  . ASN B 155 ? 1.4084 1.0040 0.9247 -0.4721 -0.0205 0.0750  155 ASN B CG  
5538 O OD1 . ASN B 155 ? 1.4959 1.0988 1.0347 -0.4765 0.0002  0.0845  155 ASN B OD1 
5539 N ND2 . ASN B 155 ? 1.3818 0.9564 0.8750 -0.4670 -0.0330 0.0587  155 ASN B ND2 
5540 N N   . ASP B 156 ? 1.5339 1.1774 1.0834 -0.4828 -0.0007 0.1329  156 ASP B N   
5541 C CA  . ASP B 156 ? 1.5829 1.2344 1.1543 -0.4852 0.0229  0.1569  156 ASP B CA  
5542 C C   . ASP B 156 ? 1.7425 1.3832 1.3101 -0.4922 0.0230  0.1710  156 ASP B C   
5543 O O   . ASP B 156 ? 1.8048 1.4262 1.3797 -0.4962 0.0400  0.1841  156 ASP B O   
5544 C CB  . ASP B 156 ? 1.6488 1.3447 1.2440 -0.4779 0.0362  0.1730  156 ASP B CB  
5545 C CG  . ASP B 156 ? 1.8232 1.5201 1.4367 -0.4730 0.0562  0.1696  156 ASP B CG  
5546 O OD1 . ASP B 156 ? 1.7749 1.4421 1.3847 -0.4775 0.0598  0.1540  156 ASP B OD1 
5547 O OD2 . ASP B 156 ? 1.9345 1.6638 1.5668 -0.4640 0.0699  0.1817  156 ASP B OD2 
5548 N N   . VAL B 157 ? 1.7609 1.4131 1.3187 -0.4947 0.0059  0.1665  157 VAL B N   
5549 C CA  . VAL B 157 ? 1.6634 1.3069 1.2205 -0.5024 0.0058  0.1761  157 VAL B CA  
5550 C C   . VAL B 157 ? 1.7011 1.2891 1.2376 -0.5061 0.0036  0.1664  157 VAL B C   
5551 O O   . VAL B 157 ? 1.7507 1.3195 1.2902 -0.5115 0.0126  0.1788  157 VAL B O   
5552 C CB  . VAL B 157 ? 1.6239 1.3006 1.1805 -0.5062 -0.0094 0.1700  157 VAL B CB  
5553 C CG1 . VAL B 157 ? 1.7119 1.3782 1.2485 -0.5052 -0.0272 0.1435  157 VAL B CG1 
5554 C CG2 . VAL B 157 ? 1.6580 1.3234 1.2166 -0.5160 -0.0085 0.1751  157 VAL B CG2 
5555 N N   . GLN B 158 ? 1.6985 1.2623 1.2141 -0.5013 -0.0073 0.1457  158 GLN B N   
5556 C CA  . GLN B 158 ? 1.6967 1.2113 1.1898 -0.4998 -0.0081 0.1379  158 GLN B CA  
5557 C C   . GLN B 158 ? 1.7115 1.2065 1.2087 -0.5006 0.0084  0.1472  158 GLN B C   
5558 O O   . GLN B 158 ? 1.8522 1.3189 1.3460 -0.5045 0.0177  0.1576  158 GLN B O   
5559 C CB  . GLN B 158 ? 1.6044 1.1051 1.0741 -0.4911 -0.0230 0.1156  158 GLN B CB  
5560 C CG  . GLN B 158 ? 1.6200 1.1253 1.0811 -0.4915 -0.0356 0.1044  158 GLN B CG  
5561 C CD  . GLN B 158 ? 1.6147 1.0908 1.0685 -0.4967 -0.0320 0.1065  158 GLN B CD  
5562 O OE1 . GLN B 158 ? 1.6315 1.0705 1.0634 -0.4901 -0.0332 0.0974  158 GLN B OE1 
5563 N NE2 . GLN B 158 ? 1.5239 1.0184 0.9976 -0.5072 -0.0256 0.1191  158 GLN B NE2 
5564 N N   . ALA B 159 ? 1.6814 1.1909 1.1875 -0.4977 0.0140  0.1419  159 ALA B N   
5565 C CA  . ALA B 159 ? 1.7063 1.2013 1.2206 -0.5011 0.0334  0.1472  159 ALA B CA  
5566 C C   . ALA B 159 ? 1.7687 1.2695 1.3064 -0.5078 0.0551  0.1740  159 ALA B C   
5567 O O   . ALA B 159 ? 1.7574 1.2402 1.2933 -0.5041 0.0664  0.1751  159 ALA B O   
5568 C CB  . ALA B 159 ? 1.5949 1.1101 1.1215 -0.4987 0.0387  0.1339  159 ALA B CB  
5569 N N   . GLU B 160 ? 1.8882 1.4260 1.4454 -0.5075 0.0570  0.1887  160 GLU B N   
5570 C CA  . GLU B 160 ? 2.0098 1.5706 1.5891 -0.5019 0.0718  0.2093  160 GLU B CA  
5571 C C   . GLU B 160 ? 2.0437 1.5812 1.6132 -0.5018 0.0676  0.2122  160 GLU B C   
5572 O O   . GLU B 160 ? 2.0485 1.5814 1.6290 -0.4957 0.0823  0.2209  160 GLU B O   
5573 C CB  . GLU B 160 ? 2.1523 1.7599 1.7488 -0.5029 0.0707  0.2260  160 GLU B CB  
5574 C CG  . GLU B 160 ? 2.2936 1.9327 1.9136 -0.4968 0.0838  0.2510  160 GLU B CG  
5575 C CD  . GLU B 160 ? 2.4352 2.1283 2.0697 -0.4966 0.0847  0.2697  160 GLU B CD  
5576 O OE1 . GLU B 160 ? 2.4594 2.1834 2.1060 -0.4967 0.0864  0.2890  160 GLU B OE1 
5577 O OE2 . GLU B 160 ? 2.4745 2.1861 2.1081 -0.4909 0.0807  0.2603  160 GLU B OE2 
5578 N N   . ASN B 161 ? 2.0481 1.5688 1.5987 -0.5086 0.0500  0.2043  161 ASN B N   
5579 C CA  . ASN B 161 ? 2.0498 1.5448 1.5916 -0.5089 0.0475  0.2051  161 ASN B CA  
5580 C C   . ASN B 161 ? 2.0529 1.4999 1.5710 -0.5027 0.0502  0.1937  161 ASN B C   
5581 O O   . ASN B 161 ? 2.1018 1.5300 1.6190 -0.4983 0.0574  0.1984  161 ASN B O   
5582 C CB  . ASN B 161 ? 1.9937 1.4872 1.5284 -0.5194 0.0332  0.1996  161 ASN B CB  
5583 C CG  . ASN B 161 ? 1.9118 1.4496 1.4717 -0.5278 0.0347  0.2152  161 ASN B CG  
5584 O OD1 . ASN B 161 ? 1.9549 1.5311 1.5192 -0.5293 0.0225  0.2071  161 ASN B OD1 
5585 N ND2 . ASN B 161 ? 1.7863 1.3311 1.3618 -0.5238 0.0449  0.2293  161 ASN B ND2 
5586 N N   . LYS B 162 ? 1.9427 1.3716 1.4420 -0.5025 0.0450  0.1796  162 LYS B N   
5587 C CA  . LYS B 162 ? 1.9206 1.3077 1.3948 -0.4975 0.0473  0.1702  162 LYS B CA  
5588 C C   . LYS B 162 ? 1.9809 1.3677 1.4651 -0.4940 0.0658  0.1735  162 LYS B C   
5589 O O   . LYS B 162 ? 1.9409 1.2951 1.4076 -0.4900 0.0714  0.1703  162 LYS B O   
5590 C CB  . LYS B 162 ? 1.8794 1.2531 1.3342 -0.4997 0.0372  0.1558  162 LYS B CB  
5591 C CG  . LYS B 162 ? 1.8559 1.1932 1.2848 -0.4953 0.0402  0.1475  162 LYS B CG  
5592 C CD  . LYS B 162 ? 1.9165 1.2749 1.3388 -0.4892 0.0313  0.1257  162 LYS B CD  
5593 C CE  . LYS B 162 ? 2.0045 1.3469 1.4147 -0.4891 0.0408  0.1171  162 LYS B CE  
5594 N NZ  . LYS B 162 ? 2.0302 1.4058 1.4512 -0.4902 0.0395  0.0963  162 LYS B NZ  
5595 N N   . ARG B 163 ? 2.0867 1.5082 1.5991 -0.4952 0.0777  0.1800  163 ARG B N   
5596 C CA  . ARG B 163 ? 2.1544 1.5765 1.6820 -0.4923 0.1005  0.1830  163 ARG B CA  
5597 C C   . ARG B 163 ? 2.2331 1.6512 1.7714 -0.4861 0.1095  0.1977  163 ARG B C   
5598 O O   . ARG B 163 ? 2.2825 1.6776 1.8168 -0.4832 0.1234  0.1963  163 ARG B O   
5599 C CB  . ARG B 163 ? 2.1219 1.5799 1.6796 -0.4931 0.1153  0.1870  163 ARG B CB  
5600 C CG  . ARG B 163 ? 2.1590 1.6186 1.7391 -0.4895 0.1449  0.1916  163 ARG B CG  
5601 C CD  . ARG B 163 ? 2.2249 1.7087 1.8302 -0.4911 0.1635  0.1884  163 ARG B CD  
5602 N NE  . ARG B 163 ? 2.2182 1.7339 1.8328 -0.4903 0.1517  0.1951  163 ARG B NE  
5603 C CZ  . ARG B 163 ? 2.1998 1.7466 1.8335 -0.4829 0.1530  0.2171  163 ARG B CZ  
5604 N NH1 . ARG B 163 ? 2.2448 1.7961 1.8932 -0.4752 0.1647  0.2352  163 ARG B NH1 
5605 N NH2 . ARG B 163 ? 2.0904 1.6655 1.7285 -0.4835 0.1427  0.2217  163 ARG B NH2 
5606 N N   . ARG B 164 ? 2.2223 1.6636 1.7749 -0.4856 0.1020  0.2114  164 ARG B N   
5607 C CA  . ARG B 164 ? 2.2702 1.7118 1.8365 -0.4813 0.1090  0.2259  164 ARG B CA  
5608 C C   . ARG B 164 ? 2.3617 1.7684 1.9046 -0.4821 0.0972  0.2196  164 ARG B C   
5609 O O   . ARG B 164 ? 2.3907 1.7879 1.9414 -0.4787 0.1041  0.2280  164 ARG B O   
5610 C CB  . ARG B 164 ? 2.2115 1.7007 1.8088 -0.4819 0.1098  0.2459  164 ARG B CB  
5611 C CG  . ARG B 164 ? 2.1982 1.7068 1.7895 -0.4910 0.0897  0.2437  164 ARG B CG  
5612 C CD  . ARG B 164 ? 2.2032 1.7542 1.8202 -0.4943 0.0896  0.2642  164 ARG B CD  
5613 N NE  . ARG B 164 ? 2.2118 1.8034 1.8589 -0.4859 0.1071  0.2855  164 ARG B NE  
5614 C CZ  . ARG B 164 ? 2.1388 1.7750 1.7990 -0.4859 0.1076  0.2967  164 ARG B CZ  
5615 N NH1 . ARG B 164 ? 2.0341 1.7042 1.7223 -0.4742 0.1280  0.3186  164 ARG B NH1 
5616 N NH2 . ARG B 164 ? 2.1111 1.7575 1.7570 -0.4964 0.0903  0.2869  164 ARG B NH2 
5617 N N   . TYR B 165 ? 2.3499 1.7362 1.8659 -0.4856 0.0818  0.2055  165 TYR B N   
5618 C CA  . TYR B 165 ? 2.2574 1.6041 1.7492 -0.4838 0.0750  0.1988  165 TYR B CA  
5619 C C   . TYR B 165 ? 2.1436 1.4496 1.6112 -0.4764 0.0836  0.1919  165 TYR B C   
5620 O O   . TYR B 165 ? 1.9713 1.2384 1.4127 -0.4716 0.0807  0.1862  165 TYR B O   
5621 C CB  . TYR B 165 ? 2.2813 1.6203 1.7548 -0.4885 0.0590  0.1879  165 TYR B CB  
5622 C CG  . TYR B 165 ? 2.3130 1.6466 1.7891 -0.4937 0.0533  0.1878  165 TYR B CG  
5623 C CD1 . TYR B 165 ? 2.3046 1.6791 1.8084 -0.5041 0.0505  0.1959  165 TYR B CD1 
5624 C CD2 . TYR B 165 ? 2.3988 1.6868 1.8506 -0.4891 0.0530  0.1794  165 TYR B CD2 
5625 C CE1 . TYR B 165 ? 2.3925 1.7636 1.9017 -0.5135 0.0473  0.1924  165 TYR B CE1 
5626 C CE2 . TYR B 165 ? 2.5256 1.8061 1.9835 -0.4957 0.0524  0.1763  165 TYR B CE2 
5627 C CZ  . TYR B 165 ? 2.5615 1.8841 2.0490 -0.5098 0.0492  0.1810  165 TYR B CZ  
5628 O OH  . TYR B 165 ? 2.6923 2.0088 2.1891 -0.5207 0.0504  0.1743  165 TYR B OH  
5629 N N   . GLY B 166 ? 2.2102 1.5250 1.6867 -0.4756 0.0967  0.1928  166 GLY B N   
5630 C CA  . GLY B 166 ? 2.2483 1.5292 1.7046 -0.4717 0.1078  0.1865  166 GLY B CA  
5631 C C   . GLY B 166 ? 2.3009 1.5905 1.7816 -0.4692 0.1287  0.1957  166 GLY B C   
5632 O O   . GLY B 166 ? 2.3702 1.6300 1.8396 -0.4647 0.1400  0.1954  166 GLY B O   
5633 N N   . GLU B 167 ? 2.3609 1.6902 1.8752 -0.4711 0.1357  0.2053  167 GLU B N   
5634 C CA  . GLU B 167 ? 2.4991 1.8390 2.0416 -0.4668 0.1587  0.2173  167 GLU B CA  
5635 C C   . GLU B 167 ? 2.6060 1.9454 2.1628 -0.4613 0.1600  0.2323  167 GLU B C   
5636 O O   . GLU B 167 ? 2.6067 1.9173 2.1570 -0.4565 0.1712  0.2328  167 GLU B O   
5637 C CB  . GLU B 167 ? 2.5118 1.8940 2.0871 -0.4676 0.1687  0.2261  167 GLU B CB  
5638 C CG  . GLU B 167 ? 2.5853 1.9680 2.1568 -0.4733 0.1781  0.2115  167 GLU B CG  
5639 C CD  . GLU B 167 ? 2.5917 2.0138 2.1979 -0.4715 0.1921  0.2216  167 GLU B CD  
5640 O OE1 . GLU B 167 ? 2.5927 2.0445 2.2226 -0.4653 0.1912  0.2419  167 GLU B OE1 
5641 O OE2 . GLU B 167 ? 2.5540 1.9782 2.1646 -0.4763 0.2055  0.2098  167 GLU B OE2 
5642 N N   . ASN B 168 ? 2.5530 2.5001 2.3482 -0.6478 0.1006  0.2548  168 ASN B N   
5643 C CA  . ASN B 168 ? 2.5738 2.5637 2.3428 -0.6798 0.0972  0.2714  168 ASN B CA  
5644 C C   . ASN B 168 ? 2.5471 2.4917 2.2331 -0.7078 0.0953  0.2530  168 ASN B C   
5645 O O   . ASN B 168 ? 2.5762 2.5496 2.2240 -0.7427 0.0947  0.2626  168 ASN B O   
5646 C CB  . ASN B 168 ? 2.5905 2.6375 2.3651 -0.6988 0.1008  0.2968  168 ASN B CB  
5647 C CG  . ASN B 168 ? 2.5117 2.6139 2.3685 -0.6745 0.1037  0.3220  168 ASN B CG  
5648 O OD1 . ASN B 168 ? 2.4841 2.5849 2.3953 -0.6461 0.1029  0.3207  168 ASN B OD1 
5649 N ND2 . ASN B 168 ? 2.4605 2.6109 2.3254 -0.6855 0.1080  0.3450  168 ASN B ND2 
5650 N N   . VAL B 169 ? 2.4659 2.3408 2.1233 -0.6928 0.0955  0.2264  169 VAL B N   
5651 C CA  . VAL B 169 ? 2.5030 2.3271 2.0820 -0.7159 0.0956  0.2091  169 VAL B CA  
5652 C C   . VAL B 169 ? 2.5088 2.2816 2.0824 -0.6912 0.0933  0.1883  169 VAL B C   
5653 O O   . VAL B 169 ? 2.5866 2.3527 2.1321 -0.7048 0.0907  0.1855  169 VAL B O   
5654 C CB  . VAL B 169 ? 2.4980 2.2728 2.0060 -0.7359 0.1022  0.1960  169 VAL B CB  
5655 C CG1 . VAL B 169 ? 2.4925 2.1975 1.9220 -0.7508 0.1047  0.1746  169 VAL B CG1 
5656 C CG2 . VAL B 169 ? 2.4681 2.2955 1.9629 -0.7710 0.1040  0.2147  169 VAL B CG2 
5657 N N   . ALA B 170 ? 2.4060 2.1457 2.0056 -0.6552 0.0945  0.1733  170 ALA B N   
5658 C CA  . ALA B 170 ? 2.3463 2.0409 1.9408 -0.6288 0.0924  0.1524  170 ALA B CA  
5659 C C   . ALA B 170 ? 2.3260 2.0658 1.9939 -0.6066 0.0862  0.1597  170 ALA B C   
5660 O O   . ALA B 170 ? 2.3314 2.0640 1.9887 -0.6051 0.0823  0.1544  170 ALA B O   
5661 C CB  . ALA B 170 ? 2.3287 1.9715 1.9159 -0.5996 0.0964  0.1308  170 ALA B CB  
5662 N N   . ARG B 171 ? 2.3523 2.1372 2.0936 -0.5891 0.0862  0.1717  171 ARG B N   
5663 C CA  . ARG B 171 ? 2.3876 2.2153 2.2022 -0.5674 0.0818  0.1789  171 ARG B CA  
5664 C C   . ARG B 171 ? 2.4296 2.3107 2.2500 -0.5907 0.0776  0.2016  171 ARG B C   
5665 O O   . ARG B 171 ? 2.4663 2.3567 2.2986 -0.5838 0.0725  0.1991  171 ARG B O   
5666 C CB  . ARG B 171 ? 2.3884 2.2464 2.2779 -0.5447 0.0855  0.1867  171 ARG B CB  
5667 C CG  . ARG B 171 ? 2.3775 2.1936 2.2784 -0.5157 0.0890  0.1621  171 ARG B CG  
5668 C CD  . ARG B 171 ? 2.3190 2.1677 2.2932 -0.4988 0.0944  0.1716  171 ARG B CD  
5669 N NE  . ARG B 171 ? 2.3260 2.1400 2.3103 -0.4740 0.0983  0.1477  171 ARG B NE  
5670 C CZ  . ARG B 171 ? 2.2960 2.1286 2.3407 -0.4575 0.1044  0.1495  171 ARG B CZ  
5671 N NH1 . ARG B 171 ? 2.2584 2.1395 2.3580 -0.4617 0.1081  0.1756  171 ARG B NH1 
5672 N NH2 . ARG B 171 ? 2.2759 2.0790 2.3253 -0.4364 0.1075  0.1255  171 ARG B NH2 
5673 N N   . GLN B 172 ? 2.4482 2.3681 2.2600 -0.6175 0.0797  0.2235  172 GLN B N   
5674 C CA  . GLN B 172 ? 2.4515 2.4304 2.2673 -0.6405 0.0759  0.2460  172 GLN B CA  
5675 C C   . GLN B 172 ? 2.4618 2.4172 2.2129 -0.6650 0.0726  0.2360  172 GLN B C   
5676 O O   . GLN B 172 ? 2.3979 2.3999 2.1468 -0.6850 0.0689  0.2509  172 GLN B O   
5677 C CB  . GLN B 172 ? 2.4883 2.5144 2.3006 -0.6650 0.0794  0.2697  172 GLN B CB  
5678 C CG  . GLN B 172 ? 2.4540 2.5203 2.3389 -0.6423 0.0833  0.2882  172 GLN B CG  
5679 C CD  . GLN B 172 ? 2.4340 2.5610 2.3192 -0.6648 0.0861  0.3163  172 GLN B CD  
5680 O OE1 . GLN B 172 ? 2.4570 2.6025 2.2908 -0.6989 0.0842  0.3213  172 GLN B OE1 
5681 N NE2 . GLN B 172 ? 2.3530 2.5126 2.2962 -0.6460 0.0914  0.3347  172 GLN B NE2 
5682 N N   . CYS B 173 ? 2.5275 2.4108 2.2252 -0.6627 0.0747  0.2112  173 CYS B N   
5683 C CA  . CYS B 173 ? 2.5516 2.4014 2.1883 -0.6811 0.0734  0.1997  173 CYS B CA  
5684 C C   . CYS B 173 ? 2.4686 2.3099 2.1377 -0.6501 0.0684  0.1889  173 CYS B C   
5685 O O   . CYS B 173 ? 2.4257 2.2118 2.0504 -0.6450 0.0693  0.1699  173 CYS B O   
5686 C CB  . CYS B 173 ? 2.6272 2.3995 2.1844 -0.6934 0.0801  0.1795  173 CYS B CB  
5687 S SG  . CYS B 173 ? 2.2208 1.9801 1.6879 -0.7496 0.0845  0.1815  173 CYS B SG  
5688 N N   . ARG B 174 ? 2.4174 2.3131 2.1638 -0.6283 0.0641  0.2013  174 ARG B N   
5689 C CA  . ARG B 174 ? 2.4018 2.3020 2.1857 -0.6005 0.0588  0.1928  174 ARG B CA  
5690 C C   . ARG B 174 ? 2.4753 2.4281 2.2640 -0.6188 0.0535  0.2093  174 ARG B C   
5691 O O   . ARG B 174 ? 2.4921 2.4799 2.3350 -0.5974 0.0486  0.2130  174 ARG B O   
5692 C CB  . ARG B 174 ? 2.3028 2.2247 2.1698 -0.5629 0.0585  0.1923  174 ARG B CB  
5693 C CG  . ARG B 174 ? 2.2526 2.2424 2.1779 -0.5659 0.0591  0.2198  174 ARG B CG  
5694 C CD  . ARG B 174 ? 2.1847 2.1826 2.1852 -0.5311 0.0623  0.2172  174 ARG B CD  
5695 N NE  . ARG B 174 ? 2.1059 2.1628 2.1584 -0.5327 0.0652  0.2454  174 ARG B NE  
5696 C CZ  . ARG B 174 ? 1.9928 2.0620 2.1102 -0.5088 0.0708  0.2496  174 ARG B CZ  
5697 N NH1 . ARG B 174 ? 2.0076 2.0380 2.1475 -0.4831 0.0732  0.2254  174 ARG B NH1 
5698 N NH2 . ARG B 174 ? 1.8661 1.9873 2.0252 -0.5104 0.0748  0.2779  174 ARG B NH2 
5699 N N   . VAL B 175 ? 2.5182 2.4780 2.2495 -0.6592 0.0548  0.2180  175 VAL B N   
5700 C CA  . VAL B 175 ? 2.5144 2.5226 2.2386 -0.6815 0.0503  0.2314  175 VAL B CA  
5701 C C   . VAL B 175 ? 2.5947 2.5629 2.2866 -0.6762 0.0481  0.2139  175 VAL B C   
5702 O O   . VAL B 175 ? 2.5879 2.5722 2.2452 -0.7026 0.0466  0.2185  175 VAL B O   
