data_4MCP # _entry.id 4MCP # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4MCP RCSB RCSB081745 WWPDB D_1000081745 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 4MCQ . unspecified PDB 4MCR . unspecified PDB 4MCS . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MCP _pdbx_database_status.recvd_initial_deposition_date 2013-08-21 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Navratil, M.' 1 'Barinka, C.' 2 'Lubkowski, J.' 3 # _citation.id primary _citation.title ;Structural and biochemical characterization of the folyl-poly-gamma-l-glutamate hydrolyzing activity of human glutamate carboxypeptidase II. ; _citation.journal_abbrev 'Febs J.' _citation.journal_volume 281 _citation.page_first 3228 _citation.page_last 3242 _citation.year 2014 _citation.journal_id_ASTM ? _citation.country UK _citation.journal_id_ISSN 1742-464X _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24863754 _citation.pdbx_database_id_DOI 10.1111/febs.12857 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Navratil, M.' 1 primary 'Ptacek, J.' 2 primary 'Sacha, P.' 3 primary 'Starkova, J.' 4 primary 'Lubkowski, J.' 5 primary 'Barinka, C.' 6 primary 'Konvalinka, J.' 7 # _cell.entry_id 4MCP _cell.length_a 101.533 _cell.length_b 130.176 _cell.length_c 158.809 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 4MCP _symmetry.space_group_name_H-M 'I 2 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 23 _symmetry.space_group_name_Hall ? # 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 'Glutamate carboxypeptidase 2' 84972.914 1 3.4.17.21 E424A 'unp residues 44-750' ? 2 non-polymer syn 'ZINC ION' 65.409 2 ? ? ? ? 3 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 4 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 11 ? ? ? ? 6 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 7 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 8 non-polymer syn 'N-(4-{[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino}benzoyl)-L-gamma-glutamyl-L-glutamic acid' 570.511 1 ? ? ? ? 9 water nat water 18.015 668 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name ;Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Membrane glutamate carboxypeptidase, mGCP, N-acetylated-alpha-linked acidic dipeptidase I, NAALADase I, Prostate-specific membrane antigen, PSM, PSMA, Pteroylpoly-gamma-glutamate carboxypeptidase ; # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;MKLCILLAVVAFVGLSLGRSGLNDIFEAQKIEWHEGSGSGSENLYFQGRSKSSNEATNITPKHNMKAFLDELKAENIKKF LYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYEN VSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPAD YFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSA PPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAA VVHEIVRSFGTLKKEGWRPRRTILFASWDAAEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSL VHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYH SVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLF SAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALF DIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _entity_poly.pdbx_seq_one_letter_code_can ;MKLCILLAVVAFVGLSLGRSGLNDIFEAQKIEWHEGSGSGSENLYFQGRSKSSNEATNITPKHNMKAFLDELKAENIKKF LYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYEN VSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPAD YFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSA PPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAA VVHEIVRSFGTLKKEGWRPRRTILFASWDAAEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSL VHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYH SVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLF SAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALF DIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 MET n 1 2 LYS n 1 3 LEU n 1 4 CYS n 1 5 ILE n 1 6 LEU n 1 7 LEU n 1 8 ALA n 1 9 VAL n 1 10 VAL n 1 11 ALA n 1 12 PHE n 1 13 VAL n 1 14 GLY n 1 15 LEU n 1 16 SER n 1 17 LEU n 1 18 GLY n 1 19 ARG n 1 20 SER n 1 21 GLY n 1 22 LEU n 1 23 ASN n 1 24 ASP n 1 25 ILE n 1 26 PHE n 1 27 GLU n 1 28 ALA n 1 29 GLN n 1 30 LYS n 1 31 ILE n 1 32 GLU n 1 33 TRP n 1 34 HIS n 1 35 GLU n 1 36 GLY n 1 37 SER n 1 38 GLY n 1 39 SER n 1 40 GLY n 1 41 SER n 1 42 GLU n 1 43 ASN n 1 44 LEU n 1 45 TYR n 1 46 PHE n 1 47 GLN n 1 48 GLY n 1 49 ARG n 1 50 SER n 1 51 LYS n 1 52 SER n 1 53 SER n 1 54 ASN n 1 55 GLU n 1 56 ALA n 1 57 THR n 1 58 ASN n 1 59 ILE n 1 60 THR n 1 61 PRO n 1 62 LYS n 1 63 HIS n 1 64 ASN n 1 65 MET n 1 66 LYS n 1 67 ALA n 1 68 PHE n 1 69 LEU n 1 70 ASP n 1 71 GLU n 1 72 LEU n 1 73 LYS n 1 74 ALA n 1 75 GLU n 1 76 ASN n 1 77 ILE n 1 78 LYS n 1 79 LYS n 1 80 PHE n 1 81 LEU n 1 82 TYR n 1 83 ASN n 1 84 PHE n 1 85 THR n 1 86 GLN n 1 87 ILE n 1 88 PRO n 1 89 HIS n 1 90 LEU n 1 91 ALA n 1 92 GLY n 1 93 THR n 1 94 GLU n 1 95 GLN n 1 96 ASN n 1 97 PHE n 1 98 GLN n 1 99 LEU n 1 100 ALA n 1 101 LYS n 1 102 GLN n 1 103 ILE n 1 104 GLN n 1 105 SER n 1 106 GLN n 1 107 TRP n 1 108 LYS n 1 109 GLU n 1 110 PHE n 1 111 GLY n 1 112 LEU n 1 113 ASP n 1 114 SER n 1 115 VAL n 1 116 GLU n 1 117 LEU n 1 118 ALA n 1 119 HIS n 1 120 TYR n 1 121 ASP n 1 122 VAL n 1 123 LEU n 1 124 LEU n 1 125 SER n 1 126 TYR n 1 127 PRO n 1 128 ASN n 1 129 LYS n 1 130 THR n 1 131 HIS n 1 132 PRO n 1 133 ASN n 1 134 TYR n 1 135 ILE n 1 136 SER n 1 137 ILE n 1 138 ILE n 1 139 ASN n 1 140 GLU n 1 141 ASP n 1 142 GLY n 1 143 ASN n 1 144 GLU n 1 145 ILE n 1 146 PHE n 1 147 ASN n 1 148 THR n 1 149 SER n 1 150 LEU n 1 151 PHE n 1 152 GLU n 1 153 PRO n 1 154 PRO n 1 155 PRO n 1 156 PRO n 1 157 GLY n 1 158 TYR n 1 159 GLU n 1 160 ASN n 1 161 VAL n 1 162 SER n 1 163 ASP n 1 164 ILE n 1 165 VAL n 1 166 PRO n 1 167 PRO n 1 168 PHE n 1 169 SER n 1 170 ALA n 1 171 PHE n 1 172 SER n 1 173 PRO n 1 174 GLN n 1 175 GLY n 1 176 MET n 1 177 PRO n 1 178 GLU n 1 179 GLY n 1 180 ASP n 1 181 LEU n 1 182 VAL n 1 183 TYR n 1 184 VAL n 1 185 ASN n 1 186 TYR n 1 187 ALA n 1 188 ARG n 1 189 THR n 1 190 GLU n 1 191 ASP n 1 192 PHE n 1 193 PHE n 1 194 LYS n 1 195 LEU n 1 196 GLU n 1 197 ARG n 1 198 ASP n 1 199 MET n 1 200 LYS n 1 201 ILE n 1 202 ASN n 1 203 CYS n 1 204 SER n 1 205 GLY n 1 206 LYS n 1 207 ILE n 1 208 VAL n 1 209 ILE n 1 210 ALA n 1 211 ARG n 1 212 TYR n 1 213 GLY n 1 214 LYS n 1 215 VAL n 1 216 PHE n 1 217 ARG n 1 218 GLY n 1 219 ASN n 1 220 LYS n 1 221 VAL n 1 222 LYS n 1 223 ASN n 1 224 ALA n 1 225 GLN n 1 226 LEU n 1 227 ALA n 1 228 GLY n 1 229 ALA n 1 230 LYS n 1 231 GLY n 1 232 VAL n 1 233 ILE n 1 234 LEU n 1 235 TYR n 1 236 SER n 1 237 ASP n 1 238 PRO n 1 239 ALA n 1 240 ASP n 1 241 TYR n 1 242 PHE n 1 243 ALA n 1 244 PRO n 1 245 GLY n 1 246 VAL n 1 247 LYS n 1 248 SER n 1 249 TYR n 1 250 PRO n 1 251 ASP n 1 252 GLY n 1 253 TRP n 1 254 ASN n 1 255 LEU n 1 256 PRO n 1 257 GLY n 1 258 GLY n 1 259 GLY n 1 260 VAL n 1 261 GLN n 1 262 ARG n 1 263 GLY n 1 264 ASN n 1 265 ILE n 1 266 LEU n 1 267 ASN n 1 268 LEU n 1 269 ASN n 1 270 GLY n 1 271 ALA n 1 272 GLY n 1 273 ASP n 1 274 PRO n 1 275 LEU n 1 276 THR n 1 277 PRO n 1 278 GLY n 1 279 TYR n 1 280 PRO n 1 281 ALA n 1 282 ASN n 1 283 GLU n 1 284 TYR n 1 285 ALA n 1 286 TYR n 1 287 ARG n 1 288 ARG n 1 289 GLY n 1 290 ILE n 1 291 ALA n 1 292 GLU n 1 293 ALA n 1 294 VAL n 1 295 GLY n 1 296 LEU n 1 297 PRO n 1 298 SER n 1 299 ILE n 1 300 PRO n 1 301 VAL n 1 302 HIS n 1 303 PRO n 1 304 ILE n 1 305 GLY n 1 306 TYR n 1 307 TYR n 1 308 ASP n 1 309 ALA n 1 310 GLN n 1 311 LYS n 1 312 LEU n 1 313 LEU n 1 314 GLU n 1 315 LYS n 1 316 MET n 1 317 GLY n 1 318 GLY n 1 319 SER n 1 320 ALA n 1 321 PRO n 1 322 PRO n 1 323 ASP n 1 324 SER n 1 325 SER n 1 326 TRP n 1 327 ARG n 1 328 GLY n 1 329 SER n 1 330 LEU n 1 331 LYS n 1 332 VAL n 1 333 PRO n 1 334 TYR n 1 335 ASN n 1 336 VAL n 1 337 GLY n 1 338 PRO n 1 339 GLY n 1 340 PHE n 1 341 THR n 1 342 GLY n 1 343 ASN n 1 344 PHE n 1 345 SER n 1 346 THR n 1 347 GLN n 1 348 LYS n 1 349 VAL n 1 350 LYS n 1 351 MET n 1 352 HIS n 1 353 ILE n 1 354 HIS n 1 355 SER n 1 356 THR n 1 357 ASN n 1 358 GLU n 1 359 VAL n 1 360 THR n 1 361 ARG n 1 362 ILE n 1 363 TYR n 1 364 ASN n 1 365 VAL n 1 366 ILE n 1 367 GLY n 1 368 THR n 1 369 LEU n 1 370 ARG n 1 371 GLY n 1 372 ALA n 1 373 VAL n 1 374 GLU n 1 375 PRO n 1 376 ASP n 1 377 ARG n 1 378 TYR n 1 379 VAL n 1 380 ILE n 1 381 LEU n 1 382 GLY n 1 383 GLY n 1 384 HIS n 1 385 ARG n 1 386 ASP n 1 387 SER n 1 388 TRP n 1 389 VAL n 1 390 PHE n 1 391 GLY n 1 392 GLY n 1 393 ILE n 1 394 ASP n 1 395 PRO n 1 396 GLN n 1 397 SER n 1 398 GLY n 1 399 ALA n 1 400 ALA n 1 401 VAL n 1 402 VAL n 1 403 HIS n 1 404 GLU n 1 405 ILE n 1 406 VAL n 1 407 ARG n 1 408 SER n 1 409 PHE n 1 410 GLY n 1 411 THR n 1 412 LEU n 1 413 LYS n 1 414 LYS n 1 415 GLU n 1 416 GLY n 1 417 TRP n 1 418 ARG n 1 419 PRO n 1 420 ARG n 1 421 ARG n 1 422 THR n 1 423 ILE n 1 424 LEU n 1 425 PHE n 1 426 ALA n 1 427 SER n 1 428 TRP n 1 429 ASP n 1 430 ALA n 1 431 ALA n 1 432 GLU n 1 433 PHE n 1 434 GLY n 1 435 LEU n 1 436 LEU n 1 437 GLY n 1 438 SER n 1 439 THR n 1 440 GLU n 1 441 TRP n 1 442 ALA n 1 443 GLU n 1 444 GLU n 1 445 ASN n 1 446 SER n 1 447 ARG n 1 448 LEU n 1 449 LEU n 1 450 GLN n 1 451 GLU n 1 452 ARG n 1 453 GLY n 1 454 VAL n 1 455 ALA n 1 456 TYR n 1 457 ILE n 1 458 ASN n 1 459 ALA n 1 460 ASP n 1 461 SER n 1 462 SER n 1 463 ILE n 1 464 GLU n 1 465 GLY n 1 466 ASN n 1 467 TYR n 1 468 THR n 1 469 LEU n 1 470 ARG n 1 471 VAL n 1 472 ASP n 1 473 CYS n 1 474 THR n 1 475 PRO n 1 476 LEU n 1 477 MET n 1 478 TYR n 1 479 SER n 1 480 LEU n 1 481 VAL n 1 482 HIS n 1 483 ASN n 1 484 LEU n 1 485 THR n 1 486 LYS n 1 487 GLU n 1 488 LEU n 1 489 LYS n 1 490 SER n 1 491 PRO n 1 492 ASP n 1 493 GLU n 1 494 GLY n 1 495 PHE n 1 496 GLU n 1 497 GLY n 1 498 LYS n 1 499 SER n 1 500 LEU n 1 501 TYR n 1 502 GLU n 1 503 SER n 1 504 TRP n 1 505 THR n 1 506 LYS n 1 507 LYS n 1 508 SER n 1 509 PRO n 1 510 SER n 1 511 PRO n 1 512 GLU n 1 513 PHE n 1 514 SER n 1 515 GLY n 1 516 MET n 1 517 PRO n 1 518 ARG n 1 519 ILE n 1 520 SER n 1 521 LYS n 1 522 LEU n 1 523 GLY n 1 524 SER n 1 525 GLY n 1 526 ASN n 1 527 ASP n 1 528 PHE n 1 529 GLU n 1 530 VAL n 1 531 PHE n 1 532 PHE n 1 533 GLN n 1 534 ARG n 1 535 LEU n 1 536 GLY n 1 537 ILE n 1 538 ALA n 1 539 SER n 1 540 GLY n 1 541 ARG n 1 542 ALA n 1 543 ARG n 1 544 TYR n 1 545 THR n 1 546 LYS n 1 547 ASN n 1 548 TRP n 1 549 GLU n 1 550 THR n 1 551 ASN n 1 552 LYS n 1 553 PHE n 1 554 SER n 1 555 GLY n 1 556 TYR n 1 557 PRO n 1 558 LEU n 1 559 TYR n 1 560 HIS n 1 561 SER n 1 562 VAL n 1 563 TYR n 1 564 GLU n 1 565 THR n 1 566 TYR n 1 567 GLU n 1 568 LEU n 1 569 VAL n 1 570 GLU n 1 571 LYS n 1 572 PHE n 1 573 TYR n 1 574 ASP n 1 575 PRO n 1 576 MET n 1 577 PHE n 1 578 LYS n 1 579 TYR n 1 580 HIS n 1 581 LEU n 1 582 THR n 1 583 VAL n 1 584 ALA n 1 585 GLN n 1 586 VAL n 1 587 ARG n 1 588 GLY n 1 589 GLY n 1 590 MET n 1 591 VAL n 1 592 PHE n 1 593 GLU n 1 594 LEU n 1 595 ALA n 1 596 ASN n 1 597 SER n 1 598 ILE n 1 599 VAL n 1 600 LEU n 1 601 PRO n 1 602 PHE n 1 603 ASP n 1 604 CYS n 1 605 ARG n 1 606 ASP n 1 607 TYR n 1 608 ALA n 1 609 VAL n 1 610 VAL n 1 611 LEU n 1 612 ARG n 1 613 LYS n 1 614 TYR n 1 615 ALA n 1 616 ASP n 1 617 LYS n 1 618 ILE n 1 619 TYR n 1 620 SER n 1 621 ILE n 1 622 SER n 1 623 MET n 1 624 LYS n 1 625 HIS n 1 626 PRO n 1 627 GLN n 1 628 GLU n 1 629 MET n 1 630 LYS n 1 631 THR n 1 632 TYR n 1 633 SER n 1 634 VAL n 1 635 SER n 1 636 PHE n 1 637 ASP n 1 638 SER n 1 639 LEU n 1 640 PHE n 1 641 SER n 1 642 ALA n 1 643 VAL n 1 644 LYS n 1 645 ASN n 1 646 PHE n 1 647 THR n 1 648 GLU n 1 649 ILE n 1 650 ALA n 1 651 SER n 1 652 LYS n 1 653 PHE n 1 654 SER n 1 655 GLU n 1 656 ARG n 1 657 LEU n 1 658 GLN n 1 659 ASP n 1 660 PHE n 1 661 ASP n 1 662 LYS n 1 663 SER n 1 664 ASN n 1 665 PRO n 1 666 ILE n 1 667 VAL n 1 668 LEU n 1 669 ARG n 1 670 MET n 1 671 MET n 1 672 ASN n 1 673 ASP n 1 674 GLN n 1 675 LEU n 1 676 MET n 1 677 PHE n 1 678 LEU n 1 679 GLU n 1 680 ARG n 1 681 ALA n 1 682 PHE n 1 683 ILE n 1 684 ASP n 1 685 PRO n 1 686 LEU n 1 687 GLY n 1 688 LEU n 1 689 PRO n 1 690 ASP n 1 691 ARG n 1 692 PRO n 1 693 PHE n 1 694 TYR n 1 695 ARG n 1 696 HIS n 1 697 VAL n 1 698 ILE n 1 699 TYR n 1 700 ALA n 1 701 PRO n 1 702 SER n 1 703 SER n 1 704 HIS n 1 705 ASN n 1 706 LYS n 1 707 TYR n 1 708 ALA n 1 709 GLY n 1 710 GLU n 1 711 SER n 1 712 PHE n 1 713 PRO n 1 714 GLY n 1 715 ILE n 1 716 TYR n 1 717 ASP n 1 718 ALA n 1 719 LEU n 1 720 PHE n 1 721 ASP n 1 722 ILE n 1 723 GLU n 1 724 SER n 1 725 LYS n 1 726 VAL n 1 727 ASP n 1 728 PRO n 1 729 SER n 1 730 LYS n 1 731 ALA n 1 732 TRP n 1 733 GLY n 1 734 GLU n 1 735 VAL n 1 736 LYS n 1 737 ARG n 1 738 GLN n 1 739 ILE n 1 740 TYR n 1 741 VAL n 1 742 ALA n 1 743 ALA n 1 744 PHE n 1 745 THR n 1 746 VAL n 1 747 GLN n 1 748 ALA n 1 749 ALA n 1 750 ALA n 1 751 GLU n 1 752 THR n 1 753 LEU n 1 754 SER n 1 755 GLU n 1 756 VAL n 1 757 ALA n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _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 human _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'FOLH1, FOLH, NAALAD1, PSM, PSMA, GIG27' _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 'Homo sapiens' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _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 'Drosophila Melanogaster' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7227 _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 ;Schneider's S2 cells ; _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 plasmid _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 ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code FOLH1_HUMAN _struct_ref.pdbx_db_accession Q04609 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;KSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKT HPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIA RYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGI AEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLR GAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQ ERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEV FFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVV LRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPD RPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _struct_ref.pdbx_align_begin 44 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4MCP _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 51 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 757 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q04609 _struct_ref_seq.db_align_beg 44 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 750 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 44 _struct_ref_seq.pdbx_auth_seq_align_end 750 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4MCP MET A 1 ? UNP Q04609 ? ? 'INITIATING METHIONINE' -6 1 1 4MCP LYS A 2 ? UNP Q04609 ? ? 'EXPRESSION TAG' -5 2 1 4MCP LEU A 3 ? UNP Q04609 ? ? 'EXPRESSION TAG' -4 3 1 4MCP CYS A 4 ? UNP Q04609 ? ? 'EXPRESSION TAG' -3 4 1 4MCP ILE A 5 ? UNP Q04609 ? ? 'EXPRESSION TAG' -2 5 1 4MCP LEU A 6 ? UNP Q04609 ? ? 'EXPRESSION TAG' -1 6 1 4MCP LEU A 7 ? UNP Q04609 ? ? 'EXPRESSION TAG' 0 7 1 4MCP ALA A 8 ? UNP Q04609 ? ? 'EXPRESSION TAG' 1 8 1 4MCP VAL A 9 ? UNP Q04609 ? ? 'EXPRESSION TAG' 2 9 1 4MCP VAL A 10 ? UNP Q04609 ? ? 'EXPRESSION TAG' 3 10 1 4MCP ALA A 11 ? UNP Q04609 ? ? 'EXPRESSION TAG' 4 11 1 4MCP PHE A 12 ? UNP Q04609 ? ? 'EXPRESSION TAG' 5 12 1 4MCP VAL A 13 ? UNP Q04609 ? ? 'EXPRESSION TAG' 6 13 1 4MCP GLY A 14 ? UNP Q04609 ? ? 'EXPRESSION TAG' 7 14 1 4MCP LEU A 15 ? UNP Q04609 ? ? 'EXPRESSION TAG' 8 15 1 4MCP SER A 16 ? UNP Q04609 ? ? 'EXPRESSION TAG' 9 16 1 4MCP LEU A 17 ? UNP Q04609 ? ? 'EXPRESSION TAG' 10 17 1 4MCP GLY A 18 ? UNP Q04609 ? ? 'EXPRESSION TAG' 11 18 1 4MCP ARG A 19 ? UNP Q04609 ? ? 'EXPRESSION TAG' 12 19 1 4MCP SER A 20 ? UNP Q04609 ? ? 'EXPRESSION TAG' 13 20 1 4MCP GLY A 21 ? UNP Q04609 ? ? 'EXPRESSION TAG' 14 21 1 4MCP LEU A 22 ? UNP Q04609 ? ? 'EXPRESSION TAG' 15 22 1 4MCP ASN A 23 ? UNP Q04609 ? ? 'EXPRESSION TAG' 16 23 1 4MCP ASP A 24 ? UNP Q04609 ? ? 'EXPRESSION TAG' 17 24 1 4MCP ILE A 25 ? UNP Q04609 ? ? 'EXPRESSION TAG' 18 25 1 4MCP PHE A 26 ? UNP Q04609 ? ? 'EXPRESSION TAG' 19 26 1 4MCP GLU A 27 ? UNP Q04609 ? ? 'EXPRESSION TAG' 20 27 1 4MCP ALA A 28 ? UNP Q04609 ? ? 'EXPRESSION TAG' 21 28 1 4MCP GLN A 29 ? UNP Q04609 ? ? 'EXPRESSION TAG' 22 29 1 4MCP LYS A 30 ? UNP Q04609 ? ? 'EXPRESSION TAG' 23 30 1 4MCP ILE A 31 ? UNP Q04609 ? ? 'EXPRESSION TAG' 24 31 1 4MCP GLU A 32 ? UNP Q04609 ? ? 'EXPRESSION TAG' 25 32 1 4MCP TRP A 33 ? UNP Q04609 ? ? 'EXPRESSION TAG' 26 33 1 4MCP HIS A 34 ? UNP Q04609 ? ? 'EXPRESSION TAG' 27 34 1 4MCP GLU A 35 ? UNP Q04609 ? ? 'EXPRESSION TAG' 28 35 1 4MCP GLY A 36 ? UNP Q04609 ? ? 'EXPRESSION TAG' 29 36 1 4MCP SER A 37 ? UNP Q04609 ? ? 'EXPRESSION TAG' 30 37 1 4MCP GLY A 38 ? UNP Q04609 ? ? 'EXPRESSION TAG' 31 38 1 4MCP SER A 39 ? UNP Q04609 ? ? 'EXPRESSION TAG' 32 39 1 4MCP GLY A 40 ? UNP Q04609 ? ? 'EXPRESSION TAG' 33 40 1 4MCP SER A 41 ? UNP Q04609 ? ? 'EXPRESSION TAG' 34 41 1 4MCP GLU A 42 ? UNP Q04609 ? ? 'EXPRESSION TAG' 35 42 1 4MCP ASN A 43 ? UNP Q04609 ? ? 'EXPRESSION TAG' 36 43 1 4MCP LEU A 44 ? UNP Q04609 ? ? 'EXPRESSION TAG' 37 44 1 4MCP TYR A 45 ? UNP Q04609 ? ? 'EXPRESSION TAG' 38 45 1 4MCP PHE A 46 ? UNP Q04609 ? ? 'EXPRESSION TAG' 39 46 1 4MCP GLN A 47 ? UNP Q04609 ? ? 'EXPRESSION TAG' 40 47 1 4MCP GLY A 48 ? UNP Q04609 ? ? 'EXPRESSION TAG' 41 48 1 4MCP ARG A 49 ? UNP Q04609 ? ? 'EXPRESSION TAG' 42 49 1 4MCP SER A 50 ? UNP Q04609 ? ? 'EXPRESSION TAG' 43 50 1 4MCP ALA A 431 ? UNP Q04609 GLU 424 'ENGINEERED MUTATION' 424 51 # 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 28Z non-polymer . 'N-(4-{[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino}benzoyl)-L-gamma-glutamyl-L-glutamic acid' ? 'C24 H26 N8 O9' 570.511 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 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 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 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 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 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.entry_id 4MCP _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.09 _exptl_crystal.density_percent_sol 60.16 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 8.0 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details ;33% (v/v) pentaerythritol propoxylate PO/OH 5/4, 0.5% (w/v) PEG 3350, 0.10 M Tris HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K ; # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'MARMOSAIC 225 mm CCD' _diffrn_detector.pdbx_collection_date 2010-02-24 _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 'Si(111), Rosenbaum-Rock double-crystal monochromator' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.00 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 22-BM' _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 22-BM _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.00 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4MCP _reflns.observed_criterion_sigma_I -3 _reflns.observed_criterion_sigma_F -3 _reflns.d_resolution_low 40.0 _reflns.d_resolution_high 1.65 _reflns.number_obs 119318 _reflns.number_all 119318 _reflns.percent_possible_obs 94.5 _reflns.pdbx_Rmerge_I_obs 0.077 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 22.6 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.65 _reflns_shell.d_res_low 1.71 _reflns_shell.percent_possible_all 61.1 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4MCP _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 117931 _refine.ls_number_reflns_all 117931 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 30.00 _refine.ls_d_res_high 1.65 _refine.ls_percent_reflns_obs 94.08 _refine.ls_R_factor_obs 0.15021 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.15007 _refine.ls_R_factor_R_free 0.16408 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 1.0 _refine.ls_number_reflns_R_free 1200 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.973 _refine.correlation_coeff_Fo_to_Fc_free 0.968 _refine.B_iso_mean 29.545 _refine.aniso_B[1][1] 0.85 _refine.aniso_B[2][2] -2.17 _refine.aniso_B[3][3] 1.32 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.070 _refine.pdbx_overall_ESU_R_Free 0.067 _refine.overall_SU_ML 0.043 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 2.821 _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.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 5516 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 221 _refine_hist.number_atoms_solvent 668 _refine_hist.number_atoms_total 6405 _refine_hist.d_res_high 1.65 _refine_hist.d_res_low 30.00 # 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 r_bond_refined_d 0.015 0.022 ? 6400 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.488 1.994 ? 8732 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.804 5.000 ? 771 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.593 23.854 ? 301 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 14.148 15.000 ? 1061 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 15.153 15.000 ? 39 'X-RAY DIFFRACTION' ? r_chiral_restr 0.110 0.200 ? 921 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.008 0.021 ? 5016 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 0.735 1.500 ? 3716 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.283 2.000 ? 6075 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.045 3.000 ? 2684 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it 3.268 4.500 ? 2655 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr 3.951 3.000 ? 6417 'X-RAY DIFFRACTION' ? r_sphericity_free 17.809 5.000 ? 195 'X-RAY DIFFRACTION' ? r_sphericity_bonded 15.987 5.000 ? 6669 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.647 _refine_ls_shell.d_res_low 1.690 _refine_ls_shell.number_reflns_R_work 5078 _refine_ls_shell.R_factor_R_work 0.220 _refine_ls_shell.percent_reflns_obs 55.22 _refine_ls_shell.R_factor_R_free 0.265 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 59 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_obs ? # _pdbx_refine.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine.entry_id 4MCP _pdbx_refine.R_factor_all_no_cutoff ? _pdbx_refine.R_factor_obs_no_cutoff ? _pdbx_refine.free_R_factor_no_cutoff ? _pdbx_refine.free_R_error_no_cutoff ? _pdbx_refine.free_R_val_test_set_size_perc_no_cutoff ? _pdbx_refine.free_R_val_test_set_ct_no_cutoff ? _pdbx_refine.R_factor_all_4sig_cutoff ? _pdbx_refine.R_factor_obs_4sig_cutoff ? _pdbx_refine.free_R_factor_4sig_cutoff ? _pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff ? _pdbx_refine.free_R_val_test_set_ct_4sig_cutoff ? _pdbx_refine.number_reflns_obs_4sig_cutoff ? # _struct.entry_id 4MCP _struct.title ;A high resolution structure of human glutamate carboxypeptidase II (GCPII) in complex with folyl-gamma-L-glutamic acid (pteroyldi-gamma-L-glutamic acid) ; _struct.pdbx_descriptor 'Glutamate carboxypeptidase 2 (E.C.3.4.17.21)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4MCP _struct_keywords.pdbx_keywords 'hydrolase/hydrolase inhibitor' _struct_keywords.text 'hydrolase, metallopeptidase, hydrolase-hydrolase inhibitor complex' # 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 2 ? D N N 3 ? E N N 4 ? F N N 5 ? G N N 5 ? H N N 5 ? I N N 5 ? J N N 5 ? K N N 5 ? L N N 5 ? M N N 5 ? N N N 5 ? O N N 5 ? P N N 5 ? Q N N 6 ? R N N 7 ? S N N 8 ? T N N 9 ? # _struct_biol.id 1 _struct_biol.details ? # 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 ASN A 64 ? LEU A 72 ? ASN A 57 LEU A 65 1 ? 9 HELX_P HELX_P2 2 LYS A 73 ? THR A 85 ? LYS A 66 THR A 78 1 ? 13 HELX_P HELX_P3 3 THR A 93 ? GLY A 111 ? THR A 86 GLY A 104 1 ? 19 HELX_P HELX_P4 4 ARG A 188 ? ASP A 198 ? ARG A 181 ASP A 191 1 ? 11 HELX_P HELX_P5 5 PHE A 216 ? ALA A 227 ? PHE A 209 ALA A 220 1 ? 12 HELX_P HELX_P6 6 ASP A 237 ? PHE A 242 ? ASP A 230 PHE A 235 1 ? 6 HELX_P HELX_P7 7 GLY A 289 ? ALA A 293 ? GLY A 282 ALA A 286 5 ? 5 HELX_P HELX_P8 8 GLY A 305 ? LYS A 315 ? GLY A 298 LYS A 308 1 ? 11 HELX_P HELX_P9 9 ASP A 323 ? ARG A 327 ? ASP A 316 ARG A 320 5 ? 5 HELX_P HELX_P10 10 THR A 341 ? SER A 345 ? THR A 334 SER A 338 5 ? 5 HELX_P HELX_P11 11 PRO A 395 ? GLU A 415 ? PRO A 388 GLU A 408 1 ? 21 HELX_P HELX_P12 12 ALA A 430 ? GLY A 434 ? ALA A 423 GLY A 427 5 ? 5 HELX_P HELX_P13 13 LEU A 435 ? ASN A 445 ? LEU A 428 ASN A 438 1 ? 11 HELX_P HELX_P14 14 ASN A 445 ? ARG A 452 ? ASN A 438 ARG A 445 1 ? 8 HELX_P HELX_P15 15 MET A 477 ? LEU A 488 ? MET A 470 LEU A 481 1 ? 12 HELX_P HELX_P16 16 SER A 499 ? SER A 508 ? SER A 492 SER A 501 1 ? 10 HELX_P HELX_P17 17 PHE A 528 ? GLN A 533 ? PHE A 521 GLN A 526 1 ? 6 HELX_P HELX_P18 18 THR A 565 ? TYR A 573 ? THR A 558 TYR A 566 1 ? 9 HELX_P HELX_P19 19 PHE A 577 ? SER A 597 ? PHE A 570 SER A 590 1 ? 21 HELX_P HELX_P20 20 ASP A 603 ? MET A 623 ? ASP A 596 MET A 616 1 ? 21 HELX_P HELX_P21 21 HIS A 625 ? TYR A 632 ? HIS A 618 TYR A 625 1 ? 8 HELX_P HELX_P22 22 PHE A 636 ? PHE A 660 ? PHE A 629 PHE A 653 1 ? 25 HELX_P HELX_P23 23 ASN A 664 ? PHE A 682 ? ASN A 657 PHE A 675 1 ? 19 HELX_P HELX_P24 24 PHE A 712 ? PHE A 720 ? PHE A 705 PHE A 713 1 ? 9 HELX_P HELX_P25 25 ASP A 721 ? LYS A 725 ? ASP A 714 LYS A 718 5 ? 5 HELX_P HELX_P26 26 ASP A 727 ? THR A 752 ? ASP A 720 THR A 745 1 ? 26 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order covale1 covale ? ? A ASN 645 ND2 ? ? ? 1_555 O NAG . C1 ? ? A ASN 638 A NAG 814 1_555 ? ? ? ? ? ? ? 1.395 ? covale2 covale ? ? P NAG . O4 ? ? ? 1_555 Q BMA . C1 ? ? A NAG 815 A BMA 816 1_555 ? ? ? ? ? ? ? 1.415 ? covale3 covale ? ? O NAG . O4 ? ? ? 1_555 P NAG . C1 ? ? A NAG 814 A NAG 815 1_555 ? ? ? ? ? ? ? 1.418 ? covale4 covale ? ? Q BMA . O3 ? ? ? 1_555 R MAN . C1 ? ? A BMA 816 A MAN 817 1_555 ? ? ? ? ? ? ? 1.425 ? covale5 covale ? ? A ASN 83 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 76 A NAG 805 1_555 ? ? ? ? ? ? ? 1.428 ? covale6 covale ? ? A ASN 483 ND2 ? ? ? 1_555 M NAG . C1 ? ? A ASN 476 A NAG 812 1_555 ? ? ? ? ? ? ? 1.435 ? covale7 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 805 A NAG 806 1_555 ? ? ? ? ? ? ? 1.438 ? covale8 covale ? ? A ASN 147 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 140 A NAG 808 1_555 ? ? ? ? ? ? ? 1.441 ? covale9 covale ? ? M NAG . O4 ? ? ? 1_555 N NAG . C1 ? ? A NAG 812 A NAG 813 1_555 ? ? ? ? ? ? ? 1.442 ? covale10 covale ? ? A ASN 128 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 121 A NAG 807 1_555 ? ? ? ? ? ? ? 1.444 ? covale11 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 808 A NAG 809 1_555 ? ? ? ? ? ? ? 1.446 ? covale12 covale ? ? A ASN 466 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 459 A NAG 811 1_555 ? ? ? ? ? ? ? 1.451 ? covale13 covale ? ? A ASN 202 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 195 A NAG 810 1_555 ? ? ? ? ? ? ? 1.452 ? metalc1 metalc ? ? C ZN . ZN ? ? ? 1_555 T HOH . O ? ? A ZN 802 A HOH 1345 1_555 ? ? ? ? ? ? ? 1.914 ? metalc2 metalc ? ? A ASP 460 OD2 ? ? ? 1_555 C ZN . ZN ? ? A ASP 453 A ZN 802 1_555 ? ? ? ? ? ? ? 1.965 ? metalc3 metalc ? ? A ASP 394 OD1 ? ? ? 1_555 C ZN . ZN ? ? A ASP 387 A ZN 802 1_555 ? ? ? ? ? ? ? 1.991 ? metalc4 metalc ? ? A HIS 384 NE2 ? ? ? 1_555 C ZN . ZN ? ? A HIS 377 A ZN 802 1_555 ? ? ? ? ? ? ? 2.006 ? metalc5 metalc ? ? B ZN . ZN ? ? ? 1_555 T HOH . O ? ? A ZN 801 A HOH 1345 1_555 ? ? ? ? ? ? ? 2.008 ? metalc6 metalc ? ? A HIS 560 NE2 ? ? ? 1_555 B ZN . ZN ? ? A HIS 553 A ZN 801 1_555 ? ? ? ? ? ? ? 2.037 ? metalc7 metalc ? ? A ASP 394 OD2 ? ? ? 1_555 B ZN . ZN ? ? A ASP 387 A ZN 801 1_555 ? ? ? ? ? ? ? 2.079 ? metalc8 metalc ? ? A GLU 432 OE2 ? ? ? 1_555 B ZN . ZN ? ? A GLU 425 A ZN 801 1_555 ? ? ? ? ? ? ? 2.181 ? metalc9 metalc ? ? A GLU 443 OE2 ? ? ? 1_555 D CA . CA ? ? A GLU 436 A CA 803 1_555 ? ? ? ? ? ? ? 2.286 ? metalc10 metalc ? ? A TYR 279 O ? ? ? 1_555 D CA . CA ? ? A TYR 272 A CA 803 1_555 ? ? ? ? ? ? ? 2.326 ? metalc11 metalc ? ? A GLU 432 OE1 ? ? ? 1_555 B ZN . ZN ? ? A GLU 425 A ZN 801 1_555 ? ? ? ? ? ? ? 2.385 ? metalc12 metalc ? ? D CA . CA ? ? ? 1_555 T HOH . O ? ? A CA 803 A HOH 906 1_555 ? ? ? ? ? ? ? 2.399 ? metalc13 metalc ? ? A THR 276 O ? ? ? 1_555 D CA . CA ? ? A THR 269 A CA 803 1_555 ? ? ? ? ? ? ? 2.418 ? metalc14 metalc ? ? A GLU 440 OE1 ? ? ? 1_555 D CA . CA ? ? A GLU 433 A CA 803 1_555 ? ? ? ? ? ? ? 2.451 ? metalc15 metalc ? ? A THR 276 OG1 ? ? ? 1_555 D CA . CA ? ? A THR 269 A CA 803 1_555 ? ? ? ? ? ? ? 2.466 ? metalc16 metalc ? ? A GLU 440 OE2 ? ? ? 1_555 D CA . CA ? ? A GLU 433 A CA 803 1_555 ? ? ? ? ? ? ? 2.522 ? metalc17 metalc ? ? B ZN . ZN ? ? ? 1_555 S 28Z . OAE ? ? A ZN 801 A 28Z 818 1_555 ? ? ? ? ? ? ? 2.465 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 TYR 249 A . ? TYR 242 A PRO 250 A ? PRO 243 A 1 8.88 2 GLY 337 A . ? GLY 330 A PRO 338 A ? PRO 331 A 1 0.23 3 ASP 394 A . ? ASP 387 A PRO 395 A ? PRO 388 A 1 7.52 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 7 ? B ? 4 ? C ? 2 ? D ? 4 ? E ? 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 A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? parallel A 4 5 ? parallel A 5 6 ? parallel A 6 7 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? parallel D 1 2 ? parallel D 2 3 ? parallel D 3 4 ? parallel E 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 A 1 SER A 114 ? TYR A 126 ? SER A 107 TYR A 119 A 2 THR A 356 ? LEU A 369 ? THR A 349 LEU A 362 A 3 ARG A 421 ? TRP A 428 ? ARG A 414 TRP A 421 A 4 GLU A 374 ? HIS A 384 ? GLU A 367 HIS A 377 A 5 GLY A 453 ? ASN A 458 ? GLY A 446 ASN A 451 A 6 ALA A 538 ? THR A 545 ? ALA A 531 THR A 538 A 7 THR A 468 ? CYS A 473 ? THR A 461 CYS A 466 B 1 GLU A 144 ? ASN A 147 ? GLU A 137 ASN A 140 B 2 TYR A 134 ? ILE A 138 ? TYR A 127 ILE A 131 B 3 LYS A 348 ? HIS A 352 ? LYS A 341 HIS A 345 B 4 GLU A 178 ? GLY A 179 ? GLU A 171 GLY A 172 C 1 SER A 169 ? ALA A 170 ? SER A 162 ALA A 163 C 2 GLY A 263 ? ASN A 264 ? GLY A 256 ASN A 257 D 1 LEU A 181 ? TYR A 183 ? LEU A 174 TYR A 176 D 2 ILE A 207 ? ARG A 211 ? ILE A 200 ARG A 204 D 3 GLY A 231 ? TYR A 235 ? GLY A 224 TYR A 228 D 4 VAL A 301 ? ILE A 304 ? VAL A 294 ILE A 297 E 1 TYR A 699 ? SER A 702 ? TYR A 692 SER A 695 E 2 ASN A 705 ? SER A 711 ? ASN A 698 SER A 704 # 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 A 1 2 N ALA A 118 ? N ALA A 111 O ASN A 364 ? O ASN A 357 A 2 3 N GLY A 367 ? N GLY A 360 O PHE A 425 ? O PHE A 418 A 3 4 O LEU A 424 ? O LEU A 417 N LEU A 381 ? N LEU A 374 A 4 5 N ILE A 380 ? N ILE A 373 O ILE A 457 ? O ILE A 450 A 5 6 N ASN A 458 ? N ASN A 451 O GLY A 540 ? O GLY A 533 A 6 7 O THR A 545 ? O THR A 538 N THR A 468 ? N THR A 461 B 1 2 O ILE A 145 ? O ILE A 138 N ILE A 137 ? N ILE A 130 B 2 3 N SER A 136 ? N SER A 129 O LYS A 350 ? O LYS A 343 B 3 4 O VAL A 349 ? O VAL A 342 N GLY A 179 ? N GLY A 172 C 1 2 O ALA A 170 ? O ALA A 163 N GLY A 263 ? N GLY A 256 D 1 2 N VAL A 182 ? N VAL A 175 O ILE A 209 ? O ILE A 202 D 2 3 N VAL A 208 ? N VAL A 201 O ILE A 233 ? O ILE A 226 D 3 4 N LEU A 234 ? N LEU A 227 O ILE A 304 ? O ILE A 297 E 1 2 N SER A 702 ? N SER A 695 O ALA A 708 ? O ALA A 701 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ZN A 801' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ZN A 802' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 803' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CL A 804' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 805' AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 806' AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 807' AC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 808' AC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 809' BC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 810' BC2 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 811' BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 812' BC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 813' BC5 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 814' BC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 815' BC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE BMA A 816' BC8 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE MAN A 817' BC9 Software ? ? ? ? 31 'BINDING SITE FOR RESIDUE 28Z A 818' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 6 ASP A 394 ? ASP A 387 . ? 1_555 ? 2 AC1 6 GLU A 432 ? GLU A 425 . ? 1_555 ? 3 AC1 6 HIS A 560 ? HIS A 553 . ? 1_555 ? 4 AC1 6 ZN C . ? ZN A 802 . ? 1_555 ? 5 AC1 6 28Z S . ? 28Z A 818 . ? 1_555 ? 6 AC1 6 HOH T . ? HOH A 1345 . ? 1_555 ? 7 AC2 6 HIS A 384 ? HIS A 377 . ? 1_555 ? 8 AC2 6 ASP A 394 ? ASP A 387 . ? 1_555 ? 9 AC2 6 GLU A 432 ? GLU A 425 . ? 1_555 ? 10 AC2 6 ASP A 460 ? ASP A 453 . ? 1_555 ? 11 AC2 6 ZN B . ? ZN A 801 . ? 1_555 ? 12 AC2 6 HOH T . ? HOH A 1345 . ? 1_555 ? 13 AC3 5 THR A 276 ? THR A 269 . ? 1_555 ? 14 AC3 5 TYR A 279 ? TYR A 272 . ? 1_555 ? 15 AC3 5 GLU A 440 ? GLU A 433 . ? 1_555 ? 16 AC3 5 GLU A 443 ? GLU A 436 . ? 1_555 ? 17 AC3 5 HOH T . ? HOH A 906 . ? 1_555 ? 18 AC4 4 ASN A 458 ? ASN A 451 . ? 1_555 ? 19 AC4 4 ASP A 460 ? ASP A 453 . ? 1_555 ? 20 AC4 4 ARG A 541 ? ARG A 534 . ? 1_555 ? 21 AC4 4 ARG A 543 ? ARG A 536 . ? 1_555 ? 22 AC5 6 ASN A 83 ? ASN A 76 . ? 1_555 ? 23 AC5 6 GLN A 102 ? GLN A 95 . ? 1_555 ? 24 AC5 6 GLN A 106 ? GLN A 99 . ? 1_555 ? 25 AC5 6 NAG G . ? NAG A 806 . ? 1_555 ? 26 AC5 6 HOH T . ? HOH A 1125 . ? 1_555 ? 27 AC5 6 HOH T . ? HOH A 1485 . ? 1_555 ? 28 AC6 3 NAG F . ? NAG A 805 . ? 1_555 ? 29 AC6 3 HOH T . ? HOH A 1452 . ? 1_555 ? 30 AC6 3 HOH T . ? HOH A 1485 . ? 1_555 ? 31 AC7 5 ASN A 128 ? ASN A 121 . ? 1_555 ? 32 AC7 5 THR A 130 ? THR A 123 . ? 1_555 ? 33 AC7 5 HIS A 131 ? HIS A 124 . ? 1_555 ? 34 AC7 5 THR A 356 ? THR A 349 . ? 1_555 ? 35 AC7 5 HOH T . ? HOH A 1294 . ? 1_555 ? 36 AC8 6 TYR A 134 ? TYR A 127 . ? 1_555 ? 37 AC8 6 GLU A 144 ? GLU A 137 . ? 1_555 ? 38 AC8 6 ILE A 145 ? ILE A 138 . ? 1_555 ? 39 AC8 6 ASN A 147 ? ASN A 140 . ? 1_555 ? 40 AC8 6 NAG J . ? NAG A 809 . ? 1_555 ? 41 AC8 6 HOH T . ? HOH A 1479 . ? 1_555 ? 42 AC9 4 NAG I . ? NAG A 808 . ? 1_555 ? 43 AC9 4 HOH T . ? HOH A 1404 . ? 1_555 ? 44 AC9 4 HOH T . ? HOH A 1477 . ? 1_555 ? 45 AC9 4 HOH T . ? HOH A 1478 . ? 1_555 ? 46 BC1 2 ASN A 202 ? ASN A 195 . ? 1_555 ? 47 BC1 2 SER A 204 ? SER A 197 . ? 1_555 ? 48 BC2 9 TRP A 253 ? TRP A 246 . ? 1_555 ? 49 BC2 9 ASN A 466 ? ASN A 459 . ? 1_555 ? 50 BC2 9 PHE A 572 ? PHE A 565 . ? 1_555 ? 51 BC2 9 TYR A 573 ? TYR A 566 . ? 1_555 ? 52 BC2 9 HOH T . ? HOH A 977 . ? 1_555 ? 53 BC2 9 HOH T . ? HOH A 1141 . ? 1_555 ? 54 BC2 9 HOH T . ? HOH A 1331 . ? 1_555 ? 55 BC2 9 HOH T . ? HOH A 1366 . ? 1_555 ? 56 BC2 9 HOH T . ? HOH A 1520 . ? 1_555 ? 57 BC3 4 SER A 479 ? SER A 472 . ? 1_555 ? 58 BC3 4 ASN A 483 ? ASN A 476 . ? 1_555 ? 59 BC3 4 PRO A 601 ? PRO A 594 . ? 1_555 ? 60 BC3 4 NAG N . ? NAG A 813 . ? 1_555 ? 61 BC4 3 NAG M . ? NAG A 812 . ? 1_555 ? 62 BC4 3 HOH T . ? HOH A 1276 . ? 1_555 ? 63 BC4 3 HOH T . ? HOH A 1552 . ? 1_555 ? 64 BC5 7 SER A 638 ? SER A 631 . ? 1_555 ? 65 BC5 7 SER A 641 ? SER A 634 . ? 1_555 ? 66 BC5 7 ASN A 645 ? ASN A 638 . ? 1_555 ? 67 BC5 7 GLN A 747 ? GLN A 740 . ? 1_555 ? 68 BC5 7 NAG P . ? NAG A 815 . ? 1_555 ? 69 BC5 7 HOH T . ? HOH A 1023 . ? 1_555 ? 70 BC5 7 HOH T . ? HOH A 1056 . ? 2_565 ? 71 BC6 5 GLU A 283 ? GLU A 276 . ? 2_565 ? 72 BC6 5 NAG O . ? NAG A 814 . ? 1_555 ? 73 BC6 5 BMA Q . ? BMA A 816 . ? 1_555 ? 74 BC6 5 HOH T . ? HOH A 1152 . ? 2_565 ? 75 BC6 5 HOH T . ? HOH A 1419 . ? 7_555 ? 76 BC7 5 HIS A 119 ? HIS A 112 . ? 2_565 ? 77 BC7 5 GLU A 283 ? GLU A 276 . ? 2_565 ? 78 BC7 5 ARG A 361 ? ARG A 354 . ? 2_565 ? 79 BC7 5 NAG P . ? NAG A 815 . ? 1_555 ? 80 BC7 5 MAN R . ? MAN A 817 . ? 1_555 ? 81 BC8 10 PHE A 242 ? PHE A 235 . ? 7_555 ? 82 BC8 10 LYS A 247 ? LYS A 240 . ? 7_555 ? 83 BC8 10 SER A 248 ? SER A 241 . ? 7_555 ? 84 BC8 10 GLU A 283 ? GLU A 276 . ? 2_565 ? 85 BC8 10 ARG A 361 ? ARG A 354 . ? 2_565 ? 86 BC8 10 BMA Q . ? BMA A 816 . ? 1_555 ? 87 BC8 10 HOH T . ? HOH A 1275 . ? 7_555 ? 88 BC8 10 HOH T . ? HOH A 1292 . ? 1_555 ? 89 BC8 10 HOH T . ? HOH A 1312 . ? 1_555 ? 90 BC8 10 HOH T . ? HOH A 1559 . ? 2_565 ? 91 BC9 31 ARG A 217 ? ARG A 210 . ? 1_555 ? 92 BC9 31 ASN A 264 ? ASN A 257 . ? 1_555 ? 93 BC9 31 ASP A 394 ? ASP A 387 . ? 1_555 ? 94 BC9 31 ALA A 431 ? ALA A 424 . ? 1_555 ? 95 BC9 31 GLU A 432 ? GLU A 425 . ? 1_555 ? 96 BC9 31 GLY A 434 ? GLY A 427 . ? 1_555 ? 97 BC9 31 LEU A 435 ? LEU A 428 . ? 1_555 ? 98 BC9 31 GLU A 464 ? GLU A 457 . ? 1_555 ? 99 BC9 31 ARG A 470 ? ARG A 463 . ? 1_555 ? 100 BC9 31 ARG A 518 ? ARG A 511 . ? 1_555 ? 101 BC9 31 GLY A 525 ? GLY A 518 . ? 1_555 ? 102 BC9 31 ASN A 526 ? ASN A 519 . ? 1_555 ? 103 BC9 31 ARG A 541 ? ARG A 534 . ? 1_555 ? 104 BC9 31 ARG A 543 ? ARG A 536 . ? 1_555 ? 105 BC9 31 THR A 545 ? THR A 538 . ? 1_555 ? 106 BC9 31 TRP A 548 ? TRP A 541 . ? 1_555 ? 107 BC9 31 SER A 554 ? SER A 547 . ? 1_555 ? 108 BC9 31 GLY A 555 ? GLY A 548 . ? 1_555 ? 109 BC9 31 TYR A 559 ? TYR A 552 . ? 1_555 ? 110 BC9 31 HIS A 560 ? HIS A 553 . ? 1_555 ? 111 BC9 31 LYS A 706 ? LYS A 699 . ? 1_555 ? 112 BC9 31 TYR A 707 ? TYR A 700 . ? 1_555 ? 113 BC9 31 ZN B . ? ZN A 801 . ? 1_555 ? 114 BC9 31 HOH T . ? HOH A 909 . ? 1_555 ? 115 BC9 31 HOH T . ? HOH A 1066 . ? 1_555 ? 116 BC9 31 HOH T . ? HOH A 1222 . ? 1_555 ? 117 BC9 31 HOH T . ? HOH A 1282 . ? 1_555 ? 118 BC9 31 HOH T . ? HOH A 1290 . ? 1_555 ? 119 BC9 31 HOH T . ? HOH A 1328 . ? 1_555 ? 120 BC9 31 HOH T . ? HOH A 1345 . ? 1_555 ? 121 BC9 31 HOH T . ? HOH A 1512 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MCP _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 4MCP _atom_sites.fract_transf_matrix[1][1] 0.009849 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.007682 _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] 0.006297 _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 CA CL N O S ZN # 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 63 ? 14.773 46.676 79.973 1.00 48.36 ? 56 HIS A N 1 ATOM 2 C CA . HIS A 1 63 ? 14.395 46.730 78.525 1.00 46.65 ? 56 HIS A CA 1 ATOM 3 C C . HIS A 1 63 ? 14.844 48.030 77.884 1.00 45.07 ? 56 HIS A C 1 ATOM 4 O O . HIS A 1 63 ? 14.154 49.053 77.984 1.00 46.23 ? 56 HIS A O 1 ATOM 5 C CB . HIS A 1 63 ? 12.884 46.596 78.339 1.00 46.99 ? 56 HIS A CB 1 ATOM 6 C CG . HIS A 1 63 ? 12.339 45.267 78.753 1.00 48.51 ? 56 HIS A CG 1 ATOM 7 N ND1 . HIS A 1 63 ? 11.208 45.142 79.535 1.00 49.91 ? 56 HIS A ND1 1 ATOM 8 C CD2 . HIS A 1 63 ? 12.765 44.009 78.495 1.00 48.78 ? 56 HIS A CD2 1 ATOM 9 C CE1 . HIS A 1 63 ? 10.961 43.860 79.737 1.00 52.50 ? 56 HIS A CE1 1 ATOM 10 N NE2 . HIS A 1 63 ? 11.891 43.152 79.118 1.00 51.19 ? 56 HIS A NE2 1 ATOM 11 N N . ASN A 1 64 ? 15.994 47.976 77.218 1.00 42.35 ? 57 ASN A N 1 ATOM 12 C CA . ASN A 1 64 ? 16.583 49.127 76.547 1.00 39.05 ? 57 ASN A CA 1 ATOM 13 C C . ASN A 1 64 ? 17.206 48.608 75.267 1.00 36.51 ? 57 ASN A C 1 ATOM 14 O O . ASN A 1 64 ? 17.050 47.426 74.935 1.00 35.07 ? 57 ASN A O 1 ATOM 15 C CB . ASN A 1 64 ? 17.648 49.797 77.428 1.00 39.34 ? 57 ASN A CB 1 ATOM 16 C CG . ASN A 1 64 ? 18.635 48.794 78.025 1.00 40.01 ? 57 ASN A CG 1 ATOM 17 O OD1 . ASN A 1 64 ? 18.750 47.651 77.565 1.00 37.97 ? 57 ASN A OD1 1 ATOM 18 N ND2 . ASN A 1 64 ? 19.346 49.219 79.074 1.00 42.95 ? 57 ASN A ND2 1 ATOM 19 N N . MET A 1 65 ? 17.914 49.469 74.543 1.00 34.96 ? 58 MET A N 1 ATOM 20 C CA . MET A 1 65 ? 18.427 48.996 73.260 1.00 33.84 ? 58 MET A CA 1 ATOM 21 C C . MET A 1 65 ? 19.429 47.867 73.459 1.00 33.51 ? 58 MET A C 1 ATOM 22 O O . MET A 1 65 ? 19.463 46.940 72.663 1.00 33.19 ? 58 MET A O 1 ATOM 23 C CB . MET A 1 65 ? 19.061 50.073 72.413 1.00 33.78 ? 58 MET A CB 1 ATOM 24 C CG . MET A 1 65 ? 19.235 49.531 70.958 1.00 34.48 ? 58 MET A CG 1 ATOM 25 S SD . MET A 1 65 ? 20.181 50.634 69.957 1.00 42.65 ? 58 MET A SD 1 ATOM 26 C CE . MET A 1 65 ? 19.074 51.963 69.859 1.00 39.38 ? 58 MET A CE 1 ATOM 27 N N . LYS A 1 66 ? 20.236 47.940 74.515 1.00 33.89 ? 59 LYS A N 1 ATOM 28 C CA . LYS A 1 66 ? 21.212 46.889 74.765 1.00 34.23 ? 59 LYS A CA 1 ATOM 29 C C . LYS A 1 66 ? 20.539 45.514 74.934 1.00 33.75 ? 59 LYS A C 1 ATOM 30 O O . LYS A 1 66 ? 21.055 44.506 74.450 1.00 33.83 ? 59 LYS A O 1 ATOM 31 C CB . LYS A 1 66 ? 22.088 47.228 75.986 1.00 35.10 ? 59 LYS A CB 1 ATOM 32 C CG . LYS A 1 66 ? 23.192 46.220 76.248 0.90 37.08 ? 59 LYS A CG 1 ATOM 33 C CD . LYS A 1 66 ? 23.942 46.563 77.557 0.80 39.60 ? 59 LYS A CD 1 ATOM 34 C CE . LYS A 1 66 ? 25.286 45.823 77.682 0.50 41.07 ? 59 LYS A CE 1 ATOM 35 N NZ . LYS A 1 66 ? 25.156 44.342 77.607 0.50 41.31 ? 59 LYS A NZ 1 ATOM 36 N N . ALA A 1 67 ? 19.373 45.484 75.583 1.00 34.17 ? 60 ALA A N 1 ATOM 37 C CA . ALA A 1 67 ? 18.648 44.220 75.760 1.00 34.70 ? 60 ALA A CA 1 ATOM 38 C C . ALA A 1 67 ? 18.224 43.691 74.393 1.00 33.22 ? 60 ALA A C 1 ATOM 39 O O . ALA A 1 67 ? 18.398 42.510 74.100 1.00 34.15 ? 60 ALA A O 1 ATOM 40 C CB . ALA A 1 67 ? 17.432 44.400 76.660 1.00 35.95 ? 60 ALA A CB 1 ATOM 41 N N . PHE A 1 68 ? 17.677 44.589 73.568 1.00 31.12 ? 61 PHE A N 1 ATOM 42 C CA . PHE A 1 68 ? 17.271 44.211 72.226 1.00 30.33 ? 61 PHE A CA 1 ATOM 43 C C . PHE A 1 68 ? 18.454 43.654 71.424 1.00 29.09 ? 61 PHE A C 1 ATOM 44 O O . PHE A 1 68 ? 18.377 42.577 70.810 1.00 28.76 ? 61 PHE A O 1 ATOM 45 C CB . PHE A 1 68 ? 16.643 45.408 71.484 1.00 28.46 ? 61 PHE A CB 1 ATOM 46 C CG . PHE A 1 68 ? 16.579 45.189 70.003 1.00 28.60 ? 61 PHE A CG 1 ATOM 47 C CD1 . PHE A 1 68 ? 15.634 44.324 69.468 1.00 28.69 ? 61 PHE A CD1 1 ATOM 48 C CD2 . PHE A 1 68 ? 17.523 45.781 69.158 1.00 26.41 ? 61 PHE A CD2 1 ATOM 49 C CE1 . PHE A 1 68 ? 15.617 44.060 68.077 1.00 27.36 ? 61 PHE A CE1 1 ATOM 50 C CE2 . PHE A 1 68 ? 17.512 45.528 67.779 1.00 27.31 ? 61 PHE A CE2 1 ATOM 51 C CZ . PHE A 1 68 ? 16.565 44.675 67.244 1.00 28.04 ? 61 PHE A CZ 1 ATOM 52 N N . LEU A 1 69 ? 19.545 44.406 71.408 1.00 29.21 ? 62 LEU A N 1 ATOM 53 C CA . LEU A 1 69 ? 20.717 44.011 70.639 1.00 29.41 ? 62 LEU A CA 1 ATOM 54 C C . LEU A 1 69 ? 21.328 42.696 71.114 1.00 30.79 ? 62 LEU A C 1 ATOM 55 O O . LEU A 1 69 ? 21.757 41.859 70.301 1.00 30.82 ? 62 LEU A O 1 ATOM 56 C CB . LEU A 1 69 ? 21.770 45.111 70.706 1.00 30.06 ? 62 LEU A CB 1 ATOM 57 C CG . LEU A 1 69 ? 21.403 46.412 70.005 1.00 28.80 ? 62 LEU A CG 1 ATOM 58 C CD1 . LEU A 1 69 ? 22.433 47.479 70.377 1.00 32.18 ? 62 LEU A CD1 1 ATOM 59 C CD2 . LEU A 1 69 ? 21.269 46.251 68.454 1.00 26.62 ? 62 LEU A CD2 1 ATOM 60 N N . ASP A 1 70 ? 21.376 42.508 72.428 1.00 32.50 ? 63 ASP A N 1 ATOM 61 C CA . ASP A 1 70 ? 22.039 41.316 72.983 1.00 34.10 ? 63 ASP A CA 1 ATOM 62 C C . ASP A 1 70 ? 21.284 40.039 72.633 1.00 33.83 ? 63 ASP A C 1 ATOM 63 O O . ASP A 1 70 ? 21.872 38.949 72.606 1.00 34.42 ? 63 ASP A O 1 ATOM 64 C CB . ASP A 1 70 ? 22.163 41.412 74.507 1.00 35.48 ? 63 ASP A CB 1 ATOM 65 C CG . ASP A 1 70 ? 23.282 42.338 74.969 1.00 38.58 ? 63 ASP A CG 1 ATOM 66 O OD1 . ASP A 1 70 ? 24.093 42.803 74.140 1.00 40.36 ? 63 ASP A OD1 1 ATOM 67 O OD2 . ASP A 1 70 ? 23.335 42.610 76.194 1.00 40.51 ? 63 ASP A OD2 1 ATOM 68 N N . GLU A 1 71 ? 19.982 40.175 72.388 1.00 32.92 ? 64 GLU A N 1 ATOM 69 C CA . GLU A 1 71 ? 19.124 39.037 72.110 1.00 32.72 ? 64 GLU A CA 1 ATOM 70 C C . GLU A 1 71 ? 19.322 38.488 70.696 1.00 31.05 ? 64 GLU A C 1 ATOM 71 O O . GLU A 1 71 ? 19.130 37.287 70.476 1.00 31.55 ? 64 GLU A O 1 ATOM 72 C CB . GLU A 1 71 ? 17.658 39.373 72.398 1.00 32.84 ? 64 GLU A CB 1 ATOM 73 C CG . GLU A 1 71 ? 16.650 38.264 72.098 1.00 35.59 ? 64 GLU A CG 1 ATOM 74 C CD . GLU A 1 71 ? 16.840 37.023 72.968 1.00 40.79 ? 64 GLU A CD 1 ATOM 75 O OE1 . GLU A 1 71 ? 17.249 37.156 74.147 1.00 42.12 ? 64 GLU A OE1 1 ATOM 76 O OE2 . GLU A 1 71 ? 16.602 35.899 72.466 1.00 41.47 ? 64 GLU A OE2 1 ATOM 77 N N . LEU A 1 72 ? 19.731 39.354 69.759 1.00 30.01 ? 65 LEU A N 1 ATOM 78 C CA . LEU A 1 72 ? 20.092 38.922 68.392 1.00 28.73 ? 65 LEU A CA 1 ATOM 79 C C . LEU A 1 72 ? 21.237 37.892 68.401 1.00 29.78 ? 65 LEU A C 1 ATOM 80 O O . LEU A 1 72 ? 22.263 38.115 69.056 1.00 29.61 ? 65 LEU A O 1 ATOM 81 C CB . LEU A 1 72 ? 20.526 40.128 67.543 1.00 27.69 ? 65 LEU A CB 1 ATOM 82 C CG . LEU A 1 72 ? 19.566 41.318 67.454 1.00 26.10 ? 65 LEU A CG 1 ATOM 83 C CD1 . LEU A 1 72 ? 20.284 42.529 66.870 1.00 25.64 ? 65 LEU A CD1 1 ATOM 84 C CD2 . LEU A 1 72 ? 18.382 40.928 66.546 1.00 24.89 ? 65 LEU A CD2 1 ATOM 85 N N . LYS A 1 73 ? 21.081 36.806 67.643 1.00 29.42 ? 66 LYS A N 1 ATOM 86 C CA . LYS A 1 73 ? 22.105 35.753 67.605 1.00 30.88 ? 66 LYS A CA 1 ATOM 87 C C . LYS A 1 73 ? 22.497 35.389 66.190 1.00 29.52 ? 66 LYS A C 1 ATOM 88 O O . LYS A 1 73 ? 21.623 35.146 65.353 1.00 29.19 ? 66 LYS A O 1 ATOM 89 C CB . LYS A 1 73 ? 21.607 34.480 68.322 1.00 32.35 ? 66 LYS A CB 1 ATOM 90 C CG . LYS A 1 73 ? 21.182 34.689 69.796 1.00 36.00 ? 66 LYS A CG 1 ATOM 91 C CD . LYS A 1 73 ? 22.379 35.078 70.663 1.00 42.92 ? 66 LYS A CD 1 ATOM 92 C CE . LYS A 1 73 ? 22.091 34.943 72.163 1.00 45.74 ? 66 LYS A CE 1 ATOM 93 N NZ . LYS A 1 73 ? 21.317 36.106 72.671 1.00 44.28 ? 66 LYS A NZ 1 ATOM 94 N N . ALA A 1 74 ? 23.802 35.331 65.940 1.00 30.09 ? 67 ALA A N 1 ATOM 95 C CA . ALA A 1 74 ? 24.338 34.893 64.647 1.00 29.44 ? 67 ALA A CA 1 ATOM 96 C C . ALA A 1 74 ? 23.809 33.522 64.262 1.00 29.27 ? 67 ALA A C 1 ATOM 97 O O . ALA A 1 74 ? 23.483 33.286 63.086 1.00 27.23 ? 67 ALA A O 1 ATOM 98 C CB . ALA A 1 74 ? 25.878 34.889 64.651 1.00 30.14 ? 67 ALA A CB 1 ATOM 99 N N . GLU A 1 75 ? 23.726 32.622 65.237 1.00 29.73 ? 68 GLU A N 1 ATOM 100 C CA . GLU A 1 75 ? 23.309 31.247 64.938 1.00 30.32 ? 68 GLU A CA 1 ATOM 101 C C . GLU A 1 75 ? 21.864 31.183 64.451 1.00 29.64 ? 68 GLU A C 1 ATOM 102 O O . GLU A 1 75 ? 21.529 30.334 63.611 1.00 29.04 ? 68 GLU A O 1 ATOM 103 C CB . GLU A 1 75 ? 23.498 30.343 66.154 1.00 31.53 ? 68 GLU A CB 1 ATOM 104 C CG . GLU A 1 75 ? 23.086 28.877 65.894 0.80 34.75 ? 68 GLU A CG 1 ATOM 105 C CD . GLU A 1 75 ? 24.079 28.056 65.052 0.50 37.89 ? 68 GLU A CD 1 ATOM 106 O OE1 . GLU A 1 75 ? 25.213 28.505 64.761 0.60 36.99 ? 68 GLU A OE1 1 ATOM 107 O OE2 . GLU A 1 75 ? 23.712 26.917 64.695 0.50 40.93 ? 68 GLU A OE2 1 ATOM 108 N N . ASN A 1 76 ? 21.017 32.070 64.973 1.00 28.17 ? 69 ASN A N 1 ATOM 109 C CA . ASN A 1 76 ? 19.630 32.137 64.509 1.00 27.60 ? 69 ASN A CA 1 ATOM 110 C C . ASN A 1 76 ? 19.532 32.622 63.079 1.00 26.68 ? 69 ASN A C 1 ATOM 111 O O . ASN A 1 76 ? 18.748 32.085 62.298 1.00 26.34 ? 69 ASN A O 1 ATOM 112 C CB . ASN A 1 76 ? 18.758 33.022 65.413 1.00 28.17 ? 69 ASN A CB 1 ATOM 113 C CG . ASN A 1 76 ? 18.478 32.369 66.771 1.00 29.14 ? 69 ASN A CG 1 ATOM 114 O OD1 . ASN A 1 76 ? 18.423 31.135 66.889 1.00 32.24 ? 69 ASN A OD1 1 ATOM 115 N ND2 . ASN A 1 76 ? 18.333 33.195 67.804 1.00 29.67 ? 69 ASN A ND2 1 ATOM 116 N N . ILE A 1 77 ? 20.304 33.649 62.746 1.00 25.90 ? 70 ILE A N 1 ATOM 117 C CA . ILE A 1 77 ? 20.313 34.197 61.391 1.00 24.78 ? 70 ILE A CA 1 ATOM 118 C C . ILE A 1 77 ? 20.748 33.085 60.422 1.00 25.39 ? 70 ILE A C 1 ATOM 119 O O . ILE A 1 77 ? 20.152 32.918 59.343 1.00 24.91 ? 70 ILE A O 1 ATOM 120 C CB . ILE A 1 77 ? 21.254 35.430 61.290 1.00 24.76 ? 70 ILE A CB 1 ATOM 121 C CG1 . ILE A 1 77 ? 20.764 36.529 62.269 1.00 24.62 ? 70 ILE A CG1 1 ATOM 122 C CG2 . ILE A 1 77 ? 21.301 35.973 59.840 1.00 23.44 ? 70 ILE A CG2 1 ATOM 123 C CD1 . ILE A 1 77 ? 21.704 37.750 62.408 1.00 26.99 ? 70 ILE A CD1 1 ATOM 124 N N . LYS A 1 78 ? 21.763 32.319 60.838 1.00 25.21 ? 71 LYS A N 1 ATOM 125 C CA . LYS A 1 78 ? 22.256 31.177 60.043 1.00 25.75 ? 71 LYS A CA 1 ATOM 126 C C . LYS A 1 78 ? 21.139 30.154 59.795 1.00 26.70 ? 71 LYS A C 1 ATOM 127 O O . LYS A 1 78 ? 20.893 29.753 58.654 1.00 26.37 ? 71 LYS A O 1 ATOM 128 C CB . LYS A 1 78 ? 23.437 30.510 60.776 1.00 26.88 ? 71 LYS A CB 1 ATOM 129 C CG . LYS A 1 78 ? 24.029 29.317 60.034 1.00 27.33 ? 71 LYS A CG 1 ATOM 130 C CD . LYS A 1 78 ? 25.270 28.840 60.781 1.00 28.76 ? 71 LYS A CD 1 ATOM 131 C CE . LYS A 1 78 ? 25.862 27.655 60.080 1.00 32.60 ? 71 LYS A CE 1 ATOM 132 N NZ . LYS A 1 78 ? 26.997 27.080 60.904 1.00 32.57 ? 71 LYS A NZ 1 ATOM 133 N N . LYS A 1 79 ? 20.455 29.733 60.863 1.00 27.07 ? 72 LYS A N 1 ATOM 134 C CA . LYS A 1 79 ? 19.357 28.777 60.748 1.00 27.67 ? 72 LYS A CA 1 ATOM 135 C C . LYS A 1 79 ? 18.238 29.290 59.828 1.00 26.35 ? 72 LYS A C 1 ATOM 136 O O . LYS A 1 79 ? 17.706 28.545 59.002 1.00 26.41 ? 72 LYS A O 1 ATOM 137 C CB . LYS A 1 79 ? 18.788 28.424 62.129 1.00 28.15 ? 72 LYS A CB 1 ATOM 138 C CG . LYS A 1 79 ? 19.710 27.563 62.964 0.75 31.14 ? 72 LYS A CG 1 ATOM 139 C CD . LYS A 1 79 ? 19.232 27.488 64.409 0.65 33.44 ? 72 LYS A CD 1 ATOM 140 C CE . LYS A 1 79 ? 20.188 26.669 65.270 0.50 35.22 ? 72 LYS A CE 1 ATOM 141 N NZ . LYS A 1 79 ? 19.719 26.627 66.694 0.45 36.77 ? 72 LYS A NZ 1 ATOM 142 N N . PHE A 1 80 ? 17.904 30.574 59.955 1.00 24.96 ? 73 PHE A N 1 ATOM 143 C CA . PHE A 1 80 ? 16.861 31.146 59.113 1.00 24.07 ? 73 PHE A CA 1 ATOM 144 C C . PHE A 1 80 ? 17.304 31.205 57.652 1.00 23.83 ? 73 PHE A C 1 ATOM 145 O O . PHE A 1 80 ? 16.532 30.875 56.737 1.00 24.42 ? 73 PHE A O 1 ATOM 146 C CB . PHE A 1 80 ? 16.467 32.548 59.620 1.00 23.04 ? 73 PHE A CB 1 ATOM 147 C CG . PHE A 1 80 ? 15.886 32.550 61.002 1.00 25.01 ? 73 PHE A CG 1 ATOM 148 C CD1 . PHE A 1 80 ? 15.186 31.441 61.487 1.00 26.36 ? 73 PHE A CD1 1 ATOM 149 C CD2 . PHE A 1 80 ? 15.991 33.695 61.811 1.00 24.70 ? 73 PHE A CD2 1 ATOM 150 C CE1 . PHE A 1 80 ? 14.636 31.453 62.770 1.00 28.44 ? 73 PHE A CE1 1 ATOM 151 C CE2 . PHE A 1 80 ? 15.437 33.720 63.093 1.00 26.38 ? 73 PHE A CE2 1 ATOM 152 C CZ . PHE A 1 80 ? 14.757 32.606 63.570 1.00 27.79 ? 73 PHE A CZ 1 ATOM 153 N N . LEU A 1 81 ? 18.549 31.616 57.415 1.00 23.14 ? 74 LEU A N 1 ATOM 154 C CA . LEU A 1 81 ? 19.039 31.662 56.043 1.00 23.03 ? 74 LEU A CA 1 ATOM 155 C C . LEU A 1 81 ? 18.979 30.287 55.402 1.00 23.59 ? 74 LEU A C 1 ATOM 156 O O . LEU A 1 81 ? 18.487 30.159 54.278 1.00 23.60 ? 74 LEU A O 1 ATOM 157 C CB . LEU A 1 81 ? 20.467 32.187 55.966 1.00 23.03 ? 74 LEU A CB 1 ATOM 158 C CG . LEU A 1 81 ? 20.960 32.351 54.523 1.00 23.13 ? 74 LEU A CG 1 ATOM 159 C CD1 . LEU A 1 81 ? 20.100 33.398 53.774 1.00 20.87 ? 74 LEU A CD1 1 ATOM 160 C CD2 . LEU A 1 81 ? 22.402 32.771 54.522 1.00 25.20 ? 74 LEU A CD2 1 ATOM 161 N N . TYR A 1 82 ? 19.456 29.255 56.108 1.00 23.47 ? 75 TYR A N 1 ATOM 162 C CA . TYR A 1 82 ? 19.365 27.898 55.583 1.00 24.44 ? 75 TYR A CA 1 ATOM 163 C C . TYR A 1 82 ? 17.890 27.556 55.253 1.00 24.65 ? 75 TYR A C 1 ATOM 164 O O . TYR A 1 82 ? 17.572 27.052 54.175 1.00 25.02 ? 75 TYR A O 1 ATOM 165 C CB . TYR A 1 82 ? 19.941 26.905 56.603 1.00 24.89 ? 75 TYR A CB 1 ATOM 166 C CG . TYR A 1 82 ? 19.892 25.501 56.089 1.00 27.23 ? 75 TYR A CG 1 ATOM 167 C CD1 . TYR A 1 82 ? 20.891 25.022 55.248 1.00 28.55 ? 75 TYR A CD1 1 ATOM 168 C CD2 . TYR A 1 82 ? 18.815 24.670 56.400 1.00 30.52 ? 75 TYR A CD2 1 ATOM 169 C CE1 . TYR A 1 82 ? 20.848 23.718 54.759 1.00 30.00 ? 75 TYR A CE1 1 ATOM 170 C CE2 . TYR A 1 82 ? 18.752 23.359 55.908 1.00 32.53 ? 75 TYR A CE2 1 ATOM 171 C CZ . TYR A 1 82 ? 19.768 22.905 55.086 1.00 31.97 ? 75 TYR A CZ 1 ATOM 172 O OH . TYR A 1 82 ? 19.730 21.623 54.579 1.00 36.53 ? 75 TYR A OH 1 ATOM 173 N N . ASN A 1 83 ? 16.988 27.876 56.174 1.00 24.72 ? 76 ASN A N 1 ATOM 174 C CA . ASN A 1 83 ? 15.576 27.551 56.017 1.00 24.85 ? 76 ASN A CA 1 ATOM 175 C C . ASN A 1 83 ? 14.917 28.236 54.813 1.00 24.05 ? 76 ASN A C 1 ATOM 176 O O . ASN A 1 83 ? 13.985 27.679 54.191 1.00 24.84 ? 76 ASN A O 1 ATOM 177 C CB . ASN A 1 83 ? 14.836 27.955 57.281 1.00 25.85 ? 76 ASN A CB 1 ATOM 178 C CG . ASN A 1 83 ? 13.376 27.634 57.229 1.00 27.53 ? 76 ASN A CG 1 ATOM 179 O OD1 . ASN A 1 83 ? 12.555 28.469 56.841 1.00 27.59 ? 76 ASN A OD1 1 ATOM 180 N ND2 . ASN A 1 83 ? 13.032 26.397 57.612 1.00 29.74 ? 76 ASN A ND2 1 ATOM 181 N N . PHE A 1 84 ? 15.400 29.434 54.490 1.00 22.17 ? 77 PHE A N 1 ATOM 182 C CA . PHE A 1 84 ? 14.785 30.249 53.433 1.00 21.32 ? 77 PHE A CA 1 ATOM 183 C C . PHE A 1 84 ? 15.340 29.985 52.021 1.00 21.66 ? 77 PHE A C 1 ATOM 184 O O . PHE A 1 84 ? 14.860 30.591 51.045 1.00 21.80 ? 77 PHE A O 1 ATOM 185 C CB . PHE A 1 84 ? 15.006 31.749 53.726 1.00 20.98 ? 77 PHE A CB 1 ATOM 186 C CG . PHE A 1 84 ? 14.273 32.291 54.935 1.00 22.19 ? 77 PHE A CG 1 ATOM 187 C CD1 . PHE A 1 84 ? 13.330 31.548 55.634 1.00 23.55 ? 77 PHE A CD1 1 ATOM 188 C CD2 . PHE A 1 84 ? 14.540 33.597 55.348 1.00 22.40 ? 77 PHE A CD2 1 ATOM 189 C CE1 . PHE A 1 84 ? 12.647 32.115 56.763 1.00 22.25 ? 77 PHE A CE1 1 ATOM 190 C CE2 . PHE A 1 84 ? 13.873 34.180 56.448 1.00 23.68 ? 77 PHE A CE2 1 ATOM 191 C CZ . PHE A 1 84 ? 12.917 33.437 57.154 1.00 22.28 ? 77 PHE A CZ 1 ATOM 192 N N . THR A 1 85 ? 16.357 29.120 51.894 1.00 22.69 ? 78 THR A N 1 ATOM 193 C CA . THR A 1 85 ? 17.112 29.039 50.647 1.00 22.36 ? 78 THR A CA 1 ATOM 194 C C . THR A 1 85 ? 17.219 27.617 50.070 1.00 23.47 ? 78 THR A C 1 ATOM 195 O O . THR A 1 85 ? 18.052 27.383 49.194 1.00 22.60 ? 78 THR A O 1 ATOM 196 C CB . THR A 1 85 ? 18.565 29.586 50.846 1.00 22.96 ? 78 THR A CB 1 ATOM 197 O OG1 . THR A 1 85 ? 19.196 28.870 51.921 1.00 22.55 ? 78 THR A OG1 1 ATOM 198 C CG2 . THR A 1 85 ? 18.541 31.120 51.169 1.00 21.78 ? 78 THR A CG2 1 ATOM 199 N N . GLN A 1 86 ? 16.395 26.686 50.553 1.00 23.91 ? 79 GLN A N 1 ATOM 200 C CA . GLN A 1 86 ? 16.489 25.282 50.098 1.00 26.73 ? 79 GLN A CA 1 ATOM 201 C C . GLN A 1 86 ? 15.794 25.046 48.761 1.00 26.80 ? 79 GLN A C 1 ATOM 202 O O . GLN A 1 86 ? 16.114 24.081 48.053 1.00 27.96 ? 79 GLN A O 1 ATOM 203 C CB . GLN A 1 86 ? 15.902 24.343 51.169 1.00 27.40 ? 79 GLN A CB 1 ATOM 204 C CG . GLN A 1 86 ? 16.711 24.351 52.452 0.90 27.77 ? 79 GLN A CG 1 ATOM 205 C CD . GLN A 1 86 ? 18.172 24.193 52.154 0.75 28.29 ? 79 GLN A CD 1 ATOM 206 O OE1 . GLN A 1 86 ? 18.589 23.107 51.733 0.75 31.14 ? 79 GLN A OE1 1 ATOM 207 N NE2 . GLN A 1 86 ? 18.965 25.274 52.316 0.75 28.40 ? 79 GLN A NE2 1 ATOM 208 N N . ILE A 1 87 ? 14.802 25.885 48.456 1.00 27.08 ? 80 ILE A N 1 ATOM 209 C CA . ILE A 1 87 ? 14.047 25.774 47.207 1.00 26.58 ? 80 ILE A CA 1 ATOM 210 C C . ILE A 1 87 ? 13.888 27.178 46.637 1.00 25.30 ? 80 ILE A C 1 ATOM 211 O O . ILE A 1 87 ? 14.010 28.144 47.402 1.00 24.78 ? 80 ILE A O 1 ATOM 212 C CB . ILE A 1 87 ? 12.647 25.114 47.422 1.00 28.12 ? 80 ILE A CB 1 ATOM 213 C CG1 . ILE A 1 87 ? 11.769 25.959 48.349 1.00 28.72 ? 80 ILE A CG1 1 ATOM 214 C CG2 . ILE A 1 87 ? 12.808 23.661 47.920 1.00 30.61 ? 80 ILE A CG2 1 ATOM 215 C CD1 . ILE A 1 87 ? 10.338 25.493 48.403 1.00 32.78 ? 80 ILE A CD1 1 ATOM 216 N N . PRO A 1 88 ? 13.590 27.297 45.321 1.00 24.49 ? 81 PRO A N 1 ATOM 217 C CA . PRO A 1 88 ? 13.368 28.645 44.774 1.00 23.63 ? 81 PRO A CA 1 ATOM 218 C C . PRO A 1 88 ? 12.101 29.277 45.336 1.00 22.54 ? 81 PRO A C 1 ATOM 219 O O . PRO A 1 88 ? 11.126 28.567 45.638 1.00 23.38 ? 81 PRO A O 1 ATOM 220 C CB . PRO A 1 88 ? 13.194 28.388 43.264 1.00 24.29 ? 81 PRO A CB 1 ATOM 221 C CG . PRO A 1 88 ? 13.954 27.090 43.017 1.00 25.58 ? 81 PRO A CG 1 ATOM 222 C CD . PRO A 1 88 ? 13.620 26.269 44.254 1.00 24.34 ? 81 PRO A CD 1 ATOM 223 N N . HIS A 1 89 ? 12.110 30.607 45.469 1.00 21.03 ? 82 HIS A N 1 ATOM 224 C CA . HIS A 1 89 ? 10.919 31.341 45.905 1.00 20.94 ? 82 HIS A CA 1 ATOM 225 C C . HIS A 1 89 ? 10.584 32.454 44.919 1.00 20.01 ? 82 HIS A C 1 ATOM 226 O O . HIS A 1 89 ? 10.493 33.630 45.301 1.00 20.49 ? 82 HIS A O 1 ATOM 227 C CB . HIS A 1 89 ? 11.103 31.909 47.334 1.00 21.64 ? 82 HIS A CB 1 ATOM 228 C CG . HIS A 1 89 ? 11.254 30.831 48.367 1.00 21.67 ? 82 HIS A CG 1 ATOM 229 N ND1 . HIS A 1 89 ? 12.479 30.491 48.892 1.00 23.22 ? 82 HIS A ND1 1 ATOM 230 C CD2 . HIS A 1 89 ? 10.356 29.959 48.897 1.00 22.15 ? 82 HIS A CD2 1 ATOM 231 C CE1 . HIS A 1 89 ? 12.327 29.481 49.734 1.00 24.93 ? 82 HIS A CE1 1 ATOM 232 N NE2 . HIS A 1 89 ? 11.048 29.142 49.761 1.00 23.74 ? 82 HIS A NE2 1 ATOM 233 N N . LEU A 1 90 ? 10.361 32.073 43.670 1.00 20.50 ? 83 LEU A N 1 ATOM 234 C CA . LEU A 1 90 ? 10.073 33.051 42.601 1.00 19.99 ? 83 LEU A CA 1 ATOM 235 C C . LEU A 1 90 ? 8.714 33.704 42.853 1.00 19.62 ? 83 LEU A C 1 ATOM 236 O O . LEU A 1 90 ? 7.763 33.030 43.249 1.00 21.03 ? 83 LEU A O 1 ATOM 237 C CB . LEU A 1 90 ? 10.088 32.355 41.223 1.00 19.86 ? 83 LEU A CB 1 ATOM 238 C CG . LEU A 1 90 ? 9.915 33.293 40.000 1.00 19.78 ? 83 LEU A CG 1 ATOM 239 C CD1 . LEU A 1 90 ? 11.117 34.171 39.784 1.00 19.15 ? 83 LEU A CD1 1 ATOM 240 C CD2 . LEU A 1 90 ? 9.793 32.269 38.705 1.00 20.49 ? 83 LEU A CD2 1 ATOM 241 N N . ALA A 1 91 ? 8.633 35.028 42.669 1.00 18.76 ? 84 ALA A N 1 ATOM 242 C CA . ALA A 1 91 ? 7.351 35.718 42.854 1.00 18.34 ? 84 ALA A CA 1 ATOM 243 C C . ALA A 1 91 ? 6.237 35.073 42.018 1.00 19.76 ? 84 ALA A C 1 ATOM 244 O O . ALA A 1 91 ? 6.441 34.696 40.845 1.00 20.33 ? 84 ALA A O 1 ATOM 245 C CB . ALA A 1 91 ? 7.466 37.183 42.486 1.00 18.76 ? 84 ALA A CB 1 ATOM 246 N N . GLY A 1 92 ? 5.085 34.931 42.658 1.00 20.40 ? 85 GLY A N 1 ATOM 247 C CA . GLY A 1 92 ? 3.866 34.418 41.997 1.00 21.53 ? 85 GLY A CA 1 ATOM 248 C C . GLY A 1 92 ? 3.815 32.907 41.968 1.00 23.32 ? 85 GLY A C 1 ATOM 249 O O . GLY A 1 92 ? 2.854 32.343 41.410 1.00 24.72 ? 85 GLY A O 1 ATOM 250 N N . THR A 1 93 ? 4.815 32.230 42.529 1.00 21.80 ? 86 THR A N 1 ATOM 251 C CA . THR A 1 93 ? 4.780 30.759 42.568 1.00 22.74 ? 86 THR A CA 1 ATOM 252 C C . THR A 1 93 ? 4.222 30.211 43.891 1.00 23.28 ? 86 THR A C 1 ATOM 253 O O . THR A 1 93 ? 4.257 30.870 44.910 1.00 22.88 ? 86 THR A O 1 ATOM 254 C CB . THR A 1 93 ? 6.179 30.118 42.301 1.00 22.78 ? 86 THR A CB 1 ATOM 255 O OG1 . THR A 1 93 ? 7.082 30.434 43.365 1.00 23.26 ? 86 THR A OG1 1 ATOM 256 C CG2 . THR A 1 93 ? 6.773 30.582 40.966 1.00 22.87 ? 86 THR A CG2 1 ATOM 257 N N . GLU A 1 94 ? 3.773 28.963 43.876 1.00 24.52 ? 87 GLU A N 1 ATOM 258 C CA . GLU A 1 94 ? 3.254 28.339 45.082 1.00 25.83 ? 87 GLU A CA 1 ATOM 259 C C . GLU A 1 94 ? 4.277 28.296 46.227 1.00 25.95 ? 87 GLU A C 1 ATOM 260 O O . GLU A 1 94 ? 3.915 28.539 47.389 1.00 26.18 ? 87 GLU A O 1 ATOM 261 C CB . GLU A 1 94 ? 2.717 26.929 44.766 1.00 28.14 ? 87 GLU A CB 1 ATOM 262 C CG . GLU A 1 94 ? 2.189 26.206 46.006 0.90 31.26 ? 87 GLU A CG 1 ATOM 263 C CD . GLU A 1 94 ? 0.878 26.779 46.570 0.70 33.81 ? 87 GLU A CD 1 ATOM 264 O OE1 . GLU A 1 94 ? 0.522 26.383 47.705 0.50 36.38 ? 87 GLU A OE1 1 ATOM 265 O OE2 . GLU A 1 94 ? 0.203 27.609 45.908 0.50 33.68 ? 87 GLU A OE2 1 ATOM 266 N N . GLN A 1 95 ? 5.541 28.027 45.886 1.00 25.53 ? 88 GLN A N 1 ATOM 267 C CA A GLN A 1 95 ? 6.601 27.952 46.883 0.50 26.00 ? 88 GLN A CA 1 ATOM 268 C CA C GLN A 1 95 ? 6.625 27.965 46.876 0.50 26.09 ? 88 GLN A CA 1 ATOM 269 C C . GLN A 1 95 ? 6.753 29.279 47.647 1.00 24.15 ? 88 GLN A C 1 ATOM 270 O O . GLN A 1 95 ? 7.007 29.288 48.857 1.00 24.37 ? 88 GLN A O 1 ATOM 271 C CB A GLN A 1 95 ? 7.915 27.528 46.225 0.50 26.38 ? 88 GLN A CB 1 ATOM 272 C CB C GLN A 1 95 ? 7.956 27.623 46.200 0.50 26.48 ? 88 GLN A CB 1 ATOM 273 C CG A GLN A 1 95 ? 7.805 26.237 45.383 0.50 28.35 ? 88 GLN A CG 1 ATOM 274 C CG C GLN A 1 95 ? 8.089 26.151 45.814 0.50 29.16 ? 88 GLN A CG 1 ATOM 275 C CD A GLN A 1 95 ? 7.591 26.494 43.885 0.50 28.06 ? 88 GLN A CD 1 ATOM 276 C CD C GLN A 1 95 ? 8.843 25.938 44.493 0.50 30.08 ? 88 GLN A CD 1 ATOM 277 O OE1 A GLN A 1 95 ? 6.573 27.023 43.476 0.50 24.29 ? 88 GLN A OE1 1 ATOM 278 O OE1 C GLN A 1 95 ? 9.899 26.551 44.220 0.50 27.81 ? 88 GLN A OE1 1 ATOM 279 N NE2 A GLN A 1 95 ? 8.554 26.048 43.054 0.50 31.89 ? 88 GLN A NE2 1 ATOM 280 N NE2 C GLN A 1 95 ? 8.287 25.056 43.650 0.50 32.94 ? 88 GLN A NE2 1 ATOM 281 N N . ASN A 1 96 ? 6.580 30.399 46.947 1.00 23.38 ? 89 ASN A N 1 ATOM 282 C CA . ASN A 1 96 ? 6.721 31.682 47.612 1.00 22.74 ? 89 ASN A CA 1 ATOM 283 C C . ASN A 1 96 ? 5.488 32.056 48.457 1.00 24.08 ? 89 ASN A C 1 ATOM 284 O O . ASN A 1 96 ? 5.608 32.790 49.459 1.00 24.88 ? 89 ASN A O 1 ATOM 285 C CB . ASN A 1 96 ? 7.038 32.791 46.609 1.00 22.29 ? 89 ASN A CB 1 ATOM 286 C CG . ASN A 1 96 ? 7.628 34.021 47.301 1.00 23.91 ? 89 ASN A CG 1 ATOM 287 O OD1 . ASN A 1 96 ? 8.348 33.890 48.299 1.00 22.91 ? 89 ASN A OD1 1 ATOM 288 N ND2 . ASN A 1 96 ? 7.369 35.191 46.759 1.00 23.02 ? 89 ASN A ND2 1 ATOM 289 N N . PHE A 1 97 ? 4.306 31.581 48.047 1.00 23.46 ? 90 PHE A N 1 ATOM 290 C CA . PHE A 1 97 ? 3.096 31.701 48.876 1.00 23.32 ? 90 PHE A CA 1 ATOM 291 C C . PHE A 1 97 ? 3.280 30.860 50.145 1.00 23.73 ? 90 PHE A C 1 ATOM 292 O O . PHE A 1 97 ? 2.969 31.326 51.241 1.00 22.74 ? 90 PHE A O 1 ATOM 293 C CB A PHE A 1 97 ? 1.875 31.237 48.057 0.65 24.18 ? 90 PHE A CB 1 ATOM 294 C CB B PHE A 1 97 ? 1.826 31.254 48.141 0.35 23.31 ? 90 PHE A CB 1 ATOM 295 C CG A PHE A 1 97 ? 0.555 31.282 48.794 0.65 25.46 ? 90 PHE A CG 1 ATOM 296 C CG B PHE A 1 97 ? 0.640 31.052 49.056 0.35 22.48 ? 90 PHE A CG 1 ATOM 297 C CD1 A PHE A 1 97 ? 0.235 32.321 49.671 0.65 25.65 ? 90 PHE A CD1 1 ATOM 298 C CD1 B PHE A 1 97 ? -0.028 32.138 49.599 0.35 21.13 ? 90 PHE A CD1 1 ATOM 299 C CD2 A PHE A 1 97 ? -0.392 30.294 48.554 0.65 30.15 ? 90 PHE A CD2 1 ATOM 300 C CD2 B PHE A 1 97 ? 0.214 29.772 49.393 0.35 21.38 ? 90 PHE A CD2 1 ATOM 301 C CE1 A PHE A 1 97 ? -1.009 32.363 50.319 0.65 27.74 ? 90 PHE A CE1 1 ATOM 302 C CE1 B PHE A 1 97 ? -1.113 31.963 50.442 0.35 21.77 ? 90 PHE A CE1 1 ATOM 303 C CE2 A PHE A 1 97 ? -1.629 30.314 49.191 0.65 31.37 ? 90 PHE A CE2 1 ATOM 304 C CE2 B PHE A 1 97 ? -0.869 29.588 50.235 0.35 21.88 ? 90 PHE A CE2 1 ATOM 305 C CZ A PHE A 1 97 ? -1.942 31.359 50.079 0.65 31.35 ? 90 PHE A CZ 1 ATOM 306 C CZ B PHE A 1 97 ? -1.532 30.679 50.766 0.35 22.19 ? 90 PHE A CZ 1 ATOM 307 N N A GLN A 1 98 ? 3.800 29.645 50.013 0.60 23.71 ? 91 GLN A N 1 ATOM 308 N N B GLN A 1 98 ? 3.801 29.643 49.974 0.40 23.70 ? 91 GLN A N 1 ATOM 309 C CA A GLN A 1 98 ? 4.016 28.838 51.224 0.60 25.11 ? 91 GLN A CA 1 ATOM 310 C CA B GLN A 1 98 ? 4.118 28.761 51.106 0.40 25.00 ? 91 GLN A CA 1 ATOM 311 C C A GLN A 1 98 ? 5.036 29.474 52.175 0.60 24.34 ? 91 GLN A C 1 ATOM 312 C C B GLN A 1 98 ? 5.028 29.450 52.123 0.40 24.26 ? 91 GLN A C 1 ATOM 313 O O A GLN A 1 98 ? 4.860 29.436 53.395 0.60 24.92 ? 91 GLN A O 1 ATOM 314 O O B GLN A 1 98 ? 4.764 29.425 53.328 0.40 24.85 ? 91 GLN A O 1 ATOM 315 C CB A GLN A 1 98 ? 4.382 27.388 50.877 0.60 26.08 ? 91 GLN A CB 1 ATOM 316 C CB B GLN A 1 98 ? 4.736 27.441 50.611 0.40 25.28 ? 91 GLN A CB 1 ATOM 317 C CG A GLN A 1 98 ? 3.232 26.641 50.175 0.60 28.74 ? 91 GLN A CG 1 ATOM 318 C CG B GLN A 1 98 ? 3.696 26.529 49.958 0.40 28.89 ? 91 GLN A CG 1 ATOM 319 C CD A GLN A 1 98 ? 1.979 26.463 51.028 0.60 33.32 ? 91 GLN A CD 1 ATOM 320 C CD B GLN A 1 98 ? 4.277 25.284 49.296 0.40 31.11 ? 91 GLN A CD 1 ATOM 321 O OE1 A GLN A 1 98 ? 0.821 26.474 50.371 0.60 36.10 ? 91 GLN A OE1 1 ATOM 322 O OE1 B GLN A 1 98 ? 5.491 25.152 49.120 0.40 35.13 ? 91 GLN A OE1 1 ATOM 323 N NE2 A GLN A 1 98 ? 2.046 26.295 52.256 0.60 35.32 ? 91 GLN A NE2 1 ATOM 324 N NE2 B GLN A 1 98 ? 3.398 24.359 48.926 0.40 35.02 ? 91 GLN A NE2 1 ATOM 325 N N . LEU A 1 99 ? 6.086 30.086 51.626 1.00 23.36 ? 92 LEU A N 1 ATOM 326 C CA . LEU A 1 99 ? 7.030 30.775 52.493 1.00 23.07 ? 92 LEU A CA 1 ATOM 327 C C . LEU A 1 99 ? 6.356 31.968 53.190 1.00 22.47 ? 92 LEU A C 1 ATOM 328 O O . LEU A 1 99 ? 6.590 32.202 54.401 1.00 22.77 ? 92 LEU A O 1 ATOM 329 C CB . LEU A 1 99 ? 8.286 31.199 51.718 1.00 21.59 ? 92 LEU A CB 1 ATOM 330 C CG . LEU A 1 99 ? 9.376 31.816 52.597 1.00 21.52 ? 92 LEU A CG 1 ATOM 331 C CD1 . LEU A 1 99 ? 9.871 30.830 53.711 1.00 23.32 ? 92 LEU A CD1 1 ATOM 332 C CD2 . LEU A 1 99 ? 10.531 32.292 51.739 1.00 20.43 ? 92 LEU A CD2 1 ATOM 333 N N . ALA A 1 100 ? 5.513 32.713 52.460 1.00 21.75 ? 93 ALA A N 1 ATOM 334 C CA . ALA A 1 100 ? 4.763 33.811 53.102 1.00 21.80 ? 93 ALA A CA 1 ATOM 335 C C . ALA A 1 100 ? 3.936 33.327 54.298 1.00 22.62 ? 93 ALA A C 1 ATOM 336 O O . ALA A 1 100 ? 3.936 33.955 55.357 1.00 22.57 ? 93 ALA A O 1 ATOM 337 C CB . ALA A 1 100 ? 3.853 34.543 52.092 1.00 21.32 ? 93 ALA A CB 1 ATOM 338 N N A LYS A 1 101 ? 3.246 32.214 54.115 0.50 22.78 ? 94 LYS A N 1 ATOM 339 N N B LYS A 1 101 ? 3.228 32.218 54.113 0.50 22.85 ? 94 LYS A N 1 ATOM 340 C CA A LYS A 1 101 ? 2.427 31.641 55.184 0.50 23.93 ? 94 LYS A CA 1 ATOM 341 C CA B LYS A 1 101 ? 2.416 31.628 55.193 0.50 24.07 ? 94 LYS A CA 1 ATOM 342 C C A LYS A 1 101 ? 3.280 31.187 56.372 0.50 24.64 ? 94 LYS A C 1 ATOM 343 C C B LYS A 1 101 ? 3.291 31.210 56.378 0.50 24.68 ? 94 LYS A C 1 ATOM 344 O O A LYS A 1 101 ? 2.875 31.349 57.536 0.50 24.84 ? 94 LYS A O 1 ATOM 345 O O B LYS A 1 101 ? 2.908 31.405 57.545 0.50 24.83 ? 94 LYS A O 1 ATOM 346 C CB A LYS A 1 101 ? 1.582 30.507 54.617 0.50 24.49 ? 94 LYS A CB 1 ATOM 347 C CB B LYS A 1 101 ? 1.604 30.437 54.672 0.50 24.68 ? 94 LYS A CB 1 ATOM 348 C CG A LYS A 1 101 ? 0.456 31.049 53.742 0.50 25.96 ? 94 LYS A CG 1 ATOM 349 C CG B LYS A 1 101 ? 0.384 30.845 53.834 0.50 26.88 ? 94 LYS A CG 1 ATOM 350 C CD A LYS A 1 101 ? -0.564 29.975 53.404 0.50 28.51 ? 94 LYS A CD 1 ATOM 351 C CD B LYS A 1 101 ? -0.449 31.951 54.503 0.50 28.15 ? 94 LYS A CD 1 ATOM 352 C CE A LYS A 1 101 ? -0.096 29.208 52.208 0.50 29.96 ? 94 LYS A CE 1 ATOM 353 C CE B LYS A 1 101 ? -1.656 31.466 55.343 0.50 30.45 ? 94 LYS A CE 1 ATOM 354 N NZ A LYS A 1 101 ? -1.056 28.165 51.793 0.50 32.58 ? 94 LYS A NZ 1 ATOM 355 N NZ B LYS A 1 101 ? -2.566 32.644 55.736 0.50 26.55 ? 94 LYS A NZ 1 ATOM 356 N N . GLN A 1 102 ? 4.465 30.645 56.081 1.00 24.96 ? 95 GLN A N 1 ATOM 357 C CA . GLN A 1 102 ? 5.411 30.249 57.139 1.00 25.42 ? 95 GLN A CA 1 ATOM 358 C C . GLN A 1 102 ? 5.867 31.472 57.945 1.00 25.16 ? 95 GLN A C 1 ATOM 359 O O . GLN A 1 102 ? 5.846 31.457 59.169 1.00 25.24 ? 95 GLN A O 1 ATOM 360 C CB . GLN A 1 102 ? 6.626 29.522 56.565 1.00 25.59 ? 95 GLN A CB 1 ATOM 361 C CG . GLN A 1 102 ? 7.635 29.168 57.677 1.00 26.07 ? 95 GLN A CG 1 ATOM 362 C CD . GLN A 1 102 ? 8.975 28.873 57.103 1.00 25.74 ? 95 GLN A CD 1 ATOM 363 O OE1 . GLN A 1 102 ? 9.088 28.145 56.095 1.00 26.70 ? 95 GLN A OE1 1 ATOM 364 N NE2 . GLN A 1 102 ? 10.015 29.405 57.733 1.00 26.23 ? 95 GLN A NE2 1 ATOM 365 N N . ILE A 1 103 ? 6.251 32.538 57.240 1.00 23.95 ? 96 ILE A N 1 ATOM 366 C CA . ILE A 1 103 ? 6.728 33.756 57.899 1.00 23.93 ? 96 ILE A CA 1 ATOM 367 C C . ILE A 1 103 ? 5.597 34.363 58.736 1.00 24.26 ? 96 ILE A C 1 ATOM 368 O O . ILE A 1 103 ? 5.804 34.792 59.876 1.00 23.80 ? 96 ILE A O 1 ATOM 369 C CB . ILE A 1 103 ? 7.244 34.785 56.859 1.00 23.53 ? 96 ILE A CB 1 ATOM 370 C CG1 A ILE A 1 103 ? 8.406 34.248 56.000 0.65 25.90 ? 96 ILE A CG1 1 ATOM 371 C CG1 B ILE A 1 103 ? 8.585 34.246 56.348 0.35 23.98 ? 96 ILE A CG1 1 ATOM 372 C CG2 . ILE A 1 103 ? 7.528 36.162 57.525 1.00 24.13 ? 96 ILE A CG2 1 ATOM 373 C CD1 A ILE A 1 103 ? 9.658 33.988 56.735 0.65 24.41 ? 96 ILE A CD1 1 ATOM 374 C CD1 B ILE A 1 103 ? 9.100 34.881 55.113 0.35 20.45 ? 96 ILE A CD1 1 ATOM 375 N N . GLN A 1 104 ? 4.401 34.404 58.165 1.00 23.36 ? 97 GLN A N 1 ATOM 376 C CA . GLN A 1 104 ? 3.245 34.913 58.920 1.00 24.92 ? 97 GLN A CA 1 ATOM 377 C C . GLN A 1 104 ? 3.078 34.140 60.236 1.00 26.05 ? 97 GLN A C 1 ATOM 378 O O . GLN A 1 104 ? 2.943 34.744 61.311 1.00 26.69 ? 97 GLN A O 1 ATOM 379 C CB . GLN A 1 104 ? 1.978 34.798 58.067 1.00 25.12 ? 97 GLN A CB 1 ATOM 380 C CG . GLN A 1 104 ? 0.687 35.213 58.804 1.00 26.50 ? 97 GLN A CG 1 ATOM 381 C CD . GLN A 1 104 ? -0.571 34.983 57.979 1.00 27.77 ? 97 GLN A CD 1 ATOM 382 O OE1 . GLN A 1 104 ? -0.626 34.094 57.117 1.00 28.36 ? 97 GLN A OE1 1 ATOM 383 N NE2 . GLN A 1 104 ? -1.586 35.787 58.237 1.00 26.84 ? 97 GLN A NE2 1 ATOM 384 N N . SER A 1 105 ? 3.114 32.812 60.154 1.00 26.93 ? 98 SER A N 1 ATOM 385 C CA . SER A 1 105 ? 2.945 31.970 61.347 1.00 27.67 ? 98 SER A CA 1 ATOM 386 C C . SER A 1 105 ? 4.040 32.232 62.370 1.00 27.51 ? 98 SER A C 1 ATOM 387 O O . SER A 1 105 ? 3.769 32.345 63.583 1.00 27.45 ? 98 SER A O 1 ATOM 388 C CB . SER A 1 105 ? 2.960 30.496 60.946 1.00 28.08 ? 98 SER A CB 1 ATOM 389 O OG A SER A 1 105 ? 2.721 29.667 62.058 0.50 28.03 ? 98 SER A OG 1 ATOM 390 O OG B SER A 1 105 ? 1.690 30.165 60.403 0.50 30.88 ? 98 SER A OG 1 ATOM 391 N N . GLN A 1 106 ? 5.283 32.309 61.888 1.00 25.80 ? 99 GLN A N 1 ATOM 392 C CA . GLN A 1 106 ? 6.403 32.509 62.811 1.00 26.60 ? 99 GLN A CA 1 ATOM 393 C C . GLN A 1 106 ? 6.363 33.894 63.450 1.00 25.32 ? 99 GLN A C 1 ATOM 394 O O . GLN A 1 106 ? 6.595 34.025 64.640 1.00 26.63 ? 99 GLN A O 1 ATOM 395 C CB . GLN A 1 106 ? 7.742 32.254 62.121 1.00 25.88 ? 99 GLN A CB 1 ATOM 396 C CG . GLN A 1 106 ? 7.869 30.790 61.725 1.00 28.04 ? 99 GLN A CG 1 ATOM 397 C CD . GLN A 1 106 ? 9.221 30.481 61.130 1.00 30.19 ? 99 GLN A CD 1 ATOM 398 O OE1 . GLN A 1 106 ? 9.564 30.970 60.068 1.00 30.61 ? 99 GLN A OE1 1 ATOM 399 N NE2 . GLN A 1 106 ? 9.995 29.646 61.827 1.00 36.67 ? 99 GLN A NE2 1 ATOM 400 N N . TRP A 1 107 ? 6.071 34.939 62.674 1.00 24.53 ? 100 TRP A N 1 ATOM 401 C CA . TRP A 1 107 ? 5.962 36.261 63.270 1.00 24.13 ? 100 TRP A CA 1 ATOM 402 C C . TRP A 1 107 ? 4.891 36.339 64.363 1.00 25.66 ? 100 TRP A C 1 ATOM 403 O O . TRP A 1 107 ? 5.082 37.042 65.360 1.00 26.10 ? 100 TRP A O 1 ATOM 404 C CB . TRP A 1 107 ? 5.704 37.317 62.182 1.00 22.91 ? 100 TRP A CB 1 ATOM 405 C CG . TRP A 1 107 ? 6.932 37.625 61.402 1.00 23.15 ? 100 TRP A CG 1 ATOM 406 C CD1 . TRP A 1 107 ? 8.160 36.982 61.464 1.00 24.49 ? 100 TRP A CD1 1 ATOM 407 C CD2 . TRP A 1 107 ? 7.050 38.609 60.369 1.00 22.33 ? 100 TRP A CD2 1 ATOM 408 N NE1 . TRP A 1 107 ? 9.027 37.543 60.561 1.00 22.99 ? 100 TRP A NE1 1 ATOM 409 C CE2 . TRP A 1 107 ? 8.372 38.533 59.863 1.00 22.33 ? 100 TRP A CE2 1 ATOM 410 C CE3 . TRP A 1 107 ? 6.160 39.562 59.826 1.00 21.68 ? 100 TRP A CE3 1 ATOM 411 C CZ2 . TRP A 1 107 ? 8.838 39.377 58.846 1.00 22.83 ? 100 TRP A CZ2 1 ATOM 412 C CZ3 . TRP A 1 107 ? 6.613 40.393 58.817 1.00 21.09 ? 100 TRP A CZ3 1 ATOM 413 C CH2 . TRP A 1 107 ? 7.942 40.307 58.334 1.00 21.93 ? 100 TRP A CH2 1 ATOM 414 N N . LYS A 1 108 ? 3.779 35.620 64.172 1.00 27.05 ? 101 LYS A N 1 ATOM 415 C CA . LYS A 1 108 ? 2.748 35.496 65.234 1.00 29.85 ? 101 LYS A CA 1 ATOM 416 C C . LYS A 1 108 ? 3.328 34.809 66.477 1.00 30.10 ? 101 LYS A C 1 ATOM 417 O O . LYS A 1 108 ? 3.165 35.316 67.600 1.00 31.38 ? 101 LYS A O 1 ATOM 418 C CB . LYS A 1 108 ? 1.526 34.710 64.748 1.00 30.85 ? 101 LYS A CB 1 ATOM 419 C CG . LYS A 1 108 ? 0.673 35.467 63.791 1.00 34.91 ? 101 LYS A CG 1 ATOM 420 C CD . LYS A 1 108 ? -0.419 34.603 63.188 1.00 40.87 ? 101 LYS A CD 1 ATOM 421 C CE . LYS A 1 108 ? -1.397 35.516 62.426 1.00 43.15 ? 101 LYS A CE 1 ATOM 422 N NZ . LYS A 1 108 ? -2.403 34.724 61.676 1.00 48.12 ? 101 LYS A NZ 1 ATOM 423 N N A GLU A 1 109 ? 3.993 33.669 66.265 0.50 30.64 ? 102 GLU A N 1 ATOM 424 N N B GLU A 1 109 ? 4.021 33.692 66.289 0.50 30.48 ? 102 GLU A N 1 ATOM 425 C CA A GLU A 1 109 ? 4.651 32.907 67.335 0.50 31.25 ? 102 GLU A CA 1 ATOM 426 C CA B GLU A 1 109 ? 4.587 32.958 67.421 0.50 31.01 ? 102 GLU A CA 1 ATOM 427 C C A GLU A 1 109 ? 5.614 33.828 68.091 0.50 30.73 ? 102 GLU A C 1 ATOM 428 C C B GLU A 1 109 ? 5.725 33.736 68.092 0.50 30.58 ? 102 GLU A C 1 ATOM 429 O O A GLU A 1 109 ? 5.640 33.849 69.328 0.50 31.13 ? 102 GLU A O 1 ATOM 430 O O B GLU A 1 109 ? 5.992 33.565 69.285 0.50 31.06 ? 102 GLU A O 1 ATOM 431 C CB A GLU A 1 109 ? 5.438 31.717 66.759 0.50 31.77 ? 102 GLU A CB 1 ATOM 432 C CB B GLU A 1 109 ? 5.066 31.582 66.977 0.50 31.55 ? 102 GLU A CB 1 ATOM 433 C CG A GLU A 1 109 ? 4.622 30.624 66.054 0.50 34.85 ? 102 GLU A CG 1 ATOM 434 C CG B GLU A 1 109 ? 5.769 30.793 68.070 0.50 34.85 ? 102 GLU A CG 1 ATOM 435 C CD A GLU A 1 109 ? 5.485 29.664 65.198 0.50 37.73 ? 102 GLU A CD 1 ATOM 436 C CD B GLU A 1 109 ? 4.831 30.397 69.196 0.50 40.95 ? 102 GLU A CD 1 ATOM 437 O OE1 A GLU A 1 109 ? 4.970 29.127 64.184 0.50 36.72 ? 102 GLU A OE1 1 ATOM 438 O OE1 B GLU A 1 109 ? 5.322 30.156 70.325 0.50 42.67 ? 102 GLU A OE1 1 ATOM 439 O OE2 A GLU A 1 109 ? 6.681 29.457 65.520 0.50 37.73 ? 102 GLU A OE2 1 ATOM 440 O OE2 B GLU A 1 109 ? 3.600 30.335 68.955 0.50 43.37 ? 102 GLU A OE2 1 ATOM 441 N N . PHE A 1 110 ? 6.377 34.611 67.326 1.00 28.34 ? 103 PHE A N 1 ATOM 442 C CA . PHE A 1 110 ? 7.444 35.464 67.868 1.00 28.41 ? 103 PHE A CA 1 ATOM 443 C C . PHE A 1 110 ? 6.876 36.566 68.773 1.00 28.67 ? 103 PHE A C 1 ATOM 444 O O . PHE A 1 110 ? 7.616 37.150 69.559 1.00 30.12 ? 103 PHE A O 1 ATOM 445 C CB . PHE A 1 110 ? 8.275 36.144 66.742 1.00 27.53 ? 103 PHE A CB 1 ATOM 446 C CG . PHE A 1 110 ? 9.203 35.210 65.966 1.00 28.25 ? 103 PHE A CG 1 ATOM 447 C CD1 . PHE A 1 110 ? 9.487 33.903 66.384 1.00 30.15 ? 103 PHE A CD1 1 ATOM 448 C CD2 . PHE A 1 110 ? 9.793 35.685 64.796 1.00 28.45 ? 103 PHE A CD2 1 ATOM 449 C CE1 . PHE A 1 110 ? 10.343 33.066 65.623 1.00 32.65 ? 103 PHE A CE1 1 ATOM 450 C CE2 . PHE A 1 110 ? 10.656 34.869 64.024 1.00 29.09 ? 103 PHE A CE2 1 ATOM 451 C CZ . PHE A 1 110 ? 10.938 33.562 64.441 1.00 30.44 ? 103 PHE A CZ 1 ATOM 452 N N . GLY A 1 111 ? 5.586 36.874 68.629 1.00 28.20 ? 104 GLY A N 1 ATOM 453 C CA . GLY A 1 111 ? 4.888 37.754 69.553 1.00 28.96 ? 104 GLY A CA 1 ATOM 454 C C . GLY A 1 111 ? 4.278 39.012 68.964 1.00 28.63 ? 104 GLY A C 1 ATOM 455 O O . GLY A 1 111 ? 3.810 39.865 69.717 1.00 29.20 ? 104 GLY A O 1 ATOM 456 N N . LEU A 1 112 ? 4.265 39.161 67.637 1.00 27.73 ? 105 LEU A N 1 ATOM 457 C CA . LEU A 1 112 ? 3.669 40.394 67.074 1.00 26.53 ? 105 LEU A CA 1 ATOM 458 C C . LEU A 1 112 ? 2.177 40.456 67.337 1.00 28.09 ? 105 LEU A C 1 ATOM 459 O O . LEU A 1 112 ? 1.522 39.417 67.485 1.00 29.70 ? 105 LEU A O 1 ATOM 460 C CB . LEU A 1 112 ? 3.954 40.499 65.563 1.00 26.06 ? 105 LEU A CB 1 ATOM 461 C CG . LEU A 1 112 ? 5.438 40.605 65.163 1.00 24.62 ? 105 LEU A CG 1 ATOM 462 C CD1 . LEU A 1 112 ? 5.559 40.994 63.683 1.00 25.46 ? 105 LEU A CD1 1 ATOM 463 C CD2 . LEU A 1 112 ? 6.188 41.656 66.017 1.00 24.13 ? 105 LEU A CD2 1 ATOM 464 N N . ASP A 1 113 ? 1.633 41.672 67.429 1.00 27.75 ? 106 ASP A N 1 ATOM 465 C CA . ASP A 1 113 ? 0.219 41.849 67.747 1.00 28.99 ? 106 ASP A CA 1 ATOM 466 C C . ASP A 1 113 ? -0.728 41.371 66.661 1.00 29.60 ? 106 ASP A C 1 ATOM 467 O O . ASP A 1 113 ? -1.776 40.800 66.959 1.00 31.03 ? 106 ASP A O 1 ATOM 468 C CB . ASP A 1 113 ? -0.073 43.314 68.073 1.00 28.70 ? 106 ASP A CB 1 ATOM 469 C CG . ASP A 1 113 ? 0.634 43.755 69.318 1.00 30.36 ? 106 ASP A CG 1 ATOM 470 O OD1 . ASP A 1 113 ? 0.374 43.134 70.387 1.00 30.47 ? 106 ASP A OD1 1 ATOM 471 O OD2 . ASP A 1 113 ? 1.479 44.660 69.231 1.00 27.99 ? 106 ASP A OD2 1 ATOM 472 N N . SER A 1 114 ? -0.357 41.616 65.405 1.00 27.70 ? 107 SER A N 1 ATOM 473 C CA . SER A 1 114 ? -1.143 41.149 64.272 1.00 27.69 ? 107 SER A CA 1 ATOM 474 C C . SER A 1 114 ? -0.165 40.841 63.142 1.00 26.04 ? 107 SER A C 1 ATOM 475 O O . SER A 1 114 ? 0.876 41.485 63.035 1.00 24.57 ? 107 SER A O 1 ATOM 476 C CB . SER A 1 114 ? -2.173 42.230 63.875 1.00 27.94 ? 107 SER A CB 1 ATOM 477 O OG A SER A 1 114 ? -1.555 43.395 63.363 0.50 25.96 ? 107 SER A OG 1 ATOM 478 O OG B SER A 1 114 ? -2.528 42.172 62.509 0.50 31.31 ? 107 SER A OG 1 ATOM 479 N N . VAL A 1 115 ? -0.471 39.831 62.337 1.00 25.32 ? 108 VAL A N 1 ATOM 480 C CA . VAL A 1 115 ? 0.364 39.537 61.166 1.00 24.84 ? 108 VAL A CA 1 ATOM 481 C C . VAL A 1 115 ? -0.602 39.096 60.076 1.00 25.27 ? 108 VAL A C 1 ATOM 482 O O . VAL A 1 115 ? -1.285 38.058 60.204 1.00 26.18 ? 108 VAL A O 1 ATOM 483 C CB . VAL A 1 115 ? 1.401 38.412 61.408 1.00 24.73 ? 108 VAL A CB 1 ATOM 484 C CG1 . VAL A 1 115 ? 2.341 38.363 60.192 1.00 24.48 ? 108 VAL A CG1 1 ATOM 485 C CG2 . VAL A 1 115 ? 2.201 38.659 62.711 1.00 24.09 ? 108 VAL A CG2 1 ATOM 486 N N A GLU A 1 116 ? -0.682 39.893 59.021 0.70 24.85 ? 109 GLU A N 1 ATOM 487 N N B GLU A 1 116 ? -0.679 39.900 59.013 0.30 24.87 ? 109 GLU A N 1 ATOM 488 C CA A GLU A 1 116 ? -1.606 39.593 57.949 0.70 25.97 ? 109 GLU A CA 1 ATOM 489 C CA B GLU A 1 116 ? -1.661 39.721 57.940 0.30 25.46 ? 109 GLU A CA 1 ATOM 490 C C A GLU A 1 116 ? -0.870 39.444 56.630 0.70 25.01 ? 109 GLU A C 1 ATOM 491 C C B GLU A 1 116 ? -0.991 39.633 56.572 0.30 24.66 ? 109 GLU A C 1 ATOM 492 O O A GLU A 1 116 ? 0.281 39.872 56.483 0.70 25.20 ? 109 GLU A O 1 ATOM 493 O O B GLU A 1 116 ? -0.005 40.333 56.319 0.30 24.34 ? 109 GLU A O 1 ATOM 494 C CB A GLU A 1 116 ? -2.685 40.695 57.835 0.70 27.32 ? 109 GLU A CB 1 ATOM 495 C CB B GLU A 1 116 ? -2.632 40.920 57.914 0.30 25.86 ? 109 GLU A CB 1 ATOM 496 C CG A GLU A 1 116 ? -3.587 40.841 59.085 0.70 32.49 ? 109 GLU A CG 1 ATOM 497 C CG B GLU A 1 116 ? -3.515 41.060 59.156 0.30 28.91 ? 109 GLU A CG 1 ATOM 498 C CD A GLU A 1 116 ? -4.391 39.586 59.418 0.70 37.76 ? 109 GLU A CD 1 ATOM 499 C CD B GLU A 1 116 ? -4.404 42.299 59.132 0.30 30.73 ? 109 GLU A CD 1 ATOM 500 O OE1 A GLU A 1 116 ? -4.922 38.943 58.491 0.70 40.23 ? 109 GLU A OE1 1 ATOM 501 O OE1 B GLU A 1 116 ? -4.122 43.243 58.361 0.30 31.83 ? 109 GLU A OE1 1 ATOM 502 O OE2 A GLU A 1 116 ? -4.510 39.244 60.622 0.70 41.74 ? 109 GLU A OE2 1 ATOM 503 O OE2 B GLU A 1 116 ? -5.385 42.343 59.908 0.30 33.44 ? 109 GLU A OE2 1 ATOM 504 N N . LEU A 1 117 ? -1.529 38.794 55.681 1.00 24.71 ? 110 LEU A N 1 ATOM 505 C CA . LEU A 1 117 ? -1.066 38.812 54.289 1.00 24.54 ? 110 LEU A CA 1 ATOM 506 C C . LEU A 1 117 ? -1.864 39.889 53.553 1.00 24.42 ? 110 LEU A C 1 ATOM 507 O O . LEU A 1 117 ? -3.096 39.994 53.726 1.00 26.21 ? 110 LEU A O 1 ATOM 508 C CB . LEU A 1 117 ? -1.329 37.475 53.613 1.00 25.41 ? 110 LEU A CB 1 ATOM 509 C CG . LEU A 1 117 ? -0.600 36.254 54.177 1.00 27.01 ? 110 LEU A CG 1 ATOM 510 C CD1 . LEU A 1 117 ? -0.827 35.079 53.196 1.00 29.89 ? 110 LEU A CD1 1 ATOM 511 C CD2 . LEU A 1 117 ? 0.874 36.495 54.335 1.00 28.17 ? 110 LEU A CD2 1 ATOM 512 N N . ALA A 1 118 ? -1.169 40.680 52.745 1.00 22.35 ? 111 ALA A N 1 ATOM 513 C CA . ALA A 1 118 ? -1.791 41.692 51.884 1.00 21.63 ? 111 ALA A CA 1 ATOM 514 C C . ALA A 1 118 ? -1.477 41.210 50.484 1.00 22.33 ? 111 ALA A C 1 ATOM 515 O O . ALA A 1 118 ? -0.300 41.152 50.124 1.00 23.06 ? 111 ALA A O 1 ATOM 516 C CB . ALA A 1 118 ? -1.151 43.075 52.138 1.00 22.06 ? 111 ALA A CB 1 ATOM 517 N N . HIS A 1 119 ? -2.508 40.839 49.719 1.00 21.46 ? 112 HIS A N 1 ATOM 518 C CA . HIS A 1 119 ? -2.271 40.287 48.370 1.00 20.78 ? 112 HIS A CA 1 ATOM 519 C C . HIS A 1 119 ? -2.733 41.267 47.293 1.00 19.88 ? 112 HIS A C 1 ATOM 520 O O . HIS A 1 119 ? -3.599 42.104 47.531 1.00 20.52 ? 112 HIS A O 1 ATOM 521 C CB . HIS A 1 119 ? -2.952 38.917 48.184 1.00 22.37 ? 112 HIS A CB 1 ATOM 522 C CG . HIS A 1 119 ? -4.448 38.967 48.205 1.00 25.01 ? 112 HIS A CG 1 ATOM 523 N ND1 . HIS A 1 119 ? -5.187 38.720 49.345 1.00 29.15 ? 112 HIS A ND1 1 ATOM 524 C CD2 . HIS A 1 119 ? -5.344 39.233 47.222 1.00 26.72 ? 112 HIS A CD2 1 ATOM 525 C CE1 . HIS A 1 119 ? -6.479 38.828 49.060 1.00 29.07 ? 112 HIS A CE1 1 ATOM 526 N NE2 . HIS A 1 119 ? -6.600 39.145 47.780 1.00 28.43 ? 112 HIS A NE2 1 ATOM 527 N N . TYR A 1 120 ? -2.114 41.158 46.116 1.00 19.18 ? 113 TYR A N 1 ATOM 528 C CA . TYR A 1 120 ? -2.409 42.014 44.943 1.00 19.38 ? 113 TYR A CA 1 ATOM 529 C C . TYR A 1 120 ? -2.278 41.136 43.727 1.00 18.88 ? 113 TYR A C 1 ATOM 530 O O . TYR A 1 120 ? -1.555 40.128 43.763 1.00 20.41 ? 113 TYR A O 1 ATOM 531 C CB . TYR A 1 120 ? -1.439 43.223 44.823 1.00 18.31 ? 113 TYR A CB 1 ATOM 532 C CG . TYR A 1 120 ? -1.451 44.014 46.115 1.00 18.89 ? 113 TYR A CG 1 ATOM 533 C CD1 . TYR A 1 120 ? -2.460 44.953 46.365 1.00 19.16 ? 113 TYR A CD1 1 ATOM 534 C CD2 . TYR A 1 120 ? -0.531 43.716 47.133 1.00 18.94 ? 113 TYR A CD2 1 ATOM 535 C CE1 . TYR A 1 120 ? -2.497 45.622 47.607 1.00 21.30 ? 113 TYR A CE1 1 ATOM 536 C CE2 . TYR A 1 120 ? -0.553 44.364 48.349 1.00 19.91 ? 113 TYR A CE2 1 ATOM 537 C CZ . TYR A 1 120 ? -1.537 45.306 48.583 1.00 21.80 ? 113 TYR A CZ 1 ATOM 538 O OH . TYR A 1 120 ? -1.598 45.958 49.799 1.00 20.47 ? 113 TYR A OH 1 ATOM 539 N N . ASP A 1 121 ? -2.942 41.524 42.644 1.00 19.11 ? 114 ASP A N 1 ATOM 540 C CA . ASP A 1 121 ? -2.817 40.777 41.365 1.00 19.88 ? 114 ASP A CA 1 ATOM 541 C C . ASP A 1 121 ? -2.111 41.697 40.398 1.00 19.06 ? 114 ASP A C 1 ATOM 542 O O . ASP A 1 121 ? -2.697 42.679 39.940 1.00 19.76 ? 114 ASP A O 1 ATOM 543 C CB . ASP A 1 121 ? -4.210 40.358 40.846 1.00 20.92 ? 114 ASP A CB 1 ATOM 544 C CG . ASP A 1 121 ? -4.902 39.423 41.815 1.00 24.74 ? 114 ASP A CG 1 ATOM 545 O OD1 . ASP A 1 121 ? -4.229 38.436 42.192 1.00 25.11 ? 114 ASP A OD1 1 ATOM 546 O OD2 . ASP A 1 121 ? -6.068 39.690 42.207 1.00 28.09 ? 114 ASP A OD2 1 ATOM 547 N N . VAL A 1 122 ? -0.846 41.367 40.101 1.00 18.78 ? 115 VAL A N 1 ATOM 548 C CA . VAL A 1 122 ? 0.047 42.282 39.338 1.00 18.06 ? 115 VAL A CA 1 ATOM 549 C C . VAL A 1 122 ? 0.610 41.623 38.097 1.00 18.67 ? 115 VAL A C 1 ATOM 550 O O . VAL A 1 122 ? 0.645 40.391 38.010 1.00 18.65 ? 115 VAL A O 1 ATOM 551 C CB . VAL A 1 122 ? 1.237 42.797 40.220 1.00 18.01 ? 115 VAL A CB 1 ATOM 552 C CG1 . VAL A 1 122 ? 0.700 43.592 41.425 1.00 17.68 ? 115 VAL A CG1 1 ATOM 553 C CG2 . VAL A 1 122 ? 2.153 41.629 40.687 1.00 17.52 ? 115 VAL A CG2 1 ATOM 554 N N . LEU A 1 123 ? 1.080 42.444 37.152 1.00 17.74 ? 116 LEU A N 1 ATOM 555 C CA . LEU A 1 123 ? 1.691 41.857 35.953 1.00 17.89 ? 116 LEU A CA 1 ATOM 556 C C . LEU A 1 123 ? 3.074 41.285 36.285 1.00 18.56 ? 116 LEU A C 1 ATOM 557 O O . LEU A 1 123 ? 3.950 42.017 36.714 1.00 19.23 ? 116 LEU A O 1 ATOM 558 C CB . LEU A 1 123 ? 1.835 42.920 34.860 1.00 17.03 ? 116 LEU A CB 1 ATOM 559 C CG . LEU A 1 123 ? 2.092 42.293 33.483 1.00 19.47 ? 116 LEU A CG 1 ATOM 560 C CD1 . LEU A 1 123 ? 0.850 41.568 32.899 1.00 21.59 ? 116 LEU A CD1 1 ATOM 561 C CD2 . LEU A 1 123 ? 2.604 43.404 32.517 1.00 20.96 ? 116 LEU A CD2 1 ATOM 562 N N . LEU A 1 124 ? 3.253 39.976 36.052 1.00 19.24 ? 117 LEU A N 1 ATOM 563 C CA . LEU A 1 124 ? 4.564 39.320 36.167 1.00 19.48 ? 117 LEU A CA 1 ATOM 564 C C . LEU A 1 124 ? 4.944 38.763 34.795 1.00 20.51 ? 117 LEU A C 1 ATOM 565 O O . LEU A 1 124 ? 4.194 38.944 33.831 1.00 21.45 ? 117 LEU A O 1 ATOM 566 C CB . LEU A 1 124 ? 4.563 38.223 37.255 1.00 19.83 ? 117 LEU A CB 1 ATOM 567 C CG . LEU A 1 124 ? 4.231 38.686 38.680 1.00 18.51 ? 117 LEU A CG 1 ATOM 568 C CD1 . LEU A 1 124 ? 4.381 37.486 39.652 1.00 18.96 ? 117 LEU A CD1 1 ATOM 569 C CD2 . LEU A 1 124 ? 5.126 39.875 39.141 1.00 18.34 ? 117 LEU A CD2 1 ATOM 570 N N . SER A 1 125 ? 6.099 38.112 34.708 1.00 20.21 ? 118 SER A N 1 ATOM 571 C CA . SER A 1 125 ? 6.609 37.641 33.409 1.00 21.30 ? 118 SER A CA 1 ATOM 572 C C . SER A 1 125 ? 7.387 36.358 33.641 1.00 21.79 ? 118 SER A C 1 ATOM 573 O O . SER A 1 125 ? 8.198 36.268 34.586 1.00 21.66 ? 118 SER A O 1 ATOM 574 C CB . SER A 1 125 ? 7.546 38.712 32.836 1.00 22.65 ? 118 SER A CB 1 ATOM 575 O OG . SER A 1 125 ? 8.326 38.209 31.727 1.00 20.98 ? 118 SER A OG 1 ATOM 576 N N . TYR A 1 126 ? 7.144 35.369 32.781 1.00 22.61 ? 119 TYR A N 1 ATOM 577 C CA . TYR A 1 126 ? 7.794 34.080 32.916 1.00 22.35 ? 119 TYR A CA 1 ATOM 578 C C . TYR A 1 126 ? 8.146 33.491 31.566 1.00 23.48 ? 119 TYR A C 1 ATOM 579 O O . TYR A 1 126 ? 7.406 33.653 30.598 1.00 23.81 ? 119 TYR A O 1 ATOM 580 C CB . TYR A 1 126 ? 6.848 33.082 33.555 1.00 22.02 ? 119 TYR A CB 1 ATOM 581 C CG . TYR A 1 126 ? 6.346 33.465 34.922 1.00 22.79 ? 119 TYR A CG 1 ATOM 582 C CD1 . TYR A 1 126 ? 7.177 33.357 36.030 1.00 22.65 ? 119 TYR A CD1 1 ATOM 583 C CD2 . TYR A 1 126 ? 5.019 33.858 35.106 1.00 24.31 ? 119 TYR A CD2 1 ATOM 584 C CE1 . TYR A 1 126 ? 6.701 33.673 37.321 1.00 22.38 ? 119 TYR A CE1 1 ATOM 585 C CE2 . TYR A 1 126 ? 4.523 34.169 36.370 1.00 26.44 ? 119 TYR A CE2 1 ATOM 586 C CZ . TYR A 1 126 ? 5.370 34.056 37.470 1.00 24.82 ? 119 TYR A CZ 1 ATOM 587 O OH . TYR A 1 126 ? 4.881 34.331 38.719 1.00 23.19 ? 119 TYR A OH 1 ATOM 588 N N . PRO A 1 127 ? 9.228 32.724 31.523 1.00 24.32 ? 120 PRO A N 1 ATOM 589 C CA . PRO A 1 127 ? 9.473 31.980 30.271 1.00 25.87 ? 120 PRO A CA 1 ATOM 590 C C . PRO A 1 127 ? 8.391 30.953 30.012 1.00 27.60 ? 120 PRO A C 1 ATOM 591 O O . PRO A 1 127 ? 7.682 30.520 30.932 1.00 27.18 ? 120 PRO A O 1 ATOM 592 C CB . PRO A 1 127 ? 10.805 31.248 30.539 1.00 26.06 ? 120 PRO A CB 1 ATOM 593 C CG . PRO A 1 127 ? 11.459 31.986 31.663 1.00 26.26 ? 120 PRO A CG 1 ATOM 594 C CD . PRO A 1 127 ? 10.327 32.572 32.497 1.00 23.96 ? 120 PRO A CD 1 ATOM 595 N N . ASN A 1 128 ? 8.294 30.540 28.751 1.00 28.57 ? 121 ASN A N 1 ATOM 596 C CA . ASN A 1 128 ? 7.410 29.446 28.368 1.00 31.88 ? 121 ASN A CA 1 ATOM 597 C C . ASN A 1 128 ? 8.175 28.135 28.584 1.00 33.26 ? 121 ASN A C 1 ATOM 598 O O . ASN A 1 128 ? 9.219 27.913 27.960 1.00 32.51 ? 121 ASN A O 1 ATOM 599 C CB . ASN A 1 128 ? 6.990 29.656 26.927 1.00 31.67 ? 121 ASN A CB 1 ATOM 600 C CG . ASN A 1 128 ? 5.974 28.623 26.464 1.00 36.20 ? 121 ASN A CG 1 ATOM 601 O OD1 . ASN A 1 128 ? 5.995 27.478 26.906 1.00 36.92 ? 121 ASN A OD1 1 ATOM 602 N ND2 . ASN A 1 128 ? 5.082 29.030 25.585 1.00 40.13 ? 121 ASN A ND2 1 ATOM 603 N N A LYS A 1 129 ? 7.648 27.296 29.480 0.70 34.80 ? 122 LYS A N 1 ATOM 604 N N B LYS A 1 129 ? 7.687 27.295 29.499 0.30 34.20 ? 122 LYS A N 1 ATOM 605 C CA A LYS A 1 129 ? 8.290 26.032 29.890 0.70 37.01 ? 122 LYS A CA 1 ATOM 606 C CA B LYS A 1 129 ? 8.383 26.044 29.850 0.30 35.80 ? 122 LYS A CA 1 ATOM 607 C C A LYS A 1 129 ? 8.469 25.029 28.754 0.70 37.88 ? 122 LYS A C 1 ATOM 608 C C B LYS A 1 129 ? 8.579 25.114 28.659 0.30 37.09 ? 122 LYS A C 1 ATOM 609 O O A LYS A 1 129 ? 9.368 24.178 28.807 0.70 38.82 ? 122 LYS A O 1 ATOM 610 O O B LYS A 1 129 ? 9.584 24.396 28.583 0.30 37.67 ? 122 LYS A O 1 ATOM 611 C CB A LYS A 1 129 ? 7.513 25.377 31.042 0.70 37.72 ? 122 LYS A CB 1 ATOM 612 C CB B LYS A 1 129 ? 7.674 25.291 30.984 0.30 35.98 ? 122 LYS A CB 1 ATOM 613 C CG A LYS A 1 129 ? 7.606 26.124 32.364 0.70 39.46 ? 122 LYS A CG 1 ATOM 614 C CG B LYS A 1 129 ? 8.193 25.616 32.380 0.30 35.83 ? 122 LYS A CG 1 ATOM 615 C CD A LYS A 1 129 ? 6.493 25.697 33.319 0.70 43.79 ? 122 LYS A CD 1 ATOM 616 C CD B LYS A 1 129 ? 7.981 24.452 33.342 0.30 36.53 ? 122 LYS A CD 1 ATOM 617 C CE A LYS A 1 129 ? 6.336 26.698 34.461 0.70 45.00 ? 122 LYS A CE 1 ATOM 618 C CE B LYS A 1 129 ? 9.027 23.366 33.139 0.30 37.54 ? 122 LYS A CE 1 ATOM 619 N NZ A LYS A 1 129 ? 5.362 26.195 35.481 0.70 49.02 ? 122 LYS A NZ 1 ATOM 620 N NZ B LYS A 1 129 ? 8.975 22.319 34.201 0.30 37.97 ? 122 LYS A NZ 1 ATOM 621 N N . THR A 1 130 ? 7.635 25.136 27.722 1.00 38.06 ? 123 THR A N 1 ATOM 622 C CA . THR A 1 130 ? 7.718 24.230 26.569 1.00 39.57 ? 123 THR A CA 1 ATOM 623 C C . THR A 1 130 ? 8.227 24.856 25.250 1.00 39.59 ? 123 THR A C 1 ATOM 624 O O . THR A 1 130 ? 8.226 24.217 24.203 1.00 41.28 ? 123 THR A O 1 ATOM 625 C CB . THR A 1 130 ? 6.387 23.454 26.365 1.00 40.66 ? 123 THR A CB 1 ATOM 626 O OG1 . THR A 1 130 ? 5.329 24.379 26.101 1.00 41.96 ? 123 THR A OG1 1 ATOM 627 C CG2 . THR A 1 130 ? 6.047 22.644 27.624 1.00 41.43 ? 123 THR A CG2 1 ATOM 628 N N . HIS A 1 131 ? 8.693 26.095 25.315 1.00 37.89 ? 124 HIS A N 1 ATOM 629 C CA . HIS A 1 131 ? 9.168 26.816 24.155 1.00 37.41 ? 124 HIS A CA 1 ATOM 630 C C . HIS A 1 131 ? 10.288 27.741 24.642 1.00 35.75 ? 124 HIS A C 1 ATOM 631 O O . HIS A 1 131 ? 10.067 28.941 24.793 1.00 34.94 ? 124 HIS A O 1 ATOM 632 C CB . HIS A 1 131 ? 8.013 27.633 23.581 1.00 37.88 ? 124 HIS A CB 1 ATOM 633 C CG . HIS A 1 131 ? 8.223 28.093 22.172 1.00 41.15 ? 124 HIS A CG 1 ATOM 634 N ND1 . HIS A 1 131 ? 7.371 28.983 21.551 0.65 43.51 ? 124 HIS A ND1 1 ATOM 635 C CD2 . HIS A 1 131 ? 9.181 27.792 21.262 0.65 44.14 ? 124 HIS A CD2 1 ATOM 636 C CE1 . HIS A 1 131 ? 7.790 29.201 20.317 0.65 44.76 ? 124 HIS A CE1 1 ATOM 637 N NE2 . HIS A 1 131 ? 8.890 28.497 20.120 0.65 45.82 ? 124 HIS A NE2 1 ATOM 638 N N . PRO A 1 132 ? 11.478 27.176 24.924 1.00 34.80 ? 125 PRO A N 1 ATOM 639 C CA . PRO A 1 132 ? 12.538 27.938 25.634 1.00 33.33 ? 125 PRO A CA 1 ATOM 640 C C . PRO A 1 132 ? 13.159 29.076 24.835 1.00 32.26 ? 125 PRO A C 1 ATOM 641 O O . PRO A 1 132 ? 13.182 29.065 23.597 1.00 32.55 ? 125 PRO A O 1 ATOM 642 C CB . PRO A 1 132 ? 13.594 26.881 25.988 1.00 34.95 ? 125 PRO A CB 1 ATOM 643 C CG . PRO A 1 132 ? 13.110 25.577 25.397 1.00 35.72 ? 125 PRO A CG 1 ATOM 644 C CD . PRO A 1 132 ? 11.894 25.801 24.580 1.00 36.32 ? 125 PRO A CD 1 ATOM 645 N N . ASN A 1 133 ? 13.607 30.090 25.572 1.00 29.59 ? 126 ASN A N 1 ATOM 646 C CA . ASN A 1 133 ? 14.315 31.241 25.010 1.00 29.02 ? 126 ASN A CA 1 ATOM 647 C C . ASN A 1 133 ? 15.754 30.877 24.713 1.00 28.98 ? 126 ASN A C 1 ATOM 648 O O . ASN A 1 133 ? 16.374 30.150 25.497 1.00 29.41 ? 126 ASN A O 1 ATOM 649 C CB . ASN A 1 133 ? 14.303 32.397 26.038 1.00 26.65 ? 126 ASN A CB 1 ATOM 650 C CG . ASN A 1 133 ? 12.888 32.852 26.393 1.00 28.88 ? 126 ASN A CG 1 ATOM 651 O OD1 . ASN A 1 133 ? 11.985 32.829 25.559 1.00 26.54 ? 126 ASN A OD1 1 ATOM 652 N ND2 . ASN A 1 133 ? 12.696 33.281 27.638 1.00 27.10 ? 126 ASN A ND2 1 ATOM 653 N N . TYR A 1 134 ? 16.272 31.351 23.572 1.00 29.32 ? 127 TYR A N 1 ATOM 654 C CA . TYR A 1 134 ? 17.697 31.170 23.237 1.00 29.63 ? 127 TYR A CA 1 ATOM 655 C C . TYR A 1 134 ? 18.062 32.090 22.088 1.00 30.08 ? 127 TYR A C 1 ATOM 656 O O . TYR A 1 134 ? 17.181 32.691 21.446 1.00 30.21 ? 127 TYR A O 1 ATOM 657 C CB . TYR A 1 134 ? 18.031 29.697 22.895 1.00 30.83 ? 127 TYR A CB 1 ATOM 658 C CG . TYR A 1 134 ? 17.477 29.182 21.587 1.00 33.03 ? 127 TYR A CG 1 ATOM 659 C CD1 . TYR A 1 134 ? 18.325 28.969 20.489 1.00 36.15 ? 127 TYR A CD1 1 ATOM 660 C CD2 . TYR A 1 134 ? 16.121 28.888 21.439 1.00 34.15 ? 127 TYR A CD2 1 ATOM 661 C CE1 . TYR A 1 134 ? 17.837 28.475 19.285 1.00 36.74 ? 127 TYR A CE1 1 ATOM 662 C CE2 . TYR A 1 134 ? 15.622 28.386 20.214 1.00 34.90 ? 127 TYR A CE2 1 ATOM 663 C CZ . TYR A 1 134 ? 16.493 28.204 19.146 1.00 36.83 ? 127 TYR A CZ 1 ATOM 664 O OH . TYR A 1 134 ? 16.025 27.723 17.934 1.00 37.74 ? 127 TYR A OH 1 ATOM 665 N N . ILE A 1 135 ? 19.369 32.206 21.849 1.00 30.17 ? 128 ILE A N 1 ATOM 666 C CA . ILE A 1 135 ? 19.902 33.019 20.772 1.00 30.08 ? 128 ILE A CA 1 ATOM 667 C C . ILE A 1 135 ? 20.740 32.096 19.897 1.00 31.01 ? 128 ILE A C 1 ATOM 668 O O . ILE A 1 135 ? 21.396 31.167 20.405 1.00 30.55 ? 128 ILE A O 1 ATOM 669 C CB . ILE A 1 135 ? 20.778 34.160 21.339 1.00 29.41 ? 128 ILE A CB 1 ATOM 670 C CG1 . ILE A 1 135 ? 19.943 35.075 22.266 1.00 28.67 ? 128 ILE A CG1 1 ATOM 671 C CG2 . ILE A 1 135 ? 21.432 34.988 20.203 1.00 30.79 ? 128 ILE A CG2 1 ATOM 672 C CD1 . ILE A 1 135 ? 20.803 35.834 23.265 1.00 29.56 ? 128 ILE A CD1 1 ATOM 673 N N . SER A 1 136 ? 20.694 32.346 18.591 1.00 31.88 ? 129 SER A N 1 ATOM 674 C CA . SER A 1 136 ? 21.480 31.577 17.618 1.00 33.25 ? 129 SER A CA 1 ATOM 675 C C . SER A 1 136 ? 22.374 32.467 16.799 1.00 34.28 ? 129 SER A C 1 ATOM 676 O O . SER A 1 136 ? 22.068 33.645 16.602 1.00 33.85 ? 129 SER A O 1 ATOM 677 C CB . SER A 1 136 ? 20.552 30.860 16.625 1.00 33.35 ? 129 SER A CB 1 ATOM 678 O OG . SER A 1 136 ? 19.761 29.903 17.285 1.00 36.55 ? 129 SER A OG 1 ATOM 679 N N . ILE A 1 137 ? 23.462 31.877 16.273 1.00 36.35 ? 130 ILE A N 1 ATOM 680 C CA . ILE A 1 137 ? 24.079 32.402 15.070 1.00 38.04 ? 130 ILE A CA 1 ATOM 681 C C . ILE A 1 137 ? 23.514 31.514 13.975 1.00 39.53 ? 130 ILE A C 1 ATOM 682 O O . ILE A 1 137 ? 23.487 30.282 14.099 1.00 38.82 ? 130 ILE A O 1 ATOM 683 C CB . ILE A 1 137 ? 25.620 32.330 15.071 1.00 38.73 ? 130 ILE A CB 1 ATOM 684 C CG1 . ILE A 1 137 ? 26.188 33.299 16.123 1.00 38.20 ? 130 ILE A CG1 1 ATOM 685 C CG2 . ILE A 1 137 ? 26.166 32.621 13.655 1.00 39.23 ? 130 ILE A CG2 1 ATOM 686 C CD1 . ILE A 1 137 ? 27.679 33.143 16.350 1.00 38.03 ? 130 ILE A CD1 1 ATOM 687 N N . ILE A 1 138 ? 23.009 32.165 12.943 1.00 41.71 ? 131 ILE A N 1 ATOM 688 C CA . ILE A 1 138 ? 22.341 31.479 11.847 1.00 44.89 ? 131 ILE A CA 1 ATOM 689 C C . ILE A 1 138 ? 23.153 31.742 10.565 1.00 46.67 ? 131 ILE A C 1 ATOM 690 O O . ILE A 1 138 ? 23.671 32.843 10.376 1.00 46.32 ? 131 ILE A O 1 ATOM 691 C CB . ILE A 1 138 ? 20.829 31.930 11.803 1.00 44.59 ? 131 ILE A CB 1 ATOM 692 C CG1 . ILE A 1 138 ? 19.960 30.955 11.005 1.00 48.09 ? 131 ILE A CG1 1 ATOM 693 C CG2 . ILE A 1 138 ? 20.671 33.383 11.335 1.00 46.40 ? 131 ILE A CG2 1 ATOM 694 C CD1 . ILE A 1 138 ? 18.443 31.118 11.290 1.00 49.82 ? 131 ILE A CD1 1 ATOM 695 N N . ASN A 1 139 ? 23.333 30.723 9.719 1.00 48.94 ? 132 ASN A N 1 ATOM 696 C CA . ASN A 1 139 ? 24.003 30.956 8.421 1.00 51.94 ? 132 ASN A CA 1 ATOM 697 C C . ASN A 1 139 ? 23.030 31.454 7.343 1.00 53.75 ? 132 ASN A C 1 ATOM 698 O O . ASN A 1 139 ? 21.834 31.603 7.611 1.00 53.78 ? 132 ASN A O 1 ATOM 699 C CB . ASN A 1 139 ? 24.850 29.749 7.958 1.00 52.54 ? 132 ASN A CB 1 ATOM 700 C CG . ASN A 1 139 ? 24.020 28.515 7.637 1.00 52.85 ? 132 ASN A CG 1 ATOM 701 O OD1 . ASN A 1 139 ? 22.833 28.606 7.316 1.00 53.23 ? 132 ASN A OD1 1 ATOM 702 N ND2 . ASN A 1 139 ? 24.656 27.345 7.714 1.00 52.01 ? 132 ASN A ND2 1 ATOM 703 N N . GLU A 1 140 ? 23.537 31.713 6.135 1.00 56.31 ? 133 GLU A N 1 ATOM 704 C CA . GLU A 1 140 ? 22.706 32.257 5.042 1.00 58.45 ? 133 GLU A CA 1 ATOM 705 C C . GLU A 1 140 ? 21.617 31.300 4.526 1.00 59.43 ? 133 GLU A C 1 ATOM 706 O O . GLU A 1 140 ? 20.666 31.732 3.870 1.00 60.17 ? 133 GLU A O 1 ATOM 707 C CB . GLU A 1 140 ? 23.579 32.738 3.884 1.00 59.53 ? 133 GLU A CB 1 ATOM 708 C CG . GLU A 1 140 ? 24.442 31.653 3.259 0.85 62.02 ? 133 GLU A CG 1 ATOM 709 C CD . GLU A 1 140 ? 25.486 32.216 2.306 0.85 63.82 ? 133 GLU A CD 1 ATOM 710 O OE1 . GLU A 1 140 ? 25.388 33.410 1.942 0.85 64.14 ? 133 GLU A OE1 1 ATOM 711 O OE2 . GLU A 1 140 ? 26.407 31.462 1.932 0.85 65.66 ? 133 GLU A OE2 1 ATOM 712 N N . ASP A 1 141 ? 21.767 30.011 4.832 1.00 59.89 ? 134 ASP A N 1 ATOM 713 C CA . ASP A 1 141 ? 20.755 28.998 4.520 1.00 60.68 ? 134 ASP A CA 1 ATOM 714 C C . ASP A 1 141 ? 19.638 28.951 5.578 1.00 59.47 ? 134 ASP A C 1 ATOM 715 O O . ASP A 1 141 ? 18.583 28.347 5.359 1.00 60.63 ? 134 ASP A O 1 ATOM 716 C CB . ASP A 1 141 ? 21.413 27.617 4.371 0.95 61.51 ? 134 ASP A CB 1 ATOM 717 C CG . ASP A 1 141 ? 22.434 27.566 3.232 0.95 64.19 ? 134 ASP A CG 1 ATOM 718 O OD1 . ASP A 1 141 ? 22.221 28.244 2.199 0.95 65.49 ? 134 ASP A OD1 1 ATOM 719 O OD2 . ASP A 1 141 ? 23.450 26.839 3.363 0.95 64.61 ? 134 ASP A OD2 1 ATOM 720 N N . GLY A 1 142 ? 19.866 29.594 6.720 1.00 57.12 ? 135 GLY A N 1 ATOM 721 C CA . GLY A 1 142 ? 18.920 29.536 7.823 1.00 54.86 ? 135 GLY A CA 1 ATOM 722 C C . GLY A 1 142 ? 19.204 28.428 8.831 1.00 53.04 ? 135 GLY A C 1 ATOM 723 O O . GLY A 1 142 ? 18.339 28.114 9.664 1.00 53.49 ? 135 GLY A O 1 ATOM 724 N N A ASN A 1 143 ? 20.398 27.840 8.751 0.70 52.41 ? 136 ASN A N 1 ATOM 725 N N B ASN A 1 143 ? 20.406 27.852 8.768 0.30 52.43 ? 136 ASN A N 1 ATOM 726 C CA A ASN A 1 143 ? 20.831 26.839 9.720 0.70 50.75 ? 136 ASN A CA 1 ATOM 727 C CA B ASN A 1 143 ? 20.844 26.827 9.720 0.30 50.71 ? 136 ASN A CA 1 ATOM 728 C C A ASN A 1 143 ? 21.381 27.528 10.968 0.70 48.65 ? 136 ASN A C 1 ATOM 729 C C B ASN A 1 143 ? 21.437 27.467 10.972 0.30 48.78 ? 136 ASN A C 1 ATOM 730 O O A ASN A 1 143 ? 22.230 28.418 10.875 0.70 48.04 ? 136 ASN A O 1 ATOM 731 O O B ASN A 1 143 ? 22.373 28.265 10.886 0.30 48.54 ? 136 ASN A O 1 ATOM 732 C CB A ASN A 1 143 ? 21.899 25.908 9.134 0.70 51.72 ? 136 ASN A CB 1 ATOM 733 C CB B ASN A 1 143 ? 21.874 25.898 9.072 0.30 51.65 ? 136 ASN A CB 1 ATOM 734 C CG A ASN A 1 143 ? 21.452 25.209 7.844 0.70 53.40 ? 136 ASN A CG 1 ATOM 735 C CG B ASN A 1 143 ? 22.150 24.647 9.897 0.30 51.11 ? 136 ASN A CG 1 ATOM 736 O OD1 A ASN A 1 143 ? 22.276 24.927 6.974 0.70 54.50 ? 136 ASN A OD1 1 ATOM 737 O OD1 B ASN A 1 143 ? 21.933 24.618 11.108 0.30 49.45 ? 136 ASN A OD1 1 ATOM 738 N ND2 A ASN A 1 143 ? 20.158 24.921 7.724 0.70 53.28 ? 136 ASN A ND2 1 ATOM 739 N ND2 B ASN A 1 143 ? 22.634 23.601 9.234 0.30 51.23 ? 136 ASN A ND2 1 ATOM 740 N N . GLU A 1 144 ? 20.890 27.108 12.130 1.00 47.08 ? 137 GLU A N 1 ATOM 741 C CA . GLU A 1 144 ? 21.361 27.655 13.409 1.00 44.66 ? 137 GLU A CA 1 ATOM 742 C C . GLU A 1 144 ? 22.604 26.889 13.832 1.00 43.71 ? 137 GLU A C 1 ATOM 743 O O . GLU A 1 144 ? 22.516 25.744 14.272 1.00 44.26 ? 137 GLU A O 1 ATOM 744 C CB . GLU A 1 144 ? 20.249 27.605 14.457 1.00 42.94 ? 137 GLU A CB 1 ATOM 745 C CG . GLU A 1 144 ? 19.058 28.471 14.060 1.00 42.36 ? 137 GLU A CG 1 ATOM 746 C CD . GLU A 1 144 ? 17.936 28.514 15.097 1.00 41.05 ? 137 GLU A CD 1 ATOM 747 O OE1 . GLU A 1 144 ? 17.900 27.664 16.016 1.00 38.77 ? 137 GLU A OE1 1 ATOM 748 O OE2 . GLU A 1 144 ? 17.080 29.408 14.966 1.00 41.06 ? 137 GLU A OE2 1 ATOM 749 N N . ILE A 1 145 ? 23.764 27.520 13.650 1.00 42.69 ? 138 ILE A N 1 ATOM 750 C CA . ILE A 1 145 ? 25.063 26.845 13.822 1.00 42.46 ? 138 ILE A CA 1 ATOM 751 C C . ILE A 1 145 ? 25.649 26.960 15.222 1.00 40.83 ? 138 ILE A C 1 ATOM 752 O O . ILE A 1 145 ? 26.619 26.263 15.568 1.00 40.67 ? 138 ILE A O 1 ATOM 753 C CB . ILE A 1 145 ? 26.119 27.277 12.744 1.00 43.24 ? 138 ILE A CB 1 ATOM 754 C CG1 . ILE A 1 145 ? 26.469 28.769 12.881 1.00 42.60 ? 138 ILE A CG1 1 ATOM 755 C CG2 . ILE A 1 145 ? 25.612 26.895 11.350 1.00 44.73 ? 138 ILE A CG2 1 ATOM 756 C CD1 . ILE A 1 145 ? 27.673 29.231 12.030 1.00 43.00 ? 138 ILE A CD1 1 ATOM 757 N N . PHE A 1 146 ? 25.061 27.836 16.030 1.00 39.03 ? 139 PHE A N 1 ATOM 758 C CA . PHE A 1 146 ? 25.445 27.950 17.420 1.00 37.58 ? 139 PHE A CA 1 ATOM 759 C C . PHE A 1 146 ? 24.207 28.384 18.185 1.00 35.51 ? 139 PHE A C 1 ATOM 760 O O . PHE A 1 146 ? 23.493 29.261 17.718 1.00 33.90 ? 139 PHE A O 1 ATOM 761 C CB . PHE A 1 146 ? 26.554 28.992 17.626 1.00 38.13 ? 139 PHE A CB 1 ATOM 762 C CG . PHE A 1 146 ? 26.694 29.428 19.059 1.00 37.87 ? 139 PHE A CG 1 ATOM 763 C CD1 . PHE A 1 146 ? 27.307 28.596 20.001 1.00 39.76 ? 139 PHE A CD1 1 ATOM 764 C CD2 . PHE A 1 146 ? 26.165 30.650 19.483 1.00 37.50 ? 139 PHE A CD2 1 ATOM 765 C CE1 . PHE A 1 146 ? 27.391 28.991 21.349 1.00 38.35 ? 139 PHE A CE1 1 ATOM 766 C CE2 . PHE A 1 146 ? 26.251 31.048 20.820 1.00 36.01 ? 139 PHE A CE2 1 ATOM 767 C CZ . PHE A 1 146 ? 26.861 30.221 21.751 1.00 36.93 ? 139 PHE A CZ 1 ATOM 768 N N . ASN A 1 147 ? 23.942 27.733 19.315 1.00 34.52 ? 140 ASN A N 1 ATOM 769 C CA . ASN A 1 147 ? 22.837 28.120 20.202 1.00 33.73 ? 140 ASN A CA 1 ATOM 770 C C . ASN A 1 147 ? 23.329 28.418 21.595 1.00 32.62 ? 140 ASN A C 1 ATOM 771 O O . ASN A 1 147 ? 24.165 27.681 22.124 1.00 32.77 ? 140 ASN A O 1 ATOM 772 C CB . ASN A 1 147 ? 21.843 26.976 20.329 1.00 34.65 ? 140 ASN A CB 1 ATOM 773 C CG . ASN A 1 147 ? 21.114 26.681 19.038 1.00 37.21 ? 140 ASN A CG 1 ATOM 774 O OD1 . ASN A 1 147 ? 20.875 27.570 18.217 1.00 38.58 ? 140 ASN A OD1 1 ATOM 775 N ND2 . ASN A 1 147 ? 20.751 25.418 18.858 1.00 40.82 ? 140 ASN A ND2 1 ATOM 776 N N . THR A 1 148 ? 22.796 29.482 22.211 1.00 31.19 ? 141 THR A N 1 ATOM 777 C CA . THR A 1 148 ? 23.129 29.760 23.603 1.00 30.65 ? 141 THR A CA 1 ATOM 778 C C . THR A 1 148 ? 22.449 28.727 24.512 1.00 30.14 ? 141 THR A C 1 ATOM 779 O O . THR A 1 148 ? 21.532 28.010 24.081 1.00 30.58 ? 141 THR A O 1 ATOM 780 C CB . THR A 1 148 ? 22.765 31.216 24.012 1.00 28.97 ? 141 THR A CB 1 ATOM 781 O OG1 . THR A 1 148 ? 21.367 31.422 23.808 1.00 30.57 ? 141 THR A OG1 1 ATOM 782 C CG2 . THR A 1 148 ? 23.552 32.210 23.167 1.00 30.32 ? 141 THR A CG2 1 ATOM 783 N N . SER A 1 149 ? 22.912 28.645 25.758 1.00 30.20 ? 142 SER A N 1 ATOM 784 C CA . SER A 1 149 ? 22.432 27.643 26.709 1.00 29.93 ? 142 SER A CA 1 ATOM 785 C C . SER A 1 149 ? 20.942 27.778 27.052 1.00 29.76 ? 142 SER A C 1 ATOM 786 O O . SER A 1 149 ? 20.396 28.890 27.052 1.00 30.41 ? 142 SER A O 1 ATOM 787 C CB . SER A 1 149 ? 23.249 27.724 27.995 1.00 30.50 ? 142 SER A CB 1 ATOM 788 O OG A SER A 1 149 ? 22.746 28.765 28.843 0.50 26.51 ? 142 SER A OG 1 ATOM 789 O OG B SER A 1 149 ? 23.088 26.547 28.755 0.50 33.71 ? 142 SER A OG 1 ATOM 790 N N . LEU A 1 150 ? 20.291 26.664 27.373 1.00 30.42 ? 143 LEU A N 1 ATOM 791 C CA . LEU A 1 150 ? 18.875 26.706 27.780 1.00 30.90 ? 143 LEU A CA 1 ATOM 792 C C . LEU A 1 150 ? 18.711 26.848 29.291 1.00 30.38 ? 143 LEU A C 1 ATOM 793 O O . LEU A 1 150 ? 17.597 27.116 29.777 1.00 30.07 ? 143 LEU A O 1 ATOM 794 C CB . LEU A 1 150 ? 18.100 25.488 27.250 1.00 32.51 ? 143 LEU A CB 1 ATOM 795 C CG . LEU A 1 150 ? 18.118 25.323 25.724 1.00 35.20 ? 143 LEU A CG 1 ATOM 796 C CD1 . LEU A 1 150 ? 17.271 24.137 25.292 1.00 39.41 ? 143 LEU A CD1 1 ATOM 797 C CD2 . LEU A 1 150 ? 17.662 26.612 25.039 1.00 36.42 ? 143 LEU A CD2 1 ATOM 798 N N . PHE A 1 151 ? 19.820 26.702 30.024 1.00 30.04 ? 144 PHE A N 1 ATOM 799 C CA . PHE A 1 151 ? 19.823 26.795 31.493 1.00 29.34 ? 144 PHE A CA 1 ATOM 800 C C . PHE A 1 151 ? 21.252 26.878 32.026 1.00 28.73 ? 144 PHE A C 1 ATOM 801 O O . PHE A 1 151 ? 22.212 26.506 31.325 1.00 29.37 ? 144 PHE A O 1 ATOM 802 C CB . PHE A 1 151 ? 19.098 25.586 32.118 1.00 30.91 ? 144 PHE A CB 1 ATOM 803 C CG . PHE A 1 151 ? 19.736 24.267 31.790 1.00 32.82 ? 144 PHE A CG 1 ATOM 804 C CD1 . PHE A 1 151 ? 20.777 23.772 32.575 1.00 34.75 ? 144 PHE A CD1 1 ATOM 805 C CD2 . PHE A 1 151 ? 19.324 23.522 30.682 1.00 38.59 ? 144 PHE A CD2 1 ATOM 806 C CE1 . PHE A 1 151 ? 21.387 22.574 32.284 1.00 39.19 ? 144 PHE A CE1 1 ATOM 807 C CE2 . PHE A 1 151 ? 19.934 22.304 30.378 1.00 40.25 ? 144 PHE A CE2 1 ATOM 808 C CZ . PHE A 1 151 ? 20.963 21.827 31.173 1.00 40.35 ? 144 PHE A CZ 1 ATOM 809 N N . GLU A 1 152 ? 21.404 27.349 33.264 1.00 27.00 ? 145 GLU A N 1 ATOM 810 C CA . GLU A 1 152 ? 22.721 27.357 33.929 1.00 27.04 ? 145 GLU A CA 1 ATOM 811 C C . GLU A 1 152 ? 22.981 25.971 34.508 1.00 27.81 ? 145 GLU A C 1 ATOM 812 O O . GLU A 1 152 ? 22.083 25.387 35.125 1.00 28.22 ? 145 GLU A O 1 ATOM 813 C CB . GLU A 1 152 ? 22.744 28.327 35.104 1.00 26.92 ? 145 GLU A CB 1 ATOM 814 C CG . GLU A 1 152 ? 22.691 29.790 34.763 1.00 25.65 ? 145 GLU A CG 1 ATOM 815 C CD . GLU A 1 152 ? 22.609 30.634 36.051 1.00 25.89 ? 145 GLU A CD 1 ATOM 816 O OE1 . GLU A 1 152 ? 21.512 30.679 36.645 1.00 26.00 ? 145 GLU A OE1 1 ATOM 817 O OE2 . GLU A 1 152 ? 23.650 31.184 36.497 1.00 25.25 ? 145 GLU A OE2 1 ATOM 818 N N . PRO A 1 153 ? 24.201 25.438 34.327 1.00 28.90 ? 146 PRO A N 1 ATOM 819 C CA . PRO A 1 153 ? 24.505 24.161 34.989 1.00 29.83 ? 146 PRO A CA 1 ATOM 820 C C . PRO A 1 153 ? 24.238 24.290 36.498 1.00 29.63 ? 146 PRO A C 1 ATOM 821 O O . PRO A 1 153 ? 24.799 25.202 37.143 1.00 30.37 ? 146 PRO A O 1 ATOM 822 C CB . PRO A 1 153 ? 26.008 23.986 34.724 1.00 30.82 ? 146 PRO A CB 1 ATOM 823 C CG . PRO A 1 153 ? 26.251 24.772 33.445 1.00 30.18 ? 146 PRO A CG 1 ATOM 824 C CD . PRO A 1 153 ? 25.319 25.944 33.508 1.00 30.21 ? 146 PRO A CD 1 ATOM 825 N N . PRO A 1 154 ? 23.334 23.463 37.056 1.00 29.82 ? 147 PRO A N 1 ATOM 826 C CA . PRO A 1 154 ? 22.988 23.672 38.462 1.00 29.58 ? 147 PRO A CA 1 ATOM 827 C C . PRO A 1 154 ? 24.134 23.308 39.411 1.00 30.17 ? 147 PRO A C 1 ATOM 828 O O . PRO A 1 154 ? 24.950 22.425 39.081 1.00 30.69 ? 147 PRO A O 1 ATOM 829 C CB . PRO A 1 154 ? 21.775 22.753 38.667 1.00 30.59 ? 147 PRO A CB 1 ATOM 830 C CG . PRO A 1 154 ? 21.858 21.781 37.553 1.00 31.78 ? 147 PRO A CG 1 ATOM 831 C CD . PRO A 1 154 ? 22.390 22.532 36.406 1.00 30.94 ? 147 PRO A CD 1 ATOM 832 N N . PRO A 1 155 ? 24.192 23.984 40.579 1.00 30.17 ? 148 PRO A N 1 ATOM 833 C CA . PRO A 1 155 ? 25.350 23.718 41.432 1.00 30.52 ? 148 PRO A CA 1 ATOM 834 C C . PRO A 1 155 ? 25.284 22.342 42.110 1.00 30.37 ? 148 PRO A C 1 ATOM 835 O O . PRO A 1 155 ? 24.202 21.728 42.158 1.00 30.25 ? 148 PRO A O 1 ATOM 836 C CB . PRO A 1 155 ? 25.287 24.847 42.469 1.00 29.78 ? 148 PRO A CB 1 ATOM 837 C CG . PRO A 1 155 ? 23.843 25.241 42.553 1.00 29.83 ? 148 PRO A CG 1 ATOM 838 C CD . PRO A 1 155 ? 23.300 25.015 41.128 1.00 30.55 ? 148 PRO A CD 1 ATOM 839 N N . PRO A 1 156 ? 26.414 21.887 42.679 1.00 30.48 ? 149 PRO A N 1 ATOM 840 C CA . PRO A 1 156 ? 26.475 20.554 43.299 1.00 31.39 ? 149 PRO A CA 1 ATOM 841 C C . PRO A 1 156 ? 25.353 20.273 44.311 1.00 31.00 ? 149 PRO A C 1 ATOM 842 O O . PRO A 1 156 ? 25.140 21.049 45.258 1.00 30.23 ? 149 PRO A O 1 ATOM 843 C CB . PRO A 1 156 ? 27.834 20.563 44.000 1.00 31.86 ? 149 PRO A CB 1 ATOM 844 C CG . PRO A 1 156 ? 28.659 21.511 43.171 1.00 31.96 ? 149 PRO A CG 1 ATOM 845 C CD . PRO A 1 156 ? 27.702 22.603 42.786 1.00 31.37 ? 149 PRO A CD 1 ATOM 846 N N . GLY A 1 157 ? 24.647 19.164 44.111 1.00 32.00 ? 150 GLY A N 1 ATOM 847 C CA . GLY A 1 157 ? 23.602 18.778 45.037 1.00 33.21 ? 150 GLY A CA 1 ATOM 848 C C . GLY A 1 157 ? 22.235 19.394 44.737 1.00 34.81 ? 150 GLY A C 1 ATOM 849 O O . GLY A 1 157 ? 21.259 19.030 45.390 1.00 35.50 ? 150 GLY A O 1 ATOM 850 N N . TYR A 1 158 ? 22.190 20.283 43.742 1.00 35.51 ? 151 TYR A N 1 ATOM 851 C CA . TYR A 1 158 ? 20.945 20.935 43.263 1.00 36.75 ? 151 TYR A CA 1 ATOM 852 C C . TYR A 1 158 ? 20.600 20.594 41.810 1.00 38.61 ? 151 TYR A C 1 ATOM 853 O O . TYR A 1 158 ? 19.713 21.239 41.216 1.00 38.59 ? 151 TYR A O 1 ATOM 854 C CB . TYR A 1 158 ? 21.104 22.442 43.280 1.00 35.28 ? 151 TYR A CB 1 ATOM 855 C CG . TYR A 1 158 ? 21.290 23.097 44.617 1.00 33.52 ? 151 TYR A CG 1 ATOM 856 C CD1 . TYR A 1 158 ? 20.199 23.636 45.312 1.00 30.26 ? 151 TYR A CD1 1 ATOM 857 C CD2 . TYR A 1 158 ? 22.553 23.247 45.156 1.00 28.52 ? 151 TYR A CD2 1 ATOM 858 C CE1 . TYR A 1 158 ? 20.369 24.278 46.518 1.00 29.57 ? 151 TYR A CE1 1 ATOM 859 C CE2 . TYR A 1 158 ? 22.740 23.879 46.367 1.00 27.41 ? 151 TYR A CE2 1 ATOM 860 C CZ . TYR A 1 158 ? 21.645 24.406 47.040 1.00 28.16 ? 151 TYR A CZ 1 ATOM 861 O OH . TYR A 1 158 ? 21.851 25.030 48.230 1.00 26.57 ? 151 TYR A OH 1 ATOM 862 N N A GLU A 1 159 ? 21.297 19.622 41.229 0.80 39.22 ? 152 GLU A N 1 ATOM 863 N N B GLU A 1 159 ? 21.308 19.621 41.232 0.20 39.46 ? 152 GLU A N 1 ATOM 864 C CA A GLU A 1 159 ? 21.053 19.232 39.852 0.60 40.69 ? 152 GLU A CA 1 ATOM 865 C CA B GLU A 1 159 ? 21.047 19.155 39.865 0.15 40.48 ? 152 GLU A CA 1 ATOM 866 C C A GLU A 1 159 ? 19.683 18.532 39.673 0.60 41.55 ? 152 GLU A C 1 ATOM 867 C C B GLU A 1 159 ? 19.617 18.652 39.687 0.15 41.33 ? 152 GLU A C 1 ATOM 868 O O A GLU A 1 159 ? 19.248 18.311 38.542 0.60 42.03 ? 152 GLU A O 1 ATOM 869 O O B GLU A 1 159 ? 19.076 18.675 38.580 0.15 41.43 ? 152 GLU A O 1 ATOM 870 C CB A GLU A 1 159 ? 22.222 18.382 39.307 0.80 41.51 ? 152 GLU A CB 1 ATOM 871 C CB B GLU A 1 159 ? 22.032 18.047 39.470 0.20 41.01 ? 152 GLU A CB 1 ATOM 872 C CG A GLU A 1 159 ? 23.632 18.908 39.680 0.80 41.59 ? 152 GLU A CG 1 ATOM 873 C CG B GLU A 1 159 ? 23.173 18.483 38.556 0.20 40.18 ? 152 GLU A CG 1 ATOM 874 C CD A GLU A 1 159 ? 24.204 18.308 40.980 0.80 42.01 ? 152 GLU A CD 1 ATOM 875 C CD B GLU A 1 159 ? 22.785 18.483 37.085 0.20 39.52 ? 152 GLU A CD 1 ATOM 876 O OE1 A GLU A 1 159 ? 23.436 17.906 41.867 0.80 40.05 ? 152 GLU A OE1 1 ATOM 877 O OE1 B GLU A 1 159 ? 23.668 18.728 36.240 0.20 37.62 ? 152 GLU A OE1 1 ATOM 878 O OE2 A GLU A 1 159 ? 25.446 18.264 41.124 0.80 41.28 ? 152 GLU A OE2 1 ATOM 879 O OE2 B GLU A 1 159 ? 21.597 18.247 36.772 0.20 39.82 ? 152 GLU A OE2 1 ATOM 880 N N . ASN A 1 160 ? 19.014 18.209 40.788 1.00 42.30 ? 153 ASN A N 1 ATOM 881 C CA . ASN A 1 160 ? 17.645 17.629 40.775 1.00 43.81 ? 153 ASN A CA 1 ATOM 882 C C . ASN A 1 160 ? 16.587 18.563 41.372 1.00 44.13 ? 153 ASN A C 1 ATOM 883 O O . ASN A 1 160 ? 15.423 18.186 41.561 1.00 44.72 ? 153 ASN A O 1 ATOM 884 C CB . ASN A 1 160 ? 17.613 16.281 41.509 1.00 44.97 ? 153 ASN A CB 1 ATOM 885 C CG . ASN A 1 160 ? 16.364 15.462 41.179 1.00 47.21 ? 153 ASN A CG 1 ATOM 886 O OD1 . ASN A 1 160 ? 16.128 15.094 40.021 1.00 48.93 ? 153 ASN A OD1 1 ATOM 887 N ND2 . ASN A 1 160 ? 15.565 15.170 42.202 1.00 49.83 ? 153 ASN A ND2 1 ATOM 888 N N . VAL A 1 161 ? 16.986 19.787 41.686 1.00 43.51 ? 154 VAL A N 1 ATOM 889 C CA . VAL A 1 161 ? 16.016 20.747 42.181 1.00 42.78 ? 154 VAL A CA 1 ATOM 890 C C . VAL A 1 161 ? 15.110 21.143 40.994 1.00 42.98 ? 154 VAL A C 1 ATOM 891 O O . VAL A 1 161 ? 15.576 21.396 39.871 1.00 44.02 ? 154 VAL A O 1 ATOM 892 C CB . VAL A 1 161 ? 16.684 21.931 42.929 1.00 42.67 ? 154 VAL A CB 1 ATOM 893 C CG1 . VAL A 1 161 ? 15.654 23.048 43.262 1.00 40.50 ? 154 VAL A CG1 1 ATOM 894 C CG2 . VAL A 1 161 ? 17.325 21.423 44.226 1.00 44.67 ? 154 VAL A CG2 1 ATOM 895 N N . SER A 1 162 ? 13.809 21.112 41.239 0.80 41.84 ? 155 SER A N 1 ATOM 896 C CA . SER A 1 162 ? 12.854 21.434 40.209 0.80 40.83 ? 155 SER A CA 1 ATOM 897 C C . SER A 1 162 ? 12.526 22.926 40.271 0.80 38.79 ? 155 SER A C 1 ATOM 898 O O . SER A 1 162 ? 12.769 23.612 41.296 0.80 37.45 ? 155 SER A O 1 ATOM 899 C CB . SER A 1 162 ? 11.576 20.595 40.397 0.80 42.26 ? 155 SER A CB 1 ATOM 900 O OG A SER A 1 162 ? 10.985 20.845 41.660 0.50 41.70 ? 155 SER A OG 1 ATOM 901 O OG B SER A 1 162 ? 11.167 20.002 39.174 0.50 42.66 ? 155 SER A OG 1 ATOM 902 N N . ASP A 1 163 ? 11.978 23.426 39.168 1.00 36.51 ? 156 ASP A N 1 ATOM 903 C CA . ASP A 1 163 ? 11.388 24.749 39.168 1.00 34.44 ? 156 ASP A CA 1 ATOM 904 C C . ASP A 1 163 ? 12.455 25.832 39.313 1.00 31.20 ? 156 ASP A C 1 ATOM 905 O O . ASP A 1 163 ? 12.160 26.894 39.850 1.00 31.11 ? 156 ASP A O 1 ATOM 906 C CB . ASP A 1 163 ? 10.369 24.910 40.316 1.00 35.71 ? 156 ASP A CB 1 ATOM 907 C CG . ASP A 1 163 ? 9.147 23.993 40.185 0.85 39.60 ? 156 ASP A CG 1 ATOM 908 O OD1 . ASP A 1 163 ? 8.693 23.724 39.046 0.75 43.86 ? 156 ASP A OD1 1 ATOM 909 O OD2 . ASP A 1 163 ? 8.636 23.551 41.241 0.75 43.74 ? 156 ASP A OD2 1 ATOM 910 N N . ILE A 1 164 ? 13.686 25.576 38.862 1.00 28.28 ? 157 ILE A N 1 ATOM 911 C CA . ILE A 1 164 ? 14.643 26.693 38.710 1.00 25.77 ? 157 ILE A CA 1 ATOM 912 C C . ILE A 1 164 ? 14.289 27.425 37.423 1.00 24.98 ? 157 ILE A C 1 ATOM 913 O O . ILE A 1 164 ? 14.338 26.832 36.334 1.00 24.90 ? 157 ILE A O 1 ATOM 914 C CB . ILE A 1 164 ? 16.113 26.185 38.643 1.00 25.75 ? 157 ILE A CB 1 ATOM 915 C CG1 . ILE A 1 164 ? 16.501 25.541 39.981 1.00 25.18 ? 157 ILE A CG1 1 ATOM 916 C CG2 . ILE A 1 164 ? 17.069 27.332 38.279 1.00 24.65 ? 157 ILE A CG2 1 ATOM 917 C CD1 . ILE A 1 164 ? 17.853 24.755 39.958 1.00 25.55 ? 157 ILE A CD1 1 ATOM 918 N N . VAL A 1 165 ? 13.919 28.701 37.510 1.00 23.34 ? 158 VAL A N 1 ATOM 919 C CA . VAL A 1 165 ? 13.548 29.431 36.303 1.00 23.10 ? 158 VAL A CA 1 ATOM 920 C C . VAL A 1 165 ? 14.811 29.650 35.472 1.00 23.89 ? 158 VAL A C 1 ATOM 921 O O . VAL A 1 165 ? 15.831 30.080 36.012 1.00 23.02 ? 158 VAL A O 1 ATOM 922 C CB . VAL A 1 165 ? 12.843 30.794 36.650 1.00 22.37 ? 158 VAL A CB 1 ATOM 923 C CG1 . VAL A 1 165 ? 13.863 31.901 37.120 1.00 21.74 ? 158 VAL A CG1 1 ATOM 924 C CG2 . VAL A 1 165 ? 12.023 31.275 35.488 1.00 22.83 ? 158 VAL A CG2 1 ATOM 925 N N . PRO A 1 166 ? 14.778 29.311 34.165 1.00 24.22 ? 159 PRO A N 1 ATOM 926 C CA . PRO A 1 166 ? 16.007 29.531 33.389 1.00 25.19 ? 159 PRO A CA 1 ATOM 927 C C . PRO A 1 166 ? 16.256 31.024 33.225 1.00 24.20 ? 159 PRO A C 1 ATOM 928 O O . PRO A 1 166 ? 15.334 31.824 33.428 1.00 24.10 ? 159 PRO A O 1 ATOM 929 C CB . PRO A 1 166 ? 15.699 28.888 32.024 1.00 26.29 ? 159 PRO A CB 1 ATOM 930 C CG . PRO A 1 166 ? 14.198 28.871 31.924 1.00 26.68 ? 159 PRO A CG 1 ATOM 931 C CD . PRO A 1 166 ? 13.696 28.706 33.362 1.00 25.73 ? 159 PRO A CD 1 ATOM 932 N N . PRO A 1 167 ? 17.507 31.404 32.902 1.00 23.65 ? 160 PRO A N 1 ATOM 933 C CA . PRO A 1 167 ? 17.796 32.824 32.700 1.00 23.22 ? 160 PRO A CA 1 ATOM 934 C C . PRO A 1 167 ? 16.887 33.459 31.641 1.00 22.08 ? 160 PRO A C 1 ATOM 935 O O . PRO A 1 167 ? 16.645 32.878 30.586 1.00 22.73 ? 160 PRO A O 1 ATOM 936 C CB . PRO A 1 167 ? 19.258 32.811 32.250 1.00 23.24 ? 160 PRO A CB 1 ATOM 937 C CG . PRO A 1 167 ? 19.798 31.537 32.909 1.00 23.23 ? 160 PRO A CG 1 ATOM 938 C CD . PRO A 1 167 ? 18.700 30.564 32.662 1.00 24.12 ? 160 PRO A CD 1 ATOM 939 N N . PHE A 1 168 ? 16.375 34.638 31.963 1.00 21.30 ? 161 PHE A N 1 ATOM 940 C CA . PHE A 1 168 ? 15.538 35.410 31.043 1.00 21.13 ? 161 PHE A CA 1 ATOM 941 C C . PHE A 1 168 ? 15.495 36.830 31.531 1.00 21.06 ? 161 PHE A C 1 ATOM 942 O O . PHE A 1 168 ? 15.834 37.093 32.685 1.00 20.86 ? 161 PHE A O 1 ATOM 943 C CB . PHE A 1 168 ? 14.102 34.838 30.946 1.00 21.23 ? 161 PHE A CB 1 ATOM 944 C CG . PHE A 1 168 ? 13.195 35.140 32.154 1.00 19.35 ? 161 PHE A CG 1 ATOM 945 C CD1 . PHE A 1 168 ? 12.019 35.908 31.978 1.00 18.97 ? 161 PHE A CD1 1 ATOM 946 C CD2 . PHE A 1 168 ? 13.454 34.585 33.417 1.00 21.91 ? 161 PHE A CD2 1 ATOM 947 C CE1 . PHE A 1 168 ? 11.148 36.152 33.051 1.00 19.58 ? 161 PHE A CE1 1 ATOM 948 C CE2 . PHE A 1 168 ? 12.598 34.864 34.529 1.00 20.32 ? 161 PHE A CE2 1 ATOM 949 C CZ . PHE A 1 168 ? 11.440 35.637 34.337 1.00 20.48 ? 161 PHE A CZ 1 ATOM 950 N N . SER A 1 169 ? 15.088 37.730 30.638 1.00 20.89 ? 162 SER A N 1 ATOM 951 C CA . SER A 1 169 ? 14.882 39.132 31.022 1.00 19.98 ? 162 SER A CA 1 ATOM 952 C C . SER A 1 169 ? 13.388 39.350 31.220 1.00 19.67 ? 162 SER A C 1 ATOM 953 O O . SER A 1 169 ? 12.626 39.349 30.258 1.00 21.19 ? 162 SER A O 1 ATOM 954 C CB . SER A 1 169 ? 15.403 40.046 29.911 1.00 20.66 ? 162 SER A CB 1 ATOM 955 O OG . SER A 1 169 ? 16.822 39.890 29.723 1.00 21.45 ? 162 SER A OG 1 ATOM 956 N N . ALA A 1 170 ? 12.980 39.562 32.471 1.00 20.06 ? 163 ALA A N 1 ATOM 957 C CA . ALA A 1 170 ? 11.541 39.666 32.780 1.00 19.80 ? 163 ALA A CA 1 ATOM 958 C C . ALA A 1 170 ? 10.957 40.887 32.105 1.00 20.23 ? 163 ALA A C 1 ATOM 959 O O . ALA A 1 170 ? 11.533 41.989 32.163 1.00 19.08 ? 163 ALA A O 1 ATOM 960 C CB . ALA A 1 170 ? 11.314 39.725 34.282 1.00 20.13 ? 163 ALA A CB 1 ATOM 961 N N . PHE A 1 171 ? 9.822 40.636 31.446 1.00 20.15 ? 164 PHE A N 1 ATOM 962 C CA . PHE A 1 171 ? 8.956 41.588 30.734 1.00 20.12 ? 164 PHE A CA 1 ATOM 963 C C . PHE A 1 171 ? 9.396 41.815 29.291 1.00 21.29 ? 164 PHE A C 1 ATOM 964 O O . PHE A 1 171 ? 8.772 42.610 28.587 1.00 21.18 ? 164 PHE A O 1 ATOM 965 C CB . PHE A 1 171 ? 8.736 42.911 31.487 1.00 19.37 ? 164 PHE A CB 1 ATOM 966 C CG . PHE A 1 171 ? 8.082 42.715 32.815 1.00 19.63 ? 164 PHE A CG 1 ATOM 967 C CD1 . PHE A 1 171 ? 6.686 42.536 32.898 1.00 20.23 ? 164 PHE A CD1 1 ATOM 968 C CD2 . PHE A 1 171 ? 8.873 42.685 33.984 1.00 19.10 ? 164 PHE A CD2 1 ATOM 969 C CE1 . PHE A 1 171 ? 6.053 42.375 34.143 1.00 18.82 ? 164 PHE A CE1 1 ATOM 970 C CE2 . PHE A 1 171 ? 8.285 42.521 35.232 1.00 18.65 ? 164 PHE A CE2 1 ATOM 971 C CZ . PHE A 1 171 ? 6.860 42.364 35.339 1.00 18.32 ? 164 PHE A CZ 1 ATOM 972 N N . SER A 1 172 ? 10.392 41.068 28.826 1.00 21.28 ? 165 SER A N 1 ATOM 973 C CA . SER A 1 172 ? 10.713 41.108 27.388 1.00 22.81 ? 165 SER A CA 1 ATOM 974 C C . SER A 1 172 ? 9.455 40.756 26.579 1.00 23.26 ? 165 SER A C 1 ATOM 975 O O . SER A 1 172 ? 8.712 39.847 26.950 1.00 24.27 ? 165 SER A O 1 ATOM 976 C CB . SER A 1 172 ? 11.784 40.078 27.005 1.00 23.37 ? 165 SER A CB 1 ATOM 977 O OG . SER A 1 172 ? 11.964 40.143 25.599 1.00 24.31 ? 165 SER A OG 1 ATOM 978 N N . PRO A 1 173 ? 9.209 41.487 25.473 1.00 23.97 ? 166 PRO A N 1 ATOM 979 C CA . PRO A 1 173 ? 8.168 40.993 24.578 1.00 24.82 ? 166 PRO A CA 1 ATOM 980 C C . PRO A 1 173 ? 8.673 39.768 23.825 1.00 26.01 ? 166 PRO A C 1 ATOM 981 O O . PRO A 1 173 ? 9.874 39.448 23.827 1.00 25.28 ? 166 PRO A O 1 ATOM 982 C CB . PRO A 1 173 ? 7.979 42.159 23.595 1.00 25.44 ? 166 PRO A CB 1 ATOM 983 C CG . PRO A 1 173 ? 9.348 42.827 23.535 1.00 25.77 ? 166 PRO A CG 1 ATOM 984 C CD . PRO A 1 173 ? 9.845 42.722 24.974 1.00 24.66 ? 166 PRO A CD 1 ATOM 985 N N . GLN A 1 174 ? 7.744 39.100 23.157 1.00 26.49 ? 167 GLN A N 1 ATOM 986 C CA . GLN A 1 174 ? 8.075 37.974 22.298 1.00 28.11 ? 167 GLN A CA 1 ATOM 987 C C . GLN A 1 174 ? 8.602 38.453 20.965 1.00 29.37 ? 167 GLN A C 1 ATOM 988 O O . GLN A 1 174 ? 8.268 39.543 20.510 1.00 30.30 ? 167 GLN A O 1 ATOM 989 C CB . GLN A 1 174 ? 6.824 37.143 22.081 1.00 29.03 ? 167 GLN A CB 1 ATOM 990 C CG . GLN A 1 174 ? 6.302 36.509 23.352 1.00 30.77 ? 167 GLN A CG 1 ATOM 991 C CD . GLN A 1 174 ? 5.020 35.718 23.161 1.00 38.01 ? 167 GLN A CD 1 ATOM 992 O OE1 . GLN A 1 174 ? 4.486 35.631 22.059 1.00 42.41 ? 167 GLN A OE1 1 ATOM 993 N NE2 . GLN A 1 174 ? 4.529 35.124 24.241 1.00 37.58 ? 167 GLN A NE2 1 ATOM 994 N N . GLY A 1 175 ? 9.432 37.630 20.334 1.00 29.57 ? 168 GLY A N 1 ATOM 995 C CA . GLY A 1 175 ? 9.892 37.948 18.991 1.00 30.75 ? 168 GLY A CA 1 ATOM 996 C C . GLY A 1 175 ? 10.989 37.003 18.589 1.00 31.49 ? 168 GLY A C 1 ATOM 997 O O . GLY A 1 175 ? 11.592 36.329 19.438 1.00 31.27 ? 168 GLY A O 1 ATOM 998 N N . MET A 1 176 ? 11.241 36.950 17.279 1.00 32.83 ? 169 MET A N 1 ATOM 999 C CA . MET A 1 176 ? 12.382 36.205 16.761 1.00 33.79 ? 169 MET A CA 1 ATOM 1000 C C . MET A 1 176 ? 13.199 37.087 15.808 1.00 34.53 ? 169 MET A C 1 ATOM 1001 O O . MET A 1 176 ? 13.440 36.685 14.648 1.00 36.55 ? 169 MET A O 1 ATOM 1002 C CB . MET A 1 176 ? 11.918 34.913 16.071 1.00 34.93 ? 169 MET A CB 1 ATOM 1003 C CG . MET A 1 176 ? 11.421 33.804 17.027 0.90 37.52 ? 169 MET A CG 1 ATOM 1004 S SD . MET A 1 176 ? 10.996 32.324 16.086 0.75 48.42 ? 169 MET A SD 1 ATOM 1005 C CE . MET A 1 176 ? 10.025 31.407 17.267 0.75 45.83 ? 169 MET A CE 1 ATOM 1006 N N . PRO A 1 177 ? 13.652 38.271 16.275 1.00 33.65 ? 170 PRO A N 1 ATOM 1007 C CA . PRO A 1 177 ? 14.399 39.190 15.406 1.00 34.71 ? 170 PRO A CA 1 ATOM 1008 C C . PRO A 1 177 ? 15.736 38.576 14.933 1.00 36.11 ? 170 PRO A C 1 ATOM 1009 O O . PRO A 1 177 ? 16.410 37.891 15.714 1.00 35.69 ? 170 PRO A O 1 ATOM 1010 C CB . PRO A 1 177 ? 14.630 40.421 16.303 1.00 33.69 ? 170 PRO A CB 1 ATOM 1011 C CG . PRO A 1 177 ? 14.553 39.897 17.687 1.00 32.77 ? 170 PRO A CG 1 ATOM 1012 C CD . PRO A 1 177 ? 13.555 38.787 17.661 1.00 32.47 ? 170 PRO A CD 1 ATOM 1013 N N A GLU A 1 178 ? 16.062 38.799 13.658 0.60 37.35 ? 171 GLU A N 1 ATOM 1014 N N B GLU A 1 178 ? 16.105 38.822 13.675 0.40 37.04 ? 171 GLU A N 1 ATOM 1015 C CA A GLU A 1 178 ? 17.335 38.382 13.066 0.60 38.72 ? 171 GLU A CA 1 ATOM 1016 C CA B GLU A 1 178 ? 17.369 38.320 13.119 0.40 38.04 ? 171 GLU A CA 1 ATOM 1017 C C A GLU A 1 178 ? 18.053 39.622 12.598 0.60 38.66 ? 171 GLU A C 1 ATOM 1018 C C B GLU A 1 178 ? 18.123 39.425 12.397 0.40 38.39 ? 171 GLU A C 1 ATOM 1019 O O A GLU A 1 178 ? 17.436 40.517 12.018 0.60 39.12 ? 171 GLU A O 1 ATOM 1020 O O B GLU A 1 178 ? 17.599 40.024 11.457 0.40 38.90 ? 171 GLU A O 1 ATOM 1021 C CB A GLU A 1 178 ? 17.124 37.499 11.833 0.60 39.96 ? 171 GLU A CB 1 ATOM 1022 C CB B GLU A 1 178 ? 17.120 37.161 12.153 0.40 39.04 ? 171 GLU A CB 1 ATOM 1023 C CG A GLU A 1 178 ? 16.113 36.387 11.971 0.60 42.39 ? 171 GLU A CG 1 ATOM 1024 C CG B GLU A 1 178 ? 18.383 36.670 11.463 0.40 40.53 ? 171 GLU A CG 1 ATOM 1025 C CD A GLU A 1 178 ? 16.012 35.531 10.721 0.60 44.53 ? 171 GLU A CD 1 ATOM 1026 C CD B GLU A 1 178 ? 18.104 35.858 10.220 0.40 43.35 ? 171 GLU A CD 1 ATOM 1027 O OE1 A GLU A 1 178 ? 15.202 34.578 10.716 0.60 46.59 ? 171 GLU A OE1 1 ATOM 1028 O OE1 B GLU A 1 178 ? 18.502 36.303 9.120 0.40 44.54 ? 171 GLU A OE1 1 ATOM 1029 O OE2 A GLU A 1 178 ? 16.732 35.809 9.734 0.60 47.04 ? 171 GLU A OE2 1 ATOM 1030 O OE2 B GLU A 1 178 ? 17.491 34.775 10.340 0.40 44.31 ? 171 GLU A OE2 1 ATOM 1031 N N . GLY A 1 179 ? 19.358 39.682 12.824 1.00 38.30 ? 172 GLY A N 1 ATOM 1032 C CA . GLY A 1 179 ? 20.133 40.783 12.275 1.00 38.45 ? 172 GLY A CA 1 ATOM 1033 C C . GLY A 1 179 ? 21.600 40.771 12.598 1.00 37.89 ? 172 GLY A C 1 ATOM 1034 O O . GLY A 1 179 ? 22.138 39.778 13.097 1.00 38.15 ? 172 GLY A O 1 ATOM 1035 N N . ASP A 1 180 ? 22.236 41.897 12.304 1.00 37.13 ? 173 ASP A N 1 ATOM 1036 C CA . ASP A 1 180 ? 23.656 42.080 12.561 1.00 37.57 ? 173 ASP A CA 1 ATOM 1037 C C . ASP A 1 180 ? 23.843 42.696 13.938 1.00 35.80 ? 173 ASP A C 1 ATOM 1038 O O . ASP A 1 180 ? 23.070 43.570 14.348 1.00 35.06 ? 173 ASP A O 1 ATOM 1039 C CB . ASP A 1 180 ? 24.264 42.993 11.504 1.00 38.69 ? 173 ASP A CB 1 ATOM 1040 C CG . ASP A 1 180 ? 24.105 42.440 10.091 0.90 41.58 ? 173 ASP A CG 1 ATOM 1041 O OD1 . ASP A 1 180 ? 24.203 41.207 9.916 0.90 44.45 ? 173 ASP A OD1 1 ATOM 1042 O OD2 . ASP A 1 180 ? 23.881 43.241 9.162 0.90 42.97 ? 173 ASP A OD2 1 ATOM 1043 N N . LEU A 1 181 ? 24.871 42.223 14.638 1.00 35.01 ? 174 LEU A N 1 ATOM 1044 C CA . LEU A 1 181 ? 25.218 42.716 15.967 1.00 33.91 ? 174 LEU A CA 1 ATOM 1045 C C . LEU A 1 181 ? 25.980 44.035 15.948 1.00 34.14 ? 174 LEU A C 1 ATOM 1046 O O . LEU A 1 181 ? 26.871 44.251 15.105 1.00 34.98 ? 174 LEU A O 1 ATOM 1047 C CB . LEU A 1 181 ? 26.099 41.662 16.655 1.00 34.08 ? 174 LEU A CB 1 ATOM 1048 C CG A LEU A 1 181 ? 25.970 41.169 18.094 0.50 33.45 ? 174 LEU A CG 1 ATOM 1049 C CG B LEU A 1 181 ? 25.517 40.312 17.077 0.50 32.28 ? 174 LEU A CG 1 ATOM 1050 C CD1 A LEU A 1 181 ? 24.521 41.076 18.584 0.50 32.35 ? 174 LEU A CD1 1 ATOM 1051 C CD1 B LEU A 1 181 ? 26.600 39.480 17.734 0.50 31.79 ? 174 LEU A CD1 1 ATOM 1052 C CD2 A LEU A 1 181 ? 26.654 39.820 18.197 0.50 33.45 ? 174 LEU A CD2 1 ATOM 1053 C CD2 B LEU A 1 181 ? 24.310 40.457 18.010 0.50 31.05 ? 174 LEU A CD2 1 ATOM 1054 N N . VAL A 1 182 ? 25.653 44.903 16.904 1.00 33.17 ? 175 VAL A N 1 ATOM 1055 C CA . VAL A 1 182 ? 26.501 46.043 17.254 1.00 32.88 ? 175 VAL A CA 1 ATOM 1056 C C . VAL A 1 182 ? 26.812 45.894 18.731 1.00 32.38 ? 175 VAL A C 1 ATOM 1057 O O . VAL A 1 182 ? 25.898 45.660 19.544 1.00 31.30 ? 175 VAL A O 1 ATOM 1058 C CB . VAL A 1 182 ? 25.811 47.405 16.975 1.00 33.07 ? 175 VAL A CB 1 ATOM 1059 C CG1 . VAL A 1 182 ? 26.600 48.562 17.588 1.00 32.02 ? 175 VAL A CG1 1 ATOM 1060 C CG2 . VAL A 1 182 ? 25.681 47.604 15.468 1.00 33.76 ? 175 VAL A CG2 1 ATOM 1061 N N . TYR A 1 183 ? 28.092 46.007 19.075 1.00 31.29 ? 176 TYR A N 1 ATOM 1062 C CA . TYR A 1 183 ? 28.507 45.985 20.474 1.00 30.28 ? 176 TYR A CA 1 ATOM 1063 C C . TYR A 1 183 ? 28.502 47.403 21.039 1.00 30.25 ? 176 TYR A C 1 ATOM 1064 O O . TYR A 1 183 ? 29.116 48.304 20.474 1.00 31.12 ? 176 TYR A O 1 ATOM 1065 C CB . TYR A 1 183 ? 29.894 45.334 20.585 1.00 30.89 ? 176 TYR A CB 1 ATOM 1066 C CG . TYR A 1 183 ? 30.546 45.506 21.941 1.00 29.40 ? 176 TYR A CG 1 ATOM 1067 C CD1 . TYR A 1 183 ? 29.976 44.936 23.085 1.00 29.18 ? 176 TYR A CD1 1 ATOM 1068 C CD2 . TYR A 1 183 ? 31.725 46.235 22.076 1.00 32.09 ? 176 TYR A CD2 1 ATOM 1069 C CE1 . TYR A 1 183 ? 30.581 45.095 24.346 1.00 30.31 ? 176 TYR A CE1 1 ATOM 1070 C CE2 . TYR A 1 183 ? 32.337 46.390 23.313 1.00 32.71 ? 176 TYR A CE2 1 ATOM 1071 C CZ . TYR A 1 183 ? 31.753 45.820 24.443 1.00 30.28 ? 176 TYR A CZ 1 ATOM 1072 O OH . TYR A 1 183 ? 32.363 45.975 25.671 1.00 29.03 ? 176 TYR A OH 1 ATOM 1073 N N . VAL A 1 184 ? 27.791 47.598 22.160 1.00 28.76 ? 177 VAL A N 1 ATOM 1074 C CA . VAL A 1 184 ? 27.521 48.949 22.676 1.00 29.43 ? 177 VAL A CA 1 ATOM 1075 C C . VAL A 1 184 ? 28.106 49.186 24.073 1.00 28.66 ? 177 VAL A C 1 ATOM 1076 O O . VAL A 1 184 ? 27.629 50.051 24.822 1.00 28.70 ? 177 VAL A O 1 ATOM 1077 C CB . VAL A 1 184 ? 26.002 49.265 22.664 1.00 29.05 ? 177 VAL A CB 1 ATOM 1078 C CG1 . VAL A 1 184 ? 25.468 49.184 21.262 1.00 31.32 ? 177 VAL A CG1 1 ATOM 1079 C CG2 . VAL A 1 184 ? 25.222 48.266 23.563 1.00 29.16 ? 177 VAL A CG2 1 ATOM 1080 N N . ASN A 1 185 ? 29.145 48.422 24.416 1.00 28.83 ? 178 ASN A N 1 ATOM 1081 C CA . ASN A 1 185 ? 29.801 48.538 25.710 1.00 27.55 ? 178 ASN A CA 1 ATOM 1082 C C . ASN A 1 185 ? 28.750 48.312 26.806 1.00 27.26 ? 178 ASN A C 1 ATOM 1083 O O . ASN A 1 185 ? 28.056 47.303 26.777 1.00 27.07 ? 178 ASN A O 1 ATOM 1084 C CB . ASN A 1 185 ? 30.532 49.892 25.838 1.00 28.17 ? 178 ASN A CB 1 ATOM 1085 C CG . ASN A 1 185 ? 31.614 49.889 26.908 1.00 27.66 ? 178 ASN A CG 1 ATOM 1086 O OD1 . ASN A 1 185 ? 32.105 48.840 27.308 1.00 29.70 ? 178 ASN A OD1 1 ATOM 1087 N ND2 . ASN A 1 185 ? 31.972 51.078 27.394 1.00 29.86 ? 178 ASN A ND2 1 ATOM 1088 N N . TYR A 1 186 ? 28.616 49.239 27.755 1.00 26.61 ? 179 TYR A N 1 ATOM 1089 C CA . TYR A 1 186 ? 27.617 49.077 28.830 1.00 25.38 ? 179 TYR A CA 1 ATOM 1090 C C . TYR A 1 186 ? 26.224 49.604 28.476 1.00 25.48 ? 179 TYR A C 1 ATOM 1091 O O . TYR A 1 186 ? 25.317 49.613 29.340 1.00 24.90 ? 179 TYR A O 1 ATOM 1092 C CB . TYR A 1 186 ? 28.091 49.784 30.124 1.00 24.73 ? 179 TYR A CB 1 ATOM 1093 C CG . TYR A 1 186 ? 29.363 49.210 30.723 1.00 26.34 ? 179 TYR A CG 1 ATOM 1094 C CD1 . TYR A 1 186 ? 29.332 48.030 31.485 1.00 26.07 ? 179 TYR A CD1 1 ATOM 1095 C CD2 . TYR A 1 186 ? 30.593 49.887 30.587 1.00 26.68 ? 179 TYR A CD2 1 ATOM 1096 C CE1 . TYR A 1 186 ? 30.507 47.520 32.072 1.00 28.90 ? 179 TYR A CE1 1 ATOM 1097 C CE2 . TYR A 1 186 ? 31.767 49.374 31.154 1.00 29.21 ? 179 TYR A CE2 1 ATOM 1098 C CZ . TYR A 1 186 ? 31.714 48.210 31.907 1.00 28.58 ? 179 TYR A CZ 1 ATOM 1099 O OH . TYR A 1 186 ? 32.867 47.738 32.483 1.00 30.41 ? 179 TYR A OH 1 ATOM 1100 N N . ALA A 1 187 ? 26.038 50.060 27.229 1.00 25.66 ? 180 ALA A N 1 ATOM 1101 C CA . ALA A 1 187 ? 24.743 50.600 26.777 1.00 25.10 ? 180 ALA A CA 1 ATOM 1102 C C . ALA A 1 187 ? 24.291 51.809 27.619 1.00 24.99 ? 180 ALA A C 1 ATOM 1103 O O . ALA A 1 187 ? 23.085 52.082 27.768 1.00 24.23 ? 180 ALA A O 1 ATOM 1104 C CB . ALA A 1 187 ? 23.650 49.500 26.750 1.00 24.60 ? 180 ALA A CB 1 ATOM 1105 N N . ARG A 1 188 ? 25.267 52.542 28.147 1.00 25.09 ? 181 ARG A N 1 ATOM 1106 C CA . ARG A 1 188 ? 24.976 53.793 28.857 1.00 24.49 ? 181 ARG A CA 1 ATOM 1107 C C . ARG A 1 188 ? 24.655 54.917 27.879 1.00 24.83 ? 181 ARG A C 1 ATOM 1108 O O . ARG A 1 188 ? 24.989 54.861 26.690 1.00 25.41 ? 181 ARG A O 1 ATOM 1109 C CB . ARG A 1 188 ? 26.174 54.217 29.701 1.00 24.88 ? 181 ARG A CB 1 ATOM 1110 C CG . ARG A 1 188 ? 26.531 53.230 30.783 1.00 25.61 ? 181 ARG A CG 1 ATOM 1111 C CD . ARG A 1 188 ? 27.861 53.525 31.394 1.00 25.41 ? 181 ARG A CD 1 ATOM 1112 N NE . ARG A 1 188 ? 28.929 53.400 30.399 1.00 26.18 ? 181 ARG A NE 1 ATOM 1113 C CZ . ARG A 1 188 ? 30.232 53.571 30.635 1.00 29.74 ? 181 ARG A CZ 1 ATOM 1114 N NH1 . ARG A 1 188 ? 30.681 53.831 31.860 1.00 29.90 ? 181 ARG A NH1 1 ATOM 1115 N NH2 . ARG A 1 188 ? 31.097 53.457 29.625 1.00 28.77 ? 181 ARG A NH2 1 ATOM 1116 N N . THR A 1 189 ? 24.044 55.985 28.397 1.00 23.81 ? 182 THR A N 1 ATOM 1117 C CA . THR A 1 189 ? 23.789 57.145 27.560 1.00 24.69 ? 182 THR A CA 1 ATOM 1118 C C . THR A 1 189 ? 25.061 57.600 26.813 1.00 26.07 ? 182 THR A C 1 ATOM 1119 O O . THR A 1 189 ? 25.027 57.866 25.594 1.00 27.03 ? 182 THR A O 1 ATOM 1120 C CB . THR A 1 189 ? 23.207 58.280 28.403 1.00 24.83 ? 182 THR A CB 1 ATOM 1121 O OG1 . THR A 1 189 ? 21.955 57.847 28.954 1.00 24.88 ? 182 THR A OG1 1 ATOM 1122 C CG2 . THR A 1 189 ? 22.971 59.525 27.516 1.00 25.07 ? 182 THR A CG2 1 ATOM 1123 N N . GLU A 1 190 ? 26.186 57.656 27.524 1.00 27.02 ? 183 GLU A N 1 ATOM 1124 C CA . GLU A 1 190 ? 27.418 58.155 26.921 1.00 28.68 ? 183 GLU A CA 1 ATOM 1125 C C . GLU A 1 190 ? 28.008 57.149 25.932 1.00 29.19 ? 183 GLU A C 1 ATOM 1126 O O . GLU A 1 190 ? 28.751 57.530 25.022 1.00 30.06 ? 183 GLU A O 1 ATOM 1127 C CB . GLU A 1 190 ? 28.452 58.525 27.979 1.00 28.79 ? 183 GLU A CB 1 ATOM 1128 C CG . GLU A 1 190 ? 28.893 57.371 28.871 0.90 31.60 ? 183 GLU A CG 1 ATOM 1129 C CD . GLU A 1 190 ? 28.154 57.320 30.205 0.85 32.16 ? 183 GLU A CD 1 ATOM 1130 O OE1 . GLU A 1 190 ? 26.931 57.683 30.285 0.85 29.36 ? 183 GLU A OE1 1 ATOM 1131 O OE2 . GLU A 1 190 ? 28.819 56.898 31.181 0.85 30.93 ? 183 GLU A OE2 1 ATOM 1132 N N . ASP A 1 191 ? 27.668 55.867 26.112 1.00 28.45 ? 184 ASP A N 1 ATOM 1133 C CA . ASP A 1 191 ? 28.136 54.843 25.146 1.00 29.06 ? 184 ASP A CA 1 ATOM 1134 C C . ASP A 1 191 ? 27.429 55.035 23.812 1.00 29.56 ? 184 ASP A C 1 ATOM 1135 O O . ASP A 1 191 ? 28.045 54.921 22.738 1.00 29.69 ? 184 ASP A O 1 ATOM 1136 C CB . ASP A 1 191 ? 27.876 53.425 25.678 1.00 28.25 ? 184 ASP A CB 1 ATOM 1137 C CG . ASP A 1 191 ? 28.741 53.092 26.869 1.00 28.30 ? 184 ASP A CG 1 ATOM 1138 O OD1 . ASP A 1 191 ? 29.917 53.536 26.896 1.00 28.07 ? 184 ASP A OD1 1 ATOM 1139 O OD2 . ASP A 1 191 ? 28.257 52.381 27.771 1.00 25.42 ? 184 ASP A OD2 1 ATOM 1140 N N A PHE A 1 192 ? 26.130 55.322 23.876 0.50 28.55 ? 185 PHE A N 1 ATOM 1141 N N B PHE A 1 192 ? 26.129 55.319 23.873 0.50 28.55 ? 185 PHE A N 1 ATOM 1142 C CA A PHE A 1 192 ? 25.362 55.593 22.669 0.50 29.02 ? 185 PHE A CA 1 ATOM 1143 C CA B PHE A 1 192 ? 25.372 55.590 22.660 0.50 29.02 ? 185 PHE A CA 1 ATOM 1144 C C A PHE A 1 192 ? 25.725 56.938 22.053 0.50 29.86 ? 185 PHE A C 1 ATOM 1145 C C B PHE A 1 192 ? 25.752 56.932 22.049 0.50 29.87 ? 185 PHE A C 1 ATOM 1146 O O A PHE A 1 192 ? 25.718 57.074 20.834 0.50 30.81 ? 185 PHE A O 1 ATOM 1147 O O B PHE A 1 192 ? 25.794 57.059 20.829 0.50 30.81 ? 185 PHE A O 1 ATOM 1148 C CB A PHE A 1 192 ? 23.857 55.457 22.928 0.50 27.94 ? 185 PHE A CB 1 ATOM 1149 C CB B PHE A 1 192 ? 23.864 55.455 22.906 0.50 27.96 ? 185 PHE A CB 1 ATOM 1150 C CG A PHE A 1 192 ? 23.398 54.033 22.946 0.50 27.05 ? 185 PHE A CG 1 ATOM 1151 C CG B PHE A 1 192 ? 23.408 54.031 22.932 0.50 27.05 ? 185 PHE A CG 1 ATOM 1152 C CD1 A PHE A 1 192 ? 23.107 53.396 24.143 0.50 26.75 ? 185 PHE A CD1 1 ATOM 1153 C CD1 B PHE A 1 192 ? 23.131 53.395 24.133 0.50 26.75 ? 185 PHE A CD1 1 ATOM 1154 C CD2 A PHE A 1 192 ? 23.310 53.312 21.762 0.50 26.99 ? 185 PHE A CD2 1 ATOM 1155 C CD2 B PHE A 1 192 ? 23.310 53.306 21.751 0.50 26.95 ? 185 PHE A CD2 1 ATOM 1156 C CE1 A PHE A 1 192 ? 22.698 52.073 24.157 0.50 26.50 ? 185 PHE A CE1 1 ATOM 1157 C CE1 B PHE A 1 192 ? 22.724 52.072 24.155 0.50 26.52 ? 185 PHE A CE1 1 ATOM 1158 C CE2 A PHE A 1 192 ? 22.901 51.988 21.771 0.50 27.31 ? 185 PHE A CE2 1 ATOM 1159 C CE2 B PHE A 1 192 ? 22.905 51.981 21.768 0.50 27.32 ? 185 PHE A CE2 1 ATOM 1160 C CZ A PHE A 1 192 ? 22.599 51.369 22.968 0.50 26.64 ? 185 PHE A CZ 1 ATOM 1161 C CZ B PHE A 1 192 ? 22.616 51.365 22.969 0.50 26.65 ? 185 PHE A CZ 1 ATOM 1162 N N . PHE A 1 193 ? 26.059 57.927 22.883 1.00 29.94 ? 186 PHE A N 1 ATOM 1163 C CA . PHE A 1 193 ? 26.586 59.218 22.359 1.00 31.43 ? 186 PHE A CA 1 ATOM 1164 C C . PHE A 1 193 ? 27.839 58.958 21.521 1.00 33.24 ? 186 PHE A C 1 ATOM 1165 O O . PHE A 1 193 ? 27.969 59.469 20.396 1.00 33.84 ? 186 PHE A O 1 ATOM 1166 C CB . PHE A 1 193 ? 26.965 60.207 23.485 1.00 31.14 ? 186 PHE A CB 1 ATOM 1167 C CG . PHE A 1 193 ? 25.798 60.948 24.107 1.00 31.18 ? 186 PHE A CG 1 ATOM 1168 C CD1 . PHE A 1 193 ? 24.559 61.016 23.493 1.00 32.41 ? 186 PHE A CD1 1 ATOM 1169 C CD2 . PHE A 1 193 ? 25.981 61.633 25.308 1.00 30.32 ? 186 PHE A CD2 1 ATOM 1170 C CE1 . PHE A 1 193 ? 23.493 61.714 24.097 1.00 31.99 ? 186 PHE A CE1 1 ATOM 1171 C CE2 . PHE A 1 193 ? 24.922 62.348 25.914 1.00 30.28 ? 186 PHE A CE2 1 ATOM 1172 C CZ . PHE A 1 193 ? 23.686 62.393 25.292 1.00 30.04 ? 186 PHE A CZ 1 ATOM 1173 N N . LYS A 1 194 ? 28.757 58.158 22.066 1.00 33.67 ? 187 LYS A N 1 ATOM 1174 C CA . LYS A 1 194 ? 30.035 57.857 21.397 1.00 35.05 ? 187 LYS A CA 1 ATOM 1175 C C . LYS A 1 194 ? 29.779 57.142 20.068 1.00 36.46 ? 187 LYS A C 1 ATOM 1176 O O . LYS A 1 194 ? 30.401 57.476 19.053 1.00 37.69 ? 187 LYS A O 1 ATOM 1177 C CB . LYS A 1 194 ? 30.931 57.006 22.310 1.00 34.99 ? 187 LYS A CB 1 ATOM 1178 C CG . LYS A 1 194 ? 32.290 56.547 21.698 0.80 37.18 ? 187 LYS A CG 1 ATOM 1179 C CD . LYS A 1 194 ? 33.413 57.566 21.909 0.66 41.14 ? 187 LYS A CD 1 ATOM 1180 C CE . LYS A 1 194 ? 33.846 57.611 23.372 0.60 42.25 ? 187 LYS A CE 1 ATOM 1181 N NZ . LYS A 1 194 ? 34.866 58.655 23.625 0.50 44.90 ? 187 LYS A NZ 1 ATOM 1182 N N . LEU A 1 195 ? 28.863 56.174 20.060 1.00 35.57 ? 188 LEU A N 1 ATOM 1183 C CA . LEU A 1 195 ? 28.544 55.447 18.823 1.00 37.38 ? 188 LEU A CA 1 ATOM 1184 C C . LEU A 1 195 ? 27.962 56.323 17.727 1.00 38.65 ? 188 LEU A C 1 ATOM 1185 O O . LEU A 1 195 ? 28.464 56.322 16.600 1.00 39.35 ? 188 LEU A O 1 ATOM 1186 C CB . LEU A 1 195 ? 27.557 54.309 19.088 1.00 36.51 ? 188 LEU A CB 1 ATOM 1187 C CG . LEU A 1 195 ? 28.095 53.101 19.816 1.00 37.57 ? 188 LEU A CG 1 ATOM 1188 C CD1 . LEU A 1 195 ? 26.907 52.284 20.331 1.00 37.47 ? 188 LEU A CD1 1 ATOM 1189 C CD2 . LEU A 1 195 ? 28.972 52.275 18.891 1.00 38.66 ? 188 LEU A CD2 1 ATOM 1190 N N A GLU A 1 196 ? 26.880 57.049 18.029 0.70 38.50 ? 189 GLU A N 1 ATOM 1191 N N B GLU A 1 196 ? 26.936 57.093 18.070 0.30 37.89 ? 189 GLU A N 1 ATOM 1192 C CA A GLU A 1 196 ? 26.219 57.835 16.973 0.70 40.45 ? 189 GLU A CA 1 ATOM 1193 C CA B GLU A 1 196 ? 26.171 57.840 17.084 0.30 38.81 ? 189 GLU A CA 1 ATOM 1194 C C A GLU A 1 196 ? 26.899 59.154 16.658 0.70 40.57 ? 189 GLU A C 1 ATOM 1195 C C B GLU A 1 196 ? 26.847 59.146 16.691 0.30 39.59 ? 189 GLU A C 1 ATOM 1196 O O A GLU A 1 196 ? 27.024 59.516 15.480 0.70 42.08 ? 189 GLU A O 1 ATOM 1197 O O B GLU A 1 196 ? 26.912 59.486 15.506 0.30 40.83 ? 189 GLU A O 1 ATOM 1198 C CB A GLU A 1 196 ? 24.693 58.016 17.167 0.70 40.61 ? 189 GLU A CB 1 ATOM 1199 C CB B GLU A 1 196 ? 24.789 58.117 17.653 0.30 37.73 ? 189 GLU A CB 1 ATOM 1200 C CG A GLU A 1 196 ? 24.149 57.911 18.570 0.70 44.02 ? 189 GLU A CG 1 ATOM 1201 C CG B GLU A 1 196 ? 24.444 57.173 18.777 0.30 37.71 ? 189 GLU A CG 1 ATOM 1202 C CD A GLU A 1 196 ? 23.237 56.675 18.809 0.70 48.71 ? 189 GLU A CD 1 ATOM 1203 C CD B GLU A 1 196 ? 23.817 55.866 18.317 0.30 37.27 ? 189 GLU A CD 1 ATOM 1204 O OE1 A GLU A 1 196 ? 22.059 56.684 18.368 0.70 50.39 ? 189 GLU A OE1 1 ATOM 1205 O OE1 B GLU A 1 196 ? 22.980 55.332 19.080 0.30 35.83 ? 189 GLU A OE1 1 ATOM 1206 O OE2 A GLU A 1 196 ? 23.695 55.708 19.465 0.70 47.69 ? 189 GLU A OE2 1 ATOM 1207 O OE2 B GLU A 1 196 ? 24.144 55.369 17.219 0.30 37.30 ? 189 GLU A OE2 1 ATOM 1208 N N . ARG A 1 197 ? 27.351 59.868 17.690 1.00 39.58 ? 190 ARG A N 1 ATOM 1209 C CA . ARG A 1 197 ? 27.930 61.212 17.493 1.00 40.12 ? 190 ARG A CA 1 ATOM 1210 C C . ARG A 1 197 ? 29.381 61.187 17.024 1.00 41.33 ? 190 ARG A C 1 ATOM 1211 O O . ARG A 1 197 ? 29.747 61.945 16.118 1.00 42.77 ? 190 ARG A O 1 ATOM 1212 C CB . ARG A 1 197 ? 27.781 62.070 18.761 1.00 39.26 ? 190 ARG A CB 1 ATOM 1213 C CG . ARG A 1 197 ? 26.339 62.291 19.169 1.00 36.09 ? 190 ARG A CG 1 ATOM 1214 C CD . ARG A 1 197 ? 26.245 62.993 20.531 1.00 34.70 ? 190 ARG A CD 1 ATOM 1215 N NE . ARG A 1 197 ? 24.863 63.364 20.824 1.00 33.87 ? 190 ARG A NE 1 ATOM 1216 C CZ . ARG A 1 197 ? 24.494 64.141 21.844 1.00 33.39 ? 190 ARG A CZ 1 ATOM 1217 N NH1 . ARG A 1 197 ? 25.398 64.639 22.679 1.00 33.13 ? 190 ARG A NH1 1 ATOM 1218 N NH2 . ARG A 1 197 ? 23.217 64.415 22.020 1.00 33.33 ? 190 ARG A NH2 1 ATOM 1219 N N . ASP A 1 198 ? 30.203 60.332 17.640 1.00 41.43 ? 191 ASP A N 1 ATOM 1220 C CA . ASP A 1 198 ? 31.637 60.279 17.326 1.00 43.24 ? 191 ASP A CA 1 ATOM 1221 C C . ASP A 1 198 ? 31.987 59.224 16.284 1.00 43.22 ? 191 ASP A C 1 ATOM 1222 O O . ASP A 1 198 ? 32.720 59.517 15.328 1.00 44.03 ? 191 ASP A O 1 ATOM 1223 C CB . ASP A 1 198 ? 32.478 60.063 18.585 1.00 43.22 ? 191 ASP A CB 1 ATOM 1224 C CG . ASP A 1 198 ? 32.193 61.087 19.654 1.00 47.16 ? 191 ASP A CG 1 ATOM 1225 O OD1 . ASP A 1 198 ? 31.779 62.214 19.302 1.00 50.94 ? 191 ASP A OD1 1 ATOM 1226 O OD2 . ASP A 1 198 ? 32.378 60.764 20.849 1.00 50.70 ? 191 ASP A OD2 1 ATOM 1227 N N . MET A 1 199 ? 31.468 58.010 16.450 1.00 41.99 ? 192 MET A N 1 ATOM 1228 C CA . MET A 1 199 ? 31.826 56.907 15.548 1.00 42.76 ? 192 MET A CA 1 ATOM 1229 C C . MET A 1 199 ? 30.918 56.795 14.324 1.00 43.00 ? 192 MET A C 1 ATOM 1230 O O . MET A 1 199 ? 31.247 56.073 13.366 1.00 43.53 ? 192 MET A O 1 ATOM 1231 C CB . MET A 1 199 ? 31.842 55.573 16.303 1.00 42.10 ? 192 MET A CB 1 ATOM 1232 C CG . MET A 1 199 ? 32.806 55.518 17.467 1.00 42.71 ? 192 MET A CG 1 ATOM 1233 S SD . MET A 1 199 ? 32.828 53.883 18.242 1.00 44.32 ? 192 MET A SD 1 ATOM 1234 C CE . MET A 1 199 ? 33.922 52.986 17.108 1.00 44.90 ? 192 MET A CE 1 ATOM 1235 N N . LYS A 1 200 ? 29.796 57.511 14.355 1.00 42.45 ? 193 LYS A N 1 ATOM 1236 C CA . LYS A 1 200 ? 28.802 57.518 13.280 1.00 43.70 ? 193 LYS A CA 1 ATOM 1237 C C . LYS A 1 200 ? 28.290 56.114 12.968 1.00 44.08 ? 193 LYS A C 1 ATOM 1238 O O . LYS A 1 200 ? 28.094 55.749 11.807 1.00 45.28 ? 193 LYS A O 1 ATOM 1239 C CB . LYS A 1 200 ? 29.337 58.239 12.012 1.00 45.22 ? 193 LYS A CB 1 ATOM 1240 C CG . LYS A 1 200 ? 29.236 59.769 12.076 1.00 48.69 ? 193 LYS A CG 1 ATOM 1241 C CD . LYS A 1 200 ? 30.331 60.407 12.946 1.00 52.11 ? 193 LYS A CD 1 ATOM 1242 C CE . LYS A 1 200 ? 30.391 61.935 12.801 1.00 52.58 ? 193 LYS A CE 1 ATOM 1243 N NZ . LYS A 1 200 ? 29.195 62.660 13.330 1.00 52.68 ? 193 LYS A NZ 1 ATOM 1244 N N . ILE A 1 201 ? 28.075 55.317 14.015 1.00 43.05 ? 194 ILE A N 1 ATOM 1245 C CA . ILE A 1 201 ? 27.528 53.976 13.843 1.00 43.57 ? 194 ILE A CA 1 ATOM 1246 C C . ILE A 1 201 ? 26.037 54.033 14.135 1.00 42.97 ? 194 ILE A C 1 ATOM 1247 O O . ILE A 1 201 ? 25.621 54.597 15.138 1.00 42.09 ? 194 ILE A O 1 ATOM 1248 C CB . ILE A 1 201 ? 28.280 52.946 14.717 1.00 43.35 ? 194 ILE A CB 1 ATOM 1249 C CG1 . ILE A 1 201 ? 29.626 52.622 14.067 1.00 45.34 ? 194 ILE A CG1 1 ATOM 1250 C CG2 . ILE A 1 201 ? 27.469 51.650 14.888 1.00 43.24 ? 194 ILE A CG2 1 ATOM 1251 C CD1 . ILE A 1 201 ? 30.716 52.253 15.029 1.00 47.69 ? 194 ILE A CD1 1 ATOM 1252 N N . ASN A 1 202 ? 25.243 53.498 13.219 1.00 43.54 ? 195 ASN A N 1 ATOM 1253 C CA . ASN A 1 202 ? 23.797 53.545 13.314 1.00 43.76 ? 195 ASN A CA 1 ATOM 1254 C C . ASN A 1 202 ? 23.287 52.205 13.860 1.00 42.35 ? 195 ASN A C 1 ATOM 1255 O O . ASN A 1 202 ? 23.520 51.151 13.254 1.00 41.43 ? 195 ASN A O 1 ATOM 1256 C CB . ASN A 1 202 ? 23.207 53.877 11.930 1.00 45.64 ? 195 ASN A CB 1 ATOM 1257 C CG . ASN A 1 202 ? 21.693 54.119 11.959 1.00 49.36 ? 195 ASN A CG 1 ATOM 1258 O OD1 . ASN A 1 202 ? 21.031 53.917 12.983 1.00 48.34 ? 195 ASN A OD1 1 ATOM 1259 N ND2 . ASN A 1 202 ? 21.142 54.552 10.809 1.00 57.26 ? 195 ASN A ND2 1 ATOM 1260 N N . CYS A 1 203 ? 22.627 52.245 15.027 1.00 40.42 ? 196 CYS A N 1 ATOM 1261 C CA . CYS A 1 203 ? 22.071 51.028 15.633 1.00 39.62 ? 196 CYS A CA 1 ATOM 1262 C C . CYS A 1 203 ? 20.706 50.645 15.094 1.00 39.30 ? 196 CYS A C 1 ATOM 1263 O O . CYS A 1 203 ? 20.167 49.595 15.457 1.00 38.71 ? 196 CYS A O 1 ATOM 1264 C CB . CYS A 1 203 ? 21.983 51.151 17.162 1.00 38.56 ? 196 CYS A CB 1 ATOM 1265 S SG . CYS A 1 203 ? 23.562 51.171 17.951 1.00 39.48 ? 196 CYS A SG 1 ATOM 1266 N N . SER A 1 204 ? 20.138 51.484 14.236 1.00 39.71 ? 197 SER A N 1 ATOM 1267 C CA . SER A 1 204 ? 18.797 51.241 13.738 1.00 40.23 ? 197 SER A CA 1 ATOM 1268 C C . SER A 1 204 ? 18.669 49.898 13.017 1.00 40.56 ? 197 SER A C 1 ATOM 1269 O O . SER A 1 204 ? 19.400 49.616 12.057 1.00 42.03 ? 197 SER A O 1 ATOM 1270 C CB . SER A 1 204 ? 18.338 52.391 12.852 1.00 41.40 ? 197 SER A CB 1 ATOM 1271 O OG . SER A 1 204 ? 17.036 52.154 12.360 1.00 43.34 ? 197 SER A OG 1 ATOM 1272 N N . GLY A 1 205 ? 17.752 49.060 13.499 1.00 39.34 ? 198 GLY A N 1 ATOM 1273 C CA . GLY A 1 205 ? 17.522 47.753 12.884 1.00 38.41 ? 198 GLY A CA 1 ATOM 1274 C C . GLY A 1 205 ? 18.568 46.708 13.220 1.00 37.77 ? 198 GLY A C 1 ATOM 1275 O O . GLY A 1 205 ? 18.537 45.616 12.657 1.00 38.28 ? 198 GLY A O 1 ATOM 1276 N N . LYS A 1 206 ? 19.478 47.026 14.146 1.00 36.48 ? 199 LYS A N 1 ATOM 1277 C CA . LYS A 1 206 ? 20.550 46.106 14.554 1.00 35.94 ? 199 LYS A CA 1 ATOM 1278 C C . LYS A 1 206 ? 20.159 45.410 15.859 1.00 34.90 ? 199 LYS A C 1 ATOM 1279 O O . LYS A 1 206 ? 19.307 45.910 16.601 1.00 33.19 ? 199 LYS A O 1 ATOM 1280 C CB . LYS A 1 206 ? 21.871 46.857 14.769 1.00 35.74 ? 199 LYS A CB 1 ATOM 1281 C CG . LYS A 1 206 ? 22.426 47.592 13.537 1.00 39.60 ? 199 LYS A CG 1 ATOM 1282 C CD . LYS A 1 206 ? 22.858 46.619 12.454 1.00 42.59 ? 199 LYS A CD 1 ATOM 1283 C CE . LYS A 1 206 ? 23.472 47.352 11.254 1.00 47.37 ? 199 LYS A CE 1 ATOM 1284 N NZ . LYS A 1 206 ? 22.429 47.955 10.380 1.00 49.23 ? 199 LYS A NZ 1 ATOM 1285 N N . ILE A 1 207 ? 20.760 44.253 16.122 1.00 34.06 ? 200 ILE A N 1 ATOM 1286 C CA . ILE A 1 207 ? 20.673 43.652 17.462 1.00 33.44 ? 200 ILE A CA 1 ATOM 1287 C C . ILE A 1 207 ? 21.858 44.169 18.247 1.00 32.48 ? 200 ILE A C 1 ATOM 1288 O O . ILE A 1 207 ? 22.991 44.078 17.790 1.00 33.73 ? 200 ILE A O 1 ATOM 1289 C CB . ILE A 1 207 ? 20.674 42.122 17.410 1.00 34.08 ? 200 ILE A CB 1 ATOM 1290 C CG1 . ILE A 1 207 ? 19.364 41.648 16.774 1.00 35.19 ? 200 ILE A CG1 1 ATOM 1291 C CG2 . ILE A 1 207 ? 20.837 41.535 18.833 1.00 33.23 ? 200 ILE A CG2 1 ATOM 1292 C CD1 . ILE A 1 207 ? 19.337 40.174 16.406 1.00 36.31 ? 200 ILE A CD1 1 ATOM 1293 N N . VAL A 1 208 ? 21.608 44.733 19.420 1.00 30.81 ? 201 VAL A N 1 ATOM 1294 C CA . VAL A 1 208 ? 22.716 45.257 20.191 1.00 30.00 ? 201 VAL A CA 1 ATOM 1295 C C . VAL A 1 208 ? 23.161 44.245 21.243 1.00 29.42 ? 201 VAL A C 1 ATOM 1296 O O . VAL A 1 208 ? 22.339 43.553 21.824 1.00 28.97 ? 201 VAL A O 1 ATOM 1297 C CB . VAL A 1 208 ? 22.367 46.674 20.757 1.00 30.20 ? 201 VAL A CB 1 ATOM 1298 C CG1 A VAL A 1 208 ? 22.105 47.669 19.614 0.50 29.03 ? 201 VAL A CG1 1 ATOM 1299 C CG1 B VAL A 1 208 ? 22.505 46.792 22.287 0.50 29.52 ? 201 VAL A CG1 1 ATOM 1300 C CG2 A VAL A 1 208 ? 21.218 46.624 21.728 0.50 25.72 ? 201 VAL A CG2 1 ATOM 1301 C CG2 B VAL A 1 208 ? 23.060 47.768 19.969 0.50 30.95 ? 201 VAL A CG2 1 ATOM 1302 N N . ILE A 1 209 ? 24.467 44.141 21.450 1.00 28.57 ? 202 ILE A N 1 ATOM 1303 C CA . ILE A 1 209 ? 24.979 43.346 22.553 1.00 28.11 ? 202 ILE A CA 1 ATOM 1304 C C . ILE A 1 209 ? 25.704 44.258 23.536 1.00 28.47 ? 202 ILE A C 1 ATOM 1305 O O . ILE A 1 209 ? 26.575 45.059 23.143 1.00 28.87 ? 202 ILE A O 1 ATOM 1306 C CB . ILE A 1 209 ? 25.838 42.127 22.075 1.00 28.69 ? 202 ILE A CB 1 ATOM 1307 C CG1 . ILE A 1 209 ? 26.323 41.295 23.277 1.00 28.54 ? 202 ILE A CG1 1 ATOM 1308 C CG2 . ILE A 1 209 ? 26.991 42.586 21.131 1.00 29.38 ? 202 ILE A CG2 1 ATOM 1309 C CD1 . ILE A 1 209 ? 26.850 39.860 22.873 1.00 30.82 ? 202 ILE A CD1 1 ATOM 1310 N N . ALA A 1 210 ? 25.289 44.168 24.806 1.00 26.86 ? 203 ALA A N 1 ATOM 1311 C CA . ALA A 1 210 ? 25.793 45.051 25.843 1.00 26.43 ? 203 ALA A CA 1 ATOM 1312 C C . ALA A 1 210 ? 26.283 44.223 27.016 1.00 25.89 ? 203 ALA A C 1 ATOM 1313 O O . ALA A 1 210 ? 25.652 43.216 27.387 1.00 25.58 ? 203 ALA A O 1 ATOM 1314 C CB . ALA A 1 210 ? 24.664 45.988 26.304 1.00 25.11 ? 203 ALA A CB 1 ATOM 1315 N N . ARG A 1 211 ? 27.400 44.635 27.611 1.00 25.99 ? 204 ARG A N 1 ATOM 1316 C CA . ARG A 1 211 ? 27.784 44.022 28.877 1.00 25.20 ? 204 ARG A CA 1 ATOM 1317 C C . ARG A 1 211 ? 27.031 44.615 30.063 1.00 24.55 ? 204 ARG A C 1 ATOM 1318 O O . ARG A 1 211 ? 26.755 45.835 30.122 1.00 23.83 ? 204 ARG A O 1 ATOM 1319 C CB . ARG A 1 211 ? 29.297 44.025 29.105 1.00 27.40 ? 204 ARG A CB 1 ATOM 1320 C CG . ARG A 1 211 ? 29.972 45.343 28.864 1.00 28.86 ? 204 ARG A CG 1 ATOM 1321 C CD . ARG A 1 211 ? 31.380 45.226 29.356 1.00 30.99 ? 204 ARG A CD 1 ATOM 1322 N NE . ARG A 1 211 ? 32.184 46.388 28.970 1.00 29.45 ? 204 ARG A NE 1 ATOM 1323 C CZ . ARG A 1 211 ? 33.413 46.602 29.425 1.00 31.32 ? 204 ARG A CZ 1 ATOM 1324 N NH1 . ARG A 1 211 ? 33.948 45.759 30.297 1.00 29.93 ? 204 ARG A NH1 1 ATOM 1325 N NH2 . ARG A 1 211 ? 34.090 47.683 29.026 1.00 30.13 ? 204 ARG A NH2 1 ATOM 1326 N N . TYR A 1 212 ? 26.679 43.738 30.997 1.00 23.13 ? 205 TYR A N 1 ATOM 1327 C CA . TYR A 1 212 ? 26.070 44.168 32.238 1.00 22.86 ? 205 TYR A CA 1 ATOM 1328 C C . TYR A 1 212 ? 27.092 44.987 33.004 1.00 23.45 ? 205 TYR A C 1 ATOM 1329 O O . TYR A 1 212 ? 28.310 44.840 32.814 1.00 23.92 ? 205 TYR A O 1 ATOM 1330 C CB . TYR A 1 212 ? 25.741 42.935 33.048 1.00 22.63 ? 205 TYR A CB 1 ATOM 1331 C CG . TYR A 1 212 ? 24.383 42.298 32.877 1.00 22.34 ? 205 TYR A CG 1 ATOM 1332 C CD1 . TYR A 1 212 ? 24.268 40.917 32.648 1.00 22.17 ? 205 TYR A CD1 1 ATOM 1333 C CD2 . TYR A 1 212 ? 23.212 43.043 33.079 1.00 21.08 ? 205 TYR A CD2 1 ATOM 1334 C CE1 . TYR A 1 212 ? 23.013 40.304 32.596 1.00 21.73 ? 205 TYR A CE1 1 ATOM 1335 C CE2 . TYR A 1 212 ? 21.961 42.444 33.045 1.00 21.77 ? 205 TYR A CE2 1 ATOM 1336 C CZ . TYR A 1 212 ? 21.867 41.071 32.830 1.00 22.76 ? 205 TYR A CZ 1 ATOM 1337 O OH . TYR A 1 212 ? 20.629 40.495 32.825 1.00 22.24 ? 205 TYR A OH 1 ATOM 1338 N N . GLY A 1 213 ? 26.601 45.877 33.856 1.00 22.69 ? 206 GLY A N 1 ATOM 1339 C CA . GLY A 1 213 ? 27.472 46.634 34.755 1.00 23.77 ? 206 GLY A CA 1 ATOM 1340 C C . GLY A 1 213 ? 27.193 48.119 34.630 1.00 23.53 ? 206 GLY A C 1 ATOM 1341 O O . GLY A 1 213 ? 26.582 48.545 33.654 1.00 23.71 ? 206 GLY A O 1 ATOM 1342 N N . LYS A 1 214 ? 27.704 48.892 35.591 1.00 23.73 ? 207 LYS A N 1 ATOM 1343 C CA . LYS A 1 214 ? 27.671 50.385 35.585 1.00 23.63 ? 207 LYS A CA 1 ATOM 1344 C C . LYS A 1 214 ? 26.307 51.004 35.836 1.00 23.47 ? 207 LYS A C 1 ATOM 1345 O O . LYS A 1 214 ? 26.193 51.943 36.660 1.00 24.11 ? 207 LYS A O 1 ATOM 1346 C CB . LYS A 1 214 ? 28.248 51.004 34.309 1.00 24.56 ? 207 LYS A CB 1 ATOM 1347 C CG . LYS A 1 214 ? 29.679 50.556 33.983 1.00 27.02 ? 207 LYS A CG 1 ATOM 1348 C CD . LYS A 1 214 ? 30.649 50.947 35.075 1.00 31.76 ? 207 LYS A CD 1 ATOM 1349 C CE . LYS A 1 214 ? 32.078 50.535 34.678 1.00 35.62 ? 207 LYS A CE 1 ATOM 1350 N NZ . LYS A 1 214 ? 33.011 50.881 35.795 1.00 40.68 ? 207 LYS A NZ 1 ATOM 1351 N N . VAL A 1 215 ? 25.281 50.508 35.136 1.00 22.21 ? 208 VAL A N 1 ATOM 1352 C CA . VAL A 1 215 ? 23.920 51.073 35.258 1.00 21.76 ? 208 VAL A CA 1 ATOM 1353 C C . VAL A 1 215 ? 22.870 49.972 35.293 1.00 20.96 ? 208 VAL A C 1 ATOM 1354 O O . VAL A 1 215 ? 23.113 48.858 34.795 1.00 21.72 ? 208 VAL A O 1 ATOM 1355 C CB . VAL A 1 215 ? 23.558 52.119 34.112 1.00 21.14 ? 208 VAL A CB 1 ATOM 1356 C CG1 . VAL A 1 215 ? 24.614 53.280 34.050 1.00 23.05 ? 208 VAL A CG1 1 ATOM 1357 C CG2 . VAL A 1 215 ? 23.419 51.460 32.727 1.00 23.89 ? 208 VAL A CG2 1 ATOM 1358 N N . PHE A 1 216 ? 21.698 50.300 35.834 1.00 19.82 ? 209 PHE A N 1 ATOM 1359 C CA . PHE A 1 216 ? 20.529 49.391 35.790 1.00 19.06 ? 209 PHE A CA 1 ATOM 1360 C C . PHE A 1 216 ? 20.192 48.917 34.365 1.00 19.60 ? 209 PHE A C 1 ATOM 1361 O O . PHE A 1 216 ? 20.149 49.723 33.406 1.00 19.85 ? 209 PHE A O 1 ATOM 1362 C CB . PHE A 1 216 ? 19.332 50.116 36.427 1.00 18.69 ? 209 PHE A CB 1 ATOM 1363 C CG . PHE A 1 216 ? 18.044 49.358 36.320 1.00 18.95 ? 209 PHE A CG 1 ATOM 1364 C CD1 . PHE A 1 216 ? 17.928 48.099 36.930 1.00 19.03 ? 209 PHE A CD1 1 ATOM 1365 C CD2 . PHE A 1 216 ? 16.923 49.932 35.675 1.00 20.42 ? 209 PHE A CD2 1 ATOM 1366 C CE1 . PHE A 1 216 ? 16.705 47.371 36.857 1.00 21.04 ? 209 PHE A CE1 1 ATOM 1367 C CE2 . PHE A 1 216 ? 15.685 49.210 35.601 1.00 19.98 ? 209 PHE A CE2 1 ATOM 1368 C CZ . PHE A 1 216 ? 15.591 47.931 36.192 1.00 20.10 ? 209 PHE A CZ 1 ATOM 1369 N N . ARG A 1 217 ? 19.935 47.610 34.225 1.00 19.43 ? 210 ARG A N 1 ATOM 1370 C CA . ARG A 1 217 ? 19.740 47.015 32.881 1.00 19.99 ? 210 ARG A CA 1 ATOM 1371 C C . ARG A 1 217 ? 18.501 47.578 32.166 1.00 20.56 ? 210 ARG A C 1 ATOM 1372 O O . ARG A 1 217 ? 18.463 47.593 30.946 1.00 20.40 ? 210 ARG A O 1 ATOM 1373 C CB . ARG A 1 217 ? 19.672 45.487 32.964 1.00 20.06 ? 210 ARG A CB 1 ATOM 1374 C CG . ARG A 1 217 ? 18.445 44.989 33.756 1.00 18.93 ? 210 ARG A CG 1 ATOM 1375 C CD . ARG A 1 217 ? 18.454 43.439 33.901 1.00 19.29 ? 210 ARG A CD 1 ATOM 1376 N NE . ARG A 1 217 ? 19.224 43.017 35.093 1.00 18.34 ? 210 ARG A NE 1 ATOM 1377 C CZ . ARG A 1 217 ? 18.819 43.227 36.360 1.00 20.67 ? 210 ARG A CZ 1 ATOM 1378 N NH1 . ARG A 1 217 ? 17.658 43.815 36.608 1.00 18.59 ? 210 ARG A NH1 1 ATOM 1379 N NH2 . ARG A 1 217 ? 19.573 42.816 37.385 1.00 19.31 ? 210 ARG A NH2 1 ATOM 1380 N N . GLY A 1 218 ? 17.500 48.054 32.917 1.00 19.33 ? 211 GLY A N 1 ATOM 1381 C CA . GLY A 1 218 ? 16.346 48.696 32.287 1.00 20.46 ? 211 GLY A CA 1 ATOM 1382 C C . GLY A 1 218 ? 16.757 49.966 31.542 1.00 19.80 ? 211 GLY A C 1 ATOM 1383 O O . GLY A 1 218 ? 16.227 50.244 30.463 1.00 20.03 ? 211 GLY A O 1 ATOM 1384 N N . ASN A 1 219 ? 17.697 50.736 32.102 1.00 20.17 ? 212 ASN A N 1 ATOM 1385 C CA . ASN A 1 219 ? 18.201 51.903 31.379 1.00 21.04 ? 212 ASN A CA 1 ATOM 1386 C C . ASN A 1 219 ? 18.941 51.536 30.103 1.00 22.32 ? 212 ASN A C 1 ATOM 1387 O O . ASN A 1 219 ? 18.776 52.209 29.078 1.00 23.19 ? 212 ASN A O 1 ATOM 1388 C CB . ASN A 1 219 ? 19.094 52.774 32.264 1.00 20.91 ? 212 ASN A CB 1 ATOM 1389 C CG . ASN A 1 219 ? 18.320 53.425 33.388 1.00 22.00 ? 212 ASN A CG 1 ATOM 1390 O OD1 . ASN A 1 219 ? 18.208 52.866 34.488 1.00 22.47 ? 212 ASN A OD1 1 ATOM 1391 N ND2 . ASN A 1 219 ? 17.715 54.578 33.105 1.00 20.30 ? 212 ASN A ND2 1 ATOM 1392 N N . LYS A 1 220 ? 19.715 50.447 30.153 1.00 21.60 ? 213 LYS A N 1 ATOM 1393 C CA . LYS A 1 220 ? 20.382 49.936 28.938 1.00 22.09 ? 213 LYS A CA 1 ATOM 1394 C C . LYS A 1 220 ? 19.360 49.653 27.834 1.00 22.52 ? 213 LYS A C 1 ATOM 1395 O O . LYS A 1 220 ? 19.600 49.993 26.644 1.00 21.87 ? 213 LYS A O 1 ATOM 1396 C CB . LYS A 1 220 ? 21.144 48.636 29.245 1.00 21.84 ? 213 LYS A CB 1 ATOM 1397 C CG . LYS A 1 220 ? 22.266 48.736 30.318 1.00 21.96 ? 213 LYS A CG 1 ATOM 1398 C CD . LYS A 1 220 ? 22.890 47.358 30.559 1.00 22.16 ? 213 LYS A CD 1 ATOM 1399 C CE . LYS A 1 220 ? 23.862 47.322 31.730 1.00 23.10 ? 213 LYS A CE 1 ATOM 1400 N NZ . LYS A 1 220 ? 25.252 47.752 31.334 1.00 23.32 ? 213 LYS A NZ 1 ATOM 1401 N N . VAL A 1 221 ? 18.266 48.985 28.205 1.00 21.02 ? 214 VAL A N 1 ATOM 1402 C CA . VAL A 1 221 ? 17.259 48.593 27.236 1.00 22.26 ? 214 VAL A CA 1 ATOM 1403 C C . VAL A 1 221 ? 16.550 49.845 26.668 1.00 22.97 ? 214 VAL A C 1 ATOM 1404 O O . VAL A 1 221 ? 16.333 49.939 25.447 1.00 23.27 ? 214 VAL A O 1 ATOM 1405 C CB . VAL A 1 221 ? 16.246 47.563 27.816 1.00 22.07 ? 214 VAL A CB 1 ATOM 1406 C CG1 . VAL A 1 221 ? 15.068 47.325 26.828 1.00 23.26 ? 214 VAL A CG1 1 ATOM 1407 C CG2 . VAL A 1 221 ? 16.947 46.222 28.160 1.00 22.28 ? 214 VAL A CG2 1 ATOM 1408 N N A LYS A 1 222 ? 16.197 50.790 27.538 0.50 22.00 ? 215 LYS A N 1 ATOM 1409 N N B LYS A 1 222 ? 16.205 50.784 27.552 0.50 22.17 ? 215 LYS A N 1 ATOM 1410 C CA A LYS A 1 222 ? 15.592 52.040 27.075 0.50 22.76 ? 215 LYS A CA 1 ATOM 1411 C CA B LYS A 1 222 ? 15.618 52.068 27.146 0.50 23.15 ? 215 LYS A CA 1 ATOM 1412 C C A LYS A 1 222 ? 16.535 52.750 26.098 0.50 23.75 ? 215 LYS A C 1 ATOM 1413 C C B LYS A 1 222 ? 16.528 52.759 26.130 0.50 23.93 ? 215 LYS A C 1 ATOM 1414 O O A LYS A 1 222 ? 16.099 53.228 25.037 0.50 24.31 ? 215 LYS A O 1 ATOM 1415 O O B LYS A 1 222 ? 16.067 53.223 25.074 0.50 24.55 ? 215 LYS A O 1 ATOM 1416 C CB A LYS A 1 222 ? 15.257 52.959 28.250 0.50 21.79 ? 215 LYS A CB 1 ATOM 1417 C CB B LYS A 1 222 ? 15.411 52.974 28.370 0.50 22.20 ? 215 LYS A CB 1 ATOM 1418 C CG A LYS A 1 222 ? 14.730 54.334 27.818 0.50 23.26 ? 215 LYS A CG 1 ATOM 1419 C CG B LYS A 1 222 ? 14.791 54.345 28.051 0.50 24.96 ? 215 LYS A CG 1 ATOM 1420 C CD A LYS A 1 222 ? 14.583 55.268 29.025 0.50 25.26 ? 215 LYS A CD 1 ATOM 1421 C CD B LYS A 1 222 ? 14.345 55.087 29.333 0.50 26.51 ? 215 LYS A CD 1 ATOM 1422 C CE A LYS A 1 222 ? 14.270 56.697 28.598 0.50 24.95 ? 215 LYS A CE 1 ATOM 1423 C CE B LYS A 1 222 ? 15.536 55.716 30.062 0.50 29.97 ? 215 LYS A CE 1 ATOM 1424 N NZ A LYS A 1 222 ? 13.974 57.557 29.792 0.50 30.98 ? 215 LYS A NZ 1 ATOM 1425 N NZ B LYS A 1 222 ? 15.240 56.725 31.163 0.50 32.94 ? 215 LYS A NZ 1 ATOM 1426 N N . ASN A 1 223 ? 17.823 52.803 26.445 1.00 23.75 ? 216 ASN A N 1 ATOM 1427 C CA . ASN A 1 223 ? 18.827 53.455 25.585 1.00 24.05 ? 216 ASN A CA 1 ATOM 1428 C C . ASN A 1 223 ? 18.937 52.748 24.237 1.00 24.21 ? 216 ASN A C 1 ATOM 1429 O O . ASN A 1 223 ? 19.002 53.409 23.187 1.00 25.42 ? 216 ASN A O 1 ATOM 1430 C CB . ASN A 1 223 ? 20.192 53.505 26.283 1.00 23.06 ? 216 ASN A CB 1 ATOM 1431 C CG . ASN A 1 223 ? 20.173 54.359 27.539 1.00 24.59 ? 216 ASN A CG 1 ATOM 1432 O OD1 . ASN A 1 223 ? 19.231 55.140 27.758 1.00 24.50 ? 216 ASN A OD1 1 ATOM 1433 N ND2 . ASN A 1 223 ? 21.221 54.245 28.361 1.00 22.74 ? 216 ASN A ND2 1 ATOM 1434 N N . ALA A 1 224 ? 18.899 51.418 24.260 1.00 24.48 ? 217 ALA A N 1 ATOM 1435 C CA . ALA A 1 224 ? 19.010 50.644 23.002 1.00 25.50 ? 217 ALA A CA 1 ATOM 1436 C C . ALA A 1 224 ? 17.757 50.874 22.139 1.00 26.71 ? 217 ALA A C 1 ATOM 1437 O O . ALA A 1 224 ? 17.849 51.002 20.916 1.00 28.33 ? 217 ALA A O 1 ATOM 1438 C CB . ALA A 1 224 ? 19.194 49.146 23.298 1.00 25.23 ? 217 ALA A CB 1 ATOM 1439 N N . GLN A 1 225 ? 16.587 50.904 22.776 1.00 27.04 ? 218 GLN A N 1 ATOM 1440 C CA . GLN A 1 225 ? 15.329 51.166 22.051 1.00 29.21 ? 218 GLN A CA 1 ATOM 1441 C C . GLN A 1 225 ? 15.360 52.497 21.348 1.00 31.05 ? 218 GLN A C 1 ATOM 1442 O O . GLN A 1 225 ? 14.951 52.604 20.185 1.00 31.20 ? 218 GLN A O 1 ATOM 1443 C CB . GLN A 1 225 ? 14.145 51.195 23.010 1.00 29.52 ? 218 GLN A CB 1 ATOM 1444 C CG . GLN A 1 225 ? 13.671 49.875 23.292 1.00 31.70 ? 218 GLN A CG 1 ATOM 1445 C CD . GLN A 1 225 ? 12.404 49.870 24.154 1.00 34.94 ? 218 GLN A CD 1 ATOM 1446 O OE1 . GLN A 1 225 ? 12.179 48.908 24.843 1.00 35.15 ? 218 GLN A OE1 1 ATOM 1447 N NE2 . GLN A 1 225 ? 11.563 50.912 24.050 1.00 37.34 ? 218 GLN A NE2 1 ATOM 1448 N N . LEU A 1 226 ? 15.815 53.524 22.069 1.00 31.16 ? 219 LEU A N 1 ATOM 1449 C CA . LEU A 1 226 ? 15.849 54.871 21.519 1.00 32.59 ? 219 LEU A CA 1 ATOM 1450 C C . LEU A 1 226 ? 16.864 55.020 20.392 1.00 33.37 ? 219 LEU A C 1 ATOM 1451 O O . LEU A 1 226 ? 16.687 55.875 19.501 1.00 33.81 ? 219 LEU A O 1 ATOM 1452 C CB . LEU A 1 226 ? 16.028 55.922 22.626 1.00 32.67 ? 219 LEU A CB 1 ATOM 1453 C CG . LEU A 1 226 ? 14.802 56.034 23.561 1.00 36.40 ? 219 LEU A CG 1 ATOM 1454 C CD1 . LEU A 1 226 ? 15.073 56.989 24.710 1.00 38.82 ? 219 LEU A CD1 1 ATOM 1455 C CD2 . LEU A 1 226 ? 13.513 56.431 22.833 1.00 41.09 ? 219 LEU A CD2 1 ATOM 1456 N N . ALA A 1 227 ? 17.889 54.157 20.389 1.00 32.14 ? 220 ALA A N 1 ATOM 1457 C CA . ALA A 1 227 ? 18.861 54.094 19.304 1.00 32.46 ? 220 ALA A CA 1 ATOM 1458 C C . ALA A 1 227 ? 18.327 53.305 18.105 1.00 32.60 ? 220 ALA A C 1 ATOM 1459 O O . ALA A 1 227 ? 19.010 53.194 17.084 1.00 34.19 ? 220 ALA A O 1 ATOM 1460 C CB . ALA A 1 227 ? 20.149 53.466 19.810 1.00 31.78 ? 220 ALA A CB 1 ATOM 1461 N N . GLY A 1 228 ? 17.130 52.739 18.231 1.00 31.51 ? 221 GLY A N 1 ATOM 1462 C CA . GLY A 1 228 ? 16.509 52.013 17.122 1.00 31.15 ? 221 GLY A CA 1 ATOM 1463 C C . GLY A 1 228 ? 16.880 50.543 17.026 1.00 31.39 ? 221 GLY A C 1 ATOM 1464 O O . GLY A 1 228 ? 16.585 49.905 16.014 1.00 32.05 ? 221 GLY A O 1 ATOM 1465 N N . ALA A 1 229 ? 17.492 49.981 18.077 1.00 30.68 ? 222 ALA A N 1 ATOM 1466 C CA . ALA A 1 229 ? 17.822 48.541 18.106 1.00 30.66 ? 222 ALA A CA 1 ATOM 1467 C C . ALA A 1 229 ? 16.560 47.700 17.934 1.00 30.65 ? 222 ALA A C 1 ATOM 1468 O O . ALA A 1 229 ? 15.464 48.124 18.357 1.00 29.50 ? 222 ALA A O 1 ATOM 1469 C CB . ALA A 1 229 ? 18.519 48.177 19.423 1.00 30.32 ? 222 ALA A CB 1 ATOM 1470 N N . LYS A 1 230 ? 16.694 46.522 17.315 1.00 30.42 ? 223 LYS A N 1 ATOM 1471 C CA . LYS A 1 230 ? 15.552 45.616 17.256 1.00 30.73 ? 223 LYS A CA 1 ATOM 1472 C C . LYS A 1 230 ? 15.609 44.467 18.279 1.00 29.96 ? 223 LYS A C 1 ATOM 1473 O O . LYS A 1 230 ? 14.682 43.648 18.364 1.00 29.81 ? 223 LYS A O 1 ATOM 1474 C CB . LYS A 1 230 ? 15.283 45.131 15.818 1.00 32.95 ? 223 LYS A CB 1 ATOM 1475 C CG . LYS A 1 230 ? 16.233 44.118 15.269 1.00 34.23 ? 223 LYS A CG 1 ATOM 1476 C CD . LYS A 1 230 ? 15.690 43.635 13.906 1.00 37.00 ? 223 LYS A CD 1 ATOM 1477 C CE . LYS A 1 230 ? 16.743 42.982 13.124 1.00 40.40 ? 223 LYS A CE 1 ATOM 1478 N NZ . LYS A 1 230 ? 16.236 42.681 11.723 1.00 40.63 ? 223 LYS A NZ 1 ATOM 1479 N N . GLY A 1 231 ? 16.673 44.445 19.078 1.00 28.74 ? 224 GLY A N 1 ATOM 1480 C CA . GLY A 1 231 ? 16.813 43.435 20.120 1.00 28.66 ? 224 GLY A CA 1 ATOM 1481 C C . GLY A 1 231 ? 18.027 43.756 20.951 1.00 27.58 ? 224 GLY A C 1 ATOM 1482 O O . GLY A 1 231 ? 18.910 44.493 20.491 1.00 27.94 ? 224 GLY A O 1 ATOM 1483 N N . VAL A 1 232 ? 18.060 43.235 22.179 1.00 26.57 ? 225 VAL A N 1 ATOM 1484 C CA . VAL A 1 232 ? 19.192 43.446 23.060 1.00 25.84 ? 225 VAL A CA 1 ATOM 1485 C C . VAL A 1 232 ? 19.639 42.119 23.663 1.00 25.97 ? 225 VAL A C 1 ATOM 1486 O O . VAL A 1 232 ? 18.827 41.361 24.217 1.00 25.23 ? 225 VAL A O 1 ATOM 1487 C CB . VAL A 1 232 ? 18.844 44.387 24.235 1.00 25.83 ? 225 VAL A CB 1 ATOM 1488 C CG1 . VAL A 1 232 ? 20.095 44.635 25.106 1.00 26.02 ? 225 VAL A CG1 1 ATOM 1489 C CG2 . VAL A 1 232 ? 18.285 45.724 23.689 1.00 25.64 ? 225 VAL A CG2 1 ATOM 1490 N N . ILE A 1 233 ? 20.933 41.867 23.581 1.00 25.38 ? 226 ILE A N 1 ATOM 1491 C CA . ILE A 1 233 ? 21.543 40.734 24.264 1.00 25.29 ? 226 ILE A CA 1 ATOM 1492 C C . ILE A 1 233 ? 22.413 41.297 25.398 1.00 25.46 ? 226 ILE A C 1 ATOM 1493 O O . ILE A 1 233 ? 23.272 42.132 25.138 1.00 27.03 ? 226 ILE A O 1 ATOM 1494 C CB . ILE A 1 233 ? 22.393 39.892 23.274 1.00 26.10 ? 226 ILE A CB 1 ATOM 1495 C CG1 . ILE A 1 233 ? 21.508 39.363 22.138 1.00 25.90 ? 226 ILE A CG1 1 ATOM 1496 C CG2 . ILE A 1 233 ? 23.157 38.776 24.042 1.00 26.34 ? 226 ILE A CG2 1 ATOM 1497 C CD1 . ILE A 1 233 ? 22.349 38.861 20.933 1.00 26.18 ? 226 ILE A CD1 1 ATOM 1498 N N . LEU A 1 234 ? 22.162 40.865 26.640 1.00 23.97 ? 227 LEU A N 1 ATOM 1499 C CA . LEU A 1 234 ? 22.920 41.314 27.825 1.00 23.90 ? 227 LEU A CA 1 ATOM 1500 C C . LEU A 1 234 ? 23.834 40.170 28.225 1.00 24.45 ? 227 LEU A C 1 ATOM 1501 O O . LEU A 1 234 ? 23.421 39.007 28.152 1.00 25.84 ? 227 LEU A O 1 ATOM 1502 C CB . LEU A 1 234 ? 21.962 41.634 28.989 1.00 22.38 ? 227 LEU A CB 1 ATOM 1503 C CG . LEU A 1 234 ? 20.957 42.778 28.735 1.00 23.92 ? 227 LEU A CG 1 ATOM 1504 C CD1 . LEU A 1 234 ? 19.849 42.806 29.847 1.00 23.44 ? 227 LEU A CD1 1 ATOM 1505 C CD2 . LEU A 1 234 ? 21.711 44.116 28.665 1.00 25.91 ? 227 LEU A CD2 1 ATOM 1506 N N . TYR A 1 235 ? 25.076 40.467 28.604 1.00 24.04 ? 228 TYR A N 1 ATOM 1507 C CA . TYR A 1 235 ? 25.964 39.378 29.038 1.00 24.32 ? 228 TYR A CA 1 ATOM 1508 C C . TYR A 1 235 ? 26.869 39.842 30.159 1.00 24.24 ? 228 TYR A C 1 ATOM 1509 O O . TYR A 1 235 ? 27.109 41.055 30.315 1.00 24.15 ? 228 TYR A O 1 ATOM 1510 C CB . TYR A 1 235 ? 26.806 38.782 27.854 1.00 24.99 ? 228 TYR A CB 1 ATOM 1511 C CG . TYR A 1 235 ? 28.039 39.604 27.540 1.00 25.04 ? 228 TYR A CG 1 ATOM 1512 C CD1 . TYR A 1 235 ? 29.295 39.250 28.069 1.00 25.19 ? 228 TYR A CD1 1 ATOM 1513 C CD2 . TYR A 1 235 ? 27.956 40.745 26.727 1.00 24.60 ? 228 TYR A CD2 1 ATOM 1514 C CE1 . TYR A 1 235 ? 30.441 40.030 27.796 1.00 26.31 ? 228 TYR A CE1 1 ATOM 1515 C CE2 . TYR A 1 235 ? 29.078 41.529 26.452 1.00 25.00 ? 228 TYR A CE2 1 ATOM 1516 C CZ . TYR A 1 235 ? 30.306 41.171 27.001 1.00 26.35 ? 228 TYR A CZ 1 ATOM 1517 O OH . TYR A 1 235 ? 31.392 41.956 26.769 1.00 27.76 ? 228 TYR A OH 1 ATOM 1518 N N . SER A 1 236 ? 27.384 38.882 30.929 1.00 24.18 ? 229 SER A N 1 ATOM 1519 C CA . SER A 1 236 ? 28.289 39.187 32.036 1.00 23.88 ? 229 SER A CA 1 ATOM 1520 C C . SER A 1 236 ? 29.735 39.038 31.601 1.00 24.72 ? 229 SER A C 1 ATOM 1521 O O . SER A 1 236 ? 30.167 37.928 31.302 1.00 25.45 ? 229 SER A O 1 ATOM 1522 C CB . SER A 1 236 ? 27.999 38.242 33.212 1.00 24.03 ? 229 SER A CB 1 ATOM 1523 O OG . SER A 1 236 ? 26.662 38.456 33.676 1.00 25.52 ? 229 SER A OG 1 ATOM 1524 N N . ASP A 1 237 ? 30.482 40.137 31.551 1.00 24.89 ? 230 ASP A N 1 ATOM 1525 C CA . ASP A 1 237 ? 31.879 40.066 31.092 1.00 27.06 ? 230 ASP A CA 1 ATOM 1526 C C . ASP A 1 237 ? 32.730 39.749 32.319 1.00 27.51 ? 230 ASP A C 1 ATOM 1527 O O . ASP A 1 237 ? 32.487 40.316 33.383 1.00 27.57 ? 230 ASP A O 1 ATOM 1528 C CB . ASP A 1 237 ? 32.310 41.399 30.435 1.00 26.82 ? 230 ASP A CB 1 ATOM 1529 C CG . ASP A 1 237 ? 33.599 41.264 29.625 1.00 29.56 ? 230 ASP A CG 1 ATOM 1530 O OD1 . ASP A 1 237 ? 33.542 41.288 28.386 1.00 30.53 ? 230 ASP A OD1 1 ATOM 1531 O OD2 . ASP A 1 237 ? 34.660 41.076 30.231 1.00 29.54 ? 230 ASP A OD2 1 ATOM 1532 N N . PRO A 1 238 ? 33.739 38.856 32.187 1.00 29.34 ? 231 PRO A N 1 ATOM 1533 C CA . PRO A 1 238 ? 34.610 38.581 33.338 1.00 30.06 ? 231 PRO A CA 1 ATOM 1534 C C . PRO A 1 238 ? 35.297 39.848 33.880 1.00 31.31 ? 231 PRO A C 1 ATOM 1535 O O . PRO A 1 238 ? 35.610 39.917 35.071 1.00 30.88 ? 231 PRO A O 1 ATOM 1536 C CB . PRO A 1 238 ? 35.662 37.608 32.772 1.00 31.69 ? 231 PRO A CB 1 ATOM 1537 C CG . PRO A 1 238 ? 35.003 36.966 31.633 1.00 32.05 ? 231 PRO A CG 1 ATOM 1538 C CD . PRO A 1 238 ? 34.042 37.975 31.037 1.00 29.28 ? 231 PRO A CD 1 ATOM 1539 N N . ALA A 1 239 ? 35.483 40.864 33.037 1.00 31.07 ? 232 ALA A N 1 ATOM 1540 C CA . ALA A 1 239 ? 36.009 42.153 33.534 1.00 32.24 ? 232 ALA A CA 1 ATOM 1541 C C . ALA A 1 239 ? 35.197 42.725 34.705 1.00 31.88 ? 232 ALA A C 1 ATOM 1542 O O . ALA A 1 239 ? 35.743 43.333 35.637 1.00 32.82 ? 232 ALA A O 1 ATOM 1543 C CB . ALA A 1 239 ? 36.089 43.172 32.392 1.00 33.01 ? 232 ALA A CB 1 ATOM 1544 N N . ASP A 1 240 ? 33.887 42.501 34.664 1.00 30.32 ? 233 ASP A N 1 ATOM 1545 C CA . ASP A 1 240 ? 32.950 43.077 35.613 1.00 29.42 ? 233 ASP A CA 1 ATOM 1546 C C . ASP A 1 240 ? 32.425 42.051 36.621 1.00 28.91 ? 233 ASP A C 1 ATOM 1547 O O . ASP A 1 240 ? 31.806 42.439 37.622 0.80 28.61 ? 233 ASP A O 1 ATOM 1548 C CB . ASP A 1 240 ? 31.775 43.687 34.825 1.00 28.70 ? 233 ASP A CB 1 ATOM 1549 C CG . ASP A 1 240 ? 32.245 44.660 33.749 1.00 29.10 ? 233 ASP A CG 1 ATOM 1550 O OD1 . ASP A 1 240 ? 32.695 45.773 34.120 1.00 30.46 ? 233 ASP A OD1 1 ATOM 1551 O OD2 . ASP A 1 240 ? 32.208 44.300 32.553 1.00 28.82 ? 233 ASP A OD2 1 ATOM 1552 N N . TYR A 1 241 ? 32.634 40.755 36.359 1.00 28.34 ? 234 TYR A N 1 ATOM 1553 C CA . TYR A 1 241 ? 32.044 39.688 37.209 1.00 28.16 ? 234 TYR A CA 1 ATOM 1554 C C . TYR A 1 241 ? 33.003 38.556 37.584 1.00 29.42 ? 234 TYR A C 1 ATOM 1555 O O . TYR A 1 241 ? 32.570 37.496 38.047 1.00 28.92 ? 234 TYR A O 1 ATOM 1556 C CB . TYR A 1 241 ? 30.764 39.114 36.562 1.00 27.98 ? 234 TYR A CB 1 ATOM 1557 C CG . TYR A 1 241 ? 29.686 40.173 36.508 1.00 27.53 ? 234 TYR A CG 1 ATOM 1558 C CD1 . TYR A 1 241 ? 29.483 40.927 35.346 1.00 27.36 ? 234 TYR A CD1 1 ATOM 1559 C CD2 . TYR A 1 241 ? 28.922 40.471 37.636 1.00 26.14 ? 234 TYR A CD2 1 ATOM 1560 C CE1 . TYR A 1 241 ? 28.538 41.967 35.308 1.00 26.27 ? 234 TYR A CE1 1 ATOM 1561 C CE2 . TYR A 1 241 ? 27.964 41.490 37.612 1.00 27.00 ? 234 TYR A CE2 1 ATOM 1562 C CZ . TYR A 1 241 ? 27.777 42.231 36.440 1.00 27.69 ? 234 TYR A CZ 1 ATOM 1563 O OH . TYR A 1 241 ? 26.842 43.234 36.414 1.00 26.14 ? 234 TYR A OH 1 ATOM 1564 N N . PHE A 1 242 ? 34.303 38.783 37.409 1.00 29.71 ? 235 PHE A N 1 ATOM 1565 C CA . PHE A 1 242 ? 35.270 37.752 37.766 1.00 31.07 ? 235 PHE A CA 1 ATOM 1566 C C . PHE A 1 242 ? 36.470 38.447 38.385 1.00 32.05 ? 235 PHE A C 1 ATOM 1567 O O . PHE A 1 242 ? 37.280 39.042 37.668 1.00 32.47 ? 235 PHE A O 1 ATOM 1568 C CB . PHE A 1 242 ? 35.676 36.954 36.538 1.00 31.65 ? 235 PHE A CB 1 ATOM 1569 C CG . PHE A 1 242 ? 36.445 35.695 36.854 1.00 31.74 ? 235 PHE A CG 1 ATOM 1570 C CD1 . PHE A 1 242 ? 35.787 34.474 36.950 1.00 32.12 ? 235 PHE A CD1 1 ATOM 1571 C CD2 . PHE A 1 242 ? 37.831 35.741 37.064 1.00 34.02 ? 235 PHE A CD2 1 ATOM 1572 C CE1 . PHE A 1 242 ? 36.494 33.301 37.235 1.00 33.90 ? 235 PHE A CE1 1 ATOM 1573 C CE2 . PHE A 1 242 ? 38.546 34.565 37.351 1.00 34.73 ? 235 PHE A CE2 1 ATOM 1574 C CZ . PHE A 1 242 ? 37.870 33.348 37.445 1.00 35.78 ? 235 PHE A CZ 1 ATOM 1575 N N . ALA A 1 243 ? 36.534 38.413 39.712 1.00 32.01 ? 236 ALA A N 1 ATOM 1576 C CA . ALA A 1 243 ? 37.655 38.989 40.437 1.00 34.34 ? 236 ALA A CA 1 ATOM 1577 C C . ALA A 1 243 ? 38.922 38.165 40.202 1.00 36.25 ? 236 ALA A C 1 ATOM 1578 O O . ALA A 1 243 ? 38.913 36.956 40.399 1.00 35.20 ? 236 ALA A O 1 ATOM 1579 C CB . ALA A 1 243 ? 37.334 39.052 41.916 1.00 34.09 ? 236 ALA A CB 1 ATOM 1580 N N . PRO A 1 244 ? 40.020 38.825 39.778 1.00 38.54 ? 237 PRO A N 1 ATOM 1581 C CA . PRO A 1 244 ? 41.300 38.131 39.589 1.00 40.02 ? 237 PRO A CA 1 ATOM 1582 C C . PRO A 1 244 ? 41.713 37.341 40.845 1.00 39.83 ? 237 PRO A C 1 ATOM 1583 O O . PRO A 1 244 ? 41.555 37.833 41.970 1.00 40.04 ? 237 PRO A O 1 ATOM 1584 C CB . PRO A 1 244 ? 42.286 39.278 39.309 1.00 40.93 ? 237 PRO A CB 1 ATOM 1585 C CG . PRO A 1 244 ? 41.425 40.381 38.733 1.00 41.53 ? 237 PRO A CG 1 ATOM 1586 C CD . PRO A 1 244 ? 40.107 40.268 39.461 1.00 38.88 ? 237 PRO A CD 1 ATOM 1587 N N . GLY A 1 245 ? 42.173 36.108 40.641 1.00 40.59 ? 238 GLY A N 1 ATOM 1588 C CA . GLY A 1 245 ? 42.726 35.293 41.721 1.00 40.21 ? 238 GLY A CA 1 ATOM 1589 C C . GLY A 1 245 ? 41.742 34.544 42.607 1.00 39.71 ? 238 GLY A C 1 ATOM 1590 O O . GLY A 1 245 ? 42.168 33.878 43.569 1.00 40.88 ? 238 GLY A O 1 ATOM 1591 N N . VAL A 1 246 ? 40.440 34.623 42.292 1.00 36.35 ? 239 VAL A N 1 ATOM 1592 C CA . VAL A 1 246 ? 39.419 33.865 43.011 1.00 34.67 ? 239 VAL A CA 1 ATOM 1593 C C . VAL A 1 246 ? 38.807 32.847 42.051 1.00 34.23 ? 239 VAL A C 1 ATOM 1594 O O . VAL A 1 246 ? 38.725 33.082 40.845 1.00 34.78 ? 239 VAL A O 1 ATOM 1595 C CB . VAL A 1 246 ? 38.360 34.807 43.767 1.00 33.76 ? 239 VAL A CB 1 ATOM 1596 C CG1 A VAL A 1 246 ? 38.702 36.275 43.594 0.50 34.54 ? 239 VAL A CG1 1 ATOM 1597 C CG1 B VAL A 1 246 ? 37.225 33.992 44.397 0.50 31.40 ? 239 VAL A CG1 1 ATOM 1598 C CG2 A VAL A 1 246 ? 36.918 34.466 43.471 0.50 32.74 ? 239 VAL A CG2 1 ATOM 1599 C CG2 B VAL A 1 246 ? 39.047 35.698 44.795 0.50 32.93 ? 239 VAL A CG2 1 ATOM 1600 N N A LYS A 1 247 ? 38.434 31.689 42.577 0.70 34.34 ? 240 LYS A N 1 ATOM 1601 N N B LYS A 1 247 ? 38.380 31.731 42.623 0.30 34.29 ? 240 LYS A N 1 ATOM 1602 C CA A LYS A 1 247 ? 37.875 30.631 41.740 0.70 34.52 ? 240 LYS A CA 1 ATOM 1603 C CA B LYS A 1 247 ? 37.799 30.616 41.895 0.30 34.34 ? 240 LYS A CA 1 ATOM 1604 C C A LYS A 1 247 ? 36.369 30.790 41.548 0.70 34.23 ? 240 LYS A C 1 ATOM 1605 C C B LYS A 1 247 ? 36.335 30.871 41.522 0.30 33.91 ? 240 LYS A C 1 ATOM 1606 O O A LYS A 1 247 ? 35.704 31.387 42.389 0.70 33.19 ? 240 LYS A O 1 ATOM 1607 O O B LYS A 1 247 ? 35.656 31.634 42.202 0.30 33.37 ? 240 LYS A O 1 ATOM 1608 C CB A LYS A 1 247 ? 38.183 29.256 42.336 0.70 36.22 ? 240 LYS A CB 1 ATOM 1609 C CB B LYS A 1 247 ? 37.900 29.377 42.780 0.30 34.72 ? 240 LYS A CB 1 ATOM 1610 C CG A LYS A 1 247 ? 39.666 28.886 42.343 0.70 35.74 ? 240 LYS A CG 1 ATOM 1611 C CG B LYS A 1 247 ? 37.864 29.686 44.280 0.30 34.42 ? 240 LYS A CG 1 ATOM 1612 C CD A LYS A 1 247 ? 40.225 28.767 40.924 0.70 40.21 ? 240 LYS A CD 1 ATOM 1613 C CD B LYS A 1 247 ? 38.906 30.717 44.705 0.30 34.42 ? 240 LYS A CD 1 ATOM 1614 C CE A LYS A 1 247 ? 41.588 28.067 40.919 0.70 43.04 ? 240 LYS A CE 1 ATOM 1615 C CE B LYS A 1 247 ? 38.647 31.237 46.103 0.30 34.22 ? 240 LYS A CE 1 ATOM 1616 N NZ A LYS A 1 247 ? 42.303 28.238 39.608 0.70 45.03 ? 240 LYS A NZ 1 ATOM 1617 N NZ B LYS A 1 247 ? 38.010 30.206 46.981 0.30 34.06 ? 240 LYS A NZ 1 ATOM 1618 N N . SER A 1 248 ? 35.873 30.242 40.437 1.00 34.03 ? 241 SER A N 1 ATOM 1619 C CA . SER A 1 248 ? 34.428 30.209 40.075 1.00 33.60 ? 241 SER A CA 1 ATOM 1620 C C . SER A 1 248 ? 33.668 29.310 41.039 1.00 32.26 ? 241 SER A C 1 ATOM 1621 O O . SER A 1 248 ? 34.220 28.303 41.516 1.00 32.78 ? 241 SER A O 1 ATOM 1622 C CB . SER A 1 248 ? 34.267 29.517 38.705 1.00 36.10 ? 241 SER A CB 1 ATOM 1623 O OG . SER A 1 248 ? 34.779 30.259 37.625 1.00 40.35 ? 241 SER A OG 1 ATOM 1624 N N . TYR A 1 249 ? 32.385 29.616 41.265 1.00 30.45 ? 242 TYR A N 1 ATOM 1625 C CA . TYR A 1 249 ? 31.519 28.725 42.004 1.00 29.72 ? 242 TYR A CA 1 ATOM 1626 C C . TYR A 1 249 ? 31.567 27.317 41.382 1.00 30.60 ? 242 TYR A C 1 ATOM 1627 O O . TYR A 1 249 ? 31.526 27.207 40.154 1.00 30.95 ? 242 TYR A O 1 ATOM 1628 C CB . TYR A 1 249 ? 30.075 29.278 42.041 1.00 28.81 ? 242 TYR A CB 1 ATOM 1629 C CG . TYR A 1 249 ? 29.374 28.703 43.223 1.00 28.52 ? 242 TYR A CG 1 ATOM 1630 C CD1 . TYR A 1 249 ? 29.695 29.154 44.513 1.00 28.82 ? 242 TYR A CD1 1 ATOM 1631 C CD2 . TYR A 1 249 ? 28.478 27.645 43.080 1.00 30.67 ? 242 TYR A CD2 1 ATOM 1632 C CE1 . TYR A 1 249 ? 29.124 28.593 45.626 1.00 30.44 ? 242 TYR A CE1 1 ATOM 1633 C CE2 . TYR A 1 249 ? 27.869 27.079 44.204 1.00 30.47 ? 242 TYR A CE2 1 ATOM 1634 C CZ . TYR A 1 249 ? 28.208 27.580 45.471 1.00 31.17 ? 242 TYR A CZ 1 ATOM 1635 O OH . TYR A 1 249 ? 27.683 27.015 46.590 1.00 34.13 ? 242 TYR A OH 1 ATOM 1636 N N . PRO A 1 250 ? 31.630 26.246 42.210 1.00 31.55 ? 243 PRO A N 1 ATOM 1637 C CA . PRO A 1 250 ? 31.493 26.137 43.678 1.00 32.12 ? 243 PRO A CA 1 ATOM 1638 C C . PRO A 1 250 ? 32.778 26.251 44.525 1.00 33.22 ? 243 PRO A C 1 ATOM 1639 O O . PRO A 1 250 ? 32.718 26.093 45.752 1.00 34.23 ? 243 PRO A O 1 ATOM 1640 C CB . PRO A 1 250 ? 30.916 24.732 43.851 1.00 32.29 ? 243 PRO A CB 1 ATOM 1641 C CG . PRO A 1 250 ? 31.635 23.945 42.771 1.00 33.27 ? 243 PRO A CG 1 ATOM 1642 C CD . PRO A 1 250 ? 31.640 24.901 41.580 1.00 32.19 ? 243 PRO A CD 1 ATOM 1643 N N A ASP A 1 251 ? 33.882 26.556 43.857 0.70 32.82 ? 244 ASP A N 1 ATOM 1644 N N B ASP A 1 251 ? 33.934 26.474 43.929 0.30 33.22 ? 244 ASP A N 1 ATOM 1645 C CA A ASP A 1 251 ? 35.213 26.563 44.477 0.70 34.23 ? 244 ASP A CA 1 ATOM 1646 C CA B ASP A 1 251 ? 35.108 26.578 44.801 0.30 33.90 ? 244 ASP A CA 1 ATOM 1647 C C A ASP A 1 251 ? 35.575 27.922 45.074 0.70 33.48 ? 244 ASP A C 1 ATOM 1648 C C B ASP A 1 251 ? 35.712 27.975 44.864 0.30 33.52 ? 244 ASP A C 1 ATOM 1649 O O A ASP A 1 251 ? 36.478 28.025 45.916 0.70 33.26 ? 244 ASP A O 1 ATOM 1650 O O B ASP A 1 251 ? 36.908 28.169 45.109 0.30 34.05 ? 244 ASP A O 1 ATOM 1651 C CB A ASP A 1 251 ? 36.266 26.097 43.468 0.70 35.30 ? 244 ASP A CB 1 ATOM 1652 C CB B ASP A 1 251 ? 36.103 25.426 44.600 0.30 34.57 ? 244 ASP A CB 1 ATOM 1653 C CG A ASP A 1 251 ? 36.033 24.652 43.005 0.70 38.34 ? 244 ASP A CG 1 ATOM 1654 C CG B ASP A 1 251 ? 35.541 24.078 45.099 0.30 35.34 ? 244 ASP A CG 1 ATOM 1655 O OD1 A ASP A 1 251 ? 35.726 23.774 43.841 0.70 40.59 ? 244 ASP A OD1 1 ATOM 1656 O OD1 B ASP A 1 251 ? 35.738 23.728 46.289 0.30 35.95 ? 244 ASP A OD1 1 ATOM 1657 O OD2 A ASP A 1 251 ? 36.161 24.388 41.797 0.70 43.49 ? 244 ASP A OD2 1 ATOM 1658 O OD2 B ASP A 1 251 ? 34.868 23.385 44.309 0.30 33.73 ? 244 ASP A OD2 1 ATOM 1659 N N . GLY A 1 252 ? 34.827 28.949 44.659 1.00 33.02 ? 245 GLY A N 1 ATOM 1660 C CA . GLY A 1 252 ? 35.062 30.324 45.065 1.00 31.92 ? 245 GLY A CA 1 ATOM 1661 C C . GLY A 1 252 ? 33.811 31.105 44.759 1.00 31.08 ? 245 GLY A C 1 ATOM 1662 O O . GLY A 1 252 ? 32.762 30.523 44.422 1.00 31.58 ? 245 GLY A O 1 ATOM 1663 N N . TRP A 1 253 ? 33.900 32.423 44.881 1.00 29.98 ? 246 TRP A N 1 ATOM 1664 C CA . TRP A 1 253 ? 32.688 33.234 44.748 1.00 28.55 ? 246 TRP A CA 1 ATOM 1665 C C . TRP A 1 253 ? 32.563 33.952 43.392 1.00 28.56 ? 246 TRP A C 1 ATOM 1666 O O . TRP A 1 253 ? 31.685 34.814 43.210 1.00 27.35 ? 246 TRP A O 1 ATOM 1667 C CB . TRP A 1 253 ? 32.546 34.206 45.939 1.00 28.39 ? 246 TRP A CB 1 ATOM 1668 C CG . TRP A 1 253 ? 33.819 34.942 46.308 1.00 31.52 ? 246 TRP A CG 1 ATOM 1669 C CD1 . TRP A 1 253 ? 34.737 34.569 47.246 1.00 33.44 ? 246 TRP A CD1 1 ATOM 1670 C CD2 . TRP A 1 253 ? 34.272 36.196 45.777 1.00 31.73 ? 246 TRP A CD2 1 ATOM 1671 N NE1 . TRP A 1 253 ? 35.746 35.507 47.321 1.00 34.22 ? 246 TRP A NE1 1 ATOM 1672 C CE2 . TRP A 1 253 ? 35.484 36.513 46.430 1.00 31.98 ? 246 TRP A CE2 1 ATOM 1673 C CE3 . TRP A 1 253 ? 33.779 37.072 44.800 1.00 32.31 ? 246 TRP A CE3 1 ATOM 1674 C CZ2 . TRP A 1 253 ? 36.219 37.666 46.135 1.00 32.52 ? 246 TRP A CZ2 1 ATOM 1675 C CZ3 . TRP A 1 253 ? 34.504 38.235 44.507 1.00 34.78 ? 246 TRP A CZ3 1 ATOM 1676 C CH2 . TRP A 1 253 ? 35.722 38.520 45.181 1.00 32.73 ? 246 TRP A CH2 1 ATOM 1677 N N . ASN A 1 254 ? 33.379 33.550 42.419 1.00 27.60 ? 247 ASN A N 1 ATOM 1678 C CA . ASN A 1 254 ? 33.290 34.136 41.074 1.00 28.15 ? 247 ASN A CA 1 ATOM 1679 C C . ASN A 1 254 ? 32.209 33.522 40.198 1.00 27.50 ? 247 ASN A C 1 ATOM 1680 O O . ASN A 1 254 ? 31.762 32.403 40.453 1.00 28.44 ? 247 ASN A O 1 ATOM 1681 C CB . ASN A 1 254 ? 34.636 34.039 40.338 1.00 28.89 ? 247 ASN A CB 1 ATOM 1682 C CG . ASN A 1 254 ? 35.482 35.290 40.524 1.00 29.69 ? 247 ASN A CG 1 ATOM 1683 O OD1 . ASN A 1 254 ? 34.973 36.343 40.942 1.00 30.36 ? 247 ASN A OD1 1 ATOM 1684 N ND2 . ASN A 1 254 ? 36.783 35.194 40.186 1.00 29.02 ? 247 ASN A ND2 1 ATOM 1685 N N . LEU A 1 255 ? 31.815 34.256 39.156 1.00 26.25 ? 248 LEU A N 1 ATOM 1686 C CA . LEU A 1 255 ? 30.818 33.776 38.204 1.00 25.68 ? 248 LEU A CA 1 ATOM 1687 C C . LEU A 1 255 ? 31.481 32.861 37.200 1.00 26.22 ? 248 LEU A C 1 ATOM 1688 O O . LEU A 1 255 ? 32.477 33.271 36.564 1.00 27.41 ? 248 LEU A O 1 ATOM 1689 C CB . LEU A 1 255 ? 30.211 34.963 37.443 1.00 24.63 ? 248 LEU A CB 1 ATOM 1690 C CG . LEU A 1 255 ? 29.053 34.671 36.492 1.00 26.10 ? 248 LEU A CG 1 ATOM 1691 C CD1 . LEU A 1 255 ? 27.779 34.216 37.197 1.00 23.65 ? 248 LEU A CD1 1 ATOM 1692 C CD2 . LEU A 1 255 ? 28.816 35.954 35.651 1.00 27.56 ? 248 LEU A CD2 1 ATOM 1693 N N . PRO A 1 256 ? 30.966 31.615 37.069 1.00 27.01 ? 249 PRO A N 1 ATOM 1694 C CA . PRO A 1 256 ? 31.459 30.728 36.007 1.00 27.04 ? 249 PRO A CA 1 ATOM 1695 C C . PRO A 1 256 ? 30.941 31.138 34.628 1.00 27.20 ? 249 PRO A C 1 ATOM 1696 O O . PRO A 1 256 ? 29.992 31.925 34.518 1.00 26.54 ? 249 PRO A O 1 ATOM 1697 C CB . PRO A 1 256 ? 30.880 29.349 36.367 1.00 28.21 ? 249 PRO A CB 1 ATOM 1698 C CG . PRO A 1 256 ? 29.958 29.550 37.461 1.00 26.77 ? 249 PRO A CG 1 ATOM 1699 C CD . PRO A 1 256 ? 29.925 30.985 37.897 1.00 26.21 ? 249 PRO A CD 1 ATOM 1700 N N . GLY A 1 257 ? 31.557 30.600 33.572 1.00 27.82 ? 250 GLY A N 1 ATOM 1701 C CA . GLY A 1 257 ? 31.204 31.044 32.228 1.00 27.96 ? 250 GLY A CA 1 ATOM 1702 C C . GLY A 1 257 ? 29.806 30.668 31.793 1.00 26.97 ? 250 GLY A C 1 ATOM 1703 O O . GLY A 1 257 ? 29.293 31.225 30.821 1.00 27.34 ? 250 GLY A O 1 ATOM 1704 N N . GLY A 1 258 ? 29.213 29.696 32.484 1.00 26.42 ? 251 GLY A N 1 ATOM 1705 C CA . GLY A 1 258 ? 27.819 29.291 32.246 1.00 25.91 ? 251 GLY A CA 1 ATOM 1706 C C . GLY A 1 258 ? 26.815 30.038 33.131 1.00 25.63 ? 251 GLY A C 1 ATOM 1707 O O . GLY A 1 258 ? 25.612 29.918 32.931 1.00 24.96 ? 251 GLY A O 1 ATOM 1708 N N . GLY A 1 259 ? 27.310 30.834 34.080 1.00 25.29 ? 252 GLY A N 1 ATOM 1709 C CA . GLY A 1 259 ? 26.424 31.639 34.946 1.00 23.60 ? 252 GLY A CA 1 ATOM 1710 C C . GLY A 1 259 ? 25.765 32.788 34.204 1.00 23.17 ? 252 GLY A C 1 ATOM 1711 O O . GLY A 1 259 ? 26.360 33.378 33.284 1.00 23.93 ? 252 GLY A O 1 ATOM 1712 N N . VAL A 1 260 ? 24.549 33.125 34.620 1.00 22.84 ? 253 VAL A N 1 ATOM 1713 C CA . VAL A 1 260 ? 23.787 34.187 33.958 1.00 21.49 ? 253 VAL A CA 1 ATOM 1714 C C . VAL A 1 260 ? 22.998 34.988 34.977 1.00 21.91 ? 253 VAL A C 1 ATOM 1715 O O . VAL A 1 260 ? 22.401 34.426 35.901 1.00 22.37 ? 253 VAL A O 1 ATOM 1716 C CB . VAL A 1 260 ? 22.747 33.611 32.919 1.00 21.61 ? 253 VAL A CB 1 ATOM 1717 C CG1 . VAL A 1 260 ? 22.152 34.766 32.104 1.00 22.66 ? 253 VAL A CG1 1 ATOM 1718 C CG2 . VAL A 1 260 ? 23.412 32.561 31.985 1.00 23.26 ? 253 VAL A CG2 1 ATOM 1719 N N . GLN A 1 261 ? 22.978 36.301 34.772 1.00 20.90 ? 254 GLN A N 1 ATOM 1720 C CA . GLN A 1 261 ? 22.270 37.215 35.667 1.00 20.24 ? 254 GLN A CA 1 ATOM 1721 C C . GLN A 1 261 ? 20.864 37.426 35.141 1.00 20.49 ? 254 GLN A C 1 ATOM 1722 O O . GLN A 1 261 ? 20.671 37.999 34.051 1.00 21.17 ? 254 GLN A O 1 ATOM 1723 C CB . GLN A 1 261 ? 23.050 38.538 35.691 1.00 20.06 ? 254 GLN A CB 1 ATOM 1724 C CG . GLN A 1 261 ? 22.344 39.637 36.544 1.00 19.24 ? 254 GLN A CG 1 ATOM 1725 C CD . GLN A 1 261 ? 22.941 41.020 36.333 1.00 20.54 ? 254 GLN A CD 1 ATOM 1726 O OE1 . GLN A 1 261 ? 22.205 42.019 36.359 1.00 20.90 ? 254 GLN A OE1 1 ATOM 1727 N NE2 . GLN A 1 261 ? 24.278 41.110 36.218 1.00 22.38 ? 254 GLN A NE2 1 ATOM 1728 N N . ARG A 1 262 ? 19.870 36.963 35.913 1.00 20.66 ? 255 ARG A N 1 ATOM 1729 C CA . ARG A 1 262 ? 18.443 37.267 35.653 1.00 20.08 ? 255 ARG A CA 1 ATOM 1730 C C . ARG A 1 262 ? 18.132 38.716 36.023 1.00 19.32 ? 255 ARG A C 1 ATOM 1731 O O . ARG A 1 262 ? 18.923 39.349 36.715 1.00 19.42 ? 255 ARG A O 1 ATOM 1732 C CB . ARG A 1 262 ? 17.547 36.345 36.484 1.00 19.77 ? 255 ARG A CB 1 ATOM 1733 C CG . ARG A 1 262 ? 17.550 34.898 35.938 1.00 19.46 ? 255 ARG A CG 1 ATOM 1734 C CD . ARG A 1 262 ? 17.160 33.945 37.090 1.00 19.75 ? 255 ARG A CD 1 ATOM 1735 N NE . ARG A 1 262 ? 17.393 32.545 36.700 1.00 21.45 ? 255 ARG A NE 1 ATOM 1736 C CZ . ARG A 1 262 ? 18.584 31.965 36.653 1.00 22.04 ? 255 ARG A CZ 1 ATOM 1737 N NH1 . ARG A 1 262 ? 19.699 32.651 36.941 1.00 22.42 ? 255 ARG A NH1 1 ATOM 1738 N NH2 . ARG A 1 262 ? 18.664 30.681 36.289 1.00 21.94 ? 255 ARG A NH2 1 ATOM 1739 N N . GLY A 1 263 ? 16.998 39.239 35.565 1.00 19.60 ? 256 GLY A N 1 ATOM 1740 C CA . GLY A 1 263 ? 16.555 40.535 36.132 1.00 18.82 ? 256 GLY A CA 1 ATOM 1741 C C . GLY A 1 263 ? 15.578 41.226 35.214 1.00 20.12 ? 256 GLY A C 1 ATOM 1742 O O . GLY A 1 263 ? 15.630 41.062 33.988 1.00 19.24 ? 256 GLY A O 1 ATOM 1743 N N . ASN A 1 264 ? 14.672 42.010 35.808 1.00 18.25 ? 257 ASN A N 1 ATOM 1744 C CA . ASN A 1 264 ? 13.689 42.670 34.958 1.00 18.33 ? 257 ASN A CA 1 ATOM 1745 C C . ASN A 1 264 ? 14.305 43.845 34.202 1.00 18.24 ? 257 ASN A C 1 ATOM 1746 O O . ASN A 1 264 ? 15.336 44.380 34.602 1.00 18.33 ? 257 ASN A O 1 ATOM 1747 C CB . ASN A 1 264 ? 12.472 43.114 35.780 1.00 16.97 ? 257 ASN A CB 1 ATOM 1748 C CG . ASN A 1 264 ? 12.694 44.463 36.494 1.00 17.43 ? 257 ASN A CG 1 ATOM 1749 O OD1 . ASN A 1 264 ? 12.667 45.530 35.857 1.00 17.65 ? 257 ASN A OD1 1 ATOM 1750 N ND2 . ASN A 1 264 ? 12.859 44.425 37.833 1.00 18.96 ? 257 ASN A ND2 1 ATOM 1751 N N . ILE A 1 265 ? 13.658 44.225 33.098 1.00 17.72 ? 258 ILE A N 1 ATOM 1752 C CA . ILE A 1 265 ? 14.147 45.296 32.229 1.00 18.47 ? 258 ILE A CA 1 ATOM 1753 C C . ILE A 1 265 ? 13.101 46.405 32.052 1.00 18.89 ? 258 ILE A C 1 ATOM 1754 O O . ILE A 1 265 ? 13.055 47.075 31.021 1.00 20.61 ? 258 ILE A O 1 ATOM 1755 C CB . ILE A 1 265 ? 14.594 44.728 30.857 1.00 20.08 ? 258 ILE A CB 1 ATOM 1756 C CG1 . ILE A 1 265 ? 13.513 43.803 30.288 1.00 19.70 ? 258 ILE A CG1 1 ATOM 1757 C CG2 . ILE A 1 265 ? 15.891 43.932 31.034 1.00 19.39 ? 258 ILE A CG2 1 ATOM 1758 C CD1 . ILE A 1 265 ? 13.705 43.494 28.746 1.00 23.33 ? 258 ILE A CD1 1 ATOM 1759 N N . LEU A 1 266 ? 12.284 46.603 33.090 1.00 18.98 ? 259 LEU A N 1 ATOM 1760 C CA . LEU A 1 266 ? 11.256 47.645 33.046 1.00 18.79 ? 259 LEU A CA 1 ATOM 1761 C C . LEU A 1 266 ? 11.853 49.019 33.262 1.00 19.10 ? 259 LEU A C 1 ATOM 1762 O O . LEU A 1 266 ? 12.927 49.161 33.834 1.00 19.64 ? 259 LEU A O 1 ATOM 1763 C CB . LEU A 1 266 ? 10.237 47.426 34.176 1.00 17.60 ? 259 LEU A CB 1 ATOM 1764 C CG . LEU A 1 266 ? 9.403 46.141 34.079 1.00 18.32 ? 259 LEU A CG 1 ATOM 1765 C CD1 . LEU A 1 266 ? 8.512 46.018 35.322 1.00 20.07 ? 259 LEU A CD1 1 ATOM 1766 C CD2 . LEU A 1 266 ? 8.531 46.170 32.842 1.00 19.80 ? 259 LEU A CD2 1 ATOM 1767 N N . ASN A 1 267 ? 11.105 50.036 32.817 1.00 18.31 ? 260 ASN A N 1 ATOM 1768 C CA . ASN A 1 267 ? 11.372 51.429 33.171 1.00 18.70 ? 260 ASN A CA 1 ATOM 1769 C C . ASN A 1 267 ? 10.122 52.026 33.824 1.00 18.58 ? 260 ASN A C 1 ATOM 1770 O O . ASN A 1 267 ? 9.382 52.804 33.203 1.00 19.49 ? 260 ASN A O 1 ATOM 1771 C CB . ASN A 1 267 ? 11.768 52.208 31.919 1.00 19.57 ? 260 ASN A CB 1 ATOM 1772 C CG . ASN A 1 267 ? 13.202 51.914 31.525 1.00 21.82 ? 260 ASN A CG 1 ATOM 1773 O OD1 . ASN A 1 267 ? 14.141 52.522 32.050 1.00 23.90 ? 260 ASN A OD1 1 ATOM 1774 N ND2 . ASN A 1 267 ? 13.383 50.911 30.666 1.00 21.74 ? 260 ASN A ND2 1 ATOM 1775 N N . LEU A 1 268 ? 9.877 51.616 35.067 1.00 17.74 ? 261 LEU A N 1 ATOM 1776 C CA . LEU A 1 268 ? 8.637 51.971 35.753 1.00 17.26 ? 261 LEU A CA 1 ATOM 1777 C C . LEU A 1 268 ? 8.646 53.371 36.319 1.00 17.34 ? 261 LEU A C 1 ATOM 1778 O O . LEU A 1 268 ? 7.569 53.938 36.531 1.00 16.67 ? 261 LEU A O 1 ATOM 1779 C CB . LEU A 1 268 ? 8.403 51.016 36.931 1.00 17.32 ? 261 LEU A CB 1 ATOM 1780 C CG . LEU A 1 268 ? 8.047 49.596 36.522 1.00 16.35 ? 261 LEU A CG 1 ATOM 1781 C CD1 . LEU A 1 268 ? 7.991 48.763 37.844 1.00 18.13 ? 261 LEU A CD1 1 ATOM 1782 C CD2 . LEU A 1 268 ? 6.683 49.575 35.810 1.00 18.50 ? 261 LEU A CD2 1 ATOM 1783 N N . ASN A 1 269 ? 9.843 53.923 36.585 1.00 17.12 ? 262 ASN A N 1 ATOM 1784 C CA . ASN A 1 269 ? 9.926 55.255 37.249 1.00 17.89 ? 262 ASN A CA 1 ATOM 1785 C C . ASN A 1 269 ? 9.042 55.393 38.493 1.00 18.26 ? 262 ASN A C 1 ATOM 1786 O O . ASN A 1 269 ? 8.407 56.438 38.715 1.00 18.76 ? 262 ASN A O 1 ATOM 1787 C CB . ASN A 1 269 ? 9.574 56.373 36.245 1.00 17.59 ? 262 ASN A CB 1 ATOM 1788 C CG . ASN A 1 269 ? 10.590 56.463 35.144 1.00 22.02 ? 262 ASN A CG 1 ATOM 1789 O OD1 . ASN A 1 269 ? 11.768 56.246 35.402 1.00 22.39 ? 262 ASN A OD1 1 ATOM 1790 N ND2 . ASN A 1 269 ? 10.152 56.770 33.916 1.00 22.73 ? 262 ASN A ND2 1 ATOM 1791 N N . GLY A 1 270 ? 8.998 54.320 39.292 1.00 16.55 ? 263 GLY A N 1 ATOM 1792 C CA . GLY A 1 270 ? 8.255 54.368 40.555 1.00 16.28 ? 263 GLY A CA 1 ATOM 1793 C C . GLY A 1 270 ? 6.789 53.939 40.471 1.00 17.07 ? 263 GLY A C 1 ATOM 1794 O O . GLY A 1 270 ? 6.106 53.963 41.479 1.00 17.19 ? 263 GLY A O 1 ATOM 1795 N N . ALA A 1 271 ? 6.316 53.497 39.299 1.00 15.29 ? 264 ALA A N 1 ATOM 1796 C CA . ALA A 1 271 ? 4.864 53.282 39.134 1.00 16.11 ? 264 ALA A CA 1 ATOM 1797 C C . ALA A 1 271 ? 4.304 52.060 39.864 1.00 16.73 ? 264 ALA A C 1 ATOM 1798 O O . ALA A 1 271 ? 3.110 52.036 40.172 1.00 18.21 ? 264 ALA A O 1 ATOM 1799 C CB . ALA A 1 271 ? 4.484 53.225 37.610 1.00 16.33 ? 264 ALA A CB 1 ATOM 1800 N N . GLY A 1 272 ? 5.138 51.062 40.115 1.00 16.24 ? 265 GLY A N 1 ATOM 1801 C CA . GLY A 1 272 ? 4.623 49.803 40.668 1.00 15.63 ? 265 GLY A CA 1 ATOM 1802 C C . GLY A 1 272 ? 4.067 48.903 39.565 1.00 16.21 ? 265 GLY A C 1 ATOM 1803 O O . GLY A 1 272 ? 4.564 48.892 38.430 1.00 17.06 ? 265 GLY A O 1 ATOM 1804 N N . ASP A 1 273 ? 3.012 48.150 39.873 1.00 15.88 ? 266 ASP A N 1 ATOM 1805 C CA . ASP A 1 273 ? 2.421 47.269 38.835 1.00 17.62 ? 266 ASP A CA 1 ATOM 1806 C C . ASP A 1 273 ? 2.190 48.037 37.534 1.00 18.18 ? 266 ASP A C 1 ATOM 1807 O O . ASP A 1 273 ? 1.504 49.069 37.544 1.00 18.55 ? 266 ASP A O 1 ATOM 1808 C CB . ASP A 1 273 ? 1.086 46.751 39.376 1.00 17.37 ? 266 ASP A CB 1 ATOM 1809 C CG . ASP A 1 273 ? 0.223 46.066 38.324 1.00 18.51 ? 266 ASP A CG 1 ATOM 1810 O OD1 . ASP A 1 273 ? 0.734 45.281 37.506 1.00 19.09 ? 266 ASP A OD1 1 ATOM 1811 O OD2 . ASP A 1 273 ? -0.994 46.331 38.350 1.00 19.64 ? 266 ASP A OD2 1 ATOM 1812 N N . PRO A 1 274 ? 2.722 47.523 36.406 1.00 18.16 ? 267 PRO A N 1 ATOM 1813 C CA . PRO A 1 274 ? 2.564 48.260 35.139 1.00 19.16 ? 267 PRO A CA 1 ATOM 1814 C C . PRO A 1 274 ? 1.115 48.579 34.754 1.00 18.84 ? 267 PRO A C 1 ATOM 1815 O O . PRO A 1 274 ? 0.865 49.550 34.002 1.00 19.87 ? 267 PRO A O 1 ATOM 1816 C CB . PRO A 1 274 ? 3.168 47.293 34.096 1.00 19.50 ? 267 PRO A CB 1 ATOM 1817 C CG . PRO A 1 274 ? 4.215 46.509 34.855 1.00 19.95 ? 267 PRO A CG 1 ATOM 1818 C CD . PRO A 1 274 ? 3.645 46.371 36.297 1.00 19.06 ? 267 PRO A CD 1 ATOM 1819 N N . LEU A 1 275 ? 0.153 47.799 35.253 1.00 18.91 ? 268 LEU A N 1 ATOM 1820 C CA . LEU A 1 275 ? -1.237 47.967 34.806 1.00 18.80 ? 268 LEU A CA 1 ATOM 1821 C C . LEU A 1 275 ? -2.088 48.895 35.689 1.00 17.64 ? 268 LEU A C 1 ATOM 1822 O O . LEU A 1 275 ? -3.187 49.286 35.277 1.00 18.61 ? 268 LEU A O 1 ATOM 1823 C CB . LEU A 1 275 ? -1.937 46.611 34.742 1.00 18.94 ? 268 LEU A CB 1 ATOM 1824 C CG . LEU A 1 275 ? -1.242 45.559 33.878 1.00 19.60 ? 268 LEU A CG 1 ATOM 1825 C CD1 . LEU A 1 275 ? -2.128 44.333 33.847 1.00 22.68 ? 268 LEU A CD1 1 ATOM 1826 C CD2 . LEU A 1 275 ? -1.001 46.109 32.444 1.00 22.46 ? 268 LEU A CD2 1 ATOM 1827 N N . THR A 1 276 ? -1.567 49.297 36.852 1.00 16.84 ? 269 THR A N 1 ATOM 1828 C CA . THR A 1 276 ? -2.409 50.036 37.837 1.00 17.01 ? 269 THR A CA 1 ATOM 1829 C C . THR A 1 276 ? -1.706 51.227 38.476 1.00 17.16 ? 269 THR A C 1 ATOM 1830 O O . THR A 1 276 ? -1.766 51.410 39.708 1.00 17.80 ? 269 THR A O 1 ATOM 1831 C CB . THR A 1 276 ? -2.914 49.085 38.994 1.00 16.66 ? 269 THR A CB 1 ATOM 1832 O OG1 . THR A 1 276 ? -1.765 48.496 39.673 1.00 17.06 ? 269 THR A OG1 1 ATOM 1833 C CG2 . THR A 1 276 ? -3.882 47.991 38.426 1.00 18.27 ? 269 THR A CG2 1 ATOM 1834 N N . PRO A 1 277 ? -1.033 52.067 37.662 1.00 17.48 ? 270 PRO A N 1 ATOM 1835 C CA . PRO A 1 277 ? -0.291 53.164 38.297 1.00 17.20 ? 270 PRO A CA 1 ATOM 1836 C C . PRO A 1 277 ? -1.190 54.108 39.103 1.00 17.93 ? 270 PRO A C 1 ATOM 1837 O O . PRO A 1 277 ? -2.237 54.573 38.580 1.00 18.72 ? 270 PRO A O 1 ATOM 1838 C CB . PRO A 1 277 ? 0.335 53.902 37.096 1.00 17.68 ? 270 PRO A CB 1 ATOM 1839 C CG . PRO A 1 277 ? -0.606 53.568 35.932 1.00 18.18 ? 270 PRO A CG 1 ATOM 1840 C CD . PRO A 1 277 ? -0.970 52.133 36.177 1.00 19.18 ? 270 PRO A CD 1 ATOM 1841 N N . GLY A 1 278 ? -0.784 54.349 40.356 1.00 17.49 ? 271 GLY A N 1 ATOM 1842 C CA . GLY A 1 278 ? -1.511 55.259 41.265 1.00 17.14 ? 271 GLY A CA 1 ATOM 1843 C C . GLY A 1 278 ? -2.382 54.583 42.304 1.00 18.17 ? 271 GLY A C 1 ATOM 1844 O O . GLY A 1 278 ? -2.773 55.221 43.275 1.00 19.51 ? 271 GLY A O 1 ATOM 1845 N N . TYR A 1 279 ? -2.754 53.319 42.072 1.00 17.71 ? 272 TYR A N 1 ATOM 1846 C CA . TYR A 1 279 ? -3.845 52.660 42.829 1.00 17.86 ? 272 TYR A CA 1 ATOM 1847 C C . TYR A 1 279 ? -3.472 51.197 43.062 1.00 16.67 ? 272 TYR A C 1 ATOM 1848 O O . TYR A 1 279 ? -2.862 50.548 42.180 1.00 17.61 ? 272 TYR A O 1 ATOM 1849 C CB . TYR A 1 279 ? -5.185 52.747 42.050 1.00 17.98 ? 272 TYR A CB 1 ATOM 1850 C CG . TYR A 1 279 ? -5.498 54.170 41.668 1.00 19.23 ? 272 TYR A CG 1 ATOM 1851 C CD1 . TYR A 1 279 ? -6.047 55.058 42.594 1.00 17.92 ? 272 TYR A CD1 1 ATOM 1852 C CD2 . TYR A 1 279 ? -5.128 54.662 40.428 1.00 19.03 ? 272 TYR A CD2 1 ATOM 1853 C CE1 . TYR A 1 279 ? -6.264 56.387 42.265 1.00 18.47 ? 272 TYR A CE1 1 ATOM 1854 C CE2 . TYR A 1 279 ? -5.318 55.981 40.081 1.00 18.76 ? 272 TYR A CE2 1 ATOM 1855 C CZ . TYR A 1 279 ? -5.924 56.847 41.003 1.00 19.08 ? 272 TYR A CZ 1 ATOM 1856 O OH . TYR A 1 279 ? -6.114 58.153 40.635 1.00 18.12 ? 272 TYR A OH 1 ATOM 1857 N N . PRO A 1 280 ? -3.879 50.619 44.203 1.00 17.77 ? 273 PRO A N 1 ATOM 1858 C CA . PRO A 1 280 ? -3.518 49.221 44.466 1.00 17.92 ? 273 PRO A CA 1 ATOM 1859 C C . PRO A 1 280 ? -4.221 48.254 43.511 1.00 18.06 ? 273 PRO A C 1 ATOM 1860 O O . PRO A 1 280 ? -5.403 48.449 43.173 1.00 19.13 ? 273 PRO A O 1 ATOM 1861 C CB . PRO A 1 280 ? -3.983 48.986 45.928 1.00 18.31 ? 273 PRO A CB 1 ATOM 1862 C CG . PRO A 1 280 ? -5.081 50.020 46.143 1.00 18.75 ? 273 PRO A CG 1 ATOM 1863 C CD . PRO A 1 280 ? -4.617 51.234 45.328 1.00 17.36 ? 273 PRO A CD 1 ATOM 1864 N N . ALA A 1 281 ? -3.480 47.218 43.111 1.00 17.89 ? 274 ALA A N 1 ATOM 1865 C CA . ALA A 1 281 ? -3.979 46.187 42.229 1.00 18.51 ? 274 ALA A CA 1 ATOM 1866 C C . ALA A 1 281 ? -4.820 45.179 43.028 1.00 19.42 ? 274 ALA A C 1 ATOM 1867 O O . ALA A 1 281 ? -4.473 43.997 43.147 1.00 20.58 ? 274 ALA A O 1 ATOM 1868 C CB . ALA A 1 281 ? -2.821 45.525 41.538 1.00 18.84 ? 274 ALA A CB 1 ATOM 1869 N N . ASN A 1 282 ? -5.923 45.693 43.584 1.00 20.00 ? 275 ASN A N 1 ATOM 1870 C CA . ASN A 1 282 ? -6.835 44.898 44.420 1.00 22.15 ? 275 ASN A CA 1 ATOM 1871 C C . ASN A 1 282 ? -7.837 44.110 43.550 1.00 23.80 ? 275 ASN A C 1 ATOM 1872 O O . ASN A 1 282 ? -7.695 44.096 42.337 1.00 22.96 ? 275 ASN A O 1 ATOM 1873 C CB . ASN A 1 282 ? -7.508 45.824 45.450 1.00 22.59 ? 275 ASN A CB 1 ATOM 1874 C CG . ASN A 1 282 ? -8.310 46.929 44.816 1.00 24.20 ? 275 ASN A CG 1 ATOM 1875 O OD1 . ASN A 1 282 ? -8.805 46.801 43.696 1.00 25.00 ? 275 ASN A OD1 1 ATOM 1876 N ND2 . ASN A 1 282 ? -8.451 48.056 45.538 1.00 26.54 ? 275 ASN A ND2 1 ATOM 1877 N N C GLU A 1 283 ? -8.896 43.639 44.164 0.50 25.97 ? 276 GLU A N 1 ATOM 1878 N N D GLU A 1 283 ? -8.891 43.638 44.173 0.50 25.02 ? 276 GLU A N 1 ATOM 1879 C CA C GLU A 1 283 ? -9.766 42.725 43.478 0.50 27.94 ? 276 GLU A CA 1 ATOM 1880 C CA D GLU A 1 283 ? -9.801 42.749 43.499 0.50 27.17 ? 276 GLU A CA 1 ATOM 1881 C C C GLU A 1 283 ? -10.642 43.394 42.411 0.50 27.84 ? 276 GLU A C 1 ATOM 1882 C C D GLU A 1 283 ? -10.596 43.415 42.382 0.50 27.25 ? 276 GLU A C 1 ATOM 1883 O O C GLU A 1 283 ? -11.050 42.774 41.471 0.50 28.08 ? 276 GLU A O 1 ATOM 1884 O O D GLU A 1 283 ? -11.051 42.773 41.480 0.50 28.33 ? 276 GLU A O 1 ATOM 1885 C CB C GLU A 1 283 ? -10.581 41.956 44.516 0.50 30.37 ? 276 GLU A CB 1 ATOM 1886 C CB D GLU A 1 283 ? -10.733 42.151 44.537 0.50 28.12 ? 276 GLU A CB 1 ATOM 1887 C CG C GLU A 1 283 ? -11.299 40.769 43.970 0.50 35.57 ? 276 GLU A CG 1 ATOM 1888 C CG D GLU A 1 283 ? -11.100 40.745 44.252 0.50 31.53 ? 276 GLU A CG 1 ATOM 1889 C CD C GLU A 1 283 ? -10.409 39.574 43.672 0.50 41.87 ? 276 GLU A CD 1 ATOM 1890 C CD D GLU A 1 283 ? -10.061 39.764 44.724 0.50 34.52 ? 276 GLU A CD 1 ATOM 1891 O OE1 C GLU A 1 283 ? -9.655 39.142 44.543 0.50 45.55 ? 276 GLU A OE1 1 ATOM 1892 O OE1 D GLU A 1 283 ? -9.759 38.879 43.951 0.50 33.70 ? 276 GLU A OE1 1 ATOM 1893 O OE2 C GLU A 1 283 ? -10.521 39.048 42.565 0.50 45.61 ? 276 GLU A OE2 1 ATOM 1894 O OE2 D GLU A 1 283 ? -9.581 39.877 45.866 0.50 36.71 ? 276 GLU A OE2 1 ATOM 1895 N N . TYR A 1 284 ? -10.961 44.656 42.587 1.00 26.89 ? 277 TYR A N 1 ATOM 1896 C CA . TYR A 1 284 ? -11.811 45.393 41.661 1.00 27.31 ? 277 TYR A CA 1 ATOM 1897 C C . TYR A 1 284 ? -11.065 46.391 40.821 1.00 26.96 ? 277 TYR A C 1 ATOM 1898 O O . TYR A 1 284 ? -11.692 47.213 40.140 1.00 28.01 ? 277 TYR A O 1 ATOM 1899 C CB . TYR A 1 284 ? -12.991 46.051 42.405 1.00 27.42 ? 277 TYR A CB 1 ATOM 1900 C CG . TYR A 1 284 ? -12.520 46.998 43.460 1.00 27.06 ? 277 TYR A CG 1 ATOM 1901 C CD1 . TYR A 1 284 ? -12.303 48.354 43.151 1.00 27.63 ? 277 TYR A CD1 1 ATOM 1902 C CD2 . TYR A 1 284 ? -12.289 46.559 44.770 1.00 26.41 ? 277 TYR A CD2 1 ATOM 1903 C CE1 . TYR A 1 284 ? -11.844 49.243 44.116 1.00 28.07 ? 277 TYR A CE1 1 ATOM 1904 C CE2 . TYR A 1 284 ? -11.841 47.451 45.751 1.00 28.19 ? 277 TYR A CE2 1 ATOM 1905 C CZ . TYR A 1 284 ? -11.611 48.789 45.392 1.00 29.41 ? 277 TYR A CZ 1 ATOM 1906 O OH . TYR A 1 284 ? -11.168 49.678 46.342 1.00 29.74 ? 277 TYR A OH 1 ATOM 1907 N N . ALA A 1 285 ? -9.734 46.329 40.840 1.00 26.62 ? 278 ALA A N 1 ATOM 1908 C CA . ALA A 1 285 ? -8.916 47.301 40.111 1.00 27.13 ? 278 ALA A CA 1 ATOM 1909 C C . ALA A 1 285 ? -9.243 47.306 38.631 1.00 27.03 ? 278 ALA A C 1 ATOM 1910 O O . ALA A 1 285 ? -9.529 46.241 38.050 1.00 28.15 ? 278 ALA A O 1 ATOM 1911 C CB . ALA A 1 285 ? -7.402 47.003 40.306 1.00 26.89 ? 278 ALA A CB 1 ATOM 1912 N N . TYR A 1 286 ? -9.266 48.505 38.052 1.00 26.66 ? 279 TYR A N 1 ATOM 1913 C CA . TYR A 1 286 ? -9.346 48.633 36.611 1.00 27.96 ? 279 TYR A CA 1 ATOM 1914 C C . TYR A 1 286 ? -7.913 48.628 36.103 1.00 27.02 ? 279 TYR A C 1 ATOM 1915 O O . TYR A 1 286 ? -7.020 49.294 36.650 1.00 28.15 ? 279 TYR A O 1 ATOM 1916 C CB . TYR A 1 286 ? -10.116 49.902 36.152 1.00 30.03 ? 279 TYR A CB 1 ATOM 1917 C CG A TYR A 1 286 ? -10.465 49.867 34.677 0.50 28.77 ? 279 TYR A CG 1 ATOM 1918 C CG B TYR A 1 286 ? -9.513 50.536 34.866 0.50 31.07 ? 279 TYR A CG 1 ATOM 1919 C CD1 A TYR A 1 286 ? -11.493 49.056 34.200 0.50 30.79 ? 279 TYR A CD1 1 ATOM 1920 C CD1 B TYR A 1 286 ? -10.187 50.489 33.652 0.50 33.92 ? 279 TYR A CD1 1 ATOM 1921 C CD2 A TYR A 1 286 ? -9.737 50.623 33.761 0.50 30.54 ? 279 TYR A CD2 1 ATOM 1922 C CD2 B TYR A 1 286 ? -8.258 51.141 34.883 0.50 32.60 ? 279 TYR A CD2 1 ATOM 1923 C CE1 A TYR A 1 286 ? -11.800 49.016 32.854 0.50 33.34 ? 279 TYR A CE1 1 ATOM 1924 C CE1 B TYR A 1 286 ? -9.634 51.044 32.505 0.50 34.45 ? 279 TYR A CE1 1 ATOM 1925 C CE2 A TYR A 1 286 ? -10.042 50.587 32.421 0.50 31.89 ? 279 TYR A CE2 1 ATOM 1926 C CE2 B TYR A 1 286 ? -7.689 51.685 33.737 0.50 34.49 ? 279 TYR A CE2 1 ATOM 1927 C CZ A TYR A 1 286 ? -11.065 49.787 31.974 0.50 33.79 ? 279 TYR A CZ 1 ATOM 1928 C CZ B TYR A 1 286 ? -8.390 51.637 32.549 0.50 35.40 ? 279 TYR A CZ 1 ATOM 1929 O OH A TYR A 1 286 ? -11.348 49.742 30.632 0.50 36.48 ? 279 TYR A OH 1 ATOM 1930 O OH B TYR A 1 286 ? -7.832 52.199 31.410 0.50 37.20 ? 279 TYR A OH 1 ATOM 1931 N N . ARG A 1 287 ? -7.662 47.796 35.110 1.00 24.33 ? 280 ARG A N 1 ATOM 1932 C CA . ARG A 1 287 ? -6.309 47.639 34.588 1.00 23.68 ? 280 ARG A CA 1 ATOM 1933 C C . ARG A 1 287 ? -6.174 48.265 33.247 1.00 24.84 ? 280 ARG A C 1 ATOM 1934 O O . ARG A 1 287 ? -7.050 48.116 32.380 1.00 25.40 ? 280 ARG A O 1 ATOM 1935 C CB A ARG A 1 287 ? -5.967 46.137 34.492 0.65 24.33 ? 280 ARG A CB 1 ATOM 1936 C CB B ARG A 1 287 ? -5.976 46.167 34.436 0.35 23.10 ? 280 ARG A CB 1 ATOM 1937 C CG A ARG A 1 287 ? -5.311 45.517 35.756 0.65 25.32 ? 280 ARG A CG 1 ATOM 1938 C CG B ARG A 1 287 ? -6.001 45.462 35.731 0.35 19.50 ? 280 ARG A CG 1 ATOM 1939 C CD A ARG A 1 287 ? -6.282 45.015 36.826 0.65 29.49 ? 280 ARG A CD 1 ATOM 1940 C CD B ARG A 1 287 ? -5.397 44.100 35.603 0.35 13.26 ? 280 ARG A CD 1 ATOM 1941 N NE A ARG A 1 287 ? -5.583 44.427 37.993 0.65 28.14 ? 280 ARG A NE 1 ATOM 1942 N NE B ARG A 1 287 ? -5.089 43.656 36.933 0.35 13.11 ? 280 ARG A NE 1 ATOM 1943 C CZ A ARG A 1 287 ? -6.196 44.024 39.102 0.65 28.80 ? 280 ARG A CZ 1 ATOM 1944 C CZ B ARG A 1 287 ? -6.004 43.307 37.825 0.35 13.13 ? 280 ARG A CZ 1 ATOM 1945 N NH1 A ARG A 1 287 ? -7.509 44.145 39.197 0.65 30.21 ? 280 ARG A NH1 1 ATOM 1946 N NH1 B ARG A 1 287 ? -7.295 43.291 37.507 0.35 14.32 ? 280 ARG A NH1 1 ATOM 1947 N NH2 A ARG A 1 287 ? -5.515 43.540 40.129 0.65 24.10 ? 280 ARG A NH2 1 ATOM 1948 N NH2 B ARG A 1 287 ? -5.638 42.951 39.033 0.35 15.64 ? 280 ARG A NH2 1 ATOM 1949 N N . ARG A 1 288 ? -5.057 48.936 33.042 1.00 23.78 ? 281 ARG A N 1 ATOM 1950 C CA . ARG A 1 288 ? -4.685 49.323 31.681 1.00 25.09 ? 281 ARG A CA 1 ATOM 1951 C C . ARG A 1 288 ? -4.545 48.091 30.789 1.00 25.79 ? 281 ARG A C 1 ATOM 1952 O O . ARG A 1 288 ? -4.216 46.982 31.259 1.00 25.67 ? 281 ARG A O 1 ATOM 1953 C CB . ARG A 1 288 ? -3.366 50.063 31.685 1.00 23.82 ? 281 ARG A CB 1 ATOM 1954 C CG . ARG A 1 288 ? -3.466 51.379 32.391 1.00 24.94 ? 281 ARG A CG 1 ATOM 1955 C CD . ARG A 1 288 ? -2.200 52.134 32.261 1.00 27.11 ? 281 ARG A CD 1 ATOM 1956 N NE . ARG A 1 288 ? -2.350 53.481 32.821 1.00 27.83 ? 281 ARG A NE 1 ATOM 1957 C CZ . ARG A 1 288 ? -1.468 54.458 32.649 1.00 29.79 ? 281 ARG A CZ 1 ATOM 1958 N NH1 . ARG A 1 288 ? -0.401 54.256 31.907 1.00 28.51 ? 281 ARG A NH1 1 ATOM 1959 N NH2 . ARG A 1 288 ? -1.667 55.638 33.216 1.00 30.26 ? 281 ARG A NH2 1 ATOM 1960 N N . GLY A 1 289 ? -4.838 48.298 29.503 1.00 27.84 ? 282 GLY A N 1 ATOM 1961 C CA . GLY A 1 289 ? -4.445 47.343 28.483 1.00 29.58 ? 282 GLY A CA 1 ATOM 1962 C C . GLY A 1 289 ? -2.934 47.305 28.377 1.00 29.96 ? 282 GLY A C 1 ATOM 1963 O O . GLY A 1 289 ? -2.261 48.277 28.728 1.00 29.07 ? 282 GLY A O 1 ATOM 1964 N N . ILE A 1 290 ? -2.401 46.187 27.895 1.00 31.49 ? 283 ILE A N 1 ATOM 1965 C CA . ILE A 1 290 ? -0.956 46.008 27.772 1.00 31.69 ? 283 ILE A CA 1 ATOM 1966 C C . ILE A 1 290 ? -0.307 47.133 26.967 1.00 32.07 ? 283 ILE A C 1 ATOM 1967 O O . ILE A 1 290 ? 0.768 47.608 27.324 1.00 32.32 ? 283 ILE A O 1 ATOM 1968 C CB A ILE A 1 290 ? -0.636 44.558 27.241 0.65 32.40 ? 283 ILE A CB 1 ATOM 1969 C CB B ILE A 1 290 ? -0.558 44.627 27.155 0.35 31.89 ? 283 ILE A CB 1 ATOM 1970 C CG1 A ILE A 1 290 ? 0.806 44.137 27.534 0.65 33.10 ? 283 ILE A CG1 1 ATOM 1971 C CG1 B ILE A 1 290 ? -0.758 43.492 28.164 0.35 30.93 ? 283 ILE A CG1 1 ATOM 1972 C CG2 A ILE A 1 290 ? -1.054 44.375 25.771 0.65 34.35 ? 283 ILE A CG2 1 ATOM 1973 C CG2 B ILE A 1 290 ? 0.899 44.641 26.642 0.35 31.02 ? 283 ILE A CG2 1 ATOM 1974 C CD1 A ILE A 1 290 ? 1.000 43.703 28.988 0.65 30.66 ? 283 ILE A CD1 1 ATOM 1975 C CD1 B ILE A 1 290 ? 0.229 43.493 29.319 0.35 29.38 ? 283 ILE A CD1 1 ATOM 1976 N N . ALA A 1 291 ? -0.976 47.610 25.917 1.00 32.95 ? 284 ALA A N 1 ATOM 1977 C CA . ALA A 1 291 ? -0.414 48.703 25.106 1.00 33.65 ? 284 ALA A CA 1 ATOM 1978 C C . ALA A 1 291 ? -0.236 50.032 25.854 1.00 33.04 ? 284 ALA A C 1 ATOM 1979 O O . ALA A 1 291 ? 0.591 50.869 25.447 1.00 33.97 ? 284 ALA A O 1 ATOM 1980 C CB . ALA A 1 291 ? -1.259 48.909 23.833 1.00 35.08 ? 284 ALA A CB 1 ATOM 1981 N N A GLU A 1 292 ? -0.990 50.223 26.937 0.80 32.08 ? 285 GLU A N 1 ATOM 1982 N N B GLU A 1 292 ? -1.026 50.239 26.914 0.20 31.99 ? 285 GLU A N 1 ATOM 1983 C CA A GLU A 1 292 ? -0.894 51.442 27.739 0.80 30.91 ? 285 GLU A CA 1 ATOM 1984 C CA B GLU A 1 292 ? -0.942 51.440 27.769 0.20 30.71 ? 285 GLU A CA 1 ATOM 1985 C C A GLU A 1 292 ? -0.181 51.200 29.083 0.80 29.40 ? 285 GLU A C 1 ATOM 1986 C C B GLU A 1 292 ? -0.167 51.210 29.068 0.20 29.34 ? 285 GLU A C 1 ATOM 1987 O O A GLU A 1 292 ? -0.082 52.108 29.911 0.80 29.75 ? 285 GLU A O 1 ATOM 1988 O O B GLU A 1 292 ? -0.010 52.140 29.862 0.20 29.05 ? 285 GLU A O 1 ATOM 1989 C CB A GLU A 1 292 ? -2.286 52.046 27.976 0.80 31.98 ? 285 GLU A CB 1 ATOM 1990 C CB B GLU A 1 292 ? -2.343 51.975 28.117 0.20 31.04 ? 285 GLU A CB 1 ATOM 1991 C CG A GLU A 1 292 ? -2.970 52.616 26.708 0.80 32.95 ? 285 GLU A CG 1 ATOM 1992 C CG B GLU A 1 292 ? -2.650 53.399 27.623 0.20 31.87 ? 285 GLU A CG 1 ATOM 1993 C CD A GLU A 1 292 ? -3.462 51.541 25.736 0.80 39.18 ? 285 GLU A CD 1 ATOM 1994 C CD B GLU A 1 292 ? -2.825 54.422 28.754 0.20 32.53 ? 285 GLU A CD 1 ATOM 1995 O OE1 A GLU A 1 292 ? -4.007 50.502 26.177 0.80 40.12 ? 285 GLU A OE1 1 ATOM 1996 O OE1 B GLU A 1 292 ? -3.422 54.081 29.804 0.20 32.39 ? 285 GLU A OE1 1 ATOM 1997 O OE2 A GLU A 1 292 ? -3.287 51.732 24.510 0.80 42.21 ? 285 GLU A OE2 1 ATOM 1998 O OE2 B GLU A 1 292 ? -2.390 55.583 28.583 0.20 31.82 ? 285 GLU A OE2 1 ATOM 1999 N N . ALA A 1 293 ? 0.311 49.984 29.278 1.00 28.08 ? 286 ALA A N 1 ATOM 2000 C CA . ALA A 1 293 ? 1.011 49.613 30.517 1.00 27.51 ? 286 ALA A CA 1 ATOM 2001 C C . ALA A 1 293 ? 2.245 50.502 30.717 1.00 26.77 ? 286 ALA A C 1 ATOM 2002 O O . ALA A 1 293 ? 2.809 51.068 29.743 1.00 26.87 ? 286 ALA A O 1 ATOM 2003 C CB . ALA A 1 293 ? 1.395 48.170 30.491 1.00 26.69 ? 286 ALA A CB 1 ATOM 2004 N N . VAL A 1 294 ? 2.634 50.677 31.971 1.00 23.94 ? 287 VAL A N 1 ATOM 2005 C CA . VAL A 1 294 ? 3.804 51.493 32.250 1.00 23.56 ? 287 VAL A CA 1 ATOM 2006 C C . VAL A 1 294 ? 5.089 50.679 32.154 1.00 23.00 ? 287 VAL A C 1 ATOM 2007 O O . VAL A 1 294 ? 5.193 49.599 32.758 1.00 22.64 ? 287 VAL A O 1 ATOM 2008 C CB . VAL A 1 294 ? 3.743 52.151 33.651 1.00 23.30 ? 287 VAL A CB 1 ATOM 2009 C CG1 . VAL A 1 294 ? 5.018 52.997 33.911 1.00 23.04 ? 287 VAL A CG1 1 ATOM 2010 C CG2 . VAL A 1 294 ? 2.489 53.045 33.758 1.00 24.76 ? 287 VAL A CG2 1 ATOM 2011 N N . GLY A 1 295 ? 6.053 51.183 31.378 1.00 22.51 ? 288 GLY A N 1 ATOM 2012 C CA . GLY A 1 295 ? 7.436 50.709 31.551 1.00 21.94 ? 288 GLY A CA 1 ATOM 2013 C C . GLY A 1 295 ? 7.890 49.494 30.762 1.00 21.79 ? 288 GLY A C 1 ATOM 2014 O O . GLY A 1 295 ? 9.024 49.100 30.917 1.00 21.90 ? 288 GLY A O 1 ATOM 2015 N N . LEU A 1 296 ? 7.011 48.910 29.942 1.00 21.60 ? 289 LEU A N 1 ATOM 2016 C CA . LEU A 1 296 ? 7.386 47.685 29.204 1.00 21.85 ? 289 LEU A CA 1 ATOM 2017 C C . LEU A 1 296 ? 8.334 47.978 28.041 1.00 22.90 ? 289 LEU A C 1 ATOM 2018 O O . LEU A 1 296 ? 8.160 48.978 27.329 1.00 23.80 ? 289 LEU A O 1 ATOM 2019 C CB A LEU A 1 296 ? 6.116 46.993 28.663 0.65 22.07 ? 289 LEU A CB 1 ATOM 2020 C CB B LEU A 1 296 ? 6.155 46.912 28.713 0.35 22.47 ? 289 LEU A CB 1 ATOM 2021 C CG A LEU A 1 296 ? 5.012 46.617 29.671 0.65 21.90 ? 289 LEU A CG 1 ATOM 2022 C CG B LEU A 1 296 ? 5.671 45.808 29.662 0.35 23.49 ? 289 LEU A CG 1 ATOM 2023 C CD1 A LEU A 1 296 ? 3.858 45.982 28.898 0.65 21.23 ? 289 LEU A CD1 1 ATOM 2024 C CD1 B LEU A 1 296 ? 5.174 46.383 31.007 0.35 22.40 ? 289 LEU A CD1 1 ATOM 2025 C CD2 A LEU A 1 296 ? 5.566 45.625 30.738 0.65 23.79 ? 289 LEU A CD2 1 ATOM 2026 C CD2 B LEU A 1 296 ? 4.580 44.992 28.974 0.35 23.87 ? 289 LEU A CD2 1 ATOM 2027 N N . PRO A 1 297 ? 9.310 47.094 27.820 1.00 23.83 ? 290 PRO A N 1 ATOM 2028 C CA . PRO A 1 297 ? 10.221 47.247 26.694 1.00 24.85 ? 290 PRO A CA 1 ATOM 2029 C C . PRO A 1 297 ? 9.516 46.876 25.385 1.00 25.89 ? 290 PRO A C 1 ATOM 2030 O O . PRO A 1 297 ? 8.583 46.045 25.391 1.00 25.71 ? 290 PRO A O 1 ATOM 2031 C CB . PRO A 1 297 ? 11.349 46.251 27.016 1.00 25.32 ? 290 PRO A CB 1 ATOM 2032 C CG . PRO A 1 297 ? 10.704 45.203 27.903 1.00 25.76 ? 290 PRO A CG 1 ATOM 2033 C CD . PRO A 1 297 ? 9.592 45.898 28.645 1.00 24.21 ? 290 PRO A CD 1 ATOM 2034 N N A SER A 1 298 ? 9.970 47.494 24.295 0.60 26.02 ? 291 SER A N 1 ATOM 2035 N N B SER A 1 298 ? 9.945 47.467 24.271 0.40 26.00 ? 291 SER A N 1 ATOM 2036 C CA A SER A 1 298 ? 9.354 47.297 22.979 0.60 26.95 ? 291 SER A CA 1 ATOM 2037 C CA B SER A 1 298 ? 9.302 47.182 22.978 0.40 26.68 ? 291 SER A CA 1 ATOM 2038 C C A SER A 1 298 ? 10.076 46.255 22.119 0.60 26.98 ? 291 SER A C 1 ATOM 2039 C C B SER A 1 298 ? 10.153 46.344 22.037 0.40 26.79 ? 291 SER A C 1 ATOM 2040 O O A SER A 1 298 ? 9.557 45.847 21.078 0.60 27.98 ? 291 SER A O 1 ATOM 2041 O O B SER A 1 298 ? 9.822 46.185 20.854 0.40 27.14 ? 291 SER A O 1 ATOM 2042 C CB A SER A 1 298 ? 9.241 48.638 22.236 0.60 28.22 ? 291 SER A CB 1 ATOM 2043 C CB B SER A 1 298 ? 8.892 48.473 22.288 0.40 27.64 ? 291 SER A CB 1 ATOM 2044 O OG A SER A 1 298 ? 10.510 49.178 21.914 0.60 29.53 ? 291 SER A OG 1 ATOM 2045 O OG B SER A 1 298 ? 8.078 49.232 23.149 0.40 28.23 ? 291 SER A OG 1 ATOM 2046 N N . ILE A 1 299 ? 11.265 45.839 22.553 1.00 26.29 ? 292 ILE A N 1 ATOM 2047 C CA . ILE A 1 299 ? 12.146 44.952 21.760 1.00 26.15 ? 292 ILE A CA 1 ATOM 2048 C C . ILE A 1 299 ? 12.559 43.766 22.621 1.00 25.46 ? 292 ILE A C 1 ATOM 2049 O O . ILE A 1 299 ? 12.653 43.899 23.836 1.00 25.62 ? 292 ILE A O 1 ATOM 2050 C CB . ILE A 1 299 ? 13.408 45.698 21.162 1.00 26.33 ? 292 ILE A CB 1 ATOM 2051 C CG1 . ILE A 1 299 ? 14.292 46.330 22.260 1.00 25.72 ? 292 ILE A CG1 1 ATOM 2052 C CG2 . ILE A 1 299 ? 12.973 46.734 20.122 1.00 28.09 ? 292 ILE A CG2 1 ATOM 2053 C CD1 . ILE A 1 299 ? 15.485 47.105 21.704 1.00 27.31 ? 292 ILE A CD1 1 ATOM 2054 N N . PRO A 1 300 ? 12.772 42.587 22.009 1.00 25.93 ? 293 PRO A N 1 ATOM 2055 C CA . PRO A 1 300 ? 13.134 41.412 22.819 1.00 25.50 ? 293 PRO A CA 1 ATOM 2056 C C . PRO A 1 300 ? 14.527 41.548 23.430 1.00 24.98 ? 293 PRO A C 1 ATOM 2057 O O . PRO A 1 300 ? 15.414 42.164 22.813 1.00 25.24 ? 293 PRO A O 1 ATOM 2058 C CB . PRO A 1 300 ? 13.170 40.279 21.780 1.00 25.89 ? 293 PRO A CB 1 ATOM 2059 C CG . PRO A 1 300 ? 12.265 40.767 20.673 1.00 28.61 ? 293 PRO A CG 1 ATOM 2060 C CD . PRO A 1 300 ? 12.579 42.234 20.592 1.00 26.62 ? 293 PRO A CD 1 ATOM 2061 N N . VAL A 1 301 ? 14.711 40.967 24.620 1.00 23.76 ? 294 VAL A N 1 ATOM 2062 C CA . VAL A 1 301 ? 15.957 41.078 25.371 1.00 23.16 ? 294 VAL A CA 1 ATOM 2063 C C . VAL A 1 301 ? 16.216 39.732 26.044 1.00 23.10 ? 294 VAL A C 1 ATOM 2064 O O . VAL A 1 301 ? 15.276 39.078 26.501 1.00 23.36 ? 294 VAL A O 1 ATOM 2065 C CB . VAL A 1 301 ? 15.815 42.156 26.474 1.00 22.49 ? 294 VAL A CB 1 ATOM 2066 C CG1 . VAL A 1 301 ? 17.104 42.283 27.287 1.00 22.08 ? 294 VAL A CG1 1 ATOM 2067 C CG2 . VAL A 1 301 ? 15.448 43.498 25.853 1.00 23.62 ? 294 VAL A CG2 1 ATOM 2068 N N . HIS A 1 302 ? 17.484 39.324 26.123 1.00 23.56 ? 295 HIS A N 1 ATOM 2069 C CA . HIS A 1 302 ? 17.829 38.063 26.765 1.00 22.55 ? 295 HIS A CA 1 ATOM 2070 C C . HIS A 1 302 ? 19.244 38.132 27.334 1.00 23.22 ? 295 HIS A C 1 ATOM 2071 O O . HIS A 1 302 ? 20.118 38.735 26.699 1.00 24.29 ? 295 HIS A O 1 ATOM 2072 C CB . HIS A 1 302 ? 17.721 36.928 25.728 1.00 23.84 ? 295 HIS A CB 1 ATOM 2073 C CG . HIS A 1 302 ? 17.777 35.554 26.320 1.00 24.01 ? 295 HIS A CG 1 ATOM 2074 N ND1 . HIS A 1 302 ? 16.807 35.079 27.172 1.00 23.15 ? 295 HIS A ND1 1 ATOM 2075 C CD2 . HIS A 1 302 ? 18.689 34.556 26.185 1.00 24.77 ? 295 HIS A CD2 1 ATOM 2076 C CE1 . HIS A 1 302 ? 17.108 33.846 27.535 1.00 24.80 ? 295 HIS A CE1 1 ATOM 2077 N NE2 . HIS A 1 302 ? 18.248 33.506 26.958 1.00 24.67 ? 295 HIS A NE2 1 ATOM 2078 N N . PRO A 1 303 ? 19.476 37.550 28.540 1.00 22.93 ? 296 PRO A N 1 ATOM 2079 C CA . PRO A 1 303 ? 20.821 37.587 29.124 1.00 22.45 ? 296 PRO A CA 1 ATOM 2080 C C . PRO A 1 303 ? 21.551 36.259 28.902 1.00 23.04 ? 296 PRO A C 1 ATOM 2081 O O . PRO A 1 303 ? 20.908 35.194 28.875 1.00 23.93 ? 296 PRO A O 1 ATOM 2082 C CB . PRO A 1 303 ? 20.546 37.775 30.629 1.00 22.57 ? 296 PRO A CB 1 ATOM 2083 C CG . PRO A 1 303 ? 19.216 37.029 30.857 1.00 21.89 ? 296 PRO A CG 1 ATOM 2084 C CD . PRO A 1 303 ? 18.486 36.988 29.490 1.00 22.51 ? 296 PRO A CD 1 ATOM 2085 N N . ILE A 1 304 ? 22.876 36.337 28.775 1.00 23.93 ? 297 ILE A N 1 ATOM 2086 C CA . ILE A 1 304 ? 23.718 35.137 28.593 1.00 24.62 ? 297 ILE A CA 1 ATOM 2087 C C . ILE A 1 304 ? 25.001 35.262 29.438 1.00 24.48 ? 297 ILE A C 1 ATOM 2088 O O . ILE A 1 304 ? 25.365 36.365 29.908 1.00 24.72 ? 297 ILE A O 1 ATOM 2089 C CB . ILE A 1 304 ? 24.101 34.923 27.115 1.00 25.18 ? 297 ILE A CB 1 ATOM 2090 C CG1 . ILE A 1 304 ? 24.948 36.097 26.586 1.00 26.46 ? 297 ILE A CG1 1 ATOM 2091 C CG2 . ILE A 1 304 ? 22.851 34.658 26.242 1.00 26.23 ? 297 ILE A CG2 1 ATOM 2092 C CD1 . ILE A 1 304 ? 25.415 35.909 25.135 1.00 26.67 ? 297 ILE A CD1 1 ATOM 2093 N N . GLY A 1 305 ? 25.694 34.135 29.594 1.00 25.60 ? 298 GLY A N 1 ATOM 2094 C CA . GLY A 1 305 ? 26.973 34.108 30.287 1.00 24.82 ? 298 GLY A CA 1 ATOM 2095 C C . GLY A 1 305 ? 28.136 34.331 29.331 1.00 25.87 ? 298 GLY A C 1 ATOM 2096 O O . GLY A 1 305 ? 27.949 34.514 28.115 1.00 25.88 ? 298 GLY A O 1 ATOM 2097 N N . TYR A 1 306 ? 29.343 34.375 29.884 1.00 25.47 ? 299 TYR A N 1 ATOM 2098 C CA . TYR A 1 306 ? 30.476 34.778 29.052 1.00 26.98 ? 299 TYR A CA 1 ATOM 2099 C C . TYR A 1 306 ? 31.011 33.682 28.121 1.00 28.12 ? 299 TYR A C 1 ATOM 2100 O O . TYR A 1 306 ? 31.646 33.996 27.115 1.00 29.59 ? 299 TYR A O 1 ATOM 2101 C CB . TYR A 1 306 ? 31.598 35.467 29.852 1.00 27.11 ? 299 TYR A CB 1 ATOM 2102 C CG . TYR A 1 306 ? 32.210 34.727 31.035 1.00 26.93 ? 299 TYR A CG 1 ATOM 2103 C CD1 . TYR A 1 306 ? 31.774 34.995 32.344 1.00 27.11 ? 299 TYR A CD1 1 ATOM 2104 C CD2 . TYR A 1 306 ? 33.282 33.836 30.860 1.00 29.40 ? 299 TYR A CD2 1 ATOM 2105 C CE1 . TYR A 1 306 ? 32.337 34.364 33.443 1.00 28.56 ? 299 TYR A CE1 1 ATOM 2106 C CE2 . TYR A 1 306 ? 33.867 33.200 31.960 1.00 29.71 ? 299 TYR A CE2 1 ATOM 2107 C CZ . TYR A 1 306 ? 33.393 33.475 33.250 1.00 28.98 ? 299 TYR A CZ 1 ATOM 2108 O OH . TYR A 1 306 ? 33.951 32.833 34.343 1.00 27.81 ? 299 TYR A OH 1 ATOM 2109 N N . TYR A 1 307 ? 30.756 32.413 28.430 1.00 28.71 ? 300 TYR A N 1 ATOM 2110 C CA . TYR A 1 307 ? 31.052 31.363 27.428 1.00 29.59 ? 300 TYR A CA 1 ATOM 2111 C C . TYR A 1 307 ? 30.263 31.601 26.141 1.00 29.97 ? 300 TYR A C 1 ATOM 2112 O O . TYR A 1 307 ? 30.832 31.542 25.031 1.00 31.69 ? 300 TYR A O 1 ATOM 2113 C CB . TYR A 1 307 ? 30.735 29.960 27.943 1.00 29.65 ? 300 TYR A CB 1 ATOM 2114 C CG . TYR A 1 307 ? 31.669 29.408 28.988 1.00 30.67 ? 300 TYR A CG 1 ATOM 2115 C CD1 . TYR A 1 307 ? 32.969 29.920 29.159 1.00 32.86 ? 300 TYR A CD1 1 ATOM 2116 C CD2 . TYR A 1 307 ? 31.265 28.343 29.800 1.00 31.07 ? 300 TYR A CD2 1 ATOM 2117 C CE1 . TYR A 1 307 ? 33.828 29.393 30.124 1.00 32.72 ? 300 TYR A CE1 1 ATOM 2118 C CE2 . TYR A 1 307 ? 32.125 27.802 30.764 1.00 31.61 ? 300 TYR A CE2 1 ATOM 2119 C CZ . TYR A 1 307 ? 33.403 28.327 30.913 1.00 34.49 ? 300 TYR A CZ 1 ATOM 2120 O OH . TYR A 1 307 ? 34.248 27.779 31.860 1.00 35.25 ? 300 TYR A OH 1 ATOM 2121 N N . ASP A 1 308 ? 28.961 31.866 26.287 1.00 29.23 ? 301 ASP A N 1 ATOM 2122 C CA . ASP A 1 308 ? 28.096 32.143 25.135 1.00 29.88 ? 301 ASP A CA 1 ATOM 2123 C C . ASP A 1 308 ? 28.404 33.493 24.487 1.00 30.03 ? 301 ASP A C 1 ATOM 2124 O O . ASP A 1 308 ? 28.375 33.619 23.248 1.00 30.98 ? 301 ASP A O 1 ATOM 2125 C CB . ASP A 1 308 ? 26.621 32.089 25.539 1.00 29.17 ? 301 ASP A CB 1 ATOM 2126 C CG . ASP A 1 308 ? 26.108 30.663 25.713 1.00 29.49 ? 301 ASP A CG 1 ATOM 2127 O OD1 . ASP A 1 308 ? 26.730 29.716 25.197 1.00 31.87 ? 301 ASP A OD1 1 ATOM 2128 O OD2 . ASP A 1 308 ? 25.062 30.482 26.374 1.00 28.71 ? 301 ASP A OD2 1 ATOM 2129 N N . ALA A 1 309 ? 28.688 34.510 25.312 1.00 29.47 ? 302 ALA A N 1 ATOM 2130 C CA . ALA A 1 309 ? 29.073 35.823 24.779 1.00 29.41 ? 302 ALA A CA 1 ATOM 2131 C C . ALA A 1 309 ? 30.320 35.740 23.905 1.00 30.61 ? 302 ALA A C 1 ATOM 2132 O O . ALA A 1 309 ? 30.403 36.424 22.881 1.00 31.51 ? 302 ALA A O 1 ATOM 2133 C CB . ALA A 1 309 ? 29.288 36.822 25.891 1.00 28.80 ? 302 ALA A CB 1 ATOM 2134 N N A GLN A 1 310 ? 31.339 35.025 24.371 0.80 30.43 ? 303 GLN A N 1 ATOM 2135 N N B GLN A 1 310 ? 31.228 34.833 24.265 0.20 30.56 ? 303 GLN A N 1 ATOM 2136 C CA A GLN A 1 310 ? 32.588 34.947 23.611 0.80 32.23 ? 303 GLN A CA 1 ATOM 2137 C CA B GLN A 1 310 ? 32.376 34.483 23.424 0.20 31.35 ? 303 GLN A CA 1 ATOM 2138 C C A GLN A 1 310 ? 32.313 34.461 22.174 0.80 32.72 ? 303 GLN A C 1 ATOM 2139 C C B GLN A 1 310 ? 31.973 34.035 22.010 0.20 32.07 ? 303 GLN A C 1 ATOM 2140 O O A GLN A 1 310 ? 32.908 34.934 21.190 0.80 33.42 ? 303 GLN A O 1 ATOM 2141 O O B GLN A 1 310 ? 32.497 34.552 21.023 0.20 32.55 ? 303 GLN A O 1 ATOM 2142 C CB A GLN A 1 310 ? 33.592 34.036 24.303 0.80 32.05 ? 303 GLN A CB 1 ATOM 2143 C CB B GLN A 1 310 ? 33.223 33.397 24.087 0.20 31.36 ? 303 GLN A CB 1 ATOM 2144 C CG A GLN A 1 310 ? 34.782 33.644 23.364 0.80 37.01 ? 303 GLN A CG 1 ATOM 2145 C CG B GLN A 1 310 ? 34.623 33.263 23.499 0.20 32.03 ? 303 GLN A CG 1 ATOM 2146 C CD A GLN A 1 310 ? 36.115 33.600 24.078 0.80 41.64 ? 303 GLN A CD 1 ATOM 2147 C CD B GLN A 1 310 ? 35.660 33.969 24.347 0.20 30.67 ? 303 GLN A CD 1 ATOM 2148 O OE1 A GLN A 1 310 ? 36.081 33.698 25.407 0.80 42.40 ? 303 GLN A OE1 1 ATOM 2149 O OE1 B GLN A 1 310 ? 36.147 35.041 23.996 0.20 29.15 ? 303 GLN A OE1 1 ATOM 2150 N NE2 A GLN A 1 310 ? 37.174 33.479 23.442 0.80 44.10 ? 303 GLN A NE2 1 ATOM 2151 N NE2 B GLN A 1 310 ? 35.984 33.376 25.489 0.20 30.63 ? 303 GLN A NE2 1 ATOM 2152 N N A LYS A 1 311 ? 31.388 33.509 22.061 0.60 32.37 ? 304 LYS A N 1 ATOM 2153 N N B LYS A 1 311 ? 31.048 33.081 21.900 0.40 32.06 ? 304 LYS A N 1 ATOM 2154 C CA A LYS A 1 311 ? 31.026 32.929 20.774 0.60 33.19 ? 304 LYS A CA 1 ATOM 2155 C CA B LYS A 1 311 ? 30.648 32.618 20.580 0.40 33.10 ? 304 LYS A CA 1 ATOM 2156 C C A LYS A 1 311 ? 30.361 33.979 19.884 0.60 33.35 ? 304 LYS A C 1 ATOM 2157 C C B LYS A 1 311 ? 29.920 33.703 19.781 0.40 33.22 ? 304 LYS A C 1 ATOM 2158 O O A LYS A 1 311 ? 30.672 34.089 18.710 0.60 33.47 ? 304 LYS A O 1 ATOM 2159 O O B LYS A 1 311 ? 29.795 33.581 18.561 0.40 33.38 ? 304 LYS A O 1 ATOM 2160 C CB A LYS A 1 311 ? 30.117 31.706 20.964 0.60 33.35 ? 304 LYS A CB 1 ATOM 2161 C CB B LYS A 1 311 ? 29.825 31.343 20.686 0.40 33.40 ? 304 LYS A CB 1 ATOM 2162 C CG A LYS A 1 311 ? 30.727 30.558 21.797 0.60 33.97 ? 304 LYS A CG 1 ATOM 2163 C CG B LYS A 1 311 ? 30.619 30.167 21.233 0.40 34.60 ? 304 LYS A CG 1 ATOM 2164 C CD A LYS A 1 311 ? 31.941 29.909 21.116 0.60 38.44 ? 304 LYS A CD 1 ATOM 2165 C CD B LYS A 1 311 ? 31.862 29.906 20.378 0.40 37.42 ? 304 LYS A CD 1 ATOM 2166 C CE A LYS A 1 311 ? 31.520 29.052 19.938 0.60 39.36 ? 304 LYS A CE 1 ATOM 2167 C CE B LYS A 1 311 ? 32.918 29.136 21.159 0.40 39.37 ? 304 LYS A CE 1 ATOM 2168 N NZ A LYS A 1 311 ? 32.689 28.693 19.083 0.60 43.27 ? 304 LYS A NZ 1 ATOM 2169 N NZ B LYS A 1 311 ? 32.761 27.660 21.030 0.40 42.73 ? 304 LYS A NZ 1 ATOM 2170 N N . LEU A 1 312 ? 29.449 34.758 20.458 1.00 31.99 ? 305 LEU A N 1 ATOM 2171 C CA . LEU A 1 312 ? 28.816 35.880 19.746 1.00 33.35 ? 305 LEU A CA 1 ATOM 2172 C C . LEU A 1 312 ? 29.759 37.030 19.380 1.00 34.36 ? 305 LEU A C 1 ATOM 2173 O O . LEU A 1 312 ? 29.594 37.636 18.312 1.00 36.11 ? 305 LEU A O 1 ATOM 2174 C CB . LEU A 1 312 ? 27.606 36.421 20.527 1.00 31.32 ? 305 LEU A CB 1 ATOM 2175 C CG . LEU A 1 312 ? 26.471 35.413 20.789 1.00 32.68 ? 305 LEU A CG 1 ATOM 2176 C CD1 . LEU A 1 312 ? 25.307 36.112 21.518 1.00 31.39 ? 305 LEU A CD1 1 ATOM 2177 C CD2 . LEU A 1 312 ? 25.962 34.756 19.515 1.00 34.17 ? 305 LEU A CD2 1 ATOM 2178 N N . LEU A 1 313 ? 30.732 37.328 20.246 1.00 33.62 ? 306 LEU A N 1 ATOM 2179 C CA . LEU A 1 313 ? 31.632 38.462 20.029 1.00 34.07 ? 306 LEU A CA 1 ATOM 2180 C C . LEU A 1 313 ? 32.838 38.146 19.158 1.00 35.64 ? 306 LEU A C 1 ATOM 2181 O O . LEU A 1 313 ? 33.405 39.048 18.539 1.00 35.72 ? 306 LEU A O 1 ATOM 2182 C CB . LEU A 1 313 ? 32.149 39.001 21.345 1.00 32.93 ? 306 LEU A CB 1 ATOM 2183 C CG . LEU A 1 313 ? 31.050 39.550 22.272 1.00 32.17 ? 306 LEU A CG 1 ATOM 2184 C CD1 . LEU A 1 313 ? 31.635 39.848 23.650 1.00 31.63 ? 306 LEU A CD1 1 ATOM 2185 C CD2 . LEU A 1 313 ? 30.351 40.786 21.683 1.00 31.44 ? 306 LEU A CD2 1 ATOM 2186 N N . GLU A 1 314 ? 33.244 36.884 19.143 1.00 36.65 ? 307 GLU A N 1 ATOM 2187 C CA . GLU A 1 314 ? 34.515 36.523 18.500 1.00 37.99 ? 307 GLU A CA 1 ATOM 2188 C C . GLU A 1 314 ? 34.564 36.811 16.998 1.00 39.57 ? 307 GLU A C 1 ATOM 2189 O O . GLU A 1 314 ? 35.635 37.110 16.459 1.00 39.64 ? 307 GLU A O 1 ATOM 2190 C CB . GLU A 1 314 ? 34.892 35.081 18.825 1.00 38.58 ? 307 GLU A CB 1 ATOM 2191 C CG . GLU A 1 314 ? 34.078 34.024 18.131 1.00 40.80 ? 307 GLU A CG 1 ATOM 2192 C CD . GLU A 1 314 ? 34.422 32.627 18.614 1.00 43.42 ? 307 GLU A CD 1 ATOM 2193 O OE1 . GLU A 1 314 ? 35.325 32.490 19.477 1.00 45.07 ? 307 GLU A OE1 1 ATOM 2194 O OE2 . GLU A 1 314 ? 33.789 31.665 18.120 1.00 43.50 ? 307 GLU A OE2 1 ATOM 2195 N N . LYS A 1 315 ? 33.411 36.745 16.336 1.00 39.42 ? 308 LYS A N 1 ATOM 2196 C CA . LYS A 1 315 ? 33.358 36.974 14.900 1.00 41.07 ? 308 LYS A CA 1 ATOM 2197 C C . LYS A 1 315 ? 33.109 38.430 14.536 1.00 40.76 ? 308 LYS A C 1 ATOM 2198 O O . LYS A 1 315 ? 33.063 38.760 13.359 1.00 41.58 ? 308 LYS A O 1 ATOM 2199 C CB . LYS A 1 315 ? 32.284 36.088 14.253 1.00 41.18 ? 308 LYS A CB 1 ATOM 2200 C CG . LYS A 1 315 ? 32.708 34.636 14.077 1.00 43.98 ? 308 LYS A CG 1 ATOM 2201 C CD . LYS A 1 315 ? 31.504 33.748 13.830 1.00 45.21 ? 308 LYS A CD 1 ATOM 2202 C CE . LYS A 1 315 ? 31.960 32.331 13.511 1.00 46.79 ? 308 LYS A CE 1 ATOM 2203 N NZ . LYS A 1 315 ? 30.800 31.462 13.221 1.00 47.68 ? 308 LYS A NZ 1 ATOM 2204 N N . MET A 1 316 ? 32.934 39.301 15.536 1.00 38.86 ? 309 MET A N 1 ATOM 2205 C CA . MET A 1 316 ? 32.611 40.704 15.247 1.00 39.10 ? 309 MET A CA 1 ATOM 2206 C C . MET A 1 316 ? 33.645 41.474 14.407 1.00 40.13 ? 309 MET A C 1 ATOM 2207 O O . MET A 1 316 ? 34.850 41.391 14.649 1.00 39.71 ? 309 MET A O 1 ATOM 2208 C CB . MET A 1 316 ? 32.286 41.450 16.528 1.00 38.08 ? 309 MET A CB 1 ATOM 2209 C CG A MET A 1 316 ? 30.983 40.863 17.079 0.50 37.27 ? 309 MET A CG 1 ATOM 2210 C CG B MET A 1 316 ? 31.065 40.984 17.264 0.50 38.61 ? 309 MET A CG 1 ATOM 2211 S SD A MET A 1 316 ? 29.955 41.903 18.102 0.50 35.14 ? 309 MET A SD 1 ATOM 2212 S SD B MET A 1 316 ? 29.616 41.647 16.483 0.50 40.38 ? 309 MET A SD 1 ATOM 2213 C CE A MET A 1 316 ? 29.619 43.290 17.007 0.50 36.73 ? 309 MET A CE 1 ATOM 2214 C CE B MET A 1 316 ? 29.848 43.417 16.671 0.50 39.86 ? 309 MET A CE 1 ATOM 2215 N N . GLY A 1 317 ? 33.129 42.237 13.445 1.00 40.93 ? 310 GLY A N 1 ATOM 2216 C CA . GLY A 1 317 ? 33.945 43.049 12.542 1.00 42.26 ? 310 GLY A CA 1 ATOM 2217 C C . GLY A 1 317 ? 33.575 44.517 12.634 1.00 42.74 ? 310 GLY A C 1 ATOM 2218 O O . GLY A 1 317 ? 33.281 45.029 13.720 1.00 41.62 ? 310 GLY A O 1 ATOM 2219 N N . GLY A 1 318 ? 33.581 45.202 11.491 1.00 43.57 ? 311 GLY A N 1 ATOM 2220 C CA . GLY A 1 318 ? 33.351 46.645 11.467 1.00 43.43 ? 311 GLY A CA 1 ATOM 2221 C C . GLY A 1 318 ? 34.437 47.385 12.236 1.00 43.95 ? 311 GLY A C 1 ATOM 2222 O O . GLY A 1 318 ? 35.606 46.970 12.240 1.00 44.25 ? 311 GLY A O 1 ATOM 2223 N N . SER A 1 319 ? 34.035 48.459 12.912 1.00 43.23 ? 312 SER A N 1 ATOM 2224 C CA . SER A 1 319 ? 34.951 49.358 13.609 1.00 44.09 ? 312 SER A CA 1 ATOM 2225 C C . SER A 1 319 ? 35.615 48.752 14.850 1.00 43.52 ? 312 SER A C 1 ATOM 2226 O O . SER A 1 319 ? 34.992 47.982 15.591 1.00 43.39 ? 312 SER A O 1 ATOM 2227 C CB . SER A 1 319 ? 34.209 50.651 13.983 1.00 43.92 ? 312 SER A CB 1 ATOM 2228 O OG . SER A 1 319 ? 33.763 51.343 12.812 1.00 45.76 ? 312 SER A OG 1 ATOM 2229 N N . ALA A 1 320 ? 36.885 49.090 15.068 1.00 44.08 ? 313 ALA A N 1 ATOM 2230 C CA . ALA A 1 320 ? 37.582 48.733 16.310 1.00 43.27 ? 313 ALA A CA 1 ATOM 2231 C C . ALA A 1 320 ? 36.869 49.393 17.504 1.00 41.96 ? 313 ALA A C 1 ATOM 2232 O O . ALA A 1 320 ? 36.179 50.399 17.308 1.00 41.29 ? 313 ALA A O 1 ATOM 2233 C CB . ALA A 1 320 ? 39.029 49.202 16.253 1.00 44.35 ? 313 ALA A CB 1 ATOM 2234 N N . PRO A 1 321 ? 37.055 48.858 18.738 1.00 41.15 ? 314 PRO A N 1 ATOM 2235 C CA . PRO A 1 321 ? 36.541 49.620 19.898 1.00 40.68 ? 314 PRO A CA 1 ATOM 2236 C C . PRO A 1 321 ? 37.253 50.980 19.940 1.00 41.34 ? 314 PRO A C 1 ATOM 2237 O O . PRO A 1 321 ? 38.423 51.060 19.549 1.00 42.27 ? 314 PRO A O 1 ATOM 2238 C CB . PRO A 1 321 ? 36.937 48.757 21.107 1.00 40.07 ? 314 PRO A CB 1 ATOM 2239 C CG . PRO A 1 321 ? 38.091 47.899 20.610 1.00 40.52 ? 314 PRO A CG 1 ATOM 2240 C CD . PRO A 1 321 ? 37.812 47.656 19.149 1.00 41.69 ? 314 PRO A CD 1 ATOM 2241 N N . PRO A 1 322 ? 36.548 52.044 20.369 1.00 40.96 ? 315 PRO A N 1 ATOM 2242 C CA . PRO A 1 322 ? 37.131 53.397 20.302 1.00 41.89 ? 315 PRO A CA 1 ATOM 2243 C C . PRO A 1 322 ? 38.304 53.612 21.261 1.00 42.44 ? 315 PRO A C 1 ATOM 2244 O O . PRO A 1 322 ? 39.160 54.471 21.012 1.00 43.13 ? 315 PRO A O 1 ATOM 2245 C CB . PRO A 1 322 ? 35.950 54.307 20.674 1.00 40.39 ? 315 PRO A CB 1 ATOM 2246 C CG . PRO A 1 322 ? 35.047 53.425 21.503 1.00 39.13 ? 315 PRO A CG 1 ATOM 2247 C CD . PRO A 1 322 ? 35.151 52.073 20.846 1.00 39.63 ? 315 PRO A CD 1 ATOM 2248 N N . ASP A 1 323 ? 38.327 52.855 22.354 1.00 42.09 ? 316 ASP A N 1 ATOM 2249 C CA . ASP A 1 323 ? 39.398 52.937 23.356 1.00 42.94 ? 316 ASP A CA 1 ATOM 2250 C C . ASP A 1 323 ? 39.301 51.764 24.338 1.00 42.66 ? 316 ASP A C 1 ATOM 2251 O O . ASP A 1 323 ? 38.349 50.966 24.270 1.00 41.68 ? 316 ASP A O 1 ATOM 2252 C CB . ASP A 1 323 ? 39.401 54.305 24.090 1.00 43.04 ? 316 ASP A CB 1 ATOM 2253 C CG . ASP A 1 323 ? 38.151 54.544 24.939 1.00 42.93 ? 316 ASP A CG 1 ATOM 2254 O OD1 . ASP A 1 323 ? 37.878 53.746 25.857 1.00 43.73 ? 316 ASP A OD1 1 ATOM 2255 O OD2 . ASP A 1 323 ? 37.453 55.560 24.724 1.00 44.52 ? 316 ASP A OD2 1 ATOM 2256 N N . SER A 1 324 ? 40.254 51.681 25.267 1.00 42.98 ? 317 SER A N 1 ATOM 2257 C CA . SER A 1 324 ? 40.344 50.536 26.191 1.00 43.16 ? 317 SER A CA 1 ATOM 2258 C C . SER A 1 324 ? 39.149 50.362 27.151 1.00 41.58 ? 317 SER A C 1 ATOM 2259 O O . SER A 1 324 ? 38.873 49.240 27.600 1.00 41.13 ? 317 SER A O 1 ATOM 2260 C CB . SER A 1 324 ? 41.678 50.561 26.965 1.00 44.17 ? 317 SER A CB 1 ATOM 2261 O OG . SER A 1 324 ? 41.670 51.579 27.954 1.00 45.61 ? 317 SER A OG 1 ATOM 2262 N N . SER A 1 325 ? 38.451 51.456 27.459 1.00 39.92 ? 318 SER A N 1 ATOM 2263 C CA . SER A 1 325 ? 37.273 51.420 28.347 1.00 37.93 ? 318 SER A CA 1 ATOM 2264 C C . SER A 1 325 ? 36.097 50.645 27.737 1.00 36.81 ? 318 SER A C 1 ATOM 2265 O O . SER A 1 325 ? 35.086 50.390 28.416 1.00 36.25 ? 318 SER A O 1 ATOM 2266 C CB . SER A 1 325 ? 36.831 52.839 28.708 1.00 37.74 ? 318 SER A CB 1 ATOM 2267 O OG . SER A 1 325 ? 36.179 53.454 27.609 1.00 37.82 ? 318 SER A OG 1 ATOM 2268 N N . TRP A 1 326 ? 36.232 50.300 26.460 1.00 35.77 ? 319 TRP A N 1 ATOM 2269 C CA . TRP A 1 326 ? 35.244 49.511 25.726 1.00 34.72 ? 319 TRP A CA 1 ATOM 2270 C C . TRP A 1 326 ? 35.607 48.015 25.666 1.00 34.72 ? 319 TRP A C 1 ATOM 2271 O O . TRP A 1 326 ? 34.778 47.195 25.250 1.00 34.09 ? 319 TRP A O 1 ATOM 2272 C CB . TRP A 1 326 ? 35.062 50.079 24.312 1.00 35.33 ? 319 TRP A CB 1 ATOM 2273 C CG . TRP A 1 326 ? 34.072 51.227 24.250 1.00 31.90 ? 319 TRP A CG 1 ATOM 2274 C CD1 . TRP A 1 326 ? 34.166 52.446 24.895 1.00 31.87 ? 319 TRP A CD1 1 ATOM 2275 C CD2 . TRP A 1 326 ? 32.846 51.258 23.513 1.00 31.27 ? 319 TRP A CD2 1 ATOM 2276 N NE1 . TRP A 1 326 ? 33.069 53.223 24.600 1.00 32.63 ? 319 TRP A NE1 1 ATOM 2277 C CE2 . TRP A 1 326 ? 32.237 52.521 23.763 1.00 32.09 ? 319 TRP A CE2 1 ATOM 2278 C CE3 . TRP A 1 326 ? 32.190 50.337 22.676 1.00 29.84 ? 319 TRP A CE3 1 ATOM 2279 C CZ2 . TRP A 1 326 ? 31.004 52.887 23.204 1.00 31.55 ? 319 TRP A CZ2 1 ATOM 2280 C CZ3 . TRP A 1 326 ? 30.969 50.705 22.102 1.00 30.37 ? 319 TRP A CZ3 1 ATOM 2281 C CH2 . TRP A 1 326 ? 30.374 51.967 22.396 1.00 29.85 ? 319 TRP A CH2 1 ATOM 2282 N N A ARG A 1 327 ? 36.819 47.676 26.104 0.50 35.02 ? 320 ARG A N 1 ATOM 2283 N N B ARG A 1 327 ? 36.831 47.671 26.077 0.50 35.03 ? 320 ARG A N 1 ATOM 2284 C CA A ARG A 1 327 ? 37.304 46.295 26.086 0.50 35.47 ? 320 ARG A CA 1 ATOM 2285 C CA B ARG A 1 327 ? 37.309 46.278 26.062 0.50 35.46 ? 320 ARG A CA 1 ATOM 2286 C C A ARG A 1 327 ? 37.126 45.608 27.443 0.50 35.06 ? 320 ARG A C 1 ATOM 2287 C C B ARG A 1 327 ? 37.149 45.595 27.426 0.50 35.07 ? 320 ARG A C 1 ATOM 2288 O O A ARG A 1 327 ? 37.600 46.101 28.465 0.50 34.92 ? 320 ARG A O 1 ATOM 2289 O O B ARG A 1 327 ? 37.659 46.076 28.437 0.50 34.99 ? 320 ARG A O 1 ATOM 2290 C CB A ARG A 1 327 ? 38.781 46.251 25.676 0.50 36.71 ? 320 ARG A CB 1 ATOM 2291 C CB B ARG A 1 327 ? 38.780 46.193 25.611 0.50 36.68 ? 320 ARG A CB 1 ATOM 2292 C CG A ARG A 1 327 ? 39.050 46.740 24.268 0.50 38.67 ? 320 ARG A CG 1 ATOM 2293 C CG B ARG A 1 327 ? 39.008 46.435 24.125 0.50 38.70 ? 320 ARG A CG 1 ATOM 2294 C CD A ARG A 1 327 ? 40.555 46.796 24.003 0.50 43.06 ? 320 ARG A CD 1 ATOM 2295 C CD B ARG A 1 327 ? 40.417 45.991 23.678 0.50 42.74 ? 320 ARG A CD 1 ATOM 2296 N NE A ARG A 1 327 ? 40.887 46.798 22.581 0.50 46.80 ? 320 ARG A NE 1 ATOM 2297 N NE B ARG A 1 327 ? 41.431 46.298 24.687 0.50 45.90 ? 320 ARG A NE 1 ATOM 2298 C CZ A ARG A 1 327 ? 41.384 47.848 21.929 0.50 48.77 ? 320 ARG A CZ 1 ATOM 2299 C CZ B ARG A 1 327 ? 42.114 47.440 24.754 0.50 48.44 ? 320 ARG A CZ 1 ATOM 2300 N NH1 A ARG A 1 327 ? 41.599 48.993 22.571 0.50 49.31 ? 320 ARG A NH1 1 ATOM 2301 N NH1 B ARG A 1 327 ? 43.010 47.620 25.717 0.50 49.34 ? 320 ARG A NH1 1 ATOM 2302 N NH2 A ARG A 1 327 ? 41.661 47.754 20.631 0.50 48.80 ? 320 ARG A NH2 1 ATOM 2303 N NH2 B ARG A 1 327 ? 41.909 48.404 23.862 0.50 49.27 ? 320 ARG A NH2 1 ATOM 2304 N N . GLY A 1 328 ? 36.434 44.472 27.442 1.00 34.70 ? 321 GLY A N 1 ATOM 2305 C CA . GLY A 1 328 ? 36.354 43.608 28.623 1.00 34.16 ? 321 GLY A CA 1 ATOM 2306 C C . GLY A 1 328 ? 37.550 42.653 28.631 1.00 35.56 ? 321 GLY A C 1 ATOM 2307 O O . GLY A 1 328 ? 38.607 42.934 28.017 1.00 35.96 ? 321 GLY A O 1 ATOM 2308 N N . SER A 1 329 ? 37.386 41.509 29.299 1.00 35.20 ? 322 SER A N 1 ATOM 2309 C CA . SER A 1 329 ? 38.496 40.564 29.525 1.00 36.85 ? 322 SER A CA 1 ATOM 2310 C C . SER A 1 329 ? 38.482 39.295 28.681 1.00 36.31 ? 322 SER A C 1 ATOM 2311 O O . SER A 1 329 ? 39.339 38.434 28.864 1.00 36.83 ? 322 SER A O 1 ATOM 2312 C CB . SER A 1 329 ? 38.528 40.152 30.998 1.00 37.10 ? 322 SER A CB 1 ATOM 2313 O OG . SER A 1 329 ? 38.796 41.277 31.798 1.00 41.21 ? 322 SER A OG 1 ATOM 2314 N N . LEU A 1 330 ? 37.526 39.167 27.770 1.00 34.75 ? 323 LEU A N 1 ATOM 2315 C CA . LEU A 1 330 ? 37.462 37.998 26.916 1.00 34.84 ? 323 LEU A CA 1 ATOM 2316 C C . LEU A 1 330 ? 38.515 38.131 25.820 1.00 36.23 ? 323 LEU A C 1 ATOM 2317 O O . LEU A 1 330 ? 38.933 39.242 25.457 1.00 35.78 ? 323 LEU A O 1 ATOM 2318 C CB . LEU A 1 330 ? 36.082 37.832 26.282 1.00 34.46 ? 323 LEU A CB 1 ATOM 2319 C CG . LEU A 1 330 ? 34.931 37.568 27.258 1.00 32.51 ? 323 LEU A CG 1 ATOM 2320 C CD1 . LEU A 1 330 ? 33.606 37.680 26.510 1.00 32.77 ? 323 LEU A CD1 1 ATOM 2321 C CD2 . LEU A 1 330 ? 35.107 36.184 27.914 1.00 31.42 ? 323 LEU A CD2 1 ATOM 2322 N N . LYS A 1 331 ? 38.903 36.990 25.284 1.00 37.53 ? 324 LYS A N 1 ATOM 2323 C CA . LYS A 1 331 ? 39.888 36.969 24.216 1.00 39.74 ? 324 LYS A CA 1 ATOM 2324 C C . LYS A 1 331 ? 39.203 37.204 22.870 1.00 39.77 ? 324 LYS A C 1 ATOM 2325 O O . LYS A 1 331 ? 39.179 36.326 21.994 1.00 40.91 ? 324 LYS A O 1 ATOM 2326 C CB . LYS A 1 331 ? 40.700 35.670 24.278 1.00 40.50 ? 324 LYS A CB 1 ATOM 2327 C CG . LYS A 1 331 ? 41.556 35.582 25.558 0.90 43.50 ? 324 LYS A CG 1 ATOM 2328 C CD . LYS A 1 331 ? 42.537 36.771 25.677 0.65 46.57 ? 324 LYS A CD 1 ATOM 2329 C CE . LYS A 1 331 ? 43.127 36.926 27.085 0.55 47.37 ? 324 LYS A CE 1 ATOM 2330 N NZ . LYS A 1 331 ? 42.135 37.419 28.089 0.50 48.03 ? 324 LYS A NZ 1 ATOM 2331 N N . VAL A 1 332 ? 38.637 38.407 22.738 1.00 38.56 ? 325 VAL A N 1 ATOM 2332 C CA . VAL A 1 332 ? 38.001 38.873 21.504 1.00 39.02 ? 325 VAL A CA 1 ATOM 2333 C C . VAL A 1 332 ? 38.432 40.330 21.264 1.00 38.70 ? 325 VAL A C 1 ATOM 2334 O O . VAL A 1 332 ? 38.930 40.974 22.191 1.00 38.66 ? 325 VAL A O 1 ATOM 2335 C CB . VAL A 1 332 ? 36.455 38.748 21.559 1.00 37.49 ? 325 VAL A CB 1 ATOM 2336 C CG1 . VAL A 1 332 ? 36.021 37.287 21.802 1.00 38.50 ? 325 VAL A CG1 1 ATOM 2337 C CG2 . VAL A 1 332 ? 35.854 39.685 22.616 1.00 37.37 ? 325 VAL A CG2 1 ATOM 2338 N N . PRO A 1 333 ? 38.242 40.859 20.034 1.00 39.56 ? 326 PRO A N 1 ATOM 2339 C CA . PRO A 1 333 ? 38.735 42.231 19.800 1.00 39.57 ? 326 PRO A CA 1 ATOM 2340 C C . PRO A 1 333 ? 37.832 43.320 20.371 1.00 38.28 ? 326 PRO A C 1 ATOM 2341 O O . PRO A 1 333 ? 38.279 44.458 20.521 1.00 38.45 ? 326 PRO A O 1 ATOM 2342 C CB . PRO A 1 333 ? 38.804 42.348 18.268 1.00 41.29 ? 326 PRO A CB 1 ATOM 2343 C CG . PRO A 1 333 ? 37.895 41.261 17.727 1.00 41.85 ? 326 PRO A CG 1 ATOM 2344 C CD . PRO A 1 333 ? 37.682 40.230 18.814 1.00 40.54 ? 326 PRO A CD 1 ATOM 2345 N N . TYR A 1 334 ? 36.586 42.968 20.687 1.00 36.65 ? 327 TYR A N 1 ATOM 2346 C CA . TYR A 1 334 ? 35.586 43.959 21.127 1.00 35.62 ? 327 TYR A CA 1 ATOM 2347 C C . TYR A 1 334 ? 35.288 44.983 20.018 1.00 36.16 ? 327 TYR A C 1 ATOM 2348 O O . TYR A 1 334 ? 35.050 46.166 20.279 1.00 36.53 ? 327 TYR A O 1 ATOM 2349 C CB . TYR A 1 334 ? 36.002 44.623 22.449 1.00 35.27 ? 327 TYR A CB 1 ATOM 2350 C CG . TYR A 1 334 ? 35.865 43.667 23.612 1.00 34.41 ? 327 TYR A CG 1 ATOM 2351 C CD1 . TYR A 1 334 ? 34.632 43.503 24.263 1.00 31.84 ? 327 TYR A CD1 1 ATOM 2352 C CD2 . TYR A 1 334 ? 36.952 42.885 24.032 1.00 34.17 ? 327 TYR A CD2 1 ATOM 2353 C CE1 . TYR A 1 334 ? 34.492 42.602 25.313 1.00 29.35 ? 327 TYR A CE1 1 ATOM 2354 C CE2 . TYR A 1 334 ? 36.816 41.982 25.087 1.00 33.09 ? 327 TYR A CE2 1 ATOM 2355 C CZ . TYR A 1 334 ? 35.590 41.841 25.718 1.00 32.29 ? 327 TYR A CZ 1 ATOM 2356 O OH . TYR A 1 334 ? 35.458 40.942 26.771 1.00 31.80 ? 327 TYR A OH 1 ATOM 2357 N N . ASN A 1 335 ? 35.311 44.509 18.773 1.00 36.88 ? 328 ASN A N 1 ATOM 2358 C CA . ASN A 1 335 ? 34.894 45.318 17.643 1.00 37.62 ? 328 ASN A CA 1 ATOM 2359 C C . ASN A 1 335 ? 33.448 45.709 17.818 1.00 37.00 ? 328 ASN A C 1 ATOM 2360 O O . ASN A 1 335 ? 32.656 44.941 18.363 1.00 35.95 ? 328 ASN A O 1 ATOM 2361 C CB . ASN A 1 335 ? 35.067 44.545 16.341 1.00 38.03 ? 328 ASN A CB 1 ATOM 2362 C CG . ASN A 1 335 ? 36.531 44.395 15.948 1.00 39.68 ? 328 ASN A CG 1 ATOM 2363 O OD1 . ASN A 1 335 ? 37.378 45.216 16.322 1.00 40.87 ? 328 ASN A OD1 1 ATOM 2364 N ND2 . ASN A 1 335 ? 36.837 43.339 15.201 1.00 38.13 ? 328 ASN A ND2 1 ATOM 2365 N N . VAL A 1 336 ? 33.112 46.911 17.361 1.00 37.80 ? 329 VAL A N 1 ATOM 2366 C CA . VAL A 1 336 ? 31.775 47.442 17.575 1.00 37.37 ? 329 VAL A CA 1 ATOM 2367 C C . VAL A 1 336 ? 30.791 46.923 16.520 1.00 37.26 ? 329 VAL A C 1 ATOM 2368 O O . VAL A 1 336 ? 29.575 46.904 16.737 1.00 35.54 ? 329 VAL A O 1 ATOM 2369 C CB . VAL A 1 336 ? 31.796 48.988 17.634 1.00 37.94 ? 329 VAL A CB 1 ATOM 2370 C CG1 . VAL A 1 336 ? 30.373 49.544 17.565 1.00 38.28 ? 329 VAL A CG1 1 ATOM 2371 C CG2 . VAL A 1 336 ? 32.443 49.435 18.945 1.00 38.86 ? 329 VAL A CG2 1 ATOM 2372 N N . GLY A 1 337 ? 31.308 46.472 15.383 1.00 38.00 ? 330 GLY A N 1 ATOM 2373 C CA . GLY A 1 337 ? 30.426 46.091 14.290 1.00 38.73 ? 330 GLY A CA 1 ATOM 2374 C C . GLY A 1 337 ? 30.119 47.300 13.424 1.00 39.49 ? 330 GLY A C 1 ATOM 2375 O O . GLY A 1 337 ? 30.920 48.240 13.361 1.00 39.56 ? 330 GLY A O 1 ATOM 2376 N N . PRO A 1 338 ? 28.971 47.281 12.729 1.00 39.97 ? 331 PRO A N 1 ATOM 2377 C CA . PRO A 1 338 ? 27.965 46.213 12.715 1.00 40.13 ? 331 PRO A CA 1 ATOM 2378 C C . PRO A 1 338 ? 28.422 44.930 12.021 1.00 40.68 ? 331 PRO A C 1 ATOM 2379 O O . PRO A 1 338 ? 29.225 44.967 11.064 1.00 41.44 ? 331 PRO A O 1 ATOM 2380 C CB . PRO A 1 338 ? 26.823 46.839 11.915 1.00 40.53 ? 331 PRO A CB 1 ATOM 2381 C CG . PRO A 1 338 ? 27.573 47.695 10.881 1.00 42.55 ? 331 PRO A CG 1 ATOM 2382 C CD . PRO A 1 338 ? 28.670 48.324 11.724 1.00 41.67 ? 331 PRO A CD 1 ATOM 2383 N N . GLY A 1 339 ? 27.907 43.803 12.500 1.00 40.06 ? 332 GLY A N 1 ATOM 2384 C CA . GLY A 1 339 ? 28.107 42.520 11.827 1.00 41.01 ? 332 GLY A CA 1 ATOM 2385 C C . GLY A 1 339 ? 29.464 41.880 12.048 1.00 41.78 ? 332 GLY A C 1 ATOM 2386 O O . GLY A 1 339 ? 30.288 42.382 12.837 1.00 40.88 ? 332 GLY A O 1 ATOM 2387 N N . PHE A 1 340 ? 29.690 40.774 11.329 1.00 42.35 ? 333 PHE A N 1 ATOM 2388 C CA . PHE A 1 340 ? 30.842 39.911 11.539 1.00 43.24 ? 333 PHE A CA 1 ATOM 2389 C C . PHE A 1 340 ? 31.907 40.209 10.476 1.00 45.42 ? 333 PHE A C 1 ATOM 2390 O O . PHE A 1 340 ? 31.590 40.836 9.458 1.00 46.07 ? 333 PHE A O 1 ATOM 2391 C CB . PHE A 1 340 ? 30.433 38.431 11.449 1.00 43.10 ? 333 PHE A CB 1 ATOM 2392 C CG . PHE A 1 340 ? 29.542 37.952 12.576 1.00 41.89 ? 333 PHE A CG 1 ATOM 2393 C CD1 . PHE A 1 340 ? 28.601 36.950 12.346 1.00 41.23 ? 333 PHE A CD1 1 ATOM 2394 C CD2 . PHE A 1 340 ? 29.646 38.493 13.860 1.00 40.49 ? 333 PHE A CD2 1 ATOM 2395 C CE1 . PHE A 1 340 ? 27.777 36.482 13.372 1.00 42.22 ? 333 PHE A CE1 1 ATOM 2396 C CE2 . PHE A 1 340 ? 28.817 38.038 14.907 1.00 40.01 ? 333 PHE A CE2 1 ATOM 2397 C CZ . PHE A 1 340 ? 27.878 37.029 14.659 1.00 38.18 ? 333 PHE A CZ 1 ATOM 2398 N N . THR A 1 341 ? 33.147 39.774 10.726 1.00 46.88 ? 334 THR A N 1 ATOM 2399 C CA . THR A 1 341 ? 34.262 39.932 9.763 1.00 49.82 ? 334 THR A CA 1 ATOM 2400 C C . THR A 1 341 ? 34.036 39.142 8.477 1.00 52.17 ? 334 THR A C 1 ATOM 2401 O O . THR A 1 341 ? 33.330 38.129 8.473 1.00 52.39 ? 334 THR A O 1 ATOM 2402 C CB . THR A 1 341 ? 35.634 39.478 10.337 1.00 50.36 ? 334 THR A CB 1 ATOM 2403 O OG1 . THR A 1 341 ? 35.561 38.115 10.786 1.00 50.12 ? 334 THR A OG1 1 ATOM 2404 C CG2 . THR A 1 341 ? 36.106 40.380 11.455 1.00 49.02 ? 334 THR A CG2 1 ATOM 2405 N N . GLY A 1 342 ? 34.705 39.589 7.410 1.00 54.25 ? 335 GLY A N 1 ATOM 2406 C CA . GLY A 1 342 ? 34.519 39.092 6.043 1.00 56.42 ? 335 GLY A CA 1 ATOM 2407 C C . GLY A 1 342 ? 34.031 37.680 5.782 1.00 57.46 ? 335 GLY A C 1 ATOM 2408 O O . GLY A 1 342 ? 33.049 37.494 5.056 1.00 58.40 ? 335 GLY A O 1 ATOM 2409 N N . ASN A 1 343 ? 34.718 36.684 6.342 1.00 57.45 ? 336 ASN A N 1 ATOM 2410 C CA . ASN A 1 343 ? 34.360 35.272 6.125 1.00 58.31 ? 336 ASN A CA 1 ATOM 2411 C C . ASN A 1 343 ? 32.979 34.873 6.662 1.00 56.43 ? 336 ASN A C 1 ATOM 2412 O O . ASN A 1 343 ? 32.375 33.900 6.199 1.00 56.67 ? 336 ASN A O 1 ATOM 2413 C CB . ASN A 1 343 ? 35.432 34.343 6.722 1.00 59.16 ? 336 ASN A CB 1 ATOM 2414 C CG . ASN A 1 343 ? 36.791 34.482 6.040 1.00 63.42 ? 336 ASN A CG 1 ATOM 2415 O OD1 . ASN A 1 343 ? 36.923 35.103 4.972 1.00 67.80 ? 336 ASN A OD1 1 ATOM 2416 N ND2 . ASN A 1 343 ? 37.813 33.876 6.647 1.00 67.06 ? 336 ASN A ND2 1 ATOM 2417 N N . PHE A 1 344 ? 32.489 35.637 7.635 1.00 54.29 ? 337 PHE A N 1 ATOM 2418 C CA . PHE A 1 344 ? 31.238 35.324 8.322 1.00 52.45 ? 337 PHE A CA 1 ATOM 2419 C C . PHE A 1 344 ? 30.182 36.410 8.104 1.00 51.37 ? 337 PHE A C 1 ATOM 2420 O O . PHE A 1 344 ? 29.130 36.402 8.750 1.00 50.18 ? 337 PHE A O 1 ATOM 2421 C CB . PHE A 1 344 ? 31.504 35.135 9.819 1.00 51.09 ? 337 PHE A CB 1 ATOM 2422 C CG . PHE A 1 344 ? 32.709 34.285 10.121 1.00 51.79 ? 337 PHE A CG 1 ATOM 2423 C CD1 . PHE A 1 344 ? 33.890 34.869 10.559 1.00 51.75 ? 337 PHE A CD1 1 ATOM 2424 C CD2 . PHE A 1 344 ? 32.662 32.899 9.961 1.00 52.21 ? 337 PHE A CD2 1 ATOM 2425 C CE1 . PHE A 1 344 ? 35.009 34.088 10.843 1.00 52.24 ? 337 PHE A CE1 1 ATOM 2426 C CE2 . PHE A 1 344 ? 33.784 32.105 10.236 1.00 52.68 ? 337 PHE A CE2 1 ATOM 2427 C CZ . PHE A 1 344 ? 34.957 32.704 10.679 1.00 52.05 ? 337 PHE A CZ 1 ATOM 2428 N N . SER A 1 345 ? 30.465 37.320 7.175 1.00 51.64 ? 338 SER A N 1 ATOM 2429 C CA . SER A 1 345 ? 29.633 38.497 6.924 1.00 51.39 ? 338 SER A CA 1 ATOM 2430 C C . SER A 1 345 ? 28.178 38.179 6.591 1.00 50.63 ? 338 SER A C 1 ATOM 2431 O O . SER A 1 345 ? 27.299 39.015 6.822 1.00 50.60 ? 338 SER A O 1 ATOM 2432 C CB . SER A 1 345 ? 30.242 39.360 5.817 1.00 52.54 ? 338 SER A CB 1 ATOM 2433 O OG . SER A 1 345 ? 30.115 38.719 4.563 1.00 54.89 ? 338 SER A OG 1 ATOM 2434 N N . THR A 1 346 ? 27.922 36.981 6.068 1.00 50.54 ? 339 THR A N 1 ATOM 2435 C CA . THR A 1 346 ? 26.555 36.583 5.697 1.00 50.24 ? 339 THR A CA 1 ATOM 2436 C C . THR A 1 346 ? 25.804 35.852 6.807 1.00 48.81 ? 339 THR A C 1 ATOM 2437 O O . THR A 1 346 ? 24.610 35.558 6.668 1.00 48.92 ? 339 THR A O 1 ATOM 2438 C CB . THR A 1 346 ? 26.523 35.716 4.430 1.00 51.52 ? 339 THR A CB 1 ATOM 2439 O OG1 . THR A 1 346 ? 27.193 34.468 4.678 1.00 52.14 ? 339 THR A OG1 1 ATOM 2440 C CG2 . THR A 1 346 ? 27.170 36.455 3.274 1.00 54.01 ? 339 THR A CG2 1 ATOM 2441 N N . GLN A 1 347 ? 26.511 35.547 7.893 1.00 46.76 ? 340 GLN A N 1 ATOM 2442 C CA . GLN A 1 347 ? 25.873 35.005 9.084 1.00 44.92 ? 340 GLN A CA 1 ATOM 2443 C C . GLN A 1 347 ? 25.210 36.136 9.853 1.00 43.45 ? 340 GLN A C 1 ATOM 2444 O O . GLN A 1 347 ? 25.626 37.300 9.761 1.00 43.11 ? 340 GLN A O 1 ATOM 2445 C CB . GLN A 1 347 ? 26.884 34.271 9.958 1.00 44.13 ? 340 GLN A CB 1 ATOM 2446 C CG . GLN A 1 347 ? 27.552 33.115 9.208 1.00 45.64 ? 340 GLN A CG 1 ATOM 2447 C CD . GLN A 1 347 ? 28.585 32.353 10.016 1.00 45.93 ? 340 GLN A CD 1 ATOM 2448 O OE1 . GLN A 1 347 ? 28.968 32.749 11.121 1.00 46.19 ? 340 GLN A OE1 1 ATOM 2449 N NE2 . GLN A 1 347 ? 29.055 31.237 9.448 1.00 47.06 ? 340 GLN A NE2 1 ATOM 2450 N N . LYS A 1 348 ? 24.151 35.790 10.580 1.00 42.13 ? 341 LYS A N 1 ATOM 2451 C CA . LYS A 1 348 ? 23.433 36.764 11.390 1.00 40.55 ? 341 LYS A CA 1 ATOM 2452 C C . LYS A 1 348 ? 23.163 36.178 12.767 1.00 39.02 ? 341 LYS A C 1 ATOM 2453 O O . LYS A 1 348 ? 23.433 35.010 13.027 1.00 38.39 ? 341 LYS A O 1 ATOM 2454 C CB . LYS A 1 348 ? 22.119 37.213 10.710 1.00 41.25 ? 341 LYS A CB 1 ATOM 2455 C CG . LYS A 1 348 ? 22.295 37.665 9.266 0.92 43.29 ? 341 LYS A CG 1 ATOM 2456 C CD . LYS A 1 348 ? 21.611 38.974 8.910 0.75 46.09 ? 341 LYS A CD 1 ATOM 2457 C CE . LYS A 1 348 ? 22.288 39.559 7.653 0.65 49.07 ? 341 LYS A CE 1 ATOM 2458 N NZ . LYS A 1 348 ? 21.487 40.638 6.977 0.55 51.21 ? 341 LYS A NZ 1 ATOM 2459 N N . VAL A 1 349 ? 22.646 37.016 13.656 1.00 37.30 ? 342 VAL A N 1 ATOM 2460 C CA . VAL A 1 349 ? 22.252 36.566 14.983 1.00 36.10 ? 342 VAL A CA 1 ATOM 2461 C C . VAL A 1 349 ? 20.731 36.587 15.055 1.00 35.47 ? 342 VAL A C 1 ATOM 2462 O O . VAL A 1 349 ? 20.108 37.517 14.553 1.00 35.85 ? 342 VAL A O 1 ATOM 2463 C CB . VAL A 1 349 ? 22.899 37.451 16.068 1.00 35.29 ? 342 VAL A CB 1 ATOM 2464 C CG1 . VAL A 1 349 ? 22.189 37.278 17.429 1.00 33.49 ? 342 VAL A CG1 1 ATOM 2465 C CG2 . VAL A 1 349 ? 24.390 37.114 16.167 1.00 36.21 ? 342 VAL A CG2 1 ATOM 2466 N N . LYS A 1 350 ? 20.145 35.549 15.649 1.00 35.03 ? 343 LYS A N 1 ATOM 2467 C CA . LYS A 1 350 ? 18.701 35.437 15.767 1.00 34.74 ? 343 LYS A CA 1 ATOM 2468 C C . LYS A 1 350 ? 18.295 35.174 17.215 1.00 33.49 ? 343 LYS A C 1 ATOM 2469 O O . LYS A 1 350 ? 18.792 34.249 17.855 1.00 32.86 ? 343 LYS A O 1 ATOM 2470 C CB . LYS A 1 350 ? 18.166 34.316 14.859 1.00 35.98 ? 343 LYS A CB 1 ATOM 2471 C CG . LYS A 1 350 ? 16.633 34.168 14.885 1.00 36.79 ? 343 LYS A CG 1 ATOM 2472 C CD . LYS A 1 350 ? 16.173 33.082 13.904 1.00 39.75 ? 343 LYS A CD 1 ATOM 2473 C CE . LYS A 1 350 ? 14.646 33.129 13.754 1.00 41.80 ? 343 LYS A CE 1 ATOM 2474 N NZ . LYS A 1 350 ? 14.146 32.263 12.643 1.00 46.22 ? 343 LYS A NZ 1 ATOM 2475 N N . MET A 1 351 ? 17.387 35.996 17.732 1.00 33.06 ? 344 MET A N 1 ATOM 2476 C CA . MET A 1 351 ? 16.855 35.767 19.071 1.00 31.62 ? 344 MET A CA 1 ATOM 2477 C C . MET A 1 351 ? 15.571 34.950 18.968 1.00 32.63 ? 344 MET A C 1 ATOM 2478 O O . MET A 1 351 ? 14.870 35.036 17.959 1.00 33.87 ? 344 MET A O 1 ATOM 2479 C CB . MET A 1 351 ? 16.560 37.114 19.747 1.00 31.16 ? 344 MET A CB 1 ATOM 2480 C CG . MET A 1 351 ? 17.781 38.032 19.790 1.00 29.22 ? 344 MET A CG 1 ATOM 2481 S SD . MET A 1 351 ? 17.466 39.600 20.668 1.00 30.50 ? 344 MET A SD 1 ATOM 2482 C CE . MET A 1 351 ? 17.240 38.985 22.354 1.00 28.85 ? 344 MET A CE 1 ATOM 2483 N N . HIS A 1 352 ? 15.265 34.159 19.994 1.00 31.45 ? 345 HIS A N 1 ATOM 2484 C CA . HIS A 1 352 ? 13.974 33.481 20.089 1.00 31.45 ? 345 HIS A CA 1 ATOM 2485 C C . HIS A 1 352 ? 13.448 33.690 21.505 1.00 29.86 ? 345 HIS A C 1 ATOM 2486 O O . HIS A 1 352 ? 13.866 32.993 22.442 1.00 29.65 ? 345 HIS A O 1 ATOM 2487 C CB . HIS A 1 352 ? 14.084 31.968 19.831 1.00 31.83 ? 345 HIS A CB 1 ATOM 2488 C CG . HIS A 1 352 ? 14.997 31.586 18.700 1.00 35.06 ? 345 HIS A CG 1 ATOM 2489 N ND1 . HIS A 1 352 ? 16.370 31.675 18.783 1.00 36.73 ? 345 HIS A ND1 1 ATOM 2490 C CD2 . HIS A 1 352 ? 14.729 31.068 17.478 1.00 36.74 ? 345 HIS A CD2 1 ATOM 2491 C CE1 . HIS A 1 352 ? 16.911 31.249 17.654 1.00 37.89 ? 345 HIS A CE1 1 ATOM 2492 N NE2 . HIS A 1 352 ? 15.936 30.880 16.842 1.00 40.46 ? 345 HIS A NE2 1 ATOM 2493 N N . ILE A 1 353 ? 12.530 34.633 21.654 1.00 29.31 ? 346 ILE A N 1 ATOM 2494 C CA . ILE A 1 353 ? 11.942 34.947 22.960 1.00 28.59 ? 346 ILE A CA 1 ATOM 2495 C C . ILE A 1 353 ? 10.444 34.674 22.943 1.00 28.81 ? 346 ILE A C 1 ATOM 2496 O O . ILE A 1 353 ? 9.707 35.222 22.107 1.00 29.20 ? 346 ILE A O 1 ATOM 2497 C CB . ILE A 1 353 ? 12.225 36.415 23.375 1.00 29.07 ? 346 ILE A CB 1 ATOM 2498 C CG1 . ILE A 1 353 ? 13.714 36.769 23.166 1.00 28.40 ? 346 ILE A CG1 1 ATOM 2499 C CG2 . ILE A 1 353 ? 11.748 36.662 24.818 1.00 27.58 ? 346 ILE A CG2 1 ATOM 2500 C CD1 . ILE A 1 353 ? 14.732 35.921 23.989 1.00 30.03 ? 346 ILE A CD1 1 ATOM 2501 N N . HIS A 1 354 ? 10.003 33.844 23.886 1.00 28.40 ? 347 HIS A N 1 ATOM 2502 C CA . HIS A 1 354 ? 8.603 33.401 23.975 1.00 29.05 ? 347 HIS A CA 1 ATOM 2503 C C . HIS A 1 354 ? 7.974 33.579 25.359 1.00 27.87 ? 347 HIS A C 1 ATOM 2504 O O . HIS A 1 354 ? 6.906 33.018 25.653 1.00 27.96 ? 347 HIS A O 1 ATOM 2505 C CB . HIS A 1 354 ? 8.539 31.937 23.575 1.00 30.12 ? 347 HIS A CB 1 ATOM 2506 C CG . HIS A 1 354 ? 9.209 31.670 22.265 1.00 34.18 ? 347 HIS A CG 1 ATOM 2507 N ND1 . HIS A 1 354 ? 10.358 30.915 22.153 1.00 38.22 ? 347 HIS A ND1 1 ATOM 2508 C CD2 . HIS A 1 354 ? 8.924 32.118 21.019 1.00 37.40 ? 347 HIS A CD2 1 ATOM 2509 C CE1 . HIS A 1 354 ? 10.728 30.875 20.884 1.00 38.64 ? 347 HIS A CE1 1 ATOM 2510 N NE2 . HIS A 1 354 ? 9.875 31.593 20.177 1.00 40.03 ? 347 HIS A NE2 1 ATOM 2511 N N . SER A 1 355 ? 8.635 34.381 26.197 1.00 26.25 ? 348 SER A N 1 ATOM 2512 C CA . SER A 1 355 ? 8.136 34.681 27.534 1.00 25.35 ? 348 SER A CA 1 ATOM 2513 C C . SER A 1 355 ? 6.772 35.339 27.442 1.00 26.26 ? 348 SER A C 1 ATOM 2514 O O . SER A 1 355 ? 6.465 35.997 26.440 1.00 26.08 ? 348 SER A O 1 ATOM 2515 C CB . SER A 1 355 ? 9.113 35.648 28.231 1.00 24.41 ? 348 SER A CB 1 ATOM 2516 O OG . SER A 1 355 ? 10.396 35.032 28.324 1.00 25.59 ? 348 SER A OG 1 ATOM 2517 N N . THR A 1 356 ? 5.961 35.187 28.492 1.00 25.77 ? 349 THR A N 1 ATOM 2518 C CA . THR A 1 356 ? 4.631 35.802 28.516 1.00 25.94 ? 349 THR A CA 1 ATOM 2519 C C . THR A 1 356 ? 4.449 36.633 29.768 1.00 25.43 ? 349 THR A C 1 ATOM 2520 O O . THR A 1 356 ? 4.971 36.296 30.827 1.00 25.87 ? 349 THR A O 1 ATOM 2521 C CB . THR A 1 356 ? 3.518 34.743 28.486 1.00 27.48 ? 349 THR A CB 1 ATOM 2522 O OG1 . THR A 1 356 ? 3.675 33.881 29.617 1.00 32.11 ? 349 THR A OG1 1 ATOM 2523 C CG2 . THR A 1 356 ? 3.684 33.896 27.284 1.00 26.96 ? 349 THR A CG2 1 ATOM 2524 N N . ASN A 1 357 ? 3.722 37.727 29.620 1.00 24.04 ? 350 ASN A N 1 ATOM 2525 C CA . ASN A 1 357 ? 3.352 38.549 30.773 1.00 24.36 ? 350 ASN A CA 1 ATOM 2526 C C . ASN A 1 357 ? 2.002 38.041 31.265 1.00 25.12 ? 350 ASN A C 1 ATOM 2527 O O . ASN A 1 357 ? 1.099 37.762 30.461 1.00 26.15 ? 350 ASN A O 1 ATOM 2528 C CB . ASN A 1 357 ? 3.229 40.011 30.347 1.00 24.11 ? 350 ASN A CB 1 ATOM 2529 C CG . ASN A 1 357 ? 4.534 40.585 29.874 1.00 25.87 ? 350 ASN A CG 1 ATOM 2530 O OD1 . ASN A 1 357 ? 5.606 40.214 30.348 1.00 26.94 ? 350 ASN A OD1 1 ATOM 2531 N ND2 . ASN A 1 357 ? 4.452 41.523 28.937 1.00 30.65 ? 350 ASN A ND2 1 ATOM 2532 N N A GLU A 1 358 ? 1.860 37.861 32.575 0.60 24.62 ? 351 GLU A N 1 ATOM 2533 N N B GLU A 1 358 ? 1.848 37.959 32.583 0.40 24.40 ? 351 GLU A N 1 ATOM 2534 C CA A GLU A 1 358 ? 0.612 37.313 33.123 0.60 25.61 ? 351 GLU A CA 1 ATOM 2535 C CA B GLU A 1 358 ? 0.712 37.266 33.190 0.40 25.10 ? 351 GLU A CA 1 ATOM 2536 C C A GLU A 1 358 ? 0.311 37.971 34.450 0.60 23.71 ? 351 GLU A C 1 ATOM 2537 C C B GLU A 1 358 ? 0.321 37.957 34.487 0.40 23.62 ? 351 GLU A C 1 ATOM 2538 O O A GLU A 1 358 ? 1.193 38.099 35.314 0.60 23.09 ? 351 GLU A O 1 ATOM 2539 O O B GLU A 1 358 ? 1.168 38.099 35.377 0.40 23.13 ? 351 GLU A O 1 ATOM 2540 C CB A GLU A 1 358 ? 0.660 35.784 33.363 0.60 26.29 ? 351 GLU A CB 1 ATOM 2541 C CB B GLU A 1 358 ? 1.112 35.818 33.515 0.40 25.38 ? 351 GLU A CB 1 ATOM 2542 C CG A GLU A 1 358 ? 1.725 34.964 32.638 0.60 31.83 ? 351 GLU A CG 1 ATOM 2543 C CG B GLU A 1 358 ? 1.687 35.022 32.339 0.40 29.19 ? 351 GLU A CG 1 ATOM 2544 C CD A GLU A 1 358 ? 1.550 33.463 32.884 0.60 34.70 ? 351 GLU A CD 1 ATOM 2545 C CD B GLU A 1 358 ? 0.614 34.391 31.476 0.40 30.42 ? 351 GLU A CD 1 ATOM 2546 O OE1 A GLU A 1 358 ? 1.247 32.727 31.919 0.60 41.19 ? 351 GLU A OE1 1 ATOM 2547 O OE1 B GLU A 1 358 ? -0.581 34.541 31.809 0.40 33.22 ? 351 GLU A OE1 1 ATOM 2548 O OE2 A GLU A 1 358 ? 1.685 33.018 34.041 0.60 34.04 ? 351 GLU A OE2 1 ATOM 2549 O OE2 B GLU A 1 358 ? 0.962 33.729 30.469 0.40 33.40 ? 351 GLU A OE2 1 ATOM 2550 N N . VAL A 1 359 ? -0.936 38.386 34.609 1.00 23.68 ? 352 VAL A N 1 ATOM 2551 C CA . VAL A 1 359 ? -1.408 38.927 35.905 1.00 22.42 ? 352 VAL A CA 1 ATOM 2552 C C . VAL A 1 359 ? -1.442 37.761 36.909 1.00 22.21 ? 352 VAL A C 1 ATOM 2553 O O . VAL A 1 359 ? -2.078 36.713 36.660 1.00 23.21 ? 352 VAL A O 1 ATOM 2554 C CB . VAL A 1 359 ? -2.776 39.604 35.790 1.00 22.81 ? 352 VAL A CB 1 ATOM 2555 C CG1 . VAL A 1 359 ? -3.287 40.017 37.161 1.00 23.25 ? 352 VAL A CG1 1 ATOM 2556 C CG2 . VAL A 1 359 ? -2.665 40.839 34.910 1.00 24.23 ? 352 VAL A CG2 1 ATOM 2557 N N . THR A 1 360 ? -0.753 37.945 38.028 1.00 20.31 ? 353 THR A N 1 ATOM 2558 C CA . THR A 1 360 ? -0.447 36.875 38.977 1.00 20.57 ? 353 THR A CA 1 ATOM 2559 C C . THR A 1 360 ? -0.566 37.402 40.400 1.00 20.15 ? 353 THR A C 1 ATOM 2560 O O . THR A 1 360 ? -0.207 38.571 40.658 1.00 19.82 ? 353 THR A O 1 ATOM 2561 C CB . THR A 1 360 ? 0.974 36.363 38.728 1.00 21.42 ? 353 THR A CB 1 ATOM 2562 O OG1 . THR A 1 360 ? 1.096 35.995 37.344 1.00 23.46 ? 353 THR A OG1 1 ATOM 2563 C CG2 . THR A 1 360 ? 1.293 35.130 39.573 1.00 21.71 ? 353 THR A CG2 1 ATOM 2564 N N . ARG A 1 361 ? -1.061 36.552 41.325 1.00 20.53 ? 354 ARG A N 1 ATOM 2565 C CA . ARG A 1 361 ? -1.237 37.002 42.706 1.00 19.93 ? 354 ARG A CA 1 ATOM 2566 C C . ARG A 1 361 ? 0.113 37.007 43.444 1.00 19.54 ? 354 ARG A C 1 ATOM 2567 O O . ARG A 1 361 ? 0.923 36.053 43.319 1.00 20.51 ? 354 ARG A O 1 ATOM 2568 C CB . ARG A 1 361 ? -2.280 36.126 43.453 1.00 20.34 ? 354 ARG A CB 1 ATOM 2569 C CG . ARG A 1 361 ? -2.625 36.686 44.843 1.00 22.51 ? 354 ARG A CG 1 ATOM 2570 C CD . ARG A 1 361 ? -3.998 36.222 45.255 1.00 23.17 ? 354 ARG A CD 1 ATOM 2571 N NE . ARG A 1 361 ? -5.003 36.980 44.518 1.00 25.19 ? 354 ARG A NE 1 ATOM 2572 C CZ . ARG A 1 361 ? -6.306 36.935 44.773 1.00 27.96 ? 354 ARG A CZ 1 ATOM 2573 N NH1 . ARG A 1 361 ? -6.781 36.135 45.746 1.00 26.92 ? 354 ARG A NH1 1 ATOM 2574 N NH2 . ARG A 1 361 ? -7.130 37.686 44.047 1.00 28.73 ? 354 ARG A NH2 1 ATOM 2575 N N . ILE A 1 362 ? 0.321 38.048 44.241 1.00 18.79 ? 355 ILE A N 1 ATOM 2576 C CA . ILE A 1 362 ? 1.538 38.169 45.081 1.00 18.93 ? 355 ILE A CA 1 ATOM 2577 C C . ILE A 1 362 ? 1.102 38.463 46.511 1.00 19.19 ? 355 ILE A C 1 ATOM 2578 O O . ILE A 1 362 ? -0.036 38.932 46.715 1.00 19.36 ? 355 ILE A O 1 ATOM 2579 C CB . ILE A 1 362 ? 2.481 39.287 44.559 1.00 17.85 ? 355 ILE A CB 1 ATOM 2580 C CG1 . ILE A 1 362 ? 1.810 40.666 44.587 1.00 17.40 ? 355 ILE A CG1 1 ATOM 2581 C CG2 . ILE A 1 362 ? 2.968 38.905 43.127 1.00 18.27 ? 355 ILE A CG2 1 ATOM 2582 C CD1 . ILE A 1 362 ? 2.842 41.842 44.476 1.00 17.68 ? 355 ILE A CD1 1 ATOM 2583 N N . TYR A 1 363 ? 1.971 38.184 47.481 1.00 18.69 ? 356 TYR A N 1 ATOM 2584 C CA . TYR A 1 363 ? 1.583 38.264 48.891 1.00 18.80 ? 356 TYR A CA 1 ATOM 2585 C C . TYR A 1 363 ? 2.639 38.953 49.723 1.00 18.63 ? 356 TYR A C 1 ATOM 2586 O O . TYR A 1 363 ? 3.756 38.445 49.858 1.00 19.32 ? 356 TYR A O 1 ATOM 2587 C CB . TYR A 1 363 ? 1.394 36.842 49.462 1.00 19.34 ? 356 TYR A CB 1 ATOM 2588 C CG . TYR A 1 363 ? 0.347 36.010 48.767 1.00 20.73 ? 356 TYR A CG 1 ATOM 2589 C CD1 . TYR A 1 363 ? -0.971 35.993 49.223 1.00 22.42 ? 356 TYR A CD1 1 ATOM 2590 C CD2 . TYR A 1 363 ? 0.683 35.248 47.623 1.00 20.81 ? 356 TYR A CD2 1 ATOM 2591 C CE1 . TYR A 1 363 ? -1.946 35.224 48.579 1.00 24.02 ? 356 TYR A CE1 1 ATOM 2592 C CE2 . TYR A 1 363 ? -0.299 34.477 46.965 1.00 22.70 ? 356 TYR A CE2 1 ATOM 2593 C CZ . TYR A 1 363 ? -1.595 34.493 47.453 1.00 24.10 ? 356 TYR A CZ 1 ATOM 2594 O OH . TYR A 1 363 ? -2.544 33.725 46.805 1.00 25.91 ? 356 TYR A OH 1 ATOM 2595 N N . ASN A 1 364 ? 2.283 40.060 50.360 1.00 18.26 ? 357 ASN A N 1 ATOM 2596 C CA . ASN A 1 364 ? 3.201 40.671 51.343 1.00 18.83 ? 357 ASN A CA 1 ATOM 2597 C C . ASN A 1 364 ? 2.799 40.160 52.720 1.00 19.61 ? 357 ASN A C 1 ATOM 2598 O O . ASN A 1 364 ? 1.601 39.981 52.973 1.00 22.18 ? 357 ASN A O 1 ATOM 2599 C CB . ASN A 1 364 ? 3.039 42.199 51.381 1.00 18.00 ? 357 ASN A CB 1 ATOM 2600 C CG . ASN A 1 364 ? 3.385 42.885 50.072 1.00 19.27 ? 357 ASN A CG 1 ATOM 2601 O OD1 . ASN A 1 364 ? 4.282 42.462 49.336 1.00 18.24 ? 357 ASN A OD1 1 ATOM 2602 N ND2 . ASN A 1 364 ? 2.707 44.013 49.805 1.00 20.60 ? 357 ASN A ND2 1 ATOM 2603 N N . VAL A 1 365 ? 3.763 39.963 53.617 1.00 20.18 ? 358 VAL A N 1 ATOM 2604 C CA . VAL A 1 365 ? 3.396 39.713 55.013 1.00 19.90 ? 358 VAL A CA 1 ATOM 2605 C C . VAL A 1 365 ? 3.643 41.031 55.755 1.00 19.67 ? 358 VAL A C 1 ATOM 2606 O O . VAL A 1 365 ? 4.713 41.636 55.625 1.00 19.53 ? 358 VAL A O 1 ATOM 2607 C CB . VAL A 1 365 ? 4.262 38.613 55.660 1.00 20.21 ? 358 VAL A CB 1 ATOM 2608 C CG1 . VAL A 1 365 ? 3.697 38.222 57.043 1.00 22.42 ? 358 VAL A CG1 1 ATOM 2609 C CG2 . VAL A 1 365 ? 4.353 37.356 54.746 1.00 21.53 ? 358 VAL A CG2 1 ATOM 2610 N N . ILE A 1 366 ? 2.647 41.459 56.519 1.00 20.26 ? 359 ILE A N 1 ATOM 2611 C CA . ILE A 1 366 ? 2.687 42.722 57.265 1.00 20.71 ? 359 ILE A CA 1 ATOM 2612 C C . ILE A 1 366 ? 2.461 42.421 58.747 1.00 20.72 ? 359 ILE A C 1 ATOM 2613 O O . ILE A 1 366 ? 1.359 41.967 59.131 1.00 22.44 ? 359 ILE A O 1 ATOM 2614 C CB . ILE A 1 366 ? 1.579 43.705 56.768 1.00 21.20 ? 359 ILE A CB 1 ATOM 2615 C CG1 . ILE A 1 366 ? 1.662 43.899 55.238 1.00 22.05 ? 359 ILE A CG1 1 ATOM 2616 C CG2 . ILE A 1 366 ? 1.687 45.051 57.555 1.00 21.80 ? 359 ILE A CG2 1 ATOM 2617 C CD1 . ILE A 1 366 ? 2.953 44.610 54.767 1.00 22.28 ? 359 ILE A CD1 1 ATOM 2618 N N . GLY A 1 367 ? 3.494 42.659 59.555 1.00 22.15 ? 360 GLY A N 1 ATOM 2619 C CA . GLY A 1 367 ? 3.426 42.386 61.012 1.00 21.93 ? 360 GLY A CA 1 ATOM 2620 C C . GLY A 1 367 ? 3.372 43.701 61.767 1.00 21.85 ? 360 GLY A C 1 ATOM 2621 O O . GLY A 1 367 ? 4.036 44.657 61.369 1.00 22.35 ? 360 GLY A O 1 ATOM 2622 N N . THR A 1 368 ? 2.590 43.770 62.845 1.00 22.17 ? 361 THR A N 1 ATOM 2623 C CA . THR A 1 368 ? 2.458 45.032 63.606 1.00 22.84 ? 361 THR A CA 1 ATOM 2624 C C . THR A 1 368 ? 2.865 44.791 65.051 1.00 23.94 ? 361 THR A C 1 ATOM 2625 O O . THR A 1 368 ? 2.426 43.822 65.672 1.00 24.24 ? 361 THR A O 1 ATOM 2626 C CB . THR A 1 368 ? 0.994 45.510 63.596 1.00 23.63 ? 361 THR A CB 1 ATOM 2627 O OG1 . THR A 1 368 ? 0.599 45.755 62.238 1.00 24.44 ? 361 THR A OG1 1 ATOM 2628 C CG2 . THR A 1 368 ? 0.787 46.817 64.392 1.00 25.58 ? 361 THR A CG2 1 ATOM 2629 N N . LEU A 1 369 ? 3.695 45.684 65.578 1.00 23.56 ? 362 LEU A N 1 ATOM 2630 C CA . LEU A 1 369 ? 3.979 45.713 67.031 1.00 24.11 ? 362 LEU A CA 1 ATOM 2631 C C . LEU A 1 369 ? 3.496 47.081 67.491 1.00 24.19 ? 362 LEU A C 1 ATOM 2632 O O . LEU A 1 369 ? 4.175 48.085 67.268 1.00 24.38 ? 362 LEU A O 1 ATOM 2633 C CB . LEU A 1 369 ? 5.480 45.528 67.277 1.00 24.93 ? 362 LEU A CB 1 ATOM 2634 C CG . LEU A 1 369 ? 5.975 45.523 68.737 1.00 29.13 ? 362 LEU A CG 1 ATOM 2635 C CD1 . LEU A 1 369 ? 5.153 44.582 69.606 1.00 30.15 ? 362 LEU A CD1 1 ATOM 2636 C CD2 . LEU A 1 369 ? 7.480 45.212 68.799 1.00 29.28 ? 362 LEU A CD2 1 ATOM 2637 N N A ARG A 1 370 ? 2.323 47.105 68.125 0.50 24.30 ? 363 ARG A N 1 ATOM 2638 N N B ARG A 1 370 ? 2.321 47.119 68.111 0.50 24.15 ? 363 ARG A N 1 ATOM 2639 C CA A ARG A 1 370 ? 1.654 48.364 68.518 0.50 24.84 ? 363 ARG A CA 1 ATOM 2640 C CA B ARG A 1 370 ? 1.655 48.397 68.432 0.50 24.49 ? 363 ARG A CA 1 ATOM 2641 C C A ARG A 1 370 ? 2.491 49.182 69.510 0.50 25.15 ? 363 ARG A C 1 ATOM 2642 C C B ARG A 1 370 ? 2.420 49.189 69.503 0.50 24.96 ? 363 ARG A C 1 ATOM 2643 O O A ARG A 1 370 ? 3.000 48.638 70.494 0.50 25.94 ? 363 ARG A O 1 ATOM 2644 O O B ARG A 1 370 ? 2.819 48.629 70.529 0.50 25.72 ? 363 ARG A O 1 ATOM 2645 C CB A ARG A 1 370 ? 0.280 48.050 69.123 0.50 26.04 ? 363 ARG A CB 1 ATOM 2646 C CB B ARG A 1 370 ? 0.217 48.112 68.866 0.50 25.43 ? 363 ARG A CB 1 ATOM 2647 C CG A ARG A 1 370 ? -0.363 49.237 69.833 0.50 26.85 ? 363 ARG A CG 1 ATOM 2648 C CG B ARG A 1 370 ? -0.606 49.340 69.255 0.50 25.88 ? 363 ARG A CG 1 ATOM 2649 C CD A ARG A 1 370 ? -1.746 48.918 70.394 0.50 33.06 ? 363 ARG A CD 1 ATOM 2650 C CD B ARG A 1 370 ? -2.052 48.932 69.429 0.50 29.07 ? 363 ARG A CD 1 ATOM 2651 N NE A ARG A 1 370 ? -1.779 47.720 71.238 0.50 36.09 ? 363 ARG A NE 1 ATOM 2652 N NE B ARG A 1 370 ? -2.158 47.805 70.347 0.50 33.92 ? 363 ARG A NE 1 ATOM 2653 C CZ A ARG A 1 370 ? -1.563 47.706 72.548 0.50 38.38 ? 363 ARG A CZ 1 ATOM 2654 C CZ B ARG A 1 370 ? -2.401 46.546 69.994 0.50 34.43 ? 363 ARG A CZ 1 ATOM 2655 N NH1 A ARG A 1 370 ? -1.279 48.826 73.201 0.50 39.56 ? 363 ARG A NH1 1 ATOM 2656 N NH1 B ARG A 1 370 ? -2.591 46.217 68.716 0.50 32.16 ? 363 ARG A NH1 1 ATOM 2657 N NH2 A ARG A 1 370 ? -1.633 46.560 73.207 0.50 40.69 ? 363 ARG A NH2 1 ATOM 2658 N NH2 B ARG A 1 370 ? -2.465 45.614 70.938 0.50 36.15 ? 363 ARG A NH2 1 ATOM 2659 N N . GLY A 1 371 ? 2.637 50.481 69.244 1.00 24.72 ? 364 GLY A N 1 ATOM 2660 C CA . GLY A 1 371 ? 3.316 51.383 70.172 1.00 25.10 ? 364 GLY A CA 1 ATOM 2661 C C . GLY A 1 371 ? 2.502 51.640 71.444 1.00 25.90 ? 364 GLY A C 1 ATOM 2662 O O . GLY A 1 371 ? 1.259 51.684 71.424 1.00 26.88 ? 364 GLY A O 1 ATOM 2663 N N . ALA A 1 372 ? 3.220 51.783 72.551 1.00 26.95 ? 365 ALA A N 1 ATOM 2664 C CA . ALA A 1 372 ? 2.616 52.039 73.866 1.00 28.04 ? 365 ALA A CA 1 ATOM 2665 C C . ALA A 1 372 ? 2.125 53.477 74.027 1.00 29.28 ? 365 ALA A C 1 ATOM 2666 O O . ALA A 1 372 ? 1.147 53.731 74.775 1.00 29.33 ? 365 ALA A O 1 ATOM 2667 C CB . ALA A 1 372 ? 3.632 51.725 74.953 1.00 28.50 ? 365 ALA A CB 1 ATOM 2668 N N . VAL A 1 373 ? 2.815 54.424 73.391 1.00 28.18 ? 366 VAL A N 1 ATOM 2669 C CA . VAL A 1 373 ? 2.535 55.868 73.612 1.00 28.82 ? 366 VAL A CA 1 ATOM 2670 C C . VAL A 1 373 ? 2.049 56.563 72.335 1.00 27.99 ? 366 VAL A C 1 ATOM 2671 O O . VAL A 1 373 ? 1.078 57.335 72.353 1.00 28.28 ? 366 VAL A O 1 ATOM 2672 C CB . VAL A 1 373 ? 3.779 56.603 74.174 1.00 30.50 ? 366 VAL A CB 1 ATOM 2673 C CG1 . VAL A 1 373 ? 3.497 58.106 74.378 1.00 31.13 ? 366 VAL A CG1 1 ATOM 2674 C CG2 . VAL A 1 373 ? 4.247 55.969 75.488 1.00 32.78 ? 366 VAL A CG2 1 ATOM 2675 N N . GLU A 1 374 ? 2.720 56.275 71.216 1.00 26.33 ? 367 GLU A N 1 ATOM 2676 C CA . GLU A 1 374 ? 2.314 56.840 69.933 1.00 26.00 ? 367 GLU A CA 1 ATOM 2677 C C . GLU A 1 374 ? 2.019 55.739 68.918 1.00 23.79 ? 367 GLU A C 1 ATOM 2678 O O . GLU A 1 374 ? 2.805 55.559 67.962 1.00 23.10 ? 367 GLU A O 1 ATOM 2679 C CB . GLU A 1 374 ? 3.403 57.748 69.407 1.00 25.21 ? 367 GLU A CB 1 ATOM 2680 C CG . GLU A 1 374 ? 3.709 58.941 70.320 1.00 27.70 ? 367 GLU A CG 1 ATOM 2681 C CD . GLU A 1 374 ? 4.699 59.874 69.639 1.00 27.03 ? 367 GLU A CD 1 ATOM 2682 O OE1 . GLU A 1 374 ? 4.263 60.809 68.928 1.00 28.82 ? 367 GLU A OE1 1 ATOM 2683 O OE2 . GLU A 1 374 ? 5.906 59.694 69.865 1.00 31.12 ? 367 GLU A OE2 1 ATOM 2684 N N . PRO A 1 375 ? 0.914 54.993 69.120 1.00 24.14 ? 368 PRO A N 1 ATOM 2685 C CA . PRO A 1 375 ? 0.588 53.899 68.205 1.00 23.91 ? 368 PRO A CA 1 ATOM 2686 C C . PRO A 1 375 ? 0.262 54.383 66.810 1.00 23.46 ? 368 PRO A C 1 ATOM 2687 O O . PRO A 1 375 ? 0.362 53.593 65.882 1.00 23.06 ? 368 PRO A O 1 ATOM 2688 C CB . PRO A 1 375 ? -0.630 53.222 68.846 1.00 24.78 ? 368 PRO A CB 1 ATOM 2689 C CG . PRO A 1 375 ? -1.227 54.261 69.700 1.00 25.60 ? 368 PRO A CG 1 ATOM 2690 C CD . PRO A 1 375 ? -0.087 55.087 70.220 1.00 25.14 ? 368 PRO A CD 1 ATOM 2691 N N . ASP A 1 376 ? -0.058 55.677 66.666 1.00 23.17 ? 369 ASP A N 1 ATOM 2692 C CA . ASP A 1 376 ? -0.315 56.249 65.341 1.00 22.63 ? 369 ASP A CA 1 ATOM 2693 C C . ASP A 1 376 ? 0.950 56.826 64.679 1.00 21.25 ? 369 ASP A C 1 ATOM 2694 O O . ASP A 1 376 ? 0.840 57.695 63.823 1.00 19.95 ? 369 ASP A O 1 ATOM 2695 C CB . ASP A 1 376 ? -1.398 57.336 65.438 1.00 23.44 ? 369 ASP A CB 1 ATOM 2696 C CG . ASP A 1 376 ? -0.915 58.566 66.167 1.00 27.51 ? 369 ASP A CG 1 ATOM 2697 O OD1 . ASP A 1 376 ? 0.035 58.477 66.983 1.00 29.93 ? 369 ASP A OD1 1 ATOM 2698 O OD2 . ASP A 1 376 ? -1.509 59.658 65.950 1.00 29.52 ? 369 ASP A OD2 1 ATOM 2699 N N . ARG A 1 377 ? 2.135 56.346 65.067 1.00 21.05 ? 370 ARG A N 1 ATOM 2700 C CA . ARG A 1 377 ? 3.376 56.732 64.415 1.00 20.78 ? 370 ARG A CA 1 ATOM 2701 C C . ARG A 1 377 ? 4.045 55.440 64.039 1.00 21.26 ? 370 ARG A C 1 ATOM 2702 O O . ARG A 1 377 ? 4.177 54.561 64.887 1.00 20.69 ? 370 ARG A O 1 ATOM 2703 C CB . ARG A 1 377 ? 4.265 57.553 65.374 1.00 21.06 ? 370 ARG A CB 1 ATOM 2704 C CG . ARG A 1 377 ? 3.618 58.944 65.688 1.00 20.54 ? 370 ARG A CG 1 ATOM 2705 C CD . ARG A 1 377 ? 3.812 59.818 64.446 1.00 21.45 ? 370 ARG A CD 1 ATOM 2706 N NE . ARG A 1 377 ? 3.182 61.162 64.497 1.00 19.93 ? 370 ARG A NE 1 ATOM 2707 C CZ . ARG A 1 377 ? 1.944 61.472 64.060 1.00 20.35 ? 370 ARG A CZ 1 ATOM 2708 N NH1 . ARG A 1 377 ? 1.075 60.543 63.639 1.00 19.79 ? 370 ARG A NH1 1 ATOM 2709 N NH2 . ARG A 1 377 ? 1.562 62.748 64.043 1.00 20.93 ? 370 ARG A NH2 1 ATOM 2710 N N . TYR A 1 378 ? 4.430 55.322 62.776 1.00 19.70 ? 371 TYR A N 1 ATOM 2711 C CA . TYR A 1 378 ? 4.918 54.041 62.257 1.00 19.68 ? 371 TYR A CA 1 ATOM 2712 C C . TYR A 1 378 ? 6.367 54.108 61.872 1.00 20.14 ? 371 TYR A C 1 ATOM 2713 O O . TYR A 1 378 ? 6.795 54.939 61.035 1.00 20.42 ? 371 TYR A O 1 ATOM 2714 C CB . TYR A 1 378 ? 4.153 53.636 60.978 1.00 19.20 ? 371 TYR A CB 1 ATOM 2715 C CG . TYR A 1 378 ? 2.655 53.562 61.114 1.00 19.36 ? 371 TYR A CG 1 ATOM 2716 C CD1 . TYR A 1 378 ? 2.029 53.195 62.313 1.00 21.21 ? 371 TYR A CD1 1 ATOM 2717 C CD2 . TYR A 1 378 ? 1.846 53.842 60.014 1.00 19.64 ? 371 TYR A CD2 1 ATOM 2718 C CE1 . TYR A 1 378 ? 0.638 53.144 62.405 1.00 20.56 ? 371 TYR A CE1 1 ATOM 2719 C CE2 . TYR A 1 378 ? 0.477 53.797 60.083 1.00 19.90 ? 371 TYR A CE2 1 ATOM 2720 C CZ . TYR A 1 378 ? -0.139 53.411 61.284 1.00 20.06 ? 371 TYR A CZ 1 ATOM 2721 O OH . TYR A 1 378 ? -1.511 53.371 61.363 1.00 22.00 ? 371 TYR A OH 1 ATOM 2722 N N . VAL A 1 379 ? 7.127 53.170 62.420 1.00 19.17 ? 372 VAL A N 1 ATOM 2723 C CA . VAL A 1 379 ? 8.513 52.949 61.989 1.00 19.11 ? 372 VAL A CA 1 ATOM 2724 C C . VAL A 1 379 ? 8.486 51.600 61.272 1.00 19.20 ? 372 VAL A C 1 ATOM 2725 O O . VAL A 1 379 ? 8.050 50.606 61.847 1.00 19.33 ? 372 VAL A O 1 ATOM 2726 C CB . VAL A 1 379 ? 9.472 52.907 63.220 1.00 20.35 ? 372 VAL A CB 1 ATOM 2727 C CG1 . VAL A 1 379 ? 10.901 52.551 62.762 1.00 21.11 ? 372 VAL A CG1 1 ATOM 2728 C CG2 . VAL A 1 379 ? 9.514 54.288 63.873 1.00 20.51 ? 372 VAL A CG2 1 ATOM 2729 N N . ILE A 1 380 ? 8.931 51.569 60.016 1.00 18.02 ? 373 ILE A N 1 ATOM 2730 C CA . ILE A 1 380 ? 8.739 50.383 59.178 1.00 17.81 ? 373 ILE A CA 1 ATOM 2731 C C . ILE A 1 380 ? 10.094 49.758 58.847 1.00 18.30 ? 373 ILE A C 1 ATOM 2732 O O . ILE A 1 380 ? 11.023 50.432 58.391 1.00 19.16 ? 373 ILE A O 1 ATOM 2733 C CB . ILE A 1 380 ? 8.023 50.779 57.865 1.00 16.66 ? 373 ILE A CB 1 ATOM 2734 C CG1 . ILE A 1 380 ? 6.723 51.525 58.212 1.00 19.05 ? 373 ILE A CG1 1 ATOM 2735 C CG2 . ILE A 1 380 ? 7.771 49.499 56.977 1.00 18.11 ? 373 ILE A CG2 1 ATOM 2736 C CD1 . ILE A 1 380 ? 6.064 52.140 56.956 1.00 22.81 ? 373 ILE A CD1 1 ATOM 2737 N N . LEU A 1 381 ? 10.190 48.455 59.093 1.00 17.64 ? 374 LEU A N 1 ATOM 2738 C CA . LEU A 1 381 ? 11.355 47.669 58.648 1.00 17.58 ? 374 LEU A CA 1 ATOM 2739 C C . LEU A 1 381 ? 10.850 46.719 57.584 1.00 17.96 ? 374 LEU A C 1 ATOM 2740 O O . LEU A 1 381 ? 10.042 45.824 57.868 1.00 18.94 ? 374 LEU A O 1 ATOM 2741 C CB . LEU A 1 381 ? 11.991 46.895 59.831 1.00 18.89 ? 374 LEU A CB 1 ATOM 2742 C CG . LEU A 1 381 ? 13.103 45.905 59.435 1.00 19.25 ? 374 LEU A CG 1 ATOM 2743 C CD1 . LEU A 1 381 ? 14.334 46.674 58.946 1.00 20.98 ? 374 LEU A CD1 1 ATOM 2744 C CD2 . LEU A 1 381 ? 13.477 45.072 60.700 1.00 20.40 ? 374 LEU A CD2 1 ATOM 2745 N N . GLY A 1 382 ? 11.309 46.914 56.348 1.00 17.59 ? 375 GLY A N 1 ATOM 2746 C CA . GLY A 1 382 ? 10.782 46.065 55.281 1.00 17.74 ? 375 GLY A CA 1 ATOM 2747 C C . GLY A 1 382 ? 11.884 45.545 54.361 1.00 18.06 ? 375 GLY A C 1 ATOM 2748 O O . GLY A 1 382 ? 12.883 46.221 54.105 1.00 19.50 ? 375 GLY A O 1 ATOM 2749 N N . GLY A 1 383 ? 11.639 44.380 53.771 1.00 18.19 ? 376 GLY A N 1 ATOM 2750 C CA . GLY A 1 383 ? 12.589 43.878 52.769 1.00 18.63 ? 376 GLY A CA 1 ATOM 2751 C C . GLY A 1 383 ? 11.856 42.785 52.019 1.00 18.38 ? 376 GLY A C 1 ATOM 2752 O O . GLY A 1 383 ? 10.869 42.252 52.526 1.00 19.03 ? 376 GLY A O 1 ATOM 2753 N N . HIS A 1 384 ? 12.343 42.406 50.841 1.00 17.92 ? 377 HIS A N 1 ATOM 2754 C CA . HIS A 1 384 ? 11.551 41.433 50.063 1.00 17.11 ? 377 HIS A CA 1 ATOM 2755 C C . HIS A 1 384 ? 11.923 39.990 50.350 1.00 18.25 ? 377 HIS A C 1 ATOM 2756 O O . HIS A 1 384 ? 12.963 39.696 50.998 1.00 19.77 ? 377 HIS A O 1 ATOM 2757 C CB . HIS A 1 384 ? 11.620 41.770 48.563 1.00 17.03 ? 377 HIS A CB 1 ATOM 2758 C CG . HIS A 1 384 ? 12.927 41.451 47.882 1.00 17.60 ? 377 HIS A CG 1 ATOM 2759 N ND1 . HIS A 1 384 ? 13.067 40.349 47.059 1.00 17.79 ? 377 HIS A ND1 1 ATOM 2760 C CD2 . HIS A 1 384 ? 14.069 42.167 47.741 1.00 16.66 ? 377 HIS A CD2 1 ATOM 2761 C CE1 . HIS A 1 384 ? 14.260 40.380 46.475 1.00 17.95 ? 377 HIS A CE1 1 ATOM 2762 N NE2 . HIS A 1 384 ? 14.900 41.457 46.899 1.00 18.03 ? 377 HIS A NE2 1 ATOM 2763 N N . ARG A 1 385 ? 11.067 39.100 49.843 1.00 16.97 ? 378 ARG A N 1 ATOM 2764 C CA . ARG A 1 385 ? 11.140 37.680 50.147 1.00 18.19 ? 378 ARG A CA 1 ATOM 2765 C C . ARG A 1 385 ? 11.295 36.897 48.866 1.00 18.31 ? 378 ARG A C 1 ATOM 2766 O O . ARG A 1 385 ? 11.858 35.800 48.864 1.00 18.71 ? 378 ARG A O 1 ATOM 2767 C CB . ARG A 1 385 ? 9.839 37.273 50.824 1.00 18.86 ? 378 ARG A CB 1 ATOM 2768 C CG . ARG A 1 385 ? 9.741 35.772 51.209 1.00 20.81 ? 378 ARG A CG 1 ATOM 2769 C CD . ARG A 1 385 ? 8.322 35.440 51.703 1.00 19.83 ? 378 ARG A CD 1 ATOM 2770 N NE . ARG A 1 385 ? 7.315 35.488 50.621 1.00 20.41 ? 378 ARG A NE 1 ATOM 2771 C CZ . ARG A 1 385 ? 6.422 36.453 50.435 1.00 19.35 ? 378 ARG A CZ 1 ATOM 2772 N NH1 . ARG A 1 385 ? 6.325 37.496 51.270 1.00 18.48 ? 378 ARG A NH1 1 ATOM 2773 N NH2 . ARG A 1 385 ? 5.565 36.365 49.410 1.00 20.47 ? 378 ARG A NH2 1 ATOM 2774 N N . ASP A 1 386 ? 10.734 37.430 47.767 1.00 18.57 ? 379 ASP A N 1 ATOM 2775 C CA . ASP A 1 386 ? 10.811 36.720 46.479 1.00 18.19 ? 379 ASP A CA 1 ATOM 2776 C C . ASP A 1 386 ? 12.252 36.745 45.977 1.00 17.90 ? 379 ASP A C 1 ATOM 2777 O O . ASP A 1 386 ? 12.964 37.732 46.168 1.00 18.05 ? 379 ASP A O 1 ATOM 2778 C CB . ASP A 1 386 ? 9.886 37.386 45.455 1.00 17.48 ? 379 ASP A CB 1 ATOM 2779 C CG . ASP A 1 386 ? 10.325 38.802 45.116 1.00 17.87 ? 379 ASP A CG 1 ATOM 2780 O OD1 . ASP A 1 386 ? 10.379 39.673 46.021 1.00 17.55 ? 379 ASP A OD1 1 ATOM 2781 O OD2 . ASP A 1 386 ? 10.596 39.056 43.933 1.00 18.13 ? 379 ASP A OD2 1 ATOM 2782 N N . SER A 1 387 ? 12.653 35.667 45.303 1.00 18.36 ? 380 SER A N 1 ATOM 2783 C CA . SER A 1 387 ? 13.991 35.569 44.793 1.00 19.38 ? 380 SER A CA 1 ATOM 2784 C C . SER A 1 387 ? 13.953 35.106 43.345 1.00 20.36 ? 380 SER A C 1 ATOM 2785 O O . SER A 1 387 ? 12.921 34.591 42.866 1.00 20.11 ? 380 SER A O 1 ATOM 2786 C CB . SER A 1 387 ? 14.776 34.568 45.660 1.00 19.95 ? 380 SER A CB 1 ATOM 2787 O OG . SER A 1 387 ? 14.200 33.254 45.596 1.00 20.88 ? 380 SER A OG 1 ATOM 2788 N N . TRP A 1 388 ? 15.051 35.293 42.627 1.00 20.41 ? 381 TRP A N 1 ATOM 2789 C CA . TRP A 1 388 ? 15.114 34.731 41.273 1.00 19.40 ? 381 TRP A CA 1 ATOM 2790 C C . TRP A 1 388 ? 15.238 33.222 41.306 1.00 21.18 ? 381 TRP A C 1 ATOM 2791 O O . TRP A 1 388 ? 14.509 32.536 40.625 1.00 20.96 ? 381 TRP A O 1 ATOM 2792 C CB . TRP A 1 388 ? 16.241 35.375 40.433 1.00 19.68 ? 381 TRP A CB 1 ATOM 2793 C CG . TRP A 1 388 ? 15.787 36.704 39.877 1.00 19.60 ? 381 TRP A CG 1 ATOM 2794 C CD1 . TRP A 1 388 ? 16.317 37.952 40.131 1.00 19.08 ? 381 TRP A CD1 1 ATOM 2795 C CD2 . TRP A 1 388 ? 14.688 36.898 38.986 1.00 18.73 ? 381 TRP A CD2 1 ATOM 2796 N NE1 . TRP A 1 388 ? 15.597 38.919 39.440 1.00 18.25 ? 381 TRP A NE1 1 ATOM 2797 C CE2 . TRP A 1 388 ? 14.587 38.290 38.739 1.00 19.02 ? 381 TRP A CE2 1 ATOM 2798 C CE3 . TRP A 1 388 ? 13.747 36.018 38.386 1.00 19.54 ? 381 TRP A CE3 1 ATOM 2799 C CZ2 . TRP A 1 388 ? 13.579 38.837 37.932 1.00 19.03 ? 381 TRP A CZ2 1 ATOM 2800 C CZ3 . TRP A 1 388 ? 12.737 36.563 37.582 1.00 18.86 ? 381 TRP A CZ3 1 ATOM 2801 C CH2 . TRP A 1 388 ? 12.652 37.963 37.377 1.00 19.25 ? 381 TRP A CH2 1 ATOM 2802 N N . VAL A 1 389 ? 16.152 32.702 42.115 1.00 21.00 ? 382 VAL A N 1 ATOM 2803 C CA . VAL A 1 389 ? 16.237 31.251 42.316 1.00 20.77 ? 382 VAL A CA 1 ATOM 2804 C C . VAL A 1 389 ? 16.290 31.012 43.833 1.00 21.38 ? 382 VAL A C 1 ATOM 2805 O O . VAL A 1 389 ? 15.276 31.191 44.511 1.00 20.64 ? 382 VAL A O 1 ATOM 2806 C CB . VAL A 1 389 ? 17.402 30.563 41.522 1.00 20.72 ? 382 VAL A CB 1 ATOM 2807 C CG1 . VAL A 1 389 ? 17.206 29.028 41.605 1.00 21.81 ? 382 VAL A CG1 1 ATOM 2808 C CG2 . VAL A 1 389 ? 17.392 30.973 40.031 1.00 22.04 ? 382 VAL A CG2 1 ATOM 2809 N N . PHE A 1 390 ? 17.446 30.632 44.380 1.00 21.24 ? 383 PHE A N 1 ATOM 2810 C CA . PHE A 1 390 ? 17.522 30.310 45.814 1.00 20.70 ? 383 PHE A CA 1 ATOM 2811 C C . PHE A 1 390 ? 17.648 31.515 46.721 1.00 21.49 ? 383 PHE A C 1 ATOM 2812 O O . PHE A 1 390 ? 17.283 31.435 47.901 1.00 22.46 ? 383 PHE A O 1 ATOM 2813 C CB . PHE A 1 390 ? 18.666 29.319 46.095 1.00 21.02 ? 383 PHE A CB 1 ATOM 2814 C CG . PHE A 1 390 ? 18.514 28.046 45.322 1.00 21.96 ? 383 PHE A CG 1 ATOM 2815 C CD1 . PHE A 1 390 ? 17.508 27.128 45.664 1.00 22.98 ? 383 PHE A CD1 1 ATOM 2816 C CD2 . PHE A 1 390 ? 19.307 27.813 44.204 1.00 23.97 ? 383 PHE A CD2 1 ATOM 2817 C CE1 . PHE A 1 390 ? 17.346 25.947 44.903 1.00 24.78 ? 383 PHE A CE1 1 ATOM 2818 C CE2 . PHE A 1 390 ? 19.148 26.627 43.452 1.00 23.37 ? 383 PHE A CE2 1 ATOM 2819 C CZ . PHE A 1 390 ? 18.163 25.728 43.801 1.00 24.37 ? 383 PHE A CZ 1 ATOM 2820 N N . GLY A 1 391 ? 18.105 32.644 46.170 1.00 20.95 ? 384 GLY A N 1 ATOM 2821 C CA . GLY A 1 391 ? 18.138 33.876 46.974 1.00 20.30 ? 384 GLY A CA 1 ATOM 2822 C C . GLY A 1 391 ? 19.105 33.847 48.161 1.00 20.64 ? 384 GLY A C 1 ATOM 2823 O O . GLY A 1 391 ? 18.859 34.549 49.167 1.00 20.97 ? 384 GLY A O 1 ATOM 2824 N N . GLY A 1 392 ? 20.211 33.101 48.019 1.00 21.71 ? 385 GLY A N 1 ATOM 2825 C CA . GLY A 1 392 ? 21.198 32.926 49.111 1.00 21.04 ? 385 GLY A CA 1 ATOM 2826 C C . GLY A 1 392 ? 21.679 34.256 49.668 1.00 21.65 ? 385 GLY A C 1 ATOM 2827 O O . GLY A 1 392 ? 21.780 34.428 50.885 1.00 22.49 ? 385 GLY A O 1 ATOM 2828 N N . ILE A 1 393 ? 21.958 35.216 48.778 1.00 21.03 ? 386 ILE A N 1 ATOM 2829 C CA . ILE A 1 393 ? 22.237 36.565 49.279 1.00 20.57 ? 386 ILE A CA 1 ATOM 2830 C C . ILE A 1 393 ? 20.979 37.423 49.092 1.00 21.11 ? 386 ILE A C 1 ATOM 2831 O O . ILE A 1 393 ? 20.459 37.998 50.062 1.00 20.22 ? 386 ILE A O 1 ATOM 2832 C CB . ILE A 1 393 ? 23.479 37.201 48.577 1.00 20.37 ? 386 ILE A CB 1 ATOM 2833 C CG1 . ILE A 1 393 ? 24.766 36.510 49.083 1.00 21.88 ? 386 ILE A CG1 1 ATOM 2834 C CG2 . ILE A 1 393 ? 23.513 38.716 48.845 1.00 19.91 ? 386 ILE A CG2 1 ATOM 2835 C CD1 . ILE A 1 393 ? 25.998 36.913 48.303 1.00 24.54 ? 386 ILE A CD1 1 ATOM 2836 N N . ASP A 1 394 ? 20.489 37.495 47.862 1.00 20.70 ? 387 ASP A N 1 ATOM 2837 C CA . ASP A 1 394 ? 19.416 38.429 47.497 1.00 19.50 ? 387 ASP A CA 1 ATOM 2838 C C . ASP A 1 394 ? 18.111 37.634 47.347 1.00 19.57 ? 387 ASP A C 1 ATOM 2839 O O . ASP A 1 394 ? 17.938 36.934 46.345 1.00 20.43 ? 387 ASP A O 1 ATOM 2840 C CB . ASP A 1 394 ? 19.810 39.055 46.160 1.00 19.68 ? 387 ASP A CB 1 ATOM 2841 C CG . ASP A 1 394 ? 18.808 40.021 45.650 1.00 20.97 ? 387 ASP A CG 1 ATOM 2842 O OD1 . ASP A 1 394 ? 17.845 40.293 46.379 1.00 18.84 ? 387 ASP A OD1 1 ATOM 2843 O OD2 . ASP A 1 394 ? 18.983 40.483 44.491 1.00 21.11 ? 387 ASP A OD2 1 ATOM 2844 N N . PRO A 1 395 ? 17.166 37.744 48.308 1.00 19.32 ? 388 PRO A N 1 ATOM 2845 C CA . PRO A 1 395 ? 17.131 38.660 49.460 1.00 18.87 ? 388 PRO A CA 1 ATOM 2846 C C . PRO A 1 395 ? 17.290 37.927 50.785 1.00 19.67 ? 388 PRO A C 1 ATOM 2847 O O . PRO A 1 395 ? 17.134 38.566 51.832 1.00 19.55 ? 388 PRO A O 1 ATOM 2848 C CB . PRO A 1 395 ? 15.681 39.169 49.420 1.00 19.21 ? 388 PRO A CB 1 ATOM 2849 C CG . PRO A 1 395 ? 14.893 37.887 49.058 1.00 18.88 ? 388 PRO A CG 1 ATOM 2850 C CD . PRO A 1 395 ? 15.821 37.146 48.075 1.00 19.35 ? 388 PRO A CD 1 ATOM 2851 N N . GLN A 1 396 ? 17.538 36.608 50.778 1.00 19.96 ? 389 GLN A N 1 ATOM 2852 C CA . GLN A 1 396 ? 17.300 35.895 52.042 1.00 20.68 ? 389 GLN A CA 1 ATOM 2853 C C . GLN A 1 396 ? 18.330 36.225 53.127 1.00 20.84 ? 389 GLN A C 1 ATOM 2854 O O . GLN A 1 396 ? 18.050 36.060 54.307 1.00 21.23 ? 389 GLN A O 1 ATOM 2855 C CB . GLN A 1 396 ? 17.214 34.370 51.848 1.00 21.06 ? 389 GLN A CB 1 ATOM 2856 C CG . GLN A 1 396 ? 16.166 33.902 50.827 1.00 19.57 ? 389 GLN A CG 1 ATOM 2857 C CD . GLN A 1 396 ? 14.730 34.467 51.070 1.00 20.03 ? 389 GLN A CD 1 ATOM 2858 O OE1 . GLN A 1 396 ? 14.415 35.056 52.110 1.00 21.58 ? 389 GLN A OE1 1 ATOM 2859 N NE2 . GLN A 1 396 ? 