5703 C CB  . VAL B 175 ? 2.4704 2.4993 2.1401 -0.7294 0.0535  0.2433  175 VAL B CB  
5704 C CG1 . VAL B 175 ? 2.5085 2.4624 2.0915 -0.7537 0.0595  0.2235  175 VAL B CG1 
5705 C CG2 . VAL B 175 ? 2.4304 2.5320 2.1104 -0.7499 0.0484  0.2617  175 VAL B CG2 
5706 N N   . VAL B 176 ? 2.6128 2.5312 2.3162 -0.6413 0.0485  0.1937  176 VAL B N   
5707 C CA  . VAL B 176 ? 2.5799 2.4581 2.2562 -0.6287 0.0470  0.1761  176 VAL B CA  
5708 C C   . VAL B 176 ? 2.5580 2.4516 2.3044 -0.5835 0.0415  0.1676  176 VAL B C   
5709 O O   . VAL B 176 ? 2.5842 2.4867 2.3371 -0.5731 0.0369  0.1630  176 VAL B O   
5710 C CB  . VAL B 176 ? 2.4920 2.2839 2.0962 -0.6305 0.0543  0.1553  176 VAL B CB  
5711 C CG1 . VAL B 176 ? 2.5238 2.2753 2.1054 -0.6100 0.0535  0.1380  176 VAL B CG1 
5712 C CG2 . VAL B 176 ? 2.3950 2.1670 1.9248 -0.6778 0.0609  0.1610  176 VAL B CG2 
5713 N N   . GLU B 177 ? 2.4918 2.3894 2.2906 -0.5578 0.0426  0.1647  177 GLU B N   
5714 C CA  . GLU B 177 ? 2.4604 2.3761 2.3312 -0.5172 0.0387  0.1555  177 GLU B CA  
5715 C C   . GLU B 177 ? 2.4769 2.4540 2.4224 -0.5106 0.0382  0.1751  177 GLU B C   
5716 O O   . GLU B 177 ? 2.4956 2.4804 2.4462 -0.5218 0.0428  0.1870  177 GLU B O   
5717 C CB  . GLU B 177 ? 2.4480 2.3105 2.3187 -0.4876 0.0421  0.1303  177 GLU B CB  
5718 C CG  . GLU B 177 ? 2.4342 2.2368 2.2408 -0.4818 0.0430  0.1093  177 GLU B CG  
5719 C CD  . GLU B 177 ? 2.3872 2.1487 2.2021 -0.4467 0.0456  0.0841  177 GLU B CD  
5720 O OE1 . GLU B 177 ? 2.3265 2.1044 2.1949 -0.4311 0.0471  0.0823  177 GLU B OE1 
5721 O OE2 . GLU B 177 ? 2.4000 2.1143 2.1676 -0.4344 0.0468  0.0664  177 GLU B OE2 
5722 N N   . PRO B 178 ? 2.4783 2.4984 2.4814 -0.4912 0.0333  0.1789  178 PRO B N   
5723 C CA  . PRO B 178 ? 2.4809 2.5563 2.5578 -0.4800 0.0341  0.1976  178 PRO B CA  
5724 C C   . PRO B 178 ? 2.5038 2.5629 2.6334 -0.4518 0.0396  0.1863  178 PRO B C   
5725 O O   . PRO B 178 ? 2.4378 2.5346 2.6319 -0.4387 0.0424  0.1995  178 PRO B O   
5726 C CB  . PRO B 178 ? 2.4355 2.5489 2.5504 -0.4641 0.0277  0.1983  178 PRO B CB  
5727 C CG  . PRO B 178 ? 2.4182 2.5066 2.4695 -0.4778 0.0230  0.1872  178 PRO B CG  
5728 C CD  . PRO B 178 ? 2.4465 2.4664 2.4432 -0.4804 0.0273  0.1676  178 PRO B CD  
5729 N N   . SER B 179 ? 2.5940 2.5980 2.6952 -0.4427 0.0420  0.1626  179 SER B N   
5730 C CA  . SER B 179 ? 2.6193 2.6069 2.7666 -0.4165 0.0472  0.1477  179 SER B CA  
5731 C C   . SER B 179 ? 2.7083 2.7229 2.8947 -0.4225 0.0542  0.1691  179 SER B C   
5732 O O   . SER B 179 ? 2.7446 2.7590 2.8926 -0.4485 0.0567  0.1854  179 SER B O   
5733 C CB  . SER B 179 ? 2.5755 2.5021 2.6715 -0.4115 0.0492  0.1229  179 SER B CB  
5734 O OG  . SER B 179 ? 2.5632 2.4653 2.5894 -0.4423 0.0515  0.1325  179 SER B OG  
5735 N N   . LEU B 180 ? 2.7422 2.7792 3.0045 -0.3982 0.0581  0.1685  180 LEU B N   
5736 C CA  . LEU B 180 ? 2.7510 2.8150 3.0579 -0.4000 0.0664  0.1906  180 LEU B CA  
5737 C C   . LEU B 180 ? 2.8667 2.8984 3.1626 -0.4014 0.0735  0.1832  180 LEU B C   
5738 O O   . LEU B 180 ? 2.9403 2.9445 3.1721 -0.4208 0.0725  0.1813  180 LEU B O   
5739 C CB  . LEU B 180 ? 2.6076 2.7006 2.9986 -0.3737 0.0705  0.1918  180 LEU B CB  
5740 C CG  . LEU B 180 ? 2.5001 2.6352 2.9155 -0.3696 0.0653  0.2049  180 LEU B CG  
5741 C CD1 . LEU B 180 ? 2.4070 2.5625 2.9060 -0.3426 0.0722  0.2045  180 LEU B CD1 
5742 C CD2 . LEU B 180 ? 2.4857 2.6599 2.8734 -0.3957 0.0638  0.2394  180 LEU B CD2 
5743 N N   . SER B 181 ? 2.8877 2.9226 3.2461 -0.3813 0.0816  0.1785  181 SER B N   
5744 C CA  . SER B 181 ? 2.9461 2.9592 3.3033 -0.3824 0.0896  0.1749  181 SER B CA  
5745 C C   . SER B 181 ? 3.0169 2.9838 3.3509 -0.3687 0.0884  0.1394  181 SER B C   
5746 O O   . SER B 181 ? 3.0620 3.0002 3.3480 -0.3793 0.0898  0.1350  181 SER B O   
5747 C CB  . SER B 181 ? 2.9067 2.9440 3.3402 -0.3692 0.1009  0.1874  181 SER B CB  
5748 O OG  . SER B 181 ? 2.8608 2.8972 3.3527 -0.3428 0.1029  0.1655  181 SER B OG  
5749 N N   . ASP B 182 ? 3.0151 2.9772 3.3828 -0.3441 0.0862  0.1140  182 ASP B N   
5750 C CA  . ASP B 182 ? 3.0089 2.9354 3.3633 -0.3261 0.0857  0.0793  182 ASP B CA  
5751 C C   . ASP B 182 ? 3.0407 2.9340 3.3204 -0.3288 0.0770  0.0643  182 ASP B C   
5752 O O   . ASP B 182 ? 3.0602 2.9168 3.2967 -0.3251 0.0778  0.0470  182 ASP B O   
5753 C CB  . ASP B 182 ? 2.9340 2.8737 3.3605 -0.2976 0.0884  0.0560  182 ASP B CB  
5754 C CG  . ASP B 182 ? 2.8673 2.8280 3.3646 -0.2938 0.1003  0.0659  182 ASP B CG  
5755 O OD1 . ASP B 182 ? 2.8628 2.8266 3.3516 -0.3106 0.1063  0.0899  182 ASP B OD1 
5756 O OD2 . ASP B 182 ? 2.8241 2.7980 3.3852 -0.2742 0.1045  0.0493  182 ASP B OD2 
5757 N N   . ASP B 183 ? 3.0400 2.9455 3.3036 -0.3345 0.0697  0.0716  183 ASP B N   
5758 C CA  . ASP B 183 ? 3.0481 2.9212 3.2413 -0.3375 0.0630  0.0592  183 ASP B CA  
5759 C C   . ASP B 183 ? 3.0270 2.8738 3.1421 -0.3681 0.0635  0.0744  183 ASP B C   
5760 O O   . ASP B 183 ? 3.0497 2.8640 3.0993 -0.3749 0.0600  0.0669  183 ASP B O   
5761 C CB  . ASP B 183 ? 3.0454 2.9421 3.2485 -0.3339 0.0556  0.0615  183 ASP B CB  
5762 C CG  . ASP B 183 ? 3.0223 2.9315 3.2826 -0.3006 0.0539  0.0362  183 ASP B CG  
5763 O OD1 . ASP B 183 ? 3.0336 2.9341 3.3257 -0.2814 0.0587  0.0159  183 ASP B OD1 
5764 O OD2 . ASP B 183 ? 2.9824 2.9129 3.2562 -0.2942 0.0480  0.0357  183 ASP B OD2 
5765 N N   . ALA B 184 ? 2.9672 2.8279 3.0890 -0.3865 0.0687  0.0954  184 ALA B N   
5766 C CA  . ALA B 184 ? 2.9428 2.7819 2.9946 -0.4164 0.0701  0.1082  184 ALA B CA  
5767 C C   . ALA B 184 ? 2.9230 2.7352 2.9645 -0.4128 0.0768  0.0997  184 ALA B C   
5768 O O   . ALA B 184 ? 2.9542 2.7357 2.9314 -0.4318 0.0787  0.1014  184 ALA B O   
5769 C CB  . ALA B 184 ? 2.9104 2.7942 2.9703 -0.4437 0.0701  0.1412  184 ALA B CB  
5770 N N   . ILE B 185 ? 2.8560 2.6806 2.9613 -0.3891 0.0809  0.0898  185 ILE B N   
5771 C CA  . ILE B 185 ? 2.8172 2.6207 2.9211 -0.3817 0.0874  0.0790  185 ILE B CA  
5772 C C   . ILE B 185 ? 2.7652 2.5346 2.8578 -0.3533 0.0863  0.0442  185 ILE B C   
5773 O O   . ILE B 185 ? 2.7995 2.5364 2.8562 -0.3487 0.0896  0.0308  185 ILE B O   
5774 C CB  . ILE B 185 ? 2.6589 2.4989 2.8408 -0.3750 0.0948  0.0903  185 ILE B CB  
5775 C CG1 . ILE B 185 ? 2.6420 2.5180 2.8324 -0.4003 0.0970  0.1267  185 ILE B CG1 
5776 C CG2 . ILE B 185 ? 2.6448 2.4647 2.8276 -0.3657 0.1016  0.0761  185 ILE B CG2 
5777 C CD1 . ILE B 185 ? 2.5783 2.4876 2.8421 -0.3934 0.1062  0.1416  185 ILE B CD1 
5778 N N   . GLN B 186 ? 2.6406 2.4202 2.7634 -0.3332 0.0817  0.0294  186 GLN B N   
5779 C CA  . GLN B 186 ? 2.5470 2.3033 2.6639 -0.3034 0.0803  -0.0040 186 GLN B CA  
5780 C C   . GLN B 186 ? 2.5986 2.3110 2.6310 -0.3055 0.0760  -0.0121 186 GLN B C   
5781 O O   . GLN B 186 ? 2.6188 2.3034 2.6261 -0.2817 0.0757  -0.0375 186 GLN B O   
5782 C CB  . GLN B 186 ? 2.4078 2.1967 2.5942 -0.2802 0.0776  -0.0179 186 GLN B CB  
5783 C CG  . GLN B 186 ? 2.3093 2.0957 2.5263 -0.2484 0.0797  -0.0520 186 GLN B CG  
5784 C CD  . GLN B 186 ? 2.1832 1.9893 2.4599 -0.2460 0.0884  -0.0533 186 GLN B CD  
5785 O OE1 . GLN B 186 ? 2.0696 1.9091 2.4118 -0.2504 0.0923  -0.0406 186 GLN B OE1 
5786 N NE2 . GLN B 186 ? 2.1673 1.9520 2.4206 -0.2383 0.0925  -0.0682 186 GLN B NE2 
5787 N N   . LYS B 187 ? 2.6381 2.3450 2.6260 -0.3340 0.0736  0.0098  187 LYS B N   
5788 C CA  . LYS B 187 ? 2.7115 2.3741 2.6172 -0.3406 0.0715  0.0048  187 LYS B CA  
5789 C C   . LYS B 187 ? 2.7960 2.4192 2.6273 -0.3673 0.0763  0.0147  187 LYS B C   
5790 O O   . LYS B 187 ? 2.8707 2.4422 2.6378 -0.3599 0.0791  -0.0002 187 LYS B O   
5791 C CB  . LYS B 187 ? 2.6625 2.3449 2.5667 -0.3523 0.0655  0.0169  187 LYS B CB  
5792 C CG  . LYS B 187 ? 2.5635 2.2731 2.5232 -0.3228 0.0604  0.0016  187 LYS B CG  
5793 C CD  . LYS B 187 ? 2.4958 2.2209 2.4433 -0.3346 0.0545  0.0131  187 LYS B CD  
5794 C CE  . LYS B 187 ? 2.3753 2.1280 2.3758 -0.3047 0.0492  -0.0033 187 LYS B CE  
5795 N NZ  . LYS B 187 ? 2.3136 2.0812 2.2986 -0.3156 0.0434  0.0077  187 LYS B NZ  
5796 N N   . VAL B 188 ? 2.7293 2.3775 2.5684 -0.3971 0.0779  0.0396  188 VAL B N   
5797 C CA  . VAL B 188 ? 2.6573 2.2741 2.4284 -0.4254 0.0824  0.0489  188 VAL B CA  
5798 C C   . VAL B 188 ? 2.6340 2.2181 2.3870 -0.4113 0.0882  0.0338  188 VAL B C   
5799 O O   . VAL B 188 ? 2.6531 2.1886 2.3324 -0.4219 0.0922  0.0287  188 VAL B O   
5800 C CB  . VAL B 188 ? 2.5674 2.2280 2.3561 -0.4587 0.0826  0.0787  188 VAL B CB  
5801 C CG1 . VAL B 188 ? 2.6082 2.2390 2.3275 -0.4882 0.0875  0.0855  188 VAL B CG1 
5802 C CG2 . VAL B 188 ? 2.4709 2.1639 2.2684 -0.4738 0.0770  0.0935  188 VAL B CG2 
5803 N N   . ILE B 189 ? 2.6089 2.2192 2.4284 -0.3876 0.0893  0.0258  189 ILE B N   
5804 C CA  . ILE B 189 ? 2.6859 2.2736 2.4963 -0.3724 0.0947  0.0108  189 ILE B CA  
5805 C C   . ILE B 189 ? 2.7687 2.3017 2.5194 -0.3490 0.0956  -0.0155 189 ILE B C   
5806 O O   . ILE B 189 ? 2.8136 2.3105 2.5175 -0.3464 0.1005  -0.0239 189 ILE B O   
5807 C CB  . ILE B 189 ? 2.1768 1.8055 2.0750 -0.3503 0.0966  0.0044  189 ILE B CB  
5808 C CG1 . ILE B 189 ? 2.0820 1.7580 2.0334 -0.3713 0.0989  0.0322  189 ILE B CG1 
5809 C CG2 . ILE B 189 ? 2.1591 1.7651 2.0454 -0.3311 0.1017  -0.0156 189 ILE B CG2 
5810 C CD1 . ILE B 189 ? 1.9448 1.6557 1.9800 -0.3526 0.1035  0.0273  189 ILE B CD1 
5811 N N   . GLU B 190 ? 2.7589 2.2870 2.5105 -0.3305 0.0912  -0.0279 190 GLU B N   
5812 C CA  . GLU B 190 ? 2.7574 2.2403 2.4606 -0.3014 0.0924  -0.0531 190 GLU B CA  
5813 C C   . GLU B 190 ? 2.7513 2.1722 2.3552 -0.3171 0.0958  -0.0501 190 GLU B C   
5814 O O   . GLU B 190 ? 2.7403 2.1129 2.2866 -0.3043 0.1013  -0.0633 190 GLU B O   
5815 C CB  . GLU B 190 ? 2.7417 2.2480 2.4885 -0.2720 0.0869  -0.0689 190 GLU B CB  
5816 C CG  . GLU B 190 ? 2.6890 2.2472 2.5284 -0.2512 0.0858  -0.0800 190 GLU B CG  
5817 C CD  . GLU B 190 ? 2.6487 2.2366 2.5359 -0.2275 0.0801  -0.0941 190 GLU B CD  
5818 O OE1 . GLU B 190 ? 2.6579 2.2336 2.5137 -0.2307 0.0761  -0.0900 190 GLU B OE1 
5819 O OE2 . GLU B 190 ? 2.5815 2.2057 2.5380 -0.2066 0.0802  -0.1099 190 GLU B OE2 
5820 N N   . HIS B 191 ? 2.7347 2.1568 2.3182 -0.3446 0.0935  -0.0332 191 HIS B N   
5821 C CA  . HIS B 191 ? 2.7673 2.1311 2.2579 -0.3661 0.0984  -0.0290 191 HIS B CA  
5822 C C   . HIS B 191 ? 2.6381 1.9790 2.0874 -0.3924 0.1048  -0.0205 191 HIS B C   
5823 O O   . HIS B 191 ? 2.6541 1.9332 2.0262 -0.3934 0.1120  -0.0288 191 HIS B O   
5824 C CB  . HIS B 191 ? 2.9021 2.2821 2.3868 -0.3945 0.0947  -0.0119 191 HIS B CB  
5825 C CG  . HIS B 191 ? 3.0038 2.3911 2.5047 -0.3709 0.0899  -0.0210 191 HIS B CG  
5826 N ND1 . HIS B 191 ? 3.0848 2.4209 2.5166 -0.3673 0.0934  -0.0276 191 HIS B ND1 
5827 C CD2 . HIS B 191 ? 2.9800 2.4200 2.5578 -0.3500 0.0825  -0.0245 191 HIS B CD2 
5828 C CE1 . HIS B 191 ? 3.0629 2.4230 2.5288 -0.3444 0.0875  -0.0344 191 HIS B CE1 
5829 N NE2 . HIS B 191 ? 2.9924 2.4157 2.5470 -0.3338 0.0806  -0.0336 191 HIS B NE2 
5830 N N   . GLY B 192 ? 2.4534 1.8443 1.9540 -0.4125 0.1027  -0.0038 192 GLY B N   
5831 C CA  . GLY B 192 ? 2.2793 1.6609 1.7506 -0.4380 0.1078  0.0058  192 GLY B CA  
5832 C C   . GLY B 192 ? 2.0798 1.4750 1.5895 -0.4160 0.1098  -0.0028 192 GLY B C   
5833 O O   . GLY B 192 ? 1.9773 1.3576 1.4955 -0.3798 0.1103  -0.0237 192 GLY B O   
5834 N N   . ASN B 210 ? 2.4119 1.8050 1.5084 -0.7945 0.1186  0.1008  210 ASN B N   
5835 C CA  . ASN B 210 ? 2.6647 1.9905 1.6707 -0.8306 0.1324  0.0916  210 ASN B CA  
5836 C C   . ASN B 210 ? 2.7773 2.0861 1.7725 -0.8320 0.1363  0.0872  210 ASN B C   
5837 O O   . ASN B 210 ? 2.8097 2.0408 1.7562 -0.8158 0.1452  0.0716  210 ASN B O   
5838 C CB  . ASN B 210 ? 2.6975 2.0562 1.6727 -0.8870 0.1353  0.1011  210 ASN B CB  
5839 C CG  . ASN B 210 ? 2.7008 2.0408 1.6488 -0.8939 0.1378  0.0998  210 ASN B CG  
5840 O OD1 . ASN B 210 ? 2.7138 1.9739 1.6126 -0.8767 0.1464  0.0867  210 ASN B OD1 
5841 N ND2 . ASN B 210 ? 2.6275 2.0427 1.6060 -0.9187 0.1309  0.1140  210 ASN B ND2 
5842 N N   . GLU B 211 ? 2.8042 2.1873 1.8439 -0.8501 0.1301  0.1016  211 GLU B N   
5843 C CA  . GLU B 211 ? 2.8039 2.1838 1.8392 -0.8538 0.1330  0.1000  211 GLU B CA  
5844 C C   . GLU B 211 ? 2.7595 2.1598 1.8647 -0.8049 0.1257  0.1009  211 GLU B C   
5845 O O   . GLU B 211 ? 2.6822 2.0746 1.7889 -0.7982 0.1279  0.0981  211 GLU B O   
5846 C CB  . GLU B 211 ? 2.7770 2.2316 1.8258 -0.8965 0.1306  0.1161  211 GLU B CB  
5847 C CG  . GLU B 211 ? 2.7116 2.2660 1.8524 -0.8827 0.1177  0.1375  211 GLU B CG  
5848 C CD  . GLU B 211 ? 2.7118 2.3385 1.8713 -0.9125 0.1159  0.1536  211 GLU B CD  
5849 O OE1 . GLU B 211 ? 2.7508 2.3511 1.8573 -0.9403 0.1237  0.1464  211 GLU B OE1 
5850 O OE2 . GLU B 211 ? 2.6638 2.3745 1.8905 -0.9067 0.1072  0.1736  211 GLU B OE2 
5851 N N   . ILE B 212 ? 2.7569 2.1858 1.9208 -0.7722 0.1172  0.1043  212 ILE B N   
5852 C CA  . ILE B 212 ? 2.7006 2.1475 1.9326 -0.7259 0.1112  0.1026  212 ILE B CA  
5853 C C   . ILE B 212 ? 2.7346 2.1002 1.9282 -0.6925 0.1172  0.0802  212 ILE B C   
5854 O O   . ILE B 212 ? 2.6578 2.0269 1.8971 -0.6528 0.1139  0.0734  212 ILE B O   
5855 C CB  . ILE B 212 ? 2.6752 2.1801 1.9817 -0.7035 0.1009  0.1117  212 ILE B CB  
5856 C CG1 . ILE B 212 ? 2.6815 2.2187 2.0672 -0.6636 0.0956  0.1124  212 ILE B CG1 
5857 C CG2 . ILE B 212 ? 2.7022 2.1635 1.9800 -0.6886 0.1016  0.0994  212 ILE B CG2 
5858 C CD1 . ILE B 212 ? 2.7407 2.3183 2.1541 -0.6757 0.0962  0.1257  212 ILE B CD1 
5859 N N   . ARG B 213 ? 2.8370 2.1299 1.9452 -0.7090 0.1270  0.0688  213 ARG B N   
5860 C CA  . ARG B 213 ? 2.8815 2.0919 1.9410 -0.6781 0.1347  0.0486  213 ARG B CA  
5861 C C   . ARG B 213 ? 2.8681 2.0386 1.8853 -0.6849 0.1427  0.0410  213 ARG B C   
5862 O O   . ARG B 213 ? 2.8175 1.9446 1.8232 -0.6498 0.1460  0.0267  213 ARG B O   
5863 C CB  . ARG B 213 ? 2.9998 2.1467 1.9856 -0.6901 0.1432  0.0414  213 ARG B CB  
5864 C CG  . ARG B 213 ? 3.0724 2.1353 2.0078 -0.6526 0.1515  0.0225  213 ARG B CG  
5865 C CD  . ARG B 213 ? 3.1199 2.1328 1.9979 -0.6596 0.1588  0.0194  213 ARG B CD  
5866 N NE  . ARG B 213 ? 3.0478 2.1233 1.9824 -0.6579 0.1481  0.0298  213 ARG B NE  
5867 C CZ  . ARG B 213 ? 3.0133 2.1323 1.9535 -0.6999 0.1456  0.0438  213 ARG B CZ  
5868 N NH1 . ARG B 213 ? 3.0477 2.1557 1.9400 -0.7488 0.1532  0.0481  213 ARG B NH1 
5869 N NH2 . ARG B 213 ? 2.9143 2.0906 1.9079 -0.6929 0.1357  0.0525  213 ARG B NH2 
5870 N N   . ASP B 214 ? 2.9249 2.1143 1.9195 -0.7297 0.1457  0.0501  214 ASP B N   
5871 C CA  . ASP B 214 ? 3.0055 2.1620 1.9582 -0.7415 0.1534  0.0434  214 ASP B CA  
5872 C C   . ASP B 214 ? 2.9407 2.1537 1.9626 -0.7225 0.1462  0.0504  214 ASP B C   
5873 O O   . ASP B 214 ? 3.0154 2.1956 2.0167 -0.7092 0.1511  0.0405  214 ASP B O   
5874 C CB  . ASP B 214 ? 3.0792 2.2346 1.9770 -0.7991 0.1603  0.0482  214 ASP B CB  
5875 C CG  . ASP B 214 ? 3.1305 2.2078 1.9417 -0.8204 0.1725  0.0371  214 ASP B CG  
5876 O OD1 . ASP B 214 ? 3.1141 2.1559 1.9185 -0.7934 0.1731  0.0313  214 ASP B OD1 
5877 O OD2 . ASP B 214 ? 3.1853 2.2372 1.9348 -0.8646 0.1822  0.0338  214 ASP B OD2 
5878 N N   . ARG B 215 ? 2.7743 2.0711 1.8769 -0.7208 0.1356  0.0677  215 ARG B N   
5879 C CA  . ARG B 215 ? 2.6155 1.9668 1.7874 -0.7028 0.1302  0.0764  215 ARG B CA  
5880 C C   . ARG B 215 ? 2.5360 1.8568 1.7300 -0.6535 0.1301  0.0609  215 ARG B C   
5881 O O   . ARG B 215 ? 2.5820 1.9198 1.8055 -0.6400 0.1302  0.0613  215 ARG B O   
5882 C CB  . ARG B 215 ? 2.5197 1.9610 1.7737 -0.7060 0.1205  0.0982  215 ARG B CB  
5883 C CG  . ARG B 215 ? 2.5430 2.0345 1.7864 -0.7531 0.1202  0.1162  215 ARG B CG  
5884 C CD  . ARG B 215 ? 2.6386 2.1241 1.8474 -0.7750 0.1262  0.1162  215 ARG B CD  
5885 N NE  . ARG B 215 ? 2.7492 2.2581 1.9161 -0.8254 0.1289  0.1243  215 ARG B NE  
5886 C CZ  . ARG B 215 ? 2.7512 2.3406 1.9545 -0.8471 0.1250  0.1451  215 ARG B CZ  
5887 N NH1 . ARG B 215 ? 2.6752 2.3251 1.9572 -0.8225 0.1191  0.1616  215 ARG B NH1 
5888 N NH2 . ARG B 215 ? 2.8182 2.4287 1.9786 -0.8936 0.1278  0.1492  215 ARG B NH2 
5889 N N   . HIS B 216 ? 2.4605 1.7393 1.6399 -0.6267 0.1304  0.0471  216 HIS B N   
5890 C CA  . HIS B 216 ? 2.4795 1.7277 1.6711 -0.5796 0.1310  0.0294  216 HIS B CA  
5891 C C   . HIS B 216 ? 2.6004 1.7852 1.7241 -0.5780 0.1407  0.0157  216 HIS B C   
5892 O O   . HIS B 216 ? 2.6273 1.8177 1.7756 -0.5538 0.1407  0.0092  216 HIS B O   
5893 C CB  . HIS B 216 ? 2.4571 1.6738 1.6391 -0.5518 0.1300  0.0174  216 HIS B CB  
5894 C CG  . HIS B 216 ? 2.4272 1.6121 1.6127 -0.5035 0.1314  -0.0028 216 HIS B CG  
5895 N ND1 . HIS B 216 ? 2.3265 1.5597 1.5927 -0.4703 0.1245  -0.0065 216 HIS B ND1 
5896 C CD2 . HIS B 216 ? 2.4783 1.5896 1.5956 -0.4824 0.1397  -0.0207 216 HIS B CD2 
5897 C CE1 . HIS B 216 ? 2.3456 1.5414 1.5945 -0.4318 0.1276  -0.0268 216 HIS B CE1 
5898 N NE2 . HIS B 216 ? 2.4528 1.5748 1.6113 -0.4366 0.1366  -0.0349 216 HIS B NE2 
5899 N N   . LYS B 217 ? 2.6572 1.7808 1.6946 -0.6042 0.1496  0.0109  217 LYS B N   
5900 C CA  . LYS B 217 ? 2.6560 1.7145 1.6212 -0.6066 0.1603  -0.0018 217 LYS B CA  
5901 C C   . LYS B 217 ? 2.5488 1.6494 1.5362 -0.6267 0.1593  0.0072  217 LYS B C   
5902 O O   . LYS B 217 ? 2.5802 1.6467 1.5347 -0.6178 0.1653  -0.0030 217 LYS B O   
5903 C CB  . LYS B 217 ? 2.7021 1.6896 1.5722 -0.6384 0.1716  -0.0069 217 LYS B CB  
5904 C CG  . LYS B 217 ? 2.6845 1.6119 1.5145 -0.6147 0.1763  -0.0177 217 LYS B CG  
5905 C CD  . LYS B 217 ? 2.6898 1.6481 1.5383 -0.6358 0.1715  -0.0062 217 LYS B CD  
5906 C CE  . LYS B 217 ? 2.8092 1.6955 1.5976 -0.6209 0.1798  -0.0162 217 LYS B CE  
5907 N NZ  . LYS B 217 ? 2.7947 1.7000 1.5826 -0.6499 0.1780  -0.0055 217 LYS B NZ  
5908 N N   . ASP B 218 ? 2.4064 1.5831 1.4495 -0.6521 0.1519  0.0270  218 ASP B N   
5909 C CA  . ASP B 218 ? 2.3922 1.6180 1.4595 -0.6727 0.1509  0.0391  218 ASP B CA  
5910 C C   . ASP B 218 ? 2.3272 1.6023 1.4754 -0.6386 0.1449  0.0433  218 ASP B C   
5911 O O   . ASP B 218 ? 2.4027 1.6952 1.5591 -0.6414 0.1468  0.0464  218 ASP B O   
5912 C CB  . ASP B 218 ? 2.3997 1.6872 1.4853 -0.7156 0.1469  0.0597  218 ASP B CB  
5913 C CG  . ASP B 218 ? 2.4810 1.7266 1.4816 -0.7601 0.1551  0.0550  218 ASP B CG  
5914 O OD1 . ASP B 218 ? 2.5228 1.6951 1.4506 -0.7624 0.1650  0.0381  218 ASP B OD1 
5915 O OD2 . ASP B 218 ? 2.4886 1.7755 1.4951 -0.7931 0.1523  0.0678  218 ASP B OD2 
5916 N N   . ILE B 219 ? 2.1416 1.4395 1.3492 -0.6075 0.1385  0.0428  219 ILE B N   
5917 C CA  . ILE B 219 ? 1.9979 1.3387 1.2835 -0.5750 0.1344  0.0441  219 ILE B CA  
5918 C C   . ILE B 219 ? 2.0288 1.3208 1.2902 -0.5404 0.1390  0.0220  219 ILE B C   
5919 O O   . ILE B 219 ? 2.1751 1.4894 1.4679 -0.5284 0.1399  0.0221  219 ILE B O   
5920 C CB  . ILE B 219 ? 2.0425 1.4264 1.4024 -0.5543 0.1266  0.0490  219 ILE B CB  
5921 C CG1 . ILE B 219 ? 1.9841 1.4453 1.4069 -0.5760 0.1217  0.0753  219 ILE B CG1 
5922 C CG2 . ILE B 219 ? 1.9842 1.3727 1.3954 -0.5097 0.1254  0.0347  219 ILE B CG2 
5923 C CD1 . ILE B 219 ? 2.0330 1.5041 1.4120 -0.6212 0.1226  0.0898  219 ILE B CD1 
5924 N N   . GLN B 220 ? 1.9829 1.2096 1.1874 -0.5236 0.1426  0.0037  220 GLN B N   
5925 C CA  . GLN B 220 ? 2.0765 1.2570 1.2534 -0.4872 0.1473  -0.0176 220 GLN B CA  
5926 C C   . GLN B 220 ? 2.0967 1.2382 1.2094 -0.5022 0.1555  -0.0220 220 GLN B C   
5927 O O   . GLN B 220 ? 2.0996 1.2138 1.1951 -0.4740 0.1595  -0.0372 220 GLN B O   
5928 C CB  . GLN B 220 ? 2.3494 1.4721 1.4808 -0.4629 0.1498  -0.0341 220 GLN B CB  
5929 C CG  . GLN B 220 ? 2.6519 1.7119 1.6940 -0.4925 0.1572  -0.0337 220 GLN B CG  
5930 C CD  . GLN B 220 ? 2.7968 1.8086 1.8031 -0.4703 0.1594  -0.0448 220 GLN B CD  
5931 O OE1 . GLN B 220 ? 2.8260 1.8670 1.8853 -0.4396 0.1527  -0.0490 220 GLN B OE1 
5932 N NE2 . GLN B 220 ? 2.8161 1.7536 1.7316 -0.4861 0.1699  -0.0498 220 GLN B NE2 
5933 N N   . GLN B 221 ? 2.1030 1.2438 1.1795 -0.5464 0.1583  -0.0098 221 GLN B N   
5934 C CA  . GLN B 221 ? 2.1780 1.2945 1.2032 -0.5649 0.1654  -0.0124 221 GLN B CA  
5935 C C   . GLN B 221 ? 2.0920 1.2721 1.1843 -0.5572 0.1616  -0.0033 221 GLN B C   
5936 O O   . GLN B 221 ? 2.0607 1.2243 1.1444 -0.5342 0.1650  -0.0149 221 GLN B O   
5937 C CB  . GLN B 221 ? 2.2549 1.3662 1.2320 -0.6169 0.1690  -0.0022 221 GLN B CB  
5938 C CG  . GLN B 221 ? 2.4203 1.4421 1.2966 -0.6304 0.1796  -0.0169 221 GLN B CG  
5939 C CD  . GLN B 221 ? 2.4906 1.4570 1.2972 -0.6339 0.1899  -0.0303 221 GLN B CD  
5940 O OE1 . GLN B 221 ? 2.5223 1.4683 1.3284 -0.5972 0.1917  -0.0421 221 GLN B OE1 
5941 N NE2 . GLN B 221 ? 2.4683 1.4117 1.2150 -0.6785 0.1972  -0.0296 221 GLN B NE2 
5942 N N   . LEU B 222 ? 1.9896 1.2431 1.1487 -0.5756 0.1551  0.0182  222 LEU B N   
5943 C CA  . LEU B 222 ? 1.9310 1.2490 1.1608 -0.5689 0.1523  0.0307  222 LEU B CA  
5944 C C   . LEU B 222 ? 2.0221 1.3411 1.2958 -0.5235 0.1515  0.0169  222 LEU B C   
5945 O O   . LEU B 222 ? 2.1236 1.4777 1.4388 -0.5139 0.1523  0.0210  222 LEU B O   
5946 C CB  . LEU B 222 ? 1.8236 1.2153 1.1232 -0.5863 0.1459  0.0555  222 LEU B CB  
5947 C CG  . LEU B 222 ? 1.9189 1.3224 1.1816 -0.6315 0.1459  0.0695  222 LEU B CG  
5948 C CD1 . LEU B 222 ? 1.9510 1.4355 1.2867 -0.6440 0.1400  0.0958  222 LEU B CD1 
5949 C CD2 . LEU B 222 ? 2.0246 1.4127 1.2304 -0.6569 0.1520  0.0681  222 LEU B CD2 
5950 N N   . GLU B 223 ? 2.0057 1.2887 1.2698 -0.4958 0.1504  0.0003  223 GLU B N   
5951 C CA  . GLU B 223 ? 2.0418 1.3301 1.3477 -0.4524 0.1494  -0.0154 223 GLU B CA  
5952 C C   . GLU B 223 ? 2.0709 1.3091 1.3215 -0.4296 0.1557  -0.0361 223 GLU B C   
5953 O O   . GLU B 223 ? 2.0750 1.3369 1.3644 -0.4051 0.1562  -0.0434 223 GLU B O   
5954 C CB  . GLU B 223 ? 2.1072 1.3885 1.4330 -0.4296 0.1449  -0.0247 223 GLU B CB  
5955 C CG  . GLU B 223 ? 2.0336 1.3820 1.4502 -0.4308 0.1381  -0.0102 223 GLU B CG  
5956 C CD  . GLU B 223 ? 2.0393 1.4347 1.5345 -0.4061 0.1377  -0.0135 223 GLU B CD  
5957 O OE1 . GLU B 223 ? 1.9038 1.2979 1.3916 -0.4012 0.1421  -0.0176 223 GLU B OE1 
5958 O OE2 . GLU B 223 ? 2.1241 1.5578 1.6887 -0.3925 0.1335  -0.0126 223 GLU B OE2 
5959 N N   . ARG B 224 ? 2.1698 1.3383 1.3295 -0.4370 0.1615  -0.0458 224 ARG B N   
5960 C CA  . ARG B 224 ? 2.1878 1.3060 1.2889 -0.4162 0.1686  -0.0640 224 ARG B CA  
5961 C C   . ARG B 224 ? 2.0986 1.2309 1.1857 -0.4420 0.1721  -0.0550 224 ARG B C   
5962 O O   . ARG B 224 ? 2.1065 1.2136 1.1597 -0.4262 0.1773  -0.0673 224 ARG B O   
5963 C CB  . ARG B 224 ? 2.2599 1.2917 1.2671 -0.4088 0.1757  -0.0789 224 ARG B CB  
5964 C CG  . ARG B 224 ? 2.4475 1.4487 1.4038 -0.4506 0.1785  -0.0686 224 ARG B CG  
5965 C CD  . ARG B 224 ? 2.6400 1.5478 1.4992 -0.4409 0.1884  -0.0843 224 ARG B CD  
5966 N NE  . ARG B 224 ? 2.7391 1.6197 1.5597 -0.4758 0.1909  -0.0762 224 ARG B NE  
5967 C CZ  . ARG B 224 ? 2.7227 1.6135 1.5679 -0.4710 0.1861  -0.0723 224 ARG B CZ  
5968 N NH1 . ARG B 224 ? 2.6151 1.5424 1.5236 -0.4328 0.1786  -0.0767 224 ARG B NH1 
5969 N NH2 . ARG B 224 ? 2.7279 1.5946 1.5349 -0.5051 0.1892  -0.0650 224 ARG B NH2 
5970 N N   . SER B 225 ? 1.9614 1.1383 1.0761 -0.4803 0.1691  -0.0333 225 SER B N   
5971 C CA  . SER B 225 ? 1.9030 1.1123 1.0228 -0.5031 0.1710  -0.0217 225 SER B CA  
5972 C C   . SER B 225 ? 1.8725 1.1414 1.0741 -0.4790 0.1682  -0.0177 225 SER B C   
5973 O O   . SER B 225 ? 1.8634 1.1287 1.0548 -0.4653 0.1720  -0.0259 225 SER B O   
5974 C CB  . SER B 225 ? 1.8399 1.0881 0.9697 -0.5483 0.1685  0.0011  225 SER B CB  
5975 O OG  . SER B 225 ? 1.9349 1.1938 1.0367 -0.5743 0.1725  0.0076  225 SER B OG  
5976 N N   . LEU B 226 ? 1.8073 1.1298 1.0894 -0.4739 0.1623  -0.0058 226 LEU B N   
5977 C CA  . LEU B 226 ? 1.6441 1.0213 1.0083 -0.4523 0.1612  -0.0025 226 LEU B CA  
5978 C C   . LEU B 226 ? 1.6300 0.9808 0.9856 -0.4119 0.1638  -0.0281 226 LEU B C   
5979 O O   . LEU B 226 ? 1.6110 0.9936 1.0051 -0.3985 0.1660  -0.0295 226 LEU B O   
5980 C CB  . LEU B 226 ? 1.5170 0.9417 0.9609 -0.4495 0.1557  0.0096  226 LEU B CB  
5981 C CG  . LEU B 226 ? 1.5957 1.0607 1.0602 -0.4859 0.1532  0.0375  226 LEU B CG  
5982 C CD1 . LEU B 226 ? 1.5222 1.0195 1.0505 -0.4797 0.1480  0.0455  226 LEU B CD1 
5983 C CD2 . LEU B 226 ? 1.6259 1.1423 1.1245 -0.5016 0.1563  0.0582  226 LEU B CD2 
5984 N N   . LEU B 227 ? 1.6582 0.9522 0.9612 -0.3923 0.1642  -0.0480 227 LEU B N   
5985 C CA  . LEU B 227 ? 1.7489 1.0178 1.0366 -0.3514 0.1668  -0.0730 227 LEU B CA  
5986 C C   . LEU B 227 ? 1.7776 1.0146 1.0043 -0.3487 0.1732  -0.0816 227 LEU B C   
5987 O O   . LEU B 227 ? 1.7311 0.9870 0.9801 -0.3239 0.1751  -0.0924 227 LEU B O   
5988 C CB  . LEU B 227 ? 1.8423 1.0613 1.0898 -0.3285 0.1660  -0.0900 227 LEU B CB  
5989 C CG  . LEU B 227 ? 1.9149 1.1663 1.2262 -0.2911 0.1621  -0.1044 227 LEU B CG  
5990 C CD1 . LEU B 227 ? 1.9516 1.1728 1.2437 -0.2770 0.1593  -0.1131 227 LEU B CD1 
5991 C CD2 . LEU B 227 ? 1.8819 1.1307 1.1856 -0.2556 0.1659  -0.1255 227 LEU B CD2 
5992 N N   . GLU B 228 ? 1.8988 1.0880 1.0485 -0.3746 0.1772  -0.0781 228 GLU B N   
5993 C CA  . GLU B 228 ? 2.0353 1.1939 1.1248 -0.3766 0.1838  -0.0851 228 GLU B CA  
5994 C C   . GLU B 228 ? 1.8944 1.1187 1.0422 -0.3854 0.1831  -0.0723 228 GLU B C   
5995 O O   . GLU B 228 ? 1.8624 1.0916 1.0092 -0.3634 0.1862  -0.0832 228 GLU B O   
5996 C CB  . GLU B 228 ? 2.2530 1.3610 1.2621 -0.4133 0.1884  -0.0801 228 GLU B CB  
5997 C CG  . GLU B 228 ? 2.4880 1.5048 1.4007 -0.3987 0.1959  -0.1000 228 GLU B CG  
5998 C CD  . GLU B 228 ? 2.5544 1.5427 1.4623 -0.3847 0.1940  -0.1051 228 GLU B CD  
5999 O OE1 . GLU B 228 ? 2.4461 1.4788 1.4247 -0.3623 0.1871  -0.1048 228 GLU B OE1 
6000 O OE2 . GLU B 228 ? 2.6449 1.5653 1.4771 -0.3964 0.2001  -0.1099 228 GLU B OE2 
6001 N N   . LEU B 229 ? 1.7339 1.0097 0.9314 -0.4171 0.1796  -0.0481 229 LEU B N   
6002 C CA  . LEU B 229 ? 1.6513 0.9933 0.9095 -0.4274 0.1796  -0.0311 229 LEU B CA  
6003 C C   . LEU B 229 ? 1.5003 0.8805 0.8277 -0.3935 0.1794  -0.0390 229 LEU B C   
6004 O O   . LEU B 229 ? 1.3773 0.7750 0.7112 -0.3839 0.1832  -0.0424 229 LEU B O   
6005 C CB  . LEU B 229 ? 1.6322 1.0244 0.9396 -0.4596 0.1758  -0.0036 229 LEU B CB  
6006 C CG  . LEU B 229 ? 1.6126 0.9848 0.8587 -0.4991 0.1766  0.0064  229 LEU B CG  
6007 C CD1 . LEU B 229 ? 1.5711 1.0015 0.8703 -0.5272 0.1724  0.0340  229 LEU B CD1 
6008 C CD2 . LEU B 229 ? 1.5275 0.8924 0.7266 -0.5110 0.1819  0.0047  229 LEU B CD2 
6009 N N   . HIS B 230 ? 1.2956 0.6905 0.6748 -0.3766 0.1755  -0.0428 230 HIS B N   
6010 C CA  . HIS B 230 ? 1.3396 0.7682 0.7828 -0.3446 0.1759  -0.0550 230 HIS B CA  
6011 C C   . HIS B 230 ? 1.3902 0.7891 0.7892 -0.3138 0.1797  -0.0801 230 HIS B C   
6012 O O   . HIS B 230 ? 1.4401 0.8740 0.8736 -0.3023 0.1829  -0.0832 230 HIS B O   
6013 C CB  . HIS B 230 ? 1.4243 0.8583 0.9094 -0.3280 0.1713  -0.0628 230 HIS B CB  
6014 C CG  . HIS B 230 ? 1.5683 1.0374 1.1176 -0.2964 0.1722  -0.0789 230 HIS B CG  
6015 N ND1 . HIS B 230 ? 1.6545 1.1824 1.2960 -0.3002 0.1727  -0.0676 230 HIS B ND1 
6016 C CD2 . HIS B 230 ? 1.6729 1.1283 1.2070 -0.2609 0.1736  -0.1061 230 HIS B CD2 
6017 C CE1 . HIS B 230 ? 1.6974 1.2460 1.3787 -0.2709 0.1745  -0.0886 230 HIS B CE1 
6018 N NE2 . HIS B 230 ? 1.7321 1.2408 1.3500 -0.2462 0.1745  -0.1122 230 HIS B NE2 
6019 N N   . GLU B 231 ? 1.4579 0.7927 0.7802 -0.2996 0.1801  -0.0977 231 GLU B N   
6020 C CA  . GLU B 231 ? 1.5377 0.8394 0.8090 -0.2679 0.1842  -0.1211 231 GLU B CA  
6021 C C   . GLU B 231 ? 1.4492 0.7612 0.7011 -0.2808 0.1888  -0.1147 231 GLU B C   
6022 O O   . GLU B 231 ? 1.4923 0.8222 0.7543 -0.2570 0.1916  -0.1271 231 GLU B O   
6023 C CB  . GLU B 231 ? 1.8058 1.0276 0.9839 -0.2574 0.1863  -0.1351 231 GLU B CB  
6024 C CG  . GLU B 231 ? 2.0646 1.2467 1.1818 -0.2217 0.1917  -0.1585 231 GLU B CG  
6025 C CD  . GLU B 231 ? 2.3699 1.4722 1.3809 -0.2318 0.1981  -0.1618 231 GLU B CD  
6026 O OE1 . GLU B 231 ? 2.4466 1.4903 1.4031 -0.2195 0.2001  -0.1709 231 GLU B OE1 
6027 O OE2 . GLU B 231 ? 2.4423 1.5401 1.4240 -0.2522 0.2018  -0.1555 231 GLU B OE2 
6028 N N   . MET B 232 ? 1.4862 0.7908 0.7106 -0.3187 0.1895  -0.0958 232 MET B N   
6029 C CA  . MET B 232 ? 1.6407 0.9539 0.8402 -0.3336 0.1938  -0.0894 232 MET B CA  
6030 C C   . MET B 232 ? 1.6154 1.0052 0.9000 -0.3342 0.1941  -0.0765 232 MET B C   
6031 O O   . MET B 232 ? 1.5472 0.9516 0.8330 -0.3168 0.1977  -0.0856 232 MET B O   
6032 C CB  . MET B 232 ? 1.6583 0.9528 0.8126 -0.3761 0.1944  -0.0728 232 MET B CB  
6033 C CG  . MET B 232 ? 1.7128 1.0151 0.8350 -0.3937 0.1987  -0.0671 232 MET B CG  