13.852 34.226 50.104 1.00 20.52 ? 389 GLN A NE2 1 ATOM 2860 N N . SER A 1 397 ? 19.507 36.714 52.744 1.00 20.73 ? 390 SER A N 1 ATOM 2861 C CA . SER A 1 397 ? 20.450 37.182 53.770 1.00 21.82 ? 390 SER A CA 1 ATOM 2862 C C . SER A 1 397 ? 19.877 38.380 54.522 1.00 21.72 ? 390 SER A C 1 ATOM 2863 O O . SER A 1 397 ? 20.183 38.575 55.731 1.00 22.18 ? 390 SER A O 1 ATOM 2864 C CB . SER A 1 397 ? 21.844 37.498 53.179 1.00 21.44 ? 390 SER A CB 1 ATOM 2865 O OG . SER A 1 397 ? 21.786 38.654 52.362 1.00 21.93 ? 390 SER A OG 1 ATOM 2866 N N . GLY A 1 398 ? 19.038 39.155 53.824 1.00 20.80 ? 391 GLY A N 1 ATOM 2867 C CA . GLY A 1 398 ? 18.313 40.272 54.431 1.00 19.44 ? 391 GLY A CA 1 ATOM 2868 C C . GLY A 1 398 ? 17.106 39.760 55.195 1.00 19.46 ? 391 GLY A C 1 ATOM 2869 O O . GLY A 1 398 ? 16.864 40.197 56.324 1.00 20.91 ? 391 GLY A O 1 ATOM 2870 N N . ALA A 1 399 ? 16.315 38.879 54.580 1.00 19.13 ? 392 ALA A N 1 ATOM 2871 C CA . ALA A 1 399 ? 15.104 38.377 55.243 1.00 20.24 ? 392 ALA A CA 1 ATOM 2872 C C . ALA A 1 399 ? 15.377 37.621 56.527 1.00 21.06 ? 392 ALA A C 1 ATOM 2873 O O . ALA A 1 399 ? 14.560 37.695 57.459 1.00 20.10 ? 392 ALA A O 1 ATOM 2874 C CB . ALA A 1 399 ? 14.247 37.525 54.296 1.00 20.67 ? 392 ALA A CB 1 ATOM 2875 N N . ALA A 1 400 ? 16.493 36.885 56.576 1.00 22.04 ? 393 ALA A N 1 ATOM 2876 C CA . ALA A 1 400 ? 16.885 36.137 57.797 1.00 21.93 ? 393 ALA A CA 1 ATOM 2877 C C . ALA A 1 400 ? 17.220 37.114 58.909 1.00 22.89 ? 393 ALA A C 1 ATOM 2878 O O . ALA A 1 400 ? 16.970 36.840 60.087 1.00 22.72 ? 393 ALA A O 1 ATOM 2879 C CB . ALA A 1 400 ? 18.121 35.217 57.510 1.00 22.34 ? 393 ALA A CB 1 ATOM 2880 N N . VAL A 1 401 ? 17.801 38.250 58.524 1.00 21.98 ? 394 VAL A N 1 ATOM 2881 C CA . VAL A 1 401 ? 18.112 39.309 59.493 1.00 21.63 ? 394 VAL A CA 1 ATOM 2882 C C . VAL A 1 401 ? 16.809 39.934 60.016 1.00 22.24 ? 394 VAL A C 1 ATOM 2883 O O . VAL A 1 401 ? 16.653 40.127 61.231 1.00 21.52 ? 394 VAL A O 1 ATOM 2884 C CB . VAL A 1 401 ? 19.096 40.356 58.891 1.00 22.27 ? 394 VAL A CB 1 ATOM 2885 C CG1 . VAL A 1 401 ? 18.975 41.723 59.599 1.00 21.73 ? 394 VAL A CG1 1 ATOM 2886 C CG2 . VAL A 1 401 ? 20.540 39.805 58.983 1.00 22.48 ? 394 VAL A CG2 1 ATOM 2887 N N . VAL A 1 402 ? 15.860 40.236 59.112 1.00 20.47 ? 395 VAL A N 1 ATOM 2888 C CA . VAL A 1 402 ? 14.580 40.771 59.580 1.00 20.85 ? 395 VAL A CA 1 ATOM 2889 C C . VAL A 1 402 ? 13.897 39.777 60.535 1.00 21.24 ? 395 VAL A C 1 ATOM 2890 O O . VAL A 1 402 ? 13.350 40.169 61.549 1.00 21.49 ? 395 VAL A O 1 ATOM 2891 C CB . VAL A 1 402 ? 13.634 41.069 58.402 1.00 20.33 ? 395 VAL A CB 1 ATOM 2892 C CG1 . VAL A 1 402 ? 12.216 41.480 58.929 1.00 21.06 ? 395 VAL A CG1 1 ATOM 2893 C CG2 . VAL A 1 402 ? 14.237 42.190 57.546 1.00 22.14 ? 395 VAL A CG2 1 ATOM 2894 N N . HIS A 1 403 ? 13.957 38.487 60.205 1.00 21.96 ? 396 HIS A N 1 ATOM 2895 C CA . HIS A 1 403 ? 13.302 37.436 60.997 1.00 21.52 ? 396 HIS A CA 1 ATOM 2896 C C . HIS A 1 403 ? 13.858 37.440 62.426 1.00 23.50 ? 396 HIS A C 1 ATOM 2897 O O . HIS A 1 403 ? 13.097 37.409 63.414 1.00 24.37 ? 396 HIS A O 1 ATOM 2898 C CB . HIS A 1 403 ? 13.526 36.070 60.312 1.00 22.93 ? 396 HIS A CB 1 ATOM 2899 C CG . HIS A 1 403 ? 12.365 35.117 60.423 1.00 22.62 ? 396 HIS A CG 1 ATOM 2900 N ND1 . HIS A 1 403 ? 11.069 35.475 60.102 1.00 24.85 ? 396 HIS A ND1 1 ATOM 2901 C CD2 . HIS A 1 403 ? 12.325 33.797 60.738 1.00 25.94 ? 396 HIS A CD2 1 ATOM 2902 C CE1 . HIS A 1 403 ? 10.273 34.431 60.266 1.00 26.21 ? 396 HIS A CE1 1 ATOM 2903 N NE2 . HIS A 1 403 ? 11.016 33.391 60.624 1.00 25.21 ? 396 HIS A NE2 1 ATOM 2904 N N . GLU A 1 404 ? 15.175 37.525 62.547 1.00 23.21 ? 397 GLU A N 1 ATOM 2905 C CA . GLU A 1 404 ? 15.820 37.561 63.873 1.00 24.07 ? 397 GLU A CA 1 ATOM 2906 C C . GLU A 1 404 ? 15.513 38.859 64.620 1.00 23.89 ? 397 GLU A C 1 ATOM 2907 O O . GLU A 1 404 ? 15.362 38.852 65.842 1.00 25.37 ? 397 GLU A O 1 ATOM 2908 C CB . GLU A 1 404 ? 17.336 37.342 63.724 1.00 25.43 ? 397 GLU A CB 1 ATOM 2909 C CG . GLU A 1 404 ? 18.159 37.347 65.043 1.00 24.67 ? 397 GLU A CG 1 ATOM 2910 C CD . GLU A 1 404 ? 17.768 36.261 66.031 1.00 29.71 ? 397 GLU A CD 1 ATOM 2911 O OE1 . GLU A 1 404 ? 16.774 35.531 65.795 1.00 29.32 ? 397 GLU A OE1 1 ATOM 2912 O OE2 . GLU A 1 404 ? 18.479 36.133 67.068 1.00 30.88 ? 397 GLU A OE2 1 ATOM 2913 N N . ILE A 1 405 ? 15.443 39.981 63.895 1.00 22.87 ? 398 ILE A N 1 ATOM 2914 C CA . ILE A 1 405 ? 15.030 41.249 64.511 1.00 23.17 ? 398 ILE A CA 1 ATOM 2915 C C . ILE A 1 405 ? 13.605 41.149 65.062 1.00 23.62 ? 398 ILE A C 1 ATOM 2916 O O . ILE A 1 405 ? 13.346 41.561 66.199 1.00 24.69 ? 398 ILE A O 1 ATOM 2917 C CB . ILE A 1 405 ? 15.179 42.419 63.507 1.00 21.85 ? 398 ILE A CB 1 ATOM 2918 C CG1 . ILE A 1 405 ? 16.676 42.753 63.331 1.00 21.45 ? 398 ILE A CG1 1 ATOM 2919 C CG2 . ILE A 1 405 ? 14.350 43.675 63.977 1.00 22.61 ? 398 ILE A CG2 1 ATOM 2920 C CD1 . ILE A 1 405 ? 16.957 43.607 62.042 1.00 20.33 ? 398 ILE A CD1 1 ATOM 2921 N N . VAL A 1 406 ? 12.676 40.586 64.284 1.00 23.76 ? 399 VAL A N 1 ATOM 2922 C CA . VAL A 1 406 ? 11.289 40.374 64.784 1.00 24.27 ? 399 VAL A CA 1 ATOM 2923 C C . VAL A 1 406 ? 11.310 39.486 66.032 1.00 24.88 ? 399 VAL A C 1 ATOM 2924 O O . VAL A 1 406 ? 10.647 39.800 67.042 1.00 26.81 ? 399 VAL A O 1 ATOM 2925 C CB . VAL A 1 406 ? 10.343 39.735 63.727 1.00 23.43 ? 399 VAL A CB 1 ATOM 2926 C CG1 . VAL A 1 406 ? 8.950 39.387 64.335 1.00 24.65 ? 399 VAL A CG1 1 ATOM 2927 C CG2 . VAL A 1 406 ? 10.197 40.669 62.465 1.00 23.22 ? 399 VAL A CG2 1 ATOM 2928 N N . ARG A 1 407 ? 12.073 38.398 65.968 1.00 25.32 ? 400 ARG A N 1 ATOM 2929 C CA . ARG A 1 407 ? 12.178 37.482 67.103 1.00 26.77 ? 400 ARG A CA 1 ATOM 2930 C C . ARG A 1 407 ? 12.632 38.218 68.355 1.00 27.84 ? 400 ARG A C 1 ATOM 2931 O O . ARG A 1 407 ? 12.080 37.985 69.455 1.00 29.27 ? 400 ARG A O 1 ATOM 2932 C CB . ARG A 1 407 ? 13.113 36.301 66.808 1.00 26.73 ? 400 ARG A CB 1 ATOM 2933 C CG . ARG A 1 407 ? 12.920 35.122 67.793 1.00 28.30 ? 400 ARG A CG 1 ATOM 2934 C CD . ARG A 1 407 ? 14.117 34.102 67.721 1.00 29.74 ? 400 ARG A CD 1 ATOM 2935 N NE . ARG A 1 407 ? 15.384 34.763 68.045 1.00 29.42 ? 400 ARG A NE 1 ATOM 2936 C CZ . ARG A 1 407 ? 15.766 35.106 69.279 1.00 32.88 ? 400 ARG A CZ 1 ATOM 2937 N NH1 . ARG A 1 407 ? 16.919 35.739 69.463 1.00 30.67 ? 400 ARG A NH1 1 ATOM 2938 N NH2 . ARG A 1 407 ? 15.006 34.804 70.336 1.00 33.01 ? 400 ARG A NH2 1 ATOM 2939 N N . SER A 1 408 ? 13.648 39.073 68.206 1.00 28.27 ? 401 SER A N 1 ATOM 2940 C CA . SER A 1 408 ? 14.199 39.805 69.344 1.00 29.23 ? 401 SER A CA 1 ATOM 2941 C C . SER A 1 408 ? 13.209 40.828 69.908 1.00 29.18 ? 401 SER A C 1 ATOM 2942 O O . SER A 1 408 ? 12.974 40.857 71.130 1.00 29.25 ? 401 SER A O 1 ATOM 2943 C CB . SER A 1 408 ? 15.564 40.449 69.030 1.00 29.85 ? 401 SER A CB 1 ATOM 2944 O OG . SER A 1 408 ? 16.017 41.215 70.167 1.00 33.05 ? 401 SER A OG 1 ATOM 2945 N N . PHE A 1 409 ? 12.604 41.659 69.048 1.00 27.74 ? 402 PHE A N 1 ATOM 2946 C CA . PHE A 1 409 ? 11.576 42.572 69.550 1.00 28.49 ? 402 PHE A CA 1 ATOM 2947 C C . PHE A 1 409 ? 10.448 41.820 70.243 1.00 29.69 ? 402 PHE A C 1 ATOM 2948 O O . PHE A 1 409 ? 9.914 42.275 71.263 1.00 31.12 ? 402 PHE A O 1 ATOM 2949 C CB . PHE A 1 409 ? 10.989 43.422 68.411 1.00 26.92 ? 402 PHE A CB 1 ATOM 2950 C CG . PHE A 1 409 ? 11.802 44.628 68.053 1.00 26.98 ? 402 PHE A CG 1 ATOM 2951 C CD1 . PHE A 1 409 ? 11.972 45.673 68.967 1.00 27.54 ? 402 PHE A CD1 1 ATOM 2952 C CD2 . PHE A 1 409 ? 12.318 44.775 66.765 1.00 25.41 ? 402 PHE A CD2 1 ATOM 2953 C CE1 . PHE A 1 409 ? 12.675 46.827 68.618 1.00 25.41 ? 402 PHE A CE1 1 ATOM 2954 C CE2 . PHE A 1 409 ? 13.025 45.935 66.397 1.00 25.16 ? 402 PHE A CE2 1 ATOM 2955 C CZ . PHE A 1 409 ? 13.217 46.955 67.324 1.00 26.04 ? 402 PHE A CZ 1 ATOM 2956 N N . GLY A 1 410 ? 10.093 40.654 69.703 1.00 29.65 ? 403 GLY A N 1 ATOM 2957 C CA . GLY A 1 410 ? 9.021 39.845 70.258 1.00 30.32 ? 403 GLY A CA 1 ATOM 2958 C C . GLY A 1 410 ? 9.365 39.260 71.625 1.00 32.19 ? 403 GLY A C 1 ATOM 2959 O O . GLY A 1 410 ? 8.480 39.086 72.470 1.00 34.19 ? 403 GLY A O 1 ATOM 2960 N N . THR A 1 411 ? 10.644 38.962 71.858 1.00 33.07 ? 404 THR A N 1 ATOM 2961 C CA . THR A 1 411 ? 11.091 38.482 73.174 1.00 33.78 ? 404 THR A CA 1 ATOM 2962 C C . THR A 1 411 ? 10.869 39.568 74.228 1.00 34.86 ? 404 THR A C 1 ATOM 2963 O O . THR A 1 411 ? 10.414 39.272 75.343 1.00 36.41 ? 404 THR A O 1 ATOM 2964 C CB . THR A 1 411 ? 12.597 38.043 73.186 1.00 34.12 ? 404 THR A CB 1 ATOM 2965 O OG1 A THR A 1 411 ? 12.792 36.967 72.255 0.50 33.89 ? 404 THR A OG1 1 ATOM 2966 O OG1 B THR A 1 411 ? 13.452 39.191 73.171 0.50 34.54 ? 404 THR A OG1 1 ATOM 2967 C CG2 A THR A 1 411 ? 13.069 37.624 74.564 0.50 33.87 ? 404 THR A CG2 1 ATOM 2968 C CG2 B THR A 1 411 ? 12.932 37.091 72.036 0.50 33.54 ? 404 THR A CG2 1 ATOM 2969 N N . LEU A 1 412 ? 11.177 40.815 73.882 1.00 33.70 ? 405 LEU A N 1 ATOM 2970 C CA . LEU A 1 412 ? 10.980 41.923 74.810 1.00 34.28 ? 405 LEU A CA 1 ATOM 2971 C C . LEU A 1 412 ? 9.490 42.123 75.058 1.00 34.80 ? 405 LEU A C 1 ATOM 2972 O O . LEU A 1 412 ? 9.070 42.318 76.200 1.00 35.15 ? 405 LEU A O 1 ATOM 2973 C CB . LEU A 1 412 ? 11.613 43.235 74.289 1.00 34.84 ? 405 LEU A CB 1 ATOM 2974 C CG A LEU A 1 412 ? 13.129 43.303 74.077 0.50 34.24 ? 405 LEU A CG 1 ATOM 2975 C CG B LEU A 1 412 ? 13.101 43.511 74.567 0.50 33.96 ? 405 LEU A CG 1 ATOM 2976 C CD1 A LEU A 1 412 ? 13.498 44.592 73.366 0.50 33.35 ? 405 LEU A CD1 1 ATOM 2977 C CD1 B LEU A 1 412 ? 14.033 42.437 73.986 0.50 32.18 ? 405 LEU A CD1 1 ATOM 2978 C CD2 A LEU A 1 412 ? 13.865 43.189 75.401 0.50 35.86 ? 405 LEU A CD2 1 ATOM 2979 C CD2 B LEU A 1 412 ? 13.480 44.875 74.022 0.50 34.35 ? 405 LEU A CD2 1 ATOM 2980 N N . LYS A 1 413 ? 8.698 42.066 73.988 1.00 33.90 ? 406 LYS A N 1 ATOM 2981 C CA . LYS A 1 413 ? 7.253 42.201 74.091 1.00 35.09 ? 406 LYS A CA 1 ATOM 2982 C C . LYS A 1 413 ? 6.647 41.158 75.049 1.00 36.42 ? 406 LYS A C 1 ATOM 2983 O O . LYS A 1 413 ? 5.776 41.495 75.845 1.00 36.75 ? 406 LYS A O 1 ATOM 2984 C CB . LYS A 1 413 ? 6.610 42.129 72.702 1.00 35.08 ? 406 LYS A CB 1 ATOM 2985 C CG . LYS A 1 413 ? 5.152 42.569 72.665 1.00 38.39 ? 406 LYS A CG 1 ATOM 2986 C CD . LYS A 1 413 ? 4.202 41.386 72.613 1.00 44.68 ? 406 LYS A CD 1 ATOM 2987 C CE . LYS A 1 413 ? 2.850 41.842 72.046 1.00 45.84 ? 406 LYS A CE 1 ATOM 2988 N NZ . LYS A 1 413 ? 1.998 40.677 71.670 1.00 48.80 ? 406 LYS A NZ 1 ATOM 2989 N N . LYS A 1 414 ? 7.104 39.911 74.966 1.00 36.32 ? 407 LYS A N 1 ATOM 2990 C CA . LYS A 1 414 ? 6.603 38.843 75.858 1.00 38.28 ? 407 LYS A CA 1 ATOM 2991 C C . LYS A 1 414 ? 6.912 39.098 77.325 1.00 39.77 ? 407 LYS A C 1 ATOM 2992 O O . LYS A 1 414 ? 6.216 38.579 78.216 1.00 41.08 ? 407 LYS A O 1 ATOM 2993 C CB . LYS A 1 414 ? 7.099 37.464 75.417 1.00 38.13 ? 407 LYS A CB 1 ATOM 2994 C CG . LYS A 1 414 ? 6.426 37.021 74.130 1.00 39.55 ? 407 LYS A CG 1 ATOM 2995 C CD . LYS A 1 414 ? 7.002 35.730 73.566 1.00 40.76 ? 407 LYS A CD 1 ATOM 2996 C CE . LYS A 1 414 ? 6.189 35.317 72.345 1.00 40.44 ? 407 LYS A CE 1 ATOM 2997 N NZ . LYS A 1 414 ? 6.570 33.960 71.903 1.00 44.31 ? 407 LYS A NZ 1 ATOM 2998 N N . GLU A 1 415 ? 7.942 39.903 77.571 1.00 39.70 ? 408 GLU A N 1 ATOM 2999 C CA . GLU A 1 415 ? 8.314 40.310 78.933 1.00 41.39 ? 408 GLU A CA 1 ATOM 3000 C C . GLU A 1 415 ? 7.606 41.589 79.403 1.00 40.90 ? 408 GLU A C 1 ATOM 3001 O O . GLU A 1 415 ? 7.861 42.079 80.518 1.00 42.02 ? 408 GLU A O 1 ATOM 3002 C CB . GLU A 1 415 ? 9.831 40.474 79.038 1.00 42.02 ? 408 GLU A CB 1 ATOM 3003 C CG . GLU A 1 415 ? 10.622 39.203 78.727 0.90 45.99 ? 408 GLU A CG 1 ATOM 3004 C CD . GLU A 1 415 ? 12.126 39.378 78.899 0.85 51.14 ? 408 GLU A CD 1 ATOM 3005 O OE1 . GLU A 1 415 ? 12.825 38.357 79.093 0.80 54.56 ? 408 GLU A OE1 1 ATOM 3006 O OE2 . GLU A 1 415 ? 12.616 40.528 78.848 0.80 53.13 ? 408 GLU A OE2 1 ATOM 3007 N N . GLY A 1 416 ? 6.717 42.127 78.571 1.00 39.05 ? 409 GLY A N 1 ATOM 3008 C CA . GLY A 1 416 ? 5.885 43.280 78.956 1.00 38.72 ? 409 GLY A CA 1 ATOM 3009 C C . GLY A 1 416 ? 6.277 44.610 78.335 1.00 37.22 ? 409 GLY A C 1 ATOM 3010 O O . GLY A 1 416 ? 5.667 45.651 78.632 1.00 37.54 ? 409 GLY A O 1 ATOM 3011 N N . TRP A 1 417 ? 7.310 44.595 77.496 1.00 35.62 ? 410 TRP A N 1 ATOM 3012 C CA . TRP A 1 417 ? 7.804 45.825 76.889 1.00 34.49 ? 410 TRP A CA 1 ATOM 3013 C C . TRP A 1 417 ? 7.011 46.118 75.628 1.00 32.46 ? 410 TRP A C 1 ATOM 3014 O O . TRP A 1 417 ? 6.565 45.198 74.927 1.00 32.57 ? 410 TRP A O 1 ATOM 3015 C CB . TRP A 1 417 ? 9.281 45.676 76.526 1.00 34.55 ? 410 TRP A CB 1 ATOM 3016 C CG . TRP A 1 417 ? 9.907 46.823 75.715 1.00 35.05 ? 410 TRP A CG 1 ATOM 3017 C CD1 . TRP A 1 417 ? 10.448 47.985 76.207 1.00 36.51 ? 410 TRP A CD1 1 ATOM 3018 C CD2 . TRP A 1 417 ? 10.061 46.886 74.286 1.00 34.67 ? 410 TRP A CD2 1 ATOM 3019 N NE1 . TRP A 1 417 ? 10.943 48.753 75.169 1.00 34.34 ? 410 TRP A NE1 1 ATOM 3020 C CE2 . TRP A 1 417 ? 10.712 48.108 73.983 1.00 34.09 ? 410 TRP A CE2 1 ATOM 3021 C CE3 . TRP A 1 417 ? 9.694 46.037 73.232 1.00 33.76 ? 410 TRP A CE3 1 ATOM 3022 C CZ2 . TRP A 1 417 ? 11.023 48.489 72.666 1.00 31.42 ? 410 TRP A CZ2 1 ATOM 3023 C CZ3 . TRP A 1 417 ? 9.998 46.408 71.945 1.00 31.97 ? 410 TRP A CZ3 1 ATOM 3024 C CH2 . TRP A 1 417 ? 10.652 47.639 71.672 1.00 31.02 ? 410 TRP A CH2 1 ATOM 3025 N N . ARG A 1 418 ? 6.841 47.395 75.336 1.00 31.28 ? 411 ARG A N 1 ATOM 3026 C CA . ARG A 1 418 ? 6.382 47.801 73.996 1.00 29.82 ? 411 ARG A CA 1 ATOM 3027 C C . ARG A 1 418 ? 7.207 48.990 73.562 1.00 28.30 ? 411 ARG A C 1 ATOM 3028 O O . ARG A 1 418 ? 7.627 49.796 74.395 1.00 29.13 ? 411 ARG A O 1 ATOM 3029 C CB . ARG A 1 418 ? 4.916 48.233 74.020 1.00 30.94 ? 411 ARG A CB 1 ATOM 3030 C CG . ARG A 1 418 ? 3.940 47.102 73.987 1.00 32.92 ? 411 ARG A CG 1 ATOM 3031 C CD . ARG A 1 418 ? 2.485 47.615 73.886 1.00 33.24 ? 411 ARG A CD 1 ATOM 3032 N NE . ARG A 1 418 ? 1.642 46.438 73.817 1.00 32.46 ? 411 ARG A NE 1 ATOM 3033 C CZ . ARG A 1 418 ? 1.469 45.697 72.714 1.00 32.26 ? 411 ARG A CZ 1 ATOM 3034 N NH1 . ARG A 1 418 ? 1.987 46.072 71.525 1.00 27.92 ? 411 ARG A NH1 1 ATOM 3035 N NH2 . ARG A 1 418 ? 0.737 44.592 72.801 1.00 32.37 ? 411 ARG A NH2 1 ATOM 3036 N N . PRO A 1 419 ? 7.435 49.128 72.251 1.00 26.30 ? 412 PRO A N 1 ATOM 3037 C CA . PRO A 1 419 ? 8.075 50.342 71.772 1.00 25.76 ? 412 PRO A CA 1 ATOM 3038 C C . PRO A 1 419 ? 7.168 51.546 71.965 1.00 24.65 ? 412 PRO A C 1 ATOM 3039 O O . PRO A 1 419 ? 5.964 51.389 72.067 1.00 25.93 ? 412 PRO A O 1 ATOM 3040 C CB . PRO A 1 419 ? 8.281 50.072 70.265 1.00 25.09 ? 412 PRO A CB 1 ATOM 3041 C CG . PRO A 1 419 ? 7.174 49.110 69.907 1.00 24.77 ? 412 PRO A CG 1 ATOM 3042 C CD . PRO A 1 419 ? 6.952 48.259 71.165 1.00 25.14 ? 412 PRO A CD 1 ATOM 3043 N N . ARG A 1 420 ? 7.744 52.735 72.021 1.00 25.12 ? 413 ARG A N 1 ATOM 3044 C CA . ARG A 1 420 ? 6.963 53.961 72.150 1.00 24.85 ? 413 ARG A CA 1 ATOM 3045 C C . ARG A 1 420 ? 6.008 54.120 70.954 1.00 24.80 ? 413 ARG A C 1 ATOM 3046 O O . ARG A 1 420 ? 4.793 54.371 71.110 1.00 25.06 ? 413 ARG A O 1 ATOM 3047 C CB . ARG A 1 420 ? 7.896 55.163 72.223 1.00 24.79 ? 413 ARG A CB 1 ATOM 3048 C CG . ARG A 1 420 ? 7.164 56.492 72.353 1.00 26.57 ? 413 ARG A CG 1 ATOM 3049 C CD . ARG A 1 420 ? 8.098 57.670 72.258 1.00 29.04 ? 413 ARG A CD 1 ATOM 3050 N NE . ARG A 1 420 ? 7.312 58.904 72.187 1.00 30.48 ? 413 ARG A NE 1 ATOM 3051 C CZ . ARG A 1 420 ? 6.883 59.593 73.247 1.00 33.42 ? 413 ARG A CZ 1 ATOM 3052 N NH1 . ARG A 1 420 ? 7.199 59.200 74.493 1.00 31.16 ? 413 ARG A NH1 1 ATOM 3053 N NH2 . ARG A 1 420 ? 6.173 60.698 73.059 1.00 32.22 ? 413 ARG A NH2 1 ATOM 3054 N N . ARG A 1 421 ? 6.589 53.963 69.767 1.00 23.44 ? 414 ARG A N 1 ATOM 3055 C CA . ARG A 1 421 ? 5.845 54.069 68.494 1.00 22.42 ? 414 ARG A CA 1 ATOM 3056 C C . ARG A 1 421 ? 5.589 52.675 67.924 1.00 22.57 ? 414 ARG A C 1 ATOM 3057 O O . ARG A 1 421 ? 6.276 51.706 68.256 1.00 23.54 ? 414 ARG A O 1 ATOM 3058 C CB . ARG A 1 421 ? 6.662 54.886 67.488 1.00 22.28 ? 414 ARG A CB 1 ATOM 3059 C CG . ARG A 1 421 ? 7.038 56.281 67.986 1.00 21.65 ? 414 ARG A CG 1 ATOM 3060 C CD . ARG A 1 421 ? 7.818 57.137 66.948 1.00 22.07 ? 414 ARG A CD 1 ATOM 3061 N NE . ARG A 1 421 ? 8.035 58.415 67.612 1.00 22.10 ? 414 ARG A NE 1 ATOM 3062 C CZ . ARG A 1 421 ? 9.008 58.651 68.495 1.00 24.07 ? 414 ARG A CZ 1 ATOM 3063 N NH1 . ARG A 1 421 ? 9.973 57.760 68.690 1.00 22.95 ? 414 ARG A NH1 1 ATOM 3064 N NH2 . ARG A 1 421 ? 9.023 59.819 69.155 1.00 25.08 ? 414 ARG A NH2 1 ATOM 3065 N N . THR A 1 422 ? 4.598 52.569 67.055 1.00 21.31 ? 415 THR A N 1 ATOM 3066 C CA . THR A 1 422 ? 4.326 51.312 66.352 1.00 21.60 ? 415 THR A CA 1 ATOM 3067 C C . THR A 1 422 ? 5.464 50.954 65.383 1.00 21.57 ? 415 THR A C 1 ATOM 3068 O O . THR A 1 422 ? 5.979 51.808 64.649 1.00 21.06 ? 415 THR A O 1 ATOM 3069 C CB . THR A 1 422 ? 2.962 51.444 65.586 1.00 20.79 ? 415 THR A CB 1 ATOM 3070 O OG1 . THR A 1 422 ? 1.906 51.467 66.563 1.00 22.36 ? 415 THR A OG1 1 ATOM 3071 C CG2 . THR A 1 422 ? 2.762 50.268 64.602 1.00 20.60 ? 415 THR A CG2 1 ATOM 3072 N N . ILE A 1 423 ? 5.845 49.684 65.401 1.00 20.37 ? 416 ILE A N 1 ATOM 3073 C CA . ILE A 1 423 ? 6.770 49.155 64.411 1.00 20.03 ? 416 ILE A CA 1 ATOM 3074 C C . ILE A 1 423 ? 5.991 48.234 63.492 1.00 20.13 ? 416 ILE A C 1 ATOM 3075 O O . ILE A 1 423 ? 5.244 47.366 63.955 1.00 21.21 ? 416 ILE A O 1 ATOM 3076 C CB . ILE A 1 423 ? 7.945 48.378 65.061 1.00 20.13 ? 416 ILE A CB 1 ATOM 3077 C CG1 . ILE A 1 423 ? 8.687 49.255 66.071 1.00 21.85 ? 416 ILE A CG1 1 ATOM 3078 C CG2 . ILE A 1 423 ? 8.905 47.914 63.937 1.00 19.51 ? 416 ILE A CG2 1 ATOM 3079 C CD1 . ILE A 1 423 ? 9.767 48.496 66.923 1.00 22.03 ? 416 ILE A CD1 1 ATOM 3080 N N . LEU A 1 424 ? 6.125 48.487 62.182 1.00 19.47 ? 417 LEU A N 1 ATOM 3081 C CA . LEU A 1 424 ? 5.579 47.599 61.158 1.00 19.46 ? 417 LEU A CA 1 ATOM 3082 C C . LEU A 1 424 ? 6.750 46.852 60.539 1.00 19.48 ? 417 LEU A C 1 ATOM 3083 O O . LEU A 1 424 ? 7.808 47.452 60.212 1.00 19.70 ? 417 LEU A O 1 ATOM 3084 C CB . LEU A 1 424 ? 4.844 48.381 60.067 1.00 18.30 ? 417 LEU A CB 1 ATOM 3085 C CG . LEU A 1 424 ? 3.704 49.291 60.595 1.00 20.08 ? 417 LEU A CG 1 ATOM 3086 C CD1 . LEU A 1 424 ? 3.028 50.043 59.392 1.00 19.23 ? 417 LEU A CD1 1 ATOM 3087 C CD2 . LEU A 1 424 ? 2.677 48.433 61.328 1.00 21.20 ? 417 LEU A CD2 1 ATOM 3088 N N . PHE A 1 425 ? 6.547 45.546 60.360 1.00 19.34 ? 418 PHE A N 1 ATOM 3089 C CA . PHE A 1 425 ? 7.539 44.681 59.711 1.00 18.39 ? 418 PHE A CA 1 ATOM 3090 C C . PHE A 1 425 ? 6.938 44.139 58.415 1.00 19.20 ? 418 PHE A C 1 ATOM 3091 O O . PHE A 1 425 ? 5.759 43.749 58.383 1.00 19.66 ? 418 PHE A O 1 ATOM 3092 C CB . PHE A 1 425 ? 7.897 43.493 60.613 1.00 18.91 ? 418 PHE A CB 1 ATOM 3093 C CG . PHE A 1 425 ? 8.457 43.901 61.931 1.00 19.82 ? 418 PHE A CG 1 ATOM 3094 C CD1 . PHE A 1 425 ? 9.821 44.153 62.064 1.00 21.80 ? 418 PHE A CD1 1 ATOM 3095 C CD2 . PHE A 1 425 ? 7.618 44.034 63.055 1.00 22.74 ? 418 PHE A CD2 1 ATOM 3096 C CE1 . PHE A 1 425 ? 10.358 44.536 63.314 1.00 22.69 ? 418 PHE A CE1 1 ATOM 3097 C CE2 . PHE A 1 425 ? 8.164 44.420 64.296 1.00 22.98 ? 418 PHE A CE2 1 ATOM 3098 C CZ . PHE A 1 425 ? 9.528 44.647 64.420 1.00 23.34 ? 418 PHE A CZ 1 ATOM 3099 N N . ALA A 1 426 ? 7.725 44.153 57.342 1.00 19.61 ? 419 ALA A N 1 ATOM 3100 C CA . ALA A 1 426 ? 7.178 43.733 56.050 1.00 18.75 ? 419 ALA A CA 1 ATOM 3101 C C . ALA A 1 426 ? 8.113 42.781 55.333 1.00 18.73 ? 419 ALA A C 1 ATOM 3102 O O . ALA A 1 426 ? 9.324 42.989 55.284 1.00 19.05 ? 419 ALA A O 1 ATOM 3103 C CB . ALA A 1 426 ? 6.886 44.955 55.147 1.00 18.31 ? 419 ALA A CB 1 ATOM 3104 N N . SER A 1 427 ? 7.500 41.727 54.800 1.00 18.63 ? 420 SER A N 1 ATOM 3105 C CA . SER A 1 427 ? 8.128 40.772 53.882 1.00 17.27 ? 420 SER A CA 1 ATOM 3106 C C . SER A 1 427 ? 7.469 41.005 52.523 1.00 18.13 ? 420 SER A C 1 ATOM 3107 O O . SER A 1 427 ? 6.328 40.545 52.288 1.00 18.11 ? 420 SER A O 1 ATOM 3108 C CB . SER A 1 427 ? 7.804 39.357 54.386 1.00 18.97 ? 420 SER A CB 1 ATOM 3109 O OG . SER A 1 427 ? 8.298 38.354 53.470 1.00 17.78 ? 420 SER A OG 1 ATOM 3110 N N . TRP A 1 428 ? 8.147 41.754 51.652 1.00 17.03 ? 421 TRP A N 1 ATOM 3111 C CA . TRP A 1 428 ? 7.528 42.162 50.393 1.00 16.70 ? 421 TRP A CA 1 ATOM 3112 C C . TRP A 1 428 ? 7.658 41.079 49.334 1.00 18.34 ? 421 TRP A C 1 ATOM 3113 O O . TRP A 1 428 ? 8.632 40.322 49.307 1.00 18.46 ? 421 TRP A O 1 ATOM 3114 C CB . TRP A 1 428 ? 8.242 43.367 49.796 1.00 16.52 ? 421 TRP A CB 1 ATOM 3115 C CG . TRP A 1 428 ? 8.321 44.604 50.673 1.00 15.31 ? 421 TRP A CG 1 ATOM 3116 C CD1 . TRP A 1 428 ? 9.471 45.281 51.013 1.00 15.70 ? 421 TRP A CD1 1 ATOM 3117 C CD2 . TRP A 1 428 ? 7.227 45.327 51.280 1.00 14.85 ? 421 TRP A CD2 1 ATOM 3118 N NE1 . TRP A 1 428 ? 9.153 46.395 51.798 1.00 15.72 ? 421 TRP A NE1 1 ATOM 3119 C CE2 . TRP A 1 428 ? 7.790 46.446 51.952 1.00 16.81 ? 421 TRP A CE2 1 ATOM 3120 C CE3 . TRP A 1 428 ? 5.829 45.164 51.285 1.00 17.25 ? 421 TRP A CE3 1 ATOM 3121 C CZ2 . TRP A 1 428 ? 7.003 47.375 52.674 1.00 17.47 ? 421 TRP A CZ2 1 ATOM 3122 C CZ3 . TRP A 1 428 ? 5.044 46.090 51.978 1.00 17.86 ? 421 TRP A CZ3 1 ATOM 3123 C CH2 . TRP A 1 428 ? 5.648 47.182 52.689 1.00 19.22 ? 421 TRP A CH2 1 ATOM 3124 N N . ASP A 1 429 ? 6.659 41.044 48.436 1.00 17.42 ? 422 ASP A N 1 ATOM 3125 C CA . ASP A 1 429 ? 6.727 40.118 47.326 1.00 17.37 ? 422 ASP A CA 1 ATOM 3126 C C . ASP A 1 429 ? 7.053 40.898 46.060 1.00 17.06 ? 422 ASP A C 1 ATOM 3127 O O . ASP A 1 429 ? 6.884 42.141 46.003 1.00 17.66 ? 422 ASP A O 1 ATOM 3128 C CB . ASP A 1 429 ? 5.364 39.424 47.169 1.00 17.28 ? 422 ASP A CB 1 ATOM 3129 C CG . ASP A 1 429 ? 5.441 38.052 46.484 1.00 18.63 ? 422 ASP A CG 1 ATOM 3130 O OD1 . ASP A 1 429 ? 6.452 37.696 45.848 1.00 18.96 ? 422 ASP A OD1 1 ATOM 3131 O OD2 . ASP A 1 429 ? 4.418 37.324 46.558 1.00 18.67 ? 422 ASP A OD2 1 ATOM 3132 N N . ALA A 1 430 ? 7.453 40.145 45.031 1.00 17.73 ? 423 ALA A N 1 ATOM 3133 C CA . ALA A 1 430 ? 7.641 40.654 43.674 1.00 17.88 ? 423 ALA A CA 1 ATOM 3134 C C . ALA A 1 430 ? 8.571 41.862 43.566 1.00 16.68 ? 423 ALA A C 1 ATOM 3135 O O . ALA A 1 430 ? 8.459 42.686 42.630 1.00 17.34 ? 423 ALA A O 1 ATOM 3136 C CB . ALA A 1 430 ? 6.276 40.921 42.988 1.00 17.98 ? 423 ALA A CB 1 ATOM 3137 N N . ALA A 1 431 ? 9.544 41.961 44.466 1.00 17.03 ? 424 ALA A N 1 ATOM 3138 C CA . ALA A 1 431 ? 10.488 43.071 44.320 1.00 16.75 ? 424 ALA A CA 1 ATOM 3139 C C . ALA A 1 431 ? 11.286 42.864 43.048 1.00 16.84 ? 424 ALA A C 1 ATOM 3140 O O . ALA A 1 431 ? 11.658 43.855 42.359 1.00 16.92 ? 424 ALA A O 1 ATOM 3141 C CB . ALA A 1 431 ? 11.460 43.170 45.536 1.00 17.00 ? 424 ALA A CB 1 ATOM 3142 N N . GLU A 1 432 ? 11.598 41.596 42.740 1.00 16.95 ? 425 GLU A N 1 ATOM 3143 C CA . GLU A 1 432 ? 12.440 41.337 41.557 1.00 17.37 ? 425 GLU A CA 1 ATOM 3144 C C . GLU A 1 432 ? 11.752 41.743 40.256 1.00 17.26 ? 425 GLU A C 1 ATOM 3145 O O . GLU A 1 432 ? 12.428 41.907 39.228 1.00 17.87 ? 425 GLU A O 1 ATOM 3146 C CB . GLU A 1 432 ? 12.892 39.874 41.488 1.00 16.71 ? 425 GLU A CB 1 ATOM 3147 C CG . GLU A 1 432 ? 13.780 39.404 42.635 1.00 17.60 ? 425 GLU A CG 1 ATOM 3148 C CD . GLU A 1 432 ? 15.144 40.125 42.744 1.00 18.37 ? 425 GLU A CD 1 ATOM 3149 O OE1 . GLU A 1 432 ? 15.434 41.125 42.034 1.00 18.60 ? 425 GLU A OE1 1 ATOM 3150 O OE2 . GLU A 1 432 ? 15.978 39.678 43.558 1.00 17.92 ? 425 GLU A OE2 1 ATOM 3151 N N . PHE A 1 433 ? 10.433 41.904 40.295 1.00 17.14 ? 426 PHE A N 1 ATOM 3152 C CA . PHE A 1 433 ? 9.673 42.245 39.112 1.00 16.72 ? 426 PHE A CA 1 ATOM 3153 C C . PHE A 1 433 ? 9.312 43.721 39.045 1.00 16.79 ? 426 PHE A C 1 ATOM 3154 O O . PHE A 1 433 ? 8.433 44.123 38.251 1.00 16.52 ? 426 PHE A O 1 ATOM 3155 C CB . PHE A 1 433 ? 8.413 41.371 39.050 1.00 18.62 ? 426 PHE A CB 1 ATOM 3156 C CG . PHE A 1 433 ? 8.711 39.934 38.686 1.00 17.98 ? 426 PHE A CG 1 ATOM 3157 C CD1 . PHE A 1 433 ? 8.608 39.517 37.360 1.00 19.02 ? 426 PHE A CD1 1 ATOM 3158 C CD2 . PHE A 1 433 ? 9.087 39.004 39.682 1.00 19.80 ? 426 PHE A CD2 1 ATOM 3159 C CE1 . PHE A 1 433 ? 8.877 38.152 37.008 1.00 19.04 ? 426 PHE A CE1 1 ATOM 3160 C CE2 . PHE A 1 433 ? 9.366 37.654 39.368 1.00 19.08 ? 426 PHE A CE2 1 ATOM 3161 C CZ . PHE A 1 433 ? 9.251 37.216 38.020 1.00 20.16 ? 426 PHE A CZ 1 ATOM 3162 N N . GLY A 1 434 ? 9.987 44.532 39.877 1.00 16.35 ? 427 GLY A N 1 ATOM 3163 C CA . GLY A 1 434 ? 9.784 45.986 39.818 1.00 15.48 ? 427 GLY A CA 1 ATOM 3164 C C . GLY A 1 434 ? 9.292 46.608 41.100 1.00 17.09 ? 427 GLY A C 1 ATOM 3165 O O . GLY A 1 434 ? 8.575 47.618 41.058 1.00 16.95 ? 427 GLY A O 1 ATOM 3166 N N . LEU A 1 435 ? 9.696 46.038 42.229 1.00 15.65 ? 428 LEU A N 1 ATOM 3167 C CA . LEU A 1 435 ? 9.303 46.626 43.540 1.00 15.35 ? 428 LEU A CA 1 ATOM 3168 C C . LEU A 1 435 ? 7.760 46.620 43.657 1.00 16.03 ? 428 LEU A C 1 ATOM 3169 O O . LEU A 1 435 ? 7.158 47.524 44.231 1.00 16.24 ? 428 LEU A O 1 ATOM 3170 C CB . LEU A 1 435 ? 9.883 48.069 43.706 1.00 16.28 ? 428 LEU A CB 1 ATOM 3171 C CG . LEU A 1 435 ? 11.313 48.256 43.186 1.00 15.43 ? 428 LEU A CG 1 ATOM 3172 C CD1 . LEU A 1 435 ? 11.735 49.720 43.399 1.00 17.17 ? 428 LEU A CD1 1 ATOM 3173 C CD2 . LEU A 1 435 ? 12.268 47.306 43.919 1.00 18.09 ? 428 LEU A CD2 1 ATOM 3174 N N . LEU A 1 436 ? 7.138 45.558 43.140 1.00 16.11 ? 429 LEU A N 1 ATOM 3175 C CA . LEU A 1 436 ? 5.679 45.608 42.986 1.00 16.05 ? 429 LEU A CA 1 ATOM 3176 C C . LEU A 1 436 ? 4.933 45.489 44.304 1.00 15.86 ? 429 LEU A C 1 ATOM 3177 O O . LEU A 1 436 ? 3.933 46.182 44.508 1.00 16.82 ? 429 LEU A O 1 ATOM 3178 C CB . LEU A 1 436 ? 5.169 44.560 41.989 1.00 15.77 ? 429 LEU A CB 1 ATOM 3179 C CG . LEU A 1 436 ? 5.923 44.587 40.643 1.00 16.93 ? 429 LEU A CG 1 ATOM 3180 C CD1 . LEU A 1 436 ? 5.282 43.524 39.740 1.00 19.36 ? 429 LEU A CD1 1 ATOM 3181 C CD2 . LEU A 1 436 ? 5.787 45.938 39.909 1.00 17.79 ? 429 LEU A CD2 1 ATOM 3182 N N . GLY A 1 437 ? 5.400 44.606 45.172 1.00 16.73 ? 430 GLY A N 1 ATOM 3183 C CA . GLY A 1 437 ? 4.687 44.348 46.429 1.00 15.74 ? 430 GLY A CA 1 ATOM 3184 C C . GLY A 1 437 ? 4.730 45.558 47.355 1.00 16.46 ? 430 GLY A C 1 ATOM 3185 O O . GLY A 1 437 ? 3.702 45.947 47.929 1.00 16.90 ? 430 GLY A O 1 ATOM 3186 N N . SER A 1 438 ? 5.905 46.148 47.531 1.00 15.75 ? 431 SER A N 1 ATOM 3187 C CA . SER A 1 438 ? 5.994 47.310 48.413 1.00 16.31 ? 431 SER A CA 1 ATOM 3188 C C . SER A 1 438 ? 5.178 48.460 47.818 1.00 15.57 ? 431 SER A C 1 ATOM 3189 O O . SER A 1 438 ? 4.475 49.186 48.529 1.00 15.20 ? 431 SER A O 1 ATOM 3190 C CB . SER A 1 438 ? 7.456 47.724 48.573 1.00 15.65 ? 431 SER A CB 1 ATOM 3191 O OG . SER A 1 438 ? 8.068 48.078 47.322 1.00 16.51 ? 431 SER A OG 1 ATOM 3192 N N . THR A 1 439 ? 5.269 48.621 46.508 1.00 15.83 ? 432 THR A N 1 ATOM 3193 C CA . THR A 1 439 ? 4.615 49.785 45.886 1.00 15.62 ? 432 THR A CA 1 ATOM 3194 C C . THR A 1 439 ? 3.089 49.655 45.945 1.00 15.08 ? 432 THR A C 1 ATOM 3195 O O . THR A 1 439 ? 2.405 50.644 46.268 1.00 16.16 ? 432 THR A O 1 ATOM 3196 C CB . THR A 1 439 ? 5.106 49.996 44.432 1.00 16.16 ? 432 THR A CB 1 ATOM 3197 O OG1 . THR A 1 439 ? 6.535 50.149 44.460 1.00 16.48 ? 432 THR A OG1 1 ATOM 3198 C CG2 . THR A 1 439 ? 4.470 51.303 43.869 1.00 16.39 ? 432 THR A CG2 1 ATOM 3199 N N . GLU A 1 440 ? 2.556 48.462 45.658 1.00 15.13 ? 433 GLU A N 1 ATOM 3200 C CA . GLU A 1 440 ? 1.091 48.310 45.702 1.00 15.69 ? 433 GLU A CA 1 ATOM 3201 C C . GLU A 1 440 ? 0.586 48.536 47.108 1.00 15.78 ? 433 GLU A C 1 ATOM 3202 O O . GLU A 1 440 ? -0.467 49.146 47.317 1.00 16.70 ? 433 GLU A O 1 ATOM 3203 C CB . GLU A 1 440 ? 0.636 46.925 45.193 1.00 16.44 ? 433 GLU A CB 1 ATOM 3204 C CG . GLU A 1 440 ? 0.960 46.731 43.677 1.00 16.83 ? 433 GLU A CG 1 ATOM 3205 C CD . GLU A 1 440 ? 0.377 47.827 42.818 1.00 17.71 ? 433 GLU A CD 1 ATOM 3206 O OE1 . GLU A 1 440 ? -0.860 48.077 42.921 1.00 18.31 ? 433 GLU A OE1 1 ATOM 3207 O OE2 . GLU A 1 440 ? 1.148 48.470 42.057 1.00 17.55 ? 433 GLU A OE2 1 ATOM 3208 N N . TRP A 1 441 ? 1.310 48.002 48.101 1.00 15.83 ? 434 TRP A N 1 ATOM 3209 C CA . TRP A 1 441 ? 0.866 48.173 49.500 1.00 16.31 ? 434 TRP A CA 1 ATOM 3210 C C . TRP A 1 441 ? 0.937 49.657 49.926 1.00 16.91 ? 434 TRP A C 1 ATOM 3211 O O . TRP A 1 441 ? 0.048 50.157 50.601 1.00 16.84 ? 434 TRP A O 1 ATOM 3212 C CB . TRP A 1 441 ? 1.743 47.305 50.410 1.00 17.20 ? 434 TRP A CB 1 ATOM 3213 C CG . TRP A 1 441 ? 1.325 47.363 51.869 1.00 16.82 ? 434 TRP A CG 1 ATOM 3214 C CD1 . TRP A 1 441 ? 0.347 46.597 52.500 1.00 17.95 ? 434 TRP A CD1 1 ATOM 3215 C CD2 . TRP A 1 441 ? 1.878 48.233 52.876 1.00 18.34 ? 434 TRP A CD2 1 ATOM 3216 N NE1 . TRP A 1 441 ? 0.277 46.950 53.850 1.00 19.18 ? 434 TRP A NE1 1 ATOM 3217 C CE2 . TRP A 1 441 ? 1.213 47.925 54.109 1.00 17.99 ? 434 TRP A CE2 1 ATOM 3218 C CE3 . TRP A 1 441 ? 2.876 49.212 52.862 1.00 17.66 ? 434 TRP A CE3 1 ATOM 3219 C CZ2 . TRP A 1 441 ? 1.504 48.602 55.319 1.00 19.47 ? 434 TRP A CZ2 1 ATOM 3220 C CZ3 . TRP A 1 441 ? 3.199 49.884 54.096 1.00 19.12 ? 434 TRP A CZ3 1 ATOM 3221 C CH2 . TRP A 1 441 ? 2.490 49.564 55.296 1.00 18.99 ? 434 TRP A CH2 1 ATOM 3222 N N . ALA A 1 442 ? 1.982 50.362 49.477 1.00 15.41 ? 435 ALA A N 1 ATOM 3223 C CA . ALA A 1 442 ? 2.092 51.779 49.801 1.00 16.08 ? 435 ALA A CA 1 ATOM 3224 C C . ALA A 1 442 ? 0.997 52.559 49.047 1.00 15.78 ? 435 ALA A C 1 ATOM 3225 O O . ALA A 1 442 ? 0.487 53.542 49.591 1.00 15.67 ? 435 ALA A O 1 ATOM 3226 C CB . ALA A 1 442 ? 3.519 52.310 49.465 1.00 15.67 ? 435 ALA A CB 1 ATOM 3227 N N . GLU A 1 443 ? 0.638 52.136 47.823 1.00 15.69 ? 436 GLU A N 1 ATOM 3228 C CA . GLU A 1 443 ? -0.488 52.808 47.118 1.00 15.58 ? 436 GLU A CA 1 ATOM 3229 C C . GLU A 1 443 ? -1.794 52.610 47.869 1.00 16.61 ? 436 GLU A C 1 ATOM 3230 O O . GLU A 1 443 ? -2.604 53.537 47.995 1.00 17.07 ? 436 GLU A O 1 ATOM 3231 C CB . GLU A 1 443 ? -0.633 52.339 45.651 1.00 16.29 ? 436 GLU A CB 1 ATOM 3232 C CG . GLU A 1 443 ? 0.549 52.880 44.793 1.00 15.77 ? 436 GLU A CG 1 ATOM 3233 C CD . GLU A 1 443 ? 0.406 52.533 43.324 1.00 18.36 ? 436 GLU A CD 1 ATOM 3234 O OE1 . GLU A 1 443 ? 0.784 53.382 42.483 1.00 17.44 ? 436 GLU A OE1 1 ATOM 3235 O OE2 . GLU A 1 443 ? -0.103 51.419 43.016 1.00 18.39 ? 436 GLU A OE2 1 ATOM 3236 N N . GLU A 1 444 ? -1.971 51.411 48.397 1.00 17.65 ? 437 GLU A N 1 ATOM 3237 C CA . GLU A 1 444 ? -3.170 51.125 49.159 1.00 17.11 ? 437 GLU A CA 1 ATOM 3238 C C . GLU A 1 444 ? -3.232 51.982 50.428 1.00 17.74 ? 437 GLU A C 1 ATOM 3239 O O . GLU A 1 444 ? -4.283 52.498 50.809 1.00 18.61 ? 437 GLU A O 1 ATOM 3240 C CB . GLU A 1 444 ? -3.165 49.658 49.540 1.00 19.03 ? 437 GLU A CB 1 ATOM 3241 C CG . GLU A 1 444 ? -4.499 49.235 50.202 1.00 22.09 ? 437 GLU A CG 1 ATOM 3242 C CD . GLU A 1 444 ? -4.767 47.759 49.918 1.00 32.70 ? 437 GLU A CD 1 ATOM 3243 O OE1 . GLU A 1 444 ? -5.716 47.419 49.172 1.00 42.69 ? 437 GLU A OE1 1 ATOM 3244 O OE2 . GLU A 1 444 ? -3.988 46.961 50.391 1.00 29.68 ? 437 GLU A OE2 1 ATOM 3245 N N . ASN A 1 445 ? -2.078 52.130 51.069 1.00 16.12 ? 438 ASN A N 1 ATOM 3246 C CA . ASN A 1 445 ? -2.018 52.720 52.424 1.00 16.86 ? 438 ASN A CA 1 ATOM 3247 C C . ASN A 1 445 ? -1.425 54.110 52.452 1.00 17.00 ? 438 ASN A C 1 ATOM 3248 O O . ASN A 1 445 ? -1.053 54.615 53.507 1.00 16.54 ? 438 ASN A O 1 ATOM 3249 C CB . ASN A 1 445 ? -1.265 51.743 53.366 1.00 17.79 ? 438 ASN A CB 1 ATOM 3250 C CG . ASN A 1 445 ? -2.054 50.492 53.572 1.00 18.57 ? 438 ASN A CG 1 ATOM 3251 O OD1 . ASN A 1 445 ? -3.138 50.526 54.226 1.00 21.09 ? 438 ASN A OD1 1 ATOM 3252 N ND2 . ASN A 1 445 ? -1.609 49.385 52.978 1.00 19.60 ? 438 ASN A ND2 1 ATOM 3253 N N . SER A 1 446 ? -1.425 54.786 51.293 1.00 16.39 ? 439 SER A N 1 ATOM 3254 C CA . SER A 1 446 ? -0.679 56.050 51.175 1.00 16.73 ? 439 SER A CA 1 ATOM 3255 C C . SER A 1 446 ? -1.109 57.114 52.190 1.00 16.21 ? 439 SER A C 1 ATOM 3256 O O . SER A 1 446 ? -0.275 57.872 52.676 1.00 17.33 ? 439 SER A O 1 ATOM 3257 C CB . SER A 1 446 ? -0.811 56.626 49.740 1.00 16.20 ? 439 SER A CB 1 ATOM 3258 O OG . SER A 1 446 ? -2.156 56.885 49.414 1.00 18.11 ? 439 SER A OG 1 ATOM 3259 N N . ARG A 1 447 ? -2.397 57.204 52.473 1.00 16.06 ? 440 ARG A N 1 ATOM 3260 C CA . ARG A 1 447 ? -2.889 58.221 53.418 1.00 16.17 ? 440 ARG A CA 1 ATOM 3261 C C . ARG A 1 447 ? -2.377 57.949 54.828 1.00 17.01 ? 440 ARG A C 1 ATOM 3262 O O . ARG A 1 447 ? -2.022 58.895 55.562 1.00 17.56 ? 440 ARG A O 1 ATOM 3263 C CB . ARG A 1 447 ? -4.398 58.279 53.391 1.00 17.30 ? 440 ARG A CB 1 ATOM 3264 C CG . ARG A 1 447 ? -4.926 58.867 52.072 1.00 19.65 ? 440 ARG A CG 1 ATOM 3265 C CD . ARG A 1 447 ? -6.218 58.202 51.605 1.00 23.82 ? 440 ARG A CD 1 ATOM 3266 N NE . ARG A 1 447 ? -6.593 58.734 50.276 1.00 20.30 ? 440 ARG A NE 1 ATOM 3267 C CZ . ARG A 1 447 ? -6.172 58.289 49.102 1.00 21.56 ? 440 ARG A CZ 1 ATOM 3268 N NH1 . ARG A 1 447 ? -5.387 57.194 49.017 1.00 23.32 ? 440 ARG A NH1 1 ATOM 3269 N NH2 . ARG A 1 447 ? -6.600 58.929 48.020 1.00 19.73 ? 440 ARG A NH2 1 ATOM 3270 N N . LEU A 1 448 ? -2.374 56.673 55.221 1.00 16.56 ? 441 LEU A N 1 ATOM 3271 C CA . LEU A 1 448 ? -1.854 56.339 56.533 1.00 17.21 ? 441 LEU A CA 1 ATOM 3272 C C . LEU A 1 448 ? -0.343 56.628 56.583 1.00 17.87 ? 441 LEU A C 1 ATOM 3273 O O . LEU A 1 448 ? 0.176 57.168 57.572 1.00 18.34 ? 441 LEU A O 1 ATOM 3274 C CB . LEU A 1 448 ? -2.100 54.856 56.856 1.00 17.74 ? 441 LEU A CB 1 ATOM 3275 C CG . LEU A 1 448 ? -3.548 54.366 56.674 1.00 18.61 ? 441 LEU A CG 1 ATOM 3276 C CD1 . LEU A 1 448 ? -3.658 52.889 57.114 1.00 21.27 ? 441 LEU A CD1 1 ATOM 3277 C CD2 . LEU A 1 448 ? -4.562 55.238 57.450 1.00 20.62 ? 441 LEU A CD2 1 ATOM 3278 N N . LEU A 1 449 ? 0.360 56.284 55.513 1.00 17.07 ? 442 LEU A N 1 ATOM 3279 C CA . LEU A 1 449 ? 1.814 56.436 55.519 1.00 18.15 ? 442 LEU A CA 1 ATOM 3280 C C . LEU A 1 449 ? 2.210 57.914 55.483 1.00 18.63 ? 442 LEU A C 1 ATOM 3281 O O . LEU A 1 449 ? 3.149 58.305 56.182 1.00 20.81 ? 442 LEU A O 1 ATOM 3282 C CB . LEU A 1 449 ? 2.429 55.676 54.320 1.00 17.39 ? 442 LEU A CB 1 ATOM 3283 C CG . LEU A 1 449 ? 2.228 54.163 54.396 1.00 16.70 ? 442 LEU A CG 1 ATOM 3284 C CD1 . LEU A 1 449 ? 2.559 53.572 52.983 1.00 16.56 ? 442 LEU A CD1 1 ATOM 3285 C CD2 . LEU A 1 449 ? 3.159 53.501 55.453 1.00 20.15 ? 442 LEU A CD2 1 ATOM 3286 N N . GLN A 1 450 ? 1.498 58.711 54.670 1.00 18.86 ? 443 GLN A N 1 ATOM 3287 C CA . GLN A 1 450 ? 1.694 60.160 54.508 1.00 21.14 ? 443 GLN A CA 1 ATOM 3288 C C . GLN A 1 450 ? 1.602 60.874 55.869 1.00 19.47 ? 443 GLN A C 1 ATOM 3289 O O . GLN A 1 450 ? 2.423 61.747 56.191 1.00 18.81 ? 443 GLN A O 1 ATOM 3290 C CB . GLN A 1 450 ? 0.481 60.678 53.661 1.00 21.58 ? 443 GLN A CB 1 ATOM 3291 C CG A GLN A 1 450 ? 0.627 61.840 52.958 0.50 25.14 ? 443 GLN A CG 1 ATOM 3292 C CG B GLN A 1 450 ? 0.211 62.181 53.765 0.50 21.58 ? 443 GLN A CG 1 ATOM 3293 C CD A GLN A 1 450 ? 0.026 61.585 51.658 0.50 19.98 ? 443 GLN A CD 1 ATOM 3294 C CD B GLN A 1 450 ? 1.194 63.011 52.953 0.50 20.87 ? 443 GLN A CD 1 ATOM 3295 O OE1 A GLN A 1 450 ? 0.723 61.169 50.754 0.50 19.01 ? 443 GLN A OE1 1 ATOM 3296 O OE1 B GLN A 1 450 ? 1.699 62.526 51.902 0.50 22.27 ? 443 GLN A OE1 1 ATOM 3297 N NE2 A GLN A 1 450 ? -1.310 61.733 51.564 0.50 18.35 ? 443 GLN A NE2 1 ATOM 3298 N NE2 B GLN A 1 450 ? 1.497 64.244 53.436 0.50 15.82 ? 443 GLN A NE2 1 ATOM 3299 N N . GLU A 1 451 ? 0.611 60.495 56.669 1.00 19.10 ? 444 GLU A N 1 ATOM 3300 C CA . GLU A 1 451 ? 0.329 61.285 57.862 1.00 17.93 ? 444 GLU A CA 1 ATOM 3301 C C . GLU A 1 451 ? 0.927 60.659 59.123 1.00 18.48 ? 444 GLU A C 1 ATOM 3302 O O . GLU A 1 451 ? 1.044 61.364 60.130 1.00 17.69 ? 444 GLU A O 1 ATOM 3303 C CB . GLU A 1 451 ? -1.179 61.475 58.049 1.00 19.67 ? 444 GLU A CB 1 ATOM 3304 C CG . GLU A 1 451 ? -1.878 62.045 56.787 1.00 20.06 ? 444 GLU A CG 1 ATOM 3305 C CD . GLU A 1 451 ? -1.290 63.357 56.270 1.00 24.04 ? 444 GLU A CD 1 ATOM 3306 O OE1 . GLU A 1 451 ? -0.321 63.901 56.855 1.00 21.50 ? 444 GLU A OE1 1 ATOM 3307 O OE2 . GLU A 1 451 ? -1.810 63.828 55.234 1.00 23.20 ? 444 GLU A OE2 1 ATOM 3308 N N . ARG A 1 452 ? 1.374 59.406 59.021 1.00 16.78 ? 445 ARG A N 1 ATOM 3309 C CA . ARG A 1 452 ? 1.852 58.670 60.212 1.00 17.56 ? 445 ARG A CA 1 ATOM 3310 C C . ARG A 1 452 ? 3.260 58.061 60.103 1.00 18.67 ? 445 ARG A C 1 ATOM 3311 O O . ARG A 1 452 ? 3.794 57.579 61.103 1.00 18.64 ? 445 ARG A O 1 ATOM 3312 C CB . ARG A 1 452 ? 0.866 57.546 60.539 1.00 17.69 ? 445 ARG A CB 1 ATOM 3313 C CG . ARG A 1 452 ? -0.576 58.071 60.807 1.00 18.66 ? 445 ARG A CG 1 ATOM 3314 C CD . ARG A 1 452 ? -1.507 56.908 61.098 1.00 19.56 ? 445 ARG A CD 1 ATOM 3315 N NE . ARG A 1 452 ? -2.903 57.337 61.046 1.00 19.80 ? 445 ARG A NE 1 ATOM 3316 C CZ . ARG A 1 452 ? -3.948 56.519 61.013 1.00 18.82 ? 445 ARG A CZ 1 ATOM 3317 N NH1 . ARG A 1 452 ? -3.748 55.188 61.041 1.00 19.81 ? 445 ARG A NH1 1 ATOM 3318 N NH2 . ARG A 1 452 ? -5.186 57.043 60.914 1.00 20.22 ? 445 ARG A NH2 1 ATOM 3319 N N . GLY A 1 453 ? 3.860 58.104 58.910 1.00 18.83 ? 446 GLY A N 1 ATOM 3320 C CA . GLY A 1 453 ? 5.114 57.366 58.648 1.00 18.77 ? 446 GLY A CA 1 ATOM 3321 C C . GLY A 1 453 ? 6.314 58.155 59.157 1.00 18.44 ? 446 GLY A C 1 ATOM 3322 O O . GLY A 1 453 ? 6.657 59.223 58.627 1.00 19.40 ? 446 GLY A O 1 ATOM 3323 N N . VAL A 1 454 ? 6.960 57.620 60.173 1.00 18.46 ? 447 VAL A N 1 ATOM 3324 C CA . VAL A 1 454 ? 8.159 58.254 60.689 1.00 18.75 ? 447 VAL A CA 1 ATOM 3325 C C . VAL A 1 454 ? 9.380 57.946 59.811 1.00 18.27 ? 447 VAL A C 1 ATOM 3326 O O . VAL A 1 454 ? 10.161 58.840 59.425 1.00 18.54 ? 447 VAL A O 1 ATOM 3327 C CB . VAL A 1 454 ? 8.397 57.749 62.111 1.00 20.39 ? 447 VAL A CB 1 ATOM 3328 C CG1 . VAL A 1 454 ? 9.783 58.129 62.619 1.00 21.45 ? 447 VAL A CG1 1 ATOM 3329 C CG2 . VAL A 1 454 ? 7.319 58.321 63.029 1.00 22.36 ? 447 VAL A CG2 1 ATOM 3330 N N . ALA A 1 455 ? 9.573 56.654 59.538 1.00 18.14 ? 448 ALA A N 1 ATOM 3331 C CA . ALA A 1 455 ? 10.790 56.198 58.857 1.00 17.28 ? 448 ALA A CA 1 ATOM 3332 C C . ALA A 1 455 ? 10.588 54.837 58.254 1.00 17.31 ? 448 ALA A C 1 ATOM 3333 O O . ALA A 1 455 ? 9.771 54.052 58.739 1.00 18.72 ? 448 ALA A O 1 ATOM 3334 C CB . ALA A 1 455 ? 11.964 56.118 59.871 1.00 18.99 ? 448 ALA A CB 1 ATOM 3335 N N . TYR A 1 456 ? 11.383 54.567 57.213 1.00 17.11 ? 449 TYR A N 1 ATOM 3336 C CA . TYR A 1 456 ? 11.423 53.264 56.562 1.00 16.96 ? 449 TYR A CA 1 ATOM 3337 C C . TYR A 1 456 ? 12.884 52.822 56.509 1.00 17.23 ? 449 TYR A C 1 ATOM 3338 O O . TYR A 1 456 ? 13.750 53.543 55.986 1.00 17.70 ? 449 TYR A O 1 ATOM 3339 C CB . TYR A 1 456 ? 10.810 53.346 55.136 1.00 16.49 ? 449 TYR A CB 1 ATOM 3340 C CG . TYR A 1 456 ? 10.918 52.013 54.447 1.00 16.87 ? 449 TYR A CG 1 ATOM 3341 C CD1 . TYR A 1 456 ? 9.918 51.043 54.597 1.00 17.57 ? 449 TYR A CD1 1 ATOM 3342 C CD2 . TYR A 1 456 ? 12.018 51.729 53.642 1.00 17.73 ? 449 TYR A CD2 1 ATOM 3343 C CE1 . TYR A 1 456 ? 10.024 49.795 53.987 1.00 17.67 ? 449 TYR A CE1 1 ATOM 3344 C CE2 . TYR A 1 456 ? 12.147 50.478 52.994 1.00 16.34 ? 449 TYR A CE2 1 ATOM 3345 C CZ . TYR A 1 456 ? 11.140 49.537 53.191 1.00 18.64 ? 449 TYR A CZ 1 ATOM 3346 O OH . TYR A 1 456 ? 11.252 48.314 52.568 1.00 18.03 ? 449 TYR A OH 1 ATOM 3347 N N . ILE A 1 457 ? 13.150 51.643 57.060 1.00 17.29 ? 450 ILE A N 1 ATOM 3348 C CA . ILE A 1 457 ? 14.462 51.010 56.956 1.00 17.66 ? 450 ILE A CA 1 ATOM 3349 C C . ILE A 1 457 ? 14.330 49.783 56.067 1.00 17.47 ? 450 ILE A C 1 ATOM 3350 O O . ILE A 1 457 ? 13.529 48.872 56.353 1.00 18.10 ? 450 ILE A O 1 ATOM 3351 C CB . ILE A 1 457 ? 14.951 50.562 58.381 1.00 17.81 ? 450 ILE A CB 1 ATOM 3352 C CG1 . ILE A 1 457 ? 15.023 51.771 59.354 1.00 18.43 ? 450 ILE A CG1 1 ATOM 3353 C CG2 . ILE A 1 457 ? 16.307 49.829 58.298 1.00 20.19 ? 450 ILE A CG2 1 ATOM 3354 C CD1 . ILE A 1 457 ? 15.900 52.952 58.799 1.00 19.96 ? 450 ILE A CD1 1 ATOM 3355 N N . ASN A 1 458 ? 15.096 49.757 54.985 1.00 17.33 ? 451 ASN A N 1 ATOM 3356 C CA . ASN A 1 458 ? 15.050 48.614 54.090 1.00 17.96 ? 451 ASN A CA 1 ATOM 3357 C C . ASN A 1 458 ? 15.880 47.439 54.612 1.00 19.57 ? 451 ASN A C 1 ATOM 3358 O O . ASN A 1 458 ? 16.735 47.602 55.480 1.00 20.86 ? 451 ASN A O 1 ATOM 3359 C CB . ASN A 1 458 ? 15.604 49.045 52.728 1.00 17.87 ? 451 ASN A CB 1 ATOM 3360 C CG . ASN A 1 458 ? 15.019 48.227 51.577 1.00 18.57 ? 451 ASN A CG 1 ATOM 3361 O OD1 . ASN A 1 458 ? 13.801 48.063 51.456 1.00 19.11 ? 451 ASN A OD1 1 ATOM 3362 N ND2 . ASN A 1 458 ? 15.911 47.687 50.736 1.00 18.29 ? 451 ASN A ND2 1 ATOM 3363 N N . ALA A 1 459 ? 15.668 46.256 54.039 1.00 18.88 ? 452 ALA A N 1 ATOM 3364 C CA . ALA A 1 459 ? 16.367 45.075 54.533 1.00 20.54 ? 452 ALA A CA 1 ATOM 3365 C C . ALA A 1 459 ? 16.454 44.036 53.435 1.00 20.05 ? 452 ALA A C 1 ATOM 3366 O O . ALA A 1 459 ? 16.003 42.890 53.578 1.00 20.94 ? 452 ALA A O 1 ATOM 3367 C CB . ALA A 1 459 ? 15.637 44.541 55.780 1.00 21.01 ? 452 ALA A CB 1 ATOM 3368 N N . ASP A 1 460 ? 17.059 44.430 52.323 1.00 19.48 ? 453 ASP A N 1 ATOM 3369 C CA . ASP A 1 460 ? 17.449 43.437 51.322 1.00 20.27 ? 453 ASP A CA 1 ATOM 3370 C C . ASP A 1 460 ? 18.807 42.854 51.750 1.00 21.01 ? 453 ASP A C 1 ATOM 3371 O O . ASP A 1 460 ? 19.165 42.902 52.932 1.00 22.05 ? 453 ASP A O 1 ATOM 3372 C CB . ASP A 1 460 ? 17.477 44.054 49.920 1.00 19.23 ? 453 ASP A CB 1 ATOM 3373 C CG . ASP A 1 460 ? 17.321 43.013 48.796 1.00 22.52 ? 453 ASP A CG 1 ATOM 3374 O OD1 . ASP A 1 460 ? 17.390 41.808 49.088 1.00 25.43 ? 453 ASP A OD1 1 ATOM 3375 O OD2 . ASP A 1 460 ? 17.143 43.415 47.608 1.00 22.38 ? 453 ASP A OD2 1 ATOM 3376 N N . SER A 1 461 ? 19.535 42.293 50.791 1.00 20.03 ? 454 SER A N 1 ATOM 3377 C CA A SER A 1 461 ? 20.797 41.587 51.053 0.70 20.86 ? 454 SER A CA 1 ATOM 3378 C CA B SER A 1 461 ? 20.784 41.579 51.060 0.30 21.46 ? 454 SER A CA 1 ATOM 3379 C C . SER A 1 461 ? 21.628 42.212 52.175 1.00 21.12 ? 454 SER A C 1 ATOM 3380 O O . SER A 1 461 ? 21.943 43.398 52.136 1.00 21.41 ? 454 SER A O 1 ATOM 3381 C CB A SER A 1 461 ? 21.632 41.521 49.789 0.70 21.22 ? 454 SER A CB 1 ATOM 3382 C CB B SER A 1 461 ? 21.593 41.441 49.774 0.30 21.62 ? 454 SER A CB 1 ATOM 3383 O OG A SER A 1 461 ? 20.872 41.085 48.689 0.70 16.83 ? 454 SER A OG 1 ATOM 3384 O OG B SER A 1 461 ? 21.995 42.707 49.284 0.30 23.37 ? 454 SER A OG 1 ATOM 3385 N N . SER A 1 462 ? 21.968 41.404 53.176 1.00 21.69 ? 455 SER A N 1 ATOM 3386 C CA . SER A 1 462 ? 22.759 41.905 54.315 1.00 23.77 ? 455 SER A CA 1 ATOM 3387 C C . SER A 1 462 ? 24.231 42.051 53.995 1.00 23.39 ? 455 SER A C 1 ATOM 3388 O O . SER A 1 462 ? 24.938 42.831 54.640 1.00 23.87 ? 455 SER A O 1 ATOM 3389 C CB . SER A 1 462 ? 22.605 40.987 55.510 1.00 24.17 ? 455 SER A CB 1 ATOM 3390 O OG . SER A 1 462 ? 21.268 41.070 55.973 1.00 25.49 ? 455 SER A OG 1 ATOM 3391 N N . ILE A 1 463 ? 24.707 41.293 53.011 1.00 24.49 ? 456 ILE A N 1 ATOM 3392 C CA . ILE A 1 463 ? 26.135 41.238 52.691 1.00 26.25 ? 456 ILE A CA 1 ATOM 3393 C C . ILE A 1 463 ? 26.339 41.182 51.181 1.00 26.75 ? 456 ILE A C 1 ATOM 3394 O O . ILE A 1 463 ? 25.583 40.495 50.484 1.00 28.36 ? 456 ILE A O 1 ATOM 3395 C CB . ILE A 1 463 ? 26.798 39.965 53.316 1.00 26.64 ? 456 ILE A CB 1 ATOM 3396 C CG1 . ILE A 1 463 ? 26.027 38.669 52.929 1.00 28.61 ? 456 ILE A CG1 1 ATOM 3397 C CG2 . ILE A 1 463 ? 26.845 40.088 54.836 1.00 28.09 ? 456 ILE A CG2 1 ATOM 3398 C CD1 . ILE A 1 463 ? 26.898 37.562 52.515 1.00 37.21 ? 456 ILE A CD1 1 ATOM 3399 N N A GLU A 1 464 ? 27.340 41.900 50.681 0.60 26.40 ? 457 GLU A N 1 ATOM 3400 N N B GLU A 1 464 ? 27.338 41.902 50.678 0.40 26.94 ? 457 GLU A N 1 ATOM 3401 C CA A GLU A 1 464 ? 27.817 41.722 49.301 0.60 26.23 ? 457 GLU A CA 1 ATOM 3402 C CA B GLU A 1 464 ? 27.829 41.705 49.306 0.40 27.13 ? 457 GLU A CA 1 ATOM 3403 C C A GLU A 1 464 ? 29.342 41.606 49.304 0.60 27.07 ? 457 GLU A C 1 ATOM 3404 C C B GLU A 1 464 ? 29.347 41.631 49.310 0.40 27.54 ? 457 GLU A C 1 ATOM 3405 O O A GLU A 1 464 ? 29.987 41.672 48.252 0.60 26.55 ? 457 GLU A O 1 ATOM 3406 O O B GLU A 1 464 ? 29.993 41.759 48.267 0.40 27.27 ? 457 GLU A O 1 ATOM 3407 C CB A GLU A 1 464 ? 27.348 42.870 48.400 0.60 26.04 ? 457 GLU A CB 1 ATOM 3408 C CB B GLU A 1 464 ? 27.362 42.821 48.377 0.40 27.04 ? 457 GLU A CB 1 ATOM 3409 C CG A GLU A 1 464 ? 27.853 44.240 48.863 0.60 25.35 ? 457 GLU A CG 1 ATOM 3410 C CG B GLU A 1 464 ? 25.865 43.011 48.356 0.40 28.22 ? 457 GLU A CG 1 ATOM 3411 C CD A GLU A 1 464 ? 27.200 45.428 48.170 0.60 29.08 ? 457 GLU A CD 1 ATOM 3412 C CD B GLU A 1 464 ? 25.425 44.089 47.389 0.40 31.17 ? 457 GLU A CD 1 ATOM 3413 O OE1 A GLU A 1 464 ? 26.185 45.276 47.458 0.60 28.72 ? 457 GLU A OE1 1 ATOM 3414 O OE1 B GLU A 1 464 ? 25.940 45.232 47.480 0.40 31.06 ? 457 GLU A OE1 1 ATOM 3415 O OE2 A GLU A 1 464 ? 27.712 46.542 48.357 0.60 30.29 ? 457 GLU A OE2 1 ATOM 3416 O OE2 B GLU A 1 464 ? 24.552 43.797 46.540 0.40 30.92 ? 457 GLU A OE2 1 ATOM 3417 N N . GLY A 1 465 ? 29.893 41.408 50.503 1.00 27.76 ? 458 GLY A N 1 ATOM 3418 C CA . GLY A 1 465 ? 31.323 41.362 50.738 1.00 27.97 ? 458 GLY A CA 1 ATOM 3419 C C . GLY A 1 465 ? 31.531 41.278 52.243 1.00 28.53 ? 458 GLY A C 1 ATOM 3420 O O . GLY A 1 465 ? 30.565 41.209 53.019 1.00 28.41 ? 458 GLY A O 1 ATOM 3421 N N . ASN A 1 466 ? 32.785 41.283 52.666 1.00 29.05 ? 459 ASN A N 1 ATOM 3422 C CA . ASN A 1 466 ? 33.108 41.070 54.079 1.00 29.33 ? 459 ASN A CA 1 ATOM 3423 C C . ASN A 1 466 ? 34.105 42.117 54.597 1.00 29.52 ? 459 ASN A C 1 ATOM 3424 O O . ASN A 1 466 ? 34.850 41.871 55.561 1.00 30.73 ? 459 ASN A O 1 ATOM 3425 C CB . ASN A 1 466 ? 33.636 39.626 54.296 1.00 31.25 ? 459 ASN A CB 1 ATOM 3426 C CG . ASN A 1 466 ? 34.941 39.342 53.530 1.00 32.16 ? 459 ASN A CG 1 ATOM 3427 O OD1 . ASN A 1 466 ? 35.552 40.245 52.952 1.00 34.01 ? 459 ASN A OD1 1 ATOM 3428 N ND2 . ASN A 1 466 ? 35.375 38.072 53.531 1.00 39.84 ? 459 ASN A ND2 1 ATOM 3429 N N . TYR A 1 467 ? 34.115 43.278 53.953 1.00 28.08 ? 460 TYR A N 1 ATOM 3430 C CA . TYR A 1 467 ? 35.135 44.292 54.215 1.00 28.29 ? 460 TYR A CA 1 ATOM 3431 C C . TYR A 1 467 ? 34.662 45.352 55.211 1.00 27.51 ? 460 TYR A C 1 ATOM 3432 O O . TYR A 1 467 ? 35.297 45.577 56.249 1.00 28.47 ? 460 TYR A O 1 ATOM 3433 C CB . TYR A 1 467 ? 35.539 44.969 52.907 1.00 28.15 ? 460 TYR A CB 1 ATOM 3434 C CG . TYR A 1 467 ? 36.662 45.977 53.074 1.00 31.11 ? 460 TYR A CG 1 ATOM 3435 C CD1 . TYR A 1 467 ? 37.918 45.580 53.546 1.00 33.86 ? 460 TYR A CD1 1 ATOM 3436 C CD2 . TYR A 1 467 ? 36.468 47.316 52.745 1.00 33.77 ? 460 TYR A CD2 1 ATOM 3437 C CE1 . TYR A 1 467 ? 38.960 46.496 53.700 1.00 36.79 ? 460 TYR A CE1 1 ATOM 3438 C CE2 . TYR A 1 467 ? 37.509 48.244 52.880 1.00 35.47 ? 460 TYR A CE2 1 ATOM 3439 C CZ . TYR A 1 467 ? 38.740 47.821 53.361 1.00 38.95 ? 460 TYR A CZ 1 ATOM 3440 O OH . TYR A 1 467 ? 39.769 48.727 53.507 1.00 43.21 ? 460 TYR A OH 1 ATOM 3441 N N . THR A 1 468 ? 33.565 46.040 54.892 1.00 26.34 ? 461 THR A N 1 ATOM 3442 C CA . THR A 1 468 ? 33.136 47.102 55.801 1.00 25.78 ? 461 THR A CA 1 ATOM 3443 C C . THR A 1 468 ? 31.641 47.403 55.618 1.00 25.57 ? 461 THR A C 1 ATOM 3444 O O . THR A 1 468 ? 30.977 46.785 54.786 1.00 24.70 ? 461 THR A O 1 ATOM 3445 C CB . THR A 1 468 ? 33.994 48.408 55.636 1.00 26.82 ? 461 THR A CB 1 ATOM 3446 O OG1 . THR A 1 468 ? 33.765 49.275 56.761 1.00 27.85 ? 461 THR A OG1 1 ATOM 3447 C CG2 . THR A 1 468 ? 33.633 49.166 54.316 1.00 25.64 ? 461 THR A CG2 1 ATOM 3448 N N . LEU A 1 469 ? 31.124 48.314 56.431 1.00 24.51 ? 462 LEU A N 1 ATOM 3449 C CA . LEU A 1 469 ? 29.730 48.751 56.302 1.00 24.47 ? 462 LEU A CA 1 ATOM 3450 C C . LEU A 1 469 ? 29.496 49.672 55.114 1.00 24.01 ? 462 LEU A C 1 ATOM 3451 O O . LEU A 1 469 ? 30.398 50.415 54.705 1.00 24.53 ? 462 LEU A O 1 ATOM 3452 C CB . LEU A 1 469 ? 29.316 49.472 57.587 1.00 24.38 ? 462 LEU A CB 1 ATOM 3453 C CG . LEU A 1 469 ? 27.823 49.647 57.837 1.00 23.83 ? 462 LEU A CG 1 ATOM 3454 C CD1 . LEU A 1 469 ? 27.184 48.290 58.150 1.00 25.83 ? 462 LEU A CD1 1 ATOM 3455 C CD2 . LEU A 1 469 ? 27.713 50.604 59.038 1.00 23.91 ? 462 LEU A CD2 1 ATOM 3456 N N . ARG A 1 470 ? 28.278 49.612 54.573 1.00 22.67 ? 463 ARG A N 1 ATOM 3457 C CA . ARG A 1 470 ? 27.838 50.492 53.493 1.00 23.16 ? 463 ARG A CA 1 ATOM 3458 C C . ARG A 1 470 ? 26.462 51.011 53.901 1.00 22.28 ? 463 ARG A C 1 ATOM 3459 O O . ARG A 1 470 ? 25.538 50.214 54.121 1.00 22.69 ? 463 ARG A O 1 ATOM 3460 C CB . ARG A 1 470 ? 27.788 49.703 52.165 1.00 23.69 ? 463 ARG A CB 1 ATOM 3461 C CG . ARG A 1 470 ? 27.307 50.518 50.974 1.00 25.97 ? 463 ARG A CG 1 ATOM 3462 C CD . ARG A 1 470 ? 27.139 49.595 49.774 1.00 29.70 ? 463 ARG A CD 1 ATOM 3463 N NE . ARG A 1 470 ? 26.807 50.343 48.564 0.70 28.40 ? 463 ARG A NE 1 ATOM 3464 C CZ . ARG A 1 470 ? 26.339 49.788 47.448 0.70 28.02 ? 463 ARG A CZ 1 ATOM 3465 N NH1 . ARG A 1 470 ? 26.132 48.475 47.383 0.70 30.17 ? 463 ARG A NH1 1 ATOM 3466 N NH2 . ARG A 1 470 ? 26.053 50.553 46.408 0.70 26.74 ? 463 ARG A NH2 1 ATOM 3467 N N . VAL A 1 471 ? 26.329 52.330 54.043 1.00 21.49 ? 464 VAL A N 1 ATOM 3468 C CA . VAL A 1 471 ? 25.041 52.931 54.444 1.00 20.64 ? 464 VAL A CA 1 ATOM 3469 C C . VAL A 1 471 ? 24.637 53.976 53.405 1.00 20.99 ? 464 VAL A C 1 ATOM 3470 O O . VAL A 1 471 ? 25.472 54.796 52.987 1.00 21.13 ? 464 VAL A O 1 ATOM 3471 C CB . VAL A 1 471 ? 25.144 53.626 55.836 1.00 22.03 ? 464 VAL A CB 1 ATOM 3472 C CG1 . VAL A 1 471 ? 23.821 54.324 56.220 1.00 21.50 ? 464 VAL A CG1 1 ATOM 3473 C CG2 . VAL A 1 471 ? 25.586 52.618 56.922 1.00 23.25 ? 464 VAL A CG2 1 ATOM 3474 N N . ASP A 1 472 ? 23.377 53.904 52.966 1.00 19.49 ? 465 ASP A N 1 ATOM 3475 C CA . ASP A 1 472 ? 22.770 54.969 52.145 1.00 20.27 ? 465 ASP A CA 1 ATOM 3476 C C . ASP A 1 472 ? 21.519 55.408 52.901 1.00 19.54 ? 465 ASP A C 1 ATOM 3477 O O . ASP A 1 472 ? 20.695 54.582 53.290 1.00 19.01 ? 465 ASP A O 1 ATOM 3478 C CB . ASP A 1 472 ? 22.281 54.486 50.755 1.00 20.47 ? 465 ASP A CB 1 ATOM 3479 C CG . ASP A 1 472 ? 23.313 53.680 49.944 1.00 24.10 ? 465 ASP A CG 1 ATOM 3480 O OD1 . ASP A 1 472 ? 24.502 53.568 50.296 1.00 25.15 ? 465 ASP A OD1 1 ATOM 3481 O OD2 . ASP A 1 472 ? 22.901 53.127 48.881 1.00 27.79 ? 465 ASP A OD2 1 ATOM 3482 N N . CYS A 1 473 ? 21.330 56.707 53.057 1.00 19.71 ? 466 CYS A N 1 ATOM 3483 C CA . CYS A 1 473 ? 20.149 57.169 53.792 1.00 19.71 ? 466 CYS A CA 1 ATOM 3484 C C . CYS A 1 473 ? 19.949 58.647 53.624 1.00 19.04 ? 466 CYS A C 1 ATOM 3485 O O . CYS A 1 473 ? 20.837 59.380 53.155 1.00 20.87 ? 466 CYS A O 1 ATOM 3486 C CB . CYS A 1 473 ? 20.268 56.836 55.307 1.00 19.88 ? 466 CYS A CB 1 ATOM 3487 S SG . CYS A 1 473 ? 21.607 57.723 56.231 1.00 21.82 ? 466 CYS A SG 1 ATOM 3488 N N . THR A 1 474 ? 18.769 59.092 54.017 1.00 18.57 ? 467 THR A N 1 ATOM 3489 C CA . THR A 1 474 ? 18.488 60.511 54.117 1.00 18.33 ? 467 THR A CA 1 ATOM 3490 C C . THR A 1 474 ? 19.476 61.208 55.074 1.00 19.64 ? 467 THR A C 1 ATOM 3491 O O . THR A 1 474 ? 19.847 60.639 56.111 1.00 20.16 ? 467 THR A O 1 ATOM 3492 C CB . THR A 1 474 ? 17.044 60.742 54.626 1.00 17.51 ? 467 THR A CB 1 ATOM 3493 O OG1 . THR A 1 474 ? 16.860 62.147 54.834 1.00 18.38 ? 467 THR A OG1 1 ATOM 3494 C CG2 . THR A 1 474 ? 16.758 59.989 55.965 1.00 18.85 ? 467 THR A CG2 1 ATOM 3495 N N . PRO A 1 475 ? 19.872 62.449 54.763 1.00 19.01 ? 468 PRO A N 1 ATOM 3496 C CA . PRO A 1 475 ? 20.683 63.204 55.738 1.00 20.47 ? 468 PRO A CA 1 ATOM 3497 C C . PRO A 1 475 ? 20.052 63.243 57.139 1.00 20.89 ? 468 PRO A C 1 ATOM 3498 O O . PRO A 1 475 ? 20.787 63.392 58.118 1.00 21.13 ? 468 PRO A O 1 ATOM 3499 C CB . PRO A 1 475 ? 20.713 64.640 55.140 1.00 21.41 ? 468 PRO A CB 1 ATOM 3500 C CG . PRO A 1 475 ? 20.531 64.403 53.669 1.00 21.41 ? 468 PRO A CG 1 ATOM 3501 C CD . PRO A 1 475 ? 19.562 63.263 53.571 1.00 18.94 ? 468 PRO A CD 1 ATOM 3502 N N . LEU A 1 476 ? 18.712 63.141 57.243 1.00 20.55 ? 469 LEU A N 1 ATOM 3503 C CA . LEU A 1 476 ? 18.063 63.159 58.570 1.00 20.41 ? 469 LEU A CA 1 ATOM 3504 C C . LEU A 1 476 ? 18.540 62.020 59.492 1.00 21.12 ? 469 LEU A C 1 ATOM 3505 O O . LEU A 1 476 ? 18.394 62.117 60.701 1.00 22.03 ? 469 LEU A O 1 ATOM 3506 C CB . LEU A 1 476 ? 16.539 63.098 58.464 1.00 20.05 ? 469 LEU A CB 1 ATOM 3507 C CG . LEU A 1 476 ? 15.950 64.366 57.864 1.00 20.47 ? 469 LEU A CG 1 ATOM 3508 C CD1 . LEU A 1 476 ? 14.450 64.179 57.775 1.00 21.66 ? 469 LEU A CD1 1 ATOM 3509 C CD2 . LEU A 1 476 ? 16.327 65.608 58.738 1.00 19.65 ? 469 LEU A CD2 1 ATOM 3510 N N . MET A 1 477 ? 19.087 60.950 58.927 1.00 20.60 ? 470 MET A N 1 ATOM 3511 C CA . MET A 1 477 ? 19.546 59.800 59.731 1.00 20.71 ? 470 MET A CA 1 ATOM 3512 C C . MET A 1 477 ? 21.059 59.736 59.917 1.00 22.15 ? 470 MET A C 1 ATOM 3513 O O . MET A 1 477 ? 21.545 58.822 60.588 1.00 21.61 ? 470 MET A O 1 ATOM 3514 C CB . MET A 1 477 ? 19.065 58.454 59.120 1.00 21.19 ? 470 MET A CB 1 ATOM 3515 C CG . MET A 1 477 ? 17.568 58.232 59.248 1.00 21.80 ? 470 MET A CG 1 ATOM 3516 S SD . MET A 1 477 ? 17.238 56.678 58.400 1.00 25.53 ? 470 MET A SD 1 ATOM 3517 C CE . MET A 1 477 ? 15.445 56.705 58.289 1.00 24.76 ? 470 MET A CE 1 ATOM 3518 N N . TYR A 1 478 ? 21.810 60.712 59.391 1.00 21.46 ? 471 TYR A N 1 ATOM 3519 C CA . TYR A 1 478 ? 23.270 60.644 59.521 1.00 22.81 ? 471 TYR A CA 1 ATOM 3520 C C . TYR A 1 478 ? 23.726 60.544 60.981 1.00 23.68 ? 471 TYR A C 1 ATOM 3521 O O . TYR A 1 478 ? 24.588 59.719 61.318 1.00 23.86 ? 471 TYR A O 1 ATOM 3522 C CB . TYR A 1 478 ? 23.964 61.861 58.908 1.00 22.67 ? 471 TYR A CB 1 ATOM 3523 C CG . TYR A 1 478 ? 23.963 61.987 57.397 1.00 22.39 ? 471 TYR A CG 1 ATOM 3524 C CD1 . TYR A 1 478 ? 23.496 60.960 56.551 1.00 21.76 ? 471 TYR A CD1 1 ATOM 3525 C CD2 . TYR A 1 478 ? 24.421 63.178 56.809 1.00 23.98 ? 471 TYR A CD2 1 ATOM 3526 C CE1 . TYR A 1 478 ? 23.488 61.153 55.151 1.00 24.45 ? 471 TYR A CE1 1 ATOM 3527 C CE2 . TYR A 1 478 ? 24.420 63.363 55.449 1.00 25.56 ? 471 TYR A CE2 1 ATOM 3528 C CZ . TYR A 1 478 ? 23.965 62.356 54.618 1.00 25.99 ? 471 TYR A CZ 1 ATOM 3529 O OH . TYR A 1 478 ? 23.979 62.593 53.246 1.00 24.74 ? 471 TYR A OH 1 ATOM 3530 N N . SER A 1 479 ? 23.167 61.413 61.827 1.00 23.78 ? 472 SER A N 1 ATOM 3531 C CA . SER A 1 479 ? 23.610 61.475 63.240 1.00 23.99 ? 472 SER A CA 1 ATOM 3532 C C . SER A 1 479 ? 23.231 60.215 63.993 1.00 24.76 ? 472 SER A C 1 ATOM 3533 O O . SER A 1 479 ? 24.031 59.699 64.813 1.00 24.90 ? 472 SER A O 1 ATOM 3534 C CB . SER A 1 479 ? 23.037 62.729 63.895 1.00 24.97 ? 472 SER A CB 1 ATOM 3535 O OG A SER A 1 479 ? 23.672 63.879 63.322 0.50 27.51 ? 472 SER A OG 1 ATOM 3536 O OG B SER A 1 479 ? 23.456 62.867 65.263 0.50 22.17 ? 472 SER A OG 1 ATOM 3537 N N . LEU A 1 480 ? 22.027 59.716 63.721 1.00 24.20 ? 473 LEU A N 1 ATOM 3538 C CA . LEU A 1 480 ? 21.568 58.452 64.290 1.00 25.15 ? 473 LEU A CA 1 ATOM 3539 C C . LEU A 1 480 ? 22.559 57.329 63.939 1.00 24.70 ? 473 LEU A C 1 ATOM 3540 O O . LEU A 1 480 ? 22.973 56.537 64.811 1.00 24.97 ? 473 LEU A O 1 ATOM 3541 C CB . LEU A 1 480 ? 20.175 58.100 63.744 1.00 24.57 ? 473 LEU A CB 1 ATOM 3542 C CG . LEU A 1 480 ? 19.659 56.658 63.906 1.00 25.21 ? 473 LEU A CG 1 ATOM 3543 C CD1 . LEU A 1 480 ? 19.510 56.254 65.381 1.00 29.15 ? 473 LEU A CD1 1 ATOM 3544 C CD2 . LEU A 1 480 ? 18.373 56.484 63.153 1.00 27.41 ? 473 LEU A CD2 1 ATOM 3545 N N . VAL A 1 481 ? 22.953 57.269 62.671 1.00 24.01 ? 474 VAL A N 1 ATOM 3546 C CA . VAL A 1 481 ? 23.877 56.200 62.211 1.00 24.02 ? 474 VAL A CA 1 ATOM 3547 C C . VAL A 1 481 ? 25.264 56.358 62.845 1.00 24.87 ? 474 VAL A C 1 ATOM 3548 O O . VAL A 1 481 ? 25.852 55.364 63.307 1.00 25.12 ? 474 VAL A O 1 ATOM 3549 C CB . VAL A 1 481 ? 23.996 56.196 60.687 1.00 24.30 ? 474 VAL A CB 1 ATOM 3550 C CG1 . VAL A 1 481 ? 25.110 55.243 60.235 1.00 26.34 ? 474 VAL A CG1 1 ATOM 3551 C CG2 . VAL A 1 481 ? 22.667 55.756 60.074 1.00 24.19 ? 474 VAL A CG2 1 ATOM 3552 N N . HIS A 1 482 ? 25.786 57.583 62.857 1.00 25.19 ? 475 HIS A N 1 ATOM 3553 C CA . HIS A 1 482 ? 27.076 57.823 63.560 1.00 27.30 ? 475 HIS A CA 1 ATOM 3554 C C . HIS A 1 482 ? 26.995 57.366 65.018 1.00 27.70 ? 475 HIS A C 1 ATOM 3555 O O . HIS A 1 482 ? 27.866 56.609 65.481 1.00 27.93 ? 475 HIS A O 1 ATOM 3556 C CB . HIS A 1 482 ? 27.490 59.288 63.498 1.00 27.18 ? 475 HIS A CB 1 ATOM 3557 C CG . HIS A 1 482 ? 27.767 59.776 62.118 1.00 31.23 ? 475 HIS A CG 1 ATOM 3558 N ND1 . HIS A 1 482 ? 27.648 61.105 61.768 0.80 35.90 ? 475 HIS A ND1 1 ATOM 3559 C CD2 . HIS A 1 482 ? 28.085 59.113 60.984 1.00 31.07 ? 475 HIS A CD2 1 ATOM 3560 C CE1 . HIS A 1 482 ? 27.914 61.239 60.480 0.80 36.39 ? 475 HIS A CE1 1 ATOM 3561 N NE2 . HIS A 1 482 ? 28.200 60.048 59.986 1.00 32.70 ? 475 HIS A NE2 1 ATOM 3562 N N . ASN A 1 483 ? 25.949 57.791 65.727 1.00 26.86 ? 476 ASN A N 1 ATOM 3563 C CA . ASN A 1 483 ? 25.846 57.472 67.151 1.00 27.89 ? 476 ASN A CA 1 ATOM 3564 C C . ASN A 1 483 ? 25.671 55.991 67.410 1.00 27.93 ? 476 ASN A C 1 ATOM 3565 O O . ASN A 1 483 ? 26.295 55.427 68.316 1.00 28.75 ? 476 ASN A O 1 ATOM 3566 C CB . ASN A 1 483 ? 24.721 58.238 67.826 1.00 27.63 ? 476 ASN A CB 1 ATOM 3567 C CG . ASN A 1 483 ? 25.012 59.706 67.946 1.00 29.76 ? 476 ASN A CG 1 ATOM 3568 O OD1 . ASN A 1 483 ? 26.055 60.184 67.519 1.00 30.60 ? 476 ASN A OD1 1 ATOM 3569 N ND2 . ASN A 1 483 ? 24.070 60.441 68.526 1.00 29.04 ? 476 ASN A ND2 1 ATOM 3570 N N . LEU A 1 484 ? 24.816 55.350 66.625 1.00 26.28 ? 477 LEU A N 1 ATOM 3571 C CA . LEU A 1 484 ? 24.596 53.922 66.808 1.00 25.82 ? 477 LEU A CA 1 ATOM 3572 C C . LEU A 1 484 ? 25.859 53.122 66.556 1.00 26.27 ? 477 LEU A C 1 ATOM 3573 O O . LEU A 1 484 ? 26.209 52.239 67.360 1.00 27.03 ? 477 LEU A O 1 ATOM 3574 C CB . LEU A 1 484 ? 23.452 53.437 65.882 1.00 25.15 ? 477 LEU A CB 1 ATOM 3575 C CG . LEU A 1 484 ? 23.221 51.926 65.940 1.00 26.75 ? 477 LEU A CG 1 ATOM 3576 C CD1 . LEU A 1 484 ? 22.871 51.453 67.345 1.00 28.47 ? 477 LEU A CD1 1 ATOM 3577 C CD2 . LEU A 1 484 ? 22.123 51.539 64.933 1.00 26.31 ? 477 LEU A CD2 1 ATOM 3578 N N . THR A 1 485 ? 26.553 53.409 65.451 1.00 25.98 ? 478 THR A N 1 ATOM 3579 C CA . THR A 1 485 ? 27.744 52.605 65.085 1.00 26.20 ? 478 THR A CA 1 ATOM 3580 C C . THR A 1 485 ? 28.899 52.814 66.080 1.00 28.01 ? 478 THR A C 1 ATOM 3581 O O . THR A 1 485 ? 29.743 51.927 66.263 1.00 27.47 ? 478 THR A O 1 ATOM 3582 C CB . THR A 1 485 ? 28.227 52.843 63.624 1.00 25.94 ? 478 THR A CB 1 ATOM 3583 O OG1 . THR A 1 485 ? 28.609 54.206 63.434 1.00 25.57 ? 478 THR A OG1 1 ATOM 3584 C CG2 . THR A 1 485 ? 27.123 52.439 62.584 1.00 24.01 ? 478 THR A CG2 1 ATOM 3585 N N . LYS A 1 486 ? 28.901 53.954 66.779 1.00 28.52 ? 479 LYS A N 1 ATOM 3586 C CA . LYS A 1 486 ? 29.889 54.138 67.866 1.00 30.29 ? 479 LYS A CA 1 ATOM 3587 C C . LYS A 1 486 ? 29.645 53.213 69.071 1.00 31.24 ? 479 LYS A C 1 ATOM 3588 O O . LYS A 1 486 ? 30.574 52.974 69.856 1.00 32.40 ? 479 LYS A O 1 ATOM 3589 C CB . LYS A 1 486 ? 29.915 55.605 68.341 1.00 30.28 ? 479 LYS A CB 1 ATOM 3590 C CG . LYS A 1 486 ? 30.572 56.560 67.348 1.00 31.09 ? 479 LYS A CG 1 ATOM 3591 C CD . LYS A 1 486 ? 30.412 58.011 67.725 1.00 33.06 ? 479 LYS A CD 1 ATOM 3592 C CE . LYS A 1 486 ? 30.967 58.885 66.614 1.00 35.72 ? 479 LYS A CE 1 ATOM 3593 N NZ . LYS A 1 486 ? 30.916 60.345 66.961 1.00 39.10 ? 479 LYS A NZ 1 ATOM 3594 N N A GLU A 1 487 ? 28.404 52.741 69.209 0.50 31.33 ? 480 GLU A N 1 ATOM 3595 N N B GLU A 1 487 ? 28.427 52.701 69.218 0.50 31.03 ? 480 GLU A N 1 ATOM 3596 C CA A GLU A 1 487 ? 27.964 51.867 70.307 0.50 32.96 ? 480 GLU A CA 1 ATOM 3597 C CA B GLU A 1 487 ? 28.080 51.839 70.355 0.50 32.39 ? 480 GLU A CA 1 ATOM 3598 C C A GLU A 1 487 ? 28.191 50.391 69.997 0.50 32.30 ? 480 GLU A C 1 ATOM 3599 C C B GLU A 1 487 ? 27.959 50.371 69.968 0.50 31.89 ? 480 GLU A C 1 ATOM 3600 O O A GLU A 1 487 ? 28.254 49.568 70.902 0.50 32.96 ? 480 GLU A O 1 ATOM 3601 O O B GLU A 1 487 ? 27.549 49.545 70.792 0.50 32.05 ? 480 GLU A O 1 ATOM 3602 C CB A GLU A 1 487 ? 26.461 52.060 70.587 0.50 33.04 ? 480 GLU A CB 1 ATOM 3603 C CB B GLU A 1 487 ? 26.771 52.295 70.996 0.50 32.70 ? 480 GLU A CB 1 ATOM 3604 C CG A GLU A 1 487 ? 26.089 53.247 71.481 0.50 38.33 ? 480 GLU A CG 1 ATOM 3605 C CG B GLU A 1 487 ? 26.730 53.776 71.330 0.50 35.75 ? 480 GLU A CG 1 ATOM 3606 C CD A GLU A 1 487 ? 24.631 53.191 71.950 0.50 42.25 ? 480 GLU A CD 1 ATOM 3607 C CD B GLU A 1 487 ? 27.680 54.147 72.437 0.50 39.55 ? 480 GLU A CD 1 ATOM 3608 O OE1 A GLU A 1 487 ? 23.863 54.131 71.658 0.50 44.10 ? 480 GLU A OE1 1 ATOM 3609 O OE1 B GLU A 1 487 ? 28.043 53.254 73.238 0.50 41.63 ? 480 GLU A OE1 1 ATOM 3610 O OE2 A GLU A 1 487 ? 24.254 52.195 72.609 0.50 46.14 ? 480 GLU A OE2 1 ATOM 3611 O OE2 B GLU A 1 487 ? 28.067 55.335 72.506 0.50 43.00 ? 480 GLU A OE2 1 ATOM 3612 N N . LEU A 1 488 ? 28.276 50.064 68.711 1.00 30.77 ? 481 LEU A N 1 ATOM 3613 C CA . LEU A 1 488 ? 28.384 48.669 68.248 1.00 30.52 ? 481 LEU A CA 1 ATOM 3614 C C . LEU A 1 488 ? 29.820 48.205 68.086 1.00 31.51 ? 481 LEU A C 1 ATOM 3615 O O . LEU A 1 488 ? 30.693 48.988 67.729 1.00 32.50 ? 481 LEU A O 1 ATOM 3616 C CB . LEU A 1 488 ? 27.657 48.472 66.897 1.00 29.16 ? 481 LEU A CB 1 ATOM 3617 C CG . LEU A 1 488 ? 26.187 48.876 66.866 1.00 28.85 ? 481 LEU A CG 1 ATOM 3618 C CD1 . LEU A 1 488 ? 25.625 48.729 65.429 1.00 25.45 ? 481 LEU A CD1 1 ATOM 3619 C CD2 . LEU A 1 488 ? 25.377 48.025 67.851 1.00 30.12 ? 481 LEU A CD2 1 ATOM 3620 N N . LYS A 1 489 ? 30.029 46.916 68.304 1.00 31.28 ? 482 LYS A N 1 ATOM 3621 C CA . LYS A 1 489 ? 31.356 46.301 68.190 1.00 33.34 ? 482 LYS A CA 1 ATOM 3622 C C . LYS A 1 489 ? 31.722 46.057 66.736 1.00 32.45 ? 482 LYS A C 1 ATOM 3623 O O . LYS A 1 489 ? 30.888 45.573 65.966 1.00 32.83 ? 482 LYS A O 1 ATOM 3624 C CB . LYS A 1 489 ? 31.375 44.968 68.933 1.00 34.21 ? 482 LYS A CB 1 ATOM 3625 C CG . LYS A 1 489 ? 31.168 45.082 70.434 1.00 39.66 ? 482 LYS A CG 1 ATOM 3626 C CD . LYS A 1 489 ? 31.252 43.686 71.083 1.00 45.78 ? 482 LYS A CD 1 ATOM 3627 C CE . LYS A 1 489 ? 31.995 43.708 72.420 1.00 52.96 ? 482 LYS A CE 1 ATOM 3628 N NZ . LYS A 1 489 ? 31.521 44.748 73.402 1.00 57.59 ? 482 LYS A NZ 1 ATOM 3629 N N . SER A 1 490 ? 32.944 46.379 66.336 1.00 31.64 ? 483 SER A N 1 ATOM 3630 C CA . SER A 1 490 ? 33.371 45.977 64.998 1.00 31.29 ? 483 SER A CA 1 ATOM 3631 C C . SER A 1 490 ? 33.559 44.464 64.906 1.00 31.15 ? 483 SER A C 1 ATOM 3632 O O . SER A 1 490 ? 34.196 43.862 65.776 1.00 32.18 ? 483 SER A O 1 ATOM 3633 C CB . SER A 1 490 ? 34.666 46.670 64.578 1.00 31.53 ? 483 SER A CB 1 ATOM 3634 O OG . SER A 1 490 ? 35.018 46.209 63.284 1.00 31.61 ? 483 SER A OG 1 ATOM 3635 N N . PRO A 1 491 ? 33.034 43.841 63.845 1.00 30.18 ? 484 PRO A N 1 ATOM 3636 C CA . PRO A 1 491 ? 33.262 42.403 63.654 1.00 30.15 ? 484 PRO A CA 1 ATOM 3637 C C . PRO A 1 491 ? 34.562 42.144 62.879 1.00 31.10 ? 484 PRO A C 1 ATOM 3638 O O . PRO A 1 491 ? 34.890 40.987 62.615 1.00 31.31 ? 484 PRO A O 1 ATOM 3639 C CB . PRO A 1 491 ? 32.072 41.993 62.780 1.00 28.51 ? 484 PRO A CB 1 ATOM 3640 C CG . PRO A 1 491 ? 31.871 43.214 61.879 1.00 27.82 ? 484 PRO A CG 1 ATOM 3641 C CD . PRO A 1 491 ? 32.124 44.407 62.824 1.00 29.56 ? 484 PRO A CD 1 ATOM 3642 N N . ASP A 1 492 ? 35.272 43.208 62.491 1.00 31.64 ? 485 ASP A N 1 ATOM 3643 C CA . ASP A 1 492 ? 36.364 43.073 61.527 1.00 32.68 ? 485 ASP A CA 1 ATOM 3644 C C . ASP A 1 492 ? 37.630 42.558 62.197 1.00 34.33 ? 485 ASP A C 1 ATOM 3645 O O . ASP A 1 492 ? 37.940 42.932 63.344 1.00 34.69 ? 485 ASP A O 1 ATOM 3646 C CB . ASP A 1 492 ? 36.727 44.412 60.896 1.00 31.98 ? 485 ASP A CB 1 ATOM 3647 C CG . ASP A 1 492 ? 35.580 45.042 60.113 1.00 31.34 ? 485 ASP A CG 1 ATOM 3648 O OD1 . ASP A 1 492 ? 34.473 44.467 60.069 1.00 32.78 ? 485 ASP A OD1 1 ATOM 3649 O OD2 . ASP A 1 492 ? 35.803 46.116 59.543 1.00 31.91 ? 485 ASP A OD2 1 ATOM 3650 N N A GLU A 1 493 ? 38.364 41.723 61.472 0.60 34.97 ? 486 GLU A N 1 ATOM 3651 N N B GLU A 1 493 ? 38.366 41.728 61.463 0.40 34.80 ? 486 GLU A N 1 ATOM 3652 C CA A GLU A 1 493 ? 39.687 41.281 61.916 0.60 37.05 ? 486 GLU A CA 1 ATOM 3653 C CA B GLU A 1 493 ? 39.709 41.298 61.856 0.40 36.54 ? 486 GLU A CA 1 ATOM 3654 C C A GLU A 1 493 ? 40.624 42.487 62.008 0.60 37.37 ? 486 GLU A C 1 ATOM 3655 C C B GLU A 1 493 ? 40.609 42.521 62.014 0.40 37.13 ? 486 GLU A C 1 ATOM 3656 O O A GLU A 1 493 ? 40.661 43.340 61.117 0.60 37.45 ? 486 GLU A O 1 ATOM 3657 O O B GLU A 1 493 ? 40.606 43.419 61.166 0.40 37.05 ? 486 GLU A O 1 ATOM 3658 C CB A GLU A 1 493 ? 40.236 40.225 60.955 0.60 37.34 ? 486 GLU A CB 1 ATOM 3659 C CB B GLU A 1 493 ? 40.274 40.365 60.785 0.40 36.60 ? 486 GLU A CB 1 ATOM 3660 C CG A GLU A 1 493 ? 39.516 38.871 61.029 0.60 40.28 ? 486 GLU A CG 1 ATOM 3661 C CG B GLU A 1 493 ? 41.646 39.795 61.090 0.40 38.97 ? 486 GLU A CG 1 ATOM 3662 C CD A GLU A 1 493 ? 38.252 38.785 60.167 0.60 42.14 ? 486 GLU A CD 1 ATOM 3663 C CD B GLU A 1 493 ? 42.003 38.637 60.174 0.40 40.63 ? 486 GLU A CD 1 ATOM 3664 O OE1 A GLU A 1 493 ? 37.839 39.801 59.537 0.60 46.35 ? 486 GLU A OE1 1 ATOM 3665 O OE1 B GLU A 1 493 ? 42.671 37.697 60.649 0.40 42.98 ? 486 GLU A OE1 1 ATOM 3666 O OE2 A GLU A 1 493 ? 37.653 37.685 60.131 0.60 43.27 ? 486 GLU A OE2 1 ATOM 3667 O OE2 B GLU A 1 493 ? 41.599 38.662 58.987 0.40 41.14 ? 486 GLU A OE2 1 ATOM 3668 N N . GLY A 1 494 ? 41.363 42.575 63.107 1.00 38.52 ? 487 GLY A N 1 ATOM 3669 C CA . GLY A 1 494 ? 42.258 43.712 63.337 1.00 39.15 ? 487 GLY A CA 1 ATOM 3670 C C . GLY A 1 494 ? 41.605 44.839 64.105 1.00 39.24 ? 487 GLY A C 1 ATOM 3671 O O . GLY A 1 494 ? 42.288 45.764 64.558 1.00 40.69 ? 487 GLY A O 1 ATOM 3672 N N . PHE A 1 495 ? 40.283 44.771 64.262 1.00 37.84 ? 488 PHE A N 1 ATOM 3673 C CA . PHE A 1 495 ? 39.555 45.789 64.999 1.00 37.47 ? 488 PHE A CA 1 ATOM 3674 C C . PHE A 1 495 ? 38.827 45.203 66.193 1.00 37.96 ? 488 PHE A C 1 ATOM 3675 O O . PHE A 1 495 ? 37.850 45.788 66.656 1.00 37.99 ? 488 PHE A O 1 ATOM 3676 C CB . PHE A 1 495 ? 38.542 46.491 64.070 1.00 35.91 ? 488 PHE A CB 1 ATOM 3677 C CG . PHE A 1 495 ? 39.183 47.327 63.019 1.00 35.13 ? 488 PHE A CG 1 ATOM 3678 C CD1 . PHE A 1 495 ? 39.403 48.675 63.237 1.00 35.95 ? 488 PHE A CD1 1 ATOM 3679 C CD2 . PHE A 1 495 ? 39.603 46.755 61.816 1.00 37.06 ? 488 PHE A CD2 1 ATOM 3680 C CE1 . PHE A 1 495 ? 40.015 49.476 62.265 1.00 37.59 ? 488 PHE A CE1 1 ATOM 3681 C CE2 . PHE A 1 495 ? 40.215 47.543 60.832 1.00 37.10 ? 488 PHE A CE2 1 ATOM 3682 C CZ . PHE A 1 495 ? 40.420 48.909 61.062 1.00 37.28 ? 488 PHE A CZ 1 ATOM 3683 N N . GLU A 1 496 ? 39.280 44.054 66.695 1.00 39.61 ? 489 GLU A N 1 ATOM 3684 C CA . GLU A 1 496 ? 38.652 43.493 67.896 1.00 40.88 ? 489 GLU A CA 1 ATOM 3685 C C . GLU A 1 496 ? 38.732 44.483 69.064 1.00 41.31 ? 489 GLU A C 1 ATOM 3686 O O . GLU A 1 496 ? 39.775 45.111 69.309 1.00 43.03 ? 489 GLU A O 1 ATOM 3687 C CB . GLU A 1 496 ? 39.146 42.065 68.262 1.00 42.41 ? 489 GLU A CB 1 ATOM 3688 C CG . GLU A 1 496 ? 40.528 41.666 67.843 1.00 46.23 ? 489 GLU A CG 1 ATOM 3689 C CD . GLU A 1 496 ? 40.751 41.531 66.339 1.00 44.21 ? 489 GLU A CD 1 ATOM 3690 O OE1 . GLU A 1 496 ? 40.291 40.561 65.684 1.00 45.70 ? 489 GLU A OE1 1 ATOM 3691 O OE2 . GLU A 1 496 ? 41.481 42.398 65.834 1.00 45.76 ? 489 GLU A OE2 1 ATOM 3692 N N . GLY A 1 497 ? 37.604 44.668 69.738 1.00 40.34 ? 490 GLY A N 1 ATOM 3693 C CA . GLY A 1 497 ? 37.492 45.647 70.816 1.00 40.83 ? 490 GLY A CA 1 ATOM 3694 C C . GLY A 1 497 ? 37.331 47.099 70.388 1.00 40.24 ? 490 GLY A C 1 ATOM 3695 O O . GLY A 1 497 ? 37.275 47.999 71.239 1.00 41.44 ? 490 GLY A O 1 ATOM 3696 N N . LYS A 1 498 ? 37.253 47.347 69.080 1.00 37.81 ? 491 LYS A N 1 ATOM 3697 C CA . LYS A 1 498 ? 37.004 48.692 68.586 1.00 37.11 ? 491 LYS A CA 1 ATOM 3698 C C . LYS A 1 498 ? 35.552 48.776 68.129 1.00 34.87 ? 491 LYS A C 1 ATOM 3699 O O . LYS A 1 498 ? 34.906 47.759 67.928 1.00 33.82 ? 491 LYS A O 1 ATOM 3700 C CB . LYS A 1 498 ? 37.935 49.035 67.417 1.00 37.69 ? 491 LYS A CB 1 ATOM 3701 C CG . LYS A 1 498 ? 39.425 48.832 67.732 1.00 40.90 ? 491 LYS A CG 1 ATOM 3702 C CD . LYS A 1 498 ? 39.823 49.681 68.933 1.00 46.19 ? 491 LYS A CD 1 ATOM 3703 C CE . LYS A 1 498 ? 41.312 49.549 69.246 1.00 51.63 ? 491 LYS A CE 1 ATOM 3704 N NZ . LYS A 1 498 ? 42.104 49.925 68.043 1.00 54.19 ? 491 LYS A NZ 1 ATOM 3705 N N . SER A 1 499 ? 35.059 49.997 67.987 1.00 33.98 ? 492 SER A N 1 ATOM 3706 C CA . SER A 1 499 ? 33.681 50.232 67.530 1.00 32.56 ? 492 SER A CA 1 ATOM 3707 C C . SER A 1 499 ? 33.554 49.988 66.028 1.00 31.09 ? 492 SER A C 1 ATOM 3708 O O . SER A 1 499 ? 34.519 50.095 65.272 1.00 30.13 ? 492 SER A O 1 ATOM 3709 C CB . SER A 1 499 ? 33.250 51.664 67.850 1.00 32.89 ? 492 SER A CB 1 ATOM 3710 O OG . SER A 1 499 ? 33.883 52.569 66.966 1.00 34.02 ? 492 SER A OG 1 ATOM 3711 N N . LEU A 1 500 ? 32.332 49.689 65.603 1.00 29.54 ? 493 LEU A N 1 ATOM 3712 C CA . LEU A 1 500 ? 32.008 49.626 64.183 1.00 28.41 ? 493 LEU A CA 1 ATOM 3713 C C . LEU A 1 500 ? 32.264 50.996 63.523 1.00 27.88 ? 493 LEU A C 1 ATOM 3714 O O . LEU A 1 500 ? 32.759 51.064 62.389 1.00 27.58 ? 493 LEU A O 1 ATOM 3715 C CB . LEU A 1 500 ? 30.544 49.186 64.014 1.00 27.08 ? 493 LEU A CB 1 ATOM 3716 C CG . LEU A 1 500 ? 29.975 49.096 62.596 1.00 26.77 ? 493 LEU A CG 1 ATOM 3717 C CD1 . LEU A 1 500 ? 30.838 48.100 61.746 1.00 26.67 ? 493 LEU A CD1 1 ATOM 3718 C CD2 . LEU A 1 500 ? 28.513 48.685 62.638 1.00 25.70 ? 493 LEU A CD2 1 ATOM 3719 N N . TYR A 1 501 ? 31.943 52.091 64.224 1.00 28.32 ? 494 TYR A N 1 ATOM 3720 C CA . TYR A 1 501 ? 32.237 53.410 63.684 1.00 29.02 ? 494 TYR A CA 1 ATOM 3721 C C . TYR A 1 501 ? 33.722 53.542 63.336 1.00 29.72 ? 494 TYR A C 1 ATOM 3722 O O . TYR A 1 501 ? 34.071 54.072 62.281 1.00 29.92 ? 494 TYR A O 1 ATOM 3723 C CB . TYR A 1 501 ? 31.868 54.514 64.688 1.00 29.74 ? 494 TYR A CB 1 ATOM 3724 C CG . TYR A 1 501 ? 32.070 55.923 64.160 1.00 29.86 ? 494 TYR A CG 1 ATOM 3725 C CD1 . TYR A 1 501 ? 31.046 56.576 63.459 1.00 28.83 ? 494 TYR A CD1 1 ATOM 3726 C CD2 . TYR A 1 501 ? 33.268 56.607 64.365 1.00 30.96 ? 494 TYR A CD2 1 ATOM 3727 C CE1 . TYR A 1 501 ? 31.215 57.877 62.977 1.00 30.50 ? 494 TYR A CE1 1 ATOM 3728 C CE2 . TYR A 1 501 ? 33.454 57.895 63.882 1.00 30.82 ? 494 TYR A CE2 1 ATOM 3729 C CZ . TYR A 1 501 ? 32.418 58.530 63.205 1.00 30.95 ? 494 TYR A CZ 1 ATOM 3730 O OH . TYR A 1 501 ? 32.604 59.796 62.717 1.00 33.58 ? 494 TYR A OH 1 ATOM 3731 N N . GLU A 1 502 ? 34.593 53.100 64.235 1.00 30.76 ? 495 GLU A N 1 ATOM 3732 C CA . GLU A 1 502 ? 36.032 53.194 63.999 1.00 32.03 ? 495 GLU A CA 1 ATOM 3733 C C . GLU A 1 502 ? 36.487 52.405 62.753 1.00 31.43 ? 495 GLU A C 1 ATOM 3734 O O . GLU A 1 502 ? 37.193 52.948 61.899 1.00 31.62 ? 495 GLU A O 1 ATOM 3735 C CB . GLU A 1 502 ? 36.844 52.761 65.241 1.00 33.42 ? 495 GLU A CB 1 ATOM 3736 C CG . GLU A 1 502 ? 38.339 52.839 64.986 1.00 36.91 ? 495 GLU A CG 1 ATOM 3737 C CD . GLU A 1 502 ? 39.187 52.644 66.236 1.00 42.80 ? 495 GLU A CD 1 ATOM 3738 O OE1 . GLU A 1 502 ? 38.746 53.018 67.350 1.00 44.96 ? 495 GLU A OE1 1 ATOM 3739 O OE2 . GLU A 1 502 ? 40.310 52.130 66.081 1.00 44.71 ? 495 GLU A OE2 1 ATOM 3740 N N . SER A 1 503 ? 36.062 51.148 62.641 1.00 31.19 ? 496 SER A N 1 ATOM 3741 C CA . SER A 1 503 ? 36.500 50.320 61.509 1.00 31.17 ? 496 SER A CA 1 ATOM 3742 C C . SER A 1 503 ? 35.902 50.828 60.205 1.00 30.67 ? 496 SER A C 1 ATOM 3743 O O . SER A 1 503 ? 36.598 50.931 59.189 1.00 30.48 ? 496 SER A O 1 ATOM 3744 C CB . SER A 1 503 ? 36.215 48.828 61.720 1.00 31.56 ? 496 SER A CB 1 ATOM 3745 O OG . SER A 1 503 ? 34.838 48.545 61.781 1.00 28.98 ? 496 SER A OG 1 ATOM 3746 N N . TRP A 1 504 ? 34.620 51.189 60.255 1.00 29.25 ? 497 TRP A N 1 ATOM 3747 C CA . TRP A 1 504 ? 33.940 51.722 59.093 1.00 29.15 ? 497 TRP A CA 1 ATOM 3748 C C . TRP A 1 504 ? 34.576 53.037 58.628 1.00 29.73 ? 497 TRP A C 1 ATOM 3749 O O . TRP A 1 504 ? 34.825 53.217 57.433 1.00 29.67 ? 497 TRP A O 1 ATOM 3750 C CB . TRP A 1 504 ? 32.457 51.869 59.422 1.00 28.51 ? 497 TRP A CB 1 ATOM 3751 C CG . TRP A 1 504 ? 31.593 52.490 58.367 1.00 27.28 ? 497 TRP A CG 1 ATOM 3752 C CD1 . TRP A 1 504 ? 31.722 52.389 56.998 1.00 25.72 ? 497 TRP A CD1 1 ATOM 3753 C CD2 . TRP A 1 504 ? 30.441 53.283 58.609 1.00 27.08 ? 497 TRP A CD2 1 ATOM 3754 N NE1 . TRP A 1 504 ? 30.708 53.102 56.382 1.00 24.84 ? 497 TRP A NE1 1 ATOM 3755 C CE2 . TRP A 1 504 ? 29.899 53.647 57.342 1.00 26.04 ? 497 TRP A CE2 1 ATOM 3756 C CE3 . TRP A 1 504 ? 29.798 53.727 59.781 1.00 27.88 ? 497 TRP A CE3 1 ATOM 3757 C CZ2 . TRP A 1 504 ? 28.759 54.458 57.215 1.00 25.63 ? 497 TRP A CZ2 1 ATOM 3758 C CZ3 . TRP A 1 504 ? 28.656 54.521 59.659 1.00 27.59 ? 497 TRP A CZ3 1 ATOM 3759 C CH2 . TRP A 1 504 ? 28.148 54.881 58.378 1.00 25.78 ? 497 TRP A CH2 1 ATOM 3760 N N . THR A 1 505 ? 34.862 53.942 59.569 1.00 30.45 ? 498 THR A N 1 ATOM 3761 C CA . THR A 1 505 ? 35.465 55.223 59.227 1.00 31.20 ? 498 THR A CA 1 ATOM 3762 C C . THR A 1 505 ? 36.885 55.049 58.640 1.00 32.54 ? 498 THR A C 1 ATOM 3763 O O . THR A 1 505 ? 37.239 55.704 57.654 1.00 32.26 ? 498 THR A O 1 ATOM 3764 C CB . THR A 1 505 ? 35.452 56.158 60.456 1.00 32.11 ? 498 THR A CB 1 ATOM 3765 O OG1 A THR A 1 505 ? 34.086 56.454 60.783 0.90 28.87 ? 498 THR A OG1 1 ATOM 3766 C CG2 A THR A 1 505 ? 36.209 57.463 60.178 0.65 31.52 ? 498 THR A CG2 1 ATOM 3767 N N . LYS A 1 506 ? 37.666 54.146 59.233 1.00 33.57 ? 499 LYS A N 1 ATOM 3768 C CA . LYS A 1 506 ? 38.998 53.813 58.733 1.00 35.63 ? 499 LYS A CA 1 ATOM 3769 C C . LYS A 1 506 ? 38.938 53.270 57.291 1.00 35.14 ? 499 LYS A C 1 ATOM 3770 O O . LYS A 1 506 ? 39.688 53.717 56.428 1.00 36.28 ? 499 LYS A O 1 ATOM 3771 C CB . LYS A 1 506 ? 39.672 52.797 59.670 1.00 36.65 ? 499 LYS A CB 1 ATOM 3772 C CG . LYS A 1 506 ? 41.192 52.828 59.684 1.00 42.02 ? 499 LYS A CG 1 ATOM 3773 C CD . LYS A 1 506 ? 41.846 52.489 58.350 1.00 48.17 ? 499 LYS A CD 1 ATOM 3774 C CE . LYS A 1 506 ? 43.394 52.412 58.478 1.00 51.55 ? 499 LYS A CE 1 ATOM 3775 N NZ . LYS A 1 506 ? 44.029 53.754 58.660 1.00 54.16 ? 499 LYS A NZ 1 ATOM 3776 N N . LYS A 1 507 ? 38.024 52.337 57.037 1.00 34.37 ? 500 LYS A N 1 ATOM 3777 C CA . LYS A 1 507 ? 37.928 51.646 55.736 1.00 33.80 ? 500 LYS A CA 1 ATOM 3778 C C . LYS A 1 507 ? 37.217 52.428 54.629 1.00 33.66 ? 500 LYS A C 1 ATOM 3779 O O . LYS A 1 507 ? 37.486 52.203 53.444 1.00 33.97 ? 500 LYS A O 1 ATOM 3780 C CB . LYS A 1 507 ? 37.260 50.282 55.930 1.00 33.57 ? 500 LYS A CB 1 ATOM 3781 C CG . LYS A 1 507 ? 38.153 49.308 56.735 1.00 32.72 ? 500 LYS A CG 1 ATOM 3782 C CD . LYS A 1 507 ? 37.487 47.929 56.917 1.00 31.72 ? 500 LYS A CD 1 ATOM 3783 C CE . LYS A 1 507 ? 38.426 46.895 57.525 1.00 34.83 ? 500 LYS A CE 1 ATOM 3784 N NZ . LYS A 1 507 ? 37.741 45.571 57.634 1.00 33.95 ? 500 LYS A NZ 1 ATOM 3785 N N . SER A 1 508 ? 36.300 53.312 55.023 1.00 32.86 ? 501 SER A N 1 ATOM 3786 C CA . SER A 1 508 ? 35.440 54.034 54.091 1.00 32.92 ? 501 SER A CA 1 ATOM 3787 C C . SER A 1 508 ? 35.314 55.501 54.520 1.00 33.73 ? 501 SER A C 1 ATOM 3788 O O . SER A 1 508 ? 34.253 55.953 54.957 1.00 32.25 ? 501 SER A O 1 ATOM 3789 C CB . SER A 1 508 ? 34.066 53.360 54.029 1.00 31.62 ? 501 SER A CB 1 ATOM 3790 O OG . SER A 1 508 ? 33.352 53.848 52.915 1.00 34.21 ? 501 SER A OG 1 ATOM 3791 N N . PRO A 1 509 ? 36.427 56.254 54.408 1.00 35.17 ? 502 PRO A N 1 ATOM 3792 C CA . PRO A 1 509 ? 36.400 57.622 54.904 1.00 36.06 ? 502 PRO A CA 1 ATOM 3793 C C . PRO A 1 509 ? 35.500 58.495 54.053 1.00 36.79 ? 502 PRO A C 1 ATOM 3794 O O . PRO A 1 509 ? 35.415 58.310 52.837 1.00 35.76 ? 502 PRO A O 1 ATOM 3795 C CB . PRO A 1 509 ? 37.867 58.073 54.795 1.00 37.58 ? 502 PRO A CB 1 ATOM 3796 C CG . PRO A 1 509 ? 38.473 57.176 53.755 1.00 37.09 ? 502 PRO A CG 1 ATOM 3797 C CD . PRO A 1 509 ? 37.752 55.860 53.879 1.00 35.68 ? 502 PRO A CD 1 ATOM 3798 N N . SER A 1 510 ? 34.815 59.416 54.714 1.00 38.47 ? 503 SER A N 1 ATOM 3799 C CA . SER A 1 510 ? 34.095 60.486 54.049 1.00 41.45 ? 503 SER A CA 1 ATOM 3800 C C . SER A 1 510 ? 35.044 61.252 53.125 1.00 43.89 ? 503 SER A C 1 ATOM 3801 O O . SER A 1 510 ? 36.181 61.552 53.510 1.00 44.77 ? 503 SER A O 1 ATOM 3802 C CB . SER A 1 510 ? 33.509 61.432 55.097 1.00 40.88 ? 503 SER A CB 1 ATOM 3803 O OG . SER A 1 510 ? 33.206 62.681 54.529 1.00 43.46 ? 503 SER A OG 1 ATOM 3804 N N . PRO A 1 511 ? 34.593 61.556 51.897 1.00 45.74 ? 504 PRO A N 1 ATOM 3805 C CA . PRO A 1 511 ? 35.393 62.442 51.041 1.00 48.30 ? 504 PRO A CA 1 ATOM 3806 C C . PRO A 1 511 ? 35.432 63.906 51.536 1.00 50.10 ? 504 PRO A C 1 ATOM 3807 O O . PRO A 1 511 ? 36.411 64.620 51.278 1.00 51.34 ? 504 PRO A O 1 ATOM 3808 C CB . PRO A 1 511 ? 34.703 62.342 49.671 1.00 47.76 ? 504 PRO A CB 1 ATOM 3809 C CG . PRO A 1 511 ? 33.336 61.831 49.942 1.00 46.46 ? 504 PRO A CG 1 ATOM 3810 C CD . PRO A 1 511 ? 33.379 61.054 51.223 1.00 45.21 ? 504 PRO A CD 1 ATOM 3811 N N A GLU A 1 512 ? 34.379 64.335 52.230 0.60 50.41 ? 505 GLU A N 1 ATOM 3812 N N B GLU A 1 512 ? 34.401 64.333 52.267 0.40 50.31 ? 505 GLU A N 1 ATOM 3813 C CA A GLU A 1 512 ? 34.291 65.717 52.704 0.60 51.25 ? 505 GLU A CA 1 ATOM 3814 C CA B GLU A 1 512 ? 34.282 65.742 52.680 0.40 51.14 ? 505 GLU A CA 1 ATOM 3815 C C A GLU A 1 512 ? 35.041 65.909 54.033 0.60 52.05 ? 505 GLU A C 1 ATOM 3816 C C B GLU A 1 512 ? 34.664 66.052 54.138 0.40 51.75 ? 505 GLU A C 1 ATOM 3817 O O A GLU A 1 512 ? 35.868 66.823 54.168 0.60 52.79 ? 505 GLU A O 1 ATOM 3818 O O B GLU A 1 512 ? 34.866 67.226 54.477 0.40 52.15 ? 505 GLU A O 1 ATOM 3819 C CB A GLU A 1 512 ? 32.821 66.180 52.829 0.60 50.78 ? 505 GLU A CB 1 ATOM 3820 C CB B GLU A 1 512 ? 32.880 66.290 52.353 0.40 50.66 ? 505 GLU A CB 1 ATOM 3821 C CG A GLU A 1 512 ? 31.970 66.128 51.535 0.60 50.91 ? 505 GLU A CG 1 ATOM 3822 C CG B GLU A 1 512 ? 32.515 67.588 53.071 0.40 51.85 ? 505 GLU A CG 1 ATOM 3823 C CD A GLU A 1 512 ? 30.914 65.026 51.547 0.60 51.09 ? 505 GLU A CD 1 ATOM 3824 C CD B GLU A 1 512 ? 32.679 68.843 52.228 0.40 53.83 ? 505 GLU A CD 1 ATOM 3825 O OE1 A GLU A 1 512 ? 30.398 64.673 50.461 0.60 51.92 ? 505 GLU A OE1 1 ATOM 3826 O OE1 B GLU A 1 512 ? 31.917 69.012 51.248 0.40 53.70 ? 505 GLU A OE1 1 ATOM 3827 O OE2 A GLU A 1 512 ? 30.582 64.517 52.640 0.60 50.99 ? 505 GLU A OE2 1 ATOM 3828 O OE2 B GLU A 1 512 ? 33.548 69.679 52.571 0.40 55.40 ? 505 GLU A OE2 1 ATOM 3829 N N . PHE A 1 513 ? 34.767 65.030 54.995 1.00 51.56 ? 506 PHE A N 1 ATOM 3830 C CA . PHE A 1 513 ? 35.129 65.270 56.406 1.00 52.14 ? 506 PHE A CA 1 ATOM 3831 C C . PHE A 1 513 ? 36.083 64.261 57.034 1.00 51.68 ? 506 PHE A C 1 ATOM 3832 O O . PHE A 1 513 ? 35.842 63.048 57.013 1.00 51.01 ? 506 PHE A O 1 ATOM 3833 C CB . PHE A 1 513 ? 33.872 65.386 57.286 1.00 52.50 ? 506 PHE A CB 1 ATOM 3834 C CG . PHE A 1 513 ? 32.877 66.440 56.835 1.00 53.61 ? 506 PHE A CG 1 ATOM 3835 C CD1 . PHE A 1 513 ? 31.688 66.066 56.192 1.00 54.42 ? 506 PHE A CD1 1 ATOM 3836 C CD2 . PHE A 1 513 ? 33.111 67.799 57.084 0.85 55.31 ? 506 PHE A CD2 1 ATOM 3837 C CE1 . PHE A 1 513 ? 30.747 67.037 55.784 0.85 54.40 ? 506 PHE A CE1 1 ATOM 3838 C CE2 . PHE A 1 513 ? 32.187 68.779 56.677 0.85 56.07 ? 506 PHE A CE2 1 ATOM 3839 C CZ . PHE A 1 513 ? 31.000 68.399 56.029 0.85 55.80 ? 506 PHE A CZ 1 ATOM 3840 N N . SER A 1 514 ? 37.160 64.773 57.623 1.00 51.86 ? 507 SER A N 1 ATOM 3841 C CA . SER A 1 514 ? 38.130 63.915 58.304 0.80 50.79 ? 507 SER A CA 1 ATOM 3842 C C . SER A 1 514 ? 37.464 63.310 59.530 1.00 48.63 ? 507 SER A C 1 ATOM 3843 O O . SER A 1 514 ? 36.769 64.018 60.275 1.00 48.84 ? 507 SER A O 1 ATOM 3844 C CB . SER A 1 514 ? 39.371 64.713 58.727 0.80 52.55 ? 507 SER A CB 1 ATOM 3845 O OG . SER A 1 514 ? 40.074 65.191 57.591 0.90 54.95 ? 507 SER A OG 1 ATOM 3846 N N . GLY A 1 515 ? 37.649 62.005 59.718 1.00 45.70 ? 508 GLY A N 1 ATOM 3847 C CA . GLY A 1 515 ? 37.201 61.347 60.944 1.00 42.36 ? 508 GLY A CA 1 ATOM 3848 C C . GLY A 1 515 ? 35.746 60.911 60.908 1.00 39.33 ? 508 GLY A C 1 ATOM 3849 O O . GLY A 1 515 ? 35.202 60.476 61.933 1.00 38.73 ? 508 GLY A O 1 ATOM 3850 N N A MET A 1 516 ? 35.128 61.056 59.732 0.50 37.78 ? 509 MET A N 1 ATOM 3851 N N B MET A 1 516 ? 35.120 61.045 59.746 0.50 37.81 ? 509 MET A N 1 ATOM 3852 C CA A MET A 1 516 ? 33.742 60.633 59.460 0.50 36.05 ? 509 MET A CA 1 ATOM 3853 C CA B MET A 1 516 ? 33.769 60.535 59.543 0.50 36.14 ? 509 MET A CA 1 ATOM 3854 C C A MET A 1 516 ? 33.697 59.554 58.374 0.50 34.82 ? 509 MET A C 1 ATOM 3855 C C B MET A 1 516 ? 33.717 59.524 58.411 0.50 34.88 ? 509 MET A C 1 ATOM 3856 O O A MET A 1 516 ? 34.510 59.579 57.451 0.50 35.16 ? 509 MET A O 1 ATOM 3857 O O B MET A 1 516 ? 34.551 59.559 57.507 0.50 35.27 ? 509 MET A O 1 ATOM 3858 C CB A MET A 1 516 ? 32.909 61.811 58.956 0.50 35.62 ? 509 MET A CB 1 ATOM 3859 C CB B MET A 1 516 ? 32.795 61.664 59.255 0.50 35.71 ? 509 MET A CB 1 ATOM 3860 C CG A MET A 1 516 ? 33.099 63.098 59.751 0.50 37.60 ? 509 MET A CG 1 ATOM 3861 C CG B MET A 1 516 ? 32.569 62.538 60.458 0.50 37.86 ? 509 MET A CG 1 ATOM 3862 S SD A MET A 1 516 ? 32.307 62.989 61.356 0.50 41.03 ? 509 MET A SD 1 ATOM 3863 S SD B MET A 1 516 ? 31.539 63.929 60.040 0.50 40.30 ? 509 MET A SD 1 ATOM 3864 C CE A MET A 1 516 ? 30.604 62.842 60.841 0.50 39.38 ? 509 MET A CE 1 ATOM 3865 C CE B MET A 1 516 ? 31.648 64.894 61.557 0.50 40.38 ? 509 MET A CE 1 ATOM 3866 N N . PRO A 1 517 ? 32.731 58.620 58.461 1.00 33.21 ? 510 PRO A N 1 ATOM 3867 C CA . PRO A 1 517 ? 32.571 57.614 57.408 1.00 32.10 ? 510 PRO A CA 1 ATOM 3868 C C . PRO A 1 517 ? 31.756 58.114 56.211 1.00 30.76 ? 510 PRO A C 1 ATOM 3869 O O . PRO A 1 517 ? 30.976 59.060 56.329 1.00 30.80 ? 510 PRO A O 1 ATOM 3870 C CB . PRO A 1 517 ? 31.786 56.513 58.117 1.00 30.98 ? 510 PRO A CB 1 ATOM 3871 C CG . PRO A 1 517 ? 30.888 57.247 59.056 1.00 30.92 ? 510 PRO A CG 1 ATOM 3872 C CD . PRO A 1 517 ? 31.797 58.383 59.581 1.00 32.81 ? 510 PRO A CD 1 ATOM 3873 N N A ARG A 1 518 ? 31.938 57.457 55.071 0.50 30.27 ? 511 ARG A N 1 ATOM 3874 N N B ARG A 1 518 ? 31.935 57.470 55.066 0.50 30.44 ? 511 ARG A N 1 ATOM 3875 C CA A ARG A 1 518 ? 31.128 57.713 53.879 0.50 29.15 ? 511 ARG A CA 1 ATOM 3876 C CA B ARG A 1 518 ? 31.123 57.784 53.894 0.50 29.52 ? 511 ARG A CA 1 ATOM 3877 C C A ARG A 1 518 ? 29.688 57.240 54.086 0.50 28.24 ? 511 ARG A C 1 ATOM 3878 C C B ARG A 1 518 ? 29.703 57.252 54.059 0.50 28.45 ? 511 ARG A C 1 ATOM 3879 O O A ARG A 1 518 ? 29.465 56.104 54.500 0.50 27.30 ? 511 ARG A O 1 ATOM 3880 O O B ARG A 1 518 ? 29.508 56.091 54.416 0.50 27.53 ? 511 ARG A O 1 ATOM 3881 C CB A ARG A 1 518 ? 31.740 56.993 52.672 0.50 30.26 ? 511 ARG A CB 1 ATOM 3882 C CB B ARG A 1 518 ? 31.760 57.206 52.632 0.50 30.75 ? 511 ARG A CB 1 ATOM 3883 C CG A ARG A 1 518 ? 30.901 57.074 51.391 0.50 30.44 ? 511 ARG A CG 1 ATOM 3884 C CG B ARG A 1 518 ? 30.977 57.496 51.354 0.50 32.02 ? 511 ARG A CG 1 ATOM 3885 C CD A ARG A 1 518 ? 31.570 56.353 50.227 0.50 34.64 ? 511 ARG A CD 1 ATOM 3886 C CD B ARG A 1 518 ? 31.829 57.211 50.132 0.50 36.90 ? 511 ARG A CD 1 ATOM 3887 N NE A ARG A 1 518 ? 32.876 56.914 49.867 0.50 35.40 ? 511 ARG A NE 1 ATOM 3888 N NE B ARG A 1 518 ? 31.975 55.781 49.857 0.50 38.65 ? 511 ARG A NE 1 ATOM 3889 C CZ A ARG A 1 518 ? 33.065 57.951 49.049 0.50 37.41 ? 511 ARG A CZ 1 ATOM 3890 C CZ B ARG A 1 518 ? 31.226 55.109 48.987 0.50 39.26 ? 511 ARG A CZ 1 ATOM 3891 N NH1 A ARG A 1 518 ? 32.029 58.575 48.503 0.50 38.49 ? 511 ARG A NH1 1 ATOM 3892 N NH1 B ARG A 1 518 ? 30.277 55.732 48.310 0.50 39.93 ? 511 ARG A NH1 1 ATOM 3893 N NH2 A ARG A 1 518 ? 34.299 58.373 48.779 0.50 39.19 ? 511 ARG A NH2 1 ATOM 3894 N NH2 B ARG A 1 518 ? 31.436 53.811 48.784 0.50 40.91 ? 511 ARG A NH2 1 ATOM 3895 N N . ILE A 1 519 ? 28.723 58.126 53.824 1.00 26.98 ? 512 ILE A N 1 ATOM 3896 C CA . ILE A 1 519 ? 27.304 57.730 53.724 1.00 26.20 ? 512 ILE A CA 1 ATOM 3897 C C . ILE A 1 519 ? 26.764 58.276 52.397 1.00 26.38 ? 512 ILE A C 1 ATOM 3898 O O . ILE A 1 519 ? 26.848 59.489 52.134 1.00 27.44 ? 512 ILE A O 1 ATOM 3899 C CB . ILE A 1 519 ? 26.428 58.268 54.891 1.00 26.45 ? 512 ILE A CB 1 ATOM 3900 C CG1 . ILE A 1 519 ? 26.952 57.761 56.244 1.00 26.21 ? 512 ILE A CG1 1 ATOM 3901 C CG2 . ILE A 1 519 ? 24.917 57.897 54.662 1.00 24.24 ? 512 ILE A CG2 1 ATOM 3902 C CD1 . ILE A 1 519 ? 26.159 58.282 57.478 1.00 27.58 ? 512 ILE A CD1 1 ATOM 3903 N N . SER A 1 520 ? 26.196 57.402 51.581 1.00 25.55 ? 513 SER A N 1 ATOM 3904 C CA . SER A 1 520 ? 25.722 57.790 50.262 1.00 25.66 ? 513 SER A CA 1 ATOM 3905 C C . SER A 1 520 ? 24.271 58.204 50.272 1.00 24.35 ? 513 SER A C 1 ATOM 3906 O O . SER A 1 520 ? 23.505 57.855 51.178 1.00 23.04 ? 513 SER A O 1 ATOM 3907 C CB . SER A 1 520 ? 25.928 56.663 49.239 1.00 26.42 ? 513 SER A CB 1 ATOM 3908 O OG . SER A 1 520 ? 27.309 56.321 49.208 1.00 31.68 ? 513 SER A OG 1 ATOM 3909 N N A LYS A 1 521 ? 23.914 58.928 49.215 0.70 24.46 ? 514 LYS A N 1 ATOM 3910 N N B LYS A 1 521 ? 23.876 58.964 49.263 0.30 23.32 ? 514 LYS A N 1 ATOM 3911 C CA A LYS A 1 521 ? 22.512 59.223 48.858 0.70 23.40 ? 514 LYS A CA 1 ATOM 3912 C CA B LYS A 1 521 ? 22.461 59.262 49.077 0.30 21.54 ? 514 LYS A CA 1 ATOM 3913 C C A LYS A 1 521 ? 21.785 57.926 48.548 0.70 22.54 ? 514 LYS A C 1 ATOM 3914 C C B LYS A 1 521 ? 21.775 58.012 48.540 0.30 21.47 ? 514 LYS A C 1 ATOM 3915 O O A LYS A 1 521 ? 22.391 56.969 48.021 0.70 23.23 ? 514 LYS A O 1 ATOM 3916 O O B LYS A 1 521 ? 22.406 57.174 47.877 0.30 21.90 ? 514 LYS A O 1 ATOM 3917 C CB A LYS A 1 521 ? 22.493 60.091 47.587 0.70 23.80 ? 514 LYS A CB 1 ATOM 3918 C CB B LYS A 1 521 ? 22.297 60.407 48.090 0.30 21.19 ? 514 LYS A CB 1 ATOM 3919 C CG A LYS A 1 521 ? 23.331 61.362 47.694 0.70 26.11 ? 514 LYS A CG 1 ATOM 3920 C CG B LYS A 1 521 ? 22.790 60.069 46.693 0.30 18.54 ? 514 LYS A CG 1 ATOM 3921 C CD A LYS A 1 521 ? 23.044 62.371 46.564 0.70 29.22 ? 514 LYS A CD 1 ATOM 3922 C CD B LYS A 1 521 ? 22.557 61.255 45.757 0.30 17.39 ? 514 LYS A CD 1 ATOM 3923 C CE A LYS A 1 521 ? 23.462 61.851 45.201 0.70 29.59 ? 514 LYS A CE 1 ATOM 3924 C CE B LYS A 1 521 ? 23.448 62.447 46.121 0.30 19.77 ? 514 LYS A CE 1 ATOM 3925 N NZ A LYS A 1 521 ? 24.955 61.829 45.096 0.70 31.98 ? 514 LYS A NZ 1 ATOM 3926 N NZ B LYS A 1 521 ? 24.876 62.144 45.839 0.30 19.22 ? 514 LYS A NZ 1 ATOM 3927 N N . LEU A 1 522 ? 20.484 57.893 48.838 1.00 20.89 ? 515 LEU A N 1 ATOM 3928 C CA . LEU A 1 522 ? 19.640 56.802 48.317 1.00 21.45 ? 515 LEU A CA 1 ATOM 3929 C C . LEU A 1 522 ? 19.526 56.941 46.823 1.00 21.80 ? 515 LEU A C 1 ATOM 3930 O O . LEU A 1 522 ? 19.297 58.060 46.305 1.00 23.15 ? 515 LEU A O 1 ATOM 3931 C CB . LEU A 1 522 ? 18.247 56.816 48.954 1.00 20.81 ? 515 LEU A CB 1 ATOM 3932 C CG . LEU A 1 522 ? 18.306 56.337 50.420 1.00 20.94 ? 515 LEU A CG 1 ATOM 3933 C CD1 . LEU A 1 522 ? 17.008 56.774 51.112 1.00 22.15 ? 515 LEU A CD1 1 ATOM 3934 C CD2 . LEU A 1 522 ? 18.521 54.834 50.489 1.00 21.72 ? 515 LEU A CD2 1 ATOM 3935 N N . GLY A 1 523 ? 19.753 55.814 46.125 1.00 21.66 ? 516 GLY A N 1 ATOM 3936 C CA . GLY A 1 523 ? 19.380 55.690 44.704 1.00 21.77 ? 516 GLY A CA 1 ATOM 3937 C C . GLY A 1 523 ? 18.052 54.987 44.617 1.00 22.44 ? 516 GLY A C 1 ATOM 3938 O O . GLY A 1 523 ? 17.096 55.374 45.250 1.00 22.56 ? 516 GLY A O 1 ATOM 3939 N N . SER A 1 524 ? 17.963 53.937 43.796 1.00 20.71 ? 517 SER A N 1 ATOM 3940 C CA . SER A 1 524 ? 16.709 53.173 43.745 1.00 20.76 ? 517 SER A CA 1 ATOM 3941 C C . SER A 1 524 ? 17.049 51.765 43.289 1.00 19.35 ? 517 SER A C 1 ATOM 3942 O O . SER A 1 524 ? 18.224 51.368 43.380 1.00 20.28 ? 517 SER A O 1 ATOM 3943 C CB . SER A 1 524 ? 15.667 53.818 42.852 1.00 20.24 ? 517 SER A CB 1 ATOM 3944 O OG . SER A 1 524 ? 14.452 53.081 42.955 1.00 21.27 ? 517 SER A OG 1 ATOM 3945 N N . GLY A 1 525 ? 16.034 50.984 42.897 1.00 18.43 ? 518 GLY A N 1 ATOM 3946 C CA . GLY A 1 525 ? 16.272 49.570 42.635 1.00 18.51 ? 518 GLY A CA 1 ATOM 3947 C C . GLY A 1 525 ? 15.959 48.727 43.864 1.00 18.57 ? 518 GLY A C 1 ATOM 3948 O O . GLY A 1 525 ? 16.257 47.526 43.877 1.00 18.15 ? 518 GLY A O 1 ATOM 3949 N N . ASN A 1 526 ? 15.341 49.337 44.896 1.00 17.72 ? 519 ASN A N 1 ATOM 3950 C CA . ASN A 1 526 ? 14.936 48.563 46.058 1.00 18.40 ? 519 ASN A CA 1 ATOM 3951 C C . ASN A 1 526 ? 13.695 49.141 46.713 1.00 17.14 ? 519 ASN A C 1 ATOM 3952 O O . ASN A 1 526 ? 13.260 50.225 46.321 1.00 16.64 ? 519 ASN A O 1 ATOM 3953 C CB . ASN A 1 526 ? 16.091 48.350 47.037 1.00 19.00 ? 519 ASN A CB 1 ATOM 3954 C CG . ASN A 1 526 ? 16.153 46.909 47.488 1.00 21.86 ? 519 ASN A CG 1 ATOM 3955 O OD1 . ASN A 1 526 ? 15.191 46.412 48.106 1.00 21.08 ? 519 ASN A OD1 1 ATOM 3956 N ND2 . ASN A 1 526 ? 17.241 46.202 47.125 1.00 19.05 ? 519 ASN A ND2 1 ATOM 3957 N N . ASP A 1 527 ? 13.144 48.428 47.708 1.00 16.24 ? 520 ASP A N 1 ATOM 3958 C CA . ASP A 1 527 ? 11.765 48.665 48.153 1.00 16.49 ? 520 ASP A CA 1 ATOM 3959 C C . ASP A 1 527 ? 11.547 49.923 48.976 1.00 16.38 ? 520 ASP A C 1 ATOM 3960 O O . ASP A 1 527 ? 10.424 50.283 49.228 1.00 17.25 ? 520 ASP A O 1 ATOM 3961 C CB . ASP A 1 527 ? 11.232 47.449 48.947 1.00 15.83 ? 520 ASP A CB 1 ATOM 3962 C CG . ASP A 1 527 ? 10.942 46.253 48.049 1.00 17.14 ? 520 ASP A CG 1 ATOM 3963 O OD1 . ASP A 1 527 ? 10.138 46.452 47.088 1.00 16.34 ? 520 ASP A OD1 1 ATOM 3964 O OD2 . ASP A 1 527 ? 11.450 45.125 48.320 1.00 18.93 ? 520 ASP A OD2 1 ATOM 3965 N N . PHE A 1 528 ? 12.600 50.665 49.268 1.00 17.17 ? 521 PHE A N 1 ATOM 3966 C CA . PHE A 1 528 ? 12.414 51.998 49.843 1.00 17.09 ? 521 PHE A CA 1 ATOM 3967 C C . PHE A 1 528 ? 11.900 53.035 48.827 1.00 17.17 ? 521 PHE A C 1 ATOM 3968 O O . PHE A 1 528 ? 11.530 54.137 49.248 1.00 16.57 ? 521 PHE A O 1 ATOM 3969 C CB . PHE A 1 528 ? 13.732 52.526 50.470 1.00 18.38 ? 521 PHE A CB 1 ATOM 3970 C CG . PHE A 1 528 ? 14.862 52.627 49.480 1.00 17.44 ? 521 PHE A CG 1 ATOM 3971 C CD1 . PHE A 1 528 ? 14.966 53.747 48.611 1.00 18.00 ? 521 PHE A CD1 1 ATOM 3972 C CD2 . PHE A 1 528 ? 15.797 51.586 49.365 1.00 19.62 ? 521 PHE A CD2 1 ATOM 3973 C CE1 . PHE A 1 528 ? 16.020 53.791 47.668 1.00 17.41 ? 521 PHE A CE1 1 ATOM 3974 C CE2 . PHE A 1 528 ? 16.850 51.647 48.423 1.00 19.53 ? 521 PHE A CE2 1 ATOM 3975 C CZ . PHE A 1 528 ? 16.929 52.756 47.553 1.00 18.32 ? 521 PHE A CZ 1 ATOM 3976 N N . GLU A 1 529 ? 11.937 52.730 47.520 1.00 16.20 ? 522 GLU A N 1 ATOM 3977 C CA . GLU A 1 529 ? 11.644 53.761 46.509 1.00 16.63 ? 522 GLU A CA 1 ATOM 3978 C C . GLU A 1 529 ? 10.280 54.434 46.739 1.00 15.90 ? 522 GLU A C 1 ATOM 3979 O O . GLU A 1 529 ? 10.167 55.677 46.675 1.00 15.98 ? 522 GLU A O 1 ATOM 3980 C CB . GLU A 1 529 ? 11.682 53.147 45.091 1.00 15.82 ? 522 GLU A CB 1 ATOM 3981 C CG . GLU A 1 529 ? 11.628 54.258 43.975 1.00 16.01 ? 522 GLU A CG 1 ATOM 3982 C CD . GLU A 1 529 ? 11.454 53.633 42.580 1.00 18.46 ? 522 GLU A CD 1 ATOM 3983 O OE1 . GLU A 1 529 ? 10.484 52.916 42.368 1.00 21.48 ? 522 GLU A OE1 1 ATOM 3984 O OE2 . GLU A 1 529 ? 12.336 53.880 41.743 1.00 19.62 ? 522 GLU A OE2 1 ATOM 3985 N N . VAL A 1 530 ? 9.213 53.640 46.938 1.00 15.80 ? 523 VAL A N 1 ATOM 3986 C CA . VAL A 1 530 ? 7.885 54.259 47.071 1.00 16.41 ? 523 VAL A CA 1 ATOM 3987 C C . VAL A 1 530 ? 7.852 55.118 48.355 1.00 16.36 ? 523 VAL A C 1 ATOM 3988 O O . VAL A 1 530 ? 7.237 56.189 48.388 1.00 15.88 ? 523 VAL A O 1 ATOM 3989 C CB . VAL A 1 530 ? 6.751 53.223 47.028 1.00 16.68 ? 523 VAL A CB 1 ATOM 3990 C CG1 . VAL A 1 530 ? 6.819 52.250 48.257 1.00 16.92 ? 523 VAL A CG1 1 ATOM 3991 C CG2 . VAL A 1 530 ? 5.376 53.915 46.881 1.00 16.64 ? 523 VAL A CG2 1 ATOM 3992 N N . PHE A 1 531 ? 8.470 54.607 49.419 1.00 16.31 ? 524 PHE A N 1 ATOM 3993 C CA . PHE A 1 531 ? 8.435 55.345 50.686 1.00 16.52 ? 524 PHE A CA 1 ATOM 3994 C C . PHE A 1 531 ? 9.171 56.667 50.635 1.00 17.01 ? 524 PHE A C 1 ATOM 3995 O O . PHE A 1 531 ? 8.698 57.662 51.208 1.00 17.16 ? 524 PHE A O 1 ATOM 3996 C CB . PHE A 1 531 ? 9.012 54.462 51.799 1.00 16.49 ? 524 PHE A CB 1 ATOM 3997 C CG . PHE A 1 531 ? 8.188 53.223 51.991 1.00 16.96 ? 524 PHE A CG 1 ATOM 3998 C CD1 . PHE A 1 531 ? 6.999 53.291 52.716 1.00 18.92 ? 524 PHE A CD1 1 ATOM 3999 C CD2 . PHE A 1 531 ? 8.568 52.016 51.380 1.00 17.22 ? 524 PHE A CD2 1 ATOM 4000 C CE1 . PHE A 1 531 ? 6.179 52.148 52.854 1.00 21.05 ? 524 PHE A CE1 1 ATOM 4001 C CE2 . PHE A 1 531 ? 7.751 50.851 51.503 1.00 17.32 ? 524 PHE A CE2 1 ATOM 4002 C CZ . PHE A 1 531 ? 6.575 50.923 52.240 1.00 19.43 ? 524 PHE A CZ 1 ATOM 4003 N N . PHE A 1 532 ? 10.327 56.666 49.974 1.00 16.44 ? 525 PHE A N 1 ATOM 4004 C CA . PHE A 1 532 ? 11.224 57.833 49.991 1.00 15.97 ? 525 PHE A CA 1 ATOM 4005 C C . PHE A 1 532 ? 10.904 58.792 48.833 1.00 16.27 ? 525 PHE A C 1 ATOM 4006 O O . PHE A 1 532 ? 10.474 59.931 49.082 1.00 16.67 ? 525 PHE A O 1 ATOM 4007 C CB . PHE A 1 532 ? 12.688 57.382 49.909 1.00 16.69 ? 525 PHE A CB 1 ATOM 4008 C CG . PHE A 1 532 ? 13.658 58.491 50.149 1.00 16.49 ? 525 PHE A CG 1 ATOM 4009 C CD1 . PHE A 1 532 ? 13.599 59.212 51.359 1.00 17.80 ? 525 PHE A CD1 1 ATOM 4010 C CD2 . PHE A 1 532 ? 14.590 58.843 49.173 1.00 18.62 ? 525 PHE A CD2 1 ATOM 4011 C CE1 . PHE A 1 532 ? 14.526 60.247 51.615 1.00 18.68 ? 525 PHE A CE1 1 ATOM 4012 C CE2 . PHE A 1 532 ? 15.537 59.881 49.420 1.00 19.53 ? 525 PHE A CE2 1 ATOM 4013 C CZ . PHE A 1 532 ? 15.473 60.589 50.652 1.00 18.85 ? 525 PHE A CZ 1 ATOM 4014 N N A GLN A 1 533 ? 11.110 58.361 47.589 0.50 15.62 ? 526 GLN A N 1 ATOM 4015 N N B GLN A 1 533 ? 11.083 58.318 47.599 0.50 17.01 ? 526 GLN A N 1 ATOM 4016 C CA A GLN A 1 533 ? 10.903 59.307 46.471 0.50 14.42 ? 526 GLN A CA 1 ATOM 4017 C CA B GLN A 1 533 ? 10.891 59.154 46.398 0.50 17.26 ? 526 GLN A CA 1 ATOM 4018 C C A GLN A 1 533 ? 9.418 59.567 46.065 0.50 14.93 ? 526 GLN A C 1 ATOM 4019 C C B GLN A 1 533 ? 9.423 59.568 46.132 0.50 16.59 ? 526 GLN A C 1 ATOM 4020 O O A GLN A 1 533 ? 9.148 60.591 45.431 0.50 15.38 ? 526 GLN A O 1 ATOM 4021 O O B GLN A 1 533 ? 9.160 60.683 45.659 0.50 16.83 ? 526 GLN A O 1 ATOM 4022 C CB A GLN A 1 533 ? 11.750 58.936 45.236 0.50 14.16 ? 526 GLN A CB 1 ATOM 4023 C CB B GLN A 1 533 ? 11.420 58.397 45.169 0.50 18.49 ? 526 GLN A CB 1 ATOM 4024 C CG A GLN A 1 533 ? 13.242 58.959 45.443 0.50 13.63 ? 526 GLN A CG 1 ATOM 4025 C CG B GLN A 1 533 ? 12.697 57.635 45.434 0.50 22.18 ? 526 GLN A CG 1 ATOM 4026 C CD A GLN A 1 533 ? 13.856 57.602 45.812 0.50 11.11 ? 526 GLN A CD 1 ATOM 4027 C CD B GLN A 1 533 ? 13.877 58.545 45.414 0.50 24.44 ? 526 GLN A CD 1 ATOM 4028 O OE1 A GLN A 1 533 ? 13.189 56.726 46.372 0.50 12.04 ? 526 GLN A OE1 1 ATOM 4029 O OE1 B GLN A 1 533 ? 13.704 59.753 45.308 0.50 25.88 ? 526 GLN A OE1 1 ATOM 4030 N NE2 A GLN A 1 533 ? 15.147 57.446 45.513 0.50 15.81 ? 526 GLN A NE2 1 ATOM 4031 N NE2 B GLN A 1 533 ? 15.093 57.986 45.491 0.50 24.34 ? 526 GLN A NE2 1 ATOM 4032 N N . ARG A 1 534 ? 8.482 58.670 46.409 1.00 15.39 ? 527 ARG A N 1 ATOM 4033 C CA . ARG A 1 534 ? 7.063 58.988 46.164 1.00 15.29 ? 527 ARG A CA 1 ATOM 4034 C C . ARG A 1 534 ? 6.421 59.663 47.375 1.00 16.71 ? 527 ARG A C 1 ATOM 4035 O O . ARG A 1 534 ? 5.856 60.754 47.240 1.00 16.21 ? 527 ARG A O 1 ATOM 4036 C CB . ARG A 1 534 ? 6.226 57.788 45.691 1.00 15.41 ? 527 ARG A CB 1 ATOM 4037 C CG . ARG A 1 534 ? 4.884 58.310 45.184 1.00 15.20 ? 527 ARG A CG 1 ATOM 4038 C CD . ARG A 1 534 ? 3.792 57.230 45.016 1.00 15.59 ? 527 ARG A CD 1 ATOM 4039 N NE . ARG A 1 534 ? 4.154 56.184 44.041 1.00 15.10 ? 527 ARG A NE 1 ATOM 4040 C CZ . ARG A 1 534 ? 3.222 55.426 43.446 1.00 16.36 ? 527 ARG A CZ 1 ATOM 4041 N NH1 . ARG A 1 534 ? 1.917 55.630 43.703 1.00 16.77 ? 527 ARG A NH1 1 ATOM 4042 N NH2 . ARG A 1 534 ? 3.577 54.454 42.602 1.00 15.06 ? 527 ARG A NH2 1 ATOM 4043 N N . LEU A 1 535 ? 6.540 59.030 48.549 1.00 15.88 ? 528 LEU A N 1 ATOM 4044 C CA . LEU A 1 535 ? 5.825 59.532 49.709 1.00 15.95 ? 528 LEU A CA 1 ATOM 4045 C C . LEU A 1 535 ? 6.592 60.495 50.623 1.00 16.33 ? 528 LEU A C 1 ATOM 4046 O O . LEU A 1 535 ? 5.935 61.155 51.443 1.00 18.09 ? 528 LEU A O 1 ATOM 4047 C CB . LEU A 1 535 ? 5.301 58.349 50.548 1.00 15.32 ? 528 LEU A CB 1 ATOM 4048 C CG . LEU A 1 535 ? 4.308 57.450 49.774 1.00 16.84 ? 528 LEU A CG 1 ATOM 4049 C CD1 . LEU A 1 535 ? 3.884 56.247 50.654 1.00 18.43 ? 528 LEU A CD1 1 ATOM 4050 C CD2 . LEU A 1 535 ? 3.035 58.226 49.287 1.00 19.01 ? 528 LEU A CD2 1 ATOM 4051 N N . GLY A 1 536 ? 7.915 60.547 50.538 1.00 15.14 ? 529 GLY A N 1 ATOM 4052 C CA . GLY A 1 536 ? 8.684 61.498 51.364 1.00 15.74 ? 529 GLY A CA 1 ATOM 4053 C C . GLY A 1 536 ? 8.800 61.081 52.813 1.00 15.52 ? 529 GLY A C 1 ATOM 4054 O O . GLY A 1 536 ? 8.780 61.947 53.703 1.00 15.79 ? 529 GLY A O 1 ATOM 4055 N N . ILE A 1 537 ? 8.979 59.779 53.019 1.00 15.77 ? 530 ILE A N 1 ATOM 4056 C CA . ILE A 1 537 ? 9.225 59.254 54.376 1.00 15.79 ? 530 ILE A CA 1 ATOM 4057 C C . ILE A 1 537 ? 10.726 59.001 54.501 1.00 16.15 ? 530 ILE A C 1 ATOM 4058 O O . ILE A 1 537 ? 11.347 58.340 53.641 1.00 16.81 ? 530 ILE A O 1 ATOM 4059 C CB . ILE A 1 537 ? 8.396 57.948 54.604 1.00 15.59 ? 530 ILE A CB 1 ATOM 4060 C CG1 . ILE A 1 537 ? 6.885 58.261 54.587 1.00 16.44 ? 530 ILE A CG1 1 ATOM 4061 C CG2 . ILE A 1 537 ? 8.833 57.248 55.940 1.00 17.55 ? 530 ILE A CG2 1 ATOM 4062 C CD1 . ILE A 1 537 ? 6.061 57.001 54.345 1.00 18.43 ? 530 ILE A CD1 1 ATOM 4063 N N . ALA A 1 538 ? 11.330 59.541 55.576 1.00 16.54 ? 531 ALA A N 1 ATOM 4064 C CA . ALA A 1 538 ? 12.783 59.378 55.846 1.00 16.45 ? 531 ALA A CA 1 ATOM 4065 C C . ALA A 1 538 ? 13.171 57.901 55.746 1.00 17.71 ? 531 ALA A C 1 ATOM 4066 O O . ALA A 1 538 ? 12.538 57.052 56.395 1.00 18.17 ? 531 ALA A O 1 ATOM 4067 C CB . ALA A 1 538 ? 13.037 59.899 57.270 1.00 17.60 ? 531 ALA A CB 1 ATOM 4068 N N . SER A 1 539 ? 14.152 57.582 54.897 1.00 16.15 ? 532 SER A N 1 ATOM 4069 C CA . SER A 1 539 ? 14.485 56.173 54.617 1.00 17.35 ? 532 SER A CA 1 ATOM 4070 C C . SER A 1 539 ? 15.992 55.935 54.757 1.00 17.70 ? 532 SER A C 1 ATOM 4071 O O . SER A 1 539 ? 16.818 56.855 54.551 1.00 17.83 ? 532 SER A O 1 ATOM 4072 C CB . SER A 1 539 ? 14.006 55.779 53.197 1.00 17.64 ? 532 SER A CB 1 ATOM 4073 O OG . SER A 1 539 ? 12.573 55.823 53.128 1.00 17.53 ? 532 SER A OG 1 ATOM 4074 N N . GLY A 1 540 ? 16.352 54.696 55.075 1.00 17.76 ? 533 GLY A N 1 ATOM 4075 C CA . GLY A 1 540 ? 17.776 54.314 55.076 1.00 18.77 ? 533 GLY A CA 1 ATOM 4076 C C . GLY A 1 540 ? 17.968 52.829 54.824 1.00 19.38 ? 533 GLY A C 1 ATOM 4077 O O . GLY A 1 540 ? 17.005 52.040 54.852 1.00 19.31 ? 533 GLY A O 1 ATOM 4078 N N . ARG A 1 541 ? 19.224 52.464 54.612 1.00 19.53 ? 534 ARG A N 1 ATOM 4079 C CA . ARG A 1 541 ? 19.594 51.065 54.385 1.00 19.44 ? 534 ARG A CA 1 ATOM 4080 C C . ARG A 1 541 ? 21.067 50.900 54.786 1.00 19.94 ? 534 ARG A C 1 ATOM 4081 O O . ARG A 1 541 ? 21.843 51.863 54.794 1.00 20.29 ? 534 ARG A O 1 ATOM 4082 C CB . ARG A 1 541 ? 19.410 50.695 52.905 1.00 19.72 ? 534 ARG A CB 1 ATOM 4083 C CG . ARG A 1 541 ? 20.419 51.422 51.979 1.00 21.64 ? 534 ARG A CG 1 ATOM 4084 C CD . ARG A 1 541 ? 20.085 51.314 50.501 1.00 25.61 ? 534 ARG A CD 1 ATOM 4085 N NE . ARG A 1 541 ? 19.978 49.913 50.066 1.00 27.68 ? 534 ARG A NE 1 ATOM 4086 C CZ . ARG A 1 541 ? 19.970 49.518 48.794 1.00 27.90 ? 534 ARG A CZ 1 ATOM 4087 N NH1 . ARG A 1 541 ? 19.801 48.233 48.505 1.00 26.00 ? 534 ARG A NH1 1 ATOM 4088 N NH2 . ARG A 1 541 ? 20.060 50.411 47.804 1.00 27.55 ? 534 ARG A NH2 1 ATOM 4089 N N . ALA A 1 542 ? 21.416 49.669 55.144 1.00 20.13 ? 535 ALA A N 1 ATOM 4090 C CA . ALA A 1 542 ? 22.782 49.331 55.575 1.00 20.97 ? 535 ALA A CA 1 ATOM 4091 C C . ALA A 1 542 ? 23.071 47.886 55.252 1.00 21.36 ? 535 ALA A C 1 ATOM 4092 O O . ALA A 1 542 ? 22.195 47.020 55.388 1.00 21.15 ? 535 ALA A O 1 ATOM 4093 C CB . ALA A 1 542 ? 22.953 49.562 57.090 1.00 21.27 ? 535 ALA A CB 1 ATOM 4094 N N A ARG A 1 543 ? 24.310 47.622 54.850 0.50 21.38 ? 536 ARG A N 1 ATOM 4095 N N B ARG A 1 543 ? 24.300 47.630 54.803 0.50 21.39 ? 536 ARG A N 1 ATOM 4096 C CA A ARG A 1 543 ? 24.751 46.248 54.578 0.50 21.68 ? 536 ARG A CA 1 ATOM 4097 C CA B ARG A 1 543 ? 24.749 46.263 54.479 0.50 21.73 ? 536 ARG A CA 1 ATOM 4098 C C A ARG A 1 543 ? 26.259 46.202 54.705 0.50 22.28 ? 536 ARG A C 1 ATOM 4099 C C B ARG A 1 543 ? 26.269 46.201 54.512 0.50 22.25 ? 536 ARG A C 1 ATOM 4100 O O A ARG A 1 543 ? 26.906 47.244 54.860 0.50 21.99 ? 536 ARG A O 1 ATOM 4101 O O B ARG A 1 543 ? 26.944 47.236 54.426 0.50 22.07 ? 536 ARG A O 1 ATOM 4102 C CB A ARG A 1 543 ? 24.320 45.811 53.164 0.50 21.55 ? 536 ARG A CB 1 ATOM 4103 C CB B ARG A 1 543 ? 24.221 45.821 53.095 0.50 21.56 ? 536 ARG A CB 1 ATOM 4104 C CG A ARG A 1 543 ? 25.091 46.488 52.034 0.50 21.57 ? 536 ARG A CG 1 ATOM 4105 C CG B ARG A 1 543 ? 24.575 46.755 51.935 0.50 21.06 ? 536 ARG A CG 1 ATOM 4106 C CD A ARG A 1 543 ? 24.717 45.887 50.709 0.50 21.08 ? 536 ARG A CD 1 ATOM 4107 C CD B ARG A 1 543 ? 23.589 47.898 51.843 0.50 24.82 ? 536 ARG A CD 1 ATOM 4108 N NE A ARG A 1 543 ? 23.270 45.682 50.667 0.50 22.84 ? 536 ARG A NE 1 ATOM 4109 N NE B ARG A 1 543 ? 23.570 48.590 50.547 0.50 23.63 ? 536 ARG A NE 1 ATOM 4110 C CZ A ARG A 1 543 ? 22.547 45.693 49.565 0.50 23.11 ? 536 ARG A CZ 1 ATOM 4111 C CZ B ARG A 1 543 ? 23.717 49.902 50.411 0.50 22.60 ? 536 ARG A CZ 1 ATOM 4112 N NH1 A ARG A 1 543 ? 23.131 45.930 48.391 0.50 21.67 ? 536 ARG A NH1 1 ATOM 4113 N NH1 B ARG A 1 543 ? 23.654 50.460 49.215 0.50 20.81 ? 536 ARG A NH1 1 ATOM 4114 N NH2 A ARG A 1 543 ? 21.238 45.474 49.652 0.50 20.37 ? 536 ARG A NH2 1 ATOM 4115 N NH2 B ARG A 1 543 ? 23.938 50.648 51.485 0.50 20.91 ? 536 ARG A NH2 1 ATOM 4116 N N . TYR A 1 544 ? 26.811 44.991 54.656 1.00 22.46 ? 537 TYR A N 1 ATOM 4117 C CA . TYR A 1 544 ? 28.246 44.805 54.552 1.00 24.32 ? 537 TYR A CA 1 ATOM 4118 C C . TYR A 1 544 ? 28.636 44.721 53.077 1.00 25.25 ? 537 TYR A C 1 ATOM 4119 O O . TYR A 1 544 ? 27.868 44.242 52.241 1.00 24.67 ? 537 TYR A O 1 ATOM 4120 C CB . TYR A 1 544 ? 28.751 43.604 55.383 1.00 24.07 ? 537 TYR A CB 1 ATOM 4121 C CG . TYR A 1 544 ? 29.671 44.081 56.483 1.00 25.21 ? 537 TYR A CG 1 ATOM 4122 C CD1 . TYR A 1 544 ? 29.179 44.866 57.527 1.00 26.02 ? 537 TYR A CD1 1 ATOM 4123 C CD2 . TYR A 1 544 ? 31.047 43.809 56.445 1.00 25.24 ? 537 TYR A CD2 1 ATOM 4124 C CE1 . TYR A 1 544 ? 30.022 45.350 58.533 1.00 26.51 ? 537 TYR A CE1 1 ATOM 4125 C CE2 . TYR A 1 544 ? 31.911 44.288 57.466 1.00 25.51 ? 537 TYR A CE2 1 ATOM 4126 C CZ . TYR A 1 544 ? 31.368 45.070 58.497 1.00 26.69 ? 537 TYR A CZ 1 ATOM 4127 O OH . TYR A 1 544 ? 32.167 45.571 59.500 1.00 28.22 ? 537 TYR A OH 1 ATOM 4128 N N . THR A 1 545 ? 29.813 45.243 52.767 1.00 25.43 ? 538 THR A N 1 ATOM 4129 C CA . THR A 1 545 ? 30.216 45.373 51.373 1.00 26.36 ? 538 THR A CA 1 ATOM 4130 C C . THR A 1 545 ? 31.691 44.980 51.218 1.00 28.21 ? 538 THR A C 1 ATOM 4131 O O . THR A 1 545 ? 32.373 44.744 52.205 1.00 27.03 ? 538 THR A O 1 ATOM 4132 C CB . THR A 1 545 ? 29.972 46.816 50.860 1.00 26.22 ? 538 THR A CB 1 ATOM 4133 O OG1 . THR A 1 545 ? 30.101 46.846 49.435 1.00 27.61 ? 538 THR A OG1 1 ATOM 4134 C CG2 . THR A 1 545 ? 30.975 47.809 51.495 1.00 25.54 ? 538 THR A CG2 1 ATOM 4135 N N . LYS A 1 546 ? 32.137 44.878 49.967 1.00 30.02 ? 539 LYS A N 1 ATOM 4136 C CA . LYS A 1 546 ? 33.540 44.602 49.615 1.00 34.03 ? 539 LYS A CA 1 ATOM 4137 C C . LYS A 1 546 ? 34.365 45.900 49.624 1.00 35.40 ? 539 LYS A C 1 ATOM 4138 O O . LYS A 1 546 ? 33.821 46.988 49.804 1.00 35.61 ? 539 LYS A O 1 ATOM 4139 C CB . LYS A 1 546 ? 33.585 43.968 48.203 1.00 33.48 ? 539 LYS A CB 1 ATOM 4140 C CG . LYS A 1 546 ? 33.188 44.993 47.153 1.00 36.91 ? 539 LYS A CG 1 ATOM 4141 C CD . LYS A 1 546 ? 33.020 44.432 45.761 1.00 44.25 ? 539 LYS A CD 1 ATOM 4142 C CE . LYS A 1 546 ? 32.059 45.346 45.014 1.00 45.22 ? 539 LYS A CE 1 ATOM 4143 N NZ . LYS A 1 546 ? 32.553 45.616 43.657 1.00 51.00 ? 539 LYS A NZ 1 ATOM 4144 N N . ASN A 1 547 ? 35.679 45.768 49.421 1.00 39.50 ? 540 ASN A N 1 ATOM 4145 C CA . ASN A 1 547 ? 36.554 46.924 49.206 1.00 42.83 ? 540 ASN A CA 1 ATOM 4146 C C . ASN A 1 547 ? 36.393 47.495 47.795 1.00 44.67 ? 540 ASN A C 1 ATOM 4147 O O . ASN A 1 547 ? 36.904 46.929 46.828 1.00 45.93 ? 540 ASN A O 1 ATOM 4148 C CB . ASN A 1 547 ? 38.020 46.542 49.475 1.00 43.54 ? 540 ASN A CB 1 ATOM 4149 C CG . ASN A 1 547 ? 38.949 47.764 49.533 1.00 44.85 ? 540 ASN A CG 1 ATOM 4150 O OD1 . ASN A 1 547 ? 38.576 48.881 49.134 1.00 46.67 ? 540 ASN A OD1 1 ATOM 4151 N ND2 . ASN A 1 547 ? 40.156 47.555 50.053 1.00 45.07 ? 540 ASN A ND2 1 ATOM 4152 N N . TRP A 1 548 ? 35.693 48.624 47.715 1.00 47.34 ? 541 TRP A N 1 ATOM 4153 C CA . TRP A 1 548 ? 35.346 49.350 46.486 1.00 50.02 ? 541 TRP A CA 1 ATOM 4154 C C . TRP A 1 548 ? 36.540 50.175 45.964 0.40 52.74 ? 541 TRP A C 1 ATOM 4155 O O . TRP A 1 548 ? 36.380 51.304 45.491 0.40 52.72 ? 541 TRP A O 1 ATOM 4156 C CB . TRP A 1 548 ? 34.140 50.248 46.823 1.00 49.78 ? 541 TRP A CB 1 ATOM 4157 C CG . TRP A 1 548 ? 33.685 51.270 45.814 0.40 50.32 ? 541 TRP A CG 1 ATOM 4158 C CD1 . TRP A 1 548 ? 33.817 52.630 45.908 0.40 51.17 ? 541 TRP A CD1 1 ATOM 4159 C CD2 . TRP A 1 548 ? 32.963 51.023 44.600 0.40 50.21 ? 541 TRP A CD2 1 ATOM 4160 N NE1 . TRP A 1 548 ? 33.245 53.240 44.817 0.40 51.03 ? 541 TRP A NE1 1 ATOM 4161 C CE2 . TRP A 1 548 ? 32.716 52.275 43.999 0.40 50.32 ? 541 TRP A CE2 1 ATOM 4162 C CE3 . TRP A 1 548 ? 32.521 49.865 43.952 0.40 49.70 ? 541 TRP A CE3 1 ATOM 4163 C CZ2 . TRP A 1 548 ? 32.048 52.399 42.785 0.40 50.08 ? 541 TRP A CZ2 1 ATOM 4164 C CZ3 . TRP A 1 548 ? 31.858 49.992 42.752 0.40 50.10 ? 541 TRP A CZ3 1 ATOM 4165 C CH2 . TRP A 1 548 ? 31.626 51.249 42.179 0.40 50.34 ? 541 TRP A CH2 1 ATOM 4166 N N . GLU A 1 549 ? 37.734 49.587 46.062 1.00 56.03 ? 542 GLU A N 1 ATOM 4167 C CA . GLU A 1 549 ? 38.988 50.219 45.638 1.00 59.35 ? 542 GLU A CA 1 ATOM 4168 C C . GLU A 1 549 ? 39.888 49.183 44.987 1.00 60.70 ? 542 GLU A C 1 ATOM 4169 O O . GLU A 1 549 ? 40.477 49.433 43.929 1.00 61.59 ? 542 GLU A O 1 ATOM 4170 C CB . GLU A 1 549 ? 39.743 50.835 46.822 1.00 60.34 ? 542 GLU A CB 1 ATOM 4171 C CG . GLU A 1 549 ? 39.093 52.060 47.445 1.00 63.54 ? 542 GLU A CG 1 ATOM 4172 C CD . GLU A 1 549 ? 40.116 53.056 47.974 1.00 69.32 ? 542 GLU A CD 1 ATOM 4173 O OE1 . GLU A 1 549 ? 41.067 52.639 48.686 1.00 72.24 ? 542 GLU A OE1 1 ATOM 4174 O OE2 . GLU A 1 549 ? 39.969 54.264 47.669 1.00 71.42 ? 542 GLU A OE2 1 ATOM 4175 N N . THR A 1 550 ? 39.989 48.024 45.638 1.00 61.53 ? 543 THR A N 1 ATOM 4176 C CA . THR A 1 550 ? 40.840 46.924 45.190 1.00 62.84 ? 543 THR A CA 1 ATOM 4177 C C . THR A 1 550 ? 40.037 45.897 44.390 1.00 62.85 ? 543 THR A C 1 ATOM 4178 O O . THR A 1 550 ? 40.563 44.848 43.983 1.00 63.29 ? 543 THR A O 1 ATOM 4179 C CB . THR A 1 550 ? 41.506 46.217 46.393 1.00 63.52 ? 543 THR A CB 1 ATOM 4180 O OG1 . THR A 1 550 ? 40.491 45.753 47.293 1.00 62.99 ? 543 THR A OG1 1 ATOM 4181 C CG2 . THR A 1 550 ? 42.450 47.173 47.134 1.00 64.23 ? 543 THR A CG2 1 ATOM 4182 N N . ASN A 1 551 ? 38.760 46.210 44.181 1.00 62.52 ? 544 ASN A N 1 ATOM 4183 C CA . ASN A 1 551 ? 37.820 45.340 43.474 1.00 62.25 ? 544 ASN A CA 1 ATOM 4184 C C . ASN A 1 551 ? 37.009 46.149 42.466 1.00 61.38 ? 544 ASN A C 1 ATOM 4185 O O . ASN A 1 551 ? 36.043 46.846 42.833 1.00 61.30 ? 544 ASN A O 1 ATOM 4186 C CB . ASN A 1 551 ? 36.890 44.613 44.462 1.00 61.90 ? 544 ASN A CB 1 ATOM 4187 C CG . ASN A 1 551 ? 37.616 43.527 45.271 0.80 63.93 ? 544 ASN A CG 1 ATOM 4188 O OD1 . ASN A 1 551 ? 38.285 42.639 44.711 0.80 64.85 ? 544 ASN A OD1 1 ATOM 4189 N ND2 . ASN A 1 551 ? 37.468 43.586 46.594 0.80 64.55 ? 544 ASN A ND2 1 ATOM 4190 N N . LYS A 1 552 ? 37.415 46.049 41.199 1.00 60.70 ? 545 LYS A N 1 ATOM 4191 C CA . LYS A 1 552 ? 36.839 46.838 40.108 1.00 59.34 ? 545 LYS A CA 1 ATOM 4192 C C . LYS A 1 552 ? 35.638 46.167 39.413 0.50 57.88 ? 545 LYS A C 1 ATOM 4193 O O . LYS A 1 552 ? 35.322 46.499 38.266 0.50 57.76 ? 545 LYS A O 1 ATOM 4194 C CB . LYS A 1 552 ? 37.934 47.168 39.083 0.50 60.17 ? 545 LYS A CB 1 ATOM 4195 C CG . LYS A 1 552 ? 39.165 47.843 39.689 0.50 60.99 ? 545 LYS A CG 1 ATOM 4196 C CD . LYS A 1 552 ? 40.383 47.741 38.778 0.50 61.99 ? 545 LYS A CD 1 ATOM 4197 C CE . LYS A 1 552 ? 40.232 48.605 37.537 0.50 61.95 ? 545 LYS A CE 1 ATOM 4198 N NZ . LYS A 1 552 ? 41.464 48.562 36.700 0.50 62.50 ? 545 LYS A NZ 1 ATOM 4199 N N . PHE A 1 553 ? 34.966 45.246 40.110 0.80 56.36 ? 546 PHE A N 1 ATOM 4200 C CA . PHE A 1 553 ? 33.844 44.483 39.528 1.00 54.37 ? 546 PHE A CA 1 ATOM 4201 C C . PHE A 1 553 ? 32.385 44.918 39.893 0.80 52.72 ? 546 PHE A C 1 ATOM 4202 O O . PHE A 1 553 ? 31.445 44.596 39.144 0.80 52.27 ? 546 PHE A O 1 ATOM 4203 C CB . PHE A 1 553 ? 34.066 42.963 39.681 1.00 54.70 ? 546 PHE A CB 1 ATOM 4204 C CG . PHE A 1 553 ? 34.189 42.492 41.099 1.00 55.19 ? 546 PHE A CG 1 ATOM 4205 C CD1 . PHE A 1 553 ? 35.446 42.240 41.655 0.80 56.79 ? 546 PHE A CD1 1 ATOM 4206 C CD2 . PHE A 1 553 ? 33.052 42.284 41.882 1.00 55.06 ? 546 PHE A CD2 1 ATOM 4207 C CE1 . PHE A 1 553 ? 35.574 41.799 42.981 0.80 56.64 ? 546 PHE A CE1 1 ATOM 4208 C CE2 . PHE A 1 553 ? 33.160 41.848 43.216 1.00 55.17 ? 546 PHE A CE2 1 ATOM 4209 C CZ . PHE A 1 553 ? 34.428 41.605 43.764 0.80 55.80 ? 546 PHE A CZ 1 ATOM 4210 N N . SER A 1 554 ? 32.190 45.649 40.999 0.80 50.97 ? 547 SER A N 1 ATOM 4211 C CA . SER A 1 554 ? 30.816 46.123 41.447 0.80 48.80 ? 547 SER A CA 1 ATOM 4212 C C . SER A 1 554 ? 29.657 45.077 41.664 0.80 45.76 ? 547 SER A C 1 ATOM 4213 O O . SER A 1 554 ? 29.408 44.195 40.832 0.80 46.20 ? 547 SER A O 1 ATOM 4214 C CB . SER A 1 554 ? 30.320 47.286 40.578 1.00 49.87 ? 547 SER A CB 1 ATOM 4215 O OG . SER A 1 554 ? 29.479 48.196 41.307 1.00 52.52 ? 547 SER A OG 1 ATOM 4216 N N . GLY A 1 555 ? 28.933 45.233 42.778 1.00 42.57 ? 548 GLY A N 1 ATOM 4217 C CA . GLY A 1 555 ? 27.967 44.236 43.284 1.00 37.42 ? 548 GLY A CA 1 ATOM 4218 C C . GLY A 1 555 ? 28.747 43.005 43.757 1.00 34.64 ? 548 GLY A C 1 ATOM 4219 O O . GLY A 1 555 ? 29.916 43.122 44.117 1.00 34.85 ? 548 GLY A O 1 ATOM 4220 N N . TYR A 1 556 ? 28.127 41.823 43.736 1.00 29.71 ? 549 TYR A N 1 ATOM 4221 C CA . TYR A 1 556 ? 28.875 40.571 43.941 1.00 27.26 ? 549 TYR A CA 1 ATOM 4222 C C . TYR A 1 556 ? 28.723 39.723 42.654 1.00 25.88 ? 549 TYR A C 1 ATOM 4223 O O . TYR A 1 556 ? 27.682 39.815 41.988 1.00 24.83 ? 549 TYR A O 1 ATOM 4224 C CB . TYR A 1 556 ? 28.384 39.821 45.196 1.00 27.01 ? 549 TYR A CB 1 ATOM 4225 C CG . TYR A 1 556 ? 26.892 39.578 45.197 1.00 25.32 ? 549 TYR A CG 1 ATOM 4226 C CD1 . TYR A 1 556 ? 26.379 38.334 44.854 1.00 24.86 ? 549 TYR A CD1 1 ATOM 4227 C CD2 . TYR A 1 556 ? 25.993 40.621 45.509 1.00 23.42 ? 549 TYR A CD2 1 ATOM 4228 C CE1 . TYR A 1 556 ? 24.988 38.124 44.845 1.00 21.42 ? 549 TYR A CE1 1 ATOM 4229 C CE2 . TYR A 1 556 ? 24.656 40.410 45.506 1.00 22.39 ? 549 TYR A CE2 1 ATOM 4230 C CZ . TYR A 1 556 ? 24.153 39.180 45.172 1.00 22.36 ? 549 TYR A CZ 1 ATOM 4231 O OH . TYR A 1 556 ? 22.793 38.989 45.139 1.00 22.17 ? 549 TYR A OH 1 ATOM 4232 N N . PRO A 1 557 ? 29.733 38.906 42.313 1.00 24.52 ? 550 PRO A N 1 ATOM 4233 C CA . PRO A 1 557 ? 29.687 38.251 40.988 1.00 23.98 ? 550 PRO A CA 1 ATOM 4234 C C . PRO A 1 557 ? 28.502 37.341 40.718 1.00 23.22 ? 550 PRO A C 1 ATOM 4235 O O . PRO A 1 557 ? 28.082 37.233 39.563 1.00 23.60 ? 550 PRO A O 1 ATOM 4236 C CB . PRO A 1 557 ? 30.987 37.421 40.944 1.00 24.52 ? 550 PRO A CB 1 ATOM 4237 C CG . PRO A 1 557 ? 31.963 38.279 41.791 1.00 24.71 ? 550 PRO A CG 1 ATOM 4238 C CD . PRO A 1 557 ? 31.063 38.732 42.964 1.00 24.92 ? 550 PRO A CD 1 ATOM 4239 N N . LEU A 1 558 ? 27.974 36.691 41.750 1.00 21.57 ? 551 LEU A N 1 ATOM 4240 C CA . LEU A 1 558 ? 26.927 35.665 41.527 1.00 21.24 ? 551 LEU A CA 1 ATOM 4241 C C . LEU A 1 558 ? 25.507 36.205 41.608 1.00 21.30 ? 551 LEU A C 1 ATOM 4242 O O . LEU A 1 558 ? 24.542 35.436 41.619 1.00 22.13 ? 551 LEU A O 1 ATOM 4243 C CB . LEU A 1 558 ? 27.093 34.498 42.498 1.00 20.73 ? 551 LEU A CB 1 ATOM 4244 C CG . LEU A 1 558 ? 28.415 33.788 42.201 1.00 21.92 ? 551 LEU A CG 1 ATOM 4245 C CD1 . LEU A 1 558 ? 28.714 32.755 43.267 1.00 23.96 ? 551 LEU A CD1 1 ATOM 4246 C CD2 . LEU A 1 558 ? 28.390 33.131 40.817 1.00 21.97 ? 551 LEU A CD2 1 ATOM 4247 N N . TYR A 1 559 ? 25.404 37.525 41.671 1.00 20.87 ? 552 TYR A N 1 ATOM 4248 C CA . TYR A 1 559 ? 24.112 38.224 41.651 1.00 20.70 ? 552 TYR A CA 1 ATOM 4249 C C . TYR A 1 559 ? 23.091 37.690 40.646 1.00 19.96 ? 552 TYR A C 1 ATOM 4250 O O . TYR A 1 559 ? 23.355 37.656 39.453 1.00 21.06 ? 552 TYR A O 1 ATOM 4251 C CB . TYR A 1 559 ? 24.438 39.683 41.425 1.00 20.29 ? 552 TYR A CB 1 ATOM 4252 C CG . TYR A 1 559 ? 23.290 40.639 41.181 1.00 21.19 ? 552 TYR A CG 1 ATOM 4253 C CD1 . TYR A 1 559 ? 22.351 40.907 42.174 1.00 21.49 ? 552 TYR A CD1 1 ATOM 4254 C CD2 . TYR A 1 559 ? 23.189 41.304 39.955 1.00 22.10 ? 552 TYR A CD2 1 ATOM 4255 C CE1 . TYR A 1 559 ? 21.291 41.834 41.947 1.00 19.71 ? 552 TYR A CE1 1 ATOM 4256 C CE2 . TYR A 1 559 ? 22.166 42.243 39.735 1.00 20.11 ? 552 TYR A CE2 1 ATOM 4257 C CZ . TYR A 1 559 ? 21.233 42.480 40.722 1.00 18.53 ? 552 TYR A CZ 1 ATOM 4258 O OH . TYR A 1 559 ? 20.222 43.391 40.458 1.00 19.73 ? 552 TYR A OH 1 ATOM 4259 N N . HIS A 1 560 ? 21.922 37.270 41.137 1.00 19.42 ? 553 HIS A N 1 ATOM 4260 C CA . HIS A 1 560 ? 20.775 36.849 40.293 1.00 19.04 ? 553 HIS A CA 1 ATOM 4261 C C . HIS A 1 560 ? 21.027 35.600 39.458 1.00 19.67 ? 553 HIS A C 1 ATOM 4262 O O . HIS A 1 560 ? 20.324 35.334 38.479 1.00 19.87 ? 553 HIS A O 1 ATOM 4263 C CB . HIS A 1 560 ? 20.274 38.005 39.416 1.00 18.79 ? 553 HIS A CB 1 ATOM 4264 C CG . HIS A 1 560 ? 19.502 39.073 40.168 1.00 18.75 ? 553 HIS A CG 1 ATOM 4265 N ND1 . HIS A 1 560 ? 18.873 40.106 39.513 1.00 17.25 ? 553 HIS A ND1 1 ATOM 4266 C CD2 . HIS A 1 560 ? 19.261 39.267 41.488 1.00 19.77 ? 553 HIS A CD2 1 ATOM 4267 C CE1 . HIS A 1 560 ? 18.241 40.878 40.393 1.00 18.33 ? 553 HIS A CE1 1 ATOM 4268 N NE2 . HIS A 1 560 ? 18.442 40.375 41.599 1.00 17.57 ? 553 HIS A NE2 1 ATOM 4269 N N . SER A 1 561 ? 22.023 34.843 39.886 1.00 20.68 ? 554 SER A N 1 ATOM 4270 C CA . SER A 1 561 ? 22.356 33.554 39.275 1.00 19.72 ? 554 SER A CA 1 ATOM 4271 C C . SER A 1 561 ? 21.895 32.368 40.166 1.00 23.08 ? 554 SER A C 1 ATOM 4272 O O . SER A 1 561 ? 21.619 32.537 41.321 1.00 21.78 ? 554 SER A O 1 ATOM 4273 C CB . SER A 1 561 ? 23.881 33.457 39.046 1.00 19.86 ? 554 SER A CB 1 ATOM 4274 O OG A SER A 1 561 ? 24.603 33.180 40.231 0.50 21.47 ? 554 SER A OG 1 ATOM 4275 O OG B SER A 1 561 ? 24.299 32.113 38.836 0.50 20.56 ? 554 SER A OG 1 ATOM 4276 N N . VAL A 1 562 ? 21.788 31.194 39.543 1.00 20.80 ? 555 VAL A N 1 ATOM 4277 C CA . VAL A 1 562 ? 21.441 29.973 40.291 1.00 22.15 ? 555 VAL A CA 1 ATOM 4278 C C . VAL A 1 562 ? 22.492 29.701 41.410 1.00 22.47 ? 555 VAL A C 1 ATOM 4279 O O . VAL A 1 562 ? 22.211 28.956 42.374 1.00 23.86 ? 555 VAL A O 1 ATOM 4280 C CB . VAL A 1 562 ? 21.354 28.765 39.335 1.00 21.59 ? 555 VAL A CB 1 ATOM 4281 C CG1 . VAL A 1 562 ? 22.782 28.324 38.831 1.00 22.16 ? 555 VAL A CG1 1 ATOM 4282 C CG2 . VAL A 1 562 ? 20.654 27.580 39.990 1.00 22.63 ? 555 VAL A CG2 1 ATOM 4283 N N . TYR A 1 563 ? 23.686 30.285 41.290 1.00 21.76 ? 556 TYR A N 1 ATOM 4284 C CA . TYR A 1 563 ? 24.799 29.938 42.205 1.00 23.41 ? 556 TYR A CA 1 ATOM 4285 C C . TYR A 1 563 ? 24.713 30.686 43.522 1.00 24.16 ? 556 TYR A C 1 ATOM 4286 O O . TYR A 1 563 ? 25.487 30.400 44.444 1.00 24.11 ? 556 TYR A O 1 ATOM 4287 C CB . TYR A 1 563 ? 26.183 30.138 41.523 1.00 22.87 ? 556 TYR A CB 1 ATOM 4288 C CG . TYR A 1 563 ? 26.265 29.338 40.256 1.00 23.55 ? 556 TYR A CG 1 ATOM 4289 C CD1 . TYR A 1 563 ? 26.213 27.932 40.291 1.00 24.81 ? 556 TYR A CD1 1 ATOM 4290 C CD2 . TYR A 1 563 ? 26.378 29.962 39.022 1.00 23.82 ? 556 TYR A CD2 1 ATOM 4291 C CE1 . TYR A 1 563 ? 26.245 27.186 39.126 1.00 24.71 ? 556 TYR A CE1 1 ATOM 4292 C CE2 . TYR A 1 563 ? 26.434 29.199 37.830 1.00 24.37 ? 556 TYR A CE2 1 ATOM 4293 C CZ . TYR A 1 563 ? 26.370 27.832 37.898 1.00 25.80 ? 556 TYR A CZ 1 ATOM 4294 O OH . TYR A 1 563 ? 26.379 27.080 36.730 1.00 27.15 ? 556 TYR A OH 1 ATOM 4295 N N . GLU A 1 564 ? 23.771 31.641 43.618 1.00 23.19 ? 557 GLU A N 1 ATOM 4296 C CA . GLU A 1 564 ? 23.575 32.399 44.844 1.00 24.47 ? 557 GLU A CA 1 ATOM 4297 C C . GLU A 1 564 ? 22.827 31.509 45.832 1.00 23.79 ? 557 GLU A C 1 ATOM 4298 O O . GLU A 1 564 ? 21.609 31.468 45.827 1.00 24.08 ? 557 GLU A O 1 ATOM 4299 C CB . GLU A 1 564 ? 22.707 33.624 44.498 1.00 25.68 ? 557 GLU A CB 1 ATOM 4300 C CG . GLU A 1 564 ? 23.275 34.861 44.828 1.00 30.63 ? 557 GLU A CG 1 ATOM 4301 C CD . GLU A 1 564 ? 22.162 35.885 44.951 1.00 24.34 ? 557 GLU A CD 1 ATOM 4302 O OE1 . GLU A 1 564 ? 21.900 36.646 43.987 1.00 26.12 ? 557 GLU A OE1 1 ATOM 4303 O OE2 . GLU A 1 564 ? 21.489 35.806 45.968 1.00 23.41 ? 557 GLU A OE2 1 ATOM 4304 N N . THR A 1 565 ? 23.565 30.767 46.661 1.00 23.29 ? 558 THR A N 1 ATOM 4305 C CA . THR A 1 565 ? 22.989 29.748 47.517 1.00 23.17 ? 558 THR A CA 1 ATOM 4306 C C . THR A 1 565 ? 23.399 29.951 48.979 1.00 22.86 ? 558 THR A C 1 ATOM 4307 O O . THR A 1 565 ? 24.296 30.743 49.286 1.00 22.79 ? 558 THR A O 1 ATOM 4308 C CB . THR A 1 565 ? 23.529 28.356 47.128 1.00 24.09 ? 558 THR A CB 1 ATOM 4309 O OG1 . THR A 1 565 ? 24.959 28.397 47.173 1.00 25.62 ? 558 THR A OG1 1 ATOM 4310 C CG2 . THR A 1 565 ? 23.069 27.936 45.720 1.00 25.48 ? 558 THR A CG2 1 ATOM 4311 N N . TYR A 1 566 ? 22.786 29.163 49.861 1.00 22.99 ? 559 TYR A N 1 ATOM 4312 C CA . TYR A 1 566 ? 23.231 29.092 51.239 1.00 24.25 ? 559 TYR A CA 1 ATOM 4313 C C . TYR A 1 566 ? 24.736 28.796 51.340 1.00 23.80 ? 559 TYR A C 1 ATOM 4314 O O . TYR A 1 566 ? 25.455 29.442 52.121 1.00 24.55 ? 559 TYR A O 1 ATOM 4315 C CB . TYR A 1 566 ? 22.456 28.024 52.011 1.00 23.24 ? 559 TYR A CB 1 ATOM 4316 C CG . TYR A 1 566 ? 23.006 27.790 53.401 1.00 25.50 ? 559 TYR A CG 1 ATOM 4317 C CD1 . TYR A 1 566 ? 22.699 28.657 54.436 1.00 26.34 ? 559 TYR A CD1 1 ATOM 4318 C CD2 . TYR A 1 566 ? 23.863 26.700 53.671 1.00 28.91 ? 559 TYR A CD2 1 ATOM 4319 C CE1 . TYR A 1 566 ? 23.216 28.464 55.725 1.00 29.03 ? 559 TYR A CE1 1 ATOM 4320 C CE2 . TYR A 1 566 ? 24.386 26.511 54.948 1.00 30.36 ? 559 TYR A CE2 1 ATOM 4321 C CZ . TYR A 1 566 ? 24.046 27.398 55.970 1.00 29.90 ? 559 TYR A CZ 1 ATOM 4322 O OH . TYR A 1 566 ? 24.542 27.213 57.252 1.00 31.96 ? 559 TYR A OH 1 ATOM 4323 N N . GLU A 1 567 ? 25.211 27.838 50.545 1.00 24.21 ? 560 GLU A N 1 ATOM 4324 C CA . GLU A 1 567 ? 26.621 27.457 50.630 1.00 25.37 ? 560 GLU A CA 1 ATOM 4325 C C . GLU A 1 567 ? 27.543 28.586 50.226 1.00 25.29 ? 560 GLU A C 1 ATOM 4326 O O . GLU A 1 567 ? 28.626 28.748 50.802 1.00 26.18 ? 560 GLU A O 1 ATOM 4327 C CB . GLU A 1 567 ? 26.895 26.197 49.803 1.00 26.17 ? 560 GLU A CB 1 ATOM 4328 C CG . GLU A 1 567 ? 26.250 24.933 50.365 1.00 27.47 ? 560 GLU A CG 1 ATOM 4329 C CD . GLU A 1 567 ? 24.745 24.868 50.086 1.00 29.13 ? 560 GLU A CD 1 ATOM 4330 O OE1 . GLU A 1 567 ? 24.308 25.432 49.072 1.00 28.29 ? 560 GLU A OE1 1 ATOM 4331 O OE2 . GLU A 1 567 ? 23.998 24.274 50.890 1.00 29.79 ? 560 GLU A OE2 1 ATOM 4332 N N . LEU A 1 568 ? 27.142 29.372 49.235 1.00 24.25 ? 561 LEU A N 1 ATOM 4333 C CA . LEU A 1 568 ? 27.929 30.528 48.864 1.00 24.55 ? 561 LEU A CA 1 ATOM 4334 C C . LEU A 1 568 ? 28.195 31.407 50.078 1.00 24.85 ? 561 LEU A C 1 ATOM 4335 O O . LEU A 1 568 ? 29.340 31.843 50.316 1.00 25.85 ? 561 LEU A O 1 ATOM 4336 C CB . LEU A 1 568 ? 27.190 31.358 47.802 1.00 24.20 ? 561 LEU A CB 1 ATOM 4337 C CG . LEU A 1 568 ? 27.856 32.689 47.436 1.00 24.45 ? 561 LEU A CG 1 ATOM 4338 C CD1 . LEU A 1 568 ? 29.225 32.436 46.836 1.00 24.72 ? 561 LEU A CD1 1 ATOM 4339 C CD2 . LEU A 1 568 ? 27.005 33.480 46.464 1.00 25.32 ? 561 LEU A CD2 1 ATOM 4340 N N . VAL A 1 569 ? 27.120 31.707 50.814 1.00 24.97 ? 562 VAL A N 1 ATOM 4341 C CA . VAL A 1 569 ? 27.231 32.587 51.984 1.00 24.65 ? 562 VAL A CA 1 ATOM 4342 C C . VAL A 1 569 ? 28.052 31.933 53.108 1.00 26.50 ? 562 VAL A C 1 ATOM 4343 O O . VAL A 1 569 ? 29.022 32.525 53.628 1.00 26.62 ? 562 VAL A O 1 ATOM 4344 C CB . VAL A 1 569 ? 25.837 33.005 52.513 1.00 24.38 ? 562 VAL A CB 1 ATOM 4345 C CG1 . VAL A 1 569 ? 25.987 33.867 53.768 1.00 24.51 ? 562 VAL A CG1 1 ATOM 4346 C CG2 . VAL A 1 569 ? 25.076 33.779 51.432 1.00 24.43 ? 562 VAL A CG2 1 ATOM 4347 N N . GLU A 1 570 ? 27.668 30.707 53.468 1.00 27.00 ? 563 GLU A N 1 ATOM 4348 C CA . GLU A 1 570 ? 28.273 30.003 54.591 1.00 28.79 ? 563 GLU A CA 1 ATOM 4349 C C . GLU A 1 570 ? 29.753 29.681 54.330 1.00 29.25 ? 563 GLU A C 1 ATOM 4350 O O . GLU A 1 570 ? 30.578 29.737 55.250 1.00 29.65 ? 563 GLU A O 1 ATOM 4351 C CB . GLU A 1 570 ? 27.492 28.713 54.855 1.00 29.77 ? 563 GLU A CB 1 ATOM 4352 C CG . GLU A 1 570 ? 27.842 28.003 56.185 1.00 33.67 ? 563 GLU A CG 1 ATOM 4353 C CD . GLU A 1 570 ? 29.042 27.072 56.076 1.00 40.55 ? 563 GLU A CD 1 ATOM 4354 O OE1 . GLU A 1 570 ? 29.373 26.608 54.952 1.00 40.32 ? 563 GLU A OE1 1 ATOM 4355 O OE2 . GLU A 1 570 ? 29.660 26.804 57.133 1.00 43.25 ? 563 GLU A OE2 1 ATOM 4356 N N . LYS A 1 571 ? 30.100 29.359 53.082 1.00 28.27 ? 564 LYS A N 1 ATOM 4357 C CA . LYS A 1 571 ? 31.500 28.981 52.782 1.00 28.70 ? 564 LYS A CA 1 ATOM 4358 C C . LYS A 1 571 ? 32.414 30.185 52.533 1.00 29.09 ? 564 LYS A C 1 ATOM 4359 O O . LYS A 1 571 ? 33.548 30.215 53.021 1.00 30.75 ? 564 LYS A O 1 ATOM 4360 C CB . LYS A 1 571 ? 31.578 28.024 51.587 1.00 28.24 ? 564 LYS A CB 1 ATOM 4361 C CG . LYS A 1 571 ? 30.968 26.662 51.860 1.00 30.42 ? 564 LYS A CG 1 ATOM 4362 C CD . LYS A 1 571 ? 31.059 25.785 50.590 1.00 33.67 ? 564 LYS A CD 1 ATOM 4363 C CE . LYS A 1 571 ? 30.313 24.429 50.699 1.00 37.25 ? 564 LYS A CE 1 ATOM 4364 N NZ . LYS A 1 571 ? 30.763 23.671 51.886 1.00 41.50 ? 564 LYS A NZ 1 ATOM 4365 N N . PHE A 1 572 ? 31.917 31.164 51.780 1.00 27.69 ? 565 PHE A N 1 ATOM 4366 C CA . PHE A 1 572 ? 32.777 32.195 51.213 1.00 27.62 ? 565 PHE A CA 1 ATOM 4367 C C . PHE A 1 572 ? 32.567 33.592 51.785 1.00 27.65 ? 565 PHE A C 1 ATOM 4368 O O . PHE A 1 572 ? 33.508 34.373 51.825 0.80 28.24 ? 565 PHE A O 1 ATOM 4369 C CB . PHE A 1 572 ? 32.652 32.204 49.687 1.00 27.49 ? 565 PHE A CB 1 ATOM 4370 C CG . PHE A 1 572 ? 33.077 30.910 49.065 1.00 29.83 ? 565 PHE A CG 1 ATOM 4371 C CD1 . PHE A 1 572 ? 34.398 30.480 49.192 1.00 33.19 ? 565 PHE A CD1 1 ATOM 4372 C CD2 . PHE A 1 572 ? 32.164 30.110 48.382 1.00 29.69 ? 565 PHE A CD2 1 ATOM 4373 C CE1 . PHE A 1 572 ? 34.802 29.276 48.651 1.00 32.48 ? 565 PHE A CE1 1 ATOM 4374 C CE2 . PHE A 1 572 ? 32.553 28.881 47.815 1.00 31.07 ? 565 PHE A CE2 1 ATOM 4375 C CZ . PHE A 1 572 ? 33.880 28.458 47.960 1.00 33.20 ? 565 PHE A CZ 1 ATOM 4376 N N . TYR A 1 573 ? 31.352 33.920 52.233 1.00 26.97 ? 566 TYR A N 1 ATOM 4377 C CA . TYR A 1 573 ? 31.099 35.293 52.682 1.00 26.46 ? 566 TYR A CA 1 ATOM 4378 C C . TYR A 1 573 ? 31.158 35.475 54.183 1.00 27.13 ? 566 TYR A C 1 ATOM 4379 O O . TYR A 1 573 ? 31.796 36.437 54.675 1.00 28.37 ? 566 TYR A O 1 ATOM 4380 C CB . TYR A 1 573 ? 29.744 35.839 52.136 1.00 24.94 ? 566 TYR A CB 1 ATOM 4381 C CG . TYR A 1 573 ? 29.857 36.319 50.710 1.00 25.31 ? 566 TYR A CG 1 ATOM 4382 C CD1 . TYR A 1 573 ? 29.849 35.392 49.662 1.00 24.57 ? 566 TYR A CD1 1 ATOM 4383 C CD2 . TYR A 1 573 ? 30.006 37.682 50.395 1.00 26.91 ? 566 TYR A CD2 1 ATOM 4384 C CE1 . TYR A 1 573 ? 29.975 35.799 48.337 1.00 25.40 ? 566 TYR A CE1 1 ATOM 4385 C CE2 . TYR A 1 573 ? 30.141 38.104 49.048 1.00 28.19 ? 566 TYR A CE2 1 ATOM 4386 C CZ . TYR A 1 573 ? 30.131 37.140 48.042 1.00 26.43 ? 566 TYR A CZ 1 ATOM 4387 O OH . TYR A 1 573 ? 30.299 37.507 46.736 1.00 27.21 ? 566 TYR A OH 1 ATOM 4388 N N . ASP A 1 574 ? 30.467 34.610 54.928 1.00 26.52 ? 567 ASP A N 1 ATOM 4389 C CA . ASP A 1 574 ? 30.269 34.897 56.358 1.00 26.68 ? 567 ASP A CA 1 ATOM 4390 C C . ASP A 1 574 ? 30.076 33.625 57.171 1.00 27.42 ? 567 ASP A C 1 ATOM 4391 O O . ASP A 1 574 ? 29.011 33.390 57.722 1.00 27.38 ? 567 ASP A O 1 ATOM 4392 C CB . ASP A 1 574 ? 29.057 35.844 56.523 1.00 25.89 ? 567 ASP A CB 1 ATOM 4393 C CG . ASP A 1 574 ? 28.991 36.512 57.901 1.00 26.21 ? 567 ASP A CG 1 ATOM 4394 O OD1 . ASP A 1 574 ? 29.981 36.470 58.692 1.00 29.19 ? 567 ASP A OD1 1 ATOM 4395 O OD2 . ASP A 1 574 ? 27.920 37.077 58.176 1.00 26.19 ? 567 ASP A OD2 1 ATOM 4396 N N . PRO A 1 575 ? 31.124 32.789 57.265 1.00 28.56 ? 568 PRO A N 1 ATOM 4397 C CA . PRO A 1 575 ? 30.946 31.491 57.911 1.00 29.70 ? 568 PRO A CA 1 ATOM 4398 C C . PRO A 1 575 ? 30.467 31.560 59.351 1.00 29.92 ? 568 PRO A C 1 ATOM 4399 O O . PRO A 1 575 ? 29.734 30.659 59.804 1.00 30.87 ? 568 PRO A O 1 ATOM 4400 C CB . PRO A 1 575 ? 32.342 30.835 57.846 1.00 30.78 ? 568 PRO A CB 1 ATOM 4401 C CG . PRO A 1 575 ? 33.194 31.712 57.038 1.00 31.14 ? 568 PRO A CG 1 ATOM 4402 C CD . PRO A 1 575 ? 32.456 32.974 56.675 1.00 29.30 ? 568 PRO A CD 1 ATOM 4403 N N A MET A 1 576 ? 30.863 32.610 60.062 0.70 29.69 ? 569 MET A N 1 ATOM 4404 N N B MET A 1 576 ? 30.877 32.611 60.059 0.30 29.76 ? 569 MET A N 1 ATOM 4405 C CA A MET A 1 576 ? 30.475 32.762 61.464 0.70 30.63 ? 569 MET A CA 1 ATOM 4406 C CA B MET A 1 576 ? 30.514 32.811 61.462 0.30 30.14 ? 569 MET A CA 1 ATOM 4407 C C A MET A 1 576 ? 29.194 33.583 61.634 0.70 29.67 ? 569 MET A C 1 ATOM 4408 C C B MET A 1 576 ? 29.223 33.608 61.633 0.30 29.27 ? 569 MET A C 1 ATOM 4409 O O A MET A 1 576 ? 28.672 33.717 62.752 0.70 29.23 ? 569 MET A O 1 ATOM 4410 O O B MET A 1 576 ? 28.734 33.768 62.758 0.30 29.20 ? 569 MET A O 1 ATOM 4411 C CB A MET A 1 576 ? 31.636 33.360 62.272 0.70 31.82 ? 569 MET A CB 1 ATOM 4412 C CB B MET A 1 576 ? 31.643 33.533 62.200 0.30 30.91 ? 569 MET A CB 1 ATOM 4413 C CG A MET A 1 576 ? 32.900 32.452 62.305 0.70 36.00 ? 569 MET A CG 1 ATOM 4414 C CG B MET A 1 576 ? 32.983 32.808 62.173 0.30 32.97 ? 569 MET A CG 1 ATOM 4415 S SD A MET A 1 576 ? 32.498 30.772 62.825 0.70 43.49 ? 569 MET A SD 1 ATOM 4416 S SD B MET A 1 576 ? 34.187 33.677 63.194 0.30 36.28 ? 569 MET A SD 1 ATOM 4417 C CE A MET A 1 576 ? 32.190 30.989 64.579 0.70 44.01 ? 569 MET A CE 1 ATOM 4418 C CE B MET A 1 576 ? 35.088 34.598 61.950 0.30 34.25 ? 569 MET A CE 1 ATOM 4419 N N . PHE A 1 577 ? 28.691 34.124 60.524 1.00 27.97 ? 570 PHE A N 1 ATOM 4420 C CA . PHE A 1 577 ? 27.476 34.959 60.540 1.00 26.88 ? 570 PHE A CA 1 ATOM 4421 C C . PHE A 1 577 ? 27.630 36.209 61.399 1.00 27.01 ? 570 PHE A C 1 ATOM 4422 O O . PHE A 1 577 ? 26.645 36.819 61.848 1.00 27.61 ? 570 PHE A O 1 ATOM 4423 C CB . PHE A 1 577 ? 26.215 34.110 60.804 1.00 26.63 ? 570 PHE A CB 1 ATOM 4424 C CG . PHE A 1 577 ? 25.801 33.321 59.594 1.00 27.36 ? 570 PHE A CG 1 ATOM 4425 C CD1 . PHE A 1 577 ? 24.830 33.821 58.734 1.00 26.83 ? 570 PHE A CD1 1 ATOM 4426 C CD2 . PHE A 1 577 ? 26.459 32.121 59.266 1.00 27.46 ? 570 PHE A CD2 1 ATOM 4427 C CE1 . PHE A 1 577 ? 24.486 33.125 57.569 1.00 25.91 ? 570 PHE A CE1 1 ATOM 4428 C CE2 . PHE A 1 577 ? 26.126 31.410 58.094 1.00 28.32 ? 570 PHE A CE2 1 ATOM 4429 C CZ . PHE A 1 577 ? 25.130 31.928 57.243 1.00 25.64 ? 570 PHE A CZ 1 ATOM 4430 N N . LYS A 1 578 ? 28.887 36.621 61.565 1.00 27.82 ? 571 LYS A N 1 ATOM 4431 C CA . LYS A 1 578 ? 29.179 37.835 62.335 1.00 27.44 ? 571 LYS A CA 1 ATOM 4432 C C . LYS A 1 578 ? 28.897 39.109 61.551 1.00 26.65 ? 571 LYS A C 1 ATOM 4433 O O . LYS A 1 578 ? 28.546 40.119 62.148 1.00 27.10 ? 571 LYS A O 1 ATOM 4434 C CB . LYS A 1 578 ? 30.619 37.847 62.862 1.00 28.33 ? 571 LYS A CB 1 ATOM 4435 C CG . LYS A 1 578 ? 31.698 37.915 61.778 1.00 28.34 ? 571 LYS A CG 1 ATOM 4436 C CD . LYS A 1 578 ? 33.073 37.826 62.434 1.00 31.80 ? 571 LYS A CD 1 ATOM 4437 C CE . LYS A 1 578 ? 34.157 38.084 61.409 1.00 35.35 ? 571 LYS A CE 1 ATOM 4438 N NZ . LYS A 1 578 ? 35.518 38.288 62.095 1.00 38.15 ? 571 LYS A NZ 1 ATOM 4439 N N . TYR A 1 579 ? 29.080 39.091 60.234 1.00 26.59 ? 572 TYR A N 1 ATOM 4440 C CA . TYR A 1 579 ? 28.741 40.275 59.444 1.00 25.94 ? 572 TYR A CA 1 ATOM 4441 C C . TYR A 1 579 ? 27.220 40.421 59.385 1.00 25.08 ? 572 TYR A C 1 ATOM 4442 O O . TYR A 1 579 ? 26.701 41.534 59.518 1.00 24.55 ? 572 TYR A O 1 ATOM 4443 C CB . TYR A 1 579 ? 29.385 40.250 58.036 1.00 26.08 ? 572 TYR A CB 1 ATOM 4444 C CG . TYR A 1 579 ? 30.887 40.140 58.145 1.00 27.88 ? 572 TYR A CG 1 ATOM 4445 C CD1 . TYR A 1 579 ? 31.620 41.128 58.805 1.00 29.29 ? 572 TYR A CD1 1 ATOM 4446 C CD2 . TYR A 1 579 ? 31.564 39.028 57.648 1.00 30.20 ? 572 TYR A CD2 1 ATOM 4447 C CE1 . TYR A 1 579 ? 32.996 41.018 58.947 1.00 33.58 ? 572 TYR A CE1 1 ATOM 4448 C CE2 . TYR A 1 579 ? 32.933 38.915 57.788 1.00 32.84 ? 572 TYR A CE2 1 ATOM 4449 C CZ . TYR A 1 579 ? 33.637 39.916 58.429 1.00 33.83 ? 572 TYR A CZ 1 ATOM 4450 O OH . TYR A 1 579 ? 35.005 39.776 58.553 1.00 37.92 ? 572 TYR A OH 1 ATOM 4451 N N . HIS A 1 580 ? 26.512 39.306 59.207 1.00 24.52 ? 573 HIS A N 1 ATOM 4452 C CA . HIS A 1 580 ? 25.034 39.305 59.310 1.00 24.46 ? 573 HIS A CA 1 ATOM 4453 C C . HIS A 1 580 ? 24.582 39.861 60.670 1.00 24.46 ? 573 HIS A C 1 ATOM 4454 O O . HIS A 1 580 ? 23.674 40.688 60.733 1.00 23.81 ? 573 HIS A O 1 ATOM 4455 C CB . HIS A 1 580 ? 24.463 37.901 59.172 1.00 24.28 ? 573 HIS A CB 1 ATOM 4456 C CG . HIS A 1 580 ? 24.368 37.403 57.768 1.00 25.32 ? 573 HIS A CG 1 ATOM 4457 N ND1 . HIS A 1 580 ? 25.455 36.928 57.061 1.00 25.32 ? 573 HIS A ND1 1 ATOM 4458 C CD2 . HIS A 1 580 ? 23.292 37.249 56.954 1.00 26.52 ? 573 HIS A CD2 1 ATOM 4459 C CE1 . HIS A 1 580 ? 25.058 36.530 55.863 1.00 27.44 ? 573 HIS A CE1 1 ATOM 4460 N NE2 . HIS A 1 580 ? 23.746 36.682 55.785 1.00 28.53 ? 573 HIS A NE2 1 ATOM 4461 N N . LEU A 1 581 ? 25.216 39.406 61.748 1.00 25.35 ? 574 LEU A N 1 ATOM 4462 C CA . LEU A 1 581 ? 24.849 39.905 63.073 1.00 25.16 ? 574 LEU A CA 1 ATOM 4463 C C . LEU A 1 581 ? 25.068 41.417 63.207 1.00 25.51 ? 574 LEU A C 1 ATOM 4464 O O . LEU A 1 581 ? 24.192 42.130 63.717 1.00 24.84 ? 574 LEU A O 1 ATOM 4465 C CB . LEU A 1 581 ? 25.592 39.139 64.188 1.00 26.16 ? 574 LEU A CB 1 ATOM 4466 C CG . LEU A 1 581 ? 25.247 39.638 65.603 1.00 26.75 ? 574 LEU A CG 1 ATOM 4467 C CD1 . LEU A 1 581 ? 23.742 39.506 65.870 1.00 26.71 ? 574 LEU A CD1 1 ATOM 4468 C CD2 . LEU A 1 581 ? 26.052 38.820 66.621 1.00 26.41 ? 574 LEU A CD2 1 ATOM 4469 N N . THR A 1 582 ? 26.208 41.907 62.719 1.00 24.81 ? 575 THR A N 1 ATOM 4470 C CA . THR A 1 582 ? 26.492 43.352 62.719 1.00 24.53 ? 575 THR A CA 1 ATOM 4471 C C . THR A 1 582 ? 25.427 44.119 61.944 1.00 23.80 ? 575 THR A C 1 ATOM 4472 O O . THR A 1 582 ? 24.920 45.134 62.424 1.00 24.11 ? 575 THR A O 1 ATOM 4473 C CB . THR A 1 582 ? 27.903 43.644 62.199 1.00 25.44 ? 575 THR A CB 1 ATOM 4474 O OG1 . THR A 1 582 ? 28.861 43.103 63.139 1.00 26.23 ? 575 THR A OG1 1 ATOM 4475 C CG2 . THR A 1 582 ? 28.146 45.164 62.023 1.00 25.66 ? 575 THR A CG2 1 ATOM 4476 N N . VAL A 1 583 ? 25.063 43.605 60.775 1.00 23.50 ? 576 VAL A N 1 ATOM 4477 C CA . VAL A 1 583 ? 23.992 44.242 59.976 1.00 22.31 ? 576 VAL A CA 1 ATOM 4478 C C . VAL A 1 583 ? 22.646 44.207 60.724 1.00 22.18 ? 576 VAL A C 1 ATOM 4479 O O . VAL A 1 583 ? 21.894 45.193 60.690 1.00 22.65 ? 576 VAL A O 1 ATOM 4480 C CB . VAL A 1 583 ? 23.948 43.666 58.548 1.00 21.75 ? 576 VAL A CB 1 ATOM 4481 C CG1 . VAL A 1 583 ? 22.737 44.266 57.739 1.00 20.57 ? 576 VAL A CG1 1 ATOM 4482 C CG2 . VAL A 1 583 ? 25.252 44.025 57.839 1.00 24.46 ? 576 VAL A CG2 1 ATOM 4483 N N . ALA A 1 584 ? 22.345 43.104 61.410 1.00 22.64 ? 577 ALA A N 1 ATOM 4484 C CA . ALA A 1 584 ? 21.117 43.032 62.225 1.00 22.51 ? 577 ALA A CA 1 ATOM 4485 C C . ALA A 1 584 ? 21.144 44.085 63.327 1.00 23.35 ? 577 ALA A C 1 ATOM 4486 O O . ALA A 1 584 ? 20.121 44.735 63.604 1.00 22.94 ? 577 ALA A O 1 ATOM 4487 C CB . ALA A 1 584 ? 20.932 41.640 62.830 1.00 23.01 ? 577 ALA A CB 1 ATOM 4488 N N . GLN A 1 585 ? 22.303 44.252 63.962 1.00 23.61 ? 578 GLN A N 1 ATOM 4489 C CA . GLN A 1 585 ? 22.456 45.306 64.975 1.00 23.38 ? 578 GLN A CA 1 ATOM 4490 C C . GLN A 1 585 ? 22.268 46.718 64.429 1.00 23.39 ? 578 GLN A C 1 ATOM 4491 O O . GLN A 1 585 ? 21.669 47.588 65.102 1.00 22.73 ? 578 GLN A O 1 ATOM 4492 C CB . GLN A 1 585 ? 23.793 45.178 65.731 1.00 24.70 ? 578 GLN A CB 1 ATOM 4493 C CG . GLN A 1 585 ? 23.899 43.858 66.471 1.00 25.83 ? 578 GLN A CG 1 ATOM 4494 C CD . GLN A 1 585 ? 25.270 43.670 67.093 1.00 29.53 ? 578 GLN A CD 1 ATOM 4495 O OE1 . GLN A 1 585 ? 26.160 44.497 66.899 1.00 29.07 ? 578 GLN A OE1 1 ATOM 4496 N NE2 . GLN A 1 585 ? 25.459 42.560 67.821 1.00 30.68 ? 578 GLN A NE2 1 ATOM 4497 N N . VAL A 1 586 ? 22.766 46.964 63.221 1.00 22.43 ? 579 VAL A N 1 ATOM 4498 C CA . VAL A 1 586 ? 22.613 48.300 62.633 1.00 21.90 ? 579 VAL A CA 1 ATOM 4499 C C . VAL A 1 586 ? 21.156 48.524 62.229 1.00 21.27 ? 579 VAL A C 1 ATOM 4500 O O . VAL A 1 586 ? 20.563 49.530 62.604 1.00 20.49 ? 579 VAL A O 1 ATOM 4501 C CB . VAL A 1 586 ? 23.529 48.488 61.388 1.00 21.91 ? 579 VAL A CB 1 ATOM 4502 C CG1 . VAL A 1 586 ? 23.237 49.846 60.737 1.00 22.34 ? 579 VAL A CG1 1 ATOM 4503 C CG2 . VAL A 1 586 ? 25.024 48.419 61.773 1.00 22.83 ? 579 VAL A CG2 1 ATOM 4504 N N . ARG A 1 587 ? 20.585 47.606 61.459 1.00 21.19 ? 580 ARG A N 1 ATOM 4505 C CA . ARG A 1 587 ? 19.196 47.806 61.010 1.00 20.85 ? 580 ARG A CA 1 ATOM 4506 C C . ARG A 1 587 ? 18.245 47.817 62.194 1.00 21.68 ? 580 ARG A C 1 ATOM 4507 O O . ARG A 1 587 ? 17.353 48.678 62.289 1.00 21.37 ? 580 ARG A O 1 ATOM 4508 C CB . ARG A 1 587 ? 18.807 46.679 60.074 1.00 21.21 ? 580 ARG A CB 1 ATOM 4509 C CG . ARG A 1 587 ? 19.547 46.747 58.749 1.00 20.16 ? 580 ARG A CG 1 ATOM 4510 C CD . ARG A 1 587 ? 19.179 45.548 57.886 1.00 22.06 ? 580 ARG A CD 1 ATOM 4511 N NE . ARG A 1 587 ? 19.900 45.621 56.613 1.00 20.48 ? 