6034 S SD  . MET B 232 ? 2.3772 1.7744 1.5903 -0.4136 0.1977  -0.0385 232 MET B SD  
6035 C CE  . MET B 232 ? 1.4083 0.8284 0.6484 -0.4520 0.1929  -0.0127 232 MET B CE  
6036 N N   . PHE B 233 ? 1.5138 0.9516 0.8687 -0.3538 0.1911  -0.0549 233 PHE B N   
6037 C CA  . PHE B 233 ? 1.3440 0.8514 0.7833 -0.3553 0.1931  -0.0402 233 PHE B CA  
6038 C C   . PHE B 233 ? 1.3496 0.8731 0.8240 -0.3188 0.1954  -0.0615 233 PHE B C   
6039 O O   . PHE B 233 ? 1.3409 0.9061 0.8531 -0.3151 0.1998  -0.0577 233 PHE B O   
6040 C CB  . PHE B 233 ? 1.2001 0.7475 0.7103 -0.3728 0.1903  -0.0180 233 PHE B CB  
6041 C CG  . PHE B 233 ? 1.2839 0.8392 0.7767 -0.4109 0.1890  0.0080  233 PHE B CG  
6042 C CD1 . PHE B 233 ? 1.2373 0.8121 0.7106 -0.4311 0.1925  0.0225  233 PHE B CD1 
6043 C CD2 . PHE B 233 ? 1.1817 0.7313 0.6804 -0.4261 0.1842  0.0178  233 PHE B CD2 
6044 C CE1 . PHE B 233 ? 1.2249 0.8147 0.6842 -0.4656 0.1912  0.0453  233 PHE B CE1 
6045 C CE2 . PHE B 233 ? 1.2304 0.7945 0.7154 -0.4605 0.1830  0.0408  233 PHE B CE2 
6046 C CZ  . PHE B 233 ? 1.3101 0.8951 0.7748 -0.4804 0.1865  0.0542  233 PHE B CZ  
6047 N N   . THR B 234 ? 1.3162 0.8095 0.7776 -0.2917 0.1926  -0.0843 234 THR B N   
6048 C CA  . THR B 234 ? 1.4234 0.9384 0.9208 -0.2566 0.1943  -0.1066 234 THR B CA  
6049 C C   . THR B 234 ? 1.5801 1.0902 1.0378 -0.2398 0.1989  -0.1202 234 THR B C   
6050 O O   . THR B 234 ? 1.5786 1.1384 1.0876 -0.2352 0.2029  -0.1190 234 THR B O   
6051 C CB  . THR B 234 ? 1.3924 0.8776 0.8769 -0.2284 0.1904  -0.1295 234 THR B CB  
6052 O OG1 . THR B 234 ? 1.4467 0.9454 0.9786 -0.2427 0.1862  -0.1174 234 THR B OG1 
6053 C CG2 . THR B 234 ? 1.2038 0.7207 0.7276 -0.1931 0.1923  -0.1537 234 THR B CG2 
6054 N N   . ASP B 235 ? 1.4050 1.2362 1.3645 0.0602  0.2555  0.2649  235 ASP B N   
6055 C CA  . ASP B 235 ? 1.5624 1.3971 1.4994 0.0597  0.2618  0.2647  235 ASP B CA  
6056 C C   . ASP B 235 ? 1.5192 1.3537 1.4770 0.0159  0.2407  0.2409  235 ASP B C   
6057 O O   . ASP B 235 ? 1.5656 1.4056 1.5063 0.0100  0.2396  0.2384  235 ASP B O   
6058 C CB  . ASP B 235 ? 1.6613 1.4592 1.5843 0.0914  0.3187  0.2799  235 ASP B CB  
6059 C CG  . ASP B 235 ? 1.7790 1.5286 1.7368 0.0713  0.3559  0.2672  235 ASP B CG  
6060 O OD1 . ASP B 235 ? 1.8626 1.5885 1.8467 0.0719  0.3749  0.2657  235 ASP B OD1 
6061 O OD2 . ASP B 235 ? 1.8071 1.5433 1.7665 0.0542  0.3674  0.2572  235 ASP B OD2 
6062 N N   . MET B 236 ? 1.3401 1.1711 1.3334 -0.0130 0.2233  0.2230  236 MET B N   
6063 C CA  . MET B 236 ? 1.2399 1.0782 1.2497 -0.0514 0.1973  0.1993  236 MET B CA  
6064 C C   . MET B 236 ? 1.2664 1.1411 1.2535 -0.0630 0.1458  0.1966  236 MET B C   
6065 O O   . MET B 236 ? 1.1673 1.0517 1.1461 -0.0842 0.1253  0.1850  236 MET B O   
6066 C CB  . MET B 236 ? 1.2540 1.0790 1.3105 -0.0761 0.2000  0.1776  236 MET B CB  
6067 C CG  . MET B 236 ? 1.4838 1.2705 1.5691 -0.0793 0.2522  0.1693  236 MET B CG  
6068 S SD  . MET B 236 ? 1.4509 1.2184 1.5271 -0.0892 0.2793  0.1629  236 MET B SD  
6069 C CE  . MET B 236 ? 0.9003 0.7052 0.9739 -0.1233 0.2212  0.1420  236 MET B CE  
6070 N N   . SER B 237 ? 1.3514 1.2434 1.3271 -0.0490 0.1273  0.2070  237 SER B N   
6071 C CA  . SER B 237 ? 1.2108 1.1329 1.1624 -0.0589 0.0836  0.2048  237 SER B CA  
6072 C C   . SER B 237 ? 1.2602 1.2023 1.1751 -0.0477 0.0823  0.2134  237 SER B C   
6073 O O   . SER B 237 ? 1.4243 1.3777 1.3251 -0.0680 0.0601  0.2034  237 SER B O   
6074 C CB  . SER B 237 ? 1.2243 1.1578 1.1738 -0.0463 0.0690  0.2133  237 SER B CB  
6075 O OG  . SER B 237 ? 1.2749 1.1935 1.2586 -0.0574 0.0676  0.2038  237 SER B OG  
6076 N N   . THR B 238 ? 1.3462 1.2941 1.2447 -0.0138 0.1068  0.2311  238 THR B N   
6077 C CA  . THR B 238 ? 1.5170 1.4917 1.3811 0.0006  0.1062  0.2375  238 THR B CA  
6078 C C   . THR B 238 ? 1.5994 1.5607 1.4611 -0.0108 0.1202  0.2315  238 THR B C   
6079 O O   . THR B 238 ? 1.4622 1.4459 1.2972 -0.0050 0.1169  0.2332  238 THR B O   
6080 C CB  . THR B 238 ? 1.5201 1.5061 1.3659 0.0455  0.1328  0.2573  238 THR B CB  
6081 O OG1 . THR B 238 ? 1.5521 1.5089 1.3981 0.0656  0.1761  0.2666  238 THR B OG1 
6082 C CG2 . THR B 238 ? 1.4432 1.4254 1.3020 0.0588  0.1324  0.2646  238 THR B CG2 
6083 N N   . LEU B 239 ? 1.8062 1.7332 1.6973 -0.0278 0.1361  0.2227  239 LEU B N   
6084 C CA  . LEU B 239 ? 1.9423 1.8514 1.8357 -0.0396 0.1538  0.2157  239 LEU B CA  
6085 C C   . LEU B 239 ? 1.8628 1.7847 1.7544 -0.0749 0.1175  0.1977  239 LEU B C   
6086 O O   . LEU B 239 ? 1.7530 1.6693 1.6382 -0.0855 0.1235  0.1919  239 LEU B O   
6087 C CB  . LEU B 239 ? 2.0843 1.9526 2.0125 -0.0451 0.1889  0.2100  239 LEU B CB  
6088 C CG  . LEU B 239 ? 2.1695 2.0093 2.0999 -0.0471 0.2251  0.2073  239 LEU B CG  
6089 C CD1 . LEU B 239 ? 2.1649 2.0093 2.1048 -0.0841 0.2019  0.1859  239 LEU B CD1 
6090 C CD2 . LEU B 239 ? 2.1882 2.0322 2.0796 -0.0113 0.2489  0.2282  239 LEU B CD2 
6091 N N   . VAL B 240 ? 1.9223 1.8584 1.8169 -0.0915 0.0813  0.1895  240 VAL B N   
6092 C CA  . VAL B 240 ? 1.9574 1.9030 1.8437 -0.1212 0.0463  0.1739  240 VAL B CA  
6093 C C   . VAL B 240 ? 2.0397 2.0148 1.8881 -0.1173 0.0261  0.1790  240 VAL B C   
6094 O O   . VAL B 240 ? 2.0598 2.0416 1.8921 -0.1379 0.0047  0.1689  240 VAL B O   
6095 C CB  . VAL B 240 ? 1.8508 1.7935 1.7549 -0.1387 0.0196  0.1622  240 VAL B CB  
6096 C CG1 . VAL B 240 ? 1.8317 1.7947 1.7109 -0.1348 -0.0075 0.1680  240 VAL B CG1 
6097 C CG2 . VAL B 240 ? 1.7942 1.7308 1.7056 -0.1677 0.0002  0.1421  240 VAL B CG2 
6098 N N   . ALA B 241 ? 2.1233 2.1175 1.9579 -0.0907 0.0343  0.1930  241 ALA B N   
6099 C CA  . ALA B 241 ? 2.2341 2.2630 2.0359 -0.0847 0.0212  0.1950  241 ALA B CA  
6100 C C   . ALA B 241 ? 2.3557 2.3886 2.1433 -0.0874 0.0314  0.1926  241 ALA B C   
6101 O O   . ALA B 241 ? 2.3311 2.3415 2.1307 -0.0807 0.0581  0.1963  241 ALA B O   
6102 C CB  . ALA B 241 ? 2.2251 2.2773 2.0174 -0.0496 0.0355  0.2095  241 ALA B CB  
6103 N N   . SER B 242 ? 2.4786 2.5388 2.2406 -0.0981 0.0121  0.1855  242 SER B N   
6104 C CA  . SER B 242 ? 2.5080 2.5743 2.2550 -0.1038 0.0177  0.1815  242 SER B CA  
6105 C C   . SER B 242 ? 2.4818 2.5115 2.2468 -0.1241 0.0231  0.1748  242 SER B C   
6106 O O   . SER B 242 ? 2.4932 2.5181 2.2526 -0.1223 0.0389  0.1753  242 SER B O   
6107 C CB  . SER B 242 ? 2.5317 2.6203 2.2649 -0.0677 0.0457  0.1943  242 SER B CB  
6108 O OG  . SER B 242 ? 2.5464 2.6095 2.2959 -0.0426 0.0770  0.2081  242 SER B OG  
6109 N N   . GLN B 243 ? 2.3783 2.3848 2.1646 -0.1424 0.0100  0.1671  243 GLN B N   
6110 C CA  . GLN B 243 ? 2.2723 2.2517 2.0773 -0.1646 0.0093  0.1552  243 GLN B CA  
6111 C C   . GLN B 243 ? 2.2888 2.2627 2.0953 -0.1890 -0.0242 0.1420  243 GLN B C   
6112 O O   . GLN B 243 ? 2.3466 2.3259 2.1526 -0.1856 -0.0380 0.1443  243 GLN B O   
6113 C CB  . GLN B 243 ? 2.1671 2.1211 2.0049 -0.1546 0.0399  0.1582  243 GLN B CB  
6114 C CG  . GLN B 243 ? 2.1113 2.0429 1.9748 -0.1792 0.0394  0.1409  243 GLN B CG  
6115 C CD  . GLN B 243 ? 2.1066 2.0132 2.0037 -0.1718 0.0760  0.1406  243 GLN B CD  
6116 O OE1 . GLN B 243 ? 2.0209 1.9163 1.9493 -0.1880 0.0735  0.1250  243 GLN B OE1 
6117 N NE2 . GLN B 243 ? 2.1255 2.0237 2.0150 -0.1461 0.1119  0.1567  243 GLN B NE2 
6118 N N   . GLY B 244 ? 2.2455 2.2084 2.0508 -0.2114 -0.0368 0.1284  244 GLY B N   
6119 C CA  . GLY B 244 ? 2.1963 2.1511 2.0005 -0.2304 -0.0662 0.1155  244 GLY B CA  
6120 C C   . GLY B 244 ? 2.0946 2.0581 1.8671 -0.2351 -0.0918 0.1165  244 GLY B C   
6121 O O   . GLY B 244 ? 2.0140 1.9877 1.7568 -0.2404 -0.0971 0.1170  244 GLY B O   
6122 N N   . GLU B 245 ? 2.0200 1.9785 1.7990 -0.2338 -0.1056 0.1155  245 GLU B N   
6123 C CA  . GLU B 245 ? 1.9178 1.8742 1.6665 -0.2415 -0.1303 0.1134  245 GLU B CA  
6124 C C   . GLU B 245 ? 1.7538 1.6934 1.4826 -0.2603 -0.1508 0.1002  245 GLU B C   
6125 O O   . GLU B 245 ? 1.5156 1.4427 1.2250 -0.2651 -0.1708 0.0962  245 GLU B O   
6126 C CB  . GLU B 245 ? 1.8822 1.8573 1.6028 -0.2377 -0.1279 0.1206  245 GLU B CB  
6127 C CG  . GLU B 245 ? 1.8733 1.8483 1.5603 -0.2548 -0.1359 0.1130  245 GLU B CG  
6128 C CD  . GLU B 245 ? 1.8255 1.8241 1.4874 -0.2539 -0.1339 0.1147  245 GLU B CD  
6129 O OE1 . GLU B 245 ? 1.7911 1.8028 1.4561 -0.2422 -0.1325 0.1205  245 GLU B OE1 
6130 O OE2 . GLU B 245 ? 1.7783 1.7847 1.4183 -0.2654 -0.1335 0.1085  245 GLU B OE2 
6131 N N   . MET B 246 ? 1.7036 1.6411 1.4356 -0.2686 -0.1443 0.0941  246 MET B N   
6132 C CA  . MET B 246 ? 1.4716 1.3950 1.1799 -0.2847 -0.1610 0.0826  246 MET B CA  
6133 C C   . MET B 246 ? 1.4485 1.3688 1.1827 -0.2904 -0.1548 0.0717  246 MET B C   
6134 O O   . MET B 246 ? 1.3338 1.2438 1.0543 -0.3013 -0.1697 0.0600  246 MET B O   
6135 C CB  . MET B 246 ? 1.2099 1.1366 0.8818 -0.2931 -0.1603 0.0851  246 MET B CB  
6136 C CG  . MET B 246 ? 1.3302 1.2363 0.9641 -0.3084 -0.1791 0.0760  246 MET B CG  
6137 S SD  . MET B 246 ? 1.4957 1.3802 1.1007 -0.3077 -0.2000 0.0749  246 MET B SD  
6138 C CE  . MET B 246 ? 0.9787 0.8682 0.5488 -0.3139 -0.1940 0.0803  246 MET B CE  
6139 N N   . ILE B 247 ? 1.4464 1.3743 1.2165 -0.2823 -0.1309 0.0750  247 ILE B N   
6140 C CA  . ILE B 247 ? 1.3907 1.3151 1.1874 -0.2890 -0.1181 0.0638  247 ILE B CA  
6141 C C   . ILE B 247 ? 1.2647 1.1869 1.0838 -0.2964 -0.1325 0.0445  247 ILE B C   
6142 O O   . ILE B 247 ? 1.2892 1.2100 1.1175 -0.3072 -0.1330 0.0297  247 ILE B O   
6143 C CB  . ILE B 247 ? 1.3440 1.2707 1.1706 -0.2773 -0.0831 0.0724  247 ILE B CB  
6144 C CG1 . ILE B 247 ? 1.3119 1.2310 1.1649 -0.2869 -0.0662 0.0590  247 ILE B CG1 
6145 C CG2 . ILE B 247 ? 1.2283 1.1570 1.0805 -0.2639 -0.0745 0.0779  247 ILE B CG2 
6146 C CD1 . ILE B 247 ? 1.2230 1.1367 1.0859 -0.2762 -0.0290 0.0701  247 ILE B CD1 
6147 N N   . ASP B 248 ? 1.0055 0.9307 0.8332 -0.2896 -0.1445 0.0432  248 ASP B N   
6148 C CA  . ASP B 248 ? 1.0793 1.0094 0.9250 -0.2936 -0.1613 0.0231  248 ASP B CA  
6149 C C   . ASP B 248 ? 1.0740 0.9982 0.8824 -0.3001 -0.1895 0.0136  248 ASP B C   
6150 O O   . ASP B 248 ? 1.0831 1.0149 0.9002 -0.3004 -0.2061 -0.0045 248 ASP B O   
6151 C CB  . ASP B 248 ? 1.2330 1.1688 1.0941 -0.2826 -0.1677 0.0248  248 ASP B CB  
6152 C CG  . ASP B 248 ? 1.3635 1.3140 1.2658 -0.2850 -0.1708 0.0013  248 ASP B CG  
6153 O OD1 . ASP B 248 ? 1.2994 1.2558 1.2309 -0.2950 -0.1562 -0.0143 248 ASP B OD1 
6154 O OD2 . ASP B 248 ? 1.4716 1.4295 1.3777 -0.2771 -0.1869 -0.0031 248 ASP B OD2 
6155 N N   . ARG B 249 ? 1.1451 1.0567 0.9108 -0.3039 -0.1940 0.0247  249 ARG B N   
6156 C CA  . ARG B 249 ? 1.0851 0.9841 0.8093 -0.3093 -0.2166 0.0177  249 ARG B CA  
6157 C C   . ARG B 249 ? 1.0350 0.9346 0.7628 -0.3206 -0.2117 0.0069  249 ARG B C   
6158 O O   . ARG B 249 ? 1.0871 0.9872 0.8198 -0.3259 -0.1923 0.0146  249 ARG B O   
6159 C CB  . ARG B 249 ? 1.1318 1.0142 0.8069 -0.3098 -0.2219 0.0328  249 ARG B CB  
6160 C CG  . ARG B 249 ? 1.2434 1.1154 0.8956 -0.3003 -0.2380 0.0367  249 ARG B CG  
6161 C CD  . ARG B 249 ? 1.3356 1.1947 0.9607 -0.2968 -0.2609 0.0241  249 ARG B CD  
6162 N NE  . ARG B 249 ? 1.3558 1.2123 0.9753 -0.2827 -0.2748 0.0240  249 ARG B NE  
6163 C CZ  . ARG B 249 ? 1.4519 1.2974 1.0421 -0.2728 -0.2950 0.0152  249 ARG B CZ  
6164 N NH1 . ARG B 249 ? 1.4712 1.3068 1.0350 -0.2755 -0.3037 0.0058  249 ARG B NH1 
6165 N NH2 . ARG B 249 ? 1.4267 1.2712 1.0115 -0.2579 -0.3063 0.0162  249 ARG B NH2 
6166 N N   . ILE B 250 ? 1.0635 0.9653 0.7889 -0.3222 -0.2288 -0.0114 250 ILE B N   
6167 C CA  . ILE B 250 ? 1.0978 1.0029 0.8316 -0.3329 -0.2243 -0.0245 250 ILE B CA  
6168 C C   . ILE B 250 ? 1.3136 1.2001 1.0045 -0.3404 -0.2229 -0.0128 250 ILE B C   
6169 O O   . ILE B 250 ? 1.3360 1.2238 1.0372 -0.3481 -0.2040 -0.0083 250 ILE B O   
6170 C CB  . ILE B 250 ? 1.0204 0.9354 0.7548 -0.3310 -0.2458 -0.0483 250 ILE B CB  
6171 C CG1 . ILE B 250 ? 1.0744 1.0148 0.8536 -0.3242 -0.2484 -0.0647 250 ILE B CG1 
6172 C CG2 . ILE B 250 ? 1.1414 1.0618 0.8880 -0.3430 -0.2390 -0.0625 250 ILE B CG2 
6173 C CD1 . ILE B 250 ? 0.9322 0.8918 0.7128 -0.3192 -0.2711 -0.0915 250 ILE B CD1 
6174 N N   . GLU B 251 ? 1.4293 1.2970 1.0707 -0.3375 -0.2411 -0.0082 251 GLU B N   
6175 C CA  . GLU B 251 ? 1.3338 1.1821 0.9313 -0.3461 -0.2393 0.0010  251 GLU B CA  
6176 C C   . GLU B 251 ? 1.3044 1.1609 0.9136 -0.3518 -0.2163 0.0145  251 GLU B C   
6177 O O   . GLU B 251 ? 1.2873 1.1403 0.8827 -0.3610 -0.2086 0.0160  251 GLU B O   
6178 C CB  . GLU B 251 ? 1.2746 1.0980 0.8201 -0.3415 -0.2533 0.0079  251 GLU B CB  
6179 C CG  . GLU B 251 ? 1.4788 1.2870 0.9942 -0.3330 -0.2750 -0.0037 251 GLU B CG  
6180 C CD  . GLU B 251 ? 1.7891 1.5598 1.2385 -0.3349 -0.2804 0.0025  251 GLU B CD  
6181 O OE1 . GLU B 251 ? 1.9685 1.7238 1.3940 -0.3373 -0.2738 0.0144  251 GLU B OE1 
6182 O OE2 . GLU B 251 ? 1.7701 1.5258 1.1908 -0.3341 -0.2894 -0.0057 251 GLU B OE2 
6183 N N   . PHE B 252 ? 1.3241 1.1932 0.9579 -0.3442 -0.2052 0.0239  252 PHE B N   
6184 C CA  . PHE B 252 ? 1.4650 1.3455 1.1057 -0.3441 -0.1840 0.0368  252 PHE B CA  
6185 C C   . PHE B 252 ? 1.4726 1.3621 1.1429 -0.3466 -0.1645 0.0341  252 PHE B C   
6186 O O   . PHE B 252 ? 1.6159 1.5086 1.2737 -0.3504 -0.1527 0.0400  252 PHE B O   
6187 C CB  . PHE B 252 ? 1.6773 1.5693 1.3352 -0.3320 -0.1760 0.0478  252 PHE B CB  
6188 C CG  . PHE B 252 ? 1.8898 1.7985 1.5566 -0.3262 -0.1531 0.0601  252 PHE B CG  
6189 C CD1 . PHE B 252 ? 1.8951 1.8094 1.5304 -0.3309 -0.1508 0.0653  252 PHE B CD1 
6190 C CD2 . PHE B 252 ? 2.0025 1.9219 1.7075 -0.3145 -0.1323 0.0653  252 PHE B CD2 
6191 C CE1 . PHE B 252 ? 1.8807 1.8172 1.5226 -0.3215 -0.1308 0.0749  252 PHE B CE1 
6192 C CE2 . PHE B 252 ? 2.0019 1.9363 1.7096 -0.3035 -0.1103 0.0776  252 PHE B CE2 
6193 C CZ  . PHE B 252 ? 1.9270 1.8730 1.6031 -0.3058 -0.1110 0.0822  252 PHE B CZ  
6194 N N   . SER B 253 ? 1.3392 1.2333 1.0485 -0.3448 -0.1595 0.0238  253 SER B N   
6195 C CA  . SER B 253 ? 1.3487 1.2464 1.0865 -0.3485 -0.1372 0.0194  253 SER B CA  
6196 C C   . SER B 253 ? 1.3464 1.2365 1.0615 -0.3606 -0.1420 0.0128  253 SER B C   
6197 O O   . SER B 253 ? 1.3573 1.2478 1.0648 -0.3619 -0.1254 0.0212  253 SER B O   
6198 C CB  . SER B 253 ? 1.3476 1.2510 1.1314 -0.3489 -0.1311 0.0034  253 SER B CB  
6199 O OG  . SER B 253 ? 1.2417 1.1438 1.0522 -0.3543 -0.1053 -0.0025 253 SER B OG  
6200 N N   . VAL B 254 ? 1.2824 1.1665 0.9841 -0.3672 -0.1648 -0.0018 254 VAL B N   
6201 C CA  . VAL B 254 ? 1.2501 1.1260 0.9315 -0.3779 -0.1702 -0.0098 254 VAL B CA  
6202 C C   . VAL B 254 ? 1.2939 1.1592 0.9297 -0.3824 -0.1723 0.0026  254 VAL B C   
6203 O O   . VAL B 254 ? 1.2874 1.1453 0.9059 -0.3912 -0.1731 -0.0015 254 VAL B O   
6204 C CB  . VAL B 254 ? 1.2339 1.1088 0.9122 -0.3799 -0.1939 -0.0303 254 VAL B CB  
6205 C CG1 . VAL B 254 ? 1.3019 1.1769 0.9707 -0.3693 -0.2133 -0.0310 254 VAL B CG1 
6206 C CG2 . VAL B 254 ? 0.9480 0.8083 0.5863 -0.3873 -0.2062 -0.0342 254 VAL B CG2 
6207 N N   . GLU B 255 ? 1.4448 1.3112 1.0631 -0.3772 -0.1719 0.0160  255 GLU B N   
6208 C CA  . GLU B 255 ? 1.5227 1.3858 1.1041 -0.3829 -0.1694 0.0247  255 GLU B CA  
6209 C C   . GLU B 255 ? 1.4664 1.3464 1.0618 -0.3807 -0.1453 0.0332  255 GLU B C   
6210 O O   . GLU B 255 ? 1.5056 1.3864 1.0779 -0.3878 -0.1413 0.0348  255 GLU B O   
6211 C CB  . GLU B 255 ? 1.7043 1.5661 1.2633 -0.3794 -0.1761 0.0323  255 GLU B CB  
6212 C CG  . GLU B 255 ? 1.8907 1.7575 1.4188 -0.3866 -0.1691 0.0379  255 GLU B CG  
6213 C CD  . GLU B 255 ? 1.9785 1.8613 1.5060 -0.3798 -0.1638 0.0460  255 GLU B CD  
6214 O OE1 . GLU B 255 ? 2.0178 1.9075 1.5711 -0.3678 -0.1633 0.0504  255 GLU B OE1 
6215 O OE2 . GLU B 255 ? 1.9642 1.8549 1.4666 -0.3870 -0.1595 0.0463  255 GLU B OE2 
6216 N N   . GLN B 256 ? 1.3671 1.2595 0.9985 -0.3691 -0.1278 0.0387  256 GLN B N   
6217 C CA  . GLN B 256 ? 1.5027 1.4085 1.1439 -0.3612 -0.1020 0.0484  256 GLN B CA  
6218 C C   . GLN B 256 ? 1.5605 1.4582 1.2227 -0.3649 -0.0866 0.0423  256 GLN B C   
6219 O O   . GLN B 256 ? 1.6563 1.5577 1.3393 -0.3539 -0.0603 0.0494  256 GLN B O   
6220 C CB  . GLN B 256 ? 1.5426 1.4629 1.2036 -0.3428 -0.0862 0.0604  256 GLN B CB  
6221 C CG  . GLN B 256 ? 1.5865 1.4996 1.2810 -0.3383 -0.0863 0.0562  256 GLN B CG  
6222 C CD  . GLN B 256 ? 1.6347 1.5590 1.3464 -0.3191 -0.0690 0.0691  256 GLN B CD  
6223 O OE1 . GLN B 256 ? 1.6596 1.5991 1.3595 -0.3061 -0.0549 0.0814  256 GLN B OE1 
6224 N NE2 . GLN B 256 ? 1.7238 1.6430 1.4631 -0.3155 -0.0698 0.0655  256 GLN B NE2 
6225 N N   . SER B 257 ? 1.4583 1.3431 1.1123 -0.3794 -0.1014 0.0289  257 SER B N   
6226 C CA  . SER B 257 ? 1.4391 1.3165 1.1117 -0.3860 -0.0887 0.0196  257 SER B CA  
6227 C C   . SER B 257 ? 1.6068 1.4849 1.2580 -0.3883 -0.0766 0.0264  257 SER B C   
6228 O O   . SER B 257 ? 1.6908 1.5753 1.3098 -0.3893 -0.0848 0.0331  257 SER B O   
6229 C CB  . SER B 257 ? 1.3255 1.1937 0.9968 -0.3983 -0.1116 0.0006  257 SER B CB  
6230 O OG  . SER B 257 ? 1.2872 1.1570 0.9605 -0.3946 -0.1312 -0.0040 257 SER B OG  
6231 N N   . HIS B 258 ? 1.6662 1.5378 1.3352 -0.3900 -0.0559 0.0230  258 HIS B N   
6232 C CA  . HIS B 258 ? 1.8362 1.7084 1.4855 -0.3902 -0.0425 0.0299  258 HIS B CA  
6233 C C   . HIS B 258 ? 2.0275 1.8872 1.6662 -0.4073 -0.0544 0.0163  258 HIS B C   
6234 O O   . HIS B 258 ? 2.0230 1.8764 1.6615 -0.4174 -0.0774 0.0023  258 HIS B O   
6235 C CB  . HIS B 258 ? 1.8687 1.7393 1.5366 -0.3758 -0.0058 0.0399  258 HIS B CB  
6236 C CG  . HIS B 258 ? 1.9471 1.8297 1.5886 -0.3642 0.0082  0.0545  258 HIS B CG  
6237 N ND1 . HIS B 258 ? 1.9968 1.8766 1.6183 -0.3730 0.0078  0.0521  258 HIS B ND1 
6238 C CD2 . HIS B 258 ? 2.0186 1.9205 1.6502 -0.3427 0.0222  0.0703  258 HIS B CD2 
6239 C CE1 . HIS B 258 ? 2.0665 1.9643 1.6677 -0.3578 0.0211  0.0653  258 HIS B CE1 
6240 N NE2 . HIS B 258 ? 2.0813 1.9945 1.6879 -0.3384 0.0298  0.0760  258 HIS B NE2 
6241 N N   . ASN B 259 ? 2.2273 2.0847 1.8554 -0.4081 -0.0385 0.0207  259 ASN B N   
6242 C CA  . ASN B 259 ? 2.4252 2.2715 2.0392 -0.4235 -0.0491 0.0095  259 ASN B CA  
6243 C C   . ASN B 259 ? 2.6954 2.5392 2.3012 -0.4215 -0.0259 0.0165  259 ASN B C   
6244 O O   . ASN B 259 ? 2.6826 2.5307 2.2969 -0.4063 0.0017  0.0290  259 ASN B O   
6245 C CB  . ASN B 259 ? 2.3243 2.1702 1.9013 -0.4318 -0.0781 0.0076  259 ASN B CB  
6246 C CG  . ASN B 259 ? 2.2941 2.1248 1.8589 -0.4460 -0.0957 -0.0075 259 ASN B CG  
6247 O OD1 . ASN B 259 ? 2.4257 2.2512 2.0155 -0.4505 -0.0928 -0.0208 259 ASN B OD1 
6248 N ND2 . ASN B 259 ? 2.1366 1.9603 1.6625 -0.4530 -0.1126 -0.0071 259 ASN B ND2 
6249 N N   . TYR B 260 ? 2.9492 2.7845 2.5361 -0.4347 -0.0366 0.0087  260 TYR B N   
6250 C CA  . TYR B 260 ? 3.0723 2.9063 2.6433 -0.4340 -0.0197 0.0155  260 TYR B CA  
6251 C C   . TYR B 260 ? 2.9862 2.8069 2.5822 -0.4313 0.0109  0.0138  260 TYR B C   
6252 O O   . TYR B 260 ? 2.9819 2.8003 2.5656 -0.4257 0.0309  0.0224  260 TYR B O   
6253 C CB  . TYR B 260 ? 3.2590 3.1143 2.8079 -0.4197 -0.0113 0.0324  260 TYR B CB  
6254 C CG  . TYR B 260 ? 3.4342 3.2945 2.9600 -0.4185 0.0002  0.0383  260 TYR B CG  
6255 C CD1 . TYR B 260 ? 3.4966 3.3641 3.0244 -0.3993 0.0308  0.0512  260 TYR B CD1 
6256 C CD2 . TYR B 260 ? 3.5161 3.3725 3.0152 -0.4346 -0.0182 0.0312  260 TYR B CD2 
6257 C CE1 . TYR B 260 ? 3.5522 3.4268 3.0575 -0.3959 0.0412  0.0565  260 TYR B CE1 
6258 C CE2 . TYR B 260 ? 3.5701 3.4328 3.0489 -0.4338 -0.0077 0.0358  260 TYR B CE2 
6259 C CZ  . TYR B 260 ? 3.5766 3.4503 3.0593 -0.4143 0.0212  0.0482  260 TYR B CZ  
6260 O OH  . TYR B 260 ? 3.5757 3.4579 3.0369 -0.4114 0.0314  0.0527  260 TYR B OH  
6261 N N   . VAL B 261 ? 2.8994 2.7114 2.5300 -0.4355 0.0161  0.0013  261 VAL B N   
6262 C CA  . VAL B 261 ? 2.8956 2.6913 2.5525 -0.4358 0.0494  -0.0035 261 VAL B CA  
6263 C C   . VAL B 261 ? 2.9327 2.7259 2.5894 -0.4133 0.0851  0.0171  261 VAL B C   
6264 O O   . VAL B 261 ? 2.9592 2.7562 2.5889 -0.4011 0.0968  0.0327  261 VAL B O   
6265 C CB  . VAL B 261 ? 2.8650 2.6486 2.5104 -0.4479 0.0540  -0.0108 261 VAL B CB  
6266 C CG1 . VAL B 261 ? 2.8518 2.6148 2.5220 -0.4480 0.0943  -0.0151 261 VAL B CG1 
6267 C CG2 . VAL B 261 ? 2.8373 2.6227 2.4815 -0.4669 0.0204  -0.0320 261 VAL B CG2 
# 
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   HIS 1   0   0   HIS HIS A . n 
A 1 2   MET 2   1   1   MET MET A . n 
A 1 3   SER 3   2   2   SER SER A . n 
A 1 4   LEU 4   3   3   LEU LEU A . n 
A 1 5   LYS 5   4   4   LYS LYS A . n 
A 1 6   SER 6   5   5   SER SER A . n 
A 1 7   ALA 7   6   6   ALA ALA A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   LYS 9   8   8   LYS LYS A . n 
A 1 10  THR 10  9   9   THR THR A . n 
A 1 11  VAL 11  10  10  VAL VAL A . n 
A 1 12  LEU 12  11  11  LEU LEU A . n 
A 1 13  THR 13  12  12  THR THR A . n 
A 1 14  ASN 14  13  13  ASN ASN A . n 
A 1 15  SER 15  14  14  SER SER A . n 
A 1 16  LEU 16  15  15  LEU LEU A . n 
A 1 17  ARG 17  16  16  ARG ARG A . n 
A 1 18  SER 18  17  17  SER SER A . n 
A 1 19  VAL 19  18  18  VAL VAL A . n 
A 1 20  ALA 20  19  19  ALA ALA A . n 
A 1 21  ASP 21  20  20  ASP ASP A . n 
A 1 22  GLY 22  21  21  GLY GLY A . n 
A 1 23  GLY 23  22  22  GLY GLY A . n 
A 1 24  ASP 24  23  23  ASP ASP A . n 
A 1 25  TRP 25  24  24  TRP TRP A . n 
A 1 26  LYS 26  25  25  LYS LYS A . n 
A 1 27  VAL 27  26  26  VAL VAL A . n 
A 1 28  LEU 28  27  27  LEU LEU A . n 
A 1 29  VAL 29  28  28  VAL VAL A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  ASP 31  30  30  ASP ASP A . n 
A 1 32  LYS 32  31  31  LYS LYS A . n 
A 1 33  PRO 33  32  32  PRO PRO A . n 
A 1 34  ALA 34  33  33  ALA ALA A . n 
A 1 35  LEU 35  34  34  LEU LEU A . n 
A 1 36  ARG 36  35  35  ARG ARG A . n 
A 1 37  MET 37  36  36  MET MET A . n 
A 1 38  ILE 38  37  37  ILE ILE A . n 
A 1 39  SER 39  38  38  SER SER A . n 
A 1 40  GLU 40  39  39  GLU GLU A . n 
A 1 41  CYS 41  40  40  CYS CYS A . n 
A 1 42  ALA 42  41  41  ALA ALA A . n 
A 1 43  ARG 43  42  42  ARG ARG A . n 
A 1 44  MET 44  43  43  MET MET A . n 
A 1 45  SER 45  44  44  SER SER A . n 
A 1 46  GLU 46  45  45  GLU GLU A . n 
A 1 47  ILE 47  46  46  ILE ILE A . n 
A 1 48  LEU 48  47  47  LEU LEU A . n 
A 1 49  ASP 49  48  48  ASP ASP A . n 
A 1 50  LEU 50  49  49  LEU LEU A . n 
A 1 51  GLY 51  50  50  GLY GLY A . n 
A 1 52  VAL 52  51  51  VAL VAL A . n 
A 1 53  THR 53  52  52  THR THR A . n 
A 1 54  VAL 54  53  53  VAL VAL A . n 
A 1 55  VAL 55  54  54  VAL VAL A . n 
A 1 56  GLU 56  55  55  GLU GLU A . n 
A 1 57  ASP 57  56  56  ASP ASP A . n 
A 1 58  VAL 58  57  57  VAL VAL A . n 
A 1 59  SER 59  58  58  SER SER A . n 
A 1 60  LYS 60  59  59  LYS LYS A . n 
A 1 61  GLN 61  60  60  GLN GLN A . n 
A 1 62  ARG 62  61  61  ARG ARG A . n 
A 1 63  LYS 63  62  62  LYS LYS A . n 
A 1 64  VAL 64  63  63  VAL VAL A . n 
A 1 65  LEU 65  64  64  LEU LEU A . n 
A 1 66  PRO 66  65  65  PRO PRO A . n 
A 1 67  GLN 67  66  66  GLN GLN A . n 
A 1 68  PHE 68  67  67  PHE PHE A . n 
A 1 69  HIS 69  68  68  HIS HIS A . n 
A 1 70  GLY 70  69  69  GLY GLY A . n 
A 1 71  VAL 71  70  70  VAL VAL A . n 
A 1 72  TYR 72  71  71  TYR TYR A . n 
A 1 73  PHE 73  72  72  PHE PHE A . n 
A 1 74  ILE 74  73  73  ILE ILE A . n 
A 1 75  GLU 75  74  74  GLU GLU A . n 
A 1 76  PRO 76  75  75  PRO PRO A . n 
A 1 77  THR 77  76  76  THR THR A . n 
A 1 78  GLU 78  77  77  GLU GLU A . n 
A 1 79  GLU 79  78  78  GLU GLU A . n 
A 1 80  ASN 80  79  79  ASN ASN A . n 
A 1 81  LEU 81  80  80  LEU LEU A . n 
A 1 82  ASP 82  81  81  ASP ASP A . n 
A 1 83  TYR 83  82  82  TYR TYR A . n 
A 1 84  VAL 84  83  83  VAL VAL A . n 
A 1 85  ILE 85  84  84  ILE ILE A . n 
A 1 86  ARG 86  85  85  ARG ARG A . n 
A 1 87  ASP 87  86  86  ASP ASP A . n 
A 1 88  PHE 88  87  87  PHE PHE A . n 
A 1 89  ALA 89  88  88  ALA ALA A . n 
A 1 90  ASP 90  89  89  ASP ASP A . n 
A 1 91  ARG 91  90  90  ARG ARG A . n 
A 1 92  THR 92  91  91  THR THR A . n 
A 1 93  PRO 93  92  92  PRO PRO A . n 
A 1 94  THR 94  93  93  THR THR A . n 
A 1 95  TYR 95  94  94  TYR TYR A . n 
A 1 96  GLU 96  95  95  GLU GLU A . n 
A 1 97  ALA 97  96  96  ALA ALA A . n 
A 1 98  ALA 98  97  97  ALA ALA A . n 
A 1 99  HIS 99  98  98  HIS HIS A . n 
A 1 100 LEU 100 99  99  LEU LEU A . n 
A 1 101 PHE 101 100 100 PHE PHE A . n 
A 1 102 PHE 102 101 101 PHE PHE A . n 
A 1 103 LEU 103 102 102 LEU LEU A . n 
A 1 104 SER 104 103 103 SER SER A . n 
A 1 105 PRO 105 104 104 PRO PRO A . n 
A 1 106 VAL 106 105 105 VAL VAL A . n 
A 1 107 PRO 107 106 106 PRO PRO A . n 
A 1 108 ASP 108 107 107 ASP ASP A . n 
A 1 109 ALA 109 108 108 ALA ALA A . n 
A 1 110 LEU 110 109 109 LEU LEU A . n 
A 1 111 MET 111 110 110 MET MET A . n 
A 1 112 ALA 112 111 111 ALA ALA A . n 
A 1 113 LYS 113 112 112 LYS LYS A . n 
A 1 114 LEU 114 113 113 LEU LEU A . n 
A 1 115 ALA 115 114 114 ALA ALA A . n 
A 1 116 SER 116 115 115 SER SER A . n 
A 1 117 ALA 117 116 116 ALA ALA A . n 
A 1 118 LYS 118 117 117 LYS LYS A . n 
A 1 119 ALA 119 118 118 ALA ALA A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 LYS 121 120 120 LYS LYS A . n 
A 1 122 TYR 122 121 121 TYR TYR A . n 
A 1 123 VAL 123 122 122 VAL VAL A . n 
A 1 124 LYS 124 123 123 LYS LYS A . n 
A 1 125 THR 125 124 124 THR THR A . n 
A 1 126 LEU 126 125 125 LEU LEU A . n 
A 1 127 LYS 127 126 126 LYS LYS A . n 
A 1 128 GLU 128 127 127 GLU GLU A . n 
A 1 129 ILE 129 128 128 ILE ILE A . n 
A 1 130 ASN 130 129 129 ASN ASN A . n 
A 1 131 THR 131 130 130 THR THR A . n 
A 1 132 LEU 132 131 131 LEU LEU A . n 
A 1 133 PHE 133 132 132 PHE PHE A . n 
A 1 134 ILE 134 133 133 ILE ILE A . n 
A 1 135 PRO 135 134 134 PRO PRO A . n 
A 1 136 LYS 136 135 135 LYS LYS A . n 
A 1 137 GLU 137 136 136 GLU GLU A . n 
A 1 138 HIS 138 137 137 HIS HIS A . n 
A 1 139 ARG 139 138 138 ARG ARG A . n 
A 1 140 VAL 140 139 139 VAL VAL A . n 
A 1 141 PHE 141 140 140 PHE PHE A . n 
A 1 142 THR 142 141 141 THR THR A . n 
A 1 143 LEU 143 142 142 LEU LEU A . n 
A 1 144 ASN 144 143 143 ASN ASN A . n 
A 1 145 GLU 145 144 144 GLU GLU A . n 
A 1 146 PRO 146 145 145 PRO PRO A . n 
A 1 147 HIS 147 146 146 HIS HIS A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 LEU 149 148 148 LEU LEU A . n 
A 1 150 VAL 150 149 149 VAL VAL A . n 
A 1 151 GLN 151 150 150 GLN GLN A . n 
A 1 152 TYR 152 151 151 TYR TYR A . n 
A 1 153 TYR 153 152 152 TYR TYR A . n 
A 1 154 GLY 154 153 153 GLY GLY A . n 
A 1 155 SER 155 154 154 SER SER A . n 
A 1 156 ARG 156 155 155 ARG ARG A . n 
A 1 157 SER 157 156 156 SER SER A . n 
A 1 158 SER 158 157 157 SER SER A . n 
A 1 159 SER 159 158 158 SER SER A . n 
A 1 160 TYR 160 159 159 TYR TYR A . n 
A 1 161 ASN 161 160 160 ASN ASN A . n 
A 1 162 ILE 162 161 161 ILE ILE A . n 
A 1 163 ASP 163 162 162 ASP ASP A . n 
A 1 164 HIS 164 163 163 HIS HIS A . n 
A 1 165 LEU 165 164 164 LEU LEU A . n 
A 1 166 VAL 166 165 165 VAL VAL A . n 
A 1 167 ARG 167 166 166 ARG ARG A . n 
A 1 168 ARG 168 167 167 ARG ARG A . n 
A 1 169 LEU 169 168 168 LEU LEU A . n 
A 1 170 SER 170 169 169 SER SER A . n 
A 1 171 THR 171 170 170 THR THR A . n 
A 1 172 LEU 172 171 171 LEU LEU A . n 
A 1 173 CYS 173 172 172 CYS CYS A . n 
A 1 174 THR 174 173 173 THR THR A . n 
A 1 175 THR 175 174 174 THR THR A . n 
A 1 176 MET 176 175 175 MET MET A . n 
A 1 177 ASN 177 176 176 ASN ASN A . n 
A 1 178 VAL 178 177 177 VAL VAL A . n 
A 1 179 ALA 179 178 178 ALA ALA A . n 
A 1 180 PRO 180 179 179 PRO PRO A . n 
A 1 181 ILE 181 180 180 ILE ILE A . n 
A 1 182 VAL 182 181 181 VAL VAL A . n 
A 1 183 ARG 183 182 182 ARG ARG A . n 
A 1 184 TYR 184 183 183 TYR TYR A . n 
A 1 185 SER 185 184 184 SER SER A . n 
A 1 186 SER 186 185 185 SER SER A . n 
A 1 187 THR 187 186 186 THR THR A . n 
A 1 188 SER 188 187 187 SER SER A . n 
A 1 189 THR 189 188 188 THR THR A . n 
A 1 190 PRO 190 189 189 PRO PRO A . n 
A 1 191 GLY 191 190 190 GLY GLY A . n 
A 1 192 THR 192 191 191 THR THR A . n 
A 1 193 GLU 193 192 192 GLU GLU A . n 
A 1 194 ARG 194 193 193 ARG ARG A . n 
A 1 195 MET 195 194 194 MET MET A . n 
A 1 196 ALA 196 195 195 ALA ALA A . n 
A 1 197 MET 197 196 196 MET MET A . n 
A 1 198 GLN 198 197 197 GLN GLN A . n 
A 1 199 LEU 199 198 198 LEU LEU A . n 
A 1 200 GLN 200 199 199 GLN GLN A . n 
A 1 201 LYS 201 200 200 LYS LYS A . n 
A 1 202 GLU 202 201 201 GLU GLU A . n 
A 1 203 ILE 203 202 202 ILE ILE A . n 
A 1 204 ASP 204 203 203 ASP ASP A . n 
A 1 205 MET 205 204 204 MET MET A . n 
A 1 206 SER 206 205 205 SER SER A . n 
A 1 207 VAL 207 206 206 VAL VAL A . n 
A 1 208 SER 208 207 207 SER SER A . n 
A 1 209 GLN 209 208 208 GLN GLN A . n 
A 1 210 GLY 210 209 209 GLY GLY A . n 