580 ARG A NE 1 ATOM 4512 C CZ . ARG A 1 587 ? 19.903 44.667 55.682 1.00 21.93 ? 580 ARG A CZ 1 ATOM 4513 N NH1 . ARG A 1 587 ? 19.228 43.537 55.872 1.00 24.21 ? 580 ARG A NH1 1 ATOM 4514 N NH2 . ARG A 1 587 ? 20.579 44.852 54.559 1.00 20.00 ? 580 ARG A NH2 1 ATOM 4515 N N . GLY A 1 588 ? 18.419 46.845 63.083 1.00 21.97 ? 581 GLY A N 1 ATOM 4516 C CA . GLY A 1 588 ? 17.567 46.724 64.261 1.00 22.24 ? 581 GLY A CA 1 ATOM 4517 C C . GLY A 1 588 ? 17.714 47.879 65.238 1.00 22.60 ? 581 GLY A C 1 ATOM 4518 O O . GLY A 1 588 ? 16.706 48.392 65.761 1.00 22.95 ? 581 GLY A O 1 ATOM 4519 N N . GLY A 1 589 ? 18.959 48.289 65.470 1.00 23.24 ? 582 GLY A N 1 ATOM 4520 C CA . GLY A 1 589 ? 19.263 49.432 66.321 1.00 23.62 ? 582 GLY A CA 1 ATOM 4521 C C . GLY A 1 589 ? 18.656 50.718 65.787 1.00 23.14 ? 582 GLY A C 1 ATOM 4522 O O . GLY A 1 589 ? 18.137 51.539 66.565 1.00 23.07 ? 582 GLY A O 1 ATOM 4523 N N . MET A 1 590 ? 18.716 50.916 64.468 1.00 22.77 ? 583 MET A N 1 ATOM 4524 C CA . MET A 1 590 ? 18.087 52.095 63.869 1.00 22.01 ? 583 MET A CA 1 ATOM 4525 C C . MET A 1 590 ? 16.592 52.068 64.131 1.00 21.64 ? 583 MET A C 1 ATOM 4526 O O . MET A 1 590 ? 16.014 53.059 64.571 1.00 21.88 ? 583 MET A O 1 ATOM 4527 C CB . MET A 1 590 ? 18.401 52.172 62.354 1.00 21.81 ? 583 MET A CB 1 ATOM 4528 C CG . MET A 1 590 ? 19.842 52.574 62.098 1.00 23.05 ? 583 MET A CG 1 ATOM 4529 S SD . MET A 1 590 ? 20.243 52.559 60.346 1.00 25.00 ? 583 MET A SD 1 ATOM 4530 C CE . MET A 1 590 ? 19.504 54.130 59.797 1.00 24.03 ? 583 MET A CE 1 ATOM 4531 N N . VAL A 1 591 ? 15.957 50.925 63.848 1.00 22.01 ? 584 VAL A N 1 ATOM 4532 C CA . VAL A 1 591 ? 14.526 50.755 64.129 1.00 22.32 ? 584 VAL A CA 1 ATOM 4533 C C . VAL A 1 591 ? 14.187 51.022 65.600 1.00 22.92 ? 584 VAL A C 1 ATOM 4534 O O . VAL A 1 591 ? 13.228 51.768 65.896 1.00 22.12 ? 584 VAL A O 1 ATOM 4535 C CB . VAL A 1 591 ? 14.019 49.351 63.685 1.00 21.94 ? 584 VAL A CB 1 ATOM 4536 C CG1 . VAL A 1 591 ? 12.571 49.083 64.203 1.00 21.80 ? 584 VAL A CG1 1 ATOM 4537 C CG2 . VAL A 1 591 ? 14.129 49.195 62.148 1.00 21.30 ? 584 VAL A CG2 1 ATOM 4538 N N . PHE A 1 592 ? 14.988 50.442 66.518 1.00 22.90 ? 585 PHE A N 1 ATOM 4539 C CA . PHE A 1 592 ? 14.785 50.612 67.950 1.00 23.01 ? 585 PHE A CA 1 ATOM 4540 C C . PHE A 1 592 ? 14.801 52.097 68.329 1.00 23.65 ? 585 PHE A C 1 ATOM 4541 O O . PHE A 1 592 ? 13.870 52.576 68.979 1.00 24.78 ? 585 PHE A O 1 ATOM 4542 C CB . PHE A 1 592 ? 15.860 49.845 68.757 1.00 23.83 ? 585 PHE A CB 1 ATOM 4543 C CG . PHE A 1 592 ? 15.555 49.794 70.210 1.00 25.90 ? 585 PHE A CG 1 ATOM 4544 C CD1 . PHE A 1 592 ? 14.996 48.652 70.767 1.00 27.56 ? 585 PHE A CD1 1 ATOM 4545 C CD2 . PHE A 1 592 ? 15.753 50.922 71.006 1.00 27.77 ? 585 PHE A CD2 1 ATOM 4546 C CE1 . PHE A 1 592 ? 14.665 48.619 72.128 1.00 29.12 ? 585 PHE A CE1 1 ATOM 4547 C CE2 . PHE A 1 592 ? 15.432 50.907 72.354 1.00 27.60 ? 585 PHE A CE2 1 ATOM 4548 C CZ . PHE A 1 592 ? 14.891 49.744 72.916 1.00 29.17 ? 585 PHE A CZ 1 ATOM 4549 N N . GLU A 1 593 ? 15.808 52.840 67.867 1.00 23.60 ? 586 GLU A N 1 ATOM 4550 C CA . GLU A 1 593 ? 15.927 54.268 68.225 1.00 25.47 ? 586 GLU A CA 1 ATOM 4551 C C . GLU A 1 593 ? 14.794 55.080 67.593 1.00 23.12 ? 586 GLU A C 1 ATOM 4552 O O . GLU A 1 593 ? 14.200 55.934 68.240 1.00 24.27 ? 586 GLU A O 1 ATOM 4553 C CB . GLU A 1 593 ? 17.252 54.859 67.754 1.00 26.37 ? 586 GLU A CB 1 ATOM 4554 C CG . GLU A 1 593 ? 18.423 54.678 68.703 1.00 35.39 ? 586 GLU A CG 1 ATOM 4555 C CD . GLU A 1 593 ? 18.098 55.226 70.115 1.00 40.20 ? 586 GLU A CD 1 ATOM 4556 O OE1 . GLU A 1 593 ? 17.802 54.386 70.976 1.00 43.85 ? 586 GLU A OE1 1 ATOM 4557 O OE2 . GLU A 1 593 ? 18.057 56.466 70.337 1.00 45.63 ? 586 GLU A OE2 1 ATOM 4558 N N . LEU A 1 594 ? 14.489 54.813 66.323 1.00 22.02 ? 587 LEU A N 1 ATOM 4559 C CA . LEU A 1 594 ? 13.390 55.527 65.667 1.00 21.85 ? 587 LEU A CA 1 ATOM 4560 C C . LEU A 1 594 ? 12.049 55.292 66.373 1.00 22.21 ? 587 LEU A C 1 ATOM 4561 O O . LEU A 1 594 ? 11.221 56.218 66.489 1.00 22.69 ? 587 LEU A O 1 ATOM 4562 C CB . LEU A 1 594 ? 13.299 55.099 64.182 1.00 21.16 ? 587 LEU A CB 1 ATOM 4563 C CG . LEU A 1 594 ? 14.475 55.622 63.358 1.00 20.93 ? 587 LEU A CG 1 ATOM 4564 C CD1 . LEU A 1 594 ? 14.677 54.701 62.140 1.00 20.41 ? 587 LEU A CD1 1 ATOM 4565 C CD2 . LEU A 1 594 ? 14.193 57.074 62.955 1.00 22.54 ? 587 LEU A CD2 1 ATOM 4566 N N . ALA A 1 595 ? 11.843 54.061 66.867 1.00 21.73 ? 588 ALA A N 1 ATOM 4567 C CA . ALA A 1 595 ? 10.556 53.714 67.463 1.00 23.47 ? 588 ALA A CA 1 ATOM 4568 C C . ALA A 1 595 ? 10.501 54.056 68.944 1.00 24.36 ? 588 ALA A C 1 ATOM 4569 O O . ALA A 1 595 ? 9.409 54.101 69.509 1.00 25.20 ? 588 ALA A O 1 ATOM 4570 C CB . ALA A 1 595 ? 10.236 52.239 67.276 1.00 23.15 ? 588 ALA A CB 1 ATOM 4571 N N . ASN A 1 596 ? 11.658 54.278 69.567 1.00 24.66 ? 589 ASN A N 1 ATOM 4572 C CA . ASN A 1 596 ? 11.668 54.441 71.031 1.00 25.45 ? 589 ASN A CA 1 ATOM 4573 C C . ASN A 1 596 ? 12.160 55.745 71.599 1.00 26.65 ? 589 ASN A C 1 ATOM 4574 O O . ASN A 1 596 ? 11.811 56.088 72.741 1.00 28.34 ? 589 ASN A O 1 ATOM 4575 C CB . ASN A 1 596 ? 12.440 53.287 71.678 1.00 25.70 ? 589 ASN A CB 1 ATOM 4576 C CG A ASN A 1 596 ? 11.780 52.796 72.926 0.50 26.55 ? 589 ASN A CG 1 ATOM 4577 C CG B ASN A 1 596 ? 11.684 51.983 71.578 0.50 26.78 ? 589 ASN A CG 1 ATOM 4578 O OD1 A ASN A 1 596 ? 10.584 52.513 72.925 0.50 26.45 ? 589 ASN A OD1 1 ATOM 4579 O OD1 B ASN A 1 596 ? 12.035 51.098 70.789 0.50 29.85 ? 589 ASN A OD1 1 ATOM 4580 N ND2 A ASN A 1 596 ? 12.552 52.678 74.007 0.50 29.44 ? 589 ASN A ND2 1 ATOM 4581 N ND2 B ASN A 1 596 ? 10.626 51.862 72.358 0.50 24.72 ? 589 ASN A ND2 1 ATOM 4582 N N . SER A 1 597 ? 12.971 56.470 70.834 1.00 25.20 ? 590 SER A N 1 ATOM 4583 C CA . SER A 1 597 ? 13.517 57.736 71.328 1.00 26.54 ? 590 SER A CA 1 ATOM 4584 C C . SER A 1 597 ? 12.389 58.728 71.572 1.00 25.68 ? 590 SER A C 1 ATOM 4585 O O . SER A 1 597 ? 11.449 58.866 70.750 1.00 24.68 ? 590 SER A O 1 ATOM 4586 C CB . SER A 1 597 ? 14.547 58.294 70.334 1.00 26.90 ? 590 SER A CB 1 ATOM 4587 O OG . SER A 1 597 ? 15.131 59.510 70.811 1.00 30.40 ? 590 SER A OG 1 ATOM 4588 N N . ILE A 1 598 ? 12.472 59.442 72.691 1.00 24.92 ? 591 ILE A N 1 ATOM 4589 C CA . ILE A 1 598 ? 11.422 60.420 72.990 1.00 25.71 ? 591 ILE A CA 1 ATOM 4590 C C . ILE A 1 598 ? 11.297 61.484 71.920 1.00 24.96 ? 591 ILE A C 1 ATOM 4591 O O . ILE A 1 598 ? 10.180 61.749 71.413 1.00 24.96 ? 591 ILE A O 1 ATOM 4592 C CB . ILE A 1 598 ? 11.694 61.067 74.386 1.00 25.85 ? 591 ILE A CB 1 ATOM 4593 C CG1 . ILE A 1 598 ? 11.623 60.000 75.487 1.00 32.61 ? 591 ILE A CG1 1 ATOM 4594 C CG2 . ILE A 1 598 ? 10.727 62.197 74.618 1.00 29.15 ? 591 ILE A CG2 1 ATOM 4595 C CD1 . ILE A 1 598 ? 10.377 59.092 75.428 1.00 37.63 ? 591 ILE A CD1 1 ATOM 4596 N N . VAL A 1 599 ? 12.427 62.094 71.579 1.00 25.32 ? 592 VAL A N 1 ATOM 4597 C CA . VAL A 1 599 ? 12.492 63.014 70.452 1.00 25.46 ? 592 VAL A CA 1 ATOM 4598 C C . VAL A 1 599 ? 12.967 62.195 69.266 1.00 23.79 ? 592 VAL A C 1 ATOM 4599 O O . VAL A 1 599 ? 13.926 61.455 69.386 1.00 24.47 ? 592 VAL A O 1 ATOM 4600 C CB . VAL A 1 599 ? 13.472 64.151 70.739 1.00 25.94 ? 592 VAL A CB 1 ATOM 4601 C CG1 . VAL A 1 599 ? 13.609 65.071 69.546 1.00 27.86 ? 592 VAL A CG1 1 ATOM 4602 C CG2 . VAL A 1 599 ? 12.990 64.965 71.952 1.00 29.27 ? 592 VAL A CG2 1 ATOM 4603 N N . LEU A 1 600 ? 12.295 62.317 68.118 1.00 23.43 ? 593 LEU A N 1 ATOM 4604 C CA . LEU A 1 600 ? 12.760 61.562 66.931 1.00 22.99 ? 593 LEU A CA 1 ATOM 4605 C C . LEU A 1 600 ? 14.239 61.848 66.642 1.00 23.38 ? 593 LEU A C 1 ATOM 4606 O O . LEU A 1 600 ? 14.698 62.997 66.723 1.00 24.29 ? 593 LEU A O 1 ATOM 4607 C CB . LEU A 1 600 ? 11.883 61.900 65.707 1.00 22.19 ? 593 LEU A CB 1 ATOM 4608 C CG . LEU A 1 600 ? 10.493 61.280 65.730 1.00 23.84 ? 593 LEU A CG 1 ATOM 4609 C CD1 . LEU A 1 600 ? 9.689 61.875 64.564 1.00 24.44 ? 593 LEU A CD1 1 ATOM 4610 C CD2 . LEU A 1 600 ? 10.659 59.719 65.638 1.00 25.48 ? 593 LEU A CD2 1 ATOM 4611 N N . PRO A 1 601 ? 15.016 60.791 66.300 1.00 23.46 ? 594 PRO A N 1 ATOM 4612 C CA . PRO A 1 601 ? 16.477 60.922 66.190 1.00 24.21 ? 594 PRO A CA 1 ATOM 4613 C C . PRO A 1 601 ? 16.917 61.423 64.796 1.00 24.02 ? 594 PRO A C 1 ATOM 4614 O O . PRO A 1 601 ? 17.694 60.748 64.074 1.00 23.16 ? 594 PRO A O 1 ATOM 4615 C CB . PRO A 1 601 ? 16.968 59.493 66.443 1.00 24.50 ? 594 PRO A CB 1 ATOM 4616 C CG . PRO A 1 601 ? 15.869 58.614 65.930 1.00 23.90 ? 594 PRO A CG 1 ATOM 4617 C CD . PRO A 1 601 ? 14.580 59.379 66.260 1.00 23.48 ? 594 PRO A CD 1 ATOM 4618 N N . PHE A 1 602 ? 16.379 62.580 64.417 1.00 23.10 ? 595 PHE A N 1 ATOM 4619 C CA . PHE A 1 602 ? 16.667 63.220 63.129 1.00 22.90 ? 595 PHE A CA 1 ATOM 4620 C C . PHE A 1 602 ? 17.352 64.547 63.417 1.00 24.49 ? 595 PHE A C 1 ATOM 4621 O O . PHE A 1 602 ? 16.920 65.297 64.309 1.00 26.20 ? 595 PHE A O 1 ATOM 4622 C CB . PHE A 1 602 ? 15.383 63.557 62.349 1.00 21.75 ? 595 PHE A CB 1 ATOM 4623 C CG . PHE A 1 602 ? 14.581 62.368 61.863 1.00 20.61 ? 595 PHE A CG 1 ATOM 4624 C CD1 . PHE A 1 602 ? 15.169 61.138 61.573 1.00 22.57 ? 595 PHE A CD1 1 ATOM 4625 C CD2 . PHE A 1 602 ? 13.220 62.527 61.618 1.00 22.15 ? 595 PHE A CD2 1 ATOM 4626 C CE1 . PHE A 1 602 ? 14.376 60.071 61.079 1.00 22.76 ? 595 PHE A CE1 1 ATOM 4627 C CE2 . PHE A 1 602 ? 12.428 61.447 61.136 1.00 22.56 ? 595 PHE A CE2 1 ATOM 4628 C CZ . PHE A 1 602 ? 13.020 60.231 60.884 1.00 21.53 ? 595 PHE A CZ 1 ATOM 4629 N N . ASP A 1 603 ? 18.396 64.873 62.667 1.00 23.75 ? 596 ASP A N 1 ATOM 4630 C CA . ASP A 1 603 ? 19.044 66.174 62.832 1.00 23.93 ? 596 ASP A CA 1 ATOM 4631 C C . ASP A 1 603 ? 18.878 66.999 61.547 1.00 23.55 ? 596 ASP A C 1 ATOM 4632 O O . ASP A 1 603 ? 19.572 66.756 60.538 1.00 23.30 ? 596 ASP A O 1 ATOM 4633 C CB . ASP A 1 603 ? 20.516 66.012 63.200 1.00 24.66 ? 596 ASP A CB 1 ATOM 4634 C CG . ASP A 1 603 ? 21.150 67.318 63.658 1.00 27.82 ? 596 ASP A CG 1 ATOM 4635 O OD1 . ASP A 1 603 ? 20.613 68.405 63.374 1.00 26.04 ? 596 ASP A OD1 1 ATOM 4636 O OD2 . ASP A 1 603 ? 22.200 67.245 64.315 1.00 31.01 ? 596 ASP A OD2 1 ATOM 4637 N N . CYS A 1 604 ? 17.942 67.946 61.588 1.00 22.68 ? 597 CYS A N 1 ATOM 4638 C CA . CYS A 1 604 ? 17.695 68.773 60.410 1.00 23.23 ? 597 CYS A CA 1 ATOM 4639 C C . CYS A 1 604 ? 18.935 69.533 59.920 1.00 23.00 ? 597 CYS A C 1 ATOM 4640 O O . CYS A 1 604 ? 19.016 69.885 58.759 1.00 22.82 ? 597 CYS A O 1 ATOM 4641 C CB . CYS A 1 604 ? 16.541 69.749 60.686 1.00 22.29 ? 597 CYS A CB 1 ATOM 4642 S SG . CYS A 1 604 ? 16.832 70.865 62.108 1.00 28.06 ? 597 CYS A SG 1 ATOM 4643 N N . ARG A 1 605 ? 19.889 69.830 60.804 1.00 23.44 ? 598 ARG A N 1 ATOM 4644 C CA . ARG A 1 605 ? 21.080 70.574 60.383 1.00 24.24 ? 598 ARG A CA 1 ATOM 4645 C C . ARG A 1 605 ? 21.918 69.792 59.367 1.00 24.79 ? 598 ARG A C 1 ATOM 4646 O O . ARG A 1 605 ? 22.628 70.380 58.546 1.00 25.21 ? 598 ARG A O 1 ATOM 4647 C CB . ARG A 1 605 ? 21.936 70.949 61.598 1.00 24.94 ? 598 ARG A CB 1 ATOM 4648 C CG . ARG A 1 605 ? 21.172 71.864 62.555 1.00 25.12 ? 598 ARG A CG 1 ATOM 4649 C CD . ARG A 1 605 ? 21.929 71.998 63.902 1.00 25.06 ? 598 ARG A CD 1 ATOM 4650 N NE . ARG A 1 605 ? 22.031 70.711 64.580 1.00 29.39 ? 598 ARG A NE 1 ATOM 4651 C CZ . ARG A 1 605 ? 22.683 70.536 65.735 1.00 33.71 ? 598 ARG A CZ 1 ATOM 4652 N NH1 . ARG A 1 605 ? 23.267 71.578 66.325 1.00 33.70 ? 598 ARG A NH1 1 ATOM 4653 N NH2 . ARG A 1 605 ? 22.752 69.331 66.304 1.00 33.06 ? 598 ARG A NH2 1 ATOM 4654 N N . ASP A 1 606 ? 21.823 68.468 59.421 1.00 24.23 ? 599 ASP A N 1 ATOM 4655 C CA . ASP A 1 606 ? 22.552 67.638 58.465 1.00 23.68 ? 599 ASP A CA 1 ATOM 4656 C C . ASP A 1 606 ? 21.965 67.823 57.059 1.00 22.96 ? 599 ASP A C 1 ATOM 4657 O O . ASP A 1 606 ? 22.704 67.734 56.077 1.00 23.19 ? 599 ASP A O 1 ATOM 4658 C CB . ASP A 1 606 ? 22.520 66.168 58.899 1.00 24.40 ? 599 ASP A CB 1 ATOM 4659 C CG . ASP A 1 606 ? 23.534 65.877 60.005 1.00 28.17 ? 599 ASP A CG 1 ATOM 4660 O OD1 . ASP A 1 606 ? 24.634 66.465 59.931 1.00 36.06 ? 599 ASP A OD1 1 ATOM 4661 O OD2 . ASP A 1 606 ? 23.251 65.109 60.956 1.00 29.37 ? 599 ASP A OD2 1 ATOM 4662 N N . TYR A 1 607 ? 20.661 68.088 56.973 1.00 21.84 ? 600 TYR A N 1 ATOM 4663 C CA . TYR A 1 607 ? 20.063 68.343 55.651 1.00 20.52 ? 600 TYR A CA 1 ATOM 4664 C C . TYR A 1 607 ? 20.608 69.670 55.131 1.00 21.72 ? 600 TYR A C 1 ATOM 4665 O O . TYR A 1 607 ? 20.908 69.803 53.946 1.00 21.45 ? 600 TYR A O 1 ATOM 4666 C CB . TYR A 1 607 ? 18.528 68.377 55.709 1.00 19.96 ? 600 TYR A CB 1 ATOM 4667 C CG . TYR A 1 607 ? 17.882 67.408 54.715 1.00 19.87 ? 600 TYR A CG 1 ATOM 4668 C CD1 . TYR A 1 607 ? 18.240 67.443 53.366 1.00 20.35 ? 600 TYR A CD1 1 ATOM 4669 C CD2 . TYR A 1 607 ? 16.924 66.494 55.137 1.00 19.87 ? 600 TYR A CD2 1 ATOM 4670 C CE1 . TYR A 1 607 ? 17.641 66.566 52.430 1.00 20.94 ? 600 TYR A CE1 1 ATOM 4671 C CE2 . TYR A 1 607 ? 16.321 65.563 54.193 1.00 19.39 ? 600 TYR A CE2 1 ATOM 4672 C CZ . TYR A 1 607 ? 16.703 65.643 52.861 1.00 21.81 ? 600 TYR A CZ 1 ATOM 4673 O OH . TYR A 1 607 ? 16.133 64.783 51.969 1.00 20.77 ? 600 TYR A OH 1 ATOM 4674 N N . ALA A 1 608 ? 20.756 70.660 56.017 1.00 21.49 ? 601 ALA A N 1 ATOM 4675 C CA . ALA A 1 608 ? 21.229 71.975 55.567 1.00 21.94 ? 601 ALA A CA 1 ATOM 4676 C C . ALA A 1 608 ? 22.630 71.864 54.926 1.00 22.55 ? 601 ALA A C 1 ATOM 4677 O O . ALA A 1 608 ? 22.896 72.503 53.911 1.00 22.63 ? 601 ALA A O 1 ATOM 4678 C CB . ALA A 1 608 ? 21.250 72.982 56.723 1.00 21.82 ? 601 ALA A CB 1 ATOM 4679 N N . VAL A 1 609 ? 23.519 71.089 55.556 1.00 22.89 ? 602 VAL A N 1 ATOM 4680 C CA . VAL A 1 609 ? 24.865 70.886 55.054 1.00 24.16 ? 602 VAL A CA 1 ATOM 4681 C C . VAL A 1 609 ? 24.832 70.284 53.642 1.00 24.40 ? 602 VAL A C 1 ATOM 4682 O O . VAL A 1 609 ? 25.488 70.821 52.724 1.00 24.78 ? 602 VAL A O 1 ATOM 4683 C CB . VAL A 1 609 ? 25.719 70.015 56.009 1.00 25.04 ? 602 VAL A CB 1 ATOM 4684 C CG1 . VAL A 1 609 ? 27.110 69.711 55.378 1.00 27.28 ? 602 VAL A CG1 1 ATOM 4685 C CG2 . VAL A 1 609 ? 25.904 70.787 57.305 1.00 26.68 ? 602 VAL A CG2 1 ATOM 4686 N N . VAL A 1 610 ? 24.051 69.218 53.462 1.00 23.23 ? 603 VAL A N 1 ATOM 4687 C CA . VAL A 1 610 ? 24.043 68.553 52.136 1.00 22.44 ? 603 VAL A CA 1 ATOM 4688 C C . VAL A 1 610 ? 23.378 69.420 51.076 1.00 22.22 ? 603 VAL A C 1 ATOM 4689 O O . VAL A 1 610 ? 23.812 69.409 49.926 1.00 21.64 ? 603 VAL A O 1 ATOM 4690 C CB . VAL A 1 610 ? 23.528 67.093 52.096 1.00 23.41 ? 603 VAL A CB 1 ATOM 4691 C CG1 . VAL A 1 610 ? 24.282 66.220 53.156 1.00 24.30 ? 603 VAL A CG1 1 ATOM 4692 C CG2 . VAL A 1 610 ? 22.080 66.998 52.254 1.00 25.61 ? 603 VAL A CG2 1 ATOM 4693 N N . LEU A 1 611 ? 22.362 70.182 51.471 1.00 20.93 ? 604 LEU A N 1 ATOM 4694 C CA . LEU A 1 611 ? 21.678 71.035 50.498 1.00 20.52 ? 604 LEU A CA 1 ATOM 4695 C C . LEU A 1 611 ? 22.682 72.027 49.918 1.00 22.21 ? 604 LEU A C 1 ATOM 4696 O O . LEU A 1 611 ? 22.607 72.340 48.719 1.00 22.71 ? 604 LEU A O 1 ATOM 4697 C CB . LEU A 1 611 ? 20.473 71.777 51.102 1.00 20.41 ? 604 LEU A CB 1 ATOM 4698 C CG . LEU A 1 611 ? 19.275 70.854 51.373 1.00 18.85 ? 604 LEU A CG 1 ATOM 4699 C CD1 . LEU A 1 611 ? 18.271 71.582 52.249 1.00 21.05 ? 604 LEU A CD1 1 ATOM 4700 C CD2 . LEU A 1 611 ? 18.604 70.332 50.077 1.00 21.06 ? 604 LEU A CD2 1 ATOM 4701 N N . ARG A 1 612 ? 23.586 72.555 50.757 1.00 22.18 ? 605 ARG A N 1 ATOM 4702 C CA . ARG A 1 612 ? 24.582 73.492 50.238 1.00 23.20 ? 605 ARG A CA 1 ATOM 4703 C C . ARG A 1 612 ? 25.538 72.782 49.283 1.00 22.94 ? 605 ARG A C 1 ATOM 4704 O O . ARG A 1 612 ? 25.866 73.320 48.237 1.00 23.02 ? 605 ARG A O 1 ATOM 4705 C CB . ARG A 1 612 ? 25.357 74.196 51.369 1.00 24.04 ? 605 ARG A CB 1 ATOM 4706 C CG . ARG A 1 612 ? 26.472 75.108 50.848 1.00 26.78 ? 605 ARG A CG 1 ATOM 4707 C CD . ARG A 1 612 ? 25.950 76.265 49.948 1.00 29.35 ? 605 ARG A CD 1 ATOM 4708 N NE . ARG A 1 612 ? 27.094 77.039 49.468 0.80 30.13 ? 605 ARG A NE 1 ATOM 4709 C CZ . ARG A 1 612 ? 27.604 78.076 50.131 0.80 36.35 ? 605 ARG A CZ 1 ATOM 4710 N NH1 . ARG A 1 612 ? 27.049 78.477 51.280 0.80 34.59 ? 605 ARG A NH1 1 ATOM 4711 N NH2 . ARG A 1 612 ? 28.663 78.716 49.654 0.80 37.59 ? 605 ARG A NH2 1 ATOM 4712 N N . LYS A 1 613 ? 25.979 71.571 49.638 1.00 23.32 ? 606 LYS A N 1 ATOM 4713 C CA . LYS A 1 613 ? 26.820 70.774 48.749 1.00 24.00 ? 606 LYS A CA 1 ATOM 4714 C C . LYS A 1 613 ? 26.137 70.560 47.380 1.00 23.01 ? 606 LYS A C 1 ATOM 4715 O O . LYS A 1 613 ? 26.755 70.748 46.318 1.00 22.91 ? 606 LYS A O 1 ATOM 4716 C CB . LYS A 1 613 ? 27.120 69.422 49.418 1.00 24.99 ? 606 LYS A CB 1 ATOM 4717 C CG . LYS A 1 613 ? 28.004 68.473 48.608 1.00 29.18 ? 606 LYS A CG 1 ATOM 4718 C CD . LYS A 1 613 ? 28.313 67.186 49.402 1.00 35.27 ? 606 LYS A CD 1 ATOM 4719 C CE . LYS A 1 613 ? 27.085 66.335 49.664 1.00 35.81 ? 606 LYS A CE 1 ATOM 4720 N NZ . LYS A 1 613 ? 27.447 65.100 50.436 1.00 38.38 ? 606 LYS A NZ 1 ATOM 4721 N N . TYR A 1 614 ? 24.866 70.171 47.411 1.00 21.35 ? 607 TYR A N 1 ATOM 4722 C CA . TYR A 1 614 ? 24.125 69.904 46.166 1.00 20.31 ? 607 TYR A CA 1 ATOM 4723 C C . TYR A 1 614 ? 23.922 71.183 45.365 1.00 20.46 ? 607 TYR A C 1 ATOM 4724 O O . TYR A 1 614 ? 23.967 71.136 44.133 1.00 21.56 ? 607 TYR A O 1 ATOM 4725 C CB . TYR A 1 614 ? 22.769 69.274 46.461 1.00 19.35 ? 607 TYR A CB 1 ATOM 4726 C CG . TYR A 1 614 ? 22.843 67.956 47.213 1.00 19.58 ? 607 TYR A CG 1 ATOM 4727 C CD1 . TYR A 1 614 ? 23.986 67.139 47.158 1.00 20.79 ? 607 TYR A CD1 1 ATOM 4728 C CD2 . TYR A 1 614 ? 21.750 67.538 47.993 1.00 20.69 ? 607 TYR A CD2 1 ATOM 4729 C CE1 . TYR A 1 614 ? 24.016 65.899 47.855 1.00 22.01 ? 607 TYR A CE1 1 ATOM 4730 C CE2 . TYR A 1 614 ? 21.768 66.335 48.686 1.00 21.12 ? 607 TYR A CE2 1 ATOM 4731 C CZ . TYR A 1 614 ? 22.908 65.519 48.610 1.00 23.66 ? 607 TYR A CZ 1 ATOM 4732 O OH . TYR A 1 614 ? 22.911 64.326 49.325 1.00 23.50 ? 607 TYR A OH 1 ATOM 4733 N N . ALA A 1 615 ? 23.702 72.308 46.047 1.00 20.38 ? 608 ALA A N 1 ATOM 4734 C CA . ALA A 1 615 ? 23.527 73.564 45.321 1.00 20.81 ? 608 ALA A CA 1 ATOM 4735 C C . ALA A 1 615 ? 24.848 73.960 44.631 1.00 22.39 ? 608 ALA A C 1 ATOM 4736 O O . ALA A 1 615 ? 24.870 74.392 43.461 1.00 23.08 ? 608 ALA A O 1 ATOM 4737 C CB . ALA A 1 615 ? 23.054 74.659 46.283 1.00 21.45 ? 608 ALA A CB 1 ATOM 4738 N N . ASP A 1 616 ? 25.963 73.832 45.356 1.00 23.58 ? 609 ASP A N 1 ATOM 4739 C CA . ASP A 1 616 ? 27.272 74.107 44.754 1.00 25.41 ? 609 ASP A CA 1 ATOM 4740 C C . ASP A 1 616 ? 27.479 73.217 43.503 1.00 24.51 ? 609 ASP A C 1 ATOM 4741 O O . ASP A 1 616 ? 28.029 73.664 42.481 1.00 24.78 ? 609 ASP A O 1 ATOM 4742 C CB . ASP A 1 616 ? 28.430 73.822 45.743 1.00 25.82 ? 609 ASP A CB 1 ATOM 4743 C CG . ASP A 1 616 ? 28.522 74.823 46.893 1.00 30.81 ? 609 ASP A CG 1 ATOM 4744 O OD1 . ASP A 1 616 ? 27.982 75.933 46.811 1.00 32.35 ? 609 ASP A OD1 1 ATOM 4745 O OD2 . ASP A 1 616 ? 29.216 74.484 47.894 1.00 37.37 ? 609 ASP A OD2 1 ATOM 4746 N N . LYS A 1 617 ? 27.091 71.949 43.624 1.00 23.79 ? 610 LYS A N 1 ATOM 4747 C CA . LYS A 1 617 ? 27.316 70.979 42.569 1.00 24.77 ? 610 LYS A CA 1 ATOM 4748 C C . LYS A 1 617 ? 26.509 71.340 41.316 1.00 24.37 ? 610 LYS A C 1 ATOM 4749 O O . LYS A 1 617 ? 27.050 71.377 40.204 1.00 24.74 ? 610 LYS A O 1 ATOM 4750 C CB . LYS A 1 617 ? 26.956 69.570 43.045 1.00 24.10 ? 610 LYS A CB 1 ATOM 4751 C CG . LYS A 1 617 ? 27.221 68.509 42.001 1.00 29.10 ? 610 LYS A CG 1 ATOM 4752 C CD . LYS A 1 617 ? 26.585 67.206 42.449 1.00 33.64 ? 610 LYS A CD 1 ATOM 4753 C CE . LYS A 1 617 ? 27.176 66.021 41.709 1.00 39.19 ? 610 LYS A CE 1 ATOM 4754 N NZ . LYS A 1 617 ? 26.380 64.816 42.039 1.00 42.59 ? 610 LYS A NZ 1 ATOM 4755 N N . ILE A 1 618 ? 25.231 71.655 41.504 1.00 23.35 ? 611 ILE A N 1 ATOM 4756 C CA . ILE A 1 618 ? 24.388 71.950 40.338 1.00 22.92 ? 611 ILE A CA 1 ATOM 4757 C C . ILE A 1 618 ? 24.780 73.306 39.708 1.00 22.94 ? 611 ILE A C 1 ATOM 4758 O O . ILE A 1 618 ? 24.820 73.451 38.476 1.00 22.19 ? 611 ILE A O 1 ATOM 4759 C CB . ILE A 1 618 ? 22.874 71.853 40.680 1.00 22.62 ? 611 ILE A CB 1 ATOM 4760 C CG1 . ILE A 1 618 ? 22.039 71.827 39.389 1.00 22.38 ? 611 ILE A CG1 1 ATOM 4761 C CG2 . ILE A 1 618 ? 22.421 72.954 41.675 1.00 22.58 ? 611 ILE A CG2 1 ATOM 4762 C CD1 . ILE A 1 618 ? 22.126 70.505 38.676 1.00 23.13 ? 611 ILE A CD1 1 ATOM 4763 N N . TYR A 1 619 ? 25.156 74.272 40.547 1.00 22.78 ? 612 TYR A N 1 ATOM 4764 C CA . TYR A 1 619 ? 25.645 75.539 40.029 1.00 25.27 ? 612 TYR A CA 1 ATOM 4765 C C . TYR A 1 619 ? 26.907 75.301 39.163 1.00 25.85 ? 612 TYR A C 1 ATOM 4766 O O . TYR A 1 619 ? 27.043 75.871 38.082 1.00 25.57 ? 612 TYR A O 1 ATOM 4767 C CB . TYR A 1 619 ? 25.912 76.497 41.205 1.00 24.86 ? 612 TYR A CB 1 ATOM 4768 C CG . TYR A 1 619 ? 26.757 77.684 40.803 1.00 29.72 ? 612 TYR A CG 1 ATOM 4769 C CD1 . TYR A 1 619 ? 26.163 78.783 40.203 1.00 32.74 ? 612 TYR A CD1 1 ATOM 4770 C CD2 . TYR A 1 619 ? 28.142 77.662 40.968 1.00 35.55 ? 612 TYR A CD2 1 ATOM 4771 C CE1 . TYR A 1 619 ? 26.931 79.878 39.818 1.00 36.68 ? 612 TYR A CE1 1 ATOM 4772 C CE2 . TYR A 1 619 ? 28.929 78.743 40.567 1.00 37.69 ? 612 TYR A CE2 1 ATOM 4773 C CZ . TYR A 1 619 ? 28.304 79.834 39.992 1.00 40.13 ? 612 TYR A CZ 1 ATOM 4774 O OH . TYR A 1 619 ? 29.048 80.922 39.593 0.80 47.26 ? 612 TYR A OH 1 ATOM 4775 N N . SER A 1 620 ? 27.814 74.439 39.639 1.00 25.85 ? 613 SER A N 1 ATOM 4776 C CA . SER A 1 620 ? 29.059 74.180 38.911 1.00 28.21 ? 613 SER A CA 1 ATOM 4777 C C . SER A 1 620 ? 28.779 73.535 37.550 1.00 27.72 ? 613 SER A C 1 ATOM 4778 O O . SER A 1 620 ? 29.496 73.829 36.591 1.00 29.25 ? 613 SER A O 1 ATOM 4779 C CB . SER A 1 620 ? 30.025 73.328 39.743 1.00 28.80 ? 613 SER A CB 1 ATOM 4780 O OG A SER A 1 620 ? 30.396 74.035 40.918 0.50 29.13 ? 613 SER A OG 1 ATOM 4781 O OG B SER A 1 620 ? 29.588 71.998 39.800 0.50 31.20 ? 613 SER A OG 1 ATOM 4782 N N . ILE A 1 621 ? 27.754 72.671 37.472 1.00 26.49 ? 614 ILE A N 1 ATOM 4783 C CA . ILE A 1 621 ? 27.355 72.088 36.193 1.00 25.84 ? 614 ILE A CA 1 ATOM 4784 C C . ILE A 1 621 ? 26.887 73.182 35.239 1.00 26.52 ? 614 ILE A C 1 ATOM 4785 O O . ILE A 1 621 ? 27.315 73.242 34.080 1.00 26.98 ? 614 ILE A O 1 ATOM 4786 C CB . ILE A 1 621 ? 26.245 71.013 36.364 1.00 25.48 ? 614 ILE A CB 1 ATOM 4787 C CG1 . ILE A 1 621 ? 26.844 69.787 37.064 1.00 24.55 ? 614 ILE A CG1 1 ATOM 4788 C CG2 . ILE A 1 621 ? 25.614 70.647 34.980 1.00 25.32 ? 614 ILE A CG2 1 ATOM 4789 C CD1 . ILE A 1 621 ? 25.770 68.732 37.503 1.00 23.94 ? 614 ILE A CD1 1 ATOM 4790 N N . SER A 1 622 ? 26.022 74.059 35.741 1.00 24.76 ? 615 SER A N 1 ATOM 4791 C CA . SER A 1 622 ? 25.483 75.134 34.910 1.00 25.31 ? 615 SER A CA 1 ATOM 4792 C C . SER A 1 622 ? 26.595 76.057 34.423 1.00 26.91 ? 615 SER A C 1 ATOM 4793 O O . SER A 1 622 ? 26.572 76.548 33.270 1.00 26.55 ? 615 SER A O 1 ATOM 4794 C CB . SER A 1 622 ? 24.428 75.921 35.700 1.00 24.86 ? 615 SER A CB 1 ATOM 4795 O OG . SER A 1 622 ? 23.797 76.870 34.872 1.00 24.88 ? 615 SER A OG 1 ATOM 4796 N N . MET A 1 623 ? 27.562 76.301 35.303 1.00 27.16 ? 616 MET A N 1 ATOM 4797 C CA . MET A 1 623 ? 28.669 77.236 34.989 1.00 30.52 ? 616 MET A CA 1 ATOM 4798 C C . MET A 1 623 ? 29.657 76.745 33.926 1.00 31.85 ? 616 MET A C 1 ATOM 4799 O O . MET A 1 623 ? 30.571 77.488 33.547 1.00 33.89 ? 616 MET A O 1 ATOM 4800 C CB . MET A 1 623 ? 29.354 77.675 36.260 1.00 30.33 ? 616 MET A CB 1 ATOM 4801 C CG . MET A 1 623 ? 28.605 78.808 36.946 0.80 33.20 ? 616 MET A CG 1 ATOM 4802 S SD . MET A 1 623 ? 28.499 80.361 35.975 0.80 41.84 ? 616 MET A SD 1 ATOM 4803 C CE . MET A 1 623 ? 30.218 80.780 35.741 0.80 38.66 ? 616 MET A CE 1 ATOM 4804 N N A LYS A 1 624 ? 29.469 75.524 33.436 0.60 32.39 ? 617 LYS A N 1 ATOM 4805 N N B LYS A 1 624 ? 29.451 75.509 33.456 0.40 31.90 ? 617 LYS A N 1 ATOM 4806 C CA A LYS A 1 624 ? 30.198 75.104 32.241 0.60 33.20 ? 617 LYS A CA 1 ATOM 4807 C CA B LYS A 1 624 ? 30.083 75.001 32.228 0.40 32.39 ? 617 LYS A CA 1 ATOM 4808 C C A LYS A 1 624 ? 29.662 75.844 31.001 0.60 33.02 ? 617 LYS A C 1 ATOM 4809 C C B LYS A 1 624 ? 29.650 75.830 31.014 0.40 32.50 ? 617 LYS A C 1 ATOM 4810 O O A LYS A 1 624 ? 30.275 75.783 29.928 0.60 33.16 ? 617 LYS A O 1 ATOM 4811 O O B LYS A 1 624 ? 30.315 75.809 29.973 0.40 32.86 ? 617 LYS A O 1 ATOM 4812 C CB A LYS A 1 624 ? 30.159 73.585 32.052 0.60 33.64 ? 617 LYS A CB 1 ATOM 4813 C CB B LYS A 1 624 ? 29.713 73.530 31.978 0.40 32.37 ? 617 LYS A CB 1 ATOM 4814 C CG A LYS A 1 624 ? 30.568 72.758 33.283 0.60 35.92 ? 617 LYS A CG 1 ATOM 4815 C CG B LYS A 1 624 ? 30.451 72.492 32.831 0.40 33.69 ? 617 LYS A CG 1 ATOM 4816 C CD A LYS A 1 624 ? 32.071 72.737 33.530 0.60 41.70 ? 617 LYS A CD 1 ATOM 4817 C CD B LYS A 1 624 ? 31.895 72.266 32.376 0.40 38.01 ? 617 LYS A CD 1 ATOM 4818 C CE A LYS A 1 624 ? 32.427 71.786 34.682 0.60 43.44 ? 617 LYS A CE 1 ATOM 4819 C CE B LYS A 1 624 ? 32.439 70.944 32.938 0.40 39.24 ? 617 LYS A CE 1 ATOM 4820 N NZ A LYS A 1 624 ? 32.253 72.423 36.028 0.60 43.69 ? 617 LYS A NZ 1 ATOM 4821 N NZ B LYS A 1 624 ? 33.843 70.648 32.513 0.40 41.35 ? 617 LYS A NZ 1 ATOM 4822 N N . HIS A 1 625 ? 28.543 76.564 31.166 1.00 31.34 ? 618 HIS A N 1 ATOM 4823 C CA . HIS A 1 625 ? 27.906 77.314 30.068 1.00 30.91 ? 618 HIS A CA 1 ATOM 4824 C C . HIS A 1 625 ? 27.724 78.807 30.396 1.00 31.09 ? 618 HIS A C 1 ATOM 4825 O O . HIS A 1 625 ? 26.583 79.311 30.378 1.00 29.46 ? 618 HIS A O 1 ATOM 4826 C CB . HIS A 1 625 ? 26.531 76.727 29.766 1.00 30.69 ? 618 HIS A CB 1 ATOM 4827 C CG . HIS A 1 625 ? 26.534 75.238 29.577 1.00 31.37 ? 618 HIS A CG 1 ATOM 4828 N ND1 . HIS A 1 625 ? 26.785 74.486 28.484 1.00 36.59 ? 618 HIS A ND1 1 ATOM 4829 C CD2 . HIS A 1 625 ? 26.246 74.354 30.598 1.00 30.73 ? 618 HIS A CD2 1 ATOM 4830 C CE1 . HIS A 1 625 ? 26.649 73.170 28.859 1.00 32.91 ? 618 HIS A CE1 1 ATOM 4831 N NE2 . HIS A 1 625 ? 26.323 73.114 30.140 1.00 34.44 ? 618 HIS A NE2 1 ATOM 4832 N N . PRO A 1 626 ? 28.838 79.524 30.679 1.00 31.96 ? 619 PRO A N 1 ATOM 4833 C CA . PRO A 1 626 ? 28.715 80.910 31.147 1.00 32.12 ? 619 PRO A CA 1 ATOM 4834 C C . PRO A 1 626 ? 28.041 81.826 30.142 1.00 32.34 ? 619 PRO A C 1 ATOM 4835 O O . PRO A 1 626 ? 27.262 82.693 30.562 1.00 31.97 ? 619 PRO A O 1 ATOM 4836 C CB . PRO A 1 626 ? 30.170 81.349 31.405 1.00 34.19 ? 619 PRO A CB 1 ATOM 4837 C CG . PRO A 1 626 ? 31.015 80.375 30.606 1.00 34.52 ? 619 PRO A CG 1 ATOM 4838 C CD . PRO A 1 626 ? 30.244 79.087 30.619 1.00 32.93 ? 619 PRO A CD 1 ATOM 4839 N N . GLN A 1 627 ? 28.294 81.635 28.841 1.00 32.75 ? 620 GLN A N 1 ATOM 4840 C CA . GLN A 1 627 ? 27.658 82.506 27.839 1.00 34.11 ? 620 GLN A CA 1 ATOM 4841 C C . GLN A 1 627 ? 26.143 82.395 27.879 1.00 32.37 ? 620 GLN A C 1 ATOM 4842 O O . GLN A 1 627 ? 25.437 83.400 27.878 1.00 31.68 ? 620 GLN A O 1 ATOM 4843 C CB . GLN A 1 627 ? 28.171 82.247 26.415 1.00 36.62 ? 620 GLN A CB 1 ATOM 4844 C CG . GLN A 1 627 ? 27.444 83.094 25.341 1.00 42.20 ? 620 GLN A CG 1 ATOM 4845 C CD . GLN A 1 627 ? 27.657 84.609 25.497 1.00 47.93 ? 620 GLN A CD 1 ATOM 4846 O OE1 . GLN A 1 627 ? 26.779 85.355 25.997 1.00 47.21 ? 620 GLN A OE1 1 ATOM 4847 N NE2 . GLN A 1 627 ? 28.828 85.069 25.077 1.00 52.43 ? 620 GLN A NE2 1 ATOM 4848 N N . GLU A 1 628 ? 25.648 81.162 27.920 1.00 29.67 ? 621 GLU A N 1 ATOM 4849 C CA . GLU A 1 628 ? 24.215 80.957 27.999 1.00 28.54 ? 621 GLU A CA 1 ATOM 4850 C C . GLU A 1 628 ? 23.616 81.477 29.297 1.00 27.63 ? 621 GLU A C 1 ATOM 4851 O O . GLU A 1 628 ? 22.482 81.987 29.308 1.00 27.77 ? 621 GLU A O 1 ATOM 4852 C CB . GLU A 1 628 ? 23.875 79.486 27.787 1.00 29.02 ? 621 GLU A CB 1 ATOM 4853 C CG . GLU A 1 628 ? 24.162 79.008 26.359 1.00 33.33 ? 621 GLU A CG 1 ATOM 4854 C CD . GLU A 1 628 ? 25.622 78.827 26.024 1.00 38.96 ? 621 GLU A CD 1 ATOM 4855 O OE1 . GLU A 1 628 ? 26.471 78.558 26.910 1.00 38.99 ? 621 GLU A OE1 1 ATOM 4856 O OE2 . GLU A 1 628 ? 25.931 78.985 24.826 1.00 44.85 ? 621 GLU A OE2 1 ATOM 4857 N N . MET A 1 629 ? 24.345 81.347 30.407 1.00 26.76 ? 622 MET A N 1 ATOM 4858 C CA . MET A 1 629 ? 23.803 81.876 31.673 1.00 26.09 ? 622 MET A CA 1 ATOM 4859 C C . MET A 1 629 ? 23.698 83.406 31.587 1.00 27.00 ? 622 MET A C 1 ATOM 4860 O O . MET A 1 629 ? 22.763 83.984 32.149 1.00 25.87 ? 622 MET A O 1 ATOM 4861 C CB . MET A 1 629 ? 24.658 81.462 32.870 1.00 26.40 ? 622 MET A CB 1 ATOM 4862 C CG . MET A 1 629 ? 24.546 79.965 33.181 1.00 26.37 ? 622 MET A CG 1 ATOM 4863 S SD . MET A 1 629 ? 25.558 79.498 34.616 1.00 27.99 ? 622 MET A SD 1 ATOM 4864 C CE . MET A 1 629 ? 24.737 80.349 35.972 1.00 27.22 ? 622 MET A CE 1 ATOM 4865 N N . LYS A 1 630 ? 24.633 84.051 30.877 1.00 27.54 ? 623 LYS A N 1 ATOM 4866 C CA . LYS A 1 630 ? 24.539 85.516 30.674 1.00 29.50 ? 623 LYS A CA 1 ATOM 4867 C C . LYS A 1 630 ? 23.351 85.875 29.769 1.00 30.09 ? 623 LYS A C 1 ATOM 4868 O O . LYS A 1 630 ? 22.508 86.727 30.118 1.00 29.56 ? 623 LYS A O 1 ATOM 4869 C CB . LYS A 1 630 ? 25.845 86.094 30.114 1.00 31.21 ? 623 LYS A CB 1 ATOM 4870 C CG . LYS A 1 630 ? 27.016 85.913 31.044 1.00 31.98 ? 623 LYS A CG 1 ATOM 4871 C CD . LYS A 1 630 ? 28.292 86.447 30.416 1.00 37.18 ? 623 LYS A CD 1 ATOM 4872 C CE . LYS A 1 630 ? 29.424 86.205 31.391 1.00 43.62 ? 623 LYS A CE 1 ATOM 4873 N NZ . LYS A 1 630 ? 30.697 85.813 30.761 1.00 50.20 ? 623 LYS A NZ 1 ATOM 4874 N N . THR A 1 631 ? 23.261 85.181 28.635 1.00 30.44 ? 624 THR A N 1 ATOM 4875 C CA . THR A 1 631 ? 22.219 85.442 27.629 1.00 32.12 ? 624 THR A CA 1 ATOM 4876 C C . THR A 1 631 ? 20.819 85.300 28.176 1.00 31.04 ? 624 THR A C 1 ATOM 4877 O O . THR A 1 631 ? 19.963 86.158 27.937 1.00 30.99 ? 624 THR A O 1 ATOM 4878 C CB . THR A 1 631 ? 22.398 84.516 26.387 1.00 33.13 ? 624 THR A CB 1 ATOM 4879 O OG1 . THR A 1 631 ? 23.643 84.842 25.759 1.00 37.57 ? 624 THR A OG1 1 ATOM 4880 C CG2 . THR A 1 631 ? 21.262 84.746 25.362 1.00 35.68 ? 624 THR A CG2 1 ATOM 4881 N N . TYR A 1 632 ? 20.598 84.217 28.927 1.00 28.40 ? 625 TYR A N 1 ATOM 4882 C CA . TYR A 1 632 ? 19.269 83.884 29.409 1.00 28.42 ? 625 TYR A CA 1 ATOM 4883 C C . TYR A 1 632 ? 19.030 84.281 30.859 1.00 27.59 ? 625 TYR A C 1 ATOM 4884 O O . TYR A 1 632 ? 17.999 83.932 31.410 1.00 27.17 ? 625 TYR A O 1 ATOM 4885 C CB . TYR A 1 632 ? 18.953 82.395 29.163 1.00 27.22 ? 625 TYR A CB 1 ATOM 4886 C CG . TYR A 1 632 ? 19.073 82.070 27.693 1.00 29.52 ? 625 TYR A CG 1 ATOM 4887 C CD1 . TYR A 1 632 ? 18.176 82.630 26.765 1.00 32.65 ? 625 TYR A CD1 1 ATOM 4888 C CD2 . TYR A 1 632 ? 20.078 81.233 27.228 1.00 31.35 ? 625 TYR A CD2 1 ATOM 4889 C CE1 . TYR A 1 632 ? 18.299 82.365 25.397 1.00 35.58 ? 625 TYR A CE1 1 ATOM 4890 C CE2 . TYR A 1 632 ? 20.208 80.953 25.860 1.00 33.85 ? 625 TYR A CE2 1 ATOM 4891 C CZ . TYR A 1 632 ? 19.308 81.519 24.961 1.00 36.49 ? 625 TYR A CZ 1 ATOM 4892 O OH . TYR A 1 632 ? 19.446 81.255 23.622 1.00 38.95 ? 625 TYR A OH 1 ATOM 4893 N N . SER A 1 633 ? 19.982 85.028 31.442 1.00 27.19 ? 626 SER A N 1 ATOM 4894 C CA . SER A 1 633 ? 19.858 85.538 32.813 1.00 26.83 ? 626 SER A CA 1 ATOM 4895 C C . SER A 1 633 ? 19.551 84.396 33.780 1.00 25.50 ? 626 SER A C 1 ATOM 4896 O O . SER A 1 633 ? 18.581 84.428 34.574 1.00 25.87 ? 626 SER A O 1 ATOM 4897 C CB A SER A 1 633 ? 18.777 86.620 32.914 0.65 26.87 ? 626 SER A CB 1 ATOM 4898 C CB B SER A 1 633 ? 18.764 86.601 32.868 0.35 27.16 ? 626 SER A CB 1 ATOM 4899 O OG A SER A 1 633 ? 19.131 87.737 32.127 0.65 26.04 ? 626 SER A OG 1 ATOM 4900 O OG B SER A 1 633 ? 18.890 87.353 34.043 0.35 29.01 ? 626 SER A OG 1 ATOM 4901 N N . VAL A 1 634 ? 20.377 83.363 33.703 1.00 25.25 ? 627 VAL A N 1 ATOM 4902 C CA . VAL A 1 634 ? 20.176 82.169 34.543 1.00 25.14 ? 627 VAL A CA 1 ATOM 4903 C C . VAL A 1 634 ? 20.875 82.397 35.892 1.00 26.52 ? 627 VAL A C 1 ATOM 4904 O O . VAL A 1 634 ? 22.110 82.443 35.943 1.00 27.65 ? 627 VAL A O 1 ATOM 4905 C CB . VAL A 1 634 ? 20.778 80.924 33.862 1.00 25.24 ? 627 VAL A CB 1 ATOM 4906 C CG1 . VAL A 1 634 ? 20.469 79.643 34.701 1.00 24.11 ? 627 VAL A CG1 1 ATOM 4907 C CG2 . VAL A 1 634 ? 20.232 80.797 32.439 1.00 26.75 ? 627 VAL A CG2 1 ATOM 4908 N N . SER A 1 635 ? 20.088 82.603 36.950 1.00 26.62 ? 628 SER A N 1 ATOM 4909 C CA . SER A 1 635 ? 20.658 82.862 38.281 1.00 27.34 ? 628 SER A CA 1 ATOM 4910 C C . SER A 1 635 ? 20.303 81.764 39.263 1.00 25.95 ? 628 SER A C 1 ATOM 4911 O O . SER A 1 635 ? 19.156 81.315 39.312 1.00 24.86 ? 628 SER A O 1 ATOM 4912 C CB . SER A 1 635 ? 20.160 84.180 38.867 1.00 28.34 ? 628 SER A CB 1 ATOM 4913 O OG . SER A 1 635 ? 20.859 84.359 40.095 1.00 31.92 ? 628 SER A OG 1 ATOM 4914 N N . PHE A 1 636 ? 21.292 81.343 40.050 1.00 25.74 ? 629 PHE A N 1 ATOM 4915 C CA . PHE A 1 636 ? 21.031 80.405 41.141 1.00 24.45 ? 629 PHE A CA 1 ATOM 4916 C C . PHE A 1 636 ? 20.830 81.122 42.484 1.00 24.70 ? 629 PHE A C 1 ATOM 4917 O O . PHE A 1 636 ? 20.736 80.464 43.524 1.00 23.53 ? 629 PHE A O 1 ATOM 4918 C CB . PHE A 1 636 ? 22.149 79.360 41.249 1.00 24.59 ? 629 PHE A CB 1 ATOM 4919 C CG . PHE A 1 636 ? 22.076 78.296 40.193 1.00 24.24 ? 629 PHE A CG 1 ATOM 4920 C CD1 . PHE A 1 636 ? 21.560 77.046 40.501 1.00 23.43 ? 629 PHE A CD1 1 ATOM 4921 C CD2 . PHE A 1 636 ? 22.539 78.542 38.899 1.00 26.05 ? 629 PHE A CD2 1 ATOM 4922 C CE1 . PHE A 1 636 ? 21.446 76.056 39.536 1.00 23.73 ? 629 PHE A CE1 1 ATOM 4923 C CE2 . PHE A 1 636 ? 22.444 77.548 37.923 1.00 25.29 ? 629 PHE A CE2 1 ATOM 4924 C CZ . PHE A 1 636 ? 21.900 76.309 38.252 1.00 23.47 ? 629 PHE A CZ 1 ATOM 4925 N N . ASP A 1 637 ? 20.746 82.453 42.444 1.00 24.71 ? 630 ASP A N 1 ATOM 4926 C CA . ASP A 1 637 ? 20.646 83.260 43.677 1.00 24.74 ? 630 ASP A CA 1 ATOM 4927 C C . ASP A 1 637 ? 19.495 82.790 44.560 1.00 24.16 ? 630 ASP A C 1 ATOM 4928 O O . ASP A 1 637 ? 19.660 82.676 45.783 1.00 24.58 ? 630 ASP A O 1 ATOM 4929 C CB . ASP A 1 637 ? 20.515 84.758 43.375 1.00 25.16 ? 630 ASP A CB 1 ATOM 4930 C CG . ASP A 1 637 ? 21.822 85.387 42.864 0.80 27.69 ? 630 ASP A CG 1 ATOM 4931 O OD1 . ASP A 1 637 ? 22.871 84.699 42.828 0.80 28.27 ? 630 ASP A OD1 1 ATOM 4932 O OD2 . ASP A 1 637 ? 21.773 86.591 42.506 0.80 29.91 ? 630 ASP A OD2 1 ATOM 4933 N N . SER A 1 638 ? 18.329 82.507 43.953 1.00 22.36 ? 631 SER A N 1 ATOM 4934 C CA . SER A 1 638 ? 17.186 82.057 44.762 1.00 22.22 ? 631 SER A CA 1 ATOM 4935 C C . SER A 1 638 ? 17.437 80.745 45.479 1.00 21.44 ? 631 SER A C 1 ATOM 4936 O O . SER A 1 638 ? 16.997 80.572 46.642 1.00 20.92 ? 631 SER A O 1 ATOM 4937 C CB . SER A 1 638 ? 15.912 81.957 43.916 1.00 22.03 ? 631 SER A CB 1 ATOM 4938 O OG . SER A 1 638 ? 16.064 81.009 42.865 1.00 24.58 ? 631 SER A OG 1 ATOM 4939 N N . LEU A 1 639 ? 18.104 79.805 44.806 1.00 20.08 ? 632 LEU A N 1 ATOM 4940 C CA . LEU A 1 639 ? 18.364 78.527 45.436 1.00 20.11 ? 632 LEU A CA 1 ATOM 4941 C C . LEU A 1 639 ? 19.362 78.671 46.607 1.00 21.72 ? 632 LEU A C 1 ATOM 4942 O O . LEU A 1 639 ? 19.136 78.124 47.684 1.00 20.95 ? 632 LEU A O 1 ATOM 4943 C CB . LEU A 1 639 ? 18.868 77.516 44.406 1.00 21.13 ? 632 LEU A CB 1 ATOM 4944 C CG . LEU A 1 639 ? 19.164 76.110 44.962 1.00 20.23 ? 632 LEU A CG 1 ATOM 4945 C CD1 . LEU A 1 639 ? 17.903 75.445 45.526 1.00 18.99 ? 632 LEU A CD1 1 ATOM 4946 C CD2 . LEU A 1 639 ? 19.686 75.279 43.786 1.00 20.68 ? 632 LEU A CD2 1 ATOM 4947 N N . PHE A 1 640 ? 20.437 79.434 46.402 1.00 21.13 ? 633 PHE A N 1 ATOM 4948 C CA . PHE A 1 640 ? 21.379 79.656 47.502 1.00 22.69 ? 633 PHE A CA 1 ATOM 4949 C C . PHE A 1 640 ? 20.721 80.385 48.663 1.00 22.67 ? 633 PHE A C 1 ATOM 4950 O O . PHE A 1 640 ? 21.003 80.080 49.831 1.00 24.81 ? 633 PHE A O 1 ATOM 4951 C CB . PHE A 1 640 ? 22.636 80.376 46.997 1.00 23.74 ? 633 PHE A CB 1 ATOM 4952 C CG . PHE A 1 640 ? 23.558 79.455 46.251 1.00 24.90 ? 633 PHE A CG 1 ATOM 4953 C CD1 . PHE A 1 640 ? 24.334 78.511 46.947 1.00 27.20 ? 633 PHE A CD1 1 ATOM 4954 C CD2 . PHE A 1 640 ? 23.635 79.489 44.867 1.00 27.82 ? 633 PHE A CD2 1 ATOM 4955 C CE1 . PHE A 1 640 ? 25.185 77.634 46.258 1.00 27.92 ? 633 PHE A CE1 1 ATOM 4956 C CE2 . PHE A 1 640 ? 24.500 78.609 44.174 1.00 28.97 ? 633 PHE A CE2 1 ATOM 4957 C CZ . PHE A 1 640 ? 25.261 77.676 44.887 1.00 28.06 ? 633 PHE A CZ 1 ATOM 4958 N N . SER A 1 641 ? 19.853 81.355 48.353 1.00 22.72 ? 634 SER A N 1 ATOM 4959 C CA . SER A 1 641 ? 19.102 82.064 49.394 1.00 23.40 ? 634 SER A CA 1 ATOM 4960 C C . SER A 1 641 ? 18.257 81.094 50.212 1.00 22.40 ? 634 SER A C 1 ATOM 4961 O O . SER A 1 641 ? 18.247 81.139 51.448 1.00 22.56 ? 634 SER A O 1 ATOM 4962 C CB . SER A 1 641 ? 18.197 83.134 48.773 1.00 23.11 ? 634 SER A CB 1 ATOM 4963 O OG . SER A 1 641 ? 17.421 83.793 49.776 1.00 25.27 ? 634 SER A OG 1 ATOM 4964 N N . ALA A 1 642 ? 17.529 80.219 49.521 1.00 20.98 ? 635 ALA A N 1 ATOM 4965 C CA . ALA A 1 642 ? 16.692 79.234 50.207 1.00 19.81 ? 635 ALA A CA 1 ATOM 4966 C C . ALA A 1 642 ? 17.526 78.313 51.111 1.00 20.91 ? 635 ALA A C 1 ATOM 4967 O O . ALA A 1 642 ? 17.119 77.988 52.243 1.00 21.38 ? 635 ALA A O 1 ATOM 4968 C CB . ALA A 1 642 ? 15.893 78.408 49.179 1.00 20.43 ? 635 ALA A CB 1 ATOM 4969 N N . VAL A 1 643 ? 18.689 77.892 50.606 1.00 20.96 ? 636 VAL A N 1 ATOM 4970 C CA . VAL A 1 643 ? 19.572 76.985 51.374 1.00 20.91 ? 636 VAL A CA 1 ATOM 4971 C C . VAL A 1 643 ? 20.116 77.728 52.605 1.00 22.62 ? 636 VAL A C 1 ATOM 4972 O O . VAL A 1 643 ? 20.168 77.159 53.685 1.00 22.63 ? 636 VAL A O 1 ATOM 4973 C CB . VAL A 1 643 ? 20.703 76.438 50.502 1.00 21.77 ? 636 VAL A CB 1 ATOM 4974 C CG1 . VAL A 1 643 ? 21.758 75.687 51.341 1.00 23.74 ? 636 VAL A CG1 1 ATOM 4975 C CG2 . VAL A 1 643 ? 20.095 75.492 49.454 1.00 19.88 ? 636 VAL A CG2 1 ATOM 4976 N N . LYS A 1 644 ? 20.488 78.994 52.434 1.00 23.27 ? 637 LYS A N 1 ATOM 4977 C CA . LYS A 1 644 ? 20.960 79.818 53.560 1.00 23.90 ? 637 LYS A CA 1 ATOM 4978 C C . LYS A 1 644 ? 19.841 79.934 54.599 1.00 23.60 ? 637 LYS A C 1 ATOM 4979 O O . LYS A 1 644 ? 20.082 79.777 55.798 1.00 23.76 ? 637 LYS A O 1 ATOM 4980 C CB . LYS A 1 644 ? 21.346 81.222 53.055 1.00 25.17 ? 637 LYS A CB 1 ATOM 4981 C CG . LYS A 1 644 ? 21.689 82.226 54.172 1.00 30.11 ? 637 LYS A CG 1 ATOM 4982 C CD . LYS A 1 644 ? 22.165 83.553 53.562 1.00 34.40 ? 637 LYS A CD 1 ATOM 4983 C CE . LYS A 1 644 ? 22.508 84.585 54.637 1.00 40.06 ? 637 LYS A CE 1 ATOM 4984 N NZ . LYS A 1 644 ? 21.256 85.167 55.229 1.00 41.23 ? 637 LYS A NZ 1 ATOM 4985 N N . ASN A 1 645 ? 18.607 80.186 54.134 1.00 22.72 ? 638 ASN A N 1 ATOM 4986 C CA . ASN A 1 645 ? 17.452 80.275 55.035 1.00 23.25 ? 638 ASN A CA 1 ATOM 4987 C C . ASN A 1 645 ? 17.179 78.959 55.768 1.00 22.55 ? 638 ASN A C 1 ATOM 4988 O O . ASN A 1 645 ? 16.908 78.949 56.989 1.00 23.33 ? 638 ASN A O 1 ATOM 4989 C CB . ASN A 1 645 ? 16.205 80.706 54.282 1.00 22.29 ? 638 ASN A CB 1 ATOM 4990 C CG . ASN A 1 645 ? 16.247 82.147 53.867 1.00 25.57 ? 638 ASN A CG 1 ATOM 4991 O OD1 . ASN A 1 645 ? 17.138 82.922 54.288 1.00 25.38 ? 638 ASN A OD1 1 ATOM 4992 N ND2 . ASN A 1 645 ? 15.274 82.540 53.033 1.00 23.88 ? 638 ASN A ND2 1 ATOM 4993 N N . PHE A 1 646 ? 17.262 77.839 55.042 1.00 20.88 ? 639 PHE A N 1 ATOM 4994 C CA . PHE A 1 646 ? 17.072 76.532 55.640 1.00 20.58 ? 639 PHE A CA 1 ATOM 4995 C C . PHE A 1 646 ? 18.122 76.332 56.754 1.00 21.99 ? 639 PHE A C 1 ATOM 4996 O O . PHE A 1 646 ? 17.804 75.858 57.868 1.00 22.55 ? 639 PHE A O 1 ATOM 4997 C CB . PHE A 1 646 ? 17.264 75.433 54.584 1.00 20.09 ? 639 PHE A CB 1 ATOM 4998 C CG . PHE A 1 646 ? 16.868 74.067 55.059 1.00 20.50 ? 639 PHE A CG 1 ATOM 4999 C CD1 . PHE A 1 646 ? 15.651 73.507 54.630 1.00 20.60 ? 639 PHE A CD1 1 ATOM 5000 C CD2 . PHE A 1 646 ? 17.695 73.311 55.897 1.00 20.82 ? 639 PHE A CD2 1 ATOM 5001 C CE1 . PHE A 1 646 ? 15.261 72.241 55.059 1.00 21.73 ? 639 PHE A CE1 1 ATOM 5002 C CE2 . PHE A 1 646 ? 17.305 72.028 56.345 1.00 21.73 ? 639 PHE A CE2 1 ATOM 5003 C CZ . PHE A 1 646 ? 16.069 71.490 55.935 1.00 22.05 ? 639 PHE A CZ 1 ATOM 5004 N N . THR A 1 647 ? 19.351 76.727 56.449 1.00 23.29 ? 640 THR A N 1 ATOM 5005 C CA . THR A 1 647 ? 20.474 76.562 57.411 1.00 24.38 ? 640 THR A CA 1 ATOM 5006 C C . THR A 1 647 ? 20.166 77.344 58.694 1.00 25.61 ? 640 THR A C 1 ATOM 5007 O O . THR A 1 647 ? 20.287 76.808 59.813 1.00 26.18 ? 640 THR A O 1 ATOM 5008 C CB . THR A 1 647 ? 21.806 76.991 56.787 1.00 25.12 ? 640 THR A CB 1 ATOM 5009 O OG1 . THR A 1 647 ? 22.024 76.236 55.579 1.00 25.55 ? 640 THR A OG1 1 ATOM 5010 C CG2 . THR A 1 647 ? 22.986 76.730 57.760 1.00 26.07 ? 640 THR A CG2 1 ATOM 5011 N N . GLU A 1 648 ? 19.752 78.598 58.521 1.00 25.33 ? 641 GLU A N 1 ATOM 5012 C CA . GLU A 1 648 ? 19.433 79.471 59.664 1.00 27.24 ? 641 GLU A CA 1 ATOM 5013 C C . GLU A 1 648 ? 18.247 78.947 60.476 1.00 26.32 ? 641 GLU A C 1 ATOM 5014 O O . GLU A 1 648 ? 18.302 78.849 61.710 1.00 25.95 ? 641 GLU A O 1 ATOM 5015 C CB . GLU A 1 648 ? 19.206 80.920 59.204 1.00 27.36 ? 641 GLU A CB 1 ATOM 5016 C CG . GLU A 1 648 ? 20.505 81.626 58.830 0.80 33.36 ? 641 GLU A CG 1 ATOM 5017 C CD . GLU A 1 648 ? 20.305 82.969 58.116 0.80 38.54 ? 641 GLU A CD 1 ATOM 5018 O OE1 . GLU A 1 648 ? 21.319 83.553 57.666 0.80 41.21 ? 641 GLU A OE1 1 ATOM 5019 O OE2 . GLU A 1 648 ? 19.144 83.419 57.985 0.80 43.00 ? 641 GLU A OE2 1 ATOM 5020 N N . ILE A 1 649 ? 17.169 78.575 59.786 1.00 24.52 ? 642 ILE A N 1 ATOM 5021 C CA . ILE A 1 649 ? 15.967 78.111 60.474 1.00 24.54 ? 642 ILE A CA 1 ATOM 5022 C C . ILE A 1 649 ? 16.199 76.772 61.167 1.00 24.26 ? 642 ILE A C 1 ATOM 5023 O O . ILE A 1 649 ? 15.727 76.538 62.286 1.00 24.34 ? 642 ILE A O 1 ATOM 5024 C CB . ILE A 1 649 ? 14.749 78.054 59.498 1.00 23.69 ? 642 ILE A CB 1 ATOM 5025 C CG1 . ILE A 1 649 ? 14.362 79.480 59.102 1.00 24.10 ? 642 ILE A CG1 1 ATOM 5026 C CG2 . ILE A 1 649 ? 13.541 77.361 60.140 1.00 24.99 ? 642 ILE A CG2 1 ATOM 5027 C CD1 . ILE A 1 649 ? 13.426 79.509 57.840 1.00 24.39 ? 642 ILE A CD1 1 ATOM 5028 N N . ALA A 1 650 ? 16.923 75.878 60.503 1.00 23.28 ? 643 ALA A N 1 ATOM 5029 C CA . ALA A 1 650 ? 17.230 74.580 61.105 1.00 24.32 ? 643 ALA A CA 1 ATOM 5030 C C . ALA A 1 650 ? 18.056 74.778 62.385 1.00 25.26 ? 643 ALA A C 1 ATOM 5031 O O . ALA A 1 650 ? 17.839 74.079 63.398 1.00 26.09 ? 643 ALA A O 1 ATOM 5032 C CB . ALA A 1 650 ? 18.003 73.691 60.101 1.00 25.06 ? 643 ALA A CB 1 ATOM 5033 N N . SER A 1 651 ? 18.997 75.724 62.341 1.00 26.07 ? 644 SER A N 1 ATOM 5034 C CA . SER A 1 651 ? 19.829 75.992 63.525 1.00 27.99 ? 644 SER A CA 1 ATOM 5035 C C . SER A 1 651 ? 18.951 76.463 64.690 1.00 28.48 ? 644 SER A C 1 ATOM 5036 O O . SER A 1 651 ? 19.130 76.004 65.845 1.00 29.07 ? 644 SER A O 1 ATOM 5037 C CB . SER A 1 651 ? 20.908 77.019 63.205 1.00 28.97 ? 644 SER A CB 1 ATOM 5038 O OG . SER A 1 651 ? 21.652 77.330 64.380 0.80 33.64 ? 644 SER A OG 1 ATOM 5039 N N . LYS A 1 652 ? 18.013 77.357 64.404 1.00 27.96 ? 645 LYS A N 1 ATOM 5040 C CA . LYS A 1 652 ? 17.092 77.832 65.436 1.00 29.07 ? 645 LYS A CA 1 ATOM 5041 C C . LYS A 1 652 ? 16.142 76.745 65.953 1.00 28.28 ? 645 LYS A C 1 ATOM 5042 O O . LYS A 1 652 ? 15.886 76.648 67.162 1.00 28.20 ? 645 LYS A O 1 ATOM 5043 C CB . LYS A 1 652 ? 16.351 79.074 64.969 1.00 29.29 ? 645 LYS A CB 1 ATOM 5044 C CG . LYS A 1 652 ? 17.262 80.305 64.846 1.00 32.36 ? 645 LYS A CG 1 ATOM 5045 C CD . LYS A 1 652 ? 17.755 80.772 66.225 0.75 36.27 ? 645 LYS A CD 1 ATOM 5046 C CE . LYS A 1 652 ? 18.830 81.850 66.143 0.50 37.66 ? 645 LYS A CE 1 ATOM 5047 N NZ . LYS A 1 652 ? 19.353 82.180 67.505 0.33 38.34 ? 645 LYS A NZ 1 ATOM 5048 N N . PHE A 1 653 ? 15.637 75.902 65.043 1.00 25.71 ? 646 PHE A N 1 ATOM 5049 C CA . PHE A 1 653 ? 14.815 74.782 65.449 1.00 25.67 ? 646 PHE A CA 1 ATOM 5050 C C . PHE A 1 653 ? 15.585 73.831 66.392 1.00 26.98 ? 646 PHE A C 1 ATOM 5051 O O . PHE A 1 653 ? 15.032 73.365 67.404 1.00 28.20 ? 646 PHE A O 1 ATOM 5052 C CB . PHE A 1 653 ? 14.317 74.011 64.199 1.00 24.26 ? 646 PHE A CB 1 ATOM 5053 C CG . PHE A 1 653 ? 13.484 72.806 64.524 1.00 24.63 ? 646 PHE A CG 1 ATOM 5054 C CD1 . PHE A 1 653 ? 12.108 72.933 64.757 1.00 25.14 ? 646 PHE A CD1 1 ATOM 5055 C CD2 . PHE A 1 653 ? 14.079 71.539 64.626 1.00 27.67 ? 646 PHE A CD2 1 ATOM 5056 C CE1 . PHE A 1 653 ? 11.333 71.826 65.058 1.00 27.38 ? 646 PHE A CE1 1 ATOM 5057 C CE2 . PHE A 1 653 ? 13.309 70.425 64.949 1.00 28.67 ? 646 PHE A CE2 1 ATOM 5058 C CZ . PHE A 1 653 ? 11.938 70.560 65.144 1.00 27.41 ? 646 PHE A CZ 1 ATOM 5059 N N . SER A 1 654 ? 16.844 73.550 66.066 1.00 26.97 ? 647 SER A N 1 ATOM 5060 C CA . SER A 1 654 ? 17.688 72.672 66.889 1.00 29.08 ? 647 SER A CA 1 ATOM 5061 C C . SER A 1 654 ? 17.846 73.228 68.310 1.00 30.28 ? 647 SER A C 1 ATOM 5062 O O . SER A 1 654 ? 17.840 72.456 69.283 1.00 31.00 ? 647 SER A O 1 ATOM 5063 C CB . SER A 1 654 ? 19.060 72.516 66.253 1.00 29.37 ? 647 SER A CB 1 ATOM 5064 O OG A SER A 1 654 ? 18.935 71.875 64.994 0.50 29.94 ? 647 SER A OG 1 ATOM 5065 O OG B SER A 1 654 ? 19.771 71.440 66.848 0.50 31.06 ? 647 SER A OG 1 ATOM 5066 N N . GLU A 1 655 ? 17.991 74.548 68.402 1.00 30.17 ? 648 GLU A N 1 ATOM 5067 C CA . GLU A 1 655 ? 18.092 75.218 69.724 1.00 32.38 ? 648 GLU A CA 1 ATOM 5068 C C . GLU A 1 655 ? 16.802 74.984 70.519 1.00 32.53 ? 648 GLU A C 1 ATOM 5069 O O . GLU A 1 655 ? 16.853 74.595 71.703 1.00 33.20 ? 648 GLU A O 1 ATOM 5070 C CB . GLU A 1 655 ? 18.351 76.713 69.575 1.00 33.51 ? 648 GLU A CB 1 ATOM 5071 C CG . GLU A 1 655 ? 19.659 77.105 68.910 0.80 37.21 ? 648 GLU A CG 1 ATOM 5072 C CD . GLU A 1 655 ? 19.866 78.635 68.856 0.80 43.66 ? 648 GLU A CD 1 ATOM 5073 O OE1 . GLU A 1 655 ? 19.016 79.419 69.346 0.80 44.78 ? 648 GLU A OE1 1 ATOM 5074 O OE2 . GLU A 1 655 ? 20.900 79.060 68.306 0.80 48.49 ? 648 GLU A OE2 1 ATOM 5075 N N . ARG A 1 656 ? 15.640 75.191 69.873 1.00 30.86 ? 649 ARG A N 1 ATOM 5076 C CA . ARG A 1 656 ? 14.366 74.984 70.571 1.00 31.06 ? 649 ARG A CA 1 ATOM 5077 C C . ARG A 1 656 ? 14.171 73.534 70.965 1.00 31.35 ? 649 ARG A C 1 ATOM 5078 O O . ARG A 1 656 ? 13.588 73.265 72.000 1.00 32.09 ? 649 ARG A O 1 ATOM 5079 C CB . ARG A 1 656 ? 13.166 75.477 69.747 1.00 30.63 ? 649 ARG A CB 1 ATOM 5080 C CG . ARG A 1 656 ? 13.219 76.957 69.410 1.00 30.55 ? 649 ARG A CG 1 ATOM 5081 C CD . ARG A 1 656 ? 11.849 77.488 68.969 1.00 29.85 ? 649 ARG A CD 1 ATOM 5082 N NE . ARG A 1 656 ? 11.313 76.736 67.821 1.00 29.05 ? 649 ARG A NE 1 ATOM 5083 C CZ . ARG A 1 656 ? 11.661 76.946 66.559 1.00 29.89 ? 649 ARG A CZ 1 ATOM 5084 N NH1 . ARG A 1 656 ? 12.568 77.886 66.271 1.00 28.98 ? 649 ARG A NH1 1 ATOM 5085 N NH2 . ARG A 1 656 ? 11.096 76.216 65.577 1.00 26.36 ? 649 ARG A NH2 1 ATOM 5086 N N . LEU A 1 657 ? 14.655 72.599 70.139 1.00 31.46 ? 650 LEU A N 1 ATOM 5087 C CA . LEU A 1 657 ? 14.487 71.171 70.383 1.00 33.26 ? 650 LEU A CA 1 ATOM 5088 C C . LEU A 1 657 ? 15.240 70.758 71.646 1.00 37.05 ? 650 LEU A C 1 ATOM 5089 O O . LEU A 1 657 ? 14.835 69.855 72.380 1.00 37.21 ? 650 LEU A O 1 ATOM 5090 C CB . LEU A 1 657 ? 15.017 70.371 69.167 1.00 32.84 ? 650 LEU A CB 1 ATOM 5091 C CG . LEU A 1 657 ? 14.555 68.931 69.003 1.00 33.73 ? 650 LEU A CG 1 ATOM 5092 C CD1 . LEU A 1 657 ? 13.067 68.857 68.744 1.00 31.23 ? 650 LEU A CD1 1 ATOM 5093 C CD2 . LEU A 1 657 ? 15.370 68.242 67.881 1.00 31.50 ? 650 LEU A CD2 1 ATOM 5094 N N . GLN A 1 658 ? 16.344 71.422 71.895 1.00 39.72 ? 651 GLN A N 1 ATOM 5095 C CA . GLN A 1 658 ? 17.092 71.035 73.071 1.00 44.76 ? 651 GLN A CA 1 ATOM 5096 C C . GLN A 1 658 ? 16.688 71.836 74.290 1.00 46.25 ? 651 GLN A C 1 ATOM 5097 O O . GLN A 1 658 ? 16.922 71.378 75.405 1.00 49.33 ? 651 GLN A O 1 ATOM 5098 C CB . GLN A 1 658 ? 18.593 71.005 72.806 1.00 45.68 ? 651 GLN A CB 1 ATOM 5099 C CG . GLN A 1 658 ? 19.253 72.345 72.545 1.00 49.56 ? 651 GLN A CG 1 ATOM 5100 C CD . GLN A 1 658 ? 20.573 72.176 71.810 0.70 53.11 ? 651 GLN A CD 1 ATOM 5101 O OE1 . GLN A 1 658 ? 20.857 70.941 71.353 0.65 54.18 ? 651 GLN A OE1 1 ATOM 5102 N NE2 . GLN A 1 658 ? 21.328 73.139 71.647 1.00 55.55 ? 651 GLN A NE2 1 ATOM 5103 N N . ASP A 1 659 ? 16.061 73.003 74.068 1.00 46.97 ? 652 ASP A N 1 ATOM 5104 C CA . ASP A 1 659 ? 15.641 73.972 75.115 1.00 48.40 ? 652 ASP A CA 1 ATOM 5105 C C . ASP A 1 659 ? 14.195 73.859 75.606 1.00 48.16 ? 652 ASP A C 1 ATOM 5106 O O . ASP A 1 659 ? 13.814 74.578 76.529 1.00 48.72 ? 652 ASP A O 1 ATOM 5107 C CB . ASP A 1 659 ? 15.782 75.428 74.618 1.00 48.63 ? 652 ASP A CB 1 ATOM 5108 C CG . ASP A 1 659 ? 17.205 75.953 74.687 0.80 51.80 ? 652 ASP A CG 1 ATOM 5109 O OD1 . ASP A 1 659 ? 17.419 77.096 74.215 0.80 54.35 ? 652 ASP A OD1 1 ATOM 5110 O OD2 . ASP A 1 659 ? 18.096 75.246 75.207 0.80 53.43 ? 652 ASP A OD2 1 ATOM 5111 N N . PHE A 1 660 ? 13.367 73.029 74.973 1.00 47.27 ? 653 PHE A N 1 ATOM 5112 C CA . PHE A 1 660 ? 11.957 72.952 75.388 1.00 46.74 ? 653 PHE A CA 1 ATOM 5113 C C . PHE A 1 660 ? 11.740 72.004 76.564 1.00 47.99 ? 653 PHE A C 1 ATOM 5114 O O . PHE A 1 660 ? 10.697 72.117 77.250 1.00 51.34 ? 653 PHE A O 1 ATOM 5115 C CB . PHE A 1 660 ? 11.038 72.580 74.210 1.00 44.63 ? 653 PHE A CB 1 ATOM 5116 C CG . PHE A 1 660 ? 10.942 71.100 73.934 1.00 40.55 ? 653 PHE A CG 1 ATOM 5117 C CD1 . PHE A 1 660 ? 9.877 70.359 74.428 1.00 37.48 ? 653 PHE A CD1 1 ATOM 5118 C CD2 . PHE A 1 660 ? 11.886 70.469 73.136 1.00 39.97 ? 653 PHE A CD2 1 ATOM 5119 C CE1 . PHE A 1 660 ? 9.742 69.017 74.140 1.00 39.15 ? 653 PHE A CE1 1 ATOM 5120 C CE2 . PHE A 1 660 ? 11.782 69.107 72.848 1.00 41.53 ? 653 PHE A CE2 1 ATOM 5121 C CZ . PHE A 1 660 ? 10.702 68.379 73.343 1.00 42.35 ? 653 PHE A CZ 1 ATOM 5122 N N A SER A 1 663 ? 8.977 68.857 79.834 0.50 30.49 ? 656 SER A N 1 ATOM 5123 N N B SER A 1 663 ? 8.028 66.357 78.905 0.50 28.63 ? 656 SER A N 1 ATOM 5124 C CA A SER A 1 663 ? 7.730 68.511 80.470 0.50 31.39 ? 656 SER A CA 1 ATOM 5125 C CA B SER A 1 663 ? 6.895 65.869 79.726 0.50 28.11 ? 656 SER A CA 1 ATOM 5126 C C A SER A 1 663 ? 6.487 68.500 79.551 0.50 28.65 ? 656 SER A C 1 ATOM 5127 C C B SER A 1 663 ? 5.540 66.448 79.410 0.50 28.44 ? 656 SER A C 1 ATOM 5128 O O A SER A 1 663 ? 5.460 67.917 79.890 0.50 28.50 ? 656 SER A O 1 ATOM 5129 O O B SER A 1 663 ? 4.526 66.066 80.006 0.50 28.38 ? 656 SER A O 1 ATOM 5130 C CB A SER A 1 663 ? 7.468 69.520 81.571 0.50 30.37 ? 656 SER A CB 1 ATOM 5131 C CB B SER A 1 663 ? 7.148 66.104 81.200 0.50 29.86 ? 656 SER A CB 1 ATOM 5132 O OG A SER A 1 663 ? 7.005 68.838 82.701 0.50 39.63 ? 656 SER A OG 1 ATOM 5133 O OG B SER A 1 663 ? 7.611 64.914 81.661 0.50 28.07 ? 656 SER A OG 1 ATOM 5134 N N A ASN A 1 664 ? 6.555 69.173 78.414 0.50 28.21 ? 657 ASN A N 1 ATOM 5135 N N B ASN A 1 664 ? 5.527 67.393 78.492 0.50 28.46 ? 657 ASN A N 1 ATOM 5136 C CA A ASN A 1 664 ? 5.354 69.404 77.621 0.50 27.18 ? 657 ASN A CA 1 ATOM 5137 C CA B ASN A 1 664 ? 4.293 67.985 78.049 0.50 29.80 ? 657 ASN A CA 1 ATOM 5138 C C A ASN A 1 664 ? 5.230 68.473 76.425 0.50 26.40 ? 657 ASN A C 1 ATOM 5139 C C B ASN A 1 664 ? 3.885 67.243 76.775 0.50 28.98 ? 657 ASN A C 1 ATOM 5140 O O A ASN A 1 664 ? 6.007 68.568 75.482 0.50 25.84 ? 657 ASN A O 1 ATOM 5141 O O B ASN A 1 664 ? 4.423 67.510 75.707 0.50 28.89 ? 657 ASN A O 1 ATOM 5142 C CB A ASN A 1 664 ? 5.298 70.861 77.183 0.50 26.93 ? 657 ASN A CB 1 ATOM 5143 C CB B ASN A 1 664 ? 4.550 69.467 77.795 0.50 29.83 ? 657 ASN A CB 1 ATOM 5144 C CG A ASN A 1 664 ? 3.947 71.237 76.654 0.50 27.49 ? 657 ASN A CG 1 ATOM 5145 C CG B ASN A 1 664 ? 3.303 70.223 77.441 0.50 32.36 ? 657 ASN A CG 1 ATOM 5146 O OD1 A ASN A 1 664 ? 3.343 70.480 75.906 0.50 25.63 ? 657 ASN A OD1 1 ATOM 5147 O OD1 B ASN A 1 664 ? 2.439 69.709 76.729 0.50 33.76 ? 657 ASN A OD1 1 ATOM 5148 N ND2 A ASN A 1 664 ? 3.447 72.390 77.069 0.50 30.36 ? 657 ASN A ND2 1 ATOM 5149 N ND2 B ASN A 1 664 ? 3.213 71.466 77.903 0.50 32.55 ? 657 ASN A ND2 1 ATOM 5150 N N A PRO A 1 665 ? 4.264 67.539 76.478 0.50 25.70 ? 658 PRO A N 1 ATOM 5151 N N B PRO A 1 665 ? 2.951 66.277 76.889 0.50 29.28 ? 658 PRO A N 1 ATOM 5152 C CA A PRO A 1 665 ? 4.167 66.512 75.440 0.50 24.55 ? 658 PRO A CA 1 ATOM 5153 C CA B PRO A 1 665 ? 2.608 65.416 75.741 0.50 28.51 ? 658 PRO A CA 1 ATOM 5154 C C A PRO A 1 665 ? 3.596 67.065 74.130 0.50 23.65 ? 658 PRO A C 1 ATOM 5155 C C B PRO A 1 665 ? 2.320 66.157 74.425 0.50 27.67 ? 658 PRO A C 1 ATOM 5156 O O A PRO A 1 665 ? 3.831 66.465 73.078 0.50 21.66 ? 658 PRO A O 1 ATOM 5157 O O B PRO A 1 665 ? 2.792 65.724 73.376 0.50 26.71 ? 658 PRO A O 1 ATOM 5158 C CB A PRO A 1 665 ? 3.190 65.499 76.056 0.50 25.14 ? 658 PRO A CB 1 ATOM 5159 C CB B PRO A 1 665 ? 1.352 64.687 76.215 0.50 29.37 ? 658 PRO A CB 1 ATOM 5160 C CG A PRO A 1 665 ? 2.264 66.388 76.876 0.50 25.26 ? 658 PRO A CG 1 ATOM 5161 C CG B PRO A 1 665 ? 1.479 64.677 77.733 0.50 29.83 ? 658 PRO A CG 1 ATOM 5162 C CD A PRO A 1 665 ? 3.208 67.398 77.502 0.50 27.15 ? 658 PRO A CD 1 ATOM 5163 C CD B PRO A 1 665 ? 2.154 65.962 78.090 0.50 30.02 ? 658 PRO A CD 1 ATOM 5164 N N A ILE A 1 666 ? 2.839 68.165 74.183 0.50 23.86 ? 659 ILE A N 1 ATOM 5165 N N B ILE A 1 666 ? 1.553 67.241 74.450 0.50 27.46 ? 659 ILE A N 1 ATOM 5166 C CA A ILE A 1 666 ? 2.319 68.791 72.953 0.50 24.63 ? 659 ILE A CA 1 ATOM 5167 C CA B ILE A 1 666 ? 1.214 67.916 73.182 0.50 27.04 ? 659 ILE A CA 1 ATOM 5168 C C A ILE A 1 666 ? 3.450 69.507 72.207 0.50 24.09 ? 659 ILE A C 1 ATOM 5169 C C B ILE A 1 666 ? 2.359 68.769 72.649 0.50 26.01 ? 659 ILE A C 1 ATOM 5170 O O A ILE A 1 666 ? 3.531 69.416 70.997 0.50 23.13 ? 659 ILE A O 1 ATOM 5171 O O B ILE A 1 666 ? 2.552 68.885 71.436 0.50 25.39 ? 659 ILE A O 1 ATOM 5172 C CB A ILE A 1 666 ? 1.197 69.856 73.174 0.50 25.75 ? 659 ILE A CB 1 ATOM 5173 C CB B ILE A 1 666 ? -0.110 68.706 73.247 0.50 27.24 ? 659 ILE A CB 1 ATOM 5174 C CG1 A ILE A 1 666 ? 0.103 69.373 74.131 0.50 27.84 ? 659 ILE A CG1 1 ATOM 5175 C CG1 B ILE A 1 666 ? -1.266 67.721 73.375 0.50 29.21 ? 659 ILE A CG1 1 ATOM 5176 C CG2 A ILE A 1 666 ? 0.624 70.303 71.821 0.50 24.56 ? 659 ILE A CG2 1 ATOM 5177 C CG2 B ILE A 1 666 ? -0.292 69.554 72.022 0.50 28.51 ? 659 ILE A CG2 1 ATOM 5178 C CD1 A ILE A 1 666 ? -0.136 67.893 74.087 0.50 30.83 ? 659 ILE A CD1 1 ATOM 5179 C CD1 B ILE A 1 666 ? -0.997 66.411 72.691 0.50 29.01 ? 659 ILE A CD1 1 ATOM 5180 N N A VAL A 1 667 ? 4.291 70.239 72.937 0.50 24.15 ? 660 VAL A N 1 ATOM 5181 N N B VAL A 1 667 ? 3.146 69.372 73.538 0.50 25.96 ? 660 VAL A N 1 ATOM 5182 C CA A VAL A 1 667 ? 5.451 70.881 72.329 0.50 24.78 ? 660 VAL A CA 1 ATOM 5183 C CA B VAL A 1 667 ? 4.325 70.100 73.040 0.50 24.28 ? 660 VAL A CA 1 ATOM 5184 C C A VAL A 1 667 ? 6.386 69.811 71.755 0.50 23.84 ? 660 VAL A C 1 ATOM 5185 C C B VAL A 1 667 ? 5.332 69.136 72.377 0.50 23.55 ? 660 VAL A C 1 ATOM 5186 O O A VAL A 1 667 ? 6.907 69.945 70.635 0.50 23.91 ? 660 VAL A O 1 ATOM 5187 O O B VAL A 1 667 ? 5.898 69.433 71.316 0.50 22.67 ? 660 VAL A O 1 ATOM 5188 C CB A VAL A 1 667 ? 6.198 71.796 73.330 0.50 25.34 ? 660 VAL A CB 1 ATOM 5189 C CB B VAL A 1 667 ? 4.985 70.966 74.131 0.50 25.74 ? 660 VAL A CB 1 ATOM 5190 C CG1 A VAL A 1 667 ? 7.484 72.340 72.697 0.50 27.06 ? 660 VAL A CG1 1 ATOM 5191 C CG1 B VAL A 1 667 ? 6.355 71.505 73.658 0.50 24.75 ? 660 VAL A CG1 1 ATOM 5192 C CG2 A VAL A 1 667 ? 5.277 72.923 73.774 0.50 26.78 ? 660 VAL A CG2 1 ATOM 5193 C CG2 B VAL A 1 667 ? 4.067 72.113 74.511 0.50 26.11 ? 660 VAL A CG2 1 ATOM 5194 N N A LEU A 1 668 ? 6.577 68.736 72.522 0.50 23.79 ? 661 LEU A N 1 ATOM 5195 N N B LEU A 1 668 ? 5.518 67.965 72.972 0.50 22.39 ? 661 LEU A N 1 ATOM 5196 C CA A LEU A 1 668 ? 7.388 67.602 72.085 0.50 22.94 ? 661 LEU A CA 1 ATOM 5197 C CA B LEU A 1 668 ? 6.415 66.959 72.412 0.50 22.36 ? 661 LEU A CA 1 ATOM 5198 C C A LEU A 1 668 ? 6.838 67.055 70.775 0.50 22.89 ? 661 LEU A C 1 ATOM 5199 C C B LEU A 1 668 ? 5.855 66.498 71.081 0.50 22.29 ? 661 LEU A C 1 ATOM 5200 O O A LEU A 1 668 ? 7.574 66.953 69.809 0.50 21.11 ? 661 LEU A O 1 ATOM 5201 O O B LEU A 1 668 ? 6.589 66.259 70.115 0.50 21.42 ? 661 LEU A O 1 ATOM 5202 C CB A LEU A 1 668 ? 7.456 66.514 73.174 0.50 24.37 ? 661 LEU A CB 1 ATOM 5203 C CB B LEU A 1 668 ? 6.550 65.773 73.374 0.50 22.69 ? 661 LEU A CB 1 ATOM 5204 C CG A LEU A 1 668 ? 7.998 65.142 72.743 0.50 23.92 ? 661 LEU A CG 1 ATOM 5205 C CG B LEU A 1 668 ? 7.425 64.597 72.908 0.50 24.36 ? 661 LEU A CG 1 ATOM 5206 C CD1 A LEU A 1 668 ? 9.399 65.244 72.172 0.50 22.51 ? 661 LEU A CD1 1 ATOM 5207 C CD1 B LEU A 1 668 ? 8.849 65.006 72.521 0.50 23.65 ? 661 LEU A CD1 1 ATOM 5208 C CD2 A LEU A 1 668 ? 7.943 64.166 73.911 0.50 23.77 ? 661 LEU A CD2 1 ATOM 5209 C CD2 B LEU A 1 668 ? 7.440 63.571 74.024 0.50 23.02 ? 661 LEU A CD2 1 ATOM 5210 N N A ARG A 1 669 ? 5.544 66.725 70.762 0.50 22.51 ? 662 ARG A N 1 ATOM 5211 N N B ARG A 1 669 ? 4.545 66.367 71.020 0.50 22.25 ? 662 ARG A N 1 ATOM 5212 C CA A ARG A 1 669 ? 4.930 66.038 69.625 0.50 22.54 ? 662 ARG A CA 1 ATOM 5213 C CA B ARG A 1 669 ? 3.957 65.976 69.733 0.50 22.57 ? 662 ARG A CA 1 ATOM 5214 C C A ARG A 1 669 ? 4.800 67.020 68.503 0.50 22.84 ? 662 ARG A C 1 ATOM 5215 C C B ARG A 1 669 ? 4.253 66.946 68.561 0.50 22.96 ? 662 ARG A C 1 ATOM 5216 O O A ARG A 1 669 ? 5.063 66.676 67.355 0.50 21.37 ? 662 ARG A O 1 ATOM 5217 O O B ARG A 1 669 ? 4.404 66.489 67.443 0.50 21.90 ? 662 ARG A O 1 ATOM 5218 C CB A ARG A 1 669 ? 3.553 65.480 69.992 0.50 22.03 ? 662 ARG A CB 1 ATOM 5219 C CB B ARG A 1 669 ? 2.473 65.652 69.875 0.50 22.50 ? 662 ARG A CB 1 ATOM 5220 C CG A ARG A 1 669 ? 2.667 65.134 68.809 0.50 21.99 ? 662 ARG A CG 1 ATOM 5221 C CG B ARG A 1 669 ? 1.839 65.157 68.597 0.50 23.17 ? 662 ARG A CG 1 ATOM 5222 C CD A ARG A 1 669 ? 3.021 63.812 68.126 0.50 19.08 ? 662 ARG A CD 1 ATOM 5223 C CD B ARG A 1 669 ? 1.937 63.650 68.406 0.50 28.55 ? 662 ARG A CD 1 ATOM 5224 N NE A ARG A 1 669 ? 1.823 63.411 67.388 0.50 24.10 ? 662 ARG A NE 1 ATOM 5225 N NE B ARG A 1 669 ? 0.771 63.260 67.607 0.50 27.12 ? 662 ARG A NE 1 ATOM 5226 C CZ A ARG A 1 669 ? 1.253 62.213 67.460 0.50 23.75 ? 662 ARG A CZ 1 ATOM 5227 C CZ B ARG A 1 669 ? 0.388 62.017 67.360 0.50 25.79 ? 662 ARG A CZ 1 ATOM 5228 N NH1 A ARG A 1 669 ? 1.822 61.225 68.148 0.50 25.74 ? 662 ARG A NH1 1 ATOM 5229 N NH1 B ARG A 1 669 ? 1.095 60.977 67.804 0.50 28.08 ? 662 ARG A NH1 1 ATOM 5230 N NH2 A ARG A 1 669 ? 0.130 62.000 66.789 0.50 25.21 ? 662 ARG A NH2 1 ATOM 5231 N NH2 B ARG A 1 669 ? -0.702 61.830 66.633 0.50 26.68 ? 662 ARG A NH2 1 ATOM 5232 N N . MET A 1 670 ? 4.405 68.256 68.822 1.00 23.96 ? 663 MET A N 1 ATOM 5233 C CA . MET A 1 670 ? 4.530 69.310 67.775 1.00 24.50 ? 663 MET A CA 1 ATOM 5234 C C . MET A 1 670 ? 5.929 69.289 67.165 1.00 24.87 ? 663 MET A C 1 ATOM 5235 O O . MET A 1 670 ? 6.099 69.316 65.958 1.00 22.86 ? 663 MET A O 1 ATOM 5236 C CB A MET A 1 670 ? 4.349 70.722 68.367 0.50 24.76 ? 663 MET A CB 1 ATOM 5237 C CB B MET A 1 670 ? 4.028 70.674 68.312 0.50 25.65 ? 663 MET A CB 1 ATOM 5238 C CG A MET A 1 670 ? 4.855 71.893 67.459 0.50 23.37 ? 663 MET A CG 1 ATOM 5239 C CG B MET A 1 670 ? 2.530 70.586 68.832 0.50 26.13 ? 663 MET A CG 1 ATOM 5240 S SD A MET A 1 670 ? 4.555 73.524 68.208 0.50 22.48 ? 663 MET A SD 1 ATOM 5241 S SD B MET A 1 670 ? 1.548 72.037 69.380 0.50 28.32 ? 663 MET A SD 1 ATOM 5242 C CE A MET A 1 670 ? 2.871 73.244 68.723 0.50 27.82 ? 663 MET A CE 1 ATOM 5243 C CE B MET A 1 670 ? 2.453 72.518 70.895 0.50 22.35 ? 663 MET A CE 1 ATOM 5244 N N . MET A 1 671 ? 6.972 69.192 68.000 1.00 23.65 ? 664 MET A N 1 ATOM 5245 C CA . MET A 1 671 ? 8.311 69.191 67.453 1.00 24.33 ? 664 MET A CA 1 ATOM 5246 C C . MET A 1 671 ? 8.622 67.876 66.740 1.00 23.12 ? 664 MET A C 1 ATOM 5247 O O . MET A 1 671 ? 9.341 67.870 65.742 1.00 24.57 ? 664 MET A O 1 ATOM 5248 C CB A MET A 1 671 ? 9.299 69.268 68.643 0.50 25.25 ? 664 MET A CB 1 ATOM 5249 C CB B MET A 1 671 ? 9.389 69.623 68.471 0.50 24.30 ? 664 MET A CB 1 ATOM 5250 C CG A MET A 1 671 ? 8.956 70.313 69.685 0.50 29.01 ? 664 MET A CG 1 ATOM 5251 C CG B MET A 1 671 ? 9.296 71.103 68.824 0.50 23.37 ? 664 MET A CG 1 ATOM 5252 S SD A MET A 1 671 ? 9.054 71.880 68.856 0.50 32.68 ? 664 MET A SD 1 ATOM 5253 S SD B MET A 1 671 ? 10.729 71.787 69.709 0.50 23.52 ? 664 MET A SD 1 ATOM 5254 C CE A MET A 1 671 ? 10.692 72.435 69.313 0.50 30.76 ? 664 MET A CE 1 ATOM 5255 C CE B MET A 1 671 ? 11.716 72.298 68.304 0.50 20.93 ? 664 MET A CE 1 ATOM 5256 N N . ASN A 1 672 ? 8.114 66.776 67.285 1.00 23.19 ? 665 ASN A N 1 ATOM 5257 C CA . ASN A 1 672 ? 8.279 65.460 66.611 1.00 22.53 ? 665 ASN A CA 1 ATOM 5258 C C . ASN A 1 672 ? 7.564 65.484 65.255 1.00 22.55 ? 665 ASN A C 1 ATOM 5259 O O . ASN A 1 672 ? 8.107 64.958 64.291 1.00 21.35 ? 665 ASN A O 1 ATOM 5260 C CB . ASN A 1 672 ? 7.787 64.301 67.473 1.00 23.84 ? 665 ASN A CB 1 ATOM 5261 C CG . ASN A 1 672 ? 8.858 63.812 68.437 1.00 23.48 ? 665 ASN A CG 1 ATOM 5262 O OD1 . ASN A 1 672 ? 10.059 64.002 68.195 1.00 24.26 ? 665 ASN A OD1 1 ATOM 5263 N ND2 . ASN A 1 672 ? 8.438 63.197 69.521 1.00 24.50 ? 665 ASN A ND2 1 ATOM 5264 N N . ASP A 1 673 ? 6.393 66.115 65.195 1.00 22.90 ? 666 ASP A N 1 ATOM 5265 C CA . ASP A 1 673 ? 5.678 66.233 63.895 1.00 22.34 ? 666 ASP A CA 1 ATOM 5266 C C . ASP A 1 673 ? 6.503 67.096 62.920 1.00 22.35 ? 666 ASP A C 1 ATOM 5267 O O . ASP A 1 673 ? 6.593 66.786 61.738 1.00 21.94 ? 666 ASP A O 1 ATOM 5268 C CB . ASP A 1 673 ? 4.284 66.814 64.063 1.00 22.31 ? 666 ASP A CB 1 ATOM 5269 C CG . ASP A 1 673 ? 3.285 65.809 64.611 1.00 23.24 ? 666 ASP A CG 1 ATOM 5270 O OD1 . ASP A 1 673 ? 3.652 64.615 64.758 1.00 24.87 ? 666 ASP A OD1 1 ATOM 5271 O OD2 . ASP A 1 673 ? 2.135 66.229 64.876 1.00 24.55 ? 666 ASP A OD2 1 ATOM 5272 N N . GLN A 1 674 ? 7.104 68.179 63.411 1.00 20.95 ? 667 GLN A N 1 ATOM 5273 C CA . GLN A 1 674 ? 7.988 68.974 62.544 1.00 20.97 ? 667 GLN A CA 1 ATOM 5274 C C . GLN A 1 674 ? 9.156 68.130 62.020 1.00 21.14 ? 667 GLN A C 1 ATOM 5275 O O . GLN A 1 674 ? 9.517 68.231 60.865 1.00 21.19 ? 667 GLN A O 1 ATOM 5276 C CB . GLN A 1 674 ? 8.494 70.227 63.271 1.00 21.02 ? 667 GLN A CB 1 ATOM 5277 C CG . GLN A 1 674 ? 7.361 71.274 63.441 1.00 20.63 ? 667 GLN A CG 1 ATOM 5278 C CD . GLN A 1 674 ? 7.851 72.503 64.155 1.00 22.85 ? 667 GLN A CD 1 ATOM 5279 O OE1 . GLN A 1 674 ? 7.952 72.488 65.365 1.00 25.18 ? 667 GLN A OE1 1 ATOM 5280 N NE2 . GLN A 1 674 ? 8.120 73.600 63.408 1.00 22.52 ? 667 GLN A NE2 1 ATOM 5281 N N . LEU A 1 675 ? 9.749 67.300 62.879 1.00 21.90 ? 668 LEU A N 1 ATOM 5282 C CA . LEU A 1 675 ? 10.810 66.403 62.422 1.00 21.55 ? 668 LEU A CA 1 ATOM 5283 C C . LEU A 1 675 ? 10.330 65.367 61.409 1.00 20.92 ? 668 LEU A C 1 ATOM 5284 O O . LEU A 1 675 ? 11.000 65.133 60.374 1.00 22.50 ? 668 LEU A O 1 ATOM 5285 C CB . LEU A 1 675 ? 11.424 65.692 63.639 1.00 22.64 ? 668 LEU A CB 1 ATOM 5286 C CG . LEU A 1 675 ? 12.329 66.669 64.439 1.00 25.56 ? 668 LEU A CG 1 ATOM 5287 C CD1 . LEU A 1 675 ? 12.766 66.005 65.746 1.00 28.08 ? 668 LEU A CD1 1 ATOM 5288 C CD2 . LEU A 1 675 ? 13.545 67.140 63.632 1.00 28.70 ? 668 LEU A CD2 1 ATOM 5289 N N . MET A 1 676 ? 9.158 64.795 61.696 1.00 21.62 ? 669 MET A N 1 ATOM 5290 C CA . MET A 1 676 ? 8.599 63.741 60.819 1.00 20.73 ? 669 MET A CA 1 ATOM 5291 C C . MET A 1 676 ? 8.209 64.297 59.445 1.00 19.78 ? 669 MET A C 1 ATOM 5292 O O . MET A 1 676 ? 8.451 63.651 58.417 1.00 19.81 ? 669 MET A O 1 ATOM 5293 C CB . MET A 1 676 ? 7.353 63.153 61.461 1.00 21.61 ? 669 MET A CB 1 ATOM 5294 C CG . MET A 1 676 ? 6.660 62.051 60.566 1.00 22.47 ? 669 MET A CG 1 ATOM 5295 S SD . MET A 1 676 ? 5.255 61.292 61.401 1.00 25.35 ? 669 MET A SD 1 ATOM 5296 C CE . MET A 1 676 ? 4.019 62.626 61.276 1.00 23.09 ? 669 MET A CE 1 ATOM 5297 N N . PHE A 1 677 ? 7.611 65.478 59.449 1.00 18.71 ? 670 PHE A N 1 ATOM 5298 C CA . PHE A 1 677 ? 7.120 66.077 58.180 1.00 18.88 ? 670 PHE A CA 1 ATOM 5299 C C . PHE A 1 677 ? 8.195 66.836 57.405 1.00 18.73 ? 670 PHE A C 1 ATOM 5300 O O . PHE A 1 677 ? 7.927 67.373 56.321 1.00 18.92 ? 670 PHE A O 1 ATOM 5301 C CB . PHE A 1 677 ? 5.897 66.962 58.433 1.00 18.25 ? 670 PHE A CB 1 ATOM 5302 C CG . PHE A 1 677 ? 4.631 66.188 58.717 1.00 19.14 ? 670 PHE A CG 1 ATOM 5303 C CD1 . PHE A 1 677 ? 4.113 65.269 57.774 1.00 19.91 ? 670 PHE A CD1 1 ATOM 5304 C CD2 . PHE A 1 677 ? 3.923 66.406 59.919 1.00 20.00 ? 670 PHE A CD2 1 ATOM 5305 C CE1 . PHE A 1 677 ? 2.936 64.565 58.023 1.00 19.64 ? 670 PHE A CE1 1 ATOM 5306 C CE2 . PHE A 1 677 ? 2.690 65.724 60.180 1.00 22.50 ? 670 PHE A CE2 1 ATOM 5307 C CZ . PHE A 1 677 ? 2.203 64.781 59.224 1.00 20.46 ? 670 PHE A CZ 1 ATOM 5308 N N . LEU A 1 678 ? 9.428 66.886 57.933 1.00 18.84 ? 671 LEU A N 1 ATOM 5309 C CA . LEU A 1 678 ? 10.501 67.590 57.226 1.00 18.80 ? 671 LEU A CA 1 ATOM 5310 C C . LEU A 1 678 ? 10.883 66.855 55.919 1.00 18.04 ? 671 LEU A C 1 ATOM 5311 O O . LEU A 1 678 ? 10.952 67.479 54.852 1.00 18.35 ? 671 LEU A O 1 ATOM 5312 C CB . LEU A 1 678 ? 11.737 67.791 58.156 1.00 20.34 ? 671 LEU A CB 1 ATOM 5313 C CG . LEU A 1 678 ? 12.893 68.500 57.488 1.00 21.09 ? 671 LEU A CG 1 ATOM 5314 C CD1 . LEU A 1 678 ? 12.542 69.880 56.908 1.00 22.83 ? 671 LEU A CD1 1 ATOM 5315 C CD2 . LEU A 1 678 ? 14.123 68.569 58.506 1.00 23.18 ? 671 LEU A CD2 1 ATOM 5316 N N . GLU A 1 679 ? 11.124 65.545 55.988 1.00 18.09 ? 672 GLU A N 1 ATOM 5317 C CA . GLU A 1 679 ? 11.330 64.808 54.743 1.00 17.43 ? 672 GLU A CA 1 ATOM 5318 C C . GLU A 1 679 ? 10.109 64.996 53.811 1.00 16.68 ? 672 GLU A C 1 ATOM 5319 O O . GLU A 1 679 ? 10.249 65.133 52.556 1.00 17.06 ? 672 GLU A O 1 ATOM 5320 C CB . GLU A 1 679 ? 11.521 63.300 55.003 1.00 17.43 ? 672 GLU A CB 1 ATOM 5321 C CG . GLU A 1 679 ? 12.095 62.622 53.774 1.00 16.72 ? 672 GLU A CG 1 ATOM 5322 C CD . GLU A 1 679 ? 13.602 62.875 53.650 1.00 18.93 ? 672 GLU A CD 1 ATOM 5323 O OE1 . GLU A 1 679 ? 14.326 62.437 54.548 1.00 19.32 ? 672 GLU A OE1 1 ATOM 5324 O OE2 . GLU A 1 679 ? 14.033 63.551 52.678 1.00 18.41 ? 672 GLU A OE2 1 ATOM 5325 N N . ARG A 1 680 ? 8.926 65.012 54.412 1.00 16.72 ? 673 ARG A N 1 ATOM 5326 C CA . ARG A 1 680 ? 7.674 65.098 53.632 1.00 16.08 ? 673 ARG A CA 1 ATOM 5327 C C . ARG A 1 680 ? 7.634 66.427 52.851 1.00 16.07 ? 673 ARG A C 1 ATOM 5328 O O . ARG A 1 680 ? 7.039 66.519 51.764 1.00 16.40 ? 673 ARG A O 1 ATOM 5329 C CB . ARG A 1 680 ? 6.439 64.987 54.554 1.00 17.51 ? 673 ARG A CB 1 ATOM 5330 C CG . ARG A 1 680 ? 5.216 64.323 53.822 1.00 15.80 ? 673 ARG A CG 1 ATOM 5331 C CD . ARG A 1 680 ? 5.321 62.805 53.970 1.00 17.04 ? 673 ARG A CD 1 ATOM 5332 N NE . ARG A 1 680 ? 4.945 62.316 55.312 1.00 15.15 ? 673 ARG A NE 1 ATOM 5333 C CZ . ARG A 1 680 ? 5.764 61.776 56.214 1.00 17.55 ? 673 ARG A CZ 1 ATOM 5334 N NH1 . ARG A 1 680 ? 7.093 61.670 56.024 1.00 17.69 ? 673 ARG A NH1 1 ATOM 5335 N NH2 . ARG A 1 680 ? 5.225 61.359 57.356 1.00 18.77 ? 673 ARG A NH2 1 ATOM 5336 N N . ALA A 1 681 ? 8.259 67.466 53.422 1.00 16.09 ? 674 ALA A N 1 ATOM 5337 C CA . ALA A 1 681 ? 8.183 68.781 52.792 1.00 16.48 ? 674 ALA A CA 1 ATOM 5338 C C . ALA A 1 681 ? 8.915 68.862 51.485 1.00 16.97 ? 674 ALA A C 1 ATOM 5339 O O . ALA A 1 681 ? 8.653 69.790 50.704 1.00 18.71 ? 674 ALA A O 1 ATOM 5340 C CB . ALA A 1 681 ? 8.703 69.841 53.766 1.00 16.62 ? 674 ALA A CB 1 ATOM 5341 N N . PHE A 1 682 ? 9.802 67.901 51.211 1.00 16.75 ? 675 PHE A N 1 ATOM 5342 C CA . PHE A 1 682 ? 10.537 67.953 49.937 1.00 16.28 ? 675 PHE A CA 1 ATOM 5343 C C . PHE A 1 682 ? 9.753 67.355 48.801 1.00 17.00 ? 675 PHE A C 1 ATOM 5344 O O . PHE A 1 682 ? 10.221 67.411 47.666 1.00 17.04 ? 675 PHE A O 1 ATOM 5345 C CB . PHE A 1 682 ? 11.904 67.261 50.052 1.00 16.74 ? 675 PHE A CB 1 ATOM 5346 C CG . PHE A 1 682 ? 12.838 68.004 50.963 1.00 17.23 ? 675 PHE A CG 1 ATOM 5347 C CD1 . PHE A 1 682 ? 13.290 69.275 50.630 1.00 17.18 ? 675 PHE A CD1 1 ATOM 5348 C CD2 . PHE A 1 682 ? 13.232 67.428 52.165 1.00 19.53 ? 675 PHE A CD2 1 ATOM 5349 C CE1 . PHE A 1 682 ? 14.183 69.986 51.505 1.00 18.57 ? 675 PHE A CE1 1 ATOM 5350 C CE2 . PHE A 1 682 ? 14.109 68.134 53.043 1.00 21.09 ? 675 PHE A CE2 1 ATOM 5351 C CZ . PHE A 1 682 ? 14.568 69.408 52.696 1.00 21.16 ? 675 PHE A CZ 1 ATOM 5352 N N . ILE A 1 683 ? 8.565 66.844 49.097 1.00 16.64 ? 676 ILE A N 1 ATOM 5353 C CA . ILE A 1 683 ? 7.680 66.256 48.073 1.00 16.99 ? 676 ILE A CA 1 ATOM 5354 C C . ILE A 1 683 ? 6.974 67.383 47.300 1.00 17.84 ? 676 ILE A C 1 ATOM 5355 O O . ILE A 1 683 ? 6.418 68.304 47.915 1.00 19.26 ? 676 ILE A O 1 ATOM 5356 C CB . ILE A 1 683 ? 6.635 65.317 48.747 1.00 16.99 ? 676 ILE A CB 1 ATOM 5357 C CG1 . ILE A 1 683 ? 7.360 64.079 49.319 1.00 16.58 ? 676 ILE A CG1 1 ATOM 5358 C CG2 . ILE A 1 683 ? 5.488 64.931 47.755 1.00 17.33 ? 676 ILE A CG2 1 ATOM 5359 C CD1 . ILE A 1 683 ? 8.184 63.251 48.247 1.00 15.95 ? 676 ILE A CD1 1 ATOM 5360 N N . ASP A 1 684 ? 6.987 67.306 45.966 1.00 16.66 ? 677 ASP A N 1 ATOM 5361 C CA . ASP A 1 684 ? 6.179 68.192 45.098 1.00 17.98 ? 677 ASP A CA 1 ATOM 5362 C C . ASP A 1 684 ? 5.018 67.361 44.545 1.00 18.27 ? 677 ASP A C 1 ATOM 5363 O O . ASP A 1 684 ? 5.253 66.352 43.899 1.00 17.13 ? 677 ASP A O 1 ATOM 5364 C CB . ASP A 1 684 ? 7.040 68.675 43.941 1.00 18.05 ? 677 ASP A CB 1 ATOM 5365 C CG . ASP A 1 684 ? 6.347 69.714 43.078 1.00 17.03 ? 677 ASP A CG 1 ATOM 5366 O OD1 . ASP A 1 684 ? 5.103 69.719 42.999 1.00 18.82 ? 677 ASP A OD1 1 ATOM 5367 O OD2 . ASP A 1 684 ? 7.097 70.512 42.467 1.00 19.34 ? 677 ASP A OD2 1 ATOM 5368 N N . PRO A 1 685 ? 3.779 67.729 44.851 1.00 20.25 ? 678 PRO A N 1 ATOM 5369 C CA . PRO A 1 685 ? 2.653 66.891 44.447 1.00 22.35 ? 678 PRO A CA 1 ATOM 5370 C C . PRO A 1 685 ? 2.499 66.843 42.914 1.00 23.09 ? 678 PRO A C 1 ATOM 5371 O O . PRO A 1 685 ? 1.782 65.997 42.397 1.00 26.13 ? 678 PRO A O 1 ATOM 5372 C CB . PRO A 1 685 ? 1.433 67.601 45.098 1.00 22.20 ? 678 PRO A CB 1 ATOM 5373 C CG . PRO A 1 685 ? 1.828 68.968 45.311 1.00 24.09 ? 678 PRO A CG 1 ATOM 5374 C CD . PRO A 1 685 ? 3.348 68.962 45.552 1.00 20.87 ? 678 PRO A CD 1 ATOM 5375 N N . LEU A 1 686 ? 3.216 67.693 42.180 1.00 20.46 ? 679 LEU A N 1 ATOM 5376 C CA . LEU A 1 686 ? 3.158 67.607 40.703 1.00 19.29 ? 679 LEU A CA 1 ATOM 5377 C C . LEU A 1 686 ? 4.222 66.658 40.104 1.00 20.17 ? 679 LEU A C 1 ATOM 5378 O O . LEU A 1 686 ? 4.196 66.373 38.900 1.00 19.42 ? 679 LEU A O 1 ATOM 5379 C CB . LEU A 1 686 ? 3.346 69.003 40.115 1.00 20.06 ? 679 LEU A CB 1 ATOM 5380 C CG . LEU A 1 686 ? 2.228 69.995 40.527 1.00 20.66 ? 679 LEU A CG 1 ATOM 5381 C CD1 . LEU A 1 686 ? 2.429 71.342 39.887 1.00 20.82 ? 679 LEU A CD1 1 ATOM 5382 C CD2 . LEU A 1 686 ? 0.817 69.444 40.146 1.00 23.64 ? 679 LEU A CD2 1 ATOM 5383 N N . GLY A 1 687 ? 5.135 66.162 40.940 1.00 19.13 ? 680 GLY A N 1 ATOM 5384 C CA . GLY A 1 687 ? 6.172 65.219 40.510 1.00 19.12 ? 680 GLY A CA 1 ATOM 5385 C C . GLY A 1 687 ? 7.239 65.905 39.683 1.00 19.88 ? 680 GLY A C 1 ATOM 5386 O O . GLY A 1 687 ? 7.150 67.093 39.403 1.00 21.39 ? 680 GLY A O 1 ATOM 5387 N N . LEU A 1 688 ? 8.219 65.132 39.239 1.00 19.05 ? 681 LEU A N 1 ATOM 5388 C CA . LEU A 1 688 ? 9.230 65.615 38.312 1.00 20.63 ? 681 LEU A CA 1 ATOM 5389 C C . LEU A 1 688 ? 8.743 65.431 36.874 1.00 20.64 ? 681 LEU A C 1 ATOM 5390 O O . LEU A 1 688 ? 7.832 64.623 36.611 1.00 20.55 ? 681 LEU A O 1 ATOM 5391 C CB . LEU A 1 688 ? 10.552 64.837 38.560 1.00 20.07 ? 681 LEU A CB 1 ATOM 5392 C CG . LEU A 1 688 ? 11.215 65.212 39.914 1.00 20.81 ? 681 LEU A CG 1 ATOM 5393 C CD1 . LEU A 1 688 ? 12.293 64.205 40.277 1.00 23.28 ? 681 LEU A CD1 1 ATOM 5394 C CD2 . LEU A 1 688 ? 11.807 66.673 39.910 1.00 24.44 ? 681 LEU A CD2 1 ATOM 5395 N N . PRO A 1 689 ? 9.332 66.174 35.913 1.00 22.21 ? 682 PRO A N 1 ATOM 5396 C CA . PRO A 1 689 ? 8.839 66.113 34.531 1.00 22.71 ? 682 PRO A CA 1 ATOM 5397 C C . PRO A 1 689 ? 8.742 64.703 33.968 1.00 22.18 ? 682 PRO A C 1 ATOM 5398 O O . PRO A 1 689 ? 9.730 63.949 33.950 1.00 22.58 ? 682 PRO A O 1 ATOM 5399 C CB . PRO A 1 689 ? 9.872 66.989 33.744 1.00 23.02 ? 682 PRO A CB 1 ATOM 5400 C CG . PRO A 1 689 ? 10.358 67.950 34.784 1.00 24.05 ? 682 PRO A CG 1 ATOM 5401 C CD . PRO A 1 689 ? 10.438 67.136 36.066 1.00 23.66 ? 682 PRO A CD 1 ATOM 5402 N N . ASP A 1 690 ? 7.525 64.329 33.551 1.00 21.99 ? 683 ASP A N 1 ATOM 5403 C CA . ASP A 1 690 ? 7.230 63.031 32.952 1.00 23.35 ? 683 ASP A CA 1 ATOM 5404 C C . ASP A 1 690 ? 7.504 61.835 33.870 1.00 21.39 ? 683 ASP A C 1 ATOM 5405 O O . ASP A 1 690 ? 7.447 60.690 33.416 1.00 21.07 ? 683 ASP A O 1 ATOM 5406 C CB . ASP A 1 690 ? 7.949 62.832 31.612 1.00 25.02 ? 683 ASP A CB 1 ATOM 5407 C CG . ASP A 1 690 ? 7.585 63.902 30.606 1.00 33.32 ? 683 ASP A CG 1 ATOM 5408 O OD1 . ASP A 1 690 ? 6.374 64.187 30.424 1.00 35.60 ? 683 ASP A OD1 1 ATOM 5409 O OD2 . ASP A 1 690 ? 8.530 64.455 30.001 1.00 39.22 ? 683 ASP A OD2 1 ATOM 5410 N N . ARG A 1 691 ? 7.748 62.105 35.155 1.00 19.36 ? 684 ARG A N 1 ATOM 5411 C CA . ARG A 1 691 ? 7.964 61.038 36.159 1.00 18.62 ? 684 ARG A CA 1 ATOM 5412 C C . ARG A 1 691 ? 7.124 61.376 37.413 1.00 17.84 ? 684 ARG A C 1 ATOM 5413 O O . ARG A 1 691 ? 7.653 61.798 38.458 1.00 17.14 ? 684 ARG A O 1 ATOM 5414 C CB . ARG A 1 691 ? 9.459 60.888 36.513 1.00 18.41 ? 684 ARG A CB 1 ATOM 5415 C CG . ARG A 1 691 ? 10.279 60.426 35.291 1.00 18.35 ? 684 ARG A CG 1 ATOM 5416 C CD . ARG A 1 691 ? 11.705 59.986 35.656 1.00 18.53 ? 684 ARG A CD 1 ATOM 5417 N NE . ARG A 1 691 ? 12.467 61.129 36.202 1.00 19.01 ? 684 ARG A NE 1 ATOM 5418 C CZ . ARG A 1 691 ? 13.631 61.034 36.852 1.00 19.47 ? 684 ARG A CZ 1 ATOM 5419 N NH1 . ARG A 1 691 ? 14.235 59.850 37.016 1.00 18.48 ? 684 ARG A NH1 1 ATOM 5420 N NH2 . ARG A 1 691 ? 14.208 62.154 37.325 1.00 19.71 ? 684 ARG A NH2 1 ATOM 5421 N N . PRO A 1 692 ? 5.809 61.183 37.307 1.00 17.67 ? 685 PRO A N 1 ATOM 5422 C CA . PRO A 1 692 ? 4.890 61.658 38.351 1.00 17.94 ? 685 PRO A CA 1 ATOM 5423 C C . PRO A 1 692 ? 5.049 60.973 39.698 1.00 16.88 ? 685 PRO A C 1 ATOM 5424 O O . PRO A 1 692 ? 4.576 61.526 40.697 1.00 17.82 ? 685 PRO A O 1 ATOM 5425 C CB . PRO A 1 692 ? 3.480 61.376 37.775 1.00 19.42 ? 685 PRO A CB 1 ATOM 5426 C CG . PRO A 1 692 ? 3.684 60.294 36.725 1.00 19.28 ? 685 PRO A CG 1 ATOM 5427 C CD . PRO A 1 692 ? 5.090 60.613 36.145 1.00 18.00 ? 685 PRO A CD 1 ATOM 5428 N N . PHE A 1 693 ? 5.672 59.800 39.727 1.00 16.59 ? 686 PHE A N 1 ATOM 5429 C CA . PHE A 1 693 ? 5.906 59.073 40.989 1.00 16.21 ? 686 PHE A CA 1 ATOM 5430 C C . PHE A 1 693 ? 7.265 59.330 41.626 1.00 16.26 ? 686 PHE A C 1 ATOM 5431 O O . PHE A 1 693 ? 7.510 58.834 42.724 1.00 16.88 ? 686 PHE A O 1 ATOM 5432 C CB . PHE A 1 693 ? 5.621 57.559 40.804 1.00 16.80 ? 686 PHE A CB 1 ATOM 5433 C CG . PHE A 1 693 ? 4.212 57.313 40.318 1.00 16.69 ? 686 PHE A CG 1 ATOM 5434 C CD1 . PHE A 1 693 ? 3.121 57.733 41.087 1.00 17.40 ? 686 PHE A CD1 1 ATOM 5435 C CD2 . PHE A 1 693 ? 3.987 56.730 39.060 1.00 17.79 ? 686 PHE A CD2 1 ATOM 5436 C CE1 . PHE A 1 693 ? 1.807 57.530 40.640 1.00 16.84 ? 686 PHE A CE1 1 ATOM 5437 C CE2 . PHE A 1 693 ? 2.699 56.541 38.584 1.00 18.73 ? 686 PHE A CE2 1 ATOM 5438 C CZ . PHE A 1 693 ? 1.604 56.938 39.383 1.00 17.05 ? 686 PHE A CZ 1 ATOM 5439 N N . TYR A 1 694 ? 8.072 60.168 40.986 1.00 15.65 ? 687 TYR A N 1 ATOM 5440 C CA . TYR A 1 694 ? 9.295 60.688 41.623 1.00 15.33 ? 687 TYR A CA 1 ATOM 5441 C C . TYR A 1 694 ? 8.962 62.095 42.013 1.00 16.01 ? 687 TYR A C 1 ATOM 5442 O O . TYR A 1 694 ? 8.990 63.025 41.180 1.00 17.38 ? 687 TYR A O 1 ATOM 5443 C CB . TYR A 1 694 ? 10.503 60.612 40.658 1.00 15.34 ? 687 TYR A CB 1 ATOM 5444 C CG . TYR A 1 694 ? 10.969 59.184 40.383 1.00 16.18 ? 687 TYR A CG 1 ATOM 5445 C CD1 . TYR A 1 694 ? 10.691 58.131 41.277 1.00 16.26 ? 687 TYR A CD1 1 ATOM 5446 C CD2 . TYR A 1 694 ? 11.686 58.902 39.215 1.00 16.80 ? 687 TYR A CD2 1 ATOM 5447 C CE1 . TYR A 1 694 ? 11.123 56.813 40.998 1.00 15.67 ? 687 TYR A CE1 1 ATOM 5448 C CE2 . TYR A 1 694 ? 12.105 57.603 38.940 1.00 18.01 ? 687 TYR A CE2 1 ATOM 5449 C CZ . TYR A 1 694 ? 11.837 56.586 39.842 1.00 16.65 ? 687 TYR A CZ 1 ATOM 5450 O OH . TYR A 1 694 ? 12.325 55.310 39.557 1.00 17.74 ? 687 TYR A OH 1 ATOM 5451 N N A ARG A 1 695 ? 8.628 62.280 43.294 0.70 14.93 ? 688 ARG A N 1 ATOM 5452 N N B ARG A 1 695 ? 8.603 62.261 43.287 0.30 15.57 ? 688 ARG A N 1 ATOM 5453 C CA A ARG A 1 695 ? 8.078 63.570 43.754 0.70 14.47 ? 688 ARG A CA 1 ATOM 5454 C CA B ARG A 1 695 ? 8.035 63.519 43.773 0.30 15.36 ? 688 ARG A CA 1 ATOM 5455 C C A ARG A 1 695 ? 9.036 64.343 44.640 0.70 15.33 ? 688 ARG A C 1 ATOM 5456 C C B ARG A 1 695 ? 8.981 64.295 44.694 0.30 15.63 ? 688 ARG A C 1 ATOM 5457 O O A ARG A 1 695 ? 8.817 65.530 44.902 0.70 16.83 ? 688 ARG A O 1 ATOM 5458 O O B ARG A 1 695 ? 8.707 65.454 45.017 0.30 16.35 ? 688 ARG A O 1 ATOM 5459 C CB A ARG A 1 695 ? 6.767 63.331 44.510 0.70 14.78 ? 688 ARG A CB 1 ATOM 5460 C CB B ARG A 1 695 ? 6.692 63.254 44.479 0.30 15.57 ? 688 ARG A CB 1 ATOM 5461 C CG A ARG A 1 695 ? 5.780 62.609 43.557 0.70 15.28 ? 688 ARG A CG 1 ATOM 5462 C CG B ARG A 1 695 ? 5.658 62.524 43.564 0.30 15.62 ? 688 ARG A CG 1 ATOM 5463 C CD A ARG A 1 695 ? 4.352 62.746 44.035 0.70 15.13 ? 688 ARG A CD 1 ATOM 5464 C CD B ARG A 1 695 ? 4.349 62.205 44.316 0.30 15.65 ? 688 ARG A CD 1 ATOM 5465 N NE A ARG A 1 695 ? 4.191 62.295 45.421 0.70 16.33 ? 688 ARG A NE 1 ATOM 5466 N NE B ARG A 1 695 ? 3.306 61.491 43.545 0.30 13.62 ? 688 ARG A NE 1 ATOM 5467 C CZ A ARG A 1 695 ? 3.140 62.553 46.195 0.70 18.04 ? 688 ARG A CZ 1 ATOM 5468 C CZ B ARG A 1 695 ? 2.284 60.844 44.129 0.30 14.96 ? 688 ARG A CZ 1 ATOM 5469 N NH1 A ARG A 1 695 ? 3.150 62.141 47.493 0.70 14.15 ? 688 ARG A NH1 1 ATOM 5470 N NH1 B ARG A 1 695 ? 2.218 60.809 45.442 0.30 17.08 ? 688 ARG A NH1 1 ATOM 5471 N NH2 A ARG A 1 695 ? 2.083 63.234 45.701 0.70 19.38 ? 688 ARG A NH2 1 ATOM 5472 N NH2 B ARG A 1 695 ? 1.343 60.192 43.448 0.30 7.37 ? 688 ARG A NH2 1 ATOM 5473 N N . HIS A 1 696 ? 10.081 63.659 45.108 1.00 15.39 ? 689 HIS A N 1 ATOM 5474 C CA . HIS A 1 696 ? 11.045 64.311 46.003 1.00 15.28 ? 689 HIS A CA 1 ATOM 5475 C C . HIS A 1 696 ? 11.915 65.265 45.146 1.00 16.01 ? 689 HIS A C 1 ATOM 5476 O O . HIS A 1 696 ? 12.448 64.873 44.122 1.00 16.77 ? 689 HIS A O 1 ATOM 5477 C CB . HIS A 1 696 ? 11.901 63.222 46.669 1.00 15.79 ? 689 HIS A CB 1 ATOM 5478 C CG . HIS A 1 696 ? 12.580 63.663 47.930 1.00 15.89 ? 689 HIS A CG 1 ATOM 5479 N ND1 . HIS A 1 696 ? 13.581 64.618 47.972 1.00 16.60 ? 689 HIS A ND1 1 ATOM 5480 C CD2 . HIS A 1 696 ? 12.432 63.205 49.194 1.00 17.21 ? 689 HIS A CD2 1 ATOM 5481 C CE1 . HIS A 1 696 ? 14.007 64.746 49.222 1.00 18.32 ? 689 HIS A CE1 1 ATOM 5482 N NE2 . HIS A 1 696 ? 13.324 63.899 49.987 1.00 16.92 ? 689 HIS A NE2 1 ATOM 5483 N N . VAL A 1 697 ? 12.015 66.529 45.557 1.00 15.48 ? 690 VAL A N 1 ATOM 5484 C CA . VAL A 1 697 ? 12.671 67.544 44.714 1.00 16.08 ? 690 VAL A CA 1 ATOM 5485 C C . VAL A 1 697 ? 14.194 67.491 44.946 1.00 16.88 ? 690 VAL A C 1 ATOM 5486 O O . VAL A 1 697 ? 14.972 67.948 44.097 1.00 17.35 ? 690 VAL A O 1 ATOM 5487 C CB . VAL A 1 697 ? 12.068 68.946 45.060 1.00 16.04 ? 690 VAL A CB 1 ATOM 5488 C CG1 . VAL A 1 697 ? 12.873 70.096 44.422 1.00 17.41 ? 690 VAL A CG1 1 ATOM 5489 C CG2 . VAL A 1 697 ? 10.627 69.017 44.580 1.00 17.17 ? 690 VAL A CG2 1 ATOM 5490 N N . ILE A 1 698 ? 14.631 66.943 46.081 1.00 16.83 ? 691 ILE A N 1 ATOM 5491 C CA . ILE A 1 698 ? 16.093 66.896 46.311 1.00 17.27 ? 691 ILE A CA 1 ATOM 5492 C C . ILE A 1 698 ? 16.734 65.654 45.698 1.00 17.61 ? 691 ILE A C 1 ATOM 5493 O O . ILE A 1 698 ? 17.849 65.723 45.201 1.00 18.13 ? 691 ILE A O 1 ATOM 5494 C CB . ILE A 1 698 ? 16.460 66.927 47.835 1.00 18.64 ? 691 ILE A CB 1 ATOM 5495 C CG1 . ILE A 1 698 ? 15.691 68.054 48.554 1.00 17.76 ? 691 ILE A CG1 1 ATOM 5496 C CG2 . ILE A 1 698 ? 17.997 67.108 48.058 1.00 20.07 ? 691 ILE A CG2 1 ATOM 5497 C CD1 . ILE A 1 698 ? 15.849 69.472 47.940 1.00 19.03 ? 691 ILE A CD1 1 ATOM 5498 N N . TYR A 1 699 ? 16.039 64.519 45.786 1.00 17.85 ? 692 TYR A N 1 ATOM 5499 C CA . TYR A 1 699 ? 16.585 63.229 45.346 1.00 17.34 ? 692 TYR A CA 1 ATOM 5500 C C . TYR A 1 699 ? 15.644 62.514 44.388 1.00 18.17 ? 692 TYR A C 1 ATOM 5501 O O . TYR A 1 699 ? 14.471 62.276 44.729 1.00 19.96 ? 692 TYR A O 1 ATOM 5502 C CB . TYR A 1 699 ? 16.736 62.305 46.568 1.00 17.76 ? 692 TYR A CB 1 ATOM 5503 C CG . TYR A 1 699 ? 17.768 62.758 47.586 1.00 18.41 ? 692 TYR A CG 1 ATOM 5504 C CD1 . TYR A 1 699 ? 19.138 62.815 47.244 1.00 20.62 ? 692 TYR A CD1 1 ATOM 5505 C CD2 . TYR A 1 699 ? 17.402 63.085 48.908 1.00 18.96 ? 692 TYR A CD2 1 ATOM 5506 C CE1 . TYR A 1 699 ? 20.093 63.194 48.172 1.00 20.15 ? 692 TYR A CE1 1 ATOM 5507 C CE2 . TYR A 1 699 ? 18.373 63.461 49.855 1.00 19.88 ? 692 TYR A CE2 1 ATOM 5508 C CZ . TYR A 1 699 ? 19.708 63.506 49.480 1.00 21.38 ? 692 TYR A CZ 1 ATOM 5509 O OH . TYR A 1 699 ? 20.694 63.844 50.397 1.00 21.65 ? 692 TYR A OH 1 ATOM 5510 N N . ALA A 1 700 ? 16.182 62.050 43.254 1.00 17.15 ? 693 ALA A N 1 ATOM 5511 C CA . ALA A 1 700 ? 15.453 61.073 42.438 1.00 16.97 ? 693 ALA A CA 1 ATOM 5512 C C . ALA A 1 700 ? 16.439 60.067 41.890 1.00 17.30 ? 693 ALA A C 1 ATOM 5513 O O . ALA A 1 700 ? 17.643 60.323 41.861 1.00 18.74 ? 693 ALA A O 1 ATOM 5514 C CB . ALA A 1 700 ? 14.695 61.765 41.268 1.00 17.06 ? 693 ALA A CB 1 ATOM 5515 N N . PRO A 1 701 ? 15.956 58.885 41.506 1.00 17.44 ? 694 PRO A N 1 ATOM 5516 C CA . PRO A 1 701 ? 16.856 57.985 40.801 1.00 17.89 ? 694 PRO A CA 1 ATOM 5517 C C . PRO A 1 701 ? 17.344 58.643 39.525 1.00 18.43 ? 694 PRO A C 1 ATOM 5518 O O . PRO A 1 701 ? 16.556 59.330 38.852 1.00 18.99 ? 694 PRO A O 1 ATOM 5519 C CB . PRO A 1 701 ? 15.953 56.799 40.437 1.00 18.56 ? 694 PRO A CB 1 ATOM 5520 C CG . PRO A 1 701 ? 14.864 56.855 41.458 1.00 17.89 ? 694 PRO A CG 1 ATOM 5521 C CD . PRO A 1 701 ? 14.581 58.351 41.586 1.00 18.31 ? 694 PRO A CD 1 ATOM 5522 N N . SER A 1 702 ? 18.626 58.456 39.189 1.00 18.25 ? 695 SER A N 1 ATOM 5523 C CA . SER A 1 702 ? 19.152 59.049 37.976 1.00 18.58 ? 695 SER A CA 1 ATOM 5524 C C . SER A 1 702 ? 18.351 58.622 36.751 1.00 19.48 ? 695 SER A C 1 ATOM 5525 O O . SER A 1 702 ? 18.087 57.436 36.562 1.00 19.50 ? 695 SER A O 1 ATOM 5526 C CB . SER A 1 702 ? 20.633 58.620 37.753 1.00 19.08 ? 695 SER A CB 1 ATOM 5527 O OG . SER A 1 702 ? 21.059 59.083 36.487 1.00 21.08 ? 695 SER A OG 1 ATOM 5528 N N . SER A 1 703 ? 18.021 59.573 35.876 1.00 18.66 ? 696 SER A N 1 ATOM 5529 C CA . SER A 1 703 ? 17.313 59.248 34.625 1.00 19.63 ? 696 SER A CA 1 ATOM 5530 C C . SER A 1 703 ? 18.155 58.362 33.687 1.00 20.37 ? 696 SER A C 1 ATOM 5531 O O . SER A 1 703 ? 17.610 57.796 32.718 1.00 21.49 ? 696 SER A O 1 ATOM 5532 C CB . SER A 1 703 ? 16.908 60.552 33.897 1.00 19.78 ? 696 SER A CB 1 ATOM 5533 O OG A SER A 1 703 ? 15.910 61.264 34.606 0.50 13.63 ? 696 SER A OG 1 ATOM 5534 O OG B SER A 1 703 ? 18.027 61.212 33.349 0.50 26.57 ? 696 SER A OG 1 ATOM 5535 N N . HIS A 1 704 ? 19.439 58.245 33.978 1.00 20.02 ? 697 HIS A N 1 ATOM 5536 C CA . HIS A 1 704 ? 20.373 57.396 33.186 1.00 21.03 ? 697 HIS A CA 1 ATOM 5537 C C . HIS A 1 704 ? 20.709 56.090 33.854 1.00 21.51 ? 697 HIS A C 1 ATOM 5538 O O . HIS A 1 704 ? 21.338 55.208 33.240 1.00 23.07 ? 697 HIS A O 1 ATOM 5539 C CB . HIS A 1 704 ? 21.665 58.196 32.868 1.00 22.07 ? 697 HIS A CB 1 ATOM 5540 C CG . HIS A 1 704 ? 21.367 59.496 32.192 1.00 23.92 ? 697 HIS A CG 1 ATOM 5541 N ND1 . HIS A 1 704 ? 21.133 59.584 30.837 1.00 24.76 ? 697 HIS A ND1 1 ATOM 5542 C CD2 . HIS A 1 704 ? 21.146 60.734 32.695 1.00 26.10 ? 697 HIS A CD2 1 ATOM 5543 C CE1 . HIS A 1 704 ? 20.801 60.824 30.529 1.00 26.30 ? 697 HIS A CE1 1 ATOM 5544 N NE2 . HIS A 1 704 ? 20.810 61.546 31.639 1.00 25.78 ? 697 HIS A NE2 1 ATOM 5545 N N . ASN A 1 705 ? 20.297 55.935 35.110 1.00 20.00 ? 698 ASN A N 1 ATOM 5546 C CA . ASN A 1 705 ? 20.693 54.761 35.889 1.00 20.43 ? 698 ASN A CA 1 ATOM 5547 C C . ASN A 1 705 ? 19.877 54.725 37.170 1.00 19.85 ? 698 ASN A C 1 ATOM 5548 O O . ASN A 1 705 ? 20.211 55.394 38.150 1.00 19.34 ? 698 ASN A O 1 ATOM 5549 C CB . ASN A 1 705 ? 22.187 54.849 36.251 1.00 21.46 ? 698 ASN A CB 1 ATOM 5550 C CG . ASN A 1 705 ? 22.614 53.740 37.216 1.00 21.10 ? 698 ASN A CG 1 ATOM 5551 O OD1 . ASN A 1 705 ? 21.886 52.755 37.367 1.00 20.07 ? 698 ASN A OD1 1 ATOM 5552 N ND2 . ASN A 1 705 ? 23.778 53.902 37.870 1.00 23.25 ? 698 ASN A ND2 1 ATOM 5553 N N . LYS A 1 706 ? 18.824 53.924 37.164 1.00 19.27 ? 699 LYS A N 1 ATOM 5554 C CA . LYS A 1 706 ? 17.908 53.831 38.311 1.00 18.84 ? 699 LYS A CA 1 ATOM 5555 C C . LYS A 1 706 ? 18.607 53.542 39.639 1.00 19.14 ? 699 LYS A C 1 ATOM 5556 O O . LYS A 1 706 ? 18.119 53.946 40.711 1.00 18.54 ? 699 LYS A O 1 ATOM 5557 C CB . LYS A 1 706 ? 16.885 52.724 38.006 1.00 19.70 ? 699 LYS A CB 1 ATOM 5558 C CG . LYS A 1 706 ? 15.796 52.593 39.062 1.00 20.84 ? 699 LYS A CG 1 ATOM 5559 C CD . LYS A 1 706 ? 14.787 51.544 38.590 1.00 18.65 ? 699 LYS A CD 1 ATOM 5560 C CE . LYS A 1 706 ? 13.481 51.744 39.401 1.00 19.10 ? 699 LYS A CE 1 ATOM 5561 N NZ . LYS A 1 706 ? 12.580 50.591 39.072 1.00 20.63 ? 699 LYS A NZ 1 ATOM 5562 N N . TYR A 1 707 ? 19.744 52.846 39.607 1.00 19.25 ? 700 TYR A N 1 ATOM 5563 C CA . TYR A 1 707 ? 20.408 52.504 40.879 1.00 18.61 ? 700 TYR A CA 1 ATOM 5564 C C . TYR A 1 707 ? 21.030 53.698 41.583 1.00 20.16 ? 700 TYR A C 1 ATOM 5565 O O . TYR A 1 707 ? 21.225 53.643 42.803 1.00 21.50 ? 700 TYR A O 1 ATOM 5566 C CB . TYR A 1 707 ? 21.529 51.505 40.652 1.00 19.73 ? 700 TYR A CB 1 ATOM 5567 C CG . TYR A 1 707 ? 21.084 50.119 40.201 1.00 18.76 ? 700 TYR A CG 1 ATOM 5568 C CD1 . TYR A 1 707 ? 19.955 49.491 40.737 1.00 19.62 ? 700 TYR A CD1 1 ATOM 5569 C CD2 . TYR A 1 707 ? 21.882 49.399 39.296 1.00 19.82 ? 700 TYR A CD2 1 ATOM 5570 C CE1 . TYR A 1 707 ? 19.593 48.173 40.329 1.00 18.94 ? 700 TYR A CE1 1 ATOM 5571 C CE2 . TYR A 1 707 ? 21.541 48.083 38.895 1.00 19.21 ? 700 TYR A CE2 1 ATOM 5572 C CZ . TYR A 1 707 ? 20.410 47.494 39.426 1.00 21.51 ? 700 TYR A CZ 1 ATOM 5573 O OH . TYR A 1 707 ? 20.094 46.220 39.027 1.00 20.91 ? 700 TYR A OH 1 ATOM 5574 N N . ALA A 1 708 ? 21.429 54.724 40.824 1.00 20.11 ? 701 ALA A N 1 ATOM 5575 C CA . ALA A 1 708 ? 22.168 55.849 41.411 1.00 20.35 ? 701 ALA A CA 1 ATOM 5576 C C . ALA A 1 708 ? 21.224 56.975 41.815 1.00 21.15 ? 701 ALA A C 1 ATOM 5577 O O . ALA A 1 708 ? 20.273 57.270 41.093 1.00 21.37 ? 701 ALA A O 1 ATOM 5578 C CB . ALA A 1 708 ? 23.170 56.385 40.393 1.00 20.60 ? 701 ALA A CB 1 ATOM 5579 N N . GLY A 1 709 ? 21.486 57.632 42.944 1.00 19.92 ? 702 GLY A N 1 ATOM 5580 C CA . GLY A 1 709 ? 20.665 58.819 43.234 1.00 20.87 ? 702 GLY A CA 1 ATOM 5581 C C . GLY A 1 709 ? 21.244 60.045 42.539 1.00 20.96 ? 702 GLY A C 1 ATOM 5582 O O . GLY A 1 709 ? 22.472 60.131 42.325 1.00 22.22 ? 702 GLY A O 1 ATOM 5583 N N . GLU A 1 710 ? 20.365 60.961 42.140 1.00 19.50 ? 703 GLU A N 1 ATOM 5584 C CA . GLU A 1 710 ? 20.781 62.251 41.594 1.00 19.11 ? 703 GLU A CA 1 ATOM 5585 C C . GLU A 1 710 ? 20.246 63.317 42.546 1.00 19.24 ? 703 GLU A C 1 ATOM 5586 O O . GLU A 1 710 ? 19.128 63.199 43.007 1.00 18.89 ? 703 GLU A O 1 ATOM 5587 C CB . GLU A 1 710 ? 20.180 62.457 40.195 1.00 20.36 ? 703 GLU A CB 1 ATOM 5588 C CG . GLU A 1 710 ? 20.795 63.701 39.470 1.00 20.58 ? 703 GLU A CG 1 ATOM 5589 C CD . GLU A 1 710 ? 22.332 63.662 39.551 1.00 24.40 ? 703 GLU A CD 1 ATOM 5590 O OE1 . GLU A 1 710 ? 22.930 62.872 38.786 1.00 22.44 ? 703 GLU A OE1 1 ATOM 5591 O OE2 . GLU A 1 710 ? 22.954 64.358 40.420 1.00 25.45 ? 703 GLU A OE2 1 ATOM 5592 N N . SER A 1 711 ? 21.038 64.344 42.838 1.00 19.56 ? 704 SER A N 1 ATOM 5593 C CA . SER A 1 711 ? 20.539 65.460 43.646 1.00 19.00 ? 704 SER A CA 1 ATOM 5594 C C . SER A 1 711 ? 20.031 66.590 42.753 1.00 19.17 ? 704 SER A C 1 ATOM 5595 O O . SER A 1 711 ? 20.526 66.746 41.626 1.00 18.92 ? 704 SER A O 1 ATOM 5596 C CB . SER A 1 711 ? 21.633 65.977 44.605 1.00 20.17 ? 704 SER A CB 1 ATOM 5597 O OG . SER A 1 711 ? 22.856 66.284 43.903 1.00 22.25 ? 704 SER A OG 1 ATOM 5598 N N . PHE A 1 712 ? 19.053 67.370 43.253 1.00 18.42 ? 705 PHE A N 1 ATOM 5599 C CA . PHE A 1 712 ? 18.331 68.388 42.437 1.00 17.92 ? 705 PHE A CA 1 ATOM 5600 C C . PHE A 1 712 ? 18.080 67.847 41.013 1.00 17.89 ? 705 PHE A C 1 ATOM 5601 O O . PHE A 1 712 ? 18.481 68.458 40.017 1.00 17.53 ? 705 PHE A O 1 ATOM 5602 C CB . PHE A 1 712 ? 19.084 69.720 42.401 1.00 18.35 ? 705 PHE A CB 1 ATOM 5603 C CG . PHE A 1 712 ? 19.030 70.465 43.725 1.00 17.88 ? 705 PHE A CG 1 ATOM 5604 C CD1 . PHE A 1 712 ? 17.795 70.791 44.306 1.00 19.13 ? 705 PHE A CD1 1 ATOM 5605 C CD2 . PHE A 1 712 ? 20.213 70.811 44.383 1.00 19.09 ? 705 PHE A CD2 1 ATOM 5606 C CE1 . PHE A 1 712 ? 17.726 71.468 45.536 1.00 19.71 ? 705 PHE A CE1 1 ATOM 5607 C CE2 . PHE A 1 712 ? 20.166 71.484 45.602 1.00 19.86 ? 705 PHE A CE2 1 ATOM 5608 C CZ . PHE A 1 712 ? 18.933 71.824 46.189 1.00 19.75 ? 705 PHE A CZ 1 ATOM 5609 N N . PRO A 1 713 ? 17.412 66.691 40.932 1.00 17.40 ? 706 PRO A N 1 ATOM 5610 C CA . PRO A 1 713 ? 17.231 65.978 39.665 1.00 17.53 ? 706 PRO A CA 1 ATOM 5611 C C . PRO A 1 713 ? 16.522 66.805 38.620 1.00 18.31 ? 706 PRO A C 1 ATOM 5612 O O . PRO A 1 713 ? 16.818 66.661 37.429 1.00 19.22 ? 706 PRO A O 1 ATOM 5613 C CB . PRO A 1 713 ? 16.338 64.764 40.043 1.00 16.57 ? 706 PRO A CB 1 ATOM 5614 C CG . PRO A 1 713 ? 15.696 65.158 41.376 1.00 17.33 ? 706 PRO A CG 1 ATOM 5615 C CD . PRO A 1 713 ? 16.783 65.972 42.061 1.00 17.20 ? 706 PRO A CD 1 ATOM 5616 N N . GLY A 1 714 ? 15.578 67.656 39.043 1.00 17.31 ? 707 GLY A N 1 ATOM 5617 C CA . GLY A 1 714 ? 14.861 68.457 38.051 1.00 18.34 ? 707 GLY A CA 1 ATOM 5618 C C . GLY A 1 714 ? 15.822 69.388 37.318 1.00 18.48 ? 707 GLY A C 1 ATOM 5619 O O . GLY A 1 714 ? 15.763 69.519 36.053 1.00 19.36 ? 707 GLY A O 1 ATOM 5620 N N . ILE A 1 715 ? 16.690 70.077 38.077 1.00 17.96 ? 708 ILE A N 1 ATOM 5621 C CA . ILE A 1 715 ? 17.675 70.971 37.437 1.00 18.64 ? 708 ILE A CA 1 ATOM 5622 C C . ILE A 1 715 ? 18.705 70.154 36.688 1.00 20.09 ? 708 ILE A C 1 ATOM 5623 O O . ILE A 1 715 ? 19.096 70.522 35.572 1.00 21.12 ? 708 ILE A O 1 ATOM 5624 C CB . ILE A 1 715 ? 18.408 71.860 38.488 1.00 18.17 ? 708 ILE A CB 1 ATOM 5625 C CG1 . ILE A 1 715 ? 17.389 72.557 39.404 1.00 19.87 ? 708 ILE A CG1 1 ATOM 5626 C CG2 . ILE A 1 715 ? 19.245 72.945 37.767 1.00 19.57 ? 708 ILE A CG2 1 ATOM 5627 C CD1 . ILE A 1 715 ? 18.083 73.325 40.589 1.00 20.70 ? 708 ILE A CD1 1 ATOM 5628 N N . TYR A 1 716 ? 19.142 69.036 37.277 1.00 19.16 ? 709 TYR A N 1 ATOM 5629 C CA . TYR A 1 716 ? 20.163 68.216 36.630 1.00 20.03 ? 709 TYR A CA 1 ATOM 5630 C C . TYR A 1 716 ? 19.693 67.773 35.241 1.00 19.83 ? 709 TYR A C 1 ATOM 5631 O O . TYR A 1 716 ? 20.429 67.921 34.251 1.00 20.57 ? 709 TYR A O 1 ATOM 5632 C CB . TYR A 1 716 ? 20.513 66.986 37.497 1.00 19.47 ? 709 TYR A CB 1 ATOM 5633 C CG . TYR A 1 716 ? 21.609 66.164 36.823 1.00 19.24 ? 709 TYR A CG 1 ATOM 5634 C CD1 . TYR A 1 716 ? 22.953 66.351 37.169 1.00 20.80 ? 709 TYR A CD1 1 ATOM 5635 C CD2 . TYR A 1 716 ? 21.282 65.239 35.799 1.00 21.63 ? 709 TYR A CD2 1 ATOM 5636 C CE1 . TYR A 1 716 ? 24.000 65.615 36.522 1.00 22.21 ? 709 TYR A CE1 1 ATOM 5637 C CE2 . TYR A 1 716 ? 22.301 64.509 35.137 1.00 21.34 ? 709 TYR A CE2 1 ATOM 5638 C CZ . TYR A 1 716 ? 23.653 64.705 35.516 1.00 23.34 ? 709 TYR A CZ 1 ATOM 5639 O OH . TYR A 1 716 ? 24.644 63.974 34.885 1.00 24.48 ? 709 TYR A OH 1 ATOM 5640 N N . ASP A 1 717 ? 18.485 67.216 35.149 1.00 19.45 ? 710 ASP A N 1 ATOM 5641 C CA . ASP A 1 717 ? 17.988 66.742 33.846 1.00 19.72 ? 710 ASP A CA 1 ATOM 5642 C C . ASP A 1 717 ? 17.773 67.899 32.882 1.00 20.44 ? 710 ASP A C 1 ATOM 5643 O O . ASP A 1 717 ? 18.024 67.752 31.683 1.00 21.73 ? 710 ASP A O 1 ATOM 5644 C CB . ASP A 1 717 ? 16.719 65.917 34.021 1.00 19.33 ? 710 ASP A CB 1 ATOM 5645 C CG . ASP A 1 717 ? 17.003 64.536 34.575 1.00 22.54 ? 710 ASP A CG 1 ATOM 5646 O OD1 . ASP A 1 717 ? 18.159 64.071 34.508 1.00 21.73 ? 710 ASP A OD1 1 ATOM 5647 O OD2 . ASP A 1 717 ? 16.054 63.890 35.031 1.00 22.22 ? 710 ASP A OD2 1 ATOM 5648 N N . ALA A 1 718 ? 17.351 69.063 33.392 1.00 20.27 ? 711 ALA A N 1 ATOM 5649 C CA . ALA A 1 718 ? 17.209 70.228 32.494 1.00 20.61 ? 711 ALA A CA 1 ATOM 5650 C C . ALA A 1 718 ? 18.564 70.660 31.893 1.00 21.82 ? 711 ALA A C 1 ATOM 5651 O O . ALA A 1 718 ? 18.618 71.130 30.731 1.00 22.11 ? 711 ALA A O 1 ATOM 5652 C CB . ALA A 1 718 ? 16.546 71.415 33.234 1.00 20.15 ? 711 ALA A CB 1 ATOM 5653 N N . LEU A 1 719 ? 19.651 70.492 32.654 1.00 21.58 ? 712 LEU A N 1 ATOM 5654 C CA . LEU A 1 719 ? 21.003 70.872 32.168 1.00 22.16 ? 712 LEU A CA 1 ATOM 5655 C C . LEU A 1 719 ? 21.697 69.787 31.340 1.00 22.67 ? 712 LEU A C 1 ATOM 5656 O O . LEU A 1 719 ? 22.656 70.067 30.649 1.00 24.67 ? 712 LEU A O 1 ATOM 5657 C CB . LEU A 1 719 ? 21.900 71.202 33.361 1.00 22.50 ? 712 LEU A CB 1 ATOM 5658 C CG . LEU A 1 719 ? 21.632 72.567 34.005 1.00 21.96 ? 712 LEU A CG 1 ATOM 5659 C CD1 . LEU A 1 719 ? 22.319 72.579 35.384 1.00 24.37 ? 712 LEU A CD1 1 ATOM 5660 C CD2 . LEU A 1 719 ? 22.161 73.659 33.073 1.00 24.95 ? 712 LEU A CD2 1 ATOM 5661 N N . PHE A 1 720 ? 21.219 68.549 31.443 1.00 22.87 ? 713 PHE A N 1 ATOM 5662 C CA . PHE A 1 720 ? 21.944 67.442 30.846 1.00 23.66 ? 713 PHE A CA 1 ATOM 5663 C C . PHE A 1 720 ? 21.959 67.545 29.325 1.00 25.20 ? 713 PHE A C 1 ATOM 5664 O O . PHE A 1 720 ? 20.895 67.670 28.681 1.00 24.46 ? 713 PHE A O 1 ATOM 5665 C CB . PHE A 1 720 ? 21.378 66.083 31.292 1.00 22.92 ? 713 PHE A CB 1 ATOM 5666 C CG . PHE A 1 720 ? 22.195 64.926 30.784 1.00 24.00 ? 713 PHE A CG 1 ATOM 5667 C CD1 . PHE A 1 720 ? 23.358 64.523 31.473 1.00 24.09 ? 713 PHE A CD1 1 ATOM 5668 C CD2 . PHE A 1 720 ? 21.858 64.303 29.592 1.00 25.98 ? 713 PHE A CD2 1 ATOM 5669 C CE1 . PHE A 1 720 ? 24.159 63.475 30.972 1.00 27.16 ? 713 PHE A CE1 1 ATOM 5670 C CE2 . PHE A 1 720 ? 22.657 63.260 29.073 1.00 25.88 ? 713 PHE A CE2 1 ATOM 5671 C CZ . PHE A 1 720 ? 23.802 62.855 29.763 1.00 27.01 ? 713 PHE A CZ 1 ATOM 5672 N N . ASP A 1 721 ? 23.166 67.498 28.771 1.00 26.19 ? 714 ASP A N 1 ATOM 5673 C CA . ASP A 1 721 ? 23.360 67.549 27.309 1.00 27.55 ? 714 ASP A CA 1 ATOM 5674 C C . ASP A 1 721 ? 22.664 68.775 26.696 1.00 28.32 ? 714 ASP A C 1 ATOM 5675 O O . ASP A 1 721 ? 22.229 68.748 25.540 1.00 28.97 ? 714 ASP A O 1 ATOM 5676 C CB . ASP A 1 721 ? 22.841 66.228 26.688 1.00 26.93 ? 714 ASP A CB 1 ATOM 5677 C CG . ASP A 1 721 ? 23.217 66.061 25.210 1.00 31.11 ? 714 ASP A CG 1 ATOM 5678 O OD1 . ASP A 1 721 ? 24.375 66.343 24.831 1.00 32.15 ? 714 ASP A OD1 1 ATOM 5679 O OD2 . ASP A 1 721 ? 22.353 65.600 24.434 1.00 31.92 ? 714 ASP A OD2 1 ATOM 5680 N N . ILE A 1 722 ? 22.587 69.877 27.455 1.00 27.76 ? 715 ILE A N 1 ATOM 5681 C CA . ILE A 1 722 ? 21.826 71.044 27.006 1.00 27.85 ? 715 ILE A CA 1 ATOM 5682 C C . ILE A 1 722 ? 22.421 71.677 25.739 1.00 30.07 ? 715 ILE A C 1 ATOM 5683 O O . ILE A 1 722 ? 21.670 72.255 24.936 1.00 29.87 ? 715 ILE A O 1 ATOM 5684 C CB . ILE A 1 722 ? 21.702 72.107 28.133 1.00 27.49 ? 715 ILE A CB 1 ATOM 5685 C CG1 . ILE A 1 722 ? 20.715 73.208 27.750 1.00 26.99 ? 715 ILE A CG1 1 ATOM 5686 C CG2 . ILE A 1 722 ? 23.085 72.659 28.543 1.00 26.38 ? 715 ILE A CG2 1 ATOM 5687 C CD1 . ILE A 1 722 ? 20.144 73.920 28.978 1.00 26.09 ? 715 ILE A CD1 1 ATOM 5688 N N . GLU A 1 723 ? 23.742 71.545 25.560 1.00 31.34 ? 716 GLU A N 1 ATOM 5689 C CA . GLU A 1 723 ? 24.422 72.129 24.392 1.00 34.66 ? 716 GLU A CA 1 ATOM 5690 C C . GLU A 1 723 ? 23.948 71.490 23.079 1.00 35.71 ? 716 GLU A C 1 ATOM 5691 O O . GLU A 1 723 ? 24.199 72.038 21.980 1.00 37.16 ? 716 GLU A O 1 ATOM 5692 C CB . GLU A 1 723 ? 25.955 72.040 24.530 1.00 34.91 ? 716 GLU A CB 1 ATOM 5693 C CG . GLU A 1 723 ? 26.530 70.621 24.439 1.00 37.00 ? 716 GLU A CG 1 ATOM 5694 C CD . GLU A 1 723 ? 26.573 69.866 25.779 0.80 37.86 ? 716 GLU A CD 1 ATOM 5695 O OE1 . GLU A 1 723 ? 25.828 70.199 26.743 1.00 35.56 ? 716 GLU A OE1 1 ATOM 5696 O OE2 . GLU A 1 723 ? 27.372 68.907 25.853 0.80 39.85 ? 716 GLU A OE2 1 ATOM 5697 N N . SER A 1 724 ? 23.269 70.349 23.182 1.00 35.82 ? 717 SER A N 1 ATOM 5698 C CA . SER A 1 724 ? 22.739 69.635 22.011 1.00 37.33 ? 717 SER A CA 1 ATOM 5699 C C . SER A 1 724 ? 21.302 69.978 21.663 1.00 38.02 ? 717 SER A C 1 ATOM 5700 O O . SER A 1 724 ? 20.808 69.555 20.612 1.00 38.60 ? 717 SER A O 1 ATOM 5701 C CB . SER A 1 724 ? 22.863 68.110 22.185 1.00 36.75 ? 717 SER A CB 1 ATOM 5702 O OG . SER A 1 724 ? 24.223 67.748 22.346 1.00 37.60 ? 717 SER A OG 1 ATOM 5703 N N A LYS A 1 725 ? 20.639 70.748 22.522 0.30 37.60 ? 718 LYS A N 1 ATOM 5704 N N B LYS A 1 725 ? 20.633 70.736 22.535 0.70 37.37 ? 718 LYS A N 1 ATOM 5705 C CA A LYS A 1 725 ? 19.236 71.086 22.318 0.30 37.76 ? 718 LYS A CA 1 ATOM 5706 C CA B LYS A 1 725 ? 19.240 71.104 22.325 0.70 37.69 ? 718 LYS A CA 1 ATOM 5707 C C A LYS A 1 725 ? 19.049 72.155 21.246 0.30 39.11 ? 718 LYS A C 1 ATOM 5708 C C B LYS A 1 725 ? 19.104 72.113 21.188 0.70 39.12 ? 718 LYS A C 1 ATOM 5709 O O A LYS A 1 725 ? 19.761 73.162 21.216 0.30 39.55 ? 718 LYS A O 1 ATOM 5710 O O B LYS A 1 725 ? 19.905 73.045 21.059 0.70 39.74 ? 718 LYS A O 1 ATOM 5711 C CB A LYS A 1 725 ? 18.584 71.502 23.638 0.30 36.66 ? 718 LYS A CB 1 ATOM 5712 C CB B LYS A 1 725 ? 18.600 71.671 23.609 0.70 36.34 ? 718 LYS A CB 1 ATOM 5713 C CG A LYS A 1 725 ? 18.628 70.399 24.678 0.30 35.82 ? 718 LYS A CG 1 ATOM 5714 C CG B LYS A 1 725 ? 18.464 70.682 24.775 0.70 36.44 ? 718 LYS A CG 1 ATOM 5715 C CD A LYS A 1 725 ? 18.180 69.071 24.080 0.30 34.99 ? 718 LYS A CD 1 ATOM 5716 C CD B LYS A 1 725 ? 17.459 69.561 24.520 0.70 37.19 ? 718 LYS A CD 1 ATOM 5717 C CE A LYS A 1 725 ? 18.706 67.882 24.883 0.30 34.36 ? 718 LYS A CE 1 ATOM 5718 C CE B LYS A 1 725 ? 17.656 68.408 25.514 0.70 36.89 ? 718 LYS A CE 1 ATOM 5719 N NZ A LYS A 1 725 ? 20.037 67.437 24.382 0.30 34.62 ? 718 LYS A NZ 1 ATOM 5720 N NZ B LYS A 1 725 ? 17.190 68.775 26.864 0.70 35.47 ? 718 LYS A NZ 1 ATOM 5721 N N . VAL A 1 726 ? 18.069 71.916 20.378 1.00 39.76 ? 719 VAL A N 1 ATOM 5722 C CA . VAL A 1 726 ? 17.842 72.724 19.170 1.00 41.80 ? 719 VAL A CA 1 ATOM 5723 C C . VAL A 1 726 ? 17.385 74.167 19.465 1.00 41.48 ? 719 VAL A C 1 ATOM 5724 O O . VAL A 1 726 ? 17.753 75.117 18.749 1.00 42.53 ? 719 VAL A O 1 ATOM 5725 C CB . VAL A 1 726 ? 16.866 71.932 18.230 1.00 42.46 ? 719 VAL A CB 1 ATOM 5726 C CG1 . VAL A 1 726 ? 15.855 72.829 17.523 1.00 45.30 ? 719 VAL A CG1 1 ATOM 5727 C CG2 . VAL A 1 726 ? 17.686 71.082 17.236 1.00 44.80 ? 719 VAL A CG2 1 ATOM 5728 N N . ASP A 1 727 ? 16.620 74.322 20.540 1.00 39.87 ? 720 ASP A N 1 ATOM 5729 C CA . ASP A 1 727 ? 16.075 75.617 20.957 1.00 38.90 ? 720 ASP A CA 1 ATOM 5730 C C . ASP A 1 727 ? 16.653 75.989 22.336 1.00 37.22 ? 720 ASP A C 1 ATOM 5731 O O . ASP A 1 727 ? 16.040 75.684 23.364 1.00 35.56 ? 720 ASP A O 1 ATOM 5732 C CB . ASP A 1 727 ? 14.549 75.491 21.056 1.00 38.91 ? 720 ASP A CB 1 ATOM 5733 C CG . ASP A 1 727 ? 13.855 76.814 21.349 1.00 40.44 ? 720 ASP A CG 1 ATOM 5734 O OD1 . ASP A 1 727 ? 14.527 77.811 21.689 1.00 41.20 ? 720 ASP A OD1 1 ATOM 5735 O OD2 . ASP A 1 727 ? 12.609 76.850 21.237 1.00 45.77 ? 720 ASP A OD2 1 ATOM 5736 N N . PRO A 1 728 ? 17.824 76.643 22.362 1.00 36.41 ? 721 PRO A N 1 ATOM 5737 C CA . PRO A 1 728 ? 18.462 76.955 23.650 1.00 35.57 ? 721 PRO A CA 1 ATOM 5738 C C . PRO A 1 728 ? 17.629 77.878 24.553 1.00 34.38 ? 721 PRO A C 1 ATOM 5739 O O . PRO A 1 728 ? 17.679 77.760 25.776 1.00 32.43 ? 721 PRO A O 1 ATOM 5740 C CB . PRO A 1 728 ? 19.774 77.638 23.244 1.00 36.66 ? 721 PRO A CB 1 ATOM 5741 C CG . PRO A 1 728 ? 19.585 78.074 21.817 1.00 38.23 ? 721 PRO A CG 1 ATOM 5742 C CD . PRO A 1 728 ? 18.648 77.071 21.212 1.00 38.08 ? 721 PRO A CD 1 ATOM 5743 N N . SER A 1 729 ? 16.876 78.798 23.959 1.00 34.29 ? 722 SER A N 1 ATOM 5744 C CA . SER A 1 729 ? 16.027 79.674 24.760 1.00 34.01 ? 722 SER A CA 1 ATOM 5745 C C . SER A 1 729 ? 15.021 78.853 25.572 1.00 32.26 ? 722 SER A C 1 ATOM 5746 O O . SER A 1 729 ? 14.846 79.073 26.775 1.00 30.72 ? 722 SER A O 1 ATOM 5747 C CB . SER A 1 729 ? 15.326 80.712 23.877 1.00 34.91 ? 722 SER A CB 1 ATOM 5748 O OG . SER A 1 729 ? 14.449 81.480 24.675 1.00 38.13 ? 722 SER A OG 1 ATOM 5749 N N . LYS A 1 730 ? 14.368 77.893 24.919 1.00 31.02 ? 723 LYS A N 1 ATOM 5750 C CA . LYS A 1 730 ? 13.442 77.024 25.602 1.00 31.29 ? 723 LYS A CA 1 ATOM 5751 C C . LYS A 1 730 ? 14.156 76.139 26.654 1.00 29.05 ? 723 LYS A C 1 ATOM 5752 O O . LYS A 1 730 ? 13.649 75.957 27.773 1.00 28.33 ? 723 LYS A O 1 ATOM 5753 C CB . LYS A 1 730 ? 12.694 76.166 24.573 1.00 32.16 ? 723 LYS A CB 1 ATOM 5754 C CG . LYS A 1 730 ? 11.687 75.213 25.171 1.00 36.74 ? 723 LYS A CG 1 ATOM 5755 C CD . LYS A 1 730 ? 11.078 74.283 24.115 1.00 44.14 ? 723 LYS A CD 1 ATOM 5756 C CE . LYS A 1 730 ? 9.993 73.408 24.757 1.00 47.56 ? 723 LYS A CE 1 ATOM 5757 N NZ . LYS A 1 730 ? 9.545 72.336 23.826 1.00 52.03 ? 723 LYS A NZ 1 ATOM 5758 N N . ALA A 1 731 ? 15.314 75.591 26.283 1.00 28.27 ? 724 ALA A N 1 ATOM 5759 C CA . ALA A 1 731 ? 16.047 74.678 27.173 1.00 26.16 ? 724 ALA A CA 1 ATOM 5760 C C . ALA A 1 731 ? 16.498 75.435 28.437 1.00 25.59 ? 724 ALA A C 1 ATOM 5761 O O . ALA A 1 731 ? 16.339 74.933 29.536 1.00 24.29 ? 724 ALA A O 1 ATOM 5762 C CB . ALA A 1 731 ? 17.266 74.093 26.465 1.00 27.17 ? 724 ALA A CB 1 ATOM 5763 N N . TRP A 1 732 ? 17.062 76.632 28.266 1.00 25.01 ? 725 TRP A N 1 ATOM 5764 C CA . TRP A 1 732 ? 17.496 77.410 29.443 1.00 24.51 ? 725 TRP A CA 1 ATOM 5765 C C . TRP A 1 732 ? 16.310 77.951 30.246 1.00 24.43 ? 725 TRP A C 1 ATOM 5766 O O . TRP A 1 732 ? 16.405 78.119 31.469 1.00 23.26 ? 725 TRP A O 1 ATOM 5767 C CB . TRP A 1 732 ? 18.476 78.505 29.018 1.00 24.64 ? 725 TRP A CB 1 ATOM 5768 C CG . TRP A 1 732 ? 19.815 77.874 28.736 1.00 24.97 ? 725 TRP A CG 1 ATOM 5769 C CD1 . TRP A 1 732 ? 20.336 77.544 27.507 1.00 26.02 ? 725 TRP A CD1 1 ATOM 5770 C CD2 . TRP A 1 732 ? 20.774 77.450 29.709 1.00 25.17 ? 725 TRP A CD2 1 ATOM 5771 N NE1 . TRP A 1 732 ? 21.590 76.963 27.663 1.00 28.01 ? 725 TRP A NE1 1 ATOM 5772 C CE2 . TRP A 1 732 ? 21.870 76.880 29.003 1.00 25.82 ? 725 TRP A CE2 1 ATOM 5773 C CE3 . TRP A 1 732 ? 20.817 77.493 31.116 1.00 23.81 ? 725 TRP A CE3 1 ATOM 5774 C CZ2 . TRP A 1 732 ? 23.020 76.388 29.657 1.00 27.23 ? 725 TRP A CZ2 1 ATOM 5775 C CZ3 . TRP A 1 732 ? 21.956 76.991 31.768 1.00 25.35 ? 725 TRP A CZ3 1 ATOM 5776 C CH2 . TRP A 1 732 ? 23.039 76.439 31.034 1.00 24.96 ? 725 TRP A CH2 1 ATOM 5777 N N . GLY A 1 733 ? 15.189 78.212 29.574 1.00 24.35 ? 726 GLY A N 1 ATOM 5778 C CA . GLY A 1 733 ? 13.943 78.580 30.282 1.00 24.30 ? 726 GLY A CA 1 ATOM 5779 C C . GLY A 1 733 ? 13.555 77.481 31.252 1.00 22.90 ? 726 GLY A C 1 ATOM 5780 O O . GLY A 1 733 ? 13.126 77.750 32.393 1.00 23.00 ? 726 GLY A O 1 ATOM 5781 N N . GLU A 1 734 ? 13.691 76.231 30.808 1.00 22.80 ? 727 GLU A N 1 ATOM 5782 C CA . GLU A 1 734 ? 13.304 75.095 31.646 1.00 22.11 ? 727 GLU A CA 1 ATOM 5783 C C . GLU A 1 734 ? 14.307 74.921 32.794 1.00 21.26 ? 727 GLU A C 1 ATOM 5784 O O . GLU A 1 734 ? 13.915 74.564 33.912 1.00 20.21 ? 727 GLU A O 1 ATOM 5785 C CB . GLU A 1 734 ? 13.174 73.831 30.800 1.00 22.49 ? 727 GLU A CB 1 ATOM 5786 C CG A GLU A 1 734 ? 12.830 72.572 31.594 1.00 23.59 ? 727 GLU A CG 1 ATOM 5787 C CD A GLU A 1 734 ? 11.452 72.630 32.305 1.00 25.89 ? 727 GLU A CD 1 ATOM 5788 O OE1 A GLU A 1 734 ? 10.617 73.534 32.032 1.00 25.53 ? 727 GLU A OE1 1 ATOM 5789 O OE2 A GLU A 1 734 ? 11.211 71.737 33.143 1.00 25.79 ? 727 GLU A OE2 1 ATOM 5790 N N . VAL A 1 735 ? 15.589 75.189 32.529 1.00 21.54 ? 728 VAL A N 1 ATOM 5791 C CA . VAL A 1 735 ? 16.565 75.233 33.631 1.00 21.13 ? 728 VAL A CA 1 ATOM 5792 C C . VAL A 1 735 ? 16.090 76.243 34.689 1.00 21.05 ? 728 VAL A C 1 ATOM 5793 O O . VAL A 1 735 ? 16.059 75.929 35.870 1.00 20.52 ? 728 VAL A O 1 ATOM 5794 C CB . VAL A 1 735 ? 18.005 75.575 33.159 1.00 22.95 ? 728 VAL A CB 1 ATOM 5795 C CG1 . VAL A 1 735 ? 18.924 75.840 34.366 1.00 23.13 ? 728 VAL A CG1 1 ATOM 5796 C CG2 . VAL A 1 735 ? 18.564 74.445 32.207 1.00 21.85 ? 728 VAL A CG2 1 ATOM 5797 N N A LYS A 1 736 ? 15.724 77.448 34.250 0.70 20.59 ? 729 LYS A N 1 ATOM 5798 N N B LYS A 1 736 ? 15.717 77.445 34.244 0.30 20.99 ? 729 LYS A N 1 ATOM 5799 C CA A LYS A 1 736 ? 15.274 78.470 35.218 0.70 20.49 ? 729 LYS A CA 1 ATOM 5800 C CA B LYS A 1 736 ? 15.254 78.503 35.158 0.30 20.87 ? 729 LYS A CA 1 ATOM 5801 C C A LYS A 1 736 ? 14.019 78.021 35.964 0.70 20.46 ? 729 LYS A C 1 ATOM 5802 C C B LYS A 1 736 ? 13.977 78.131 35.911 0.30 20.35 ? 729 LYS A C 1 ATOM 5803 O O A LYS A 1 736 ? 13.899 78.232 37.175 0.70 19.35 ? 729 LYS A O 1 ATOM 5804 O O B LYS A 1 736 ? 13.800 78.509 37.079 0.30 19.63 ? 729 LYS A O 1 ATOM 5805 C CB A LYS A 1 736 ? 15.073 79.817 34.541 0.70 21.06 ? 729 LYS A CB 1 ATOM 5806 C CB B LYS A 1 736 ? 15.067 79.818 34.408 0.30 21.58 ? 729 LYS A CB 1 ATOM 5807 C CG A LYS A 1 736 ? 16.403 80.395 34.029 0.70 21.53 ? 729 LYS A CG 1 ATOM 5808 C CG B LYS A 1 736 ? 16.383 80.452 33.983 0.30 22.47 ? 729 LYS A CG 1 ATOM 5809 C CD A LYS A 1 736 ? 16.196 81.663 33.187 0.70 23.79 ? 729 LYS A CD 1 ATOM 5810 C CD B LYS A 1 736 ? 16.145 81.767 33.252 0.30 23.81 ? 729 LYS A CD 1 ATOM 5811 C CE A LYS A 1 736 ? 15.657 82.850 33.953 0.70 25.08 ? 729 LYS A CE 1 ATOM 5812 C CE B LYS A 1 736 ? 15.832 81.518 31.776 0.30 25.65 ? 729 LYS A CE 1 ATOM 5813 N NZ A LYS A 1 736 ? 15.691 84.110 33.115 0.70 27.46 ? 729 LYS A NZ 1 ATOM 5814 N NZ B LYS A 1 736 ? 15.631 82.791 31.018 0.30 26.32 ? 729 LYS A NZ 1 ATOM 5815 N N . ARG A 1 737 ? 13.089 77.398 35.238 1.00 19.39 ? 730 ARG A N 1 ATOM 5816 C CA . ARG A 1 737 ? 11.902 76.888 35.900 1.00 19.13 ? 730 ARG A CA 1 ATOM 5817 C C . ARG A 1 737 ? 12.273 75.902 37.010 1.00 18.96 ? 730 ARG A C 1 ATOM 5818 O O . ARG A 1 737 ? 11.737 75.984 38.109 1.00 17.95 ? 730 ARG A O 1 ATOM 5819 C CB . ARG A 1 737 ? 10.920 76.254 34.910 1.00 19.44 ? 730 ARG A CB 1 ATOM 5820 C CG . ARG A 1 737 ? 9.569 75.972 35.614 1.00 21.18 ? 730 ARG A CG 1 ATOM 5821 C CD . ARG A 1 737 ? 8.610 75.413 34.563 1.00 22.24 ? 730 ARG A CD 1 ATOM 5822 N NE . ARG A 1 737 ? 8.827 74.007 34.318 1.00 22.43 ? 730 ARG A NE 1 ATOM 5823 C CZ . ARG A 1 737 ? 8.327 73.030 35.071 1.00 24.91 ? 730 ARG A CZ 1 ATOM 5824 N NH1 . ARG A 1 737 ? 7.653 73.308 36.205 1.00 28.27 ? 730 ARG A NH1 1 ATOM 5825 N NH2 . ARG A 1 737 ? 8.558 71.772 34.730 1.00 27.01 ? 730 ARG A NH2 1 ATOM 5826 N N . GLN A 1 738 ? 13.213 75.008 36.737 1.00 18.41 ? 731 GLN A N 1 ATOM 5827 C CA . GLN A 1 738 ? 13.599 74.009 37.740 1.00 17.66 ? 731 GLN A CA 1 ATOM 5828 C C . GLN A 1 738 ? 14.358 74.644 38.908 1.00 19.24 ? 731 GLN A C 1 ATOM 5829 O O . GLN A 1 738 ? 14.211 74.190 40.044 1.00 18.87 ? 731 GLN A O 1 ATOM 5830 C CB . GLN A 1 738 ? 14.410 72.873 37.095 1.00 18.51 ? 731 GLN A CB 1 ATOM 5831 C CG . GLN A 1 738 ? 13.570 72.100 36.066 1.00 17.48 ? 731 GLN A CG 1 ATOM 5832 C CD . GLN A 1 738 ? 12.417 71.360 36.733 1.00 20.03 ? 731 GLN A CD 1 ATOM 5833 O OE1 . GLN A 1 738 ? 12.516 70.941 37.901 1.00 19.82 ? 731 GLN A OE1 1 ATOM 5834 N NE2 . GLN A 1 738 ? 11.306 71.189 35.997 1.00 22.44 ? 731 GLN A NE2 1 ATOM 5835 N N . ILE A 1 739 ? 15.123 75.709 38.632 1.00 19.40 ? 732 ILE A N 1 ATOM 5836 C CA . ILE A 1 739 ? 15.748 76.442 39.745 1.00 19.40 ? 732 ILE A CA 1 ATOM 5837 C C . ILE A 1 739 ? 14.678 77.019 40.686 1.00 20.04 ? 732 ILE A C 1 ATOM 5838 O O . ILE A 1 739 ? 14.790 76.909 41.905 1.00 20.25 ? 732 ILE A O 1 ATOM 5839 C CB . ILE A 1 739 ? 16.674 77.554 39.237 1.00 19.77 ? 732 ILE A CB 1 ATOM 5840 C CG1 . ILE A 1 739 ? 17.878 76.921 38.545 1.00 19.16 ? 732 ILE A CG1 1 ATOM 5841 C CG2 . ILE A 1 739 ? 17.156 78.465 40.437 1.00 20.97 ? 732 ILE A CG2 1 ATOM 5842 C CD1 . ILE A 1 739 ? 18.738 77.985 37.744 1.00 21.25 ? 732 ILE A CD1 1 ATOM 5843 N N . TYR A 1 740 ? 13.661 77.650 40.103 1.00 19.45 ? 733 TYR A N 1 ATOM 5844 C CA . TYR A 1 740 ? 12.521 78.219 40.860 1.00 19.94 ? 733 TYR A CA 1 ATOM 5845 C C . TYR A 1 740 ? 11.831 77.137 41.671 1.00 19.16 ? 733 TYR A C 1 ATOM 5846 O O . TYR A 1 740 ? 11.591 77.337 42.874 1.00 19.08 ? 733 TYR A O 1 ATOM 5847 C CB . TYR A 1 740 ? 11.563 78.827 39.867 1.00 19.74 ? 733 TYR A CB 1 ATOM 5848 C CG . TYR A 1 740 ? 10.084 79.090 40.260 0.80 20.41 ? 733 TYR A CG 1 ATOM 5849 C CD1 . TYR A 1 740 ? 9.766 79.823 41.404 0.80 22.81 ? 733 TYR A CD1 1 ATOM 5850 C CD2 . TYR A 1 740 ? 9.022 78.675 39.401 1.00 22.39 ? 733 TYR A CD2 1 ATOM 5851 C CE1 . TYR A 1 740 ? 8.402 80.144 41.704 0.80 20.13 ? 733 TYR A CE1 1 ATOM 5852 C CE2 . TYR A 1 740 ? 7.702 78.977 39.672 1.00 20.72 ? 733 TYR A CE2 1 ATOM 5853 C CZ . TYR A 1 740 ? 7.390 79.724 40.827 0.80 21.13 ? 733 TYR A CZ 1 ATOM 5854 O OH . TYR A 1 740 ? 6.062 80.065 41.093 0.80 23.60 ? 733 TYR A OH 1 ATOM 5855 N N . VAL A 1 741 ? 11.524 76.003 41.047 1.00 18.51 ? 734 VAL A N 1 ATOM 5856 C CA . VAL A 1 741 ? 10.838 74.929 41.805 1.00 17.60 ? 734 VAL A CA 1 ATOM 5857 C C . VAL A 1 741 ? 11.705 74.437 42.985 1.00 18.26 ? 734 VAL A C 1 ATOM 5858 O O . VAL A 1 741 ? 11.213 74.272 44.126 1.00 18.46 ? 734 VAL A O 1 ATOM 5859 C CB . VAL A 1 741 ? 10.464 73.737 40.876 1.00 17.05 ? 734 VAL A CB 1 ATOM 5860 C CG1 . VAL A 1 741 ? 10.014 72.509 41.698 1.00 18.20 ? 734 VAL A CG1 1 ATOM 5861 C CG2 . VAL A 1 741 ? 9.348 74.196 39.890 1.00 19.45 ? 734 VAL A CG2 1 ATOM 5862 N N . ALA A 1 742 ? 13.010 74.270 42.737 1.00 17.94 ? 735 ALA A N 1 ATOM 5863 C CA . ALA A 1 742 ? 13.911 73.779 43.798 1.00 17.89 ? 735 ALA A CA 1 ATOM 5864 C C . ALA A 1 742 ? 14.064 74.823 44.906 1.00 17.55 ? 735 ALA A C 1 ATOM 5865 O O . ALA A 1 742 ? 14.015 74.461 46.101 1.00 17.52 ? 735 ALA A O 1 ATOM 5866 C CB . ALA A 1 742 ? 15.300 73.419 43.206 1.00 18.27 ? 735 ALA A CB 1 ATOM 5867 N N . ALA A 1 743 ? 14.254 76.094 44.540 1.00 17.01 ? 736 ALA A N 1 ATOM 5868 C CA . ALA A 1 743 ? 14.398 77.160 45.577 1.00 17.91 ? 736 ALA A CA 1 ATOM 5869 C C . ALA A 1 743 ? 13.121 77.250 46.425 1.00 18.97 ? 736 ALA A C 1 ATOM 5870 O O . ALA A 1 743 ? 13.170 77.350 47.657 1.00 19.18 ? 736 ALA A O 1 ATOM 5871 C CB . ALA A 1 743 ? 14.663 78.526 44.919 1.00 19.12 ? 736 ALA A CB 1 ATOM 5872 N N . PHE A 1 744 ? 11.975 77.221 45.745 1.00 18.27 ? 737 PHE A N 1 ATOM 5873 C CA . PHE A 1 744 ? 10.698 77.306 46.448 1.00 18.49 ? 737 PHE A CA 1 ATOM 5874 C C . PHE A 1 744 ? 10.561 76.126 47.410 1.00 17.73 ? 737 PHE A C 1 ATOM 5875 O O . PHE A 1 744 ? 10.193 76.304 48.579 1.00 17.97 ? 737 PHE A O 1 ATOM 5876 C CB . PHE A 1 744 ? 9.517 77.321 45.469 1.00 18.66 ? 737 PHE A CB 1 ATOM 5877 C CG . PHE A 1 744 ? 8.234 76.998 46.150 1.00 19.07 ? 737 PHE A CG 1 ATOM 5878 C CD1 . PHE A 1 744 ? 7.724 77.892 47.117 1.00 19.88 ? 737 PHE A CD1 1 ATOM 5879 C CD2 . PHE A 1 744 ? 7.639 75.751 45.955 1.00 19.22 ? 737 PHE A CD2 1 ATOM 5880 C CE1 . PHE A 1 744 ? 6.557 77.537 47.843 1.00 20.91 ? 737 PHE A CE1 1 ATOM 5881 C CE2 . PHE A 1 744 ? 6.395 75.404 46.673 1.00 18.65 ? 737 PHE A CE2 1 ATOM 5882 C CZ . PHE A 1 744 ? 5.909 76.323 47.595 1.00 18.89 ? 737 PHE A CZ 1 ATOM 5883 N N . THR A 1 745 ? 10.881 74.930 46.931 1.00 16.41 ? 738 THR A N 1 ATOM 5884 C CA . THR A 1 745 ? 10.685 73.718 47.762 1.00 15.99 ? 738 THR A CA 1 ATOM 5885 C C . THR A 1 745 ? 11.596 73.758 48.984 1.00 17.95 ? 738 THR A C 1 ATOM 5886 O O . THR A 1 745 ? 11.161 73.418 50.100 1.00 18.22 ? 738 THR A O 1 ATOM 5887 C CB . THR A 1 745 ? 10.908 72.443 46.949 1.00 16.35 ? 738 THR A CB 1 ATOM 5888 O OG1 . THR A 1 745 ? 10.016 72.467 45.827 1.00 16.73 ? 738 THR A OG1 1 ATOM 5889 C CG2 . THR A 1 745 ? 10.573 71.219 47.807 1.00 17.79 ? 738 THR A CG2 1 ATOM 5890 N N . VAL A 1 746 ? 12.850 74.178 48.780 1.00 17.70 ? 739 VAL A N 1 ATOM 5891 C CA . VAL A 1 746 ? 13.809 74.264 49.926 1.00 18.17 ? 739 VAL A CA 1 ATOM 5892 C C . VAL A 1 746 ? 13.308 75.281 50.949 1.00 18.54 ? 739 VAL A C 1 ATOM 5893 O O . VAL A 1 746 ? 13.310 74.997 52.147 1.00 18.34 ? 739 VAL A O 1 ATOM 5894 C CB . VAL A 1 746 ? 15.251 74.567 49.448 1.00 18.82 ? 739 VAL A CB 1 ATOM 5895 C CG1 . VAL A 1 746 ? 16.221 74.884 50.634 1.00 20.48 ? 739 VAL A CG1 1 ATOM 5896 C CG2 . VAL A 1 746 ? 15.791 73.382 48.657 1.00 18.12 ? 739 VAL A CG2 1 ATOM 5897 N N . GLN A 1 747 ? 12.877 76.454 50.482 1.00 18.49 ? 740 GLN A N 1 ATOM 5898 C CA . GLN A 1 747 ? 12.309 77.470 51.399 1.00 19.06 ? 740 GLN A CA 1 ATOM 5899 C C . GLN A 1 747 ? 11.060 76.944 52.119 1.00 18.49 ? 740 GLN A C 1 ATOM 5900 O O . GLN A 1 747 ? 10.873 77.170 53.323 1.00 18.70 ? 740 GLN A O 1 ATOM 5901 C CB . GLN A 1 747 ? 11.937 78.751 50.653 1.00 19.73 ? 740 GLN A CB 1 ATOM 5902 C CG . GLN A 1 747 ? 11.397 79.841 51.582 1.00 20.23 ? 740 GLN A CG 1 ATOM 5903 C CD . GLN A 1 747 ? 12.450 80.447 52.491 1.00 23.42 ? 740 GLN A CD 1 ATOM 5904 O OE1 . GLN A 1 747 ? 13.661 80.410 52.200 1.00 23.12 ? 740 GLN A OE1 1 ATOM 5905 N NE2 . GLN A 1 747 ? 11.995 81.029 53.610 1.00 22.74 ? 740 GLN A NE2 1 ATOM 5906 N N . ALA A 1 748 ? 10.185 76.260 51.382 1.00 18.05 ? 741 ALA A N 1 ATOM 5907 C CA . ALA A 1 748 ? 8.951 75.776 51.984 1.00 17.76 ? 741 ALA A CA 1 ATOM 5908 C C . ALA A 1 748 ? 9.287 74.731 53.043 1.00 17.92 ? 741 ALA A C 1 ATOM 5909 O O . ALA A 1 748 ? 8.699 74.719 54.136 1.00 18.68 ? 741 ALA A O 1 ATOM 5910 C CB . ALA A 1 748 ? 8.042 75.165 50.898 1.00 17.30 ? 741 ALA A CB 1 ATOM 5911 N N . ALA A 1 749 ? 10.249 73.857 52.744 1.00 17.80 ? 742 ALA A N 1 ATOM 5912 C CA . ALA A 1 749 ? 10.671 72.849 53.745 1.00 17.90 ? 742 ALA A CA 1 ATOM 5913 C C . ALA A 1 749 ? 11.253 73.567 54.968 1.00 19.78 ? 742 ALA A C 1 ATOM 5914 O O . ALA A 1 749 ? 10.924 73.199 56.114 1.00 19.06 ? 742 ALA A O 1 ATOM 5915 C CB . ALA A 1 749 ? 11.704 71.880 53.154 1.00 17.91 ? 742 ALA A CB 1 ATOM 5916 N N . ALA A 1 750 ? 12.101 74.572 54.724 1.00 19.52 ? 743 ALA A N 1 ATOM 5917 C CA . ALA A 1 750 ? 12.663 75.358 55.854 1.00 20.83 ? 743 ALA A CA 1 ATOM 5918 C C . ALA A 1 750 ? 11.535 75.901 56.729 1.00 20.84 ? 743 ALA A C 1 ATOM 5919 O O . ALA A 1 750 ? 11.600 75.843 57.964 1.00 20.53 ? 743 ALA A O 1 ATOM 5920 C CB . ALA A 1 750 ? 13.525 76.518 55.340 1.00 20.76 ? 743 ALA A CB 1 ATOM 5921 N N . GLU A 1 751 ? 10.496 76.445 56.098 1.00 19.50 ? 744 GLU A N 1 ATOM 5922 C CA . GLU A 1 751 ? 9.441 77.120 56.855 1.00 20.36 ? 744 GLU A CA 1 ATOM 5923 C C . GLU A 1 751 ? 8.622 76.168 57.700 1.00 19.74 ? 744 GLU A C 1 ATOM 5924 O O . GLU A 1 751 ? 7.991 76.611 58.654 1.00 20.61 ? 744 GLU A O 1 ATOM 5925 C CB . GLU A 1 751 ? 8.558 77.971 55.927 1.00 20.27 ? 744 GLU A CB 1 ATOM 5926 C CG . GLU A 1 751 ? 9.358 79.186 55.456 1.00 22.54 ? 744 GLU A CG 1 ATOM 5927 C CD . GLU A 1 751 ? 8.602 80.113 54.519 1.00 26.79 ? 744 GLU A CD 1 ATOM 5928 O OE1 . GLU A 1 751 ? 7.465 79.787 54.105 1.00 28.03 ? 744 GLU A OE1 1 ATOM 5929 O OE2 . GLU A 1 751 ? 9.158 81.189 54.188 1.00 26.96 ? 744 GLU A OE2 1 ATOM 5930 N N . THR A 1 752 ? 8.658 74.860 57.383 1.00 19.86 ? 745 THR A N 1 ATOM 5931 C CA . THR A 1 752 ? 7.989 73.876 58.264 1.00 19.52 ? 745 THR A CA 1 ATOM 5932 C C . THR A 1 752 ? 8.694 73.756 59.629 1.00 20.26 ? 745 THR A C 1 ATOM 5933 O O . THR A 1 752 ? 8.109 73.244 60.582 1.00 20.81 ? 745 THR A O 1 ATOM 5934 C CB . THR A 1 752 ? 7.859 72.462 57.649 1.00 18.82 ? 745 THR A CB 1 ATOM 5935 O OG1 . THR A 1 752 ? 9.144 71.799 57.640 1.00 19.28 ? 745 THR A OG1 1 ATOM 5936 C CG2 . THR A 1 752 ? 7.245 72.549 56.219 1.00 19.40 ? 745 THR A CG2 1 ATOM 5937 N N . LEU A 1 753 ? 9.938 74.244 59.704 1.00 19.97 ? 746 LEU A N 1 ATOM 5938 C CA . LEU A 1 753 ? 10.703 74.214 60.958 1.00 20.54 ? 746 LEU A CA 1 ATOM 5939 C C . LEU A 1 753 ? 10.638 75.529 61.721 1.00 21.98 ? 746 LEU A C 1 ATOM 5940 O O . LEU A 1 753 ? 11.143 75.611 62.858 1.00 22.71 ? 746 LEU A O 1 ATOM 5941 C CB . LEU A 1 753 ? 12.153 73.873 60.682 1.00 20.14 ? 746 LEU A CB 1 ATOM 5942 C CG . LEU A 1 753 ? 12.394 72.533 59.982 1.00 21.49 ? 746 LEU A CG 1 ATOM 5943 C CD1 . LEU A 1 753 ? 13.889 72.384 59.704 1.00 23.07 ? 746 LEU A CD1 1 ATOM 5944 C CD2 . LEU A 1 753 ? 11.862 71.357 60.811 1.00 23.84 ? 746 LEU A CD2 1 ATOM 5945 N N . SER A 1 754 ? 10.078 76.566 61.102 1.00 21.61 ? 747 SER A N 1 ATOM 5946 C CA . SER A 1 754 ? 9.826 77.827 61.830 1.00 22.39 ? 747 SER A CA 1 ATOM 5947 C C . SER A 1 754 ? 8.852 77.605 62.994 1.00 23.34 ? 747 SER A C 1 ATOM 5948 O O . SER A 1 754 ? 8.107 76.613 63.038 1.00 23.42 ? 747 SER A O 1 ATOM 5949 C CB . SER A 1 754 ? 9.269 78.873 60.865 1.00 23.23 ? 747 SER A CB 1 ATOM 5950 O OG . SER A 1 754 ? 10.244 79.173 59.875 1.00 26.13 ? 747 SER A OG 1 ATOM 5951 N N . GLU A 1 755 ? 8.844 78.531 63.946 1.00 23.89 ? 748 GLU A N 1 ATOM 5952 C CA . GLU A 1 755 ? 7.766 78.519 64.942 1.00 26.20 ? 748 GLU A CA 1 ATOM 5953 C C . GLU A 1 755 ? 6.392 78.455 64.241 1.00 25.01 ? 748 GLU A C 1 ATOM 5954 O O . GLU A 1 755 ? 6.163 79.117 63.216 1.00 24.69 ? 748 GLU A O 1 ATOM 5955 C CB . GLU A 1 755 ? 7.871 79.719 65.875 1.00 28.10 ? 748 GLU A CB 1 ATOM 5956 C CG . GLU A 1 755 ? 9.146 79.578 66.709 1.00 32.52 ? 748 GLU A CG 1 ATOM 5957 C CD . GLU A 1 755 ? 9.221 80.537 67.856 1.00 42.47 ? 748 GLU A CD 1 ATOM 5958 O OE1 . GLU A 1 755 ? 9.568 81.716 67.629 1.00 45.81 ? 748 GLU A OE1 1 ATOM 5959 O OE2 . GLU A 1 755 ? 8.961 80.083 68.981 1.00 45.72 ? 748 GLU A OE2 1 ATOM 5960 N N . VAL A 1 756 ? 5.513 77.624 64.787 1.00 24.92 ? 749 VAL A N 1 ATOM 5961 C CA . VAL A 1 756 ? 4.260 77.280 64.085 1.00 25.19 ? 749 VAL A CA 1 ATOM 5962 C C . VAL A 1 756 ? 3.229 78.408 64.071 1.00 26.10 ? 749 VAL A C 1 ATOM 5963 O O . VAL A 1 756 ? 2.319 78.411 63.245 1.00 25.48 ? 749 VAL A O 1 ATOM 5964 C CB . VAL A 1 756 ? 3.657 75.945 64.594 1.00 25.18 ? 749 VAL A CB 1 ATOM 5965 C CG1 . VAL A 1 756 ? 4.695 74.816 64.478 1.00 24.85 ? 749 VAL A CG1 1 ATOM 5966 C CG2 . VAL A 1 756 ? 3.135 76.090 66.064 1.00 24.93 ? 749 VAL A CG2 1 ATOM 5967 N N . ALA A 1 757 ? 3.382 79.359 65.000 1.00 26.48 ? 750 ALA A N 1 ATOM 5968 C CA . ALA A 1 757 ? 2.442 80.488 65.167 1.00 28.84 ? 750 ALA A CA 1 ATOM 5969 C C . ALA A 1 757 ? 3.051 81.478 66.126 1.00 30.93 ? 750 ALA A C 1 ATOM 5970 O O . ALA A 1 757 ? 2.477 82.569 66.305 1.00 34.58 ? 750 ALA A O 1 ATOM 5971 C CB . ALA A 1 757 ? 1.103 80.027 65.725 1.00 27.95 ? 750 ALA A CB 1 ATOM 5972 O OXT . ALA A 1 757 ? 4.062 81.190 66.779 1.00 31.81 ? 750 ALA A OXT 1 HETATM 5973 ZN ZN . ZN B 2 . ? 17.507 41.195 43.212 1.00 19.84 ? 801 ZN A ZN 1 HETATM 5974 ZN ZN . ZN C 2 . ? 16.760 41.962 46.341 1.00 20.97 ? 802 ZN A ZN 1 HETATM 5975 CA CA . CA D 3 . ? -0.758 49.973 41.371 1.00 16.89 ? 803 CA A CA 1 HETATM 5976 CL CL . CL E 4 . ? 19.051 47.050 51.652 1.00 23.47 ? 804 CL A CL 1 HETATM 5977 C C1 . NAG F 5 . ? 11.652 26.033 57.646 1.00 34.07 ? 805 NAG A C1 1 HETATM 5978 C C2 . NAG F 5 . ? 11.442 24.596 57.201 1.00 38.71 ? 805 NAG A C2 1 HETATM 5979 C C3 . NAG F 5 . ? 9.993 24.169 57.449 1.00 40.04 ? 805 NAG A C3 1 HETATM 5980 C C4 . NAG F 5 . ? 9.484 24.509 58.850 1.00 38.89 ? 805 NAG A C4 1 HETATM 5981 C C5 . NAG F 5 . ? 9.859 25.956 59.197 1.00 37.71 ? 805 NAG A C5 1 HETATM 5982 C C6 . NAG F 5 . ? 9.531 26.346 60.643 1.00 39.18 ? 805 NAG A C6 1 HETATM 5983 C C7 . NAG F 5 . ? 12.877 23.873 55.392 1.00 45.12 ? 805 NAG A C7 1 HETATM 5984 C C8 . NAG F 5 . ? 13.112 23.829 53.916 1.00 44.70 ? 805 NAG A C8 1 HETATM 5985 N N2 . NAG F 5 . ? 11.760 24.492 55.787 1.00 41.97 ? 805 NAG A N2 1 HETATM 5986 O O3 . NAG F 5 . ? 9.936 22.781 57.256 1.00 40.70 ? 805 NAG A O3 1 HETATM 5987 O O4 . NAG F 5 . ? 8.071 24.411 58.831 1.00 40.67 ? 805 NAG A O4 1 HETATM 5988 O O5 . NAG F 5 . ? 11.244 26.156 58.991 1.00 34.43 ? 805 NAG A O5 1 HETATM 5989 O O6 . NAG F 5 . ? 10.151 25.413 61.496 1.00 42.65 ? 805 NAG A O6 1 HETATM 5990 O O7 . NAG F 5 . ? 13.686 23.370 56.173 1.00 48.43 ? 805 NAG A O7 1 HETATM 5991 C C1 . NAG G 5 . ? 7.575 23.529 59.853 1.00 44.99 ? 806 NAG A C1 1 HETATM 5992 C C2 . NAG G 5 . ? 6.102 23.864 60.113 1.00 46.48 ? 806 NAG A C2 1 HETATM 5993 C C3 . NAG G 5 . ? 5.433 22.846 61.049 1.00 49.86 ? 806 NAG A C3 1 HETATM 5994 C C4 . NAG G 5 . ? 5.810 21.392 60.733 1.00 51.73 ? 806 NAG A C4 1 HETATM 5995 C C5 . NAG G 5 . ? 7.327 21.261 60.499 1.00 51.49 ? 806 NAG A C5 1 HETATM 5996 C C6 . NAG G 5 . ? 7.748 19.857 60.076 1.00 52.87 ? 806 NAG A C6 1 HETATM 5997 C C7 . NAG G 5 . ? 5.554 26.316 59.986 1.00 44.99 ? 806 NAG A C7 1 HETATM 5998 C C8 . NAG G 5 . ? 5.312 26.193 58.520 1.00 41.05 ? 806 NAG A C8 1 HETATM 5999 N N2 . NAG G 5 . ? 5.918 25.209 60.662 1.00 44.07 ? 806 NAG A N2 1 HETATM 6000 O O3 . NAG G 5 . ? 4.036 23.053 60.926 1.00 50.95 ? 806 NAG A O3 1 HETATM 6001 O O4 . NAG G 5 . ? 5.369 20.502 61.762 1.00 55.21 ? 806 NAG A O4 1 HETATM 6002 O O5 . NAG G 5 . ? 7.715 22.172 59.470 1.00 47.92 ? 806 NAG A O5 1 HETATM 6003 O O6 . NAG G 5 . ? 7.344 19.652 58.733 1.00 53.75 ? 806 NAG A O6 1 HETATM 6004 O O7 . NAG G 5 . ? 5.406 27.435 60.528 1.00 45.03 ? 806 NAG A O7 1 HETATM 6005 C C1 . NAG H 5 . ? 4.104 28.067 25.136 1.00 46.71 ? 807 NAG A C1 1 HETATM 6006 C C2 . NAG H 5 . ? 2.689 28.615 24.998 1.00 49.19 ? 807 NAG A C2 1 HETATM 6007 C C3 . NAG H 5 . ? 1.676 27.629 24.399 1.00 53.08 ? 807 NAG A C3 1 HETATM 6008 C C4 . NAG H 5 . ? 2.281 26.746 23.300 1.00 55.39 ? 807 NAG A C4 1 HETATM 6009 C C5 . NAG H 5 . ? 3.662 26.227 23.748 1.00 55.48 ? 807 NAG A C5 1 HETATM 6010 C C6 . NAG H 5 . ? 4.267 25.162 22.806 1.00 58.85 ? 807 NAG A C6 1 HETATM 6011 C C7 . NAG H 5 . ? 1.974 30.337 26.550 1.00 51.25 ? 807 NAG A C7 1 HETATM 6012 C C8 . NAG H 5 . ? 2.039 31.297 25.398 1.00 50.76 ? 807 NAG A C8 1 HETATM 6013 N N2 . NAG H 5 . ? 2.276 29.064 26.312 1.00 49.53 ? 807 NAG A N2 1 HETATM 6014 O O3 . NAG H 5 . ? 0.617 28.397 23.875 1.00 53.65 ? 807 NAG A O3 1 HETATM 6015 O O4 . NAG H 5 . ? 1.398 25.672 22.977 1.00 58.16 ? 807 NAG A O4 1 HETATM 6016 O O5 . NAG H 5 . ? 4.532 27.339 24.010 1.00 51.86 ? 807 NAG A O5 1 HETATM 6017 O O6 . NAG H 5 . ? 5.161 25.661 21.824 1.00 63.26 ? 807 NAG A O6 1 HETATM 6018 O O7 . NAG H 5 . ? 1.631 30.744 27.658 1.00 54.28 ? 807 NAG A O7 1 HETATM 6019 C C1 . NAG I 5 . ? 20.025 25.001 17.685 1.00 42.90 ? 808 NAG A C1 1 HETATM 6020 C C2 . NAG I 5 . ? 20.626 23.795 16.969 1.00 45.41 ? 808 NAG A C2 1 HETATM 6021 C C3 . NAG I 5 . ? 19.789 23.422 15.752 1.00 46.84 ? 808 NAG A C3 1 HETATM 6022 C C4 . NAG I 5 . ? 18.285 23.349 16.042 1.00 47.41 ? 808 NAG A C4 1 HETATM 6023 C C5 . NAG I 5 . ? 17.789 24.520 16.925 1.00 43.73 ? 808 NAG A C5 1 HETATM 6024 C C6 . NAG I 5 . ? 16.367 24.317 17.470 1.00 42.31 ? 808 NAG A C6 1 HETATM 6025 C C7 . NAG I 5 . ? 23.032 23.566 17.200 1.00 50.25 ? 808 NAG A C7 1 HETATM 6026 C C8 . NAG I 5 . ? 24.410 23.878 16.682 1.00 50.62 ? 808 NAG A C8 1 HETATM 6027 N N2 . NAG I 5 . ? 21.989 24.068 16.543 1.00 47.18 ? 808 NAG A N2 1 HETATM 6028 O O3 . NAG I 5 . ? 20.267 22.190 15.237 1.00 46.92 ? 808 NAG A O3 1 HETATM 6029 O O4 . NAG I 5 . ? 17.636 23.392 14.788 1.00 52.91 ? 808 NAG A O4 1 HETATM 6030 O O5 . NAG I 5 . ? 18.671 24.737 18.013 1.00 43.05 ? 808 NAG A O5 1 HETATM 6031 O O6 . NAG I 5 . ? 16.245 23.124 18.229 1.00 41.67 ? 808 NAG A O6 1 HETATM 6032 O O7 . NAG I 5 . ? 22.896 22.870 18.201 1.00 51.85 ? 808 NAG A O7 1 HETATM 6033 C C1 . NAG J 5 . ? 16.661 22.334 14.647 1.00 56.76 ? 809 NAG A C1 1 HETATM 6034 C C2 . NAG J 5 . ? 15.641 22.790 13.605 1.00 58.18 ? 809 NAG A C2 1 HETATM 6035 C C3 . NAG J 5 . ? 14.616 21.698 13.295 1.00 61.69 ? 809 NAG A C3 1 HETATM 6036 C C4 . NAG J 5 . ? 15.311 20.360 13.026 1.00 63.21 ? 809 NAG A C4 1 HETATM 6037 C C5 . NAG J 5 . ? 16.278 20.034 14.181 1.00 62.45 ? 809 NAG A C5 1 HETATM 6038 C C6 . NAG J 5 . ? 17.001 18.698 14.016 1.00 63.67 ? 809 NAG A C6 1 HETATM 6039 C C7 . NAG J 5 . ? 15.369 25.225 13.586 1.00 56.32 ? 809 NAG A C7 1 HETATM 6040 C C8 . NAG J 5 . ? 14.601 26.407 14.111 1.00 53.87 ? 809 NAG A C8 1 HETATM 6041 N N2 . NAG J 5 . ? 14.982 24.020 14.030 1.00 56.55 ? 809 NAG A N2 1 HETATM 6042 O O3 . NAG J 5 . ? 13.879 22.075 12.152 1.00 63.30 ? 809 NAG A O3 1 HETATM 6043 O O4 . NAG J 5 . ? 14.338 19.349 12.809 1.00 66.57 ? 809 NAG A O4 1 HETATM 6044 O O5 . NAG J 5 . ? 17.238 21.080 14.317 1.00 59.58 ? 809 NAG A O5 1 HETATM 6045 O O6 . NAG J 5 . ? 18.116 18.872 13.172 1.00 64.67 ? 809 NAG A O6 1 HETATM 6046 O O7 . NAG J 5 . ? 16.310 25.397 12.797 1.00 55.90 ? 809 NAG A O7 1 HETATM 6047 C C1 . NAG K 5 . ? 19.734 54.824 10.579 1.00 65.13 ? 810 NAG A C1 1 HETATM 6048 C C2 . NAG K 5 . ? 19.403 56.263 10.173 1.00 70.83 ? 810 NAG A C2 1 HETATM 6049 C C3 . NAG K 5 . ? 17.904 56.374 9.917 1.00 71.60 ? 810 NAG A C3 1 HETATM 6050 C C4 . NAG K 5 . ? 17.512 55.455 8.763 1.00 72.54 ? 810 NAG A C4 1 HETATM 6051 C C5 . NAG K 5 . ? 17.943 54.003 8.999 1.00 70.97 ? 810 NAG A C5 1 HETATM 6052 C C6 . NAG K 5 . ? 18.014 53.320 7.626 1.00 72.45 ? 810 NAG A C6 1 HETATM 6053 C C7 . NAG K 5 . ? 20.959 57.944 11.110 1.00 73.22 ? 810 NAG A C7 1 HETATM 6054 C C8 . NAG K 5 . ? 21.194 58.904 12.241 1.00 72.62 ? 810 NAG A C8 1 HETATM 6055 N N2 . NAG K 5 . ? 19.821 57.239 11.174 1.00 71.43 ? 810 NAG A N2 1 HETATM 6056 O O3 . NAG K 5 . ? 17.578 57.702 9.579 1.00 73.57 ? 810 NAG A O3 1 HETATM 6057 O O4 . NAG K 5 . ? 16.117 55.530 8.534 1.00 73.88 ? 810 NAG A O4 1 HETATM 6058 O O5 . NAG K 5 . ? 19.211 53.860 9.655 1.00 68.51 ? 810 NAG A O5 1 HETATM 6059 O O6 . NAG K 5 . ? 17.928 51.916 7.726 1.00 72.85 ? 810 NAG A O6 1 HETATM 6060 O O7 . NAG K 5 . ? 21.800 57.845 10.207 1.00 75.10 ? 810 NAG A O7 1 HETATM 6061 C C1 . NAG L 5 . ? 36.604 37.712 52.849 1.00 42.22 ? 811 NAG A C1 1 HETATM 6062 C C2 . NAG L 5 . ? 36.596 37.807 51.310 1.00 41.70 ? 811 NAG A C2 1 HETATM 6063 C C3 . NAG L 5 . ? 37.948 37.386 50.658 1.00 45.79 ? 811 NAG A C3 1 HETATM 6064 C C4 . NAG L 5 . ? 39.164 37.997 51.368 1.00 47.94 ? 811 NAG A C4 1 HETATM 6065 C C5 . NAG L 5 . ? 39.016 37.912 52.897 1.00 48.05 ? 811 NAG A C5 1 HETATM 6066 C C6 . NAG L 5 . ? 40.174 38.639 53.596 1.00 48.22 ? 811 NAG A C6 1 HETATM 6067 C C7 . NAG L 5 . ? 34.523 37.686 50.048 1.00 34.85 ? 811 NAG A C7 1 HETATM 6068 C C8 . NAG L 5 . ? 33.377 36.886 49.509 1.00 32.12 ? 811 NAG A C8 1 HETATM 6069 N N2 . NAG L 5 . ? 35.451 37.073 50.781 1.00 38.95 ? 811 NAG A N2 1 HETATM 6070 O O3 . NAG L 5 . ? 38.002 37.859 49.323 1.00 47.36 ? 811 NAG A O3 1 HETATM 6071 O O4 . NAG L 5 . ? 40.417 37.418 50.934 1.00 49.14 ? 811 NAG A O4 1 HETATM 6072 O O5 . NAG L 5 . ? 37.752 38.407 53.352 1.00 43.85 ? 811 NAG A O5 1 HETATM 6073 O O6 . NAG L 5 . ? 40.163 40.024 53.285 1.00 50.68 ? 811 NAG A O6 1 HETATM 6074 O O7 . NAG L 5 . ? 34.578 38.868 49.766 1.00 32.30 ? 811 NAG A O7 1 HETATM 6075 C C1 . NAG M 5 . ? 24.263 61.848 68.729 1.00 29.60 ? 812 NAG A C1 1 HETATM 6076 C C2 . NAG M 5 . ? 22.900 62.489 68.948 1.00 30.01 ? 812 NAG A C2 1 HETATM 6077 C C3 . NAG M 5 . ? 23.096 63.936 69.342 1.00 30.59 ? 812 NAG A C3 1 HETATM 6078 C C4 . NAG M 5 . ? 24.037 64.040 70.534 1.00 32.57 ? 812 NAG A C4 1 HETATM 6079 C C5 . NAG M 5 . ? 25.350 63.305 70.258 1.00 32.19 ? 812 NAG A C5 1 HETATM 6080 C C6 . NAG M 5 . ? 26.319 63.281 71.448 1.00 37.29 ? 812 NAG A C6 1 HETATM 6081 C C7 . NAG M 5 . ? 20.968 61.819 67.675 1.00 36.58 ? 812 NAG A C7 1 HETATM 6082 C C8 . NAG M 5 . ? 20.216 61.816 66.376 1.00 33.47 ? 812 NAG A C8 1 HETATM 6083 N N2 . NAG M 5 . ? 22.133 62.440 67.712 1.00 31.49 ? 812 NAG A N2 1 HETATM 6084 O O3 . NAG M 5 . ? 21.853 64.521 69.653 1.00 33.14 ? 812 NAG A O3 1 HETATM 6085 O O4 . NAG M 5 . ? 24.336 65.398 70.690 1.00 36.46 ? 812 NAG A O4 1 HETATM 6086 O O5 . NAG M 5 . ? 25.064 61.956 69.900 1.00 31.73 ? 812 NAG A O5 1 HETATM 6087 O O6 . NAG M 5 . ? 25.705 62.752 72.609 1.00 39.70 ? 812 NAG A O6 1 HETATM 6088 O O7 . NAG M 5 . ? 20.483 61.283 68.672 1.00 42.95 ? 812 NAG A O7 1 HETATM 6089 C C1 . NAG N 5 . ? 24.110 65.823 72.049 1.00 39.55 ? 813 NAG A C1 1 HETATM 6090 C C2 . NAG N 5 . ? 24.731 67.220 72.144 1.00 43.46 ? 813 NAG A C2 1 HETATM 6091 C C3 . NAG N 5 . ? 24.508 67.817 73.531 1.00 46.82 ? 813 NAG A C3 1 HETATM 6092 C C4 . NAG N 5 . ? 23.022 67.746 73.911 1.00 45.65 ? 813 NAG A C4 1 HETATM 6093 C C5 . NAG N 5 . ? 22.482 66.327 73.700 1.00 44.53 ? 813 NAG A C5 1 HETATM 6094 C C6 . NAG N 5 . ? 20.987 66.276 74.007 1.00 44.95 ? 813 NAG A C6 1 HETATM 6095 C C7 . NAG N 5 . ? 26.711 67.547 70.726 1.00 47.53 ? 813 NAG A C7 1 HETATM 6096 C C8 . NAG N 5 . ? 25.858 68.209 69.694 1.00 45.83 ? 813 NAG A C8 1 HETATM 6097 N N2 . NAG N 5 . ? 26.146 67.104 71.853 1.00 46.72 ? 813 NAG A N2 1 HETATM 6098 O O3 . NAG N 5 . ? 24.977 69.152 73.547 1.00 46.54 ? 813 NAG A O3 1 HETATM 6099 O O4 . NAG N 5 . ? 22.899 68.080 75.280 1.00 49.83 ? 813 NAG A O4 1 HETATM 6100 O O5 . NAG N 5 . ? 22.726 65.906 72.353 1.00 39.23 ? 813 NAG A O5 1 HETATM 6101 O O6 . NAG N 5 . ? 20.281 67.130 73.119 1.00 48.78 ? 813 NAG A O6 1 HETATM 6102 O O7 . NAG N 5 . ? 27.923 67.409 70.522 1.00 52.46 ? 813 NAG A O7 1 HETATM 6103 C C1 . NAG O 5 . ? 15.171 83.867 52.616 1.00 35.06 ? 814 NAG A C1 1 HETATM 6104 C C2 . NAG O 5 . ? 14.203 84.051 51.449 1.00 35.44 ? 814 NAG A C2 1 HETATM 6105 C C3 . NAG O 5 . ? 14.040 85.536 51.142 1.00 41.90 ? 814 NAG A C3 1 HETATM 6106 C C4 . NAG O 5 . ? 13.642 86.300 52.402 1.00 41.97 ? 814 NAG A C4 1 HETATM 6107 C C5 . NAG O 5 . ? 14.598 85.989 53.529 1.00 44.97 ? 814 NAG A C5 1 HETATM 6108 C C6 . NAG O 5 . ? 14.063 86.672 54.783 1.00 47.31 ? 814 NAG A C6 1 HETATM 6109 C C7 . NAG O 5 . ? 13.754 82.566 49.590 1.00 35.42 ? 814 NAG A C7 1 HETATM 6110 C C8 . NAG O 5 . ? 14.306 81.861 48.413 1.00 34.95 ? 814 NAG A C8 1 HETATM 6111 N N2 . NAG O 5 . ? 14.607 83.296 50.291 1.00 32.41 ? 814 NAG A N2 1 HETATM 6112 O O3 . NAG O 5 . ? 13.034 85.658 50.186 1.00 41.14 ? 814 NAG A O3 1 HETATM 6113 O O4 . NAG O 5 . ? 13.723 87.708 52.238 1.00 48.76 ? 814 NAG A O4 1 HETATM 6114 O O5 . NAG O 5 . ? 14.690 84.594 53.722 1.00 39.78 ? 814 NAG A O5 1 HETATM 6115 O O6 . NAG O 5 . ? 15.053 86.751 55.790 1.00 58.54 ? 814 NAG A O6 1 HETATM 6116 O O7 . NAG O 5 . ? 12.620 82.477 49.852 1.00 33.10 ? 814 NAG A O7 1 HETATM 6117 C C1 . NAG P 5 . ? 12.613 88.211 51.513 1.00 48.38 ? 815 NAG A C1 1 HETATM 6118 C C2 . NAG P 5 . ? 12.103 89.493 52.150 1.00 50.59 ? 815 NAG A C2 1 HETATM 6119 C C3 . NAG P 5 . ? 11.109 90.208 51.237 1.00 50.67 ? 815 NAG A C3 1 HETATM 6120 C C4 . NAG P 5 . ? 11.684 90.372 49.841 1.00 50.80 ? 815 NAG A C4 1 HETATM 6121 C C5 . NAG P 5 . ? 12.063 88.978 49.351 1.00 51.38 ? 815 NAG A C5 1 HETATM 6122 C C6 . NAG P 5 . ? 12.633 89.006 47.969 1.00 57.26 ? 815 NAG A C6 1 HETATM 6123 C C7 . NAG P 5 . ? 11.989 89.502 54.582 1.00 55.13 ? 815 NAG A C7 1 HETATM 6124 C C8 . NAG P 5 . ? 13.306 90.190 54.638 1.00 54.23 ? 815 NAG A C8 1 HETATM 6125 N N2 . NAG P 5 . ? 11.458 89.235 53.400 1.00 50.98 ? 815 NAG A N2 1 HETATM 6126 O O3 . NAG P 5 . ? 10.745 91.457 51.820 1.00 54.68 ? 815 NAG A O3 1 HETATM 6127 O O4 . NAG P 5 . ? 10.706 90.874 48.942 1.00 52.89 ? 815 NAG A O4 1 HETATM 6128 O O5 . NAG P 5 . ? 13.051 88.460 50.220 1.00 49.63 ? 815 NAG A O5 1 HETATM 6129 O O6 . NAG P 5 . ? 13.687 89.934 48.057 1.00 63.59 ? 815 NAG A O6 1 HETATM 6130 O O7 . NAG P 5 . ? 11.422 89.188 55.595 1.00 59.59 ? 815 NAG A O7 1 HETATM 6131 C C1 . BMA Q 6 . ? 10.622 92.286 48.933 1.00 51.76 ? 816 BMA A C1 1 HETATM 6132 C C2 . BMA Q 6 . ? 10.388 92.709 47.491 1.00 52.90 ? 816 BMA A C2 1 HETATM 6133 C C3 . BMA Q 6 . ? 10.124 94.187 47.361 1.00 55.18 ? 816 BMA A C3 1 HETATM 6134 C C4 . BMA Q 6 . ? 9.028 94.574 48.334 1.00 57.12 ? 816 BMA A C4 1 HETATM 6135 C C5 . BMA Q 6 . ? 9.346 94.092 49.752 1.00 57.30 ? 816 BMA A C5 1 HETATM 6136 C C6 . BMA Q 6 . ? 8.282 94.379 50.777 1.00 57.89 ? 816 BMA A C6 1 HETATM 6137 O O2 . BMA Q 6 . ? 9.247 92.037 47.004 1.00 50.78 ? 816 BMA A O2 1 HETATM 6138 O O3 . BMA Q 6 . ? 9.721 94.381 46.020 1.00 53.87 ? 816 BMA A O3 1 HETATM 6139 O O4 . BMA Q 6 . ? 8.875 95.969 48.281 1.00 58.79 ? 816 BMA A O4 1 HETATM 6140 O O5 . BMA Q 6 . ? 9.549 92.693 49.729 1.00 53.48 ? 816 BMA A O5 1 HETATM 6141 O O6 . BMA Q 6 . ? 8.641 93.816 52.021 1.00 57.27 ? 816 BMA A O6 1 HETATM 6142 C C1 . MAN R 7 . ? 10.325 95.523 45.418 1.00 60.09 ? 817 MAN A C1 1 HETATM 6143 C C2 . MAN R 7 . ? 9.507 95.916 44.201 1.00 59.91 ? 817 MAN A C2 1 HETATM 6144 C C3 . MAN R 7 . ? 9.688 94.923 43.081 1.00 60.99 ? 817 MAN A C3 1 HETATM 6145 C C4 . MAN R 7 . ? 11.159 94.661 42.813 1.00 63.39 ? 817 MAN A C4 1 HETATM 6146 C C5 . MAN R 7 . ? 11.857 94.307 44.110 1.00 62.21 ? 817 MAN A C5 1 HETATM 6147 C C6 . MAN R 7 . ? 13.323 93.937 43.927 1.00 66.17 ? 817 MAN A C6 1 HETATM 6148 O O2 . MAN R 7 . ? 10.050 97.116 43.751 1.00 62.20 ? 817 MAN A O2 1 HETATM 6149 O O3 . MAN R 7 . ? 9.086 95.405 41.900 1.00 64.40 ? 817 MAN A O3 1 HETATM 6150 O O4 . MAN R 7 . ? 11.295 93.571 41.903 1.00 63.25 ? 817 MAN A O4 1 HETATM 6151 O O5 . MAN R 7 . ? 11.679 95.365 45.016 1.00 59.66 ? 817 MAN A O5 1 HETATM 6152 O O6 . MAN R 7 . ? 14.080 95.008 43.403 1.00 69.53 ? 817 MAN A O6 1 HETATM 6153 O O4 . 28Z S 8 . ? 29.047 47.531 44.912 0.80 57.16 ? 818 28Z A O4 1 HETATM 6154 C C4 . 28Z S 8 . ? 29.346 48.704 45.546 0.80 58.23 ? 818 28Z A C4 1 HETATM 6155 C C4A . 28Z S 8 . ? 29.068 49.974 45.012 1.00 56.83 ? 818 28Z A C4A 1 HETATM 6156 N N3 . 28Z S 8 . ? 29.939 48.626 46.751 0.75 60.31 ? 818 28Z A N3 1 HETATM 6157 C C8A . 28Z S 8 . ? 29.417 51.095 45.783 0.80 57.54 ? 818 28Z A C8A 1 HETATM 6158 N N5 . 28Z S 8 . ? 28.472 50.170 43.803 1.00 55.13 ? 818 28Z A N5 1 HETATM 6159 C C2 . 28Z S 8 . ? 30.260 49.725 47.457 0.80 60.15 ? 818 28Z A C2 1 HETATM 6160 N N8 . 28Z S 8 . ? 29.170 52.337 45.339 0.80 57.51 ? 818 28Z A N8 1 HETATM 6161 N N1 . 28Z S 8 . ? 30.001 50.952 46.981 1.00 59.24 ? 818 28Z A N1 1 HETATM 6162 C C6 . 28Z S 8 . ? 28.230 51.432 43.365 1.00 52.49 ? 818 28Z A C6 1 HETATM 6163 N N2 . 28Z S 8 . ? 30.845 49.593 48.642 0.80 61.58 ? 818 28Z A N2 1 HETATM 6164 C C7 . 28Z S 8 . ? 28.593 52.518 44.161 0.80 54.74 ? 818 28Z A C7 1 HETATM 6165 C C9 . 28Z S 8 . ? 27.581 51.784 42.010 1.00 48.75 ? 818 28Z A C9 1 HETATM 6166 N N10 . 28Z S 8 . ? 26.799 50.702 41.379 1.00 45.32 ? 818 28Z A N10 1 HETATM 6167 C CBH . 28Z S 8 . ? 25.660 50.223 41.918 1.00 40.29 ? 818 28Z A CBH 1 HETATM 6168 C CAL . 28Z S 8 . ? 25.076 50.835 43.029 1.00 37.51 ? 818 28Z A CAL 1 HETATM 6169 C CAK . 28Z S 8 . ? 25.072 49.091 41.352 1.00 38.51 ? 818 28Z A CAK 1 HETATM 6170 C CAN . 28Z S 8 . ? 23.925 50.340 43.607 1.00 34.44 ? 818 28Z A CAN 1 HETATM 6171 C CAM . 28Z S 8 . ? 23.906 48.573 41.932 1.00 34.01 ? 818 28Z A CAM 1 HETATM 6172 C CBI . 28Z S 8 . ? 23.340 49.200 43.044 1.00 32.10 ? 818 28Z A CBI 1 HETATM 6173 C CBF . 28Z S 8 . ? 22.087 48.691 43.699 1.00 31.57 ? 818 28Z A CBF 1 HETATM 6174 O OAF . 28Z S 8 . ? 21.574 49.330 44.615 1.00 33.73 ? 818 28Z A OAF 1 HETATM 6175 N NBA . 28Z S 8 . ? 21.620 47.500 43.312 1.00 29.27 ? 818 28Z A NBA 1 HETATM 6176 C CBO . 28Z S 8 . ? 20.372 47.020 43.949 1.00 27.71 ? 818 28Z A CBO 1 HETATM 6177 C CBD . 28Z S 8 . ? 20.608 46.725 45.400 1.00 31.88 ? 818 28Z A CBD 1 HETATM 6178 O OAI . 28Z S 8 . ? 19.719 47.161 46.150 1.00 36.87 ? 818 28Z A OAI 1 HETATM 6179 C CAS . 28Z S 8 . ? 19.882 45.728 43.257 1.00 24.39 ? 818 28Z A CAS 1 HETATM 6180 C CAQ . 28Z S 8 . ? 18.686 45.085 43.960 1.00 24.61 ? 818 28Z A CAQ 1 HETATM 6181 C CBE . 28Z S 8 . ? 17.897 44.398 42.847 1.00 25.28 ? 818 28Z A CBE 1 HETATM 6182 O OAE . 28Z S 8 . ? 18.305 43.354 42.329 1.00 23.05 ? 818 28Z A OAE 1 HETATM 6183 O OAD . 28Z S 8 . ? 21.663 46.105 45.722 1.00 35.35 ? 818 28Z A OAD 1 HETATM 6184 N N . 28Z S 8 . ? 16.747 44.957 42.464 1.00 23.38 ? 818 28Z A N 1 HETATM 6185 C CA . 28Z S 8 . ? 16.058 44.389 41.292 1.00 23.39 ? 818 28Z A CA 1 HETATM 6186 C C . 28Z S 8 . ? 17.015 44.523 40.075 1.00 24.40 ? 818 28Z A C 1 HETATM 6187 O OXT . 28Z S 8 . ? 17.895 45.437 40.089 1.00 24.69 ? 818 28Z A OXT 1 HETATM 6188 C CB . 28Z S 8 . ? 14.748 45.169 41.009 1.00 23.23 ? 818 28Z A CB 1 HETATM 6189 C CG . 28Z S 8 . ? 15.046 46.649 40.727 1.00 23.24 ? 818 28Z A CG 1 HETATM 6190 C CD . 28Z S 8 . ? 13.826 47.429 40.186 1.00 25.51 ? 818 28Z A CD 1 HETATM 6191 O OE1 . 28Z S 8 . ? 12.985 46.840 39.464 1.00 23.08 ? 818 28Z A OE1 1 HETATM 6192 O OE2 . 28Z S 8 . ? 13.771 48.647 40.472 1.00 22.28 ? 818 28Z A OE2 1 HETATM 6193 O O . 28Z S 8 . ? 16.865 43.687 39.147 1.00 24.81 ? 818 28Z A O 1 HETATM 6194 O O . HOH T 9 . ? 8.224 44.735 46.337 1.00 16.61 ? 901 HOH A O 1 HETATM 6195 O O . HOH T 9 . ? 6.889 58.305 37.530 1.00 17.88 ? 902 HOH A O 1 HETATM 6196 O O . HOH T 9 . ? 7.939 69.626 59.073 1.00 19.38 ? 903 HOH A O 1 HETATM 6197 O O . HOH T 9 . ? 13.634 44.778 49.798 1.00 21.66 ? 904 HOH A O 1 HETATM 6198 O O . HOH T 9 . ? 9.212 50.711 46.436 1.00 17.09 ? 905 HOH A O 1 HETATM 6199 O O . HOH T 9 . ? 0.976 50.500 39.799 1.00 16.66 ? 906 HOH A O 1 HETATM 6200 O O . HOH T 9 . ? 12.031 61.998 43.439 1.00 17.90 ? 907 HOH A O 1 HETATM 6201 O O . HOH T 9 . ? 13.652 29.901 40.081 1.00 22.06 ? 908 HOH A O 1 HETATM 6202 O O . HOH T 9 . ? 15.128 41.830 38.675 1.00 19.76 ? 909 HOH A O 1 HETATM 6203 O O . HOH T 9 . ? 9.624 60.882 57.601 1.00 18.28 ? 910 HOH A O 1 HETATM 6204 O O . HOH T 9 . ? 10.918 36.766 42.279 1.00 18.20 ? 911 HOH A O 1 HETATM 6205 O O . HOH T 9 . ? -5.469 59.769 59.746 1.00 19.90 ? 912 HOH A O 1 HETATM 6206 O O . HOH T 9 . ? 13.645 27.077 51.582 1.00 24.53 ? 913 HOH A O 1 HETATM 6207 O O . HOH T 9 . ? 7.410 71.848 45.177 1.00 20.97 ? 914 HOH A O 1 HETATM 6208 O O . HOH T 9 . ? 5.756 68.936 55.294 1.00 20.25 ? 915 HOH A O 1 HETATM 6209 O O . HOH T 9 . ? 16.839 37.142 43.914 1.00 18.93 ? 916 HOH A O 1 HETATM 6210 O O . HOH T 9 . ? -3.631 62.239 53.888 1.00 21.25 ? 917 HOH A O 1 HETATM 6211 O O . HOH T 9 . ? 29.432 36.144 44.413 1.00 23.61 ? 918 HOH A O 1 HETATM 6212 O O . HOH T 9 . ? 6.436 75.981 60.923 1.00 21.29 ? 919 HOH A O 1 HETATM 6213 O O . HOH T 9 . ? -3.484 60.145 61.752 1.00 20.81 ? 920 HOH A O 1 HETATM 6214 O O . HOH T 9 . ? 19.302 47.822 54.730 1.00 21.12 ? 921 HOH A O 1 HETATM 6215 O O . HOH T 9 . ? 3.950 70.483 64.316 1.00 24.14 ? 922 HOH A O 1 HETATM 6216 O O . HOH T 9 . ? 18.956 62.247 36.268 1.00 19.88 ? 923 HOH A O 1 HETATM 6217 O O . HOH T 9 . ? -7.053 51.653 51.422 1.00 20.44 ? 924 HOH A O 1 HETATM 6218 O O . HOH T 9 . ? 17.848 40.596 32.195 1.00 21.59 ? 925 HOH A O 1 HETATM 6219 O O . HOH T 9 . ? 20.060 61.511 62.856 1.00 22.96 ? 926 HOH A O 1 HETATM 6220 O O . HOH T 9 . ? -4.434 59.524 57.117 1.00 20.83 ? 927 HOH A O 1 HETATM 6221 O O . HOH T 9 . ? 3.517 72.002 43.449 1.00 19.36 ? 928 HOH A O 1 HETATM 6222 O O . HOH T 9 . ? 29.996 42.758 32.157 1.00 26.70 ? 929 HOH A O 1 HETATM 6223 O O . HOH T 9 . ? 23.876 46.176 34.581 1.00 22.17 ? 930 HOH A O 1 HETATM 6224 O O . HOH T 9 . ? 14.747 36.874 27.913 1.00 22.00 ? 931 HOH A O 1 HETATM 6225 O O . HOH T 9 . ? 18.463 33.621 43.489 1.00 22.35 ? 932 HOH A O 1 HETATM 6226 O O . HOH T 9 . ? 28.937 33.993 32.762 1.00 26.53 ? 933 HOH A O 1 HETATM 6227 O O . HOH T 9 . ? 6.005 75.390 54.090 1.00 22.98 ? 934 HOH A O 1 HETATM 6228 O O . HOH T 9 . ? 3.635 62.357 50.413 1.00 20.46 ? 935 HOH A O 1 HETATM 6229 O O . HOH T 9 . ? 14.626 32.158 48.077 1.00 20.80 ? 936 HOH A O 1 HETATM 6230 O O . HOH T 9 . ? 4.621 35.019 45.361 1.00 21.32 ? 937 HOH A O 1 HETATM 6231 O O . HOH T 9 . ? 0.241 56.988 45.669 1.00 23.33 ? 938 HOH A O 1 HETATM 6232 O O . HOH T 9 . ? -0.381 43.540 60.639 1.00 28.02 ? 939 HOH A O 1 HETATM 6233 O O . HOH T 9 . ? 14.424 38.145 34.806 1.00 21.57 ? 940 HOH A O 1 HETATM 6234 O O . HOH T 9 . ? 22.127 88.077 32.427 1.00 31.53 ? 941 HOH A O 1 HETATM 6235 O O . HOH T 9 . ? 23.201 67.837 34.168 1.00 24.18 ? 942 HOH A O 1 HETATM 6236 O O . HOH T 9 . ? 23.130 68.741 42.862 1.00 24.40 ? 943 HOH A O 1 HETATM 6237 O O . HOH T 9 . ? 20.580 45.833 36.306 1.00 19.85 ? 944 HOH A O 1 HETATM 6238 O O . HOH T 9 . ? 24.450 37.312 32.505 1.00 23.71 ? 945 HOH A O 1 HETATM 6239 O O . HOH T 9 . ? 16.152 55.715 35.471 1.00 19.86 ? 946 HOH A O 1 HETATM 6240 O O . HOH T 9 . ? 25.778 37.164 38.071 1.00 23.72 ? 947 HOH A O 1 HETATM 6241 O O . HOH T 9 . ? 9.572 29.241 43.018 1.00 23.12 ? 948 HOH A O 1 HETATM 6242 O O . HOH T 9 . ? 27.521 31.186 28.752 1.00 28.71 ? 949 HOH A O 1 HETATM 6243 O O . HOH T 9 . ? 20.674 27.582 48.775 1.00 26.29 ? 950 HOH A O 1 HETATM 6244 O O . HOH T 9 . ? 10.165 30.972 26.678 1.00 28.49 ? 951 HOH A O 1 HETATM 6245 O O . HOH T 9 . ? 29.110 60.627 57.451 1.00 35.73 ? 952 HOH A O 1 HETATM 6246 O O . HOH T 9 . ? 16.907 62.033 38.225 1.00 19.45 ? 953 HOH A O 1 HETATM 6247 O O . HOH T 9 . ? 19.266 36.152 43.101 1.00 21.44 ? 954 HOH A O 1 HETATM 6248 O O . HOH T 9 . ? 20.187 31.337 43.500 1.00 25.50 ? 955 HOH A O 1 HETATM 6249 O O . HOH T 9 . ? 8.015 50.336 40.854 1.00 18.73 ? 956 HOH A O 1 HETATM 6250 O O . HOH T 9 . ? -2.580 44.221 37.662 1.00 21.66 ? 957 HOH A O 1 HETATM 6251 O O . HOH T 9 . ? 6.470 60.855 67.022 1.00 24.86 ? 958 HOH A O 1 HETATM 6252 O O . HOH T 9 . ? 5.148 64.657 37.023 1.00 19.88 ? 959 HOH A O 1 HETATM 6253 O O . HOH T 9 . ? 14.701 80.836 38.153 1.00 25.65 ? 960 HOH A O 1 HETATM 6254 O O . HOH T 9 . ? 6.794 54.978 43.831 1.00 18.23 ? 961 HOH A O 1 HETATM 6255 O O . HOH T 9 . ? 13.957 40.890 53.470 1.00 20.55 ? 962 HOH A O 1 HETATM 6256 O O . HOH T 9 . ? 11.097 27.507 54.258 1.00 27.20 ? 963 HOH A O 1 HETATM 6257 O O . HOH T 9 . ? 22.987 44.568 36.535 1.00 22.18 ? 964 HOH A O 1 HETATM 6258 O O . HOH T 9 . ? 13.846 67.990 34.740 1.00 24.23 ? 965 HOH A O 1 HETATM 6259 O O . HOH T 9 . ? 4.345 67.030 51.438 1.00 21.48 ? 966 HOH A O 1 HETATM 6260 O O . HOH T 9 . ? 4.019 68.626 49.190 1.00 22.57 ? 967 HOH A O 1 HETATM 6261 O O . HOH T 9 . ? -4.534 55.281 51.696 1.00 23.01 ? 968 HOH A O 1 HETATM 6262 O O . HOH T 9 . ? 1.250 59.295 46.433 1.00 26.90 ? 969 HOH A O 1 HETATM 6263 O O . HOH T 9 . ? 2.604 33.174 45.227 1.00 24.25 ? 970 HOH A O 1 HETATM 6264 O O . HOH T 9 . ? -3.890 57.688 46.334 1.00 24.35 ? 971 HOH A O 1 HETATM 6265 O O . HOH T 9 . ? 11.183 63.484 58.190 1.00 25.85 ? 972 HOH A O 1 HETATM 6266 O O . HOH T 9 . ? 28.701 53.819 53.202 1.00 26.90 ? 973 HOH A O 1 HETATM 6267 O O . HOH T 9 . ? 13.717 71.438 40.426 1.00 20.98 ? 974 HOH A O 1 HETATM 6268 O O . HOH T 9 . ? 19.010 27.768 35.059 1.00 23.72 ? 975 HOH A O 1 HETATM 6269 O O . HOH T 9 . ? 13.350 77.827 63.515 1.00 31.36 ? 976 HOH A O 1 HETATM 6270 O O . HOH T 9 . ? 34.624 41.575 50.487 1.00 35.04 ? 977 HOH A O 1 HETATM 6271 O O . HOH T 9 . ? 26.425 38.969 36.258 1.00 24.81 ? 978 HOH A O 1 HETATM 6272 O O . HOH T 9 . ? -2.535 59.337 48.463 1.00 24.60 ? 979 HOH A O 1 HETATM 6273 O O . HOH T 9 . ? 8.795 74.652 66.641 1.00 28.03 ? 980 HOH A O 1 HETATM 6274 O O . HOH T 9 . ? 24.414 31.789 28.718 1.00 28.92 ? 981 HOH A O 1 HETATM 6275 O O . HOH T 9 . ? 5.606 62.743 64.998 1.00 28.53 ? 982 HOH A O 1 HETATM 6276 O O . HOH T 9 . ? 14.341 31.902 29.470 1.00 27.08 ? 983 HOH A O 1 HETATM 6277 O O . HOH T 9 . ? 12.057 35.065 53.638 1.00 23.25 ? 984 HOH A O 1 HETATM 6278 O O . HOH T 9 . ? 10.599 37.356 54.391 1.00 30.63 ? 985 HOH A O 1 HETATM 6279 O O . HOH T 9 . ? 21.173 63.537 60.956 1.00 25.25 ? 986 HOH A O 1 HETATM 6280 O O . HOH T 9 . ? 3.559 27.654 41.382 1.00 31.08 ? 987 HOH A O 1 HETATM 6281 O O . HOH T 9 . ? 19.272 60.160 50.103 1.00 25.60 ? 988 HOH A O 1 HETATM 6282 O O . HOH T 9 . ? 20.686 53.296 47.402 1.00 23.72 ? 989 HOH A O 1 HETATM 6283 O O . HOH T 9 . ? 31.351 40.004 46.592 1.00 28.13 ? 990 HOH A O 1 HETATM 6284 O O . HOH T 9 . ? 5.467 78.074 54.444 1.00 26.22 ? 991 HOH A O 1 HETATM 6285 O O . HOH T 9 . ? 32.215 35.088 59.361 1.00 31.28 ? 992 HOH A O 1 HETATM 6286 O O . HOH T 9 . ? 21.819 61.663 36.582 1.00 25.14 ? 993 HOH A O 1 HETATM 6287 O O . HOH T 9 . ? 16.259 72.184 29.584 1.00 23.99 ? 994 HOH A O 1 HETATM 6288 O O . HOH T 9 . ? 14.636 58.988 74.468 1.00 32.47 ? 995 HOH A O 1 HETATM 6289 O O . HOH T 9 . ? 29.450 70.271 45.969 1.00 27.66 ? 996 HOH A O 1 HETATM 6290 O O . HOH T 9 . ? -2.162 55.592 46.114 1.00 22.61 ? 997 HOH A O 1 HETATM 6291 O O . HOH T 9 . ? 23.879 40.593 69.428 1.00 33.86 ? 998 HOH A O 1 HETATM 6292 O O . HOH T 9 . ? 5.650 62.858 70.450 1.00 26.65 ? 999 HOH A O 1 HETATM 6293 O O . HOH T 9 . ? 16.732 68.237 64.244 1.00 28.08 ? 1000 HOH A O 1 HETATM 6294 O O . HOH T 9 . ? 25.015 32.821 67.827 1.00 34.10 ? 1001 HOH A O 1 HETATM 6295 O O . HOH T 9 . ? -6.283 58.741 37.997 1.00 28.79 ? 1002 HOH A O 1 HETATM 6296 O O . HOH T 9 . ? 14.992 61.872 73.105 1.00 30.99 ? 1003 HOH A O 1 HETATM 6297 O O . HOH T 9 . ? 0.241 31.420 58.185 1.00 31.39 ? 1004 HOH A O 1 HETATM 6298 O O . HOH T 9 . ? 18.366 55.585 30.364 1.00 28.10 ? 1005 HOH A O 1 HETATM 6299 O O . HOH T 9 . ? 8.964 69.066 40.850 1.00 23.06 ? 1006 HOH A O 1 HETATM 6300 O O . HOH T 9 . ? 12.145 37.043 28.619 1.00 23.37 ? 1007 HOH A O 1 HETATM 6301 O O . HOH T 9 . ? 0.516 33.391 43.303 1.00 26.23 ? 1008 HOH A O 1 HETATM 6302 O O . HOH T 9 . ? 33.919 47.919 59.244 1.00 30.94 ? 1009 HOH A O 1 HETATM 6303 O O . HOH T 9 . ? 17.220 81.713 37.346 1.00 30.49 ? 1010 HOH A O 1 HETATM 6304 O O . HOH T 9 . ? 15.172 69.084 41.517 1.00 27.74 ? 1011 HOH A O 1 HETATM 6305 O O . HOH T 9 . ? 16.413 26.236 34.666 1.00 26.74 ? 1012 HOH A O 1 HETATM 6306 O O . HOH T 9 . ? 23.121 55.315 31.144 1.00 25.31 ? 1013 HOH A O 1 HETATM 6307 O O . HOH T 9 . ? 17.647 82.554 41.171 1.00 36.02 ? 1014 HOH A O 1 HETATM 6308 O O . HOH T 9 . ? 24.066 75.066 54.430 1.00 29.27 ? 1015 HOH A O 1 HETATM 6309 O O . HOH T 9 . ? 23.070 67.507 40.475 1.00 28.04 ? 1016 HOH A O 1 HETATM 6310 O O . HOH T 9 . ? 8.239 51.709 43.234 1.00 25.57 ? 1017 HOH A O 1 HETATM 6311 O O . HOH T 9 . ? 30.053 27.159 33.734 1.00 31.89 ? 1018 HOH A O 1 HETATM 6312 O O . HOH T 9 . ? 6.157 38.728 26.325 1.00 29.42 ? 1019 HOH A O 1 HETATM 6313 O O . HOH T 9 . ? 18.884 69.046 65.728 1.00 34.70 ? 1020 HOH A O 1 HETATM 6314 O O . HOH T 9 . ? 21.832 74.541 60.575 1.00 31.22 ? 1021 HOH A O 1 HETATM 6315 O O . HOH T 9 . ? -2.163 33.991 40.502 1.00 27.10 ? 1022 HOH A O 1 HETATM 6316 O O . HOH T 9 . ? 13.556 82.784 55.704 1.00 28.66 ? 1023 HOH A O 1 HETATM 6317 O O . HOH T 9 . ? 25.656 35.562 68.148 1.00 32.24 ? 1024 HOH A O 1 HETATM 6318 O O . HOH T 9 . ? 23.789 73.174 59.303 1.00 32.13 ? 1025 HOH A O 1 HETATM 6319 O O . HOH T 9 . ? -1.352 61.652 62.254 1.00 31.05 ? 1026 HOH A O 1 HETATM 6320 O O . HOH T 9 . ? 10.080 36.084 69.945 1.00 35.40 ? 1027 HOH A O 1 HETATM 6321 O O . HOH T 9 . ? 14.030 57.574 35.060 1.00 22.53 ? 1028 HOH A O 1 HETATM 6322 O O . HOH T 9 . ? 13.601 29.520 28.518 1.00 28.20 ? 1029 HOH A O 1 HETATM 6323 O O . HOH T 9 . ? 10.854 29.053 40.433 1.00 28.83 ? 1030 HOH A O 1 HETATM 6324 O O . HOH T 9 . ? 11.789 41.013 55.369 1.00 24.72 ? 1031 HOH A O 1 HETATM 6325 O O . HOH T 9 . ? 19.248 63.760 32.094 1.00 30.18 ? 1032 HOH A O 1 HETATM 6326 O O . HOH T 9 . ? 12.608 53.421 35.860 1.00 24.27 ? 1033 HOH A O 1 HETATM 6327 O O . HOH T 9 . ? 23.271 56.687 45.108 1.00 33.59 ? 1034 HOH A O 1 HETATM 6328 O O . HOH T 9 . ? 21.858 61.370 51.637 1.00 28.16 ? 1035 HOH A O 1 HETATM 6329 O O . HOH T 9 . ? 25.793 27.300 24.360 1.00 35.24 ? 1036 HOH A O 1 HETATM 6330 O O . HOH T 9 . ? 25.357 56.225 37.137 1.00 30.79 ? 1037 HOH A O 1 HETATM 6331 O O . HOH T 9 . ? 20.198 31.473 26.208 1.00 32.21 ? 1038 HOH A O 1 HETATM 6332 O O . HOH T 9 . ? 31.039 52.466 53.001 1.00 32.38 ? 1039 HOH A O 1 HETATM 6333 O O . HOH T 9 . ? 6.485 76.379 67.295 1.00 33.18 ? 1040 HOH A O 1 HETATM 6334 O O . HOH T 9 . ? 10.473 55.545 75.134 1.00 37.28 ? 1041 HOH A O 1 HETATM 6335 O O . HOH T 9 . ? 21.396 32.515 28.639 1.00 29.42 ? 1042 HOH A O 1 HETATM 6336 O O . HOH T 9 . ? 25.333 70.650 31.178 1.00 29.08 ? 1043 HOH A O 1 HETATM 6337 O O . HOH T 9 . ? 19.079 69.678 28.439 1.00 29.92 ? 1044 HOH A O 1 HETATM 6338 O O . HOH T 9 . ? 23.481 78.995 50.487 1.00 31.50 ? 1045 HOH A O 1 HETATM 6339 O O . HOH T 9 . ? -9.668 46.015 34.269 1.00 34.92 ? 1046 HOH A O 1 HETATM 6340 O O . HOH T 9 . ? 29.040 40.386 64.944 1.00 31.76 ? 1047 HOH A O 1 HETATM 6341 O O . HOH T 9 . ? 11.646 27.779 29.237 1.00 34.45 ? 1048 HOH A O 1 HETATM 6342 O O . HOH T 9 . ? 25.356 63.370 49.821 1.00 30.18 ? 1049 HOH A O 1 HETATM 6343 O O . HOH T 9 . ? 16.237 29.114 28.068 1.00 29.03 ? 1050 HOH A O 1 HETATM 6344 O O . HOH T 9 . ? 13.836 79.925 67.881 1.00 35.86 ? 1051 HOH A O 1 HETATM 6345 O O . HOH T 9 . ? 4.879 31.527 30.457 1.00 38.80 ? 1052 HOH A O 1 HETATM 6346 O O . HOH T 9 . ? 14.345 81.357 40.763 1.00 41.09 ? 1053 HOH A O 1 HETATM 6347 O O . HOH T 9 . ? 10.314 81.100 63.522 1.00 31.70 ? 1054 HOH A O 1 HETATM 6348 O O . HOH T 9 . ? 4.218 63.510 72.632 1.00 31.31 ? 1055 HOH A O 1 HETATM 6349 O O . HOH T 9 . ? -10.418 48.646 48.573 1.00 30.53 ? 1056 HOH A O 1 HETATM 6350 O O . HOH T 9 . ? 21.718 84.064 47.157 1.00 35.86 ? 1057 HOH A O 1 HETATM 6351 O O . HOH T 9 . ? 18.126 21.298 38.753 1.00 42.48 ? 1058 HOH A O 1 HETATM 6352 O O . HOH T 9 . ? 27.480 54.201 50.786 1.00 35.38 ? 1059 HOH A O 1 HETATM 6353 O O . HOH T 9 . ? 7.530 38.583 29.309 1.00 29.09 ? 1060 HOH A O 1 HETATM 6354 O O . HOH T 9 . ? 38.225 34.490 26.559 1.00 40.67 ? 1061 HOH A O 1 HETATM 6355 O O . HOH T 9 . ? 4.719 62.178 75.097 1.00 29.10 ? 1062 HOH A O 1 HETATM 6356 O O . HOH T 9 . ? -1.644 32.326 44.580 1.00 34.45 ? 1063 HOH A O 1 HETATM 6357 O O . HOH T 9 . ? -10.104 43.888 46.992 1.00 35.99 ? 1064 HOH A O 1 HETATM 6358 O O . HOH T 9 . ? 29.390 54.586 34.536 1.00 32.58 ? 1065 HOH A O 1 HETATM 6359 O O . HOH T 9 . ? 11.709 47.678 37.335 1.00 20.43 ? 1066 HOH A O 1 HETATM 6360 O O . HOH T 9 . ? -0.716 58.212 43.318 1.00 22.97 ? 1067 HOH A O 1 HETATM 6361 O O . HOH T 9 . ? 22.537 58.515 24.180 1.00 33.21 ? 1068 HOH A O 1 HETATM 6362 O O . HOH T 9 . ? -3.051 38.617 63.012 1.00 37.79 ? 1069 HOH A O 1 HETATM 6363 O O . HOH T 9 . ? 11.626 38.476 56.575 1.00 32.05 ? 1070 HOH A O 1 HETATM 6364 O O . HOH T 9 . ? 25.597 67.054 30.058 1.00 29.08 ? 1071 HOH A O 1 HETATM 6365 O O . HOH T 9 . ? 16.797 69.265 20.667 1.00 48.14 ? 1072 HOH A O 1 HETATM 6366 O O . HOH T 9 . ? 11.973 63.787 35.397 1.00 29.40 ? 1073 HOH A O 1 HETATM 6367 O O . HOH T 9 . ? 25.157 66.002 40.079 1.00 41.50 ? 1074 HOH A O 1 HETATM 6368 O O . HOH T 9 . ? 31.775 55.334 26.138 1.00 36.95 ? 1075 HOH A O 1 HETATM 6369 O O . HOH T 9 . ? 18.057 30.984 29.112 1.00 27.66 ? 1076 HOH A O 1 HETATM 6370 O O . HOH T 9 . ? 28.985 26.137 36.053 1.00 33.33 ? 1077 HOH A O 1 HETATM 6371 O O . HOH T 9 . ? 16.653 79.743 21.015 1.00 45.71 ? 1078 HOH A O 1 HETATM 6372 O O . HOH T 9 . ? 19.973 25.767 36.814 1.00 28.21 ? 1079 HOH A O 1 HETATM 6373 O O . HOH T 9 . ? 27.889 45.253 69.049 1.00 34.76 ? 1080 HOH A O 1 HETATM 6374 O O . HOH T 9 . ? 17.758 52.383 75.104 1.00 37.70 ? 1081 HOH A O 1 HETATM 6375 O O . HOH T 9 . ? 0.392 33.569 36.455 1.00 42.13 ? 1082 HOH A O 1 HETATM 6376 O O . HOH T 9 . ? 25.720 25.444 20.192 1.00 43.14 ? 1083 HOH A O 1 HETATM 6377 O O . HOH T 9 . ? 20.633 30.248 29.907 1.00 30.16 ? 1084 HOH A O 1 HETATM 6378 O O . HOH T 9 . ? 12.862 69.473 32.591 1.00 29.67 ? 1085 HOH A O 1 HETATM 6379 O O . HOH T 9 . ? 24.652 29.549 30.379 1.00 32.59 ? 1086 HOH A O 1 HETATM 6380 O O . HOH T 9 . ? 24.036 82.254 42.296 1.00 36.06 ? 1087 HOH A O 1 HETATM 6381 O O . HOH T 9 . ? 29.211 79.091 27.498 1.00 44.39 ? 1088 HOH A O 1 HETATM 6382 O O . HOH T 9 . ? 10.443 27.162 51.568 1.00 29.86 ? 1089 HOH A O 1 HETATM 6383 O O . HOH T 9 . ? 5.039 40.156 23.124 1.00 35.31 ? 1090 HOH A O 1 HETATM 6384 O O . HOH T 9 . ? 36.159 42.830 57.794 1.00 36.93 ? 1091 HOH A O 1 HETATM 6385 O O . HOH T 9 . ? 36.687 52.254 68.849 1.00 39.95 ? 1092 HOH A O 1 HETATM 6386 O O . HOH T 9 . ? 9.920 69.849 38.530 1.00 26.49 ? 1093 HOH A O 1 HETATM 6387 O O . HOH T 9 . ? 22.902 65.438 66.054 1.00 36.52 ? 1094 HOH A O 1 HETATM 6388 O O . HOH T 9 . ? 27.129 57.028 70.495 1.00 35.12 ? 1095 HOH A O 1 HETATM 6389 O O . HOH T 9 . ? 6.973 75.832 37.605 1.00 28.28 ? 1096 HOH A O 1 HETATM 6390 O O . HOH T 9 . ? 39.721 43.807 58.626 1.00 37.82 ? 1097 HOH A O 1 HETATM 6391 O O . HOH T 9 . ? 26.889 16.758 40.122 1.00 44.98 ? 1098 HOH A O 1 HETATM 6392 O O . HOH T 9 . ? 28.013 71.871 52.659 1.00 37.20 ? 1099 HOH A O 1 HETATM 6393 O O . HOH T 9 . ? 4.989 31.568 24.449 1.00 36.39 ? 1100 HOH A O 1 HETATM 6394 O O . HOH T 9 . ? 26.326 60.219 30.464 1.00 38.51 ? 1101 HOH A O 1 HETATM 6395 O O . HOH T 9 . ? -1.723 46.049 55.692 1.00 35.98 ? 1102 HOH A O 1 HETATM 6396 O O . HOH T 9 . ? 1.479 31.088 64.751 1.00 38.50 ? 1103 HOH A O 1 HETATM 6397 O O . HOH T 9 . ? 21.561 25.258 23.787 1.00 39.53 ? 1104 HOH A O 1 HETATM 6398 O O . HOH T 9 . ? 23.841 61.471 34.631 1.00 31.49 ? 1105 HOH A O 1 HETATM 6399 O O . HOH T 9 . ? 11.103 76.724 28.500 1.00 35.11 ? 1106 HOH A O 1 HETATM 6400 O O . HOH T 9 . ? 26.331 23.530 45.723 1.00 35.88 ? 1107 HOH A O 1 HETATM 6401 O O . HOH T 9 . ? 20.393 44.012 11.292 1.00 40.40 ? 1108 HOH A O 1 HETATM 6402 O O . HOH T 9 . ? -3.983 37.400 56.508 1.00 38.58 ? 1109 HOH A O 1 HETATM 6403 O O . HOH T 9 . ? 16.122 67.423 72.502 1.00 51.81 ? 1110 HOH A O 1 HETATM 6404 O O . HOH T 9 . ? 11.526 48.879 29.562 1.00 22.71 ? 1111 HOH A O 1 HETATM 6405 O O . HOH T 9 . ? 5.290 66.051 33.717 1.00 39.53 ? 1112 HOH A O 1 HETATM 6406 O O . HOH T 9 . ? -2.877 38.018 32.484 1.00 32.52 ? 1113 HOH A O 1 HETATM 6407 O O . HOH T 9 . ? 24.272 77.738 53.050 1.00 38.19 ? 1114 HOH A O 1 HETATM 6408 O O . HOH T 9 . ? 20.914 74.579 23.709 1.00 38.90 ? 1115 HOH A O 1 HETATM 6409 O O . HOH T 9 . ? 10.179 51.756 39.965 1.00 17.12 ? 1116 HOH A O 1 HETATM 6410 O O . HOH T 9 . ? 30.705 84.223 28.526 1.00 43.81 ? 1117 HOH A O 1 HETATM 6411 O O . HOH T 9 . ? 0.449 63.238 48.077 1.00 31.67 ? 1118 HOH A O 1 HETATM 6412 O O . HOH T 9 . ? 26.568 66.221 26.225 1.00 35.81 ? 1119 HOH A O 1 HETATM 6413 O O . HOH T 9 . ? -4.277 53.264 37.157 1.00 30.11 ? 1120 HOH A O 1 HETATM 6414 O O . HOH T 9 . ? 28.455 44.495 65.579 1.00 39.39 ? 1121 HOH A O 1 HETATM 6415 O O . HOH T 9 . ? 8.373 82.536 52.009 1.00 33.16 ? 1122 HOH A O 1 HETATM 6416 O O . HOH T 9 . ? 33.025 30.077 24.437 1.00 41.58 ? 1123 HOH A O 1 HETATM 6417 O O . HOH T 9 . ? 14.902 52.598 34.702 1.00 26.44 ? 1124 HOH A O 1 HETATM 6418 O O . HOH T 9 . ? 15.053 24.614 58.501 1.00 38.37 ? 1125 HOH A O 1 HETATM 6419 O O . HOH T 9 . ? 4.238 43.734 75.851 1.00 44.26 ? 1126 HOH A O 1 HETATM 6420 O O . HOH T 9 . ? 8.753 51.988 75.313 1.00 41.59 ? 1127 HOH A O 1 HETATM 6421 O O . HOH T 9 . ? 18.858 66.073 27.843 1.00 36.46 ? 1128 HOH A O 1 HETATM 6422 O O . HOH T 9 . ? 17.838 32.318 70.505 1.00 37.30 ? 1129 HOH A O 1 HETATM 6423 O O . HOH T 9 . ? 13.828 50.265 18.816 1.00 37.57 ? 1130 HOH A O 1 HETATM 6424 O O . HOH T 9 . ? 17.673 65.326 30.300 1.00 32.21 ? 1131 HOH A O 1 HETATM 6425 O O . HOH T 9 . ? 25.829 24.836 57.644 1.00 34.69 ? 1132 HOH A O 1 HETATM 6426 O O . HOH T 9 . ? 29.239 69.791 39.502 1.00 38.05 ? 1133 HOH A O 1 HETATM 6427 O O . HOH T 9 . ? 3.598 27.266 54.588 1.00 34.35 ? 1134 HOH A O 1 HETATM 6428 O O . HOH T 9 . ? 15.098 81.647 28.367 1.00 42.86 ? 1135 HOH A O 1 HETATM 6429 O O . HOH T 9 . ? -4.566 53.985 34.596 1.00 35.92 ? 1136 HOH A O 1 HETATM 6430 O O . HOH T 9 . ? 21.543 75.287 66.968 1.00 46.36 ? 1137 HOH A O 1 HETATM 6431 O O . HOH T 9 . ? 21.322 88.527 44.161 1.00 36.25 ? 1138 HOH A O 1 HETATM 6432 O O . HOH T 9 . ? -4.253 37.224 51.422 1.00 48.62 ? 1139 HOH A O 1 HETATM 6433 O O . HOH T 9 . ? 13.843 65.329 35.801 1.00 36.44 ? 1140 HOH A O 1 HETATM 6434 O O . HOH T 9 . ? 33.965 40.014 47.484 1.00 36.73 ? 1141 HOH A O 1 HETATM 6435 O O . HOH T 9 . ? 11.966 50.064 36.374 1.00 21.00 ? 1142 HOH A O 1 HETATM 6436 O O . HOH T 9 . ? 31.155 31.781 17.042 0.80 36.93 ? 1143 HOH A O 1 HETATM 6437 O O . HOH T 9 . ? 30.189 59.870 24.993 0.50 28.73 ? 1144 HOH A O 1 HETATM 6438 O O . HOH T 9 . ? 12.221 43.606 17.199 1.00 40.89 ? 1145 HOH A O 1 HETATM 6439 O O . HOH T 9 . ? 26.664 69.303 29.046 1.00 35.60 ? 1146 HOH A O 1 HETATM 6440 O O . HOH T 9 . ? -5.075 42.088 50.504 1.00 37.54 ? 1147 HOH A O 1 HETATM 6441 O O . HOH T 9 . ? 36.734 43.171 49.575 1.00 44.82 ? 1148 HOH A O 1 HETATM 6442 O O . HOH T 9 . ? -3.379 47.104 53.072 1.00 35.35 ? 1149 HOH A O 1 HETATM 6443 O O . HOH T 9 . ? -0.879 32.420 60.596 1.00 42.34 ? 1150 HOH A O 1 HETATM 6444 O O . HOH T 9 . ? 16.256 79.524 69.373 1.00 49.90 ? 1151 HOH A O 1 HETATM 6445 O O . HOH T 9 . ? -8.679 41.511 48.158 1.00 38.46 ? 1152 HOH A O 1 HETATM 6446 O O . HOH T 9 . ? 19.704 56.052 22.834 1.00 37.12 ? 1153 HOH A O 1 HETATM 6447 O O . HOH T 9 . ? 32.516 42.831 20.010 1.00 43.25 ? 1154 HOH A O 1 HETATM 6448 O O . HOH T 9 . ? 21.267 24.095 51.064 1.00 42.08 ? 1155 HOH A O 1 HETATM 6449 O O . HOH T 9 . ? 27.311 20.237 39.907 1.00 36.32 ? 1156 HOH A O 1 HETATM 6450 O O . HOH T 9 . ? 5.557 81.711 53.966 1.00 37.80 ? 1157 HOH A O 1 HETATM 6451 O O . HOH T 9 . ? 8.238 29.408 33.480 1.00 39.28 ? 1158 HOH A O 1 HETATM 6452 O O . HOH T 9 . ? -1.131 51.580 72.597 0.50 25.61 ? 1159 HOH A O 1 HETATM 6453 O O . HOH T 9 . ? 9.014 56.604 43.784 1.00 19.73 ? 1160 HOH A O 1 HETATM 6454 O O . HOH T 9 . ? 23.049 75.772 25.618 1.00 40.03 ? 1161 HOH A O 1 HETATM 6455 O O . HOH T 9 . ? 6.068 68.381 37.088 1.00 33.94 ? 1162 HOH A O 1 HETATM 6456 O O . HOH T 9 . ? 38.681 55.197 62.535 1.00 45.30 ? 1163 HOH A O 1 HETATM 6457 O O . HOH T 9 . ? 12.969 71.854 80.037 1.00 43.24 ? 1164 HOH A O 1 HETATM 6458 O O . HOH T 9 . ? 11.742 81.052 61.268 1.00 38.00 ? 1165 HOH A O 1 HETATM 6459 O O . HOH T 9 . ? 1.498 37.060 68.644 1.00 37.16 ? 1166 HOH A O 1 HETATM 6460 O O . HOH T 9 . ? 12.876 32.889 70.863 1.00 40.31 ? 1167 HOH A O 1 HETATM 6461 O O . HOH T 9 . ? 18.763 40.529 76.022 1.00 39.51 ? 1168 HOH A O 1 HETATM 6462 O O . HOH T 9 . ? 20.187 45.748 79.093 1.00 44.42 ? 1169 HOH A O 1 HETATM 6463 O O . HOH T 9 . ? 5.870 56.278 35.855 1.00 23.08 ? 1170 HOH A O 1 HETATM 6464 O O . HOH T 9 . ? 23.353 60.211 39.540 1.00 32.25 ? 1171 HOH A O 1 HETATM 6465 O O . HOH T 9 . ? 30.625 71.447 43.583 1.00 37.40 ? 1172 HOH A O 1 HETATM 6466 O O . HOH T 9 . ? 8.496 74.875 75.459 1.00 44.36 ? 1173 HOH A O 1 HETATM 6467 O O . HOH T 9 . ? 3.110 38.544 27.018 1.00 36.63 ? 1174 HOH A O 1 HETATM 6468 O O . HOH T 9 . ? 38.491 42.906 55.628 1.00 44.29 ? 1175 HOH A O 1 HETATM 6469 O O . HOH T 9 . ? 25.279 85.939 42.657 1.00 36.04 ? 1176 HOH A O 1 HETATM 6470 O O . HOH T 9 . ? 11.960 56.368 31.487 1.00 39.74 ? 1177 HOH A O 1 HETATM 6471 O O . HOH T 9 . ? 21.976 80.824 22.780 1.00 46.78 ? 1178 HOH A O 1 HETATM 6472 O O . HOH T 9 . ? 13.623 55.168 32.785 1.00 30.31 ? 1179 HOH A O 1 HETATM 6473 O O . HOH T 9 . ? 28.292 53.537 37.060 0.50 27.44 ? 1180 HOH A O 1 HETATM 6474 O O . HOH T 9 . ? 24.729 23.116 53.102 1.00 40.38 ? 1181 HOH A O 1 HETATM 6475 O O . HOH T 9 . ? 25.252 66.614 56.593 1.00 34.30 ? 1182 HOH A O 1 HETATM 6476 O O . HOH T 9 . ? 15.414 25.577 30.048 0.50 30.95 ? 1183 HOH A O 1 HETATM 6477 O O . HOH T 9 . ? 6.539 42.864 27.129 1.00 36.65 ? 1184 HOH A O 1 HETATM 6478 O O . HOH T 9 . ? 34.926 43.896 68.441 1.00 43.71 ? 1185 HOH A O 1 HETATM 6479 O O . HOH T 9 . ? 9.587 74.904 69.328 0.50 32.01 ? 1186 HOH A O 1 HETATM 6480 O O . HOH T 9 . ? 10.408 84.093 51.317 1.00 37.43 ? 1187 HOH A O 1 HETATM 6481 O O . HOH T 9 . ? 25.000 64.819 44.465 0.50 20.44 ? 1188 HOH A O 1 HETATM 6482 O O . HOH T 9 . ? 24.996 56.960 32.185 1.00 35.60 ? 1189 HOH A O 1 HETATM 6483 O O . HOH T 9 . ? 39.345 57.519 58.234 1.00 42.90 ? 1190 HOH A O 1 HETATM 6484 O O . HOH T 9 . ? 8.699 54.506 31.317 1.00 34.20 ? 1191 HOH A O 1 HETATM 6485 O O . HOH T 9 . ? 23.747 24.529 30.475 1.00 43.04 ? 1192 HOH A O 1 HETATM 6486 O O . HOH T 9 . ? 5.976 44.885 25.543 1.00 41.63 ? 1193 HOH A O 1 HETATM 6487 O O . HOH T 9 . ? 17.303 25.882 59.488 1.00 33.12 ? 1194 HOH A O 1 HETATM 6488 O O . HOH T 9 . ? 2.557 63.257 40.620 1.00 35.20 ? 1195 HOH A O 1 HETATM 6489 O O . HOH T 9 . ? 22.583 58.828 21.396 1.00 44.93 ? 1196 HOH A O 1 HETATM 6490 O O . HOH T 9 . ? -4.182 44.164 26.989 1.00 45.78 ? 1197 HOH A O 1 HETATM 6491 O O . HOH T 9 . ? 21.386 24.084 27.029 0.50 28.00 ? 1198 HOH A O 1 HETATM 6492 O O . HOH T 9 . ? 22.140 83.595 49.879 1.00 40.11 ? 1199 HOH A O 1 HETATM 6493 O O . HOH T 9 . ? 24.235 83.484 45.596 1.00 53.54 ? 1200 HOH A O 1 HETATM 6494 O O . HOH T 9 . ? 24.808 68.100 63.034 0.40 27.12 ? 1201 HOH A O 1 HETATM 6495 O O . HOH T 9 . ? -5.101 44.545 30.839 1.00 38.96 ? 1202 HOH A O 1 HETATM 6496 O O . HOH T 9 . ? 26.991 64.990 34.682 0.40 23.78 ? 1203 HOH A O 1 HETATM 6497 O O . HOH T 9 . ? 17.599 64.668 67.179 0.50 29.98 ? 1204 HOH A O 1 HETATM 6498 O O . HOH T 9 . ? 33.677 53.484 31.834 1.00 43.51 ? 1205 HOH A O 1 HETATM 6499 O O . HOH T 9 . ? 2.992 64.935 50.862 1.00 25.94 ? 1206 HOH A O 1 HETATM 6500 O O . HOH T 9 . ? 4.138 71.921 36.250 1.00 34.26 ? 1207 HOH A O 1 HETATM 6501 O O . HOH T 9 . ? 9.398 28.680 38.019 1.00 39.13 ? 1208 HOH A O 1 HETATM 6502 O O . HOH T 9 . ? 15.188 24.989 32.478 1.00 41.20 ? 1209 HOH A O 1 HETATM 6503 O O . HOH T 9 . ? -1.828 63.619 48.889 1.00 31.72 ? 1210 HOH A O 1 HETATM 6504 O O . HOH T 9 . ? 29.032 25.828 31.471 1.00 41.00 ? 1211 HOH A O 1 HETATM 6505 O O . HOH T 9 . ? 26.794 64.833 28.796 1.00 36.76 ? 1212 HOH A O 1 HETATM 6506 O O . HOH T 9 . ? 25.547 68.112 32.661 1.00 33.02 ? 1213 HOH A O 1 HETATM 6507 O O . HOH T 9 . ? 29.656 67.475 45.321 1.00 46.04 ? 1214 HOH A O 1 HETATM 6508 O O . HOH T 9 . ? 34.730 35.574 58.379 1.00 46.18 ? 1215 HOH A O 1 HETATM 6509 O O . HOH T 9 . ? 21.175 56.617 25.131 1.00 33.15 ? 1216 HOH A O 1 HETATM 6510 O O . HOH T 9 . ? 28.245 35.931 67.328 0.50 30.64 ? 1217 HOH A O 1 HETATM 6511 O O . HOH T 9 . ? 29.556 37.931 66.374 1.00 38.36 ? 1218 HOH A O 1 HETATM 6512 O O . HOH T 9 . ? 13.912 80.551 62.953 1.00 39.54 ? 1219 HOH A O 1 HETATM 6513 O O . HOH T 9 . ? 11.910 73.812 81.582 0.20 22.80 ? 1220 HOH A O 1 HETATM 6514 O O . HOH T 9 . ? 35.076 49.288 33.162 0.50 26.45 ? 1221 HOH A O 1 HETATM 6515 O O . HOH T 9 . ? 31.154 51.761 50.071 1.00 55.16 ? 1222 HOH A O 1 HETATM 6516 O O . HOH T 9 . ? 14.956 69.937 81.806 1.00 49.12 ? 1223 HOH A O 1 HETATM 6517 O O . HOH T 9 . ? 4.903 50.179 28.238 1.00 33.81 ? 1224 HOH A O 1 HETATM 6518 O O . HOH T 9 . ? 23.512 74.543 65.461 1.00 41.18 ? 1225 HOH A O 1 HETATM 6519 O O . HOH T 9 . ? -16.490 45.319 40.953 1.00 46.29 ? 1226 HOH A O 1 HETATM 6520 O O . HOH T 9 . ? -1.902 44.685 58.487 0.50 31.65 ? 1227 HOH A O 1 HETATM 6521 O O . HOH T 9 . ? -5.426 34.088 47.384 1.00 43.12 ? 1228 HOH A O 1 HETATM 6522 O O . HOH T 9 . ? 12.548 50.327 27.359 1.00 33.16 ? 1229 HOH A O 1 HETATM 6523 O O . HOH T 9 . ? 17.825 58.376 29.714 1.00 38.74 ? 1230 HOH A O 1 HETATM 6524 O O . HOH T 9 . ? 16.809 71.080 79.118 0.50 33.47 ? 1231 HOH A O 1 HETATM 6525 O O . HOH T 9 . ? 15.776 82.612 57.646 1.00 51.48 ? 1232 HOH A O 1 HETATM 6526 O O . HOH T 9 . ? 10.892 41.222 17.487 1.00 41.89 ? 1233 HOH A O 1 HETATM 6527 O O . HOH T 9 . ? 18.913 54.090 73.023 1.00 46.01 ? 1234 HOH A O 1 HETATM 6528 O O . HOH T 9 . ? 25.941 74.484 58.285 1.00 45.22 ? 1235 HOH A O 1 HETATM 6529 O O . HOH T 9 . ? 29.993 42.096 66.574 1.00 40.83 ? 1236 HOH A O 1 HETATM 6530 O O . HOH T 9 . ? 28.714 64.459 25.480 1.00 37.32 ? 1237 HOH A O 1 HETATM 6531 O O . HOH T 9 . ? 26.247 74.765 55.747 1.00 41.57 ? 1238 HOH A O 1 HETATM 6532 O O . HOH T 9 . ? -9.252 45.787 48.607 1.00 43.70 ? 1239 HOH A O 1 HETATM 6533 O O . HOH T 9 . ? 24.561 60.014 32.365 1.00 38.19 ? 1240 HOH A O 1 HETATM 6534 O O . HOH T 9 . ? -3.499 46.790 24.838 1.00 40.04 ? 1241 HOH A O 1 HETATM 6535 O O . HOH T 9 . ? -10.582 43.579 38.437 1.00 46.47 ? 1242 HOH A O 1 HETATM 6536 O O . HOH T 9 . ? 1.958 66.662 37.190 1.00 41.33 ? 1243 HOH A O 1 HETATM 6537 O O . HOH T 9 . ? -5.528 50.825 28.430 1.00 39.61 ? 1244 HOH A O 1 HETATM 6538 O O . HOH T 9 . ? 28.212 41.868 68.639 1.00 39.10 ? 1245 HOH A O 1 HETATM 6539 O O . HOH T 9 . ? 19.910 57.867 27.336 1.00 36.80 ? 1246 HOH A O 1 HETATM 6540 O O . HOH T 9 . ? 14.063 68.719 75.361 1.00 43.53 ? 1247 HOH A O 1 HETATM 6541 O O . HOH T 9 . ? 33.622 54.452 28.130 0.50 28.23 ? 1248 HOH A O 1 HETATM 6542 O O . HOH T 9 . ? 30.584 25.857 38.162 1.00 45.87 ? 1249 HOH A O 1 HETATM 6543 O O . HOH T 9 . ? 35.680 33.783 54.886 0.80 44.37 ? 1250 HOH A O 1 HETATM 6544 O O . HOH T 9 . ? 38.610 38.552 64.963 0.50 34.29 ? 1251 HOH A O 1 HETATM 6545 O O . HOH T 9 . ? 5.969 53.775 30.123 1.00 30.26 ? 1252 HOH A O 1 HETATM 6546 O O . HOH T 9 . ? -0.067 60.395 48.306 1.00 34.01 ? 1253 HOH A O 1 HETATM 6547 O O . HOH T 9 . ? 9.887 75.897 30.869 1.00 38.45 ? 1254 HOH A O 1 HETATM 6548 O O . HOH T 9 . ? 7.960 56.473 75.712 1.00 33.13 ? 1255 HOH A O 1 HETATM 6549 O O . HOH T 9 . ? 6.722 53.876 75.515 1.00 35.82 ? 1256 HOH A O 1 HETATM 6550 O O . HOH T 9 . ? 11.328 52.669 27.904 1.00 44.53 ? 1257 HOH A O 1 HETATM 6551 O O . HOH T 9 . ? 29.784 60.908 52.834 1.00 41.27 ? 1258 HOH A O 1 HETATM 6552 O O . HOH T 9 . ? 36.521 46.585 31.671 0.50 30.28 ? 1259 HOH A O 1 HETATM 6553 O O . HOH T 9 . ? 3.886 63.936 34.783 1.00 39.02 ? 1260 HOH A O 1 HETATM 6554 O O . HOH T 9 . ? 17.433 59.176 44.807 1.00 22.15 ? 1261 HOH A O 1 HETATM 6555 O O . HOH T 9 . ? 15.664 55.151 72.167 0.50 34.46 ? 1262 HOH A O 1 HETATM 6556 O O . HOH T 9 . ? 26.741 30.896 63.808 1.00 48.98 ? 1263 HOH A O 1 HETATM 6557 O O . HOH T 9 . ? 29.424 28.048 59.392 1.00 45.03 ? 1264 HOH A O 1 HETATM 6558 O O . HOH T 9 . ? 12.446 28.655 60.597 1.00 45.35 ? 1265 HOH A O 1 HETATM 6559 O O . HOH T 9 . ? -4.234 36.309 60.410 0.20 28.68 ? 1266 HOH A O 1 HETATM 6560 O O . HOH T 9 . ? -6.845 45.058 49.519 1.00 49.94 ? 1267 HOH A O 1 HETATM 6561 O O . HOH T 9 . ? -7.548 41.720 40.863 1.00 37.50 ? 1268 HOH A O 1 HETATM 6562 O O . HOH T 9 . ? -5.987 41.611 44.273 1.00 44.33 ? 1269 HOH A O 1 HETATM 6563 O O . HOH T 9 . ? 42.254 34.948 37.577 1.00 49.84 ? 1270 HOH A O 1 HETATM 6564 O O . HOH T 9 . ? 34.324 32.729 27.381 1.00 42.24 ? 1271 HOH A O 1 HETATM 6565 O O . HOH T 9 . ? 26.568 42.239 40.876 1.00 32.56 ? 1272 HOH A O 1 HETATM 6566 O O . HOH T 9 . ? 22.439 45.508 41.055 1.00 20.42 ? 1273 HOH A O 1 HETATM 6567 O O . HOH T 9 . ? 25.818 25.823 46.486 1.00 33.42 ? 1274 HOH A O 1 HETATM 6568 O O . HOH T 9 . ? 37.506 28.538 39.058 1.00 43.91 ? 1275 HOH A O 1 HETATM 6569 O O . HOH T 9 . ? 23.274 68.480 69.007 1.00 52.52 ? 1276 HOH A O 1 HETATM 6570 O O . HOH T 9 . ? -12.788 47.503 37.543 1.00 33.27 ? 1277 HOH A O 1 HETATM 6571 O O . HOH T 9 . ? 24.193 45.643 38.831 1.00 26.32 ? 1278 HOH A O 1 HETATM 6572 O O . HOH T 9 . ? 25.009 48.010 37.624 1.00 32.05 ? 1279 HOH A O 1 HETATM 6573 O O . HOH T 9 . ? 26.388 40.150 13.351 1.00 36.71 ? 1280 HOH A O 1 HETATM 6574 O O . HOH T 9 . ? 20.674 50.383 76.063 1.00 41.56 ? 1281 HOH A O 1 HETATM 6575 O O . HOH T 9 . ? 18.685 49.796 45.485 1.00 32.84 ? 1282 HOH A O 1 HETATM 6576 O O . HOH T 9 . ? 0.206 63.782 61.557 1.00 37.55 ? 1283 HOH A O 1 HETATM 6577 O O . HOH T 9 . ? 25.863 43.837 38.752 1.00 37.72 ? 1284 HOH A O 1 HETATM 6578 O O . HOH T 9 . ? 34.640 41.225 19.415 1.00 44.89 ? 1285 HOH A O 1 HETATM 6579 O O . HOH T 9 . ? 16.786 63.454 68.908 0.50 29.34 ? 1286 HOH A O 1 HETATM 6580 O O . HOH T 9 . ? 34.800 51.237 31.041 1.00 41.91 ? 1287 HOH A O 1 HETATM 6581 O O . HOH T 9 . ? 24.175 43.968 42.382 1.00 33.13 ? 1288 HOH A O 1 HETATM 6582 O O . HOH T 9 . ? 11.815 29.114 19.067 1.00 42.85 ? 1289 HOH A O 1 HETATM 6583 O O . HOH T 9 . ? 21.290 52.049 44.991 1.00 28.36 ? 1290 HOH A O 1 HETATM 6584 O O . HOH T 9 . ? 29.559 47.970 37.489 1.00 49.02 ? 1291 HOH A O 1 HETATM 6585 O O . HOH T 9 . ? 9.838 97.394 40.072 1.00 39.22 ? 1292 HOH A O 1 HETATM 6586 O O . HOH T 9 . ? 30.813 35.552 16.773 1.00 43.09 ? 1293 HOH A O 1 HETATM 6587 O O . HOH T 9 . ? 2.160 33.722 24.115 1.00 53.75 ? 1294 HOH A O 1 HETATM 6588 O O . HOH T 9 . ? 20.932 79.405 65.705 1.00 47.55 ? 1295 HOH A O 1 HETATM 6589 O O . HOH T 9 . ? 26.240 59.796 47.248 1.00 40.22 ? 1296 HOH A O 1 HETATM 6590 O O . HOH T 9 . ? 35.223 56.163 51.325 1.00 49.65 ? 1297 HOH A O 1 HETATM 6591 O O . HOH T 9 . ? 22.290 59.966 16.810 1.00 67.95 ? 1298 HOH A O 1 HETATM 6592 O O . HOH T 9 . ? 27.940 71.091 32.558 0.50 32.07 ? 1299 HOH A O 1 HETATM 6593 O O . HOH T 9 . ? 25.611 63.251 38.746 1.00 36.50 ? 1300 HOH A O 1 HETATM 6594 O O . HOH T 9 . ? 36.839 48.595 30.154 1.00 45.27 ? 1301 HOH A O 1 HETATM 6595 O O . HOH T 9 . ? 25.424 74.704 21.986 1.00 51.06 ? 1302 HOH A O 1 HETATM 6596 O O . HOH T 9 . ? 34.490 36.178 55.105 1.00 48.08 ? 1303 HOH A O 1 HETATM 6597 O O . HOH T 9 . ? 31.075 69.861 41.479 1.00 40.44 ? 1304 HOH A O 1 HETATM 6598 O O . HOH T 9 . ? 30.169 75.866 43.116 1.00 51.91 ? 1305 HOH A O 1 HETATM 6599 O O . HOH T 9 . ? 13.305 27.962 17.053 1.00 46.71 ? 1306 HOH A O 1 HETATM 6600 O O . HOH T 9 . ? 33.941 29.086 34.135 1.00 38.03 ? 1307 HOH A O 1 HETATM 6601 O O . HOH T 9 . ? 14.142 54.825 37.349 0.50 17.62 ? 1308 HOH A O 1 HETATM 6602 O O . HOH T 9 . ? 22.461 80.531 57.181 1.00 43.31 ? 1309 HOH A O 1 HETATM 6603 O O . HOH T 9 . ? 22.090 58.709 69.916 1.00 54.74 ? 1310 HOH A O 1 HETATM 6604 O O . HOH T 9 . ? 12.271 27.588 21.427 1.00 46.00 ? 1311 HOH A O 1 HETATM 6605 O O . HOH T 9 . ? 14.232 96.748 45.439 1.00 49.99 ? 1312 HOH A O 1 HETATM 6606 O O . HOH T 9 . ? 37.283 41.860 37.611 1.00 47.75 ? 1313 HOH A O 1 HETATM 6607 O O . HOH T 9 . ? 26.688 53.041 48.680 1.00 44.26 ? 1314 HOH A O 1 HETATM 6608 O O . HOH T 9 . ? 13.827 61.622 32.872 1.00 42.89 ? 1315 HOH A O 1 HETATM 6609 O O A HOH T 9 . ? -5.597 44.040 47.389 0.50 26.10 ? 1316 HOH A O 1 HETATM 6610 O O B HOH T 9 . ? -6.461 42.476 46.801 0.50 31.17 ? 1316 HOH A O 1 HETATM 6611 O O . HOH T 9 . ? 29.324 72.758 50.049 1.00 43.48 ? 1317 HOH A O 1 HETATM 6612 O O . HOH T 9 . ? 40.664 45.258 19.583 1.00 48.10 ? 1318 HOH A O 1 HETATM 6613 O O . HOH T 9 . ? 7.660 26.554 54.577 1.00 47.82 ? 1319 HOH A O 1 HETATM 6614 O O . HOH T 9 . ? 40.371 41.570 26.351 1.00 49.26 ? 1320 HOH A O 1 HETATM 6615 O O . HOH T 9 . ? 28.580 29.536 62.081 1.00 42.74 ? 1321 HOH A O 1 HETATM 6616 O O . HOH T 9 . ? 32.683 54.306 70.774 1.00 48.39 ? 1322 HOH A O 1 HETATM 6617 O O . HOH T 9 . ? 14.113 40.684 12.211 1.00 48.69 ? 1323 HOH A O 1 HETATM 6618 O O . HOH T 9 . ? 24.651 53.053 46.581 1.00 39.05 ? 1324 HOH A O 1 HETATM 6619 O O . HOH T 9 . ? 29.964 25.347 47.462 1.00 39.62 ? 1325 HOH A O 1 HETATM 6620 O O . HOH T 9 . ? 10.622 36.654 76.374 1.00 40.46 ? 1326 HOH A O 1 HETATM 6621 O O . HOH T 9 . ? 27.880 67.230 52.898 1.00 46.33 ? 1327 HOH A O 1 HETATM 6622 O O . HOH T 9 . ? 23.063 48.781 46.885 1.00 38.76 ? 1328 HOH A O 1 HETATM 6623 O O . HOH T 9 . ? 9.144 41.901 19.685 1.00 54.57 ? 1329 HOH A O 1 HETATM 6624 O O . HOH T 9 . ? 8.016 34.538 19.321 1.00 51.91 ? 1330 HOH A O 1 HETATM 6625 O O . HOH T 9 . ? 35.939 34.414 50.905 1.00 45.78 ? 1331 HOH A O 1 HETATM 6626 O O . HOH T 9 . ? 18.787 34.332 72.540 0.25 20.43 ? 1332 HOH A O 1 HETATM 6627 O O . HOH T 9 . ? 27.379 63.308 63.363 1.00 54.14 ? 1333 HOH A O 1 HETATM 6628 O O . HOH T 9 . ? 29.412 30.530 14.999 1.00 45.43 ? 1334 HOH A O 1 HETATM 6629 O O . HOH T 9 . ? 33.931 54.999 68.065 1.00 50.34 ? 1335 HOH A O 1 HETATM 6630 O O . HOH T 9 . ? 40.499 42.655 23.605 1.00 53.27 ? 1336 HOH A O 1 HETATM 6631 O O . HOH T 9 . ? 7.459 57.384 33.639 1.00 42.16 ? 1337 HOH A O 1 HETATM 6632 O O . HOH T 9 . ? 31.468 50.257 11.608 1.00 47.29 ? 1338 HOH A O 1 HETATM 6633 O O . HOH T 9 . ? 23.272 78.454 22.967 1.00 46.20 ? 1339 HOH A O 1 HETATM 6634 O O . HOH T 9 . ? 21.305 42.388 46.139 1.00 48.09 ? 1340 HOH A O 1 HETATM 6635 O O . HOH T 9 . ? 42.769 31.125 40.933 1.00 51.94 ? 1341 HOH A O 1 HETATM 6636 O O . HOH T 9 . ? 7.280 81.698 62.558 1.00 47.35 ? 1342 HOH A O 1 HETATM 6637 O O . HOH T 9 . ? 24.458 79.506 55.370 1.00 46.28 ? 1343 HOH A O 1 HETATM 6638 O O . HOH T 9 . ? 27.531 66.000 55.227 1.00 38.99 ? 1344 HOH A O 1 HETATM 6639 O O . HOH T 9 . ? 16.712 42.507 44.507 1.00 18.66 ? 1345 HOH A O 1 HETATM 6640 O O . HOH T 9 . ? 14.681 41.381 77.712 0.50 43.27 ? 1346 HOH A O 1 HETATM 6641 O O . HOH T 9 . ? 15.415 39.501 75.812 0.50 41.25 ? 1347 HOH A O 1 HETATM 6642 O O . HOH T 9 . ? 12.233 50.909 76.351 1.00 47.82 ? 1348 HOH A O 1 HETATM 6643 O O . HOH T 9 . ? 24.942 43.217 71.576 1.00 51.83 ? 1349 HOH A O 1 HETATM 6644 O O . HOH T 9 . ? 23.306 31.305 69.722 0.50 39.28 ? 1350 HOH A O 1 HETATM 6645 O O . HOH T 9 . ? 18.510 24.529 61.317 1.00 54.38 ? 1351 HOH A O 1 HETATM 6646 O O . HOH T 9 . ? 12.391 22.873 44.060 0.50 30.68 ? 1352 HOH A O 1 HETATM 6647 O O . HOH T 9 . ? 8.743 53.094 79.495 0.70 59.49 ? 1353 HOH A O 1 HETATM 6648 O O . HOH T 9 . ? 22.316 55.310 69.718 1.00 59.63 ? 1354 HOH A O 1 HETATM 6649 O O . HOH T 9 . ? -0.444 30.718 62.917 0.70 38.80 ? 1355 HOH A O 1 HETATM 6650 O O . HOH T 9 . ? 15.372 29.856 12.937 0.50 32.08 ? 1356 HOH A O 1 HETATM 6651 O O . HOH T 9 . ? 5.802 33.009 21.024 1.00 58.93 ? 1357 HOH A O 1 HETATM 6652 O O . HOH T 9 . ? 20.255 61.816 27.057 1.00 44.08 ? 1358 HOH A O 1 HETATM 6653 O O . HOH T 9 . ? 20.400 60.084 24.838 1.00 48.51 ? 1359 HOH A O 1 HETATM 6654 O O . HOH T 9 . ? 32.962 21.748 40.142 0.50 38.00 ? 1360 HOH A O 1 HETATM 6655 O O . HOH T 9 . ? 26.933 28.464 28.406 1.00 49.73 ? 1361 HOH A O 1 HETATM 6656 O O . HOH T 9 . ? -7.349 48.342 47.963 1.00 38.03 ? 1362 HOH A O 1 HETATM 6657 O O . HOH T 9 . ? 42.602 53.056 24.578 1.00 53.06 ? 1363 HOH A O 1 HETATM 6658 O O . HOH T 9 . ? 31.417 29.383 11.097 1.00 55.47 ? 1364 HOH A O 1 HETATM 6659 O O . HOH T 9 . ? 28.033 30.609 6.594 1.00 54.25 ? 1365 HOH A O 1 HETATM 6660 O O . HOH T 9 . ? 37.949 41.770 53.083 1.00 47.77 ? 1366 HOH A O 1 HETATM 6661 O O . HOH T 9 . ? 40.732 44.930 51.143 1.00 49.83 ? 1367 HOH A O 1 HETATM 6662 O O . HOH T 9 . ? 34.088 49.676 50.567 1.00 50.58 ? 1368 HOH A O 1 HETATM 6663 O O . HOH T 9 . ? 25.535 71.590 60.648 1.00 47.34 ? 1369 HOH A O 1 HETATM 6664 O O . HOH T 9 . ? 30.556 76.567 48.959 1.00 52.30 ? 1370 HOH A O 1 HETATM 6665 O O . HOH T 9 . ? 24.829 59.631 43.197 0.50 36.42 ? 1371 HOH A O 1 HETATM 6666 O O . HOH T 9 . ? 24.704 62.935 42.264 0.50 28.33 ? 1372 HOH A O 1 HETATM 6667 O O . HOH T 9 . ? 9.695 47.378 80.078 1.00 58.48 ? 1373 HOH A O 1 HETATM 6668 O O . HOH T 9 . ? 15.745 30.348 67.531 0.50 48.01 ? 1374 HOH A O 1 HETATM 6669 O O . HOH T 9 . ? 13.390 30.771 66.425 0.50 30.46 ? 1375 HOH A O 1 HETATM 6670 O O . HOH T 9 . ? -0.018 29.792 44.702 0.50 33.77 ? 1376 HOH A O 1 HETATM 6671 O O . HOH T 9 . ? -3.721 32.570 53.294 0.50 33.37 ? 1377 HOH A O 1 HETATM 6672 O O . HOH T 9 . ? -4.144 29.430 52.937 0.50 36.75 ? 1378 HOH A O 1 HETATM 6673 O O . HOH T 9 . ? 1.680 40.847 27.118 1.00 40.83 ? 1379 HOH A O 1 HETATM 6674 O O . HOH T 9 . ? 3.343 48.879 26.635 1.00 40.17 ? 1380 HOH A O 1 HETATM 6675 O O . HOH T 9 . ? 8.338 30.278 36.095 0.50 30.00 ? 1381 HOH A O 1 HETATM 6676 O O . HOH T 9 . ? 5.343 30.224 37.044 0.60 39.73 ? 1382 HOH A O 1 HETATM 6677 O O . HOH T 9 . ? 11.087 27.301 31.979 0.50 30.54 ? 1383 HOH A O 1 HETATM 6678 O O . HOH T 9 . ? 17.447 61.223 30.409 0.50 32.33 ? 1384 HOH A O 1 HETATM 6679 O O . HOH T 9 . ? 15.055 61.313 30.546 0.50 31.06 ? 1385 HOH A O 1 HETATM 6680 O O . HOH T 9 . ? 13.302 65.364 31.775 0.50 30.27 ? 1386 HOH A O 1 HETATM 6681 O O . HOH T 9 . ? 14.517 69.976 30.152 0.70 27.72 ? 1387 HOH A O 1 HETATM 6682 O O . HOH T 9 . ? 16.069 68.068 29.285 0.50 27.91 ? 1388 HOH A O 1 HETATM 6683 O O . HOH T 9 . ? 14.807 73.067 23.802 0.50 30.88 ? 1389 HOH A O 1 HETATM 6684 O O . HOH T 9 . ? 15.149 71.989 21.837 0.50 28.82 ? 1390 HOH A O 1 HETATM 6685 O O . HOH T 9 . ? 20.183 64.311 25.317 0.50 31.08 ? 1391 HOH A O 1 HETATM 6686 O O . HOH T 9 . ? 29.191 61.989 26.793 1.00 39.25 ? 1392 HOH A O 1 HETATM 6687 O O . HOH T 9 . ? 27.188 62.086 28.850 0.50 28.86 ? 1393 HOH A O 1 HETATM 6688 O O . HOH T 9 . ? 31.998 58.137 26.498 0.50 37.21 ? 1394 HOH A O 1 HETATM 6689 O O . HOH T 9 . ? 31.380 57.374 31.229 0.50 35.58 ? 1395 HOH A O 1 HETATM 6690 O O . HOH T 9 . ? 8.828 51.865 28.658 0.50 33.13 ? 1396 HOH A O 1 HETATM 6691 O O . HOH T 9 . ? 8.483 50.626 25.314 1.00 49.02 ? 1397 HOH A O 1 HETATM 6692 O O . HOH T 9 . ? 6.730 52.537 27.779 0.50 30.79 ? 1398 HOH A O 1 HETATM 6693 O O . HOH T 9 . ? 10.485 54.844 29.516 0.40 28.20 ? 1399 HOH A O 1 HETATM 6694 O O . HOH T 9 . ? 11.361 54.718 26.166 0.50 37.90 ? 1400 HOH A O 1 HETATM 6695 O O . HOH T 9 . ? 23.558 54.181 44.461 0.50 27.64 ? 1401 HOH A O 1 HETATM 6696 O O . HOH T 9 . ? 26.825 55.091 46.467 0.40 27.50 ? 1402 HOH A O 1 HETATM 6697 O O . HOH T 9 . ? 29.464 60.940 50.314 0.40 37.23 ? 1403 HOH A O 1 HETATM 6698 O O . HOH T 9 . ? 19.200 24.894 12.260 1.00 54.73 ? 1404 HOH A O 1 HETATM 6699 O O . HOH T 9 . ? 18.687 15.249 38.523 1.00 56.39 ? 1405 HOH A O 1 HETATM 6700 O O . HOH T 9 . ? 10.177 39.178 15.540 0.40 34.31 ? 1406 HOH A O 1 HETATM 6701 O O . HOH T 9 . ? 30.849 54.809 10.526 0.50 43.74 ? 1407 HOH A O 1 HETATM 6702 O O . HOH T 9 . ? 26.567 52.098 11.057 1.00 52.15 ? 1408 HOH A O 1 HETATM 6703 O O . HOH T 9 . ? 23.642 55.135 8.772 1.00 56.19 ? 1409 HOH A O 1 HETATM 6704 O O . HOH T 9 . ? 21.283 54.457 16.194 0.50 30.23 ? 1410 HOH A O 1 HETATM 6705 O O . HOH T 9 . ? 32.319 46.672 36.673 0.50 34.78 ? 1411 HOH A O 1 HETATM 6706 O O . HOH T 9 . ? 38.787 38.878 35.251 0.40 28.77 ? 1412 HOH A O 1 HETATM 6707 O O . HOH T 9 . ? 35.022 20.947 44.173 1.00 46.99 ? 1413 HOH A O 1 HETATM 6708 O O . HOH T 9 . ? -14.161 42.516 41.401 0.60 37.78 ? 1414 HOH A O 1 HETATM 6709 O O . HOH T 9 . ? -8.241 49.598 49.981 1.00 34.02 ? 1415 HOH A O 1 HETATM 6710 O O . HOH T 9 . ? -16.124 44.193 29.516 0.50 47.30 ? 1416 HOH A O 1 HETATM 6711 O O . HOH T 9 . ? -8.679 43.246 34.766 0.50 27.76 ? 1417 HOH A O 1 HETATM 6712 O O . HOH T 9 . ? 2.623 52.773 27.168 0.50 39.47 ? 1418 HOH A O 1 HETATM 6713 O O . HOH T 9 . ? 36.812 27.813 31.308 0.30 28.36 ? 1419 HOH A O 1 HETATM 6714 O O . HOH T 9 . ? 29.199 28.580 24.701 0.30 22.45 ? 1420 HOH A O 1 HETATM 6715 O O . HOH T 9 . ? 37.813 51.198 13.333 1.00 58.55 ? 1421 HOH A O 1 HETATM 6716 O O . HOH T 9 . ? 37.597 52.659 16.460 1.00 54.27 ? 1422 HOH A O 1 HETATM 6717 O O . HOH T 9 . ? 40.971 50.391 19.402 0.40 37.60 ? 1423 HOH A O 1 HETATM 6718 O O . HOH T 9 . ? 40.111 45.583 16.470 0.50 34.53 ? 1424 HOH A O 1 HETATM 6719 O O . HOH T 9 . ? 29.700 34.480 5.438 0.50 44.35 ? 1425 HOH A O 1 HETATM 6720 O O . HOH T 9 . ? 36.153 37.599 57.381 0.80 44.92 ? 1426 HOH A O 1 HETATM 6721 O O . HOH T 9 . ? 36.439 41.326 47.368 0.40 29.32 ? 1427 HOH A O 1 HETATM 6722 O O . HOH T 9 . ? 36.528 42.396 65.484 1.00 35.77 ? 1428 HOH A O 1 HETATM 6723 O O . HOH T 9 . ? 43.377 39.779 64.170 1.00 65.08 ? 1429 HOH A O 1 HETATM 6724 O O . HOH T 9 . ? 42.134 45.669 68.134 0.30 31.22 ? 1430 HOH A O 1 HETATM 6725 O O . HOH T 9 . ? 39.537 50.935 52.198 1.00 51.38 ? 1431 HOH A O 1 HETATM 6726 O O . HOH T 9 . ? 29.548 69.148 52.609 0.70 35.31 ? 1432 HOH A O 1 HETATM 6727 O O . HOH T 9 . ? 28.398 73.681 54.625 0.60 35.61 ? 1433 HOH A O 1 HETATM 6728 O O . HOH T 9 . ? 30.143 72.021 56.369 0.50 36.22 ? 1434 HOH A O 1 HETATM 6729 O O . HOH T 9 . ? 37.014 59.491 63.884 0.50 35.15 ? 1435 HOH A O 1 HETATM 6730 O O . HOH T 9 . ? 37.148 56.818 64.276 1.00 46.07 ? 1436 HOH A O 1 HETATM 6731 O O . HOH T 9 . ? 40.007 56.903 60.723 0.70 41.79 ? 1437 HOH A O 1 HETATM 6732 O O . HOH T 9 . ? 32.569 27.644 56.328 0.50 29.30 ? 1438 HOH A O 1 HETATM 6733 O O . HOH T 9 . ? 35.615 31.552 53.951 0.20 25.57 ? 1439 HOH A O 1 HETATM 6734 O O . HOH T 9 . ? 24.287 82.348 24.394 1.00 50.90 ? 1440 HOH A O 1 HETATM 6735 O O . HOH T 9 . ? -0.242 58.933 76.357 0.70 53.19 ? 1441 HOH A O 1 HETATM 6736 O O . HOH T 9 . ? 8.256 69.724 36.853 0.80 32.85 ? 1442 HOH A O 1 HETATM 6737 O O . HOH T 9 . ? 11.005 64.117 30.226 1.00 59.68 ? 1443 HOH A O 1 HETATM 6738 O O . HOH T 9 . ? 10.284 82.780 56.119 0.40 27.91 ? 1444 HOH A O 1 HETATM 6739 O O . HOH T 9 . ? 15.435 34.504 74.625 0.50 39.21 ? 1445 HOH A O 1 HETATM 6740 O O . HOH T 9 . ? 14.713 52.708 75.742 0.30 34.76 ? 1446 HOH A O 1 HETATM 6741 O O . HOH T 9 . ? 17.823 59.888 77.371 0.50 58.77 ? 1447 HOH A O 1 HETATM 6742 O O . HOH T 9 . ? 21.139 43.126 77.942 0.40 35.14 ? 1448 HOH A O 1 HETATM 6743 O O . HOH T 9 . ? 32.398 41.439 67.498 0.40 29.14 ? 1449 HOH A O 1 HETATM 6744 O O . HOH T 9 . ? 28.429 38.996 69.538 0.30 25.48 ? 1450 HOH A O 1 HETATM 6745 O O . HOH T 9 . ? 19.661 30.352 70.674 0.30 27.58 ? 1451 HOH A O 1 HETATM 6746 O O . HOH T 9 . ? 3.310 27.448 57.182 0.65 37.79 ? 1452 HOH A O 1 HETATM 6747 O O . HOH T 9 . ? 5.068 32.638 74.104 0.50 46.50 ? 1453 HOH A O 1 HETATM 6748 O O . HOH T 9 . ? 1.118 31.929 67.447 0.50 33.19 ? 1454 HOH A O 1 HETATM 6749 O O . HOH T 9 . ? -1.878 45.147 65.797 0.40 32.33 ? 1455 HOH A O 1 HETATM 6750 O O . HOH T 9 . ? -1.379 47.883 61.530 1.00 62.06 ? 1456 HOH A O 1 HETATM 6751 O O . HOH T 9 . ? -9.370 48.833 58.365 0.50 42.30 ? 1457 HOH A O 1 HETATM 6752 O O . HOH T 9 . ? -6.031 46.622 56.059 0.50 53.19 ? 1458 HOH A O 1 HETATM 6753 O O . HOH T 9 . ? -2.340 43.774 56.291 0.50 37.00 ? 1459 HOH A O 1 HETATM 6754 O O . HOH T 9 . ? -4.038 43.029 54.369 0.50 35.22 ? 1460 HOH A O 1 HETATM 6755 O O . HOH T 9 . ? -3.653 46.953 62.077 0.35 37.38 ? 1461 HOH A O 1 HETATM 6756 O O . HOH T 9 . ? -6.717 32.403 45.085 0.25 29.86 ? 1462 HOH A O 1 HETATM 6757 O O . HOH T 9 . ? -8.276 31.052 45.837 0.50 48.49 ? 1463 HOH A O 1 HETATM 6758 O O . HOH T 9 . ? -5.163 39.644 32.379 0.35 33.05 ? 1464 HOH A O 1 HETATM 6759 O O . HOH T 9 . ? 4.048 46.651 24.881 0.40 28.67 ? 1465 HOH A O 1 HETATM 6760 O O . HOH T 9 . ? 4.213 55.709 30.907 0.25 23.41 ? 1466 HOH A O 1 HETATM 6761 O O . HOH T 9 . ? 4.417 59.615 32.630 0.25 24.78 ? 1467 HOH A O 1 HETATM 6762 O O . HOH T 9 . ? 3.399 61.956 33.147 0.25 21.44 ? 1468 HOH A O 1 HETATM 6763 O O . HOH T 9 . ? 0.367 57.919 35.566 0.85 44.50 ? 1469 HOH A O 1 HETATM 6764 O O . HOH T 9 . ? 0.873 63.678 38.290 0.80 34.63 ? 1470 HOH A O 1 HETATM 6765 O O . HOH T 9 . ? 2.694 56.703 35.037 0.30 24.81 ? 1471 HOH A O 1 HETATM 6766 O O . HOH T 9 . ? 4.653 29.692 34.588 0.60 45.58 ? 1472 HOH A O 1 HETATM 6767 O O . HOH T 9 . ? 10.335 28.285 33.734 0.50 33.10 ? 1473 HOH A O 1 HETATM 6768 O O . HOH T 9 . ? 10.655 26.963 36.181 0.50 31.61 ? 1474 HOH A O 1 HETATM 6769 O O . HOH T 9 . ? 27.732 24.788 18.380 0.40 34.25 ? 1475 HOH A O 1 HETATM 6770 O O . HOH T 9 . ? 27.387 25.683 22.595 0.40 28.37 ? 1476 HOH A O 1 HETATM 6771 O O . HOH T 9 . ? 12.896 23.403 15.700 0.80 53.87 ? 1477 HOH A O 1 HETATM 6772 O O . HOH T 9 . ? 16.434 27.624 11.281 0.20 22.65 ? 1478 HOH A O 1 HETATM 6773 O O . HOH T 9 . ? 19.722 22.163 12.646 0.30 32.30 ? 1479 HOH A O 1 HETATM 6774 O O . HOH T 9 . ? 3.388 28.917 21.003 0.50 44.02 ? 1480 HOH A O 1 HETATM 6775 O O . HOH T 9 . ? 33.325 21.028 42.427 0.80 50.24 ? 1481 HOH A O 1 HETATM 6776 O O . HOH T 9 . ? 17.391 19.904 36.963 0.40 33.61 ? 1482 HOH A O 1 HETATM 6777 O O . HOH T 9 . ? 10.238 23.933 44.513 1.00 50.73 ? 1483 HOH A O 1 HETATM 6778 O O . HOH T 9 . ? 8.614 22.617 46.420 0.50 33.50 ? 1484 HOH A O 1 HETATM 6779 O O . HOH T 9 . ? 6.306 24.285 56.499 0.70 42.48 ? 1485 HOH A O 1 HETATM 6780 O O . HOH T 9 . ? 11.215 21.388 59.786 1.00 56.14 ? 1486 HOH A O 1 HETATM 6781 O O . HOH T 9 . ? 9.958 44.203 18.849 0.35 27.84 ? 1487 HOH A O 1 HETATM 6782 O O . HOH T 9 . ? 12.829 36.202 12.143 0.50 35.77 ? 1488 HOH A O 1 HETATM 6783 O O . HOH T 9 . ? 25.937 56.953 34.698 0.50 32.30 ? 1489 HOH A O 1 HETATM 6784 O O . HOH T 9 . ? 25.958 60.501 36.465 0.40 26.61 ? 1490 HOH A O 1 HETATM 6785 O O . HOH T 9 . ? 25.172 58.821 38.519 0.25 20.74 ? 1491 HOH A O 1 HETATM 6786 O O . HOH T 9 . ? 25.315 54.727 42.787 0.50 32.34 ? 1492 HOH A O 1 HETATM 6787 O O . HOH T 9 . ? 20.482 57.032 20.565 0.70 38.30 ? 1493 HOH A O 1 HETATM 6788 O O . HOH T 9 . ? 23.020 61.044 20.006 1.00 48.23 ? 1494 HOH A O 1 HETATM 6789 O O . HOH T 9 . ? 18.366 59.170 19.368 0.40 35.80 ? 1495 HOH A O 1 HETATM 6790 O O . HOH T 9 . ? 28.229 63.885 22.964 1.00 43.77 ? 1496 HOH A O 1 HETATM 6791 O O . HOH T 9 . ? 26.191 32.260 6.002 0.50 45.90 ? 1497 HOH A O 1 HETATM 6792 O O . HOH T 9 . ? 15.862 45.050 10.522 0.50 45.33 ? 1498 HOH A O 1 HETATM 6793 O O . HOH T 9 . ? 21.722 50.699 10.943 1.00 46.81 ? 1499 HOH A O 1 HETATM 6794 O O . HOH T 9 . ? 13.783 59.005 32.677 0.65 34.01 ? 1500 HOH A O 1 HETATM 6795 O O . HOH T 9 . ? 39.735 41.443 34.140 1.00 49.92 ? 1501 HOH A O 1 HETATM 6796 O O . HOH T 9 . ? 40.691 40.036 43.174 0.30 31.59 ? 1502 HOH A O 1 HETATM 6797 O O . HOH T 9 . ? 35.622 26.007 40.000 1.00 48.55 ? 1503 HOH A O 1 HETATM 6798 O O . HOH T 9 . ? -5.462 51.187 38.489 0.50 27.30 ? 1504 HOH A O 1 HETATM 6799 O O . HOH T 9 . ? 40.427 47.629 28.962 0.50 43.08 ? 1505 HOH A O 1 HETATM 6800 O O . HOH T 9 . ? 30.305 61.473 22.730 1.00 50.48 ? 1506 HOH A O 1 HETATM 6801 O O . HOH T 9 . ? 39.118 39.915 14.548 0.70 44.66 ? 1507 HOH A O 1 HETATM 6802 O O . HOH T 9 . ? 39.507 42.515 14.286 0.40 33.04 ? 1508 HOH A O 1 HETATM 6803 O O . HOH T 9 . ? 36.347 39.101 14.940 0.20 22.80 ? 1509 HOH A O 1 HETATM 6804 O O . HOH T 9 . ? 25.908 39.665 10.852 0.30 29.46 ? 1510 HOH A O 1 HETATM 6805 O O . HOH T 9 . ? 25.822 47.439 44.872 1.00 47.35 ? 1511 HOH A O 1 HETATM 6806 O O . HOH T 9 . ? 20.237 44.781 47.664 1.00 42.98 ? 1512 HOH A O 1 HETATM 6807 O O . HOH T 9 . ? 26.218 62.431 65.673 0.65 35.42 ? 1513 HOH A O 1 HETATM 6808 O O . HOH T 9 . ? 26.673 64.632 67.359 0.70 53.27 ? 1514 HOH A O 1 HETATM 6809 O O . HOH T 9 . ? 28.853 63.842 68.870 0.60 40.75 ? 1515 HOH A O 1 HETATM 6810 O O . HOH T 9 . ? 30.778 61.421 64.244 0.50 32.17 ? 1516 HOH A O 1 HETATM 6811 O O . HOH T 9 . ? 27.031 64.548 59.902 0.45 34.08 ? 1517 HOH A O 1 HETATM 6812 O O . HOH T 9 . ? 28.033 63.514 57.948 0.40 40.10 ? 1518 HOH A O 1 HETATM 6813 O O . HOH T 9 . ? 28.402 60.990 68.800 0.45 33.07 ? 1519 HOH A O 1 HETATM 6814 O O . HOH T 9 . ? 37.034 39.880 55.973 0.50 33.01 ? 1520 HOH A O 1 HETATM 6815 O O . HOH T 9 . ? 29.543 34.705 65.087 0.60 41.14 ? 1521 HOH A O 1 HETATM 6816 O O . HOH T 9 . ? 18.073 59.752 70.112 1.00 49.45 ? 1522 HOH A O 1 HETATM 6817 O O . HOH T 9 . ? 5.223 53.224 77.808 1.00 48.18 ? 1523 HOH A O 1 HETATM 6818 O O . HOH T 9 . ? -1.054 57.081 73.933 1.00 47.23 ? 1524 HOH A O 1 HETATM 6819 O O . HOH T 9 . ? 1.151 57.781 77.881 1.00 59.87 ? 1525 HOH A O 1 HETATM 6820 O O A HOH T 9 . ? 27.290 65.869 46.025 0.70 29.02 ? 1526 HOH A O 1 HETATM 6821 O O B HOH T 9 . ? 27.118 63.648 47.147 0.30 27.51 ? 1526 HOH A O 1 HETATM 6822 O O . HOH T 9 . ? 30.827 67.099 42.766 1.00 52.25 ? 1527 HOH A O 1 HETATM 6823 O O . HOH T 9 . ? 30.689 71.944 47.883 1.00 47.08 ? 1528 HOH A O 1 HETATM 6824 O O . HOH T 9 . ? 32.007 73.683 44.222 0.60 38.91 ? 1529 HOH A O 1 HETATM 6825 O O . HOH T 9 . ? 31.993 74.665 36.417 0.70 39.72 ? 1530 HOH A O 1 HETATM 6826 O O . HOH T 9 . ? 31.866 76.946 38.419 1.00 54.93 ? 1531 HOH A O 1 HETATM 6827 O O . HOH T 9 . ? 30.647 70.269 37.172 0.70 37.96 ? 1532 HOH A O 1 HETATM 6828 O O . HOH T 9 . ? 28.878 67.148 38.886 1.00 51.97 ? 1533 HOH A O 1 HETATM 6829 O O . HOH T 9 . ? 27.118 65.134 38.126 0.50 28.39 ? 1534 HOH A O 1 HETATM 6830 O O . HOH T 9 . ? 28.324 66.210 36.257 1.00 44.67 ? 1535 HOH A O 1 HETATM 6831 O O . HOH T 9 . ? 27.756 67.477 33.770 1.00 45.57 ? 1536 HOH A O 1 HETATM 6832 O O . HOH T 9 . ? 28.967 77.601 44.737 0.35 35.40 ? 1537 HOH A O 1 HETATM 6833 O O . HOH T 9 . ? 29.703 86.339 27.206 1.00 54.76 ? 1538 HOH A O 1 HETATM 6834 O O . HOH T 9 . ? 17.998 21.758 59.983 1.00 65.65 ? 1539 HOH A O 1 HETATM 6835 O O . HOH T 9 . ? 32.632 87.421 30.768 0.50 35.31 ? 1540 HOH A O 1 HETATM 6836 O O . HOH T 9 . ? 32.352 84.706 32.465 1.00 57.42 ? 1541 HOH A O 1 HETATM 6837 O O . HOH T 9 . ? 21.694 88.100 46.743 0.30 31.90 ? 1542 HOH A O 1 HETATM 6838 O O . HOH T 9 . ? 26.221 85.784 45.414 0.80 40.32 ? 1543 HOH A O 1 HETATM 6839 O O . HOH T 9 . ? 16.571 85.962 43.385 0.50 33.08 ? 1544 HOH A O 1 HETATM 6840 O O . HOH T 9 . ? 23.634 75.016 62.664 0.60 32.76 ? 1545 HOH A O 1 HETATM 6841 O O . HOH T 9 . ? 20.343 80.794 62.860 0.30 26.33 ? 1546 HOH A O 1 HETATM 6842 O O . HOH T 9 . ? 22.957 79.496 60.137 0.50 32.69 ? 1547 HOH A O 1 HETATM 6843 O O . HOH T 9 . ? 13.723 81.559 65.675 0.50 32.75 ? 1548 HOH A O 1 HETATM 6844 O O . HOH T 9 . ? 15.537 78.391 72.047 0.30 30.72 ? 1549 HOH A O 1 HETATM 6845 O O . HOH T 9 . ? 12.411 81.217 69.740 0.25 27.75 ? 1550 HOH A O 1 HETATM 6846 O O . HOH T 9 . ? 17.375 66.139 70.544 0.70 42.49 ? 1551 HOH A O 1 HETATM 6847 O O . HOH T 9 . ? 18.332 68.248 74.935 0.30 25.23 ? 1552 HOH A O 1 HETATM 6848 O O . HOH T 9 . ? 9.135 59.254 31.525 0.30 22.37 ? 1553 HOH A O 1 HETATM 6849 O O . HOH T 9 . ? 5.975 75.268 76.905 0.85 43.37 ? 1554 HOH A O 1 HETATM 6850 O O . HOH T 9 . ? 11.499 67.306 30.632 0.35 33.51 ? 1555 HOH A O 1 HETATM 6851 O O . HOH T 9 . ? 17.833 62.004 27.968 0.40 27.62 ? 1556 HOH A O 1 HETATM 6852 O O . HOH T 9 . ? 25.192 69.261 60.787 0.25 22.34 ? 1557 HOH A O 1 HETATM 6853 O O A HOH T 9 . ? -3.798 29.595 46.795 0.70 47.90 ? 1558 HOH A O 1 HETATM 6854 O O B HOH T 9 . ? -4.790 29.952 48.568 0.30 36.59 ? 1558 HOH A O 1 HETATM 6855 O O . HOH T 9 . ? -6.409 34.384 42.245 0.60 36.07 ? 1559 HOH A O 1 HETATM 6856 O O . HOH T 9 . ? -5.355 36.354 40.589 1.00 51.90 ? 1560 HOH A O 1 HETATM 6857 O O . HOH T 9 . ? 4.938 27.531 30.453 0.80 45.71 ? 1561 HOH A O 1 HETATM 6858 O O . HOH T 9 . ? 24.470 22.017 31.398 1.00 51.49 ? 1562 HOH A O 1 HETATM 6859 O O . HOH T 9 . ? -4.394 56.509 34.269 1.00 47.68 ? 1563 HOH A O 1 HETATM 6860 O O . HOH T 9 . ? 41.432 39.072 20.440 1.00 54.32 ? 1564 HOH A O 1 HETATM 6861 O O . HOH T 9 . ? 24.479 81.617 50.237 0.70 43.46 ? 1565 HOH A O 1 HETATM 6862 O O . HOH T 9 . ? 25.498 82.005 53.159 1.00 53.74 ? 1566 HOH A O 1 HETATM 6863 O O . HOH T 9 . ? 1.189 63.279 42.920 1.00 30.52 ? 1567 HOH A O 1 HETATM 6864 O O . HOH T 9 . ? 11.370 74.748 20.133 0.50 37.97 ? 1568 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . HIS A 63 ? 0.7877 0.6189 0.4311 0.2088 -0.0536 0.0278 56 HIS A N 2 C CA . HIS A 63 ? 0.7529 0.5961 0.4235 0.1959 -0.0476 0.0271 56 HIS A CA 3 C C . HIS A 63 ? 0.7252 0.5776 0.4098 0.1906 -0.0560 0.0172 56 HIS A C 4 O O . HIS A 63 ? 0.7409 0.5944 0.4213 0.1901 -0.0538 0.0147 56 HIS A O 5 C CB . HIS A 63 ? 0.7575 0.6007 0.4274 0.1923 -0.0322 0.0340 56 HIS A CB 6 C CG . HIS A 63 ? 0.7822 0.6176 0.4435 0.1953 -0.0220 0.0444 56 HIS A CG 7 N ND1 . HIS A 63 ? 0.8081 0.6361 0.4522 0.2001 -0.0109 0.0514 56 HIS A ND1 8 C CD2 . HIS A 63 ? 0.7839 0.6176 0.4519 0.1942 -0.0208 0.0490 56 HIS A CD2 9 C CE1 . HIS A 63 ? 0.8440 0.6659 0.4850 0.2016 -0.0032 0.0603 56 HIS A CE1 10 N NE2 . HIS A 63 ? 0.8216 0.6467 0.4767 0.1982 -0.0092 0.0589 56 HIS A NE2 11 N N . ASN A 64 ? 0.6828 0.5418 0.3847 0.1866 -0.0652 0.0119 57 ASN A N 12 C CA . ASN A 64 ? 0.6327 0.5006 0.3503 0.1812 -0.0735 0.0027 57 ASN A CA 13 C C . ASN A 64 ? 0.5888 0.4662 0.3320 0.1721 -0.0738 0.0017 57 ASN A C 14 O O . ASN A 64 ? 0.5694 0.4461 0.3170 0.1702 -0.0672 0.0078 57 ASN A O 15 C CB . ASN A 64 ? 0.6410 0.5050 0.3486 0.1891 -0.0882 -0.0047 57 ASN A CB 16 C CG . ASN A 64 ? 0.6536 0.5120 0.3547 0.1960 -0.0953 -0.0032 57 ASN A CG 17 O OD1 . ASN A 64 ? 0.6247 0.4841 0.3340 0.1933 -0.0905 0.0021 57 ASN A OD1 18 N ND2 . ASN A 64 ? 0.6980 0.5500 0.3838 0.2054 -0.1071 -0.0080 57 ASN A ND2 19 N N . MET A 65 ? 0.5607 0.4466 0.3209 0.1666 -0.0811 -0.0059 58 MET A N 20 C CA . MET A 65 ? 0.5355 0.4306 0.3198 0.1578 -0.0800 -0.0066 58 MET A CA 21 C C . MET A 65 ? 0.5314 0.4243 0.3175 0.1615 -0.0848 -0.0053 58 MET A C 22 O O . MET A 65 ? 0.5220 0.4184 0.3206 0.1565 -0.0794 -0.0019 58 MET A O 23 C CB . MET A 65 ? 0.5254 0.4299 0.3283 0.1512 -0.0862 -0.0145 58 MET A CB 24 C CG . MET A 65 ? 0.5234 0.4372 0.3495 0.1413 -0.0810 -0.0135 58 MET A CG 25 S SD . MET A 65 ? 0.6158 0.5403 0.4644 0.1341 -0.0882 -0.0220 58 MET A SD 26 C CE . MET A 65 ? 0.5756 0.5008 0.4197 0.1311 -0.0842 -0.0232 58 MET A CE 27 N N . LYS A 66 ? 0.5424 0.4292 0.3161 0.1705 -0.0953 -0.0082 59 LYS A N 28 C CA . LYS A 66 ? 0.5471 0.4314 0.3222 0.1748 -0.1008 -0.0070 59 LYS A CA 29 C C . LYS A 66 ? 0.5462 0.4239 0.3125 0.1767 -0.0906 0.0027 59 LYS A C 30 O O . LYS A 66 ? 0.5429 0.4224 0.3202 0.1748 -0.0899 0.0048 59 LYS A O 31 C CB . LYS A 66 ? 0.5651 0.4429 0.3256 0.1853 -0.1142 -0.0115 59 LYS A CB 32 C CG . LYS A 66 ? 0.5901 0.4658 0.3531 0.1902 -0.1215 -0.0111 59 LYS A CG 33 C CD . LYS A 66 ? 0.6304 0.4984 0.3759 0.2016 -0.1351 -0.0154 59 LYS A CD 34 C CE . LYS A 66 ? 0.6461 0.5147 0.3999 0.2056 -0.1455 -0.0176 59 LYS A CE 35 N NZ . LYS A 66 ? 0.6512 0.5154 0.4028 0.2070 -0.1384 -0.0092 59 LYS A NZ 36 N N . ALA A 67 ? 0.5601 0.4303 0.3078 0.1801 -0.0822 0.0085 60 ALA A N 37 C CA . ALA A 67 ? 0.5716 0.4352 0.3117 0.1816 -0.0716 0.0181 60 ALA A CA 38 C C . ALA A 67 ? 0.5428 0.4146 0.3047 0.1707 -0.0625 0.0203 60 ALA A C 39 O O . ALA A 67 ? 0.5532 0.4235 0.3210 0.1697 -0.0591 0.0247 60 ALA A O 40 C CB . ALA A 67 ? 0.5977 0.4528 0.3155 0.1867 -0.0634 0.0237 60 ALA A CB 41 N N . PHE A 68 ? 0.5098 0.3898 0.2830 0.1628 -0.0590 0.0170 61 PHE A N 42 C CA . PHE A 68 ? 0.4904 0.3784 0.2838 0.1526 -0.0513 0.0182 61 PHE A CA 43 C C . PHE A 68 ? 0.4665 0.3604 0.2782 0.1491 -0.0569 0.0148 61 PHE A C 44 O O . PHE A 68 ? 0.4590 0.3536 0.2800 0.1456 -0.0513 0.0186 61 PHE A O 45 C CB . PHE A 68 ? 0.4611 0.3569 0.2632 0.1454 -0.0488 0.0143 61 PHE A CB 46 C CG . PHE A 68 ? 0.4523 0.3575 0.2767 0.1351 -0.0444 0.0132 61 PHE A CG 47 C CD1 . PHE A 68 ? 0.4521 0.3570 0.2808 0.1307 -0.0337 0.0192 61 PHE A CD1 48 C CD2 . PHE A 68 ? 0.4163 0.3301 0.2571 0.1302 -0.0512 0.0063 61 PHE A CD2 49 C CE1 . PHE A 68 ? 0.4260 0.3392 0.2745 0.1216 -0.0303 0.0178 61 PHE A CE1 50 C CE2 . PHE A 68 ? 0.4186 0.3405 0.2785 0.1213 -0.0470 0.0054 61 PHE A CE2 51 C CZ . PHE A 68 ? 0.4269 0.3484 0.2900 0.1172 -0.0369 0.0109 61 PHE A CZ 52 N N . LEU A 69 ? 0.4645 0.3629 0.2823 0.1499 -0.0678 0.0074 62 LEU A N 53 C CA . LEU A 69 ? 0.4586 0.3636 0.2951 0.1467 -0.0732 0.0034 62 LEU A CA 54 C C . LEU A 69 ? 0.4794 0.3783 0.3122 0.1525 -0.0752 0.0072 62 LEU A C 55 O O . LEU A 69 ? 0.4735 0.3762 0.3212 0.1484 -0.0732 0.0077 62 LEU A O 56 C CB . LEU A 69 ? 0.4629 0.3731 0.3061 0.1474 -0.0849 -0.0051 62 LEU A CB 57 C CG . LEU A 69 ? 0.4415 0.3591 0.2935 0.1405 -0.0838 -0.0096 62 LEU A CG 58 C CD1 . LEU A 69 ? 0.4823 0.4026 0.3377 0.1431 -0.0962 -0.0176 62 LEU A CD1 59 C CD2 . LEU A 69 ? 0.4038 0.3308 0.2769 0.1299 -0.0769 -0.0099 62 LEU A CD2 60 N N . ASP A 70 ? 0.5112 0.4001 0.3234 0.1623 -0.0792 0.0098 63 ASP A N 61 C CA . ASP A 70 ? 0.5355 0.4176 0.3426 0.1690 -0.0824 0.0133 63 ASP A CA 62 C C . ASP A 70 ? 0.5330 0.4112 0.3411 0.1665 -0.0709 0.0215 63 ASP A C 63 O O . ASP A 70 ? 0.5400 0.4155 0.3522 0.1687 -0.0720 0.0239 63 ASP A O 64 C CB . ASP A 70 ? 0.5650 0.4361 0.3472 0.1807 -0.0888 0.0149 63 ASP A CB 65 C CG . ASP A 70 ? 0.6033 0.4769 0.3857 0.1852 -0.1034 0.0064 63 ASP A CG 66 O OD1 . ASP A 70 ? 0.6154 0.4993 0.4188 0.1795 -0.1089 -0.0005 63 ASP A OD1 67 O OD2 . ASP A 70 ? 0.6376 0.5026 0.3988 0.1947 -0.1094 0.0065 63 ASP A OD2 68 N N . GLU A 71 ? 0.5227 0.4005 0.3276 0.1620 -0.0600 0.0257 64 GLU A N 69 C CA . GLU A 71 ? 0.5213 0.3950 0.3271 0.1594 -0.0487 0.0335 64 GLU A CA 70 C C . GLU A 71 ? 0.4895 0.3715 0.3188 0.1503 -0.0452 0.0317 64 GLU A C 71 O O . GLU A 71 ? 0.4958 0.3740 0.3288 0.1495 -0.0395 0.0368 64 GLU A O 72 C CB . GLU A 71 ? 0.5275 0.3978 0.3223 0.1583 -0.0385 0.0385 64 GLU A CB 73 C CG . GLU A 71 ? 0.5628 0.4292 0.3601 0.1549 -0.0261 0.0465 64 GLU A CG 74 C CD . GLU A 71 ? 0.6366 0.4915 0.4218 0.1626 -0.0248 0.0538 64 GLU A CD 75 O OE1 . GLU A 71 ? 0.6624 0.5094 0.4286 0.1722 -0.0306 0.0549 64 GLU A OE1 76 O OE2 . GLU A 71 ? 0.6426 0.4959 0.4372 0.1592 -0.0184 0.0583 64 GLU A OE2 77 N N . LEU A 72 ? 0.4676 0.3604 0.3124 0.1438 -0.0488 0.0244 65 LEU A N 78 C CA . LEU A 72 ? 0.4413 0.3424 0.3079 0.1357 -0.0467 0.0217 65 LEU A CA 79 C C . LEU A 72 ? 0.4530 0.3525 0.3262 0.1392 -0.0518 0.0213 65 LEU A C 80 O O . LEU A 72 ? 0.4523 0.3508 0.3220 0.1454 -0.0617 0.0181 65 LEU A O 81 C CB . LEU A 72 ? 0.4199 0.3321 0.2999 0.1297 -0.0510 0.0138 65 LEU A CB 82 C CG . LEU A 72 ? 0.4004 0.3154 0.2760 0.1262 -0.0476 0.0128 65 LEU A CG 83 C CD1 . LEU A 72 ? 0.3876 0.3118 0.2747 0.1223 -0.0543 0.0050 65 LEU A CD1 84 C CD2 . LEU A 72 ? 0.3821 0.2991 0.2643 0.1187 -0.0365 0.0165 65 LEU A CD2 85 N N . LYS A 73 ? 0.4448 0.3445 0.3286 0.1352 -0.0456 0.0240 66 LYS A N 86 C CA . LYS A 73 ? 0.4616 0.3594 0.3524 0.1384 -0.0496 0.0239 66 LYS A CA 87 C C . LYS A 73 ? 0.4344 0.3408 0.3467 0.1308 -0.0472 0.0199 66 LYS A C 88 O O . LYS A 73 ? 0.4274 0.3358 0.3459 0.1240 -0.0387 0.0215 66 LYS A O 89 C CB . LYS A 73 ? 0.4880 0.3740 0.3673 0.1435 -0.0444 0.0324 66 LYS A CB 90 C CG . LYS A 73 ? 0.5456 0.4212 0.4010 0.1522 -0.0456 0.0375 66 LYS A CG 91 C CD . LYS A 73 ? 0.6361 0.5103 0.4842 0.1606 -0.0582 0.0337 66 LYS A CD 92 C CE . LYS A 73 ? 0.6845 0.5462 0.5073 0.1708 -0.0596 0.0396 66 LYS A CE 93 N NZ . LYS A 73 ? 0.6706 0.5320 0.4800 0.1713 -0.0584 0.0390 66 LYS A NZ 94 N N . ALA A 74 ? 0.4362 0.3475 0.3597 0.1322 -0.0548 0.0148 67 ALA A N 95 C CA . ALA A 74 ? 0.4187 0.3377 0.3623 0.1262 -0.0528 0.0109 67 ALA A CA 96 C C . ALA A 74 ? 0.4176 0.3310 0.3637 0.1247 -0.0450 0.0158 67 ALA A C 97 O O . ALA A 74 ? 0.3860 0.3044 0.3442 0.1174 -0.0390 0.0142 67 ALA A O 98 C CB . ALA A 74 ? 0.4224 0.3460 0.3768 0.1297 -0.0622 0.0055 67 ALA A CB 99 N N . GLU A 75 ? 0.4307 0.3335 0.3652 0.1316 -0.0452 0.0218 68 GLU A N 100 C CA . GLU A 75 ? 0.4392 0.3358 0.3770 0.1306 -0.0384 0.0266 68 GLU A CA 101 C C . GLU A 75 ? 0.4314 0.3268 0.3680 0.1241 -0.0280 0.0302 68 GLU A C 102 O O . GLU A 75 ? 0.4204 0.3157 0.3672 0.1194 -0.0221 0.0309 68 GLU A O 103 C CB . GLU A 75 ? 0.4630 0.3475 0.3875 0.1398 -0.0406 0.0330 68 GLU A CB 104 C CG . GLU A 75 ? 0.5051 0.3820 0.4334 0.1391 -0.0335 0.0384 68 GLU A CG 105 C CD . GLU A 75 ? 0.5378 0.4183 0.4835 0.1379 -0.0358 0.0342 68 GLU A CD 106 O OE1 . GLU A 75 ? 0.5206 0.4090 0.4757 0.1388 -0.0432 0.0277 68 GLU A OE1 107 O OE2 . GLU A 75 ? 0.5764 0.4515 0.5271 0.1364 -0.0298 0.0377 68 GLU A OE2 108 N N . ASN A 76 ? 0.4170 0.3117 0.3417 0.1240 -0.0262 0.0322 69 ASN A N 109 C CA . ASN A 76 ? 0.4096 0.3045 0.3345 0.1177 -0.0168 0.0351 69 ASN A CA 110 C C . ASN A 76 ? 0.3891 0.2947 0.3297 0.1087 -0.0149 0.0290 69 ASN A C 111 O O . ASN A 76 ? 0.3824 0.2882 0.3302 0.1031 -0.0079 0.0302 69 ASN A O 112 C CB . ASN A 76 ? 0.4232 0.3151 0.3321 0.1200 -0.0152 0.0384 69 ASN A CB 113 C CG . ASN A 76 ? 0.4454 0.3248 0.3369 0.1282 -0.0138 0.0463 69 ASN A CG 114 O OD1 . ASN A 76 ? 0.4868 0.3589 0.3793 0.1299 -0.0102 0.0512 69 ASN A OD1 115 N ND2 . ASN A 76 ? 0.4585 0.3349 0.3338 0.1336 -0.0166 0.0474 69 ASN A ND2 116 N N . ILE A 77 ? 0.3749 0.2890 0.3204 0.1076 -0.0210 0.0226 70 ILE A N 117 C CA . ILE A 77 ? 0.3528 0.2769 0.3120 0.0996 -0.0194 0.0169 70 ILE A CA 118 C C . ILE A 77 ? 0.3554 0.2807 0.3284 0.0968 -0.0171 0.0152 70 ILE A C 119 O O . ILE A 77 ? 0.3455 0.2742 0.3268 0.0902 -0.0116 0.0138 70 ILE A O 120 C CB . ILE A 77 ? 0.3485 0.2808 0.3114 0.0997 -0.0268 0.0106 70 ILE A CB 121 C CG1 . ILE A 77 ? 0.3521 0.2825 0.3008 0.1027 -0.0292 0.0119 70 ILE A CG1 122 C CG2 . ILE A 77 ? 0.3238 0.2660 0.3006 0.0916 -0.0245 0.0052 70 ILE A CG2 123 C CD1 . ILE A 77 ? 0.3793 0.3160 0.3303 0.1039 -0.0376 0.0060 70 ILE A CD1 124 N N . LYS A 78 ? 0.3538 0.2756 0.3285 0.1023 -0.0216 0.0153 71 LYS A N 125 C CA . LYS A 78 ? 0.3565 0.2782 0.3436 0.1009 -0.0197 0.0137 71 LYS A CA 126 C C . LYS A 78 ? 0.3709 0.2860 0.3576 0.0981 -0.0116 0.0185 71 LYS A C 127 O O . LYS A 78 ? 0.3621 0.2804 0.3595 0.0923 -0.0074 0.0158 71 LYS A O 128 C CB . LYS A 78 ? 0.3722 0.2898 0.3592 0.1086 -0.0262 0.0141 71 LYS A CB 129 C CG . LYS A 78 ? 0.3738 0.2910 0.3737 0.1081 -0.0247 0.0124 71 LYS A CG 130 C CD . LYS A 78 ? 0.3927 0.3070 0.3930 0.1160 -0.0322 0.0122 71 LYS A CD 131 C CE . LYS A 78 ? 0.4374 0.3509 0.4505 0.1159 -0.0308 0.0105 71 LYS A CE 132 N NZ . LYS A 78 ? 0.4383 0.3478 0.4513 0.1244 -0.0381 0.0112 71 LYS A NZ 133 N N . LYS A 79 ? 0.3829 0.2884 0.3573 0.1023 -0.0094 0.0256 72 LYS A N 134 C CA . LYS A 79 ? 0.3927 0.2913 0.3672 0.0998 -0.0015 0.0308 72 LYS A CA 135 C C . LYS A 79 ? 0.3726 0.2767 0.3520 0.0916 0.0043 0.0292 72 LYS A C 136 O O . LYS A 79 ? 0.3706 0.2740 0.3590 0.0868 0.0092 0.0288 72 LYS A O 137 C CB . LYS A 79 ? 0.4076 0.2952 0.3667 0.1058 0.0005 0.0392 72 LYS A CB 138 C CG . LYS A 79 ? 0.4497 0.3294 0.4042 0.1139 -0.0039 0.0422 72 LYS A CG 139 C CD . LYS A 79 ? 0.4883 0.3577 0.4245 0.1208 -0.0028 0.0502 72 LYS A CD 140 C CE . LYS A 79 ? 0.5157 0.3768 0.4459 0.1295 -0.0079 0.0533 72 LYS A CE 141 N NZ . LYS A 79 ? 0.5456 0.3960 0.4557 0.1368 -0.0067 0.0613 72 LYS A NZ 142 N N . PHE A 80 ? 0.3551 0.2646 0.3288 0.0901 0.0031 0.0277 73 PHE A N 143 C CA . PHE A 80 ? 0.3406 0.2555 0.3186 0.0829 0.0078 0.0261 73 PHE A CA 144 C C . PHE A 80 ? 0.3302 0.2533 0.3219 0.0771 0.0072 0.0191 73 PHE A C 145 O O . PHE A 80 ? 0.3348 0.2593 0.3337 0.0713 0.0119 0.0181 73 PHE A O 146 C CB . PHE A 80 ? 0.3295 0.2480 0.2980 0.0833 0.0062 0.0261 73 PHE A CB 147 C CG . PHE A 80 ? 0.3621 0.2725 0.3158 0.0888 0.0079 0.0329 73 PHE A CG 148 C CD1 . PHE A 80 ? 0.3831 0.2845 0.3340 0.0904 0.0137 0.0396 73 PHE A CD1 149 C CD2 . PHE A 80 ? 0.3615 0.2731 0.3040 0.0925 0.0040 0.0326 73 PHE A CD2 150 C CE1 . PHE A 80 ? 0.4169 0.3104 0.3532 0.0959 0.0162 0.0464 73 PHE A CE1 151 C CE2 . PHE A 80 ? 0.3904 0.2941 0.3176 0.0981 0.0059 0.0388 73 PHE A CE2 152 C CZ . PHE A 80 ? 0.4124 0.3072 0.3362 0.0999 0.0123 0.0459 73 PHE A CZ 153 N N . LEU A 81 ? 0.3183 0.2469 0.3141 0.0786 0.0014 0.0141 74 LEU A N 154 C CA . LEU A 81 ? 0.3102 0.2463 0.3184 0.0736 0.0014 0.0077 74 LEU A CA 155 C C . LEU A 81 ? 0.3159 0.2480 0.3324 0.0722 0.0050 0.0076 74 LEU A C 156 O O . LEU A 81 ? 0.3127 0.2479 0.3361 0.0665 0.0085 0.0046 74 LEU A O 157 C CB . LEU A 81 ? 0.3068 0.2489 0.3195 0.0761 -0.0048 0.0029 74 LEU A CB 158 C CG . LEU A 81 ? 0.3012 0.2515 0.3261 0.0709 -0.0038 -0.0035 74 LEU A CG 159 C CD1 . LEU A 81 ? 0.2711 0.2270 0.2950 0.0648 -0.0010 -0.0051 74 LEU A CD1 160 C CD2 . LEU A 81 ? 0.3235 0.2794 0.3544 0.0737 -0.0093 -0.0077 74 LEU A CD2 161 N N . TYR A 82 ? 0.3173 0.2420 0.3327 0.0775 0.0039 0.0108 75 TYR A N 162 C CA . TYR A 82 ? 0.3286 0.2482 0.3518 0.0765 0.0073 0.0109 75 TYR A CA 163 C C . TYR A 82 ? 0.3323 0.2486 0.3557 0.0715 0.0137 0.0137 75 TYR A C 164 O O . TYR A 82 ? 0.3336 0.2512 0.3659 0.0667 0.0166 0.0104 75 TYR A O 165 C CB . TYR A 82 ? 0.3384 0.2491 0.3582 0.0836 0.0053 0.0154 75 TYR A CB 166 C CG . TYR A 82 ? 0.3671 0.2720 0.3955 0.0828 0.0085 0.0155 75 TYR A CG 167 C CD1 . TYR A 82 ? 0.3790 0.2874 0.4182 0.0828 0.0066 0.0097 75 TYR A CD1 168 C CD2 . TYR A 82 ? 0.4123 0.3084 0.4387 0.0818 0.0139 0.0212 75 TYR A CD2 169 C CE1 . TYR A 82 ? 0.3968 0.2993 0.4439 0.0822 0.0095 0.0094 75 TYR A CE1 170 C CE2 . TYR A 82 ? 0.4368 0.3271 0.4721 0.0809 0.0167 0.0211 75 TYR A CE2 171 C CZ . TYR A 82 ? 0.4254 0.3188 0.4705 0.0811 0.0143 0.0149 75 TYR A CZ 172 O OH . TYR A 82 ? 0.4822 0.3697 0.5361 0.0804 0.0168 0.0142 75 TYR A OH 173 N N . ASN A 83 ? 0.3377 0.2499 0.3515 0.0726 0.0159 0.0196 76 ASN A N 174 C CA . ASN A 83 ? 0.3401 0.2491 0.3550 0.0683 0.0220 0.0230 76 ASN A CA 175 C C . ASN A 83 ? 0.3253 0.2423 0.3463 0.0611 0.0236 0.0179 76 ASN A C 176 O O . ASN A 83 ? 0.3336 0.2491 0.3611 0.0565 0.0277 0.0179 76 ASN A O 177 C CB . ASN A 83 ? 0.3583 0.2625 0.3611 0.0715 0.0241 0.0300 76 ASN A CB 178 C CG . ASN A 83 ? 0.3801 0.2810 0.3848 0.0674 0.0308 0.0340 76 ASN A CG 179 O OD1 . ASN A 83 ? 0.3788 0.2854 0.3840 0.0631 0.0325 0.0327 76 ASN A OD1 180 N ND2 . ASN A 83 ? 0.4104 0.3021 0.4174 0.0687 0.0348 0.0391 76 ASN A ND2 181 N N . PHE A 84 ? 0.2993 0.2246 0.3183 0.0602 0.0200 0.0137 77 PHE A N 182 C CA . PHE A 84 ? 0.2848 0.2177 0.3075 0.0540 0.0211 0.0095 77 PHE A CA 183 C C . PHE A 84 ? 0.2843 0.2220 0.3166 0.0504 0.0204 0.0026 77 PHE A C 184 O O . PHE A 84 ? 0.2833 0.2267 0.3182 0.0455 0.0212 -0.0011 77 PHE A O 185 C CB . PHE A 84 ? 0.2808 0.2200 0.2966 0.0546 0.0179 0.0084 77 PHE A CB 186 C CG . PHE A 84 ? 0.3007 0.2365 0.3060 0.0573 0.0189 0.0142 77 PHE A CG 187 C CD1 . PHE A 84 ? 0.3214 0.2497 0.3238 0.0584 0.0235 0.0203 77 PHE A CD1 188 C CD2 . PHE A 84 ? 0.3041 0.2444 0.3025 0.0588 0.0154 0.0132 77 PHE A CD2 189 C CE1 . PHE A 84 ? 0.3094 0.2348 0.3012 0.0613 0.0251 0.0256 77 PHE A CE1 190 C CE2 . PHE A 84 ? 0.3249 0.2622 0.3127 0.0616 0.0163 0.0179 77 PHE A CE2 191 C CZ . PHE A 84 ? 0.3108 0.2408 0.2949 0.0630 0.0214 0.0242 77 PHE A CZ 192 N N . THR A 85 ? 0.2965 0.2319 0.3337 0.0532 0.0189 0.0007 78 THR A N 193 C CA . THR A 85 ? 0.2879 0.2288 0.3330 0.0509 0.0179 -0.0061 78 THR A CA 194 C C . THR A 85 ? 0.3011 0.2367 0.3541 0.0506 0.0199 -0.0080 78 THR A C 195 O O . THR A 85 ? 0.2869 0.2258 0.3459 0.0503 0.0191 -0.0135 78 THR A O 196 C CB . THR A 85 ? 0.2938 0.2395 0.3391 0.0547 0.0135 -0.0087 78 THR A CB 197 O OG1 . THR A 85 ? 0.2912 0.2307 0.3348 0.0607 0.0114 -0.0051 78 THR A OG1 198 C CG2 . THR A 85 ? 0.2789 0.2308 0.3179 0.0541 0.0111 -0.0085 78 THR A CG2 199 N N . GLN A 86 ? 0.3092 0.2367 0.3626 0.0508 0.0227 -0.0035 79 GLN A N 200 C CA . GLN A 86 ? 0.3443 0.2657 0.4057 0.0508 0.0243 -0.0050 79 GLN A CA 201 C C . GLN A 86 ? 0.3423 0.2657 0.4101 0.0449 0.0264 -0.0103 79 GLN A C 202 O O . GLN A 86 ? 0.3556 0.2762 0.4305 0.0446 0.0268 -0.0142 79 GLN A O 203 C CB . GLN A 86 ? 0.3567 0.2679 0.4166 0.0533 0.0267 0.0022 79 GLN A CB 204 C CG . GLN A 86 ? 0.3649 0.2725 0.4178 0.0602 0.0242 0.0071 79 GLN A CG 205 C CD . GLN A 86 ? 0.3691 0.2797 0.4260 0.0636 0.0202 0.0025 79 GLN A CD 206 O OE1 . GLN A 86 ? 0.4041 0.3105 0.4684 0.0645 0.0207 0.0004 79 GLN A OE1 207 N NE2 . GLN A 86 ? 0.3694 0.2873 0.4225 0.0654 0.0164 0.0004 79 GLN A NE2 208 N N . ILE A 87 ? 0.3454 0.2730 0.4106 0.0406 0.0274 -0.0103 80 ILE A N 209 C CA . ILE A 87 ? 0.3367 0.2664 0.4070 0.0352 0.0285 -0.0153 80 ILE A CA 210 C C . ILE A 87 ? 0.3191 0.2576 0.3846 0.0324 0.0273 -0.0180 80 ILE A C 211 O O . ILE A 87 ? 0.3136 0.2552 0.3726 0.0341 0.0263 -0.0146 80 ILE A O 212 C CB . ILE A 87 ? 0.3568 0.2805 0.4310 0.0322 0.0315 -0.0119 80 ILE A CB 213 C CG1 . ILE A 87 ? 0.3660 0.2909 0.4342 0.0319 0.0329 -0.0057 80 ILE A CG1 214 C CG2 . ILE A 87 ? 0.3898 0.3038 0.4695 0.0348 0.0331 -0.0091 80 ILE A CG2 215 C CD1 . ILE A 87 ? 0.4169 0.3380 0.4906 0.0282 0.0361 -0.0029 80 ILE A CD1 216 N N . PRO A 88 ? 0.3068 0.2489 0.3749 0.0284 0.0272 -0.0240 81 PRO A N 217 C CA . PRO A 88 ? 0.2950 0.2449 0.3581 0.0258 0.0261 -0.0259 81 PRO A CA 218 C C . PRO A 88 ? 0.2819 0.2322 0.3422 0.0236 0.0269 -0.0214 81 PRO A C 219 O O . PRO A 88 ? 0.2929 0.2382 0.3572 0.0222 0.0288 -0.0187 81 PRO A O 220 C CB . PRO A 88 ? 0.3017 0.2534 0.3680 0.0224 0.0260 -0.0329 81 PRO A CB 221 C CG . PRO A 88 ? 0.3178 0.2644 0.3898 0.0247 0.0265 -0.0358 81 PRO A CG 222 C CD . PRO A 88 ? 0.3036 0.2429 0.3784 0.0268 0.0276 -0.0296 81 PRO A CD 223 N N . HIS A 89 ? 0.2629 0.2191 0.3170 0.0233 0.0258 -0.0205 82 HIS A N 224 C CA . HIS A 89 ? 0.2622 0.2197 0.3135 0.0213 0.0265 -0.0168 82 HIS A CA 225 C C . HIS A 89 ? 0.2491 0.2134 0.2979 0.0180 0.0251 -0.0205 82 HIS A C 226 O O . HIS A 89 ? 0.2557 0.2239 0.2990 0.0182 0.0243 -0.0185 82 HIS A O 227 C CB . HIS A 89 ? 0.2736 0.2302 0.3186 0.0251 0.0265 -0.0109 82 HIS A CB 228 C CG . HIS A 89 ? 0.2760 0.2251 0.3222 0.0286 0.0281 -0.0063 82 HIS A CG 229 N ND1 . HIS A 89 ? 0.2969 0.2439 0.3415 0.0331 0.0266 -0.0059 82 HIS A ND1 230 C CD2 . HIS A 89 ? 0.2831 0.2259 0.3326 0.0283 0.0313 -0.0021 82 HIS A CD2 231 C CE1 . HIS A 89 ? 0.3207 0.2601 0.3663 0.0358 0.0284 -0.0013 82 HIS A CE1 232 N NE2 . HIS A 89 ? 0.3057 0.2423 0.3542 0.0328 0.0316 0.0012 82 HIS A NE2 233 N N . LEU A 90 ? 0.2539 0.2189 0.3061 0.0150 0.0247 -0.0257 83 LEU A N 234 C CA . LEU A 90 ? 0.2466 0.2173 0.2955 0.0121 0.0233 -0.0294 83 LEU A CA 235 C C . LEU A 90 ? 0.2417 0.2138 0.2901 0.0097 0.0232 -0.0265 83 LEU A C 236 O O . LEU A 90 ? 0.2590 0.2275 0.3126 0.0087 0.0245 -0.0243 83 LEU A O 237 C CB . LEU A 90 ? 0.2442 0.2141 0.2961 0.0101 0.0227 -0.0358 83 LEU A CB 238 C CG . LEU A 90 ? 0.2433 0.2182 0.2902 0.0078 0.0211 -0.0399 83 LEU A CG 239 C CD1 . LEU A 90 ? 0.2355 0.2150 0.2771 0.0094 0.0213 -0.0407 83 LEU A CD1 240 C CD2 . LEU A 90 ? 0.2521 0.2243 0.3020 0.0063 0.0205 -0.0466 83 LEU A CD2 241 N N . ALA A 91 ? 0.2308 0.2082 0.2736 0.0090 0.0220 -0.0264 84 ALA A N 242 C CA . ALA A 91 ? 0.2250 0.2042 0.2674 0.0069 0.0218 -0.0240 84 ALA A CA 243 C C . ALA A 91 ? 0.2414 0.2195 0.2900 0.0036 0.0212 -0.0269 84 ALA A C 244 O O . ALA A 91 ? 0.2484 0.2265 0.2976 0.0022 0.0196 -0.0323 84 ALA A O 245 C CB . ALA A 91 ? 0.2308 0.2155 0.2667 0.0064 0.0201 -0.0246 84 ALA A CB 246 N N . GLY A 92 ? 0.2483 0.2251 0.3016 0.0025 0.0224 -0.0233 85 GLY A N 247 C CA . GLY A 92 ? 0.2602 0.2365 0.3213 -0.0009 0.0215 -0.0256 85 GLY A CA 248 C C . GLY A 92 ? 0.2819 0.2525 0.3515 -0.0014 0.0227 -0.0268 85 GLY A C 249 O O . GLY A 92 ? 0.2973 0.2669 0.3750 -0.0043 0.0216 -0.0293 85 GLY A O 250 N N . THR A 93 ? 0.2644 0.2310 0.3330 0.0014 0.0245 -0.0254 86 THR A N 251 C CA . THR A 93 ? 0.2756 0.2359 0.3526 0.0011 0.0258 -0.0261 86 THR A CA 252 C C . THR A 93 ? 0.2823 0.2380 0.3643 0.0021 0.0297 -0.0191 86 THR A C 253 O O . THR A 93 ? 0.2787 0.2353 0.3553 0.0043 0.0317 -0.0137 86 THR A O 254 C CB . THR A 93 ? 0.2779 0.2354 0.3524 0.0037 0.0255 -0.0291 86 THR A CB 255 O OG1 . THR A 93 ? 0.2860 0.2431 0.3547 0.0076 0.0271 -0.0244 86 THR A OG1 256 C CG2 . THR A 93 ? 0.2793 0.2409 0.3487 0.0031 0.0226 -0.0358 86 THR A CG2 257 N N . GLU A 94 ? 0.2966 0.2467 0.3885 0.0007 0.0311 -0.0193 87 GLU A N 258 C CA . GLU A 94 ? 0.3132 0.2581 0.4102 0.0016 0.0356 -0.0123 87 GLU A CA 259 C C . GLU A 94 ? 0.3185 0.2600 0.4075 0.0066 0.0378 -0.0070 87 GLU A C 260 O O . GLU A 94 ? 0.3229 0.2628 0.4092 0.0085 0.0413 -0.0002 87 GLU A O 261 C CB . GLU A 94 ? 0.3401 0.2789 0.4501 -0.0009 0.0365 -0.0138 87 GLU A CB 262 C CG . GLU A 94 ? 0.3797 0.3123 0.4956 0.0000 0.0420 -0.0060 87 GLU A CG 263 C CD . GLU A 94 ? 0.4096 0.3451 0.5297 -0.0020 0.0450 -0.0011 87 GLU A CD 264 O OE1 . GLU A 94 ? 0.4431 0.3739 0.5654 -0.0005 0.0504 0.0063 87 GLU A OE1 265 O OE2 . GLU A 94 ? 0.4054 0.3476 0.5267 -0.0047 0.0423 -0.0045 87 GLU A OE2 266 N N . GLN A 95 ? 0.3149 0.2553 0.3997 0.0090 0.0358 -0.0104 88 GLN A N 267 C CA A GLN A 95 ? 0.3241 0.2616 0.4021 0.0140 0.0368 -0.0063 88 GLN A CA 268 C CA C GLN A 95 ? 0.3253 0.2628 0.4031 0.0140 0.0367 -0.0063 88 GLN A CA 269 C C . GLN A 95 ? 0.3027 0.2447 0.3704 0.0163 0.0366 -0.0027 88 GLN A C 270 O O . GLN A 95 ? 0.3082 0.2469 0.3707 0.0202 0.0385 0.0032 88 GLN A O 271 C CB A GLN A 95 ? 0.3295 0.2665 0.4064 0.0158 0.0342 -0.0115 88 GLN A CB 272 C CB C GLN A 95 ? 0.3307 0.2683 0.4070 0.0158 0.0340 -0.0117 88 GLN A CB 273 C CG A GLN A 95 ? 0.3527 0.2850 0.4393 0.0137 0.0340 -0.0161 88 GLN A CG 274 C CG C GLN A 95 ? 0.3640 0.2949 0.4490 0.0154 0.0346 -0.0141 88 GLN A CG 275 C CD A GLN A 95 ? 0.3469 0.2839 0.4352 0.0101 0.0310 -0.0241 88 GLN A CD 276 C CD C GLN A 95 ? 0.3746 0.3077 0.4607 0.0147 0.0317 -0.0224 88 GLN A CD 277 O OE1 A GLN A 95 ? 0.2975 0.2379 0.3874 0.0066 0.0303 -0.0251 88 GLN A OE1 278 O OE1 C GLN A 95 ? 0.3465 0.2840 0.4264 0.0168 0.0300 -0.0249 88 GLN A OE1 279 N NE2 A GLN A 95 ? 0.3956 0.3322 0.4838 0.0111 0.0293 -0.0300 88 GLN A NE2 280 N NE2 C GLN A 95 ? 0.4090 0.3390 0.5034 0.0117 0.0313 -0.0268 88 GLN A NE2 281 N N . ASN A 96 ? 0.2916 0.2408 0.3561 0.0141 0.0341 -0.0062 89 ASN A N 282 C CA . ASN A 96 ? 0.2852 0.2385 0.3406 0.0162 0.0336 -0.0033 89 ASN A CA 283 C C . ASN A 96 ? 0.3022 0.2551 0.3577 0.0157 0.0368 0.0023 89 ASN A C 284 O O . ASN A 96 ? 0.3148 0.2681 0.3623 0.0189 0.0376 0.0065 89 ASN A O 285 C CB . ASN A 96 ? 0.2782 0.2388 0.3299 0.0144 0.0302 -0.0085 89 ASN A CB 286 C CG . ASN A 96 ? 0.3007 0.2647 0.3431 0.0172 0.0290 -0.0064 89 ASN A CG 287 O OD1 . ASN A 96 ? 0.2904 0.2514 0.3285 0.0214 0.0292 -0.0032 89 ASN A OD1 288 N ND2 . ASN A 96 ? 0.2886 0.2584 0.3279 0.0153 0.0272 -0.0085 89 ASN A ND2 289 N N . PHE A 97 ? 0.2914 0.2438 0.3561 0.0119 0.0385 0.0020 90 PHE A N 290 C CA . PHE A 97 ? 0.2891 0.2405 0.3565 0.0115 0.0426 0.0077 90 PHE A CA 291 C C . PHE A 97 ? 0.2974 0.2411 0.3633 0.0152 0.0470 0.0144 90 PHE A C 292 O O . PHE A 97 ? 0.2872 0.2297 0.3470 0.0180 0.0501 0.0202 90 PHE A O 293 C CB A PHE A 97 ? 0.2954 0.2480 0.3755 0.0063 0.0430 0.0052 90 PHE A CB 294 C CB B PHE A 97 ? 0.2843 0.2368 0.3644 0.0065 0.0433 0.0057 90 PHE A CB 295 C CG A PHE A 97 ? 0.3097 0.2619 0.3957 0.0053 0.0477 0.0107 90 PHE A CG 296 C CG B PHE A 97 ? 0.2727 0.2230 0.3585 0.0061 0.0488 0.0121 90 PHE A CG 297 C CD1 A PHE A 97 ? 0.3138 0.2685 0.3923 0.0076 0.0498 0.0152 90 PHE A CD1 298 C CD1 B PHE A 97 ? 0.2556 0.2100 0.3373 0.0067 0.0504 0.0153 90 PHE A CD1 299 C CD2 A PHE A 97 ? 0.3653 0.3148 0.4654 0.0018 0.0500 0.0110 90 PHE A CD2 300 C CD2 B PHE A 97 ? 0.2577 0.2015 0.3533 0.0052 0.0527 0.0152 90 PHE A CD2 301 C CE1 A PHE A 97 ? 0.3382 0.2929 0.4227 0.0068 0.0548 0.0202 90 PHE A CE1 302 C CE1 B PHE A 97 ? 0.2624 0.2151 0.3496 0.0066 0.0562 0.0213 90 PHE A CE1 303 C CE2 A PHE A 97 ? 0.3783 0.3279 0.4856 0.0006 0.0549 0.0161 90 PHE A CE2 304 C CE2 B PHE A 97 ? 0.2626 0.2045 0.3642 0.0048 0.0586 0.0216 90 PHE A CE2 305 C CZ A PHE A 97 ? 0.3798 0.3322 0.4791 0.0032 0.0576 0.0208 90 PHE A CZ 306 C CZ B PHE A 97 ? 0.2664 0.2129 0.3637 0.0056 0.0606 0.0246 90 PHE A CZ 307 N N A GLN A 98 ? 0.2975 0.2354 0.3680 0.0157 0.0473 0.0138 91 GLN A N 308 N N B GLN A 98 ? 0.2973 0.2353 0.3681 0.0155 0.0472 0.0136 91 GLN A N 309 C CA A GLN A 98 ? 0.3187 0.2485 0.3870 0.0197 0.0513 0.0206 91 GLN A CA 310 C CA B GLN A 98 ? 0.3171 0.2468 0.3859 0.0195 0.0509 0.0199 91 GLN A CA 311 C C A GLN A 98 ? 0.3137 0.2429 0.3680 0.0255 0.0500 0.0234 91 GLN A C 312 C C B GLN A 98 ? 0.3126 0.2418 0.3673 0.0253 0.0499 0.0232 91 GLN A C 313 O O A GLN A 98 ? 0.3248 0.2493 0.3728 0.0293 0.0536 0.0302 91 GLN A O 314 O O B GLN A 98 ? 0.3235 0.2483 0.3725 0.0288 0.0537 0.0300 91 GLN A O 315 C CB A GLN A 98 ? 0.3303 0.2535 0.4069 0.0191 0.0517 0.0193 91 GLN A CB 316 C CB B GLN A 98 ? 0.3202 0.2444 0.3959 0.0193 0.0500 0.0172 91 GLN A CB 317 C CG A GLN A 98 ? 0.3595 0.2817 0.4509 0.0137 0.0534 0.0176 91 GLN A CG 318 C CG B GLN A 98 ? 0.3618 0.2837 0.4520 0.0143 0.0519 0.0157 91 GLN A CG 319 C CD A GLN A 98 ? 0.4165 0.3360 0.5134 0.0127 0.0596 0.0247 91 GLN A CD 320 C CD B GLN A 98 ? 0.3892 0.3060 0.4868 0.0136 0.0503 0.0116 91 GLN A CD 321 O OE1 A GLN A 98 ? 0.4467 0.3696 0.5552 0.0076 0.0600 0.0224 91 GLN A OE1 322 O OE1 B GLN A 98 ? 0.4422 0.3583 0.5345 0.0166 0.0475 0.0088 91 GLN A OE1 323 N NE2 A GLN A 98 ? 0.4457 0.3598 0.5365 0.0167 0.0640 0.0322 91 GLN A NE2 324 N NE2 B GLN A 98 ? 0.4356 0.3488 0.5464 0.0098 0.0522 0.0110 91 GLN A NE2 325 N N . LEU A 99 ? 0.3015 0.2353 0.3508 0.0264 0.0449 0.0182 92 LEU A N 326 C CA . LEU A 99 ? 0.3017 0.2356 0.3391 0.0316 0.0429 0.0202 92 LEU A CA 327 C C . LEU A 99 ? 0.2957 0.2327 0.3255 0.0326 0.0441 0.0234 92 LEU A C 328 O O . LEU A 99 ? 0.3039 0.2374 0.3240 0.0376 0.0451 0.0283 92 LEU A O 329 C CB . LEU A 99 ? 0.2820 0.2207 0.3176 0.0319 0.0375 0.0138 92 LEU A CB 330 C CG . LEU A 99 ? 0.2845 0.2233 0.3099 0.0374 0.0346 0.0152 92 LEU A CG 331 C CD1 . LEU A 99 ? 0.3114 0.2416 0.3333 0.0428 0.0358 0.0204 92 LEU A CD1 332 C CD2 . LEU A 99 ? 0.2685 0.2130 0.2946 0.0369 0.0299 0.0088 92 LEU A CD2 333 N N . ALA A 100 ? 0.2831 0.2264 0.3168 0.0282 0.0439 0.0206 93 ALA A N 334 C CA . ALA A 100 ? 0.2848 0.2309 0.3126 0.0290 0.0455 0.0236 93 ALA A CA 335 C C . ALA A 100 ? 0.2978 0.2378 0.3241 0.0315 0.0516 0.0313 93 ALA A C 336 O O . ALA A 100 ? 0.3011 0.2397 0.3170 0.0357 0.0529 0.0352 93 ALA A O 337 C CB . ALA A 100 ? 0.2743 0.2274 0.3082 0.0239 0.0445 0.0198 93 ALA A CB 338 N N A LYS A 101 ? 0.2975 0.2337 0.3342 0.0288 0.0556 0.0332 94 LYS A N 339 N N B LYS A 101 ? 0.2983 0.2346 0.3352 0.0288 0.0556 0.0332 94 LYS A N 340 C CA A LYS A 101 ? 0.3141 0.2441 0.3512 0.0307 0.0625 0.0409 94 LYS A CA 341 C CA B LYS A 101 ? 0.3159 0.2458 0.3530 0.0307 0.0626 0.0410 94 LYS A CA 342 C C A LYS A 101 ? 0.3294 0.2515 0.3551 0.0373 0.0636 0.0461 94 LYS A C 343 C C B LYS A 101 ? 0.3299 0.2522 0.3555 0.0373 0.0635 0.0461 94 LYS A C 344 O O A LYS A 101 ? 0.3361 0.2542 0.3537 0.0412 0.0682 0.0526 94 LYS A O 345 O O B LYS A 101 ? 0.3360 0.2543 0.3531 0.0414 0.0679 0.0525 94 LYS A O 346 C CB A LYS A 101 ? 0.3167 0.2444 0.3695 0.0260 0.0659 0.0412 94 LYS A CB 347 C CB B LYS A 101 ? 0.3193 0.2464 0.3720 0.0262 0.0662 0.0416 94 LYS A CB 348 C CG A LYS A 101 ? 0.3294 0.2644 0.3924 0.0204 0.0657 0.0377 94 LYS A CG 349 C CG B LYS A 101 ? 0.3411 0.2749 0.4053 0.0204 0.0666 0.0386 94 LYS A CG 350 C CD A LYS A 101 ? 0.3572 0.2896 0.4366 0.0159 0.0697 0.0389 94 LYS A CD 351 C CD B LYS A 101 ? 0.3577 0.2953 0.4168 0.0216 0.0697 0.0420 94 LYS A CD 352 C CE A LYS A 101 ? 0.3728 0.3051 0.4606 0.0126 0.0650 0.0322 94 LYS A CE 353 C CE B LYS A 101 ? 0.3859 0.3198 0.4514 0.0215 0.0782 0.0494 94 LYS A CE 354 N NZ A LYS A 101 ? 0.4012 0.3309 0.5060 0.0080 0.0678 0.0323 94 LYS A NZ 355 N NZ B LYS A 101 ? 0.3355 0.2750 0.3983 0.0219 0.0807 0.0511 94 LYS A NZ 356 N N . GLN A 102 ? 0.3346 0.2545 0.3593 0.0388 0.0593 0.0432 95 GLN A N 357 C CA . GLN A 102 ? 0.3464 0.2592 0.3603 0.0455 0.0589 0.0473 95 GLN A CA 358 C C . GLN A 102 ? 0.3473 0.2623 0.3463 0.0503 0.0560 0.0479 95 GLN A C 359 O O . GLN A 102 ? 0.3539 0.2630 0.3420 0.0558 0.0586 0.0539 95 GLN A O 360 C CB . GLN A 102 ? 0.3480 0.2593 0.3651 0.0461 0.0542 0.0430 95 GLN A CB 361 C CG . GLN A 102 ? 0.3601 0.2643 0.3660 0.0534 0.0528 0.0471 95 GLN A CG 362 C CD . GLN A 102 ? 0.3549 0.2604 0.3628 0.0545 0.0468 0.0417 95 GLN A CD 363 O OE1 . GLN A 102 ? 0.3630 0.2692 0.3822 0.0507 0.0463 0.0376 95 GLN A OE1 364 N NE2 . GLN A 102 ? 0.3644 0.2701 0.3620 0.0599 0.0421 0.0413 95 GLN A NE2 365 N N . ILE A 103 ? 0.3294 0.2526 0.3279 0.0483 0.0508 0.0416 96 ILE A N 366 C CA . ILE A 103 ? 0.3326 0.2582 0.3185 0.0524 0.0473 0.0411 96 ILE A CA 367 C C . ILE A 103 ? 0.3391 0.2638 0.3188 0.0538 0.0523 0.0461 96 ILE A C 368 O O . ILE A 103 ? 0.3389 0.2599 0.3054 0.0597 0.0524 0.0496 96 ILE A O 369 C CB . ILE A 103 ? 0.3236 0.2582 0.3123 0.0491 0.0414 0.0336 96 ILE A CB 370 C CG1 A ILE A 103 ? 0.3512 0.2872 0.3458 0.0480 0.0370 0.0285 96 ILE A CG1 371 C CG1 B ILE A 103 ? 0.3284 0.2629 0.3200 0.0498 0.0367 0.0295 96 ILE A CG1 372 C CG2 . ILE A 103 ? 0.3341 0.2715 0.3113 0.0526 0.0382 0.0331 96 ILE A CG2 373 C CD1 A ILE A 103 ? 0.3359 0.2680 0.3236 0.0538 0.0333 0.0292 96 ILE A CD1 374 C CD1 B ILE A 103 ? 0.2791 0.2216 0.2764 0.0458 0.0324 0.0224 96 ILE A CD1 375 N N . GLN A 104 ? 0.3233 0.2515 0.3127 0.0486 0.0564 0.0462 97 GLN A N 376 C CA . GLN A 104 ? 0.3445 0.2722 0.3300 0.0497 0.0621 0.0510 97 GLN A CA 377 C C . GLN A 104 ? 0.3647 0.2829 0.3423 0.0552 0.0680 0.0592 97 GLN A C 378 O O . GLN A 104 ? 0.3780 0.2935 0.3426 0.0604 0.0699 0.0629 97 GLN A O 379 C CB . GLN A 104 ? 0.3406 0.2729 0.3408 0.0432 0.0657 0.0501 97 GLN A CB 380 C CG . GLN A 104 ? 0.3585 0.2907 0.3578 0.0440 0.0726 0.0553 97 GLN A CG 381 C CD . GLN A 104 ? 0.3674 0.3042 0.3834 0.0375 0.0760 0.0545 97 GLN A CD 382 O OE1 . GLN A 104 ? 0.3707 0.3076 0.3992 0.0330 0.0753 0.0522 97 GLN A OE1 383 N NE2 . GLN A 104 ? 0.3541 0.2948 0.3707 0.0372 0.0794 0.0560 97 GLN A NE2 384 N N . SER A 105 ? 0.3753 0.2877 0.3601 0.0543 0.0709 0.0619 98 SER A N 385 C CA . SER A 105 ? 0.3904 0.2928 0.3682 0.0593 0.0770 0.0703 98 SER A CA 386 C C . SER A 105 ? 0.3961 0.2934 0.3558 0.0673 0.0731 0.0720 98 SER A C 387 O O . SER A 105 ? 0.4017 0.2929 0.3483 0.0731 0.0774 0.0783 98 SER A O 388 C CB . SER A 105 ? 0.3934 0.2904 0.3830 0.0567 0.0795 0.0721 98 SER A CB 389 O OG A SER A 105 ? 0.3981 0.2850 0.3818 0.0612 0.0862 0.0808 98 SER A OG 390 O OG B SER A 105 ? 0.4230 0.3225 0.4278 0.0506 0.0852 0.0730 98 SER A OG 391 N N . GLN A 106 ? 0.3740 0.2735 0.3330 0.0679 0.0650 0.0662 99 GLN A N 392 C CA . GLN A 106 ? 0.3907 0.2856 0.3342 0.0754 0.0601 0.0671 99 GLN A CA 393 C C . GLN A 106 ? 0.3779 0.2758 0.3083 0.0790 0.0578 0.0660 99 GLN A C 394 O O . GLN A 106 ? 0.4017 0.2933 0.3167 0.0861 0.0580 0.0701 99 GLN A O 395 C CB . GLN A 106 ? 0.3793 0.2766 0.3273 0.0751 0.0522 0.0610 99 GLN A CB 396 C CG . GLN A 106 ? 0.4050 0.2971 0.3632 0.0733 0.0546 0.0628 99 GLN A CG 397 C CD . GLN A 106 ? 0.4303 0.3241 0.3925 0.0738 0.0473 0.0571 99 GLN A CD 398 O OE1 . GLN A 106 ? 0.4303 0.3323 0.4005 0.0693 0.0433 0.0501 99 GLN A OE1 399 N NE2 . GLN A 106 ? 0.5170 0.4029 0.4736 0.0795 0.0460 0.0605 99 GLN A NE2 400 N N . TRP A 107 ? 0.3630 0.2700 0.2989 0.0744 0.0554 0.0604 100 TRP A N 401 C CA . TRP A 107 ? 0.3609 0.2704 0.2854 0.0776 0.0534 0.0593 100 TRP A CA 402 C C . TRP A 107 ? 0.3853 0.2895 0.3003 0.0813 0.0613 0.0664 100 TRP A C 403 O O . TRP A 107 ? 0.3970 0.2983 0.2964 0.0876 0.0599 0.0676 100 TRP A O 404 C CB . TRP A 107 ? 0.3391 0.2589 0.2724 0.0715 0.0503 0.0527 100 TRP A CB 405 C CG . TRP A 107 ? 0.3393 0.2640 0.2764 0.0699 0.0420 0.0458 100 TRP A CG 406 C CD1 . TRP A 107 ? 0.3575 0.2793 0.2937 0.0726 0.0373 0.0446 100 TRP A CD1 407 C CD2 . TRP A 107 ? 0.3237 0.2572 0.2675 0.0651 0.0378 0.0393 100 TRP A CD2 408 N NE1 . TRP A 107 ? 0.3343 0.2629 0.2764 0.0697 0.0309 0.0377 100 TRP A NE1 409 C CE2 . TRP A 107 ? 0.3220 0.2577 0.2686 0.0650 0.0312 0.0345 100 TRP A CE2 410 C CE3 . TRP A 107 ? 0.3121 0.2518 0.2599 0.0610 0.0391 0.0373 100 TRP A CE3 411 C CZ2 . TRP A 107 ? 0.3238 0.2672 0.2766 0.0609 0.0265 0.0281 100 TRP A CZ2 412 C CZ3 . TRP A 107 ? 0.3003 0.2474 0.2536 0.0571 0.0339 0.0311 100 TRP A CZ3 413 C CH2 . TRP A 107 ? 0.3096 0.2584 0.2651 0.0570 0.0279 0.0267 100 TRP A CH2 414 N N . LYS A 108 ? 0.4000 0.3031 0.3248 0.0776 0.0696 0.0709 101 LYS A N 415 C CA . LYS A 108 ? 0.4399 0.3372 0.3571 0.0813 0.0788 0.0788 101 LYS A CA 416 C C . LYS A 108 ? 0.4520 0.3381 0.3534 0.0895 0.0802 0.0850 101 LYS A C 417 O O . LYS A 108 ? 0.4754 0.3569 0.3602 0.0961 0.0824 0.0887 101 LYS A O 418 C CB . LYS A 108 ? 0.4469 0.3449 0.3803 0.0754 0.0873 0.0824 101 LYS A CB 419 C CG . LYS A 108 ? 0.4907 0.3986 0.4370 0.0687 0.0874 0.0778 101 LYS A CG 420 C CD . LYS A 108 ? 0.5597 0.4688 0.5246 0.0625 0.0942 0.0803 101 LYS A CD 421 C CE . LYS A 108 ? 0.5817 0.5005 0.5572 0.0571 0.0945 0.0763 101 LYS A CE 422 N NZ . LYS A 108 ? 0.6373 0.5584 0.6328 0.0505 0.0992 0.0771 101 LYS A NZ 423 N N A GLU A 109 ? 0.4589 0.3404 0.3649 0.0893 0.0787 0.0861 102 GLU A N 424 N N B GLU A 109 ? 0.4571 0.3385 0.3626 0.0895 0.0785 0.0860 102 GLU A N 425 C CA A GLU A 109 ? 0.4749 0.3455 0.3670 0.0970 0.0790 0.0918 102 GLU A CA 426 C CA B GLU A 109 ? 0.4723 0.3426 0.3633 0.0974 0.0795 0.0923 102 GLU A CA 427 C C A GLU A 109 ? 0.4748 0.3443 0.3484 0.1043 0.0710 0.0889 102 GLU A C 428 C C B GLU A 109 ? 0.4731 0.3421 0.3467 0.1045 0.0705 0.0889 102 GLU A C 429 O O A GLU A 109 ? 0.4887 0.3500 0.3442 0.1122 0.0731 0.0943 102 GLU A O 430 O O B GLU A 109 ? 0.4880 0.3480 0.3441 0.1127 0.0713 0.0941 102 GLU A O 431 C CB A GLU A 109 ? 0.4792 0.3469 0.3810 0.0951 0.0760 0.0910 102 GLU A CB 432 C CB B GLU A 109 ? 0.4773 0.3431 0.3784 0.0954 0.0794 0.0937 102 GLU A CB 433 C CG A GLU A 109 ? 0.5124 0.3793 0.4325 0.0885 0.0830 0.0937 102 GLU A CG 434 C CG B GLU A 109 ? 0.5278 0.3819 0.4143 0.1037 0.0792 0.0998 102 GLU A CG 435 C CD A GLU A 109 ? 0.5450 0.4116 0.4768 0.0856 0.0782 0.0900 102 GLU A CD 436 C CD B GLU A 109 ? 0.6116 0.4564 0.4877 0.1082 0.0898 0.1100 102 GLU A CD 437 O OE1 A GLU A 109 ? 0.5252 0.3953 0.4747 0.0784 0.0804 0.0879 102 GLU A OE1 438 O OE1 B GLU A 109 ? 0.6427 0.4780 0.5006 0.1168 0.0895 0.1152 102 GLU A OE1 439 O OE2 A GLU A 109 ? 0.5490 0.4120 0.4726 0.0907 0.0718 0.0889 102 GLU A OE2 440 O OE2 B GLU A 109 ? 0.6381 0.4853 0.5245 0.1032 0.0985 0.1129 102 GLU A OE2 441 N N . PHE A 110 ? 0.4402 0.3180 0.3187 0.1015 0.0620 0.0803 103 PHE A N 442 C CA . PHE A 110 ? 0.4455 0.3235 0.3104 0.1074 0.0527 0.0761 103 PHE A CA 443 C C . PHE A 110 ? 0.4542 0.3312 0.3039 0.1120 0.0545 0.0773 103 PHE A C 444 O O . PHE A 110 ? 0.4787 0.3527 0.3132 0.1188 0.0481 0.0755 103 PHE A O 445 C CB . PHE A 110 ? 0.4273 0.3153 0.3034 0.1024 0.0438 0.0666 103 PHE A CB 446 C CG . PHE A 110 ? 0.4323 0.3210 0.3200 0.0998 0.0398 0.0640 103 PHE A CG 447 C CD1 . PHE A 110 ? 0.4597 0.3399 0.3460 0.1031 0.0420 0.0693 103 PHE A CD1 448 C CD2 . PHE A 110 ? 0.4276 0.3256 0.3278 0.0942 0.0339 0.0562 103 PHE A CD2 449 C CE1 . PHE A 110 ? 0.4871 0.3683 0.3850 0.1007 0.0383 0.0663 103 PHE A CE1 450 C CE2 . PHE A 110 ? 0.4316 0.3309 0.3429 0.0919 0.0306 0.0532 103 PHE A CE2 451 C CZ . PHE A 110 ? 0.4518 0.3427 0.3620 0.0952 0.0325 0.0580 103 PHE A CZ 452 N N . GLY A 111 ? 0.4458 0.3256 0.3002 0.1084 0.0625 0.0796 104 GLY A N 453 C CA . GLY A 111 ? 0.4608 0.3387 0.3010 0.1132 0.0663 0.0820 104 GLY A CA 454 C C . GLY A 111 ? 0.4513 0.3386 0.2978 0.1086 0.0656 0.0766 104 GLY A C 455 O O . GLY A 111 ? 0.4631 0.3491 0.2974 0.1129 0.0675 0.0774 104 GLY A O 456 N N . LEU A 112 ? 0.4309 0.3272 0.2955 0.1003 0.0628 0.0713 105 LEU A N 457 C CA . LEU A 112 ? 0.4110 0.3158 0.2811 0.0962 0.0619 0.0665 105 LEU A CA 458 C C . LEU A 112 ? 0.4300 0.3350 0.3024 0.0952 0.0723 0.0715 105 LEU A C 459 O O . LEU A 112 ? 0.4500 0.3511 0.3274 0.0943 0.0804 0.0778 105 LEU A O 460 C CB . LEU A 112 ? 0.3960 0.3100 0.2843 0.0878 0.0571 0.0601 105 LEU A CB 461 C CG . LEU A 112 ? 0.3771 0.2928 0.2655 0.0881 0.0470 0.0542 105 LEU A CG 462 C CD1 . LEU A 112 ? 0.3793 0.3045 0.2837 0.0801 0.0432 0.0478 105 LEU A CD1 463 C CD2 . LEU A 112 ? 0.3766 0.2906 0.2495 0.0946 0.0401 0.0513 105 LEU A CD2 464 N N . ASP A 113 ? 0.4252 0.3345 0.2945 0.0956 0.0722 0.0689 106 ASP A N 465 C CA . ASP A 113 ? 0.4401 0.3500 0.3113 0.0953 0.0820 0.0734 106 ASP A CA 466 C C . ASP A 113 ? 0.4385 0.3548 0.3313 0.0867 0.0869 0.0738 106 ASP A C 467 O O . ASP A 113 ? 0.4556 0.3701 0.3534 0.0862 0.0965 0.0799 106 ASP A O 468 C CB . ASP A 113 ? 0.4382 0.3513 0.3011 0.0979 0.0800 0.0698 106 ASP A CB 469 C CG . ASP A 113 ? 0.4692 0.3748 0.3096 0.1072 0.0766 0.0701 106 ASP A CG 470 O OD1 . ASP A 113 ? 0.4775 0.3746 0.3055 0.1133 0.0832 0.0769 106 ASP A OD1 471 O OD2 . ASP A 113 ? 0.4403 0.3480 0.2754 0.1085 0.0672 0.0637 106 ASP A OD2 472 N N . SER A 114 ? 0.4076 0.3315 0.3133 0.0803 0.0801 0.0674 107 SER A N 473 C CA . SER A 114 ? 0.3988 0.3287 0.3247 0.0723 0.0830 0.0667 107 SER A CA 474 C C . SER A 114 ? 0.3739 0.3073 0.3083 0.0676 0.0749 0.0610 107 SER A C 475 O O . SER A 114 ? 0.3572 0.2917 0.2847 0.0692 0.0670 0.0562 107 SER A O 476 C CB . SER A 114 ? 0.3972 0.3347 0.3297 0.0694 0.0845 0.0643 107 SER A CB 477 O OG A SER A 114 ? 0.3715 0.3139 0.3011 0.0687 0.0759 0.0575 107 SER A OG 478 O OG B SER A 114 ? 0.4315 0.3765 0.3817 0.0616 0.0821 0.0603 107 SER A OG 479 N N . VAL A 115 ? 0.3594 0.2940 0.3088 0.0621 0.0771 0.0615 108 VAL A N 480 C CA . VAL A 115 ? 0.3492 0.2874 0.3073 0.0574 0.0702 0.0558 108 VAL A CA 481 C C . VAL A 115 ? 0.3467 0.2900 0.3232 0.0501 0.0729 0.0546 108 VAL A C 482 O O . VAL A 115 ? 0.3567 0.2967 0.3414 0.0486 0.0793 0.0592 108 VAL A O 483 C CB . VAL A 115 ? 0.3511 0.2826 0.3060 0.0597 0.0685 0.0573 108 VAL A CB 484 C CG1 . VAL A 115 ? 0.3438 0.2801 0.3064 0.0555 0.0609 0.0504 108 VAL A CG1 485 C CG2 . VAL A 115 ? 0.3515 0.2763 0.2875 0.0680 0.0669 0.0599 108 VAL A CG2 486 N N A GLU A 116 ? 0.3367 0.2877 0.3198 0.0457 0.0680 0.0487 109 GLU A N 487 N N B GLU A 116 ? 0.3369 0.2879 0.3200 0.0457 0.0679 0.0486 109 GLU A N 488 C CA A GLU A 116 ? 0.3437 0.2998 0.3434 0.0391 0.0693 0.0468 109 GLU A CA 489 C CA B GLU A 116 ? 0.3371 0.2938 0.3366 0.0391 0.0692 0.0466 109 GLU A CA 490 C C A GLU A 116 ? 0.3280 0.2879 0.3342 0.0347 0.0625 0.0404 109 GLU A C 491 C C B GLU A 116 ? 0.3231 0.2841 0.3297 0.0344 0.0623 0.0400 109 GLU A C 492 O O A GLU A 116 ? 0.3329 0.2931 0.3315 0.0363 0.0567 0.0369 109 GLU A O 493 O O B GLU A 116 ? 0.3210 0.2837 0.3203 0.0355 0.0562 0.0360 109 GLU A O 494 C CB A GLU A 116 ? 0.3577 0.3199 0.3604 0.0379 0.0707 0.0461 109 GLU A CB 495 C CB B GLU A 116 ? 0.3398 0.3023 0.3404 0.0385 0.0703 0.0459 109 GLU A CB 496 C CG A GLU A 116 ? 0.4259 0.3850 0.4237 0.0421 0.0788 0.0525 109 GLU A CG 497 C CG B GLU A 116 ? 0.3811 0.3405 0.3767 0.0428 0.0782 0.0522 109 GLU A CG 498 C CD A GLU A 116 ? 0.4907 0.4459 0.4982 0.0409 0.0870 0.0584 109 GLU A CD 499 C CD B GLU A 116 ? 0.4020 0.3671 0.3984 0.0426 0.0789 0.0509 109 GLU A CD 500 O OE1 A GLU A 116 ? 0.5156 0.4739 0.5392 0.0351 0.0872 0.0567 109 GLU A OE1 501 O OE1 B GLU A 116 ? 0.4141 0.3846 0.4107 0.0407 0.0723 0.0454 109 GLU A OE1 502 O OE2 A GLU A 116 ? 0.5462 0.4949 0.5450 0.0459 0.0935 0.0648 109 GLU A OE2 503 O OE2 B GLU A 116 ? 0.4364 0.4006 0.4334 0.0448 0.0863 0.0558 109 GLU A OE2 504 N N . LEU A 117 ? 0.3186 0.2810 0.3394 0.0292 0.0633 0.0387 110 LEU A N 505 C CA . LEU A 117 ? 0.3129 0.2798 0.3399 0.0248 0.0570 0.0321 110 LEU A CA 506 C C . LEU A 117 ? 0.3073 0.2816 0.3389 0.0217 0.0549 0.0288 110 LEU A C 507 O O . LEU A 117 ? 0.3270 0.3033 0.3657 0.0204 0.0590 0.0312 110 LEU A O 508 C CB . LEU A 117 ? 0.3201 0.2852 0.3601 0.0208 0.0583 0.0314 110 LEU A CB 509 C CG . LEU A 117 ? 0.3437 0.3010 0.3816 0.0232 0.0604 0.0345 110 LEU A CG 510 C CD1 . LEU A 117 ? 0.3756 0.3322 0.4277 0.0184 0.0601 0.0318 110 LEU A CD1 511 C CD2 . LEU A 117 ? 0.3628 0.3185 0.3892 0.0268 0.0556 0.0324 110 LEU A CD2 512 N N . ALA A 118 ? 0.2811 0.2593 0.3089 0.0206 0.0487 0.0236 111 ALA A N 513 C CA . ALA A 118 ? 0.2685 0.2532 0.2999 0.0176 0.0456 0.0200 111 ALA A CA 514 C C . ALA A 118 ? 0.2745 0.2614 0.3127 0.0133 0.0413 0.0148 111 ALA A C 515 O O . ALA A 118 ? 0.2857 0.2716 0.3187 0.0138 0.0379 0.0120 111 ALA A O 516 C CB . ALA A 118 ? 0.2771 0.2638 0.2971 0.0204 0.0421 0.0186 111 ALA A CB 517 N N . HIS A 119 ? 0.2586 0.2482 0.3086 0.0093 0.0416 0.0133 112 HIS A N 518 C CA . HIS A 119 ? 0.2476 0.2385 0.3036 0.0055 0.0374 0.0079 112 HIS A CA 519 C C . HIS A 119 ? 0.2339 0.2306 0.2910 0.0030 0.0328 0.0038 112 HIS A C 520 O O . HIS A 119 ? 0.2404 0.2404 0.2988 0.0032 0.0335 0.0052 112 HIS A O 521 C CB . HIS A 119 ? 0.2642 0.2526 0.3330 0.0027 0.0400 0.0084 112 HIS A CB 522 C CG . HIS A 119 ? 0.2929 0.2843 0.3732 0.0005 0.0423 0.0099 112 HIS A CG 523 N ND1 . HIS A 119 ? 0.3447 0.3342 0.4288 0.0021 0.0488 0.0159 112 HIS A ND1 524 C CD2 . HIS A 119 ? 0.3099 0.3063 0.3991 -0.0030 0.0389 0.0062 112 HIS A CD2 525 C CE1 . HIS A 119 ? 0.3382 0.3318 0.4345 -0.0006 0.0497 0.0158 112 HIS A CE1 526 N NE2 . HIS A 119 ? 0.3275 0.3254 0.4271 -0.0037 0.0433 0.0098 112 HIS A NE2 527 N N . TYR A 120 ? 0.2250 0.2227 0.2810 0.0010 0.0283 -0.0013 113 TYR A N 528 C CA . TYR A 120 ? 0.2262 0.2285 0.2817 -0.0012 0.0234 -0.0055 113 TYR A CA 529 C C . TYR A 120 ? 0.2185 0.2201 0.2786 -0.0041 0.0204 -0.0105 113 TYR A C 530 O O . TYR A 120 ? 0.2390 0.2368 0.2997 -0.0038 0.0215 -0.0112 113 TYR A O 531 C CB . TYR A 120 ? 0.2162 0.2199 0.2598 0.0007 0.0209 -0.0064 113 TYR A CB 532 C CG . TYR A 120 ? 0.2254 0.2288 0.2636 0.0040 0.0236 -0.0020 113 TYR A CG 533 C CD1 . TYR A 120 ? 0.2274 0.2339 0.2669 0.0043 0.0239 -0.0004 113 TYR A CD1 534 C CD2 . TYR A 120 ? 0.2293 0.2289 0.2616 0.0072 0.0259 0.0006 113 TYR A CD2 535 C CE1 . TYR A 120 ? 0.2566 0.2621 0.2905 0.0078 0.0267 0.0035 113 TYR A CE1 536 C CE2 . TYR A 120 ? 0.2439 0.2424 0.2703 0.0107 0.0282 0.0044 113 TYR A CE2 537 C CZ . TYR A 120 ? 0.2666 0.2680 0.2936 0.0110 0.0288 0.0058 113 TYR A CZ 538 O OH . TYR A 120 ? 0.2524 0.2523 0.2729 0.0149 0.0311 0.0092 113 TYR A OH 539 N N . ASP A 121 ? 0.2193 0.2244 0.2824 -0.0064 0.0163 -0.0142 114 ASP A N 540 C CA . ASP A 121 ? 0.2285 0.2328 0.2942 -0.0088 0.0126 -0.0198 114 ASP A CA 541 C C . ASP A 121 ? 0.2210 0.2271 0.2760 -0.0084 0.0088 -0.0230 114 ASP A C 542 O O . ASP A 121 ? 0.2293 0.2389 0.2825 -0.0088 0.0060 -0.0236 114 ASP A O 543 C CB . ASP A 121 ? 0.2368 0.2431 0.3150 -0.0116 0.0105 -0.0218 114 ASP A CB 544 C CG . ASP A 121 ? 0.2819 0.2861 0.3719 -0.0122 0.0151 -0.0182 114 ASP A CG 545 O OD1 . ASP A 121 ? 0.2881 0.2877 0.3785 -0.0117 0.0179 -0.0174 114 ASP A OD1 546 O OD2 . ASP A 121 ? 0.3204 0.3276 0.4191 -0.0130 0.0164 -0.0158 114 ASP A OD2 547 N N . VAL A 122 ? 0.2205 0.2243 0.2690 -0.0075 0.0090 -0.0248 115 VAL A N 548 C CA . VAL A 122 ? 0.2145 0.2196 0.2522 -0.0068 0.0068 -0.0269 115 VAL A CA 549 C C . VAL A 122 ? 0.2236 0.2271 0.2588 -0.0077 0.0047 -0.0322 115 VAL A C 550 O O . VAL A 122 ? 0.2224 0.2230 0.2633 -0.0083 0.0053 -0.0343 115 VAL A O 551 C CB . VAL A 122 ? 0.2163 0.2207 0.2471 -0.0042 0.0095 -0.0237 115 VAL A CB 552 C CG1 . VAL A 122 ? 0.2117 0.2174 0.2428 -0.0027 0.0113 -0.0189 115 VAL A CG1 553 C CG2 . VAL A 122 ? 0.2108 0.2116 0.2435 -0.0031 0.0121 -0.0237 115 VAL A CG2 554 N N . LEU A 123 ? 0.2142 0.2191 0.2406 -0.0075 0.0025 -0.0344 116 LEU A N 555 C CA . LEU A 123 ? 0.2181 0.2212 0.2404 -0.0078 0.0011 -0.0395 116 LEU A CA 556 C C . LEU A 123 ? 0.2279 0.2288 0.2483 -0.0063 0.0045 -0.0395 116 LEU A C 557 O O . LEU A 123 ? 0.2376 0.2398 0.2532 -0.0049 0.0064 -0.0370 116 LEU A O 558 C CB . LEU A 123 ? 0.2099 0.2147 0.2223 -0.0077 -0.0014 -0.0411 116 LEU A CB 559 C CG . LEU A 123 ? 0.2432 0.2458 0.2509 -0.0079 -0.0035 -0.0469 116 LEU A CG 560 C CD1 . LEU A 123 ? 0.2682 0.2700 0.2821 -0.0094 -0.0079 -0.0508 116 LEU A CD1 561 C CD2 . LEU A 123 ? 0.2658 0.2694 0.2613 -0.0070 -0.0042 -0.0473 116 LEU A CD2 562 N N . LEU A 124 ? 0.2361 0.2339 0.2611 -0.0066 0.0049 -0.0426 117 LEU A N 563 C CA . LEU A 124 ? 0.2403 0.2358 0.2640 -0.0050 0.0077 -0.0435 117 LEU A CA 564 C C . LEU A 124 ? 0.2552 0.2491 0.2750 -0.0052 0.0063 -0.0496 117 LEU A C 565 O O . LEU A 124 ? 0.2679 0.2621 0.2851 -0.0063 0.0030 -0.0528 117 LEU A O 566 C CB . LEU A 124 ? 0.2429 0.2353 0.2751 -0.0044 0.0100 -0.0413 117 LEU A CB 567 C CG . LEU A 124 ? 0.2251 0.2184 0.2599 -0.0036 0.0119 -0.0352 117 LEU A CG 568 C CD1 . LEU A 124 ? 0.2300 0.2190 0.2716 -0.0025 0.0146 -0.0330 117 LEU A CD1 569 C CD2 . LEU A 124 ? 0.2245 0.2205 0.2519 -0.0017 0.0128 -0.0324 117 LEU A CD2 570 N N . SER A 125 ? 0.2523 0.2443 0.2713 -0.0036 0.0087 -0.0514 118 SER A N 571 C CA . SER A 125 ? 0.2684 0.2587 0.2823 -0.0032 0.0083 -0.0572 118 SER A CA 572 C C . SER A 125 ? 0.2741 0.2609 0.2931 -0.0019 0.0105 -0.0592 118 SER A C 573 O O . SER A 125 ? 0.2714 0.2584 0.2934 -0.0004 0.0133 -0.0559 118 SER A O 574 C CB . SER A 125 ? 0.2878 0.2809 0.2919 -0.0021 0.0100 -0.0568 118 SER A CB 575 O OG . SER A 125 ? 0.2689 0.2603 0.2678 -0.0009 0.0112 -0.0619 118 SER A OG 576 N N . TYR A 126 ? 0.2852 0.2685 0.3053 -0.0022 0.0088 -0.0649 119 TYR A N 577 C CA . TYR A 126 ? 0.2815 0.2607 0.3070 -0.0009 0.0106 -0.0673 119 TYR A CA 578 C C . TYR A 126 ? 0.2984 0.2751 0.3187 0.0000 0.0098 -0.0745 119 TYR A C 579 O O . TYR A 126 ? 0.3043 0.2806 0.3199 -0.0010 0.0063 -0.0783 119 TYR A O 580 C CB . TYR A 126 ? 0.2748 0.2505 0.3113 -0.0024 0.0091 -0.0668 119 TYR A CB 581 C CG . TYR A 126 ? 0.2822 0.2594 0.3242 -0.0031 0.0103 -0.0598 119 TYR A CG 582 C CD1 . TYR A 126 ? 0.2800 0.2567 0.3239 -0.0011 0.0136 -0.0553 119 TYR A CD1 583 C CD2 . TYR A 126 ? 0.2999 0.2785 0.3454 -0.0054 0.0080 -0.0579 119 TYR A CD2 584 C CE1 . TYR A 126 ? 0.2751 0.2525 0.3227 -0.0011 0.0148 -0.0489 119 TYR A CE1 585 C CE2 . TYR A 126 ? 0.3249 0.3046 0.3752 -0.0057 0.0097 -0.0516 119 TYR A CE2 586 C CZ . TYR A 126 ? 0.3045 0.2832 0.3552 -0.0034 0.0132 -0.0471 119 TYR A CZ 587 O OH . TYR A 126 ? 0.2827 0.2618 0.3367 -0.0032 0.0150 -0.0410 119 TYR A OH 588 N N . PRO A 127 ? 0.3094 0.2839 0.3309 0.0021 0.0127 -0.0767 120 PRO A N 589 C CA . PRO A 127 ? 0.3315 0.3025 0.3487 0.0032 0.0119 -0.0842 120 PRO A CA 590 C C . PRO A 127 ? 0.3529 0.3192 0.3765 0.0016 0.0078 -0.0884 120 PRO A C 591 O O . PRO A 127 ? 0.3447 0.3096 0.3786 -0.0001 0.0068 -0.0852 120 PRO A O 592 C CB . PRO A 127 ? 0.3333 0.3029 0.3538 0.0059 0.0161 -0.0849 120 PRO A CB 593 C CG . PRO A 127 ? 0.3337 0.3074 0.3565 0.0065 0.0189 -0.0781 120 PRO A CG 594 C CD . PRO A 127 ? 0.3031 0.2783 0.3289 0.0040 0.0165 -0.0730 120 PRO A CD 595 N N . ASN A 128 ? 0.3682 0.3316 0.3858 0.0023 0.0055 -0.0956 121 ASN A N 596 C CA . ASN A 128 ? 0.4097 0.3679 0.4337 0.0011 0.0011 -0.1011 121 ASN A CA 597 C C . ASN A 128 ? 0.4266 0.3798 0.4575 0.0028 0.0035 -0.1038 121 ASN A C 598 O O . ASN A 128 ? 0.4195 0.3717 0.4438 0.0057 0.0063 -0.1075 121 ASN A O 599 C CB . ASN A 128 ? 0.4110 0.3681 0.4241 0.0016 -0.0030 -0.1079 121 ASN A CB 600 C CG . ASN A 128 ? 0.4679 0.4198 0.4878 0.0002 -0.0089 -0.1143 121 ASN A CG 601 O OD1 . ASN A 128 ? 0.4747 0.4224 0.5057 -0.0002 -0.0085 -0.1158 121 ASN A OD1 602 N ND2 . ASN A 128 ? 0.5196 0.4718 0.5335 -0.0005 -0.0145 -0.1181 121 ASN A ND2 603 N N A LYS A 129 ? 0.4427 0.3927 0.4867 0.0012 0.0029 -0.1017 122 LYS A N 604 N N B LYS A 129 ? 0.4351 0.3851 0.4791 0.0012 0.0031 -0.1016 122 LYS A N 605 C CA A LYS A 129 ? 0.4697 0.4144 0.5220 0.0027 0.0052 -0.1030 122 LYS A CA 606 C CA B LYS A 129 ? 0.4546 0.3994 0.5062 0.0029 0.0054 -0.1032 122 LYS A CA 607 C C A LYS A 129 ? 0.4832 0.4222 0.5337 0.0041 0.0031 -0.1124 122 LYS A C 608 C C B LYS A 129 ? 0.4737 0.4131 0.5226 0.0045 0.0034 -0.1126 122 LYS A C 609 O O A LYS A 129 ? 0.4955 0.4308 0.5486 0.0066 0.0059 -0.1145 122 LYS A O 610 O O B LYS A 129 ? 0.4817 0.4182 0.5312 0.0073 0.0064 -0.1151 122 LYS A O 611 C CB A LYS A 129 ? 0.4749 0.4168 0.5415 0.0003 0.0048 -0.0984 122 LYS A CB 612 C CB B LYS A 129 ? 0.4531 0.3946 0.5193 0.0008 0.0051 -0.0989 122 LYS A CB 613 C CG A LYS A 129 ? 0.4949 0.4409 0.5634 0.0001 0.0080 -0.0889 122 LYS A CG 614 C CG B LYS A 129 ? 0.4494 0.3931 0.5189 0.0016 0.0094 -0.0901 122 LYS A CG 615 C CD A LYS A 129 ? 0.5465 0.4902 0.6272 -0.0027 0.0074 -0.0844 122 LYS A CD 616 C CD B LYS A 129 ? 0.4560 0.3937 0.5384 0.0013 0.0106 -0.0873 122 LYS A CD 617 C CE A LYS A 129 ? 0.5605 0.5090 0.6402 -0.0030 0.0098 -0.0757 122 LYS A CE 618 C CE B LYS A 129 ? 0.4698 0.4022 0.5542 0.0043 0.0123 -0.0912 122 LYS A CE 619 N NZ A LYS A 129 ? 0.6084 0.5542 0.6999 -0.0051 0.0106 -0.0706 122 LYS A NZ 620 N NZ B LYS A 129 ? 0.4734 0.3998 0.5694 0.0045 0.0141 -0.0870 122 LYS A NZ 621 N N . THR A 130 ? 0.4874 0.4256 0.5330 0.0030 -0.0019 -0.1182 123 THR A N 622 C CA . THR A 130 ? 0.5096 0.4420 0.5520 0.0046 -0.0046 -0.1279 123 THR A CA 623 C C . THR A 130 ? 0.5152 0.4491 0.5400 0.0075 -0.0047 -0.1332 123 THR A C 624 O O . THR A 130 ? 0.5399 0.4689 0.5595 0.0092 -0.0074 -0.1417 123 THR A O 625 C CB . THR A 130 ? 0.5216 0.4493 0.5741 0.0016 -0.0112 -0.1324 123 THR A CB 626 O OG1 . THR A 130 ? 0.5377 0.4697 0.5870 -0.0007 -0.0156 -0.1314 123 THR A OG1 627 C CG2 . THR A 130 ? 0.5264 0.4514 0.5965 -0.0007 -0.0097 -0.1274 123 THR A CG2 628 N N . HIS A 131 ? 0.4947 0.4348 0.5103 0.0081 -0.0014 -0.1280 124 HIS A N 629 C CA . HIS A 131 ? 0.4937 0.4353 0.4924 0.0107 -0.0004 -0.1314 124 HIS A CA 630 C C . HIS A 131 ? 0.4720 0.4195 0.4667 0.0120 0.0064 -0.1247 124 HIS A C 631 O O . HIS A 131 ? 0.4618 0.4144 0.4514 0.0108 0.0066 -0.1195 124 HIS A O 632 C CB . HIS A 131 ? 0.5014 0.4448 0.4932 0.0089 -0.0062 -0.1320 124 HIS A CB 633 C CG . HIS A 131 ? 0.5492 0.4916 0.5228 0.0117 -0.0071 -0.1374 124 HIS A CG 634 N ND1 . HIS A 131 ? 0.5816 0.5257 0.5459 0.0110 -0.0118 -0.1376 124 HIS A ND1 635 C CD2 . HIS A 131 ? 0.5916 0.5313 0.5543 0.0157 -0.0036 -0.1426 124 HIS A CD2 636 C CE1 . HIS A 131 ? 0.6038 0.5457 0.5511 0.0145 -0.0113 -0.1425 124 HIS A CE1 637 N NE2 . HIS A 131 ? 0.6186 0.5580 0.5646 0.0173 -0.0060 -0.1456 124 HIS A NE2 638 N N . PRO A 132 ? 0.4591 0.4058 0.4572 0.0145 0.0116 -0.1248 125 PRO A N 639 C CA . PRO A 132 ? 0.4384 0.3909 0.4372 0.0154 0.0176 -0.1180 125 PRO A CA 640 C C . PRO A 132 ? 0.4279 0.3847 0.4130 0.0169 0.0211 -0.1173 125 PRO A C 641 O O . PRO A 132 ? 0.4363 0.3908 0.4096 0.0188 0.0209 -0.1231 125 PRO A O 642 C CB . PRO A 132 ? 0.4572 0.4071 0.4639 0.0180 0.0213 -0.1197 125 PRO A CB 643 C CG . PRO A 132 ? 0.4686 0.4109 0.4778 0.0186 0.0178 -0.1276 125 PRO A CG 644 C CD . PRO A 132 ? 0.4791 0.4195 0.4814 0.0167 0.0119 -0.1315 125 PRO A CD 645 N N . ASN A 133 ? 0.3916 0.3544 0.3782 0.0161 0.0242 -0.1101 126 ASN A N 646 C CA . ASN A 133 ? 0.3864 0.3537 0.3626 0.0172 0.0285 -0.1080 126 ASN A CA 647 C C . ASN A 133 ? 0.3856 0.3536 0.3619 0.0206 0.0350 -0.1101 126 ASN A C 648 O O . ASN A 133 ? 0.3874 0.3551 0.3749 0.0215 0.0366 -0.1094 126 ASN A O 649 C CB . ASN A 133 ? 0.3530 0.3261 0.3333 0.0150 0.0291 -0.0996 126 ASN A CB 650 C CG . ASN A 133 ? 0.3812 0.3543 0.3619 0.0118 0.0233 -0.0970 126 ASN A CG 651 O OD1 . ASN A 133 ? 0.3548 0.3252 0.3285 0.0113 0.0193 -0.1008 126 ASN A OD1 652 N ND2 . ASN A 133 ? 0.3548 0.3309 0.3438 0.0100 0.0228 -0.0907 126 ASN A ND2 653 N N . TYR A 134 ? 0.3938 0.3624 0.3577 0.0227 0.0388 -0.1126 127 TYR A N 654 C CA . TYR A 134 ? 0.3971 0.3674 0.3612 0.0260 0.0462 -0.1140 127 TYR A CA 655 C C . TYR A 134 ? 0.4072 0.3791 0.3565 0.0274 0.0507 -0.1143 127 TYR A C 656 O O . TYR A 134 ? 0.4133 0.3837 0.3509 0.0264 0.0474 -0.1145 127 TYR A O 657 C CB . TYR A 134 ? 0.4129 0.3778 0.3805 0.0289 0.0465 -0.1213 127 TYR A CB 658 C CG . TYR A 134 ? 0.4471 0.4059 0.4018 0.0307 0.0443 -0.1291 127 TYR A CG 659 C CD1 . TYR A 134 ? 0.4904 0.4477 0.4354 0.0347 0.0499 -0.1342 127 TYR A CD1 660 C CD2 . TYR A 134 ? 0.4636 0.4179 0.4160 0.0286 0.0365 -0.1318 127 TYR A CD2 661 C CE1 . TYR A 134 ? 0.5043 0.4553 0.4361 0.0370 0.0476 -0.1419 127 TYR A CE1 662 C CE2 . TYR A 134 ? 0.4791 0.4274 0.4195 0.0306 0.0335 -0.1399 127 TYR A CE2 663 C CZ . TYR A 134 ? 0.5079 0.4544 0.4371 0.0349 0.0390 -0.1448 127 TYR A CZ 664 O OH . TYR A 134 ? 0.5260 0.4661 0.4419 0.0375 0.0359 -0.1531 127 TYR A OH 665 N N . ILE A 135 ? 0.4070 0.3821 0.3573 0.0299 0.0583 -0.1140 128 ILE A N 666 C CA . ILE A 135 ? 0.4097 0.3862 0.3469 0.0317 0.0644 -0.1139 128 ILE A CA 667 C C . ILE A 135 ? 0.4237 0.3972 0.3571 0.0361 0.0698 -0.1206 128 ILE A C 668 O O . ILE A 135 ? 0.4139 0.3875 0.3594 0.0376 0.0712 -0.1228 128 ILE A O 669 C CB . ILE A 135 ? 0.3967 0.3805 0.3403 0.0304 0.0698 -0.1065 128 ILE A CB 670 C CG1 . ILE A 135 ? 0.3852 0.3717 0.3326 0.0262 0.0643 -0.1001 128 ILE A CG1 671 C CG2 . ILE A 135 ? 0.4179 0.4031 0.3489 0.0322 0.0775 -0.1058 128 ILE A CG2 672 C CD1 . ILE A 135 ? 0.3901 0.3833 0.3498 0.0248 0.0675 -0.0938 128 ILE A CD1 673 N N . SER A 136 ? 0.4415 0.4120 0.3576 0.0386 0.0726 -0.1238 129 SER A N 674 C CA . SER A 136 ? 0.4622 0.4295 0.3717 0.0433 0.0786 -0.1304 129 SER A CA 675 C C . SER A 136 ? 0.4775 0.4479 0.3772 0.0454 0.0882 -0.1278 129 SER A C 676 O O . SER A 136 ? 0.4741 0.4464 0.3658 0.0436 0.0887 -0.1225 129 SER A O 677 C CB . SER A 136 ? 0.4711 0.4300 0.3659 0.0454 0.0731 -0.1384 129 SER A CB 678 O OG . SER A 136 ? 0.5095 0.4650 0.4144 0.0436 0.0649 -0.1415 129 SER A OG 679 N N . ILE A 137 ? 0.5035 0.4739 0.4037 0.0496 0.0961 -0.1317 130 ILE A N 680 C CA . ILE A 137 ? 0.5302 0.5001 0.4150 0.0529 0.1050 -0.1321 130 ILE A CA 681 C C . ILE A 137 ? 0.5576 0.5187 0.4256 0.0569 0.1022 -0.1411 130 ILE A C 682 O O . ILE A 137 ? 0.5479 0.5053 0.4218 0.0586 0.0991 -0.1478 130 ILE A O 683 C CB . ILE A 137 ? 0.5337 0.5092 0.4287 0.0554 0.1162 -0.1312 130 ILE A CB 684 C CG1 . ILE A 137 ? 0.5185 0.5028 0.4302 0.0515 0.1185 -0.1225 130 ILE A CG1 685 C CG2 . ILE A 137 ? 0.5468 0.5200 0.4236 0.0599 0.1260 -0.1332 130 ILE A CG2 686 C CD1 . ILE A 137 ? 0.5092 0.4999 0.4360 0.0534 0.1278 -0.1217 130 ILE A CD1 687 N N . ILE A 138 ? 0.5935 0.5508 0.4405 0.0583 0.1025 -0.1412 131 ILE A N 688 C CA . ILE A 138 ? 0.6430 0.5913 0.4712 0.0621 0.0984 -0.1497 131 ILE A CA 689 C C . ILE A 138 ? 0.6723 0.6186 0.4823 0.0676 0.1092 -0.1513 131 ILE A C 690 O O . ILE A 138 ? 0.6678 0.6183 0.4737 0.0671 0.1168 -0.1442 131 ILE A O 691 C CB . ILE A 138 ? 0.6436 0.5883 0.4625 0.0593 0.0871 -0.1490 131 ILE A CB 692 C CG1 . ILE A 138 ? 0.6951 0.6308 0.5012 0.0622 0.0792 -0.1590 131 ILE A CG1 693 C CG2 . ILE A 138 ? 0.6705 0.6169 0.4755 0.0585 0.0900 -0.1419 131 ILE A CG2 694 C CD1 . ILE A 138 ? 0.7181 0.6513 0.5235 0.0586 0.0664 -0.1591 131 ILE A CD1 695 N N . ASN A 139 ? 0.7066 0.6465 0.5065 0.0728 0.1105 -0.1604 132 ASN A N 696 C CA . ASN A 139 ? 0.7524 0.6893 0.5320 0.0786 0.1207 -0.1622 132 ASN A CA 697 C C . ASN A 139 ? 0.7868 0.7162 0.5391 0.0808 0.1160 -0.1639 132 ASN A C 698 O O . ASN A 139 ? 0.7885 0.7157 0.5393 0.0776 0.1045 -0.1640 132 ASN A O 699 C CB . ASN A 139 ? 0.7607 0.6946 0.5411 0.0841 0.1267 -0.1707 132 ASN A CB 700 C CG . ASN A 139 ? 0.7696 0.6946 0.5439 0.0864 0.1166 -0.1815 132 ASN A CG 701 O OD1 . ASN A 139 ? 0.7803 0.6998 0.5424 0.0855 0.1065 -0.1839 132 ASN A OD1 702 N ND2 . ASN A 139 ? 0.7562 0.6797 0.5401 0.0894 0.1191 -0.1882 132 ASN A ND2 703 N N . GLU A 140 ? 0.8276 0.7532 0.5586 0.0864 0.1249 -0.1653 133 GLU A N 704 C CA . GLU A 140 ? 0.8667 0.7848 0.5694 0.0893 0.1212 -0.1663 133 GLU A CA 705 C C . GLU A 140 ? 0.8861 0.7950 0.5768 0.0918 0.1086 -0.1771 133 GLU A C 706 O O . GLU A 140 ? 0.9039 0.8071 0.5751 0.0930 0.1015 -0.1781 133 GLU A O 707 C CB . GLU A 140 ? 0.8880 0.8038 0.5701 0.0951 0.1347 -0.1648 133 GLU A CB 708 C CG . GLU A 140 ? 0.9220 0.8344 0.6000 0.1014 0.1424 -0.1732 133 GLU A CG 709 C CD . GLU A 140 ? 0.9501 0.8624 0.6125 0.1065 0.1584 -0.1698 133 GLU A CD 710 O OE1 . GLU A 140 ? 0.9582 0.8708 0.6082 0.1059 0.1623 -0.1617 133 GLU A OE1 711 O OE2 . GLU A 140 ? 0.9733 0.8851 0.6365 0.1112 0.1673 -0.1749 133 GLU A OE2 712 N N . ASP A 141 ? 0.8885 0.7957 0.5913 0.0927 0.1057 -0.1851 134 ASP A N 713 C CA . ASP A 141 ? 0.9032 0.8022 0.6002 0.0942 0.0932 -0.1957 134 ASP A CA 714 C C . ASP A 141 ? 0.8812 0.7825 0.5958 0.0874 0.0801 -0.1939 134 ASP A C 715 O O . ASP A 141 ? 0.8993 0.7944 0.6098 0.0875 0.0682 -0.2012 134 ASP A O 716 C CB . ASP A 141 ? 0.9129 0.8084 0.6157 0.0983 0.0961 -0.2052 134 ASP A CB 717 C CG . ASP A 141 ? 0.9543 0.8465 0.6379 0.1058 0.1088 -0.2082 134 ASP A CG 718 O OD1 . ASP A 141 ? 0.9811 0.8687 0.6387 0.1096 0.1108 -0.2076 134 ASP A OD1 719 O OD2 . ASP A 141 ? 0.9556 0.8496 0.6498 0.1082 0.1168 -0.2112 134 ASP A OD2 720 N N . GLY A 142 ? 0.8419 0.7521 0.5765 0.0816 0.0823 -0.1844 135 GLY A N 721 C CA . GLY A 142 ? 0.8062 0.7192 0.5590 0.0753 0.0715 -0.1821 135 GLY A CA 722 C C . GLY A 142 ? 0.7744 0.6894 0.5517 0.0730 0.0699 -0.1849 135 GLY A C 723 O O . GLY A 142 ? 0.7752 0.6906 0.5667 0.0685 0.0605 -0.1848 135 GLY A O 724 N N A ASN A 143 ? 0.7644 0.6803 0.5466 0.0764 0.0793 -0.1872 136 ASN A N 725 N N B ASN A 143 ? 0.7646 0.6806 0.5470 0.0763 0.0794 -0.1870 136 ASN A N 726 C CA A ASN A 143 ? 0.7350 0.6529 0.5404 0.0748 0.0790 -0.1890 136 ASN A CA 727 C CA B ASN A 143 ? 0.7344 0.6523 0.5399 0.0749 0.0791 -0.1890 136 ASN A CA 728 C C A ASN A 143 ? 0.6983 0.6262 0.5238 0.0700 0.0832 -0.1786 136 ASN A C 729 C C B ASN A 143 ? 0.6999 0.6277 0.5259 0.0702 0.0835 -0.1788 136 ASN A C 730 O O A ASN A 143 ? 0.6895 0.6230 0.5130 0.0705 0.0927 -0.1723 136 ASN A O 731 O O B ASN A 143 ? 0.6953 0.6288 0.5202 0.0710 0.0935 -0.1730 136 ASN A O 732 C CB A ASN A 143 ? 0.7490 0.6639 0.5522 0.0807 0.0871 -0.1960 136 ASN A CB 733 C CB B ASN A 143 ? 0.7486 0.6631 0.5507 0.0810 0.0869 -0.1964 136 ASN A CB 734 C CG A ASN A 143 ? 0.7809 0.6855 0.5627 0.0863 0.0835 -0.2071 136 ASN A CG 735 C CG B ASN A 143 ? 0.7348 0.6488 0.5583 0.0803 0.0847 -0.2004 136 ASN A CG 736 O OD1 A ASN A 143 ? 0.7996 0.7015 0.5696 0.0923 0.0919 -0.2116 136 ASN A OD1 737 O OD1 B ASN A 143 ? 0.7057 0.6240 0.5491 0.0753 0.0806 -0.1953 136 ASN A OD1 738 N ND2 A ASN A 143 ? 0.7828 0.6816 0.5600 0.0846 0.0710 -0.2117 136 ASN A ND2 739 N ND2 B ASN A 143 ? 0.7399 0.6480 0.5588 0.0858 0.0874 -0.2096 136 ASN A ND2 740 N N . GLU A 144 ? 0.6715 0.6010 0.5162 0.0655 0.0761 -0.1769 137 GLU A N 741 C CA . GLU A 144 ? 0.6315 0.5696 0.4956 0.0613 0.0788 -0.1677 137 GLU A CA 742 C C . GLU A 144 ? 0.6137 0.5545 0.4926 0.0636 0.0858 -0.1691 137 GLU A C 743 O O . GLU A 144 ? 0.6181 0.5554 0.5081 0.0640 0.0818 -0.1738 137 GLU A O 744 C CB . GLU A 144 ? 0.6055 0.5441 0.4819 0.0559 0.0685 -0.1648 137 GLU A CB 745 C CG . GLU A 144 ? 0.6031 0.5402 0.4662 0.0536 0.0619 -0.1629 137 GLU A CG 746 C CD . GLU A 144 ? 0.5820 0.5201 0.4576 0.0482 0.0525 -0.1596 137 GLU A CD 747 O OE1 . GLU A 144 ? 0.5475 0.4854 0.4403 0.0465 0.0497 -0.1602 137 GLU A OE1 748 O OE2 . GLU A 144 ? 0.5844 0.5233 0.4523 0.0460 0.0480 -0.1562 137 GLU A OE2 749 N N . ILE A 145 ? 0.5989 0.5455 0.4778 0.0654 0.0964 -0.1650 138 ILE A N 750 C CA . ILE A 145 ? 0.5910 0.5403 0.4820 0.0687 0.1044 -0.1670 138 ILE A CA 751 C C . ILE A 145 ? 0.5599 0.5169 0.4746 0.0655 0.1049 -0.1604 138 ILE A C 752 O O . ILE A 145 ? 0.5527 0.5117 0.4808 0.0679 0.1094 -0.1621 138 ILE A O 753 C CB . ILE A 145 ? 0.6043 0.5554 0.4833 0.0734 0.1167 -0.1676 138 ILE A CB 754 C CG1 . ILE A 145 ? 0.5938 0.5525 0.4721 0.0706 0.1225 -0.1579 138 ILE A CG1 755 C CG2 . ILE A 145 ? 0.6343 0.5762 0.4891 0.0780 0.1160 -0.1758 138 ILE A CG2 756 C CD1 . ILE A 145 ? 0.6001 0.5620 0.4718 0.0747 0.1362 -0.1568 138 ILE A CD1 757 N N . PHE A 146 ? 0.5342 0.4951 0.4537 0.0604 0.1002 -0.1530 139 PHE A N 758 C CA . PHE A 146 ? 0.5068 0.4739 0.4472 0.0573 0.0989 -0.1469 139 PHE A CA 759 C C . PHE A 146 ? 0.4803 0.4468 0.4221 0.0522 0.0894 -0.1426 139 PHE A C 760 O O . PHE A 146 ? 0.4644 0.4304 0.3932 0.0504 0.0876 -0.1404 139 PHE A O 761 C CB . PHE A 146 ? 0.5086 0.4848 0.4555 0.0569 0.1075 -0.1402 139 PHE A CB 762 C CG . PHE A 146 ? 0.4972 0.4796 0.4621 0.0530 0.1043 -0.1331 139 PHE A CG 763 C CD1 . PHE A 146 ? 0.5145 0.4986 0.4975 0.0540 0.1033 -0.1337 139 PHE A CD1 764 C CD2 . PHE A 146 ? 0.4920 0.4779 0.4549 0.0488 0.1016 -0.1261 139 PHE A CD2 765 C CE1 . PHE A 146 ? 0.4899 0.4791 0.4879 0.0508 0.0995 -0.1273 139 PHE A CE1 766 C CE2 . PHE A 146 ? 0.4663 0.4574 0.4446 0.0455 0.0981 -0.1200 139 PHE A CE2 767 C CZ . PHE A 146 ? 0.4718 0.4644 0.4671 0.0466 0.0970 -0.1206 139 PHE A CZ 768 N N . ASN A 147 ? 0.4629 0.4290 0.4198 0.0503 0.0837 -0.1416 140 ASN A N 769 C CA . ASN A 147 ? 0.4516 0.4177 0.4123 0.0455 0.0755 -0.1369 140 ASN A CA 770 C C . ASN A 147 ? 0.4298 0.4021 0.4076 0.0434 0.0754 -0.1300 140 ASN A C 771 O O . ASN A 147 ? 0.4271 0.4004 0.4176 0.0455 0.0776 -0.1309 140 ASN A O 772 C CB . ASN A 147 ? 0.4652 0.4238 0.4277 0.0450 0.0676 -0.1421 140 ASN A CB 773 C CG . ASN A 147 ? 0.5055 0.4573 0.4511 0.0467 0.0652 -0.1494 140 ASN A CG 774 O OD1 . ASN A 147 ? 0.5276 0.4800 0.4582 0.0468 0.0666 -0.1487 140 ASN A OD1 775 N ND2 . ASN A 147 ? 0.5528 0.4975 0.5007 0.0482 0.0611 -0.1565 140 ASN A ND2 776 N N . THR A 148 ? 0.4103 0.3864 0.3884 0.0395 0.0725 -0.1232 141 THR A N 777 C CA . THR A 148 ? 0.3968 0.3778 0.3900 0.0376 0.0712 -0.1169 141 THR A CA 778 C C . THR A 148 ? 0.3889 0.3652 0.3912 0.0367 0.0645 -0.1177 141 THR A C 779 O O . THR A 148 ? 0.3984 0.3681 0.3954 0.0364 0.0601 -0.1223 141 THR A O 780 C CB . THR A 148 ? 0.3747 0.3607 0.3654 0.0340 0.0701 -0.1097 141 THR A CB 781 O OG1 . THR A 148 ? 0.3994 0.3815 0.3808 0.0314 0.0640 -0.1098 141 THR A OG1 782 C CG2 . THR A 148 ? 0.3926 0.3831 0.3761 0.0349 0.0776 -0.1083 141 THR A CG2 783 N N . SER A 149 ? 0.3840 0.3633 0.4001 0.0363 0.0636 -0.1132 142 SER A N 784 C CA . SER A 149 ? 0.3790 0.3537 0.4045 0.0360 0.0584 -0.1131 142 SER A CA 785 C C . SER A 149 ? 0.3792 0.3504 0.4011 0.0322 0.0518 -0.1110 142 SER A C 786 O O . SER A 149 ? 0.3883 0.3628 0.4041 0.0295 0.0506 -0.1072 142 SER A O 787 C CB . SER A 149 ? 0.3803 0.3593 0.4193 0.0367 0.0587 -0.1078 142 SER A CB 788 O OG A SER A 149 ? 0.3285 0.3111 0.3677 0.0335 0.0558 -0.1010 142 SER A OG 789 O OG B SER A 149 ? 0.4197 0.3934 0.4676 0.0378 0.0554 -0.1085 142 SER A OG 790 N N . LEU A 150 ? 0.3881 0.3529 0.4149 0.0321 0.0477 -0.1134 143 LEU A N 791 C CA . LEU A 150 ? 0.3954 0.3571 0.4216 0.0285 0.0418 -0.1113 143 LEU A CA 792 C C . LEU A 150 ? 0.3851 0.3483 0.4211 0.0270 0.0396 -0.1040 143 LEU A C 793 O O . LEU A 150 ? 0.3815 0.3437 0.4174 0.0239 0.0357 -0.1008 143 LEU A O 794 C CB . LEU A 150 ? 0.4185 0.3721 0.4447 0.0285 0.0382 -0.1178 143 LEU A CB 795 C CG . LEU A 150 ? 0.4573 0.4083 0.4718 0.0303 0.0393 -0.1257 143 LEU A CG 796 C CD1 . LEU A 150 ? 0.5129 0.4557 0.5286 0.0301 0.0347 -0.1324 143 LEU A CD1 797 C CD2 . LEU A 150 ? 0.4757 0.4307 0.4773 0.0286 0.0392 -0.1243 143 LEU A CD2 798 N N . PHE A 151 ? 0.3772 0.3429 0.4213 0.0294 0.0423 -0.1015 144 PHE A N 799 C CA . PHE A 151 ? 0.3652 0.3320 0.4177 0.0290 0.0403 -0.0948 144 PHE A CA 800 C C . PHE A 151 ? 0.3537 0.3248 0.4132 0.0323 0.0434 -0.0929 144 PHE A C 801 O O . PHE A 151 ? 0.3611 0.3331 0.4217 0.0351 0.0471 -0.0974 144 PHE A O 802 C CB . PHE A 151 ? 0.3853 0.3445 0.4445 0.0288 0.0370 -0.0947 144 PHE A CB 803 C CG . PHE A 151 ? 0.4094 0.3635 0.4742 0.0320 0.0384 -0.1000 144 PHE A CG 804 C CD1 . PHE A 151 ? 0.4309 0.3850 0.5043 0.0354 0.0398 -0.0980 144 PHE A CD1 805 C CD2 . PHE A 151 ? 0.4854 0.4343 0.5465 0.0320 0.0380 -0.1073 144 PHE A CD2 806 C CE1 . PHE A 151 ? 0.4869 0.4363 0.5660 0.0388 0.0411 -0.1028 144 PHE A CE1 807 C CE2 . PHE A 151 ? 0.5064 0.4502 0.5728 0.0353 0.0393 -0.1125 144 PHE A CE2 808 C CZ . PHE A 151 ? 0.5045 0.4486 0.5800 0.0387 0.0410 -0.1102 144 PHE A CZ 809 N N . GLU A 152 ? 0.3293 0.3030 0.3937 0.0322 0.0417 -0.0866 145 GLU A N 810 C CA . GLU A 152 ? 0.3257 0.3032 0.3983 0.0355 0.0433 -0.0848 145 GLU A CA 811 C C . GLU A 152 ? 0.3348 0.3062 0.4157 0.0385 0.0421 -0.0857 145 GLU A C 812 O O . GLU A 152 ? 0.3416 0.3071 0.4234 0.0375 0.0390 -0.0835 145 GLU A O 813 C CB . GLU A 152 ? 0.3224 0.3041 0.3966 0.0347 0.0410 -0.0781 145 GLU A CB 814 C CG . GLU A 152 ? 0.3062 0.2943 0.3743 0.0321 0.0420 -0.0763 145 GLU A CG 815 C CD . GLU A 152 ? 0.3076 0.2985 0.3775 0.0315 0.0389 -0.0699 145 GLU A CD 816 O OE1 . GLU A 152 ? 0.3113 0.2988 0.3778 0.0297 0.0359 -0.0667 145 GLU A OE1 817 O OE2 . GLU A 152 ? 0.2960 0.2921 0.3713 0.0332 0.0394 -0.0684 145 GLU A OE2 818 N N . PRO A 153 ? 0.3459 0.3186 0.4335 0.0424 0.0447 -0.0887 146 PRO A N 819 C CA . PRO A 153 ? 0.3569 0.3237 0.4530 0.0457 0.0432 -0.0888 146 PRO A CA 820 C C . PRO A 153 ? 0.3537 0.3191 0.4528 0.0459 0.0393 -0.0816 146 PRO A C 821 O O . PRO A 153 ? 0.3607 0.3322 0.4611 0.0464 0.0385 -0.0778 146 PRO A O 822 C CB . PRO A 153 ? 0.3654 0.3367 0.4689 0.0498 0.0466 -0.0918 146 PRO A CB 823 C CG . PRO A 153 ? 0.3575 0.3345 0.4548 0.0484 0.0511 -0.0957 146 PRO A CG 824 C CD . PRO A 153 ? 0.3599 0.3394 0.4484 0.0439 0.0494 -0.0919 146 PRO A CD 825 N N . PRO A 154 ? 0.3587 0.3161 0.4583 0.0453 0.0367 -0.0795 147 PRO A N 826 C CA . PRO A 154 ? 0.3559 0.3117 0.4561 0.0455 0.0336 -0.0722 147 PRO A CA 827 C C . PRO A 154 ? 0.3608 0.3169 0.4685 0.0505 0.0324 -0.0698 147 PRO A C 828 O O . PRO A 154 ? 0.3659 0.3201 0.4801 0.0539 0.0337 -0.0736 147 PRO A O 829 C CB . PRO A 154 ? 0.3719 0.3187 0.4719 0.0437 0.0323 -0.0711 147 PRO A CB 830 C CG . PRO A 154 ? 0.3875 0.3303 0.4898 0.0441 0.0340 -0.0783 147 PRO A CG 831 C CD . PRO A 154 ? 0.3759 0.3258 0.4740 0.0435 0.0366 -0.0833 147 PRO A CD 832 N N . PRO A 155 ? 0.3605 0.3186 0.4670 0.0513 0.0297 -0.0637 148 PRO A N 833 C CA . PRO A 155 ? 0.3624 0.3214 0.4757 0.0565 0.0278 -0.0619 148 PRO A CA 834 C C . PRO A 155 ? 0.3625 0.3118 0.4798 0.0599 0.0264 -0.0600 148 PRO A C 835 O O . PRO A 155 ? 0.3643 0.3062 0.4789 0.0578 0.0267 -0.0585 148 PRO A O 836 C CB . PRO A 155 ? 0.3531 0.3160 0.4623 0.0563 0.0248 -0.0563 148 PRO A CB 837 C CG . PRO A 155 ? 0.3576 0.3177 0.4582 0.0519 0.0248 -0.0533 148 PRO A CG 838 C CD . PRO A 155 ? 0.3672 0.3272 0.4664 0.0482 0.0281 -0.0589 148 PRO A CD 839 N N . PRO A 156 ? 0.3615 0.3108 0.4859 0.0652 0.0248 -0.0596 149 PRO A N 840 C CA . PRO A 156 ? 0.3747 0.3146 0.5034 0.0691 0.0235 -0.0577 149 PRO A CA 841 C C . PRO A 156 ? 0.3745 0.3061 0.4973 0.0683 0.0219 -0.0508 149 PRO A C 842 O O . PRO A 156 ? 0.3661 0.2993 0.4832 0.0685 0.0195 -0.0453 149 PRO A O 843 C CB . PRO A 156 ? 0.3773 0.3206 0.5127 0.0749 0.0206 -0.0568 149 PRO A CB 844 C CG . PRO A 156 ? 0.3737 0.3282 0.5124 0.0738 0.0224 -0.0616 149 PRO A CG 845 C CD . PRO A 156 ? 0.3680 0.3263 0.4977 0.0679 0.0238 -0.0608 149 PRO A CD 846 N N . GLY A 157 ? 0.3896 0.3121 0.5139 0.0674 0.0233 -0.0511 150 GLY A N 847 C CA . GLY A 157 ? 0.4091 0.3232 0.5294 0.0666 0.0228 -0.0443 150 GLY A CA 848 C C . GLY A 157 ? 0.4311 0.3461 0.5453 0.0605 0.0243 -0.0433 150 GLY A C 849 O O . GLY A 157 ? 0.4429 0.3510 0.5549 0.0593 0.0248 -0.0380 150 GLY A O 850 N N . TYR A 158 ? 0.4380 0.3612 0.5498 0.0569 0.0254 -0.0481 151 TYR A N 851 C CA . TYR A 158 ? 0.4550 0.3800 0.5613 0.0511 0.0265 -0.0483 151 TYR A CA 852 C C . TYR A 158 ? 0.4779 0.4031 0.5860 0.0477 0.0283 -0.0558 151 TYR A C 853 O O . TYR A 158 ? 0.4781 0.4063 0.5817 0.0432 0.0287 -0.0572 151 TYR A O 854 C CB . TYR A 158 ? 0.4352 0.3698 0.5355 0.0496 0.0257 -0.0475 151 TYR A CB 855 C CG . TYR A 158 ? 0.4139 0.3497 0.5102 0.0522 0.0234 -0.0408 151 TYR A CG 856 C CD1 . TYR A 158 ? 0.3751 0.3094 0.4651 0.0499 0.0232 -0.0353 151 TYR A CD1 857 C CD2 . TYR A 158 ? 0.3487 0.2874 0.4475 0.0569 0.0212 -0.0403 151 TYR A CD2 858 C CE1 . TYR A 158 ? 0.3678 0.3030 0.4528 0.0526 0.0210 -0.0297 151 TYR A CE1 859 C CE2 . TYR A 158 ? 0.3358 0.2754 0.4302 0.0596 0.0184 -0.0348 151 TYR A CE2 860 C CZ . TYR A 158 ? 0.3485 0.2861 0.4352 0.0575 0.0183 -0.0296 151 TYR A CZ 861 O OH . TYR A 158 ? 0.3300 0.2681 0.4113 0.0606 0.0154 -0.0246 151 TYR A OH 862 N N A GLU A 159 ? 0.4846 0.4067 0.5988 0.0502 0.0291 -0.0609 152 GLU A N 863 N N B GLU A 159 ? 0.4876 0.4097 0.6019 0.0503 0.0291 -0.0609 152 GLU A N 864 C CA A GLU A 159 ? 0.5031 0.4246 0.6182 0.0479 0.0306 -0.0686 152 GLU A CA 865 C CA B GLU A 159 ? 0.5005 0.4215 0.6160 0.0480 0.0306 -0.0687 152 GLU A CA 866 C C A GLU A 159 ? 0.5163 0.4300 0.6325 0.0441 0.0303 -0.0688 152 GLU A C 867 C C B GLU A 159 ? 0.5134 0.4278 0.6290 0.0438 0.0303 -0.0685 152 GLU A C 868 O O A GLU A 159 ? 0.5227 0.4358 0.6384 0.0416 0.0307 -0.0752 152 GLU A O 869 O O B GLU A 159 ? 0.5151 0.4301 0.6288 0.0406 0.0306 -0.0743 152 GLU A O 870 C CB A GLU A 159 ? 0.5119 0.4321 0.6332 0.0521 0.0318 -0.0743 152 GLU A CB 871 C CB B GLU A 159 ? 0.5061 0.4232 0.6287 0.0522 0.0315 -0.0736 152 GLU A CB 872 C CG A GLU A 159 ? 0.5099 0.4372 0.6334 0.0564 0.0318 -0.0734 152 GLU A CG 873 C CG B GLU A 159 ? 0.4929 0.4179 0.6157 0.0542 0.0334 -0.0796 152 GLU A CG 874 C CD A GLU A 159 ? 0.5149 0.4376 0.6436 0.0613 0.0297 -0.0679 152 GLU A CD 875 C CD B GLU A 159 ? 0.4856 0.4114 0.6045 0.0514 0.0352 -0.0873 152 GLU A CD 876 O OE1 A GLU A 159 ? 0.4928 0.4085 0.6205 0.0609 0.0284 -0.0621 152 GLU A OE1 877 O OE1 B GLU A 159 ? 0.4599 0.3910 0.5785 0.0531 0.0377 -0.0925 152 GLU A OE1 878 O OE2 A GLU A 159 ? 0.5028 0.4291 0.6365 0.0657 0.0294 -0.0691 152 GLU A OE2 879 O OE2 B GLU A 159 ? 0.4919 0.4130 0.6082 0.0476 0.0342 -0.0882 152 GLU A OE2 880 N N . ASN A 160 ? 0.5271 0.4351 0.6449 0.0439 0.0297 -0.0617 153 ASN A N 881 C CA . ASN A 160 ? 0.5476 0.4488 0.6681 0.0399 0.0297 -0.0607 153 ASN A CA 882 C C . ASN A 160 ? 0.5524 0.4566 0.6679 0.0364 0.0295 -0.0547 153 ASN A C 883 O O . ASN A 160 ? 0.5604 0.4596 0.6790 0.0331 0.0299 -0.0524 153 ASN A O 884 C CB . ASN A 160 ? 0.5634 0.4537 0.6915 0.0423 0.0301 -0.0573 153 ASN A CB 885 C CG . ASN A 160 ? 0.5923 0.4751 0.7264 0.0381 0.0303 -0.0586 153 ASN A CG 886 O OD1 . ASN A 160 ? 0.6135 0.4955 0.7500 0.0360 0.0297 -0.0665 153 ASN A OD1 887 N ND2 . ASN A 160 ? 0.6265 0.5036 0.7631 0.0371 0.0313 -0.0509 153 ASN A ND2 888 N N . VAL A 161 ? 0.5441 0.4564 0.6527 0.0370 0.0291 -0.0523 154 VAL A N 889 C CA . VAL A 161 ? 0.5355 0.4510 0.6389 0.0339 0.0290 -0.0473 154 VAL A CA 890 C C . VAL A 161 ? 0.5374 0.4561 0.6395 0.0289 0.0286 -0.0527 154 VAL A C 891 O O . VAL A 161 ? 0.5499 0.4729 0.6498 0.0285 0.0282 -0.0595 154 VAL A O 892 C CB . VAL A 161 ? 0.5340 0.4564 0.6308 0.0362 0.0283 -0.0431 154 VAL A CB 893 C CG1 . VAL A 161 ? 0.5072 0.4337 0.5980 0.0328 0.0282 -0.0392 154 VAL A CG1 894 C CG2 . VAL A 161 ? 0.5606 0.4781 0.6585 0.0413 0.0280 -0.0371 154 VAL A CG2 895 N N . SER A 162 ? 0.5232 0.4394 0.6271 0.0253 0.0287 -0.0498 155 SER A N 896 C CA . SER A 162 ? 0.5098 0.4286 0.6132 0.0207 0.0275 -0.0546 155 SER A CA 897 C C . SER A 162 ? 0.4837 0.4108 0.5792 0.0190 0.0270 -0.0523 155 SER A C 898 O O . SER A 162 ? 0.4673 0.3969 0.5588 0.0207 0.0277 -0.0461 155 SER A O 899 C CB . SER A 162 ? 0.5274 0.4393 0.6391 0.0175 0.0277 -0.0531 155 SER A CB 900 O OG A SER A 162 ? 0.5206 0.4313 0.6327 0.0173 0.0294 -0.0444 155 SER A OG 901 O OG B SER A 162 ? 0.5317 0.4416 0.6475 0.0150 0.0258 -0.0611 155 SER A OG 902 N N . ASP A 163 ? 0.4545 0.3855 0.5472 0.0158 0.0255 -0.0575 156 ASP A N 903 C CA . ASP A 163 ? 0.4281 0.3658 0.5146 0.0135 0.0247 -0.0553 156 ASP A CA 904 C C . ASP A 163 ? 0.3875 0.3318 0.4663 0.0159 0.0252 -0.0541 156 ASP A C 905 O O . ASP A 163 ? 0.3864 0.3351 0.4607 0.0153 0.0251 -0.0498 156 ASP A O 906 C CB . ASP A 163 ? 0.4439 0.3800 0.5330 0.0121 0.0256 -0.0479 156 ASP A CB 907 C CG . ASP A 163 ? 0.4919 0.4224 0.5903 0.0088 0.0253 -0.0486 156 ASP A CG 908 O OD1 . ASP A 163 ? 0.5452 0.4756 0.6458 0.0063 0.0231 -0.0552 156 ASP A OD1 909 O OD2 . ASP A 163 ? 0.5441 0.4703 0.6476 0.0089 0.0274 -0.0423 156 ASP A OD2 910 N N . ILE A 164 ? 0.3504 0.2955 0.4285 0.0188 0.0259 -0.0578 157 ILE A N 911 C CA . ILE A 164 ? 0.3184 0.2707 0.3902 0.0203 0.0263 -0.0579 157 ILE A CA 912 C C . ILE A 164 ? 0.3088 0.2655 0.3747 0.0176 0.0257 -0.0628 157 ILE A C 913 O O . ILE A 164 ? 0.3085 0.2631 0.3744 0.0173 0.0257 -0.0691 157 ILE A O 914 C CB . ILE A 164 ? 0.3172 0.2695 0.3918 0.0243 0.0276 -0.0603 157 ILE A CB 915 C CG1 . ILE A 164 ? 0.3098 0.2577 0.3892 0.0276 0.0276 -0.0550 157 ILE A CG1 916 C CG2 . ILE A 164 ? 0.3021 0.2624 0.3719 0.0252 0.0284 -0.0613 157 ILE A CG2 917 C CD1 . ILE A 164 ? 0.3134 0.2598 0.3977 0.0320 0.0284 -0.0576 157 ILE A CD1 918 N N . VAL A 165 ? 0.2882 0.2502 0.3483 0.0158 0.0251 -0.0601 158 VAL A N 919 C CA . VAL A 165 ? 0.2861 0.2517 0.3397 0.0135 0.0245 -0.0641 158 VAL A CA 920 C C . VAL A 165 ? 0.2962 0.2651 0.3463 0.0156 0.0266 -0.0681 158 VAL A C 921 O O . VAL A 165 ? 0.2838 0.2560 0.3348 0.0178 0.0281 -0.0657 158 VAL A O 922 C CB . VAL A 165 ? 0.2769 0.2473 0.3256 0.0114 0.0233 -0.0597 158 VAL A CB 923 C CG1 . VAL A 165 ? 0.2683 0.2443 0.3135 0.0131 0.0246 -0.0566 158 VAL A CG1 924 C CG2 . VAL A 165 ? 0.2841 0.2560 0.3273 0.0087 0.0217 -0.0635 158 VAL A CG2 925 N N . PRO A 166 ? 0.3020 0.2697 0.3487 0.0152 0.0268 -0.0746 159 PRO A N 926 C CA . PRO A 166 ? 0.3144 0.2852 0.3576 0.0175 0.0299 -0.0780 159 PRO A CA 927 C C . PRO A 166 ? 0.3017 0.2792 0.3384 0.0166 0.0309 -0.0753 159 PRO A C 928 O O . PRO A 166 ? 0.3012 0.2802 0.3343 0.0141 0.0288 -0.0723 159 PRO A O 929 C CB . PRO A 166 ? 0.3309 0.2982 0.3699 0.0173 0.0296 -0.0854 159 PRO A CB 930 C CG . PRO A 166 ? 0.3371 0.3018 0.3749 0.0141 0.0256 -0.0854 159 PRO A CG 931 C CD . PRO A 166 ? 0.3228 0.2862 0.3686 0.0131 0.0243 -0.0791 159 PRO A CD 932 N N . PRO A 167 ? 0.2937 0.2752 0.3297 0.0186 0.0344 -0.0763 160 PRO A N 933 C CA . PRO A 167 ? 0.2880 0.2755 0.3187 0.0176 0.0357 -0.0737 160 PRO A CA 934 C C . PRO A 167 ? 0.2771 0.2645 0.2975 0.0153 0.0348 -0.0755 160 PRO A C 935 O O . PRO A 167 ? 0.2878 0.2721 0.3035 0.0156 0.0350 -0.0808 160 PRO A O 936 C CB . PRO A 167 ? 0.2865 0.2772 0.3194 0.0202 0.0403 -0.0760 160 PRO A CB 937 C CG . PRO A 167 ? 0.2843 0.2716 0.3266 0.0230 0.0401 -0.0771 160 PRO A CG 938 C CD . PRO A 167 ? 0.2982 0.2790 0.3392 0.0219 0.0374 -0.0798 160 PRO A CD 939 N N . PHE A 168 ? 0.2673 0.2579 0.2843 0.0132 0.0334 -0.0712 161 PHE A N 940 C CA . PHE A 168 ? 0.2682 0.2591 0.2754 0.0112 0.0322 -0.0720 161 PHE A CA 941 C C . PHE A 168 ? 0.2664 0.2619 0.2717 0.0098 0.0320 -0.0667 161 PHE A C 942 O O . PHE A 168 ? 0.2611 0.2586 0.2728 0.0101 0.0317 -0.0626 161 PHE A O 943 C CB . PHE A 168 ? 0.2711 0.2578 0.2776 0.0094 0.0276 -0.0737 161 PHE A CB 944 C CG . PHE A 168 ? 0.2455 0.2325 0.2571 0.0076 0.0246 -0.0685 161 PHE A CG 945 C CD1 . PHE A 168 ? 0.2419 0.2298 0.2491 0.0053 0.0215 -0.0670 161 PHE A CD1 946 C CD2 . PHE A 168 ? 0.2753 0.2613 0.2957 0.0085 0.0248 -0.0653 161 PHE A CD2 947 C CE1 . PHE A 168 ? 0.2478 0.2361 0.2599 0.0038 0.0193 -0.0624 161 PHE A CE1 948 C CE2 . PHE A 168 ? 0.2540 0.2400 0.2780 0.0072 0.0226 -0.0604 161 PHE A CE2 949 C CZ . PHE A 168 ? 0.2570 0.2442 0.2771 0.0048 0.0201 -0.0590 161 PHE A CZ 950 N N . SER A 169 ? 0.2670 0.2636 0.2630 0.0086 0.0320 -0.0669 162 SER A N 951 C CA . SER A 169 ? 0.2552 0.2553 0.2489 0.0071 0.0314 -0.0619 162 SER A CA 952 C C . SER A 169 ? 0.2524 0.2509 0.2439 0.0051 0.0266 -0.0606 162 SER A C 953 O O . SER A 169 ? 0.2748 0.2714 0.2591 0.0044 0.0248 -0.0633 162 SER A O 954 C CB . SER A 169 ? 0.2659 0.2680 0.2509 0.0072 0.0348 -0.0623 162 SER A CB 955 O OG . SER A 169 ? 0.2740 0.2783 0.2625 0.0090 0.0400 -0.0633 162 SER A OG 956 N N . ALA A 170 ? 0.2551 0.2545 0.2526 0.0044 0.0246 -0.0565 163 ALA A N 957 C CA . ALA A 170 ? 0.2522 0.2503 0.2497 0.0026 0.0206 -0.0551 163 ALA A CA 958 C C . ALA A 170 ? 0.2598 0.2597 0.2492 0.0013 0.0192 -0.0540 163 ALA A C 959 O O . ALA A 170 ? 0.2452 0.2480 0.2318 0.0013 0.0210 -0.0511 163 ALA A O 960 C CB . ALA A 170 ? 0.2539 0.2526 0.2585 0.0026 0.0197 -0.0505 163 ALA A CB 961 N N . PHE A 171 ? 0.2605 0.2583 0.2467 0.0002 0.0159 -0.0565 164 PHE A N 962 C CA . PHE A 171 ? 0.2625 0.2610 0.2411 -0.0008 0.0132 -0.0560 164 PHE A CA 963 C C . PHE A 171 ? 0.2813 0.2787 0.2489 0.0002 0.0145 -0.0593 164 PHE A C 964 O O . PHE A 171 ? 0.2825 0.2799 0.2422 -0.0002 0.0122 -0.0590 164 PHE A O 965 C CB . PHE A 171 ? 0.2518 0.2535 0.2306 -0.0016 0.0128 -0.0505 164 PHE A CB 966 C CG . PHE A 171 ? 0.2521 0.2542 0.2397 -0.0022 0.0113 -0.0475 164 PHE A CG 967 C CD1 . PHE A 171 ? 0.2589 0.2604 0.2493 -0.0035 0.0076 -0.0477 164 PHE A CD1 968 C CD2 . PHE A 171 ? 0.2431 0.2463 0.2363 -0.0013 0.0137 -0.0445 164 PHE A CD2 969 C CE1 . PHE A 171 ? 0.2383 0.2401 0.2367 -0.0039 0.0072 -0.0445 164 PHE A CE1 970 C CE2 . PHE A 171 ? 0.2353 0.2384 0.2350 -0.0013 0.0128 -0.0414 164 PHE A CE2 971 C CZ . PHE A 171 ? 0.2305 0.2329 0.2328 -0.0027 0.0100 -0.0411 164 PHE A CZ 972 N N . SER A 172 ? 0.2819 0.2780 0.2487 0.0017 0.0179 -0.0626 165 SER A N 973 C CA . SER A 172 ? 0.3057 0.3000 0.2611 0.0031 0.0193 -0.0663 165 SER A CA 974 C C . SER A 172 ? 0.3143 0.3054 0.2641 0.0028 0.0138 -0.0704 165 SER A C 975 O O . SER A 172 ? 0.3252 0.3145 0.2823 0.0020 0.0102 -0.0727 165 SER A O 976 C CB . SER A 172 ? 0.3129 0.3056 0.2693 0.0051 0.0234 -0.0705 165 SER A CB 977 O OG . SER A 172 ? 0.3298 0.3202 0.2736 0.0067 0.0248 -0.0741 165 SER A OG 978 N N . PRO A 173 ? 0.3279 0.3180 0.2650 0.0036 0.0129 -0.0711 166 PRO A N 979 C CA . PRO A 173 ? 0.3417 0.3283 0.2730 0.0040 0.0072 -0.0762 166 PRO A CA 980 C C . PRO A 173 ? 0.3592 0.3418 0.2874 0.0060 0.0084 -0.0828 166 PRO A C 981 O O . PRO A 173 ? 0.3497 0.3326 0.2784 0.0073 0.0142 -0.0832 166 PRO A O 982 C CB . PRO A 173 ? 