A 1 211 LEU 211 210 210 LEU LEU A . n 
A 1 212 ILE 212 211 211 ILE ILE A . n 
A 1 213 ASN 213 212 212 ASN ASN A . n 
A 1 214 ALA 214 213 213 ALA ALA A . n 
A 1 215 ARG 215 214 214 ARG ARG A . n 
A 1 216 GLU 216 215 215 GLU GLU A . n 
A 1 217 GLY 217 216 216 GLY GLY A . n 
A 1 218 LYS 218 217 217 LYS LYS A . n 
A 1 219 LEU 219 218 218 LEU LEU A . n 
A 1 220 LYS 220 219 219 LYS LYS A . n 
A 1 221 SER 221 220 220 SER SER A . n 
A 1 222 GLN 222 221 221 GLN GLN A . n 
A 1 223 PHE 223 222 222 PHE PHE A . n 
A 1 224 LEU 224 223 223 LEU LEU A . n 
A 1 225 ILE 225 224 224 ILE ILE A . n 
A 1 226 LEU 226 225 225 LEU LEU A . n 
A 1 227 ASP 227 226 226 ASP ASP A . n 
A 1 228 ARG 228 227 227 ARG ARG A . n 
A 1 229 ALA 229 228 228 ALA ALA A . n 
A 1 230 VAL 230 229 229 VAL VAL A . n 
A 1 231 ASP 231 230 230 ASP ASP A . n 
A 1 232 LEU 232 231 231 LEU LEU A . n 
A 1 233 LYS 233 232 232 LYS LYS A . n 
A 1 234 SER 234 233 233 SER SER A . n 
A 1 235 PRO 235 234 234 PRO PRO A . n 
A 1 236 LEU 236 235 235 LEU LEU A . n 
A 1 237 VAL 237 236 236 VAL VAL A . n 
A 1 238 HIS 238 237 237 HIS HIS A . n 
A 1 239 GLU 239 238 238 GLU GLU A . n 
A 1 240 LEU 240 239 239 LEU LEU A . n 
A 1 241 THR 241 240 240 THR THR A . n 
A 1 242 TYR 242 241 241 TYR TYR A . n 
A 1 243 GLN 243 242 242 GLN GLN A . n 
A 1 244 ALA 244 243 243 ALA ALA A . n 
A 1 245 ALA 245 244 244 ALA ALA A . n 
A 1 246 ALA 246 245 245 ALA ALA A . n 
A 1 247 TYR 247 246 246 TYR TYR A . n 
A 1 248 ASP 248 247 247 ASP ASP A . n 
A 1 249 LEU 249 248 248 LEU LEU A . n 
A 1 250 LEU 250 249 249 LEU LEU A . n 
A 1 251 ASN 251 250 250 ASN ASN A . n 
A 1 252 ILE 252 251 251 ILE ILE A . n 
A 1 253 GLU 253 252 252 GLU GLU A . n 
A 1 254 ASN 254 253 253 ASN ASN A . n 
A 1 255 ASP 255 254 254 ASP ASP A . n 
A 1 256 ILE 256 255 255 ILE ILE A . n 
A 1 257 TYR 257 256 256 TYR TYR A . n 
A 1 258 SER 258 257 257 SER SER A . n 
A 1 259 TYR 259 258 258 TYR TYR A . n 
A 1 260 SER 260 259 259 SER SER A . n 
A 1 261 THR 261 260 260 THR THR A . n 
A 1 262 VAL 262 261 261 VAL VAL A . n 
A 1 263 ASP 263 262 262 ASP ASP A . n 
A 1 264 ALA 264 263 263 ALA ALA A . n 
A 1 265 GLY 265 264 264 GLY GLY A . n 
A 1 266 GLY 266 265 265 GLY GLY A . n 
A 1 267 ARG 267 266 266 ARG ARG A . n 
A 1 268 GLU 268 267 267 GLU GLU A . n 
A 1 269 GLN 269 268 268 GLN GLN A . n 
A 1 270 GLN 270 269 269 GLN GLN A . n 
A 1 271 ARG 271 270 270 ARG ARG A . n 
A 1 272 GLN 272 271 271 GLN GLN A . n 
A 1 273 VAL 273 272 272 VAL VAL A . n 
A 1 274 VAL 274 273 273 VAL VAL A . n 
A 1 275 LEU 275 274 274 LEU LEU A . n 
A 1 276 GLY 276 275 275 GLY GLY A . n 
A 1 277 GLU 277 276 276 GLU GLU A . n 
A 1 278 ASP 278 277 277 ASP ASP A . n 
A 1 279 ASP 279 278 278 ASP ASP A . n 
A 1 280 ASP 280 279 279 ASP ASP A . n 
A 1 281 ILE 281 280 280 ILE ILE A . n 
A 1 282 TRP 282 281 281 TRP TRP A . n 
A 1 283 LEU 283 282 282 LEU LEU A . n 
A 1 284 GLN 284 283 283 GLN GLN A . n 
A 1 285 MET 285 284 284 MET MET A . n 
A 1 286 ARG 286 285 285 ARG ARG A . n 
A 1 287 HIS 287 286 286 HIS HIS A . n 
A 1 288 LEU 288 287 287 LEU LEU A . n 
A 1 289 HIS 289 288 288 HIS HIS A . n 
A 1 290 ILE 290 289 289 ILE ILE A . n 
A 1 291 SER 291 290 290 SER SER A . n 
A 1 292 GLU 292 291 291 GLU GLU A . n 
A 1 293 VAL 293 292 292 VAL VAL A . n 
A 1 294 PHE 294 293 293 PHE PHE A . n 
A 1 295 ARG 295 294 294 ARG ARG A . n 
A 1 296 LYS 296 295 295 LYS LYS A . n 
A 1 297 VAL 297 296 296 VAL VAL A . n 
A 1 298 LYS 298 297 297 LYS LYS A . n 
A 1 299 SER 299 298 298 SER SER A . n 
A 1 300 SER 300 299 299 SER SER A . n 
A 1 301 PHE 301 300 300 PHE PHE A . n 
A 1 302 ASP 302 301 301 ASP ASP A . n 
A 1 303 GLU 303 302 302 GLU GLU A . n 
A 1 304 PHE 304 303 303 PHE PHE A . n 
A 1 305 CYS 305 304 304 CYS CYS A . n 
A 1 306 VAL 306 305 305 VAL VAL A . n 
A 1 307 SER 307 306 306 SER SER A . n 
A 1 308 ALA 308 307 307 ALA ALA A . n 
A 1 309 ARG 309 308 308 ARG ARG A . n 
A 1 310 ARG 310 309 309 ARG ARG A . n 
A 1 311 LEU 311 310 310 LEU LEU A . n 
A 1 312 GLN 312 311 311 GLN GLN A . n 
A 1 313 GLY 313 312 312 GLY GLY A . n 
A 1 314 LEU 314 313 313 LEU LEU A . n 
A 1 315 ARG 315 314 314 ARG ARG A . n 
A 1 316 ASP 316 315 315 ASP ASP A . n 
A 1 317 SER 317 316 316 SER SER A . n 
A 1 318 GLN 318 317 317 GLN GLN A . n 
A 1 319 GLN 319 318 318 GLN GLN A . n 
A 1 320 GLY 320 319 319 GLY GLY A . n 
A 1 321 GLU 321 320 320 GLU GLU A . n 
A 1 322 GLY 322 321 321 GLY GLY A . n 
A 1 323 GLY 323 322 322 GLY GLY A . n 
A 1 324 ALA 324 323 323 ALA ALA A . n 
A 1 325 GLY 325 324 324 GLY GLY A . n 
A 1 326 ALA 326 325 325 ALA ALA A . n 
A 1 327 LEU 327 326 326 LEU LEU A . n 
A 1 328 LYS 328 327 327 LYS LYS A . n 
A 1 329 GLN 329 328 328 GLN GLN A . n 
A 1 330 MET 330 329 329 MET MET A . n 
A 1 331 LEU 331 330 330 LEU LEU A . n 
A 1 332 LYS 332 331 331 LYS LYS A . n 
A 1 333 ASP 333 332 332 ASP ASP A . n 
A 1 334 LEU 334 333 333 LEU LEU A . n 
A 1 335 PRO 335 334 334 PRO PRO A . n 
A 1 336 GLN 336 335 335 GLN GLN A . n 
A 1 337 HIS 337 336 336 HIS HIS A . n 
A 1 338 ARG 338 337 337 ARG ARG A . n 
A 1 339 GLU 339 338 338 GLU GLU A . n 
A 1 340 GLN 340 339 339 GLN GLN A . n 
A 1 341 MET 341 340 340 MET MET A . n 
A 1 342 GLN 342 341 341 GLN GLN A . n 
A 1 343 LYS 343 342 342 LYS LYS A . n 
A 1 344 TYR 344 343 343 TYR TYR A . n 
A 1 345 SER 345 344 344 SER SER A . n 
A 1 346 LEU 346 345 345 LEU LEU A . n 
A 1 347 HIS 347 346 346 HIS HIS A . n 
A 1 348 LEU 348 347 347 LEU LEU A . n 
A 1 349 ASP 349 348 348 ASP ASP A . n 
A 1 350 MET 350 349 349 MET MET A . n 
A 1 351 SER 351 350 350 SER SER A . n 
A 1 352 ASN 352 351 351 ASN ASN A . n 
A 1 353 ALA 353 352 352 ALA ALA A . n 
A 1 354 ILE 354 353 353 ILE ILE A . n 
A 1 355 ASN 355 354 354 ASN ASN A . n 
A 1 356 MET 356 355 355 MET MET A . n 
A 1 357 ALA 357 356 356 ALA ALA A . n 
A 1 358 PHE 358 357 357 PHE PHE A . n 
A 1 359 SER 359 358 358 SER SER A . n 
A 1 360 SER 360 359 359 SER SER A . n 
A 1 361 THR 361 360 360 THR THR A . n 
A 1 362 ILE 362 361 361 ILE ILE A . n 
A 1 363 ASP 363 362 362 ASP ASP A . n 
A 1 364 SER 364 363 363 SER SER A . n 
A 1 365 CYS 365 364 364 CYS CYS A . n 
A 1 366 THR 366 365 365 THR THR A . n 
A 1 367 LYS 367 366 366 LYS LYS A . n 
A 1 368 ALA 368 367 367 ALA ALA A . n 
A 1 369 GLU 369 368 368 GLU GLU A . n 
A 1 370 GLN 370 369 369 GLN GLN A . n 
A 1 371 ASN 371 370 370 ASN ASN A . n 
A 1 372 ILE 372 371 371 ILE ILE A . n 
A 1 373 VAL 373 372 372 VAL VAL A . n 
A 1 374 THR 374 373 373 THR THR A . n 
A 1 375 GLU 375 374 374 GLU GLU A . n 
A 1 376 GLU 376 375 375 GLU GLU A . n 
A 1 377 GLU 377 376 376 GLU GLU A . n 
A 1 378 GLN 378 377 377 GLN GLN A . n 
A 1 379 ASP 379 378 378 ASP ASP A . n 
A 1 380 GLY 380 379 379 GLY GLY A . n 
A 1 381 ASN 381 380 380 ASN ASN A . n 
A 1 382 LYS 382 381 381 LYS LYS A . n 
A 1 383 VAL 383 382 382 VAL VAL A . n 
A 1 384 ARG 384 383 383 ARG ARG A . n 
A 1 385 ASP 385 384 384 ASP ASP A . n 
A 1 386 PHE 386 385 385 PHE PHE A . n 
A 1 387 ILE 387 386 386 ILE ILE A . n 
A 1 388 GLY 388 387 387 GLY GLY A . n 
A 1 389 GLU 389 388 388 GLU GLU A . n 
A 1 390 VAL 390 389 389 VAL VAL A . n 
A 1 391 ALA 391 390 390 ALA ALA A . n 
A 1 392 SER 392 391 391 SER SER A . n 
A 1 393 VAL 393 392 392 VAL VAL A . n 
A 1 394 VAL 394 393 393 VAL VAL A . n 
A 1 395 VAL 395 394 394 VAL VAL A . n 
A 1 396 ASP 396 395 395 ASP ASP A . n 
A 1 397 ARG 397 396 396 ARG ARG A . n 
A 1 398 ARG 398 397 397 ARG ARG A . n 
A 1 399 VAL 399 398 398 VAL VAL A . n 
A 1 400 SER 400 399 399 SER SER A . n 
A 1 401 THR 401 400 400 THR THR A . n 
A 1 402 GLU 402 401 401 GLU GLU A . n 
A 1 403 ASP 403 402 402 ASP ASP A . n 
A 1 404 LYS 404 403 403 LYS LYS A . n 
A 1 405 LEU 405 404 404 LEU LEU A . n 
A 1 406 ARG 406 405 405 ARG ARG A . n 
A 1 407 CYS 407 406 406 CYS CYS A . n 
A 1 408 LEU 408 407 407 LEU LEU A . n 
A 1 409 MET 409 408 408 MET MET A . n 
A 1 410 LEU 410 409 409 LEU LEU A . n 
A 1 411 CYS 411 410 410 CYS CYS A . n 
A 1 412 VAL 412 411 411 VAL VAL A . n 
A 1 413 LEU 413 412 412 LEU LEU A . n 
A 1 414 ALA 414 413 413 ALA ALA A . n 
A 1 415 LYS 415 414 414 LYS LYS A . n 
A 1 416 ASN 416 415 415 ASN ASN A . n 
A 1 417 GLY 417 416 416 GLY GLY A . n 
A 1 418 THR 418 417 417 THR THR A . n 
A 1 419 SER 419 418 418 SER SER A . n 
A 1 420 SER 420 419 419 SER SER A . n 
A 1 421 HIS 421 420 420 HIS HIS A . n 
A 1 422 GLU 422 421 421 GLU GLU A . n 
A 1 423 LEU 423 422 422 LEU LEU A . n 
A 1 424 ASN 424 423 423 ASN ASN A . n 
A 1 425 ASN 425 424 424 ASN ASN A . n 
A 1 426 LEU 426 425 425 LEU LEU A . n 
A 1 427 LEU 427 426 426 LEU LEU A . n 
A 1 428 ASP 428 427 427 ASP ASP A . n 
A 1 429 ASN 429 428 428 ASN ASN A . n 
A 1 430 ALA 430 429 429 ALA ALA A . n 
A 1 431 ASN 431 430 430 ASN ASN A . n 
A 1 432 ILE 432 431 431 ILE ILE A . n 
A 1 433 ALA 433 432 432 ALA ALA A . n 
A 1 434 THR 434 433 433 THR THR A . n 
A 1 435 PRO 435 434 434 PRO PRO A . n 
A 1 436 SER 436 435 435 SER SER A . n 
A 1 437 ARG 437 436 436 ARG ARG A . n 
A 1 438 SER 438 437 437 SER SER A . n 
A 1 439 ALA 439 438 438 ALA ALA A . n 
A 1 440 ILE 440 439 439 ILE ILE A . n 
A 1 441 TYR 441 440 440 TYR TYR A . n 
A 1 442 ASN 442 441 441 ASN ASN A . n 
A 1 443 LEU 443 442 442 LEU LEU A . n 
A 1 444 GLU 444 443 443 GLU GLU A . n 
A 1 445 MET 445 444 444 MET MET A . n 
A 1 446 LEU 446 445 445 LEU LEU A . n 
A 1 447 GLY 447 446 446 GLY GLY A . n 
A 1 448 ALA 448 447 447 ALA ALA A . n 
A 1 449 THR 449 448 448 THR THR A . n 
A 1 450 VAL 450 449 449 VAL VAL A . n 
A 1 451 VAL 451 450 450 VAL VAL A . n 
A 1 452 ALA 452 451 451 ALA ALA A . n 
A 1 453 ASP 453 452 452 ASP ASP A . n 
A 1 454 ARG 454 453 453 ARG ARG A . n 
A 1 455 ARG 455 454 454 ARG ARG A . n 
A 1 456 GLY 456 455 455 GLY GLY A . n 
A 1 457 ARG 457 456 456 ARG ARG A . n 
A 1 458 LYS 458 457 457 LYS LYS A . n 
A 1 459 PRO 459 458 458 PRO PRO A . n 
A 1 460 LYS 460 459 459 LYS LYS A . n 
A 1 461 THR 461 460 460 THR THR A . n 
A 1 462 MET 462 461 461 MET MET A . n 
A 1 463 LYS 463 462 462 LYS LYS A . n 
A 1 464 ARG 464 463 463 ARG ARG A . n 
A 1 465 ILE 465 464 464 ILE ILE A . n 
A 1 466 GLU 466 465 465 GLU GLU A . n 
A 1 467 ARG 467 466 466 ARG ARG A . n 
A 1 468 ASP 468 467 467 ASP ASP A . n 
A 1 469 MET 469 468 468 MET MET A . n 
A 1 470 PRO 470 469 469 PRO PRO A . n 
A 1 471 TYR 471 470 470 TYR TYR A . n 
A 1 472 VAL 472 471 471 VAL VAL A . n 
A 1 473 LEU 473 472 472 LEU LEU A . n 
A 1 474 SER 474 473 473 SER SER A . n 
A 1 475 ARG 475 474 474 ARG ARG A . n 
A 1 476 TRP 476 475 475 TRP TRP A . n 
A 1 477 THR 477 476 476 THR THR A . n 
A 1 478 PRO 478 477 477 PRO PRO A . n 
A 1 479 ILE 479 478 478 ILE ILE A . n 
A 1 480 VAL 480 479 479 VAL VAL A . n 
A 1 481 LYS 481 480 480 LYS LYS A . n 
A 1 482 ASP 482 481 481 ASP ASP A . n 
A 1 483 LEU 483 482 482 LEU LEU A . n 
A 1 484 MET 484 483 483 MET MET A . n 
A 1 485 GLU 485 484 484 GLU GLU A . n 
A 1 486 TYR 486 485 485 TYR TYR A . n 
A 1 487 ILE 487 486 486 ILE ILE A . n 
A 1 488 ALA 488 487 487 ALA ALA A . n 
A 1 489 THR 489 488 488 THR THR A . n 
A 1 490 GLY 490 489 489 GLY GLY A . n 
A 1 491 GLN 491 490 490 GLN GLN A . n 
A 1 492 LEU 492 491 491 LEU LEU A . n 
A 1 493 ASP 493 492 492 ASP ASP A . n 
A 1 494 LEU 494 493 493 LEU LEU A . n 
A 1 495 GLU 495 494 494 GLU GLU A . n 
A 1 496 SER 496 495 495 SER SER A . n 
A 1 497 TYR 497 496 496 TYR TYR A . n 
A 1 498 PRO 498 497 497 PRO PRO A . n 
A 1 499 ALA 499 498 498 ALA ALA A . n 
A 1 500 VAL 500 499 499 VAL VAL A . n 
A 1 501 ARG 501 500 500 ARG ARG A . n 
A 1 502 ASP 502 501 501 ASP ASP A . n 
A 1 503 GLY 503 502 502 GLY GLY A . n 
A 1 504 PRO 504 503 503 PRO PRO A . n 
A 1 505 SER 505 504 504 SER SER A . n 
A 1 506 VAL 506 505 505 VAL VAL A . n 
A 1 507 VAL 507 506 506 VAL VAL A . n 
A 1 508 GLN 508 507 507 GLN GLN A . n 
A 1 509 PRO 509 508 508 PRO PRO A . n 
A 1 510 LYS 510 509 509 LYS LYS A . n 
A 1 511 ARG 511 510 ?   ?   ?   A . n 
A 1 512 ALA 512 511 ?   ?   ?   A . n 
A 1 513 SER 513 512 ?   ?   ?   A . n 
A 1 514 LYS 514 513 ?   ?   ?   A . n 
A 1 515 SER 515 514 ?   ?   ?   A . n 
A 1 516 VAL 516 515 ?   ?   ?   A . n 
A 1 517 GLU 517 516 ?   ?   ?   A . n 
A 1 518 GLU 518 517 ?   ?   ?   A . n 
A 1 519 ASP 519 518 ?   ?   ?   A . n 
A 1 520 ASP 520 519 ?   ?   ?   A . n 
A 1 521 ASP 521 520 ?   ?   ?   A . n 
A 1 522 GLY 522 521 ?   ?   ?   A . n 
A 1 523 PRO 523 522 ?   ?   ?   A . n 
A 1 524 ALA 524 523 ?   ?   ?   A . n 
A 1 525 THR 525 524 ?   ?   ?   A . n 
A 1 526 SER 526 525 ?   ?   ?   A . n 
A 1 527 ALA 527 526 ?   ?   ?   A . n 
A 1 528 ARG 528 527 ?   ?   ?   A . n 
A 1 529 LYS 529 528 ?   ?   ?   A . n 
A 1 530 ARG 530 529 ?   ?   ?   A . n 
A 1 531 GLY 531 530 ?   ?   ?   A . n 
A 1 532 ASN 532 531 ?   ?   ?   A . n 
A 1 533 TRP 533 532 ?   ?   ?   A . n 
A 1 534 ALA 534 533 ?   ?   ?   A . n 
A 1 535 LYS 535 534 ?   ?   ?   A . n 
A 1 536 ASN 536 535 ?   ?   ?   A . n 
A 1 537 LYS 537 536 ?   ?   ?   A . n 
A 1 538 GLY 538 537 ?   ?   ?   A . n 
A 1 539 ASN 539 538 ?   ?   ?   A . n 
A 1 540 ASN 540 539 ?   ?   ?   A . n 
A 1 541 ARG 541 540 ?   ?   ?   A . n 
A 1 542 SER 542 541 ?   ?   ?   A . n 
A 1 543 LEU 543 542 ?   ?   ?   A . n 
A 1 544 PRO 544 543 ?   ?   ?   A . n 
A 1 545 SER 545 544 ?   ?   ?   A . n 
A 1 546 THR 546 545 ?   ?   ?   A . n 
A 1 547 PRO 547 546 ?   ?   ?   A . n 
A 1 548 SER 548 547 ?   ?   ?   A . n 
A 1 549 GLY 549 548 ?   ?   ?   A . n 
A 1 550 VAL 550 549 ?   ?   ?   A . n 
A 1 551 ALA 551 550 ?   ?   ?   A . n 
A 1 552 VAL 552 551 ?   ?   ?   A . n 
A 1 553 SER 553 552 ?   ?   ?   A . n 
A 1 554 GLY 554 553 ?   ?   ?   A . n 
A 1 555 ASN 555 554 ?   ?   ?   A . n 
A 1 556 GLY 556 555 ?   ?   ?   A . n 
A 1 557 ALA 557 556 ?   ?   ?   A . n 
A 1 558 ALA 558 557 ?   ?   ?   A . n 
A 1 559 GLY 559 558 ?   ?   ?   A . n 
A 1 560 ALA 560 559 ?   ?   ?   A . n 
A 1 561 ALA 561 560 ?   ?   ?   A . n 
A 1 562 GLU 562 561 561 GLU GLU A . n 
A 1 563 SER 563 562 562 SER SER A . n 
A 1 564 ALA 564 563 563 ALA ALA A . n 
A 1 565 LYS 565 564 564 LYS LYS A . n 
A 1 566 PRO 566 565 565 PRO PRO A . n 
A 1 567 LYS 567 566 566 LYS LYS A . n 
A 1 568 LEU 568 567 567 LEU LEU A . n 
A 1 569 PHE 569 568 568 PHE PHE A . n 
A 1 570 VAL 570 569 569 VAL VAL A . n 
A 1 571 PHE 571 570 570 PHE PHE A . n 