0.3546 0.3407 0.2713 0.0050 0.0066 -0.0747 166 PRO A CB 983 C CG . PRO A 173 ? 0.3596 0.3474 0.2723 0.0059 0.0143 -0.0711 166 PRO A CG 984 C CD . PRO A 173 ? 0.3392 0.3308 0.2669 0.0043 0.0167 -0.0675 166 PRO A CD 985 N N . GLN A 174 ? 0.3672 0.3463 0.2928 0.0063 0.0025 -0.0884 167 GLN A N 986 C CA . GLN A 174 ? 0.3909 0.3654 0.3119 0.0085 0.0026 -0.0957 167 GLN A CA 987 C C . GLN A 174 ? 0.4136 0.3858 0.3164 0.0115 0.0051 -0.0977 167 GLN A C 988 O O . GLN A 174 ? 0.4285 0.4014 0.3214 0.0118 0.0040 -0.0947 167 GLN A O 989 C CB . GLN A 174 ? 0.4021 0.3736 0.3274 0.0076 -0.0053 -0.1011 167 GLN A CB 990 C CG . GLN A 174 ? 0.4176 0.3905 0.3611 0.0047 -0.0070 -0.0993 167 GLN A CG 991 C CD . GLN A 174 ? 0.5080 0.4782 0.4581 0.0033 -0.0147 -0.1043 167 GLN A CD 992 O OE1 . GLN A 174 ? 0.5678 0.5350 0.5086 0.0046 -0.0197 -0.1098 167 GLN A OE1 993 N NE2 . GLN A 174 ? 0.4969 0.4679 0.4631 0.0008 -0.0155 -0.1025 167 GLN A NE2 994 N N . GLY A 175 ? 0.4187 0.3879 0.3169 0.0141 0.0087 -0.1027 168 GLY A N 995 C CA . GLY A 175 ? 0.4409 0.4070 0.3205 0.0176 0.0114 -0.1053 168 GLY A CA 996 C C . GLY A 175 ? 0.4515 0.4152 0.3297 0.0203 0.0171 -0.1100 168 GLY A C 997 O O . GLY A 175 ? 0.4435 0.4090 0.3354 0.0194 0.0201 -0.1096 168 GLY A O 998 N N . MET A 176 ? 0.4757 0.4351 0.3366 0.0240 0.0186 -0.1144 169 MET A N 999 C CA . MET A 176 ? 0.4898 0.4471 0.3471 0.0273 0.0254 -0.1186 169 MET A CA 1000 C C . MET A 176 ? 0.5048 0.4618 0.3453 0.0303 0.0329 -0.1162 169 MET A C 1001 O O . MET A 176 ? 0.5372 0.4891 0.3624 0.0344 0.0346 -0.1218 169 MET A O 1002 C CB . MET A 176 ? 0.5076 0.4584 0.3611 0.0296 0.0201 -0.1284 169 MET A CB 1003 C CG . MET A 176 ? 0.5342 0.4847 0.4066 0.0269 0.0150 -0.1311 169 MET A CG 1004 S SD . MET A 176 ? 0.6767 0.6190 0.5440 0.0298 0.0093 -0.1432 169 MET A SD 1005 C CE . MET A 176 ? 0.6363 0.5786 0.5263 0.0254 0.0019 -0.1440 169 MET A CE 1006 N N . PRO A 177 ? 0.4911 0.4532 0.3341 0.0285 0.0378 -0.1079 170 PRO A N 1007 C CA . PRO A 177 ? 0.5097 0.4715 0.3378 0.0309 0.0455 -0.1046 170 PRO A CA 1008 C C . PRO A 177 ? 0.5282 0.4895 0.3545 0.0342 0.0549 -0.1075 170 PRO A C 1009 O O . PRO A 177 ? 0.5165 0.4809 0.3586 0.0333 0.0577 -0.1082 170 PRO A O 1010 C CB . PRO A 177 ? 0.4916 0.4594 0.3289 0.0274 0.0482 -0.0953 170 PRO A CB 1011 C CG . PRO A 177 ? 0.4717 0.4436 0.3299 0.0241 0.0453 -0.0946 170 PRO A CG 1012 C CD . PRO A 177 ? 0.4685 0.4365 0.3286 0.0242 0.0369 -0.1013 170 PRO A CD 1013 N N A GLU A 178 ? 0.5518 0.5089 0.3586 0.0383 0.0596 -0.1093 171 GLU A N 1014 N N B GLU A 178 ? 0.5477 0.5050 0.3548 0.0382 0.0599 -0.1090 171 GLU A N 1015 C CA A GLU A 178 ? 0.5706 0.5272 0.3735 0.0419 0.0698 -0.1115 171 GLU A CA 1016 C CA B GLU A 178 ? 0.5615 0.5183 0.3655 0.0418 0.0699 -0.1117 171 GLU A CA 1017 C C A GLU A 178 ? 0.5721 0.5307 0.3662 0.0426 0.0789 -0.1044 171 GLU A C 1018 C C B GLU A 178 ? 0.5698 0.5273 0.3615 0.0436 0.0795 -0.1059 171 GLU A C 1019 O O A GLU A 178 ? 0.5837 0.5395 0.3630 0.0430 0.0768 -0.1012 171 GLU A O 1020 O O B GLU A 178 ? 0.5844 0.5372 0.3564 0.0457 0.0783 -0.1053 171 GLU A O 1021 C CB A GLU A 178 ? 0.5947 0.5437 0.3798 0.0470 0.0683 -0.1204 171 GLU A CB 1022 C CB B GLU A 178 ? 0.5807 0.5304 0.3723 0.0462 0.0671 -0.1215 171 GLU A CB 1023 C CG A GLU A 178 ? 0.6257 0.5706 0.4144 0.0467 0.0575 -0.1282 171 GLU A CG 1024 C CG B GLU A 178 ? 0.6018 0.5504 0.3879 0.0506 0.0778 -0.1246 171 GLU A CG 1025 C CD A GLU A 178 ? 0.6614 0.5984 0.4322 0.0521 0.0562 -0.1375 171 GLU A CD 1026 C CD B GLU A 178 ? 0.6467 0.5869 0.4134 0.0560 0.0758 -0.1337 171 GLU A CD 1027 O OE1 A GLU A 178 ? 0.6880 0.6209 0.4613 0.0521 0.0472 -0.1448 171 GLU A OE1 1028 O OE1 B GLU A 178 ? 0.6694 0.6063 0.4164 0.0602 0.0823 -0.1334 171 GLU A OE1 1029 O OE2 A GLU A 178 ? 0.6995 0.6340 0.4538 0.0564 0.0644 -0.1377 171 GLU A OE2 1030 O OE2 B GLU A 178 ? 0.6585 0.5953 0.4296 0.0562 0.0678 -0.1411 171 GLU A OE2 1031 N N . GLY A 179 ? 0.5629 0.5260 0.3662 0.0428 0.0892 -0.1017 172 GLY A N 1032 C CA . GLY A 179 ? 0.5670 0.5316 0.3624 0.0437 0.0992 -0.0953 172 GLY A CA 1033 C C . GLY A 179 ? 0.5534 0.5238 0.3626 0.0437 0.1103 -0.0928 172 GLY A C 1034 O O . GLY A 179 ? 0.5513 0.5241 0.3742 0.0441 0.1110 -0.0971 172 GLY A O 1035 N N . ASP A 180 ? 0.5439 0.5166 0.3501 0.0433 0.1188 -0.0858 173 ASP A N 1036 C CA . ASP A 180 ? 0.5428 0.5217 0.3630 0.0430 0.1300 -0.0826 173 ASP A CA 1037 C C . ASP A 180 ? 0.5104 0.4967 0.3533 0.0376 0.1274 -0.0769 173 ASP A C 1038 O O . ASP A 180 ? 0.5013 0.4876 0.3434 0.0345 0.1215 -0.0722 173 ASP A O 1039 C CB . ASP A 180 ? 0.5624 0.5396 0.3683 0.0452 0.1411 -0.0777 173 ASP A CB 1040 C CG . ASP A 180 ? 0.6100 0.5791 0.3908 0.0512 0.1441 -0.0831 173 ASP A CG 1041 O OD1 . ASP A 180 ? 0.6471 0.6143 0.4276 0.0541 0.1428 -0.0911 173 ASP A OD1 1042 O OD2 . ASP A 180 ? 0.6358 0.6001 0.3968 0.0531 0.1476 -0.0794 173 ASP A OD2 1043 N N . LEU A 181 ? 0.4918 0.4842 0.3544 0.0370 0.1317 -0.0776 174 LEU A N 1044 C CA . LEU A 181 ? 0.4680 0.4676 0.3528 0.0327 0.1296 -0.0730 174 LEU A CA 1045 C C . LEU A 181 ? 0.4677 0.4716 0.3577 0.0306 0.1376 -0.0652 174 LEU A C 1046 O O . LEU A 181 ? 0.4797 0.4840 0.3654 0.0328 0.1487 -0.0640 174 LEU A O 1047 C CB . LEU A 181 ? 0.4624 0.4666 0.3659 0.0335 0.1311 -0.0770 174 LEU A CB 1048 C CG A LEU A 181 ? 0.4467 0.4547 0.3695 0.0310 0.1231 -0.0778 174 LEU A CG 1049 C CG B LEU A 181 ? 0.4397 0.4410 0.3459 0.0346 0.1229 -0.0839 174 LEU A CG 1050 C CD1 A LEU A 181 ? 0.4359 0.4399 0.3534 0.0289 0.1113 -0.0784 174 LEU A CD1 1051 C CD1 B LEU A 181 ? 0.4253 0.4317 0.3509 0.0357 0.1261 -0.0864 174 LEU A CD1 1052 C CD2 A LEU A 181 ? 0.4434 0.4522 0.3752 0.0340 0.1250 -0.0840 174 LEU A CD2 1053 C CD2 B LEU A 181 ? 0.4234 0.4237 0.3325 0.0311 0.1112 -0.0825 174 LEU A CD2 1054 N N . VAL A 182 ? 0.4510 0.4580 0.3512 0.0263 0.1324 -0.0601 175 VAL A N 1055 C CA . VAL A 182 ? 0.4414 0.4539 0.3540 0.0236 0.1386 -0.0533 175 VAL A CA 1056 C C . VAL A 182 ? 0.4251 0.4441 0.3610 0.0207 0.1332 -0.0532 175 VAL A C 1057 O O . VAL A 182 ? 0.4112 0.4290 0.3489 0.0192 0.1230 -0.0544 175 VAL A O 1058 C CB . VAL A 182 ? 0.4485 0.4580 0.3501 0.0214 0.1374 -0.0469 175 VAL A CB 1059 C CG1 . VAL A 182 ? 0.4278 0.4430 0.3458 0.0178 0.1417 -0.0402 175 VAL A CG1 1060 C CG2 . VAL A 182 ? 0.4671 0.4702 0.3453 0.0248 0.1440 -0.0464 175 VAL A CG2 1061 N N . TYR A 183 ? 0.4033 0.4288 0.3569 0.0202 0.1400 -0.0518 176 TYR A N 1062 C CA . TYR A 183 ? 0.3811 0.4127 0.3568 0.0178 0.1351 -0.0513 176 TYR A CA 1063 C C . TYR A 183 ? 0.3773 0.4116 0.3603 0.0138 0.1339 -0.0447 176 TYR A C 1064 O O . TYR A 183 ? 0.3877 0.4234 0.3713 0.0129 0.1421 -0.0404 176 TYR A O 1065 C CB . TYR A 183 ? 0.3812 0.4188 0.3737 0.0197 0.1420 -0.0539 176 TYR A CB 1066 C CG . TYR A 183 ? 0.3520 0.3967 0.3683 0.0174 0.1382 -0.0526 176 TYR A CG 1067 C CD1 . TYR A 183 ? 0.3475 0.3918 0.3695 0.0169 0.1276 -0.0548 176 TYR A CD1 1068 C CD2 . TYR A 183 ? 0.3784 0.4296 0.4112 0.0160 0.1450 -0.0493 176 TYR A CD2 1069 C CE1 . TYR A 183 ? 0.3530 0.4032 0.3954 0.0155 0.1235 -0.0537 176 TYR A CE1 1070 C CE2 . TYR A 183 ? 0.3769 0.4345 0.4315 0.0143 0.1406 -0.0487 176 TYR A CE2 1071 C CZ . TYR A 183 ? 0.3452 0.4019 0.4034 0.0142 0.1297 -0.0510 176 TYR A CZ 1072 O OH . TYR A 183 ? 0.3207 0.3832 0.3990 0.0131 0.1250 -0.0505 176 TYR A OH 1073 N N . VAL A 184 ? 0.3566 0.3912 0.3450 0.0115 0.1238 -0.0439 177 VAL A N 1074 C CA . VAL A 184 ? 0.3636 0.3991 0.3555 0.0079 0.1211 -0.0382 177 VAL A CA 1075 C C . VAL A 184 ? 0.3446 0.3862 0.3583 0.0058 0.1168 -0.0374 177 VAL A C 1076 O O . VAL A 184 ? 0.3441 0.3856 0.3607 0.0032 0.1110 -0.0342 177 VAL A O 1077 C CB . VAL A 184 ? 0.3661 0.3955 0.3420 0.0071 0.1130 -0.0372 177 VAL A CB 1078 C CG1 . VAL A 184 ? 0.4041 0.4275 0.3585 0.0093 0.1168 -0.0378 177 VAL A CG1 1079 C CG2 . VAL A 184 ? 0.3671 0.3956 0.3450 0.0076 0.1032 -0.0415 177 VAL A CG2 1080 N N . ASN A 185 ? 0.3401 0.3866 0.3686 0.0073 0.1194 -0.0405 178 ASN A N 1081 C CA . ASN A 185 ? 0.3151 0.3675 0.3643 0.0060 0.1151 -0.0404 178 ASN A CA 1082 C C . ASN A 185 ? 0.3131 0.3629 0.3598 0.0055 0.1036 -0.0412 178 ASN A C 1083 O O . ASN A 185 ? 0.3148 0.3609 0.3529 0.0074 0.0998 -0.0446 178 ASN A O 1084 C CB . ASN A 185 ? 0.3176 0.3740 0.3786 0.0030 0.1190 -0.0355 178 ASN A CB 1085 C CG . ASN A 185 ? 0.3007 0.3644 0.3857 0.0025 0.1170 -0.0364 178 ASN A CG 1086 O OD1 . ASN A 185 ? 0.3229 0.3892 0.4162 0.0050 0.1156 -0.0405 178 ASN A OD1 1087 N ND2 . ASN A 185 ? 0.3240 0.3905 0.4201 -0.0005 0.1163 -0.0328 178 ASN A ND2 1088 N N . TYR A 186 ? 0.3019 0.3532 0.3561 0.0030 0.0982 -0.0381 179 TYR A N 1089 C CA . TYR A 186 ? 0.2880 0.3369 0.3396 0.0027 0.0880 -0.0386 179 TYR A CA 1090 C C . TYR A 186 ? 0.2969 0.3400 0.3313 0.0015 0.0847 -0.0364 179 TYR A C 1091 O O . TYR A 186 ? 0.2910 0.3321 0.3231 0.0010 0.0768 -0.0362 179 TYR A O 1092 C CB . TYR A 186 ? 0.2732 0.3260 0.3404 0.0013 0.0830 -0.0369 179 TYR A CB 1093 C CG . TYR A 186 ? 0.2855 0.3442 0.3711 0.0028 0.0837 -0.0394 179 TYR A CG 1094 C CD1 . TYR A 186 ? 0.2810 0.3395 0.3699 0.0055 0.0785 -0.0429 179 TYR A CD1 1095 C CD2 . TYR A 186 ? 0.2829 0.3472 0.3837 0.0016 0.0890 -0.0382 179 TYR A CD2 1096 C CE1 . TYR A 186 ? 0.3094 0.3731 0.4154 0.0074 0.0785 -0.0451 179 TYR A CE1 1097 C CE2 . TYR A 186 ? 0.3069 0.3771 0.4260 0.0032 0.0891 -0.0407 179 TYR A CE2 1098 C CZ . TYR A 186 ? 0.2983 0.3681 0.4195 0.0062 0.0834 -0.0442 179 TYR A CZ 1099 O OH . TYR A 186 ? 0.3136 0.3890 0.4529 0.0081 0.0829 -0.0466 179 TYR A OH 1100 N N . ALA A 187 ? 0.3041 0.3444 0.3263 0.0011 0.0906 -0.0347 180 ALA A N 1101 C CA . ALA A 187 ? 0.3044 0.3393 0.3101 0.0003 0.0875 -0.0326 180 ALA A CA 1102 C C . ALA A 187 ? 0.3017 0.3367 0.3111 -0.0024 0.0822 -0.0286 180 ALA A C 1103 O O . ALA A 187 ? 0.2966 0.3279 0.2962 -0.0029 0.0765 -0.0276 180 ALA A O 1104 C CB . ALA A 187 ? 0.3031 0.3338 0.2980 0.0020 0.0819 -0.0364 180 ALA A CB 1105 N N . ARG A 188 ? 0.2966 0.3360 0.3208 -0.0039 0.0842 -0.0265 181 ARG A N 1106 C CA . ARG A 188 ? 0.2877 0.3270 0.3160 -0.0064 0.0800 -0.0229 181 ARG A CA 1107 C C . ARG A 188 ? 0.2965 0.3323 0.3146 -0.0079 0.0843 -0.0184 181 ARG A C 1108 O O . ARG A 188 ? 0.3066 0.3413 0.3176 -0.0073 0.0920 -0.0176 181 ARG A O 1109 C CB . ARG A 188 ? 0.2841 0.3290 0.3323 -0.0075 0.0803 -0.0226 181 ARG A CB 1110 C CG . ARG A 188 ? 0.2888 0.3368 0.3474 -0.0057 0.0752 -0.0265 181 ARG A CG 1111 C CD . ARG A 188 ? 0.2777 0.3317 0.3562 -0.0062 0.0763 -0.0269 181 ARG A CD 1112 N NE . ARG A 188 ? 0.2844 0.3416 0.3689 -0.0063 0.0860 -0.0269 181 ARG A NE 1113 C CZ . ARG A 188 ? 0.3213 0.3845 0.4244 -0.0067 0.0892 -0.0274 181 ARG A CZ 1114 N NH1 . ARG A 188 ? 0.3172 0.3838 0.4351 -0.0070 0.0826 -0.0284 181 ARG A NH1 1115 N NH2 . ARG A 188 ? 0.3067 0.3725 0.4139 -0.0067 0.0990 -0.0270 181 ARG A NH2 1116 N N . THR A 189 ? 0.2844 0.3185 0.3020 -0.0098 0.0796 -0.0153 182 THR A N 1117 C CA . THR A 189 ? 0.2995 0.3300 0.3088 -0.0113 0.0834 -0.0106 182 THR A CA 1118 C C . THR A 189 ? 0.3137 0.3465 0.3305 -0.0123 0.0934 -0.0081 182 THR A C 1119 O O . THR A 189 ? 0.3307 0.3602 0.3360 -0.0119 0.1002 -0.0054 182 THR A O 1120 C CB . THR A 189 ? 0.3006 0.3297 0.3129 -0.0132 0.0771 -0.0079 182 THR A CB 1121 O OG1 . THR A 189 ? 0.3048 0.3316 0.3088 -0.0120 0.0690 -0.0098 182 THR A OG1 1122 C CG2 . THR A 189 ? 0.3078 0.3326 0.3119 -0.0147 0.0812 -0.0025 182 THR A CG2 1123 N N . GLU A 190 ? 0.3173 0.3558 0.3535 -0.0134 0.0945 -0.0090 183 GLU A N 1124 C CA . GLU A 190 ? 0.3338 0.3753 0.3805 -0.0148 0.1040 -0.0064 183 GLU A CA 1125 C C . GLU A 190 ? 0.3413 0.3840 0.3839 -0.0125 0.1123 -0.0085 183 GLU A C 1126 O O . GLU A 190 ? 0.3517 0.3949 0.3956 -0.0130 0.1221 -0.0056 183 GLU A O 1127 C CB . GLU A 190 ? 0.3253 0.3728 0.3956 -0.0167 0.1021 -0.0072 183 GLU A CB 1128 C CG . GLU A 190 ? 0.3558 0.4081 0.4365 -0.0147 0.0975 -0.0127 183 GLU A CG 1129 C CD . GLU A 190 ? 0.3630 0.4145 0.4444 -0.0143 0.0859 -0.0148 183 GLU A CD 1130 O OE1 . GLU A 190 ? 0.3339 0.3802 0.4015 -0.0144 0.0810 -0.0133 183 GLU A OE1 1131 O OE2 . GLU A 190 ? 0.3411 0.3971 0.4370 -0.0135 0.0819 -0.0179 183 GLU A OE2 1132 N N . ASP A 191 ? 0.3334 0.3764 0.3710 -0.0098 0.1086 -0.0134 184 ASP A N 1133 C CA . ASP A 191 ? 0.3429 0.3863 0.3749 -0.0071 0.1160 -0.0160 184 ASP A CA 1134 C C . ASP A 191 ? 0.3589 0.3957 0.3687 -0.0060 0.1205 -0.0138 184 ASP A C 1135 O O . ASP A 191 ? 0.3621 0.3986 0.3673 -0.0047 0.1303 -0.0129 184 ASP A O 1136 C CB . ASP A 191 ? 0.3325 0.3767 0.3643 -0.0045 0.1103 -0.0219 184 ASP A CB 1137 C CG . ASP A 191 ? 0.3240 0.3745 0.3769 -0.0048 0.1069 -0.0244 184 ASP A CG 1138 O OD1 . ASP A 191 ? 0.3140 0.3696 0.3829 -0.0059 0.1124 -0.0231 184 ASP A OD1 1139 O OD2 . ASP A 191 ? 0.2871 0.3375 0.3411 -0.0036 0.0988 -0.0275 184 ASP A OD2 1140 N N A PHE A 192 ? 0.3525 0.3841 0.3483 -0.0061 0.1134 -0.0129 185 PHE A N 1141 N N B PHE A 192 ? 0.3525 0.3841 0.3483 -0.0061 0.1134 -0.0129 185 PHE A N 1142 C CA A PHE A 192 ? 0.3677 0.3928 0.3421 -0.0048 0.1161 -0.0107 185 PHE A CA 1143 C CA B PHE A 192 ? 0.3677 0.3928 0.3420 -0.0048 0.1162 -0.0107 185 PHE A CA 1144 C C A PHE A 192 ? 0.3795 0.4026 0.3525 -0.0067 0.1230 -0.0040 185 PHE A C 1145 C C B PHE A 192 ? 0.3795 0.4028 0.3528 -0.0067 0.1232 -0.0040 185 PHE A C 1146 O O A PHE A 192 ? 0.3978 0.4167 0.3561 -0.0050 0.1300 -0.0018 185 PHE A O 1147 O O B PHE A 192 ? 0.3974 0.4167 0.3565 -0.0050 0.1305 -0.0018 185 PHE A O 1148 C CB A PHE A 192 ? 0.3599 0.3804 0.3212 -0.0042 0.1060 -0.0120 185 PHE A CB 1149 C CB B PHE A 192 ? 0.3602 0.3808 0.3214 -0.0042 0.1062 -0.0120 185 PHE A CB 1150 C CG A PHE A 192 ? 0.3506 0.3707 0.3065 -0.0017 0.1020 -0.0181 185 PHE A CG 1151 C CG B PHE A 192 ? 0.3507 0.3708 0.3065 -0.0017 0.1021 -0.0181 185 PHE A CG 1152 C CD1 A PHE A 192 ? 0.3426 0.3654 0.3084 -0.0020 0.0942 -0.0215 185 PHE A CD1 1153 C CD1 B PHE A 192 ? 0.3426 0.3654 0.3085 -0.0020 0.0943 -0.0215 185 PHE A CD1 1154 C CD2 A PHE A 192 ? 0.3559 0.3726 0.2969 0.0013 0.1063 -0.0206 185 PHE A CD2 1155 C CD2 B PHE A 192 ? 0.3556 0.3722 0.2964 0.0013 0.1064 -0.0206 185 PHE A CD2 1156 C CE1 A PHE A 192 ? 0.3411 0.3631 0.3029 0.0002 0.0908 -0.0268 185 PHE A CE1 1157 C CE1 B PHE A 192 ? 0.3413 0.3633 0.3032 0.0002 0.0909 -0.0268 185 PHE A CE1 1158 C CE2 A PHE A 192 ? 0.3616 0.3775 0.2985 0.0035 0.1024 -0.0266 185 PHE A CE2 1159 C CE2 B PHE A 192 ? 0.3618 0.3776 0.2987 0.0036 0.1024 -0.0266 185 PHE A CE2 1160 C CZ A PHE A 192 ? 0.3486 0.3671 0.2964 0.0028 0.0948 -0.0295 185 PHE A CZ 1161 C CZ B PHE A 192 ? 0.3487 0.3672 0.2967 0.0028 0.0949 -0.0295 185 PHE A CZ 1162 N N . PHE A 193 ? 0.3746 0.4004 0.3627 -0.0099 0.1212 -0.0009 186 PHE A N 1163 C CA . PHE A 193 ? 0.3930 0.4174 0.3839 -0.0121 0.1287 0.0056 186 PHE A CA 1164 C C . PHE A 193 ? 0.4133 0.4404 0.4092 -0.0114 0.1411 0.0065 186 PHE A C 1165 O O . PHE A 193 ? 0.4261 0.4490 0.4107 -0.0108 0.1498 0.0110 186 PHE A O 1166 C CB . PHE A 193 ? 0.3816 0.4093 0.3922 -0.0158 0.1248 0.0077 186 PHE A CB 1167 C CG . PHE A 193 ? 0.3855 0.4091 0.3902 -0.0169 0.1152 0.0092 186 PHE A CG 1168 C CD1 . PHE A 193 ? 0.4102 0.4274 0.3938 -0.0152 0.1120 0.0103 186 PHE A CD1 1169 C CD2 . PHE A 193 ? 0.3681 0.3945 0.3894 -0.0194 0.1093 0.0093 186 PHE A CD2 1170 C CE1 . PHE A 193 ? 0.4073 0.4212 0.3870 -0.0160 0.1033 0.0116 186 PHE A CE1 1171 C CE2 . PHE A 193 ? 0.3705 0.3932 0.3868 -0.0202 0.1008 0.0106 186 PHE A CE2 1172 C CZ . PHE A 193 ? 0.3762 0.3929 0.3721 -0.0185 0.0982 0.0119 186 PHE A CZ 1173 N N . LYS A 194 ? 0.4109 0.4449 0.4236 -0.0111 0.1422 0.0022 187 LYS A N 1174 C CA . LYS A 194 ? 0.4242 0.4622 0.4454 -0.0104 0.1541 0.0025 187 LYS A CA 1175 C C . LYS A 194 ? 0.4509 0.4841 0.4502 -0.0064 0.1607 0.0015 187 LYS A C 1176 O O . LYS A 194 ? 0.4683 0.5003 0.4635 -0.0058 0.1723 0.0052 187 LYS A O 1177 C CB . LYS A 194 ? 0.4136 0.4597 0.4562 -0.0102 0.1521 -0.0027 187 LYS A CB 1178 C CG . LYS A 194 ? 0.4358 0.4872 0.4897 -0.0090 0.1640 -0.0034 187 LYS A CG 1179 C CD . LYS A 194 ? 0.4767 0.5332 0.5531 -0.0126 0.1704 0.0008 187 LYS A CD 1180 C CE . LYS A 194 ? 0.4806 0.5437 0.5809 -0.0147 0.1614 -0.0021 187 LYS A CE 1181 N NZ . LYS A 194 ? 0.5051 0.5729 0.6281 -0.0184 0.1661 0.0015 187 LYS A NZ 1182 N N . LEU A 195 ? 0.4454 0.4757 0.4305 -0.0037 0.1536 -0.0034 188 LEU A N 1183 C CA . LEU A 195 ? 0.4772 0.5024 0.4406 0.0003 0.1584 -0.0053 188 LEU A CA 1184 C C . LEU A 195 ? 0.5029 0.5203 0.4453 0.0011 0.1625 0.0002 188 LEU A C 1185 O O . LEU A 195 ? 0.5159 0.5309 0.4483 0.0033 0.1732 0.0022 188 LEU A O 1186 C CB . LEU A 195 ? 0.4703 0.4933 0.4236 0.0027 0.1485 -0.0117 188 LEU A CB 1187 C CG . LEU A 195 ? 0.4771 0.5057 0.4447 0.0037 0.1461 -0.0180 188 LEU A CG 1188 C CD1 . LEU A 195 ? 0.4794 0.5051 0.4390 0.0047 0.1344 -0.0227 188 LEU A CD1 1189 C CD2 . LEU A 195 ? 0.4913 0.5209 0.4565 0.0070 0.1563 -0.0207 188 LEU A CD2 1190 N N A GLU A 196 ? 0.5050 0.5182 0.4396 -0.0004 0.1541 0.0027 189 GLU A N 1191 N N B GLU A 196 ? 0.4967 0.5103 0.4327 -0.0006 0.1543 0.0029 189 GLU A N 1192 C CA A GLU A 196 ? 0.5396 0.5448 0.4525 0.0008 0.1568 0.0079 189 GLU A CA 1193 C CA B GLU A 196 ? 0.5184 0.5238 0.4323 0.0006 0.1558 0.0077 189 GLU A CA 1194 C C A GLU A 196 ? 0.5395 0.5438 0.4582 -0.0016 0.1657 0.0159 189 GLU A C 1195 C C B GLU A 196 ? 0.5272 0.5315 0.4457 -0.0017 0.1651 0.0157 189 GLU A C 1196 O O A GLU A 196 ? 0.5656 0.5646 0.4687 0.0004 0.1745 0.0201 189 GLU A O 1197 O O B GLU A 196 ? 0.5502 0.5489 0.4522 0.0005 0.1735 0.0198 189 GLU A O 1198 C CB A GLU A 196 ? 0.5482 0.5481 0.4468 0.0012 0.1448 0.0072 189 GLU A CB 1199 C CB B GLU A 196 ? 0.5082 0.5102 0.4150 -0.0002 0.1430 0.0071 189 GLU A CB 1200 C CG A GLU A 196 ? 0.5854 0.5892 0.4979 -0.0013 0.1332 0.0043 189 GLU A CG 1201 C CG B GLU A 196 ? 0.5029 0.5095 0.4204 -0.0006 0.1332 0.0006 189 GLU A CG 1202 C CD A GLU A 196 ? 0.6475 0.6507 0.5525 0.0010 0.1241 -0.0028 189 GLU A CD 1203 C CD B GLU A 196 ? 0.5028 0.5070 0.4062 0.0031 0.1295 -0.0058 189 GLU A CD 1204 O OE1 A GLU A 196 ? 0.6765 0.6741 0.5641 0.0026 0.1182 -0.0032 189 GLU A OE1 1205 O OE1 B GLU A 196 ? 0.4838 0.4886 0.3889 0.0028 0.1193 -0.0097 189 GLU A OE1 1206 O OE2 A GLU A 196 ? 0.6287 0.6370 0.5462 0.0011 0.1227 -0.0078 189 GLU A OE2 1207 O OE2 B GLU A 196 ? 0.5083 0.5098 0.3991 0.0062 0.1367 -0.0070 189 GLU A OE2 1208 N N . ARG A 197 ? 0.5178 0.5271 0.4587 -0.0059 0.1636 0.0180 190 ARG A N 1209 C CA . ARG A 197 ? 0.5225 0.5307 0.4711 -0.0088 0.1710 0.0257 190 ARG A CA 1210 C C . ARG A 197 ? 0.5321 0.5447 0.4936 -0.0093 0.1847 0.0277 190 ARG A C 1211 O O . ARG A 197 ? 0.5537 0.5624 0.5089 -0.0093 0.1951 0.0342 190 ARG A O 1212 C CB . ARG A 197 ? 0.5046 0.5155 0.4714 -0.0131 0.1626 0.0269 190 ARG A CB 1213 C CG . ARG A 197 ? 0.4703 0.4764 0.4244 -0.0127 0.1504 0.0261 190 ARG A CG 1214 C CD . ARG A 197 ? 0.4455 0.4548 0.4182 -0.0164 0.1420 0.0261 190 ARG A CD 1215 N NE . ARG A 197 ? 0.4407 0.4450 0.4010 -0.0160 0.1317 0.0264 190 ARG A NE 1216 C CZ . ARG A 197 ? 0.4311 0.4359 0.4016 -0.0185 0.1241 0.0271 190 ARG A CZ 1217 N NH1 . ARG A 197 ? 0.4188 0.4284 0.4117 -0.0217 0.1248 0.0275 190 ARG A NH1 1218 N NH2 . ARG A 197 ? 0.4359 0.4361 0.3943 -0.0176 0.1155 0.0273 190 ARG A NH2 1219 N N . ASP A 198 ? 0.5245 0.5453 0.5045 -0.0095 0.1850 0.0224 191 ASP A N 1220 C CA . ASP A 198 ? 0.5400 0.5665 0.5364 -0.0101 0.1976 0.0237 191 ASP A CA 1221 C C . ASP A 198 ? 0.5444 0.5702 0.5277 -0.0055 0.2064 0.0208 191 ASP A C 1222 O O . ASP A 198 ? 0.5558 0.5806 0.5366 -0.0046 0.2199 0.0252 191 ASP A O 1223 C CB . ASP A 198 ? 0.5265 0.5627 0.5531 -0.0129 0.1936 0.0200 191 ASP A CB 1224 C CG . ASP A 198 ? 0.5717 0.6085 0.6116 -0.0172 0.1848 0.0221 191 ASP A CG 1225 O OD1 . ASP A 198 ? 0.6241 0.6551 0.6565 -0.0189 0.1862 0.0283 191 ASP A OD1 1226 O OD2 . ASP A 198 ? 0.6088 0.6514 0.6660 -0.0185 0.1762 0.0175 191 ASP A OD2 1227 N N . MET A 199 ? 0.5315 0.5575 0.5064 -0.0024 0.1993 0.0136 192 MET A N 1228 C CA . MET A 199 ? 0.5452 0.5707 0.5089 0.0022 0.2067 0.0096 192 MET A CA 1229 C C . MET A 199 ? 0.5623 0.5781 0.4935 0.0063 0.2082 0.0105 192 MET A C 1230 O O . MET A 199 ? 0.5738 0.5876 0.4925 0.0106 0.2163 0.0083 192 MET A O 1231 C CB . MET A 199 ? 0.5322 0.5627 0.5046 0.0037 0.1991 0.0011 192 MET A CB 1232 C CG . MET A 199 ? 0.5264 0.5666 0.5298 0.0007 0.1975 -0.0006 192 MET A CG 1233 S SD . MET A 199 ? 0.5428 0.5875 0.5537 0.0033 0.1893 -0.0102 192 MET A SD 1234 C CE . MET A 199 ? 0.5499 0.5967 0.5592 0.0077 0.2039 -0.0127 192 MET A CE 1235 N N . LYS A 200 ? 0.5619 0.5714 0.4795 0.0054 0.2003 0.0136 193 LYS A N 1236 C CA . LYS A 200 ? 0.5913 0.5910 0.4780 0.0092 0.1994 0.0145 193 LYS A CA 1237 C C . LYS A 200 ? 0.6014 0.5994 0.4740 0.0136 0.1944 0.0062 193 LYS A C 1238 O O . LYS A 200 ? 0.6262 0.6181 0.4761 0.0182 0.1993 0.0054 193 LYS A O 1239 C CB . LYS A 200 ? 0.6166 0.6112 0.4903 0.0110 0.2138 0.0217 193 LYS A CB 1240 C CG . LYS A 200 ? 0.6606 0.6521 0.5372 0.0074 0.2155 0.0308 193 LYS A CG 1241 C CD . LYS A 200 ? 0.6906 0.6903 0.5991 0.0021 0.2200 0.0339 193 LYS A CD 1242 C CE . LYS A 200 ? 0.6970 0.6929 0.6081 -0.0012 0.2245 0.0434 193 LYS A CE 1243 N NZ . LYS A 200 ? 0.7019 0.6930 0.6066 -0.0030 0.2119 0.0450 193 LYS A NZ 1244 N N . ILE A 201 ? 0.5822 0.5854 0.4683 0.0124 0.1846 -0.0001 194 ILE A N 1245 C CA . ILE A 201 ? 0.5930 0.5944 0.4680 0.0161 0.1788 -0.0082 194 ILE A CA 1246 C C . ILE A 201 ? 0.5911 0.5877 0.4539 0.0158 0.1652 -0.0097 194 ILE A C 1247 O O . ILE A 201 ? 0.5752 0.5742 0.4498 0.0122 0.1574 -0.0078 194 ILE A O 1248 C CB . ILE A 201 ? 0.5802 0.5897 0.4771 0.0156 0.1777 -0.0141 194 ILE A CB 1249 C CG1 . ILE A 201 ? 0.6023 0.6152 0.5052 0.0176 0.1917 -0.0142 194 ILE A CG1 1250 C CG2 . ILE A 201 ? 0.5821 0.5896 0.4710 0.0181 0.1680 -0.0223 194 ILE A CG2 1251 C CD1 . ILE A 201 ? 0.6194 0.6418 0.5510 0.0155 0.1934 -0.0163 194 ILE A CD1 1252 N N . ASN A 202 ? 0.6086 0.5983 0.4476 0.0199 0.1627 -0.0129 195 ASN A N 1253 C CA . ASN A 202 ? 0.6173 0.6021 0.4434 0.0202 0.1503 -0.0144 195 ASN A CA 1254 C C . ASN A 202 ? 0.5975 0.5841 0.4275 0.0211 0.1412 -0.0230 195 ASN A C 1255 O O . ASN A 202 ? 0.5889 0.5739 0.4112 0.0247 0.1439 -0.0287 195 ASN A O 1256 C CB . ASN A 202 ? 0.6539 0.6294 0.4511 0.0243 0.1526 -0.0124 195 ASN A CB 1257 C CG . ASN A 202 ? 0.7071 0.6774 0.4911 0.0246 0.1399 -0.0131 195 ASN A CG 1258 O OD1 . ASN A 202 ? 0.6891 0.6628 0.4850 0.0219 0.1296 -0.0156 195 ASN A OD1 1259 N ND2 . ASN A 202 ? 0.8181 0.7803 0.5773 0.0281 0.1408 -0.0106 195 ASN A ND2 1260 N N . CYS A 203 ? 0.5679 0.5574 0.4103 0.0179 0.1308 -0.0239 196 CYS A N 1261 C CA . CYS A 203 ? 0.5558 0.5467 0.4030 0.0183 0.1219 -0.0312 196 CYS A CA 1262 C C . CYS A 203 ? 0.5601 0.5445 0.3885 0.0206 0.1130 -0.0349 196 CYS A C 1263 O O . CYS A 203 ? 0.5517 0.5363 0.3826 0.0212 0.1058 -0.0411 196 CYS A O 1264 C CB . CYS A 203 ? 0.5331 0.5300 0.4020 0.0142 0.1151 -0.0306 196 CYS A CB 1265 S SG . CYS A 203 ? 0.5336 0.5388 0.4274 0.0121 0.1228 -0.0293 196 CYS A SG 1266 N N . SER A 204 ? 0.5733 0.5519 0.3836 0.0220 0.1132 -0.0310 197 SER A N 1267 C CA . SER A 204 ? 0.5875 0.5602 0.3807 0.0241 0.1037 -0.0342 197 SER A CA 1268 C C . SER A 204 ? 0.5965 0.5660 0.3787 0.0282 0.1026 -0.0424 197 SER A C 1269 O O . SER A 204 ? 0.6196 0.5864 0.3907 0.0317 0.1112 -0.0435 197 SER A O 1270 C CB . SER A 204 ? 0.6105 0.5772 0.3851 0.0256 0.1049 -0.0283 197 SER A CB 1271 O OG . SER A 204 ? 0.6423 0.6035 0.4009 0.0279 0.0950 -0.0318 197 SER A OG 1272 N N . GLY A 205 ? 0.5798 0.5493 0.3655 0.0278 0.0921 -0.0483 198 GLY A N 1273 C CA . GLY A 205 ? 0.5723 0.5383 0.3490 0.0313 0.0896 -0.0567 198 GLY A CA 1274 C C . GLY A 205 ? 0.5585 0.5284 0.3482 0.0317 0.0953 -0.0610 198 GLY A C 1275 O O . GLY A 205 ? 0.5685 0.5352 0.3508 0.0350 0.0945 -0.0681 198 GLY A O 1276 N N . LYS A 206 ? 0.5334 0.5101 0.3427 0.0285 0.1004 -0.0571 199 LYS A N 1277 C CA . LYS A 206 ? 0.5202 0.5013 0.3441 0.0289 0.1059 -0.0606 199 LYS A CA 1278 C C . LYS A 206 ? 0.4996 0.4846 0.3418 0.0261 0.0975 -0.0634 199 LYS A C 1279 O O . LYS A 206 ? 0.4761 0.4620 0.3231 0.0231 0.0899 -0.0608 199 LYS A O 1280 C CB . LYS A 206 ? 0.5120 0.4984 0.3475 0.0274 0.1167 -0.0547 199 LYS A CB 1281 C CG . LYS A 206 ? 0.5673 0.5503 0.3869 0.0300 0.1271 -0.0507 199 LYS A CG 1282 C CD . LYS A 206 ? 0.6109 0.5901 0.4171 0.0351 0.1330 -0.0566 199 LYS A CD 1283 C CE . LYS A 206 ? 0.6780 0.6537 0.4681 0.0380 0.1446 -0.0520 199 LYS A CE 1284 N NZ . LYS A 206 ? 0.7124 0.6801 0.4781 0.0400 0.1403 -0.0502 199 LYS A NZ 1285 N N . ILE A 207 ? 0.4852 0.4720 0.3370 0.0273 0.0992 -0.0687 200 ILE A N 1286 C CA . ILE A 207 ? 0.4694 0.4605 0.3407 0.0247 0.0934 -0.0700 200 ILE A CA 1287 C C . ILE A 207 ? 0.4491 0.4470 0.3380 0.0227 0.0996 -0.0654 200 ILE A C 1288 O O . ILE A 207 ? 0.4635 0.4634 0.3545 0.0245 0.1088 -0.0655 200 ILE A O 1289 C CB . ILE A 207 ? 0.4775 0.4664 0.3509 0.0271 0.0911 -0.0779 200 ILE A CB 1290 C CG1 . ILE A 207 ? 0.4988 0.4811 0.3571 0.0284 0.0830 -0.0827 200 ILE A CG1 1291 C CG2 . ILE A 207 ? 0.4581 0.4516 0.3527 0.0247 0.0871 -0.0783 200 ILE A CG2 1292 C CD1 . ILE A 207 ? 0.5148 0.4933 0.3713 0.0314 0.0813 -0.0912 200 ILE A CD1 1293 N N . VAL A 208 ? 0.4224 0.4241 0.3242 0.0191 0.0948 -0.0615 201 VAL A N 1294 C CA . VAL A 208 ? 0.4042 0.4124 0.3232 0.0173 0.0997 -0.0575 201 VAL A CA 1295 C C . VAL A 208 ? 0.3899 0.4017 0.3261 0.0173 0.0970 -0.0608 201 VAL A C 1296 O O . VAL A 208 ? 0.3844 0.3943 0.3220 0.0169 0.0892 -0.0635 201 VAL A O 1297 C CB . VAL A 208 ? 0.4052 0.4152 0.3272 0.0138 0.0972 -0.0507 201 VAL A CB 1298 C CG1 A VAL A 208 ? 0.3974 0.4034 0.3023 0.0143 0.1012 -0.0470 201 VAL A CG1 1299 C CG1 B VAL A 208 ? 0.3886 0.4035 0.3295 0.0111 0.0922 -0.0490 201 VAL A CG1 1300 C CG2 A VAL A 208 ? 0.3476 0.3569 0.2727 0.0118 0.0867 -0.0508 201 VAL A CG2 1301 C CG2 B VAL A 208 ? 0.4162 0.4265 0.3332 0.0137 0.1060 -0.0458 201 VAL A CG2 1302 N N . ILE A 209 ? 0.3732 0.3900 0.3223 0.0178 0.1037 -0.0605 202 ILE A N 1303 C CA . ILE A 209 ? 0.3603 0.3809 0.3269 0.0179 0.1010 -0.0626 202 ILE A CA 1304 C C . ILE A 209 ? 0.3572 0.3841 0.3402 0.0153 0.1016 -0.0577 202 ILE A C 1305 O O . ILE A 209 ? 0.3600 0.3902 0.3467 0.0148 0.1090 -0.0546 202 ILE A O 1306 C CB . ILE A 209 ? 0.3665 0.3873 0.3362 0.0215 0.1064 -0.0682 202 ILE A CB 1307 C CG1 . ILE A 209 ? 0.3574 0.3816 0.3453 0.0218 0.1027 -0.0701 202 ILE A CG1 1308 C CG2 . ILE A 209 ? 0.3746 0.3981 0.3437 0.0230 0.1179 -0.0669 202 ILE A CG2 1309 C CD1 . ILE A 209 ? 0.3862 0.4089 0.3758 0.0257 0.1056 -0.0766 202 ILE A CD1 1310 N N . ALA A 210 ? 0.3334 0.3615 0.3257 0.0138 0.0938 -0.0570 203 ALA A N 1311 C CA . ALA A 210 ? 0.3216 0.3548 0.3280 0.0115 0.0923 -0.0528 203 ALA A CA 1312 C C . ALA A 210 ? 0.3086 0.3447 0.3303 0.0125 0.0884 -0.0550 203 ALA A C 1313 O O . ALA A 210 ? 0.3065 0.3394 0.3261 0.0137 0.0832 -0.0580 203 ALA A O 1314 C CB . ALA A 210 ? 0.3076 0.3386 0.3078 0.0088 0.0858 -0.0491 203 ALA A CB 1315 N N . ARG A 211 ? 0.3026 0.3446 0.3402 0.0121 0.0905 -0.0534 204 ARG A N 1316 C CA . ARG A 211 ? 0.2871 0.3317 0.3387 0.0131 0.0852 -0.0546 204 ARG A CA 1317 C C . ARG A 211 ? 0.2787 0.3225 0.3315 0.0112 0.0769 -0.0517 204 ARG A C 1318 O O . ARG A 211 ? 0.2702 0.3145 0.3207 0.0086 0.0763 -0.0479 204 ARG A O 1319 C CB . ARG A 211 ? 0.3069 0.3581 0.3762 0.0141 0.0897 -0.0551 204 ARG A CB 1320 C CG . ARG A 211 ? 0.3218 0.3775 0.3975 0.0117 0.0946 -0.0514 204 ARG A CG 1321 C CD . ARG A 211 ? 0.3396 0.4022 0.4358 0.0128 0.0969 -0.0524 204 ARG A CD 1322 N NE . ARG A 211 ? 0.3156 0.3830 0.4202 0.0105 0.1031 -0.0492 204 ARG A NE 1323 C CZ . ARG A 211 ? 0.3303 0.4046 0.4550 0.0106 0.1049 -0.0493 204 ARG A CZ 1324 N NH1 . ARG A 211 ? 0.3077 0.3847 0.4447 0.0130 0.1003 -0.0524 204 ARG A NH1 1325 N NH2 . ARG A 211 ? 0.3112 0.3895 0.4441 0.0081 0.1110 -0.0462 204 ARG A NH2 1326 N N . TYR A 212 ? 0.2603 0.3024 0.3160 0.0126 0.0708 -0.0533 205 TYR A N 1327 C CA . TYR A 212 ? 0.2566 0.2980 0.3141 0.0116 0.0633 -0.0507 205 TYR A CA 1328 C C . TYR A 212 ? 0.2574 0.3043 0.3291 0.0111 0.0627 -0.0488 205 TYR A C 1329 O O . TYR A 212 ? 0.2581 0.3095 0.3411 0.0121 0.0669 -0.0502 205 TYR A O 1330 C CB . TYR A 212 ? 0.2540 0.2924 0.3133 0.0138 0.0583 -0.0528 205 TYR A CB 1331 C CG . TYR A 212 ? 0.2563 0.2887 0.3036 0.0136 0.0552 -0.0537 205 TYR A CG 1332 C CD1 . TYR A 212 ? 0.2557 0.2848 0.3020 0.0158 0.0554 -0.0573 205 TYR A CD1 1333 C CD2 . TYR A 212 ? 0.2441 0.2742 0.2829 0.0114 0.0515 -0.0509 205 TYR A CD2 1334 C CE1 . TYR A 212 ? 0.2548 0.2784 0.2924 0.0154 0.0520 -0.0582 205 TYR A CE1 1335 C CE2 . TYR A 212 ? 0.2573 0.2824 0.2876 0.0111 0.0482 -0.0516 205 TYR A CE2 1336 C CZ . TYR A 212 ? 0.2709 0.2928 0.3010 0.0130 0.0483 -0.0552 205 TYR A CZ 1337 O OH . TYR A 212 ? 0.2681 0.2853 0.2917 0.0124 0.0449 -0.0560 205 TYR A OH 1338 N N . GLY A 213 ? 0.2480 0.2946 0.3194 0.0095 0.0574 -0.0459 206 GLY A N 1339 C CA . GLY A 213 ? 0.2557 0.3069 0.3406 0.0092 0.0550 -0.0445 206 GLY A CA 1340 C C . GLY A 213 ? 0.2533 0.3049 0.3357 0.0060 0.0552 -0.0411 206 GLY A C 1341 O O . GLY A 213 ? 0.2600 0.3093 0.3316 0.0043 0.0588 -0.0397 206 GLY A O 1342 N N . LYS A 214 ? 0.2514 0.3060 0.3443 0.0056 0.0512 -0.0400 207 LYS A N 1343 C CA . LYS A 214 ? 0.2494 0.3049 0.3437 0.0026 0.0511 -0.0370 207 LYS A CA 1344 C C . LYS A 214 ? 0.2534 0.3040 0.3346 0.0013 0.0469 -0.0346 207 LYS A C 1345 O O . LYS A 214 ? 0.2603 0.3110 0.3447 0.0004 0.0421 -0.0331 207 LYS A O 1346 C CB . LYS A 214 ? 0.2599 0.3175 0.3558 0.0004 0.0597 -0.0356 207 LYS A CB 1347 C CG . LYS A 214 ? 0.2841 0.3475 0.3949 0.0014 0.0652 -0.0377 207 LYS A CG 1348 C CD . LYS A 214 ? 0.3365 0.4047 0.4654 0.0016 0.0607 -0.0385 207 LYS A CD 1349 C CE . LYS A 214 ? 0.3779 0.4524 0.5232 0.0026 0.0666 -0.0405 207 LYS A CE 1350 N NZ . LYS A 214 ? 0.4341 0.5136 0.5981 0.0031 0.0609 -0.0418 207 LYS A NZ 1351 N N . VAL A 215 ? 0.2434 0.2899 0.3106 0.0013 0.0483 -0.0345 208 VAL A N 1352 C CA . VAL A 215 ? 0.2431 0.2853 0.2982 0.0001 0.0447 -0.0323 208 VAL A CA 1353 C C . VAL A 215 ? 0.2376 0.2758 0.2829 0.0017 0.0423 -0.0337 208 VAL A C 1354 O O . VAL A 215 ? 0.2474 0.2855 0.2922 0.0031 0.0450 -0.0363 208 VAL A O 1355 C CB . VAL A 215 ? 0.2385 0.2792 0.2856 -0.0025 0.0491 -0.0295 208 VAL A CB 1356 C CG1 . VAL A 215 ? 0.2578 0.3020 0.3159 -0.0044 0.0521 -0.0276 208 VAL A CG1 1357 C CG2 . VAL A 215 ? 0.2770 0.3161 0.3148 -0.0021 0.0550 -0.0306 208 VAL A CG2 1358 N N . PHE A 216 ? 0.2266 0.2617 0.2646 0.0013 0.0376 -0.0321 209 PHE A N 1359 C CA . PHE A 216 ? 0.2213 0.2526 0.2502 0.0021 0.0355 -0.0330 209 PHE A CA 1360 C C . PHE A 216 ? 0.2317 0.2612 0.2520 0.0016 0.0398 -0.0345 209 PHE A C 1361 O O . PHE A 216 ? 0.2367 0.2660 0.2516 0.0000 0.0430 -0.0331 209 PHE A O 1362 C CB . PHE A 216 ? 0.2195 0.2483 0.2425 0.0014 0.0308 -0.0306 209 PHE A CB 1363 C CG . PHE A 216 ? 0.2266 0.2519 0.2415 0.0017 0.0289 -0.0311 209 PHE A CG 1364 C CD1 . PHE A 216 ? 0.2272 0.2512 0.2445 0.0036 0.0273 -0.0328 209 PHE A CD1 1365 C CD2 . PHE A 216 ? 0.2489 0.2721 0.2547 0.0002 0.0283 -0.0298 209 PHE A CD2 1366 C CE1 . PHE A 216 ? 0.2557 0.2764 0.2672 0.0036 0.0257 -0.0333 209 PHE A CE1 1367 C CE2 . PHE A 216 ? 0.2462 0.2665 0.2462 0.0003 0.0261 -0.0306 209 PHE A CE2 1368 C CZ . PHE A 216 ? 0.2470 0.2662 0.2504 0.0019 0.0250 -0.0323 209 PHE A CZ 1369 N N . ARG A 217 ? 0.2307 0.2583 0.2493 0.0031 0.0397 -0.0373 210 ARG A N 1370 C CA . ARG A 217 ? 0.2410 0.2667 0.2517 0.0031 0.0434 -0.0397 210 ARG A CA 1371 C C . ARG A 217 ? 0.2533 0.2760 0.2519 0.0017 0.0421 -0.0385 210 ARG A C 1372 O O . ARG A 217 ? 0.2544 0.2757 0.2451 0.0016 0.0455 -0.0396 210 ARG A O 1373 C CB . ARG A 217 ? 0.2421 0.2659 0.2542 0.0051 0.0428 -0.0433 210 ARG A CB 1374 C CG . ARG A 217 ? 0.2296 0.2501 0.2395 0.0051 0.0373 -0.0428 210 ARG A CG 1375 C CD . ARG A 217 ? 0.2340 0.2521 0.2469 0.0069 0.0369 -0.0461 210 ARG A CD 1376 N NE . ARG A 217 ? 0.2181 0.2376 0.2410 0.0088 0.0356 -0.0455 210 ARG A NE 1377 C CZ . ARG A 217 ? 0.2470 0.2660 0.2723 0.0092 0.0315 -0.0427 210 ARG A CZ 1378 N NH1 . ARG A 217 ? 0.2231 0.2405 0.2427 0.0077 0.0288 -0.0404 210 ARG A NH1 1379 N NH2 . ARG A 217 ? 0.2269 0.2466 0.2601 0.0114 0.0301 -0.0423 210 ARG A NH2 1380 N N . GLY A 218 ? 0.2387 0.2601 0.2357 0.0008 0.0372 -0.0363 211 GLY A N 1381 C CA . GLY A 218 ? 0.2571 0.2762 0.2440 -0.0004 0.0355 -0.0350 211 GLY A CA 1382 C C . GLY A 218 ? 0.2498 0.2697 0.2329 -0.0016 0.0387 -0.0324 211 GLY A C 1383 O O . GLY A 218 ? 0.2569 0.2745 0.2298 -0.0019 0.0398 -0.0323 211 GLY A O 1384 N N . ASN A 219 ? 0.2508 0.2736 0.2420 -0.0022 0.0402 -0.0303 212 ASN A N 1385 C CA . ASN A 219 ? 0.2623 0.2857 0.2516 -0.0035 0.0442 -0.0276 212 ASN A CA 1386 C C . ASN A 219 ? 0.2798 0.3031 0.2651 -0.0029 0.0508 -0.0290 212 ASN A C 1387 O O . ASN A 219 ? 0.2944 0.3158 0.2708 -0.0035 0.0538 -0.0272 212 ASN A O 1388 C CB . ASN A 219 ? 0.2558 0.2823 0.2565 -0.0044 0.0442 -0.0255 212 ASN A CB 1389 C CG . ASN A 219 ? 0.2694 0.2952 0.2714 -0.0048 0.0381 -0.0237 212 ASN A CG 1390 O OD1 . ASN A 219 ? 0.2734 0.2998 0.2804 -0.0036 0.0342 -0.0249 212 ASN A OD1 1391 N ND2 . ASN A 219 ? 0.2503 0.2743 0.2468 -0.0061 0.0373 -0.0208 212 ASN A ND2 1392 N N . LYS A 220 ? 0.2681 0.2933 0.2594 -0.0015 0.0531 -0.0323 213 LYS A N 1393 C CA . LYS A 220 ? 0.2758 0.3007 0.2628 -0.0004 0.0597 -0.0343 213 LYS A CA 1394 C C . LYS A 220 ? 0.2881 0.3083 0.2593 0.0003 0.0592 -0.0356 213 LYS A C 1395 O O . LYS A 220 ? 0.2833 0.3020 0.2456 0.0007 0.0644 -0.0350 213 LYS A O 1396 C CB . LYS A 220 ? 0.2692 0.2961 0.2647 0.0015 0.0609 -0.0382 213 LYS A CB 1397 C CG . LYS A 220 ? 0.2636 0.2953 0.2755 0.0015 0.0609 -0.0377 213 LYS A CG 1398 C CD . LYS A 220 ? 0.2634 0.2962 0.2822 0.0039 0.0616 -0.0417 213 LYS A CD 1399 C CE . LYS A 220 ? 0.2687 0.3059 0.3032 0.0045 0.0599 -0.0416 213 LYS A CE 1400 N NZ . LYS A 220 ? 0.2665 0.3085 0.3111 0.0043 0.0662 -0.0413 213 LYS A NZ 1401 N N . VAL A 221 ? 0.2709 0.2888 0.2389 0.0007 0.0532 -0.0377 214 VAL A N 1402 C CA . VAL A 221 ? 0.2925 0.3061 0.2471 0.0014 0.0514 -0.0398 214 VAL A CA 1403 C C . VAL A 221 ? 0.3056 0.3171 0.2501 0.0004 0.0504 -0.0361 214 VAL A C 1404 O O . VAL A 221 ? 0.3146 0.3230 0.2465 0.0015 0.0525 -0.0367 214 VAL A O 1405 C CB . VAL A 221 ? 0.2902 0.3022 0.2463 0.0018 0.0451 -0.0428 214 VAL A CB 1406 C CG1 . VAL A 221 ? 0.3111 0.3187 0.2541 0.0023 0.0420 -0.0451 214 VAL A CG1 1407 C CG2 . VAL A 221 ? 0.2899 0.3026 0.2540 0.0032 0.0466 -0.0467 214 VAL A CG2 1408 N N A LYS A 222 ? 0.2912 0.3040 0.2406 -0.0012 0.0472 -0.0325 215 LYS A N 1409 N N B LYS A 222 ? 0.2932 0.3061 0.2428 -0.0012 0.0471 -0.0325 215 LYS A N 1410 C CA A LYS A 222 ? 0.3043 0.3151 0.2455 -0.0021 0.0463 -0.0286 215 LYS A CA 1411 C CA B LYS A 222 ? 0.3089 0.3199 0.2508 -0.0022 0.0462 -0.0285 215 LYS A CA 1412 C C A LYS A 222 ? 0.3185 0.3288 0.2551 -0.0021 0.0535 -0.0262 215 LYS A C 1413 C C B LYS A 222 ? 0.3207 0.3311 0.2576 -0.0021 0.0534 -0.0261 215 LYS A C 1414 O O A LYS A 222 ? 0.3311 0.3379 0.2547 -0.0014 0.0546 -0.0248 215 LYS A O 1415 O O B LYS A 222 ? 0.3341 0.3408 0.2578 -0.0014 0.0544 -0.0248 215 LYS A O 1416 C CB A LYS A 222 ? 0.2889 0.3013 0.2378 -0.0037 0.0423 -0.0253 215 LYS A CB 1417 C CB B LYS A 222 ? 0.2934 0.3063 0.2440 -0.0038 0.0427 -0.0252 215 LYS A CB 1418 C CG A LYS A 222 ? 0.3106 0.3208 0.2523 -0.0046 0.0416 -0.0211 215 LYS A CG 1419 C CG B LYS A 222 ? 0.3312 0.3419 0.2751 -0.0047 0.0413 -0.0210 215 LYS A CG 1420 C CD A LYS A 222 ? 0.3325 0.3443 0.2829 -0.0059 0.0384 -0.0181 215 LYS A CD 1421 C CD B LYS A 222 ? 0.3478 0.3599 0.2996 -0.0058 0.0366 -0.0187 215 LYS A CD 1422 C CE A LYS A 222 ? 0.3312 0.3406 0.2760 -0.0068 0.0385 -0.0137 215 LYS A CE 1423 C CE B LYS A 222 ? 0.3869 0.4019 0.3501 -0.0069 0.0394 -0.0168 215 LYS A CE 1424 N NZ A LYS A 222 ? 0.4047 0.4152 0.3573 -0.0078 0.0345 -0.0116 215 LYS A NZ 1425 N NZ B LYS A 222 ? 0.4223 0.4378 0.3916 -0.0079 0.0354 -0.0143 215 LYS A NZ 1426 N N . ASN A 223 ? 0.3137 0.3276 0.2612 -0.0026 0.0586 -0.0256 216 ASN A N 1427 C CA . ASN A 223 ? 0.3179 0.3320 0.2637 -0.0027 0.0666 -0.0229 216 ASN A CA 1428 C C . ASN A 223 ? 0.3253 0.3365 0.2583 -0.0004 0.0713 -0.0255 216 ASN A C 1429 O O . ASN A 223 ? 0.3452 0.3534 0.2672 0.0001 0.0759 -0.0227 216 ASN A O 1430 C CB . ASN A 223 ? 0.2981 0.3174 0.2605 -0.0037 0.0706 -0.0225 216 ASN A CB 1431 C CG . ASN A 223 ? 0.3129 0.3345 0.2868 -0.0057 0.0661 -0.0200 216 ASN A CG 1432 O OD1 . ASN A 223 ? 0.3144 0.3335 0.2831 -0.0066 0.0616 -0.0176 216 ASN A OD1 1433 N ND2 . ASN A 223 ? 0.2828 0.3090 0.2722 -0.0062 0.0672 -0.0207 216 ASN A ND2 1434 N N . ALA A 224 ? 0.3284 0.3399 0.2620 0.0012 0.0700 -0.0307 217 ALA A N 1435 C CA . ALA A 224 ? 0.3465 0.3548 0.2677 0.0039 0.0740 -0.0341 217 ALA A CA 1436 C C . ALA A 224 ? 0.3696 0.3723 0.2730 0.0049 0.0699 -0.0342 217 ALA A C 1437 O O . ALA A 224 ? 0.3960 0.3951 0.2854 0.0069 0.0742 -0.0341 217 ALA A O 1438 C CB . ALA A 224 ? 0.3409 0.3502 0.2677 0.0054 0.0727 -0.0400 217 ALA A CB 1439 N N . GLN A 225 ? 0.3737 0.3757 0.2779 0.0039 0.0615 -0.0345 218 GLN A N 1440 C CA . GLN A 225 ? 0.4077 0.4050 0.2971 0.0049 0.0563 -0.0346 218 GLN A CA 1441 C C . GLN A 225 ? 0.4351 0.4299 0.3147 0.0048 0.0595 -0.0292 218 GLN A C 1442 O O . GLN A 225 ? 0.4441 0.4341 0.3072 0.0070 0.0598 -0.0295 218 GLN A O 1443 C CB . GLN A 225 ? 0.4095 0.4076 0.3046 0.0034 0.0475 -0.0347 218 GLN A CB 1444 C CG . GLN A 225 ? 0.4360 0.4340 0.3345 0.0040 0.0433 -0.0402 218 GLN A CG 1445 C CD . GLN A 225 ? 0.4751 0.4736 0.3787 0.0026 0.0352 -0.0402 218 GLN A CD 1446 O OE1 . GLN A 225 ? 0.4745 0.4743 0.3866 0.0023 0.0325 -0.0432 218 GLN A OE1 1447 N NE2 . GLN A 225 ? 0.5077 0.5050 0.4060 0.0021 0.0317 -0.0368 218 GLN A NE2 1448 N N . LEU A 226 ? 0.4323 0.4299 0.3218 0.0025 0.0613 -0.0242 219 LEU A N 1449 C CA . LEU A 226 ? 0.4537 0.4486 0.3359 0.0021 0.0642 -0.0184 219 LEU A CA 1450 C C . LEU A 226 ? 0.4669 0.4599 0.3410 0.0035 0.0740 -0.0167 219 LEU A C 1451 O O . LEU A 226 ? 0.4783 0.4669 0.3395 0.0045 0.0765 -0.0127 219 LEU A O 1452 C CB . LEU A 226 ? 0.4492 0.4471 0.3449 -0.0009 0.0631 -0.0140 219 LEU A CB 1453 C CG . LEU A 226 ? 0.4951 0.4934 0.3944 -0.0018 0.0537 -0.0146 219 LEU A CG 1454 C CD1 . LEU A 226 ? 0.5204 0.5215 0.4331 -0.0042 0.0527 -0.0111 219 LEU A CD1 1455 C CD2 . LEU A 226 ? 0.5610 0.5545 0.4456 -0.0004 0.0486 -0.0138 219 LEU A CD2 1456 N N . ALA A 227 ? 0.4480 0.4440 0.3290 0.0041 0.0795 -0.0198 220 ALA A N 1457 C CA . ALA A 227 ? 0.4550 0.4496 0.3286 0.0060 0.0894 -0.0191 220 ALA A CA 1458 C C . ALA A 227 ? 0.4651 0.4543 0.3192 0.0098 0.0890 -0.0232 220 ALA A C 1459 O O . ALA A 227 ? 0.4892 0.4762 0.3336 0.0122 0.0971 -0.0230 220 ALA A O 1460 C CB . ALA A 227 ? 0.4391 0.4394 0.3290 0.0054 0.0952 -0.0211 220 ALA A CB 1461 N N . GLY A 228 ? 0.4538 0.4410 0.3025 0.0105 0.0796 -0.0272 221 GLY A N 1462 C CA . GLY A 228 ? 0.4572 0.4390 0.2875 0.0142 0.0774 -0.0318 221 GLY A CA 1463 C C . GLY A 228 ? 0.4591 0.4418 0.2919 0.0160 0.0782 -0.0390 221 GLY A C 1464 O O . GLY A 228 ? 0.4742 0.4521 0.2915 0.0194 0.0778 -0.0433 221 GLY A O 1465 N N . ALA A 229 ? 0.4419 0.4302 0.2935 0.0140 0.0788 -0.0406 222 ALA A N 1466 C CA . ALA A 229 ? 0.4401 0.4291 0.2958 0.0157 0.0791 -0.0474 222 ALA A CA 1467 C C . ALA A 229 ? 0.4438 0.4290 0.2920 0.0169 0.0697 -0.0530 222 ALA A C 1468 O O . ALA A 229 ? 0.4292 0.4139 0.2776 0.0152 0.0619 -0.0516 222 ALA A O 1469 C CB . ALA A 229 ? 0.4264 0.4218 0.3041 0.0133 0.0795 -0.0475 222 ALA A CB 1470 N N . LYS A 230 ? 0.4435 0.4261 0.2860 0.0197 0.0704 -0.0595 223 LYS A N 1471 C CA . LYS A 230 ? 0.4497 0.4292 0.2886 0.0204 0.0612 -0.0655 223 LYS A CA 1472 C C . LYS A 230 ? 0.4334 0.4157 0.2892 0.0191 0.0581 -0.0695 223 LYS A C 1473 O O . LYS A 230 ? 0.4321 0.4121 0.2882 0.0192 0.0506 -0.0743 223 LYS A O 1474 C CB . LYS A 230 ? 0.4869 0.4597 0.3052 0.0247 0.0611 -0.0706 223 LYS A CB 1475 C CG . LYS A 230 ? 0.5042 0.4758 0.3204 0.0277 0.0676 -0.0758 223 LYS A CG 1476 C CD . LYS A 230 ? 0.5491 0.5133 0.3436 0.0321 0.0651 -0.0816 223 LYS A CD 1477 C CE . LYS A 230 ? 0.5950 0.5574 0.3827 0.0359 0.0738 -0.0854 223 LYS A CE 1478 N NZ . LYS A 230 ? 0.6086 0.5630 0.3721 0.0408 0.0716 -0.0906 223 LYS A NZ 1479 N N . GLY A 231 ? 0.4114 0.3987 0.2819 0.0178 0.0635 -0.0672 224 GLY A N 1480 C CA . GLY A 231 ? 0.4041 0.3940 0.2908 0.0167 0.0609 -0.0701 224 GLY A CA 1481 C C . GLY A 231 ? 0.3836 0.3792 0.2850 0.0155 0.0669 -0.0663 224 GLY A C 1482 O O . GLY A 231 ? 0.3884 0.3857 0.2874 0.0160 0.0743 -0.0631 224 GLY A O 1483 N N . VAL A 232 ? 0.3647 0.3633 0.2816 0.0140 0.0636 -0.0665 225 VAL A N 1484 C CA . VAL A 232 ? 0.3487 0.3526 0.2806 0.0131 0.0678 -0.0636 225 VAL A CA 1485 C C . VAL A 232 ? 0.3463 0.3509 0.2894 0.0143 0.0672 -0.0678 225 VAL A C 1486 O O . VAL A 232 ? 0.3366 0.3391 0.2828 0.0139 0.0609 -0.0701 225 VAL A O 1487 C CB . VAL A 232 ? 0.3445 0.3517 0.2852 0.0101 0.0637 -0.0582 225 VAL A CB 1488 C CG1 . VAL A 232 ? 0.3400 0.3527 0.2961 0.0095 0.0677 -0.0557 225 VAL A CG1 1489 C CG2 . VAL A 232 ? 0.3462 0.3521 0.2761 0.0088 0.0635 -0.0539 225 VAL A CG2 1490 N N . ILE A 233 ? 0.3355 0.3431 0.2857 0.0158 0.0739 -0.0685 226 ILE A N 1491 C CA . ILE A 233 ? 0.3296 0.3386 0.2925 0.0171 0.0738 -0.0717 226 ILE A CA 1492 C C . ILE A 233 ? 0.3245 0.3396 0.3031 0.0158 0.0749 -0.0674 226 ILE A C 1493 O O . ILE A 233 ? 0.3424 0.3611 0.3234 0.0155 0.0807 -0.0646 226 ILE A O 1494 C CB . ILE A 233 ? 0.3414 0.3492 0.3010 0.0206 0.0804 -0.0767 226 ILE A CB 1495 C CG1 . ILE A 233 ? 0.3467 0.3479 0.2896 0.0222 0.0785 -0.0815 226 ILE A CG1 1496 C CG2 . ILE A 233 ? 0.3389 0.3485 0.3135 0.0222 0.0805 -0.0795 226 ILE A CG2 1497 C CD1 . ILE A 233 ? 0.3533 0.3528 0.2885 0.0259 0.0863 -0.0858 226 ILE A CD1 1498 N N . LEU A 234 ? 0.3021 0.3178 0.2909 0.0151 0.0693 -0.0668 227 LEU A N 1499 C CA . LEU A 234 ? 0.2946 0.3155 0.2979 0.0143 0.0688 -0.0633 227 LEU A CA 1500 C C . LEU A 234 ? 0.2975 0.3195 0.3120 0.0169 0.0702 -0.0666 227 LEU A C 1501 O O . LEU A 234 ? 0.3170 0.3349 0.3297 0.0184 0.0680 -0.0704 227 LEU A O 1502 C CB . LEU A 234 ? 0.2750 0.2950 0.2804 0.0124 0.0613 -0.0602 227 LEU A CB 1503 C CG . LEU A 234 ? 0.2981 0.3170 0.2936 0.0099 0.0590 -0.0569 227 LEU A CG 1504 C CD1 . LEU A 234 ? 0.2921 0.3093 0.2891 0.0086 0.0516 -0.0549 227 LEU A CD1 1505 C CD2 . LEU A 234 ? 0.3210 0.3440 0.3193 0.0086 0.0629 -0.0529 227 LEU A CD2 1506 N N . TYR A 235 ? 0.2864 0.3139 0.3131 0.0176 0.0737 -0.0653 228 TYR A N 1507 C CA . TYR A 235 ? 0.2857 0.3145 0.3240 0.0204 0.0745 -0.0684 228 TYR A CA 1508 C C . TYR A 235 ? 0.2776 0.3121 0.3312 0.0203 0.0732 -0.0656 228 TYR A C 1509 O O . TYR A 235 ? 0.2744 0.3126 0.3305 0.0182 0.0740 -0.0619 228 TYR A O 1510 C CB . TYR A 235 ? 0.2944 0.3236 0.3314 0.0230 0.0823 -0.0726 228 TYR A CB 1511 C CG . TYR A 235 ? 0.2903 0.3259 0.3352 0.0229 0.0894 -0.0707 228 TYR A CG 1512 C CD1 . TYR A 235 ? 0.2848 0.3257 0.3465 0.0249 0.0916 -0.0716 228 TYR A CD1 1513 C CD2 . TYR A 235 ? 0.2872 0.3237 0.3238 0.0210 0.0940 -0.0678 228 TYR A CD2 1514 C CE1 . TYR A 235 ? 0.2937 0.3411 0.3650 0.0245 0.0983 -0.0698 228 TYR A CE1 1515 C CE2 . TYR A 235 ? 0.2875 0.3298 0.3327 0.0206 0.1010 -0.0656 228 TYR A CE2 1516 C CZ . TYR A 235 ? 0.2967 0.3447 0.3598 0.0222 0.1031 -0.0667 228 TYR A CZ 1517 O OH . TYR A 235 ? 0.3090 0.3632 0.3826 0.0215 0.1098 -0.0645 228 TYR A OH 1518 N N . SER A 236 ? 0.2733 0.3082 0.3373 0.0228 0.0709 -0.0674 229 SER A N 1519 C CA . SER A 236 ? 0.2629 0.3028 0.3417 0.0235 0.0686 -0.0654 229 SER A CA 1520 C C . SER A 236 ? 0.2677 0.3132 0.3584 0.0255 0.0749 -0.0675 229 SER A C 1521 O O . SER A 236 ? 0.2763 0.3206 0.3701 0.0285 0.0771 -0.0713 229 SER A O 1522 C CB . SER A 236 ? 0.2644 0.3011 0.3475 0.0255 0.0619 -0.0657 229 SER A CB 1523 O OG . SER A 236 ? 0.2881 0.3201 0.3613 0.0235 0.0566 -0.0633 229 SER A OG 1524 N N . ASP A 237 ? 0.2654 0.3168 0.3636 0.0239 0.0780 -0.0652 230 ASP A N 1525 C CA . ASP A 237 ? 0.2865 0.3439 0.3976 0.0256 0.0848 -0.0669 230 ASP A CA 1526 C C . ASP A 237 ? 0.2851 0.3466 0.4136 0.0277 0.0799 -0.0673 230 ASP A C 1527 O O . ASP A 237 ? 0.2847 0.3467 0.4161 0.0266 0.0731 -0.0646 230 ASP A O 1528 C CB . ASP A 237 ? 0.2815 0.3435 0.3940 0.0227 0.0910 -0.0640 230 ASP A CB 1529 C CG . ASP A 237 ? 0.3110 0.3783 0.4339 0.0243 0.1004 -0.0659 230 ASP A CG 1530 O OD1 . ASP A 237 ? 0.3271 0.3929 0.4401 0.0244 0.1081 -0.0667 230 ASP A OD1 1531 O OD2 . ASP A 237 ? 0.3028 0.3759 0.4437 0.0259 0.1000 -0.0669 230 ASP A OD2 1532 N N . PRO A 238 ? 0.3035 0.3678 0.4433 0.0311 0.0831 -0.0707 231 PRO A N 1533 C CA . PRO A 238 ? 0.3056 0.3740 0.4624 0.0336 0.0779 -0.0711 231 PRO A CA 1534 C C . PRO A 238 ? 0.3150 0.3903 0.4844 0.0314 0.0766 -0.0683 231 PRO A C 1535 O O . PRO A 238 ? 0.3057 0.3828 0.4847 0.0326 0.0692 -0.0676 231 PRO A O 1536 C CB . PRO A 238 ? 0.3219 0.3932 0.4891 0.0373 0.0838 -0.0752 231 PRO A CB 1537 C CG . PRO A 238 ? 0.3333 0.3990 0.4853 0.0376 0.0890 -0.0776 231 PRO A CG 1538 C CD . PRO A 238 ? 0.3044 0.3675 0.4409 0.0335 0.0906 -0.0747 231 PRO A CD 1539 N N . ALA A 239 ? 0.3111 0.3896 0.4798 0.0283 0.0833 -0.0666 232 ALA A N 1540 C CA . ALA A 239 ? 0.3202 0.4044 0.5004 0.0257 0.0817 -0.0638 232 ALA A CA 1541 C C . ALA A 239 ? 0.3184 0.3994 0.4934 0.0243 0.0717 -0.0612 232 ALA A C 1542 O O . ALA A 239 ? 0.3249 0.4099 0.5124 0.0241 0.0664 -0.0604 232 ALA A O 1543 C CB . ALA A 239 ? 0.3305 0.4167 0.5072 0.0222 0.0906 -0.0616 232 ALA A CB 1544 N N . ASP A 240 ? 0.3072 0.3809 0.4640 0.0235 0.0691 -0.0601 233 ASP A N 1545 C CA . ASP A 240 ? 0.2995 0.3695 0.4487 0.0221 0.0611 -0.0574 233 ASP A CA 1546 C C . ASP A 240 ? 0.2960 0.3611 0.4413 0.0252 0.0537 -0.0582 233 ASP A C 1547 O O . ASP A 240 ? 0.2945 0.3571 0.4356 0.0249 0.0466 -0.0561 233 ASP A O 1548 C CB . ASP A 240 ? 0.2977 0.3632 0.4295 0.0188 0.0637 -0.0551 233 ASP A CB 1549 C CG . ASP A 240 ? 0.3009 0.3701 0.4345 0.0160 0.0718 -0.0537 233 ASP A CG 1550 O OD1 . ASP A 240 ? 0.3138 0.3869 0.4565 0.0139 0.0708 -0.0516 233 ASP A OD1 1551 O OD2 . ASP A 240 ? 0.3002 0.3682 0.4266 0.0162 0.0791 -0.0549 233 ASP A OD2 1552 N N . TYR A 241 ? 0.2891 0.3525 0.4351 0.0282 0.0555 -0.0611 234 TYR A N 1553 C CA . TYR A 241 ? 0.2905 0.3479 0.4315 0.0311 0.0494 -0.0615 234 TYR A CA 1554 C C . TYR A 241 ? 0.3019 0.3608 0.4550 0.0356 0.0484 -0.0643 234 TYR A C 1555 O O . TYR A 241 ? 0.2989 0.3522 0.4477 0.0382 0.0451 -0.0649 234 TYR A O 1556 C CB . TYR A 241 ? 0.2961 0.3465 0.4206 0.0300 0.0510 -0.0617 234 TYR A CB 1557 C CG . TYR A 241 ? 0.2950 0.3433 0.4078 0.0262 0.0496 -0.0585 234 TYR A CG 1558 C CD1 . TYR A 241 ? 0.2945 0.3441 0.4010 0.0232 0.0554 -0.0581 234 TYR A CD1 1559 C CD2 . TYR A 241 ? 0.2798 0.3251 0.3881 0.0260 0.0426 -0.0556 234 TYR A CD2 1560 C CE1 . TYR A 241 ? 0.2845 0.3324 0.3812 0.0199 0.0539 -0.0550 234 TYR A CE1 1561 C CE2 . TYR A 241 ? 0.2945 0.3383 0.3932 0.0227 0.0414 -0.0528 234 TYR A CE2 1562 C CZ . TYR A 241 ? 0.3046 0.3497 0.3978 0.0197 0.0468 -0.0526 234 TYR A CZ 1563 O OH . TYR A 241 ? 0.2885 0.3320 0.3726 0.0168 0.0453 -0.0497 234 TYR A OH 1564 N N . PHE A 242 ? 0.2980 0.3641 0.4668 0.0366 0.0513 -0.0660 235 PHE A N 1565 C CA . PHE A 242 ? 0.3104 0.3784 0.4919 0.0412 0.0501 -0.0688 235 PHE A CA 1566 C C . PHE A 242 ? 0.3140 0.3900 0.5138 0.0419 0.0474 -0.0689 235 PHE A C 1567 O O . PHE A 242 ? 0.3136 0.3964 0.5238 0.0403 0.0536 -0.0698 235 PHE A O 1568 C CB . PHE A 242 ? 0.3170 0.3857 0.4999 0.0423 0.0587 -0.0723 235 PHE A CB 1569 C CG . PHE A 242 ? 0.3146 0.3833 0.5080 0.0474 0.0574 -0.0753 235 PHE A CG 1570 C CD1 . PHE A 242 ? 0.3249 0.3858 0.5095 0.0497 0.0556 -0.0765 235 PHE A CD1 1571 C CD2 . PHE A 242 ? 0.3344 0.4109 0.5474 0.0498 0.0580 -0.0771 235 PHE A CD2 1572 C CE1 . PHE A 242 ? 0.3445 0.4047 0.5388 0.0546 0.0544 -0.0792 235 PHE A CE1 1573 C CE2 . PHE A 242 ? 0.3400 0.4165 0.5631 0.0549 0.0567 -0.0800 235 PHE A CE2 1574 C CZ . PHE A 242 ? 0.3594 0.4274 0.5726 0.0573 0.0548 -0.0809 235 PHE A CZ 1575 N N . ALA A 243 ? 0.3127 0.3876 0.5159 0.0443 0.0383 -0.0679 236 ALA A N 1576 C CA . ALA A 243 ? 0.3341 0.4159 0.5549 0.0457 0.0338 -0.0686 236 ALA A CA 1577 C C . ALA A 243 ? 0.3507 0.4379 0.5889 0.0495 0.0364 -0.0721 236 ALA A C 1578 O O . ALA A 243 ? 0.3392 0.4224 0.5758 0.0534 0.0349 -0.0735 236 ALA A O 1579 C CB . ALA A 243 ? 0.3333 0.4113 0.5506 0.0481 0.0229 -0.0668 236 ALA A CB 1580 N N . PRO A 244 ? 0.3707 0.4670 0.6265 0.0483 0.0404 -0.0736 237 PRO A N 1581 C CA . PRO A 244 ? 0.3810 0.4836 0.6559 0.0519 0.0429 -0.0770 237 PRO A CA 1582 C C . PRO A 244 ? 0.3768 0.4779 0.6586 0.0576 0.0327 -0.0781 237 PRO A C 1583 O O . PRO A 244 ? 0.3802 0.4800 0.6610 0.0582 0.0233 -0.0766 237 PRO A O 1584 C CB . PRO A 244 ? 0.3830 0.4956 0.6765 0.0491 0.0461 -0.0774 237 PRO A CB 1585 C CG . PRO A 244 ? 0.3958 0.5063 0.6759 0.0433 0.0503 -0.0742 237 PRO A CG 1586 C CD . PRO A 244 ? 0.3723 0.4734 0.6317 0.0433 0.0430 -0.0718 237 PRO A CD 1587 N N . GLY A 245 ? 0.3849 0.4853 0.6719 0.0619 0.0347 -0.0807 238 GLY A N 1588 C CA . GLY A 245 ? 0.3776 0.4770 0.6730 0.0679 0.0259 -0.0819 238 GLY A CA 1589 C C . GLY A 245 ? 0.3807 0.4693 0.6588 0.0706 0.0187 -0.0796 238 GLY A C 1590 O O . GLY A 245 ? 0.3943 0.4811 0.6778 0.0759 0.0109 -0.0800 238 GLY A O 1591 N N . VAL A 246 ? 0.3474 0.4287 0.6052 0.0672 0.0212 -0.0770 239 VAL A N 1592 C CA . VAL A 246 ? 0.3350 0.4057 0.5764 0.0693 0.0161 -0.0745 239 VAL A CA 1593 C C . VAL A 246 ? 0.3346 0.3996 0.5665 0.0689 0.0233 -0.0756 239 VAL A C 1594 O O . VAL A 246 ? 0.3412 0.4088 0.5717 0.0655 0.0318 -0.0772 239 VAL A O 1595 C CB . VAL A 246 ? 0.3299 0.3963 0.5564 0.0663 0.0107 -0.0705 239 VAL A CB 1596 C CG1 A VAL A 246 ? 0.3350 0.4091 0.5683 0.0622 0.0113 -0.0705 239 VAL A CG1 1597 C CG1 B VAL A 246 ? 0.3095 0.3649 0.5189 0.0681 0.0072 -0.0675 239 VAL A CG1 1598 C CG2 A VAL A 246 ? 0.3266 0.3842 0.5331 0.0639 0.0134 -0.0680 239 VAL A CG2 1599 C CG2 B VAL A 246 ? 0.3145 0.3859 0.5508 0.0677 0.0025 -0.0702 239 VAL A CG2 1600 N N A LYS A 247 ? 0.3406 0.3976 0.5666 0.0727 0.0198 -0.0750 240 LYS A N 1601 N N B LYS A 247 ? 0.3403 0.3970 0.5656 0.0726 0.0195 -0.0747 240 LYS A N 1602 C CA A LYS A 247 ? 0.3475 0.3983 0.5657 0.0727 0.0257 -0.0765 240 LYS A CA 1603 C CA B LYS A 247 ? 0.3458 0.3958 0.5630 0.0729 0.0246 -0.0760 240 LYS A CA 1604 C C A LYS A 247 ? 0.3528 0.3962 0.5516 0.0686 0.0267 -0.0738 240 LYS A C 1605 C C B LYS A 247 ? 0.3488 0.3924 0.5472 0.0682 0.0269 -0.0737 240 LYS A C 1606 O O A LYS A 247 ? 0.3432 0.3840 0.5338 0.0673 0.0215 -0.0700 240 LYS A O 1607 O O B LYS A 247 ? 0.3453 0.3873 0.5353 0.0661 0.0226 -0.0701 240 LYS A O 1608 C CB A LYS A 247 ? 0.3696 0.4148 0.5918 0.0787 0.0219 -0.0771 240 LYS A CB 1609 C CB B LYS A 247 ? 0.3527 0.3958 0.5709 0.0787 0.0190 -0.0754 240 LYS A CB 1610 C CG A LYS A 247 ? 0.3545 0.4067 0.5967 0.0833 0.0216 -0.0806 240 LYS A CG 1611 C CG B LYS A 247 ? 0.3502 0.3911 0.5666 0.0814 0.0091 -0.0716 240 LYS A CG 1612 C CD A LYS A 247 ? 0.4067 0.4645 0.6566 0.0820 0.0317 -0.0851 240 LYS A CD 1613 C CD B LYS A 247 ? 0.3424 0.3930 0.5725 0.0819 0.0052 -0.0725 240 LYS A CD 1614 C CE A LYS A 247 ? 0.4342 0.4973 0.7037 0.0874 0.0320 -0.0888 240 LYS A CE 1615 C CE B LYS A 247 ? 0.3428 0.3905 0.5670 0.0837 -0.0044 -0.0689 240 LYS A CE 1616 N NZ A LYS A 247 ? 0.4536 0.5245 0.7328 0.0861 0.0421 -0.0929 240 LYS A NZ 1617 N NZ B LYS A 247 ? 0.3481 0.3849 0.5610 0.0878 -0.0090 -0.0657 240 LYS A NZ 1618 N N . SER A 248 ? 0.3535 0.3937 0.5458 0.0668 0.0335 -0.0760 241 SER A N 1619 C CA . SER A 248 ? 0.3562 0.3893 0.5313 0.0630 0.0350 -0.0744 241 SER A CA 1620 C C . SER A 248 ? 0.3447 0.3682 0.5127 0.0653 0.0294 -0.0716 241 SER A C 1621 O O . SER A 248 ? 0.3499 0.3706 0.5249 0.0701 0.0270 -0.0723 241 SER A O 1622 C CB . SER A 248 ? 0.3896 0.4207 0.5614 0.0622 0.0425 -0.0786 241 SER A CB 1623 O OG . SER A 248 ? 0.4399 0.4782 0.6148 0.0599 0.0492 -0.0810 241 SER A OG 1624 N N . TYR A 249 ? 0.3281 0.3464 0.4826 0.0621 0.0280 -0.0683 242 TYR A N 1625 C CA . TYR A 249 ? 0.3245 0.3332 0.4716 0.0636 0.0245 -0.0655 242 TYR A CA 1626 C C . TYR A 249 ? 0.3367 0.3399 0.4862 0.0657 0.0276 -0.0689 242 TYR A C 1627 O O . TYR A 249 ? 0.3409 0.3456 0.4896 0.0637 0.0333 -0.0730 242 TYR A O 1628 C CB . TYR A 249 ? 0.3188 0.3236 0.4520 0.0590 0.0242 -0.0623 242 TYR A CB 1629 C CG . TYR A 249 ? 0.3198 0.3165 0.4474 0.0611 0.0195 -0.0577 242 TYR A CG 1630 C CD1 . TYR A 249 ? 0.3232 0.3205 0.4514 0.0639 0.0137 -0.0540 242 TYR A CD1 1631 C CD2 . TYR A 249 ? 0.3516 0.3398 0.4741 0.0608 0.0208 -0.0573 242 TYR A CD2 1632 C CE1 . TYR A 249 ? 0.3483 0.3377 0.4706 0.0666 0.0099 -0.0495 242 TYR A CE1 1633 C CE2 . TYR A 249 ? 0.3531 0.3335 0.4711 0.0629 0.0172 -0.0525 242 TYR A CE2 1634 C CZ . TYR A 249 ? 0.3620 0.3430 0.4792 0.0659 0.0121 -0.0485 242 TYR A CZ 1635 O OH . TYR A 249 ? 0.4040 0.3770 0.5159 0.0686 0.0090 -0.0435 242 TYR A OH 1636 N N . PRO A 250 ? 0.3502 0.3466 0.5020 0.0700 0.0240 -0.0672 243 PRO A N 1637 C CA . PRO A 250 ? 0.3595 0.3515 0.5092 0.0731 0.0175 -0.0620 243 PRO A CA 1638 C C . PRO A 250 ? 0.3684 0.3649 0.5288 0.0783 0.0126 -0.0616 243 PRO A C 1639 O O . PRO A 250 ? 0.3837 0.3757 0.5413 0.0817 0.0068 -0.0575 243 PRO A O 1640 C CB . PRO A 250 ? 0.3663 0.3475 0.5132 0.0751 0.0175 -0.0611 243 PRO A CB 1641 C CG . PRO A 250 ? 0.3752 0.3579 0.5310 0.0765 0.0220 -0.0671 243 PRO A CG 1642 C CD . PRO A 250 ? 0.3594 0.3500 0.5138 0.0719 0.0271 -0.0708 243 PRO A CD 1643 N N A ASP A 251 ? 0.3567 0.3618 0.5286 0.0788 0.0151 -0.0660 244 ASP A N 1644 N N B ASP A 251 ? 0.3616 0.3664 0.5341 0.0793 0.0147 -0.0659 244 ASP A N 1645 C CA A ASP A 251 ? 0.3682 0.3786 0.5536 0.0838 0.0108 -0.0669 244 ASP A CA 1646 C CA B ASP A 251 ? 0.3651 0.3742 0.5488 0.0843 0.0091 -0.0656 244 ASP A CA 1647 C C A ASP A 251 ? 0.3557 0.3734 0.5431 0.0827 0.0067 -0.0653 244 ASP A C 1648 C C B ASP A 251 ? 0.3550 0.3743 0.5444 0.0824 0.0077 -0.0662 244 ASP A C 1649 O O A ASP A 251 ? 0.3489 0.3697 0.5452 0.0870 0.0007 -0.0650 244 ASP A O 1650 O O B ASP A 251 ? 0.3549 0.3809 0.5580 0.0855 0.0051 -0.0681 244 ASP A O 1651 C CB A ASP A 251 ? 0.3754 0.3914 0.5744 0.0854 0.0160 -0.0725 244 ASP A CB 1652 C CB B ASP A 251 ? 0.3696 0.3783 0.5658 0.0895 0.0098 -0.0690 244 ASP A CB 1653 C CG A ASP A 251 ? 0.4169 0.4249 0.6150 0.0876 0.0190 -0.0746 244 ASP A CG 1654 C CG B ASP A 251 ? 0.3851 0.3819 0.5756 0.0928 0.0080 -0.0667 244 ASP A CG 1655 O OD1 A ASP A 251 ? 0.4493 0.4487 0.6442 0.0910 0.0148 -0.0717 244 ASP A OD1 1656 O OD1 B ASP A 251 ? 0.3945 0.3868 0.5848 0.0976 0.0015 -0.0631 244 ASP A OD1 1657 O OD2 A ASP A 251 ? 0.4807 0.4907 0.6812 0.0860 0.0258 -0.0791 244 ASP A OD2 1658 O OD2 B ASP A 251 ? 0.3681 0.3595 0.5538 0.0907 0.0130 -0.0684 244 ASP A OD2 1659 N N . GLY A 252 ? 0.3519 0.3719 0.5310 0.0771 0.0092 -0.0643 245 GLY A N 1660 C CA . GLY A 252 ? 0.3352 0.3618 0.5157 0.0752 0.0061 -0.0632 245 GLY A CA 1661 C C . GLY A 252 ? 0.3299 0.3545 0.4964 0.0696 0.0085 -0.0609 245 GLY A C 1662 O O . GLY A 252 ? 0.3421 0.3597 0.4980 0.0678 0.0114 -0.0598 245 GLY A O 1663 N N . TRP A 253 ? 0.3139 0.3443 0.4808 0.0668 0.0072 -0.0602 246 TRP A N 1664 C CA . TRP A 253 ? 0.3010 0.3292 0.4544 0.0620 0.0084 -0.0575 246 TRP A CA 1665 C C . TRP A 253 ? 0.2995 0.3329 0.4529 0.0567 0.0156 -0.0597 246 TRP A C 1666 O O . TRP A 253 ? 0.2876 0.3204 0.4313 0.0526 0.0165 -0.0578 246 TRP A O 1667 C CB . TRP A 253 ? 0.3002 0.3287 0.4499 0.0626 0.0015 -0.0544 246 TRP A CB 1668 C CG . TRP A 253 ? 0.3325 0.3690 0.4960 0.0643 -0.0025 -0.0564 246 TRP A CG 1669 C CD1 . TRP A 253 ? 0.3538 0.3909 0.5258 0.0698 -0.0090 -0.0569 246 TRP A CD1 1670 C CD2 . TRP A 253 ? 0.3301 0.3748 0.5007 0.0605 -0.0005 -0.0580 246 TRP A CD2 1671 N NE1 . TRP A 253 ? 0.3565 0.4022 0.5416 0.0695 -0.0115 -0.0592 246 TRP A NE1 1672 C CE2 . TRP A 253 ? 0.3267 0.3770 0.5114 0.0637 -0.0061 -0.0597 246 TRP A CE2 1673 C CE3 . TRP A 253 ? 0.3378 0.3853 0.5044 0.0548 0.0054 -0.0580 246 TRP A CE3 1674 C CZ2 . TRP A 253 ? 0.3268 0.3858 0.5232 0.0610 -0.0056 -0.0615 246 TRP A CZ2 1675 C CZ3 . TRP A 253 ? 0.3630 0.4185 0.5398 0.0523 0.0061 -0.0593 246 TRP A CZ3 1676 C CH2 . TRP A 253 ? 0.3300 0.3913 0.5223 0.0553 0.0008 -0.0611 246 TRP A CH2 1677 N N . ASN A 254 ? 0.2827 0.3204 0.4456 0.0571 0.0210 -0.0636 247 ASN A N 1678 C CA . ASN A 254 ? 0.2888 0.3305 0.4503 0.0527 0.0285 -0.0655 247 ASN A CA 1679 C C . ASN A 254 ? 0.2867 0.3223 0.4358 0.0505 0.0329 -0.0662 247 ASN A C 1680 O O . ASN A 254 ? 0.3022 0.3309 0.4474 0.0527 0.0315 -0.0662 247 ASN A O 1681 C CB . ASN A 254 ? 0.2906 0.3399 0.4673 0.0540 0.0333 -0.0694 247 ASN A CB 1682 C CG . ASN A 254 ? 0.2941 0.3522 0.4819 0.0526 0.0325 -0.0690 247 ASN A CG 1683 O OD1 . ASN A 254 ? 0.3044 0.3627 0.4865 0.0498 0.0294 -0.0663 247 ASN A OD1 1684 N ND2 . ASN A 254 ? 0.2776 0.3429 0.4820 0.0545 0.0354 -0.0720 247 ASN A ND2 1685 N N . LEU A 255 ? 0.2721 0.3099 0.4152 0.0463 0.0382 -0.0667 248 LEU A N 1686 C CA . LEU A 255 ? 0.2706 0.3031 0.4019 0.0442 0.0421 -0.0680 248 LEU A CA 1687 C C . LEU A 255 ? 0.2757 0.3087 0.4120 0.0462 0.0479 -0.0727 248 LEU A C 1688 O O . LEU A 255 ? 0.2857 0.3255 0.4303 0.0464 0.0527 -0.0747 248 LEU A O 1689 C CB . LEU A 255 ? 0.2595 0.2942 0.3821 0.0394 0.0452 -0.0669 248 LEU A CB 1690 C CG . LEU A 255 ? 0.2843 0.3137 0.3935 0.0370 0.0481 -0.0680 248 LEU A CG 1691 C CD1 . LEU A 255 ? 0.2587 0.2808 0.3592 0.0364 0.0431 -0.0656 248 LEU A CD1 1692 C CD2 . LEU A 255 ? 0.3037 0.3367 0.4066 0.0331 0.0518 -0.0670 248 LEU A CD2 1693 N N . PRO A 256 ? 0.2895 0.3153 0.4215 0.0479 0.0476 -0.0745 249 PRO A N 1694 C CA . PRO A 256 ? 0.2892 0.3144 0.4238 0.0498 0.0533 -0.0796 249 PRO A CA 1695 C C . PRO A 256 ? 0.2946 0.3199 0.4188 0.0466 0.0592 -0.0819 249 PRO A C 1696 O O . PRO A 256 ? 0.2902 0.3144 0.4039 0.0429 0.0581 -0.0794 249 PRO A O 1697 C CB . PRO A 256 ? 0.3078 0.3242 0.4400 0.0521 0.0503 -0.0805 249 PRO A CB 1698 C CG . PRO A 256 ? 0.2928 0.3050 0.4193 0.0508 0.0442 -0.0757 249 PRO A CG 1699 C CD . PRO A 256 ? 0.2843 0.3022 0.4094 0.0482 0.0424 -0.0720 249 PRO A CD 1700 N N . GLY A 257 ? 0.3014 0.3278 0.4278 0.0485 0.0654 -0.0866 250 GLY A N 1701 C CA . GLY A 257 ? 0.3067 0.3332 0.4223 0.0461 0.0713 -0.0887 250 GLY A CA 1702 C C . GLY A 257 ? 0.3018 0.3204 0.4027 0.0441 0.0693 -0.0897 250 GLY A C 1703 O O . GLY A 257 ? 0.3103 0.3286 0.4001 0.0417 0.0725 -0.0905 250 GLY A O 1704 N N . GLY A 258 ? 0.2968 0.3089 0.3980 0.0451 0.0642 -0.0897 251 GLY A N 1705 C CA . GLY A 258 ? 0.2967 0.3013 0.3864 0.0430 0.0613 -0.0903 251 GLY A CA 1706 C C . GLY A 258 ? 0.2949 0.2987 0.3800 0.0396 0.0559 -0.0848 251 GLY A C 1707 O O . GLY A 258 ? 0.2911 0.2899 0.3673 0.0373 0.0537 -0.0847 251 GLY A O 1708 N N . GLY A 259 ? 0.2870 0.2958 0.3783 0.0395 0.0539 -0.0804 252 GLY A N 1709 C CA . GLY A 259 ? 0.2672 0.2756 0.3539 0.0368 0.0492 -0.0752 252 GLY A CA 1710 C C . GLY A 259 ? 0.2644 0.2750 0.3411 0.0329 0.0508 -0.0742 252 GLY A C 1711 O O . GLY A 259 ? 0.2729 0.2879 0.3486 0.0325 0.0557 -0.0759 252 GLY A O 1712 N N . VAL A 260 ? 0.2635 0.2710 0.3331 0.0303 0.0470 -0.0712 253 VAL A N 1713 C CA . VAL A 260 ? 0.2493 0.2581 0.3090 0.0268 0.0477 -0.0701 253 VAL A CA 1714 C C . VAL A 260 ? 0.2553 0.2642 0.3129 0.0248 0.0431 -0.0650 253 VAL A C 1715 O O . VAL A 260 ? 0.2620 0.2669 0.3208 0.0253 0.0393 -0.0630 253 VAL A O 1716 C CB . VAL A 260 ? 0.2559 0.2593 0.3058 0.0255 0.0481 -0.0737 253 VAL A CB 1717 C CG1 . VAL A 260 ? 0.2721 0.2774 0.3117 0.0226 0.0492 -0.0729 253 VAL A CG1 1718 C CG2 . VAL A 260 ? 0.2770 0.2785 0.3283 0.0282 0.0521 -0.0796 253 VAL A CG2 1719 N N . GLN A 261 ? 0.2423 0.2554 0.2963 0.0226 0.0439 -0.0627 254 GLN A N 1720 C CA . GLN A 261 ? 0.2346 0.2482 0.2862 0.0207 0.0399 -0.0581 254 GLN A CA 1721 C C . GLN A 261 ? 0.2423 0.2526 0.2837 0.0180 0.0387 -0.0579 254 GLN A C 1722 O O . GLN A 261 ? 0.2528 0.2642 0.2873 0.0163 0.0412 -0.0592 254 GLN A O 1723 C CB . GLN A 261 ? 0.2294 0.2491 0.2838 0.0199 0.0413 -0.0562 254 GLN A CB 1724 C CG . GLN A 261 ? 0.2198 0.2401 0.2710 0.0180 0.0373 -0.0517 254 GLN A CG 1725 C CD . GLN A 261 ? 0.2340 0.2595 0.2869 0.0164 0.0390 -0.0501 254 GLN A CD 1726 O OE1 . GLN A 261 ? 0.2406 0.2660 0.2875 0.0141 0.0375 -0.0476 254 GLN A OE1 1727 N NE2 . GLN A 261 ? 0.2527 0.2827 0.3149 0.0177 0.0417 -0.0514 254 GLN A NE2 1728 N N . ARG A 262 ? 0.2461 0.2523 0.2865 0.0177 0.0350 -0.0561 255 ARG A N 1729 C CA . ARG A 262 ? 0.2422 0.2459 0.2749 0.0150 0.0329 -0.0551 255 ARG A CA 1730 C C . ARG A 262 ? 0.2325 0.2395 0.2618 0.0132 0.0316 -0.0512 255 ARG A C 1731 O O . ARG A 262 ? 0.2313 0.2416 0.2649 0.0141 0.0314 -0.0490 255 ARG A O 1732 C CB . ARG A 262 ? 0.2392 0.2379 0.2739 0.0153 0.0300 -0.0538 255 ARG A CB 1733 C CG . ARG A 262 ? 0.2360 0.2301 0.2731 0.0164 0.0309 -0.0582 255 ARG A CG 1734 C CD . ARG A 262 ? 0.2394 0.2289 0.2820 0.0176 0.0288 -0.0557 255 ARG A CD 1735 N NE . ARG A 262 ? 0.2611 0.2460 0.3078 0.0191 0.0298 -0.0597 255 ARG A NE 1736 C CZ . ARG A 262 ? 0.2668 0.2521 0.3185 0.0221 0.0316 -0.0618 255 ARG A CZ 1737 N NH1 . ARG A 262 ? 0.2691 0.2596 0.3233 0.0237 0.0327 -0.0606 255 ARG A NH1 1738 N NH2 . ARG A 262 ? 0.2660 0.2465 0.3212 0.0234 0.0322 -0.0656 255 ARG A NH2 1739 N N . GLY A 263 ? 0.2387 0.2448 0.2610 0.0108 0.0303 -0.0506 256 GLY A N 1740 C CA . GLY A 263 ? 0.2290 0.2374 0.2488 0.0094 0.0284 -0.0465 256 GLY A CA 1741 C C . GLY A 263 ? 0.2483 0.2565 0.2598 0.0070 0.0279 -0.0467 256 GLY A C 1742 O O . GLY A 263 ? 0.2388 0.2465 0.2456 0.0066 0.0299 -0.0499 256 GLY A O 1743 N N . ASN A 264 ? 0.2251 0.2335 0.2346 0.0058 0.0252 -0.0434 257 ASN A N 1744 C CA . ASN A 264 ? 0.2287 0.2369 0.2308 0.0038 0.0242 -0.0435 257 ASN A CA 1745 C C . ASN A 264 ? 0.2282 0.2392 0.2257 0.0031 0.0264 -0.0429 257 ASN A C 1746 O O . ASN A 264 ? 0.2271 0.2408 0.2286 0.0037 0.0281 -0.0414 257 ASN A O 1747 C CB . ASN A 264 ? 0.2118 0.2194 0.2137 0.0028 0.0208 -0.0403 257 ASN A CB 1748 C CG . ASN A 264 ? 0.2168 0.2270 0.2184 0.0027 0.0202 -0.0365 257 ASN A CG 1749 O OD1 . ASN A 264 ? 0.2206 0.2325 0.2175 0.0016 0.0205 -0.0358 257 ASN A OD1 1750 N ND2 . ASN A 264 ? 0.2347 0.2449 0.2409 0.0041 0.0191 -0.0340 257 ASN A ND2 1751 N N . ILE A 265 ? 0.2246 0.2347 0.2140 0.0019 0.0262 -0.0440 258 ILE A N 1752 C CA . ILE A 265 ? 0.2355 0.2472 0.2191 0.0014 0.0288 -0.0431 258 ILE A CA 1753 C C . ILE A 265 ? 0.2430 0.2545 0.2203 -0.0001 0.0261 -0.0405 258 ILE A C 1754 O O . ILE A 265 ? 0.2675 0.2785 0.2369 -0.0005 0.0273 -0.0403 258 ILE A O 1755 C CB . ILE A 265 ? 0.2584 0.2687 0.2359 0.0022 0.0322 -0.0470 258 ILE A CB 1756 C CG1 . ILE A 265 ? 0.2564 0.2629 0.2293 0.0022 0.0291 -0.0506 258 ILE A CG1 1757 C CG2 . ILE A 265 ? 0.2468 0.2583 0.2315 0.0038 0.0359 -0.0490 258 ILE A CG2 1758 C CD1 . ILE A 265 ? 0.3064 0.3107 0.2694 0.0033 0.0315 -0.0547 258 ILE A CD1 1759 N N . LEU A 266 ? 0.2430 0.2545 0.2238 -0.0006 0.0225 -0.0382 259 LEU A N 1760 C CA . LEU A 266 ? 0.2420 0.2535 0.2183 -0.0017 0.0197 -0.0357 259 LEU A CA 1761 C C . LEU A 266 ? 0.2455 0.2589 0.2215 -0.0021 0.0210 -0.0323 259 LEU A C 1762 O O . LEU A 266 ? 0.2498 0.2651 0.2315 -0.0016 0.0230 -0.0315 259 LEU A O 1763 C CB . LEU A 266 ? 0.2255 0.2366 0.2066 -0.0018 0.0162 -0.0342 259 LEU A CB 1764 C CG . LEU A 266 ? 0.2346 0.2437 0.2179 -0.0018 0.0145 -0.0370 259 LEU A CG 1765 C CD1 . LEU A 266 ? 0.2549 0.2638 0.2438 -0.0018 0.0123 -0.0345 259 LEU A CD1 1766 C CD2 . LEU A 266 ? 0.2561 0.2638 0.2326 -0.0026 0.0124 -0.0393 259 LEU A CD2 1767 N N . ASN A 267 ? 0.2376 0.2505 0.2076 -0.0029 0.0193 -0.0304 260 ASN A N 1768 C CA . ASN A 267 ? 0.2420 0.2560 0.2123 -0.0035 0.0195 -0.0268 260 ASN A CA 1769 C C . ASN A 267 ? 0.2408 0.2544 0.2108 -0.0037 0.0153 -0.0247 260 ASN A C 1770 O O . ASN A 267 ? 0.2546 0.2672 0.2187 -0.0042 0.0137 -0.0234 260 ASN A O 1771 C CB . ASN A 267 ? 0.2559 0.2691 0.2187 -0.0040 0.0223 -0.0259 260 ASN A CB 1772 C CG . ASN A 267 ? 0.2831 0.2976 0.2485 -0.0038 0.0275 -0.0270 260 ASN A CG 1773 O OD1 . ASN A 267 ? 0.3066 0.3231 0.2783 -0.0042 0.0295 -0.0252 260 ASN A OD1 1774 N ND2 . ASN A 267 ? 0.2838 0.2971 0.2453 -0.0030 0.0296 -0.0303 260 ASN A ND2 1775 N N . LEU A 268 ? 0.2278 0.2421 0.2042 -0.0030 0.0137 -0.0243 261 LEU A N 1776 C CA . LEU A 268 ? 0.2216 0.2356 0.1985 -0.0029 0.0103 -0.0227 261 LEU A CA 1777 C C . LEU A 268 ? 0.2225 0.2369 0.1994 -0.0028 0.0093 -0.0196 261 LEU A C 1778 O O . LEU A 268 ? 0.2146 0.2287 0.1901 -0.0028 0.0068 -0.0182 261 LEU A O 1779 C CB . LEU A 268 ? 0.2203 0.2343 0.2034 -0.0019 0.0097 -0.0229 261 LEU A CB 1780 C CG . LEU A 268 ? 0.2080 0.2208 0.1924 -0.0020 0.0099 -0.0257 261 LEU A CG 1781 C CD1 . LEU A 268 ? 0.2286 0.2409 0.2193 -0.0008 0.0101 -0.0250 261 LEU A CD1 1782 C CD2 . LEU A 268 ? 0.2363 0.2486 0.2180 -0.0030 0.0073 -0.0266 261 LEU A CD2 1783 N N . ASN A 269 ? 0.2187 0.2339 0.1979 -0.0028 0.0112 -0.0189 262 ASN A N 1784 C CA . ASN A 269 ? 0.2280 0.2433 0.2084 -0.0027 0.0098 -0.0164 262 ASN A CA 1785 C C . ASN A 269 ? 0.2323 0.2472 0.2144 -0.0013 0.0070 -0.0153 262 ASN A C 1786 O O . ASN A 269 ? 0.2394 0.2537 0.2198 -0.0011 0.0051 -0.0135 262 ASN A O 1787 C CB . ASN A 269 ? 0.2266 0.2408 0.2012 -0.0038 0.0098 -0.0147 262 ASN A CB 1788 C CG . ASN A 269 ? 0.2834 0.2975 0.2558 -0.0049 0.0135 -0.0149 262 ASN A CG 1789 O OD1 . ASN A 269 ? 0.2859 0.3014 0.2636 -0.0050 0.0158 -0.0156 262 ASN A OD1 1790 N ND2 . ASN A 269 ? 0.2954 0.3080 0.2602 -0.0055 0.0140 -0.0143 262 ASN A ND2 1791 N N . GLY A 270 ? 0.2094 0.2245 0.1948 0.0000 0.0070 -0.0163 263 GLY A N 1792 C CA . GLY A 270 ? 0.2059 0.2203 0.1926 0.0018 0.0052 -0.0150 263 GLY A CA 1793 C C . GLY A 270 ? 0.2162 0.2303 0.2020 0.0017 0.0044 -0.0146 263 GLY A C 1794 O O . GLY A 270 ? 0.2175 0.2312 0.2045 0.0032 0.0038 -0.0133 263 GLY A O 1795 N N . ALA A 271 ? 0.1941 0.2085 0.1782 0.0001 0.0045 -0.0159 264 ALA A N 1796 C CA . ALA A 271 ? 0.2043 0.2188 0.1888 -0.0003 0.0029 -0.0158 264 ALA A CA 1797 C C . ALA A 271 ? 0.2106 0.2249 0.2001 0.0004 0.0037 -0.0160 264 ALA A C 1798 O O . ALA A 271 ? 0.2284 0.2432 0.2204 0.0005 0.0029 -0.0151 264 ALA A O 1799 C CB . ALA A 271 ? 0.2084 0.2230 0.1892 -0.0019 0.0019 -0.0175 264 ALA A CB 1800 N N . GLY A 272 ? 0.2041 0.2175 0.1956 0.0008 0.0055 -0.0171 265 GLY A N 1801 C CA . GLY A 272 ? 0.1951 0.2076 0.1913 0.0012 0.0065 -0.0172 265 GLY A CA 1802 C C . GLY A 272 ? 0.2020 0.2143 0.1998 -0.0007 0.0059 -0.0200 265 GLY A C 1803 O O . GLY A 272 ? 0.2138 0.2262 0.2082 -0.0018 0.0055 -0.0224 265 GLY A O 1804 N N . ASP A 273 ? 0.1961 0.2081 0.1993 -0.0011 0.0059 -0.0198 266 ASP A N 1805 C CA . ASP A 273 ? 0.2174 0.2290 0.2232 -0.0029 0.0045 -0.0230 266 ASP A CA 1806 C C . ASP A 273 ? 0.2260 0.2387 0.2262 -0.0040 0.0016 -0.0250 266 ASP A C 1807 O O . ASP A 273 ? 0.2305 0.2448 0.2293 -0.0039 -0.0001 -0.0233 266 ASP A O 1808 C CB . ASP A 273 ? 0.2115 0.2234 0.2250 -0.0034 0.0044 -0.0219 266 ASP A CB 1809 C CG . ASP A 273 ? 0.2246 0.2366 0.2421 -0.0055 0.0017 -0.0254 266 ASP A CG 1810 O OD1 . ASP A 273 ? 0.2328 0.2432 0.2492 -0.0062 0.0011 -0.0289 266 ASP A OD1 1811 O OD2 . ASP A 273 ? 0.2367 0.2506 0.2590 -0.0061 0.0000 -0.0248 266 ASP A OD2 1812 N N . PRO A 274 ? 0.2273 0.2389 0.2240 -0.0047 0.0011 -0.0285 267 PRO A N 1813 C CA . PRO A 274 ? 0.2422 0.2542 0.2317 -0.0052 -0.0013 -0.0300 267 PRO A CA 1814 C C . PRO A 274 ? 0.2372 0.2503 0.2284 -0.0058 -0.0053 -0.0304 267 PRO A C 1815 O O . PRO A 274 ? 0.2522 0.2656 0.2370 -0.0057 -0.0077 -0.0301 267 PRO A O 1816 C CB . PRO A 274 ? 0.2482 0.2581 0.2346 -0.0055 -0.0010 -0.0343 267 PRO A CB 1817 C CG . PRO A 274 ? 0.2529 0.2620 0.2430 -0.0048 0.0026 -0.0341 267 PRO A CG 1818 C CD . PRO A 274 ? 0.2388 0.2485 0.2367 -0.0045 0.0033 -0.0308 267 PRO A CD 1819 N N . LEU A 275 ? 0.2348 0.2485 0.2351 -0.0065 -0.0062 -0.0308 268 LEU A N 1820 C CA . LEU A 275 ? 0.2317 0.2469 0.2356 -0.0072 -0.0103 -0.0318 268 LEU A CA 1821 C C . LEU A 275 ? 0.2148 0.2326 0.2229 -0.0067 -0.0104 -0.0280 268 LEU A C 1822 O O . LEU A 275 ? 0.2256 0.2452 0.2364 -0.0069 -0.0141 -0.0286 268 LEU A O 1823 C CB . LEU A 275 ? 0.2306 0.2452 0.2439 -0.0086 -0.0115 -0.0348 268 LEU A CB 1824 C CG . LEU A 275 ? 0.2408 0.2526 0.2512 -0.0090 -0.0118 -0.0393 268 LEU A CG 1825 C CD1 . LEU A 275 ? 0.2765 0.2876 0.2978 -0.0105 -0.0136 -0.0423 268 LEU A CD1 1826 C CD2 . LEU A 275 ? 0.2812 0.2921 0.2801 -0.0084 -0.0151 -0.0423 268 LEU A CD2 1827 N N . THR A 276 ? 0.2046 0.2224 0.2128 -0.0055 -0.0067 -0.0244 269 THR A N 1828 C CA . THR A 276 ? 0.2046 0.2244 0.2172 -0.0046 -0.0061 -0.0209 269 THR A CA 1829 C C . THR A 276 ? 0.2086 0.2282 0.2150 -0.0029 -0.0045 -0.0179 269 THR A C 1830 O O . THR A 276 ? 0.2159 0.2356 0.2248 -0.0015 -0.0019 -0.0151 269 THR A O 1831 C CB . THR A 276 ? 0.1968 0.2168 0.2192 -0.0046 -0.0028 -0.0193 269 THR A CB 1832 O OG1 . THR A 276 ? 0.2036 0.2210 0.2237 -0.0037 0.0008 -0.0184 269 THR A OG1 1833 C CG2 . THR A 276 ? 0.2140 0.2346 0.2457 -0.0065 -0.0048 -0.0221 269 THR A CG2 1834 N N . PRO A 277 ? 0.2157 0.2346 0.2138 -0.0029 -0.0060 -0.0184 270 PRO A N 1835 C CA . PRO A 277 ? 0.2139 0.2322 0.2075 -0.0016 -0.0046 -0.0158 270 PRO A CA 1836 C C . PRO A 277 ? 0.2219 0.2415 0.2179 -0.0002 -0.0051 -0.0133 270 PRO A C 1837 O O . PRO A 277 ? 0.2309 0.2519 0.2283 -0.0004 -0.0080 -0.0134 270 PRO A O 1838 C CB . PRO A 277 ? 0.2230 0.2403 0.2085 -0.0022 -0.0061 -0.0167 270 PRO A CB 1839 C CG . PRO A 277 ? 0.2293 0.2470 0.2144 -0.0031 -0.0096 -0.0190 270 PRO A CG 1840 C CD . PRO A 277 ? 0.2394 0.2577 0.2318 -0.0039 -0.0090 -0.0211 270 PRO A CD 1841 N N . GLY A 278 ? 0.2163 0.2353 0.2128 0.0015 -0.0026 -0.0112 271 GLY A N 1842 C CA . GLY A 278 ? 0.2112 0.2309 0.2091 0.0034 -0.0025 -0.0089 271 GLY A CA 1843 C C . GLY A 278 ? 0.2218 0.2424 0.2263 0.0045 0.0000 -0.0075 271 GLY A C 1844 O O . GLY A 278 ? 0.2387 0.2593 0.2434 0.0067 0.0013 -0.0055 271 GLY A O 1845 N N . TYR A 279 ? 0.2139 0.2351 0.2241 0.0030 0.0009 -0.0086 272 TYR A N 1846 C CA . TYR A 279 ? 0.2126 0.2350 0.2311 0.0035 0.0034 -0.0071 272 TYR A CA 1847 C C . TYR A 279 ? 0.1968 0.2176 0.2189 0.0026 0.0060 -0.0075 272 TYR A C 1848 O O . TYR A 279 ? 0.2094 0.2293 0.2303 0.0008 0.0045 -0.0102 272 TYR A O 1849 C CB . TYR A 279 ? 0.2106 0.2363 0.2363 0.0021 0.0006 -0.0083 272 TYR A CB 1850 C CG . TYR A 279 ? 0.2273 0.2542 0.2491 0.0030 -0.0025 -0.0080 272 TYR A CG 1851 C CD1 . TYR A 279 ? 0.2102 0.2379 0.2329 0.0054 -0.0010 -0.0056 272 TYR A CD1 1852 C CD2 . TYR A 279 ? 0.2269 0.2533 0.2429 0.0019 -0.0066 -0.0100 272 TYR A CD2 1853 C CE1 . TYR A 279 ? 0.2183 0.2464 0.2373 0.0065 -0.0039 -0.0053 272 TYR A CE1 1854 C CE2 . TYR A 279 ? 0.2248 0.2515 0.2366 0.0029 -0.0092 -0.0093 272 TYR A CE2 1855 C CZ . TYR A 279 ? 0.2278 0.2554 0.2418 0.0051 -0.0081 -0.0070 272 TYR A CZ 1856 O OH . TYR A 279 ? 0.2170 0.2443 0.2271 0.0062 -0.0109 -0.0063 272 TYR A OH 1857 N N . PRO A 280 ? 0.2096 0.2296 0.2361 0.0040 0.0101 -0.0049 273 PRO A N 1858 C CA . PRO A 280 ? 0.2111 0.2288 0.2409 0.0033 0.0127 -0.0048 273 PRO A CA 1859 C C . PRO A 280 ? 0.2095 0.2285 0.2483 0.0002 0.0112 -0.0074 273 PRO A C 1860 O O . PRO A 280 ? 0.2197 0.2417 0.2657 -0.0009 0.0098 -0.0078 273 PRO A O 1861 C CB . PRO A 280 ? 0.2157 0.2321 0.2478 0.0059 0.0178 -0.0007 273 PRO A CB 1862 C CG . PRO A 280 ? 0.2195 0.2390 0.2540 0.0068 0.0177 0.0006 273 PRO A CG 1863 C CD . PRO A 280 ? 0.2038 0.2245 0.2314 0.0065 0.0129 -0.0017 273 PRO A CD 1864 N N . ALA A 281 ? 0.2082 0.2248 0.2469 -0.0010 0.0112 -0.0093 274 ALA A N 1865 C CA . ALA A 281 ? 0.2134 0.2301 0.2599 -0.0038 0.0095 -0.0124 274 ALA A CA 1866 C C . ALA A 281 ? 0.2214 0.2374 0.2790 -0.0042 0.0134 -0.0100 274 ALA A C 1867 O O . ALA A 281 ? 0.2360 0.2490 0.2971 -0.0049 0.0153 -0.0103 274 ALA A O 1868 C CB . ALA A 281 ? 0.2200 0.2342 0.2617 -0.0045 0.0083 -0.0155 274 ALA A CB 1869 N N . ASN A 282 ? 0.2259 0.2447 0.2892 -0.0037 0.0150 -0.0074 275 ASN A N 1870 C CA . ASN A 282 ? 0.2495 0.2680 0.3240 -0.0040 0.0198 -0.0043 275 ASN A CA 1871 C C . ASN A 282 ? 0.2650 0.2857 0.3534 -0.0075 0.0173 -0.0074 275 ASN A C 1872 O O . ASN A 282 ? 0.2546 0.2761 0.3418 -0.0093 0.0117 -0.0122 275 ASN A O 1873 C CB . ASN A 282 ? 0.2544 0.2750 0.3287 -0.0014 0.0233 -0.0001 275 ASN A CB 1874 C CG . ASN A 282 ? 0.2727 0.2980 0.3489 -0.0018 0.0193 -0.0018 275 ASN A CG 1875 O OD1 . ASN A 282 ? 0.2800 0.3079 0.3622 -0.0044 0.0145 -0.0056 275 ASN A OD1 1876 N ND2 . ASN A 282 ? 0.3038 0.3302 0.3746 0.0011 0.0209 0.0007 275 ASN A ND2 1877 N N C GLU A 283 ? 0.2880 0.3099 0.3890 -0.0082 0.0211 -0.0047 276 GLU A N 1878 N N D GLU A 283 ? 0.2760 0.2978 0.3769 -0.0082 0.0212 -0.0047 276 GLU A N 1879 C CA C GLU A 283 ? 0.3075 0.3307 0.4233 -0.0116 0.0191 -0.0076 276 GLU A CA 1880 C CA D GLU A 283 ? 0.2977 0.3210 0.4137 -0.0116 0.0192 -0.0075 276 GLU A CA 1881 C C C GLU A 283 ? 0.3028 0.3312 0.4239 -0.0132 0.0126 -0.0117 276 GLU A C 1882 C C D GLU A 283 ? 0.2955 0.3239 0.4160 -0.0131 0.0124 -0.0118 276 GLU A C 1883 O O C GLU A 283 ? 0.3029 0.3321 0.4321 -0.0158 0.0080 -0.0161 276 GLU A O 1884 O O D GLU A 283 ? 0.3060 0.3353 0.4353 -0.0158 0.0081 -0.0160 276 GLU A O 1885 C CB C GLU A 283 ? 0.3340 0.3567 0.4630 -0.0120 0.0261 -0.0030 276 GLU A CB 1886 C CB D GLU A 283 ? 0.3052 0.3288 0.4346 -0.0119 0.0260 -0.0028 276 GLU A CB 1887 C CG C GLU A 283 ? 0.3943 0.4170 0.5399 -0.0158 0.0249 -0.0056 276 GLU A CG 1888 C CG D GLU A 283 ? 0.3443 0.3660 0.4876 -0.0151 0.0265 -0.0043 276 GLU A CG 1889 C CD C GLU A 283 ? 0.4767 0.4936 0.6204 -0.0170 0.0245 -0.0077 276 GLU A CD 1890 C CD D GLU A 283 ? 0.3864 0.4014 0.5240 -0.0144 0.0301 -0.0026 276 GLU A CD 1891 O OE1 C GLU A 283 ? 0.5271 0.5392 0.6645 -0.0151 0.0297 -0.0038 276 GLU A OE1 1892 O OE1 D GLU A 283 ? 0.3757 0.3882 0.5167 -0.0167 0.0268 -0.0067 276 GLU A OE1 1893 O OE2 C GLU A 283 ? 0.5223 0.5394 0.6714 -0.0196 0.0188 -0.0133 276 GLU A OE2 1894 O OE2 D GLU A 283 ? 0.4177 0.4296 0.5474 -0.0113 0.0359 0.0026 276 GLU A OE2 1895 N N . TYR A 284 ? 0.2911 0.3230 0.4077 -0.0112 0.0119 -0.0102 277 TYR A N 1896 C CA . TYR A 284 ? 0.2934 0.3300 0.4143 -0.0120 0.0057 -0.0134 277 TYR A CA 1897 C C . TYR A 284 ? 0.2941 0.3304 0.3999 -0.0108 0.0002 -0.0159 277 TYR A C 1898 O O . TYR A 284 ? 0.3060 0.3456 0.4125 -0.0106 -0.0048 -0.0178 277 TYR A O 1899 C CB . TYR A 284 ? 0.2900 0.3313 0.4206 -0.0109 0.0088 -0.0100 277 TYR A CB 1900 C CG . TYR A 284 ? 0.2895 0.3297 0.4088 -0.0073 0.0135 -0.0055 277 TYR A CG 1901 C CD1 . TYR A 284 ? 0.2998 0.3413 0.4086 -0.0052 0.0098 -0.0061 277 TYR A CD1 1902 C CD2 . TYR A 284 ? 0.2825 0.3198 0.4011 -0.0056 0.0215 -0.0007 277 TYR A CD2 1903 C CE1 . TYR A 284 ? 0.3093 0.3494 0.4079 -0.0018 0.0137 -0.0026 277 TYR A CE1 1904 C CE2 . TYR A 284 ? 0.3094 0.3452 0.4166 -0.0018 0.0252 0.0029 277 TYR A CE2 1905 C CZ . TYR A 284 ? 0.3275 0.3648 0.4251 -0.0001 0.0210 0.0016 277 TYR A CZ 1906 O OH . TYR A 284 ? 0.3358 0.3714 0.4226 0.0036 0.0240 0.0045 277 TYR A OH 1907 N N . ALA A 285 ? 0.2956 0.3276 0.3881 -0.0099 0.0012 -0.0159 278 ALA A N 1908 C CA . ALA A 285 ? 0.3072 0.3385 0.3853 -0.0087 -0.0028 -0.0176 278 ALA A CA 1909 C C . ALA A 285 ? 0.3055 0.3379 0.3837 -0.0103 -0.0101 -0.0227 278 ALA A C 1910 O O . ALA A 285 ? 0.3174 0.3492 0.4030 -0.0124 -0.0122 -0.0262 278 ALA A O 1911 C CB . ALA A 285 ? 0.3094 0.3362 0.3761 -0.0079 -0.0004 -0.0173 278 ALA A CB 1912 N N . TYR A 286 ? 0.3030 0.3368 0.3732 -0.0090 -0.0139 -0.0232 279 TYR A N 1913 C CA . TYR A 286 ? 0.3210 0.3548 0.3867 -0.0097 -0.0208 -0.0277 279 TYR A CA 1914 C C . TYR A 286 ? 0.3153 0.3449 0.3664 -0.0093 -0.0204 -0.0288 279 TYR A C 1915 O O . TYR A 286 ? 0.3330 0.3612 0.3754 -0.0078 -0.0170 -0.0258 279 TYR A O 1916 C CB . TYR A 286 ? 0.3467 0.3834 0.4108 -0.0083 -0.0254 -0.0274 279 TYR A CB 1917 C CG A TYR A 286 ? 0.3318 0.3684 0.3931 -0.0088 -0.0332 -0.0322 279 TYR A CG 1918 C CG B TYR A 286 ? 0.3655 0.3999 0.4151 -0.0076 -0.0305 -0.0298 279 TYR A CG 1919 C CD1 A TYR A 286 ? 0.3523 0.3912 0.4264 -0.0104 -0.0375 -0.0359 279 TYR A CD1 1920 C CD1 B TYR A 286 ? 0.4011 0.4363 0.4513 -0.0078 -0.0377 -0.0339 279 TYR A CD1 1921 C CD2 A TYR A 286 ? 0.3602 0.3942 0.4060 -0.0075 -0.0361 -0.0330 279 TYR A CD2 1922 C CD2 B TYR A 286 ? 0.3906 0.4218 0.4264 -0.0064 -0.0279 -0.0280 279 TYR A CD2 1923 C CE1 A TYR A 286 ? 0.3861 0.4244 0.4564 -0.0104 -0.0453 -0.0407 279 TYR A CE1 1924 C CE1 B TYR A 286 ? 0.4136 0.4460 0.4493 -0.0067 -0.0417 -0.0356 279 TYR A CE1 1925 C CE2 A TYR A 286 ? 0.3790 0.4122 0.4203 -0.0074 -0.0431 -0.0372 279 TYR A CE2 1926 C CE2 B TYR A 286 ? 0.4196 0.4485 0.4425 -0.0057 -0.0314 -0.0296 279 TYR A CE2 1927 C CZ A TYR A 286 ? 0.3985 0.4338 0.4515 -0.0087 -0.0480 -0.0413 279 TYR A CZ 1928 C CZ B TYR A 286 ? 0.4312 0.4604 0.4533 -0.0057 -0.0381 -0.0332 279 TYR A CZ 1929 O OH A TYR A 286 ? 0.4349 0.4690 0.4823 -0.0081 -0.0557 -0.0459 279 TYR A OH 1930 O OH B TYR A 286 ? 0.4599 0.4860 0.4677 -0.0046 -0.0412 -0.0344 279 TYR A OH 1931 N N . ARG A 287 ? 0.2825 0.3100 0.3318 -0.0105 -0.0235 -0.0333 280 ARG A N 1932 C CA . ARG A 287 ? 0.2796 0.3035 0.3164 -0.0101 -0.0225 -0.0347 280 ARG A CA 1933 C C . ARG A 287 ? 0.2983 0.3212 0.3241 -0.0093 -0.0276 -0.0374 280 ARG A C 1934 O O . ARG A 287 ? 0.3042 0.3280 0.3328 -0.0097 -0.0334 -0.0409 280 ARG A O 1935 C CB A ARG A 287 ? 0.2871 0.3084 0.3288 -0.0116 -0.0213 -0.0378 280 ARG A CB 1936 C CB B ARG A 287 ? 0.2717 0.2929 0.3130 -0.0115 -0.0216 -0.0379 280 ARG A CB 1937 C CG A ARG A 287 ? 0.2990 0.3188 0.3444 -0.0115 -0.0147 -0.0344 280 ARG A CG 1938 C CG B ARG A 287 ? 0.2230 0.2441 0.2739 -0.0121 -0.0161 -0.0348 280 ARG A CG 1939 C CD A ARG A 287 ? 0.3464 0.3679 0.4062 -0.0123 -0.0119 -0.0317 280 ARG A CD 1940 C CD B ARG A 287 ? 0.1443 0.1619 0.1976 -0.0131 -0.0146 -0.0375 280 ARG A CD 1941 N NE A ARG A 287 ? 0.3297 0.3488 0.3906 -0.0117 -0.0057 -0.0283 280 ARG A NE 1942 N NE B ARG A 287 ? 0.1412 0.1578 0.1993 -0.0127 -0.0086 -0.0333 280 ARG A NE 1943 C CZ A ARG A 287 ? 0.3347 0.3542 0.4054 -0.0118 -0.0015 -0.0247 280 ARG A CZ 1944 C CZ B ARG A 287 ? 0.1369 0.1549 0.2071 -0.0134 -0.0060 -0.0305 280 ARG A CZ 1945 N NH1 A ARG A 287 ? 0.3478 0.3707 0.4294 -0.0127 -0.0025 -0.0242 280 ARG A NH1 1946 N NH1 B ARG A 287 ? 0.1475 0.1684 0.2281 -0.0149 -0.0092 -0.0319 280 ARG A NH1 1947 N NH2 A ARG A 287 ? 0.2764 0.2931 0.3460 -0.0106 0.0038 -0.0215 280 ARG A NH2 1948 N NH2 B ARG A 287 ? 0.1687 0.1849 0.2407 -0.0125 -0.0003 -0.0263 280 ARG A NH2 1949 N N . ARG A 288 ? 0.2898 0.3107 0.3030 -0.0082 -0.0256 -0.0360 281 ARG A N 1950 C CA . ARG A 288 ? 0.3113 0.3300 0.3121 -0.0073 -0.0292 -0.0386 281 ARG A CA 1951 C C . ARG A 288 ? 0.3213 0.3375 0.3213 -0.0081 -0.0314 -0.0441 281 ARG A C 1952 O O . ARG A 288 ? 0.3179 0.3332 0.3244 -0.0092 -0.0286 -0.0453 281 ARG A O 1953 C CB . ARG A 288 ? 0.2997 0.3164 0.2890 -0.0063 -0.0252 -0.0360 281 ARG A CB 1954 C CG . ARG A 288 ? 0.3137 0.3319 0.3021 -0.0054 -0.0239 -0.0312 281 ARG A CG 1955 C CD . ARG A 288 ? 0.3452 0.3615 0.3233 -0.0047 -0.0207 -0.0291 281 ARG A CD 1956 N NE . ARG A 288 ? 0.3544 0.3716 0.3315 -0.0038 -0.0203 -0.0249 281 ARG A NE 1957 C CZ . ARG A 288 ? 0.3825 0.3980 0.3514 -0.0031 -0.0184 -0.0226 281 ARG A CZ 1958 N NH1 . ARG A 288 ? 0.3697 0.3829 0.3308 -0.0033 -0.0164 -0.0237 281 ARG A NH1 1959 N NH2 . ARG A 288 ? 0.3882 0.4042 0.3573 -0.0023 -0.0184 -0.0192 281 ARG A NH2 1960 N N . GLY A 289 ? 0.3504 0.3652 0.3422 -0.0072 -0.0369 -0.0475 282 GLY A N 1961 C CA . GLY A 289 ? 0.3754 0.3869 0.3617 -0.0071 -0.0389 -0.0529 282 GLY A CA 1962 C C . GLY A 289 ? 0.3845 0.3932 0.3604 -0.0064 -0.0332 -0.0521 282 GLY A C 1963 O O . GLY A 289 ? 0.3750 0.3841 0.3452 -0.0057 -0.0294 -0.0476 282 GLY A O 1964 N N . ILE A 290 ? 0.4054 0.4113 0.3798 -0.0065 -0.0326 -0.0565 283 ILE A N 1965 C CA . ILE A 290 ? 0.4115 0.4150 0.3777 -0.0057 -0.0270 -0.0562 283 ILE A CA 1966 C C . ILE A 290 ? 0.4218 0.4241 0.3728 -0.0040 -0.0259 -0.0543 283 ILE A C 1967 O O . ILE A 290 ? 0.4261 0.4284 0.3735 -0.0037 -0.0203 -0.0509 283 ILE A O 1968 C CB A ILE A 290 ? 0.4212 0.4216 0.3884 -0.0058 -0.0273 -0.0622 283 ILE A CB 1969 C CB B ILE A 290 ? 0.4152 0.4155 0.3810 -0.0056 -0.0272 -0.0622 283 ILE A CB 1970 C CG1 A ILE A 290 ? 0.4313 0.4303 0.3960 -0.0054 -0.0206 -0.0615 283 ILE A CG1 1971 C CG1 B ILE A 290 ? 0.3978 0.3987 0.3788 -0.0075 -0.0256 -0.0627 283 ILE A CG1 1972 C CG2 A ILE A 290 ? 0.4501 0.4476 0.4074 -0.0044 -0.0332 -0.0679 283 ILE A CG2 1973 C CG2 B ILE A 290 ? 0.4088 0.4066 0.3630 -0.0041 -0.0221 -0.0625 283 ILE A CG2 1974 C CD1 A ILE A 290 ? 0.3956 0.3964 0.3731 -0.0067 -0.0167 -0.0582 283 ILE A CD1 1975 C CD1 B ILE A 290 ? 0.3767 0.3784 0.3613 -0.0076 -0.0188 -0.0582 283 ILE A CD1 1976 N N . ALA A 291 ? 0.4362 0.4371 0.3786 -0.0027 -0.0313 -0.0561 284 ALA A N 1977 C CA . ALA A 291 ? 0.4508 0.4497 0.3779 -0.0008 -0.0300 -0.0537 284 ALA A CA 1978 C C . ALA A 291 ? 0.4421 0.4432 0.3700 -0.0011 -0.0271 -0.0471 284 ALA A C 1979 O O . ALA A 291 ? 0.4579 0.4574 0.3755 -0.0001 -0.0236 -0.0442 284 ALA A O 1980 C CB . ALA A 291 ? 0.4731 0.4696 0.3902 0.0012 -0.0372 -0.0570 284 ALA A CB 1981 N N A GLU A 292 ? 0.4246 0.4292 0.3649 -0.0024 -0.0283 -0.0448 285 GLU A N 1982 N N B GLU A 292 ? 0.4236 0.4281 0.3638 -0.0024 -0.0285 -0.0448 285 GLU A N 1983 C CA A GLU A 292 ? 0.4087 0.4152 0.3507 -0.0025 -0.0259 -0.0391 285 GLU A CA 1984 C CA B GLU A 292 ? 0.4059 0.4125 0.3483 -0.0025 -0.0261 -0.0391 285 GLU A CA 1985 C C A GLU A 292 ? 0.3859 0.3943 0.3369 -0.0037 -0.0203 -0.0366 285 GLU A C 1986 C C B GLU A 292 ? 0.3852 0.3936 0.3360 -0.0037 -0.0203 -0.0366 285 GLU A C 1987 O O A GLU A 292 ? 0.3890 0.3989 0.3426 -0.0038 -0.0185 -0.0324 285 GLU A O 1988 O O B GLU A 292 ? 0.3804 0.3901 0.3332 -0.0037 -0.0183 -0.0323 285 GLU A O 1989 C CB A GLU A 292 ? 0.4195 0.4283 0.3673 -0.0023 -0.0312 -0.0379 285 GLU A CB 1990 C CB B GLU A 292 ? 0.4069 0.4161 0.3564 -0.0025 -0.0311 -0.0379 285 GLU A CB 1991 C CG A GLU A 292 ? 0.4359 0.4427 0.3736 -0.0005 -0.0373 -0.0392 285 GLU A CG 1992 C CG B GLU A 292 ? 0.4205 0.4288 0.3616 -0.0010 -0.0335 -0.0347 285 GLU A CG 1993 C CD A GLU A 292 ? 0.5159 0.5211 0.4517 -0.0001 -0.0424 -0.0455 285 GLU A CD 1994 C CD B GLU A 292 ? 0.4260 0.4366 0.3734 -0.0012 -0.0316 -0.0297 285 GLU A CD 1995 O OE1 A GLU A 292 ? 0.5231 0.5302 0.4710 -0.0016 -0.0439 -0.0486 285 GLU A OE1 1996 O OE1 B GLU A 292 ? 0.4190 0.4329 0.3789 -0.0021 -0.0313 -0.0294 285 GLU A OE1 1997 O OE2 A GLU A 292 ? 0.5602 0.5617 0.4820 0.0019 -0.0448 -0.0472 285 GLU A OE2 1998 O OE2 B GLU A 292 ? 0.4200 0.4290 0.3600 -0.0003 -0.0302 -0.0261 285 GLU A OE2 1999 N N . ALA A 293 ? 0.3679 0.3758 0.3232 -0.0044 -0.0181 -0.0394 286 ALA A N 2000 C CA . ALA A 293 ? 0.3576 0.3668 0.3208 -0.0051 -0.0133 -0.0374 286 ALA A CA 2001 C C . ALA A 293 ? 0.3501 0.3591 0.3078 -0.0046 -0.0088 -0.0340 286 ALA A C 2002 O O . ALA A 293 ? 0.3554 0.3627 0.3029 -0.0039 -0.0080 -0.0340 286 ALA A O 2003 C CB . ALA A 293 ? 0.3463 0.3542 0.3136 -0.0056 -0.0120 -0.0412 286 ALA A CB 2004 N N . VAL A 294 ? 0.3116 0.3222 0.2760 -0.0048 -0.0060 -0.0311 287 VAL A N 2005 C CA . VAL A 294 ? 0.3078 0.3184 0.2690 -0.0045 -0.0023 -0.0283 287 VAL A CA 2006 C C . VAL A 294 ? 0.3009 0.3108 0.2622 -0.0044 0.0017 -0.0302 287 VAL A C 2007 O O . VAL A 294 ? 0.2942 0.3042 0.2620 -0.0045 0.0025 -0.0317 287 VAL A O 2008 C CB . VAL A 294 ? 0.3018 0.3141 0.2693 -0.0043 -0.0016 -0.0247 287 VAL A CB 2009 C CG1 . VAL A 294 ? 0.2993 0.3115 0.2645 -0.0041 0.0017 -0.0224 287 VAL A CG1 2010 C CG2 . VAL A 294 ? 0.3199 0.3330 0.2877 -0.0041 -0.0051 -0.0229 287 VAL A CG2 2011 N N . GLY A 295 ? 0.2973 0.3063 0.2516 -0.0041 0.0044 -0.0298 288 GLY A N 2012 C CA . GLY A 295 ? 0.2892 0.2986 0.2457 -0.0039 0.0089 -0.0305 288 GLY A CA 2013 C C . GLY A 295 ? 0.2885 0.2964 0.2429 -0.0035 0.0105 -0.0348 288 GLY A C 2014 O O . GLY A 295 ? 0.2888 0.2973 0.2459 -0.0031 0.0143 -0.0354 288 GLY A O 2015 N N . LEU A 296 ? 0.2881 0.2942 0.2384 -0.0033 0.0074 -0.0380 289 LEU A N 2016 C CA . LEU A 296 ? 0.2925 0.2967 0.2408 -0.0026 0.0085 -0.0427 289 LEU A CA 2017 C C . LEU A 296 ? 0.3097 0.3125 0.2479 -0.0016 0.0123 -0.0436 289 LEU A C 2018 O O . LEU A 296 ? 0.3244 0.3263 0.2537 -0.0013 0.0120 -0.0416 289 LEU A O 2019 C CB A LEU A 296 ? 0.2963 0.2987 0.2435 -0.0028 0.0032 -0.0464 289 LEU A CB 2020 C CB B LEU A 296 ? 0.3012 0.3036 0.2490 -0.0028 0.0034 -0.0465 289 LEU A CB 2021 C CG A LEU A 296 ? 0.2903 0.2940 0.2480 -0.0039 -0.0003 -0.0458 289 LEU A CG 2022 C CG B LEU A 296 ? 0.3101 0.3129 0.2696 -0.0036 0.0020 -0.0479 289 LEU A CG 2023 C CD1 A LEU A 296 ? 0.2826 0.2846 0.2394 -0.0041 -0.0056 -0.0501 289 LEU A CD1 2024 C CD1 B LEU A 296 ? 0.2928 0.2981 0.2603 -0.0044 0.0014 -0.0433 289 LEU A CD1 2025 C CD2 A LEU A 296 ? 0.3107 0.3147 0.2785 -0.0041 0.0025 -0.0458 289 LEU A CD2 2026 C CD2 B LEU A 296 ? 0.3156 0.3164 0.2751 -0.0039 -0.0029 -0.0525 289 LEU A CD2 2027 N N . PRO A 297 ? 0.3212 0.3235 0.2605 -0.0007 0.0161 -0.0464 290 PRO A N 2028 C CA . PRO A 297 ? 0.3378 0.3387 0.2678 0.0006 0.0206 -0.0474 290 PRO A CA 2029 C C . PRO A 297 ? 0.3562 0.3533 0.2744 0.0019 0.0177 -0.0515 290 PRO A C 2030 O O . PRO A 297 ? 0.3536 0.3493 0.2740 0.0017 0.0127 -0.0551 290 PRO A O 2031 C CB . PRO A 297 ? 0.3412 0.3429 0.2781 0.0013 0.0248 -0.0498 290 PRO A CB 2032 C CG . PRO A 297 ? 0.3435 0.3452 0.2900 0.0007 0.0210 -0.0518 290 PRO A CG 2033 C CD . PRO A 297 ? 0.3225 0.3252 0.2720 -0.0008 0.0165 -0.0484 290 PRO A CD 2034 N N A SER A 298 ? 0.3624 0.3577 0.2684 0.0032 0.0208 -0.0508 291 SER A N 2035 N N B SER A 298 ? 0.3623 0.3574 0.2681 0.0032 0.0207 -0.0510 291 SER A N 2036 C CA A SER A 298 ? 0.3803 0.3713 0.2724 0.0051 0.0180 -0.0544 291 SER A CA 2037 C CA B SER A 298 ? 0.3768 0.3678 0.2692 0.0051 0.0176 -0.0549 291 SER A CA 2038 C C A SER A 298 ? 0.3836 0.3720 0.2697 0.0073 0.0215 -0.0596 291 SER A C 2039 C C B SER A 298 ? 0.3815 0.3698 0.2665 0.0074 0.0220 -0.0594 291 SER A C 2040 O O A SER A 298 ? 0.4012 0.3857 0.2761 0.0092 0.0184 -0.0639 291 SER A O 2041 O O B SER A 298 ? 0.3919 0.3761 0.2632 0.0096 0.0204 -0.0626 291 SER A O 2042 C CB A SER A 298 ? 0.4010 0.3904 0.2808 0.0058 0.0187 -0.0502 291 SER A CB 2043 C CB B SER A 298 ? 0.3935 0.3828 0.2741 0.0057 0.0166 -0.0511 291 SER A CB 2044 O OG A SER A 298 ? 0.4187 0.4085 0.2950 0.0064 0.0267 -0.0472 291 SER A OG 2045 O OG B SER A 298 ? 0.3978 0.3894 0.2855 0.0039 0.0124 -0.0474 291 SER A OG 2046 N N . ILE A 299 ? 0.3715 0.3621 0.2652 0.0072 0.0275 -0.0595 292 ILE A N 2047 C CA . ILE A 299 ? 0.3721 0.3606 0.2608 0.0096 0.0323 -0.0641 292 ILE A CA 2048 C C . ILE A 299 ? 0.3582 0.3483 0.2608 0.0091 0.0328 -0.0670 292 ILE A C 2049 O O . ILE A 299 ? 0.3548 0.3484 0.2701 0.0072 0.0323 -0.0639 292 ILE A O 2050 C CB . ILE A 299 ? 0.3763 0.3655 0.2587 0.0108 0.0412 -0.0609 292 ILE A CB 2051 C CG1 . ILE A 299 ? 0.3623 0.3567 0.2585 0.0087 0.0453 -0.0557 292 ILE A CG1 2052 C CG2 . ILE A 299 ? 0.4052 0.3911 0.2711 0.0119 0.0410 -0.0583 292 ILE A CG2 2053 C CD1 . ILE A 299 ? 0.3832 0.3787 0.2757 0.0093 0.0540 -0.0523 292 ILE A CD1 2054 N N . PRO A 300 ? 0.3662 0.3533 0.2659 0.0112 0.0333 -0.0732 293 PRO A N 2055 C CA . PRO A 300 ? 0.3560 0.3440 0.2690 0.0109 0.0335 -0.0759 293 PRO A CA 2056 C C . PRO A 300 ? 0.3451 0.3370 0.2671 0.0110 0.0404 -0.0730 293 PRO A C 2057 O O . PRO A 300 ? 0.3499 0.3429 0.2661 0.0121 0.0466 -0.0713 293 PRO A O 2058 C CB . PRO A 300 ? 0.3650 0.3482 0.2704 0.0136 0.0334 -0.0833 293 PRO A CB 2059 C CG . PRO A 300 ? 0.4059 0.3855 0.2955 0.0146 0.0294 -0.0848 293 PRO A CG 2060 C CD . PRO A 300 ? 0.3817 0.3639 0.2657 0.0140 0.0330 -0.0782 293 PRO A CD 2061 N N . VAL A 301 ? 0.3242 0.3182 0.2605 0.0100 0.0393 -0.0723 294 VAL A N 2062 C CA . VAL A 301 ? 0.3116 0.3098 0.2584 0.0102 0.0444 -0.0697 294 VAL A CA 2063 C C . VAL A 301 ? 0.3076 0.3049 0.2651 0.0110 0.0434 -0.0729 294 VAL A C 2064 O O . VAL A 301 ? 0.3106 0.3054 0.2715 0.0101 0.0382 -0.0742 294 VAL A O 2065 C CB . VAL A 301 ? 0.2996 0.3016 0.2532 0.0078 0.0427 -0.0634 294 VAL A CB 2066 C CG1 . VAL A 301 ? 0.2892 0.2954 0.2542 0.0081 0.0469 -0.0611 294 VAL A CG1 2067 C CG2 . VAL A 301 ? 0.3173 0.3195 0.2608 0.0069 0.0430 -0.0600 294 VAL A CG2 2068 N N . HIS A 302 ? 0.3107 0.3099 0.2743 0.0127 0.0487 -0.0738 295 HIS A N 2069 C CA . HIS A 302 ? 0.2949 0.2930 0.2689 0.0140 0.0480 -0.0766 295 HIS A CA 2070 C C . HIS A 302 ? 0.2984 0.3010 0.2827 0.0152 0.0529 -0.0748 295 HIS A C 2071 O O . HIS A 302 ? 0.3120 0.3173 0.2936 0.0160 0.0585 -0.0742 295 HIS A O 2072 C CB . HIS A 302 ? 0.3149 0.3081 0.2827 0.0161 0.0485 -0.0835 295 HIS A CB 2073 C CG . HIS A 302 ? 0.3148 0.3052 0.2922 0.0172 0.0466 -0.0867 295 HIS A CG 2074 N ND1 . HIS A 302 ? 0.3026 0.2909 0.2861 0.0155 0.0409 -0.0857 295 HIS A ND1 2075 C CD2 . HIS A 302 ? 0.3231 0.3125 0.3057 0.0199 0.0500 -0.0905 295 HIS A CD2 2076 C CE1 . HIS A 302 ? 0.3217 0.3072 0.3132 0.0170 0.0408 -0.0886 295 HIS A CE1 2077 N NE2 . HIS A 302 ? 0.3200 0.3062 0.3112 0.0197 0.0459 -0.0917 295 HIS A NE2 2078 N N . PRO A 303 ? 0.2905 0.2938 0.2868 0.0154 0.0507 -0.0736 296 PRO A N 2079 C CA . PRO A 303 ? 0.2794 0.2871 0.2864 0.0169 0.0543 -0.0723 296 PRO A CA 2080 C C . PRO A 303 ? 0.2857 0.2915 0.2980 0.0199 0.0567 -0.0771 296 PRO A C 2081 O O . PRO A 303 ? 0.2990 0.2997 0.3105 0.0205 0.0537 -0.0803 296 PRO A O 2082 C CB . PRO A 303 ? 0.2777 0.2866 0.2932 0.0159 0.0496 -0.0680 296 PRO A CB 2083 C CG . PRO A 303 ? 0.2719 0.2754 0.2844 0.0150 0.0445 -0.0690 296 PRO A CG 2084 C CD . PRO A 303 ? 0.2847 0.2851 0.2853 0.0144 0.0448 -0.0727 296 PRO A CD 2085 N N . ILE A 304 ? 0.2935 0.3035 0.3123 0.0218 0.0620 -0.0775 297 ILE A N 2086 C CA . ILE A 304 ? 0.3005 0.3094 0.3257 0.0250 0.0648 -0.0820 297 ILE A CA 2087 C C . ILE A 304 ? 0.2919 0.3065 0.3317 0.0265 0.0667 -0.0799 297 ILE A C 2088 O O . ILE A 304 ? 0.2920 0.3116 0.3357 0.0249 0.0670 -0.0756 297 ILE A O 2089 C CB . ILE A 304 ? 0.3108 0.3186 0.3274 0.0269 0.0709 -0.0866 297 ILE A CB 2090 C CG1 . ILE A 304 ? 0.3255 0.3390 0.3411 0.0264 0.0774 -0.0840 297 ILE A CG1 2091 C CG2 . ILE A 304 ? 0.3309 0.3325 0.3331 0.0261 0.0681 -0.0898 297 ILE A CG2 2092 C CD1 . ILE A 304 ? 0.3315 0.3438 0.3379 0.0288 0.0846 -0.0881 297 ILE A CD1 2093 N N . GLY A 305 ? 0.3037 0.3173 0.3516 0.0296 0.0678 -0.0832 298 GLY A N 2094 C CA . GLY A 305 ? 0.2873 0.3062 0.3496 0.0316 0.0694 -0.0821 298 GLY A CA 2095 C C . GLY A 305 ? 0.2981 0.3217 0.3632 0.0333 0.0774 -0.0844 298 GLY A C 2096 O O . GLY A 305 ? 0.3022 0.3245 0.3565 0.0330 0.0821 -0.0866 298 GLY A O 2097 N N . TYR A 306 ? 0.2863 0.3155 0.3659 0.0351 0.0791 -0.0837 299 TYR A N 2098 C CA . TYR A 306 ? 0.3019 0.3369 0.3862 0.0361 0.0874 -0.0849 299 TYR A CA 2099 C C . TYR A 306 ? 0.3172 0.3502 0.4011 0.0399 0.0931 -0.0908 299 TYR A C 2100 O O . TYR A 306 ? 0.3354 0.3713 0.4175 0.0406 0.1010 -0.0922 299 TYR A O 2101 C CB . TYR A 306 ? 0.2954 0.3384 0.3964 0.0361 0.0877 -0.0819 299 TYR A CB 2102 C CG . TYR A 306 ? 0.2878 0.3320 0.4034 0.0389 0.0827 -0.0823 299 TYR A CG 2103 C CD1 . TYR A 306 ? 0.2894 0.3329 0.4076 0.0379 0.0746 -0.0787 299 TYR A CD1 2104 C CD2 . TYR A 306 ? 0.3145 0.3610 0.4415 0.0429 0.0864 -0.0861 299 TYR A CD2 2105 C CE1 . TYR A 306 ? 0.3035 0.3477 0.4338 0.0409 0.0697 -0.0787 299 TYR A CE1 2106 C CE2 . TYR A 306 ? 0.3135 0.3612 0.4540 0.0458 0.0813 -0.0862 299 TYR A CE2 2107 C CZ . TYR A 306 ? 0.3044 0.3507 0.4459 0.0448 0.0729 -0.0824 299 TYR A CZ 2108 O OH . TYR A 306 ? 0.2857 0.3323 0.4389 0.0481 0.0676 -0.0822 299 TYR A OH 2109 N N . TYR A 307 ? 0.3259 0.3537 0.4112 0.0422 0.0894 -0.0941 300 TYR A N 2110 C CA . TYR A 307 ? 0.3394 0.3637 0.4213 0.0457 0.0943 -0.1003 300 TYR A CA 2111 C C . TYR A 307 ? 0.3518 0.3718 0.4152 0.0446 0.0974 -0.1025 300 TYR A C 2112 O O . TYR A 307 ? 0.3747 0.3956 0.4337 0.0467 0.1051 -0.1058 300 TYR A O 2113 C CB . TYR A 307 ? 0.3412 0.3591 0.4264 0.0481 0.0892 -0.1035 300 TYR A CB 2114 C CG . TYR A 307 ? 0.3473 0.3682 0.4500 0.0509 0.0872 -0.1028 300 TYR A CG 2115 C CD1 . TYR A 307 ? 0.3676 0.3970 0.4837 0.0523 0.0913 -0.1016 300 TYR A CD1 2116 C CD2 . TYR A 307 ? 0.3532 0.3681 0.4594 0.0524 0.0810 -0.1034 300 TYR A CD2 2117 C CE1 . TYR A 307 ? 0.3595 0.3917 0.4919 0.0553 0.0886 -0.1013 300 TYR A CE1 2118 C CE2 . TYR A 307 ? 0.3542 0.3712 0.4756 0.0555 0.0787 -0.1027 300 TYR A CE2 2119 C CZ . TYR A 307 ? 0.3836 0.4092 0.5177 0.0571 0.0822 -0.1018 300 TYR A CZ 2120 O OH . TYR A 307 ? 0.3875 0.4152 0.5368 0.0606 0.0791 -0.1014 300 TYR A OH 2121 N N . ASP A 308 ? 0.3476 0.3629 0.4001 0.0415 0.0915 -0.1008 301 ASP A N 2122 C CA . ASP A 308 ? 0.3633 0.3743 0.3978 0.0404 0.0928 -0.1027 301 ASP A CA 2123 C C . ASP A 308 ? 0.3656 0.3814 0.3941 0.0388 0.0986 -0.0992 301 ASP A C 2124 O O . ASP A 308 ? 0.3826 0.3963 0.3983 0.0400 0.1039 -0.1017 301 ASP A O 2125 C CB . ASP A 308 ? 0.3587 0.3641 0.3855 0.0375 0.0844 -0.1015 301 ASP A CB 2126 C CG . ASP A 308 ? 0.3646 0.3631 0.3928 0.0392 0.0799 -0.1062 301 ASP A CG 2127 O OD1 . ASP A 308 ? 0.3947 0.3912 0.4250 0.0427 0.0834 -0.1115 301 ASP A OD1 2128 O OD2 . ASP A 308 ? 0.3562 0.3510 0.3836 0.0369 0.0731 -0.1046 301 ASP A OD2 2129 N N . ALA A 309 ? 0.3536 0.3752 0.3907 0.0362 0.0975 -0.0933 302 ALA A N 2130 C CA . ALA A 309 ? 0.3525 0.3787 0.3863 0.0345 0.1032 -0.0895 302 ALA A CA 2131 C C . ALA A 309 ? 0.3652 0.3951 0.4027 0.0373 0.1135 -0.0917 302 ALA A C 2132 O O . ALA A 309 ? 0.3800 0.4101 0.4071 0.0372 0.1200 -0.0908 302 ALA A O 2133 C CB . ALA A 309 ? 0.3392 0.3709 0.3843 0.0315 0.1000 -0.0836 302 ALA A CB 2134 N N A GLN A 310 ? 0.3564 0.3900 0.4098 0.0400 0.1152 -0.0938 303 GLN A N 2135 N N B GLN A 310 ? 0.3592 0.3914 0.4105 0.0404 0.1150 -0.0948 303 GLN A N 2136 C CA A GLN A 310 ? 0.3757 0.4138 0.4351 0.0428 0.1254 -0.0958 303 GLN A CA 2137 C CA B GLN A 310 ? 0.3669 0.4021 0.4224 0.0439 0.1248 -0.0981 303 GLN A CA 2138 C C A GLN A 310 ? 0.3898 0.4221 0.4314 0.0456 0.1312 -0.1006 303 GLN A C 2139 C C B GLN A 310 ? 0.3844 0.4133 0.4209 0.0463 0.1296 -0.1028 303 GLN A C 2140 O O A GLN A 310 ? 0.3995 0.4339 0.4363 0.0467 0.1407 -0.1004 303 GLN A O 2141 O O B GLN A 310 ? 0.3918 0.4226 0.4224 0.0474 0.1387 -0.1024 303 GLN A O 2142 C CB A GLN A 310 ? 0.3659 0.4076 0.4442 0.0459 0.1253 -0.0984 303 GLN A CB 2143 C CB B GLN A 310 ? 0.3606 0.3979 0.4331 0.0472 0.1239 -0.1013 303 GLN A CB 2144 C CG A GLN A 310 ? 0.4259 0.4710 0.5092 0.0499 0.1362 -0.1021 303 GLN A CG 2145 C CG B GLN A 310 ? 0.3636 0.4068 0.4466 0.0505 0.1341 -0.1034 303 GLN A CG 2146 C CD A GLN A 310 ? 0.4739 0.5275 0.5809 0.0513 0.1384 -0.1014 303 GLN A CD 2147 C CD B GLN A 310 ? 0.3363 0.3890 0.4401 0.0493 0.1350 -0.0993 303 GLN A CD 2148 O OE1 A GLN A 310 ? 0.4787 0.5346 0.5979 0.0498 0.1299 -0.0987 303 GLN A OE1 2149 O OE1 B GLN A 310 ? 0.3144 0.3725 0.4207 0.0474 0.1411 -0.0957 303 GLN A OE1 2150 N NE2 A GLN A 310 ? 0.5009 0.5591 0.6155 0.0541 0.1477 -0.1034 303 GLN A NE2 2151 N NE2 B GLN A 310 ? 0.3302 0.3846 0.4490 0.0505 0.1285 -0.0997 303 GLN A NE2 2152 N N A LYS A 311 ? 0.3912 0.4158 0.4229 0.0466 0.1254 -0.1050 304 LYS A N 2153 N N B LYS A 311 ? 0.3899 0.4112 0.4170 0.0474 0.1237 -0.1072 304 LYS A N 2154 C CA A LYS A 311 ? 0.4096 0.4277 0.4239 0.0495 0.1289 -0.1105 304 LYS A CA 2155 C CA B LYS A 311 ? 0.4114 0.4261 0.4202 0.0500 0.1271 -0.1125 304 LYS A CA 2156 C C A LYS A 311 ? 0.4186 0.4345 0.4142 0.0477 0.1311 -0.1078 304 LYS A C 2157 C C B LYS A 311 ? 0.4197 0.4324 0.4102 0.0478 0.1284 -0.1094 304 LYS A C 2158 O O A LYS A 311 ? 0.4244 0.4388 0.4083 0.0502 0.1390 -0.1097 304 LYS A O 2159 O O B LYS A 311 ? 0.4286 0.4370 0.4029 0.0504 0.1332 -0.1129 304 LYS A O 2160 C CB A LYS A 311 ? 0.4156 0.4258 0.4255 0.0506 0.1208 -0.1158 304 LYS A CB 2161 C CB B LYS A 311 ? 0.4191 0.4260 0.4238 0.0514 0.1198 -0.1182 304 LYS A CB 2162 C CG A LYS A 311 ? 0.4176 0.4284 0.4446 0.0530 0.1185 -0.1186 304 LYS A CG 2163 C CG B LYS A 311 ? 0.4288 0.4365 0.4494 0.0546 0.1200 -0.1219 304 LYS A CG 2164 C CD A LYS A 311 ? 0.4718 0.4846 0.5041 0.0579 0.1276 -0.1234 304 LYS A CD 2165 C CD B LYS A 311 ? 0.4627 0.4734 0.4857 0.0590 0.1307 -0.1254 304 LYS A CD 2166 C CE A LYS A 311 ? 0.4915 0.4962 0.5077 0.0613 0.1294 -0.1308 304 LYS A CE 2167 C CE B LYS A 311 ? 0.4789 0.4938 0.5230 0.0616 0.1316 -0.1267 304 LYS A CE 2168 N NZ A LYS A 311 ? 0.5397 0.5467 0.5577 0.0662 0.1400 -0.1348 304 LYS A NZ 2169 N NZ B LYS A 311 ? 0.5240 0.5318 0.5678 0.0653 0.1289 -0.1338 304 LYS A NZ 2170 N N . LEU A 312 ? 0.4025 0.4179 0.3951 0.0435 0.1241 -0.1031 305 LEU A N 2171 C CA . LEU A 312 ? 0.4256 0.4394 0.4021 0.0415 0.1254 -0.0995 305 LEU A CA 2172 C C . LEU A 312 ? 0.4354 0.4552 0.4149 0.0408 0.1349 -0.0943 305 LEU A C 2173 O O . LEU A 312 ? 0.4638 0.4811 0.4273 0.0414 0.1402 -0.0933 305 LEU A O 2174 C CB . LEU A 312 ? 0.4013 0.4134 0.3755 0.0373 0.1154 -0.0957 305 LEU A CB 2175 C CG . LEU A 312 ? 0.4222 0.4278 0.3919 0.0374 0.1061 -0.1001 305 LEU A CG 2176 C CD1 . LEU A 312 ? 0.4068 0.4116 0.3745 0.0332 0.0976 -0.0957 305 LEU A CD1 2177 C CD2 . LEU A 312 ? 0.4494 0.4477 0.4011 0.0404 0.1069 -0.1064 305 LEU A CD2 2178 N N . LEU A 313 ? 0.4167 0.4442 0.4166 0.0396 0.1369 -0.0912 306 LEU A N 2179 C CA . LEU A 313 ? 0.4182 0.4520 0.4244 0.0383 0.1454 -0.0860 306 LEU A CA 2180 C C . LEU A 313 ? 0.4361 0.4727 0.4455 0.0420 0.1574 -0.0884 306 LEU A C 2181 O O . LEU A 313 ? 0.4365 0.4761 0.4446 0.0415 0.1663 -0.0845 306 LEU A O 2182 C CB . LEU A 313 ? 0.3942 0.4352 0.4218 0.0353 0.1417 -0.0818 306 LEU A CB 2183 C CG . LEU A 313 ? 0.3860 0.4250 0.4114 0.0314 0.1310 -0.0783 306 LEU A CG 2184 C CD1 . LEU A 313 ? 0.3699 0.4155 0.4165 0.0295 0.1268 -0.0755 306 LEU A CD1 2185 C CD2 . LEU A 313 ? 0.3824 0.4191 0.3930 0.0287 0.1321 -0.0736 306 LEU A CD2 2186 N N . GLU A 314 ? 0.4474 0.4832 0.4620 0.0458 0.1579 -0.0945 307 GLU A N 2187 C CA . GLU A 314 ? 0.4605 0.5004 0.4826 0.0496 0.1693 -0.0969 307 GLU A CA 2188 C C . GLU A 314 ? 0.4884 0.5245 0.4908 0.0521 0.1796 -0.0975 307 GLU A C 2189 O O . GLU A 314 ? 0.4856 0.5266 0.4942 0.0538 0.1911 -0.0962 307 GLU A O 2190 C CB . GLU A 314 ? 0.4650 0.5042 0.4966 0.0533 0.1671 -0.1036 307 GLU A CB 2191 C CG . GLU A 314 ? 0.5023 0.5320 0.5158 0.0565 0.1640 -0.1102 307 GLU A CG 2192 C CD . GLU A 314 ? 0.5319 0.5607 0.5571 0.0598 0.1608 -0.1162 307 GLU A CD 2193 O OE1 . GLU A 314 ? 0.5433 0.5790 0.5902 0.0599 0.1610 -0.1150 307 GLU A OE1 2194 O OE2 . GLU A 314 ? 0.5398 0.5606 0.5524 0.0624 0.1577 -0.1223 307 GLU A OE2 2195 N N . LYS A 315 ? 0.4970 0.5246 0.4761 0.0525 0.1754 -0.0993 308 LYS A N 2196 C CA . LYS A 315 ? 0.5268 0.5495 0.4842 0.0555 0.1841 -0.1001 308 LYS A CA 2197 C C . LYS A 315 ? 0.5258 0.5489 0.4739 0.0524 0.1874 -0.0925 308 LYS A C 2198 O O . LYS A 315 ? 0.5440 0.5627 0.4731 0.0549 0.1949 -0.0920 308 LYS A O 2199 C CB . LYS A 315 ? 0.5387 0.5514 0.4746 0.0584 0.1778 -0.1069 308 LYS A CB 2200 C CG . LYS A 315 ? 0.5737 0.5842 0.5132 0.0632 0.1788 -0.1152 308 LYS A CG 2201 C CD . LYS A 315 ? 0.5976 0.5987 0.5216 0.0645 0.1689 -0.1217 308 LYS A CD 2202 C CE . LYS A 315 ? 0.6179 0.6159 0.5440 0.0697 0.1709 -0.1304 308 LYS A CE 2203 N NZ . LYS A 315 ? 0.6372 0.6256 0.5488 0.0709 0.1613 -0.1371 308 LYS A NZ 2204 N N . MET A 316 ? 0.4962 0.5237 0.4568 0.0473 0.1819 -0.0866 309 MET A N 2205 C CA . MET A 316 ? 0.5022 0.5293 0.4542 0.0442 0.1841 -0.0793 309 MET A CA 2206 C C . MET A 316 ? 0.5140 0.5444 0.4662 0.0452 0.1988 -0.0749 309 MET A C 2207 O O . MET A 316 ? 0.4997 0.5375 0.4715 0.0456 0.2063 -0.0745 309 MET A O 2208 C CB . MET A 316 ? 0.4830 0.5143 0.4497 0.0388 0.1754 -0.0744 309 MET A CB 2209 C CG A MET A 316 ? 0.4770 0.5029 0.4363 0.0379 0.1619 -0.0777 309 MET A CG 2210 C CG B MET A 316 ? 0.4923 0.5195 0.4551 0.0373 0.1616 -0.0768 309 MET A CG 2211 S SD A MET A 316 ? 0.4493 0.4754 0.4107 0.0324 0.1510 -0.0719 309 MET A SD 2212 S SD B MET A 316 ? 0.5268 0.5453 0.4622 0.0365 0.1570 -0.0749 309 MET A SD 2213 C CE A MET A 316 ? 0.4770 0.4995 0.4193 0.0315 0.1571 -0.0658 309 MET A CE 2214 C CE B MET A 316 ? 0.5173 0.5398 0.4574 0.0321 0.1608 -0.0652 309 MET A CE 2215 N N . GLY A 317 ? 0.5333 0.5580 0.4639 0.0456 0.2025 -0.0715 310 GLY A N 2216 C CA . GLY A 317 ? 0.5510 0.5771 0.4778 0.0465 0.2169 -0.0664 310 GLY A CA 2217 C C . GLY A 317 ? 0.5581 0.5839 0.4821 0.0421 0.2165 -0.0578 310 GLY A C 2218 O O . GLY A 317 ? 0.5381 0.5674 0.4760 0.0375 0.2079 -0.0549 310 GLY A O 2219 N N . GLY A 318 ? 0.5764 0.5975 0.4817 0.0439 0.2258 -0.0537 311 GLY A N 2220 C CA . GLY A 318 ? 0.5757 0.5961 0.4784 0.0401 0.2273 -0.0449 311 GLY A CA 2221 C C . GLY A 318 ? 0.5694 0.5995 0.5011 0.0358 0.2328 -0.0396 311 GLY A C 2222 O O . GLY A 318 ? 0.5655 0.6021 0.5139 0.0371 0.2417 -0.0412 311 GLY A O 2223 N N . SER A 319 ? 0.5576 0.5887 0.4961 0.0307 0.2270 -0.0338 312 SER A N 2224 C CA . SER A 319 ? 0.5571 0.5964 0.5218 0.0262 0.2312 -0.0283 312 SER A CA 2225 C C . SER A 319 ? 0.5373 0.5856 0.5306 0.0246 0.2258 -0.0324 312 SER A C 2226 O O . SER A 319 ? 0.5356 0.5833 0.5296 0.0248 0.2140 -0.0376 312 SER A O 2227 C CB . SER A 319 ? 0.5568 0.5934 0.5185 0.0217 0.2251 -0.0217 312 SER A CB 2228 O OG . SER A 319 ? 0.5909 0.6195 0.5281 0.0232 0.2316 -0.0167 312 SER A OG 2229 N N . ALA A 320 ? 0.5337 0.5903 0.5508 0.0230 0.2346 -0.0300 313 ALA A N 2230 C CA . ALA A 320 ? 0.5106 0.5764 0.5569 0.0211 0.2291 -0.0328 313 ALA A CA 2231 C C . ALA A 320 ? 0.4917 0.5576 0.5449 0.0165 0.2155 -0.0308 313 ALA A C 2232 O O . ALA A 320 ? 0.4887 0.5498 0.5303 0.0140 0.2140 -0.0256 313 ALA A O 2233 C CB . ALA A 320 ? 0.5133 0.5878 0.5841 0.0199 0.2411 -0.0297 313 ALA A CB 2234 N N . PRO A 321 ? 0.4735 0.5448 0.5455 0.0157 0.2059 -0.0347 314 PRO A N 2235 C CA . PRO A 321 ? 0.4643 0.5365 0.5448 0.0114 0.1945 -0.0322 314 PRO A CA 2236 C C . PRO A 321 ? 0.4661 0.5426 0.5619 0.0073 0.2008 -0.0257 314 PRO A C 2237 O O . PRO A 321 ? 0.4710 0.5533 0.5817 0.0076 0.2118 -0.0246 314 PRO A O 2238 C CB . PRO A 321 ? 0.4481 0.5261 0.5481 0.0120 0.1860 -0.0374 314 PRO A CB 2239 C CG . PRO A 321 ? 0.4485 0.5317 0.5593 0.0155 0.1958 -0.0409 314 PRO A CG 2240 C CD . PRO A 321 ? 0.4733 0.5502 0.5605 0.0186 0.2056 -0.0409 314 PRO A CD 2241 N N . PRO A 322 ? 0.4635 0.5369 0.5558 0.0036 0.1945 -0.0213 315 PRO A N 2242 C CA . PRO A 322 ? 0.4702 0.5463 0.5751 -0.0004 0.2007 -0.0148 315 PRO A CA 2243 C C . PRO A 322 ? 0.4629 0.5489 0.6006 -0.0028 0.2000 -0.0155 315 PRO A C 2244 O O . PRO A 322 ? 0.4654 0.5553 0.6182 -0.0054 0.2087 -0.0111 315 PRO A O 2245 C CB . PRO A 322 ? 0.4574 0.5272 0.5499 -0.0033 0.1915 -0.0113 315 PRO A CB 2246 C CG . PRO A 322 ? 0.4444 0.5123 0.5301 -0.0017 0.1781 -0.0167 315 PRO A CG 2247 C CD . PRO A 322 ? 0.4542 0.5212 0.5303 0.0030 0.1820 -0.0219 315 PRO A CD 2248 N N . ASP A 323 ? 0.4537 0.5433 0.6023 -0.0019 0.1895 -0.0209 316 ASP A N 2249 C CA . ASP A 323 ? 0.4512 0.5501 0.6304 -0.0034 0.1867 -0.0226 316 ASP A CA 2250 C C . ASP A 323 ? 0.4452 0.5462 0.6293 -0.0006 0.1760 -0.0291 316 ASP A C 2251 O O . ASP A 323 ? 0.4414 0.5364 0.6058 0.0019 0.1707 -0.0319 316 ASP A O 2252 C CB . ASP A 323 ? 0.4477 0.5478 0.6397 -0.0084 0.1817 -0.0184 316 ASP A CB 2253 C CG . ASP A 323 ? 0.4526 0.5469 0.6317 -0.0094 0.1679 -0.0187 316 ASP A CG 2254 O OD1 . ASP A 323 ? 0.4620 0.5571 0.6427 -0.0075 0.1577 -0.0235 316 ASP A OD1 2255 O OD2 . ASP A 323 ? 0.4782 0.5671 0.6463 -0.0120 0.1673 -0.0140 316 ASP A OD2 2256 N N . SER A 324 ? 0.4378 0.5469 0.6483 -0.0011 0.1723 -0.0314 317 SER A N 2257 C CA . SER A 324 ? 0.4371 0.5486 0.6543 0.0021 0.1631 -0.0373 317 SER A CA 2258 C C . SER A 324 ? 0.4233 0.5290 0.6274 0.0021 0.1490 -0.0386 317 SER A C 2259 O O . SER A 324 ? 0.4195 0.5238 0.6194 0.0054 0.1428 -0.0429 317 SER A O 2260 C CB . SER A 324 ? 0.4358 0.5574 0.6849 0.0018 0.1620 -0.0393 317 SER A CB 2261 O OG . SER A 324 ? 0.4496 0.5729 0.7107 -0.0018 0.1536 -0.0375 317 SER A OG 2262 N N . SER A 325 ? 0.4056 0.5076 0.6035 -0.0013 0.1442 -0.0348 318 SER A N 2263 C CA . SER A 325 ? 0.3864 0.4829 0.5718 -0.0015 0.1317 -0.0355 318 SER A CA 2264 C C . SER A 325 ? 0.3836 0.4723 0.5427 0.0008 0.1311 -0.0366 318 SER A C 2265 O O . SER A 325 ? 0.3816 0.4657 0.5299 0.0012 0.1214 -0.0376 318 SER A O 2266 C CB . SER A 325 ? 0.3848 0.4792 0.5700 -0.0056 0.1280 -0.0310 318 SER A CB 2267 O OG . SER A 325 ? 0.3938 0.4825 0.5609 -0.0071 0.1348 -0.0268 318 SER A OG 2268 N N . TRP A 326 ? 0.3743 0.4615 0.5234 0.0023 0.1415 -0.0364 319 TRP A N 2269 C CA . TRP A 326 ? 0.3714 0.4514 0.4964 0.0048 0.1418 -0.0381 319 TRP A CA 2270 C C . TRP A 326 ? 0.3704 0.4516 0.4973 0.0090 0.1425 -0.0439 319 TRP A C 2271 O O . TRP A 326 ? 0.3703 0.4455 0.4794 0.0113 0.1407 -0.0465 319 TRP A O 2272 C CB . TRP A 326 ? 0.3856 0.4616 0.4950 0.0043 0.1523 -0.0346 319 TRP A CB 2273 C CG . TRP A 326 ? 0.3484 0.4190 0.4448 0.0012 0.1489 -0.0297 319 TRP A CG 2274 C CD1 . TRP A 326 ? 0.3437 0.4162 0.4509 -0.0026 0.1458 -0.0257 319 TRP A CD1 2275 C CD2 . TRP A 326 ? 0.3517 0.4141 0.4225 0.0019 0.1478 -0.0286 319 TRP A CD2 2276 N NE1 . TRP A 326 ? 0.3614 0.4273 0.4510 -0.0042 0.1432 -0.0220 319 TRP A NE1 2277 C CE2 . TRP A 326 ? 0.3640 0.4238 0.4314 -0.0015 0.1441 -0.0237 319 TRP A CE2 2278 C CE3 . TRP A 326 ? 0.3421 0.3990 0.3928 0.0052 0.1489 -0.0318 319 TRP A CE3 2279 C CZ2 . TRP A 326 ? 0.3672 0.4194 0.4122 -0.0015 0.1417 -0.0216 319 TRP A CZ2 2280 C CZ3 . TRP A 326 ? 0.3587 0.4081 0.3872 0.0050 0.1462 -0.0299 319 TRP A CZ3 2281 C CH2 . TRP A 326 ? 0.3536 0.4009 0.3796 0.0017 0.1424 -0.0247 319 TRP A CH2 2282 N N A ARG A 327 ? 0.3644 0.4530 0.5134 0.0101 0.1444 -0.0460 320 ARG A N 2283 N N B ARG A 327 ? 0.3645 0.4531 0.5134 0.0101 0.1447 -0.0460 320 ARG A N 2284 C CA A ARG A 327 ? 0.3679 0.4582 0.5216 0.0143 0.1454 -0.0513 320 ARG A CA 2285 C CA B ARG A 327 ? 0.3679 0.4582 0.5214 0.0144 0.1456 -0.0514 320 ARG A CA 2286 C C A ARG A 327 ? 0.3599 0.4507 0.5214 0.0156 0.1333 -0.0543 320 ARG A C 2287 C C B ARG A 327 ? 0.3600 0.4508 0.5217 0.0157 0.1335 -0.0544 320 ARG A C 2288 O O A ARG A 327 ? 0.3510 0.4465 0.5293 0.0142 0.1277 -0.0534 320 ARG A O 2289 O O B ARG A 327 ? 0.3515 0.4473 0.5305 0.0143 0.1281 -0.0535 320 ARG A O 2290 C CB A ARG A 327 ? 0.3744 0.4727 0.5479 0.0154 0.1555 -0.0520 320 ARG A CB 2291 C CB B ARG A 327 ? 0.3743 0.4724 0.5470 0.0156 0.1560 -0.0522 320 ARG A CB 2292 C CG A ARG A 327 ? 0.4021 0.4997 0.5674 0.0150 0.1692 -0.0492 320 ARG A CG 2293 C CG B ARG A 327 ? 0.4037 0.5005 0.5661 0.0161 0.1698 -0.0503 320 ARG A CG 2294 C CD A ARG A 327 ? 0.4470 0.5536 0.6355 0.0157 0.1793 -0.0494 320 ARG A CD 2295 C CD B ARG A 327 ? 0.4462 0.5506 0.6269 0.0185 0.1803 -0.0524 320 ARG A CD 2296 N NE A ARG A 327 ? 0.4979 0.6034 0.6770 0.0172 0.1937 -0.0482 320 ARG A NE 2297 N NE B ARG A 327 ? 0.4736 0.5870 0.6834 0.0171 0.1770 -0.0524 320 ARG A NE 2298 C CZ A ARG A 327 ? 0.5206 0.6284 0.7041 0.0147 0.2039 -0.0430 320 ARG A CZ 2299 C CZ B ARG A 327 ? 0.4984 0.6174 0.7246 0.0135 0.1813 -0.0483 320 ARG A CZ 2300 N NH1 A ARG A 327 ? 0.5213 0.6326 0.7194 0.0101 0.2009 -0.0388 320 ARG A NH1 2301 N NH1 B ARG A 327 ? 0.4982 0.6254 0.7512 0.0126 0.1768 -0.0493 320 ARG A NH1 2302 N NH2 A ARG A 327 ? 0.5251 0.6311 0.6979 0.0168 0.2173 -0.0420 320 ARG A NH2 2303 N NH2 B ARG A 327 ? 0.5132 0.6294 0.7293 0.0109 0.1898 -0.0432 320 ARG A NH2 2304 N N . GLY A 328 ? 0.3613 0.4467 0.5103 0.0185 0.1293 -0.0579 321 GLY A N 2305 C CA . GLY A 328 ? 0.3523 0.4376 0.5082 0.0206 0.1194 -0.0608 321 GLY A CA 2306 C C . GLY A 328 ? 0.3626 0.4533 0.5351 0.0243 0.1231 -0.0648 321 GLY A C 2307 O O . GLY A 328 ? 0.3617 0.4584 0.5462 0.0244 0.1323 -0.0646 321 GLY A O 2308 N N . SER A 329 ? 0.3585 0.4469 0.5319 0.0274 0.1165 -0.0682 322 SER A N 2309 C CA . SER A 329 ? 0.3721 0.4653 0.5627 0.0313 0.1180 -0.0721 322 SER A CA 2310 C C . SER A 329 ? 0.3692 0.4587 0.5517 0.0352 0.1232 -0.0765 322 SER A C 2311 O O . SER A 329 ? 0.3702 0.4630 0.5662 0.0388 0.1242 -0.0799 322 SER A O 2312 C CB . SER A 329 ? 0.3719 0.4654 0.5722 0.0328 0.1065 -0.0727 322 SER A CB 2313 O OG . SER A 329 ? 0.4189 0.5169 0.6300 0.0300 0.1019 -0.0696 322 SER A OG 2314 N N . LEU A 330 ? 0.3589 0.4414 0.5200 0.0347 0.1261 -0.0768 323 LEU A N 2315 C CA . LEU A 330 ? 0.3645 0.4427 0.5166 0.0384 0.1308 -0.0815 323 LEU A CA 2316 C C . LEU A 330 ? 0.3784 0.4618 0.5365 0.0399 0.1436 -0.0826 323 LEU A C 2317 O O . LEU A 330 ? 0.3698 0.4577 0.5320 0.0372 0.1497 -0.0788 323 LEU A O 2318 C CB . LEU A 330 ? 0.3710 0.4400 0.4983 0.0375 0.1291 -0.0819 323 LEU A CB 2319 C CG . LEU A 330 ? 0.3505 0.4138 0.4708 0.0362 0.1174 -0.0811 323 LEU A CG 2320 C CD1 . LEU A 330 ? 0.3640 0.4196 0.4614 0.0346 0.1166 -0.0810 323 LEU A CD1 2321 C CD2 . LEU A 330 ? 0.3350 0.3962 0.4627 0.0399 0.1125 -0.0852 323 LEU A CD2 2322 N N . LYS A 331 ? 0.3953 0.4773 0.5533 0.0443 0.1480 -0.0876 324 LYS A N 2323 C CA . LYS A 331 ? 0.4203 0.5067 0.5831 0.0465 0.1608 -0.0892 324 LYS A CA 2324 C C . LYS A 331 ? 0.4308 0.5108 0.5694 0.0463 0.1679 -0.0891 324 LYS A C 2325 O O . LYS A 331 ? 0.4501 0.5259 0.5783 0.0501 0.1730 -0.0937 324 LYS A O 2326 C CB . LYS A 331 ? 0.4253 0.5134 0.6002 0.0517 0.1624 -0.0948 324 LYS A CB 2327 C CG . LYS A 331 ? 0.4523 0.5478 0.6529 0.0522 0.1562 -0.0944 324 LYS A CG 2328 C CD . LYS A 331 ? 0.4815 0.5871 0.7007 0.0495 0.1613 -0.0904 324 LYS A CD 2329 C CE . LYS A 331 ? 0.4821 0.5940 0.7239 0.0491 0.1520 -0.0895 324 LYS A CE 2330 N NZ . LYS A 331 ? 0.4946 0.6021 0.7284 0.0458 0.1400 -0.0863 324 LYS A NZ 2331 N N . VAL A 332 ? 0.4188 0.4979 0.5484 0.0421 0.1677 -0.0838 325 VAL A N 2332 C CA . VAL A 332 ? 0.4342 0.5076 0.5409 0.0416 0.1741 -0.0825 325 VAL A CA 2333 C C . VAL A 332 ? 0.4268 0.5052 0.5386 0.0379 0.1807 -0.0761 325 VAL A C 2334 O O . VAL A 332 ? 0.4178 0.5026 0.5485 0.0351 0.1774 -0.0730 325 VAL A O 2335 C CB . VAL A 332 ? 0.4251 0.4892 0.5101 0.0402 0.1647 -0.0828 325 VAL A CB 2336 C CG1 . VAL A 332 ? 0.4409 0.4997 0.5223 0.0435 0.1583 -0.0890 325 VAL A CG1 2337 C CG2 . VAL A 332 ? 0.4220 0.4871 0.5110 0.0355 0.1554 -0.0777 325 VAL A CG2 2338 N N . PRO A 333 ? 0.4445 0.5194 0.5392 0.0380 0.1899 -0.0740 326 PRO A N 2339 C CA . PRO A 333 ? 0.4410 0.5204 0.5420 0.0346 0.1971 -0.0675 326 PRO A CA 2340 C C . PRO A 333 ? 0.4274 0.5043 0.5229 0.0297 0.1888 -0.0623 326 PRO A C 2341 O O . PRO A 333 ? 0.4245 0.5059 0.5306 0.0262 0.1922 -0.0570 326 PRO A O 2342 C CB . PRO A 333 ? 0.4704 0.5457 0.5529 0.0371 0.2099 -0.0670 326 PRO A CB 2343 C CG . PRO A 333 ? 0.4880 0.5544 0.5479 0.0408 0.2059 -0.0728 326 PRO A CG 2344 C CD . PRO A 333 ? 0.4678 0.5346 0.5380 0.0416 0.1944 -0.0776 326 PRO A CD 2345 N N . TYR A 334 ? 0.4141 0.4841 0.4941 0.0294 0.1783 -0.0639 327 TYR A N 2346 C CA . TYR A 334 ? 0.4049 0.4717 0.4768 0.0253 0.1707 -0.0593 327 TYR A CA 2347 C C . TYR A 334 ? 0.4186 0.4816 0.4738 0.0240 0.1784 -0.0545 327 TYR A C 2348 O O . TYR A 334 ? 0.4226 0.4861 0.4791 0.0202 0.1769 -0.0490 327 TYR A O 2349 C CB . TYR A 334 ? 0.3910 0.4643 0.4849 0.0218 0.1644 -0.0565 327 TYR A CB 2350 C CG . TYR A 334 ? 0.3767 0.4508 0.4799 0.0231 0.1539 -0.0605 327 TYR A CG 2351 C CD1 . TYR A 334 ? 0.3497 0.4181 0.4420 0.0220 0.1427 -0.0608 327 TYR A CD1 2352 C CD2 . TYR A 334 ? 0.3652 0.4453 0.4878 0.0257 0.1554 -0.0640 327 TYR A CD2 2353 C CE1 . TYR A 334 ? 0.3156 0.3841 0.4155 0.0234 0.1338 -0.0640 327 TYR A CE1 2354 C CE2 . TYR A 334 ? 0.3491 0.4290 0.4790 0.0272 0.1458 -0.0674 327 TYR A CE2 2355 C CZ . TYR A 334 ? 0.3449 0.4188 0.4630 0.0261 0.1353 -0.0672 327 TYR A CZ 2356 O OH . TYR A 334 ? 0.3367 0.4099 0.4617 0.0278 0.1264 -0.0699 327 TYR A OH 2357 N N . ASN A 335 ? 0.4344 0.4932 0.4735 0.0276 0.1868 -0.0567 328 ASN A N 2358 C CA . ASN A 335 ? 0.4524 0.5059 0.4712 0.0275 0.1934 -0.0526 328 ASN A CA 2359 C C . ASN A 335 ? 0.4527 0.4992 0.4541 0.0255 0.1830 -0.0512 328 ASN A C 2360 O O . ASN A 335 ? 0.4415 0.4851 0.4392 0.0260 0.1727 -0.0553 328 ASN A O 2361 C CB . ASN A 335 ? 0.4647 0.5138 0.4667 0.0326 0.2025 -0.0565 328 ASN A CB 2362 C CG . ASN A 335 ? 0.4781 0.5340 0.4956 0.0346 0.2157 -0.0567 328 ASN A CG 2363 O OD1 . ASN A 335 ? 0.4843 0.5473 0.5213 0.0317 0.2207 -0.0520 328 ASN A OD1 2364 N ND2 . ASN A 335 ? 0.4616 0.5155 0.4715 0.0398 0.2215 -0.0623 328 ASN A ND2 2365 N N . VAL A 336 ? 0.4669 0.5108 0.4586 0.0232 0.1858 -0.0450 329 VAL A N 2366 C CA . VAL A 336 ? 0.4681 0.5062 0.4456 0.0211 0.1760 -0.0430 329 VAL A CA 2367 C C . VAL A 336 ? 0.4790 0.5081 0.4287 0.0246 0.1748 -0.0461 329 VAL A C 2368 O O . VAL A 336 ? 0.4625 0.4868 0.4008 0.0238 0.1647 -0.0469 329 VAL A O 2369 C CB . VAL A 336 ? 0.4742 0.5130 0.4543 0.0171 0.1784 -0.0350 329 VAL A CB 2370 C CG1 . VAL A 336 ? 0.4871 0.5189 0.4486 0.0159 0.1698 -0.0329 329 VAL A CG1 2371 C CG2 . VAL A 336 ? 0.4742 0.5209 0.4814 0.0134 0.1747 -0.0332 329 VAL A CG2 2372 N N . GLY A 337 ? 0.4925 0.5196 0.4316 0.0286 0.1848 -0.0481 330 GLY A N 2373 C CA . GLY A 337 ? 0.5141 0.5321 0.4254 0.0323 0.1840 -0.0510 330 GLY A CA 2374 C C . GLY A 337 ? 0.5309 0.5442 0.4252 0.0319 0.1892 -0.0443 330 GLY A C 2375 O O . GLY A 337 ? 0.5275 0.5445 0.4311 0.0299 0.1980 -0.0380 330 GLY A O 2376 N N . PRO A 338 ? 0.5481 0.5530 0.4176 0.0339 0.1838 -0.0455 331 PRO A N 2377 C CA . PRO A 338 ? 0.5556 0.5555 0.4138 0.0361 0.1733 -0.0529 331 PRO A CA 2378 C C . PRO A 338 ? 0.5652 0.5633 0.4170 0.0412 0.1781 -0.0604 331 PRO A C 2379 O O . PRO A 338 ? 0.5777 0.5749 0.4219 0.0446 0.1903 -0.0598 331 PRO A O 2380 C CB . PRO A 338 ? 0.5719 0.5635 0.4047 0.0371 0.1693 -0.0507 331 PRO A CB 2381 C CG . PRO A 338 ? 0.6014 0.5913 0.4239 0.0389 0.1830 -0.0447 331 PRO A CG 2382 C CD . PRO A 338 ? 0.5783 0.5772 0.4277 0.0347 0.1892 -0.0395 331 PRO A CD 2383 N N . GLY A 339 ? 0.5567 0.5538 0.4117 0.0420 0.1689 -0.0675 332 GLY A N 2384 C CA . GLY A 339 ? 0.5726 0.5663 0.4193 0.0470 0.1712 -0.0756 332 GLY A CA 2385 C C . GLY A 339 ? 0.5742 0.5742 0.4391 0.0485 0.1800 -0.0779 332 GLY A C 2386 O O . GLY A 339 ? 0.5528 0.5609 0.4396 0.0453 0.1836 -0.0734 332 GLY A O 2387 N N . PHE A 340 ? 0.5856 0.5820 0.4416 0.0536 0.1832 -0.0852 333 PHE A N 2388 C CA . PHE A 340 ? 0.5895 0.5911 0.4623 0.0559 0.1899 -0.0891 333 PHE A CA 2389 C C . PHE A 340 ? 0.6190 0.6214 0.4854 0.0595 0.2058 -0.0873 333 PHE A C 2390 O O . PHE A 340 ? 0.6365 0.6332 0.4808 0.0614 0.2105 -0.0846 333 PHE A O 2391 C CB . PHE A 340 ? 0.5909 0.5876 0.4590 0.0594 0.1834 -0.0988 333 PHE A CB 2392 C CG . PHE A 340 ? 0.5723 0.5688 0.4506 0.0560 0.1691 -0.1009 333 PHE A CG 2393 C CD1 . PHE A 340 ? 0.5702 0.5594 0.4370 0.0580 0.1603 -0.1083 333 PHE A CD1 2394 C CD2 . PHE A 340 ? 0.5454 0.5487 0.4445 0.0509 0.1647 -0.0956 333 PHE A CD2 2395 C CE1 . PHE A 340 ? 0.5795 0.5684 0.4561 0.0549 0.1480 -0.1098 333 PHE A CE1 2396 C CE2 . PHE A 340 ? 0.5366 0.5394 0.4440 0.0481 0.1522 -0.0972 333 PHE A CE2 2397 C CZ . PHE A 340 ? 0.5195 0.5151 0.4160 0.0500 0.1442 -0.1041 333 PHE A CZ 2398 N N . THR A 341 ? 0.6286 0.6380 0.5145 0.0607 0.2140 -0.0886 334 THR A N 2399 C CA . THR A 341 ? 0.6662 0.6773 0.5492 0.0645 0.2303 -0.0873 334 THR A CA 2400 C C . THR A 341 ? 0.7077 0.7100 0.5646 0.0713 0.2345 -0.0940 334 THR A C 2401 O O . THR A 341 ? 0.7151 0.7118 0.5637 0.0735 0.2252 -0.1016 334 THR A O 2402 C CB . THR A 341 ? 0.6604 0.6813 0.5718 0.0649 0.2375 -0.0884 334 THR A CB 2403 O OG1 . THR A 341 ? 0.6552 0.6754 0.5736 0.0672 0.2304 -0.0968 334 THR A OG1 2404 C CG2 . THR A 341 ? 0.6317 0.6618 0.5690 0.0589 0.2361 -0.0815 334 THR A CG2 2405 N N . GLY A 342 ? 0.7383 0.7394 0.5835 0.0748 0.2489 -0.0911 335 GLY A N 2406 C CA . GLY A 342 ? 0.7785 0.7705 0.5948 0.0817 0.2546 -0.0961 335 GLY A CA 2407 C C . GLY A 342 ? 0.7973 0.7828 0.6030 0.0863 0.2472 -0.1072 335 GLY A C 2408 O O . GLY A 342 ? 0.8212 0.7969 0.6006 0.0892 0.2412 -0.1109 335 GLY A O 2409 N N . ASN A 343 ? 0.7887 0.7792 0.6149 0.0874 0.2476 -0.1127 336 ASN A N 2410 C CA . ASN A 343 ? 0.8041 0.7885 0.6229 0.0919 0.2413 -0.1236 336 ASN A CA 2411 C C . ASN A 343 ? 0.7839 0.7627 0.5974 0.0892 0.2235 -0.1273 336 ASN A C 2412 O O . ASN A 343 ? 0.7943 0.7652 0.5936 0.0930 0.2174 -0.1359 336 ASN A O 2413 C CB . ASN A 343 ? 0.8038 0.7954 0.6486 0.0933 0.2453 -0.1278 336 ASN A CB 2414 C CG . ASN A 343 ? 0.8548 0.8511 0.7037 0.0973 0.2634 -0.1263 336 ASN A CG 2415 O OD1 . ASN A 343 ? 0.9182 0.9109 0.7471 0.1002 0.2738 -0.1232 336 ASN A OD1 2416 N ND2 . ASN A 343 ? 0.8895 0.8938 0.7646 0.0979 0.2675 -0.1284 336 ASN A ND2 2417 N N . PHE A 344 ? 0.7514 0.7344 0.5770 0.0826 0.2155 -0.1209 337 PHE A N 2418 C CA . PHE A 344 ? 0.7294 0.7088 0.5547 0.0792 0.1992 -0.1233 337 PHE A CA 2419 C C . PHE A 344 ? 0.7226 0.6980 0.5313 0.0763 0.1934 -0.1177 337 PHE A C 2420 O O . PHE A 344 ? 0.7075 0.6812 0.5178 0.0727 0.1805 -0.1179 337 PHE A O 2421 C CB . PHE A 344 ? 0.6994 0.6870 0.5549 0.0743 0.1932 -0.1214 337 PHE A CB 2422 C CG . PHE A 344 ? 0.6999 0.6929 0.5750 0.0769 0.2000 -0.1250 337 PHE A CG 2423 C CD1 . PHE A 344 ? 0.6893 0.6921 0.5848 0.0753 0.2092 -0.1193 337 PHE A CD1 2424 C CD2 . PHE A 344 ? 0.7071 0.6955 0.5810 0.0811 0.1969 -0.1343 337 PHE A CD2 2425 C CE1 . PHE A 344 ? 0.6873 0.6956 0.6020 0.0779 0.2151 -0.1227 337 PHE A CE1 2426 C CE2 . PHE A 344 ? 0.7054 0.6987 0.5977 0.0838 0.2031 -0.1378 337 PHE A CE2 2427 C CZ . PHE A 344 ? 0.6872 0.6907 0.6000 0.0823 0.2121 -0.1319 337 PHE A CZ 2428 N N . SER A 345 ? 0.7319 0.7057 0.5246 0.0782 0.2033 -0.1127 338 SER A N 2429 C CA . SER A 345 ? 0.7348 0.7053 0.5125 0.0756 0.1998 -0.1061 338 SER A CA 2430 C C . SER A 345 ? 0.7349 0.6964 0.4923 0.0766 0.1864 -0.1110 338 SER A C 2431 O O . SER A 345 ? 0.7366 0.6969 0.4891 0.0730 0.1791 -0.1061 338 SER A O 2432 C CB . SER A 345 ? 0.7555 0.7242 0.5166 0.0788 0.2140 -0.1006 338 SER A CB 2433 O OG . SER A 345 ? 0.7969 0.7568 0.5320 0.0859 0.2175 -0.1072 338 SER A OG 2434 N N . THR A 346 ? 0.7393 0.6946 0.4863 0.0813 0.1830 -0.1208 339 THR A N 2435 C CA . THR A 346 ? 0.7445 0.6912 0.4733 0.0825 0.1699 -0.1266 339 THR A CA 2436 C C . THR A 346 ? 0.7200 0.6682 0.4665 0.0783 0.1561 -0.1306 339 THR A C 2437 O O . THR A 346 ? 0.7269 0.6690 0.4627 0.0782 0.1442 -0.1349 339 THR A O 2438 C CB . THR A 346 ? 0.7717 0.7092 0.4766 0.0901 0.1722 -0.1358 339 THR A CB 2439 O OG1 . THR A 346 ? 0.7745 0.7136 0.4931 0.0923 0.1744 -0.1432 339 THR A OG1 2440 C CG2 . THR A 346 ? 0.8111 0.7459 0.4953 0.0947 0.1859 -0.1316 339 THR A CG2 2441 N N . GLN A 347 ? 0.6824 0.6385 0.4558 0.0751 0.1578 -0.1291 340 GLN A N 2442 C CA . GLN A 347 ? 0.6522 0.6105 0.4439 0.0708 0.1459 -0.1308 340 GLN A CA 2443 C C . GLN A 347 ? 0.6305 0.5924 0.4282 0.0648 0.1399 -0.1225 340 GLN A C 2444 O O . GLN A 347 ? 0.6252 0.5908 0.4218 0.0633 0.1468 -0.1146 340 GLN A O 2445 C CB . GLN A 347 ? 0.6317 0.5965 0.4486 0.0702 0.1497 -0.1321 340 GLN A CB 2446 C CG . GLN A 347 ? 0.6538 0.6148 0.4656 0.0763 0.1557 -0.1407 340 GLN A CG 2447 C CD . GLN A 347 ? 0.6471 0.6143 0.4836 0.0764 0.1596 -0.1422 340 GLN A CD 2448 O OE1 . GLN A 347 ? 0.6406 0.6157 0.4985 0.0721 0.1591 -0.1364 340 GLN A OE1 2449 N NE2 . GLN A 347 ? 0.6638 0.6272 0.4971 0.0818 0.1633 -0.1505 340 GLN A NE2 2450 N N . LYS A 348 ? 0.6121 0.5727 0.4159 0.0616 0.1273 -0.1244 341 LYS A N 2451 C CA . LYS A 348 ? 0.5887 0.5527 0.3991 0.0561 0.1207 -0.1173 341 LYS A CA 2452 C C . LYS A 348 ? 0.5606 0.5284 0.3935 0.0522 0.1128 -0.1178 341 LYS A C 2453 O O . LYS A 348 ? 0.5499 0.5169 0.3919 0.0537 0.1117 -0.1237 341 LYS A O 2454 C CB . LYS A 348 ? 0.6069 0.5641 0.3964 0.0565 0.1126 -0.1179 341 LYS A CB 2455 C CG . LYS A 348 ? 0.6432 0.5949 0.4069 0.0614 0.1195 -0.1181 341 LYS A CG 2456 C CD . LYS A 348 ? 0.6838 0.6337 0.4335 0.0600 0.1175 -0.1114 341 LYS A CD 2457 C CE . LYS A 348 ? 0.7297 0.6761 0.4586 0.0647 0.1291 -0.1090 341 LYS A CE 2458 N NZ . LYS A 348 ? 0.7653 0.7068 0.4735 0.0653 0.1263 -0.1042 341 LYS A NZ 2459 N N . VAL A 349 ? 0.5346 0.5062 0.3763 0.0473 0.1077 -0.1114 342 VAL A N 2460 C CA . VAL A 349 ? 0.5120 0.4866 0.3728 0.0436 0.0999 -0.1111 342 VAL A CA 2461 C C . VAL A 349 ? 0.5080 0.4782 0.3616 0.0416 0.0884 -0.1123 342 VAL A C 2462 O O . VAL A 349 ? 0.5178 0.4862 0.3581 0.0411 0.0867 -0.1091 342 VAL A O 2463 C CB . VAL A 349 ? 0.4933 0.4761 0.3716 0.0398 0.1030 -0.1030 342 VAL A CB 2464 C CG1 . VAL A 349 ? 0.4648 0.4496 0.3582 0.0358 0.0936 -0.1014 342 VAL A CG1 2465 C CG2 . VAL A 349 ? 0.4992 0.4868 0.3897 0.0418 0.1127 -0.1034 342 VAL A CG2 2466 N N . LYS A 350 ? 0.5000 0.4682 0.3628 0.0407 0.0808 -0.1170 343 LYS A N 2467 C CA . LYS A 350 ? 0.4988 0.4633 0.3578 0.0387 0.0699 -0.1187 343 LYS A CA 2468 C C . LYS A 350 ? 0.4753 0.4431 0.3540 0.0346 0.0640 -0.1161 343 LYS A C 2469 O O . LYS A 350 ? 0.4625 0.4312 0.3549 0.0348 0.0648 -0.1183 343 LYS A O 2470 C CB . LYS A 350 ? 0.5208 0.4775 0.3687 0.0421 0.0655 -0.1283 343 LYS A CB 2471 C CG . LYS A 350 ? 0.5335 0.4862 0.3781 0.0401 0.0538 -0.1308 343 LYS A CG 2472 C CD . LYS A 350 ? 0.5773 0.5222 0.4108 0.0437 0.0493 -0.1409 343 LYS A CD 2473 C CE . LYS A 350 ? 0.6061 0.5474 0.4348 0.0420 0.0377 -0.1433 343 LYS A CE 2474 N NZ . LYS A 350 ? 0.6693 0.6025 0.4843 0.0458 0.0325 -0.1533 343 LYS A NZ 2475 N N . MET A 351 ? 0.4689 0.4384 0.3489 0.0311 0.0584 -0.1112 344 MET A N 2476 C CA . MET A 351 ? 0.4442 0.4162 0.3409 0.0275 0.0526 -0.1087 344 MET A CA 2477 C C . MET A 351 ? 0.4591 0.4259 0.3546 0.0269 0.0434 -0.1140 344 MET A C 2478 O O . MET A 351 ? 0.4812 0.4437 0.3621 0.0283 0.0399 -0.1177 344 MET A O 2479 C CB . MET A 351 ? 0.4358 0.4126 0.3354 0.0241 0.0518 -0.1005 344 MET A CB 2480 C CG . MET A 351 ? 0.4091 0.3909 0.3101 0.0244 0.0605 -0.0951 344 MET A CG 2481 S SD . MET A 351 ? 0.4221 0.4090 0.3279 0.0205 0.0590 -0.0860 344 MET A SD 2482 C CE . MET A 351 ? 0.3935 0.3832 0.3196 0.0179 0.0539 -0.0846 344 MET A CE 2483 N N . HIS A 352 ? 0.4390 0.4061 0.3500 0.0249 0.0396 -0.1145 345 HIS A N 2484 C CA . HIS A 352 ? 0.4395 0.4025 0.3530 0.0233 0.0308 -0.1183 345 HIS A CA 2485 C C . HIS A 352 ? 0.4131 0.3796 0.3418 0.0195 0.0276 -0.1124 345 HIS A C 2486 O O . HIS A 352 ? 0.4056 0.3729 0.3480 0.0189 0.0288 -0.1115 345 HIS A O 2487 C CB . HIS A 352 ? 0.4448 0.4024 0.3622 0.0254 0.0295 -0.1262 345 HIS A CB 2488 C CG . HIS A 352 ? 0.4905 0.4452 0.3964 0.0299 0.0350 -0.1317 345 HIS A CG 2489 N ND1 . HIS A 352 ? 0.5098 0.4677 0.4182 0.0319 0.0438 -0.1298 345 HIS A ND1 2490 C CD2 . HIS A 352 ? 0.5184 0.4670 0.4106 0.0330 0.0330 -0.1395 345 HIS A CD2 2491 C CE1 . HIS A 352 ? 0.5297 0.4839 0.4263 0.0360 0.0477 -0.1358 345 HIS A CE1 2492 N NE2 . HIS A 352 ? 0.5678 0.5160 0.4536 0.0369 0.0412 -0.1418 345 HIS A NE2 2493 N N . ILE A 353 ? 0.4064 0.3748 0.3322 0.0171 0.0235 -0.1085 346 ILE A N 2494 C CA . ILE A 353 ? 0.3920 0.3637 0.3305 0.0137 0.0206 -0.1027 346 ILE A CA 2495 C C . ILE A 353 ? 0.3950 0.3642 0.3354 0.0117 0.0125 -0.1050 346 ILE A C 2496 O O . ILE A 353 ? 0.4039 0.3720 0.3335 0.0119 0.0086 -0.1065 346 ILE A O 2497 C CB . ILE A 353 ? 0.3970 0.3742 0.3335 0.0125 0.0236 -0.0951 346 ILE A CB 2498 C CG1 . ILE A 353 ? 0.3884 0.3681 0.3224 0.0145 0.0317 -0.0935 346 ILE A CG1 2499 C CG2 . ILE A 353 ? 0.3726 0.3530 0.3224 0.0096 0.0213 -0.0895 346 ILE A CG2 2500 C CD1 . ILE A 353 ? 0.4042 0.3853 0.3514 0.0153 0.0355 -0.0936 346 ILE A CD1 2501 N N . HIS A 354 ? 0.3853 0.3538 0.3400 0.0099 0.0100 -0.1048 347 HIS A N 2502 C CA . HIS A 354 ? 0.3924 0.3586 0.3528 0.0077 0.0027 -0.1071 347 HIS A CA 2503 C C . HIS A 354 ? 0.3720 0.3411 0.3460 0.0046 0.0015 -0.1009 347 HIS A C 2504 O O . HIS A 354 ? 0.3706 0.3381 0.3535 0.0025 -0.0033 -0.1023 347 HIS A O 2505 C CB . HIS A 354 ? 0.4065 0.3669 0.3710 0.0087 0.0006 -0.1147 347 HIS A CB 2506 C CG . HIS A 354 ? 0.4636 0.4206 0.4144 0.0122 0.0023 -0.1212 347 HIS A CG 2507 N ND1 . HIS A 354 ? 0.5153 0.4702 0.4667 0.0148 0.0075 -0.1239 347 HIS A ND1 2508 C CD2 . HIS A 354 ? 0.5103 0.4654 0.4453 0.0141 -0.0002 -0.1251 347 HIS A CD2 2509 C CE1 . HIS A 354 ? 0.5264 0.4784 0.4633 0.0180 0.0085 -0.1295 347 HIS A CE1 2510 N NE2 . HIS A 354 ? 0.5477 0.4995 0.4739 0.0177 0.0039 -0.1303 347 HIS A NE2 2511 N N . SER A 355 ? 0.3493 0.3228 0.3251 0.0043 0.0060 -0.0942 348 SER A N 2512 C CA . SER A 355 ? 0.3333 0.3097 0.3199 0.0021 0.0055 -0.0880 348 SER A CA 2513 C C . SER A 355 ? 0.3447 0.3225 0.3307 -0.0001 0.0002 -0.0868 348 SER A C 2514 O O . SER A 355 ? 0.3460 0.3239 0.3210 0.0005 -0.0021 -0.0888 348 SER A O 2515 C CB . SER A 355 ? 0.3204 0.3012 0.3059 0.0027 0.0105 -0.0817 348 SER A CB 2516 O OG . SER A 355 ? 0.3348 0.3150 0.3223 0.0048 0.0151 -0.0830 348 SER A OG 2517 N N . THR A 356 ? 0.3344 0.3130 0.3318 -0.0022 -0.0014 -0.0833 349 THR A N 2518 C CA . THR A 356 ? 0.3352 0.3158 0.3344 -0.0042 -0.0061 -0.0818 349 THR A CA 2519 C C . THR A 356 ? 0.3257 0.3104 0.3301 -0.0053 -0.0040 -0.0743 349 THR A C 2520 O O . THR A 356 ? 0.3290 0.3137 0.3401 -0.0051 -0.0004 -0.0707 349 THR A O 2521 C CB . THR A 356 ? 0.3523 0.3299 0.3619 -0.0061 -0.0107 -0.0857 349 THR A CB 2522 O OG1 . THR A 356 ? 0.4072 0.3834 0.4293 -0.0068 -0.0077 -0.0831 349 THR A OG1 2523 C CG2 . THR A 356 ? 0.3489 0.3220 0.3534 -0.0048 -0.0133 -0.0938 349 THR A CG2 2524 N N . ASN A 357 ? 0.3084 0.2961 0.3089 -0.0061 -0.0066 -0.0720 350 ASN A N 2525 C CA . ASN A 357 ? 0.3096 0.3009 0.3150 -0.0070 -0.0053 -0.0654 350 ASN A CA 2526 C C . ASN A 357 ? 0.3153 0.3065 0.3326 -0.0091 -0.0084 -0.0652 350 ASN A C 2527 O O . ASN A 357 ? 0.3282 0.3185 0.3468 -0.0100 -0.0134 -0.0696 350 ASN A O 2528 C CB . ASN A 357 ? 0.3086 0.3030 0.3044 -0.0066 -0.0064 -0.0630 350 ASN A CB 2529 C CG . ASN A 357 ? 0.3344 0.3290 0.3196 -0.0049 -0.0027 -0.0626 350 ASN A CG 2530 O OD1 . ASN A 357 ? 0.3474 0.3417 0.3344 -0.0040 0.0016 -0.0617 350 ASN A OD1 2531 N ND2 . ASN A 357 ? 0.3983 0.3935 0.3726 -0.0043 -0.0042 -0.0630 350 ASN A ND2 2532 N N A GLU A 358 ? 0.3056 0.2975 0.3322 -0.0097 -0.0055 -0.0603 351 GLU A N 2533 N N B GLU A 358 ? 0.3029 0.2951 0.3290 -0.0097 -0.0056 -0.0601 351 GLU A N 2534 C CA A GLU A 358 ? 0.3141 0.3058 0.3533 -0.0117 -0.0072 -0.0596 351 GLU A CA 2535 C CA B GLU A 358 ? 0.3077 0.2992 0.3469 -0.0116 -0.0068 -0.0594 351 GLU A CA 2536 C C A GLU A 358 ? 0.2876 0.2821 0.3311 -0.0118 -0.0042 -0.0526 351 GLU A C 2537 C C B GLU A 358 ? 0.2865 0.2809 0.3302 -0.0118 -0.0041 -0.0524 351 GLU A C 2538 O O A GLU A 358 ? 0.2805 0.2747 0.3219 -0.0103 0.0000 -0.0487 351 GLU A O 2539 O O B GLU A 358 ? 0.2809 0.2751 0.3227 -0.0103 0.0002 -0.0484 351 GLU A O 2540 C CB A GLU A 358 ? 0.3209 0.3081 0.3700 -0.0124 -0.0062 -0.0619 351 GLU A CB 2541 C CB B GLU A 358 ? 0.3102 0.2971 0.3571 -0.0117 -0.0047 -0.0611 351 GLU A CB 2542 C CG A GLU A 358 ? 0.3940 0.3774 0.4381 -0.0110 -0.0056 -0.0669 351 GLU A CG 2543 C CG B GLU A 358 ? 0.3611 0.3445 0.4035 -0.0110 -0.0065 -0.0681 351 GLU A CG 2544 C CD A GLU A 358 ? 0.4282 0.4066 0.4837 -0.0119 -0.0053 -0.0692 351 GLU A CD 2545 C CD B GLU A 358 ? 0.3755 0.3571 0.4234 -0.0127 -0.0122 -0.0740 351 GLU A CD 2546 O OE1 A GLU A 358 ? 0.5109 0.4864 0.5678 -0.0125 -0.0090 -0.0758 351 GLU A OE1 2547 O OE1 B GLU A 358 ? 0.4073 0.3909 0.4641 -0.0148 -0.0145 -0.0725 351 GLU A OE1 2548 O OE2 A GLU A 358 ? 0.4177 0.3949 0.4806 -0.0119 -0.0014 -0.0645 351 GLU A OE2 2549 O OE2 B GLU A 358 ? 0.4157 0.3938 0.4594 -0.0120 -0.0144 -0.0805 351 GLU A OE2 2550 N N . VAL A 359 ? 0.2844 0.2815 0.3340 -0.0132 -0.0065 -0.0512 352 VAL A N 2551 C CA . VAL A 359 ? 0.2659 0.2654 0.3206 -0.0131 -0.0034 -0.0448 352 VAL A CA 2552 C C . VAL A 359 ? 0.2609 0.2572 0.3259 -0.0135 0.0005 -0.0424 352 VAL A C 2553 O O . VAL A 359 ? 0.2709 0.2650 0.3460 -0.0154 -0.0008 -0.0452 352 VAL A O 2554 C CB . VAL A 359 ? 0.2679 0.2711 0.3277 -0.0144 -0.0066 -0.0442 352 VAL A CB 2555 C CG1 . VAL A 359 ? 0.2708 0.2760 0.3365 -0.0141 -0.0026 -0.0378 352 VAL A CG1 2556 C CG2 . VAL A 359 ? 0.2888 0.2946 0.3372 -0.0136 -0.0100 -0.0455 352 VAL A CG2 2557 N N . THR A 360 ? 0.2380 0.2336 0.3003 -0.0116 0.0051 -0.0373 353 THR A N 2558 C CA . THR A 360 ? 0.2405 0.2320 0.3090 -0.0110 0.0092 -0.0346 353 THR A CA 2559 C C . THR A 360 ? 0.2350 0.2272 0.3033 -0.0093 0.0133 -0.0277 353 THR A C 2560 O O . THR A 360 ? 0.2327 0.2278 0.2926 -0.0078 0.0134 -0.0256 353 THR A O 2561 C CB . THR A 360 ? 0.2544 0.2428 0.3166 -0.0093 0.0101 -0.0368 353 THR A CB 2562 O OG1 . THR A 360 ? 0.2811 0.2688 0.3414 -0.0104 0.0064 -0.0435 353 THR A OG1 2563 C CG2 . THR A 360 ? 0.2576 0.2410 0.3264 -0.0085 0.0136 -0.0346 353 THR A CG2 2564 N N . ARG A 361 ? 0.2378 0.2271 0.3152 -0.0095 0.0169 -0.0241 354 ARG A N 2565 C CA . ARG A 361 ? 0.2305 0.2199 0.3067 -0.0075 0.0213 -0.0174 354 ARG A CA 2566 C C . ARG A 361 ? 0.2296 0.2162 0.2967 -0.0040 0.0234 -0.0150 354 ARG A C 2567 O O . ARG A 361 ? 0.2430 0.2257 0.3105 -0.0034 0.0238 -0.0166 354 ARG A O 2568 C CB . ARG A 361 ? 0.2323 0.2193 0.3210 -0.0087 0.0251 -0.0138 354 ARG A CB 2569 C CG . ARG A 361 ? 0.2604 0.2477 0.3470 -0.0062 0.0300 -0.0068 354 ARG A CG 2570 C CD . ARG A 361 ? 0.2643 0.2517 0.3643 -0.0082 0.0333 -0.0039 354 ARG A CD 2571 N NE . ARG A 361 ? 0.2862 0.2796 0.3913 -0.0106 0.0298 -0.0067 354 ARG A NE 2572 C CZ . ARG A 361 ? 0.3165 0.3123 0.4337 -0.0124 0.0318 -0.0047 354 ARG A CZ 2573 N NH1 . ARG A 361 ? 0.3015 0.2940 0.4272 -0.0123 0.0381 0.0005 354 ARG A NH1 2574 N NH2 . ARG A 361 ? 0.3230 0.3244 0.4441 -0.0141 0.0277 -0.0077 354 ARG A NH2 2575 N N . ILE A 362 ? 0.2219 0.2104 0.2815 -0.0016 0.0246 -0.0113 355 ILE A N 2576 C CA . ILE A 362 ? 0.2273 0.2134 0.2785 0.0021 0.0261 -0.0088 355 ILE A CA 2577 C C . ILE A 362 ? 0.2316 0.2163 0.2811 0.0047 0.0299 -0.0026 355 ILE A C 2578 O O . ILE A 362 ? 0.2319 0.2189 0.2849 0.0037 0.0311 -0.0007 355 ILE A O 2579 C CB . ILE A 362 ? 0.2156 0.2052 0.2575 0.0029 0.0229 -0.0114 355 ILE A CB 2580 C CG1 . ILE A 362 ? 0.2095 0.2035 0.2481 0.0026 0.0217 -0.0104 355 ILE A CG1 2581 C CG2 . ILE A 362 ? 0.2204 0.2107 0.2630 0.0008 0.0200 -0.0174 355 ILE A CG2 2582 C CD1 . ILE A 362 ? 0.2154 0.2117 0.2446 0.0042 0.0196 -0.0113 355 ILE A CD1 2583 N N . TYR A 363 ? 0.2284 0.2093 0.2724 0.0083 0.0317 0.0005 356 TYR A N 2584 C CA . TYR A 363 ? 0.2317 0.2098 0.2728 0.0114 0.0357 0.0066 356 TYR A CA 2585 C C . TYR A 363 ? 0.2337 0.2109 0.2634 0.0158 0.0347 0.0081 356 TYR A C 2586 O O . TYR A 363 ? 0.2443 0.2187 0.2711 0.0178 0.0336 0.0075 356 TYR A O 2587 C CB . TYR A 363 ? 0.2386 0.2106 0.2857 0.0120 0.0398 0.0100 356 TYR A CB 2588 C CG . TYR A 363 ? 0.2519 0.2238 0.3120 0.0077 0.0410 0.0086 356 TYR A CG 2589 C CD1 . TYR A 363 ? 0.2707 0.2432 0.3379 0.0065 0.0449 0.0123 356 TYR A CD1 2590 C CD2 . TYR A 363 ? 0.2510 0.2226 0.3169 0.0049 0.0380 0.0033 356 TYR A CD2 2591 C CE1 . TYR A 363 ? 0.2862 0.2590 0.3673 0.0023 0.0455 0.0107 356 TYR A CE1 2592 C CE2 . TYR A 363 ? 0.2709 0.2423 0.3494 0.0009 0.0383 0.0013 356 TYR A CE2 2593 C CZ . TYR A 363 ? 0.2857 0.2579 0.3722 -0.0005 0.0418 0.0050 356 TYR A CZ 2594 O OH . TYR A 363 ? 0.3040 0.2762 0.4044 -0.0045 0.0416 0.0028 356 TYR A OH 2595 N N . ASN A 364 ? 0.2303 0.2095 0.2542 0.0176 0.0350 0.0103 357 ASN A N 2596 C CA . ASN A 364 ? 0.2417 0.2191 0.2547 0.0224 0.0339 0.0120 357 ASN A CA 2597 C C . ASN A 364 ? 0.2544 0.2264 0.2641 0.0262 0.0387 0.0180 357 ASN A C 2598 O O . ASN A 364 ? 0.2855 0.2572 0.3000 0.0251 0.0429 0.0211 357 ASN A O 2599 C CB . ASN A 364 ? 0.2316 0.2133 0.2391 0.0228 0.0317 0.0110 357 ASN A CB 2600 C CG . ASN A 364 ? 0.2453 0.2322 0.2547 0.0194 0.0275 0.0058 357 ASN A CG 2601 O OD1 . ASN A 364 ? 0.2317 0.2188 0.2426 0.0182 0.0253 0.0026 357 ASN A OD1 2602 N ND2 . ASN A 364 ? 0.2611 0.2518 0.2697 0.0182 0.0264 0.0052 357 ASN A ND2 2603 N N . VAL A 365 ? 0.2659 0.2335 0.2675 0.0308 0.0380 0.0199 358 VAL A N 2604 C CA . VAL A 365 ? 0.2664 0.2285 0.2614 0.0354 0.0423 0.0259 358 VAL A CA 2605 C C . VAL A 365 ? 0.2668 0.2300 0.2506 0.0392 0.0401 0.0259 358 VAL A C 2606 O O . VAL A 365 ? 0.2660 0.2308 0.2451 0.0405 0.0348 0.0225 358 VAL A O 2607 C CB . VAL A 365 ? 0.2736 0.2289 0.2653 0.0391 0.0428 0.0284 358 VAL A CB 2608 C CG1 . VAL A 365 ? 0.3061 0.2548 0.2910 0.0437 0.0484 0.0355 358 VAL A CG1 2609 C CG2 . VAL A 365 ? 0.2869 0.2412 0.2898 0.0352 0.0434 0.0266 358 VAL A CG2 2610 N N . ILE A 366 ? 0.2757 0.2380 0.2560 0.0411 0.0442 0.0297 359 ILE A N 2611 C CA . ILE A 366 ? 0.2848 0.2477 0.2545 0.0449 0.0426 0.0297 359 ILE A CA 2612 C C . ILE A 366 ? 0.2906 0.2467 0.2500 0.0510 0.0471 0.0356 359 ILE A C 2613 O O . ILE A 366 ? 0.3120 0.2663 0.2744 0.0509 0.0540 0.0402 359 ILE A O 2614 C CB . ILE A 366 ? 0.2874 0.2561 0.2619 0.0418 0.0437 0.0285 359 ILE A CB 2615 C CG1 . ILE A 366 ? 0.2929 0.2677 0.2773 0.0357 0.0398 0.0233 359 ILE A CG1 2616 C CG2 . ILE A 366 ? 0.2988 0.2676 0.2620 0.0460 0.0417 0.0280 359 ILE A CG2 2617 C CD1 . ILE A 366 ? 0.2965 0.2734 0.2767 0.0358 0.0331 0.0185 359 ILE A CD1 2618 N N . GLY A 367 ? 0.3140 0.2662 0.2616 0.0563 0.0434 0.0354 360 GLY A N 2619 C CA . GLY A 367 ? 0.3179 0.2626 0.2527 0.0632 0.0469 0.0408 360 GLY A CA 2620 C C . GLY A 367 ? 0.3208 0.2656 0.2439 0.0675 0.0449 0.0397 360 GLY A C 2621 O O . GLY A 367 ? 0.3261 0.2749 0.2484 0.0667 0.0383 0.0345 360 GLY A O 2622 N N . THR A 368 ? 0.3293 0.2697 0.2435 0.0721 0.0507 0.0447 361 THR A N 2623 C CA . THR A 368 ? 0.3418 0.2818 0.2441 0.0766 0.0491 0.0435 361 THR A CA 2624 C C . THR A 368 ? 0.3645 0.2957 0.2492 0.0851 0.0499 0.0472 361 THR A C 2625 O O . THR A 368 ? 0.3713 0.2967 0.2529 0.0876 0.0567 0.0534 361 THR A O 2626 C CB . THR A 368 ? 0.3495 0.2925 0.2560 0.0750 0.0559 0.0457 361 THR A CB 2627 O OG1 . THR A 368 ? 0.3519 0.3029 0.2740 0.0675 0.0545 0.0420 361 THR A OG1 2628 C CG2 . THR A 368 ? 0.3785 0.3208 0.2727 0.0800 0.0548 0.0443 361 THR A CG2 2629 N N . LEU A 369 ? 0.3640 0.2939 0.2374 0.0897 0.0429 0.0434 362 LEU A N 2630 C CA . LEU A 369 ? 0.3803 0.3016 0.2344 0.0987 0.0429 0.0463 362 LEU A CA 2631 C C . LEU A 369 ? 0.3836 0.3060 0.2295 0.1015 0.0422 0.0438 362 LEU A C 2632 O O . LEU A 369 ? 0.3852 0.3106 0.2303 0.1014 0.0342 0.0376 362 LEU A O 2633 C CB . LEU A 369 ? 0.3936 0.3120 0.2417 0.1021 0.0339 0.0431 362 LEU A CB 2634 C CG . LEU A 369 ? 0.4568 0.3659 0.2841 0.1120 0.0317 0.0452 362 LEU A CG 2635 C CD1 . LEU A 369 ? 0.4752 0.3767 0.2938 0.1162 0.0415 0.0537 362 LEU A CD1 2636 C CD2 . LEU A 369 ? 0.4599 0.3673 0.2854 0.1144 0.0222 0.0418 362 LEU A CD2 2637 N N A ARG A 370 ? 0.3875 0.3074 0.2282 0.1041 0.0510 0.0486 363 ARG A N 2638 N N B ARG A 370 ? 0.3855 0.3055 0.2264 0.1040 0.0509 0.0486 363 ARG A N 2639 C CA A ARG A 370 ? 0.3961 0.3173 0.2305 0.1066 0.0519 0.0467 363 ARG A CA 2640 C CA B ARG A 370 ? 0.3911 0.3128 0.2265 0.1061 0.0517 0.0463 363 ARG A CA 2641 C C A ARG A 370 ? 0.4080 0.3238 0.2240 0.1143 0.0447 0.0431 363 ARG A C 2642 C C B ARG A 370 ? 0.4053 0.3213 0.2216 0.1142 0.0452 0.0433 363 ARG A C 2643 O O A ARG A 370 ? 0.4254 0.3333 0.2268 0.1211 0.0442 0.0459 363 ARG A O 2644 O O B ARG A 370 ? 0.4227 0.3304 0.2241 0.1211 0.0456 0.0465 363 ARG A O 2645 C CB A ARG A 370 ? 0.4130 0.3317 0.2448 0.1087 0.0637 0.0534 363 ARG A CB 2646 C CB B ARG A 370 ? 0.4034 0.3239 0.2389 0.1070 0.0634 0.0527 363 ARG A CB 2647 C CG A ARG A 370 ? 0.4271 0.3450 0.2483 0.1135 0.0656 0.0521 363 ARG A CG 2648 C CG B ARG A 370 ? 0.4104 0.3324 0.2406 0.1096 0.0658 0.0511 363 ARG A CG 2649 C CD A ARG A 370 ? 0.5065 0.4227 0.3268 0.1155 0.0782 0.0589 363 ARG A CD 2650 C CD B ARG A 370 ? 0.4486 0.3714 0.2845 0.1089 0.0779 0.0573 363 ARG A CD 2651 N NE A ARG A 370 ? 0.5507 0.4587 0.3620 0.1200 0.0851 0.0663 363 ARG A NE 2652 N NE B ARG A 370 ? 0.5159 0.4307 0.3424 0.1136 0.0852 0.0647 363 ARG A NE 2653 C CZ A ARG A 370 ? 0.5899 0.4887 0.3795 0.1292 0.0869 0.0693 363 ARG A CZ 2654 C CZ B ARG A 370 ? 0.5189 0.4333 0.3560 0.1098 0.0906 0.0697 363 ARG A CZ 2655 N NH1 A ARG A 370 ? 0.6108 0.5071 0.3852 0.1352 0.0819 0.0648 363 ARG A NH1 2656 N NH1 B ARG A 370 ? 0.4807 0.4026 0.3385 0.1010 0.0893 0.0677 363 ARG A NH1 2657 N NH2 A ARG A 370 ? 0.6239 0.5153 0.4067 0.1327 0.0936 0.0767 363 ARG A NH2 2658 N NH2 B ARG A 370 ? 0.5470 0.4529 0.3736 0.1150 0.0973 0.0767 363 ARG A NH2 2659 N N . GLY A 371 ? 0.4009 0.3207 0.2178 0.1135 0.0388 0.0369 364 GLY A N 2660 C CA . GLY A 371 ? 0.4128 0.3277 0.2133 0.1206 0.0317 0.0328 364 GLY A CA 2661 C C . GLY A 371 ? 0.4311 0.3392 0.2139 0.1287 0.0381 0.0363 364 GLY A C 2662 O O . GLY A 371 ? 0.4418 0.3516 0.2280 0.1276 0.0474 0.0400 364 GLY A O 2663 N N . ALA A 372 ? 0.4533 0.3535 0.2172 0.1372 0.0332 0.0351 365 ALA A N 2664 C CA . ALA A 372 ? 0.4767 0.3689 0.2200 0.1463 0.0384 0.0380 365 ALA A CA 2665 C C . ALA A 372 ? 0.4929 0.3868 0.2326 0.1480 0.0369 0.0330 365 ALA A C 2666 O O . ALA A 372 ? 0.4983 0.3887 0.2274 0.1530 0.0450 0.0361 365 ALA A O 2667 C CB . ALA A 372 ? 0.4921 0.3750 0.2156 0.1551 0.0321 0.0377 365 ALA A CB 2668 N N . VAL A 373 ? 0.4747 0.3735 0.2225 0.1443 0.0269 0.0254 366 VAL A N 2669 C CA . VAL A 373 ? 0.4842 0.3834 0.2274 0.1466 0.0237 0.0197 366 VAL A CA 2670 C C . VAL A 373 ? 0.4636 0.3725 0.2274 0.1376 0.0238 0.0169 366 VAL A C 2671 O O . VAL A 373 ? 0.4665 0.3771 0.2311 0.1379 0.0284 0.0166 366 VAL A O 2672 C CB . VAL A 373 ? 0.5106 0.4053 0.2428 0.1517 0.0108 0.0124 366 VAL A CB 2673 C CG1 . VAL A 373 ? 0.5198 0.4145 0.2482 0.1539 0.0072 0.0062 366 VAL A CG1 2674 C CG2 . VAL A 373 ? 0.5503 0.4347 0.2602 0.1616 0.0098 0.0148 366 VAL A CG2 2675 N N . GLU A 374 ? 0.4351 0.3501 0.2152 0.1299 0.0190 0.0152 367 GLU A N 2676 C CA . GLU A 374 ? 0.4217 0.3455 0.2207 0.1214 0.0190 0.0130 367 GLU A CA 2677 C C . GLU A 374 ? 0.3865 0.3159 0.2013 0.1140 0.0242 0.0174 367 GLU A C 2678 O O . GLU A 374 ? 0.3724 0.3063 0.1990 0.1081 0.0187 0.0149 367 GLU A O 2679 C CB . GLU A 374 ? 0.4089 0.3353 0.2136 0.1187 0.0077 0.0057 367 GLU A CB 2680 C CG . GLU A 374 ? 0.4467 0.3678 0.2378 0.1254 0.0014 0.0002 367 GLU A CG 2681 C CD . GLU A 374 ? 0.4340 0.3585 0.2346 0.1213 -0.0090 -0.0067 367 GLU A CD 2682 O OE1 . GLU A 374 ? 0.4519 0.3809 0.2623 0.1170 -0.0092 -0.0091 367 GLU A OE1 2683 O OE2 . GLU A 374 ? 0.4872 0.4096 0.2855 0.1229 -0.0169 -0.0097 367 GLU A OE2 2684 N N . PRO A 375 ? 0.3910 0.3200 0.2064 0.1143 0.0347 0.0238 368 PRO A N 2685 C CA . PRO A 375 ? 0.3814 0.3151 0.2119 0.1075 0.0396 0.0278 368 PRO A CA 2686 C C . PRO A 375 ? 0.3666 0.3091 0.2154 0.0991 0.0380 0.0249 368 PRO A C 2687 O O . PRO A 375 ? 0.3561 0.3026 0.2175 0.0930 0.0386 0.0261 368 PRO A O 2688 C CB . PRO A 375 ? 0.3945 0.3255 0.2216 0.1103 0.0513 0.0349 368 PRO A CB 2689 C CG . PRO A 375 ? 0.4097 0.3379 0.2249 0.1163 0.0533 0.0337 368 PRO A CG 2690 C CD . PRO A 375 ? 0.4096 0.3335 0.2120 0.1211 0.0430 0.0277 368 PRO A CD 2691 N N . ASP A 376 ? 0.3620 0.3069 0.2114 0.0990 0.0354 0.0210 369 ASP A N 2692 C CA . ASP A 376 ? 0.3473 0.3000 0.2127 0.0916 0.0331 0.0181 369 ASP A CA 2693 C C . ASP A 376 ? 0.3281 0.2825 0.1970 0.0885 0.0230 0.0124 369 ASP A C 2694 O O . ASP A 376 ? 0.3072 0.2662 0.1848 0.0843 0.0199 0.0093 369 ASP A O 2695 C CB . ASP A 376 ? 0.3568 0.3113 0.2227 0.0928 0.0360 0.0173 369 ASP A CB 2696 C CG . ASP A 376 ? 0.4136 0.3640 0.2675 0.0982 0.0301 0.0125 369 ASP A CG 2697 O OD1 . ASP A 376 ? 0.4505 0.3949 0.2918 0.1031 0.0256 0.0109 369 ASP A OD1 2698 O OD2 . ASP A 376 ? 0.4374 0.3900 0.2942 0.0978 0.0296 0.0101 369 ASP A OD2 2699 N N . ARG A 377 ? 0.3287 0.2795 0.1915 0.0908 0.0181 0.0113 370 ARG A N 2700 C CA . ARG A 377 ? 0.3227 0.2757 0.1910 0.0875 0.0093 0.0064 370 ARG A CA 2701 C C . ARG A 377 ? 0.3270 0.2805 0.2002 0.0851 0.0095 0.0084 370 ARG A C 2702 O O . ARG A 377 ? 0.3244 0.2728 0.1888 0.0896 0.0118 0.0117 370 ARG A O 2703 C CB . ARG A 377 ? 0.3321 0.2799 0.1883 0.0936 0.0019 0.0020 370 ARG A CB 2704 C CG . ARG A 377 ? 0.3271 0.2742 0.1791 0.0960 0.0012 -0.0008 370 ARG A CG 2705 C CD . ARG A 377 ? 0.3321 0.2851 0.1979 0.0891 -0.0028 -0.0044 370 ARG A CD 2706 N NE . ARG A 377 ? 0.3130 0.2661 0.1780 0.0900 -0.0036 -0.0071 370 ARG A NE 2707 C CZ . ARG A 377 ? 0.3156 0.2719 0.1859 0.0879 0.0021 -0.0050 370 ARG A CZ 2708 N NH1 . ARG A 377 ? 0.3053 0.2649 0.1817 0.0851 0.0095 -0.0001 370 ARG A NH1 2709 N NH2 . ARG A 377 ? 0.3229 0.2791 0.1933 0.0887 0.0000 -0.0080 370 ARG A NH2 2710 N N . TYR A 378 ? 0.3009 0.2602 0.1876 0.0782 0.0073 0.0068 371 TYR A N 2711 C CA . TYR A 378 ? 0.2981 0.2585 0.1912 0.0752 0.0084 0.0087 371 TYR A CA 2712 C C . TYR A 378 ? 0.3023 0.2638 0.1990 0.0738 0.0009 0.0046 371 TYR A C 2713 O O . TYR A 378 ? 0.3019 0.2677 0.2063 0.0697 -0.0033 0.0007 371 TYR A O 2714 C CB . TYR A 378 ? 0.2855 0.2518 0.1923 0.0681 0.0129 0.0102 371 TYR A CB 2715 C CG . TYR A 378 ? 0.2870 0.2538 0.1947 0.0680 0.0203 0.0140 371 TYR A CG 2716 C CD1 . TYR A 378 ? 0.3155 0.2772 0.2132 0.0737 0.0257 0.0180 371 TYR A CD1 2717 C CD2 . TYR A 378 ? 0.2848 0.2574 0.2039 0.0624 0.0222 0.0136 371 TYR A CD2 2718 C CE1 . TYR A 378 ? 0.3058 0.2688 0.2064 0.0735 0.0331 0.0215 371 TYR A CE1 2719 C CE2 . TYR A 378 ? 0.2867 0.2607 0.2089 0.0621 0.0285 0.0167 371 TYR A CE2 2720 C CZ . TYR A 378 ? 0.2930 0.2624 0.2067 0.0675 0.0344 0.0208 371 TYR A CZ 2721 O OH . TYR A 378 ? 0.3154 0.2867 0.2336 0.0672 0.0413 0.0239 371 TYR A OH 2722 N N . VAL A 379 ? 0.2927 0.2506 0.1850 0.0770 -0.0004 0.0058 372 VAL A N 2723 C CA . VAL A 379 ? 0.2895 0.2491 0.1876 0.0754 -0.0066 0.0024 372 VAL A CA 2724 C C . VAL A 379 ? 0.2873 0.2486 0.1936 0.0717 -0.0024 0.0054 372 VAL A C 2725 O O . VAL A 379 ? 0.2920 0.2492 0.1933 0.0744 0.0022 0.0098 372 VAL A O 2726 C CB . VAL A 379 ? 0.3109 0.2647 0.1976 0.0826 -0.0124 0.0011 372 VAL A CB 2727 C CG1 . VAL A 379 ? 0.3171 0.2732 0.2118 0.0810 -0.0186 -0.0021 372 VAL A CG1 2728 C CG2 . VAL A 379 ? 0.3161 0.2681 0.1953 0.0862 -0.0173 -0.0027 372 VAL A CG2 2729 N N . ILE A 380 ? 0.2664 0.2334 0.1850 0.0656 -0.0037 0.0029 373 ILE A N 2730 C CA . ILE A 380 ? 0.2602 0.2291 0.1873 0.0614 0.0006 0.0051 373 ILE A CA 2731 C C . ILE A 380 ? 0.2644 0.2342 0.1967 0.0609 -0.0035 0.0029 373 ILE A C 2732 O O . ILE A 380 ? 0.2725 0.2456 0.2097 0.0593 -0.0086 -0.0013 373 ILE A O 2733 C CB . ILE A 380 ? 0.2404 0.2152 0.1774 0.0547 0.0030 0.0042 373 ILE A CB 2734 C CG1 . ILE A 380 ? 0.2722 0.2466 0.2049 0.0555 0.0064 0.0059 373 ILE A CG1 2735 C CG2 . ILE A 380 ? 0.2554 0.2318 0.2009 0.0506 0.0072 0.0059 373 ILE A CG2 2736 C CD1 . ILE A 380 ? 0.3150 0.2950 0.2566 0.0496 0.0074 0.0045 373 ILE A CD1 2737 N N . LEU A 381 ? 0.2573 0.2239 0.1891 0.0625 -0.0009 0.0058 374 LEU A N 2738 C CA . LEU A 381 ? 0.2539 0.2216 0.1923 0.0616 -0.0037 0.0040 374 LEU A CA 2739 C C . LEU A 381 ? 0.2550 0.2249 0.2025 0.0565 0.0014 0.0053 374 LEU A C 2740 O O . LEU A 381 ? 0.2692 0.2356 0.2150 0.0571 0.0065 0.0095 374 LEU A O 2741 C CB . LEU A 381 ? 0.2754 0.2367 0.2055 0.0683 -0.0058 0.0060 374 LEU A CB 2742 C CG . LEU A 381 ? 0.2774 0.2393 0.2148 0.0680 -0.0080 0.0048 374 LEU A CG 2743 C CD1 . LEU A 381 ? 0.2952 0.2623 0.2397 0.0665 -0.0145 -0.0008 374 LEU A CD1 2744 C CD2 . LEU A 381 ? 0.2978 0.2522 0.2252 0.0752 -0.0093 0.0079 374 LEU A CD2 2745 N N . GLY A 382 ? 0.2452 0.2207 0.2026 0.0514 0.0002 0.0018 375 GLY A N 2746 C CA . GLY A 382 ? 0.2438 0.2212 0.2091 0.0466 0.0046 0.0024 375 GLY A CA 2747 C C . GLY A 382 ? 0.2440 0.2244 0.2178 0.0442 0.0028 -0.0008 375 GLY A C 2748 O O . GLY A 382 ? 0.2603 0.2438 0.2367 0.0439 -0.0013 -0.0042 375 GLY A O 2749 N N . GLY A 383 ? 0.2442 0.2238 0.2231 0.0421 0.0062 0.0000 376 GLY A N 2750 C CA . GLY A 383 ? 0.2461 0.2286 0.2331 0.0396 0.0052 -0.0034 376 GLY A CA 2751 C C . GLY A 383 ? 0.2416 0.2231 0.2336 0.0365 0.0096 -0.0025 376 GLY A C 2752 O O . GLY A 383 ? 0.2519 0.2297 0.2416 0.0372 0.0128 0.0011 376 GLY A O 2753 N N . HIS A 384 ? 0.2324 0.2170 0.2314 0.0332 0.0098 -0.0059 377 HIS A N 2754 C CA . HIS A 384 ? 0.2210 0.2045 0.2246 0.0301 0.0134 -0.0058 377 HIS A CA 2755 C C . HIS A 384 ? 0.2361 0.2149 0.2425 0.0321 0.0147 -0.0047 377 HIS A C 2756 O O . HIS A 384 ? 0.2563 0.2333 0.2617 0.0360 0.0125 -0.0046 377 HIS A O 2757 C CB . HIS A 384 ? 0.2168 0.2053 0.2251 0.0254 0.0135 -0.0099 377 HIS A CB 2758 C CG . HIS A 384 ? 0.2218 0.2123 0.2346 0.0254 0.0124 -0.0136 377 HIS A CG 2759 N ND1 . HIS A 384 ? 0.2229 0.2125 0.2407 0.0239 0.0142 -0.0157 377 HIS A ND1 2760 C CD2 . HIS A 384 ? 0.2084 0.2025 0.2223 0.0260 0.0100 -0.0158 377 HIS A CD2 2761 C CE1 . HIS A 384 ? 0.2228 0.2152 0.2440 0.0240 0.0133 -0.0190 377 HIS A CE1 2762 N NE2 . HIS A 384 ? 0.2234 0.2188 0.2429 0.0253 0.0109 -0.0190 377 HIS A NE2 2763 N N . ARG A 385 ? 0.2191 0.1960 0.2298 0.0295 0.0179 -0.0042 378 ARG A N 2764 C CA . ARG A 385 ? 0.2353 0.2067 0.2490 0.0311 0.0198 -0.0025 378 ARG A CA 2765 C C . ARG A 385 ? 0.2341 0.2065 0.2553 0.0278 0.0206 -0.0066 378 ARG A C 2766 O O . ARG A 385 ? 0.2391 0.2080 0.2639 0.0293 0.0210 -0.0071 378 ARG A O 2767 C CB . ARG A 385 ? 0.2456 0.2128 0.2583 0.0312 0.0234 0.0023 378 ARG A CB 2768 C CG . ARG A 385 ? 0.2714 0.2317 0.2876 0.0326 0.0262 0.0051 378 ARG A CG 2769 C CD . ARG A 385 ? 0.2597 0.2167 0.2770 0.0316 0.0306 0.0097 378 ARG A CD 2770 N NE . ARG A 385 ? 0.2635 0.2240 0.2881 0.0261 0.0318 0.0071 378 ARG A NE 2771 C CZ . ARG A 385 ? 0.2489 0.2137 0.2727 0.0238 0.0320 0.0071 378 ARG A CZ 2772 N NH1 . ARG A 385 ? 0.2400 0.2060 0.2560 0.0264 0.0318 0.0096 378 ARG A NH1 2773 N NH2 . ARG A 385 ? 0.2597 0.2273 0.2907 0.0192 0.0324 0.0044 378 ARG A NH2 2774 N N . ASP A 386 ? 0.2353 0.2120 0.2584 0.0235 0.0207 -0.0097 379 ASP A N 2775 C CA . ASP A 386 ? 0.2283 0.2057 0.2572 0.0205 0.0212 -0.0141 379 ASP A CA 2776 C C . ASP A 386 ? 0.2235 0.2033 0.2533 0.0218 0.0196 -0.0178 379 ASP A C 2777 O O . ASP A 386 ? 0.2252 0.2087 0.2521 0.0229 0.0178 -0.0181 379 ASP A O 2778 C CB . ASP A 386 ? 0.2180 0.1992 0.2470 0.0163 0.0210 -0.0164 379 ASP A CB 2779 C CG . ASP A 386 ? 0.2227 0.2093 0.2471 0.0158 0.0191 -0.0178 379 ASP A CG 2780 O OD1 . ASP A 386 ? 0.2197 0.2072 0.2398 0.0177 0.0182 -0.0149 379 ASP A OD1 2781 O OD2 . ASP A 386 ? 0.2248 0.2145 0.2496 0.0135 0.0186 -0.0218 379 ASP A OD2 2782 N N . SER A 387 ? 0.2283 0.2062 0.2631 0.0214 0.0205 -0.0209 380 SER A N 2783 C CA . SER A 387 ? 0.2397 0.2198 0.2766 0.0227 0.0198 -0.0245 380 SER A CA 2784 C C . SER A 387 ? 0.2509 0.2320 0.2907 0.0199 0.0209 -0.0296 380 SER A C 2785 O O . SER A 387 ? 0.2481 0.2268 0.2892 0.0174 0.0217 -0.0304 380 SER A O 2786 C CB . SER A 387 ? 0.2475 0.2232 0.2872 0.0269 0.0195 -0.0228 380 SER A CB 2787 O OG . SER A 387 ? 0.2601 0.2298 0.3036 0.0266 0.0213 -0.0225 380 SER A OG 2788 N N . TRP A 388 ? 0.2500 0.2346 0.2910 0.0204 0.0211 -0.0333 381 TRP A N 2789 C CA . TRP A 388 ? 0.2366 0.2212 0.2792 0.0186 0.0225 -0.0384 381 TRP A CA 2790 C C . TRP A 388 ? 0.2592 0.2383 0.3072 0.0200 0.0233 -0.0399 381 TRP A C 2791 O O . TRP A 388 ? 0.2570 0.2332 0.3062 0.0181 0.0238 -0.0424 381 TRP A O 2792 C CB . TRP A 388 ? 0.2386 0.2284 0.2808 0.0187 0.0234 -0.0418 381 TRP A CB 2793 C CG . TRP A 388 ? 0.2379 0.2321 0.2745 0.0159 0.0232 -0.0416 381 TRP A CG 2794 C CD1 . TRP A 388 ? 0.2304 0.2291 0.2653 0.0160 0.0227 -0.0399 381 TRP A CD1 2795 C CD2 . TRP A 388 ? 0.2285 0.2223 0.2609 0.0129 0.0232 -0.0431 381 TRP A CD2 2796 N NE1 . TRP A 388 ? 0.2210 0.2219 0.2505 0.0132 0.0226 -0.0400 381 TRP A NE1 2797 C CE2 . TRP A 388 ? 0.2324 0.2304 0.2599 0.0113 0.0228 -0.0419 381 TRP A CE2 2798 C CE3 . TRP A 388 ? 0.2399 0.2299 0.2726 0.0113 0.0230 -0.0455 381 TRP A CE3 2799 C CZ2 . TRP A 388 ? 0.2340 0.2326 0.2564 0.0086 0.0221 -0.0427 381 TRP A CZ2 2800 C CZ3 . TRP A 388 ? 0.2325 0.2235 0.2606 0.0085 0.0219 -0.0467 381 TRP A CZ3 2801 C CH2 . TRP A 388 ? 0.2378 0.2330 0.2605 0.0073 0.0215 -0.0451 381 TRP A CH2 2802 N N . VAL A 389 ? 0.2564 0.2337 0.3078 0.0237 0.0231 -0.0384 382 VAL A N 2803 C CA . VAL A 389 ? 0.2539 0.2250 0.3105 0.0255 0.0237 -0.0388 382 VAL A CA 2804 C C . VAL A 389 ? 0.2628 0.2301 0.3194 0.0288 0.0227 -0.0330 382 VAL A C 2805 O O . VAL A 389 ? 0.2551 0.2201 0.3089 0.0279 0.0227 -0.0288 382 VAL A O 2806 C CB . VAL A 389 ? 0.2515 0.2230 0.3126 0.0273 0.0248 -0.0440 382 VAL A CB 2807 C CG1 . VAL A 389 ? 0.2660 0.2301 0.3325 0.0285 0.0255 -0.0448 382 VAL A CG1 2808 C CG2 . VAL A 389 ? 0.2677 0.2432 0.3265 0.0245 0.0262 -0.0494 382 VAL A CG2 2809 N N . PHE A 390 ? 0.2603 0.2270 0.3197 0.0329 0.0218 -0.0327 383 PHE A N 2810 C CA . PHE A 390 ? 0.2554 0.2174 0.3136 0.0367 0.0204 -0.0272 383 PHE A CA 2811 C C . PHE A 390 ? 0.2663 0.2317 0.3187 0.0382 0.0182 -0.0238 383 PHE A C 2812 O O . PHE A 390 ? 0.2812 0.2424 0.3296 0.0406 0.0174 -0.0186 383 PHE A O 2813 C CB . PHE A 390 ? 0.2587 0.2177 0.3223 0.0412 0.0197 -0.0281 383 PHE A CB 2814 C CG . PHE A 390 ? 0.2703 0.2246 0.3395 0.0403 0.0218 -0.0313 383 PHE A CG 2815 C CD1 . PHE A 390 ? 0.2854 0.2321 0.3555 0.0395 0.0232 -0.0284 383 PHE A CD1 2816 C CD2 . PHE A 390 ? 0.2932 0.2507 0.3670 0.0400 0.0226 -0.0375 383 PHE A CD2 2817 C CE1 . PHE A 390 ? 0.3078 0.2498 0.3839 0.0384 0.0248 -0.0320 383 PHE A CE1 2818 C CE2 . PHE A 390 ? 0.2856 0.2383 0.3642 0.0393 0.0244 -0.0411 383 PHE A CE2 2819 C CZ . PHE A 390 ? 0.3003 0.2454 0.3802 0.0384 0.0251 -0.0385 383 PHE A CZ 2820 N N . GLY A 391 ? 0.2573 0.2299 0.3088 0.0366 0.0173 -0.0265 384 GLY A N 2821 C CA . GLY A 391 ? 0.2498 0.2255 0.2960 0.0375 0.0149 -0.0237 384 GLY A CA 2822 C C . GLY A 391 ? 0.2545 0.2290 0.3006 0.0428 0.0115 -0.0216 384 GLY A C 2823 O O . GLY A 391 ? 0.2610 0.2348 0.3009 0.0446 0.0094 -0.0181 384 GLY A O 2824 N N . GLY A 392 ? 0.2660 0.2404 0.3186 0.0456 0.0108 -0.0239 385 GLY A N 2825 C CA . GLY A 392 ? 0.2577 0.2306 0.3111 0.0512 0.0069 -0.0223 385 GLY A CA 2826 C C . GLY A 392 ? 0.2646 0.2426 0.3154 0.0522 0.0031 -0.0221 385 GLY A C 2827 O O . GLY A 392 ? 0.2780 0.2530 0.3237 0.0563 -0.0005 -0.0189 385 GLY A O 2828 N N . ILE A 393 ? 0.2532 0.2384 0.3072 0.0486 0.0038 -0.0256 386 ILE A N 2829 C CA . ILE A 393 ? 0.2468 0.2363 0.2984 0.0489 0.0004 -0.0253 386 ILE A CA 2830 C C . ILE A 393 ? 0.2561 0.2458 0.3002 0.0449 0.0022 -0.0236 386 ILE A C 2831 O O . ILE A 393 ? 0.2480 0.2355 0.2849 0.0465 0.0000 -0.0204 386 ILE A O 2832 C CB . ILE A 393 ? 0.2385 0.2358 0.2995 0.0479 -0.0004 -0.0298 386 ILE A CB 2833 C CG1 . ILE A 393 ? 0.2550 0.2525 0.3238 0.0529 -0.0037 -0.0311 386 ILE A CG1 2834 C CG2 . ILE A 393 ? 0.2319 0.2337 0.2908 0.0465 -0.0030 -0.0297 386 ILE A CG2 2835 C CD1 . ILE A 393 ? 0.2823 0.2876 0.3627 0.0519 -0.0033 -0.0355 386 ILE A CD1 2836 N N . ASP A 394 ? 0.2496 0.2417 0.2952 0.0402 0.0061 -0.0257 387 ASP A N 2837 C CA . ASP A 394 ? 0.2358 0.2293 0.2757 0.0363 0.0075 -0.0248 387 ASP A CA 2838 C C . ASP A 394 ? 0.2396 0.2281 0.2760 0.0346 0.0104 -0.0228 387 ASP A C 2839 O O . ASP A 394 ? 0.2494 0.2376 0.2891 0.0323 0.0132 -0.0253 387 ASP A O 2840 C CB . ASP A 394 ? 0.2347 0.2343 0.2787 0.0325 0.0096 -0.0286 387 ASP A CB 2841 C CG . ASP A 394 ? 0.2524 0.2536 0.2910 0.0286 0.0108 -0.0280 387 ASP A CG 2842 O OD1 . ASP A 394 ? 0.2283 0.2267 0.2609 0.0289 0.0098 -0.0248 387 ASP A OD1 2843 O OD2 . ASP A 394 ? 0.2522 0.2573 0.2925 0.0256 0.0129 -0.0306 387 ASP A OD2 2844 N N . PRO A 395 ? 0.2398 0.2244 0.2698 0.0357 0.0100 -0.0186 388 PRO A N 2845 C CA . PRO A 395 ? 0.2363 0.2206 0.2602 0.0383 0.0070 -0.0158 388 PRO A CA 2846 C C . PRO A 395 ? 0.2495 0.2277 0.2700 0.0436 0.0055 -0.0121 388 PRO A C 2847 O O . PRO A 395 ? 0.2508 0.2275 0.2644 0.0464 0.0032 -0.0095 388 PRO A O 2848 C CB . PRO A 395 ? 0.2426 0.2262 0.2613 0.0354 0.0092 -0.0135 388 PRO A CB 2849 C CG . PRO A 395 ? 0.2390 0.2182 0.2601 0.0340 0.0127 -0.0125 388 PRO A CG 2850 C CD . PRO A 395 ? 0.2420 0.2228 0.2703 0.0332 0.0132 -0.0167 388 PRO A CD 2851 N N . GLN A 396 ? 0.2534 0.2274 0.2774 0.0452 0.0068 -0.0117 389 GLN A N 2852 C CA . GLN A 396 ? 0.2668 0.2335 0.2854 0.0499 0.0064 -0.0069 389 GLN A CA 2853 C C . GLN A 396 ? 0.2702 0.2362 0.2854 0.0556 0.0012 -0.0062 389 GLN A C 2854 O O . GLN A 396 ? 0.2797 0.2400 0.2869 0.0598 0.0003 -0.0019 389 GLN A O 2855 C CB . GLN A 396 ? 0.2719 0.2331 0.2950 0.0504 0.0091 -0.0060 389 GLN A CB 2856 C CG . GLN A 396 ? 0.2519 0.2128 0.2789 0.0451 0.0136 -0.0069 389 GLN A CG 2857 C CD . GLN A 396 ? 0.2596 0.2199 0.2814 0.0426 0.0160 -0.0037 389 GLN A CD 2858 O OE1 . GLN A 396 ? 0.2823 0.2410 0.2966 0.0451 0.0153 0.0001 389 GLN A OE1 2859 N NE2 . GLN A 396 ? 0.2641 0.2254 0.2902 0.0378 0.0189 -0.0053 389 GLN A NE2 2860 N N . SER A 397 ? 0.2649 0.2367 0.2861 0.0558 -0.0022 -0.0105 390 SER A N 2861 C CA . SER A 397 ? 0.2795 0.2514 0.2982 0.0610 -0.0081 -0.0105 390 SER A CA 2862 C C . SER A 397 ? 0.2813 0.2532 0.2908 0.0616 -0.0101 -0.0088 390 SER A C 2863 O O . SER A 397 ? 0.2906 0.2590 0.2930 0.0670 -0.0144 -0.0070 390 SER A O 2864 C CB . SER A 397 ? 0.2688 0.2476 0.2982 0.0608 -0.0112 -0.0157 390 SER A CB 2865 O OG . SER A 397 ? 0.2718 0.2573 0.3041 0.0560 -0.0104 -0.0185 390 SER A OG 2866 N N . GLY A 398 ? 0.2686 0.2440 0.2776 0.0565 -0.0071 -0.0094 391 GLY A N 2867 C CA . GLY A 398 ? 0.2543 0.2295 0.2548 0.0567 -0.0080 -0.0078 391 GLY A CA 2868 C C . GLY A 398 ? 0.2599 0.2282 0.2512 0.0584 -0.0046 -0.0024 391 GLY A C 2869 O O . GLY A 398 ? 0.2827 0.2474 0.2644 0.0625 -0.0065 0.0001 391 GLY A O 2870 N N . ALA A 399 ? 0.2554 0.2219 0.2498 0.0553 0.0007 -0.0009 392 ALA A N 2871 C CA . ALA A 399 ? 0.2736 0.2340 0.2614 0.0563 0.0048 0.0044 392 ALA A CA 2872 C C . ALA A 399 ? 0.2889 0.2416 0.2695 0.0628 0.0038 0.0087 392 ALA A C 2873 O O . ALA A 399 ? 0.2815 0.2293 0.2528 0.0654 0.0060 0.0133 392 ALA A O 2874 C CB . ALA A 399 ? 0.2770 0.2369 0.2714 0.0515 0.0101 0.0048 392 ALA A CB 2875 N N . ALA A 400 ? 0.3005 0.2520 0.2851 0.0657 0.0009 0.0073 393 ALA A N 2876 C CA . ALA A 400 ? 0.3041 0.2478 0.2814 0.0726 -0.0009 0.0113 393 ALA A CA 2877 C C . ALA A 400 ? 0.3201 0.2630 0.2868 0.0777 -0.0061 0.0117 393 ALA A C 2878 O O . ALA A 400 ? 0.3240 0.2596 0.2795 0.0832 -0.0061 0.0164 393 ALA A O 2879 C CB . ALA A 400 ? 0.3066 0.2501 0.2920 0.0746 -0.0039 0.0089 393 ALA A CB 2880 N N . VAL A 401 ? 0.3049 0.2549 0.2751 0.0759 -0.0104 0.0068 394 VAL A N 2881 C CA . VAL A 401 ? 0.3037 0.2534 0.2648 0.0802 -0.0159 0.0061 394 VAL A CA 2882 C C . VAL A 401 ? 0.3158 0.2628 0.2663 0.0800 -0.0122 0.0096 394 VAL A C 2883 O O . VAL A 401 ? 0.3129 0.2543 0.2507 0.0859 -0.0139 0.0125 394 VAL A O 2884 C CB . VAL A 401 ? 0.3061 0.2642 0.2758 0.0778 -0.0213 -0.0003 394 VAL A CB 2885 C CG1 . VAL A 401 ? 0.3018 0.2606 0.2634 0.0798 -0.0254 -0.0014 394 VAL A CG1 2886 C CG2 . VAL A 401 ? 0.3061 0.2651 0.2829 0.0813 -0.0268 -0.0030 394 VAL A CG2 2887 N N . VAL A 402 ? 0.2904 0.2414 0.2459 0.0737 -0.0070 0.0093 395 VAL A N 2888 C CA . VAL A 402 ? 0.2989 0.2477 0.2458 0.0736 -0.0030 0.0127 395 VAL A CA 2889 C C . VAL A 402 ? 0.3097 0.2497 0.2478 0.0778 0.0016 0.0193 395 VAL A C 2890 O O . VAL A 402 ? 0.3183 0.2539 0.2445 0.0819 0.0025 0.0225 395 VAL A O 2891 C CB . VAL A 402 ? 0.2879 0.2419 0.2426 0.0662 0.0018 0.0116 395 VAL A CB 2892 C CG1 . VAL A 402 ? 0.3004 0.2520 0.2476 0.0663 0.0067 0.0156 395 VAL A CG1 2893 C CG2 . VAL A 402 ? 0.3060 0.2679 0.2673 0.0625 -0.0022 0.0059 395 VAL A CG2 2894 N N . HIS A 403 ? 0.3178 0.2549 0.2618 0.0769 0.0046 0.0213 396 HIS A N 2895 C CA . HIS A 403 ? 0.3172 0.2456 0.2549 0.0803 0.0097 0.0280 396 HIS A CA 2896 C C . HIS A 403 ? 0.3494 0.2709 0.2728 0.0889 0.0059 0.0309 396 HIS A C 2897 O O . HIS A 403 ? 0.3664 0.2816 0.2779 0.0928 0.0097 0.0363 396 HIS A O 2898 C CB . HIS A 403 ? 0.3321 0.2589 0.2804 0.0779 0.0122 0.0285 396 HIS A CB 2899 C CG . HIS A 403 ? 0.3298 0.2508 0.2789 0.0765 0.0200 0.0343 396 HIS A CG 2900 N ND1 . HIS A 403 ? 0.3565 0.2798 0.3079 0.0720 0.0256 0.0357 396 HIS A ND1 2901 C CD2 . HIS A 403 ? 0.3740 0.2876 0.3240 0.0785 0.0233 0.0388 396 HIS A CD2 2902 C CE1 . HIS A 403 ? 0.3748 0.2924 0.3286 0.0713 0.0319 0.0409 396 HIS A CE1 2903 N NE2 . HIS A 403 ? 0.3644 0.2758 0.3176 0.0751 0.0308 0.0429 396 HIS A NE2 2904 N N . GLU A 404 ? 0.3449 0.2677 0.2691 0.0921 -0.0016 0.0272 397 GLU A N 2905 C CA . GLU A 404 ? 0.3626 0.2789 0.2732 0.1007 -0.0069 0.0290 397 GLU A CA 2906 C C . GLU A 404 ? 0.3642 0.2808 0.2629 0.1036 -0.0094 0.0281 397 GLU A C 2907 O O . GLU A 404 ? 0.3906 0.2997 0.2738 0.1105 -0.0100 0.0319 397 GLU A O 2908 C CB . GLU A 404 ? 0.3768 0.2954 0.2939 0.1031 -0.0149 0.0244 397 GLU A CB 2909 C CG . GLU A 404 ? 0.3736 0.2859 0.2777 0.1124 -0.0222 0.0254 397 GLU A CG 2910 C CD . GLU A 404 ? 0.4453 0.3464 0.3372 0.1185 -0.0185 0.0331 397 GLU A CD 2911 O OE1 . GLU A 404 ? 0.4410 0.3387 0.3343 0.1155 -0.0098 0.0381 397 GLU A OE1 2912 O OE2 . GLU A 404 ? 0.4658 0.3609 0.3467 0.1266 -0.0247 0.0341 397 GLU A OE2 2913 N N . ILE A 405 ? 0.3463 0.2711 0.2516 0.0985 -0.0110 0.0230 398 ILE A N 2914 C CA . ILE A 405 ? 0.3534 0.2784 0.2485 0.1005 -0.0128 0.0219 398 ILE A CA 2915 C C . ILE A 405 ? 0.3640 0.2840 0.2494 0.1014 -0.0046 0.0280 398 ILE A C 2916 O O . ILE A 405 ? 0.3846 0.2990 0.2546 0.1076 -0.0052 0.0302 398 ILE A O 2917 C CB . ILE A 405 ? 0.3299 0.2645 0.2357 0.0943 -0.0154 0.0157 398 ILE A CB 2918 C CG1 . ILE A 405 ? 0.3212 0.2599 0.2338 0.0953 -0.0244 0.0098 398 ILE A CG1 2919 C CG2 . ILE A 405 ? 0.3425 0.2773 0.2392 0.0950 -0.0147 0.0155 398 ILE A CG2 2920 C CD1 . ILE A 405 ? 0.2991 0.2475 0.2260 0.0879 -0.0255 0.0043 398 ILE A CD1 2921 N N . VAL A 406 ? 0.3623 0.2840 0.2565 0.0956 0.0032 0.0306 399 VAL A N 2922 C CA . VAL A 406 ? 0.3726 0.2897 0.2600 0.0961 0.0118 0.0368 399 VAL A CA 2923 C C . VAL A 406 ? 0.3882 0.2949 0.2621 0.1038 0.0139 0.0432 399 VAL A C 2924 O O . VAL A 406 ? 0.4191 0.3204 0.2789 0.1086 0.0172 0.0472 399 VAL A O 2925 C CB . VAL A 406 ? 0.3563 0.2767 0.2574 0.0886 0.0192 0.0385 399 VAL A CB 2926 C CG1 . VAL A 406 ? 0.3751 0.2905 0.2708 0.0895 0.0285 0.0454 399 VAL A CG1 2927 C CG2 . VAL A 406 ? 0.3463 0.2767 0.2593 0.0812 0.0175 0.0325 399 VAL A CG2 2928 N N . ARG A 407 ? 0.3937 0.2970 0.2712 0.1052 0.0122 0.0443 400 ARG A N 2929 C CA . ARG A 407 ? 0.4199 0.3126 0.2846 0.1126 0.0139 0.0508 400 ARG A CA 2930 C C . ARG A 407 ? 0.4412 0.3292 0.2874 0.1212 0.0081 0.0505 400 ARG A C 2931 O O . ARG A 407 ? 0.4675 0.3468 0.2979 0.1274 0.0124 0.0567 400 ARG A O 2932 C CB . ARG A 407 ? 0.4177 0.3080 0.2898 0.1132 0.0111 0.0509 400 ARG A CB 2933 C CG . ARG A 407 ? 0.4450 0.3236 0.3065 0.1195 0.0156 0.0592 400 ARG A CG 2934 C CD . ARG A 407 ? 0.4628 0.3382 0.3288 0.1223 0.0103 0.0586 400 ARG A CD 2935 N NE . ARG A 407 ? 0.4594 0.3372 0.3210 0.1269 -0.0007 0.0529 400 ARG A NE 2936 C CZ . ARG A 407 ? 0.5113 0.3828 0.3551 0.1357 -0.0057 0.0545 400 ARG A CZ 2937 N NH1 . ARG A 407 ? 0.4827 0.3574 0.3253 0.1391 -0.0163 0.0484 400 ARG A NH1 2938 N NH2 . ARG A 407 ? 0.5218 0.3835 0.3490 0.1412 0.0000 0.0620 400 ARG A NH2 2939 N N . SER A 408 ? 0.4444 0.3375 0.2922 0.1219 -0.0016 0.0434 401 SER A N 2940 C CA . SER A 408 ? 0.4634 0.3524 0.2947 0.1301 -0.0088 0.0418 401 SER A CA 2941 C C . SER A 408 ? 0.4671 0.3551 0.2867 0.1315 -0.0053 0.0427 401 SER A C 2942 O O . SER A 408 ? 0.4770 0.3565 0.2777 0.1395 -0.0045 0.0466 401 SER A O 2943 C CB . SER A 408 ? 0.4670 0.3620 0.3053 0.1301 -0.0203 0.0337 401 SER A CB 2944 O OG . SER A 408 ? 0.5143 0.4049 0.3364 0.1381 -0.0278 0.0317 401 SER A OG 2945 N N . PHE A 409 ? 0.4426 0.3388 0.2726 0.1244 -0.0028 0.0393 402 PHE A N 2946 C CA . PHE A 409 ? 0.4558 0.3511 0.2758 0.1257 0.0014 0.0405 402 PHE A CA 2947 C C . PHE A 409 ? 0.4767 0.3643 0.2869 0.1287 0.0119 0.0491 402 PHE A C 2948 O O . PHE A 409 ? 0.5022 0.3843 0.2959 0.1347 0.0144 0.0518 402 PHE A O 2949 C CB . PHE A 409 ? 0.4279 0.3329 0.2622 0.1171 0.0034 0.0364 402 PHE A CB 2950 C CG . PHE A 409 ? 0.4250 0.3364 0.2637 0.1157 -0.0058 0.0284 402 PHE A CG 2951 C CD1 . PHE A 409 ? 0.4377 0.3462 0.2627 0.1216 -0.0111 0.0257 402 PHE A CD1 2952 C CD2 . PHE A 409 ? 0.3963 0.3162 0.2528 0.1082 -0.0086 0.0237 402 PHE A CD2 2953 C CE1 . PHE A 409 ? 0.4069 0.3211 0.2373 0.1198 -0.0194 0.0183 402 PHE A CE1 2954 C CE2 . PHE A 409 ? 0.3895 0.3153 0.2511 0.1064 -0.0163 0.0167 402 PHE A CE2 2955 C CZ . PHE A 409 ? 0.4057 0.3286 0.2550 0.1120 -0.0218 0.0140 402 PHE A CZ 2956 N N . GLY A 410 ? 0.4730 0.3601 0.2936 0.1246 0.0185 0.0536 403 GLY A N 2957 C CA . GLY A 410 ? 0.4858 0.3659 0.3004 0.1264 0.0292 0.0622 403 GLY A CA 2958 C C . GLY A 410 ? 0.5200 0.3883 0.3146 0.1364 0.0291 0.0678 403 GLY A C 2959 O O . GLY A 410 ? 0.5518 0.4133 0.3341 0.1406 0.0372 0.0745 403 GLY A O 2960 N N . THR A 411 ? 0.5333 0.3990 0.3243 0.1406 0.0200 0.0653 404 THR A N 2961 C CA . THR A 411 ? 0.5528 0.4071 0.3234 0.1511 0.0180 0.0699 404 THR A CA 2962 C C . THR A 411 ? 0.5745 0.4252 0.3249 0.1582 0.0159 0.0689 404 THR A C 2963 O O . THR A 411 ? 0.6038 0.4445 0.3352 0.1657 0.0210 0.0755 404 THR A O 2964 C CB . THR A 411 ? 0.5572 0.4103 0.3291 0.1544 0.0069 0.0663 404 THR A CB 2965 O OG1 A THR A 411 ? 0.5474 0.4030 0.3371 0.1485 0.0094 0.0674 404 THR A OG1 2966 O OG1 B THR A 411 ? 0.5609 0.4196 0.3320 0.1557 -0.0042 0.0577 404 THR A OG1 2967 C CG2 A THR A 411 ? 0.5655 0.4066 0.3150 0.1658 0.0037 0.0707 404 THR A CG2 2968 C CG2 B THR A 411 ? 0.5412 0.3990 0.3343 0.1472 0.0079 0.0657 404 THR A CG2 2969 N N . LEU A 412 ? 0.5561 0.4143 0.3101 0.1560 0.0088 0.0608 405 LEU A N 2970 C CA . LEU A 412 ? 0.5704 0.4256 0.3065 0.1624 0.0062 0.0586 405 LEU A CA 2971 C C . LEU A 412 ? 0.5791 0.4328 0.3102 0.1616 0.0185 0.0641 405 LEU A C 2972 O O . LEU A 412 ? 0.5933 0.4387 0.3037 0.1696 0.0217 0.0678 405 LEU A O 2973 C CB . LEU A 412 ? 0.5720 0.4360 0.3159 0.1592 -0.0039 0.0486 405 LEU A CB 2974 C CG A LEU A 412 ? 0.5615 0.4282 0.3113 0.1602 -0.0169 0.0419 405 LEU A CG 2975 C CG B LEU A 412 ? 0.5619 0.4255 0.3031 0.1637 -0.0180 0.0421 405 LEU A CG 2976 C CD1 A LEU A 412 ? 0.5431 0.4195 0.3047 0.1549 -0.0239 0.0330 405 LEU A CD1 2977 C CD1 B LEU A 412 ? 0.5344 0.3996 0.2886 0.1614 -0.0214 0.0423 405 LEU A CD1 2978 C CD2 A LEU A 412 ? 0.5924 0.4492 0.3209 0.1715 -0.0244 0.0424 405 LEU A CD2 2979 C CD2 B LEU A 412 ? 0.5609 0.4332 0.3112 0.1597 -0.0256 0.0330 405 LEU A CD2 2980 N N . LYS A 413 ? 0.5589 0.4204 0.3089 0.1521 0.0254 0.0644 406 LYS A N 2981 C CA . LYS A 413 ? 0.5741 0.4356 0.3235 0.1504 0.0372 0.0694 406 LYS A CA 2982 C C . LYS A 413 ? 0.5989 0.4496 0.3351 0.1562 0.0472 0.0796 406 LYS A C 2983 O O . LYS A 413 ? 0.6091 0.4554 0.3321 0.1607 0.0545 0.0836 406 LYS A O 2984 C CB . LYS A 413 ? 0.5625 0.4342 0.3363 0.1391 0.0418 0.0680 406 LYS A CB 2985 C CG . LYS A 413 ? 0.6027 0.4770 0.3790 0.1365 0.0521 0.0710 406 LYS A CG 2986 C CD . LYS A 413 ? 0.6811 0.5523 0.4642 0.1340 0.0640 0.0795 406 LYS A CD 2987 C CE . LYS A 413 ? 0.6893 0.5675 0.4849 0.1278 0.0723 0.0801 406 LYS A CE 2988 N NZ . LYS A 413 ? 0.7225 0.6001 0.5315 0.1230 0.0825 0.0868 406 LYS A NZ 2989 N N . LYS A 414 ? 0.5978 0.4442 0.3378 0.1562 0.0478 0.0838 407 LYS A N 2990 C CA . LYS A 414 ? 0.6305 0.4657 0.3583 0.1618 0.0573 0.0941 407 LYS A CA 2991 C C . LYS A 414 ? 0.6625 0.4867 0.3617 0.1739 0.0551 0.0966 407 LYS A C 2992 O O . LYS A 414 ? 0.6869 0.5019 0.3720 0.1795 0.0649 0.1054 407 LYS A O 2993 C CB . LYS A 414 ? 0.6259 0.4585 0.3646 0.1592 0.0576 0.0976 407 LYS A CB 2994 C CG . LYS A 414 ? 0.6325 0.4734 0.3970 0.1480 0.0636 0.0975 407 LYS A CG 2995 C CD . LYS A 414 ? 0.6443 0.4834 0.4211 0.1449 0.0626 0.0993 407 LYS A CD 2996 C CE . LYS A 414 ? 0.6296 0.4763 0.4306 0.1342 0.0691 0.0992 407 LYS A CE 2997 N NZ . LYS A 414 ? 0.6761 0.5193 0.4881 0.1317 0.0699 0.1020 407 LYS A NZ 2998 N N . GLU A 415 ? 0.6642 0.4894 0.3550 0.1782 0.0423 0.0890 408 GLU A N 2999 C CA . GLU A 415 ? 0.6981 0.5135 0.3610 0.1900 0.0379 0.0895 408 GLU A CA 3000 C C . GLU A 415 ? 0.6952 0.5118 0.3470 0.1927 0.0399 0.0866 408 GLU A C 3001 O O . GLU A 415 ? 0.7201 0.5288 0.3479 0.2027 0.0359 0.0859 408 GLU A O 3002 C CB . GLU A 415 ? 0.7074 0.5225 0.3669 0.1940 0.0222 0.0826 408 GLU A CB 3003 C CG . GLU A 415 ? 0.7556 0.5682 0.4235 0.1931 0.0195 0.0854 408 GLU A CG 3004 C CD . GLU A 415 ? 0.8220 0.6344 0.4867 0.1977 0.0039 0.0786 408 GLU A CD 3005 O OE1 . GLU A 415 ? 0.8677 0.6745 0.5309 0.2011 0.0010 0.0819 408 GLU A OE1 3006 O OE2 . GLU A 415 ? 0.8454 0.6633 0.5099 0.1980 -0.0055 0.0699 408 GLU A OE2 3007 N N . GLY A 416 ? 0.6631 0.4891 0.3314 0.1843 0.0458 0.0848 409 GLY A N 3008 C CA . GLY A 416 ? 0.6613 0.4887 0.3211 0.1863 0.0495 0.0828 409 GLY A CA 3009 C C . GLY A 416 ? 0.6362 0.4730 0.3049 0.1822 0.0396 0.0721 409 GLY A C 3010 O O . GLY A 416 ? 0.6421 0.4801 0.3041 0.1840 0.0414 0.0695 409 GLY A O 3011 N N . TRP A 417 ? 0.6090 0.4521 0.2925 0.1771 0.0293 0.0660 410 TRP A N 3012 C CA . TRP A 417 ? 0.5888 0.4404 0.2814 0.1732 0.0195 0.0561 410 TRP A CA 3013 C C . TRP A 417 ? 0.5518 0.4143 0.2673 0.1623 0.0252 0.0548 410 TRP A C 3014 O O . TRP A 417 ? 0.5475 0.4128 0.2773 0.1561 0.0323 0.0595 410 TRP A O 3015 C CB . TRP A 417 ? 0.5865 0.4403 0.2859 0.1725 0.0066 0.0503 410 TRP A CB 3016 C CG . TRP A 417 ? 0.5851 0.4485 0.2983 0.1670 -0.0033 0.0404 410 TRP A CG 3017 C CD1 . TRP A 417 ? 0.6068 0.4696 0.3110 0.1715 -0.0130 0.0332 410 TRP A CD1 3018 C CD2 . TRP A 417 ? 0.5683 0.4426 0.3065 0.1563 -0.0042 0.0369 410 TRP A CD2 3019 N NE1 . TRP A 417 ? 0.5697 0.4424 0.2926 0.1639 -0.0195 0.0258 410 TRP A NE1 3020 C CE2 . TRP A 417 ? 0.5574 0.4372 0.3006 0.1547 -0.0141 0.0281 410 TRP A CE2 3021 C CE3 . TRP A 417 ? 0.5489 0.4286 0.3053 0.1480 0.0024 0.0403 410 TRP A CE3 3022 C CZ2 . TRP A 417 ? 0.5128 0.4031 0.2779 0.1453 -0.0170 0.0232 410 TRP A CZ2 3023 C CZ3 . TRP A 417 ? 0.5160 0.4058 0.2930 0.1391 -0.0009 0.0350 410 TRP A CZ3 3024 C CH2 . TRP A 417 ? 0.5009 0.3959 0.2817 0.1379 -0.0102 0.0268 410 TRP A CH2 3025 N N . ARG A 418 ? 0.5338 0.4020 0.2527 0.1600 0.0216 0.0484 411 ARG A N 3026 C CA . ARG A 418 ? 0.5040 0.3834 0.2457 0.1495 0.0234 0.0454 411 ARG A CA 3027 C C . ARG A 418 ? 0.4811 0.3660 0.2280 0.1475 0.0119 0.0360 411 ARG A C 3028 O O . ARG A 418 ? 0.4981 0.3787 0.2303 0.1542 0.0053 0.0320 411 ARG A O 3029 C CB . ARG A 418 ? 0.5173 0.3984 0.2597 0.1480 0.0341 0.0486 411 ARG A CB 3030 C CG . ARG A 418 ? 0.5415 0.4208 0.2884 0.1460 0.0467 0.0574 411 ARG A CG 3031 C CD . ARG A 418 ? 0.5429 0.4258 0.2943 0.1437 0.0568 0.0598 411 ARG A CD 3032 N NE . ARG A 418 ? 0.5313 0.4127 0.2894 0.1414 0.0683 0.0681 411 ARG A NE 3033 C CZ . ARG A 418 ? 0.5198 0.4072 0.2987 0.1327 0.0705 0.0692 411 ARG A CZ 3034 N NH1 . ARG A 418 ? 0.4567 0.3527 0.2516 0.1254 0.0628 0.0626 411 ARG A NH1 3035 N NH2 . ARG A 418 ? 0.5206 0.4052 0.3043 0.1315 0.0808 0.0770 411 ARG A NH2 3036 N N . PRO A 419 ? 0.4456 0.3399 0.2136 0.1383 0.0095 0.0324 412 PRO A N 3037 C CA . PRO A 419 ? 0.4347 0.3347 0.2092 0.1356 0.0001 0.0241 412 PRO A CA 3038 C C . PRO A 419 ? 0.4219 0.3229 0.1920 0.1363 0.0028 0.0221 412 PRO A C 3039 O O . PRO A 419 ? 0.4387 0.3393 0.2075 0.1360 0.0127 0.0270 412 PRO A O 3040 C CB . PRO A 419 ? 0.4155 0.3248 0.2131 0.1254 0.0000 0.0225 412 PRO A CB 3041 C CG . PRO A 419 ? 0.4092 0.3190 0.2128 0.1218 0.0114 0.0295 412 PRO A CG 3042 C CD . PRO A 419 ? 0.4231 0.3229 0.2092 0.1300 0.0163 0.0360 412 PRO A CD 3043 N N . ARG A 420 ? 0.4278 0.3302 0.1966 0.1373 -0.0061 0.0149 413 ARG A N 3044 C CA . ARG A 420 ? 0.4250 0.3285 0.1908 0.1379 -0.0046 0.0123 413 ARG A CA 3045 C C . ARG A 420 ? 0.4156 0.3275 0.1992 0.1289 0.0023 0.0137 413 ARG A C 3046 O O . ARG A 420 ? 0.4197 0.3316 0.2010 0.1293 0.0105 0.0167 413 ARG A O 3047 C CB . ARG A 420 ? 0.4241 0.3283 0.1893 0.1391 -0.0164 0.0038 413 ARG A CB 3048 C CG . ARG A 420 ? 0.4475 0.3522 0.2097 0.1398 -0.0158 0.0003 413 ARG A CG 3049 C CD . ARG A 420 ? 0.4773 0.3833 0.2427 0.1396 -0.0274 -0.0082 413 ARG A CD 3050 N NE . ARG A 420 ? 0.4951 0.4023 0.2607 0.1390 -0.0259 -0.0110 413 ARG A NE 3051 C CZ . ARG A 420 ? 0.5401 0.4408 0.2888 0.1468 -0.0261 -0.0128 413 ARG A CZ 3052 N NH1 . ARG A 420 ? 0.5211 0.4130 0.2497 0.1561 -0.0281 -0.0121 413 ARG A NH1 3053 N NH2 . ARG A 420 ? 0.5235 0.4259 0.2747 0.1456 -0.0246 -0.0154 413 ARG A NH2 3054 N N . ARG A 421 ? 0.3902 0.3091 0.1914 0.1212 -0.0013 0.0114 414 ARG A N 3055 C CA . ARG A 421 ? 0.3687 0.2957 0.1874 0.1124 0.0037 0.0122 414 ARG A CA 3056 C C . ARG A 421 ? 0.3670 0.2958 0.1947 0.1082 0.0101 0.0176 414 ARG A C 3057 O O . ARG A 421 ? 0.3818 0.3068 0.2058 0.1106 0.0087 0.0196 414 ARG A O 3058 C CB . ARG A 421 ? 0.3604 0.2937 0.1922 0.1066 -0.0044 0.0058 414 ARG A CB 3059 C CG . ARG A 421 ? 0.3553 0.2868 0.1804 0.1101 -0.0117 -0.0002 414 ARG A CG 3060 C CD . ARG A 421 ? 0.3538 0.2915 0.1933 0.1038 -0.0189 -0.0060 414 ARG A CD 3061 N NE . ARG A 421 ? 0.3578 0.2923 0.1894 0.1081 -0.0252 -0.0112 414 ARG A NE 3062 C CZ . ARG A 421 ? 0.3875 0.3171 0.2098 0.1140 -0.0334 -0.0151 414 ARG A CZ 3063 N NH1 . ARG A 421 ? 0.3740 0.3023 0.1957 0.1155 -0.0371 -0.0148 414 ARG A NH1 3064 N NH2 . ARG A 421 ? 0.4042 0.3302 0.2184 0.1183 -0.0384 -0.0199 414 ARG A NH2 3065 N N . THR A 422 ? 0.3452 0.2794 0.1850 0.1021 0.0166 0.0198 415 THR A N 3066 C CA . THR A 422 ? 0.3444 0.2809 0.1952 0.0972 0.0220 0.0240 415 THR A CA 3067 C C . THR A 422 ? 0.3390 0.2796 0.2011 0.0922 0.0157 0.0206 415 THR A C 3068 O O . THR A 422 ? 0.3285 0.2739 0.1977 0.0885 0.0098 0.0154 415 THR A O 3069 C CB . THR A 422 ? 0.3284 0.2705 0.1908 0.0916 0.0293 0.0261 415 THR A CB 3070 O OG1 . THR A 422 ? 0.3530 0.2910 0.2057 0.0966 0.0369 0.0305 415 THR A OG1 3071 C CG2 . THR A 422 ? 0.3202 0.2658 0.1969 0.0852 0.0331 0.0288 415 THR A CG2 3072 N N . ILE A 423 ? 0.3242 0.2623 0.1876 0.0923 0.0173 0.0238 416 ILE A N 3073 C CA . ILE A 423 ? 0.3145 0.2566 0.1899 0.0873 0.0132 0.0213 416 ILE A CA 3074 C C . ILE A 423 ? 0.3105 0.2559 0.1984 0.0812 0.0200 0.0245 416 ILE A C 3075 O O . ILE A 423 ? 0.3263 0.2678 0.2116 0.0828 0.0270 0.0300 416 ILE A O 3076 C CB . ILE A 423 ? 0.3197 0.2566 0.1884 0.0921 0.0086 0.0216 416 ILE A CB 3077 C CG1 . ILE A 423 ? 0.3472 0.2803 0.2029 0.0989 0.0012 0.0181 416 ILE A CG1 3078 C CG2 . ILE A 423 ? 0.3055 0.2476 0.1883 0.0867 0.0046 0.0184 416 ILE A CG2 3079 C CD1 . ILE A 423 ? 0.3545 0.2813 0.2011 0.1052 -0.0036 0.0188 416 ILE A CD1 3080 N N . LEU A 424 ? 0.2954 0.2477 0.1967 0.0743 0.0179 0.0209 417 LEU A N 3081 C CA . LEU A 424 ? 0.2899 0.2457 0.2040 0.0683 0.0225 0.0226 417 LEU A CA 3082 C C . LEU A 424 ? 0.2877 0.2443 0.2080 0.0663 0.0185 0.0204 417 LEU A C 3083 O O . LEU A 424 ? 0.2892 0.2484 0.2109 0.0658 0.0119 0.0157 417 LEU A O 3084 C CB . LEU A 424 ? 0.2697 0.2322 0.1935 0.0623 0.0232 0.0202 417 LEU A CB 3085 C CG . LEU A 424 ? 0.2938 0.2564 0.2127 0.0642 0.0266 0.0216 417 LEU A CG 3086 C CD1 . LEU A 424 ? 0.2772 0.2467 0.2068 0.0582 0.0264 0.0190 417 LEU A CD1 3087 C CD2 . LEU A 424 ? 0.3103 0.2689 0.2266 0.0666 0.0348 0.0277 417 LEU A CD2 3088 N N . PHE A 425 ? 0.2851 0.2397 0.2102 0.0650 0.0228 0.0237 418 PHE A N 3089 C CA . PHE A 425 ? 0.2704 0.2257 0.2026 0.0630 0.0200 0.0218 418 PHE A CA 3090 C C . PHE A 425 ? 0.2748 0.2345 0.2203 0.0560 0.0233 0.0212 418 PHE A C 3091 O O . PHE A 425 ? 0.2797 0.2388 0.2284 0.0543 0.0292 0.0245 418 PHE A O 3092 C CB . PHE A 425 ? 0.2814 0.2293 0.2076 0.0679 0.0217 0.0260 418 PHE A CB 3093 C CG . PHE A 425 ? 0.2996 0.2422 0.2113 0.0754 0.0182 0.0269 418 PHE A CG 3094 C CD1 . PHE A 425 ? 0.3253 0.2682 0.2350 0.0779 0.0104 0.0229 418 PHE A CD1 3095 C CD2 . PHE A 425 ? 0.3423 0.2795 0.2422 0.0803 0.0227 0.0315 418 PHE A CD2 3096 C CE1 . PHE A 425 ? 0.3428 0.2805 0.2387 0.0854 0.0061 0.0232 418 PHE A CE1 3097 C CE2 . PHE A 425 ? 0.3523 0.2839 0.2369 0.0879 0.0189 0.0319 418 PHE A CE2 3098 C CZ . PHE A 425 ? 0.3575 0.2893 0.2402 0.0905 0.0103 0.0276 418 PHE A CZ 3099 N N . ALA A 426 ? 0.2759 0.2400 0.2294 0.0522 0.0196 0.0167 419 ALA A N 3100 C CA . ALA A 426 ? 0.2599 0.2280 0.2247 0.0459 0.0220 0.0153 419 ALA A CA 3101 C C . ALA A 426 ? 0.2572 0.2256 0.2287 0.0442 0.0203 0.0131 419 ALA A C 3102 O O . ALA A 426 ? 0.2612 0.2307 0.2320 0.0456 0.0158 0.0102 419 ALA A O 3103 C CB . ALA A 426 ? 0.2510 0.2256 0.2192 0.0419 0.0199 0.0117 419 ALA A CB 3104 N N . SER A 427 ? 0.2539 0.2213 0.2326 0.0412 0.0242 0.0144 420 SER A N 3105 C CA . SER A 427 ? 0.2339 0.2019 0.2205 0.0386 0.0235 0.0118 420 SER A CA 3106 C C . SER A 427 ? 0.2403 0.2135 0.2349 0.0327 0.0241 0.0086 420 SER A C 3107 O O . SER A 427 ? 0.2387 0.2114 0.2381 0.0301 0.0278 0.0103 420 SER A O 3108 C CB . SER A 427 ? 0.2570 0.2186 0.2454 0.0401 0.0276 0.0159 420 SER A CB 3109 O OG . SER A 427 ? 0.2390 0.2007 0.2358 0.0375 0.0272 0.0132 420 SER A OG 3110 N N . TRP A 428 ? 0.2244 0.2025 0.2203 0.0306 0.0205 0.0041 421 TRP A N 3111 C CA . TRP A 428 ? 0.2169 0.1998 0.2180 0.0256 0.0206 0.0012 421 TRP A CA 3112 C C . TRP A 428 ? 0.2352 0.2180 0.2437 0.0225 0.0213 -0.0015 421 TRP A C 3113 O O . TRP A 428 ? 0.2369 0.2178 0.2468 0.0239 0.0207 -0.0026 421 TRP A O 3114 C CB . TRP A 428 ? 0.2136 0.2011 0.2128 0.0245 0.0170 -0.0023 421 TRP A CB 3115 C CG . TRP A 428 ? 0.2005 0.1885 0.1929 0.0272 0.0150 -0.0011 421 TRP A CG 3116 C CD1 . TRP A 428 ? 0.2061 0.1949 0.1955 0.0295 0.0114 -0.0027 421 TRP A CD1 3117 C CD2 . TRP A 428 ? 0.1960 0.1838 0.1846 0.0281 0.0164 0.0015 421 TRP A CD2 3118 N NE1 . TRP A 428 ? 0.2085 0.1972 0.1918 0.0316 0.0101 -0.0016 421 TRP A NE1 3119 C CE2 . TRP A 428 ? 0.2228 0.2109 0.2052 0.0309 0.0133 0.0010 421 TRP A CE2 3120 C CE3 . TRP A 428 ? 0.2258 0.2134 0.2165 0.0266 0.0199 0.0039 421 TRP A CE3 3121 C CZ2 . TRP A 428 ? 0.2331 0.2207 0.2101 0.0327 0.0137 0.0029 421 TRP A CZ2 3122 C CZ3 . TRP A 428 ? 0.2349 0.2226 0.2210 0.0283 0.0206 0.0059 421 TRP A CZ3 3123 C CH2 . TRP A 428 ? 0.2547 0.2421 0.2334 0.0316 0.0176 0.0054 421 TRP A CH2 3124 N N . ASP A 429 ? 0.2213 0.2062 0.2345 0.0186 0.0224 -0.0028 422 ASP A N 3125 C CA . ASP A 429 ? 0.2185 0.2034 0.2381 0.0156 0.0225 -0.0062 422 ASP A CA 3126 C C . ASP A 429 ? 0.2132 0.2029 0.2321 0.0129 0.0199 -0.0106 422 ASP A C 3127 O O . ASP A 429 ? 0.2210 0.2140 0.2361 0.0126 0.0185 -0.0106 422 ASP A O 3128 C CB . ASP A 429 ? 0.2157 0.1991 0.2417 0.0132 0.0249 -0.0049 422 ASP A CB 3129 C CG . ASP A 429 ? 0.2314 0.2120 0.2645 0.0114 0.0256 -0.0073 422 ASP A CG 3130 O OD1 . ASP A 429 ? 0.2356 0.2162 0.2686 0.0115 0.0241 -0.0109 422 ASP A OD1 3131 O OD2 . ASP A 429 ? 0.2305 0.2089 0.2701 0.0098 0.0277 -0.0058 422 ASP A OD2 3132 N N . ALA A 430 ? 0.2204 0.2100 0.2431 0.0112 0.0196 -0.0144 423 ALA A N 3133 C CA . ALA A 430 ? 0.2214 0.2147 0.2433 0.0085 0.0180 -0.0187 423 ALA A CA 3134 C C . ALA A 430 ? 0.2068 0.2035 0.2236 0.0093 0.0165 -0.0194 423 ALA A C 3135 O O . ALA A 430 ? 0.2148 0.2147 0.2293 0.0073 0.0154 -0.0214 423 ALA A O 3136 C CB . ALA A 430 ? 0.2216 0.2164 0.2451 0.0055 0.0174 -0.0195 423 ALA A CB 3137 N N . ALA A 431 ? 0.2119 0.2078 0.2273 0.0124 0.0162 -0.0179 424 ALA A N 3138 C CA . ALA A 431 ? 0.2082 0.2075 0.2208 0.0128 0.0147 -0.0189 424 ALA A CA 3139 C C . ALA A 431 ? 0.2080 0.2094 0.2224 0.0112 0.0152 -0.0230 424 ALA A C 3140 O O . ALA A 431 ? 0.2086 0.2133 0.2210 0.0098 0.0147 -0.0243 424 ALA A O 3141 C CB . ALA A 431 ? 0.2120 0.2103 0.2238 0.0166 0.0135 -0.0172 424 ALA A CB 3142 N N . GLU A 432 ? 0.2089 0.2080 0.2270 0.0115 0.0164 -0.0248 425 GLU A N 3143 C CA . GLU A 432 ? 0.2133 0.2141 0.2327 0.0106 0.0174 -0.0289 425 GLU A CA 3144 C C . GLU A 432 ? 0.2125 0.2147 0.2287 0.0075 0.0175 -0.0312 425 GLU A C 3145 O O . GLU A 432 ? 0.2200 0.2241 0.2349 0.0068 0.0186 -0.0341 425 GLU A O 3146 C CB . GLU A 432 ? 0.2044 0.2020 0.2284 0.0118 0.0186 -0.0308 425 GLU A CB 3147 C CG . GLU A 432 ? 0.2153 0.2112 0.2422 0.0154 0.0182 -0.0290 425 GLU A CG 3148 C CD . GLU A 432 ? 0.2234 0.2232 0.2514 0.0170 0.0175 -0.0297 425 GLU A CD 3149 O OE1 . GLU A 432 ? 0.2255 0.2292 0.2519 0.0152 0.0177 -0.0311 425 GLU A OE1 3150 O OE2 . GLU A 432 ? 0.2171 0.2157 0.2481 0.0201 0.0166 -0.0290 425 GLU A OE2 3151 N N . PHE A 433 ? 0.2117 0.2131 0.2266 0.0060 0.0165 -0.0299 426 PHE A N 3152 C CA . PHE A 433 ? 0.2070 0.2096 0.2188 0.0035 0.0158 -0.0321 426 PHE A CA 3153 C C . PHE A 433 ? 0.2085 0.2138 0.2157 0.0026 0.0146 -0.0301 426 PHE A C 3154 O O . PHE A 433 ? 0.2057 0.2118 0.2101 0.0008 0.0133 -0.0310 426 PHE A O 3155 C CB . PHE A 433 ? 0.2308 0.2308 0.2459 0.0022 0.0150 -0.0326 426 PHE A CB 3156 C CG . PHE A 433 ? 0.2224 0.2192 0.2416 0.0024 0.0159 -0.0357 426 PHE A CG 3157 C CD1 . PHE A 433 ? 0.2363 0.2325 0.2539 0.0011 0.0153 -0.0405 426 PHE A CD1 3158 C CD2 . PHE A 433 ? 0.2448 0.2386 0.2690 0.0043 0.0173 -0.0340 426 PHE A CD2 3159 C CE1 . PHE A 433 ? 0.2363 0.2290 0.2579 0.0015 0.0160 -0.0439 426 PHE A CE1 3160 C CE2 . PHE A 433 ? 0.2353 0.2256 0.2638 0.0047 0.0181 -0.0368 426 PHE A CE2 3161 C CZ . PHE A 433 ? 0.2495 0.2393 0.2772 0.0032 0.0174 -0.0420 426 PHE A CZ 3162 N N . GLY A 434 ? 0.2025 0.2093 0.2092 0.0040 0.0146 -0.0277 427 GLY A N 3163 C CA . GLY A 434 ? 0.1921 0.2012 0.1949 0.0033 0.0134 -0.0260 427 GLY A CA 3164 C C . GLY A 434 ? 0.2126 0.2215 0.2153 0.0046 0.0122 -0.0225 427 GLY A C 3165 O O . GLY A 434 ? 0.2114 0.2214 0.2114 0.0039 0.0110 -0.0211 427 GLY A O 3166 N N . LEU A 435 ? 0.1941 0.2013 0.1993 0.0070 0.0125 -0.0211 428 LEU A N 3167 C CA . LEU A 435 ? 0.1910 0.1975 0.1948 0.0090 0.0116 -0.0178 428 LEU A CA 3168 C C . LEU A 435 ? 0.2000 0.2057 0.2035 0.0081 0.0118 -0.0161 428 LEU A C 3169 O O . LEU A 435 ? 0.2032 0.2095 0.2044 0.0087 0.0111 -0.0140 428 LEU A O 3170 C CB . LEU A 435 ? 0.2030 0.2116 0.2041 0.0094 0.0099 -0.0174 428 LEU A CB 3171 C CG . LEU A 435 ? 0.1909 0.2014 0.1939 0.0092 0.0100 -0.0196 428 LEU A CG 3172 C CD1 . LEU A 435 ? 0.2129 0.2251 0.2146 0.0092 0.0083 -0.0189 428 LEU A CD1 3173 C CD2 . LEU A 435 ? 0.2239 0.2330 0.2303 0.0118 0.0101 -0.0200 428 LEU A CD2 3174 N N . LEU A 436 ? 0.2002 0.2048 0.2070 0.0066 0.0128 -0.0172 429 LEU A N 3175 C CA . LEU A 436 ? 0.1988 0.2037 0.2073 0.0051 0.0127 -0.0163 429 LEU A CA 3176 C C . LEU A 436 ? 0.1966 0.1998 0.2063 0.0070 0.0142 -0.0125 429 LEU A C 3177 O O . LEU A 436 ? 0.2084 0.2129 0.2179 0.0067 0.0140 -0.0109 429 LEU A O 3178 C CB . LEU A 436 ? 0.1941 0.1983 0.2067 0.0028 0.0128 -0.0191 429 LEU A CB 3179 C CG . LEU A 436 ? 0.2094 0.2147 0.2193 0.0014 0.0118 -0.0231 429 LEU A CG 3180 C CD1 . LEU A 436 ? 0.2393 0.2433 0.2529 -0.0005 0.0113 -0.0263 429 LEU A CD1 3181 C CD2 . LEU A 436 ? 0.2211 0.2291 0.2258 0.0004 0.0101 -0.0234 429 LEU A CD2 3182 N N . GLY A 437 ? 0.2082 0.2083 0.2190 0.0092 0.0159 -0.0110 430 GLY A N 3183 C CA . GLY A 437 ? 0.1964 0.1941 0.2076 0.0113 0.0181 -0.0069 430 GLY A CA 3184 C C . GLY A 437 ? 0.2073 0.2055 0.2125 0.0139 0.0174 -0.0047 430 GLY A C 3185 O O . GLY A 437 ? 0.2130 0.2113 0.2179 0.0146 0.0189 -0.0021 430 GLY A O 3186 N N . SER A 438 ? 0.1997 0.1983 0.2006 0.0156 0.0153 -0.0057 431 SER A N 3187 C CA . SER A 438 ? 0.2086 0.2072 0.2039 0.0182 0.0140 -0.0043 431 SER A CA 3188 C C . SER A 438 ? 0.1983 0.2001 0.1933 0.0161 0.0130 -0.0048 431 SER A C 3189 O O . SER A 438 ? 0.1946 0.1962 0.1869 0.0177 0.0134 -0.0028 431 SER A O 3190 C CB . SER A 438 ? 0.2009 0.1998 0.1938 0.0198 0.0113 -0.0060 431 SER A CB 3191 O OG . SER A 438 ? 0.2099 0.2120 0.2052 0.0167 0.0100 -0.0092 431 SER A OG 3192 N N . THR A 439 ? 0.1999 0.2044 0.1972 0.0128 0.0118 -0.0075 432 THR A N 3193 C CA . THR A 439 ? 0.1967 0.2037 0.1929 0.0111 0.0103 -0.0080 432 THR A CA 3194 C C . THR A 439 ? 0.1887 0.1963 0.1880 0.0104 0.0116 -0.0064 432 THR A C 3195 O O . THR A 439 ? 0.2025 0.2111 0.2003 0.0112 0.0111 -0.0051 432 THR A O 3196 C CB . THR A 439 ? 0.2028 0.2119 0.1994 0.0081 0.0088 -0.0109 432 THR A CB 3197 O OG1 . THR A 439 ? 0.2074 0.2164 0.2025 0.0088 0.0082 -0.0121 432 THR A OG1 3198 C CG2 . THR A 439 ? 0.2058 0.2169 0.2002 0.0069 0.0070 -0.0108 432 THR A CG2 3199 N N . GLU A 440 ? 0.1878 0.1948 0.1924 0.0089 0.0133 -0.0065 433 GLU A N 3200 C CA . GLU A 440 ? 0.1927 0.2009 0.2025 0.0080 0.0146 -0.0052 433 GLU A CA 3201 C C . GLU A 440 ? 0.1948 0.2015 0.2032 0.0112 0.0173 -0.0014 433 GLU A C 3202 O O . GLU A 440 ? 0.2053 0.2138 0.2156 0.0114 0.0180 0.0000 433 GLU A O 3203 C CB . GLU A 440 ? 0.2000 0.2074 0.2172 0.0058 0.0158 -0.0062 433 GLU A CB 3204 C CG . GLU A 440 ? 0.2044 0.2131 0.2221 0.0029 0.0128 -0.0105 433 GLU A CG 3205 C CD . GLU A 440 ? 0.2150 0.2269 0.2311 0.0016 0.0098 -0.0118 433 GLU A CD 3206 O OE1 . GLU A 440 ? 0.2205 0.2342 0.2411 0.0011 0.0097 -0.0107 433 GLU A OE1 3207 O OE2 . GLU A 440 ? 0.2147 0.2272 0.2251 0.0011 0.0078 -0.0137 433 GLU A OE2 3208 N N . TRP A 441 ? 0.1977 0.2009 0.2028 0.0139 0.0191 0.0003 434 TRP A N 3209 C CA . TRP A 441 ? 0.2056 0.2067 0.2076 0.0176 0.0221 0.0041 434 TRP A CA 3210 C C . TRP A 441 ? 0.2150 0.2170 0.2105 0.0198 0.0201 0.0041 434 TRP A C 3211 O O . TRP A 441 ? 0.2143 0.2164 0.2089 0.0216 0.0221 0.0062 434 TRP A O 3212 C CB . TRP A 441 ? 0.2196 0.2162 0.2179 0.0206 0.0237 0.0058 434 TRP A CB 3213 C CG . TRP A 441 ? 0.2176 0.2108 0.2107 0.0250 0.0271 0.0100 434 TRP A CG 3214 C CD1 . TRP A 441 ? 0.2315 0.2227 0.2280 0.0258 0.0323 0.0138 434 TRP A CD1 3215 C CD2 . TRP A 441 ? 0.2407 0.2319 0.2241 0.0294 0.0257 0.0106 434 TRP A CD2 3216 N NE1 . TRP A 441 ? 0.2509 0.2387 0.2391 0.0308 0.0346 0.0171 434 TRP A NE1 3217 C CE2 . TRP A 441 ? 0.2388 0.2264 0.2185 0.0332 0.0303 0.0150 434 TRP A CE2 3218 C CE3 . TRP A 441 ? 0.2338 0.2256 0.2117 0.0305 0.0211 0.0079 434 TRP A CE3 3219 C CZ2 . TRP A 441 ? 0.2621 0.2465 0.2311 0.0385 0.0300 0.0163 434 TRP A CZ2 3220 C CZ3 . TRP A 441 ? 0.2564 0.2451 0.2249 0.0356 0.0202 0.0090 434 TRP A CZ3 3221 C CH2 . TRP A 441 ? 0.2577 0.2426 0.2213 0.0396 0.0246 0.0130 434 TRP A CH2 3222 N N . ALA A 442 ? 0.1971 0.1998 0.1888 0.0194 0.0163 0.0014 435 ALA A N 3223 C CA . ALA A 442 ? 0.2071 0.2103 0.1937 0.0211 0.0141 0.0010 435 ALA A CA 3224 C C . ALA A 442 ? 0.2010 0.2075 0.1910 0.0189 0.0135 0.0006 435 ALA A C 3225 O O . ALA A 442 ? 0.2005 0.2071 0.1878 0.0209 0.0133 0.0015 435 ALA A O 3226 C CB . ALA A 442 ? 0.2029 0.2061 0.1864 0.0209 0.0104 -0.0016 435 ALA A CB 3227 N N . GLU A 443 ? 0.1972 0.2062 0.1928 0.0151 0.0128 -0.0009 436 GLU A N 3228 C CA . GLU A 443 ? 0.1936 0.2056 0.1927 0.0134 0.0117 -0.0012 436 GLU A CA 3229 C C . GLU A 443 ? 0.2051 0.2177 0.2084 0.0148 0.0150 0.0014 436 GLU A C 3230 O O . GLU A 443 ? 0.2102 0.2245 0.2141 0.0157 0.0147 0.0020 436 GLU A O 3231 C CB . GLU A 443 ? 0.2005 0.2146 0.2039 0.0095 0.0098 -0.0036 436 GLU A CB 3232 C CG . GLU A 443 ? 0.1956 0.2096 0.1941 0.0083 0.0070 -0.0059 436 GLU A CG 3233 C CD . GLU A 443 ? 0.2272 0.2427 0.2276 0.0052 0.0051 -0.0083 436 GLU A CD 3234 O OE1 . GLU A 443 ? 0.2167 0.2327 0.2132 0.0042 0.0028 -0.0094 436 GLU A OE1 3235 O OE2 . GLU A 443 ? 0.2258 0.2416 0.2314 0.0038 0.0059 -0.0091 436 GLU A OE2 3236 N N . GLU A 444 ? 0.2176 0.2286 0.2242 0.0151 0.0185 0.0031 437 GLU A N 3237 C CA . GLU A 444 ? 0.2091 0.2205 0.2206 0.0165 0.0227 0.0060 437 GLU A CA 3238 C C . GLU A 444 ? 0.2200 0.2295 0.2244 0.0210 0.0246 0.0083 437 GLU A C 3239 O O . GLU A 444 ? 0.2297 0.2409 0.2367 0.0222 0.0267 0.0098 437 GLU A O 3240 C CB . GLU A 444 ? 0.2328 0.2418 0.2484 0.0162 0.0265 0.0078 437 GLU A CB 3241 C CG . GLU A 444 ? 0.2689 0.2786 0.2919 0.0168 0.0317 0.0112 437 GLU A CG 3242 C CD . GLU A 444 ? 0.4005 0.4093 0.4327 0.0142 0.0341 0.0117 437 GLU A CD 3243 O OE1 . GLU A 444 ? 0.5223 0.5344 0.5655 0.0110 0.0337 0.0106 437 GLU A OE1 3244 O OE2 . GLU A 444 ? 0.3648 0.3695 0.3933 0.0154 0.0357 0.0129 437 GLU A OE2 3245 N N . ASN A 445 ? 0.2035 0.2096 0.1992 0.0236 0.0236 0.0081 438 ASN A N 3246 C CA . ASN A 445 ? 0.2167 0.2197 0.2041 0.0286 0.0254 0.0101 438 ASN A CA 3247 C C . ASN A 445 ? 0.2207 0.2236 0.2016 0.0300 0.0211 0.0078 438 ASN A C 3248 O O . ASN A 445 ? 0.2187 0.2183 0.1914 0.0342 0.0210 0.0083 438 ASN A O 3249 C CB . ASN A 445 ? 0.2319 0.2302 0.2140 0.0314 0.0277 0.0120 438 ASN A CB 3250 C CG . ASN A 445 ? 0.2398 0.2375 0.2284 0.0307 0.0330 0.0152 438 ASN A CG 3251 O OD1 . ASN A 445 ? 0.2710 0.2688 0.2614 0.0324 0.0378 0.0182 438 ASN A OD1 3252 N ND2 . ASN A 445 ? 0.2514 0.2487 0.2448 0.0279 0.0327 0.0146 438 ASN A ND2 3253 N N . SER A 446 ? 0.2108 0.2168 0.1951 0.0267 0.0174 0.0053 439 SER A N 3254 C CA . SER A 446 ? 0.2170 0.2224 0.1961 0.0273 0.0131 0.0031 439 SER A CA 3255 C C . SER A 446 ? 0.2127 0.2164 0.1866 0.0315 0.0135 0.0037 439 SER A C 3256 O O . SER A 446 ? 0.2299 0.2311 0.1975 0.0337 0.0106 0.0022 439 SER A O 3257 C CB . SER A 446 ? 0.2078 0.2165 0.1913 0.0233 0.0099 0.0012 439 SER A CB 3258 O OG . SER A 446 ? 0.2293 0.2407 0.2180 0.0226 0.0110 0.0021 439 SER A OG 3259 N N . ARG A 447 ? 0.2094 0.2145 0.1863 0.0326 0.0168 0.0056 440 ARG A N 3260 C CA . ARG A 447 ? 0.2129 0.2165 0.1849 0.0369 0.0176 0.0060 440 ARG A CA 3261 C C . ARG A 447 ? 0.2283 0.2270 0.1909 0.0419 0.0196 0.0071 440 ARG A C 3262 O O . ARG A 447 ? 0.2388 0.2345 0.1937 0.0456 0.0175 0.0057 440 ARG A O 3263 C CB . ARG A 447 ? 0.2240 0.2306 0.2026 0.0370 0.0213 0.0078 440 ARG A CB 3264 C CG . ARG A 447 ? 0.2498 0.2607 0.2360 0.0332 0.0180 0.0063 440 ARG A CG 3265 C CD . ARG A 447 ? 0.2976 0.3128 0.2946 0.0311 0.0210 0.0079 440 ARG A CD 3266 N NE . ARG A 447 ? 0.2500 0.2687 0.2528 0.0277 0.0167 0.0061 440 ARG A NE 3267 C CZ . ARG A 447 ? 0.2647 0.2846 0.2700 0.0236 0.0134 0.0046 440 ARG A CZ 3268 N NH1 . ARG A 447 ? 0.2877 0.3063 0.2920 0.0220 0.0142 0.0044 440 ARG A NH1 3269 N NH2 . ARG A 447 ? 0.2394 0.2619 0.2482 0.0216 0.0096 0.0032 440 ARG A NH2 3270 N N . LEU A 448 ? 0.2228 0.2203 0.1858 0.0423 0.0234 0.0095 441 LEU A N 3271 C CA . LEU A 448 ? 0.2361 0.2285 0.1892 0.0474 0.0251 0.0108 441 LEU A CA 3272 C C . LEU A 448 ? 0.2475 0.2373 0.1945 0.0480 0.0192 0.0078 441 LEU A C 3273 O O . LEU A 448 ? 0.2578 0.2436 0.1953 0.0527 0.0172 0.0068 441 LEU A O 3274 C CB . LEU A 448 ? 0.2426 0.2337 0.1978 0.0474 0.0304 0.0145 441 LEU A CB 3275 C CG . LEU A 448 ? 0.2494 0.2436 0.2139 0.0457 0.0364 0.0175 441 LEU A CG 3276 C CD1 . LEU A 448 ? 0.2834 0.2752 0.2496 0.0460 0.0417 0.0213 441 LEU A CD1 3277 C CD2 . LEU A 448 ? 0.2759 0.2701 0.2376 0.0497 0.0399 0.0187 441 LEU A CD2 3278 N N . LEU A 449 ? 0.2345 0.2267 0.1874 0.0434 0.0162 0.0061 442 LEU A N 3279 C CA . LEU A 449 ? 0.2498 0.2404 0.1992 0.0437 0.0111 0.0035 442 LEU A CA 3280 C C . LEU A 449 ? 0.2569 0.2472 0.2038 0.0443 0.0063 0.0004 442 LEU A C 3281 O O . LEU A 449 ? 0.2876 0.2748 0.2285 0.0473 0.0027 -0.0016 442 LEU A O 3282 C CB . LEU A 449 ? 0.2369 0.2303 0.1938 0.0386 0.0100 0.0025 442 LEU A CB 3283 C CG . LEU A 449 ? 0.2275 0.2202 0.1869 0.0381 0.0140 0.0050 442 LEU A CG 3284 C CD1 . LEU A 449 ? 0.2218 0.2179 0.1896 0.0327 0.0130 0.0035 442 LEU A CD1 3285 C CD2 . LEU A 449 ? 0.2750 0.2631 0.2275 0.0423 0.0136 0.0058 442 LEU A CD2 3286 N N . GLN A 450 ? 0.2571 0.2505 0.2090 0.0415 0.0060 -0.0002 443 GLN A N 3287 C CA . GLN A 450 ? 0.2864 0.2794 0.2373 0.0416 0.0020 -0.0027 443 GLN A CA 3288 C C . GLN A 450 ? 0.2697 0.2585 0.2118 0.0475 0.0013 -0.0034 443 GLN A C 3289 O O . GLN A 450 ? 0.2633 0.2496 0.2020 0.0490 -0.0034 -0.0063 443 GLN A O 3290 C CB . GLN A 450 ? 0.2889 0.2853 0.2456 0.0390 0.0035 -0.0017 443 GLN A CB 3291 C CG A GLN A 450 ? 0.3331 0.3303 0.2919 0.0371 -0.0001 -0.0035 443 GLN A CG 3292 C CG B GLN A 450 ? 0.2898 0.2852 0.2449 0.0405 0.0008 -0.0033 443 GLN A CG 3293 C CD A GLN A 450 ? 0.2641 0.2653 0.2300 0.0326 0.0007 -0.0026 443 GLN A CD 3294 C CD B GLN A 450 ? 0.2801 0.2755 0.2373 0.0375 -0.0041 -0.0057 443 GLN A CD 3295 O OE1 A GLN A 450 ? 0.2503 0.2529 0.2191 0.0291 -0.0005 -0.0032 443 GLN A OE1 3296 O OE1 B GLN A 450 ? 0.2955 0.2933 0.2573 0.0332 -0.0046 -0.0057 443 GLN A OE1 3297 N NE2 A GLN A 450 ? 0.2417 0.2449 0.2107 0.0330 0.0031 -0.0011 443 GLN A NE2 3298 N NE2 B GLN A 450 ? 0.2183 0.2106 0.1721 0.0398 -0.0074 -0.0078 443 GLN A NE2 3299 N N . GLU A 451 ? 0.2665 0.2541 0.2050 0.0510 0.0061 -0.0008 444 GLU A N 3300 C CA . GLU A 451 ? 0.2560 0.2396 0.1856 0.0568 0.0061 -0.0016 444 GLU A CA 3301 C C . GLU A 451 ? 0.2682 0.2468 0.1874 0.0621 0.0065 -0.0011 444 GLU A C 3302 O O . GLU A 451 ? 0.2626 0.2369 0.1726 0.0673 0.0047 -0.0028 444 GLU A O 3303 C CB . GLU A 451 ? 0.2771 0.2621 0.2082 0.0582 0.0115 0.0008 444 GLU A CB 3304 C CG . GLU A 451 ? 0.2769 0.2669 0.2184 0.0534 0.0108 0.0005 444 GLU A CG 3305 C CD . GLU A 451 ? 0.3273 0.3168 0.2693 0.0521 0.0048 -0.0029 444 GLU A CD 3306 O OE1 . GLU A 451 ? 0.2985 0.2841 0.2343 0.0545 0.0007 -0.0055 444 GLU A OE1 3307 O OE2 . GLU A 451 ? 0.3131 0.3059 0.2624 0.0485 0.0040 -0.0028 444 GLU A OE2 3308 N N . ARG A 452 ? 0.2460 0.2249 0.1666 0.0607 0.0080 0.0008 445 ARG A N 3309 C CA . ARG A 452 ? 0.2609 0.2347 0.1714 0.0660 0.0089 0.0021 445 ARG A CA 3310 C C . ARG A 452 ? 0.2753 0.2481 0.1859 0.0652 0.0043 0.0005 445 ARG A C 3311 O O . ARG A 452 ? 0.2796 0.2477 0.1811 0.0701 0.0035 0.0010 445 ARG A O 3312 C CB . ARG A 452 ? 0.2627 0.2362 0.1733 0.0669 0.0168 0.0071 445 ARG A CB 3313 C CG . ARG A 452 ? 0.2744 0.2490 0.1854 0.0685 0.0222 0.0090 445 ARG A CG 3314 C CD . ARG A 452 ? 0.2851 0.2598 0.1982 0.0689 0.0304 0.0142 445 ARG A CD 3315 N NE . ARG A 452 ? 0.2855 0.2632 0.2037 0.0689 0.0357 0.0159 445 ARG A NE 3316 C CZ . ARG A 452 ? 0.2702 0.2499 0.1952 0.0677 0.0429 0.0201 445 ARG A CZ 3317 N NH1 . ARG A 452 ? 0.2824 0.2608 0.2094 0.0664 0.0460 0.0232 445 ARG A NH1 3318 N NH2 . ARG A 452 ? 0.2846 0.2678 0.2157 0.0676 0.0469 0.0210 445 ARG A NH2 3319 N N . GLY A 453 ? 0.2727 0.2497 0.1931 0.0595 0.0013 -0.0014 446 GLY A N 3320 C CA . GLY A 453 ? 0.2710 0.2482 0.1940 0.0580 -0.0019 -0.0025 446 GLY A CA 3321 C C . GLY A 453 ? 0.2689 0.2438 0.1880 0.0607 -0.0090 -0.0067 446 GLY A C 3322 O O . GLY A 453 ? 0.2790 0.2557 0.2025 0.0583 -0.0129 -0.0098 446 GLY A O 3323 N N . VAL A 454 ? 0.2732 0.2438 0.1843 0.0656 -0.0110 -0.0067 447 VAL A N 3324 C CA . VAL A 454 ? 0.2785 0.2469 0.1869 0.0683 -0.0185 -0.0110 447 VAL A CA 3325 C C . VAL A 454 ? 0.2677 0.2399 0.1867 0.0640 -0.0221 -0.0131 447 VAL A C 3326 O O . VAL A 454 ? 0.2685 0.2426 0.1934 0.0619 -0.0273 -0.0169 447 VAL A O 3327 C CB . VAL A 454 ? 0.3058 0.2679 0.2010 0.0758 -0.0197 -0.0102 447 VAL A CB 3328 C CG1 . VAL A 454 ? 0.3205 0.2806 0.2140 0.0787 -0.0284 -0.0149 447 VAL A CG1 3329 C CG2 . VAL A 454 ? 0.3358 0.2939 0.2197 0.0808 -0.0167 -0.0090 447 VAL A CG2 3330 N N . ALA A 455 ? 0.2648 0.2379 0.1865 0.0628 -0.0193 -0.0106 448 ALA A N 3331 C CA . ALA A 455 ? 0.2498 0.2261 0.1806 0.0598 -0.0223 -0.0126 448 ALA A CA 3332 C C . ALA A 455 ? 0.2483 0.2261 0.1834 0.0572 -0.0172 -0.0094 448 ALA A C 3333 O O . ALA A 455 ? 0.2689 0.2440 0.1984 0.0594 -0.0126 -0.0057 448 ALA A O 3334 C CB . ALA A 455 ? 0.2742 0.2470 0.2003 0.0650 -0.0288 -0.0152 448 ALA A CB 3335 N N . TYR A 456 ? 0.2408 0.2229 0.1863 0.0527 -0.0181 -0.0111 449 TYR A N 3336 C CA . TYR A 456 ? 0.2367 0.2203 0.1873 0.0502 -0.0144 -0.0091 449 TYR A CA 3337 C C . TYR A 456 ? 0.2381 0.2228 0.1940 0.0508 -0.0185 -0.0116 449 TYR A C 3338 O O . TYR A 456 ? 0.2406 0.2286 0.2034 0.0485 -0.0220 -0.0150 449 TYR A O 3339 C CB . TYR A 456 ? 0.2266 0.2148 0.1851 0.0439 -0.0105 -0.0088 449 TYR A CB 3340 C CG . TYR A 456 ? 0.2293 0.2187 0.1931 0.0415 -0.0072 -0.0076 449 TYR A CG 3341 C CD1 . TYR A 456 ? 0.2395 0.2268 0.2012 0.0418 -0.0024 -0.0041 449 TYR A CD1 3342 C CD2 . TYR A 456 ? 0.2366 0.2291 0.2081 0.0389 -0.0088 -0.0101 449 TYR A CD2 3343 C CE1 . TYR A 456 ? 0.2389 0.2268 0.2058 0.0398 0.0003 -0.0034 449 TYR A CE1 3344 C CE2 . TYR A 456 ? 0.2171 0.2103 0.1934 0.0371 -0.0058 -0.0094 449 TYR A CE2 3345 C CZ . TYR A 456 ? 0.2479 0.2386 0.2217 0.0375 -0.0016 -0.0062 449 TYR A CZ 3346 O OH . TYR A 456 ? 0.2385 0.2293 0.2172 0.0357 0.0010 -0.0059 449 TYR A OH 3347 N N . ILE A 457 ? 0.2408 0.2224 0.1938 0.0540 -0.0178 -0.0098 450 ILE A N 3348 C CA . ILE A 457 ? 0.2431 0.2258 0.2020 0.0547 -0.0211 -0.0118 450 ILE A CA 3349 C C . ILE A 457 ? 0.2381 0.2223 0.2032 0.0514 -0.0162 -0.0101 450 ILE A C 3350 O O . ILE A 457 ? 0.2487 0.2296 0.2095 0.0525 -0.0120 -0.0065 450 ILE A O 3351 C CB . ILE A 457 ? 0.2498 0.2269 0.1998 0.0619 -0.0250 -0.0111 450 ILE A CB 3352 C CG1 . ILE A 457 ? 0.2612 0.2358 0.2033 0.0659 -0.0303 -0.0132 450 ILE A CG1 3353 C CG2 . ILE A 457 ? 0.2773 0.2557 0.2342 0.0630 -0.0287 -0.0131 450 ILE A CG2 3354 C CD1 . ILE A 457 ? 0.2758 0.2553 0.2274 0.0628 -0.0355 -0.0182 450 ILE A CD1 3355 N N . ASN A 458 ? 0.2312 0.2204 0.2067 0.0473 -0.0165 -0.0127 451 ASN A N 3356 C CA . ASN A 458 ? 0.2369 0.2274 0.2182 0.0444 -0.0123 -0.0119 451 ASN A CA 3357 C C . ASN A 458 ? 0.2578 0.2457 0.2400 0.0481 -0.0137 -0.0116 451 ASN A C 3358 O O . ASN A 458 ? 0.2753 0.2617 0.2557 0.0524 -0.0188 -0.0128 451 ASN A O 3359 C CB . ASN A 458 ? 0.2306 0.2269 0.2216 0.0392 -0.0118 -0.0149 451 ASN A CB 3360 C CG . ASN A 458 ? 0.2377 0.2354 0.2324 0.0351 -0.0065 -0.0142 451 ASN A CG 3361 O OD1 . ASN A 458 ? 0.2463 0.2425 0.2372 0.0338 -0.0033 -0.0119 451 ASN A OD1 3362 N ND2 . ASN A 458 ? 0.2307 0.2313 0.2331 0.0333 -0.0059 -0.0164 451 ASN A ND2 3363 N N . ALA A 459 ? 0.2482 0.2355 0.2338 0.0465 -0.0097 -0.0103 452 ALA A N 3364 C CA . ALA A 459 ? 0.2700 0.2541 0.2564 0.0501 -0.0106 -0.0095 452 ALA A CA 3365 C C . ALA A 459 ? 0.2605 0.2463 0.2549 0.0467 -0.0068 -0.0102 452 ALA A C 3366 O O . ALA A 459 ? 0.2736 0.2553 0.2668 0.0476 -0.0038 -0.0076 452 ALA A O 3367 C CB . ALA A 459 ? 0.2818 0.2589 0.2576 0.0549 -0.0096 -0.0051 452 ALA A CB 3368 N N . ASP A 460 ? 0.2487 0.2402 0.2513 0.0428 -0.0068 -0.0138 453 ASP A N 3369 C CA . ASP A 460 ? 0.2557 0.2486 0.2659 0.0406 -0.0040 -0.0154 453 ASP A CA 3370 C C . ASP A 460 ? 0.2635 0.2563 0.2786 0.0444 -0.0073 -0.0169 453 ASP A C 3371 O O . ASP A 460 ? 0.2790 0.2688 0.2898 0.0492 -0.0114 -0.0158 453 ASP A O 3372 C CB . ASP A 460 ? 0.2388 0.2373 0.2544 0.0352 -0.0018 -0.0182 453 ASP A CB 3373 C CG . ASP A 460 ? 0.2789 0.2776 0.2990 0.0325 0.0023 -0.0194 453 ASP A CG 3374 O OD1 . ASP A 460 ? 0.3167 0.3118 0.3377 0.0346 0.0032 -0.0185 453 ASP A OD1 3375 O OD2 . ASP A 460 ? 0.2752 0.2775 0.2975 0.0283 0.0046 -0.0213 453 ASP A OD2 3376 N N . SER A 461 ? 0.2471 0.2430 0.2709 0.0425 -0.0057 -0.0197 454 SER A N 3377 C CA A SER A 461 ? 0.2553 0.2516 0.2857 0.0460 -0.0083 -0.0214 454 SER A CA 3378 C CA B SER A 461 ? 0.2630 0.2591 0.2932 0.0460 -0.0082 -0.0213 454 SER A CA 3379 C C . SER A 461 ? 0.2588 0.2553 0.2885 0.0504 -0.0147 -0.0218 454 SER A C 3380 O O . SER A 461 ? 0.2605 0.2610 0.2921 0.0491 -0.0171 -0.0237 454 SER A O 3381 C CB A SER A 461 ? 0.2545 0.2565 0.2953 0.0428 -0.0061 -0.0253 454 SER A CB 3382 C CB B SER A 461 ? 0.2597 0.2614 0.3004 0.0428 -0.0058 -0.0252 454 SER A CB 3383 O OG A SER A 461 ? 0.1990 0.2009 0.2396 0.0388 -0.0008 -0.0255 454 SER A OG 3384 O OG B SER A 461 ? 0.2787 0.2861 0.3231 0.0401 -0.0066 -0.0273 454 SER A OG 3385 N N . SER A 462 ? 0.2685 0.2602 0.2954 0.0558 -0.0176 -0.0202 455 SER A N 3386 C CA . SER A 462 ? 0.2956 0.2867 0.3208 0.0608 -0.0246 -0.0209 455 SER A CA 3387 C C . SER A 462 ? 0.2846 0.2816 0.3227 0.0613 -0.0283 -0.0252 455 SER A C 3388 O O . SER A 462 ? 0.2893 0.2882 0.3292 0.0638 -0.0344 -0.0272 455 SER A O 3389 C CB . SER A 462 ? 0.3062 0.2896 0.3227 0.0670 -0.0267 -0.0173 455 SER A CB 3390 O OG . SER A 462 ? 0.3287 0.3068 0.3332 0.0669 -0.0236 -0.0131 455 SER A OG 3391 N N . ILE A 463 ? 0.2942 0.2942 0.3419 0.0592 -0.0246 -0.0269 456 ILE A N 3392 C CA . ILE A 463 ? 0.3101 0.3158 0.3715 0.0601 -0.0271 -0.0308 456 ILE A CA 3393 C C . ILE A 463 ? 0.3114 0.3227 0.3822 0.0548 -0.0209 -0.0333 456 ILE A C 3394 O O . ILE A 463 ? 0.3338 0.3427 0.4012 0.0523 -0.0154 -0.0321 456 ILE A O 3395 C CB . ILE A 463 ? 0.3155 0.3175 0.3791 0.0658 -0.0299 -0.0303 456 ILE A CB 3396 C CG1 . ILE A 463 ? 0.3437 0.3402 0.4030 0.0653 -0.0241 -0.0276 456 ILE A CG1 3397 C CG2 . ILE A 463 ? 0.3387 0.3353 0.3932 0.0720 -0.0370 -0.0283 456 ILE A CG2 3398 C CD1 . ILE A 463 ? 0.4492 0.4464 0.5184 0.0671 -0.0233 -0.0295 456 ILE A CD1 3399 N N A GLU A 464 ? 0.3007 0.3192 0.3832 0.0530 -0.0218 -0.0367 457 GLU A N 3400 N N B GLU A 464 ? 0.3075 0.3260 0.3900 0.0530 -0.0218 -0.0367 457 GLU A N 3401 C CA A GLU A 464 ? 0.2934 0.3173 0.3859 0.0492 -0.0159 -0.0393 457 GLU A CA 3402 C CA B GLU A 464 ? 0.3047 0.3286 0.3973 0.0493 -0.0159 -0.0393 457 GLU A CA 3403 C C A GLU A 464 ? 0.2970 0.3266 0.4049 0.0515 -0.0185 -0.0427 457 GLU A C 3404 C C B GLU A 464 ? 0.3029 0.3326 0.4109 0.0514 -0.0186 -0.0427 457 GLU A C 3405 O O A GLU A 464 ? 0.2850 0.3204 0.4034 0.0487 -0.0140 -0.0452 457 GLU A O 3406 O O B GLU A 464 ? 0.2941 0.3297 0.4125 0.0486 -0.0142 -0.0452 457 GLU A O 3407 C CB A GLU A 464 ? 0.2902 0.3177 0.3816 0.0435 -0.0120 -0.0395 457 GLU A CB 3408 C CB B GLU A 464 ? 0.3027 0.3303 0.3944 0.0435 -0.0118 -0.0396 457 GLU A CB 3409 C CG A GLU A 464 ? 0.2786 0.3099 0.3745 0.0430 -0.0166 -0.0406 457 GLU A CG 3410 C CG B GLU A 464 ? 0.3239 0.3465 0.4017 0.0413 -0.0097 -0.0365 457 GLU A CG 3411 C CD A GLU A 464 ? 0.3265 0.3596 0.4189 0.0378 -0.0134 -0.0399 457 GLU A CD 3412 C CD B GLU A 464 ? 0.3604 0.3864 0.4373 0.0360 -0.0059 -0.0367 457 GLU A CD 3413 O OE1 A GLU A 464 ? 0.3254 0.3563 0.4097 0.0349 -0.0084 -0.0382 457 GLU A OE1 3414 O OE1 B GLU A 464 ? 0.3562 0.3861 0.4381 0.0348 -0.0081 -0.0377 457 GLU A OE1 3415 O OE2 A GLU A 464 ? 0.3386 0.3753 0.4370 0.0368 -0.0163 -0.0411 457 GLU A OE2 3416 O OE2 B GLU A 464 ? 0.3597 0.3841 0.4309 0.0331 -0.0010 -0.0359 457 GLU A OE2 3417 N N . GLY A 465 ? 0.3061 0.3338 0.4150 0.0568 -0.0258 -0.0427 458 GLY A N 3418 C CA . GLY A 465 ? 0.3019 0.3349 0.4258 0.0598 -0.0301 -0.0460 458 GLY A CA 3419 C C . GLY A 465 ? 0.3121 0.3408 0.4312 0.0660 -0.0393 -0.0452 458 GLY A C 3420 O O . GLY A 465 ? 0.3181 0.3395 0.4218 0.0679 -0.0410 -0.0418 458 GLY A O 3421 N N . ASN A 466 ? 0.3130 0.3458 0.4449 0.0695 -0.0452 -0.0482 459 ASN A N 3422 C CA . ASN A 466 ? 0.3196 0.3480 0.4469 0.0763 -0.0546 -0.0478 459 ASN A CA 3423 C C . ASN A 466 ? 0.3163 0.3505 0.4550 0.0775 -0.0627 -0.0517 459 ASN A C 3424 O O . ASN A 466 ? 0.3308 0.3641 0.4725 0.0835 -0.0713 -0.0531 459 ASN A O 3425 C CB . ASN A 466 ? 0.3436 0.3693 0.4743 0.0815 -0.0556 -0.0475 459 ASN A CB 3426 C CG . ASN A 466 ? 0.3454 0.3795 0.4972 0.0810 -0.0543 -0.0517 459 ASN A CG 3427 O OD1 . ASN A 466 ? 0.3617 0.4041 0.5265 0.0773 -0.0534 -0.0548 459 ASN A OD1 3428 N ND2 . ASN A 466 ? 0.4420 0.4741 0.5977 0.0850 -0.0540 -0.0516 459 ASN A ND2 3429 N N . TYR A 467 ? 0.2940 0.3338 0.4390 0.0719 -0.0601 -0.0533 460 TYR A N 3430 C CA . TYR A 467 ? 0.2895 0.3359 0.4493 0.0717 -0.0665 -0.0574 460 TYR A CA 3431 C C . TYR A 467 ? 0.2845 0.3271 0.4337 0.0730 -0.0736 -0.0574 460 TYR A C 3432 O O . TYR A 467 ? 0.2960 0.3381 0.4477 0.0780 -0.0837 -0.0599 460 TYR A O 3433 C CB . TYR A 467 ? 0.2800 0.3349 0.4548 0.0649 -0.0592 -0.0592 460 TYR A CB 3434 C CG . TYR A 467 ? 0.3088 0.3711 0.5022 0.0641 -0.0649 -0.0634 460 TYR A CG 3435 C CD1 . TYR A 467 ? 0.3369 0.4035 0.5460 0.0685 -0.0716 -0.0669 460 TYR A CD1 3436 C CD2 . TYR A 467 ? 0.3407 0.4057 0.5368 0.0590 -0.0636 -0.0640 460 TYR A CD2 3437 C CE1 . TYR A 467 ? 0.3653 0.4392 0.5935 0.0676 -0.0771 -0.0711 460 TYR A CE1 3438 C CE2 . TYR A 467 ? 0.3537 0.4254 0.5685 0.0579 -0.0687 -0.0679 460 TYR A CE2 3439 C CZ . TYR A 467 ? 0.3908 0.4671 0.6219 0.0621 -0.0754 -0.0715 460 TYR A CZ 3440 O OH . TYR A 467 ? 0.4358 0.5190 0.6870 0.0610 -0.0808 -0.0757 460 TYR A OH 3441 N N . THR A 468 ? 0.2743 0.3143 0.4121 0.0687 -0.0689 -0.0550 461 THR A N 3442 C CA . THR A 468 ? 0.2716 0.3081 0.4000 0.0699 -0.0754 -0.0554 461 THR A CA 3443 C C . THR A 468 ? 0.2766 0.3076 0.3872 0.0670 -0.0695 -0.0514 461 THR A C 3444 O O . THR A 468 ? 0.2674 0.2975 0.3737 0.0639 -0.0611 -0.0486 461 THR A O 3445 C CB . THR A 468 ? 0.2769 0.3204 0.4219 0.0668 -0.0794 -0.0598 461 THR A CB 3446 O OG1 . THR A 468 ? 0.2942 0.3335 0.4305 0.0699 -0.0881 -0.0612 461 THR A OG1 3447 C CG2 . THR A 468 ? 0.2586 0.3066 0.4091 0.0587 -0.0700 -0.0589 461 THR A CG2 3448 N N . LEU A 469 ? 0.2679 0.2950 0.3683 0.0683 -0.0745 -0.0515 462 LEU A N 3449 C CA . LEU A 469 ? 0.2741 0.2966 0.3591 0.0656 -0.0695 -0.0481 462 LEU A CA 3450 C C . LEU A 469 ? 0.2641 0.2917 0.3564 0.0581 -0.0631 -0.0484 462 LEU A C 3451 O O . LEU A 469 ? 0.2634 0.2972 0.3713 0.0554 -0.0647 -0.0516 462 LEU A O 3452 C CB . LEU A 469 ? 0.2791 0.2958 0.3512 0.0700 -0.0770 -0.0485 462 LEU A CB 3453 C CG . LEU A 469 ? 0.2807 0.2909 0.3339 0.0698 -0.0729 -0.0445 462 LEU A CG 3454 C CD1 . LEU A 469 ? 0.3120 0.3163 0.3531 0.0733 -0.0693 -0.0401 462 LEU A CD1 3455 C CD2 . LEU A 469 ? 0.2862 0.2922 0.3303 0.0740 -0.0812 -0.0464 462 LEU A CD2 3456 N N . ARG A 470 ? 0.2518 0.2765 0.3331 0.0550 -0.0560 -0.0448 463 ARG A N 3457 C CA . ARG A 470 ? 0.2558 0.2838 0.3402 0.0484 -0.0500 -0.0443 463 ARG A CA 3458 C C . ARG A 470 ? 0.2521 0.2743 0.3200 0.0484 -0.0493 -0.0415 463 ARG A C 3459 O O . ARG A 470 ? 0.2631 0.2804 0.3188 0.0501 -0.0464 -0.0383 463 ARG A O 3460 C CB . ARG A 470 ? 0.2599 0.2910 0.3491 0.0445 -0.0412 -0.0429 463 ARG A CB 3461 C CG . ARG A 470 ? 0.2874 0.3212 0.3781 0.0382 -0.0347 -0.0420 463 ARG A CG 3462 C CD . ARG A 470 ? 0.3337 0.3691 0.4257 0.0355 -0.0266 -0.0408 463 ARG A CD 3463 N NE . ARG A 470 ? 0.3158 0.3539 0.4093 0.0298 -0.0205 -0.0401 463 ARG A NE 3464 C CZ . ARG A 470 ? 0.3119 0.3502 0.4024 0.0270 -0.0133 -0.0388 463 ARG A CZ 3465 N NH1 . ARG A 470 ? 0.3411 0.3772 0.4280 0.0290 -0.0113 -0.0383 463 ARG A NH1 3466 N NH2 . ARG A 470 ? 0.2950 0.3352 0.3857 0.0224 -0.0084 -0.0380 463 ARG A NH2 3467 N N . VAL A 471 ? 0.2418 0.2644 0.3101 0.0467 -0.0519 -0.0428 464 VAL A N 3468 C CA . VAL A 471 ? 0.2377 0.2551 0.2913 0.0468 -0.0513 -0.0406 464 VAL A CA 3469 C C . VAL A 471 ? 0.2400 0.2602 0.2974 0.0406 -0.0466 -0.0401 464 VAL A C 3470 O O . VAL A 471 ? 0.2360 0.2607 0.3062 0.0378 -0.0480 -0.0427 464 VAL A O 3471 C CB . VAL A 471 ? 0.2588 0.2722 0.3061 0.0519 -0.0601 -0.0427 464 VAL A CB 3472 C CG1 . VAL A 471 ? 0.2587 0.2670 0.2914 0.0521 -0.0589 -0.0406 464 VAL A CG1 3473 C CG2 . VAL A 471 ? 0.2771 0.2870 0.3193 0.0588 -0.0653 -0.0430 464 VAL A CG2 3474 N N . ASP A 472 ? 0.2252 0.2429 0.2724 0.0386 -0.0411 -0.0368 465 ASP A N 3475 C CA . ASP A 472 ? 0.2346 0.2535 0.2820 0.0337 -0.0375 -0.0359 465 ASP A CA 3476 C C . ASP A 472 ? 0.2319 0.2454 0.2651 0.0359 -0.0386 -0.0341 465 ASP A C 3477 O O . ASP A 472 ? 0.2298 0.2397 0.2527 0.0383 -0.0367 -0.0316 465 ASP A O 3478 C CB . ASP A 472 ? 0.2362 0.2573 0.2842 0.0291 -0.0293 -0.0336 465 ASP A CB 3479 C CG . ASP A 472 ? 0.2769 0.3027 0.3361 0.0276 -0.0262 -0.0347 465 ASP A CG 3480 O OD1 . ASP A 472 ? 0.2859 0.3144 0.3553 0.0293 -0.0299 -0.0374 465 ASP A OD1 3481 O OD2 . ASP A 472 ? 0.3238 0.3506 0.3817 0.0247 -0.0199 -0.0332 465 ASP A OD2 3482 N N . CYS A 473 ? 0.2344 0.2471 0.2674 0.0348 -0.0411 -0.0352 466 CYS A N 3483 C CA . CYS A 473 ? 0.2405 0.2482 0.2603 0.0372 -0.0421 -0.0337 466 CYS A CA 3484 C C . CYS A 473 ? 0.2314 0.2388 0.2531 0.0348 -0.0436 -0.0349 466 CYS A C 3485 O O . CYS A 473 ? 0.2496 0.2603 0.2831 0.0319 -0.0452 -0.0371 466 CYS A O 3486 C CB . CYS A 473 ? 0.2470 0.2501 0.2583 0.0441 -0.0481 -0.0349 466 CYS A CB 3487 S SG . CYS A 473 ? 0.2690 0.2722 0.2878 0.0472 -0.0583 -0.0404 466 CYS A SG 3488 N N . THR A 474 ? 0.2305 0.2340 0.2412 0.0362 -0.0429 -0.0332 467 THR A N 3489 C CA . THR A 474 ? 0.2279 0.2299 0.2386 0.0352 -0.0453 -0.0345 467 THR A CA 3490 C C . THR A 474 ? 0.2435 0.2442 0.2584 0.0382 -0.0536 -0.0390 467 THR A C 3491 O O . THR A 474 ? 0.2524 0.2509 0.2628 0.0434 -0.0581 -0.0406 467 THR A O 3492 C CB . THR A 474 ? 0.2234 0.2211 0.2206 0.0376 -0.0436 -0.0323 467 THR A CB 3493 O OG1 . THR A 474 ? 0.2351 0.2307 0.2324 0.0373 -0.0468 -0.0342 467 THR A OG1 3494 C CG2 . THR A 474 ? 0.2458 0.2391 0.2314 0.0441 -0.0459 -0.0321 467 THR A CG2 3495 N N . PRO A 475 ? 0.2324 0.2339 0.2558 0.0353 -0.0559 -0.0412 468 PRO A N 3496 C CA . PRO A 475 ? 0.2503 0.2499 0.2775 0.0384 -0.0645 -0.0460 468 PRO A CA 3497 C C . PRO A 475 ? 0.2627 0.2562 0.2747 0.0451 -0.0692 -0.0472 468 PRO A C 3498 O O . PRO A 475 ? 0.2663 0.2578 0.2787 0.0494 -0.0769 -0.0513 468 PRO A O 3499 C CB . PRO A 475 ? 0.2594 0.2593 0.2949 0.0339 -0.0647 -0.0469 468 PRO A CB 3500 C CG . PRO A 475 ? 0.2561 0.2602 0.2972 0.0280 -0.0564 -0.0430 468 PRO A CG 3501 C CD . PRO A 475 ? 0.2290 0.2325 0.2582 0.0295 -0.0512 -0.0393 468 PRO A CD 3502 N N . LEU A 476 ? 0.2639 0.2542 0.2628 0.0464 -0.0647 -0.0439 469 LEU A N 3503 C CA . LEU A 476 ? 0.2692 0.2534 0.2528 0.0531 -0.0679 -0.0447 469 LEU A CA 3504 C C . LEU A 476 ? 0.2810 0.2635 0.2582 0.0587 -0.0708 -0.0450 469 LEU A C 3505 O O . LEU A 476 ? 0.2980 0.2752 0.2637 0.0650 -0.0755 -0.0468 469 LEU A O 3506 C CB . LEU A 476 ? 0.2691 0.2511 0.2414 0.0534 -0.0614 -0.0406 469 LEU A CB 3507 C CG . LEU A 476 ? 0.2735 0.2554 0.2489 0.0498 -0.0600 -0.0406 469 LEU A CG 3508 C CD1 . LEU A 476 ? 0.2924 0.2728 0.2577 0.0503 -0.0537 -0.0366 469 LEU A CD1 3509 C CD2 . LEU A 476 ? 0.2647 0.2425 0.2394 0.0529 -0.0678 -0.0457 469 LEU A CD2 3510 N N . MET A 477 ? 0.2707 0.2572 0.2546 0.0567 -0.0681 -0.0433 470 MET A N 3511 C CA . MET A 477 ? 0.2746 0.2592 0.2529 0.0620 -0.0706 -0.0432 470 MET A CA 3512 C C . MET A 477 ? 0.2881 0.2754 0.2781 0.0628 -0.0778 -0.0475 470 MET A C 3513 O O . MET A 477 ? 0.2831 0.2688 0.2693 0.0675 -0.0809 -0.0476 470 MET A O 3514 C CB . MET A 477 ? 0.2808 0.2671 0.2574 0.0603 -0.0628 -0.0382 470 MET A CB 3515 C CG . MET A 477 ? 0.2939 0.2768 0.2578 0.0612 -0.0565 -0.0339 470 MET A CG 3516 S SD . MET A 477 ? 0.3394 0.3250 0.3057 0.0583 -0.0485 -0.0292 470 MET A SD 3517 C CE . MET A 477 ? 0.3339 0.3170 0.2899 0.0575 -0.0411 -0.0248 470 MET A CE 3518 N N . TYR A 478 ? 0.2733 0.2643 0.2777 0.0587 -0.0809 -0.0509 471 TYR A N 3519 C CA . TYR A 478 ? 0.2848 0.2792 0.3028 0.0592 -0.0875 -0.0551 471 TYR A CA 3520 C C . TYR A 478 ? 0.3002 0.2897 0.3099 0.0671 -0.0971 -0.0588 471 TYR A C 3521 O O . TYR A 478 ? 0.3008 0.2917 0.3142 0.0701 -0.1010 -0.0600 471 TYR A O 3522 C CB . TYR A 478 ? 0.2762 0.2744 0.3108 0.0541 -0.0899 -0.0585 471 TYR A CB 3523 C CG . TYR A 478 ? 0.2668 0.2706 0.3134 0.0463 -0.0817 -0.0556 471 TYR A CG 3524 C CD1 . TYR A 478 ? 0.2588 0.2651 0.3029 0.0439 -0.0731 -0.0510 471 TYR A CD1 3525 C CD2 . TYR A 478 ? 0.2815 0.2878 0.3417 0.0415 -0.0825 -0.0576 471 TYR A CD2 3526 C CE1 . TYR A 478 ? 0.2882 0.2990 0.3418 0.0372 -0.0659 -0.0486 471 TYR A CE1 3527 C CE2 . TYR A 478 ? 0.2969 0.3076 0.3666 0.0349 -0.0749 -0.0548 471 TYR A CE2 3528 C CZ . TYR A 478 ? 0.3029 0.3158 0.3688 0.0329 -0.0667 -0.0504 471 TYR A CZ 3529 O OH . TYR A 478 ? 0.2830 0.2998 0.3571 0.0267 -0.0594 -0.0478 471 TYR A OH 3530 N N . SER A 479 ? 0.3070 0.2909 0.3055 0.0707 -0.1013 -0.0608 472 SER A N 3531 C CA . SER A 479 ? 0.3145 0.2930 0.3039 0.0786 -0.1114 -0.0651 472 SER A CA 3532 C C . SER A 479 ? 0.3312 0.3053 0.3042 0.0850 -0.1099 -0.0616 472 SER A C 3533 O O . SER A 479 ? 0.3343 0.3065 0.3051 0.0906 -0.1173 -0.0640 472 SER A O 3534 C CB . SER A 479 ? 0.3318 0.3048 0.3123 0.0810 -0.1154 -0.0681 472 SER A CB 3535 O OG A SER A 479 ? 0.3569 0.3335 0.3548 0.0757 -0.1187 -0.0722 472 SER A OG 3536 O OG B SER A 479 ? 0.3016 0.2688 0.2720 0.0891 -0.1256 -0.0729 472 SER A OG 3537 N N . LEU A 480 ? 0.3283 0.3006 0.2905 0.0841 -0.1006 -0.0558 473 LEU A N 3538 C CA . LEU A 480 ? 0.3465 0.3147 0.2945 0.0890 -0.0973 -0.0514 473 LEU A CA 3539 C C . LEU A 480 ? 0.3359 0.3082 0.2944 0.0885 -0.0980 -0.0508 473 LEU A C 3540 O O . LEU A 480 ? 0.3431 0.3117 0.2938 0.0949 -0.1024 -0.0507 473 LEU A O 3541 C CB . LEU A 480 ? 0.3417 0.3094 0.2825 0.0861 -0.0863 -0.0453 473 LEU A CB 3542 C CG . LEU A 480 ? 0.3537 0.3190 0.2854 0.0885 -0.0801 -0.0396 473 LEU A CG 3543 C CD1 . LEU A 480 ? 0.4125 0.3696 0.3254 0.0978 -0.0839 -0.0389 473 LEU A CD1 3544 C CD2 . LEU A 480 ? 0.3817 0.3482 0.3114 0.0840 -0.0698 -0.0346 473 LEU A CD2 3545 N N . VAL A 481 ? 0.3190 0.2987 0.2947 0.0812 -0.0938 -0.0505 474 VAL A N 3546 C CA . VAL A 481 ? 0.3139 0.2979 0.3007 0.0802 -0.0934 -0.0500 474 VAL A CA 3547 C C . VAL A 481 ? 0.3215 0.3066 0.3169 0.0840 -0.1043 -0.0556 474 VAL A C 3548 O O . VAL A 481 ? 0.3254 0.3096 0.3196 0.0885 -0.1073 -0.0553 474 VAL A O 3549 C CB . VAL A 481 ? 0.3097 0.3012 0.3124 0.0718 -0.0862 -0.0488 474 VAL A CB 3550 C CG1 . VAL A 481 ? 0.3295 0.3259 0.3456 0.0711 -0.0866 -0.0494 474 VAL A CG1 3551 C CG2 . VAL A 481 ? 0.3115 0.3018 0.3057 0.0689 -0.0760 -0.0432 474 VAL A CG2 3552 N N . HIS A 482 ? 0.3216 0.3089 0.3265 0.0822 -0.1102 -0.0606 475 HIS A N 3553 C CA . HIS A 482 ? 0.3452 0.3333 0.3587 0.0861 -0.1218 -0.0667 475 HIS A CA 3554 C C . HIS A 482 ? 0.3592 0.3393 0.3539 0.0959 -0.1290 -0.0673 475 HIS A C 3555 O O . HIS A 482 ? 0.3612 0.3415 0.3585 0.1003 -0.1348 -0.0687 475 HIS A O 3556 C CB . HIS A 482 ? 0.3393 0.3294 0.3640 0.0832 -0.1275 -0.0721 475 HIS A CB 3557 C CG . HIS A 482 ? 0.3815 0.3792 0.4258 0.0742 -0.1213 -0.0716 475 HIS A CG 3558 N ND1 . HIS A 482 ? 0.4380 0.4365 0.4894 0.0698 -0.1218 -0.0739 475 HIS A ND1 3559 C CD2 . HIS A 482 ? 0.3732 0.3774 0.4300 0.0690 -0.1139 -0.0688 475 HIS A CD2 3560 C CE1 . HIS A 482 ? 0.4366 0.4418 0.5041 0.0623 -0.1149 -0.0722 475 HIS A CE1 3561 N NE2 . HIS A 482 ? 0.3876 0.3964 0.4584 0.0618 -0.1100 -0.0693 475 HIS A NE2 3562 N N . ASN A 483 ? 0.3574 0.3303 0.3328 0.0994 -0.1282 -0.0661 476 ASN A N 3563 C CA . ASN A 483 ? 0.3799 0.3443 0.3355 0.1092 -0.1349 -0.0667 476 ASN A CA 3564 C C . ASN A 483 ? 0.3847 0.3462 0.3303 0.1132 -0.1308 -0.0612 476 ASN A C 3565 O O . ASN A 483 ? 0.3986 0.3563 0.3375 0.1204 -0.1384 -0.0626 476 ASN A O 3566 C CB . ASN A 483 ? 0.3852 0.3426 0.3220 0.1123 -0.1338 -0.0663 476 ASN A CB 3567 C CG . ASN A 483 ? 0.4098 0.3676 0.3533 0.1109 -0.1409 -0.0729 476 ASN A CG 3568 O OD1 . ASN A 483 ? 0.4120 0.3756 0.3751 0.1073 -0.1466 -0.0776 476 ASN A OD1 3569 N ND2 . ASN A 483 ? 0.4080 0.3596 0.3358 0.1138 -0.1402 -0.0731 476 ASN A ND2 3570 N N . LEU A 484 ? 0.3637 0.3266 0.3081 0.1087 -0.1193 -0.0551 477 LEU A N 3571 C CA . LEU A 484 ? 0.3617 0.3215 0.2977 0.1119 -0.1147 -0.0496 477 LEU A CA 3572 C C . LEU A 484 ? 0.3612 0.3255 0.3115 0.1122 -0.1190 -0.0512 477 LEU A C 3573 O O . LEU A 484 ? 0.3753 0.3348 0.3168 0.1192 -0.1230 -0.0500 477 LEU A O 3574 C CB . LEU A 484 ? 0.3530 0.3143 0.2881 0.1060 -0.1016 -0.0433 477 LEU A CB 3575 C CG . LEU A 484 ? 0.3762 0.3347 0.3054 0.1083 -0.0962 -0.0376 477 LEU A CG 3576 C CD1 . LEU A 484 ? 0.4086 0.3572 0.3159 0.1177 -0.0989 -0.0350 477 LEU A CD1 3577 C CD2 . LEU A 484 ? 0.3693 0.3299 0.3003 0.1018 -0.0841 -0.0325 477 LEU A CD2 3578 N N . THR A 485 ? 0.3472 0.3204 0.3194 0.1051 -0.1180 -0.0538 478 THR A N 3579 C CA . THR A 485 ? 0.3430 0.3215 0.3310 0.1049 -0.1208 -0.0553 478 THR A CA 3580 C C . THR A 485 ? 0.3655 0.3428 0.3560 0.1116 -0.1343 -0.0610 478 THR A C 3581 O O . THR A 485 ? 0.3566 0.3348 0.3525 0.1150 -0.1382 -0.0614 478 THR A O 3582 C CB . THR A 485 ? 0.3288 0.3172 0.3397 0.0958 -0.1156 -0.0565 478 THR A CB 3583 O OG1 . THR A 485 ? 0.3192 0.3114 0.3410 0.0924 -0.1200 -0.0615 478 THR A OG1 3584 C CG2 . THR A 485 ? 0.3049 0.2943 0.3131 0.0898 -0.1026 -0.0508 478 THR A CG2 3585 N N . LYS A 486 ? 0.3745 0.3491 0.3599 0.1140 -0.1419 -0.0655 479 LYS A N 3586 C CA . LYS A 486 ? 0.3980 0.3701 0.3826 0.1214 -0.1557 -0.0712 479 LYS A CA 3587 C C . LYS A 486 ? 0.4208 0.3833 0.3827 0.1314 -0.1592 -0.0682 479 LYS A C 3588 O O . LYS A 486 ? 0.4361 0.3968 0.3981 0.1381 -0.1701 -0.0718 479 LYS A O 3589 C CB . LYS A 486 ? 0.3987 0.3693 0.3827 0.1218 -0.1634 -0.0772 479 LYS A CB 3590 C CG . LYS A 486 ? 0.3972 0.3771 0.4069 0.1134 -0.1637 -0.0816 479 LYS A CG 3591 C CD . LYS A 486 ? 0.4233 0.4010 0.4319 0.1130 -0.1696 -0.0867 479 LYS A CD 3592 C CE . LYS A 486 ? 0.4453 0.4320 0.4798 0.1038 -0.1677 -0.0896 479 LYS A CE 3593 N NZ . LYS A 486 ? 0.4883 0.4729 0.5244 0.1031 -0.1741 -0.0951 479 LYS A NZ 3594 N N A GLU A 487 ? 0.4304 0.3867 0.3734 0.1324 -0.1499 -0.0616 480 GLU A N 3595 N N B GLU A 487 ? 0.4266 0.3829 0.3696 0.1326 -0.1500 -0.0615 480 GLU A N 3596 C CA A GLU A 487 ? 0.4622 0.4085 0.3816 0.1414 -0.1506 -0.0572 480 GLU A CA 3597 C CA B GLU A 487 ? 0.4548 0.4011 0.3747 0.1419 -0.1516 -0.0576 480 GLU A CA 3598 C C A GLU A 487 ? 0.4528 0.3994 0.3752 0.1420 -0.1458 -0.0521 480 GLU A C 3599 C C B GLU A 487 ? 0.4486 0.3945 0.3687 0.1417 -0.1439 -0.0511 480 GLU A C 3600 O O A GLU A 487 ? 0.4686 0.4076 0.3761 0.1501 -0.1489 -0.0494 480 GLU A O 3601 O O B GLU A 487 ? 0.4597 0.3970 0.3610 0.1486 -0.1429 -0.0463 480 GLU A O 3602 C CB A GLU A 487 ? 0.4723 0.4119 0.3712 0.1419 -0.1417 -0.0521 480 GLU A CB 3603 C CB B GLU A 487 ? 0.4691 0.4074 0.3660 0.1448 -0.1470 -0.0546 480 GLU A CB 3604 C CG A GLU A 487 ? 0.5459 0.4800 0.4306 0.1463 -0.1476 -0.0561 480 GLU A CG 3605 C CG B GLU A 487 ? 0.5083 0.4462 0.4040 0.1447 -0.1534 -0.0608 480 GLU A CG 3606 C CD A GLU A 487 ? 0.6056 0.5320 0.4677 0.1488 -0.1387 -0.0503 480 GLU A CD 3607 C CD B GLU A 487 ? 0.5594 0.4934 0.4502 0.1530 -0.1683 -0.0674 480 GLU A CD 3608 O OE1 A GLU A 487 ? 0.6289 0.5563 0.4902 0.1448 -0.1344 -0.0510 480 GLU A OE1 3609 O OE1 B GLU A 487 ? 0.5914 0.5197 0.4707 0.1609 -0.1730 -0.0658 480 GLU A OE1 3610 O OE2 A GLU A 487 ? 0.6628 0.5820 0.5083 0.1549 -0.1356 -0.0447 480 GLU A OE2 3611 O OE2 B GLU A 487 ? 0.5997 0.5360 0.4982 0.1516 -0.1758 -0.0743 480 GLU A OE2 3612 N N . LEU A 488 ? 0.4246 0.3793 0.3654 0.1337 -0.1381 -0.0507 481 LEU A N 3613 C CA . LEU A 488 ? 0.4199 0.3751 0.3648 0.1332 -0.1321 -0.0458 481 LEU A CA 3614 C C . LEU A 488 ? 0.4246 0.3853 0.3873 0.1345 -0.1396 -0.0497 481 LEU A C 3615 O O . LEU A 488 ? 0.4288 0.3969 0.4092 0.1314 -0.1455 -0.0559 481 LEU A O 3616 C CB . LEU A 488 ? 0.3977 0.3583 0.3520 0.1238 -0.1192 -0.0422 481 LEU A CB 3617 C CG . LEU A 488 ? 0.3998 0.3565 0.3400 0.1214 -0.1107 -0.0381 481 LEU A CG 3618 C CD1 . LEU A 488 ? 0.3506 0.3137 0.3028 0.1119 -0.0996 -0.0357 481 LEU A CD1 3619 C CD2 . LEU A 488 ? 0.4269 0.3731 0.3445 0.1283 -0.1077 -0.0320 481 LEU A CD2 3620 N N . LYS A 489 ? 0.4241 0.3813 0.3831 0.1387 -0.1386 -0.0459 482 LYS A N 3621 C CA . LYS A 489 ? 0.4432 0.4050 0.4184 0.1409 -0.1453 -0.0490 482 LYS A CA 3622 C C . LYS A 489 ? 0.4208 0.3927 0.4194 0.1321 -0.1379 -0.0496 482 LYS A C 3623 O O . LYS A 489 ? 0.4261 0.3980 0.4230 0.1270 -0.1266 -0.0449 482 LYS A O 3624 C CB . LYS A 489 ? 0.4616 0.4149 0.4234 0.1488 -0.1463 -0.0441 482 LYS A CB 3625 C CG . LYS A 489 ? 0.5423 0.4849 0.4800 0.1589 -0.1543 -0.0433 482 LYS A CG 3626 C CD . LYS A 489 ? 0.6266 0.5608 0.5522 0.1666 -0.1546 -0.0378 482 LYS A CD 3627 C CE . LYS A 489 ? 0.7237 0.6513 0.6374 0.1777 -0.1687 -0.0406 482 LYS A CE 3628 N NZ . LYS A 489 ? 0.7907 0.7122 0.6851 0.1823 -0.1742 -0.0427 482 LYS A NZ 3629 N N . SER A 490 ? 0.4004 0.3809 0.4209 0.1303 -0.1440 -0.0554 483 SER A N 3630 C CA . SER A 490 ? 0.3859 0.3754 0.4275 0.1232 -0.1366 -0.0556 483 SER A CA 3631 C C . SER A 490 ? 0.3851 0.3721 0.4264 0.1263 -0.1334 -0.0517 483 SER A C 3632 O O . SER A 490 ? 0.4006 0.3836 0.4383 0.1342 -0.1417 -0.0522 483 SER A O 3633 C CB . SER A 490 ? 0.3772 0.3770 0.4439 0.1204 -0.1431 -0.0626 483 SER A CB 3634 O OG . SER A 490 ? 0.3694 0.3772 0.4545 0.1140 -0.1346 -0.0621 483 SER A OG 3635 N N . PRO A 491 ? 0.3708 0.3599 0.4162 0.1205 -0.1218 -0.0481 484 PRO A N 3636 C CA . PRO A 491 ? 0.3705 0.3574 0.4178 0.1229 -0.1186 -0.0450 484 PRO A CA 3637 C C . PRO A 491 ? 0.3709 0.3675 0.4434 0.1209 -0.1201 -0.0495 484 PRO A C 3638 O O . PRO A 491 ? 0.3720 0.3681 0.4495 0.1227 -0.1176 -0.0478 484 PRO A O 3639 C CB . PRO A 491 ? 0.3521 0.3374 0.3936 0.1168 -0.1055 -0.0400 484 PRO A CB 3640 C CG . PRO A 491 ? 0.3377 0.3307 0.3886 0.1087 -0.1017 -0.0430 484 PRO A CG 3641 C CD . PRO A 491 ? 0.3616 0.3538 0.4079 0.1119 -0.1116 -0.0467 484 PRO A CD 3642 N N . ASP A 492 ? 0.3692 0.3747 0.4583 0.1171 -0.1236 -0.0550 485 ASP A N 3643 C CA . ASP A 492 ? 0.3703 0.3863 0.4849 0.1134 -0.1221 -0.0588 485 ASP A CA 3644 C C . ASP A 492 ? 0.3873 0.4048 0.5124 0.1205 -0.1327 -0.0622 485 ASP A C 3645 O O . ASP A 492 ? 0.3953 0.4091 0.5137 0.1268 -0.1440 -0.0643 485 ASP A O 3646 C CB . ASP A 492 ? 0.3534 0.3782 0.4834 0.1068 -0.1220 -0.0633 485 ASP A CB 3647 C CG . ASP A 492 ? 0.3480 0.3724 0.4702 0.0994 -0.1120 -0.0605 485 ASP A CG 3648 O OD1 . ASP A 492 ? 0.3741 0.3918 0.4795 0.0992 -0.1053 -0.0555 485 ASP A OD1 3649 O OD2 . ASP A 492 ? 0.3492 0.3801 0.4831 0.0939 -0.1109 -0.0635 485 ASP A OD2 3650 N N A GLU A 493 ? 0.3880 0.4110 0.5296 0.1197 -0.1292 -0.0629 486 GLU A N 3651 N N B GLU A 493 ? 0.3858 0.4088 0.5275 0.1197 -0.1291 -0.0630 486 GLU A N 3652 C CA A GLU A 493 ? 0.4081 0.4347 0.5648 0.1257 -0.1387 -0.0668 486 GLU A CA 3653 C CA B GLU A 493 ? 0.4012 0.4283 0.5589 0.1253 -0.1383 -0.0669 486 GLU A CA 3654 C C A GLU A 493 ? 0.4031 0.4385 0.5781 0.1241 -0.1468 -0.0734 486 GLU A C 3655 C C B GLU A 493 ? 0.4002 0.4356 0.5750 0.1240 -0.1468 -0.0734 486 GLU A C 3656 O O A GLU A 493 ? 0.3975 0.4404 0.5851 0.1164 -0.1411 -0.0753 486 GLU A O 3657 O O B GLU A 493 ? 0.3930 0.4355 0.5794 0.1164 -0.1414 -0.0753 486 GLU A O 3658 C CB A GLU A 493 ? 0.4049 0.4365 0.5772 0.1241 -0.1316 -0.0665 486 GLU A CB 3659 C CB B GLU A 493 ? 0.3941 0.4273 0.5692 0.1228 -0.1307 -0.0670 486 GLU A CB 3660 C CG A GLU A 493 ? 0.4505 0.4728 0.6070 0.1273 -0.1260 -0.0607 486 GLU A CG 3661 C CG B GLU A 493 ? 0.4166 0.4545 0.6097 0.1286 -0.1390 -0.0709 486 GLU A CG 3662 C CD A GLU A 493 ? 0.4788 0.4982 0.6243 0.1204 -0.1130 -0.0564 486 GLU A CD 3663 C CD B GLU A 493 ? 0.4327 0.4737 0.6375 0.1277 -0.1309 -0.0699 486 GLU A CD 3664 O OE1 A GLU A 493 ? 0.5298 0.5538 0.6774 0.1135 -0.1083 -0.0574 486 GLU A OE1 3665 O OE1 B GLU A 493 ? 0.4617 0.5009 0.6706 0.1346 -0.1365 -0.0702 486 GLU A OE1 3666 O OE2 A GLU A 493 ? 0.4990 0.5112 0.6338 0.1221 -0.1079 -0.0518 486 GLU A OE2 3667 O OE2 B GLU A 493 ? 0.4365 0.4812 0.6456 0.1204 -0.1191 -0.0689 486 GLU A OE2 3668 N N . GLY A 494 ? 0.4179 0.4518 0.5940 0.1315 -0.1603 -0.0767 487 GLY A N 3669 C CA . GLY A 494 ? 0.4175 0.4590 0.6110 0.1307 -0.1698 -0.0834 487 GLY A CA 3670 C C . GLY A 494 ? 0.4258 0.4618 0.6033 0.1311 -0.1754 -0.0844 487 GLY A C 3671 O O . GLY A 494 ? 0.4392 0.4792 0.6276 0.1320 -0.1855 -0.0902 487 GLY A O 3672 N N . PHE A 495 ? 0.4194 0.4464 0.5718 0.1306 -0.1689 -0.0789 488 PHE A N 3673 C CA . PHE A 495 ? 0.4225 0.4435 0.5576 0.1313 -0.1732 -0.0794 488 PHE A CA 3674 C C . PHE A 495 ? 0.4428 0.4509 0.5488 0.1398 -0.1773 -0.0753 488 PHE A C 3675 O O . PHE A 495 ? 0.4518 0.4532 0.5383 0.1400 -0.1762 -0.0734 488 PHE A O 3676 C CB . PHE A 495 ? 0.4034 0.4259 0.5351 0.1223 -0.1612 -0.0768 488 PHE A CB 3677 C CG . PHE A 495 ? 0.3812 0.4151 0.5385 0.1142 -0.1579 -0.0808 488 PHE A CG 3678 C CD1 . PHE A 495 ? 0.3884 0.4251 0.5526 0.1119 -0.1639 -0.0855 488 PHE A CD1 3679 C CD2 . PHE A 495 ? 0.3972 0.4388 0.5722 0.1091 -0.1486 -0.0799 488 PHE A CD2 3680 C CE1 . PHE A 495 ? 0.3975 0.4444 0.5862 0.1042 -0.1604 -0.0887 488 PHE A CE1 3681 C CE2 . PHE A 495 ? 0.3864 0.4384 0.5849 0.1018 -0.1448 -0.0832 488 PHE A CE2 3682 C CZ . PHE A 495 ? 0.3854 0.4400 0.5910 0.0992 -0.1505 -0.0873 488 PHE A CZ 3683 N N . GLU A 496 ? 0.4659 0.4702 0.5689 0.1470 -0.1814 -0.0736 489 GLU A N 3684 C CA . GLU A 496 ? 0.4956 0.4869 0.5705 0.1558 -0.1856 -0.0693 489 GLU A CA 3685 C C . GLU A 496 ? 0.5065 0.4933 0.5698 0.1614 -0.1981 -0.0735 489 GLU A C 3686 O O . GLU A 496 ? 0.5210 0.5138 0.6004 0.1629 -0.2093 -0.0806 489 GLU A O 3687 C CB . GLU A 496 ? 0.5171 0.5042 0.5901 0.1631 -0.1882 -0.0664 489 GLU A CB 3688 C CG . GLU A 496 ? 0.5533 0.5498 0.6534 0.1637 -0.1933 -0.0710 489 GLU A CG 3689 C CD . GLU A 496 ? 0.5164 0.5237 0.6397 0.1543 -0.1818 -0.0715 489 GLU A CD 3690 O OE1 . GLU A 496 ? 0.5368 0.5421 0.6576 0.1520 -0.1712 -0.0666 489 GLU A OE1 3691 O OE2 . GLU A 496 ? 0.5253 0.5430 0.6705 0.1495 -0.1842 -0.0773 489 GLU A OE2 3692 N N . GLY A 497 ? 0.5067 0.4833 0.5429 0.1641 -0.1959 -0.0695 490 GLY A N 3693 C CA . GLY A 497 ? 0.5195 0.4907 0.5414 0.1692 -0.2063 -0.0732 490 GLY A CA 3694 C C . GLY A 497 ? 0.5068 0.4840 0.5380 0.1620 -0.2059 -0.0781 490 GLY A C 3695 O O . GLY A 497 ? 0.5269 0.4999 0.5478 0.1659 -0.2149 -0.0821 490 GLY A O 3696 N N . LYS A 498 ? 0.4668 0.4531 0.5167 0.1518 -0.1956 -0.0778 491 LYS A N 3697 C CA . LYS A 498 ? 0.4536 0.4449 0.5116 0.1445 -0.1937 -0.0813 491 LYS A CA 3698 C C . LYS A 498 ? 0.4320 0.4190 0.4739 0.1396 -0.1804 -0.0750 491 LYS A C 3699 O O . LYS A 498 ? 0.4236 0.4066 0.4550 0.1400 -0.1717 -0.0686 491 LYS A O 3700 C CB . LYS A 498 ? 0.4457 0.4502 0.5361 0.1365 -0.1914 -0.0852 491 LYS A CB 3701 C CG . LYS A 498 ? 0.4777 0.4880 0.5883 0.1407 -0.2034 -0.0912 491 LYS A CG 3702 C CD . LYS A 498 ? 0.5479 0.5543 0.6529 0.1472 -0.2190 -0.0975 491 LYS A CD 3703 C CE . LYS A 498 ? 0.6073 0.6201 0.7342 0.1513 -0.2319 -0.1040 491 LYS A CE 3704 N NZ . LYS A 498 ? 0.6241 0.6504 0.7844 0.1423 -0.2271 -0.1071 491 LYS A NZ 3705 N N . SER A 499 ? 0.4207 0.4086 0.4616 0.1352 -0.1794 -0.0772 492 SER A N 3706 C CA . SER A 499 ? 0.4083 0.3930 0.4358 0.1302 -0.1674 -0.0720 492 SER A CA 3707 C C . SER A 499 ? 0.3814 0.3743 0.4254 0.1207 -0.1551 -0.0694 492 SER A C 3708 O O . SER A 499 ? 0.3584 0.3604 0.4261 0.1164 -0.1558 -0.0728 492 SER A O 3709 C CB . SER A 499 ? 0.4148 0.3979 0.4370 0.1288 -0.1709 -0.0756 492 SER A CB 3710 O OG . SER A 499 ? 0.4177 0.4105 0.4643 0.1212 -0.1710 -0.0802 492 SER A OG 3711 N N . LEU A 500 ? 0.3674 0.3567 0.3985 0.1175 -0.1439 -0.0634 493 LEU A N 3712 C CA . LEU A 500 ? 0.3468 0.3427 0.3901 0.1085 -0.1322 -0.0611 493 LEU A CA 3713 C C . LEU A 500 ? 0.3326 0.3355 0.3911 0.1016 -0.1325 -0.0654 493 LEU A C 3714 O O . LEU A 500 ? 0.3197 0.3308 0.3974 0.0951 -0.1274 -0.0664 493 LEU A O 3715 C CB . LEU A 500 ? 0.3381 0.3279 0.3630 0.1070 -0.1217 -0.0544 493 LEU A CB 3716 C CG . LEU A 500 ? 0.3297 0.3247 0.3628 0.0982 -0.1095 -0.0516 493 LEU A CG 3717 C CD1 . LEU A 500 ? 0.3208 0.3218 0.3709 0.0962 -0.1064 -0.0517 493 LEU A CD1 3718 C CD2 . LEU A 500 ? 0.3246 0.3129 0.3390 0.0979 -0.1011 -0.0455 493 LEU A CD2 3719 N N . TYR A 501 ? 0.3423 0.3415 0.3922 0.1033 -0.1383 -0.0681 494 TYR A N 3720 C CA . TYR A 501 ? 0.3444 0.3493 0.4091 0.0973 -0.1394 -0.0723 494 TYR A CA 3721 C C . TYR A 501 ? 0.3416 0.3553 0.4324 0.0956 -0.1453 -0.0776 494 TYR A C 3722 O O . TYR A 501 ? 0.3354 0.3567 0.4448 0.0882 -0.1403 -0.0786 494 TYR A O 3723 C CB . TYR A 501 ? 0.3595 0.3585 0.4119 0.1009 -0.1473 -0.0756 494 TYR A CB 3724 C CG . TYR A 501 ? 0.3546 0.3584 0.4214 0.0946 -0.1483 -0.0797 494 TYR A CG 3725 C CD1 . TYR A 501 ? 0.3432 0.3466 0.4055 0.0886 -0.1393 -0.0766 494 TYR A CD1 3726 C CD2 . TYR A 501 ? 0.3608 0.3693 0.4462 0.0947 -0.1583 -0.0864 494 TYR A CD2 3727 C CE1 . TYR A 501 ? 0.3589 0.3659 0.4341 0.0830 -0.1400 -0.0799 494 TYR A CE1 3728 C CE2 . TYR A 501 ? 0.3531 0.3654 0.4526 0.0887 -0.1588 -0.0898 494 TYR A CE2 3729 C CZ . TYR A 501 ? 0.3570 0.3682 0.4506 0.0831 -0.1496 -0.0864 494 TYR A CZ 3730 O OH . TYR A 501 ? 0.3846 0.3991 0.4920 0.0773 -0.1500 -0.0893 494 TYR A OH 3731 N N . GLU A 502 ? 0.3546 0.3672 0.4471 0.1027 -0.1559 -0.0809 495 GLU A N 3732 C CA . GLU A 502 ? 0.3592 0.3803 0.4776 0.1018 -0.1623 -0.0862 495 GLU A CA 3733 C C . GLU A 502 ? 0.3431 0.3722 0.4790 0.0965 -0.1527 -0.0838 495 GLU A C 3734 O O . GLU A 502 ? 0.3350 0.3729 0.4937 0.0904 -0.1505 -0.0864 495 GLU A O 3735 C CB . GLU A 502 ? 0.3789 0.3967 0.4944 0.1112 -0.1761 -0.0900 495 GLU A CB 3736 C CG . GLU A 502 ? 0.4102 0.4376 0.5546 0.1103 -0.1830 -0.0957 495 GLU A CG 3737 C CD . GLU A 502 ? 0.4861 0.5107 0.6294 0.1196 -0.1986 -0.1008 495 GLU A CD 3738 O OE1 . GLU A 502 ? 0.5231 0.5389 0.6462 0.1258 -0.2067 -0.1022 495 GLU A OE1 3739 O OE2 . GLU A 502 ? 0.5014 0.5327 0.6646 0.1208 -0.2029 -0.1035 495 GLU A OE2 3740 N N . SER A 503 ? 0.3447 0.3706 0.4698 0.0988 -0.1467 -0.0787 496 SER A N 3741 C CA . SER A 503 ? 0.3371 0.3698 0.4774 0.0946 -0.1380 -0.0769 496 SER A CA 3742 C C . SER A 503 ? 0.3278 0.3646 0.4730 0.0855 -0.1259 -0.0744 496 SER A C 3743 O O . SER A 503 ? 0.3157 0.3610 0.4815 0.0802 -0.1211 -0.0758 496 SER A O 3744 C CB . SER A 503 ? 0.3478 0.3754 0.4760 0.0995 -0.1350 -0.0724 496 SER A CB 3745 O OG . SER A 503 ? 0.3252 0.3451 0.4309 0.0992 -0.1279 -0.0668 496 SER A OG 3746 N N . TRP A 504 ? 0.3181 0.3488 0.4444 0.0840 -0.1211 -0.0709 497 TRP A N 3747 C CA . TRP A 504 ? 0.3152 0.3487 0.4435 0.0760 -0.1105 -0.0684 497 TRP A CA 3748 C C . TRP A 504 ? 0.3143 0.3543 0.4611 0.0707 -0.1123 -0.0725 497 TRP A C 3749 O O . TRP A 504 ? 0.3068 0.3532 0.4675 0.0642 -0.1043 -0.0718 497 TRP A O 3750 C CB . TRP A 504 ? 0.3179 0.3431 0.4224 0.0765 -0.1068 -0.0642 497 TRP A CB 3751 C CG . TRP A 504 ? 0.3021 0.3289 0.4055 0.0691 -0.0971 -0.0616 497 TRP A CG 3752 C CD1 . TRP A 504 ? 0.2763 0.3092 0.3917 0.0626 -0.0879 -0.0603 497 TRP A CD1 3753 C CD2 . TRP A 504 ? 0.3064 0.3279 0.3947 0.0681 -0.0956 -0.0598 497 TRP A CD2 3754 N NE1 . TRP A 504 ? 0.2679 0.2995 0.3762 0.0576 -0.0814 -0.0578 497 TRP A NE1 3755 C CE2 . TRP A 504 ? 0.2908 0.3157 0.3831 0.0608 -0.0859 -0.0574 497 TRP A CE2 3756 C CE3 . TRP A 504 ? 0.3246 0.3388 0.3959 0.0731 -0.1015 -0.0601 497 TRP A CE3 3757 C CZ2 . TRP A 504 ? 0.2904 0.3119 0.3716 0.0582 -0.0824 -0.0554 497 TRP A CZ2 3758 C CZ3 . TRP A 504 ? 0.3257 0.3365 0.3860 0.0705 -0.0974 -0.0581 497 TRP A CZ3 3759 C CH2 . TRP A 504 ? 0.2996 0.3143 0.3655 0.0630 -0.0881 -0.0557 497 TRP A CH2 3760 N N . THR A 505 ? 0.3241 0.3621 0.4709 0.0736 -0.1227 -0.0767 498 THR A N 3761 C CA . THR A 505 ? 0.3257 0.3691 0.4905 0.0687 -0.1251 -0.0807 498 THR A CA 3762 C C . THR A 505 ? 0.3302 0.3834 0.5228 0.0665 -0.1258 -0.0840 498 THR A C 3763 O O . THR A 505 ? 0.3189 0.3785 0.5285 0.0597 -0.1200 -0.0843 498 THR A O 3764 C CB . THR A 505 ? 0.3413 0.3795 0.4992 0.0731 -0.1372 -0.0851 498 THR A CB 3765 O OG1 A THR A 505 ? 0.3108 0.3410 0.4451 0.0739 -0.1342 -0.0818 498 THR A OG1 3766 C CG2 A THR A 505 ? 0.3248 0.3686 0.5042 0.0683 -0.1411 -0.0900 498 THR A CG2 3767 N N . LYS A 506 ? 0.3414 0.3957 0.5384 0.0723 -0.1324 -0.0860 499 LYS A N 3768 C CA . LYS A 506 ? 0.3556 0.4193 0.5788 0.0711 -0.1329 -0.0889 499 LYS A CA 3769 C C . LYS A 506 ? 0.3450 0.4141 0.5760 0.0651 -0.1187 -0.0849 499 LYS A C 3770 O O . LYS A 506 ? 0.3494 0.4267 0.6023 0.0598 -0.1144 -0.0864 499 LYS A O 3771 C CB . LYS A 506 ? 0.3692 0.4316 0.5918 0.0794 -0.1423 -0.0910 499 LYS A CB 3772 C CG . LYS A 506 ? 0.4248 0.4962 0.6756 0.0802 -0.1492 -0.0965 499 LYS A CG 3773 C CD . LYS A 506 ? 0.4920 0.5732 0.7650 0.0743 -0.1385 -0.0955 499 LYS A CD 3774 C CE . LYS A 506 ? 0.5221 0.6126 0.8242 0.0761 -0.1460 -0.1011 499 LYS A CE 3775 N NZ . LYS A 506 ? 0.5473 0.6424 0.8683 0.0729 -0.1529 -0.1063 499 LYS A NZ 3776 N N . LYS A 507 ? 0.3430 0.4071 0.5556 0.0660 -0.1114 -0.0799 500 LYS A N 3777 C CA . LYS A 507 ? 0.3330 0.4011 0.5503 0.0616 -0.0988 -0.0765 500 LYS A CA 3778 C C . LYS A 507 ? 0.3315 0.4006 0.5470 0.0539 -0.0884 -0.0737 500 LYS A C 3779 O O . LYS A 507 ? 0.3300 0.4046 0.5560 0.0493 -0.0789 -0.0723 500 LYS A O 3780 C CB . LYS A 507 ? 0.3380 0.4000 0.5374 0.0658 -0.0959 -0.0728 500 LYS A CB 3781 C CG . LYS A 507 ? 0.3254 0.3876 0.5302 0.0731 -0.1041 -0.0751 500 LYS A CG 3782 C CD . LYS A 507 ? 0.3208 0.3763 0.5083 0.0772 -0.1008 -0.0709 500 LYS A CD 3783 C CE . LYS A 507 ? 0.3576 0.4137 0.5522 0.0840 -0.1076 -0.0727 500 LYS A CE 3784 N NZ . LYS A 507 ? 0.3542 0.4031 0.5324 0.0875 -0.1035 -0.0682 500 LYS A NZ 3785 N N . SER A 508 ? 0.3278 0.3913 0.5293 0.0530 -0.0903 -0.0727 501 SER A N 3786 C CA . SER A 508 ? 0.3306 0.3934 0.5266 0.0466 -0.0812 -0.0695 501 SER A CA 3787 C C . SER A 508 ? 0.3409 0.4023 0.5384 0.0447 -0.0867 -0.0716 501 SER A C 3788 O O . SER A 508 ? 0.3304 0.3851 0.5101 0.0454 -0.0878 -0.0700 501 SER A O 3789 C CB . SER A 508 ? 0.3245 0.3802 0.4967 0.0475 -0.0758 -0.0647 501 SER A CB 3790 O OG . SER A 508 ? 0.3581 0.4143 0.5273 0.0413 -0.0662 -0.0616 501 SER A OG 3791 N N . PRO A 509 ? 0.3495 0.4172 0.5694 0.0424 -0.0903 -0.0756 502 PRO A N 3792 C CA . PRO A 509 ? 0.3604 0.4264 0.5834 0.0410 -0.0967 -0.0783 502 PRO A CA 3793 C C . PRO A 509 ? 0.3725 0.4365 0.5891 0.0349 -0.0883 -0.0747 502 PRO A C 3794 O O . PRO A 509 ? 0.3568 0.4243 0.5775 0.0301 -0.0775 -0.0713 502 PRO A O 3795 C CB . PRO A 509 ? 0.3673 0.4416 0.6191 0.0392 -0.1009 -0.0830 502 PRO A CB 3796 C CG . PRO A 509 ? 0.3546 0.4358 0.6188 0.0370 -0.0917 -0.0810 502 PRO A CG 3797 C CD . PRO A 509 ? 0.3449 0.4215 0.5891 0.0412 -0.0888 -0.0778 502 PRO A CD 3798 N N . SER A 510 ? 0.3993 0.4574 0.6050 0.0357 -0.0934 -0.0755 503 SER A N 3799 C CA . SER A 510 ? 0.4387 0.4949 0.6414 0.0302 -0.0877 -0.0730 503 SER A CA 3800 C C . SER A 510 ? 0.4590 0.5222 0.6862 0.0239 -0.0836 -0.0738 503 SER A C 3801 O O . SER A 510 ? 0.4622 0.5299 0.7090 0.0244 -0.0903 -0.0784 503 SER A O 3802 C CB . SER A 510 ? 0.4374 0.4867 0.6290 0.0329 -0.0962 -0.0754 503 SER A CB 3803 O OG . SER A 510 ? 0.4689 0.5175 0.6649 0.0275 -0.0929 -0.0745 503 SER A OG 3804 N N . PRO A 511 ? 0.4824 0.5466 0.7091 0.0182 -0.0725 -0.0693 504 PRO A N 3805 C CA . PRO A 511 ? 0.5057 0.5753 0.7541 0.0121 -0.0680 -0.0694 504 PRO A CA 3806 C C . PRO A 511 ? 0.5272 0.5940 0.7823 0.0103 -0.0746 -0.0721 504 PRO A C 3807 O O . PRO A 511 ? 0.5338 0.6054 0.8117 0.0067 -0.0752 -0.0742 504 PRO A O 3808 C CB . PRO A 511 ? 0.5016 0.5710 0.7421 0.0075 -0.0548 -0.0633 504 PRO A CB 3809 C CG . PRO A 511 ? 0.4962 0.5588 0.7105 0.0105 -0.0543 -0.0607 504 PRO A CG 3810 C CD . PRO A 511 ? 0.4835 0.5439 0.6903 0.0172 -0.0637 -0.0640 504 PRO A CD 3811 N N A GLU A 512 ? 0.5402 0.5992 0.7761 0.0128 -0.0792 -0.0720 505 GLU A N 3812 N N B GLU A 512 ? 0.5388 0.5979 0.7750 0.0129 -0.0796 -0.0722 505 GLU A N 3813 C CA A GLU A 512 ? 0.5507 0.6059 0.7906 0.0114 -0.0854 -0.0747 505 GLU A CA 3814 C CA B GLU A 512 ? 0.5492 0.6045 0.7893 0.0113 -0.0852 -0.0746 505 GLU A CA 3815 C C A GLU A 512 ? 0.5582 0.6132 0.8061 0.0162 -0.0994 -0.0818 505 GLU A C 3816 C C B GLU A 512 ? 0.5575 0.6100 0.7989 0.0166 -0.0996 -0.0813 505 GLU A C 3817 O O A GLU A 512 ? 0.5602 0.6175 0.8281 0.0137 -0.1044 -0.0856 505 GLU A O 3818 O O B GLU A 512 ? 0.5602 0.6107 0.8104 0.0150 -0.1052 -0.0845 505 GLU A O 3819 C CB A GLU A 512 ? 0.5552 0.6023 0.7718 0.0120 -0.0839 -0.0717 505 GLU A CB 3820 C CB B GLU A 512 ? 0.5520 0.6004 0.7724 0.0097 -0.0802 -0.0703 505 GLU A CB 3821 C CG A GLU A 512 ? 0.5600 0.6066 0.7677 0.0076 -0.0712 -0.0650 505 GLU A CG 3822 C CG B GLU A 512 ? 0.5699 0.6123 0.7880 0.0101 -0.0876 -0.0732 505 GLU A CG 3823 C CD A GLU A 512 ? 0.5708 0.6145 0.7560 0.0109 -0.0675 -0.0617 505 GLU A CD 3824 C CD B GLU A 512 ? 0.5902 0.6330 0.8221 0.0035 -0.0829 -0.0715 505 GLU A CD 3825 O OE1 A GLU A 512 ? 0.5829 0.6274 0.7624 0.0078 -0.0576 -0.0568 505 GLU A OE1 3826 O OE1 B GLU A 512 ? 0.5918 0.6330 0.8155 -0.0001 -0.0733 -0.0658 505 GLU A OE1 3827 O OE2 A GLU A 512 ? 0.5748 0.6150 0.7478 0.0167 -0.0744 -0.0639 505 GLU A OE2 3828 O OE2 B GLU A 512 ? 0.6034 0.6475 0.8541 0.0019 -0.0891 -0.0758 505 GLU A OE2 3829 N N . PHE A 513 ? 0.5582 0.6101 0.7908 0.0230 -0.1056 -0.0834 506 PHE A N 3830 C CA . PHE A 513 ? 0.5669 0.6156 0.7986 0.0289 -0.1198 -0.0899 506 PHE A CA 3831 C C . PHE A 513 ? 0.5574 0.6101 0.7963 0.0340 -0.1267 -0.0934 506 PHE A C 3832 O O . PHE A 513 ? 0.5526 0.6053 0.7802 0.0372 -0.1233 -0.0906 506 PHE A O 3833 C CB . PHE A 513 ? 0.5838 0.6230 0.7881 0.0339 -0.1235 -0.0894 506 PHE A CB 3834 C CG . PHE A 513 ? 0.6020 0.6366 0.7983 0.0299 -0.1183 -0.0866 506 PHE A CG 3835 C CD1 . PHE A 513 ? 0.6190 0.6509 0.7978 0.0285 -0.1083 -0.0803 506 PHE A CD1 3836 C CD2 . PHE A 513 ? 0.6208 0.6533 0.8273 0.0278 -0.1241 -0.0905 506 PHE A CD2 3837 C CE1 . PHE A 513 ? 0.6226 0.6502 0.7940 0.0252 -0.1040 -0.0778 506 PHE A CE1 3838 C CE2 . PHE A 513 ? 0.6344 0.6622 0.8336 0.0244 -0.1195 -0.0878 506 PHE A CE2 3839 C CZ . PHE A 513 ? 0.6378 0.6632 0.8192 0.0232 -0.1095 -0.0814 506 PHE A CZ 3840 N N . SER A 514 ? 0.5523 0.6079 0.8101 0.0350 -0.1370 -0.0998 507 SER A N 3841 C CA . SER A 514 ? 0.5349 0.5941 0.8009 0.0404 -0.1454 -0.1039 507 SER A CA 3842 C C . SER A 514 ? 0.5189 0.5701 0.7586 0.0490 -0.1532 -0.1048 507 SER A C 3843 O O . SER A 514 ? 0.5291 0.5727 0.7537 0.0516 -0.1588 -0.1066 507 SER A O 3844 C CB . SER A 514 ? 0.5469 0.6106 0.8393 0.0397 -0.1561 -0.1111 507 SER A CB 3845 O OG . SER A 514 ? 0.5660 0.6376 0.8844 0.0318 -0.1481 -0.1098 507 SER A OG 3846 N N . GLY A 515 ? 0.4834 0.5358 0.7172 0.0535 -0.1530 -0.1034 508 GLY A N 3847 C CA . GLY A 515 ? 0.4513 0.4962 0.6621 0.0624 -0.1609 -0.1043 508 GLY A CA 3848 C C . GLY A 515 ? 0.4247 0.4624 0.6073 0.0636 -0.1529 -0.0981 508 GLY A C 3849 O O . GLY A 515 ? 0.4267 0.4571 0.5879 0.0708 -0.1582 -0.0981 508 GLY A O 3850 N N A MET A 516 ? 0.4042 0.4439 0.5872 0.0568 -0.1403 -0.0930 509 MET A N 3851 N N B MET A 516 ? 0.4048 0.4444 0.5875 0.0569 -0.1404 -0.0930 509 MET A N 3852 C CA A MET A 516 ? 0.3918 0.4261 0.5517 0.0567 -0.1312 -0.0868 509 MET A CA 3853 C CA B MET A 516 ? 0.3933 0.4275 0.5526 0.0573 -0.1318 -0.0869 509 MET A CA 3854 C C A MET A 516 ? 0.3737 0.4127 0.5365 0.0535 -0.1199 -0.0817 509 MET A C 3855 C C B MET A 516 ? 0.3745 0.4134 0.5372 0.0537 -0.1202 -0.0818 509 MET A C 3856 O O A MET A 516 ? 0.3687 0.4153 0.5520 0.0485 -0.1155 -0.0819 509 MET A O 3857 O O B MET A 516 ? 0.3700 0.4166 0.5535 0.0489 -0.1161 -0.0821 509 MET A O 3858 C CB A MET A 516 ? 0.3884 0.4203 0.5448 0.0514 -0.1262 -0.0851 509 MET A CB 3859 C CB B MET A 516 ? 0.3917 0.4220 0.5432 0.0534 -0.1279 -0.0853 509 MET A CB 3860 C CG A MET A 516 ? 0.4136 0.4421 0.5731 0.0527 -0.1363 -0.0907 509 MET A CG 3861 C CG B MET A 516 ? 0.4243 0.4478 0.5662 0.0581 -0.1385 -0.0899 509 MET A CG 3862 S SD A MET A 516 ? 0.4697 0.4877 0.6015 0.0623 -0.1456 -0.0927 509 MET A SD 3863 S SD B MET A 516 ? 0.4585 0.4780 0.5948 0.0531 -0.1339 -0.0884 509 MET A SD 3864 C CE A MET A 516 ? 0.4579 0.4710 0.5673 0.0603 -0.1334 -0.0853 509 MET A CE 3865 C CE B MET A 516 ? 0.4642 0.4766 0.5936 0.0596 -0.1487 -0.0958 509 MET A CE 3866 N N . PRO A 517 ? 0.3617 0.3960 0.5043 0.0562 -0.1148 -0.0771 510 PRO A N 3867 C CA . PRO A 517 ? 0.3460 0.3838 0.4899 0.0531 -0.1041 -0.0724 510 PRO A CA 3868 C C . PRO A 517 ? 0.3293 0.3680 0.4715 0.0461 -0.0932 -0.0684 510 PRO A C 3869 O O . PRO A 517 ? 0.3339 0.3686 0.4677 0.0447 -0.0933 -0.0678 510 PRO A O 3870 C CB . PRO A 517 ? 0.3412 0.3725 0.4636 0.0591 -0.1042 -0.0694 510 PRO A CB 3871 C CG . PRO A 517 ? 0.3489 0.3725 0.4536 0.0623 -0.1089 -0.0698 510 PRO A CG 3872 C CD . PRO A 517 ? 0.3676 0.3930 0.4858 0.0627 -0.1190 -0.0761 510 PRO A CD 3873 N N A ARG A 518 ? 0.3190 0.3626 0.4686 0.0423 -0.0842 -0.0656 511 ARG A N 3874 N N B ARG A 518 ? 0.3211 0.3647 0.4708 0.0422 -0.0841 -0.0656 511 ARG A N 3875 C CA A ARG A 518 ? 0.3060 0.3500 0.4517 0.0364 -0.0735 -0.0614 511 ARG A CA 3876 C CA B ARG A 518 ? 0.3107 0.3546 0.4565 0.0363 -0.0738 -0.0615 511 ARG A CA 3877 C C A ARG A 518 ? 0.3043 0.3416 0.4270 0.0383 -0.0702 -0.0574 511 ARG A C 3878 C C B ARG A 518 ? 0.3069 0.3443 0.4300 0.0382 -0.0701 -0.0574 511 ARG A C 3879 O O A ARG A 518 ? 0.2963 0.3312 0.4098 0.0424 -0.0703 -0.0561 511 ARG A O 3880 O O B ARG A 518 ? 0.2988 0.3341 0.4133 0.0421 -0.0699 -0.0561 511 ARG A O 3881 C CB A ARG A 518 ? 0.3137 0.3641 0.4718 0.0328 -0.0652 -0.0599 511 ARG A CB 3882 C CB B ARG A 518 ? 0.3194 0.3701 0.4788 0.0322 -0.0653 -0.0601 511 ARG A CB 3883 C CG A ARG A 518 ? 0.3180 0.3685 0.4701 0.0275 -0.0542 -0.0555 511 ARG A CG 3884 C CG B ARG A 518 ? 0.3369 0.3877 0.4918 0.0265 -0.0547 -0.0559 511 ARG A CG 3885 C CD A ARG A 518 ? 0.3653 0.4218 0.5289 0.0247 -0.0462 -0.0546 511 ARG A CD 3886 C CD B ARG A 518 ? 0.3911 0.4490 0.5619 0.0224 -0.0471 -0.0555 511 ARG A CD 3887 N NE A ARG A 518 ? 0.3651 0.4285 0.5514 0.0220 -0.0465 -0.0573 511 ARG A NE 3888 N NE B ARG A 518 ? 0.4135 0.4727 0.5822 0.0246 -0.0434 -0.0546 511 ARG A NE 3889 C CZ A ARG A 518 ? 0.3865 0.4525 0.5822 0.0166 -0.0418 -0.0564 511 ARG A CZ 3890 C CZ B ARG A 518 ? 0.4252 0.4830 0.5836 0.0230 -0.0352 -0.0513 511 ARG A CZ 3891 N NH1 A ARG A 518 ? 0.4056 0.4676 0.5894 0.0135 -0.0370 -0.0530 511 ARG A NH1 3892 N NH1 B ARG A 518 ? 0.4376 0.4929 0.5868 0.0193 -0.0300 -0.0483 511 ARG A NH1 3893 N NH2 A ARG A 518 ? 0.3996 0.4720 0.6174 0.0144 -0.0418 -0.0587 511 ARG A NH2 3894 N NH2 B ARG A 518 ? 0.4459 0.5047 0.6038 0.0252 -0.0325 -0.0511 511 ARG A NH2 3895 N N . ILE A 519 ? 0.2922 0.3264 0.4065 0.0355 -0.0673 -0.0555 512 ILE A N 3896 C CA . ILE A 519 ? 0.2902 0.3194 0.3857 0.0359 -0.0621 -0.0513 512 ILE A CA 3897 C C . ILE A 519 ? 0.2914 0.3225 0.3886 0.0295 -0.0536 -0.0483 512 ILE A C 3898 O O . ILE A 519 ? 0.3025 0.3342 0.4058 0.0263 -0.0542 -0.0491 512 ILE A O 3899 C CB . ILE A 519 ? 0.3010 0.3233 0.3808 0.0401 -0.0677 -0.0516 512 ILE A CB 3900 C CG1 . ILE A 519 ? 0.3001 0.3196 0.3760 0.0471 -0.0765 -0.0544 512 ILE A CG1 3901 C CG2 . ILE A 519 ? 0.2801 0.2981 0.3428 0.0398 -0.0612 -0.0469 512 ILE A CG2 3902 C CD1 . ILE A 519 ? 0.3255 0.3376 0.3848 0.0522 -0.0822 -0.0551 512 ILE A CD1 3903 N N . SER A 520 ? 0.2826 0.3142 0.3742 0.0279 -0.0461 -0.0450 513 SER A N 3904 C CA . SER A 520 ? 0.2832 0.3164 0.3754 0.0223 -0.0381 -0.0423 513 SER A CA 3905 C C . SER A 520 ? 0.2732 0.3015 0.3503 0.0219 -0.0362 -0.0395 513 SER A C 3906 O O . SER A 520 ? 0.2623 0.2861 0.3271 0.0259 -0.0390 -0.0389 513 SER A O 3907 C CB . SER A 520 ? 0.2908 0.3273 0.3857 0.0207 -0.0310 -0.0408 513 SER A CB 3908 O OG . SER A 520 ? 0.3506 0.3921 0.4609 0.0211 -0.0324 -0.0435 513 SER A OG 3909 N N A LYS A 521 ? 0.2739 0.3032 0.3524 0.0172 -0.0310 -0.0375 514 LYS A N 3910 N N B LYS A 521 ? 0.2596 0.2887 0.3377 0.0173 -0.0313 -0.0375 514 LYS A N 3911 C CA A LYS A 521 ? 0.2659 0.2916 0.3316 0.0159 -0.0277 -0.0344 514 LYS A CA 3912 C CA B LYS A 521 ? 0.2429 0.2680 0.3076 0.0166 -0.0287 -0.0346 514 LYS A CA 3913 C C A LYS A 521 ? 0.2583 0.2832 0.3150 0.0169 -0.0234 -0.0323 514 LYS A C 3914 C C B LYS A 521 ? 0.2447 0.2696 0.3015 0.0167 -0.0234 -0.0323 514 LYS A C 3915 O O A LYS A 521 ? 0.2643 0.2922 0.3262 0.0164 -0.0203 -0.0326 514 LYS A O 3916 O O B LYS A 521 ? 0.2471 0.2752 0.3098 0.0157 -0.0199 -0.0325 514 LYS A O 3917 C CB A LYS A 521 ? 0.2688 0.2963 0.3393 0.0106 -0.0224 -0.0326 514 LYS A CB 3918 C CB B LYS A 521 ? 0.2371 0.2628 0.3053 0.0118 -0.0252 -0.0331 514 LYS A CB 3919 C CG A LYS A 521 ? 0.2937 0.3223 0.3761 0.0087 -0.0255 -0.0344 514 LYS A CG 3920 C CG B LYS A 521 ? 0.1999 0.2297 0.2749 0.0079 -0.0181 -0.0317 514 LYS A CG 3921 C CD A LYS A 521 ? 0.3326 0.3610 0.4166 0.0040 -0.0205 -0.0318 514 LYS A CD 3922 C CD B LYS A 521 ? 0.1849 0.2143 0.2616 0.0036 -0.0145 -0.0296 514 LYS A CD 3923 C CE A LYS A 521 ? 0.3346 0.3667 0.4230 0.0007 -0.0126 -0.0298 514 LYS A CE 3924 C CE B LYS A 521 ? 0.2106 0.2408 0.2998 0.0023 -0.0184 -0.0315 514 LYS A CE 3925 N NZ A LYS A 521 ? 0.3576 0.3946 0.4630 -0.0004 -0.0124 -0.0320 514 LYS A NZ 3926 N NZ B LYS A 521 ? 0.1966 0.2321 0.3015 0.0011 -0.0171 -0.0333 514 LYS A NZ 3927 N N . LEU A 522 ? 0.2429 0.2639 0.2871 0.0181 -0.0229 -0.0302 515 LEU A N 3928 C CA . LEU A 522 ? 0.2527 0.2730 0.2895 0.0178 -0.0181 -0.0279 515 LEU A CA 3929 C C . LEU A 522 ? 0.2555 0.2781 0.2946 0.0132 -0.0122 -0.0266 515 LEU A C 3930 O O . LEU A 522 ? 0.2724 0.2950 0.3121 0.0105 -0.0114 -0.0257 515 LEU A O 3931 C CB . LEU A 522 ? 0.2501 0.2660 0.2746 0.0199 -0.0187 -0.0260 515 LEU A CB 3932 C CG . LEU A 522 ? 0.2544 0.2672 0.2740 0.0253 -0.0233 -0.0267 515 LEU A CG 3933 C CD1 . LEU A 522 ? 0.2748 0.2834 0.2833 0.0273 -0.0239 -0.0250 515 LEU A CD1 3934 C CD2 . LEU A 522 ? 0.2644 0.2773 0.2837 0.0271 -0.0216 -0.0262 515 LEU A CD2 3935 N N . GLY A 523 ? 0.2526 0.2771 0.2932 0.0125 -0.0082 -0.0265 516 GLY A N 3936 C CA . GLY A 523 ? 0.2542 0.2799 0.2931 0.0090 -0.0024 -0.0252 516 GLY A CA 3937 C C . GLY A 523 ? 0.2670 0.2899 0.2958 0.0096 -0.0010 -0.0236 516 GLY A C 3938 O O . GLY A 523 ? 0.2717 0.2918 0.2939 0.0107 -0.0031 -0.0223 516 GLY A O 3939 N N . SER A 524 ? 0.2451 0.2687 0.2729 0.0087 0.0029 -0.0237 517 SER A N 3940 C CA . SER A 524 ? 0.2494 0.2703 0.2692 0.0092 0.0039 -0.0225 517 SER A CA 3941 C C . SER A 524 ? 0.2306 0.2521 0.2524 0.0096 0.0065 -0.0238 517 SER A C 3942 O O . SER A 524 ? 0.2394 0.2629 0.2682 0.0105 0.0066 -0.0255 517 SER A O 3943 C CB . SER A 524 ? 0.2449 0.2651 0.2589 0.0065 0.0057 -0.0210 517 SER A CB 3944 O OG . SER A 524 ? 0.2606 0.2787 0.2689 0.0072 0.0059 -0.0201 517 SER A OG 3945 N N . GLY A 525 ? 0.2215 0.2410 0.2380 0.0091 0.0082 -0.0233 518 GLY A N 3946 C CA . GLY A 525 ? 0.2220 0.2410 0.2403 0.0099 0.0101 -0.0247 518 GLY A CA 3947 C C . GLY A 525 ? 0.2240 0.2402 0.2414 0.0131 0.0080 -0.0238 518 GLY A C 3948 O O . GLY A 525 ? 0.2182 0.2333 0.2379 0.0143 0.0091 -0.0247 518 GLY A O 3949 N N . ASN A 526 ? 0.2151 0.2295 0.2287 0.0146 0.0053 -0.0218 519 ASN A N 3950 C CA . ASN A 526 ? 0.2257 0.2366 0.2367 0.0178 0.0040 -0.0202 519 ASN A CA 3951 C C . ASN A 526 ? 0.2126 0.2213 0.2174 0.0184 0.0032 -0.0177 519 ASN A C 3952 O O . ASN A 526 ? 0.2064 0.2165 0.2094 0.0165 0.0029 -0.0175 519 ASN A O 3953 C CB . ASN A 526 ? 0.2323 0.2429 0.2467 0.0214 0.0011 -0.0209 519 ASN A CB 3954 C CG . ASN A 526 ? 0.2695 0.2771 0.2841 0.0239 0.0019 -0.0204 519 ASN A CG 3955 O OD1 . ASN A 526 ? 0.2624 0.2663 0.2721 0.0253 0.0025 -0.0179 519 ASN A OD1 3956 N ND2 . ASN A 526 ? 0.2312 0.2403 0.2523 0.0245 0.0023 -0.0225 519 ASN A ND2 3957 N N . ASP A 527 ? 0.2034 0.2086 0.2050 0.0212 0.0031 -0.0157 520 ASP A N 3958 C CA . ASP A 527 ? 0.2089 0.2121 0.2055 0.0214 0.0040 -0.0131 520 ASP A CA 3959 C C . ASP A 527 ? 0.2091 0.2118 0.2012 0.0232 0.0015 -0.0122 520 ASP A C 3960 O O . ASP A 527 ? 0.2217 0.2234 0.2102 0.0232 0.0025 -0.0104 520 ASP A O 3961 C CB . ASP A 527 ? 0.2024 0.2016 0.1974 0.0239 0.0058 -0.0107 520 ASP A CB 3962 C CG . ASP A 527 ? 0.2177 0.2167 0.2170 0.0215 0.0086 -0.0114 520 ASP A CG 3963 O OD1 . ASP A 527 ? 0.2066 0.2074 0.2069 0.0180 0.0099 -0.0121 520 ASP A OD1 3964 O OD2 . ASP A 527 ? 0.2404 0.2370 0.2418 0.0232 0.0093 -0.0113 520 ASP A OD2 3965 N N . PHE A 528 ? 0.2183 0.2222 0.2117 0.0244 -0.0017 -0.0139 521 PHE A N 3966 C CA . PHE A 528 ? 0.2187 0.2222 0.2086 0.0254 -0.0043 -0.0138 521 PHE A CA 3967 C C . PHE A 528 ? 0.2185 0.2246 0.2094 0.0216 -0.0035 -0.0142 521 PHE A C 3968 O O . PHE A 528 ? 0.2121 0.2174 0.2000 0.0223 -0.0054 -0.0139 521 PHE A O 3969 C CB . PHE A 528 ? 0.2341 0.2380 0.2262 0.0277 -0.0087 -0.0160 521 PHE A CB 3970 C CG . PHE A 528 ? 0.2181 0.2259 0.2186 0.0248 -0.0088 -0.0184 521 PHE A CG 3971 C CD1 . PHE A 528 ? 0.2233 0.2337 0.2269 0.0213 -0.0085 -0.0193 521 PHE A CD1 3972 C CD2 . PHE A 528 ? 0.2438 0.2524 0.2492 0.0256 -0.0084 -0.0196 521 PHE A CD2 3973 C CE1 . PHE A 528 ? 0.2120 0.2260 0.2235 0.0186 -0.0075 -0.0211 521 PHE A CE1 3974 C CE2 . PHE A 528 ? 0.2386 0.2512 0.2524 0.0230 -0.0076 -0.0218 521 PHE A CE2 3975 C CZ . PHE A 528 ? 0.2214 0.2367 0.2380 0.0194 -0.0067 -0.0224 521 PHE A CZ 3976 N N . GLU A 529 ? 0.2042 0.2127 0.1988 0.0179 -0.0011 -0.0149 522 GLU A N 3977 C CA . GLU A 529 ? 0.2088 0.2192 0.2037 0.0146 -0.0007 -0.0152 522 GLU A CA 3978 C C . GLU A 529 ? 0.2015 0.2108 0.1918 0.0148 -0.0008 -0.0133 522 GLU A C 3979 O O . GLU A 529 ? 0.2028 0.2122 0.1921 0.0142 -0.0024 -0.0133 522 GLU A O 3980 C CB . GLU A 529 ? 0.1971 0.2095 0.1943 0.0113 0.0022 -0.0160 522 GLU A CB 3981 C CG . GLU A 529 ? 0.1991 0.2131 0.1960 0.0083 0.0027 -0.0161 522 GLU A CG 3982 C CD . GLU A 529 ? 0.2300 0.2451 0.2266 0.0057 0.0055 -0.0169 522 GLU A CD 3983 O OE1 . GLU A 529 ? 0.2690 0.2833 0.2636 0.0054 0.0062 -0.0167 522 GLU A OE1 3984 O OE2 . GLU A 529 ? 0.2433 0.2600 0.2420 0.0041 0.0069 -0.0179 522 GLU A OE2 3985 N N . VAL A 530 ? 0.2012 0.2093 0.1896 0.0154 0.0011 -0.0118 523 VAL A N 3986 C CA . VAL A 530 ? 0.2101 0.2178 0.1957 0.0154 0.0013 -0.0102 523 VAL A CA 3987 C C . VAL A 530 ? 0.2114 0.2170 0.1931 0.0189 -0.0007 -0.0095 523 VAL A C 3988 O O . VAL A 530 ? 0.2060 0.2116 0.1859 0.0189 -0.0017 -0.0091 523 VAL A O 3989 C CB . VAL A 530 ? 0.2135 0.2208 0.1997 0.0151 0.0039 -0.0088 523 VAL A CB 3990 C CG1 . VAL A 530 ? 0.2178 0.2224 0.2028 0.0185 0.0052 -0.0073 523 VAL A CG1 3991 C CG2 . VAL A 530 ? 0.2129 0.2210 0.1982 0.0145 0.0042 -0.0075 523 VAL A CG2 3992 N N . PHE A 531 ? 0.2120 0.2156 0.1921 0.0222 -0.0015 -0.0095 524 PHE A N 3993 C CA . PHE A 531 ? 0.2173 0.2182 0.1922 0.0262 -0.0038 -0.0092 524 PHE A CA 3994 C C . PHE A 531 ? 0.2231 0.2244 0.1989 0.0259 -0.0075 -0.0114 524 PHE A C 3995 O O . PHE A 531 ? 0.2267 0.2264 0.1988 0.0277 -0.0090 -0.0113 524 PHE A O 3996 C CB . PHE A 531 ? 0.2189 0.2169 0.1908 0.0302 -0.0043 -0.0088 524 PHE A CB 3997 C CG . PHE A 531 ? 0.2256 0.2223 0.1966 0.0308 -0.0002 -0.0062 524 PHE A CG 3998 C CD1 . PHE A 531 ? 0.2526 0.2473 0.2191 0.0331 0.0022 -0.0036 524 PHE A CD1 3999 C CD2 . PHE A 531 ? 0.2271 0.2245 0.2027 0.0290 0.0015 -0.0063 524 PHE A CD2 4000 C CE1 . PHE A 531 ? 0.2797 0.2732 0.2470 0.0332 0.0066 -0.0008 524 PHE A CE1 4001 C CE2 . PHE A 531 ? 0.2288 0.2246 0.2048 0.0291 0.0054 -0.0038 524 PHE A CE2 4002 C CZ . PHE A 531 ? 0.2573 0.2512 0.2296 0.0310 0.0079 -0.0009 524 PHE A CZ 4003 N N . PHE A 532 ? 0.2134 0.2167 0.1945 0.0237 -0.0087 -0.0132 525 PHE A N 4004 C CA . PHE A 532 ? 0.2064 0.2101 0.1903 0.0233 -0.0122 -0.0153 525 PHE A CA 4005 C C . PHE A 532 ? 0.2088 0.2143 0.1953 0.0193 -0.0113 -0.0150 525 PHE A C 4006 O O . PHE A 532 ? 0.2150 0.2190 0.1995 0.0198 -0.0130 -0.0150 525 PHE A O 4007 C CB . PHE A 532 ? 0.2130 0.2183 0.2029 0.0230 -0.0138 -0.0174 525 PHE A CB 4008 C CG . PHE A 532 ? 0.2089 0.2144 0.2031 0.0231 -0.0178 -0.0197 525 PHE A CG 4009 C CD1 . PHE A 532 ? 0.2281 0.2304 0.2179 0.0269 -0.0221 -0.0208 525 PHE A CD1 4010 C CD2 . PHE A 532 ? 0.2321 0.2407 0.2345 0.0194 -0.0173 -0.0208 525 PHE A CD2 4011 C CE1 . PHE A 532 ? 0.2375 0.2399 0.2325 0.0269 -0.0266 -0.0236 525 PHE A CE1 4012 C CE2 . PHE A 532 ? 0.2415 0.2504 0.2500 0.0192 -0.0211 -0.0230 525 PHE A CE2 4013 C CZ . PHE A 532 ? 0.2352 0.2408 0.2401 0.0229 -0.0261 -0.0246 525 PHE A CZ 4014 N N A GLN A 533 ? 0.1985 0.2065 0.1885 0.0157 -0.0086 -0.0148 526 GLN A N 4015 N N B GLN A 533 ? 0.2161 0.2241 0.2060 0.0158 -0.0085 -0.0148 526 GLN A N 4016 C CA A GLN A 533 ? 0.1825 0.1915 0.1739 0.0123 -0.0078 -0.0142 526 GLN A CA 4017 C CA B GLN A 533 ? 0.2184 0.2276 0.2098 0.0122 -0.0074 -0.0142 526 GLN A CA 4018 C C A GLN A 533 ? 0.1906 0.1990 0.1775 0.0117 -0.0066 -0.0123 526 GLN A C 4019 C C B GLN A 533 ? 0.2117 0.2201 0.1986 0.0119 -0.0067 -0.0123 526 GLN A C 4020 O O A GLN A 533 ? 0.1965 0.2048 0.1833 0.0100 -0.0069 -0.0116 526 GLN A O 4021 O O B GLN A 533 ? 0.2150 0.2229 0.2016 0.0106 -0.0074 -0.0117 526 GLN A O 4022 C CB A GLN A 533 ? 0.1769 0.1885 0.1728 0.0091 -0.0053 -0.0147 526 GLN A CB 4023 C CB B GLN A 533 ? 0.2322 0.2438 0.2267 0.0092 -0.0044 -0.0145 526 GLN A CB 4024 C CG A GLN A 533 ? 0.1676 0.1804 0.1700 0.0091 -0.0064 -0.0166 526 GLN A CG 4025 C CG B GLN A 533 ? 0.2768 0.2898 0.2762 0.0100 -0.0045 -0.0162 526 GLN A CG 4026 C CD A GLN A 533 ? 0.1346 0.1484 0.1390 0.0107 -0.0059 -0.0178 526 GLN A CD 4027 C CD B GLN A 533 ? 0.3031 0.3170 0.3085 0.0091 -0.0061 -0.0174 526 GLN A CD 4028 O OE1 A GLN A 533 ? 0.1482 0.1607 0.1485 0.0128 -0.0056 -0.0171 526 GLN A OE1 4029 O OE1 B GLN A 533 ? 0.3217 0.3347 0.3270 0.0081 -0.0073 -0.0169 526 GLN A OE1 4030 N NE2 A GLN A 533 ? 0.1911 0.2072 0.2026 0.0098 -0.0055 -0.0193 526 GLN A NE2 4031 N NE2 B GLN A 533 ? 0.2991 0.3149 0.3107 0.0093 -0.0061 -0.0191 526 GLN A NE2 4032 N N . ARG A 534 ? 0.1974 0.2056 0.1817 0.0131 -0.0051 -0.0114 527 ARG A N 4033 C CA . ARG A 534 ? 0.1970 0.2051 0.1788 0.0129 -0.0044 -0.0098 527 ARG A CA 4034 C C . ARG A 534 ? 0.2168 0.2228 0.1954 0.0163 -0.0058 -0.0092 527 ARG A C 4035 O O . ARG A 534 ? 0.2110 0.2164 0.1886 0.0162 -0.0070 -0.0088 527 ARG A O 4036 C CB . ARG A 534 ? 0.1980 0.2074 0.1802 0.0119 -0.0019 -0.0091 527 ARG A CB 4037 C CG . ARG A 534 ? 0.1954 0.2054 0.1768 0.0111 -0.0019 -0.0079 527 ARG A CG 4038 C CD . ARG A 534 ? 0.1994 0.2106 0.1825 0.0107 -0.0001 -0.0072 527 ARG A CD 4039 N NE . ARG A 534 ? 0.1922 0.2045 0.1771 0.0083 0.0010 -0.0085 527 ARG A NE 4040 C CZ . ARG A 534 ? 0.2070 0.2204 0.1942 0.0069 0.0017 -0.0086 527 ARG A CZ 4041 N NH1 . ARG A 534 ? 0.2115 0.2256 0.2002 0.0076 0.0016 -0.0074 527 ARG A NH1 4042 N NH2 . ARG A 534 ? 0.1899 0.2038 0.1783 0.0051 0.0025 -0.0102 527 ARG A NH2 4043 N N . LEU A 535 ? 0.2075 0.2120 0.1840 0.0195 -0.0057 -0.0092 528 LEU A N 4044 C CA . LEU A 535 ? 0.2105 0.2127 0.1827 0.0233 -0.0062 -0.0086 528 LEU A CA 4045 C C . LEU A 535 ? 0.2170 0.2166 0.1867 0.0261 -0.0098 -0.0104 528 LEU A C 4046 O O . LEU A 535 ? 0.2414 0.2388 0.2069 0.0292 -0.0104 -0.0102 528 LEU A O 4047 C CB . LEU A 535 ? 0.2037 0.2049 0.1735 0.0259 -0.0034 -0.0070 528 LEU A CB 4048 C CG . LEU A 535 ? 0.2210 0.2245 0.1943 0.0234 0.0001 -0.0053 528 LEU A CG 4049 C CD1 . LEU A 535 ? 0.2421 0.2441 0.2141 0.0259 0.0032 -0.0034 528 LEU A CD1 4050 C CD2 . LEU A 535 ? 0.2476 0.2526 0.2221 0.0224 0.0005 -0.0044 528 LEU A CD2 4051 N N . GLY A 536 ? 0.2011 0.2008 0.1736 0.0253 -0.0122 -0.0123 529 GLY A N 4052 C CA . GLY A 536 ? 0.2098 0.2070 0.1813 0.0277 -0.0165 -0.0146 529 GLY A CA 4053 C C . GLY A 536 ? 0.2100 0.2042 0.1754 0.0330 -0.0180 -0.0152 529 GLY A C 4054 O O . GLY A 536 ? 0.2158 0.2070 0.1771 0.0363 -0.0211 -0.0168 529 GLY A O 4055 N N . ILE A 537 ? 0.2134 0.2079 0.1779 0.0339 -0.0160 -0.0142 530 ILE A N 4056 C CA . ILE A 537 ? 0.2169 0.2080 0.1749 0.0392 -0.0174 -0.0143 530 ILE A CA 4057 C C . ILE A 537 ? 0.2201 0.2115 0.1820 0.0395 -0.0214 -0.0169 530 ILE A C 4058 O O . ILE A 537 ? 0.2252 0.2197 0.1938 0.0362 -0.0202 -0.0169 530 ILE A O 4059 C CB . ILE A 537 ? 0.2158 0.2063 0.1704 0.0404 -0.0125 -0.0110 530 ILE A CB 4060 C CG1 . ILE A 537 ? 0.2274 0.2178 0.1795 0.0405 -0.0087 -0.0087 530 ILE A CG1 4061 C CG2 . ILE A 537 ? 0.2444 0.2307 0.1917 0.0460 -0.0137 -0.0107 530 ILE A CG2 4062 C CD1 . ILE A 537 ? 0.2519 0.2433 0.2053 0.0394 -0.0034 -0.0055 530 ILE A CD1 4063 N N . ALA A 538 ? 0.2274 0.2157 0.1853 0.0438 -0.0264 -0.0193 531 ALA A N 4064 C CA . ALA A 538 ? 0.2247 0.2134 0.1870 0.0447 -0.0313 -0.0223 531 ALA A CA 4065 C C . ALA A 538 ? 0.2398 0.2295 0.2035 0.0450 -0.0291 -0.0207 531 ALA A C 4066 O O . ALA A 538 ? 0.2491 0.2360 0.2051 0.0483 -0.0265 -0.0181 531 ALA A O 4067 C CB . ALA A 538 ? 0.2435 0.2274 0.1978 0.0509 -0.0368 -0.0247 531 ALA A CB 4068 N N . SER A 539 ? 0.2155 0.2090 0.1890 0.0415 -0.0294 -0.0220 532 SER A N 4069 C CA . SER A 539 ? 0.2295 0.2242 0.2054 0.0413 -0.0267 -0.0206 532 SER A CA 4070 C C . SER A 539 ? 0.2310 0.2274 0.2142 0.0422 -0.0311 -0.0235 532 SER A C 4071 O O . SER A 539 ? 0.2295 0.2281 0.2199 0.0406 -0.0348 -0.0265 532 SER A O 4072 C CB . SER A 539 ? 0.2302 0.2286 0.2114 0.0357 -0.0211 -0.0189 532 SER A CB 4073 O OG . SER A 539 ? 0.2312 0.2282 0.2066 0.0353 -0.0174 -0.0162 532 SER A OG 4074 N N . GLY A 540 ? 0.2323 0.2277 0.2146 0.0446 -0.0306 -0.0226 533 GLY A N 4075 C CA . GLY A 540 ? 0.2415 0.2392 0.2323 0.0453 -0.0343 -0.0253 533 GLY A CA 4076 C C . GLY A 540 ? 0.2487 0.2466 0.2411 0.0457 -0.0312 -0.0236 533 GLY A C 4077 O O . GLY A 540 ? 0.2509 0.2462 0.2368 0.0461 -0.0267 -0.0203 533 GLY A O 4078 N N . ARG A 541 ? 0.2465 0.2473 0.2483 0.0457 -0.0336 -0.0260 534 ARG A N 4079 C CA . ARG A 541 ? 0.2444 0.2454 0.2490 0.0465 -0.0313 -0.0250 534 ARG A CA 4080 C C . ARG A 541 ? 0.2473 0.2501 0.2601 0.0492 -0.0370 -0.0282 534 ARG A C 4081 O O . ARG A 541 ? 0.2483 0.2542 0.2684 0.0484 -0.0412 -0.0314 534 ARG A O 4082 C CB . ARG A 541 ? 0.2443 0.2493 0.2558 0.0408 -0.0250 -0.0245 534 ARG A CB 4083 C CG . ARG A 541 ? 0.2625 0.2734 0.2863 0.0370 -0.0255 -0.0276 534 ARG A CG 4084 C CD . ARG A 541 ? 0.3105 0.3246 0.3380 0.0316 -0.0191 -0.0270 534 ARG A CD 4085 N NE . ARG A 541 ? 0.3368 0.3503 0.3645 0.0317 -0.0153 -0.0261 534 ARG A NE 4086 C CZ . ARG A 541 ? 0.3374 0.3536 0.3692 0.0279 -0.0104 -0.0264 534 ARG A CZ 4087 N NH1 . ARG A 541 ? 0.3140 0.3287 0.3452 0.0284 -0.0075 -0.0259 534 ARG A NH1 4088 N NH2 . ARG A 541 ? 0.3306 0.3501 0.3660 0.0239 -0.0082 -0.0272 534 ARG A NH2 4089 N N . ALA A 542 ? 0.2506 0.2515 0.2628 0.0525 -0.0372 -0.0272 535 ALA A N 4090 C CA . ALA A 542 ? 0.2581 0.2606 0.2782 0.0559 -0.0428 -0.0301 535 ALA A CA 4091 C C . ALA A 542 ? 0.2620 0.2641 0.2853 0.0567 -0.0397 -0.0288 535 ALA A C 4092 O O . ALA A 542 ? 0.2638 0.2614 0.2785 0.0577 -0.0357 -0.0252 535 ALA A O 4093 C CB . ALA A 542 ? 0.2666 0.2640 0.2775 0.0626 -0.0502 -0.0306 535 ALA A CB 4094 N N A ARG A 543 ? 0.2565 0.2633 0.2927 0.0565 -0.0415 -0.0318 536 ARG A N 4095 N N B ARG A 543 ? 0.2564 0.2634 0.2929 0.0562 -0.0413 -0.0318 536 ARG A N 4096 C CA A ARG A 543 ? 0.2589 0.2654 0.2995 0.0579 -0.0393 -0.0312 536 ARG A CA 4097 C CA B ARG A 543 ? 0.2591 0.2661 0.3004 0.0574 -0.0389 -0.0313 536 ARG A CA 4098 C C A ARG A 543 ? 0.2605 0.2715 0.3144 0.0600 -0.0446 -0.0350 536 ARG A C 4099 C C B ARG A 543 ? 0.2596 0.2713 0.3147 0.0592 -0.0437 -0.0351 536 ARG A C 4100 O O A ARG A 543 ? 0.2534 0.2681 0.3140 0.0595 -0.0492 -0.0380 536 ARG A O 4101 O O B ARG A 543 ? 0.2528 0.2693 0.3166 0.0577 -0.0471 -0.0382 536 ARG A O 4102 C CB A ARG A 543 ? 0.2548 0.2642 0.2998 0.0522 -0.0311 -0.0305 536 ARG A CB 4103 C CB B ARG A 543 ? 0.2552 0.2645 0.2997 0.0519 -0.0306 -0.0304 536 ARG A CB 4104 C CG A ARG A 543 ? 0.2482 0.2651 0.3064 0.0475 -0.0292 -0.0337 536 ARG A CG 4105 C CG B ARG A 543 ? 0.2433 0.2593 0.2975 0.0462 -0.0279 -0.0328 536 ARG A CG 4106 C CD A ARG A 543 ? 0.2407 0.2592 0.3011 0.0432 -0.0215 -0.0332 536 ARG A CD 4107 C CD B ARG A 543 ? 0.2936 0.3088 0.3405 0.0433 -0.0268 -0.0316 536 ARG A CD 4108 N NE A ARG A 543 ? 0.2685 0.2823 0.3168 0.0420 -0.0181 -0.0300 536 ARG A NE 4109 N NE B ARG A 543 ? 0.2749 0.2950 0.3280 0.0375 -0.0222 -0.0325 536 ARG A NE 4110 C CZ A ARG A 543 ? 0.2720 0.2869 0.3190 0.0374 -0.0124 -0.0294 536 ARG A CZ 4111 C CZ B ARG A 543 ? 0.2600 0.2826 0.3161 0.0351 -0.0238 -0.0336 536 ARG A CZ 4112 N NH1 A ARG A 543 ? 0.2493 0.2693 0.3047 0.0338 -0.0091 -0.0316 536 ARG A NH1 4113 N NH1 B ARG A 543 ? 0.2347 0.2608 0.2952 0.0301 -0.0190 -0.0338 536 ARG A NH1 4114 N NH2 A ARG A 543 ? 0.2420 0.2527 0.2792 0.0367 -0.0100 -0.0266 536 ARG A NH2 4115 N NH2 B ARG A 543 ? 0.2395 0.2607 0.2941 0.0380 -0.0302 -0.0346 536 ARG A NH2 4116 N N . TYR A 544 ? 0.2616 0.2721 0.3198 0.0625 -0.0441 -0.0349 537 TYR A N 4117 C CA . TYR A 544 ? 0.2783 0.2940 0.3516 0.0640 -0.0478 -0.0385 537 TYR A CA 4118 C C . TYR A 544 ? 0.2836 0.3061 0.3698 0.0585 -0.0410 -0.0403 537 TYR A C 4119 O O . TYR A 544 ? 0.2780 0.2993 0.3600 0.0552 -0.0339 -0.0384 537 TYR A O 4120 C CB . TYR A 544 ? 0.2770 0.2886 0.3488 0.0706 -0.0519 -0.0378 537 TYR A CB 4121 C CG . TYR A 544 ? 0.2905 0.3024 0.3651 0.0759 -0.0620 -0.0405 537 TYR A CG 4122 C CD1 . TYR A 544 ? 0.3064 0.3137 0.3686 0.0787 -0.0673 -0.0398 537 TYR A CD1 4123 C CD2 . TYR A 544 ? 0.2838 0.3009 0.3741 0.0780 -0.0664 -0.0441 537 TYR A CD2 4124 C CE1 . TYR A 544 ? 0.3119 0.3192 0.3761 0.0837 -0.0774 -0.0430 537 TYR A CE1 4125 C CE2 . TYR A 544 ? 0.2859 0.3035 0.3797 0.0830 -0.0768 -0.0472 537 TYR A CE2 4126 C CZ . TYR A 544 ? 0.3071 0.3196 0.3873 0.0857 -0.0824 -0.0467 537 TYR A CZ 4127 O OH . TYR A 544 ? 0.3257 0.3382 0.4082 0.0908 -0.0932 -0.0501 537 TYR A OH 4128 N N . THR A 545 ? 0.2784 0.3078 0.3800 0.0574 -0.0433 -0.0440 538 THR A N 4129 C CA . THR A 545 ? 0.2841 0.3200 0.3975 0.0521 -0.0364 -0.0455 538 THR A CA 4130 C C . THR A 545 ? 0.2996 0.3416 0.4308 0.0539 -0.0383 -0.0490 538 THR A C 4131 O O . THR A 545 ? 0.2837 0.3250 0.4184 0.0591 -0.0458 -0.0504 538 THR A O 4132 C CB . THR A 545 ? 0.2806 0.3199 0.3957 0.0469 -0.0347 -0.0459 538 THR A CB 4133 O OG1 . THR A 545 ? 0.2943 0.3382 0.4165 0.0419 -0.0265 -0.0463 538 THR A OG1 4134 C CG2 . THR A 545 ? 0.2669 0.3102 0.3933 0.0481 -0.0421 -0.0491 538 THR A CG2 4135 N N . LYS A 546 ? 0.3170 0.3646 0.4589 0.0500 -0.0312 -0.0502 539 LYS A N 4136 C CA . LYS A 546 ? 0.3591 0.4137 0.5201 0.0509 -0.0312 -0.0536 539 LYS A CA 4137 C C . LYS A 546 ? 0.3695 0.4308 0.5446 0.0486 -0.0342 -0.0562 539 LYS A C 4138 O O . LYS A 546 ? 0.3745 0.4346 0.5439 0.0461 -0.0357 -0.0553 539 LYS A O 4139 C CB . LYS A 546 ? 0.3498 0.4073 0.5149 0.0477 -0.0212 -0.0538 539 LYS A CB 4140 C CG . LYS A 546 ? 0.3926 0.4528 0.5570 0.0414 -0.0147 -0.0531 539 LYS A CG 4141 C CD . LYS A 546 ? 0.4854 0.5468 0.6493 0.0385 -0.0049 -0.0530 539 LYS A CD 4142 C CE . LYS A 546 ? 0.5014 0.5616 0.6554 0.0333 -0.0001 -0.0508 539 LYS A CE 4143 N NZ . LYS A 546 ? 0.5702 0.6356 0.7320 0.0296 0.0083 -0.0517 539 LYS A NZ 4144 N N . ASN A 547 ? 0.4127 0.4811 0.6072 0.0495 -0.0349 -0.0593 540 ASN A N 4145 C CA . ASN A 547 ? 0.4468 0.5225 0.6582 0.0464 -0.0360 -0.0618 540 ASN A CA 4146 C C . ASN A 547 ? 0.4676 0.5471 0.6824 0.0399 -0.0254 -0.0607 540 ASN A C 4147 O O . ASN A 547 ? 0.4793 0.5630 0.7027 0.0388 -0.0180 -0.0613 540 ASN A O 4148 C CB . ASN A 547 ? 0.4464 0.5289 0.6791 0.0497 -0.0403 -0.0656 540 ASN A CB 4149 C CG . ASN A 547 ? 0.4542 0.5439 0.7060 0.0472 -0.0436 -0.0685 540 ASN A CG 4150 O OD1 . ASN A 547 ? 0.4775 0.5677 0.7281 0.0422 -0.0407 -0.0675 540 ASN A OD1 4151 N ND2 . ASN A 547 ? 0.4492 0.5442 0.7191 0.0507 -0.0501 -0.0722 540 ASN A ND2 4152 N N . TRP A 548 ? 0.5046 0.5821 0.7120 0.0361 -0.0250 -0.0590 541 TRP A N 4153 C CA . TRP A 548 ? 0.5380 0.6174 0.7449 0.0301 -0.0159 -0.0571 541 TRP A CA 4154 C C . TRP A 548 ? 0.5624 0.6501 0.7913 0.0270 -0.0134 -0.0591 541 TRP A C 4155 O O . TRP A 548 ? 0.5612 0.6499 0.7919 0.0225 -0.0104 -0.0578 541 TRP A O 4156 C CB . TRP A 548 ? 0.5424 0.6159 0.7332 0.0282 -0.0180 -0.0546 541 TRP A CB 4157 C CG . TRP A 548 ? 0.5497 0.6239 0.7384 0.0225 -0.0111 -0.0525 541 TRP A CG 4158 C CD1 . TRP A 548 ? 0.5581 0.6336 0.7527 0.0194 -0.0131 -0.0525 541 TRP A CD1 4159 C CD2 . TRP A 548 ? 0.5521 0.6247 0.7309 0.0194 -0.0018 -0.0499 541 TRP A CD2 4160 N NE1 . TRP A 548 ? 0.5583 0.6332 0.7475 0.0147 -0.0052 -0.0497 541 TRP A NE1 4161 C CE2 . TRP A 548 ? 0.5533 0.6264 0.7323 0.0147 0.0016 -0.0481 541 TRP A CE2 4162 C CE3 . TRP A 548 ? 0.5492 0.6197 0.7192 0.0203 0.0036 -0.0491 541 TRP A CE3 4163 C CZ2 . TRP A 548 ? 0.5538 0.6255 0.7237 0.0113 0.0101 -0.0454 541 TRP A CZ2 4164 C CZ3 . TRP A 548 ? 0.5577 0.6269 0.7190 0.0167 0.0117 -0.0470 541 TRP A CZ3 4165 C CH2 . TRP A 548 ? 0.5606 0.6305 0.7215 0.0124 0.0148 -0.0451 541 TRP A CH2 4166 N N . GLU A 549 ? 0.5963 0.6899 0.8426 0.0295 -0.0146 -0.0620 542 GLU A N 4167 C CA . GLU A 549 ? 0.6274 0.7297 0.8978 0.0271 -0.0124 -0.0641 542 GLU A CA 4168 C C . GLU A 549 ? 0.6385 0.7464 0.9216 0.0288 -0.0065 -0.0657 542 GLU A C 4169 O O . GLU A 549 ? 0.6437 0.7574 0.9390 0.0254 0.0026 -0.0655 542 GLU A O 4170 C CB . GLU A 549 ? 0.6345 0.7395 0.9187 0.0293 -0.0239 -0.0675 542 GLU A CB 4171 C CG . GLU A 549 ? 0.6792 0.7798 0.9554 0.0274 -0.0298 -0.0668 542 GLU A CG 4172 C CD . GLU A 549 ? 0.7434 0.8495 1.0411 0.0265 -0.0367 -0.0703 542 GLU A CD 4173 O OE1 . GLU A 549 ? 0.7744 0.8844 1.0862 0.0306 -0.0442 -0.0741 542 GLU A OE1 4174 O OE2 . GLU A 549 ? 0.7686 0.8751 1.0698 0.0218 -0.0348 -0.0693 542 GLU A OE2 4175 N N . THR A 550 ? 0.6507 0.7565 0.9307 0.0343 -0.0116 -0.0672 543 THR A N 4176 C CA . THR A 550 ? 0.6619 0.7722 0.9536 0.0369 -0.0075 -0.0692 543 THR A CA 4177 C C . THR A 550 ? 0.6693 0.7745 0.9443 0.0372 0.0005 -0.0672 543 THR A C 4178 O O . THR A 550 ? 0.6720 0.7794 0.9532 0.0398 0.0043 -0.0687 543 THR A O 4179 C CB . THR A 550 ? 0.6678 0.7785 0.9672 0.0433 -0.0183 -0.0721 543 THR A CB 4180 O OG1 . THR A 550 ? 0.6714 0.7728 0.9493 0.0468 -0.0249 -0.0704 543 THR A OG1 4181 C CG2 . THR A 550 ? 0.6683 0.7850 0.9871 0.0434 -0.0267 -0.0751 543 THR A CG2 4182 N N . ASN A 551 ? 0.6742 0.7727 0.9288 0.0346 0.0025 -0.0641 544 ASN A N 4183 C CA . ASN A 551 ? 0.6784 0.7712 0.9157 0.0345 0.0089 -0.0623 544 ASN A CA 4184 C C . ASN A 551 ? 0.6714 0.7626 0.8981 0.0291 0.0164 -0.0595 544 ASN A C 4185 O O . ASN A 551 ? 0.6764 0.7628 0.8901 0.0273 0.0132 -0.0573 544 ASN A O 4186 C CB . ASN A 551 ? 0.6823 0.7667 0.9029 0.0383 0.0018 -0.0611 544 ASN A CB 4187 C CG . ASN A 551 ? 0.7054 0.7901 0.9337 0.0443 -0.0041 -0.0633 544 ASN A CG 4188 O OD1 . ASN A 551 ? 0.7131 0.8007 0.9504 0.0460 0.0003 -0.0651 544 ASN A OD1 4189 N ND2 . ASN A 551 ? 0.7159 0.7968 0.9398 0.0479 -0.0142 -0.0630 544 ASN A ND2 4190 N N . LYS A 552 ? 0.6597 0.7547 0.8917 0.0268 0.0265 -0.0598 545 LYS A N 4191 C CA . LYS A 552 ? 0.6457 0.7398 0.8692 0.0220 0.0345 -0.0572 545 LYS A CA 4192 C C . LYS A 552 ? 0.6365 0.7237 0.8390 0.0217 0.0388 -0.0558 545 LYS A C 4193 O O . LYS A 552 ? 0.6374 0.7242 0.8333 0.0187 0.0469 -0.0544 545 LYS A O 4194 C CB . LYS A 552 ? 0.6482 0.7499 0.8881 0.0199 0.0437 -0.0580 545 LYS A CB 4195 C CG . LYS A 552 ? 0.6482 0.7574 0.9118 0.0198 0.0398 -0.0596 545 LYS A CG 4196 C CD . LYS A 552 ? 0.6519 0.7692 0.9344 0.0191 0.0490 -0.0610 545 LYS A CD 4197 C CE . LYS A 552 ? 0.6522 0.7702 0.9315 0.0143 0.0598 -0.0579 545 LYS A CE 4198 N NZ . LYS A 552 ? 0.6499 0.7760 0.9486 0.0138 0.0694 -0.0589 545 LYS A NZ 4199 N N . PHE A 553 ? 0.6226 0.7042 0.8147 0.0249 0.0334 -0.0561 546 PHE A N 4200 C CA . PHE A 553 ? 0.6056 0.6806 0.7796 0.0248 0.0366 -0.0553 546 PHE A CA 4201 C C . PHE A 553 ? 0.5929 0.6612 0.7490 0.0231 0.0328 -0.0524 546 PHE A C 4202 O O . PHE A 553 ? 0.5932 0.6572 0.7358 0.0218 0.0367 -0.0516 546 PHE A O 4203 C CB . PHE A 553 ? 0.6101 0.6832 0.7852 0.0292 0.0360 -0.0576 546 PHE A CB 4204 C CG . PHE A 553 ? 0.6160 0.6871 0.7939 0.0332 0.0267 -0.0579 546 PHE A CG 4205 C CD1 . PHE A 553 ? 0.6288 0.7051 0.8240 0.0364 0.0235 -0.0602 546 PHE A CD1 4206 C CD2 . PHE A 553 ? 0.6216 0.6855 0.7850 0.0340 0.0213 -0.0557 546 PHE A CD2 4207 C CE1 . PHE A 553 ? 0.6273 0.7011 0.8238 0.0407 0.0143 -0.0604 546 PHE A CE1 4208 C CE2 . PHE A 553 ? 0.6235 0.6848 0.7879 0.0382 0.0130 -0.0555 546 PHE A CE2 4209 C CZ . PHE A 553 ? 0.6246 0.6906 0.8049 0.0417 0.0093 -0.0578 546 PHE A CZ 4210 N N . SER A 554 ? 0.5709 0.6384 0.7272 0.0233 0.0254 -0.0511 547 SER A N 4211 C CA . SER A 554 ? 0.5509 0.6122 0.6910 0.0220 0.0217 -0.0483 547 SER A CA 4212 C C . SER A 554 ? 0.5196 0.5740 0.6451 0.0238 0.0205 -0.0474 547 SER A C 4213 O O . SER A 554 ? 0.5272 0.5798 0.6483 0.0238 0.0254 -0.0483 547 SER A O 4214 C CB . SER A 554 ? 0.5661 0.6279 0.7010 0.0174 0.0263 -0.0463 547 SER A CB 4215 O OG . SER A 554 ? 0.6033 0.6618 0.7303 0.0164 0.0210 -0.0441 547 SER A OG 4216 N N . GLY A 555 ? 0.4832 0.5333 0.6011 0.0252 0.0140 -0.0457 548 GLY A N 4217 C CA . GLY A 555 ? 0.4238 0.4674 0.5306 0.0275 0.0120 -0.0445 548 GLY A CA 4218 C C . GLY A 555 ? 0.3863 0.4296 0.5002 0.0319 0.0101 -0.0463 548 GLY A C 4219 O O . GLY A 555 ? 0.3833 0.4312 0.5098 0.0338 0.0077 -0.0481 548 GLY A O 4220 N N . TYR A 556 ? 0.3278 0.3660 0.4349 0.0334 0.0111 -0.0459 549 TYR A N 4221 C CA . TYR A 556 ? 0.2947 0.3323 0.4088 0.0374 0.0106 -0.0478 549 TYR A CA 4222 C C . TYR A 556 ? 0.2777 0.3147 0.3908 0.0360 0.0176 -0.0497 549 TYR A C 4223 O O . TYR A 556 ? 0.2688 0.3029 0.3717 0.0329 0.0207 -0.0489 549 TYR A O 4224 C CB . TYR A 556 ? 0.2958 0.3269 0.4036 0.0414 0.0052 -0.0456 549 TYR A CB 4225 C CG . TYR A 556 ? 0.2812 0.3059 0.3751 0.0397 0.0064 -0.0428 549 TYR A CG 4226 C CD1 . TYR A 556 ? 0.2781 0.2979 0.3686 0.0403 0.0091 -0.0429 549 TYR A CD1 4227 C CD2 . TYR A 556 ? 0.2602 0.2839 0.3457 0.0374 0.0049 -0.0404 549 TYR A CD2 4228 C CE1 . TYR A 556 ? 0.2400 0.2543 0.3196 0.0385 0.0102 -0.0405 549 TYR A CE1 4229 C CE2 . TYR A 556 ? 0.2526 0.2712 0.3271 0.0359 0.0061 -0.0380 549 TYR A CE2 4230 C CZ . TYR A 556 ? 0.2544 0.2686 0.3265 0.0363 0.0088 -0.0381 549 TYR A CZ 4231 O OH . TYR A 556 ? 0.2566 0.2661 0.3195 0.0345 0.0100 -0.0359 549 TYR A OH 4232 N N . PRO A 557 ? 0.2564 0.2957 0.3796 0.0384 0.0197 -0.0526 550 PRO A N 4233 C CA . PRO A 557 ? 0.2499 0.2891 0.3720 0.0370 0.0267 -0.0551 550 PRO A CA 4234 C C . PRO A 557 ? 0.2466 0.2785 0.3572 0.0366 0.0277 -0.0547 550 PRO A C 4235 O O . PRO A 557 ? 0.2533 0.2845 0.3587 0.0342 0.0328 -0.0564 550 PRO A O 4236 C CB . PRO A 557 ? 0.2512 0.2936 0.3869 0.0407 0.0277 -0.0582 550 PRO A CB 4237 C CG . PRO A 557 ? 0.2478 0.2961 0.3950 0.0420 0.0230 -0.0577 550 PRO A CG 4238 C CD . PRO A 557 ? 0.2553 0.2989 0.3926 0.0421 0.0162 -0.0542 550 PRO A CD 4239 N N . LEU A 558 ? 0.2289 0.2551 0.3357 0.0390 0.0231 -0.0526 551 LEU A N 4240 C CA . LEU A 558 ? 0.2298 0.2489 0.3284 0.0388 0.0242 -0.0524 551 LEU A CA 4241 C C . LEU A 558 ? 0.2357 0.2513 0.3225 0.0355 0.0234 -0.0496 551 LEU A C 4242 O O . LEU A 558 ? 0.2501 0.2598 0.3310 0.0352 0.0235 -0.0488 551 LEU A O 4243 C CB . LEU A 558 ? 0.2242 0.2380 0.3254 0.0432 0.0207 -0.0515 551 LEU A CB 4244 C CG . LEU A 558 ? 0.2343 0.2511 0.3474 0.0465 0.0222 -0.0550 551 LEU A CG 4245 C CD1 . LEU A 558 ? 0.2606 0.2726 0.3771 0.0514 0.0179 -0.0536 551 LEU A CD1 4246 C CD2 . LEU A 558 ? 0.2350 0.2514 0.3482 0.0451 0.0283 -0.0590 551 LEU A CD2 4247 N N . TYR A 559 ? 0.2296 0.2490 0.3143 0.0332 0.0226 -0.0480 552 TYR A N 4248 C CA . TYR A 559 ? 0.2316 0.2489 0.3060 0.0300 0.0221 -0.0455 552 TYR A CA 4249 C C . TYR A 559 ? 0.2257 0.2395 0.2931 0.0275 0.0254 -0.0468 552 TYR A C 4250 O O . TYR A 559 ? 0.2389 0.2547 0.3065 0.0260 0.0294 -0.0498 552 TYR A O 4251 C CB . TYR A 559 ? 0.2242 0.2471 0.2995 0.0276 0.0223 -0.0450 552 TYR A CB 4252 C CG . TYR A 559 ? 0.2390 0.2611 0.3049 0.0241 0.0224 -0.0429 552 TYR A CG 4253 C CD1 . TYR A 559 ? 0.2460 0.2647 0.3058 0.0244 0.0186 -0.0397 552 TYR A CD1 4254 C CD2 . TYR A 559 ? 0.2505 0.2753 0.3138 0.0209 0.0264 -0.0441 552 TYR A CD2 4255 C CE1 . TYR A 559 ? 0.2262 0.2445 0.2782 0.0214 0.0186 -0.0378 552 TYR A CE1 4256 C CE2 . TYR A 559 ? 0.2283 0.2523 0.2833 0.0180 0.0260 -0.0420 552 TYR A CE2 4257 C CZ . TYR A 559 ? 0.2110 0.2320 0.2611 0.0182 0.0221 -0.0391 552 TYR A CZ 4258 O OH . TYR A 559 ? 0.2288 0.2493 0.2715 0.0155 0.0218 -0.0373 552 TYR A OH 4259 N N . HIS A 560 ? 0.2227 0.2311 0.2840 0.0271 0.0236 -0.0446 553 HIS A N 4260 C CA . HIS A 560 ? 0.2211 0.2261 0.2762 0.0244 0.0255 -0.0457 553 HIS A CA 4261 C C . HIS A 560 ? 0.2290 0.2315 0.2869 0.0253 0.0282 -0.0497 553 HIS A C 4262 O O . HIS A 560 ? 0.2337 0.2344 0.2870 0.0231 0.0299 -0.0521 553 HIS A O 4263 C CB . HIS A 560 ? 0.2189 0.2271 0.2681 0.0208 0.0269 -0.0459 553 HIS A CB 4264 C CG . HIS A 560 ? 0.2198 0.2284 0.2643 0.0195 0.0241 -0.0420 553 HIS A CG 4265 N ND1 . HIS A 560 ? 0.2020 0.2126 0.2408 0.0165 0.0248 -0.0415 553 HIS A ND1 4266 C CD2 . HIS A 560 ? 0.2332 0.2403 0.2775 0.0212 0.0208 -0.0384 553 HIS A CD2 4267 C CE1 . HIS A 560 ? 0.2168 0.2271 0.2526 0.0162 0.0220 -0.0380 553 HIS A CE1 4268 N NE2 . HIS A 560 ? 