A 1 572 ILE 572 571 571 ILE ILE A . n 
A 1 573 ASN 573 572 572 ASN ASN A . n 
A 1 574 GLY 574 573 573 GLY GLY A . n 
A 1 575 THR 575 574 574 THR THR A . n 
A 1 576 VAL 576 575 575 VAL VAL A . n 
A 1 577 SER 577 576 576 SER SER A . n 
A 1 578 TYR 578 577 577 TYR TYR A . n 
A 1 579 ASN 579 578 578 ASN ASN A . n 
A 1 580 GLU 580 579 579 GLU GLU A . n 
A 1 581 ILE 581 580 580 ILE ILE A . n 
A 1 582 ARG 582 581 581 ARG ARG A . n 
A 1 583 CYS 583 582 582 CYS CYS A . n 
A 1 584 ALA 584 583 583 ALA ALA A . n 
A 1 585 TYR 585 584 584 TYR TYR A . n 
A 1 586 GLU 586 585 585 GLU GLU A . n 
A 1 587 VAL 587 586 586 VAL VAL A . n 
A 1 588 SER 588 587 587 SER SER A . n 
A 1 589 GLN 589 588 588 GLN GLN A . n 
A 1 590 SER 590 589 589 SER SER A . n 
A 1 591 SER 591 590 590 SER SER A . n 
A 1 592 GLY 592 591 591 GLY GLY A . n 
A 1 593 TYR 593 592 592 TYR TYR A . n 
A 1 594 GLU 594 593 593 GLU GLU A . n 
A 1 595 VAL 595 594 594 VAL VAL A . n 
A 1 596 TYR 596 595 595 TYR TYR A . n 
A 1 597 ILE 597 596 596 ILE ILE A . n 
A 1 598 GLY 598 597 597 GLY GLY A . n 
A 1 599 ALA 599 598 598 ALA ALA A . n 
A 1 600 HIS 600 599 599 HIS HIS A . n 
A 1 601 ASN 601 600 600 ASN ASN A . n 
A 1 602 ILE 602 601 601 ILE ILE A . n 
A 1 603 ALA 603 602 602 ALA ALA A . n 
A 1 604 THR 604 603 603 THR THR A . n 
A 1 605 PRO 605 604 604 PRO PRO A . n 
A 1 606 ALA 606 605 605 ALA ALA A . n 
A 1 607 GLU 607 606 606 GLU GLU A . n 
A 1 608 PHE 608 607 607 PHE PHE A . n 
A 1 609 VAL 609 608 608 VAL VAL A . n 
A 1 610 GLU 610 609 609 GLU GLU A . n 
A 1 611 LEU 611 610 610 LEU LEU A . n 
A 1 612 VAL 612 611 611 VAL VAL A . n 
A 1 613 SER 613 612 612 SER SER A . n 
A 1 614 LEU 614 613 613 LEU LEU A . n 
A 1 615 LEU 615 614 614 LEU LEU A . n 
A 1 616 ASP 616 615 615 ASP ASP A . n 
A 1 617 LYS 617 616 616 LYS LYS A . n 
A 1 618 ALA 618 617 617 ALA ALA A . n 
A 1 619 ASP 619 618 ?   ?   ?   A . n 
A 1 620 GLN 620 619 ?   ?   ?   A . n 
A 1 621 ASP 621 620 ?   ?   ?   A . n 
A 1 622 VAL 622 621 ?   ?   ?   A . n 
A 1 623 GLN 623 622 ?   ?   ?   A . n 
A 1 624 VAL 624 623 ?   ?   ?   A . n 
A 1 625 LEU 625 624 ?   ?   ?   A . n 
A 1 626 THR 626 625 ?   ?   ?   A . n 
A 1 627 GLN 627 626 ?   ?   ?   A . n 
A 1 628 GLY 628 627 ?   ?   ?   A . n 
A 1 629 GLN 629 628 ?   ?   ?   A . n 
A 1 630 GLY 630 629 ?   ?   ?   A . n 
A 1 631 ASP 631 630 ?   ?   ?   A . n 
A 1 632 GLY 632 631 ?   ?   ?   A . n 
A 1 633 GLY 633 632 ?   ?   ?   A . n 
A 1 634 LEU 634 633 ?   ?   ?   A . n 
A 1 635 VAL 635 634 ?   ?   ?   A . n 
A 1 636 ILE 636 635 ?   ?   ?   A . n 
A 1 637 THR 637 636 ?   ?   ?   A . n 
A 1 638 THR 638 637 ?   ?   ?   A . n 
A 1 639 GLY 639 638 ?   ?   ?   A . n 
A 1 640 SER 640 639 ?   ?   ?   A . n 
A 1 641 ALA 641 640 ?   ?   ?   A . n 
A 1 642 GLN 642 641 ?   ?   ?   A . n 
A 1 643 ALA 643 642 ?   ?   ?   A . n 
A 1 644 GLY 644 643 ?   ?   ?   A . n 
A 1 645 LEU 645 644 ?   ?   ?   A . n 
A 1 646 ASN 646 645 ?   ?   ?   A . n 
A 1 647 LEU 647 646 ?   ?   ?   A . n 
A 1 648 ALA 648 647 ?   ?   ?   A . n 
A 1 649 GLU 649 648 ?   ?   ?   A . n 
A 1 650 VAL 650 649 ?   ?   ?   A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   ASP 2   2   2   ASP ASP B . n 
B 2 3   ARG 3   3   3   ARG ARG B . n 
B 2 4   LEU 4   4   4   LEU LEU B . n 
B 2 5   SER 5   5   5   SER SER B . n 
B 2 6   ARG 6   6   6   ARG ARG B . n 
B 2 7   LEU 7   7   7   LEU LEU B . n 
B 2 8   ARG 8   8   8   ARG ARG B . n 
B 2 9   GLN 9   9   9   GLN GLN B . n 
B 2 10  MET 10  10  10  MET MET B . n 
B 2 11  ALA 11  11  11  ALA ALA B . n 
B 2 12  ALA 12  12  12  ALA ALA B . n 
B 2 13  GLU 13  13  13  GLU GLU B . n 
B 2 14  ASN 14  14  14  ASN ASN B . n 
B 2 15  GLN 15  15  15  GLN GLN B . n 
B 2 16  PRO 16  16  ?   ?   ?   B . n 
B 2 17  ALA 17  17  ?   ?   ?   B . n 
B 2 18  GLU 18  18  ?   ?   ?   B . n 
B 2 19  ALA 19  19  ?   ?   ?   B . n 
B 2 20  SER 20  20  ?   ?   ?   B . n 
B 2 21  ASP 21  21  ?   ?   ?   B . n 
B 2 22  ALA 22  22  ?   ?   ?   B . n 
B 2 23  ALA 23  23  ?   ?   ?   B . n 
B 2 24  GLY 24  24  ?   ?   ?   B . n 
B 2 25  GLY 25  25  ?   ?   ?   B . n 
B 2 26  ALA 26  26  ?   ?   ?   B . n 
B 2 27  GLU 27  27  ?   ?   ?   B . n 
B 2 28  ALA 28  28  ?   ?   ?   B . n 
B 2 29  GLN 29  29  ?   ?   ?   B . n 
B 2 30  ILE 30  30  ?   ?   ?   B . n 
B 2 31  GLU 31  31  ?   ?   ?   B . n 
B 2 32  GLU 32  32  ?   ?   ?   B . n 
B 2 33  THR 33  33  ?   ?   ?   B . n 
B 2 34  SER 34  34  ?   ?   ?   B . n 
B 2 35  LEU 35  35  ?   ?   ?   B . n 
B 2 36  SER 36  36  ?   ?   ?   B . n 
B 2 37  ALA 37  37  ?   ?   ?   B . n 
B 2 38  GLN 38  38  ?   ?   ?   B . n 
B 2 39  PRO 39  39  39  PRO PRO B . n 
B 2 40  GLU 40  40  40  GLU GLU B . n 
B 2 41  PRO 41  41  41  PRO PRO B . n 
B 2 42  PHE 42  42  42  PHE PHE B . n 
B 2 43  MET 43  43  43  MET MET B . n 
B 2 44  ALA 44  44  44  ALA ALA B . n 
B 2 45  ASP 45  45  45  ASP ASP B . n 
B 2 46  PHE 46  46  46  PHE PHE B . n 
B 2 47  PHE 47  47  47  PHE PHE B . n 
B 2 48  ASN 48  48  48  ASN ASN B . n 
B 2 49  ARG 49  49  49  ARG ARG B . n 
B 2 50  VAL 50  50  50  VAL VAL B . n 
B 2 51  LYS 51  51  51  LYS LYS B . n 
B 2 52  ARG 52  52  52  ARG ARG B . n 
B 2 53  ILE 53  53  53  ILE ILE B . n 
B 2 54  ARG 54  54  54  ARG ARG B . n 
B 2 55  ASP 55  55  55  ASP ASP B . n 
B 2 56  ASN 56  56  56  ASN ASN B . n 
B 2 57  ILE 57  57  57  ILE ILE B . n 
B 2 58  GLU 58  58  58  GLU GLU B . n 
B 2 59  ASP 59  59  59  ASP ASP B . n 
B 2 60  ILE 60  60  60  ILE ILE B . n 
B 2 61  GLU 61  61  61  GLU GLU B . n 
B 2 62  GLN 62  62  62  GLN GLN B . n 
B 2 63  ALA 63  63  63  ALA ALA B . n 
B 2 64  ILE 64  64  64  ILE ILE B . n 
B 2 65  GLU 65  65  65  GLU GLU B . n 
B 2 66  GLN 66  66  66  GLN GLN B . n 
B 2 67  VAL 67  67  67  VAL VAL B . n 
B 2 68  ALA 68  68  68  ALA ALA B . n 
B 2 69  GLN 69  69  69  GLN GLN B . n 
B 2 70  LEU 70  70  70  LEU LEU B . n 
B 2 71  HIS 71  71  71  HIS HIS B . n 
B 2 72  THR 72  72  72  THR THR B . n 
B 2 73  GLU 73  73  73  GLU GLU B . n 
B 2 74  SER 74  74  74  SER SER B . n 
B 2 75  LEU 75  75  75  LEU LEU B . n 
B 2 76  VAL 76  76  76  VAL VAL B . n 
B 2 77  ALA 77  77  77  ALA ALA B . n 
B 2 78  VAL 78  78  78  VAL VAL B . n 
B 2 79  SER 79  79  79  SER SER B . n 
B 2 80  LYS 80  80  80  LYS LYS B . n 
B 2 81  GLU 81  81  81  GLU GLU B . n 
B 2 82  ASP 82  82  82  ASP ASP B . n 
B 2 83  ARG 83  83  83  ARG ARG B . n 
B 2 84  ASP 84  84  84  ASP ASP B . n 
B 2 85  ARG 85  85  85  ARG ARG B . n 
B 2 86  LEU 86  86  86  LEU LEU B . n 
B 2 87  ASN 87  87  87  ASN ASN B . n 
B 2 88  GLU 88  88  88  GLU GLU B . n 
B 2 89  LYS 89  89  89  LYS LYS B . n 
B 2 90  LEU 90  90  90  LEU LEU B . n 
B 2 91  GLN 91  91  91  GLN GLN B . n 
B 2 92  ASP 92  92  92  ASP ASP B . n 
B 2 93  THR 93  93  93  THR THR B . n 
B 2 94  MET 94  94  94  MET MET B . n 
B 2 95  ALA 95  95  95  ALA ALA B . n 
B 2 96  ARG 96  96  96  ARG ARG B . n 
B 2 97  ILE 97  97  97  ILE ILE B . n 
B 2 98  SER 98  98  98  SER SER B . n 
B 2 99  ALA 99  99  99  ALA ALA B . n 
B 2 100 LEU 100 100 100 LEU LEU B . n 
B 2 101 GLY 101 101 101 GLY GLY B . n 
B 2 102 ASN 102 102 102 ASN ASN B . n 
B 2 103 LYS 103 103 103 LYS LYS B . n 
B 2 104 ILE 104 104 104 ILE ILE B . n 
B 2 105 ARG 105 105 105 ARG ARG B . n 
B 2 106 ALA 106 106 106 ALA ALA B . n 
B 2 107 ASP 107 107 107 ASP ASP B . n 
B 2 108 LEU 108 108 108 LEU LEU B . n 
B 2 109 LYS 109 109 109 LYS LYS B . n 
B 2 110 GLN 110 110 110 GLN GLN B . n 
B 2 111 ILE 111 111 111 ILE ILE B . n 
B 2 112 GLU 112 112 112 GLU GLU B . n 
B 2 113 LYS 113 113 113 LYS LYS B . n 
B 2 114 GLU 114 114 114 GLU GLU B . n 
B 2 115 ASN 115 115 115 ASN ASN B . n 
B 2 116 LYS 116 116 116 LYS LYS B . n 
B 2 117 ARG 117 117 117 ARG ARG B . n 
B 2 118 ALA 118 118 118 ALA ALA B . n 
B 2 119 GLN 119 119 119 GLN GLN B . n 
B 2 120 GLN 120 120 120 GLN GLN B . n 
B 2 121 GLU 121 121 121 GLU GLU B . n 
B 2 122 GLY 122 122 122 GLY GLY B . n 
B 2 123 THR 123 123 123 THR THR B . n 
B 2 124 PHE 124 124 124 PHE PHE B . n 
B 2 125 GLU 125 125 125 GLU GLU B . n 
B 2 126 ASP 126 126 126 ASP ASP B . n 
B 2 127 GLY 127 127 127 GLY GLY B . n 
B 2 128 THR 128 128 128 THR THR B . n 
B 2 129 VAL 129 129 129 VAL VAL B . n 
B 2 130 SER 130 130 130 SER SER B . n 
B 2 131 THR 131 131 131 THR THR B . n 
B 2 132 ASP 132 132 132 ASP ASP B . n 
B 2 133 LEU 133 133 133 LEU LEU B . n 
B 2 134 ARG 134 134 134 ARG ARG B . n 
B 2 135 ILE 135 135 135 ILE ILE B . n 
B 2 136 ARG 136 136 136 ARG ARG B . n 
B 2 137 GLN 137 137 137 GLN GLN B . n 
B 2 138 SER 138 138 138 SER SER B . n 
B 2 139 GLN 139 139 139 GLN GLN B . n 
B 2 140 HIS 140 140 140 HIS HIS B . n 
B 2 141 SER 141 141 141 SER SER B . n 
B 2 142 SER 142 142 142 SER SER B . n 
B 2 143 LEU 143 143 143 LEU LEU B . n 
B 2 144 SER 144 144 144 SER SER B . n 
B 2 145 ARG 145 145 145 ARG ARG B . n 
B 2 146 LYS 146 146 146 LYS LYS B . n 
B 2 147 PHE 147 147 147 PHE PHE B . n 
B 2 148 VAL 148 148 148 VAL VAL B . n 
B 2 149 LYS 149 149 149 LYS LYS B . n 
B 2 150 VAL 150 150 150 VAL VAL B . n 
B 2 151 MET 151 151 151 MET MET B . n 
B 2 152 THR 152 152 152 THR THR B . n 
B 2 153 ARG 153 153 153 ARG ARG B . n 
B 2 154 TYR 154 154 154 TYR TYR B . n 
B 2 155 ASN 155 155 155 ASN ASN B . n 
B 2 156 ASP 156 156 156 ASP ASP B . n 
B 2 157 VAL 157 157 157 VAL VAL B . n 
B 2 158 GLN 158 158 158 GLN GLN B . n 
B 2 159 ALA 159 159 159 ALA ALA B . n 
B 2 160 GLU 160 160 160 GLU GLU B . n 
B 2 161 ASN 161 161 161 ASN ASN B . n 
B 2 162 LYS 162 162 162 LYS LYS B . n 
B 2 163 ARG 163 163 163 ARG ARG B . n 
B 2 164 ARG 164 164 164 ARG ARG B . n 
B 2 165 TYR 165 165 165 TYR TYR B . n 
B 2 166 GLY 166 166 166 GLY GLY B . n 
B 2 167 GLU 167 167 167 GLU GLU B . n 
B 2 168 ASN 168 168 168 ASN ASN B . n 
B 2 169 VAL 169 169 169 VAL VAL B . n 
B 2 170 ALA 170 170 170 ALA ALA B . n 
B 2 171 ARG 171 171 171 ARG ARG B . n 
B 2 172 GLN 172 172 172 GLN GLN B . n 
B 2 173 CYS 173 173 173 CYS CYS B . n 
B 2 174 ARG 174 174 174 ARG ARG B . n 
B 2 175 VAL 175 175 175 VAL VAL B . n 
B 2 176 VAL 176 176 176 VAL VAL B . n 
B 2 177 GLU 177 177 177 GLU GLU B . n 
B 2 178 PRO 178 178 178 PRO PRO B . n 
B 2 179 SER 179 179 179 SER SER B . n 
B 2 180 LEU 180 180 180 LEU LEU B . n 
B 2 181 SER 181 181 181 SER SER B . n 
B 2 182 ASP 182 182 182 ASP ASP B . n 
B 2 183 ASP 183 183 183 ASP ASP B . n 
B 2 184 ALA 184 184 184 ALA ALA B . n 
B 2 185 ILE 185 185 185 ILE ILE B . n 
B 2 186 GLN 186 186 186 GLN GLN B . n 
B 2 187 LYS 187 187 187 LYS LYS B . n 
B 2 188 VAL 188 188 188 VAL VAL B . n 
B 2 189 ILE 189 189 189 ILE ILE B . n 
B 2 190 GLU 190 190 190 GLU GLU B . n 
B 2 191 HIS 191 191 191 HIS HIS B . n 
B 2 192 GLY 192 192 192 GLY GLY B . n 
B 2 193 THR 193 193 ?   ?   ?   B . n 
B 2 194 GLU 194 194 ?   ?   ?   B . n 
B 2 195 GLY 195 195 ?   ?   ?   B . n 
B 2 196 ILE 196 196 ?   ?   ?   B . n 
B 2 197 PHE 197 197 ?   ?   ?   B . n 
B 2 198 SER 198 198 ?   ?   ?   B . n 
B 2 199 GLY 199 199 ?   ?   ?   B . n 
B 2 200 MET 200 200 ?   ?   ?   B . n 
B 2 201 ARG 201 201 ?   ?   ?   B . n 
B 2 202 LEU 202 202 ?   ?   ?   B . n 
B 2 203 GLU 203 203 ?   ?   ?   B . n 
B 2 204 GLY 204 204 ?   ?   ?   B . n 
B 2 205 ALA 205 205 ?   ?   ?   B . n 
B 2 206 GLU 206 206 ?   ?   ?   B . n 
B 2 207 ALA 207 207 ?   ?   ?   B . n 
B 2 208 LYS 208 208 ?   ?   ?   B . n 
B 2 209 LEU 209 209 ?   ?   ?   B . n 
B 2 210 ASN 210 210 210 ASN ASN B . n 
B 2 211 GLU 211 211 211 GLU GLU B . n 
B 2 212 ILE 212 212 212 ILE ILE B . n 
B 2 213 ARG 213 213 213 ARG ARG B . n 
B 2 214 ASP 214 214 214 ASP ASP B . n 
B 2 215 ARG 215 215 215 ARG ARG B . n 
B 2 216 HIS 216 216 216 HIS HIS B . n 
B 2 217 LYS 217 217 217 LYS LYS B . n 
B 2 218 ASP 218 218 218 ASP ASP B . n 
B 2 219 ILE 219 219 219 ILE ILE B . n 
B 2 220 GLN 220 220 220 GLN GLN B . n 
B 2 221 GLN 221 221 221 GLN GLN B . n 
B 2 222 LEU 222 222 222 LEU LEU B . n 
B 2 223 GLU 223 223 223 GLU GLU B . n 
B 2 224 ARG 224 224 224 ARG ARG B . n 
B 2 225 SER 225 225 225 SER SER B . n 
B 2 226 LEU 226 226 226 LEU LEU B . n 
B 2 227 LEU 227 227 227 LEU LEU B . n 
B 2 228 GLU 228 228 228 GLU GLU B . n 
B 2 229 LEU 229 229 229 LEU LEU B . n 
B 2 230 HIS 230 230 230 HIS HIS B . n 
B 2 231 GLU 231 231 231 GLU GLU B . n 
B 2 232 MET 232 232 232 MET MET B . n 
B 2 233 PHE 233 233 233 PHE PHE B . n 
B 2 234 THR 234 234 234 THR THR B . n 
B 2 235 ASP 235 235 235 ASP ASP B . n 
B 2 236 MET 236 236 236 MET MET B . n 
B 2 237 SER 237 237 237 SER SER B . n 
B 2 238 THR 238 238 238 THR THR B . n 
B 2 239 LEU 239 239 239 LEU LEU B . n 
B 2 240 VAL 240 240 240 VAL VAL B . n 
B 2 241 ALA 241 241 241 ALA ALA B . n 
B 2 242 SER 242 242 242 SER SER B . n 
B 2 243 GLN 243 243 243 GLN GLN B . n 
B 2 244 GLY 244 244 244 GLY GLY B . n 
B 2 245 GLU 245 245 245 GLU GLU B . n 
B 2 246 MET 246 246 246 MET MET B . n 
B 2 247 ILE 247 247 247 ILE ILE B . n 
B 2 248 ASP 248 248 248 ASP ASP B . n 
B 2 249 ARG 249 249 249 ARG ARG B . n 
B 2 250 ILE 250 250 250 ILE ILE B . n 
B 2 251 GLU 251 251 251 GLU GLU B . n 
B 2 252 PHE 252 252 252 PHE PHE B . n 
B 2 253 SER 253 253 253 SER SER B . n 
B 2 254 VAL 254 254 254 VAL VAL B . n 
B 2 255 GLU 255 255 255 GLU GLU B . n 
B 2 256 GLN 256 256 256 GLN GLN B . n 
B 2 257 SER 257 257 257 SER SER B . n 
B 2 258 HIS 258 258 258 HIS HIS B . n 
B 2 259 ASN 259 259 259 ASN ASN B . n 
B 2 260 TYR 260 260 260 TYR TYR B . n 
B 2 261 VAL 261 261 261 VAL VAL B . n 
B 2 262 LYS 262 262 ?   ?   ?   B . n 
B 2 263 LYS 263 263 ?   ?   ?   B . n 
B 2 264 ALA 264 264 ?   ?   ?   B . n 
B 2 265 THR 265 265 ?   ?   ?   B . n 
B 2 266 GLU 266 266 ?   ?   ?   B . n 
B 2 267 GLN 267 267 ?   ?   ?   B . n 
B 2 268 VAL 268 268 ?   ?   ?   B . n 
B 2 269 VAL 269 269 ?   ?   ?   B . n 
B 2 270 GLN 270 270 ?   ?   ?   B . n 
B 2 271 ALA 271 271 ?   ?   ?   B . n 
B 2 272 ARG 272 272 ?   ?   ?   B . n 
B 2 273 HIS 273 273 ?   ?   ?   B . n 
B 2 274 TYR 274 274 ?   ?   ?   B . n 
B 2 275 GLN 275 275 ?   ?   ?   B . n 
B 2 276 GLU 276 276 ?   ?   ?   B . n 
B 2 277 SER 277 277 ?   ?   ?   B . n 
B 2 278 ALA 278 278 ?   ?   ?   B . n 
B 2 279 ARG 279 279 ?   ?   ?   B . n 
# 
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 
C 3 HOH 1  2001 2001 HOH HOH A . 
C 3 HOH 2  2002 2002 HOH HOH A . 
C 3 HOH 3  2003 2003 HOH HOH A . 
C 3 HOH 4  2004 2004 HOH HOH A . 
C 3 HOH 5  2005 2005 HOH HOH A . 
C 3 HOH 6  2006 2006 HOH HOH A . 
C 3 HOH 7  2007 2007 HOH HOH A . 
C 3 HOH 8  2008 2008 HOH HOH A . 
C 3 HOH 9  2009 2009 HOH HOH A . 
C 3 HOH 10 2010 2010 HOH HOH A . 
C 3 HOH 11 2011 2011 HOH HOH A . 
C 3 HOH 12 2012 2012 HOH HOH A . 
C 3 HOH 13 2013 2013 HOH HOH A . 
C 3 HOH 14 2014 2014 HOH HOH A . 
C 3 HOH 15 2015 2015 HOH HOH A . 
C 3 HOH 16 2016 2016 HOH HOH A . 
C 3 HOH 17 2017 2017 HOH HOH A . 
C 3 HOH 18 2018 2018 HOH HOH A . 
C 3 HOH 19 2019 2019 HOH HOH A . 
C 3 HOH 20 2020 2020 HOH HOH A . 
C 3 HOH 21 2021 2021 HOH HOH A . 
C 3 HOH 22 2022 2022 HOH HOH A . 
C 3 HOH 23 2023 2023 HOH HOH A . 
C 3 HOH 24 2024 2024 HOH HOH A . 
C 3 HOH 25 2025 2025 HOH HOH A . 
C 3 HOH 26 2026 2026 HOH HOH A . 
C 3 HOH 27 2027 2027 HOH HOH A . 
C 3 HOH 28 2028 2028 HOH HOH A . 
C 3 HOH 29 2029 2029 HOH HOH A . 
C 3 HOH 30 2030 2030 HOH HOH A . 
C 3 HOH 31 2031 2031 HOH HOH A . 
C 3 HOH 32 2032 2032 HOH HOH A . 
C 3 HOH 33 2033 2033 HOH HOH A . 
C 3 HOH 34 2034 2034 HOH HOH A . 
C 3 HOH 35 2035 2035 HOH HOH A . 
C 3 HOH 36 2036 2036 HOH HOH A . 
C 3 HOH 37 2037 2037 HOH HOH A . 
C 3 HOH 38 2038 2038 HOH HOH A . 
C 3 HOH 39 2039 2039 HOH HOH A . 
C 3 HOH 40 2040 2040 HOH HOH A . 
C 3 HOH 41 2041 2041 HOH HOH A . 
C 3 HOH 42 2042 2042 HOH HOH A . 
C 3 HOH 43 2043 2043 HOH HOH A . 
C 3 HOH 44 2044 2044 HOH HOH A . 
C 3 HOH 45 2045 2045 HOH HOH A . 
C 3 HOH 46 2046 2046 HOH HOH A . 
D 3 HOH 1  2001 2001 HOH HOH B . 
D 3 HOH 2  2002 2002 HOH HOH B . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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 
# 
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)' 4680  ? 
1 MORE         -19.8 ? 
1 'SSA (A^2)'  36850 ? 
# 
_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_
_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 
1 'Structure model' 1 0 2011-06-29 
2 'Structure model' 1 1 2012-03-14 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'       
2 2 'Structure model' 'Version format compliance' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.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[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 0.2382   -65.1054 0.2208  1.1601 0.5409 0.3277 -0.5676 0.0841  -0.1324 1.5091 3.0537 0.2119 
-1.0216 0.0059  -0.1177 -0.2893 0.3242  -0.2213 -0.6332 0.3399  0.1634  0.7089 -0.1265 -0.0041 
'X-RAY DIFFRACTION' 2 ? refined -3.9215  -38.8999 -4.6076 0.8695 0.6749 0.3253 -0.4210 -0.0937 0.0614  3.1744 4.0671 0.5992 1.8773 
-0.1373 1.1970  -0.2862 0.5680  -0.4413 -1.0202 0.3814  -0.1645 0.4123 -0.3982 -0.0707 
'X-RAY DIFFRACTION' 3 ? refined 4.9819   -30.7289 20.7622 0.3559 0.2519 0.3193 -0.0998 0.0511  -0.0767 2.3108 2.5159 3.0938 1.7690 
-1.3899 -1.1660 0.0364  -0.0175 0.2099  -0.0355 0.0479  0.1401  0.1520 -0.1378 -0.0500 
'X-RAY DIFFRACTION' 4 ? refined -6.7206  -31.6400 2.7672  0.4869 0.5255 0.2938 -0.3095 -0.1055 0.1345  0.5156 3.3962 1.8195 0.0921 
0.0564  -0.2311 -0.2179 0.1419  0.2476  -0.4204 0.2812  0.4257  0.4662 -0.4265 -0.1002 
'X-RAY DIFFRACTION' 5 ? refined -2.6289  -75.1004 1.1768  0.8619 0.5070 0.4151 -0.3435 -0.1428 0.0796  0.7385 1.6338 0.6068 0.4948 
-0.2256 -0.0162 -0.4432 0.2975  0.2534  -0.2093 -0.2996 0.1906  0.3139 -0.3965 0.1704  
'X-RAY DIFFRACTION' 6 ? refined -10.1169 -69.0591 31.9884 0.9182 0.5790 0.3620 -0.4738 -0.1042 0.0053  2.9730 1.3862 1.6552 
-0.9108 -3.0521 0.2944  -0.0302 0.5965  -0.1336 0.1562  0.1484  0.1180  0.4596 -0.1883 0.0409  
'X-RAY DIFFRACTION' 7 ? refined -21.4294 -61.3563 52.9882 1.0731 0.5667 0.6064 -0.5165 0.1108  0.0636  1.8855 0.0727 2.8673 
-0.4993 -1.0947 0.3721  -0.3658 0.4705  0.5497  -0.1229 0.5614  -0.1479 1.2890 -0.5100 0.0543  
'X-RAY DIFFRACTION' 8 ? refined 8.4716   -62.0416 19.4130 0.8227 0.7499 0.5985 -0.2905 -0.0697 0.0765  1.3673 1.0407 3.1048 
-1.2993 -2.1764 1.5439  -0.6390 -0.0142 -0.5866 -0.1618 0.1239  0.6164  0.1015 0.1670  0.2359  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 0:129)'   
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 130:237)' 
'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 238:476)' 
'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 477:616)' 
'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? '(CHAIN B AND RESID 2:53)'    
'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? '(CHAIN B AND RESID 54:167)'  
'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? '(CHAIN B AND RESID 168:234)' 
'X-RAY DIFFRACTION' 8 8 ? ? ? ? ? ? ? ? ? '(CHAIN B AND RESID 235:261)' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
PHENIX refinement       '(PHENIX.REFINE)' ? 1 
XDS    'data reduction' .                 ? 2 
XDS    'data scaling'   .                 ? 3 
PHASER phasing          .                 ? 4 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 MET A 1   ? ? 77.36   -67.68  
2  1 ASP A 48  ? ? -89.94  37.43   
3  1 LYS A 59  ? ? 93.76   -64.52  
4  1 GLN A 60  ? ? 32.84   69.19   
5  1 LYS A 62  ? ? 49.55   98.81   
6  1 PRO A 75  ? ? -66.33  60.57   
7  1 ALA A 88  ? ? 5.13    -68.07  
8  1 ASP A 89  ? ? -56.66  175.16  
9  1 THR A 124 ? ? 62.03   138.15  
10 1 LEU A 125 ? ? -160.34 104.94  
11 1 SER A 154 ? ? -79.57  34.29   
12 1 ASN A 160 ? ? 77.61   71.69   
13 1 GLU A 215 ? ? 72.80   55.99   
14 1 ASP A 230 ? ? -166.66 104.36  
15 1 ASP A 262 ? ? -105.05 -149.95 
16 1 GLU A 267 ? ? 26.04   50.21   
17 1 GLN A 283 ? ? 76.71   -39.02  
18 1 GLN A 311 ? ? -90.62  -124.90 
19 1 ARG A 314 ? ? -172.80 139.09  
20 1 GLN A 335 ? ? -39.53  -39.39  
21 1 THR A 448 ? ? 60.13   108.43  
22 1 ARG A 454 ? ? 80.31   123.80  
23 1 ILE A 464 ? ? 75.22   -44.59  
24 1 GLU A 465 ? ? 66.83   125.64  
25 1 THR A 488 ? ? -157.46 19.80   
26 1 ASP A 492 ? ? -27.35  137.60  
27 1 PRO A 503 ? ? -68.26  4.13    
28 1 ALA A 563 ? ? -75.51  -163.34 
29 1 LYS A 564 ? ? 71.25   136.04  
30 1 SER A 589 ? ? -101.91 -76.64  
31 1 PHE B 42  ? ? 84.09   93.58   
32 1 VAL B 76  ? ? 44.56   -116.27 
33 1 SER B 79  ? ? 45.69   -135.58 
34 1 ARG B 117 ? ? -81.01  31.64   
35 1 ALA B 118 ? ? -147.53 -5.92   
36 1 PHE B 124 ? ? -107.47 43.92   
37 1 GLU B 125 ? ? 58.22   -151.71 
38 1 ASP B 126 ? ? 61.24   -8.76   
39 1 VAL B 129 ? ? -116.21 -126.95 
40 1 GLU B 167 ? ? -74.96  -71.43  
41 1 VAL B 169 ? ? -145.14 -49.02  
42 1 CYS B 173 ? ? -90.13  39.00   
43 1 ARG B 174 ? ? -99.67  30.41   
44 1 VAL B 175 ? ? -74.02  23.11   
45 1 LEU B 180 ? ? -73.74  -122.92 
46 1 SER B 242 ? ? 47.78   23.98   
47 1 GLU B 245 ? ? 71.34   -27.51  
48 1 MET B 246 ? ? -141.35 -11.51  
49 1 GLU B 251 ? ? -39.97  -38.44  
50 1 GLN B 256 ? ? -92.93  36.31   
51 1 HIS B 258 ? ? -105.76 -165.17 
52 1 ASN B 259 ? ? -174.69 -168.11 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   SER 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    590 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    591 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            146.31 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ALA 617 ? CA ? A ALA 618 CA 
2 1 Y 1 A ALA 617 ? C  ? A ALA 618 C  
3 1 Y 1 A ALA 617 ? O  ? A ALA 618 O  
4 1 Y 1 A ALA 617 ? CB ? A ALA 618 CB 
# 
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 ARG 510 ? A ARG 511 
2   1 Y 1 A ALA 511 ? A ALA 512 
3   1 Y 1 A SER 512 ? A SER 513 
4   1 Y 1 A LYS 513 ? A LYS 514 
5   1 Y 1 A SER 514 ? A SER 515 
6   1 Y 1 A VAL 515 ? A VAL 516 
7   1 Y 1 A GLU 516 ? A GLU 517 
8   1 Y 1 A GLU 517 ? A GLU 518 
9   1 Y 1 A ASP 518 ? A ASP 519 
10  1 Y 1 A ASP 519 ? A ASP 520 
11  1 Y 1 A ASP 520 ? A ASP 521 
12  1 Y 1 A GLY 521 ? A GLY 522 
13  1 Y 1 A PRO 522 ? A PRO 523 
14  1 Y 1 A ALA 523 ? A ALA 524 
15  1 Y 1 A THR 524 ? A THR 525 
16  1 Y 1 A SER 525 ? A SER 526 
17  1 Y 1 A ALA 526 ? A ALA 527 
18  1 Y 1 A ARG 527 ? A ARG 528 
19  1 Y 1 A LYS 528 ? A LYS 529 
20  1 Y 1 A ARG 529 ? A ARG 530 
21  1 Y 1 A GLY 530 ? A GLY 531 
22  1 Y 1 A ASN 531 ? A ASN 532 
23  1 Y 1 A TRP 532 ? A TRP 533 
24  1 Y 1 A ALA 533 ? A ALA 534 
25  1 Y 1 A LYS 534 ? A LYS 535 
26  1 Y 1 A ASN 535 ? A ASN 536 
27  1 Y 1 A LYS 536 ? A LYS 537 
28  1 Y 1 A GLY 537 ? A GLY 538 
29  1 Y 1 A ASN 538 ? A ASN 539 
30  1 Y 1 A ASN 539 ? A ASN 540 
31  1 Y 1 A ARG 540 ? A ARG 541 
32  1 Y 1 A SER 541 ? A SER 542 
33  1 Y 1 A LEU 542 ? A LEU 543 
34  1 Y 1 A PRO 543 ? A PRO 544 
35  1 Y 1 A SER 544 ? A SER 545 
36  1 Y 1 A THR 545 ? A THR 546 
37  1 Y 1 A PRO 546 ? A PRO 547 
38  1 Y 1 A SER 547 ? A SER 548 
39  1 Y 1 A GLY 548 ? A GLY 549 
40  1 Y 1 A VAL 549 ? A VAL 550 
41  1 Y 1 A ALA 550 ? A ALA 551 
42  1 Y 1 A VAL 551 ? A VAL 552 
43  1 Y 1 A SER 552 ? A SER 553 
44  1 Y 1 A GLY 553 ? A GLY 554 
45  1 Y 1 A ASN 554 ? A ASN 555 
46  1 Y 1 A GLY 555 ? A GLY 556 
47  1 Y 1 A ALA 556 ? A ALA 557 
48  1 Y 1 A ALA 557 ? A ALA 558 
49  1 Y 1 A GLY 558 ? A GLY 559 
50  1 Y 1 A ALA 559 ? A ALA 560 
51  1 Y 1 A ALA 560 ? A ALA 561 
52  1 Y 1 A ASP 618 ? A ASP 619 
53  1 Y 1 A GLN 619 ? A GLN 620 
54  1 Y 1 A ASP 620 ? A ASP 621 
55  1 Y 1 A VAL 621 ? A VAL 622 
56  1 Y 1 A GLN 622 ? A GLN 623 
57  1 Y 1 A VAL 623 ? A VAL 624 
58  1 Y 1 A LEU 624 ? A LEU 625 
59  1 Y 1 A THR 625 ? A THR 626 
60  1 Y 1 A GLN 626 ? A GLN 627 
61  1 Y 1 A GLY 627 ? A GLY 628 
62  1 Y 1 A GLN 628 ? A GLN 629 
63  1 Y 1 A GLY 629 ? A GLY 630 
64  1 Y 1 A ASP 630 ? A ASP 631 
65  1 Y 1 A GLY 631 ? A GLY 632 
66  1 Y 1 A GLY 632 ? A GLY 633 
67  1 Y 1 A LEU 633 ? A LEU 634 
68  1 Y 1 A VAL 634 ? A VAL 635 
69  1 Y 1 A ILE 635 ? A ILE 636 
70  1 Y 1 A THR 636 ? A THR 637 
71  1 Y 1 A THR 637 ? A THR 638 
72  1 Y 1 A GLY 638 ? A GLY 639 
73  1 Y 1 A SER 639 ? A SER 640 
74  1 Y 1 A ALA 640 ? A ALA 641 
75  1 Y 1 A GLN 641 ? A GLN 642 
76  1 Y 1 A ALA 642 ? A ALA 643 
77  1 Y 1 A GLY 643 ? A GLY 644 
78  1 Y 1 A LEU 644 ? A LEU 645 
79  1 Y 1 A ASN 645 ? A ASN 646 
80  1 Y 1 A LEU 646 ? A LEU 647 
81  1 Y 1 A ALA 647 ? A ALA 648 
82  1 Y 1 A GLU 648 ? A GLU 649 
83  1 Y 1 A VAL 649 ? A VAL 650 
84  1 Y 1 B MET 1   ? B MET 1   
85  1 Y 1 B PRO 16  ? B PRO 16  
86  1 Y 1 B ALA 17  ? B ALA 17  
87  1 Y 1 B GLU 18  ? B GLU 18  
88  1 Y 1 B ALA 19  ? B ALA 19  
89  1 Y 1 B SER 20  ? B SER 20  
90  1 Y 1 B ASP 21  ? B ASP 21  
91  1 Y 1 B ALA 22  ? B ALA 22  
92  1 Y 1 B ALA 23  ? B ALA 23  
93  1 Y 1 B GLY 24  ? B GLY 24  
94  1 Y 1 B GLY 25  ? B GLY 25  
95  1 Y 1 B ALA 26  ? B ALA 26  
96  1 Y 1 B GLU 27  ? B GLU 27  
97  1 Y 1 B ALA 28  ? B ALA 28  
98  1 Y 1 B GLN 29  ? B GLN 29  
99  1 Y 1 B ILE 30  ? B ILE 30  
100 1 Y 1 B GLU 31  ? B GLU 31  
101 1 Y 1 B GLU 32  ? B GLU 32  
102 1 Y 1 B THR 33  ? B THR 33  
103 1 Y 1 B SER 34  ? B SER 34  
104 1 Y 1 B LEU 35  ? B LEU 35  
105 1 Y 1 B SER 36  ? B SER 36  
106 1 Y 1 B ALA 37  ? B ALA 37  
107 1 Y 1 B GLN 38  ? B GLN 38  
108 1 Y 1 B THR 193 ? B THR 193 
109 1 Y 1 B GLU 194 ? B GLU 194 
110 1 Y 1 B GLY 195 ? B GLY 195 
111 1 Y 1 B ILE 196 ? B ILE 196 
112 1 Y 1 B PHE 197 ? B PHE 197 
113 1 Y 1 B SER 198 ? B SER 198 
114 1 Y 1 B GLY 199 ? B GLY 199 
115 1 Y 1 B MET 200 ? B MET 200 
116 1 Y 1 B ARG 201 ? B ARG 201 
117 1 Y 1 B LEU 202 ? B LEU 202 
118 1 Y 1 B GLU 203 ? B GLU 203 
119 1 Y 1 B GLY 204 ? B GLY 204 
120 1 Y 1 B ALA 205 ? B ALA 205 
121 1 Y 1 B GLU 206 ? B GLU 206 
122 1 Y 1 B ALA 207 ? B ALA 207 
123 1 Y 1 B LYS 208 ? B LYS 208 
124 1 Y 1 B LEU 209 ? B LEU 209 
125 1 Y 1 B LYS 262 ? B LYS 262 
126 1 Y 1 B LYS 263 ? B LYS 263 
127 1 Y 1 B ALA 264 ? B ALA 264 
128 1 Y 1 B THR 265 ? B THR 265 
129 1 Y 1 B GLU 266 ? B GLU 266 
130 1 Y 1 B GLN 267 ? B GLN 267 
131 1 Y 1 B VAL 268 ? B VAL 268 
132 1 Y 1 B VAL 269 ? B VAL 269 
133 1 Y 1 B GLN 270 ? B GLN 270 
134 1 Y 1 B ALA 271 ? B ALA 271 
135 1 Y 1 B ARG 272 ? B ARG 272 
136 1 Y 1 B HIS 273 ? B HIS 273 
137 1 Y 1 B TYR 274 ? B TYR 274 
138 1 Y 1 B GLN 275 ? B GLN 275 
139 1 Y 1 B GLU 276 ? B GLU 276 
140 1 Y 1 B SER 277 ? B SER 277 
141 1 Y 1 B ALA 278 ? B ALA 278 
142 1 Y 1 B ARG 279 ? B ARG 279 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
#