0.2070 0.2151 0.2456 0.0190 0.0197 -0.0362 553 HIS A NE2 4269 N N . SER A 561 ? 0.2394 0.2416 0.3046 0.0287 0.0280 -0.0507 554 SER A N 4270 C CA . SER A 561 ? 0.2272 0.2262 0.2960 0.0303 0.0302 -0.0545 554 SER A CA 4271 C C . SER A 561 ? 0.2714 0.2634 0.3419 0.0324 0.0279 -0.0526 554 SER A C 4272 O O . SER A 561 ? 0.2558 0.2461 0.3254 0.0335 0.0250 -0.0483 554 SER A O 4273 C CB . SER A 561 ? 0.2245 0.2281 0.3019 0.0330 0.0321 -0.0571 554 SER A CB 4274 O OG A SER A 561 ? 0.2427 0.2462 0.3268 0.0366 0.0289 -0.0550 554 SER A OG 4275 O OG B SER A 561 ? 0.2329 0.2329 0.3153 0.0357 0.0333 -0.0602 554 SER A OG 4276 N N . VAL A 562 ? 0.2434 0.2311 0.3157 0.0329 0.0296 -0.0560 555 VAL A N 4277 C CA . VAL A 562 ? 0.2621 0.2425 0.3372 0.0350 0.0281 -0.0544 555 VAL A CA 4278 C C . VAL A 562 ? 0.2641 0.2445 0.3452 0.0396 0.0260 -0.0520 555 VAL A C 4279 O O . VAL A 562 ? 0.2834 0.2579 0.3654 0.0418 0.0241 -0.0486 555 VAL A O 4280 C CB . VAL A 562 ? 0.2556 0.2316 0.3330 0.0350 0.0303 -0.0594 555 VAL A CB 4281 C CG1 . VAL A 562 ? 0.2597 0.2383 0.3438 0.0384 0.0324 -0.0637 555 VAL A CG1 4282 C CG2 . VAL A 562 ? 0.2709 0.2384 0.3505 0.0359 0.0289 -0.0574 555 VAL A CG2 4283 N N . TYR A 563 ? 0.2514 0.2383 0.3370 0.0412 0.0263 -0.0535 556 TYR A N 4284 C CA . TYR A 563 ? 0.2697 0.2571 0.3626 0.0460 0.0238 -0.0524 556 TYR A CA 4285 C C . TYR A 563 ? 0.2801 0.2679 0.3701 0.0472 0.0195 -0.0473 556 TYR A C 4286 O O . TYR A 563 ? 0.2782 0.2654 0.3727 0.0516 0.0163 -0.0457 556 TYR A O 4287 C CB . TYR A 563 ? 0.2578 0.2521 0.3592 0.0474 0.0259 -0.0566 556 TYR A CB 4288 C CG . TYR A 563 ? 0.2663 0.2593 0.3692 0.0469 0.0304 -0.0618 556 TYR A CG 4289 C CD1 . TYR A 563 ? 0.2835 0.2697 0.3894 0.0493 0.0305 -0.0633 556 TYR A CD1 4290 C CD2 . TYR A 563 ? 0.2688 0.2667 0.3696 0.0441 0.0346 -0.0653 556 TYR A CD2 4291 C CE1 . TYR A 563 ? 0.2826 0.2669 0.3893 0.0490 0.0343 -0.0686 556 TYR A CE1 4292 C CE2 . TYR A 563 ? 0.2764 0.2725 0.3771 0.0441 0.0387 -0.0705 556 TYR A CE2 4293 C CZ . TYR A 563 ? 0.2957 0.2851 0.3994 0.0465 0.0384 -0.0724 556 TYR A CZ 4294 O OH . TYR A 563 ? 0.3139 0.3009 0.4168 0.0467 0.0420 -0.0780 556 TYR A OH 4295 N N . GLU A 564 ? 0.2700 0.2588 0.3524 0.0439 0.0191 -0.0448 557 GLU A N 4296 C CA . GLU A 564 ? 0.2876 0.2764 0.3658 0.0451 0.0152 -0.0402 557 GLU A CA 4297 C C . GLU A 564 ? 0.2831 0.2634 0.3573 0.0473 0.0138 -0.0360 557 GLU A C 4298 O O . GLU A 564 ? 0.2900 0.2667 0.3584 0.0446 0.0152 -0.0338 557 GLU A O 4299 C CB . GLU A 564 ? 0.3042 0.2961 0.3755 0.0407 0.0160 -0.0393 557 GLU A CB 4300 C CG . GLU A 564 ? 0.3647 0.3624 0.4367 0.0407 0.0138 -0.0388 557 GLU A CG 4301 C CD . GLU A 564 ? 0.2878 0.2857 0.3514 0.0375 0.0135 -0.0363 557 GLU A CD 4302 O OE1 . GLU A 564 ? 0.3096 0.3114 0.3716 0.0337 0.0158 -0.0380 557 GLU A OE1 4303 O OE2 . GLU A 564 ? 0.2792 0.2727 0.3375 0.0389 0.0114 -0.0324 557 GLU A OE2 4304 N N . THR A 565 ? 0.2766 0.2537 0.3545 0.0523 0.0113 -0.0347 558 THR A N 4305 C CA . THR A 565 ? 0.2791 0.2473 0.3539 0.0548 0.0108 -0.0305 558 THR A CA 4306 C C . THR A 565 ? 0.2771 0.2431 0.3485 0.0599 0.0061 -0.0262 558 THR A C 4307 O O . THR A 565 ? 0.2737 0.2452 0.3471 0.0618 0.0027 -0.0274 558 THR A O 4308 C CB . THR A 565 ? 0.2897 0.2538 0.3719 0.0571 0.0121 -0.0330 558 THR A CB 4309 O OG1 . THR A 565 ? 0.3049 0.2737 0.3947 0.0608 0.0099 -0.0357 558 THR A OG1 4310 C CG2 . THR A 565 ? 0.3063 0.2708 0.3910 0.0529 0.0165 -0.0376 558 THR A CG2 4311 N N . TYR A 566 ? 0.2832 0.2406 0.3497 0.0624 0.0060 -0.0213 559 TYR A N 4312 C CA . TYR A 566 ? 0.3019 0.2554 0.3642 0.0683 0.0017 -0.0172 559 TYR A CA 4313 C C . TYR A 566 ? 0.2925 0.2488 0.3631 0.0729 -0.0021 -0.0201 559 TYR A C 4314 O O . TYR A 566 ? 0.3014 0.2604 0.3708 0.0765 -0.0072 -0.0196 559 TYR A O 4315 C CB . TYR A 566 ? 0.2943 0.2372 0.3515 0.0706 0.0033 -0.0115 559 TYR A CB 4316 C CG . TYR A 566 ? 0.3264 0.2641 0.3784 0.0776 -0.0012 -0.0071 559 TYR A CG 4317 C CD1 . TYR A 566 ? 0.3407 0.2777 0.3823 0.0797 -0.0038 -0.0034 559 TYR A CD1 4318 C CD2 . TYR A 566 ? 0.3695 0.3025 0.4266 0.0826 -0.0031 -0.0070 559 TYR A CD2 4319 C CE1 . TYR A 566 ? 0.3787 0.3104 0.4138 0.0868 -0.0085 0.0004 559 TYR A CE1 4320 C CE2 . TYR A 566 ? 0.3914 0.3194 0.4428 0.0896 -0.0079 -0.0030 559 TYR A CE2 4321 C CZ . TYR A 566 ? 0.3896 0.3169 0.4295 0.0917 -0.0106 0.0007 559 TYR A CZ 4322 O OH . TYR A 566 ? 0.4201 0.3417 0.4526 0.0991 -0.0157 0.0047 559 TYR A OH 4323 N N . GLU A 567 ? 0.2949 0.2506 0.3743 0.0729 0.0001 -0.0235 560 GLU A N 4324 C CA . GLU A 567 ? 0.3057 0.2639 0.3943 0.0776 -0.0032 -0.0263 560 GLU A CA 4325 C C . GLU A 567 ? 0.2990 0.2680 0.3938 0.0766 -0.0051 -0.0306 560 GLU A C 4326 O O . GLU A 567 ? 0.3077 0.2795 0.4076 0.0810 -0.0101 -0.0315 560 GLU A O 4327 C CB . GLU A 567 ? 0.3140 0.2694 0.4109 0.0778 0.0002 -0.0295 560 GLU A CB 4328 C CG . GLU A 567 ? 0.3355 0.2794 0.4288 0.0801 0.0012 -0.0250 560 GLU A CG 4329 C CD . GLU A 567 ? 0.3603 0.2998 0.4468 0.0749 0.0056 -0.0226 560 GLU A CD 4330 O OE1 . GLU A 567 ? 0.3476 0.2924 0.4348 0.0695 0.0085 -0.0262 560 GLU A OE1 4331 O OE2 . GLU A 567 ? 0.3735 0.3042 0.4543 0.0764 0.0061 -0.0170 560 GLU A OE2 4332 N N . LEU A 568 ? 0.2840 0.2588 0.3787 0.0708 -0.0015 -0.0334 561 LEU A N 4333 C CA . LEU A 568 ? 0.2827 0.2672 0.3830 0.0693 -0.0027 -0.0367 561 LEU A CA 4334 C C . LEU A 568 ? 0.2874 0.2730 0.3837 0.0723 -0.0090 -0.0341 561 LEU A C 4335 O O . LEU A 568 ? 0.2954 0.2867 0.4000 0.0748 -0.0130 -0.0365 561 LEU A O 4336 C CB . LEU A 568 ? 0.2778 0.2666 0.3750 0.0627 0.0019 -0.0384 561 LEU A CB 4337 C CG . LEU A 568 ? 0.2763 0.2745 0.3782 0.0606 0.0012 -0.0410 561 LEU A CG 4338 C CD1 . LEU A 568 ? 0.2732 0.2774 0.3887 0.0623 0.0021 -0.0455 561 LEU A CD1 4339 C CD2 . LEU A 568 ? 0.2881 0.2890 0.3848 0.0546 0.0056 -0.0418 561 LEU A CD2 4340 N N . VAL A 569 ? 0.2947 0.2751 0.3789 0.0718 -0.0097 -0.0296 562 VAL A N 4341 C CA . VAL A 569 ? 0.2927 0.2732 0.3707 0.0747 -0.0155 -0.0272 562 VAL A CA 4342 C C . VAL A 569 ? 0.3172 0.2935 0.3961 0.0822 -0.0215 -0.0256 562 VAL A C 4343 O O . VAL A 569 ? 0.3159 0.2965 0.3992 0.0853 -0.0275 -0.0275 562 VAL A O 4344 C CB . VAL A 569 ? 0.2955 0.2710 0.3598 0.0729 -0.0142 -0.0226 562 VAL A CB 4345 C CG1 . VAL A 569 ? 0.2998 0.2746 0.3567 0.0768 -0.0204 -0.0205 562 VAL A CG1 4346 C CG2 . VAL A 569 ? 0.2948 0.2750 0.3585 0.0660 -0.0094 -0.0244 562 VAL A CG2 4347 N N . GLU A 570 ? 0.3278 0.2954 0.4027 0.0850 -0.0201 -0.0222 563 GLU A N 4348 C CA . GLU A 570 ? 0.3531 0.3147 0.4262 0.0924 -0.0255 -0.0196 563 GLU A CA 4349 C C . GLU A 570 ? 0.3523 0.3193 0.4398 0.0957 -0.0291 -0.0242 563 GLU A C 4350 O O . GLU A 570 ? 0.3572 0.3239 0.4455 0.1016 -0.0362 -0.0239 563 GLU A O 4351 C CB . GLU A 570 ? 0.3711 0.3220 0.4381 0.0940 -0.0220 -0.0149 563 GLU A CB 4352 C CG . GLU A 570 ? 0.4254 0.3677 0.4861 0.1020 -0.0271 -0.0103 563 GLU A CG 4353 C CD . GLU A 570 ? 0.5088 0.4511 0.5809 0.1066 -0.0299 -0.0128 563 GLU A CD 4354 O OE1 . GLU A 570 ? 0.5007 0.4469 0.5845 0.1035 -0.0261 -0.0171 563 GLU A OE1 4355 O OE2 . GLU A 570 ? 0.5455 0.4836 0.6143 0.1138 -0.0362 -0.0105 563 GLU A OE2 4356 N N . LYS A 571 ? 0.3343 0.3064 0.4332 0.0921 -0.0243 -0.0286 564 LYS A N 4357 C CA . LYS A 571 ? 0.3331 0.3105 0.4469 0.0953 -0.0267 -0.0330 564 LYS A CA 4358 C C . LYS A 571 ? 0.3310 0.3196 0.4545 0.0939 -0.0296 -0.0374 564 LYS A C 4359 O O . LYS A 571 ? 0.3479 0.3400 0.4805 0.0986 -0.0356 -0.0393 564 LYS A O 4360 C CB . LYS A 571 ? 0.3244 0.3019 0.4467 0.0930 -0.0203 -0.0361 564 LYS A CB 4361 C CG . LYS A 571 ? 0.3574 0.3239 0.4743 0.0954 -0.0184 -0.0325 564 LYS A CG 4362 C CD . LYS A 571 ? 0.3956 0.3624 0.5212 0.0929 -0.0122 -0.0366 564 LYS A CD 4363 C CE . LYS A 571 ? 0.4462 0.4016 0.5673 0.0941 -0.0095 -0.0335 564 LYS A CE 4364 N NZ . LYS A 571 ? 0.5030 0.4511 0.6228 0.1014 -0.0147 -0.0295 564 LYS A NZ 4365 N N . PHE A 572 ? 0.3120 0.3059 0.4342 0.0876 -0.0255 -0.0388 565 PHE A N 4366 C CA . PHE A 572 ? 0.3037 0.3084 0.4375 0.0850 -0.0259 -0.0432 565 PHE A CA 4367 C C . PHE A 572 ? 0.3047 0.3124 0.4332 0.0835 -0.0300 -0.0424 565 PHE A C 4368 O O . PHE A 572 ? 0.3062 0.3215 0.4453 0.0837 -0.0336 -0.0455 565 PHE A O 4369 C CB . PHE A 572 ? 0.2984 0.3080 0.4379 0.0792 -0.0175 -0.0464 565 PHE A CB 4370 C CG . PHE A 572 ? 0.3262 0.3340 0.4731 0.0812 -0.0138 -0.0486 565 PHE A CG 4371 C CD1 . PHE A 572 ? 0.3627 0.3745 0.5238 0.0857 -0.0168 -0.0515 565 PHE A CD1 4372 C CD2 . PHE A 572 ? 0.3286 0.3305 0.4690 0.0787 -0.0079 -0.0479 565 PHE A CD2 4373 C CE1 . PHE A 572 ? 0.3521 0.3619 0.5202 0.0879 -0.0135 -0.0536 565 PHE A CE1 4374 C CE2 . PHE A 572 ? 0.3445 0.3441 0.4918 0.0807 -0.0048 -0.0503 565 PHE A CE2 4375 C CZ . PHE A 572 ? 0.3658 0.3691 0.5266 0.0855 -0.0075 -0.0530 565 PHE A CZ 4376 N N . TYR A 573 ? 0.3032 0.3051 0.4164 0.0819 -0.0295 -0.0384 566 TYR A N 4377 C CA . TYR A 573 ? 0.2974 0.3022 0.4056 0.0801 -0.0328 -0.0381 566 TYR A CA 4378 C C . TYR A 573 ? 0.3104 0.3102 0.4101 0.0860 -0.0411 -0.0356 566 TYR A C 4379 O O . TYR A 573 ? 0.3233 0.3276 0.4269 0.0873 -0.0472 -0.0377 566 TYR A O 4380 C CB . TYR A 573 ? 0.2823 0.2855 0.3798 0.0742 -0.0270 -0.0360 566 TYR A CB 4381 C CG . TYR A 573 ? 0.2819 0.2923 0.3876 0.0681 -0.0209 -0.0394 566 TYR A CG 4382 C CD1 . TYR A 573 ? 0.2710 0.2814 0.3812 0.0663 -0.0147 -0.0409 566 TYR A CD1 4383 C CD2 . TYR A 573 ? 0.2989 0.3159 0.4076 0.0644 -0.0212 -0.0411 566 TYR A CD2 4384 C CE1 . TYR A 573 ? 0.2774 0.2939 0.3936 0.0613 -0.0088 -0.0440 566 TYR A CE1 4385 C CE2 . TYR A 573 ? 0.3108 0.3340 0.4263 0.0591 -0.0149 -0.0437 566 TYR A CE2 4386 C CZ . TYR A 573 ? 0.2876 0.3104 0.4063 0.0578 -0.0088 -0.0451 566 TYR A CZ 4387 O OH . TYR A 573 ? 0.2938 0.3221 0.4178 0.0534 -0.0026 -0.0476 566 TYR A OH 4388 N N . ASP A 574 ? 0.3100 0.3001 0.3975 0.0897 -0.0413 -0.0310 567 ASP A N 4389 C CA . ASP A 574 ? 0.3181 0.3023 0.3932 0.0951 -0.0481 -0.0278 567 ASP A CA 4390 C C . ASP A 574 ? 0.3336 0.3077 0.4004 0.1011 -0.0492 -0.0234 567 ASP A C 4391 O O . ASP A 574 ? 0.3406 0.3068 0.3931 0.1018 -0.0469 -0.0184 567 ASP A O 4392 C CB . ASP A 574 ? 0.3131 0.2955 0.3752 0.0915 -0.0458 -0.0254 567 ASP A CB 4393 C CG . ASP A 574 ? 0.3224 0.3008 0.3727 0.0966 -0.0532 -0.0237 567 ASP A CG 4394 O OD1 . ASP A 574 ? 0.3592 0.3375 0.4123 0.1025 -0.0612 -0.0252 567 ASP A OD1 4395 O OD2 . ASP A 574 ? 0.3272 0.3024 0.3654 0.0948 -0.0509 -0.0209 567 ASP A OD2 4396 N N . PRO A 575 ? 0.3448 0.3191 0.4213 0.1057 -0.0526 -0.0250 568 PRO A N 4397 C CA . PRO A 575 ? 0.3649 0.3292 0.4344 0.1112 -0.0528 -0.0205 568 PRO A CA 4398 C C . PRO A 575 ? 0.3766 0.3318 0.4285 0.1171 -0.0576 -0.0153 568 PRO A C 4399 O O . PRO A 575 ? 0.3955 0.3408 0.4368 0.1194 -0.0545 -0.0097 568 PRO A O 4400 C CB . PRO A 575 ? 0.3727 0.3401 0.4568 0.1157 -0.0575 -0.0240 568 PRO A CB 4401 C CG . PRO A 575 ? 0.3679 0.3475 0.4678 0.1119 -0.0582 -0.0303 568 PRO A CG 4402 C CD . PRO A 575 ? 0.3448 0.3286 0.4398 0.1055 -0.0552 -0.0308 568 PRO A CD 4403 N N A MET A 576 ? 0.3737 0.3318 0.4223 0.1195 -0.0649 -0.0171 569 MET A N 4404 N N B MET A 576 ? 0.3746 0.3328 0.4233 0.1195 -0.0650 -0.0172 569 MET A N 4405 C CA A MET A 576 ? 0.3946 0.3441 0.4252 0.1258 -0.0700 -0.0127 569 MET A CA 4406 C CA B MET A 576 ? 0.3882 0.3381 0.4191 0.1258 -0.0703 -0.0130 569 MET A CA 4407 C C A MET A 576 ? 0.3878 0.3350 0.4044 0.1221 -0.0657 -0.0099 569 MET A C 4408 C C B MET A 576 ? 0.3826 0.3301 0.3995 0.1222 -0.0659 -0.0101 569 MET A C 4409 O O A MET A 576 ? 0.3905 0.3300 0.3903 0.1270 -0.0682 -0.0058 569 MET A O 4410 O O B MET A 576 ? 0.3898 0.3297 0.3901 0.1270 -0.0687 -0.0061 569 MET A O 4411 C CB A MET A 576 ? 0.4076 0.3602 0.4411 0.1319 -0.0816 -0.0165 569 MET A CB 4412 C CB B MET A 576 ? 0.3954 0.3492 0.4297 0.1311 -0.0816 -0.0171 569 MET A CB 4413 C CG A MET A 576 ? 0.4560 0.4096 0.5022 0.1371 -0.0868 -0.0186 569 MET A CG 4414 C CG B MET A 576 ? 0.4158 0.3724 0.4646 0.1357 -0.0873 -0.0202 569 MET A CG 4415 S SD A MET A 576 ? 0.5588 0.4991 0.5947 0.1428 -0.0838 -0.0115 569 MET A SD 4416 S SD B MET A 576 ? 0.4556 0.4158 0.5071 0.1424 -0.1017 -0.0248 569 MET A SD 4417 C CE A MET A 576 ? 0.5771 0.5063 0.5890 0.1520 -0.0915 -0.0064 569 MET A CE 4418 C CE B MET A 576 ? 0.4161 0.3922 0.4932 0.1350 -0.1010 -0.0328 569 MET A CE 4419 N N . PHE A 577 ? 0.3618 0.3157 0.3853 0.1139 -0.0593 -0.0121 570 PHE A N 4420 C CA . PHE A 577 ? 0.3519 0.3048 0.3645 0.1098 -0.0550 -0.0100 570 PHE A CA 4421 C C . PHE A 577 ? 0.3557 0.3099 0.3607 0.1125 -0.0620 -0.0116 570 PHE A C 4422 O O . PHE A 577 ? 0.3688 0.3196 0.3607 0.1119 -0.0601 -0.0089 570 PHE A O 4423 C CB . PHE A 577 ? 0.3560 0.2994 0.3564 0.1099 -0.0479 -0.0033 570 PHE A CB 4424 C CG . PHE A 577 ? 0.3616 0.3065 0.3714 0.1040 -0.0399 -0.0034 570 PHE A CG 4425 C CD1 . PHE A 577 ? 0.3535 0.3019 0.3641 0.0966 -0.0333 -0.0038 570 PHE A CD1 4426 C CD2 . PHE A 577 ? 0.3605 0.3036 0.3793 0.1058 -0.0395 -0.0038 570 PHE A CD2 4427 C CE1 . PHE A 577 ? 0.3384 0.2883 0.3577 0.0913 -0.0267 -0.0047 570 PHE A CE1 4428 C CE2 . PHE A 577 ? 0.3678 0.3124 0.3957 0.1005 -0.0324 -0.0048 570 PHE A CE2 4429 C CZ . PHE A 577 ? 0.3328 0.2808 0.3606 0.0932 -0.0262 -0.0054 570 PHE A CZ 4430 N N . LYS A 578 ? 0.3609 0.3206 0.3756 0.1152 -0.0702 -0.0166 571 LYS A N 4431 C CA . LYS A 578 ? 0.3571 0.3184 0.3669 0.1178 -0.0781 -0.0193 571 LYS A CA 4432 C C . LYS A 578 ? 0.3424 0.3117 0.3585 0.1104 -0.0755 -0.0228 571 LYS A C 4433 O O . LYS A 578 ? 0.3515 0.3197 0.3586 0.1112 -0.0788 -0.0234 571 LYS A O 4434 C CB . LYS A 578 ? 0.3645 0.3286 0.3832 0.1236 -0.0887 -0.0236 571 LYS A CB 4435 C CG . LYS A 578 ? 0.3531 0.3282 0.3954 0.1193 -0.0888 -0.0292 571 LYS A CG 4436 C CD . LYS A 578 ? 0.3933 0.3705 0.4443 0.1259 -0.0998 -0.0330 571 LYS A CD 4437 C CE . LYS A 578 ? 0.4263 0.4152 0.5018 0.1216 -0.0998 -0.0388 571 LYS A CE 4438 N NZ . LYS A 578 ? 0.4569 0.4495 0.5432 0.1275 -0.1118 -0.0435 571 LYS A NZ 4439 N N . TYR A 579 ? 0.3341 0.3110 0.3652 0.1036 -0.0698 -0.0253 572 TYR A N 4440 C CA . TYR A 579 ? 0.3220 0.3056 0.3579 0.0966 -0.0667 -0.0279 572 TYR A CA 4441 C C . TYR A 579 ? 0.3174 0.2961 0.3394 0.0935 -0.0597 -0.0235 572 TYR A C 4442 O O . TYR A 579 ? 0.3122 0.2920 0.3288 0.0915 -0.0602 -0.0240 572 TYR A O 4443 C CB . TYR A 579 ? 0.3145 0.3073 0.3694 0.0906 -0.0623 -0.0316 572 TYR A CB 4444 C CG . TYR A 579 ? 0.3304 0.3285 0.4005 0.0938 -0.0690 -0.0360 572 TYR A CG 4445 C CD1 . TYR A 579 ? 0.3459 0.3472 0.4198 0.0962 -0.0778 -0.0396 572 TYR A CD1 4446 C CD2 . TYR A 579 ? 0.3558 0.3553 0.4364 0.0949 -0.0671 -0.0366 572 TYR A CD2 4447 C CE1 . TYR A 579 ? 0.3935 0.3999 0.4826 0.0994 -0.0845 -0.0437 572 TYR A CE1 4448 C CE2 . TYR A 579 ? 0.3826 0.3873 0.4780 0.0982 -0.0734 -0.0406 572 TYR A CE2 4449 C CZ . TYR A 579 ? 0.3924 0.4007 0.4923 0.1003 -0.0821 -0.0441 572 TYR A CZ 4450 O OH . TYR A 579 ? 0.4369 0.4508 0.5533 0.1036 -0.0886 -0.0483 572 TYR A OH 4451 N N . HIS A 580 ? 0.3137 0.2871 0.3306 0.0934 -0.0535 -0.0192 573 HIS A N 4452 C CA . HIS A 580 ? 0.3192 0.2872 0.3231 0.0913 -0.0472 -0.0145 573 HIS A CA 4453 C C . HIS A 580 ? 0.3268 0.2885 0.3142 0.0968 -0.0514 -0.0120 573 HIS A C 4454 O O . HIS A 580 ? 0.3211 0.2826 0.3011 0.0943 -0.0490 -0.0110 573 HIS A O 4455 C CB . HIS A 580 ? 0.3199 0.2817 0.3210 0.0918 -0.0412 -0.0101 573 HIS A CB 4456 C CG . HIS A 580 ? 0.3276 0.2940 0.3405 0.0855 -0.0348 -0.0118 573 HIS A CG 4457 N ND1 . HIS A 580 ? 0.3213 0.2926 0.3483 0.0850 -0.0357 -0.0156 573 HIS A ND1 4458 C CD2 . HIS A 580 ? 0.3429 0.3093 0.3553 0.0799 -0.0273 -0.0102 573 HIS A CD2 4459 C CE1 . HIS A 580 ? 0.3451 0.3189 0.3786 0.0794 -0.0291 -0.0164 573 HIS A CE1 4460 N NE2 . HIS A 580 ? 0.3629 0.3335 0.3876 0.0763 -0.0242 -0.0133 573 HIS A NE2 4461 N N . LEU A 581 ? 0.3417 0.2982 0.3231 0.1044 -0.0579 -0.0110 574 LEU A N 4462 C CA . LEU A 581 ? 0.3473 0.2971 0.3116 0.1104 -0.0623 -0.0088 574 LEU A CA 4463 C C . LEU A 581 ? 0.3498 0.3046 0.3147 0.1093 -0.0676 -0.0136 574 LEU A C 4464 O O . LEU A 581 ? 0.3466 0.2982 0.2990 0.1097 -0.0665 -0.0119 574 LEU A O 4465 C CB . LEU A 581 ? 0.3646 0.3075 0.3218 0.1195 -0.0691 -0.0073 574 LEU A CB 4466 C CG . LEU A 581 ? 0.3814 0.3165 0.3187 0.1267 -0.0739 -0.0051 574 LEU A CG 4467 C CD1 . LEU A 581 ? 0.3879 0.3165 0.3104 0.1258 -0.0651 0.0012 574 LEU A CD1 4468 C CD2 . LEU A 581 ? 0.3815 0.3098 0.3121 0.1359 -0.0811 -0.0036 574 LEU A CD2 4469 N N . THR A 582 ? 0.3332 0.2960 0.3136 0.1075 -0.0730 -0.0194 575 THR A N 4470 C CA . THR A 582 ? 0.3266 0.2946 0.3107 0.1055 -0.0780 -0.0243 575 THR A CA 4471 C C . THR A 582 ? 0.3168 0.2876 0.3001 0.0984 -0.0706 -0.0235 575 THR A C 4472 O O . THR A 582 ? 0.3240 0.2933 0.2988 0.0988 -0.0724 -0.0241 575 THR A O 4473 C CB . THR A 582 ? 0.3287 0.3053 0.3325 0.1040 -0.0837 -0.0303 575 THR A CB 4474 O OG1 . THR A 582 ? 0.3401 0.3135 0.3429 0.1118 -0.0925 -0.0314 575 THR A OG1 4475 C CG2 . THR A 582 ? 0.3274 0.3098 0.3376 0.1005 -0.0875 -0.0351 575 THR A CG2 4476 N N . VAL A 583 ? 0.3090 0.2833 0.3006 0.0923 -0.0625 -0.0222 576 VAL A N 4477 C CA . VAL A 583 ? 0.2935 0.2701 0.2841 0.0856 -0.0554 -0.0212 576 VAL A CA 4478 C C . VAL A 583 ? 0.3002 0.2693 0.2733 0.0879 -0.0518 -0.0162 576 VAL A C 4479 O O . VAL A 583 ? 0.3075 0.2773 0.2758 0.0854 -0.0503 -0.0163 576 VAL A O 4480 C CB . VAL A 583 ? 0.2806 0.2623 0.2834 0.0792 -0.0482 -0.0213 576 VAL A CB 4481 C CG1 . VAL A 583 ? 0.2660 0.2494 0.2663 0.0728 -0.0413 -0.0200 576 VAL A CG1 4482 C CG2 . VAL A 583 ? 0.3065 0.2964 0.3264 0.0769 -0.0514 -0.0265 576 VAL A CG2 4483 N N . ALA A 584 ? 0.3116 0.2734 0.2754 0.0926 -0.0503 -0.0117 577 ALA A N 4484 C CA . ALA A 584 ? 0.3179 0.2722 0.2651 0.0954 -0.0465 -0.0066 577 ALA A CA 4485 C C . ALA A 584 ? 0.3335 0.2849 0.2689 0.1004 -0.0528 -0.0080 577 ALA A C 4486 O O . ALA A 584 ? 0.3321 0.2814 0.2580 0.0999 -0.0496 -0.0062 577 ALA A O 4487 C CB . ALA A 584 ? 0.3293 0.2757 0.2691 0.1001 -0.0439 -0.0012 577 ALA A CB 4488 N N . GLN A 585 ? 0.3366 0.2878 0.2728 0.1055 -0.0619 -0.0115 578 GLN A N 4489 C CA . GLN A 585 ? 0.3379 0.2866 0.2640 0.1104 -0.0693 -0.0141 578 GLN A CA 4490 C C . GLN A 585 ? 0.3340 0.2887 0.2661 0.1050 -0.0699 -0.0183 578 GLN A C 4491 O O . GLN A 585 ? 0.3306 0.2820 0.2510 0.1073 -0.0712 -0.0185 578 GLN A O 4492 C CB . GLN A 585 ? 0.3546 0.3021 0.2818 0.1170 -0.0801 -0.0177 578 GLN A CB 4493 C CG . GLN A 585 ? 0.3747 0.3144 0.2923 0.1236 -0.0801 -0.0130 578 GLN A CG 4494 C CD . GLN A 585 ? 0.4206 0.3600 0.3414 0.1299 -0.0912 -0.0167 578 GLN A CD 4495 O OE1 . GLN A 585 ? 0.4088 0.3546 0.3411 0.1287 -0.0984 -0.0230 578 GLN A OE1 4496 N NE2 . GLN A 585 ? 0.4408 0.3727 0.3524 0.1367 -0.0925 -0.0127 578 GLN A NE2 4497 N N . VAL A 586 ? 0.3130 0.2763 0.2629 0.0982 -0.0686 -0.0215 579 VAL A N 4498 C CA . VAL A 586 ? 0.3024 0.2711 0.2587 0.0928 -0.0688 -0.0250 579 VAL A CA 4499 C C . VAL A 586 ? 0.2971 0.2646 0.2466 0.0889 -0.0602 -0.0212 579 VAL A C 4500 O O . VAL A 586 ? 0.2900 0.2561 0.2323 0.0893 -0.0610 -0.0219 579 VAL A O 4501 C CB . VAL A 586 ? 0.2925 0.2704 0.2695 0.0865 -0.0688 -0.0289 579 VAL A CB 4502 C CG1 . VAL A 586 ? 0.2946 0.2772 0.2772 0.0808 -0.0677 -0.0314 579 VAL A CG1 4503 C CG2 . VAL A 586 ? 0.3002 0.2805 0.2867 0.0902 -0.0779 -0.0333 579 VAL A CG2 4504 N N . ARG A 587 ? 0.2947 0.2629 0.2474 0.0852 -0.0523 -0.0176 580 ARG A N 4505 C CA . ARG A 587 ? 0.2920 0.2598 0.2402 0.0811 -0.0444 -0.0144 580 ARG A CA 4506 C C . ARG A 587 ? 0.3110 0.2711 0.2417 0.0866 -0.0432 -0.0106 580 ARG A C 4507 O O . ARG A 587 ? 0.3090 0.2688 0.2340 0.0855 -0.0410 -0.0101 580 ARG A O 4508 C CB . ARG A 587 ? 0.2941 0.2632 0.2486 0.0770 -0.0371 -0.0114 580 ARG A CB 4509 C CG . ARG A 587 ? 0.2727 0.2496 0.2435 0.0710 -0.0367 -0.0150 580 ARG A CG 4510 C CD . ARG A 587 ? 0.2950 0.2722 0.2708 0.0677 -0.0300 -0.0126 580 ARG A CD 4511 N NE . ARG A 587 ? 0.2680 0.2522 0.2579 0.0625 -0.0292 -0.0161 580 ARG A NE 4512 C CZ . ARG A 587 ? 0.2836 0.2694 0.2804 0.0595 -0.0245 -0.0157 580 ARG A CZ 4513 N NH1 . ARG A 587 ? 0.3157 0.2965 0.3078 0.0607 -0.0205 -0.0120 580 ARG A NH1 4514 N NH2 . ARG A 587 ? 0.2531 0.2452 0.2616 0.0552 -0.0236 -0.0190 580 ARG A NH2 4515 N N . GLY A 588 ? 0.3196 0.2734 0.2417 0.0927 -0.0441 -0.0075 581 GLY A N 4516 C CA . GLY A 588 ? 0.3317 0.2774 0.2360 0.0986 -0.0421 -0.0032 581 GLY A CA 4517 C C . GLY A 588 ? 0.3407 0.2837 0.2343 0.1036 -0.0487 -0.0063 581 GLY A C 4518 O O . GLY A 588 ? 0.3501 0.2895 0.2323 0.1053 -0.0454 -0.0042 581 GLY A O 4519 N N . GLY A 589 ? 0.3467 0.2915 0.2448 0.1059 -0.0581 -0.0115 582 GLY A N 4520 C CA . GLY A 589 ? 0.3548 0.2976 0.2451 0.1104 -0.0659 -0.0157 582 GLY A CA 4521 C C . GLY A 589 ? 0.3461 0.2930 0.2402 0.1053 -0.0642 -0.0182 582 GLY A C 4522 O O . GLY A 589 ? 0.3505 0.2934 0.2325 0.1090 -0.0658 -0.0190 582 GLY A O 4523 N N . MET A 590 ? 0.3334 0.2881 0.2437 0.0971 -0.0608 -0.0195 583 MET A N 4524 C CA . MET A 590 ? 0.3212 0.2796 0.2354 0.0920 -0.0586 -0.0212 583 MET A CA 4525 C C . MET A 590 ? 0.3218 0.2763 0.2242 0.0926 -0.0509 -0.0164 583 MET A C 4526 O O . MET A 590 ? 0.3280 0.2805 0.2230 0.0941 -0.0517 -0.0176 583 MET A O 4527 C CB . MET A 590 ? 0.3098 0.2766 0.2424 0.0835 -0.0557 -0.0226 583 MET A CB 4528 C CG . MET A 590 ? 0.3197 0.2910 0.2652 0.0825 -0.0632 -0.0280 583 MET A CG 4529 S SD . MET A 590 ? 0.3346 0.3151 0.3001 0.0733 -0.0586 -0.0290 583 MET A SD 4530 C CE . MET A 590 ? 0.3211 0.3039 0.2881 0.0684 -0.0569 -0.0304 583 MET A CE 4531 N N . VAL A 591 ? 0.3271 0.2805 0.2288 0.0914 -0.0435 -0.0112 584 VAL A N 4532 C CA . VAL A 591 ? 0.3355 0.2853 0.2275 0.0920 -0.0356 -0.0062 584 VAL A CA 4533 C C . VAL A 591 ? 0.3519 0.2938 0.2253 0.1003 -0.0373 -0.0050 584 VAL A C 4534 O O . VAL A 591 ? 0.3447 0.2851 0.2109 0.1010 -0.0343 -0.0043 584 VAL A O 4535 C CB . VAL A 591 ? 0.3298 0.2790 0.2249 0.0898 -0.0279 -0.0009 584 VAL A CB 4536 C CG1 . VAL A 591 ? 0.3330 0.2776 0.2177 0.0916 -0.0198 0.0047 584 VAL A CG1 4537 C CG2 . VAL A 591 ? 0.3135 0.2703 0.2255 0.0814 -0.0253 -0.0024 584 VAL A CG2 4538 N N . PHE A 592 ? 0.3560 0.2926 0.2213 0.1070 -0.0425 -0.0049 585 PHE A N 4539 C CA . PHE A 592 ? 0.3668 0.2950 0.2125 0.1158 -0.0447 -0.0038 585 PHE A CA 4540 C C . PHE A 592 ? 0.3763 0.3047 0.2177 0.1175 -0.0504 -0.0091 585 PHE A C 4541 O O . PHE A 592 ? 0.3962 0.3203 0.2248 0.1208 -0.0470 -0.0075 585 PHE A O 4542 C CB . PHE A 592 ? 0.3810 0.3042 0.2203 0.1226 -0.0514 -0.0039 585 PHE A CB 4543 C CG . PHE A 592 ? 0.4178 0.3312 0.2349 0.1322 -0.0524 -0.0015 585 PHE A CG 4544 C CD1 . PHE A 592 ? 0.4448 0.3515 0.2510 0.1362 -0.0457 0.0057 585 PHE A CD1 4545 C CD2 . PHE A 592 ? 0.4460 0.3566 0.2527 0.1372 -0.0596 -0.0064 585 PHE A CD2 4546 C CE1 . PHE A 592 ? 0.4752 0.3722 0.2591 0.1455 -0.0457 0.0085 585 PHE A CE1 4547 C CE2 . PHE A 592 ? 0.4544 0.3554 0.2388 0.1466 -0.0602 -0.0043 585 PHE A CE2 4548 C CZ . PHE A 592 ? 0.4805 0.3747 0.2530 0.1509 -0.0530 0.0034 585 PHE A CZ 4549 N N . GLU A 593 ? 0.3701 0.3035 0.2230 0.1147 -0.0584 -0.0154 586 GLU A N 4550 C CA . GLU A 593 ? 0.3948 0.3280 0.2450 0.1161 -0.0647 -0.0211 586 GLU A CA 4551 C C . GLU A 593 ? 0.3630 0.2993 0.2163 0.1109 -0.0581 -0.0203 586 GLU A C 4552 O O . GLU A 593 ? 0.3824 0.3149 0.2251 0.1144 -0.0586 -0.0215 586 GLU A O 4553 C CB . GLU A 593 ? 0.3995 0.3380 0.2645 0.1133 -0.0740 -0.0277 586 GLU A CB 4554 C CG . GLU A 593 ? 0.5168 0.4514 0.3765 0.1203 -0.0844 -0.0313 586 GLU A CG 4555 C CD . GLU A 593 ? 0.5876 0.5135 0.4262 0.1293 -0.0888 -0.0328 586 GLU A CD 4556 O OE1 . GLU A 593 ? 0.6416 0.5605 0.4641 0.1360 -0.0867 -0.0285 586 GLU A OE1 4557 O OE2 . GLU A 593 ? 0.6570 0.5824 0.4943 0.1298 -0.0935 -0.0377 586 GLU A OE2 4558 N N . LEU A 594 ? 0.3420 0.2849 0.2098 0.1029 -0.0522 -0.0183 587 LEU A N 4559 C CA . LEU A 594 ? 0.3376 0.2836 0.2089 0.0980 -0.0462 -0.0173 587 LEU A CA 4560 C C . LEU A 594 ? 0.3486 0.2894 0.2057 0.1019 -0.0387 -0.0124 587 LEU A C 4561 O O . LEU A 594 ? 0.3562 0.2965 0.2095 0.1021 -0.0367 -0.0130 587 LEU A O 4562 C CB . LEU A 594 ? 0.3210 0.2743 0.2088 0.0893 -0.0412 -0.0158 587 LEU A CB 4563 C CG . LEU A 594 ? 0.3112 0.2702 0.2138 0.0847 -0.0473 -0.0207 587 LEU A CG 4564 C CD1 . LEU A 594 ? 0.2984 0.2629 0.2140 0.0785 -0.0428 -0.0187 587 LEU A CD1 4565 C CD2 . LEU A 594 ? 0.3294 0.2908 0.2362 0.0815 -0.0489 -0.0240 587 LEU A CD2 4566 N N . ALA A 595 ? 0.3463 0.2831 0.1961 0.1053 -0.0344 -0.0073 588 ALA A N 4567 C CA . ALA A 595 ? 0.3737 0.3061 0.2121 0.1084 -0.0259 -0.0018 588 ALA A CA 4568 C C . ALA A 595 ? 0.3944 0.3183 0.2127 0.1180 -0.0285 -0.0021 588 ALA A C 4569 O O . ALA A 595 ? 0.4097 0.3300 0.2177 0.1211 -0.0216 0.0016 588 ALA A O 4570 C CB . ALA A 595 ? 0.3693 0.3007 0.2096 0.1073 -0.0188 0.0044 588 ALA A CB 4571 N N . ASN A 596 ? 0.4011 0.3220 0.2141 0.1227 -0.0382 -0.0065 589 ASN A N 4572 C CA . ASN A 596 ? 0.4210 0.3329 0.2128 0.1328 -0.0412 -0.0067 589 ASN A CA 4573 C C . ASN A 596 ? 0.4390 0.3488 0.2248 0.1367 -0.0506 -0.0139 589 ASN A C 4574 O O . ASN A 596 ? 0.4691 0.3714 0.2361 0.1447 -0.0512 -0.0141 589 ASN A O 4575 C CB . ASN A 596 ? 0.4286 0.3353 0.2127 0.1382 -0.0440 -0.0042 589 ASN A CB 4576 C CG A ASN A 596 ? 0.4498 0.3469 0.2120 0.1469 -0.0391 0.0011 589 ASN A CG 4577 C CG B ASN A 596 ? 0.4433 0.3481 0.2262 0.1373 -0.0334 0.0041 589 ASN A CG 4578 O OD1 A ASN A 596 ? 0.4500 0.3461 0.2090 0.1460 -0.0284 0.0067 589 ASN A OD1 4579 O OD1 B ASN A 596 ? 0.4765 0.3853 0.2723 0.1323 -0.0319 0.0060 589 ASN A OD1 4580 N ND2 A ASN A 596 ? 0.4940 0.3838 0.2410 0.1556 -0.0467 -0.0006 589 ASN A ND2 4581 N ND2 B ASN A 596 ? 0.4241 0.3230 0.1922 0.1420 -0.0257 0.0091 589 ASN A ND2 4582 N N . SER A 597 ? 0.4135 0.3295 0.2146 0.1314 -0.0577 -0.0198 590 SER A N 4583 C CA . SER A 597 ? 0.4322 0.3463 0.2299 0.1345 -0.0674 -0.0272 590 SER A CA 4584 C C . SER A 597 ? 0.4245 0.3366 0.2147 0.1356 -0.0631 -0.0276 590 SER A C 4585 O O . SER A 597 ? 0.4074 0.3242 0.2061 0.1296 -0.0549 -0.0246 590 SER A O 4586 C CB . SER A 597 ? 0.4273 0.3489 0.2458 0.1275 -0.0744 -0.0327 590 SER A CB 4587 O OG . SER A 597 ? 0.4727 0.3924 0.2897 0.1302 -0.0843 -0.0401 590 SER A OG 4588 N N . ILE A 598 ? 0.4225 0.3276 0.1968 0.1435 -0.0688 -0.0317 591 ILE A N 4589 C CA . ILE A 598 ? 0.4358 0.3386 0.2023 0.1453 -0.0649 -0.0325 591 ILE A CA 4590 C C . ILE A 598 ? 0.4182 0.3279 0.2024 0.1373 -0.0657 -0.0360 591 ILE A C 4591 O O . ILE A 598 ? 0.4161 0.3285 0.2038 0.1337 -0.0573 -0.0329 591 ILE A O 4592 C CB . ILE A 598 ? 0.4476 0.3411 0.1937 0.1557 -0.0726 -0.0376 591 ILE A CB 4593 C CG1 . ILE A 598 ? 0.5427 0.4282 0.2682 0.1645 -0.0701 -0.0328 591 ILE A CG1 4594 C CG2 . ILE A 598 ? 0.4920 0.3835 0.2320 0.1573 -0.0696 -0.0397 591 ILE A CG2 4595 C CD1 . ILE A 598 ? 0.6080 0.4932 0.3286 0.1640 -0.0557 -0.0235 591 ILE A CD1 4596 N N . VAL A 599 ? 0.4180 0.3304 0.2136 0.1345 -0.0757 -0.0423 592 VAL A N 4597 C CA . VAL A 599 ? 0.4115 0.3305 0.2256 0.1262 -0.0766 -0.0452 592 VAL A CA 4598 C C . VAL A 599 ? 0.3819 0.3086 0.2136 0.1183 -0.0739 -0.0421 592 VAL A C 4599 O O . VAL A 599 ? 0.3896 0.3167 0.2236 0.1193 -0.0783 -0.0425 592 VAL A O 4600 C CB . VAL A 599 ? 0.4167 0.3341 0.2347 0.1275 -0.0886 -0.0537 592 VAL A CB 4601 C CG1 . VAL A 599 ? 0.4322 0.3562 0.2701 0.1188 -0.0892 -0.0560 592 VAL A CG1 4602 C CG2 . VAL A 599 ? 0.4679 0.3769 0.2671 0.1361 -0.0916 -0.0573 592 VAL A CG2 4603 N N . LEU A 600 ? 0.3712 0.3040 0.2150 0.1107 -0.0669 -0.0391 593 LEU A N 4604 C CA . LEU A 600 ? 0.3578 0.2977 0.2179 0.1032 -0.0644 -0.0366 593 LEU A CA 4605 C C . LEU A 600 ? 0.3578 0.3005 0.2301 0.1010 -0.0736 -0.0419 593 LEU A C 4606 O O . LEU A 600 ? 0.3681 0.3103 0.2446 0.1008 -0.0804 -0.0475 593 LEU A O 4607 C CB . LEU A 600 ? 0.3421 0.2877 0.2132 0.0956 -0.0572 -0.0339 593 LEU A CB 4608 C CG . LEU A 600 ? 0.3656 0.3106 0.2297 0.0962 -0.0471 -0.0278 593 LEU A CG 4609 C CD1 . LEU A 600 ? 0.3676 0.3179 0.2429 0.0893 -0.0422 -0.0266 593 LEU A CD1 4610 C CD2 . LEU A 600 ? 0.3860 0.3318 0.2502 0.0959 -0.0429 -0.0231 593 LEU A CD2 4611 N N . PRO A 601 ? 0.3555 0.3012 0.2346 0.0993 -0.0740 -0.0403 594 PRO A N 4612 C CA . PRO A 601 ? 0.3604 0.3086 0.2507 0.0984 -0.0829 -0.0453 594 PRO A CA 4613 C C . PRO A 601 ? 0.3485 0.3045 0.2595 0.0894 -0.0820 -0.0465 594 PRO A C 4614 O O . PRO A 601 ? 0.3319 0.2931 0.2551 0.0855 -0.0816 -0.0459 594 PRO A O 4615 C CB . PRO A 601 ? 0.3651 0.3129 0.2528 0.1011 -0.0823 -0.0423 594 PRO A CB 4616 C CG . PRO A 601 ? 0.3581 0.3069 0.2431 0.0984 -0.0712 -0.0354 594 PRO A CG 4617 C CD . PRO A 601 ? 0.3574 0.3029 0.2320 0.0999 -0.0668 -0.0341 594 PRO A CD 4618 N N . PHE A 602 ? 0.3357 0.2923 0.2497 0.0863 -0.0810 -0.0479 595 PHE A N 4619 C CA . PHE A 602 ? 0.3253 0.2880 0.2567 0.0782 -0.0797 -0.0487 595 PHE A CA 4620 C C . PHE A 602 ? 0.3440 0.3053 0.2813 0.0785 -0.0882 -0.0550 595 PHE A C 4621 O O . PHE A 602 ? 0.3712 0.3268 0.2976 0.0833 -0.0917 -0.0577 595 PHE A O 4622 C CB . PHE A 602 ? 0.3105 0.2746 0.2413 0.0740 -0.0714 -0.0447 595 PHE A CB 4623 C CG . PHE A 602 ? 0.2964 0.2625 0.2242 0.0724 -0.0625 -0.0387 595 PHE A CG 4624 C CD1 . PHE A 602 ? 0.3189 0.2877 0.2509 0.0714 -0.0611 -0.0367 595 PHE A CD1 4625 C CD2 . PHE A 602 ? 0.3178 0.2834 0.2403 0.0714 -0.0557 -0.0351 595 PHE A CD2 4626 C CE1 . PHE A 602 ? 0.3215 0.2918 0.2516 0.0695 -0.0529 -0.0314 595 PHE A CE1 4627 C CE2 . PHE A 602 ? 0.3228 0.2904 0.2440 0.0695 -0.0478 -0.0298 595 PHE A CE2 4628 C CZ . PHE A 602 ? 0.3078 0.2775 0.2327 0.0686 -0.0466 -0.0281 595 PHE A CZ 4629 N N . ASP A 603 ? 0.3271 0.2933 0.2818 0.0733 -0.0913 -0.0575 596 ASP A N 4630 C CA . ASP A 603 ? 0.3270 0.2922 0.2901 0.0726 -0.0990 -0.0633 596 ASP A CA 4631 C C . ASP A 603 ? 0.3163 0.2855 0.2930 0.0646 -0.0944 -0.0620 596 ASP A C 4632 O O . ASP A 603 ? 0.3061 0.2814 0.2978 0.0588 -0.0921 -0.0608 596 ASP A O 4633 C CB . ASP A 603 ? 0.3323 0.2992 0.3054 0.0739 -0.1078 -0.0681 596 ASP A CB 4634 C CG . ASP A 603 ? 0.3709 0.3353 0.3508 0.0747 -0.1172 -0.0750 596 ASP A CG 4635 O OD1 . ASP A 603 ? 0.3484 0.3112 0.3299 0.0722 -0.1160 -0.0757 596 ASP A OD1 4636 O OD2 . ASP A 603 ? 0.4101 0.3741 0.3942 0.0780 -0.1261 -0.0799 596 ASP A OD2 4637 N N . CYS A 604 ? 0.3083 0.2741 0.2792 0.0647 -0.0929 -0.0619 597 CYS A N 4638 C CA . CYS A 604 ? 0.3106 0.2792 0.2927 0.0577 -0.0887 -0.0602 597 CYS A CA 4639 C C . CYS A 604 ? 0.3006 0.2720 0.3014 0.0532 -0.0936 -0.0638 597 CYS A C 4640 O O . CYS A 604 ? 0.2933 0.2684 0.3055 0.0467 -0.0891 -0.0614 597 CYS A O 4641 C CB . CYS A 604 ? 0.3034 0.2671 0.2763 0.0595 -0.0875 -0.0602 597 CYS A CB 4642 S SG . CYS A 604 ? 0.3811 0.3372 0.3476 0.0662 -0.0983 -0.0679 597 CYS A SG 4643 N N . ARG A 605 ? 0.3057 0.2751 0.3098 0.0566 -0.1030 -0.0698 598 ARG A N 4644 C CA . ARG A 605 ? 0.3084 0.2805 0.3321 0.0522 -0.1079 -0.0735 598 ARG A CA 4645 C C . ARG A 605 ? 0.3079 0.2877 0.3462 0.0469 -0.1035 -0.0707 598 ARG A C 4646 O O . ARG A 605 ? 0.3063 0.2897 0.3620 0.0411 -0.1029 -0.0711 598 ARG A O 4647 C CB . ARG A 605 ? 0.3182 0.2868 0.3427 0.0575 -0.1197 -0.0809 598 ARG A CB 4648 C CG . ARG A 605 ? 0.3277 0.2883 0.3385 0.0628 -0.1242 -0.0844 598 ARG A CG 4649 C CD . ARG A 605 ? 0.3297 0.2860 0.3366 0.0697 -0.1363 -0.0919 598 ARG A CD 4650 N NE . ARG A 605 ? 0.3885 0.3448 0.3832 0.0754 -0.1370 -0.0907 598 ARG A NE 4651 C CZ . ARG A 605 ? 0.4465 0.3992 0.4353 0.0822 -0.1470 -0.0962 598 ARG A CZ 4652 N NH1 . ARG A 605 ? 0.4456 0.3948 0.4400 0.0840 -0.1573 -0.1037 598 ARG A NH1 4653 N NH2 . ARG A 605 ? 0.4422 0.3945 0.4195 0.0874 -0.1471 -0.0943 598 ARG A NH2 4654 N N . ASP A 606 ? 0.3025 0.2845 0.3337 0.0490 -0.1001 -0.0678 599 ASP A N 4655 C CA . ASP A 606 ? 0.2891 0.2780 0.3327 0.0445 -0.0955 -0.0652 599 ASP A CA 4656 C C . ASP A 606 ? 0.2775 0.2694 0.3253 0.0378 -0.0858 -0.0599 599 ASP A C 4657 O O . ASP A 606 ? 0.2738 0.2710 0.3362 0.0326 -0.0824 -0.0588 599 ASP A O 4658 C CB . ASP A 606 ? 0.3011 0.2907 0.3352 0.0487 -0.0943 -0.0633 599 ASP A CB 4659 C CG . ASP A 606 ? 0.3488 0.3373 0.3843 0.0542 -0.1041 -0.0685 599 ASP A CG 4660 O OD1 . ASP A 606 ? 0.4423 0.4336 0.4942 0.0521 -0.1098 -0.0728 599 ASP A OD1 4661 O OD2 . ASP A 606 ? 0.3701 0.3549 0.3909 0.0606 -0.1064 -0.0684 599 ASP A OD2 4662 N N . TYR A 607 ? 0.2687 0.2571 0.3039 0.0383 -0.0815 -0.0569 600 TYR A N 4663 C CA . TYR A 607 ? 0.2502 0.2409 0.2886 0.0324 -0.0733 -0.0522 600 TYR A CA 4664 C C . TYR A 607 ? 0.2608 0.2515 0.3130 0.0279 -0.0751 -0.0539 600 TYR A C 4665 O O . TYR A 607 ? 0.2527 0.2471 0.3151 0.0223 -0.0697 -0.0510 600 TYR A O 4666 C CB . TYR A 607 ? 0.2494 0.2366 0.2725 0.0342 -0.0690 -0.0489 600 TYR A CB 4667 C CG . TYR A 607 ? 0.2481 0.2388 0.2679 0.0313 -0.0604 -0.0435 600 TYR A CG 4668 C CD1 . TYR A 607 ? 0.2494 0.2443 0.2795 0.0253 -0.0553 -0.0409 600 TYR A CD1 4669 C CD2 . TYR A 607 ? 0.2531 0.2424 0.2596 0.0348 -0.0575 -0.0411 600 TYR A CD2 4670 C CE1 . TYR A 607 ? 0.2572 0.2549 0.2837 0.0230 -0.0481 -0.0366 600 TYR A CE1 4671 C CE2 . TYR A 607 ? 0.2466 0.2391 0.2511 0.0321 -0.0501 -0.0365 600 TYR A CE2 4672 C CZ . TYR A 607 ? 0.2726 0.2691 0.2870 0.0263 -0.0459 -0.0347 600 TYR A CZ 4673 O OH . TYR A 607 ? 0.2594 0.2584 0.2713 0.0240 -0.0396 -0.0310 600 TYR A OH 4674 N N . ALA A 608 ? 0.2592 0.2454 0.3118 0.0306 -0.0825 -0.0585 601 ALA A N 4675 C CA . ALA A 608 ? 0.2606 0.2460 0.3269 0.0263 -0.0844 -0.0601 601 ALA A CA 4676 C C . ALA A 608 ? 0.2598 0.2510 0.3460 0.0217 -0.0843 -0.0609 601 ALA A C 4677 O O . ALA A 608 ? 0.2564 0.2492 0.3542 0.0160 -0.0800 -0.0586 601 ALA A O 4678 C CB . ALA A 608 ? 0.2620 0.2412 0.3260 0.0304 -0.0935 -0.0660 601 ALA A CB 4679 N N . VAL A 609 ? 0.2620 0.2558 0.3520 0.0245 -0.0891 -0.0642 602 VAL A N 4680 C CA . VAL A 609 ? 0.2696 0.2695 0.3790 0.0209 -0.0892 -0.0654 602 VAL A CA 4681 C C . VAL A 609 ? 0.2694 0.2746 0.3830 0.0157 -0.0786 -0.0594 602 VAL A C 4682 O O . VAL A 609 ? 0.2681 0.2763 0.3972 0.0101 -0.0749 -0.0581 602 VAL A O 4683 C CB . VAL A 609 ? 0.2795 0.2814 0.3906 0.0257 -0.0964 -0.0697 602 VAL A CB 4684 C CG1 . VAL A 609 ? 0.2980 0.3074 0.4309 0.0217 -0.0955 -0.0705 602 VAL A CG1 4685 C CG2 . VAL A 609 ? 0.3026 0.2992 0.4117 0.0305 -0.1076 -0.0762 602 VAL A CG2 4686 N N . VAL A 610 ? 0.2591 0.2648 0.3586 0.0175 -0.0734 -0.0558 603 VAL A N 4687 C CA . VAL A 610 ? 0.2467 0.2570 0.3491 0.0131 -0.0638 -0.0508 603 VAL A CA 4688 C C . VAL A 610 ? 0.2446 0.2533 0.3465 0.0084 -0.0575 -0.0466 603 VAL A C 4689 O O . VAL A 610 ? 0.2330 0.2454 0.3439 0.0036 -0.0511 -0.0437 603 VAL A O 4690 C CB . VAL A 610 ? 0.2624 0.2742 0.3528 0.0156 -0.0599 -0.0483 603 VAL A CB 4691 C CG1 . VAL A 610 ? 0.2731 0.2861 0.3643 0.0206 -0.0663 -0.0521 603 VAL A CG1 4692 C CG2 . VAL A 610 ? 0.2976 0.3051 0.3702 0.0177 -0.0576 -0.0455 603 VAL A CG2 4693 N N . LEU A 611 ? 0.2335 0.2367 0.3249 0.0100 -0.0594 -0.0465 604 LEU A N 4694 C CA . LEU A 611 ? 0.2295 0.2305 0.3198 0.0061 -0.0541 -0.0424 604 LEU A CA 4695 C C . LEU A 611 ? 0.2445 0.2466 0.3528 0.0012 -0.0538 -0.0428 604 LEU A C 4696 O O . LEU A 611 ? 0.2494 0.2524 0.3611 -0.0033 -0.0468 -0.0384 604 LEU A O 4697 C CB . LEU A 611 ? 0.2344 0.2292 0.3120 0.0090 -0.0569 -0.0427 604 LEU A CB 4698 C CG . LEU A 611 ? 0.2207 0.2147 0.2809 0.0127 -0.0545 -0.0406 604 LEU A CG 4699 C CD1 . LEU A 611 ? 0.2541 0.2422 0.3036 0.0167 -0.0584 -0.0421 604 LEU A CD1 4700 C CD2 . LEU A 611 ? 0.2493 0.2457 0.3051 0.0094 -0.0459 -0.0350 604 LEU A CD2 4701 N N . ARG A 612 ? 0.2404 0.2421 0.3601 0.0022 -0.0614 -0.0481 605 ARG A N 4702 C CA . ARG A 612 ? 0.2465 0.2494 0.3856 -0.0027 -0.0611 -0.0485 605 ARG A CA 4703 C C . ARG A 612 ? 0.2368 0.2467 0.3881 -0.0064 -0.0545 -0.0462 605 ARG A C 4704 O O . ARG A 612 ? 0.2343 0.2452 0.3952 -0.0114 -0.0483 -0.0426 605 ARG A O 4705 C CB . ARG A 612 ? 0.2541 0.2551 0.4041 -0.0008 -0.0714 -0.0553 605 ARG A CB 4706 C CG . ARG A 612 ? 0.2806 0.2834 0.4537 -0.0062 -0.0711 -0.0560 605 ARG A CG 4707 C CD . ARG A 612 ? 0.3140 0.3125 0.4885 -0.0107 -0.0656 -0.0514 605 ARG A CD 4708 N NE . ARG A 612 ? 0.3156 0.3160 0.5133 -0.0159 -0.0647 -0.0517 605 ARG A NE 4709 C CZ . ARG A 612 ? 0.3910 0.3883 0.6017 -0.0164 -0.0723 -0.0566 605 ARG A CZ 4710 N NH1 . ARG A 612 ? 0.3739 0.3655 0.5748 -0.0116 -0.0814 -0.0616 605 ARG A NH1 4711 N NH2 . ARG A 612 ? 0.3984 0.3979 0.6318 -0.0215 -0.0708 -0.0565 605 ARG A NH2 4712 N N . LYS A 613 ? 0.2404 0.2547 0.3909 -0.0037 -0.0557 -0.0479 606 LYS A N 4713 C CA . LYS A 613 ? 0.2434 0.2644 0.4041 -0.0066 -0.0491 -0.0459 606 LYS A CA 4714 C C . LYS A 613 ? 0.2336 0.2548 0.3860 -0.0098 -0.0385 -0.0394 606 LYS A C 4715 O O . LYS A 613 ? 0.2277 0.2519 0.3910 -0.0143 -0.0316 -0.0365 606 LYS A O 4716 C CB . LYS A 613 ? 0.2561 0.2805 0.4129 -0.0022 -0.0522 -0.0485 606 LYS A CB 4717 C CG . LYS A 613 ? 0.3035 0.3348 0.4704 -0.0043 -0.0460 -0.0471 606 LYS A CG 4718 C CD . LYS A 613 ? 0.3809 0.4148 0.5443 0.0007 -0.0503 -0.0500 606 LYS A CD 4719 C CE . LYS A 613 ? 0.3962 0.4266 0.5377 0.0044 -0.0492 -0.0480 606 LYS A CE 4720 N NZ . LYS A 613 ? 0.4291 0.4612 0.5678 0.0092 -0.0532 -0.0504 606 LYS A NZ 4721 N N . TYR A 614 ? 0.2201 0.2379 0.3534 -0.0074 -0.0372 -0.0372 607 TYR A N 4722 C CA . TYR A 614 ? 0.2100 0.2276 0.3339 -0.0098 -0.0283 -0.0316 607 TYR A CA 4723 C C . TYR A 614 ? 0.2119 0.2262 0.3392 -0.0138 -0.0248 -0.0282 607 TYR A C 4724 O O . TYR A 614 ? 0.2253 0.2409 0.3530 -0.0171 -0.0168 -0.0238 607 TYR A O 4725 C CB . TYR A 614 ? 0.2053 0.2202 0.3097 -0.0062 -0.0287 -0.0305 607 TYR A CB 4726 C CG . TYR A 614 ? 0.2092 0.2264 0.3084 -0.0021 -0.0314 -0.0330 607 TYR A CG 4727 C CD1 . TYR A 614 ? 0.2191 0.2417 0.3290 -0.0023 -0.0308 -0.0347 607 TYR A CD1 4728 C CD2 . TYR A 614 ? 0.2294 0.2433 0.3133 0.0021 -0.0343 -0.0333 607 TYR A CD2 4729 C CE1 . TYR A 614 ? 0.2360 0.2600 0.3405 0.0018 -0.0333 -0.0367 607 TYR A CE1 4730 C CE2 . TYR A 614 ? 0.2363 0.2515 0.3148 0.0060 -0.0363 -0.0350 607 TYR A CE2 4731 C CZ . TYR A 614 ? 0.2634 0.2834 0.3520 0.0058 -0.0360 -0.0366 607 TYR A CZ 4732 O OH . TYR A 614 ? 0.2631 0.2838 0.3460 0.0100 -0.0382 -0.0379 607 TYR A OH 4733 N N . ALA A 615 ? 0.2118 0.2214 0.3410 -0.0133 -0.0306 -0.0301 608 ALA A N 4734 C CA . ALA A 615 ? 0.2173 0.2230 0.3503 -0.0170 -0.0274 -0.0267 608 ALA A CA 4735 C C . ALA A 615 ? 0.2296 0.2387 0.3824 -0.0217 -0.0233 -0.0257 608 ALA A C 4736 O O . ALA A 615 ? 0.2380 0.2463 0.3927 -0.0255 -0.0156 -0.0206 608 ALA A O 4737 C CB . ALA A 615 ? 0.2279 0.2276 0.3596 -0.0151 -0.0351 -0.0297 608 ALA A CB 4738 N N . ASP A 616 ? 0.2384 0.2513 0.4064 -0.0214 -0.0283 -0.0306 609 ASP A N 4739 C CA . ASP A 616 ? 0.2532 0.2702 0.4420 -0.0258 -0.0242 -0.0299 609 ASP A CA 4740 C C . ASP A 616 ? 0.2409 0.2626 0.4276 -0.0278 -0.0136 -0.0252 609 ASP A C 4741 O O . ASP A 616 ? 0.2407 0.2634 0.4372 -0.0321 -0.0059 -0.0212 609 ASP A O 4742 C CB . ASP A 616 ? 0.2515 0.2732 0.4566 -0.0244 -0.0316 -0.0363 609 ASP A CB 4743 C CG . ASP A 616 ? 0.3139 0.3313 0.5254 -0.0231 -0.0421 -0.0416 609 ASP A CG 4744 O OD1 . ASP A 616 ? 0.3360 0.3475 0.5456 -0.0245 -0.0427 -0.0402 609 ASP A OD1 4745 O OD2 . ASP A 616 ? 0.3934 0.4136 0.6129 -0.0203 -0.0502 -0.0476 609 ASP A OD2 4746 N N . LYS A 617 ? 0.2351 0.2593 0.4096 -0.0245 -0.0134 -0.0259 610 LYS A N 4747 C CA . LYS A 617 ? 0.2468 0.2753 0.4188 -0.0256 -0.0045 -0.0227 610 LYS A CA 4748 C C . LYS A 617 ? 0.2470 0.2718 0.4071 -0.0278 0.0036 -0.0164 610 LYS A C 4749 O O . LYS A 617 ? 0.2492 0.2759 0.4149 -0.0310 0.0122 -0.0127 610 LYS A O 4750 C CB . LYS A 617 ? 0.2413 0.2723 0.4020 -0.0213 -0.0068 -0.0251 610 LYS A CB 4751 C CG . LYS A 617 ? 0.3040 0.3391 0.4624 -0.0221 0.0017 -0.0226 610 LYS A CG 4752 C CD . LYS A 617 ? 0.3660 0.4017 0.5106 -0.0179 -0.0006 -0.0243 610 LYS A CD 4753 C CE . LYS A 617 ? 0.4338 0.4746 0.5807 -0.0179 0.0058 -0.0238 610 LYS A CE 4754 N NZ . LYS A 617 ? 0.4820 0.5221 0.6141 -0.0142 0.0040 -0.0248 610 LYS A NZ 4755 N N . ILE A 618 ? 0.2413 0.2605 0.3853 -0.0260 0.0009 -0.0152 611 ILE A N 4756 C CA . ILE A 618 ? 0.2413 0.2568 0.3728 -0.0275 0.0076 -0.0095 611 ILE A CA 4757 C C . ILE A 618 ? 0.2394 0.2515 0.3807 -0.0316 0.0113 -0.0058 611 ILE A C 4758 O O . ILE A 618 ? 0.2311 0.2422 0.3697 -0.0340 0.0197 -0.0005 611 ILE A O 4759 C CB . ILE A 618 ? 0.2454 0.2564 0.3578 -0.0243 0.0037 -0.0092 611 ILE A CB 4760 C CG1 . ILE A 618 ? 0.2478 0.2562 0.3465 -0.0252 0.0105 -0.0037 611 ILE A CG1 4761 C CG2 . ILE A 618 ? 0.2461 0.2522 0.3595 -0.0232 -0.0039 -0.0113 611 ILE A CG2 4762 C CD1 . ILE A 618 ? 0.2579 0.2704 0.3504 -0.0246 0.0159 -0.0031 611 ILE A CD1 4763 N N . TYR A 619 ? 0.2340 0.2440 0.3874 -0.0323 0.0052 -0.0085 612 TYR A N 4764 C CA . TYR A 619 ? 0.2626 0.2695 0.4281 -0.0365 0.0085 -0.0053 612 TYR A CA 4765 C C . TYR A 619 ? 0.2631 0.2752 0.4436 -0.0401 0.0170 -0.0030 612 TYR A C 4766 O O . TYR A 619 ? 0.2599 0.2697 0.4418 -0.0432 0.0252 0.0028 612 TYR A O 4767 C CB . TYR A 619 ? 0.2543 0.2586 0.4317 -0.0363 -0.0007 -0.0100 612 TYR A CB 4768 C CG . TYR A 619 ? 0.3103 0.3127 0.5064 -0.0411 0.0023 -0.0078 612 TYR A CG 4769 C CD1 . TYR A 619 ? 0.3524 0.3476 0.5441 -0.0430 0.0052 -0.0028 612 TYR A CD1 4770 C CD2 . TYR A 619 ? 0.3748 0.3826 0.5932 -0.0437 0.0026 -0.0103 612 TYR A CD2 4771 C CE1 . TYR A 619 ? 0.3971 0.3900 0.6064 -0.0476 0.0084 -0.0002 612 TYR A CE1 4772 C CE2 . TYR A 619 ? 0.3962 0.4024 0.6335 -0.0484 0.0060 -0.0080 612 TYR A CE2 4773 C CZ . TYR A 619 ? 0.4314 0.4298 0.6635 -0.0504 0.0091 -0.0028 612 TYR A CZ 4774 O OH . TYR A 619 ? 0.5163 0.5124 0.7670 -0.0551 0.0128 0.0000 612 TYR A OH 4775 N N . SER A 620 ? 0.2573 0.2763 0.4486 -0.0393 0.0153 -0.0073 613 SER A N 4776 C CA . SER A 620 ? 0.2799 0.3046 0.4873 -0.0424 0.0232 -0.0058 613 SER A CA 4777 C C . SER A 620 ? 0.2779 0.3031 0.4724 -0.0427 0.0340 -0.0003 613 SER A C 4778 O O . SER A 620 ? 0.2937 0.3202 0.4973 -0.0460 0.0432 0.0039 613 SER A O 4779 C CB . SER A 620 ? 0.2803 0.3125 0.5014 -0.0408 0.0184 -0.0119 613 SER A CB 4780 O OG A SER A 620 ? 0.2804 0.3118 0.5147 -0.0406 0.0085 -0.0170 613 SER A OG 4781 O OG B SER A 620 ? 0.3146 0.3494 0.5214 -0.0371 0.0182 -0.0133 613 SER A OG 4782 N N . ILE A 621 ? 0.2696 0.2937 0.4432 -0.0393 0.0330 -0.0004 614 ILE A N 4783 C CA . ILE A 621 ? 0.2663 0.2899 0.4255 -0.0392 0.0420 0.0043 614 ILE A CA 4784 C C . ILE A 621 ? 0.2794 0.2963 0.4321 -0.0415 0.0476 0.0108 614 ILE A C 4785 O O . ILE A 621 ? 0.2850 0.3019 0.4380 -0.0436 0.0575 0.0156 614 ILE A O 4786 C CB . ILE A 621 ? 0.2687 0.2917 0.4076 -0.0351 0.0386 0.0025 614 ILE A CB 4787 C CG1 . ILE A 621 ? 0.2528 0.2823 0.3978 -0.0328 0.0355 -0.0028 614 ILE A CG1 4788 C CG2 . ILE A 621 ? 0.2732 0.2937 0.3949 -0.0349 0.0469 0.0075 614 ILE A CG2 4789 C CD1 . ILE A 621 ? 0.2510 0.2799 0.3785 -0.0287 0.0308 -0.0052 614 ILE A CD1 4790 N N . SER A 622 ? 0.2609 0.2719 0.4078 -0.0410 0.0414 0.0111 615 SER A N 4791 C CA . SER A 622 ? 0.2727 0.2765 0.4126 -0.0428 0.0456 0.0173 615 SER A CA 4792 C C . SER A 622 ? 0.2868 0.2903 0.4452 -0.0472 0.0520 0.0208 615 SER A C 4793 O O . SER A 622 ? 0.2852 0.2847 0.4388 -0.0491 0.0606 0.0274 615 SER A O 4794 C CB . SER A 622 ? 0.2712 0.2691 0.4042 -0.0412 0.0368 0.0160 615 SER A CB 4795 O OG . SER A 622 ? 0.2767 0.2675 0.4011 -0.0423 0.0405 0.0221 615 SER A OG 4796 N N . MET A 623 ? 0.2817 0.2890 0.4613 -0.0489 0.0478 0.0164 616 MET A N 4797 C CA . MET A 623 ? 0.3170 0.3244 0.5181 -0.0535 0.0531 0.0191 616 MET A CA 4798 C C . MET A 623 ? 0.3298 0.3421 0.5384 -0.0556 0.0650 0.0228 616 MET A C 4799 O O . MET A 623 ? 0.3495 0.3619 0.5761 -0.0596 0.0710 0.0259 616 MET A O 4800 C CB . MET A 623 ? 0.3069 0.3168 0.5287 -0.0544 0.0440 0.0129 616 MET A CB 4801 C CG . MET A 623 ? 0.3467 0.3490 0.5660 -0.0542 0.0359 0.0120 616 MET A CG 4802 S SD . MET A 623 ? 0.4580 0.4513 0.6805 -0.0584 0.0431 0.0203 616 MET A SD 4803 C CE . MET A 623 ? 0.4054 0.4037 0.6596 -0.0639 0.0495 0.0210 616 MET A CE 4804 N N A LYS A 624 ? 0.3399 0.3557 0.5352 -0.0530 0.0688 0.0225 617 LYS A N 4805 N N B LYS A 624 ? 0.3337 0.3496 0.5288 -0.0529 0.0685 0.0224 617 LYS A N 4806 C CA A LYS A 624 ? 0.3485 0.3673 0.5458 -0.0544 0.0813 0.0268 617 LYS A CA 4807 C CA B LYS A 624 ? 0.3392 0.3578 0.5338 -0.0540 0.0810 0.0267 617 LYS A CA 4808 C C A LYS A 624 ? 0.3535 0.3644 0.5368 -0.0555 0.0898 0.0352 617 LYS A C 4809 C C B LYS A 624 ? 0.3470 0.3579 0.5301 -0.0555 0.0897 0.0351 617 LYS A C 4810 O O A LYS A 624 ? 0.3545 0.3662 0.5394 -0.0570 0.1014 0.0401 617 LYS A O 4811 O O B LYS A 624 ? 0.3502 0.3620 0.5363 -0.0571 0.1012 0.0400 617 LYS A O 4812 C CB A LYS A 624 ? 0.3557 0.3800 0.5426 -0.0511 0.0827 0.0238 617 LYS A CB 4813 C CB B LYS A 624 ? 0.3429 0.3654 0.5216 -0.0501 0.0818 0.0242 617 LYS A CB 4814 C CG A LYS A 624 ? 0.3787 0.4099 0.5762 -0.0491 0.0738 0.0158 617 LYS A CG 4815 C CG B LYS A 624 ? 0.3526 0.3836 0.5439 -0.0487 0.0772 0.0173 617 LYS A CG 4816 C CD A LYS A 624 ? 0.4403 0.4790 0.6651 -0.0516 0.0764 0.0135 617 LYS A CD 4817 C CD B LYS A 624 ? 0.3983 0.4361 0.6099 -0.0510 0.0859 0.0178 617 LYS A CD 4818 C CE A LYS A 624 ? 0.4577 0.5029 0.6901 -0.0489 0.0674 0.0058 617 LYS A CE 4819 C CE B LYS A 624 ? 0.4092 0.4550 0.6268 -0.0484 0.0828 0.0115 617 LYS A CE 4820 N NZ A LYS A 624 ? 0.4589 0.5024 0.6988 -0.0485 0.0549 0.0011 617 LYS A NZ 4821 N NZ B LYS A 624 ? 0.4265 0.4798 0.6648 -0.0503 0.0911 0.0116 617 LYS A NZ 4822 N N . HIS A 625 ? 0.3391 0.3425 0.5091 -0.0546 0.0842 0.0369 618 HIS A N 4823 C CA . HIS A 625 ? 0.3415 0.3364 0.4966 -0.0550 0.0907 0.0448 618 HIS A CA 4824 C C . HIS A 625 ? 0.3434 0.3313 0.5067 -0.0575 0.0874 0.0475 618 HIS A C 4825 O O . HIS A 625 ? 0.3302 0.3111 0.4779 -0.0557 0.0829 0.0494 618 HIS A O 4826 C CB . HIS A 625 ? 0.3489 0.3403 0.4767 -0.0507 0.0873 0.0448 618 HIS A CB 4827 C CG . HIS A 625 ? 0.3585 0.3561 0.4773 -0.0479 0.0885 0.0412 618 HIS A CG 4828 N ND1 . HIS A 625 ? 0.4273 0.4263 0.5367 -0.0469 0.0977 0.0438 618 HIS A ND1 4829 C CD2 . HIS A 625 ? 0.3489 0.3512 0.4674 -0.0455 0.0797 0.0341 618 HIS A CD2 4830 C CE1 . HIS A 625 ? 0.3805 0.3851 0.4850 -0.0441 0.0940 0.0380 618 HIS A CE1 4831 N NE2 . HIS A 625 ? 0.3973 0.4038 0.5075 -0.0434 0.0832 0.0325 618 HIS A NE2 4832 N N . PRO A 626 ? 0.3454 0.3351 0.5338 -0.0617 0.0895 0.0477 619 PRO A N 4833 C CA . PRO A 626 ? 0.3463 0.3294 0.5448 -0.0641 0.0850 0.0490 619 PRO A CA 4834 C C . PRO A 626 ? 0.3570 0.3300 0.5416 -0.0646 0.0909 0.0577 619 PRO A C 4835 O O . PRO A 626 ? 0.3560 0.3222 0.5364 -0.0641 0.0842 0.0579 619 PRO A O 4836 C CB . PRO A 626 ? 0.3608 0.3484 0.5899 -0.0688 0.0884 0.0481 619 PRO A CB 4837 C CG . PRO A 626 ? 0.3617 0.3566 0.5935 -0.0691 0.0990 0.0497 619 PRO A CG 4838 C CD . PRO A 626 ? 0.3479 0.3457 0.5576 -0.0642 0.0957 0.0462 619 PRO A CD 4839 N N . GLN A 627 ? 0.3654 0.3372 0.5418 -0.0650 0.1031 0.0646 620 GLN A N 4840 C CA . GLN A 627 ? 0.3910 0.3525 0.5526 -0.0649 0.1089 0.0734 620 GLN A CA 4841 C C . GLN A 627 ? 0.3791 0.3354 0.5154 -0.0604 0.1012 0.0728 620 GLN A C 4842 O O . GLN A 627 ? 0.3750 0.3229 0.5060 -0.0603 0.0980 0.0762 620 GLN A O 4843 C CB . GLN A 627 ? 0.4255 0.3861 0.5800 -0.0654 0.1235 0.0810 620 GLN A CB 4844 C CG . GLN A 627 ? 0.5061 0.4553 0.6419 -0.0645 0.1291 0.0905 620 GLN A CG 4845 C CD . GLN A 627 ? 0.5762 0.5178 0.7270 -0.0683 0.1296 0.0952 620 GLN A CD 4846 O OE1 . GLN A 627 ? 0.5708 0.5060 0.7169 -0.0674 0.1208 0.0947 620 GLN A OE1 4847 N NE2 . GLN A 627 ? 0.6267 0.5688 0.7966 -0.0726 0.1400 0.0999 620 GLN A NE2 4848 N N . GLU A 628 ? 0.3481 0.3094 0.4698 -0.0568 0.0983 0.0685 621 GLU A N 4849 C CA . GLU A 628 ? 0.3425 0.3000 0.4420 -0.0526 0.0908 0.0673 621 GLU A CA 4850 C C . GLU A 628 ? 0.3293 0.2857 0.4347 -0.0520 0.0786 0.0620 621 GLU A C 4851 O O . GLU A 628 ? 0.3377 0.2877 0.4297 -0.0498 0.0735 0.0635 621 GLU A O 4852 C CB . GLU A 628 ? 0.3515 0.3149 0.4363 -0.0491 0.0905 0.0635 621 GLU A CB 4853 C CG . GLU A 628 ? 0.4105 0.3730 0.4829 -0.0485 0.1020 0.0691 621 GLU A CG 4854 C CD . GLU A 628 ? 0.4744 0.4420 0.5640 -0.0516 0.1120 0.0705 621 GLU A CD 4855 O OE1 . GLU A 628 ? 0.4654 0.4402 0.5756 -0.0537 0.1095 0.0651 621 GLU A OE1 4856 O OE2 . GLU A 628 ? 0.5526 0.5166 0.6348 -0.0519 0.1229 0.0773 621 GLU A OE2 4857 N N . MET A 629 ? 0.3098 0.2721 0.4347 -0.0537 0.0735 0.0555 622 MET A N 4858 C CA . MET A 629 ? 0.3003 0.2609 0.4300 -0.0527 0.0619 0.0502 622 MET A CA 4859 C C . MET A 629 ? 0.3126 0.2643 0.4489 -0.0550 0.0619 0.0547 622 MET A C 4860 O O . MET A 629 ? 0.3021 0.2488 0.4322 -0.0530 0.0541 0.0532 622 MET A O 4861 C CB . MET A 629 ? 0.2954 0.2636 0.4442 -0.0537 0.0562 0.0423 622 MET A CB 4862 C CG . MET A 629 ? 0.2950 0.2711 0.4358 -0.0506 0.0539 0.0370 622 MET A CG 4863 S SD . MET A 629 ? 0.3055 0.2899 0.4680 -0.0511 0.0464 0.0280 622 MET A SD 4864 C CE . MET A 629 ? 0.2976 0.2768 0.4598 -0.0491 0.0335 0.0231 622 MET A CE 4865 N N . LYS A 630 ? 0.3161 0.2655 0.4649 -0.0590 0.0709 0.0605 623 LYS A N 4866 C CA . LYS A 630 ? 0.3420 0.2819 0.4968 -0.0613 0.0719 0.0658 623 LYS A CA 4867 C C . LYS A 630 ? 0.3604 0.2917 0.4913 -0.0585 0.0738 0.0726 623 LYS A C 4868 O O . LYS A 630 ? 0.3575 0.2818 0.4839 -0.0571 0.0675 0.0729 623 LYS A O 4869 C CB . LYS A 630 ? 0.3571 0.2967 0.5320 -0.0665 0.0818 0.0708 623 LYS A CB 4870 C CG . LYS A 630 ? 0.3555 0.3030 0.5567 -0.0695 0.0788 0.0641 623 LYS A CG 4871 C CD . LYS A 630 ? 0.4143 0.3620 0.6365 -0.0748 0.0896 0.0694 623 LYS A CD 4872 C CE . LYS A 630 ? 0.4840 0.4405 0.7331 -0.0774 0.0853 0.0618 623 LYS A CE 4873 N NZ . LYS A 630 ? 0.5597 0.5228 0.8249 -0.0807 0.0963 0.0645 623 LYS A NZ 4874 N N . THR A 631 ? 0.3698 0.3018 0.4849 -0.0570 0.0820 0.0773 624 THR A N 4875 C CA . THR A 631 ? 0.4015 0.3256 0.4931 -0.0540 0.0844 0.0840 624 THR A CA 4876 C C . THR A 631 ? 0.3934 0.3160 0.4698 -0.0497 0.0738 0.0800 624 THR A C 4877 O O . THR A 631 ? 0.3987 0.3128 0.4658 -0.0481 0.0713 0.0840 624 THR A O 4878 C CB . THR A 631 ? 0.4188 0.3450 0.4951 -0.0526 0.0942 0.0882 624 THR A CB 4879 O OG1 . THR A 631 ? 0.4706 0.3966 0.5604 -0.0566 0.1056 0.0935 624 THR A OG1 4880 C CG2 . THR A 631 ? 0.4626 0.3803 0.5130 -0.0489 0.0954 0.0945 624 THR A CG2 4881 N N . TYR A 632 ? 0.3580 0.2887 0.4325 -0.0476 0.0676 0.0723 625 TYR A N 4882 C CA . TYR A 632 ? 0.3631 0.2936 0.4230 -0.0433 0.0586 0.0684 625 TYR A CA 4883 C C . TYR A 632 ? 0.3486 0.2801 0.4197 -0.0430 0.0484 0.0616 625 TYR A C 4884 O O . TYR A 632 ? 0.3463 0.2787 0.4074 -0.0395 0.0410 0.0577 625 TYR A O 4885 C CB . TYR A 632 ? 0.3501 0.2876 0.3966 -0.0406 0.0588 0.0651 625 TYR A CB 4886 C CG . TYR A 632 ? 0.3845 0.3198 0.4173 -0.0401 0.0683 0.0716 625 TYR A CG 4887 C CD1 . TYR A 632 ? 0.4328 0.3598 0.4481 -0.0378 0.0695 0.0779 625 TYR A CD1 4888 C CD2 . TYR A 632 ? 0.4045 0.3456 0.4412 -0.0416 0.0760 0.0715 625 TYR A CD2 4889 C CE1 . TYR A 632 ? 0.4755 0.3996 0.4766 -0.0369 0.0781 0.0840 625 TYR A CE1 4890 C CE2 . TYR A 632 ? 0.4415 0.3800 0.4645 -0.0408 0.0853 0.0774 625 TYR A CE2 4891 C CZ . TYR A 632 ? 0.4841 0.4139 0.4886 -0.0384 0.0861 0.0836 625 TYR A CZ 4892 O OH . TYR A 632 ? 0.5213 0.4479 0.5109 -0.0371 0.0950 0.0894 625 TYR A OH 4893 N N . SER A 633 ? 0.3367 0.2677 0.4287 -0.0466 0.0482 0.0604 626 SER A N 4894 C CA . SER A 633 ? 0.3285 0.2592 0.4317 -0.0463 0.0385 0.0538 626 SER A CA 4895 C C . SER A 633 ? 0.3102 0.2488 0.4098 -0.0433 0.0316 0.0457 626 SER A C 4896 O O . SER A 633 ? 0.3176 0.2553 0.4102 -0.0400 0.0236 0.0417 626 SER A O 4897 C CB A SER A 633 ? 0.3345 0.2562 0.4304 -0.0443 0.0335 0.0560 626 SER A CB 4898 C CB B SER A 633 ? 0.3384 0.2601 0.4336 -0.0442 0.0338 0.0562 626 SER A CB 4899 O OG A SER A 633 ? 0.3249 0.2385 0.4259 -0.0472 0.0395 0.0634 626 SER A OG 4900 O OG B SER A 633 ? 0.3578 0.2776 0.4669 -0.0447 0.0262 0.0510 626 SER A OG 4901 N N . VAL A 634 ? 0.3029 0.2494 0.4073 -0.0444 0.0353 0.0436 627 VAL A N 4902 C CA . VAL A 634 ? 0.3002 0.2542 0.4009 -0.0416 0.0298 0.0366 627 VAL A CA 4903 C C . VAL A 634 ? 0.3108 0.2676 0.4294 -0.0424 0.0228 0.0296 627 VAL A C 4904 O O . VAL A 634 ? 0.3182 0.2783 0.4541 -0.0457 0.0257 0.0288 627 VAL A O 4905 C CB . VAL A 634 ? 0.3000 0.2609 0.3980 -0.0421 0.0366 0.0371 627 VAL A CB 4906 C CG1 . VAL A 634 ? 0.2851 0.2530 0.3781 -0.0389 0.0309 0.0303 627 VAL A CG1 4907 C CG2 . VAL A 634 ? 0.3261 0.2834 0.4070 -0.0414 0.0439 0.0441 627 VAL A CG2 4908 N N . SER A 635 ? 0.3139 0.2690 0.4287 -0.0393 0.0139 0.0248 628 SER A N 4909 C CA . SER A 635 ? 0.3176 0.2743 0.4470 -0.0393 0.0062 0.0178 628 SER A CA 4910 C C . SER A 635 ? 0.3004 0.2627 0.4228 -0.0354 0.0001 0.0113 628 SER A C 4911 O O . SER A 635 ? 0.2922 0.2540 0.3983 -0.0318 -0.0017 0.0114 628 SER A O 4912 C CB . SER A 635 ? 0.3319 0.2807 0.4642 -0.0387 0.0002 0.0168 628 SER A CB 4913 O OG . SER A 635 ? 0.3718 0.3224 0.5186 -0.0387 -0.0070 0.0096 628 SER A OG 4914 N N . PHE A 636 ? 0.2916 0.2591 0.4272 -0.0359 -0.0030 0.0059 629 PHE A N 4915 C CA . PHE A 636 ? 0.2757 0.2476 0.4057 -0.0319 -0.0096 -0.0004 629 PHE A CA 4916 C C . PHE A 636 ? 0.2788 0.2471 0.4128 -0.0294 -0.0193 -0.0063 629 PHE A C 4917 O O . PHE A 636 ? 0.2641 0.2352 0.3947 -0.0259 -0.0252 -0.0119 629 PHE A O 4918 C CB . PHE A 636 ? 0.2716 0.2514 0.4111 -0.0328 -0.0079 -0.0031 629 PHE A CB 4919 C CG . PHE A 636 ? 0.2688 0.2529 0.3993 -0.0332 0.0000 0.0009 629 PHE A CG 4920 C CD1 . PHE A 636 ? 0.2612 0.2493 0.3798 -0.0297 -0.0015 -0.0014 629 PHE A CD1 4921 C CD2 . PHE A 636 ? 0.2908 0.2744 0.4247 -0.0369 0.0092 0.0069 629 PHE A CD2 4922 C CE1 . PHE A 636 ? 0.2667 0.2582 0.3766 -0.0299 0.0053 0.0017 629 PHE A CE1 4923 C CE2 . PHE A 636 ? 0.2833 0.2703 0.4073 -0.0367 0.0162 0.0101 629 PHE A CE2 4924 C CZ . PHE A 636 ? 0.2629 0.2538 0.3752 -0.0333 0.0140 0.0072 629 PHE A CZ 4925 N N . ASP A 637 ? 0.2792 0.2406 0.4192 -0.0310 -0.0207 -0.0050 630 ASP A N 4926 C CA . ASP A 637 ? 0.2793 0.2364 0.4242 -0.0289 -0.0299 -0.0110 630 ASP A CA 4927 C C . ASP A 637 ? 0.2778 0.2343 0.4059 -0.0231 -0.0354 -0.0146 630 ASP A C 4928 O O . ASP A 637 ? 0.2824 0.2394 0.4122 -0.0200 -0.0429 -0.0212 630 ASP A O 4929 C CB . ASP A 637 ? 0.2852 0.2340 0.4368 -0.0312 -0.0300 -0.0083 630 ASP A CB 4930 C CG . ASP A 637 ? 0.3102 0.2589 0.4830 -0.0369 -0.0263 -0.0064 630 ASP A CG 4931 O OD1 . ASP A 637 ? 0.3117 0.2672 0.4953 -0.0389 -0.0244 -0.0079 630 ASP A OD1 4932 O OD2 . ASP A 637 ? 0.3386 0.2802 0.5177 -0.0393 -0.0253 -0.0033 630 ASP A OD2 4933 N N . SER A 638 ? 0.2607 0.2161 0.3726 -0.0214 -0.0317 -0.0102 631 SER A N 4934 C CA . SER A 638 ? 0.2640 0.2192 0.3610 -0.0160 -0.0361 -0.0131 631 SER A CA 4935 C C . SER A 638 ? 0.2532 0.2148 0.3467 -0.0134 -0.0381 -0.0173 631 SER A C 4936 O O . SER A 638 ? 0.2488 0.2098 0.3364 -0.0089 -0.0441 -0.0222 631 SER A O 4937 C CB . SER A 638 ? 0.2671 0.2206 0.3493 -0.0149 -0.0318 -0.0077 631 SER A CB 4938 O OG . SER A 638 ? 0.2990 0.2574 0.3773 -0.0170 -0.0250 -0.0034 631 SER A OG 4939 N N . LEU A 639 ? 0.2330 0.2006 0.3294 -0.0158 -0.0329 -0.0152 632 LEU A N 4940 C CA . LEU A 639 ? 0.2324 0.2059 0.3259 -0.0133 -0.0346 -0.0187 632 LEU A CA 4941 C C . LEU A 639 ? 0.2487 0.2229 0.3538 -0.0123 -0.0417 -0.0253 632 LEU A C 4942 O O . LEU A 639 ? 0.2407 0.2157 0.3394 -0.0079 -0.0470 -0.0298 632 LEU A O 4943 C CB . LEU A 639 ? 0.2431 0.2223 0.3374 -0.0160 -0.0273 -0.0152 632 LEU A CB 4944 C CG . LEU A 639 ? 0.2307 0.2159 0.3223 -0.0136 -0.0285 -0.0184 632 LEU A CG 4945 C CD1 . LEU A 639 ? 0.2206 0.2052 0.2958 -0.0090 -0.0306 -0.0192 632 LEU A CD1 4946 C CD2 . LEU A 639 ? 0.2341 0.2242 0.3275 -0.0166 -0.0207 -0.0147 632 LEU A CD2 4947 N N . PHE A 640 ? 0.2358 0.2094 0.3578 -0.0161 -0.0420 -0.0259 633 PHE A N 4948 C CA . PHE A 640 ? 0.2512 0.2254 0.3855 -0.0150 -0.0498 -0.0326 633 PHE A CA 4949 C C . PHE A 640 ? 0.2552 0.2232 0.3832 -0.0107 -0.0580 -0.0374 633 PHE A C 4950 O O . PHE A 640 ? 0.2822 0.2508 0.4097 -0.0069 -0.0653 -0.0435 633 PHE A O 4951 C CB . PHE A 640 ? 0.2571 0.2320 0.4128 -0.0204 -0.0482 -0.0321 633 PHE A CB 4952 C CG . PHE A 640 ? 0.2667 0.2490 0.4305 -0.0234 -0.0419 -0.0298 633 PHE A CG 4953 C CD1 . PHE A 640 ? 0.2921 0.2804 0.4611 -0.0214 -0.0457 -0.0345 633 PHE A CD1 4954 C CD2 . PHE A 640 ? 0.3029 0.2862 0.4681 -0.0276 -0.0321 -0.0229 633 PHE A CD2 4955 C CE1 . PHE A 640 ? 0.2962 0.2915 0.4732 -0.0239 -0.0398 -0.0326 633 PHE A CE1 4956 C CE2 . PHE A 640 ? 0.3127 0.3030 0.4852 -0.0299 -0.0258 -0.0210 633 PHE A CE2 4957 C CZ . PHE A 640 ? 0.2971 0.2935 0.4757 -0.0281 -0.0297 -0.0260 633 PHE A CZ 4958 N N . SER A 641 ? 0.2596 0.2214 0.3824 -0.0110 -0.0570 -0.0347 634 SER A N 4959 C CA . SER A 641 ? 0.2727 0.2283 0.3882 -0.0065 -0.0640 -0.0390 634 SER A CA 4960 C C . SER A 641 ? 0.2652 0.2224 0.3635 -0.0006 -0.0660 -0.0412 634 SER A C 4961 O O . SER A 641 ? 0.2691 0.2243 0.3640 0.0040 -0.0733 -0.0472 634 SER A O 4962 C CB . SER A 641 ? 0.2723 0.2216 0.3840 -0.0075 -0.0614 -0.0348 634 SER A CB 4963 O OG . SER A 641 ? 0.3042 0.2475 0.4083 -0.0028 -0.0677 -0.0391 634 SER A OG 4964 N N . ALA A 642 ? 0.2497 0.2104 0.3371 -0.0005 -0.0596 -0.0363 635 ALA A N 4965 C CA . ALA A 642 ? 0.2394 0.2019 0.3115 0.0046 -0.0604 -0.0375 635 ALA A CA 4966 C C . ALA A 642 ? 0.2514 0.2176 0.3253 0.0070 -0.0645 -0.0422 635 ALA A C 4967 O O . ALA A 642 ? 0.2611 0.2259 0.3254 0.0124 -0.0691 -0.0460 635 ALA A O 4968 C CB . ALA A 642 ? 0.2491 0.2150 0.3120 0.0033 -0.0527 -0.0314 635 ALA A CB 4969 N N . VAL A 643 ? 0.2464 0.2175 0.3327 0.0033 -0.0627 -0.0418 636 VAL A N 4970 C CA . VAL A 643 ? 0.2432 0.2184 0.3328 0.0054 -0.0668 -0.0460 636 VAL A CA 4971 C C . VAL A 643 ? 0.2643 0.2356 0.3595 0.0084 -0.0765 -0.0531 636 VAL A C 4972 O O . VAL A 643 ? 0.2668 0.2380 0.3550 0.0134 -0.0819 -0.0573 636 VAL A O 4973 C CB . VAL A 643 ? 0.2475 0.2289 0.3506 0.0007 -0.0623 -0.0440 636 VAL A CB 4974 C CG1 . VAL A 643 ? 0.2690 0.2543 0.3787 0.0030 -0.0678 -0.0490 636 VAL A CG1 4975 C CG2 . VAL A 643 ? 0.2254 0.2104 0.3196 -0.0008 -0.0536 -0.0380 636 VAL A CG2 4976 N N . LYS A 644 ? 0.2699 0.2374 0.3768 0.0055 -0.0788 -0.0543 637 LYS A N 4977 C CA . LYS A 644 ? 0.2775 0.2405 0.3902 0.0082 -0.0886 -0.0615 637 LYS A CA 4978 C C . LYS A 644 ? 0.2817 0.2391 0.3760 0.0148 -0.0927 -0.0643 637 LYS A C 4979 O O . LYS A 644 ? 0.2857 0.2414 0.3757 0.0200 -0.1004 -0.0703 637 LYS A O 4980 C CB . LYS A 644 ? 0.2899 0.2488 0.4178 0.0034 -0.0892 -0.0613 637 LYS A CB 4981 C CG . LYS A 644 ? 0.3525 0.3055 0.4861 0.0061 -0.0996 -0.0691 637 LYS A CG 4982 C CD . LYS A 644 ? 0.4021 0.3514 0.5534 0.0006 -0.0994 -0.0683 637 LYS A CD 4983 C CE . LYS A 644 ? 0.4737 0.4165 0.6317 0.0031 -0.1102 -0.0765 637 LYS A CE 4984 N NZ . LYS A 644 ? 0.4967 0.4320 0.6378 0.0082 -0.1126 -0.0780 637 LYS A NZ 4985 N N . ASN A 645 ? 0.2751 0.2299 0.3584 0.0151 -0.0875 -0.0598 638 ASN A N 4986 C CA . ASN A 645 ? 0.2890 0.2391 0.3552 0.0214 -0.0899 -0.0618 638 ASN A CA 4987 C C . ASN A 645 ? 0.2836 0.2368 0.3363 0.0265 -0.0900 -0.0625 638 ASN A C 4988 O O . ASN A 645 ? 0.2982 0.2476 0.3405 0.0327 -0.0956 -0.0672 638 ASN A O 4989 C CB . ASN A 645 ? 0.2801 0.2280 0.3388 0.0204 -0.0838 -0.0563 638 ASN A CB 4990 C CG . ASN A 645 ? 0.3202 0.2627 0.3886 0.0174 -0.0850 -0.0563 638 ASN A CG 4991 O OD1 . ASN A 645 ? 0.3148 0.2543 0.3951 0.0165 -0.0912 -0.0611 638 ASN A OD1 4992 N ND2 . ASN A 645 ? 0.3009 0.2417 0.3647 0.0159 -0.0795 -0.0509 638 ASN A ND2 4993 N N . PHE A 646 ? 0.2606 0.2201 0.3128 0.0240 -0.0837 -0.0579 639 PHE A N 4994 C CA . PHE A 646 ? 0.2596 0.2219 0.3006 0.0282 -0.0832 -0.0580 639 PHE A CA 4995 C C . PHE A 646 ? 0.2765 0.2384 0.3208 0.0317 -0.0917 -0.0644 639 PHE A C 4996 O O . PHE A 646 ? 0.2887 0.2482 0.3200 0.0381 -0.0953 -0.0672 639 PHE A O 4997 C CB . PHE A 646 ? 0.2501 0.2192 0.2940 0.0242 -0.0759 -0.0527 639 PHE A CB 4998 C CG . PHE A 646 ? 0.2585 0.2301 0.2904 0.0281 -0.0740 -0.0517 639 PHE A CG 4999 C CD1 . PHE A 646 ? 0.2631 0.2355 0.2840 0.0285 -0.0675 -0.0469 639 PHE A CD1 5000 C CD2 . PHE A 646 ? 0.2620 0.2350 0.2941 0.0313 -0.0787 -0.0553 639 PHE A CD2 5001 C CE1 . PHE A 646 ? 0.2802 0.2545 0.2910 0.0318 -0.0654 -0.0457 639 PHE A CE1 5002 C CE2 . PHE A 646 ? 0.2769 0.2514 0.2975 0.0350 -0.0766 -0.0538 639 PHE A CE2 5003 C CZ . PHE A 646 ? 0.2842 0.2593 0.2942 0.0352 -0.0697 -0.0489 639 PHE A CZ 5004 N N . THR A 647 ? 0.2865 0.2503 0.3481 0.0278 -0.0948 -0.0667 640 THR A N 5005 C CA . THR A 647 ? 0.2982 0.2623 0.3659 0.0306 -0.1036 -0.0731 640 THR A CA 5006 C C . THR A 647 ? 0.3191 0.2758 0.3782 0.0367 -0.1122 -0.0794 640 THR A C 5007 O O . THR A 647 ? 0.3302 0.2852 0.3793 0.0430 -0.1179 -0.0834 640 THR A O 5008 C CB . THR A 647 ? 0.2988 0.2665 0.3893 0.0248 -0.1051 -0.0744 640 THR A CB 5009 O OG1 . THR A 647 ? 0.3000 0.2744 0.3966 0.0197 -0.0963 -0.0684 640 THR A OG1 5010 C CG2 . THR A 647 ? 0.3078 0.2767 0.4059 0.0278 -0.1148 -0.0813 640 THR A CG2 5011 N N . GLU A 648 ? 0.3162 0.2680 0.3783 0.0352 -0.1129 -0.0802 641 GLU A N 5012 C CA . GLU A 648 ? 0.3455 0.2895 0.3999 0.0408 -0.1209 -0.0865 641 GLU A CA 5013 C C . GLU A 648 ? 0.3427 0.2835 0.3740 0.0480 -0.1193 -0.0859 641 GLU A C 5014 O O . GLU A 648 ? 0.3428 0.2796 0.3636 0.0548 -0.1262 -0.0914 641 GLU A O 5015 C CB . GLU A 648 ? 0.3456 0.2848 0.4089 0.0373 -0.1212 -0.0869 641 GLU A CB 5016 C CG . GLU A 648 ? 0.4136 0.3539 0.5000 0.0318 -0.1255 -0.0898 641 GLU A CG 5017 C CD . GLU A 648 ? 0.4771 0.4131 0.5740 0.0271 -0.1238 -0.0882 641 GLU A CD 5018 O OE1 . GLU A 648 ? 0.5039 0.4409 0.6211 0.0217 -0.1257 -0.0893 641 GLU A OE1 5019 O OE2 . GLU A 648 ? 0.5387 0.4705 0.6245 0.0286 -0.1202 -0.0856 641 GLU A OE2 5020 N N . ILE A 649 ? 0.3219 0.2645 0.3452 0.0466 -0.1102 -0.0793 642 ILE A N 5021 C CA . ILE A 649 ? 0.3297 0.2698 0.3330 0.0528 -0.1075 -0.0781 642 ILE A CA 5022 C C . ILE A 649 ? 0.3286 0.2711 0.3221 0.0572 -0.1080 -0.0782 642 ILE A C 5023 O O . ILE A 649 ? 0.3362 0.2745 0.3140 0.0644 -0.1105 -0.0807 642 ILE A O 5024 C CB . ILE A 649 ? 0.3197 0.2616 0.3190 0.0499 -0.0978 -0.0710 642 ILE A CB 5025 C CG1 . ILE A 649 ? 0.3244 0.2618 0.3296 0.0477 -0.0985 -0.0715 642 ILE A CG1 5026 C CG2 . ILE A 649 ? 0.3427 0.2835 0.3234 0.0558 -0.0939 -0.0690 642 ILE A CG2 5027 C CD1 . ILE A 649 ? 0.3269 0.2669 0.3329 0.0432 -0.0896 -0.0642 642 ILE A CD1 5028 N N . ALA A 650 ? 0.3111 0.2601 0.3134 0.0531 -0.1053 -0.0753 643 ALA A N 5029 C CA . ALA A 650 ? 0.3262 0.2774 0.3205 0.0570 -0.1060 -0.0752 643 ALA A CA 5030 C C . ALA A 650 ? 0.3403 0.2874 0.3322 0.0628 -0.1168 -0.0827 643 ALA A C 5031 O O . ALA A 650 ? 0.3567 0.3011 0.3333 0.0696 -0.1188 -0.0838 643 ALA A O 5032 C CB . ALA A 650 ? 0.3289 0.2877 0.3356 0.0513 -0.1018 -0.0715 643 ALA A CB 5033 N N . SER A 651 ? 0.3458 0.2920 0.3526 0.0602 -0.1237 -0.0877 644 SER A N 5034 C CA . SER A 651 ? 0.3718 0.3140 0.3778 0.0656 -0.1353 -0.0957 644 SER A CA 5035 C C . SER A 651 ? 0.3872 0.3210 0.3737 0.0736 -0.1388 -0.0992 644 SER A C 5036 O O . SER A 651 ? 0.4003 0.3306 0.3737 0.0810 -0.1447 -0.1030 644 SER A O 5037 C CB . SER A 651 ? 0.3768 0.3195 0.4044 0.0608 -0.1418 -0.1004 644 SER A CB 5038 O OG . SER A 651 ? 0.4376 0.3760 0.4643 0.0664 -0.1539 -0.1088 644 SER A OG 5039 N N . LYS A 652 ? 0.3828 0.3132 0.3665 0.0725 -0.1350 -0.0980 645 LYS A N 5040 C CA . LYS A 652 ? 0.4054 0.3282 0.3708 0.0800 -0.1371 -0.1010 645 LYS A CA 5041 C C . LYS A 652 ? 0.4025 0.3249 0.3473 0.0857 -0.1308 -0.0967 645 LYS A C 5042 O O . LYS A 652 ? 0.4091 0.3257 0.3369 0.0939 -0.1347 -0.1003 645 LYS A O 5043 C CB . LYS A 652 ? 0.4081 0.3274 0.3772 0.0775 -0.1347 -0.1008 645 LYS A CB 5044 C CG . LYS A 652 ? 0.4421 0.3589 0.4286 0.0740 -0.1429 -0.1068 645 LYS A CG 5045 C CD . LYS A 652 ? 0.4964 0.4060 0.4758 0.0814 -0.1548 -0.1163 645 LYS A CD 5046 C CE . LYS A 652 ? 0.5080 0.4157 0.5071 0.0778 -0.1640 -0.1229 645 LYS A CE 5047 N NZ . LYS A 652 ? 0.5214 0.4223 0.5130 0.0854 -0.1765 -0.1326 645 LYS A NZ 5048 N N . PHE A 653 ? 0.3674 0.2959 0.3137 0.0813 -0.1209 -0.0890 646 PHE A N 5049 C CA . PHE A 653 ? 0.3723 0.3011 0.3020 0.0858 -0.1146 -0.0844 646 PHE A CA 5050 C C . PHE A 653 ? 0.3919 0.3198 0.3136 0.0913 -0.1199 -0.0868 646 PHE A C 5051 O O . PHE A 653 ? 0.4151 0.3384 0.3180 0.0988 -0.1194 -0.0867 646 PHE A O 5052 C CB . PHE A 653 ? 0.3499 0.2860 0.2859 0.0792 -0.1042 -0.0763 646 PHE A CB 5053 C CG . PHE A 653 ? 0.3591 0.2960 0.2807 0.0829 -0.0972 -0.0713 646 PHE A CG 5054 C CD1 . PHE A 653 ? 0.3704 0.3048 0.2801 0.0860 -0.0910 -0.0685 646 PHE A CD1 5055 C CD2 . PHE A 653 ? 0.3969 0.3368 0.3174 0.0835 -0.0968 -0.0693 646 PHE A CD2 5056 C CE1 . PHE A 653 ? 0.4025 0.3376 0.3004 0.0890 -0.0842 -0.0636 646 PHE A CE1 5057 C CE2 . PHE A 653 ? 0.4139 0.3539 0.3217 0.0868 -0.0902 -0.0645 646 PHE A CE2 5058 C CZ . PHE A 653 ? 0.4023 0.3400 0.2992 0.0893 -0.0837 -0.0615 646 PHE A CZ 5059 N N . SER A 654 ? 0.3856 0.3176 0.3214 0.0878 -0.1248 -0.0886 647 SER A N 5060 C CA . SER A 654 ? 0.4143 0.3457 0.3447 0.0928 -0.1308 -0.0910 647 SER A CA 5061 C C . SER A 654 ? 0.4369 0.3599 0.3538 0.1015 -0.1407 -0.0984 647 SER A C 5062 O O . SER A 654 ? 0.4526 0.3722 0.3533 0.1089 -0.1428 -0.0987 647 SER A O 5063 C CB . SER A 654 ? 0.4091 0.3466 0.3602 0.0872 -0.1352 -0.0927 647 SER A CB 5064 O OG A SER A 654 ? 0.4105 0.3553 0.3718 0.0800 -0.1260 -0.0860 647 SER A OG 5065 O OG B SER A 654 ? 0.4317 0.3700 0.3785 0.0913 -0.1391 -0.0934 647 SER A OG 5066 N N . GLU A 655 ? 0.4345 0.3540 0.3578 0.1009 -0.1467 -0.1041 648 GLU A N 5067 C CA . GLU A 655 ? 0.4697 0.3805 0.3800 0.1093 -0.1565 -0.1120 648 GLU A CA 5068 C C . GLU A 655 ? 0.4820 0.3869 0.3673 0.1169 -0.1508 -0.1096 648 GLU A C 5069 O O . GLU A 655 ? 0.4984 0.3975 0.3655 0.1257 -0.1555 -0.1124 648 GLU A O 5070 C CB . GLU A 655 ? 0.4810 0.3888 0.4036 0.1066 -0.1628 -0.1183 648 GLU A CB 5071 C CG . GLU A 655 ? 0.5177 0.4303 0.4658 0.0996 -0.1691 -0.1215 648 GLU A CG 5072 C CD . GLU A 655 ? 0.5969 0.5053 0.5568 0.0973 -0.1755 -0.1278 648 GLU A CD 5073 O OE1 . GLU A 655 ? 0.6173 0.5188 0.5653 0.1014 -0.1757 -0.1302 648 GLU A OE1 5074 O OE2 . GLU A 655 ? 0.6494 0.5614 0.6315 0.0912 -0.1801 -0.1304 648 GLU A OE2 5075 N N . ARG A 656 ? 0.4607 0.3670 0.3448 0.1137 -0.1406 -0.1041 649 ARG A N 5076 C CA . ARG A 656 ? 0.4720 0.3735 0.3345 0.1204 -0.1341 -0.1014 649 ARG A CA 5077 C C . ARG A 656 ? 0.4797 0.3824 0.3291 0.1242 -0.1290 -0.0960 649 ARG A C 5078 O O . ARG A 656 ? 0.4979 0.3946 0.3267 0.1326 -0.1278 -0.0960 649 ARG A O 5079 C CB . ARG A 656 ? 0.4647 0.3683 0.3309 0.1160 -0.1244 -0.0966 649 ARG A CB 5080 C CG . ARG A 656 ? 0.4607 0.3619 0.3380 0.1130 -0.1289 -0.1014 649 ARG A CG 5081 C CD . ARG A 656 ? 0.4529 0.3537 0.3276 0.1119 -0.1202 -0.0975 649 ARG A CD 5082 N NE . ARG A 656 ? 0.4375 0.3463 0.3199 0.1052 -0.1099 -0.0889 649 ARG A NE 5083 C CZ . ARG A 656 ? 0.4401 0.3545 0.3410 0.0965 -0.1082 -0.0863 649 ARG A CZ 5084 N NH1 . ARG A 656 ? 0.4243 0.3376 0.3392 0.0928 -0.1156 -0.0911 649 ARG A NH1 5085 N NH2 . ARG A 656 ? 0.3918 0.3127 0.2971 0.0914 -0.0991 -0.0788 649 ARG A NH2 5086 N N . LEU A 657 ? 0.4748 0.3848 0.3359 0.1183 -0.1255 -0.0912 650 LEU A N 5087 C CA . LEU A 657 ? 0.5004 0.4118 0.3514 0.1210 -0.1201 -0.0855 650 LEU A CA 5088 C C . LEU A 657 ? 0.5549 0.4606 0.3923 0.1296 -0.1290 -0.0899 650 LEU A C 5089 O O . LEU A 657 ? 0.5639 0.4662 0.3839 0.1359 -0.1254 -0.0865 650 LEU A O 5090 C CB . LEU A 657 ? 0.4862 0.4066 0.3551 0.1124 -0.1161 -0.0807 650 LEU A CB 5091 C CG . LEU A 657 ? 0.4985 0.4218 0.3612 0.1125 -0.1073 -0.0732 650 LEU A CG 5092 C CD1 . LEU A 657 ? 0.4693 0.3926 0.3247 0.1120 -0.0963 -0.0674 650 LEU A CD1 5093 C CD2 . LEU A 657 ? 0.4615 0.3929 0.3426 0.1048 -0.1060 -0.0705 650 LEU A CD2 5094 N N . GLN A 658 ? 0.5864 0.4907 0.4321 0.1299 -0.1407 -0.0975 651 GLN A N 5095 C CA . GLN A 658 ? 0.6563 0.5551 0.4893 0.1383 -0.1501 -0.1020 651 GLN A CA 5096 C C . GLN A 658 ? 0.6850 0.5739 0.4985 0.1475 -0.1556 -0.1080 651 GLN A C 5097 O O . GLN A 658 ? 0.7320 0.6147 0.5274 0.1565 -0.1608 -0.1101 651 GLN A O 5098 C CB . GLN A 658 ? 0.6604 0.5634 0.5117 0.1350 -0.1603 -0.1067 651 GLN A CB 5099 C CG . GLN A 658 ? 0.7039 0.6071 0.5721 0.1311 -0.1690 -0.1144 651 GLN A CG 5100 C CD . GLN A 658 ? 0.7382 0.6490 0.6309 0.1244 -0.1742 -0.1160 651 GLN A CD 5101 O OE1 . GLN A 658 ? 0.7484 0.6651 0.6450 0.1221 -0.1692 -0.1103 651 GLN A OE1 5102 N NE2 . GLN A 658 ? 0.7634 0.6748 0.6722 0.1213 -0.1823 -0.1224 651 GLN A NE2 5103 N N . ASP A 659 ? 0.6937 0.5808 0.5102 0.1456 -0.1543 -0.1104 652 ASP A N 5104 C CA . ASP A 659 ? 0.7203 0.5980 0.5205 0.1537 -0.1594 -0.1170 652 ASP A CA 5105 C C . ASP A 659 ? 0.7258 0.5989 0.5051 0.1593 -0.1491 -0.1125 652 ASP A C 5106 O O . ASP A 659 ? 0.7408 0.6057 0.5044 0.1669 -0.1526 -0.1177 652 ASP A O 5107 C CB . ASP A 659 ? 0.7179 0.5955 0.5342 0.1487 -0.1643 -0.1229 652 ASP A CB 5108 C CG . ASP A 659 ? 0.7530 0.6306 0.5844 0.1471 -0.1782 -0.1311 652 ASP A CG 5109 O OD1 . ASP A 659 ? 0.7800 0.6578 0.6271 0.1422 -0.1822 -0.1356 652 ASP A OD1 5110 O OD2 . ASP A 659 ? 0.7747 0.6522 0.6032 0.1506 -0.1853 -0.1332 652 ASP A OD2 5111 N N . PHE A 660 ? 0.7126 0.5910 0.4925 0.1556 -0.1363 -0.1032 653 PHE A N 5112 C CA . PHE A 660 ? 0.7127 0.5876 0.4755 0.1604 -0.1258 -0.0988 653 PHE A CA 5113 C C . PHE A 660 ? 0.7389 0.6076 0.4769 0.1702 -0.1238 -0.0964 653 PHE A C 5114 O O . PHE A 660 ? 0.7891 0.6525 0.5091 0.1768 -0.1173 -0.0948 653 PHE A O 5115 C CB . PHE A 660 ? 0.6793 0.5623 0.4541 0.1522 -0.1130 -0.0903 653 PHE A CB 5116 C CG . PHE A 660 ? 0.6265 0.5140 0.4002 0.1504 -0.1054 -0.0821 653 PHE A CG 5117 C CD1 . PHE A 660 ? 0.5936 0.4789 0.3514 0.1552 -0.0952 -0.0759 653 PHE A CD1 5118 C CD2 . PHE A 660 ? 0.6116 0.5057 0.4015 0.1437 -0.1079 -0.0806 653 PHE A CD2 5119 C CE1 . PHE A 660 ? 0.6134 0.5026 0.3715 0.1532 -0.0879 -0.0683 653 PHE A CE1 5120 C CE2 . PHE A 660 ? 0.6301 0.5281 0.4197 0.1420 -0.1009 -0.0733 653 PHE A CE2 5121 C CZ . PHE A 660 ? 0.6466 0.5420 0.4205 0.1466 -0.0910 -0.0672 653 PHE A CZ 5122 N N A SER A 663 ? 0.5518 0.4010 0.2055 0.2001 -0.0934 -0.0757 656 SER A N 5123 N N B SER A 663 ? 0.5224 0.3812 0.1843 0.1924 -0.0713 -0.0561 656 SER A N 5124 C CA A SER A 663 ? 0.5707 0.4156 0.2063 0.2062 -0.0810 -0.0698 656 SER A CA 5125 C CA B SER A 663 ? 0.5243 0.3775 0.1662 0.1996 -0.0596 -0.0499 656 SER A CA 5126 C C A SER A 663 ? 0.5289 0.3814 0.1782 0.1990 -0.0675 -0.0632 656 SER A C 5127 C C B SER A 663 ? 0.5262 0.3823 0.1720 0.1976 -0.0489 -0.0475 656 SER A C 5128 O O A SER A 663 ? 0.5309 0.3820 0.1698 0.2022 -0.0554 -0.0563 656 SER A O 5129 O O B SER A 663 ? 0.5312 0.3838 0.1632 0.2029 -0.0379 -0.0420 656 SER A O 5130 C CB A SER A 663 ? 0.5678 0.4030 0.1831 0.2163 -0.0852 -0.0768 656 SER A CB 5131 C CB B SER A 663 ? 0.5598 0.4011 0.1738 0.2124 -0.0652 -0.0541 656 SER A CB 5132 O OG A SER A 663 ? 0.6966 0.5237 0.2855 0.2266 -0.0791 -0.0726 656 SER A OG 5133 O OG B SER A 663 ? 0.5415 0.3796 0.1453 0.2162 -0.0649 -0.0494 656 SER A OG 5134 N N A ASN A 664 ? 0.5132 0.3733 0.1854 0.1895 -0.0695 -0.0654 657 ASN A N 5135 N N B ASN A 664 ? 0.5183 0.3804 0.1828 0.1902 -0.0521 -0.0516 657 ASN A N 5136 C CA A ASN A 664 ? 0.4943 0.3605 0.1781 0.1838 -0.0585 -0.0607 657 ASN A CA 5137 C CA B ASN A 664 ? 0.5317 0.3975 0.2031 0.1874 -0.0429 -0.0497 657 ASN A CA 5138 C C A ASN A 664 ? 0.4747 0.3506 0.1776 0.1739 -0.0519 -0.0534 657 ASN A C 5139 C C B ASN A 664 ? 0.5109 0.3869 0.2034 0.1769 -0.0351 -0.0426 657 ASN A C 5140 O O A ASN A 664 ? 0.4596 0.3413 0.1807 0.1660 -0.0578 -0.0552 657 ASN A O 5141 O O B ASN A 664 ? 0.5009 0.3835 0.2131 0.1683 -0.0401 -0.0446 657 ASN A O 5142 C CB A ASN A 664 ? 0.4871 0.3543 0.1817 0.1808 -0.0639 -0.0676 657 ASN A CB 5143 C CB B ASN A 664 ? 0.5297 0.3952 0.2087 0.1858 -0.0517 -0.0584 657 ASN A CB 5144 C CG A ASN A 664 ? 0.4905 0.3618 0.1920 0.1779 -0.0531 -0.0637 657 ASN A CG 5145 C CG B ASN A 664 ? 0.5590 0.4271 0.2435 0.1842 -0.0436 -0.0573 657 ASN A CG 5146 O OD1 A ASN A 664 ? 0.4612 0.3395 0.1730 0.1720 -0.0439 -0.0563 657 ASN A OD1 5147 O OD1 B ASN A 664 ? 0.5708 0.4457 0.2661 0.1788 -0.0332 -0.0504 657 ASN A OD1 5148 N ND2 A ASN A 664 ? 0.5304 0.3973 0.2260 0.1822 -0.0543 -0.0688 657 ASN A ND2 5149 N ND2 B ASN A 664 ? 0.5651 0.4281 0.2435 0.1887 -0.0488 -0.0646 657 ASN A ND2 5150 N N A PRO A 665 ? 0.4669 0.3442 0.1655 0.1745 -0.0395 -0.0451 658 PRO A N 5151 N N B PRO A 665 ? 0.5157 0.3927 0.2042 0.1777 -0.0226 -0.0342 658 PRO A N 5152 C CA A PRO A 665 ? 0.4441 0.3297 0.1591 0.1660 -0.0335 -0.0383 658 PRO A CA 5153 C CA B PRO A 665 ? 0.4966 0.3827 0.2041 0.1683 -0.0157 -0.0275 658 PRO A CA 5154 C C A PRO A 665 ? 0.4226 0.3169 0.1592 0.1565 -0.0303 -0.0376 658 PRO A C 5155 C C B PRO A 665 ? 0.4756 0.3702 0.2056 0.1588 -0.0163 -0.0292 658 PRO A C 5156 O O A PRO A 665 ? 0.3896 0.2910 0.1425 0.1483 -0.0292 -0.0344 658 PRO A O 5157 O O B PRO A 665 ? 0.4557 0.3569 0.2024 0.1506 -0.0181 -0.0278 658 PRO A O 5158 C CB A PRO A 665 ? 0.4565 0.3397 0.1589 0.1706 -0.0211 -0.0302 658 PRO A CB 5159 C CB B PRO A 665 ? 0.5107 0.3955 0.2097 0.1719 -0.0017 -0.0197 658 PRO A CB 5160 C CG A PRO A 665 ? 0.4644 0.3423 0.1529 0.1780 -0.0171 -0.0323 658 PRO A CG 5161 C CG B PRO A 665 ? 0.5292 0.4031 0.2012 0.1840 -0.0023 -0.0209 658 PRO A CG 5162 C CD A PRO A 665 ? 0.4937 0.3651 0.1727 0.1832 -0.0301 -0.0418 658 PRO A CD 5163 C CD B PRO A 665 ? 0.5350 0.4046 0.2012 0.1876 -0.0143 -0.0306 658 PRO A CD 5164 N N A ILE A 666 ? 0.4256 0.3191 0.1620 0.1579 -0.0288 -0.0405 659 ILE A N 5165 N N B ILE A 666 ? 0.4729 0.3673 0.2033 0.1601 -0.0145 -0.0320 659 ILE A N 5166 C CA A ILE A 666 ? 0.4263 0.3273 0.1824 0.1495 -0.0268 -0.0402 659 ILE A CA 5167 C CA B ILE A 666 ? 0.4579 0.3601 0.2092 0.1514 -0.0147 -0.0329 659 ILE A CA 5168 C C A ILE A 666 ? 0.4141 0.3173 0.1837 0.1437 -0.0379 -0.0460 659 ILE A C 5169 C C B ILE A 666 ? 0.4416 0.3445 0.2024 0.1473 -0.0269 -0.0398 659 ILE A C 5170 O O A ILE A 666 ? 0.3936 0.3041 0.1810 0.1350 -0.0373 -0.0440 659 ILE A O 5171 O O B ILE A 666 ? 0.4253 0.3350 0.2045 0.1386 -0.0284 -0.0393 659 ILE A O 5172 C CB A ILE A 666 ? 0.4418 0.3413 0.1952 0.1527 -0.0226 -0.0419 659 ILE A CB 5173 C CB B ILE A 666 ? 0.4603 0.3630 0.2116 0.1533 -0.0076 -0.0325 659 ILE A CB 5174 C CG1 A ILE A 666 ? 0.4747 0.3706 0.2125 0.1602 -0.0119 -0.0373 659 ILE A CG1 5175 C CG1 B ILE A 666 ? 0.4848 0.3901 0.2348 0.1541 0.0056 -0.0243 659 ILE A CG1 5176 C CG2 A ILE A 666 ? 0.4170 0.3247 0.1913 0.1438 -0.0199 -0.0403 659 ILE A CG2 5177 C CG2 B ILE A 666 ? 0.4678 0.3770 0.2386 0.1454 -0.0101 -0.0344 659 ILE A CG2 5178 C CD1 A ILE A 666 ? 0.5118 0.4104 0.2493 0.1588 -0.0037 -0.0293 659 ILE A CD1 5179 C CD1 B ILE A 666 ? 0.4773 0.3877 0.2372 0.1478 0.0085 -0.0186 659 ILE A CD1 5180 N N A VAL A 667 ? 0.4198 0.3166 0.1810 0.1486 -0.0479 -0.0532 660 VAL A N 5181 N N B VAL A 667 ? 0.4474 0.3430 0.1960 0.1536 -0.0359 -0.0464 660 VAL A N 5182 C CA A VAL A 667 ? 0.4228 0.3214 0.1973 0.1434 -0.0586 -0.0588 660 VAL A CA 5183 C CA B VAL A 667 ? 0.4223 0.3187 0.1817 0.1493 -0.0477 -0.0529 660 VAL A CA 5184 C C A VAL A 667 ? 0.4063 0.3097 0.1899 0.1382 -0.0605 -0.0560 660 VAL A C 5185 C C B VAL A 667 ? 0.4079 0.3091 0.1779 0.1433 -0.0508 -0.0506 660 VAL A C 5186 O O A VAL A 667 ? 0.3991 0.3086 0.2008 0.1299 -0.0630 -0.0561 660 VAL A O 5187 O O B VAL A 667 ? 0.3889 0.2957 0.1767 0.1354 -0.0548 -0.0520 660 VAL A O 5188 C CB A VAL A 667 ? 0.4363 0.3266 0.1998 0.1503 -0.0696 -0.0675 660 VAL A CB 5189 C CB B VAL A 667 ? 0.4483 0.3359 0.1937 0.1572 -0.0577 -0.0611 660 VAL A CB 5190 C CG1 A VAL A 667 ? 0.4521 0.3447 0.2315 0.1445 -0.0805 -0.0729 660 VAL A CG1 5191 C CG1 B VAL A 667 ? 0.4311 0.3199 0.1893 0.1526 -0.0701 -0.0674 660 VAL A CG1 5192 C CG2 A VAL A 667 ? 0.4585 0.3443 0.2148 0.1549 -0.0677 -0.0708 660 VAL A CG2 5193 C CG2 B VAL A 667 ? 0.4563 0.3401 0.1958 0.1614 -0.0556 -0.0644 660 VAL A CG2 5194 N N A LEU A 668 ? 0.4110 0.3113 0.1815 0.1434 -0.0588 -0.0531 661 LEU A N 5195 N N B LEU A 668 ? 0.3974 0.2964 0.1568 0.1472 -0.0482 -0.0468 661 LEU A N 5196 C CA A LEU A 668 ? 0.3967 0.3009 0.1742 0.1395 -0.0598 -0.0500 661 LEU A CA 5197 C CA B LEU A 668 ? 0.3925 0.2958 0.1611 0.1423 -0.0504 -0.0444 661 LEU A CA 5198 C C A LEU A 668 ? 0.3876 0.3004 0.1816 0.1304 -0.0517 -0.0439 661 LEU A C 5199 C C B LEU A 668 ? 0.3829 0.2950 0.1692 0.1330 -0.0429 -0.0388 661 LEU A C 5200 O O A LEU A 668 ? 0.3580 0.2764 0.1677 0.1233 -0.0550 -0.0444 661 LEU A O 5201 O O B LEU A 668 ? 0.3649 0.2826 0.1664 0.1259 -0.0461 -0.0389 661 LEU A O 5202 C CB A LEU A 668 ? 0.4228 0.3214 0.1818 0.1472 -0.0578 -0.0469 661 LEU A CB 5203 C CB B LEU A 668 ? 0.4039 0.3022 0.1561 0.1490 -0.0480 -0.0406 661 LEU A CB 5204 C CG A LEU A 668 ? 0.4138 0.3162 0.1789 0.1437 -0.0559 -0.0419 661 LEU A CG 5205 C CG B LEU A 668 ? 0.4213 0.3231 0.1813 0.1450 -0.0496 -0.0376 661 LEU A CG 5206 C CD1 A LEU A 668 ? 0.3902 0.2960 0.1691 0.1390 -0.0660 -0.0464 661 LEU A CD1 5207 C CD1 B LEU A 668 ? 0.4079 0.3117 0.1790 0.1417 -0.0616 -0.0439 661 LEU A CD1 5208 C CD2 A LEU A 668 ? 0.4209 0.3163 0.1658 0.1523 -0.0534 -0.0384 661 LEU A CD2 5209 C CD2 B LEU A 668 ? 0.4129 0.3080 0.1538 0.1532 -0.0471 -0.0339 661 LEU A CD2 5210 N N A ARG A 669 ? 0.3836 0.2975 0.1742 0.1310 -0.0412 -0.0384 662 ARG A N 5211 N N B ARG A 669 ? 0.3825 0.2959 0.1671 0.1332 -0.0328 -0.0341 662 ARG A N 5212 C CA A ARG A 669 ? 0.3767 0.2983 0.1813 0.1233 -0.0332 -0.0324 662 ARG A CA 5213 C CA B ARG A 669 ? 0.3780 0.2998 0.1797 0.1245 -0.0263 -0.0293 662 ARG A CA 5214 C C A ARG A 669 ? 0.3736 0.3003 0.1941 0.1163 -0.0350 -0.0346 662 ARG A C 5215 C C B ARG A 669 ? 0.3755 0.3024 0.1943 0.1170 -0.0312 -0.0328 662 ARG A C 5216 O O A ARG A 669 ? 0.3478 0.2809 0.1831 0.1087 -0.0344 -0.0327 662 ARG A O 5217 O O B ARG A 669 ? 0.3553 0.2886 0.1882 0.1096 -0.0297 -0.0303 662 ARG A O 5218 C CB A ARG A 669 ? 0.3728 0.2939 0.1701 0.1263 -0.0218 -0.0263 662 ARG A CB 5219 C CB B ARG A 669 ? 0.3779 0.3007 0.1764 0.1261 -0.0149 -0.0237 662 ARG A CB 5220 C CG A ARG A 669 ? 0.3646 0.2936 0.1774 0.1186 -0.0142 -0.0214 662 ARG A CG 5221 C CG B ARG A 669 ? 0.3779 0.3089 0.1935 0.1176 -0.0088 -0.0190 662 ARG A CG 5222 C CD A ARG A 669 ? 0.3234 0.2568 0.1447 0.1134 -0.0116 -0.0169 662 ARG A CD 5223 C CD B ARG A 669 ? 0.4446 0.3778 0.2623 0.1154 -0.0040 -0.0134 662 ARG A CD 5224 N NE A ARG A 669 ? 0.3819 0.3208 0.2128 0.1089 -0.0026 -0.0118 662 ARG A NE 5225 N NE B ARG A 669 ? 0.4207 0.3599 0.2497 0.1105 0.0047 -0.0084 662 ARG A NE 5226 C CZ A ARG A 669 ? 0.3773 0.3172 0.2079 0.1087 0.0053 -0.0058 662 ARG A CZ 5227 C CZ B ARG A 669 ? 0.4018 0.3435 0.2349 0.1081 0.0114 -0.0028 662 ARG A CZ 5228 N NH1 A ARG A 669 ? 0.4069 0.3426 0.2283 0.1123 0.0054 -0.0037 662 ARG A NH1 5229 N NH1 B ARG A 669 ? 0.4338 0.3724 0.2606 0.1101 0.0109 -0.0008 662 ARG A NH1 5230 N NH2 A ARG A 669 ? 0.3907 0.3358 0.2313 0.1047 0.0126 -0.0021 662 ARG A NH2 5231 N NH2 B ARG A 669 ? 0.4073 0.3546 0.2516 0.1037 0.0181 0.0007 662 ARG A NH2 5232 N N . MET A 670 ? 0.3898 0.3135 0.2070 0.1191 -0.0372 -0.0387 663 MET A N 5233 C CA . MET A 670 ? 0.3904 0.3178 0.2228 0.1126 -0.0408 -0.0415 663 MET A CA 5234 C C . MET A 670 ? 0.3906 0.3203 0.2339 0.1075 -0.0488 -0.0443 663 MET A C 5235 O O . MET A 670 ? 0.3583 0.2938 0.2165 0.0999 -0.0482 -0.0428 663 MET A O 5236 C CB A MET A 670 ? 0.3973 0.3192 0.2241 0.1171 -0.0454 -0.0473 663 MET A CB 5237 C CB B MET A 670 ? 0.4084 0.3310 0.2352 0.1171 -0.0431 -0.0461 663 MET A CB 5238 C CG A MET A 670 ? 0.3742 0.2980 0.2158 0.1112 -0.0518 -0.0514 663 MET A CG 5239 C CG B MET A 670 ? 0.4180 0.3394 0.2355 0.1219 -0.0335 -0.0425 663 MET A CG 5240 S SD A MET A 670 ? 0.3677 0.2840 0.2024 0.1169 -0.0569 -0.0583 663 MET A SD 5241 S SD B MET A 670 ? 0.4493 0.3661 0.2606 0.1273 -0.0327 -0.0464 663 MET A SD 5242 C CE A MET A 670 ? 0.4391 0.3550 0.2628 0.1222 -0.0456 -0.0536 663 MET A CE 5243 C CE B MET A 670 ? 0.3836 0.2899 0.1758 0.1370 -0.0417 -0.0539 663 MET A CE 5244 N N . MET A 671 ? 0.3792 0.3044 0.2151 0.1120 -0.0562 -0.0484 664 MET A N 5245 C CA . MET A 671 ? 0.3830 0.3108 0.2306 0.1073 -0.0636 -0.0513 664 MET A CA 5246 C C . MET A 671 ? 0.3633 0.2968 0.2183 0.1026 -0.0596 -0.0462 664 MET A C 5247 O O . MET A 671 ? 0.3750 0.3136 0.2448 0.0958 -0.0617 -0.0465 664 MET A O 5248 C CB A MET A 671 ? 0.4003 0.3218 0.2372 0.1143 -0.0728 -0.0569 664 MET A CB 5249 C CB B MET A 671 ? 0.3870 0.3088 0.2274 0.1130 -0.0742 -0.0582 664 MET A CB 5250 C CG A MET A 671 ? 0.4548 0.3687 0.2788 0.1216 -0.0767 -0.0621 664 MET A CG 5251 C CG B MET A 671 ? 0.3772 0.2943 0.2163 0.1154 -0.0798 -0.0644 664 MET A CG 5252 S SD A MET A 671 ? 0.4956 0.4109 0.3352 0.1158 -0.0811 -0.0667 664 MET A SD 5253 S SD B MET A 671 ? 0.3818 0.2931 0.2187 0.1198 -0.0942 -0.0738 664 MET A SD 5254 C CE A MET A 671 ? 0.4709 0.3830 0.3150 0.1170 -0.0952 -0.0752 664 MET A CE 5255 C CE B MET A 671 ? 0.3380 0.2562 0.2011 0.1091 -0.0983 -0.0751 664 MET A CE 5256 N N . ASN A 672 ? 0.3682 0.3005 0.2126 0.1063 -0.0537 -0.0417 665 ASN A N 5257 C CA . ASN A 672 ? 0.3559 0.2931 0.2071 0.1020 -0.0491 -0.0366 665 ASN A CA 5258 C C . ASN A 672 ? 0.3494 0.2934 0.2142 0.0941 -0.0428 -0.0330 665 ASN A C 5259 O O . ASN A 672 ? 0.3284 0.2776 0.2050 0.0881 -0.0427 -0.0316 665 ASN A O 5260 C CB . ASN A 672 ? 0.3782 0.3120 0.2156 0.1076 -0.0434 -0.0320 665 ASN A CB 5261 C CG . ASN A 672 ? 0.3785 0.3074 0.2061 0.1134 -0.0502 -0.0344 665 ASN A CG 5262 O OD1 . ASN A 672 ? 0.3853 0.3156 0.2209 0.1114 -0.0582 -0.0385 665 ASN A OD1 5263 N ND2 . ASN A 672 ? 0.3990 0.3221 0.2098 0.1208 -0.0469 -0.0317 665 ASN A ND2 5264 N N . ASP A 673 ? 0.3543 0.2982 0.2175 0.0945 -0.0382 -0.0318 666 ASP A N 5265 C CA . ASP A 673 ? 0.3410 0.2910 0.2169 0.0873 -0.0331 -0.0288 666 ASP A CA 5266 C C . ASP A 673 ? 0.3358 0.2886 0.2248 0.0814 -0.0390 -0.0322 666 ASP A C 5267 O O . ASP A 673 ? 0.3251 0.2833 0.2254 0.0749 -0.0369 -0.0299 666 ASP A O 5268 C CB . ASP A 673 ? 0.3420 0.2914 0.2143 0.0894 -0.0277 -0.0273 666 ASP A CB 5269 C CG . ASP A 673 ? 0.3564 0.3054 0.2210 0.0928 -0.0193 -0.0222 666 ASP A CG 5270 O OD1 . ASP A 673 ? 0.3777 0.3269 0.2403 0.0929 -0.0175 -0.0194 666 ASP A OD1 5271 O OD2 . ASP A 673 ? 0.3743 0.3227 0.2357 0.0952 -0.0144 -0.0209 666 ASP A OD2 5272 N N . GLN A 674 ? 0.3199 0.2688 0.2072 0.0839 -0.0461 -0.0376 667 GLN A N 5273 C CA . GLN A 674 ? 0.3150 0.2661 0.2155 0.0783 -0.0515 -0.0406 667 GLN A CA 5274 C C . GLN A 674 ? 0.3133 0.2681 0.2220 0.0744 -0.0535 -0.0402 667 GLN A C 5275 O O . GLN A 674 ? 0.3081 0.2675 0.2293 0.0679 -0.0529 -0.0392 667 GLN A O 5276 C CB . GLN A 674 ? 0.3185 0.2641 0.2163 0.0818 -0.0594 -0.0469 667 GLN A CB 5277 C CG . GLN A 674 ? 0.3159 0.2585 0.2096 0.0840 -0.0573 -0.0474 667 GLN A CG 5278 C CD . GLN A 674 ? 0.3467 0.2834 0.2379 0.0877 -0.0652 -0.0540 667 GLN A CD 5279 O OE1 . GLN A 674 ? 0.3824 0.3137 0.2608 0.0947 -0.0684 -0.0572 667 GLN A OE1 5280 N NE2 . GLN A 674 ? 0.3385 0.2756 0.2414 0.0830 -0.0685 -0.0561 667 GLN A NE2 5281 N N . LEU A 675 ? 0.3260 0.2788 0.2274 0.0788 -0.0558 -0.0409 668 LEU A N 5282 C CA . LEU A 675 ? 0.3178 0.2742 0.2269 0.0756 -0.0573 -0.0404 668 LEU A CA 5283 C C . LEU A 675 ? 0.3062 0.2679 0.2209 0.0707 -0.0496 -0.0348 668 LEU A C 5284 O O . LEU A 675 ? 0.3205 0.2870 0.2472 0.0649 -0.0496 -0.0344 668 LEU A O 5285 C CB . LEU A 675 ? 0.3365 0.2887 0.2349 0.0823 -0.0613 -0.0419 668 LEU A CB 5286 C CG . LEU A 675 ? 0.3754 0.3233 0.2723 0.0861 -0.0714 -0.0488 668 LEU A CG 5287 C CD1 . LEU A 675 ? 0.4136 0.3564 0.2968 0.0940 -0.0755 -0.0502 668 LEU A CD1 5288 C CD2 . LEU A 675 ? 0.4081 0.3601 0.3222 0.0803 -0.0768 -0.0521 668 LEU A CD2 5289 N N . MET A 676 ? 0.3181 0.2789 0.2245 0.0730 -0.0431 -0.0308 669 MET A N 5290 C CA . MET A 676 ? 0.3036 0.2690 0.2149 0.0687 -0.0360 -0.0258 669 MET A CA 5291 C C . MET A 676 ? 0.2863 0.2565 0.2088 0.0619 -0.0336 -0.0248 669 MET A C 5292 O O . MET A 676 ? 0.2823 0.2570 0.2132 0.0568 -0.0313 -0.0229 669 MET A O 5293 C CB . MET A 676 ? 0.3188 0.2822 0.2202 0.0726 -0.0294 -0.0218 669 MET A CB 5294 C CG . MET A 676 ? 0.3262 0.2941 0.2336 0.0681 -0.0222 -0.0168 669 MET A CG 5295 S SD . MET A 676 ? 0.3667 0.3322 0.2644 0.0727 -0.0141 -0.0120 669 MET A SD 5296 C CE . MET A 676 ? 0.3378 0.3038 0.2358 0.0728 -0.0121 -0.0126 669 MET A CE 5297 N N . PHE A 677 ? 0.2734 0.2422 0.1954 0.0623 -0.0344 -0.0261 670 PHE A N 5298 C CA . PHE A 677 ? 0.2712 0.2437 0.2024 0.0565 -0.0322 -0.0248 670 PHE A CA 5299 C C . PHE A 677 ? 0.2655 0.2394 0.2066 0.0521 -0.0369 -0.0274 670 PHE A C 5300 O O . PHE A 677 ? 0.2648 0.2411 0.2130 0.0474 -0.0354 -0.0262 670 PHE A O 5301 C CB . PHE A 677 ? 0.2653 0.2358 0.1923 0.0588 -0.0303 -0.0244 670 PHE A CB 5302 C CG . PHE A 677 ? 0.2781 0.2494 0.1998 0.0609 -0.0236 -0.0206 670 PHE A CG 5303 C CD1 . PHE A 677 ? 0.2842 0.2604 0.2119 0.0566 -0.0186 -0.0167 670 PHE A CD1 5304 C CD2 . PHE A 677 ? 0.2938 0.2610 0.2050 0.0674 -0.0221 -0.0208 670 PHE A CD2 5305 C CE1 . PHE A 677 ? 0.2813 0.2585 0.2063 0.0582 -0.0124 -0.0132 670 PHE A CE1 5306 C CE2 . PHE A 677 ? 0.3263 0.2945 0.2340 0.0692 -0.0150 -0.0169 670 PHE A CE2 5307 C CZ . PHE A 677 ? 0.2962 0.2696 0.2117 0.0644 -0.0102 -0.0130 670 PHE A CZ 5308 N N . LEU A 678 ? 0.2671 0.2394 0.2093 0.0535 -0.0425 -0.0309 671 LEU A N 5309 C CA . LEU A 678 ? 0.2624 0.2362 0.2157 0.0492 -0.0465 -0.0334 671 LEU A CA 5310 C C . LEU A 678 ? 0.2478 0.2272 0.2103 0.0431 -0.0427 -0.0305 671 LEU A C 5311 O O . LEU A 678 ? 0.2485 0.2299 0.2189 0.0383 -0.0416 -0.0297 671 LEU A O 5312 C CB . LEU A 678 ? 0.2827 0.2539 0.2363 0.0524 -0.0539 -0.0382 671 LEU A CB 5313 C CG . LEU A 678 ? 0.2871 0.2601 0.2541 0.0478 -0.0579 -0.0408 671 LEU A CG 5314 C CD1 . LEU A 678 ? 0.3079 0.2796 0.2801 0.0448 -0.0583 -0.0412 671 LEU A CD1 5315 C CD2 . LEU A 678 ? 0.3139 0.2847 0.2820 0.0515 -0.0660 -0.0460 671 LEU A CD2 5316 N N . GLU A 679 ? 0.2483 0.2297 0.2094 0.0437 -0.0405 -0.0290 672 GLU A N 5317 C CA . GLU A 679 ? 0.2359 0.2221 0.2043 0.0384 -0.0364 -0.0264 672 GLU A CA 5318 C C . GLU A 679 ? 0.2259 0.2137 0.1941 0.0354 -0.0314 -0.0231 672 GLU A C 5319 O O . GLU A 679 ? 0.2275 0.2183 0.2025 0.0304 -0.0293 -0.0218 672 GLU A O 5320 C CB . GLU A 679 ? 0.2363 0.2238 0.2021 0.0399 -0.0342 -0.0250 672 GLU A CB 5321 C CG . GLU A 679 ? 0.2229 0.2150 0.1975 0.0348 -0.0313 -0.0237 672 GLU A CG 5322 C CD . GLU A 679 ? 0.2474 0.2411 0.2310 0.0334 -0.0355 -0.0268 672 GLU A CD 5323 O OE1 . GLU A 679 ? 0.2531 0.2455 0.2354 0.0370 -0.0392 -0.0288 672 GLU A OE1 5324 O OE2 . GLU A 679 ? 0.2372 0.2331 0.2292 0.0290 -0.0350 -0.0271 672 GLU A OE2 5325 N N . ARG A 680 ? 0.2298 0.2155 0.1901 0.0387 -0.0294 -0.0218 673 ARG A N 5326 C CA . ARG A 680 ? 0.2211 0.2085 0.1815 0.0365 -0.0250 -0.0188 673 ARG A CA 5327 C C . ARG A 680 ? 0.2193 0.2065 0.1846 0.0335 -0.0266 -0.0193 673 ARG A C 5328 O O . ARG A 680 ? 0.2218 0.2113 0.1900 0.0300 -0.0239 -0.0170 673 ARG A O 5329 C CB . ARG A 680 ? 0.2427 0.2279 0.1949 0.0410 -0.0227 -0.0175 673 ARG A CB 5330 C CG . ARG A 680 ? 0.2195 0.2079 0.1730 0.0388 -0.0172 -0.0139 673 ARG A CG 5331 C CD . ARG A 680 ? 0.2349 0.2247 0.1876 0.0391 -0.0141 -0.0121 673 ARG A CD 5332 N NE . ARG A 680 ? 0.2148 0.2015 0.1594 0.0445 -0.0127 -0.0114 673 ARG A NE 5333 C CZ . ARG A 680 ? 0.2476 0.2317 0.1875 0.0479 -0.0145 -0.0124 673 ARG A CZ 5334 N NH1 . ARG A 680 ? 0.2481 0.2325 0.1914 0.0466 -0.0184 -0.0146 673 ARG A NH1 5335 N NH2 . ARG A 680 ? 0.2670 0.2478 0.1984 0.0530 -0.0122 -0.0110 673 ARG A NH2 5336 N N . ALA A 681 ? 0.2205 0.2045 0.1864 0.0350 -0.0314 -0.0224 674 ALA A N 5337 C CA . ALA A 681 ? 0.2243 0.2071 0.1947 0.0326 -0.0329 -0.0227 674 ALA A CA 5338 C C . ALA A 681 ? 0.2268 0.2124 0.2057 0.0269 -0.0319 -0.0215 674 ALA A C 5339 O O . ALA A 681 ? 0.2480 0.2328 0.2300 0.0244 -0.0316 -0.0203 674 ALA A O 5340 C CB . ALA A 681 ? 0.2278 0.2061 0.1975 0.0357 -0.0385 -0.0267 674 ALA A CB 5341 N N . PHE A 682 ? 0.2218 0.2104 0.2042 0.0252 -0.0310 -0.0215 675 PHE A N 5342 C CA . PHE A 682 ? 0.2124 0.2036 0.2026 0.0200 -0.0292 -0.0203 675 PHE A CA 5343 C C . PHE A 682 ? 0.2212 0.2151 0.2097 0.0174 -0.0244 -0.0169 675 PHE A C 5344 O O . PHE A 682 ? 0.2196 0.2153 0.2127 0.0135 -0.0223 -0.0155 675 PHE A O 5345 C CB . PHE A 682 ? 0.2155 0.2090 0.2114 0.0193 -0.0303 -0.0222 675 PHE A CB 5346 C CG . PHE A 682 ? 0.2211 0.2122 0.2211 0.0211 -0.0359 -0.0260 675 PHE A CG 5347 C CD1 . PHE A 682 ? 0.2188 0.2082 0.2257 0.0188 -0.0380 -0.0269 675 PHE A CD1 5348 C CD2 . PHE A 682 ? 0.2518 0.2420 0.2484 0.0254 -0.0394 -0.0286 675 PHE A CD2 5349 C CE1 . PHE A 682 ? 0.2356 0.2226 0.2475 0.0204 -0.0441 -0.0311 675 PHE A CE1 5350 C CE2 . PHE A 682 ? 0.2712 0.2589 0.2714 0.0275 -0.0457 -0.0328 675 PHE A CE2 5351 C CZ . PHE A 682 ? 0.2697 0.2560 0.2781 0.0249 -0.0481 -0.0342 675 PHE A CZ 5352 N N . ILE A 683 ? 0.2186 0.2126 0.2009 0.0196 -0.0226 -0.0156 676 ILE A N 5353 C CA . ILE A 683 ? 0.2226 0.2191 0.2036 0.0174 -0.0188 -0.0128 676 ILE A CA 5354 C C . ILE A 683 ? 0.2338 0.2290 0.2149 0.0159 -0.0190 -0.0111 676 ILE A C 5355 O O . ILE A 683 ? 0.2533 0.2457 0.2326 0.0182 -0.0210 -0.0117 676 ILE A O 5356 C CB . ILE A 683 ? 0.2241 0.2212 0.2001 0.0203 -0.0170 -0.0120 676 ILE A CB 5357 C CG1 . ILE A 683 ? 0.2187 0.2168 0.1944 0.0215 -0.0164 -0.0129 676 ILE A CG1 5358 C CG2 . ILE A 683 ? 0.2278 0.2272 0.2034 0.0184 -0.0140 -0.0095 676 ILE A CG2 5359 C CD1 . ILE A 683 ? 0.2082 0.2093 0.1885 0.0178 -0.0145 -0.0126 676 ILE A CD1 5360 N N . ASP A 684 ? 0.2179 0.2147 0.2005 0.0123 -0.0168 -0.0092 677 ASP A N 5361 C CA . ASP A 684 ? 0.2354 0.2309 0.2169 0.0111 -0.0168 -0.0070 677 ASP A CA 5362 C C . ASP A 684 ? 0.2392 0.2372 0.2176 0.0110 -0.0148 -0.0055 677 ASP A C 5363 O O . ASP A 684 ? 0.2239 0.2245 0.2025 0.0092 -0.0127 -0.0052 677 ASP A O 5364 C CB . ASP A 684 ? 0.2354 0.2304 0.2198 0.0074 -0.0157 -0.0057 677 ASP A CB 5365 C CG . ASP A 684 ? 0.2240 0.2166 0.2066 0.0065 -0.0160 -0.0032 677 ASP A CG 5366 O OD1 . ASP A 684 ? 0.2477 0.2406 0.2270 0.0080 -0.0165 -0.0022 677 ASP A OD1 5367 O OD2 . ASP A 684 ? 0.2529 0.2434 0.2383 0.0042 -0.0157 -0.0020 677 ASP A OD2 5368 N N . PRO A 685 ? 0.2651 0.2627 0.2417 0.0132 -0.0155 -0.0049 678 PRO A N 5369 C CA . PRO A 685 ? 0.2911 0.2915 0.2666 0.0133 -0.0140 -0.0038 678 PRO A CA 5370 C C . PRO A 685 ? 0.3004 0.3017 0.2752 0.0103 -0.0136 -0.0022 678 PRO A C 5371 O O . PRO A 685 ? 0.3382 0.3420 0.3127 0.0097 -0.0127 -0.0019 678 PRO A O 5372 C CB . PRO A 685 ? 0.2897 0.2892 0.2647 0.0164 -0.0151 -0.0035 678 PRO A CB 5373 C CG . PRO A 685 ? 0.3150 0.3107 0.2898 0.0171 -0.0174 -0.0038 678 PRO A CG 5374 C CD . PRO A 685 ? 0.2741 0.2685 0.2502 0.0157 -0.0179 -0.0052 678 PRO A CD 5375 N N . LEU A 686 ? 0.2680 0.2670 0.2425 0.0084 -0.0141 -0.0013 679 LEU A N 5376 C CA . LEU A 686 ? 0.2540 0.2531 0.2259 0.0060 -0.0133 0.0004 679 LEU A CA 5377 C C . LEU A 686 ? 0.2646 0.2653 0.2364 0.0036 -0.0107 -0.0002 679 LEU A C 5378 O O . LEU A 686 ? 0.2560 0.2570 0.2247 0.0020 -0.0097 0.0008 679 LEU A O 5379 C CB . LEU A 686 ? 0.2653 0.2607 0.2362 0.0053 -0.0144 0.0025 679 LEU A CB 5380 C CG . LEU A 686 ? 0.2736 0.2670 0.2443 0.0078 -0.0171 0.0033 679 LEU A CG 5381 C CD1 . LEU A 686 ? 0.2774 0.2664 0.2472 0.0070 -0.0182 0.0056 679 LEU A CD1 5382 C CD2 . LEU A 686 ? 0.3109 0.3071 0.2802 0.0089 -0.0180 0.0036 679 LEU A CD2 5383 N N . GLY A 687 ? 0.2501 0.2517 0.2251 0.0038 -0.0098 -0.0020 680 GLY A N 5384 C CA . GLY A 687 ? 0.2490 0.2524 0.2251 0.0020 -0.0073 -0.0029 680 GLY A CA 5385 C C . GLY A 687 ? 0.2588 0.2607 0.2358 -0.0004 -0.0058 -0.0017 680 GLY A C 5386 O O . GLY A 687 ? 0.2790 0.2782 0.2556 -0.0008 -0.0067 0.0001 680 GLY A O 5387 N N . LEU A 688 ? 0.2472 0.2509 0.2258 -0.0019 -0.0031 -0.0025 681 LEU A N 5388 C CA . LEU A 688 ? 0.2671 0.2698 0.2467 -0.0043 -0.0003 -0.0011 681 LEU A CA 5389 C C . LEU A 688 ? 0.2700 0.2720 0.2424 -0.0052 0.0017 0.0007 681 LEU A C 5390 O O . LEU A 688 ? 0.2699 0.2730 0.2380 -0.0044 0.0008 -0.0002 681 LEU A O 5391 C CB . LEU A 688 ? 0.2572 0.2626 0.2427 -0.0051 0.0020 -0.0031 681 LEU A CB 5392 C CG . LEU A 688 ? 0.2642 0.2697 0.2569 -0.0040 -0.0006 -0.0049 681 LEU A CG 5393 C CD1 . LEU A 688 ? 0.2926 0.3011 0.2906 -0.0039 0.0006 -0.0072 681 LEU A CD1 5394 C CD2 . LEU A 688 ? 0.3094 0.3123 0.3067 -0.0053 -0.0012 -0.0036 681 LEU A CD2 5395 N N . PRO A 689 ? 0.2911 0.2908 0.2619 -0.0069 0.0043 0.0032 682 PRO A N 5396 C CA . PRO A 689 ? 0.3010 0.2991 0.2630 -0.0073 0.0058 0.0051 682 PRO A CA 5397 C C . PRO A 689 ? 0.2947 0.2952 0.2528 -0.0070 0.0072 0.0029 682 PRO A C 5398 O O . PRO A 689 ? 0.2979 0.3005 0.2593 -0.0078 0.0103 0.0013 682 PRO A O 5399 C CB . PRO A 689 ? 0.3055 0.3010 0.2679 -0.0092 0.0099 0.0082 682 PRO A CB 5400 C CG . PRO A 689 ? 0.3160 0.3107 0.2873 -0.0096 0.0084 0.0083 682 PRO A CG 5401 C CD . PRO A 689 ? 0.3077 0.3061 0.2850 -0.0085 0.0059 0.0045 682 PRO A CD 5402 N N . ASP A 690 ? 0.2945 0.2947 0.2464 -0.0058 0.0045 0.0024 683 ASP A N 5403 C CA . ASP A 690 ? 0.3125 0.3143 0.2604 -0.0055 0.0049 0.0000 683 ASP A CA 5404 C C . ASP A 690 ? 0.2844 0.2897 0.2388 -0.0053 0.0051 -0.0033 683 ASP A C 5405 O O . ASP A 690 ? 0.2806 0.2870 0.2329 -0.0053 0.0058 -0.0056 683 ASP A O 5406 C CB . ASP A 690 ? 0.3364 0.3367 0.2775 -0.0063 0.0090 0.0007 683 ASP A CB 5407 C CG . ASP A 690 ? 0.4458 0.4419 0.3784 -0.0060 0.0088 0.0042 683 ASP A CG 5408 O OD1 . ASP A 690 ? 0.4765 0.4714 0.4047 -0.0047 0.0045 0.0047 683 ASP A OD1 5409 O OD2 . ASP A 690 ? 0.5218 0.5159 0.4525 -0.0070 0.0133 0.0067 683 ASP A OD2 5410 N N . ARG A 691 ? 0.2558 0.2622 0.2174 -0.0050 0.0041 -0.0035 684 ARG A N 5411 C CA . ARG A 691 ? 0.2438 0.2527 0.2109 -0.0043 0.0039 -0.0060 684 ARG A CA 5412 C C . ARG A 691 ? 0.2328 0.2419 0.2030 -0.0026 0.0007 -0.0059 684 ARG A C 5413 O O . ARG A 691 ? 0.2226 0.2316 0.1972 -0.0019 0.0001 -0.0059 684 ARG A O 5414 C CB . ARG A 691 ? 0.2388 0.2489 0.2117 -0.0050 0.0067 -0.0068 684 ARG A CB 5415 C CG . ARG A 691 ? 0.2389 0.2492 0.2092 -0.0063 0.0108 -0.0072 684 ARG A CG 5416 C CD . ARG A 691 ? 0.2381 0.2505 0.2156 -0.0067 0.0136 -0.0085 684 ARG A CD 5417 N NE . ARG A 691 ? 0.2421 0.2543 0.2257 -0.0074 0.0135 -0.0071 684 ARG A NE 5418 C CZ . ARG A 691 ? 0.2445 0.2587 0.2368 -0.0075 0.0142 -0.0083 684 ARG A CZ 5419 N NH1 . ARG A 691 ? 0.2300 0.2466 0.2256 -0.0069 0.0156 -0.0107 684 ARG A NH1 5420 N NH2 . ARG A 691 ? 0.2457 0.2593 0.2439 -0.0083 0.0133 -0.0073 684 ARG A NH2 5421 N N . PRO A 692 ? 0.2314 0.2406 0.1992 -0.0018 -0.0015 -0.0058 685 PRO A N 5422 C CA . PRO A 692 ? 0.2341 0.2433 0.2041 -0.0001 -0.0040 -0.0052 685 PRO A CA 5423 C C . PRO A 692 ? 0.2189 0.2292 0.1932 0.0014 -0.0037 -0.0065 685 PRO A C 5424 O O . PRO A 692 ? 0.2305 0.2403 0.2062 0.0032 -0.0051 -0.0059 685 PRO A O 5425 C CB . PRO A 692 ? 0.2535 0.2633 0.2212 0.0003 -0.0059 -0.0052 685 PRO A CB 5426 C CG . PRO A 692 ? 0.2523 0.2628 0.2175 -0.0011 -0.0047 -0.0069 685 PRO A CG 5427 C CD . PRO A 692 ? 0.2372 0.2464 0.2001 -0.0023 -0.0020 -0.0064 685 PRO A CD 5428 N N . PHE A 693 ? 0.2143 0.2259 0.1903 0.0010 -0.0018 -0.0081 686 PHE A N 5429 C CA . PHE A 693 ? 0.2081 0.2202 0.1875 0.0027 -0.0015 -0.0089 686 PHE A CA 5430 C C . PHE A 693 ? 0.2081 0.2198 0.1899 0.0031 -0.0012 -0.0095 686 PHE A C 5431 O O . PHE A 693 ? 0.2154 0.2270 0.1990 0.0051 -0.0015 -0.0101 686 PHE A O 5432 C CB . PHE A 693 ? 0.2148 0.2281 0.1954 0.0024 -0.0001 -0.0102 686 PHE A CB 5433 C CG . PHE A 693 ? 0.2134 0.2273 0.1933 0.0020 -0.0011 -0.0100 686 PHE A CG 5434 C CD1 . PHE A 693 ? 0.2220 0.2360 0.2031 0.0036 -0.0022 -0.0087 686 PHE A CD1 5435 C CD2 . PHE A 693 ? 0.2278 0.2421 0.2060 0.0003 -0.0011 -0.0113 686 PHE A CD2 5436 C CE1 . PHE A 693 ? 0.2141 0.2293 0.1965 0.0032 -0.0033 -0.0086 686 PHE A CE1 5437 C CE2 . PHE A 693 ? 0.2394 0.2544 0.2178 0.0000 -0.0028 -0.0115 686 PHE A CE2 5438 C CZ . PHE A 693 ? 0.2169 0.2326 0.1983 0.0014 -0.0040 -0.0101 686 PHE A CZ 5439 N N . TYR A 694 ? 0.2004 0.2117 0.1825 0.0016 -0.0008 -0.0092 687 TYR A N 5440 C CA . TYR A 694 ? 0.1951 0.2061 0.1813 0.0019 -0.0013 -0.0098 687 TYR A CA 5441 C C . TYR A 694 ? 0.2046 0.2136 0.1903 0.0025 -0.0037 -0.0087 687 TYR A C 5442 O O . TYR A 694 ? 0.2226 0.2304 0.2073 0.0008 -0.0033 -0.0072 687 TYR A O 5443 C CB . TYR A 694 ? 0.1940 0.2061 0.1827 -0.0004 0.0013 -0.0101 687 TYR A CB 5444 C CG . TYR A 694 ? 0.2036 0.2176 0.1935 -0.0005 0.0036 -0.0118 687 TYR A CG 5445 C CD1 . TYR A 694 ? 0.2043 0.2186 0.1949 0.0015 0.0027 -0.0129 687 TYR A CD1 5446 C CD2 . TYR A 694 ? 0.2112 0.2261 0.2012 -0.0024 0.0069 -0.0121 687 TYR A CD2 5447 C CE1 . TYR A 694 ? 0.1959 0.2114 0.1880 0.0015 0.0048 -0.0144 687 TYR A CE1 5448 C CE2 . TYR A 694 ? 0.2256 0.2419 0.2167 -0.0023 0.0089 -0.0139 687 TYR A CE2 5449 C CZ . TYR A 694 ? 0.2078 0.2244 0.2004 -0.0004 0.0076 -0.0151 687 TYR A CZ 5450 O OH . TYR A 694 ? 0.2207 0.2382 0.2150 -0.0002 0.0097 -0.0170 687 TYR A OH 5451 N N A ARG A 695 ? 0.1912 0.1991 0.1769 0.0052 -0.0060 -0.0092 688 ARG A N 5452 N N B ARG A 695 ? 0.1994 0.2073 0.1850 0.0052 -0.0059 -0.0092 688 ARG A N 5453 C CA A ARG A 695 ? 0.1865 0.1921 0.1710 0.0063 -0.0084 -0.0085 688 ARG A CA 5454 C CA B ARG A 695 ? 0.1978 0.2035 0.1822 0.0064 -0.0083 -0.0085 688 ARG A CA 5455 C C A ARG A 695 ? 0.1969 0.2009 0.1848 0.0074 -0.0108 -0.0100 688 ARG A C 5456 C C B ARG A 695 ? 0.2007 0.2048 0.1885 0.0076 -0.0108 -0.0100 688 ARG A C 5457 O O A ARG A 695 ? 0.2166 0.2183 0.2046 0.0080 -0.0129 -0.0098 688 ARG A O 5458 O O B ARG A 695 ? 0.2107 0.2124 0.1981 0.0084 -0.0130 -0.0098 688 ARG A O 5459 C CB A ARG A 695 ? 0.1917 0.1970 0.1729 0.0090 -0.0090 -0.0081 688 ARG A CB 5460 C CB B ARG A 695 ? 0.2017 0.2071 0.1828 0.0090 -0.0089 -0.0081 688 ARG A CB 5461 C CG A ARG A 695 ? 0.1981 0.2051 0.1775 0.0076 -0.0072 -0.0070 688 ARG A CG 5462 C CG B ARG A 695 ? 0.2024 0.2096 0.1817 0.0077 -0.0071 -0.0069 688 ARG A CG 5463 C CD A ARG A 695 ? 0.1967 0.2036 0.1746 0.0097 -0.0078 -0.0061 688 ARG A CD 5464 C CD B ARG A 695 ? 0.2030 0.2105 0.1812 0.0102 -0.0072 -0.0064 688 ARG A CD 5465 N NE A ARG A 695 ? 0.2121 0.2186 0.1897 0.0128 -0.0076 -0.0066 688 ARG A NE 5466 N NE B ARG A 695 ? 0.1765 0.1860 0.1549 0.0090 -0.0061 -0.0058 688 ARG A NE 5467 C CZ A ARG A 695 ? 0.2344 0.2404 0.2108 0.0154 -0.0076 -0.0060 688 ARG A CZ 5468 C CZ B ARG A 695 ? 0.1928 0.2033 0.1724 0.0105 -0.0052 -0.0054 688 ARG A CZ 5469 N NH1 A ARG A 695 ? 0.1860 0.1909 0.1608 0.0186 -0.0069 -0.0063 688 ARG A NH1 5470 N NH1 B ARG A 695 ? 0.2202 0.2296 0.1993 0.0134 -0.0046 -0.0052 688 ARG A NH1 5471 N NH2 A ARG A 695 ? 0.2512 0.2575 0.2278 0.0152 -0.0083 -0.0049 688 ARG A NH2 5472 N NH2 B ARG A 695 ? 0.0954 0.1078 0.0767 0.0093 -0.0047 -0.0052 688 ARG A NH2 5473 N N . HIS A 696 ? 0.1961 0.2013 0.1874 0.0079 -0.0109 -0.0117 689 HIS A N 5474 C CA . HIS A 696 ? 0.1938 0.1978 0.1892 0.0092 -0.0141 -0.0138 689 HIS A CA 5475 C C . HIS A 696 ? 0.2010 0.2050 0.2025 0.0058 -0.0137 -0.0134 689 HIS A C 5476 O O . HIS A 696 ? 0.2090 0.2151 0.2130 0.0031 -0.0104 -0.0125 689 HIS A O 5477 C CB . HIS A 696 ? 0.1989 0.2044 0.1965 0.0108 -0.0146 -0.0157 689 HIS A CB 5478 C CG . HIS A 696 ? 0.2001 0.2039 0.1996 0.0137 -0.0191 -0.0182 689 HIS A CG 5479 N ND1 . HIS A 696 ? 0.2069 0.2103 0.2135 0.0125 -0.0218 -0.0199 689 HIS A ND1 5480 C CD2 . HIS A 696 ? 0.2188 0.2209 0.2140 0.0179 -0.0215 -0.0194 689 HIS A CD2 5481 C CE1 . HIS A 696 ? 0.2293 0.2310 0.2358 0.0160 -0.0264 -0.0226 689 HIS A CE1 5482 N NE2 . HIS A 696 ? 0.2144 0.2151 0.2132 0.0195 -0.0262 -0.0222 689 HIS A NE2 5483 N N . VAL A 697 ? 0.1944 0.1957 0.1980 0.0062 -0.0166 -0.0139 690 VAL A N 5484 C CA . VAL A 697 ? 0.2004 0.2008 0.2097 0.0028 -0.0157 -0.0128 690 VAL A CA 5485 C C . VAL A 697 ? 0.2066 0.2089 0.2257 0.0017 -0.0165 -0.0150 690 VAL A C 5486 O O . VAL A 697 ? 0.2102 0.2131 0.2359 -0.0016 -0.0140 -0.0138 690 VAL A O 5487 C CB . VAL A 697 ? 0.2017 0.1980 0.2099 0.0037 -0.0186 -0.0125 690 VAL A CB 5488 C CG1 . VAL A 697 ? 0.2171 0.2116 0.2328 0.0005 -0.0182 -0.0115 690 VAL A CG1 5489 C CG2 . VAL A 697 ? 0.2189 0.2141 0.2192 0.0043 -0.0173 -0.0099 690 VAL A CG2 5490 N N . ILE A 698 ? 0.2053 0.2083 0.2257 0.0046 -0.0198 -0.0180 691 ILE A N 5491 C CA . ILE A 698 ? 0.2067 0.2118 0.2377 0.0037 -0.0213 -0.0204 691 ILE A CA 5492 C C . ILE A 698 ? 0.2087 0.2180 0.2424 0.0025 -0.0174 -0.0201 691 ILE A C 5493 O O . ILE A 698 ? 0.2112 0.2230 0.2546 0.0001 -0.0158 -0.0205 691 ILE A O 5494 C CB . ILE A 698 ? 0.2243 0.2279 0.2561 0.0078 -0.0277 -0.0243 691 ILE A CB 5495 C CG1 . ILE A 698 ? 0.2163 0.2152 0.2434 0.0099 -0.0316 -0.0251 691 ILE A CG1 5496 C CG2 . ILE A 698 ? 0.2372 0.2431 0.2822 0.0067 -0.0304 -0.0272 691 ILE A CG2 5497 C CD1 . ILE A 698 ? 0.2309 0.2277 0.2643 0.0067 -0.0316 -0.0242 691 ILE A CD1 5498 N N . TYR A 699 ? 0.2141 0.2241 0.2401 0.0044 -0.0160 -0.0196 692 TYR A N 5499 C CA . TYR A 699 ? 0.2058 0.2193 0.2338 0.0039 -0.0128 -0.0198 692 TYR A CA 5500 C C . TYR A 699 ? 0.2186 0.2324 0.2391 0.0028 -0.0083 -0.0174 692 TYR A C 5501 O O . TYR A 699 ? 0.2446 0.2566 0.2571 0.0046 -0.0090 -0.0165 692 TYR A O 5502 C CB . TYR A 699 ? 0.2117 0.2252 0.2380 0.0079 -0.0162 -0.0220 692 TYR A CB 5503 C CG . TYR A 699 ? 0.2176 0.2309 0.2511 0.0098 -0.0216 -0.0251 692 TYR A CG 5504 C CD1 . TYR A 699 ? 0.2404 0.2570 0.2861 0.0079 -0.0215 -0.0267 692 TYR A CD1 5505 C CD2 . TYR A 699 ? 0.2274 0.2373 0.2557 0.0139 -0.0270 -0.0268 692 TYR A CD2 5506 C CE1 . TYR A 699 ? 0.2317 0.2486 0.2853 0.0097 -0.0271 -0.0300 692 TYR A CE1 5507 C CE2 . TYR A 699 ? 0.2371 0.2467 0.2716 0.0160 -0.0328 -0.0303 692 TYR A CE2 5508 C CZ . TYR A 699 ? 0.2505 0.2637 0.2980 0.0138 -0.0332 -0.0320 692 TYR A CZ 5509 O OH . TYR A 699 ? 0.2515 0.2647 0.3065 0.0160 -0.0397 -0.0359 692 TYR A OH 5510 N N . ALA A 700 ? 0.2040 0.2203 0.2274 0.0002 -0.0038 -0.0167 693 ALA A N 5511 C CA . ALA A 700 ? 0.2038 0.2205 0.2204 -0.0002 -0.0003 -0.0155 693 ALA A CA 5512 C C . ALA A 700 ? 0.2053 0.2251 0.2267 -0.0010 0.0030 -0.0167 693 ALA A C 5513 O O . ALA A 700 ? 0.2199 0.2418 0.2503 -0.0019 0.0036 -0.0177 693 ALA A O 5514 C CB . ALA A 700 ? 0.2073 0.2226 0.2184 -0.0026 0.0023 -0.0129 693 ALA A CB 5515 N N . PRO A 701 ? 0.2086 0.2289 0.2253 -0.0004 0.0051 -0.0169 694 PRO A N 5516 C CA . PRO A 701 ? 0.2121 0.2349 0.2328 -0.0012 0.0088 -0.0181 694 PRO A CA 5517 C C . PRO A 701 ? 0.2182 0.2418 0.2403 -0.0041 0.0132 -0.0167 694 PRO A C 5518 O O . PRO A 701 ? 0.2281 0.2496 0.2437 -0.0054 0.0140 -0.0146 694 PRO A O 5519 C CB . PRO A 701 ? 0.2232 0.2452 0.2369 -0.0005 0.0101 -0.0183 694 PRO A CB 5520 C CG . PRO A 701 ? 0.2170 0.2367 0.2260 0.0014 0.0063 -0.0176 694 PRO A CG 5521 C CD . PRO A 701 ? 0.2231 0.2414 0.2313 0.0006 0.0044 -0.0161 694 PRO A CD 5522 N N . SER A 702 ? 0.2121 0.2387 0.2427 -0.0050 0.0161 -0.0178 695 SER A N 5523 C CA . SER A 702 ? 0.2156 0.2428 0.2476 -0.0076 0.0214 -0.0161 695 SER A CA 5524 C C . SER A 702 ? 0.2313 0.2567 0.2521 -0.0081 0.0249 -0.0149 695 SER A C 5525 O O . SER A 702 ? 0.2327 0.2584 0.2497 -0.0069 0.0256 -0.0167 695 SER A O 5526 C CB . SER A 702 ? 0.2169 0.2481 0.2601 -0.0080 0.0249 -0.0177 695 SER A CB 5527 O OG . SER A 702 ? 0.2421 0.2737 0.2852 -0.0103 0.0312 -0.0157 695 SER A OG 5528 N N . SER A 703 ? 0.2233 0.2466 0.2390 -0.0099 0.0272 -0.0121 696 SER A N 5529 C CA . SER A 703 ? 0.2401 0.2613 0.2444 -0.0101 0.0303 -0.0111 696 SER A CA 5530 C C . SER A 703 ? 0.2488 0.2718 0.2534 -0.0102 0.0361 -0.0125 696 SER A C 5531 O O . SER A 703 ? 0.2669 0.2882 0.2615 -0.0097 0.0381 -0.0128 696 SER A O 5532 C CB . SER A 703 ? 0.2450 0.2630 0.2437 -0.0116 0.0315 -0.0074 696 SER A CB 5533 O OG A SER A 703 ? 0.1686 0.1844 0.1648 -0.0112 0.0262 -0.0063 696 SER A OG 5534 O OG B SER A 703 ? 0.3287 0.3475 0.3334 -0.0134 0.0366 -0.0055 696 SER A OG 5535 N N . HIS A 704 ? 0.2393 0.2658 0.2555 -0.0105 0.0385 -0.0135 697 HIS A N 5536 C CA . HIS A 704 ? 0.2506 0.2794 0.2692 -0.0102 0.0445 -0.0151 697 HIS A CA 5537 C C . HIS A 704 ? 0.2541 0.2853 0.2779 -0.0082 0.0427 -0.0188 697 HIS A C 5538 O O . HIS A 704 ? 0.2728 0.3058 0.2979 -0.0075 0.0471 -0.0208 697 HIS A O 5539 C CB . HIS A 704 ? 0.2593 0.2906 0.2885 -0.0121 0.0497 -0.0134 697 HIS A CB 5540 C CG . HIS A 704 ? 0.2855 0.3138 0.3097 -0.0140 0.0519 -0.0092 697 HIS A CG 5541 N ND1 . HIS A 704 ? 0.3008 0.3263 0.3137 -0.0142 0.0575 -0.0070 697 HIS A ND1 5542 C CD2 . HIS A 704 ? 0.3126 0.3391 0.3398 -0.0154 0.0489 -0.0067 697 HIS A CD2 5543 C CE1 . HIS A 704 ? 0.3225 0.3448 0.3320 -0.0157 0.0579 -0.0030 697 HIS A CE1 5544 N NE2 . HIS A 704 ? 0.3127 0.3356 0.3313 -0.0166 0.0528 -0.0028 697 HIS A NE2 5545 N N . ASN A 705 ? 0.2340 0.2652 0.2606 -0.0071 0.0364 -0.0199 698 ASN A N 5546 C CA . ASN A 705 ? 0.2369 0.2700 0.2693 -0.0049 0.0344 -0.0229 698 ASN A CA 5547 C C . ASN A 705 ? 0.2307 0.2620 0.2615 -0.0035 0.0277 -0.0230 698 ASN A C 5548 O O . ASN A 705 ? 0.2219 0.2539 0.2590 -0.0032 0.0241 -0.0227 698 ASN A O 5549 C CB . ASN A 705 ? 0.2437 0.2811 0.2905 -0.0049 0.0359 -0.0240 698 ASN A CB 5550 C CG . ASN A 705 ? 0.2365 0.2755 0.2897 -0.0022 0.0326 -0.0269 698 ASN A CG 5551 O OD1 . ASN A 705 ? 0.2265 0.2632 0.2729 -0.0006 0.0310 -0.0280 698 ASN A OD1 5552 N ND2 . ASN A 705 ? 0.2581 0.3007 0.3245 -0.0016 0.0314 -0.0281 698 ASN A ND2 5553 N N . LYS A 706 ? 0.2270 0.2558 0.2495 -0.0025 0.0262 -0.0235 699 LYS A N 5554 C CA . LYS A 706 ? 0.2230 0.2498 0.2429 -0.0010 0.0209 -0.0231 699 LYS A CA 5555 C C . LYS A 706 ? 0.2237 0.2518 0.2516 0.0012 0.0175 -0.0243 699 LYS A C 5556 O O . LYS A 706 ? 0.2170 0.2436 0.2437 0.0025 0.0131 -0.0235 699 LYS A O 5557 C CB . LYS A 706 ? 0.2370 0.2617 0.2497 -0.0003 0.0209 -0.0240 699 LYS A CB 5558 C CG . LYS A 706 ? 0.2532 0.2757 0.2629 0.0011 0.0166 -0.0231 699 LYS A CG 5559 C CD . LYS A 706 ? 0.2279 0.2484 0.2321 0.0011 0.0170 -0.0240 699 LYS A CD 5560 C CE . LYS A 706 ? 0.2355 0.2540 0.2362 0.0018 0.0137 -0.0223 699 LYS A CE 5561 N NZ . LYS A 706 ? 0.2563 0.2732 0.2543 0.0018 0.0140 -0.0234 699 LYS A NZ 5562 N N . TYR A 707 ? 0.2218 0.2524 0.2573 0.0021 0.0192 -0.0262 700 TYR A N 5563 C CA . TYR A 707 ? 0.2110 0.2425 0.2536 0.0048 0.0152 -0.0275 700 TYR A CA 5564 C C . TYR A 707 ? 0.2280 0.2609 0.2772 0.0046 0.0120 -0.0272 700 TYR A C 5565 O O . TYR A 707 ? 0.2443 0.2766 0.2960 0.0072 0.0071 -0.0279 700 TYR A O 5566 C CB . TYR A 707 ? 0.2217 0.2559 0.2722 0.0060 0.0175 -0.0298 700 TYR A CB 5567 C CG . TYR A 707 ? 0.2115 0.2439 0.2573 0.0069 0.0198 -0.0309 700 TYR A CG 5568 C CD1 . TYR A 707 ? 0.2262 0.2547 0.2645 0.0082 0.0173 -0.0301 700 TYR A CD1 5569 C CD2 . TYR A 707 ? 0.2229 0.2573 0.2728 0.0068 0.0244 -0.0329 700 TYR A CD2 5570 C CE1 . TYR A 707 ? 0.2191 0.2457 0.2547 0.0089 0.0192 -0.0314 700 TYR A CE1 5571 C CE2 . TYR A 707 ? 0.2171 0.2495 0.2634 0.0079 0.0261 -0.0345 700 TYR A CE2 5572 C CZ . TYR A 707 ? 0.2498 0.2782 0.2893 0.0088 0.0233 -0.0338 700 TYR A CZ 5573 O OH . TYR A 707 ? 0.2437 0.2699 0.2809 0.0097 0.0248 -0.0355 700 TYR A OH 5574 N N . ALA A 708 ? 0.2256 0.2602 0.2782 0.0018 0.0147 -0.0263 701 ALA A N 5575 C CA . ALA A 708 ? 0.2252 0.2613 0.2866 0.0013 0.0118 -0.0264 701 ALA A CA 5576 C C . ALA A 708 ? 0.2386 0.2715 0.2936 0.0007 0.0086 -0.0246 701 ALA A C 5577 O O . ALA A 708 ? 0.2450 0.2757 0.2913 -0.0009 0.0109 -0.0226 701 ALA A O 5578 C CB . ALA A 708 ? 0.2242 0.2638 0.2945 -0.0016 0.0171 -0.0261 701 ALA A CB 5579 N N . GLY A 709 ? 0.2217 0.2541 0.2810 0.0021 0.0031 -0.0256 702 GLY A N 5580 C CA . GLY A 709 ? 0.2366 0.2659 0.2906 0.0014 0.0005 -0.0241 702 GLY A CA 5581 C C . GLY A 709 ? 0.2350 0.2653 0.2962 -0.0020 0.0027 -0.0230 702 GLY A C 5582 O O . GLY A 709 ? 0.2458 0.2796 0.3190 -0.0031 0.0042 -0.0242 702 GLY A O 5583 N N . GLU A 710 ? 0.2198 0.2470 0.2742 -0.0035 0.0033 -0.0206 703 GLU A N 5584 C CA . GLU A 710 ? 0.2129 0.2399 0.2733 -0.0066 0.0050 -0.0190 703 GLU A CA 5585 C C . GLU A 710 ? 0.2162 0.2398 0.2751 -0.0056 -0.0008 -0.0193 703 GLU A C 5586 O O . GLU A 710 ? 0.2161 0.2368 0.2647 -0.0036 -0.0032 -0.0190 703 GLU A O 5587 C CB . GLU A 710 ? 0.2318 0.2574 0.2845 -0.0090 0.0109 -0.0157 703 GLU A CB 5588 C CG . GLU A 710 ? 0.2324 0.2576 0.2920 -0.0123 0.0142 -0.0133 703 GLU A CG 5589 C CD . GLU A 710 ? 0.2740 0.3036 0.3496 -0.0135 0.0158 -0.0151 703 GLU A CD 5590 O OE1 . GLU A 710 ? 0.2474 0.2801 0.3253 -0.0140 0.0213 -0.0151 703 GLU A OE1 5591 O OE2 . GLU A 710 ? 0.2835 0.3136 0.3698 -0.0136 0.0113 -0.0169 703 GLU A OE2 5592 N N . SER A 711 ? 0.2166 0.2404 0.2861 -0.0069 -0.0029 -0.0202 704 SER A N 5593 C CA . SER A 711 ? 0.2114 0.2312 0.2793 -0.0060 -0.0083 -0.0207 704 SER A CA 5594 C C . SER A 711 ? 0.2154 0.2322 0.2808 -0.0090 -0.0052 -0.0172 704 SER A C 5595 O O . SER A 711 ? 0.2104 0.2286 0.2799 -0.0121 0.0007 -0.0147 704 SER A O 5596 C CB . SER A 711 ? 0.2215 0.2424 0.3024 -0.0054 -0.0137 -0.0242 704 SER A CB 5597 O OG . SER A 711 ? 0.2419 0.2663 0.3373 -0.0088 -0.0101 -0.0240 704 SER A OG 5598 N N . PHE A 712 ? 0.2096 0.2222 0.2681 -0.0077 -0.0088 -0.0167 705 PHE A N 5599 C CA . PHE A 712 ? 0.2061 0.2150 0.2599 -0.0098 -0.0064 -0.0131 705 PHE A CA 5600 C C . PHE A 712 ? 0.2073 0.2173 0.2552 -0.0117 0.0005 -0.0096 705 PHE A C 5601 O O . PHE A 712 ? 0.2019 0.2112 0.2530 -0.0147 0.0050 -0.0067 705 PHE A O 5602 C CB . PHE A 712 ? 0.2083 0.2154 0.2734 -0.0123 -0.0072 -0.0128 705 PHE A CB 5603 C CG . PHE A 712 ? 0.2023 0.2066 0.2704 -0.0101 -0.0147 -0.0163 705 PHE A CG 5604 C CD1 . PHE A 712 ? 0.2230 0.2234 0.2803 -0.0072 -0.0182 -0.0164 705 PHE A CD1 5605 C CD2 . PHE A 712 ? 0.2125 0.2183 0.2945 -0.0105 -0.0183 -0.0197 705 PHE A CD2 5606 C CE1 . PHE A 712 ? 0.2309 0.2283 0.2897 -0.0046 -0.0249 -0.0199 705 PHE A CE1 5607 C CE2 . PHE A 712 ? 0.2227 0.2255 0.3065 -0.0081 -0.0258 -0.0234 705 PHE A CE2 5608 C CZ . PHE A 712 ? 0.2268 0.2251 0.2984 -0.0050 -0.0290 -0.0236 705 PHE A CZ 5609 N N . PRO A 713 ? 0.2036 0.2149 0.2425 -0.0099 0.0013 -0.0099 706 PRO A N 5610 C CA . PRO A 713 ? 0.2069 0.2194 0.2399 -0.0112 0.0071 -0.0078 706 PRO A CA 5611 C C . PRO A 713 ? 0.2203 0.2293 0.2462 -0.0128 0.0097 -0.0039 706 PRO A C 5612 O O . PRO A 713 ? 0.2323 0.2417 0.2562 -0.0145 0.0152 -0.0016 706 PRO A O 5613 C CB . PRO A 713 ? 0.1973 0.2106 0.2217 -0.0085 0.0054 -0.0093 706 PRO A CB 5614 C CG . PRO A 713 ? 0.2081 0.2194 0.2310 -0.0059 -0.0005 -0.0108 706 PRO A CG 5615 C CD . PRO A 713 ? 0.2028 0.2142 0.2367 -0.0064 -0.0032 -0.0125 706 PRO A CD 5616 N N . GLY A 714 ? 0.2103 0.2157 0.2318 -0.0118 0.0059 -0.0030 707 GLY A N 5617 C CA . GLY A 714 ? 0.2269 0.2286 0.2413 -0.0129 0.0079 0.0008 707 GLY A CA 5618 C C . GLY A 714 ? 0.2269 0.2271 0.2482 -0.0159 0.0119 0.0036 707 GLY A C 5619 O O . GLY A 714 ? 0.2405 0.2391 0.2561 -0.0173 0.0169 0.0072 707 GLY A O 5620 N N . ILE A 715 ? 0.2163 0.2166 0.2495 -0.0168 0.0099 0.0021 708 ILE A N 5621 C CA . ILE A 715 ? 0.2223 0.2215 0.2646 -0.0201 0.0140 0.0048 708 ILE A CA 5622 C C . ILE A 715 ? 0.2377 0.2411 0.2844 -0.0217 0.0203 0.0051 708 ILE A C 5623 O O . ILE A 715 ? 0.2513 0.2534 0.2978 -0.0239 0.0266 0.0090 708 ILE A O 5624 C CB . ILE A 715 ? 0.2119 0.2105 0.2680 -0.0208 0.0096 0.0024 708 ILE A CB 5625 C CG1 . ILE A 715 ? 0.2364 0.2309 0.2876 -0.0184 0.0030 0.0010 708 ILE A CG1 5626 C CG2 . ILE A 715 ? 0.2271 0.2234 0.2929 -0.0245 0.0141 0.0059 708 ILE A CG2 5627 C CD1 . ILE A 715 ? 0.2429 0.2367 0.3068 -0.0184 -0.0026 -0.0027 708 ILE A CD1 5628 N N . TYR A 716 ? 0.2233 0.2314 0.2734 -0.0203 0.0189 0.0012 709 TYR A N 5629 C CA . TYR A 716 ? 0.2310 0.2435 0.2865 -0.0214 0.0248 0.0010 709 TYR A CA 5630 C C . TYR A 716 ? 0.2331 0.2442 0.2760 -0.0217 0.0309 0.0042 709 TYR A C 5631 O O . TYR A 716 ? 0.2415 0.2531 0.2871 -0.0236 0.0379 0.0069 709 TYR A O 5632 C CB . TYR A 716 ? 0.2212 0.2383 0.2803 -0.0192 0.0217 -0.0037 709 TYR A CB 5633 C CG . TYR A 716 ? 0.2146 0.2362 0.2802 -0.0203 0.0278 -0.0041 709 TYR A CG 5634 C CD1 . TYR A 716 ? 0.2274 0.2528 0.3099 -0.0217 0.0285 -0.0058 709 TYR A CD1 5635 C CD2 . TYR A 716 ? 0.2482 0.2702 0.3033 -0.0197 0.0329 -0.0031 709 TYR A CD2 5636 C CE1 . TYR A 716 ? 0.2413 0.2713 0.3311 -0.0225 0.0348 -0.0061 709 TYR A CE1 5637 C CE2 . TYR A 716 ? 0.2414 0.2673 0.3022 -0.0203 0.0391 -0.0036 709 TYR A CE2 5638 C CZ . TYR A 716 ? 0.2594 0.2894 0.3378 -0.0217 0.0402 -0.0050 709 TYR A CZ 5639 O OH . TYR A 716 ? 0.2703 0.3046 0.3551 -0.0221 0.0466 -0.0056 709 TYR A OH 5640 N N . ASP A 717 ? 0.2334 0.2430 0.2628 -0.0195 0.0285 0.0039 710 ASP A N 5641 C CA . ASP A 717 ? 0.2414 0.2495 0.2582 -0.0193 0.0332 0.0062 710 ASP A CA 5642 C C . ASP A 717 ? 0.2540 0.2572 0.2656 -0.0207 0.0366 0.0113 710 ASP A C 5643 O O . ASP A 717 ? 0.2726 0.2748 0.2781 -0.0213 0.0428 0.0139 710 ASP A O 5644 C CB . ASP A 717 ? 0.2404 0.2481 0.2458 -0.0167 0.0291 0.0044 710 ASP A CB 5645 C CG . ASP A 717 ? 0.2787 0.2908 0.2871 -0.0153 0.0281 0.0002 710 ASP A CG 5646 O OD1 . ASP A 717 ? 0.2646 0.2800 0.2812 -0.0161 0.0316 -0.0011 710 ASP A OD1 5647 O OD2 . ASP A 717 ? 0.2766 0.2886 0.2791 -0.0134 0.0241 -0.0016 710 ASP A OD2 5648 N N . ALA A 718 ? 0.2522 0.2520 0.2660 -0.0211 0.0327 0.0128 711 ALA A N 5649 C CA . ALA A 718 ? 0.2596 0.2541 0.2693 -0.0225 0.0360 0.0181 711 ALA A CA 5650 C C . ALA A 718 ? 0.2715 0.2665 0.2910 -0.0254 0.0434 0.0208 711 ALA A C 5651 O O . ALA A 718 ? 0.2786 0.2699 0.2916 -0.0263 0.0493 0.0257 711 ALA A O 5652 C CB . ALA A 718 ? 0.2546 0.2450 0.2662 -0.0223 0.0302 0.0189 711 ALA A CB 5653 N N . LEU A 719 ? 0.2617 0.2612 0.2970 -0.0267 0.0432 0.0178 712 LEU A N 5654 C CA . LEU A 719 ? 0.2643 0.2654 0.3122 -0.0296 0.0503 0.0200 712 LEU A CA 5655 C C . LEU A 719 ? 0.2699 0.2750 0.3163 -0.0295 0.0576 0.0197 712 LEU A C 5656 O O . LEU A 719 ? 0.2927 0.2984 0.3461 -0.0316 0.0652 0.0226 712 LEU A O 5657 C CB . LEU A 719 ? 0.2611 0.2655 0.3282 -0.0310 0.0463 0.0165 712 LEU A CB 5658 C CG . LEU A 719 ? 0.2539 0.2538 0.3268 -0.0321 0.0414 0.0174 712 LEU A CG 5659 C CD1 . LEU A 719 ? 0.2778 0.2815 0.3667 -0.0322 0.0349 0.0120 712 LEU A CD1 5660 C CD2 . LEU A 719 ? 0.2914 0.2874 0.3692 -0.0353 0.0484 0.0233 712 LEU A CD2 5661 N N . PHE A 720 ? 0.2745 0.2822 0.3124 -0.0269 0.0553 0.0162 713 PHE A N 5662 C CA . PHE A 720 ? 0.2829 0.2948 0.3213 -0.0265 0.0612 0.0147 713 PHE A CA 5663 C C . PHE A 720 ? 0.3073 0.3159 0.3342 -0.0266 0.0698 0.0193 713 PHE A C 5664 O O . PHE A 720 ? 0.3052 0.3088 0.3153 -0.0252 0.0688 0.0215 713 PHE A O 5665 C CB . PHE A 720 ? 0.2748 0.2894 0.3066 -0.0237 0.0567 0.0099 713 PHE A CB 5666 C CG . PHE A 720 ? 0.2864 0.3052 0.3202 -0.0230 0.0623 0.0078 713 PHE A CG 5667 C CD1 . PHE A 720 ? 0.2800 0.3046 0.3307 -0.0236 0.0626 0.0047 713 PHE A CD1 5668 C CD2 . PHE A 720 ? 0.3168 0.3338 0.3364 -0.0217 0.0673 0.0088 713 PHE A CD2 5669 C CE1 . PHE A 720 ? 0.3166 0.3452 0.3701 -0.0228 0.0682 0.0028 713 PHE A CE1 5670 C CE2 . PHE A 720 ? 0.3137 0.3344 0.3352 -0.0209 0.0730 0.0067 713 PHE A CE2 5671 C CZ . PHE A 720 ? 0.3203 0.3468 0.3591 -0.0215 0.0737 0.0038 713 PHE A CZ 5672 N N . ASP A 721 ? 0.3160 0.3272 0.3520 -0.0282 0.0780 0.0207 714 ASP A N 5673 C CA . ASP A 721 ? 0.3378 0.3459 0.3631 -0.0280 0.0876 0.0252 714 ASP A CA 5674 C C . ASP A 721 ? 0.3536 0.3541 0.3685 -0.0286 0.0884 0.0312 714 ASP A C 5675 O O . ASP A 721 ? 0.3689 0.3649 0.3670 -0.0271 0.0930 0.0346 714 ASP A O 5676 C CB . ASP A 721 ? 0.3351 0.3436 0.3446 -0.0248 0.0882 0.0223 714 ASP A CB 5677 C CG . ASP A 721 ? 0.3924 0.3985 0.3909 -0.0240 0.0985 0.0258 714 ASP A CG 5678 O OD1 . ASP A 721 ? 0.4014 0.4095 0.4105 -0.0257 0.1071 0.0282 714 ASP A OD1 5679 O OD2 . ASP A 721 ? 0.4105 0.4127 0.3898 -0.0214 0.0980 0.0258 714 ASP A OD2 5680 N N . ILE A 722 ? 0.3437 0.3425 0.3684 -0.0307 0.0840 0.0326 715 ILE A N 5681 C CA . ILE A 722 ? 0.3506 0.3418 0.3659 -0.0309 0.0834 0.0380 715 ILE A CA 5682 C C . ILE A 722 ? 0.3812 0.3682 0.3930 -0.0322 0.0942 0.0448 715 ILE A C 5683 O O . ILE A 722 ? 0.3862 0.3662 0.3825 -0.0310 0.0953 0.0496 715 ILE A O 5684 C CB . ILE A 722 ? 0.3421 0.3321 0.3701 -0.0328 0.0765 0.0375 715 ILE A CB 5685 C CG1 . ILE A 722 ? 0.3423 0.3242 0.3591 -0.0323 0.0744 0.0424 715 ILE A CG1 5686 C CG2 . ILE A 722 ? 0.3195 0.3127 0.3702 -0.0363 0.0803 0.0379 715 ILE A CG2 5687 C CD1 . ILE A 722 ? 0.3290 0.3097 0.3528 -0.0325 0.0650 0.0400 715 ILE A CD1 5688 N N . GLU A 723 ? 0.3912 0.3825 0.4172 -0.0343 0.1022 0.0453 716 GLU A N 5689 C CA . GLU A 723 ? 0.4349 0.4226 0.4594 -0.0356 0.1138 0.0521 716 GLU A CA 5690 C C . GLU A 723 ? 0.4573 0.4413 0.4581 -0.0322 0.1193 0.0543 716 GLU A C 5691 O O . GLU A 723 ? 0.4801 0.4588 0.4728 -0.0322 0.1284 0.0609 716 GLU A O 5692 C CB . GLU A 723 ? 0.4285 0.4226 0.4752 -0.0385 0.1213 0.0517 716 GLU A CB 5693 C CG . GLU A 723 ? 0.4521 0.4534 0.5002 -0.0368 0.1242 0.0466 716 GLU A CG 5694 C CD . GLU A 723 ? 0.4568 0.4650 0.5169 -0.0364 0.1145 0.0388 716 GLU A CD 5695 O OE1 . GLU A 723 ? 0.4279 0.4348 0.4885 -0.0363 0.1042 0.0364 716 GLU A OE1 5696 O OE2 . GLU A 723 ? 0.4769 0.4917 0.5454 -0.0359 0.1175 0.0350 716 GLU A OE2 5697 N N . SER A 724 ? 0.4617 0.4480 0.4512 -0.0291 0.1138 0.0489 717 SER A N 5698 C CA . SER A 724 ? 0.4896 0.4725 0.4563 -0.0255 0.1172 0.0496 717 SER A CA 5699 C C . SER A 724 ? 0.5073 0.4832 0.4540 -0.0230 0.1106 0.0513 717 SER A C 5700 O O . SER A 724 ? 0.5227 0.4945 0.4493 -0.0198 0.1128 0.0523 717 SER A O 5701 C CB . SER A 724 ? 0.4805 0.4695 0.4463 -0.0234 0.1157 0.0425 717 SER A CB 5702 O OG . SER A 724 ? 0.4833 0.4787 0.4665 -0.0252 0.1226 0.0412 717 SER A OG 5703 N N A LYS A 725 ? 0.5008 0.4752 0.4528 -0.0241 0.1023 0.0514 718 LYS A N 5704 N N B LYS A 725 ? 0.4978 0.4722 0.4499 -0.0241 0.1022 0.0513 718 LYS A N 5705 C CA A LYS A 725 ? 0.5102 0.4788 0.4458 -0.0217 0.0951 0.0525 718 LYS A CA 5706 C CA B LYS A 725 ? 0.5093 0.4778 0.4450 -0.0217 0.0951 0.0526 718 LYS A CA 5707 C C A LYS A 725 ? 0.5344 0.4942 0.4575 -0.0211 0.1003 0.0606 718 LYS A C 5708 C C B LYS A 725 ? 0.5346 0.4944 0.4574 -0.0210 0.1009 0.0606 718 LYS A C 5709 O O A LYS A 725 ? 0.5374 0.4948 0.4706 -0.0238 0.1058 0.0657 718 LYS A O 5710 O O B LYS A 725 ? 0.5399 0.4976 0.4723 -0.0237 0.1075 0.0659 718 LYS A O 5711 C CB A LYS A 725 ? 0.4923 0.4624 0.4380 -0.0227 0.0848 0.0496 718 LYS A CB 5712 C CB B LYS A 725 ? 0.4885 0.4579 0.4344 -0.0229 0.0851 0.0504 718 LYS A CB 5713 C CG A LYS A 725 ? 0.4761 0.4539 0.4310 -0.0226 0.0792 0.0420 718 LYS A CG 5714 C CG B LYS A 725 ? 0.4843 0.4609 0.4394 -0.0227 0.0780 0.0427 718 LYS A CG 5715 C CD A LYS A 725 ? 0.4698 0.4491 0.4106 -0.0195 0.0789 0.0384 718 LYS A CD 5716 C CD B LYS A 725 ? 0.4985 0.4759 0.4386 -0.0194 0.0732 0.0387 718 LYS A CD 5717 C CE A LYS A 725 ? 0.4556 0.4425 0.4076 -0.0198 0.0774 0.0319 718 LYS A CE 5718 C CE B LYS A 725 ? 0.4890 0.4737 0.4390 -0.0194 0.0692 0.0317 718 LYS A CE 5719 N NZ A LYS A 725 ? 0.4556 0.4457 0.4142 -0.0207 0.0868 0.0321 718 LYS A NZ 5720 N NZ B LYS A 725 ? 0.4671 0.4535 0.4273 -0.0201 0.0610 0.0293 718 LYS A NZ 5721 N N . VAL A 726 ? 0.5516 0.5064 0.4528 -0.0174 0.0981 0.0615 719 VAL A N 5722 C CA . VAL A 726 ? 0.5860 0.5317 0.4705 -0.0156 0.1032 0.0691 719 VAL A CA 5723 C C . VAL A 726 ? 0.5828 0.5225 0.4707 -0.0169 0.0999 0.0744 719 VAL A C 5724 O O . VAL A 726 ? 0.5996 0.5326 0.4838 -0.0174 0.1069 0.0820 719 VAL A O 5725 C CB . VAL A 726 ? 0.6036 0.5460 0.4635 -0.0107 0.0999 0.0672 719 VAL A CB 5726 C CG1 . VAL A 726 ? 0.6485 0.5817 0.4909 -0.0080 0.0966 0.0727 719 VAL A CG1 5727 C CG2 . VAL A 726 ? 0.6360 0.5791 0.4870 -0.0091 0.1097 0.0670 719 VAL A CG2 5728 N N . ASP A 727 ? 0.5591 0.5011 0.4546 -0.0174 0.0896 0.0705 720 ASP A N 5729 C CA . ASP A 727 ? 0.5473 0.4840 0.4467 -0.0182 0.0850 0.0743 720 ASP A CA 5730 C C . ASP A 727 ? 0.5162 0.4581 0.4399 -0.0221 0.0823 0.0713 720 ASP A C 5731 O O . ASP A 727 ? 0.4919 0.4379 0.4213 -0.0217 0.0735 0.0656 720 ASP A O 5732 C CB . ASP A 727 ? 0.5522 0.4871 0.4389 -0.0147 0.0745 0.0719 720 ASP A CB 5733 C CG . ASP A 727 ? 0.5733 0.5020 0.4613 -0.0147 0.0696 0.0759 720 ASP A CG 5734 O OD1 . ASP A 727 ? 0.5794 0.5057 0.4803 -0.0177 0.0730 0.0796 720 ASP A OD1 5735 O OD2 . ASP A 727 ? 0.6454 0.5716 0.5220 -0.0115 0.0619 0.0752 720 ASP A OD2 5736 N N . PRO A 728 ? 0.5013 0.4429 0.4393 -0.0256 0.0898 0.0749 721 PRO A N 5737 C CA . PRO A 728 ? 0.4812 0.4277 0.4426 -0.0291 0.0869 0.0713 721 PRO A CA 5738 C C . PRO A 728 ? 0.4657 0.4090 0.4318 -0.0292 0.0777 0.0706 721 PRO A C 5739 O O . PRO A 728 ? 0.4348 0.3830 0.4143 -0.0302 0.0714 0.0650 721 PRO A O 5740 C CB . PRO A 728 ? 0.4912 0.4362 0.4653 -0.0327 0.0974 0.0767 721 PRO A CB 5741 C CG . PRO A 728 ? 0.5200 0.4567 0.4759 -0.0309 0.1049 0.0847 721 PRO A CG 5742 C CD . PRO A 728 ? 0.5255 0.4623 0.4592 -0.0264 0.1016 0.0821 721 PRO A CD 5743 N N . SER A 729 ? 0.4711 0.4060 0.4258 -0.0277 0.0769 0.0763 722 SER A N 5744 C CA . SER A 729 ? 0.4675 0.3991 0.4257 -0.0272 0.0682 0.0756 722 SER A CA 5745 C C . SER A 729 ? 0.4449 0.3816 0.3994 -0.0246 0.0585 0.0684 722 SER A C 5746 O O . SER A 729 ? 0.4205 0.3599 0.3867 -0.0253 0.0520 0.0640 722 SER A O 5747 C CB . SER A 729 ? 0.4867 0.4081 0.4316 -0.0254 0.0690 0.0831 722 SER A CB 5748 O OG . SER A 729 ? 0.5272 0.4459 0.4755 -0.0245 0.0603 0.0817 722 SER A OG 5749 N N . LYS A 730 ? 0.4340 0.3722 0.3724 -0.0216 0.0577 0.0671 723 LYS A N 5750 C CA . LYS A 730 ? 0.4368 0.3800 0.3721 -0.0193 0.0495 0.0606 723 LYS A CA 5751 C C . LYS A 730 ? 0.4008 0.3526 0.3506 -0.0211 0.0487 0.0540 723 LYS A C 5752 O O . LYS A 730 ? 0.3884 0.3437 0.3444 -0.0205 0.0415 0.0491 723 LYS A O 5753 C CB . LYS A 730 ? 0.4545 0.3971 0.3705 -0.0159 0.0493 0.0606 723 LYS A CB 5754 C CG . LYS A 730 ? 0.5118 0.4595 0.4249 -0.0137 0.0413 0.0542 723 LYS A CG 5755 C CD . LYS A 730 ? 0.6114 0.5587 0.5069 -0.0106 0.0412 0.0535 723 LYS A CD 5756 C CE . LYS A 730 ? 0.6534 0.6056 0.5480 -0.0087 0.0329 0.0474 723 LYS A CE 5757 N NZ . LYS A 730 ? 0.7146 0.6674 0.5949 -0.0062 0.0325 0.0453 723 LYS A NZ 5758 N N . ALA A 731 ? 0.3881 0.3433 0.3428 -0.0229 0.0560 0.0541 724 ALA A N 5759 C CA . ALA A 731 ? 0.3544 0.3176 0.3220 -0.0243 0.0555 0.0481 724 ALA A CA 5760 C C . ALA A 731 ? 0.3406 0.3050 0.3265 -0.0266 0.0517 0.0461 724 ALA A C 5761 O O . ALA A 731 ? 0.3205 0.2896 0.3130 -0.0260 0.0458 0.0405 724 ALA A O 5762 C CB . ALA A 731 ? 0.3653 0.3313 0.3357 -0.0258 0.0647 0.0491 724 ALA A CB 5763 N N . TRP A 732 ? 0.3323 0.2921 0.3261 -0.0290 0.0552 0.0507 725 TRP A N 5764 C CA . TRP A 732 ? 0.3198 0.2801 0.3313 -0.0311 0.0511 0.0485 725 TRP A CA 5765 C C . TRP A 732 ? 0.3209 0.2783 0.3290 -0.0289 0.0420 0.0465 725 TRP A C 5766 O O . TRP A 732 ? 0.3016 0.2613 0.3208 -0.0292 0.0362 0.0419 725 TRP A O 5767 C CB . TRP A 732 ? 0.3191 0.2753 0.3417 -0.0346 0.0576 0.0538 725 TRP A CB 5768 C CG . TRP A 732 ? 0.3179 0.2798 0.3510 -0.0370 0.0652 0.0533 725 TRP A CG 5769 C CD1 . TRP A 732 ? 0.3336 0.2950 0.3601 -0.0374 0.0750 0.0578 725 TRP A CD1 5770 C CD2 . TRP A 732 ? 0.3120 0.2810 0.3633 -0.0388 0.0635 0.0478 725 TRP A CD2 5771 N NE1 . TRP A 732 ? 0.3517 0.3198 0.3927 -0.0396 0.0799 0.0554 725 TRP A NE1 5772 C CE2 . TRP A 732 ? 0.3171 0.2901 0.3737 -0.0404 0.0726 0.0492 725 TRP A CE2 5773 C CE3 . TRP A 732 ? 0.2897 0.2619 0.3531 -0.0388 0.0550 0.0416 725 TRP A CE3 5774 C CZ2 . TRP A 732 ? 0.3264 0.3067 0.4014 -0.0423 0.0733 0.0448 725 TRP A CZ2 5775 C CZ3 . TRP A 732 ? 0.3012 0.2803 0.3816 -0.0405 0.0552 0.0372 725 TRP A CZ3 5776 C CH2 . TRP A 732 ? 0.2928 0.2762 0.3794 -0.0422 0.0642 0.0388 725 TRP A CH2 5777 N N . GLY A 733 ? 0.3268 0.2791 0.3193 -0.0265 0.0405 0.0498 726 GLY A N 5778 C CA . GLY A 733 ? 0.3282 0.2786 0.3165 -0.0238 0.0320 0.0477 726 GLY A CA 5779 C C . GLY A 733 ? 0.3079 0.2652 0.2971 -0.0221 0.0266 0.0408 726 GLY A C 5780 O O . GLY A 733 ? 0.3070 0.2650 0.3018 -0.0210 0.0202 0.0371 726 GLY A O 5781 N N . GLU A 734 ? 0.3070 0.2690 0.2902 -0.0215 0.0293 0.0391 727 GLU A N 5782 C CA . GLU A 734 ? 0.2962 0.2644 0.2796 -0.0198 0.0247 0.0331 727 GLU A CA 5783 C C . GLU A 734 ? 0.2787 0.2514 0.2777 -0.0214 0.0237 0.0288 727 GLU A C 5784 O O . GLU A 734 ? 0.2635 0.2390 0.2654 -0.0198 0.0180 0.0242 727 GLU A O 5785 C CB . GLU A 734 ? 0.3034 0.2747 0.2763 -0.0187 0.0278 0.0325 727 GLU A CB 5786 C CG A GLU A 734 ? 0.3152 0.2925 0.2887 -0.0172 0.0239 0.0267 727 GLU A CG 5787 C CD A GLU A 734 ? 0.3458 0.3227 0.3151 -0.0146 0.0166 0.0246 727 GLU A CD 5788 O OE1 A GLU A 734 ? 0.3446 0.3168 0.3086 -0.0135 0.0143 0.0275 727 GLU A OE1 5789 O OE2 A GLU A 734 ? 0.3423 0.3236 0.3140 -0.0135 0.0136 0.0202 727 GLU A OE2 5790 N N . VAL A 735 ? 0.2787 0.2519 0.2879 -0.0244 0.0290 0.0303 728 VAL A N 5791 C CA . VAL A 735 ? 0.2668 0.2436 0.2924 -0.0259 0.0271 0.0263 728 VAL A CA 5792 C C . VAL A 735 ? 0.2652 0.2386 0.2959 -0.0251 0.0201 0.0246 728 VAL A C 5793 O O . VAL A 735 ? 0.2559 0.2323 0.2916 -0.0238 0.0146 0.0196 728 VAL A O 5794 C CB . VAL A 735 ? 0.2854 0.2630 0.3236 -0.0295 0.0339 0.0286 728 VAL A CB 5795 C CG1 . VAL A 735 ? 0.2805 0.2612 0.3370 -0.0309 0.0301 0.0242 728 VAL A CG1 5796 C CG2 . VAL A 735 ? 0.2716 0.2533 0.3053 -0.0297 0.0411 0.0294 728 VAL A CG2 5797 N N A LYS A 736 ? 0.2622 0.2291 0.2911 -0.0258 0.0205 0.0290 729 LYS A N 5798 N N B LYS A 736 ? 0.2673 0.2341 0.2961 -0.0257 0.0205 0.0290 729 LYS A N 5799 C CA A LYS A 736 ? 0.2606 0.2235 0.2943 -0.0249 0.0141 0.0273 729 LYS A CA 5800 C CA B LYS A 736 ? 0.2656 0.2283 0.2990 -0.0249 0.0143 0.0276 729 LYS A CA 5801 C C A LYS A 736 ? 0.2628 0.2269 0.2875 -0.0210 0.0077 0.0237 729 LYS A C 5802 C C B LYS A 736 ? 0.2618 0.2253 0.2863 -0.0210 0.0077 0.0241 729 LYS A C 5803 O O A LYS A 736 ? 0.2469 0.2114 0.2770 -0.0196 0.0020 0.0193 729 LYS A O 5804 O O B LYS A 736 ? 0.2510 0.2140 0.2808 -0.0196 0.0019 0.0202 729 LYS A O 5805 C CB A LYS A 736 ? 0.2707 0.2258 0.3037 -0.0261 0.0159 0.0329 729 LYS A CB 5806 C CB B LYS A 736 ? 0.2776 0.2324 0.3098 -0.0262 0.0166 0.0335 729 LYS A CB 5807 C CG A LYS A 736 ? 0.2730 0.2267 0.3186 -0.0303 0.0222 0.0362 729 LYS A CG 5808 C CG B LYS A 736 ? 0.2851 0.2384 0.3304 -0.0303 0.0224 0.0366 729 LYS A CG 5809 C CD A LYS A 736 ? 0.3052 0.2504 0.3485 -0.0314 0.0253 0.0431 729 LYS A CD 5810 C CD B LYS A 736 ? 0.3054 0.2501 0.3491 -0.0314 0.0248 0.0430 729 LYS A CD 5811 C CE A LYS A 736 ? 0.3219 0.2613 0.3697 -0.0306 0.0190 0.0421 729 LYS A CE 5812 C CE B LYS A 736 ? 0.3344 0.2767 0.3633 -0.0309 0.0315 0.0494 729 LYS A CE 5813 N NZ A LYS A 736 ? 0.3549 0.2855 0.4031 -0.0324 0.0228 0.0492 729 LYS A NZ 5814 N NZ B LYS A 736 ? 0.3468 0.2799 0.3731 -0.0317 0.0342 0.0564 729 LYS A NZ 5815 N N . ARG A 737 ? 0.2537 0.2183 0.2648 -0.0191 0.0087 0.0255 730 ARG A N 5816 C CA . ARG A 737 ? 0.2522 0.2185 0.2561 -0.0157 0.0034 0.0224 730 ARG A CA 5817 C C . ARG A 737 ? 0.2464 0.2186 0.2555 -0.0148 0.0009 0.0167 730 ARG A C 5818 O O . ARG A 737 ? 0.2332 0.2056 0.2431 -0.0124 -0.0042 0.0132 730 ARG A O 5819 C CB . ARG A 737 ? 0.2607 0.2273 0.2507 -0.0141 0.0047 0.0247 730 ARG A CB 5820 C CG . ARG A 737 ? 0.2841 0.2519 0.2687 -0.0106 -0.0010 0.0220 730 ARG A CG 5821 C CD . ARG A 737 ? 0.3016 0.2696 0.2739 -0.0092 -0.0002 0.0241 730 ARG A CD 5822 N NE . ARG A 737 ? 0.3031 0.2764 0.2726 -0.0094 0.0019 0.0219 730 ARG A NE 5823 C CZ . ARG A 737 ? 0.3330 0.3108 0.3026 -0.0078 -0.0007 0.0179 730 ARG A CZ 5824 N NH1 . ARG A 737 ? 0.3744 0.3525 0.3471 -0.0058 -0.0052 0.0156 730 ARG A NH1 5825 N NH2 . ARG A 737 ? 0.3591 0.3409 0.3261 -0.0081 0.0015 0.0163 730 ARG A NH2 5826 N N . GLN A 738 ? 0.2368 0.2134 0.2493 -0.0164 0.0047 0.0158 731 GLN A N 5827 C CA . GLN A 738 ? 0.2241 0.2060 0.2410 -0.0153 0.0024 0.0107 731 GLN A CA 5828 C C . GLN A 738 ? 0.2402 0.2217 0.2693 -0.0156 -0.0014 0.0074 731 GLN A C 5829 O O . GLN A 738 ? 0.2345 0.2181 0.2644 -0.0132 -0.0059 0.0031 731 GLN A O 5830 C CB . GLN A 738 ? 0.2330 0.2196 0.2507 -0.0168 0.0075 0.0106 731 GLN A CB 5831 C CG . GLN A 738 ? 0.2242 0.2112 0.2288 -0.0158 0.0101 0.0126 731 GLN A CG 5832 C CD . GLN A 738 ? 0.2582 0.2469 0.2561 -0.0128 0.0056 0.0099 731 GLN A CD 5833 O OE1 . GLN A 738 ? 0.2531 0.2443 0.2556 -0.0114 0.0022 0.0061 731 GLN A OE1 5834 N NE2 . GLN A 738 ? 0.2926 0.2800 0.2799 -0.0116 0.0055 0.0118 731 GLN A NE2 5835 N N . ILE A 739 ? 0.2402 0.2186 0.2783 -0.0183 0.0001 0.0094 732 ILE A N 5836 C CA . ILE A 739 ? 0.2366 0.2138 0.2866 -0.0185 -0.0047 0.0058 732 ILE A CA 5837 C C . ILE A 739 ? 0.2478 0.2213 0.2925 -0.0151 -0.0110 0.0036 732 ILE A C 5838 O O . ILE A 739 ? 0.2490 0.2235 0.2970 -0.0129 -0.0162 -0.0013 732 ILE A O 5839 C CB . ILE A 739 ? 0.2386 0.2125 0.3001 -0.0222 -0.0018 0.0086 732 ILE A CB 5840 C CG1 . ILE A 739 ? 0.2267 0.2052 0.2959 -0.0252 0.0044 0.0097 732 ILE A CG1 5841 C CG2 . ILE A 739 ? 0.2505 0.2221 0.3243 -0.0221 -0.0082 0.0043 732 ILE A CG2 5842 C CD1 . ILE A 739 ? 0.2507 0.2259 0.3306 -0.0294 0.0096 0.0142 732 ILE A CD1 5843 N N . TYR A 740 ? 0.2445 0.2136 0.2811 -0.0144 -0.0105 0.0072 733 TYR A N 5844 C CA . TYR A 740 ? 0.2536 0.2192 0.2847 -0.0110 -0.0157 0.0056 733 TYR A CA 5845 C C . TYR A 740 ? 0.2447 0.2145 0.2688 -0.0074 -0.0182 0.0021 733 TYR A C 5846 O O . TYR A 740 ? 0.2438 0.2126 0.2687 -0.0046 -0.0231 -0.0019 733 TYR A O 5847 C CB . TYR A 740 ? 0.2551 0.2166 0.2782 -0.0109 -0.0138 0.0107 733 TYR A CB 5848 C CG . TYR A 740 ? 0.2672 0.2265 0.2817 -0.0070 -0.0176 0.0102 733 TYR A CG 5849 C CD1 . TYR A 740 ? 0.2977 0.2540 0.3150 -0.0045 -0.0228 0.0067 733 TYR A CD1 5850 C CD2 . TYR A 740 ? 0.2956 0.2556 0.2995 -0.0058 -0.0160 0.0134 733 TYR A CD2 5851 C CE1 . TYR A 740 ? 0.2667 0.2211 0.2770 -0.0008 -0.0256 0.0066 733 TYR A CE1 5852 C CE2 . TYR A 740 ? 0.2770 0.2354 0.2749 -0.0025 -0.0192 0.0132 733 TYR A CE2 5853 C CZ . TYR A 740 ? 0.2820 0.2375 0.2833 0.0000 -0.0236 0.0100 733 TYR A CZ 5854 O OH . TYR A 740 ? 0.3155 0.2695 0.3116 0.0036 -0.0264 0.0099 733 TYR A OH 5855 N N . VAL A 741 ? 0.2374 0.2113 0.2547 -0.0074 -0.0149 0.0034 734 VAL A N 5856 C CA . VAL A 741 ? 0.2266 0.2042 0.2379 -0.0042 -0.0169 0.0005 734 VAL A CA 5857 C C . VAL A 741 ? 0.2321 0.2122 0.2496 -0.0032 -0.0195 -0.0042 734 VAL A C 5858 O O . VAL A 741 ? 0.2355 0.2156 0.2502 0.0003 -0.0233 -0.0074 734 VAL A O 5859 C CB . VAL A 741 ? 0.2207 0.2021 0.2250 -0.0048 -0.0129 0.0025 734 VAL A CB 5860 C CG1 . VAL A 741 ? 0.2351 0.2206 0.2359 -0.0021 -0.0143 -0.0006 734 VAL A CG1 5861 C CG2 . VAL A 741 ? 0.2547 0.2334 0.2511 -0.0046 -0.0120 0.0064 734 VAL A CG2 5862 N N . ALA A 742 ? 0.2244 0.2066 0.2505 -0.0060 -0.0177 -0.0046 735 ALA A N 5863 C CA . ALA A 742 ? 0.2208 0.2056 0.2534 -0.0049 -0.0207 -0.0092 735 ALA A CA 5864 C C . ALA A 742 ? 0.2163 0.1971 0.2537 -0.0031 -0.0266 -0.0126 735 ALA A C 5865 O O . ALA A 742 ? 0.2163 0.1976 0.2519 0.0004 -0.0309 -0.0166 735 ALA A O 5866 C CB . ALA A 742 ? 0.2212 0.2094 0.2637 -0.0083 -0.0173 -0.0088 735 ALA A CB 5867 N N . ALA A 743 ? 0.2089 0.1854 0.2520 -0.0053 -0.0269 -0.0111 736 ALA A N 5868 C CA . ALA A 743 ? 0.2201 0.1921 0.2683 -0.0036 -0.0329 -0.0148 736 ALA A CA 5869 C C . ALA A 743 ? 0.2379 0.2074 0.2753 0.0012 -0.0364 -0.0165 736 ALA A C 5870 O O . ALA A 743 ? 0.2412 0.2093 0.2781 0.0047 -0.0416 -0.0212 736 ALA A O 5871 C CB . ALA A 743 ? 0.2346 0.2017 0.2904 -0.0068 -0.0321 -0.0122 736 ALA A CB 5872 N N . PHE A 744 ? 0.2322 0.2010 0.2609 0.0016 -0.0334 -0.0127 737 PHE A N 5873 C CA . PHE A 744 ? 0.2387 0.2057 0.2582 0.0061 -0.0357 -0.0139 737 PHE A CA 5874 C C . PHE A 744 ? 0.2296 0.2003 0.2438 0.0095 -0.0368 -0.0169 737 PHE A C 5875 O O . PHE A 744 ? 0.2345 0.2031 0.2450 0.0136 -0.0406 -0.0204 737 PHE A O 5876 C CB . PHE A 744 ? 0.2433 0.2101 0.2556 0.0058 -0.0323 -0.0092 737 PHE A CB 5877 C CG . PHE A 744 ? 0.2511 0.2184 0.2550 0.0102 -0.0335 -0.0103 737 PHE A CG 5878 C CD1 . PHE A 744 ? 0.2633 0.2262 0.2660 0.0138 -0.0375 -0.0130 737 PHE A CD1 5879 C CD2 . PHE A 744 ? 0.2534 0.2255 0.2514 0.0109 -0.0308 -0.0092 737 PHE A CD2 5880 C CE1 . PHE A 744 ? 0.2786 0.2423 0.2738 0.0182 -0.0379 -0.0141 737 PHE A CE1 5881 C CE2 . PHE A 744 ? 0.2482 0.2210 0.2394 0.0151 -0.0314 -0.0101 737 PHE A CE2 5882 C CZ . PHE A 744 ? 0.2530 0.2217 0.2431 0.0187 -0.0346 -0.0124 737 PHE A CZ 5883 N N . THR A 745 ? 0.2114 0.1871 0.2249 0.0079 -0.0334 -0.0156 738 THR A N 5884 C CA . THR A 745 ? 0.2069 0.1857 0.2148 0.0111 -0.0338 -0.0177 738 THR A CA 5885 C C . THR A 745 ? 0.2308 0.2087 0.2424 0.0134 -0.0386 -0.0225 738 THR A C 5886 O O . THR A 745 ? 0.2367 0.2137 0.2418 0.0179 -0.0410 -0.0250 738 THR A O 5887 C CB . THR A 745 ? 0.2100 0.1939 0.2173 0.0088 -0.0293 -0.0155 738 THR A CB 5888 O OG1 . THR A 745 ? 0.2161 0.2003 0.2192 0.0072 -0.0257 -0.0115 738 THR A OG1 5889 C CG2 . THR A 745 ? 0.2294 0.2157 0.2308 0.0122 -0.0295 -0.0171 738 THR A CG2 5890 N N . VAL A 746 ? 0.2242 0.2021 0.2462 0.0105 -0.0400 -0.0237 739 VAL A N 5891 C CA . VAL A 746 ? 0.2288 0.2060 0.2557 0.0127 -0.0457 -0.0289 739 VAL A CA 5892 C C . VAL A 746 ? 0.2366 0.2080 0.2599 0.0165 -0.0510 -0.0322 739 VAL A C 5893 O O . VAL A 746 ? 0.2362 0.2064 0.2543 0.0211 -0.0551 -0.0360 739 VAL A O 5894 C CB . VAL A 746 ? 0.2317 0.2105 0.2729 0.0084 -0.0461 -0.0297 739 VAL A CB 5895 C CG1 . VAL A 746 ? 0.2509 0.2283 0.2988 0.0107 -0.0534 -0.0356 739 VAL A CG1 5896 C CG2 . VAL A 746 ? 0.2201 0.2047 0.2637 0.0059 -0.0411 -0.0273 739 VAL A CG2 5897 N N . GLN A 747 ? 0.2365 0.2041 0.2619 0.0150 -0.0508 -0.0307 740 GLN A N 5898 C CA . GLN A 747 ? 0.2469 0.2086 0.2685 0.0188 -0.0556 -0.0340 740 GLN A CA 5899 C C . GLN A 747 ? 0.2443 0.2057 0.2525 0.0241 -0.0548 -0.0341 740 GLN A C 5900 O O . GLN A 747 ? 0.2500 0.2081 0.2526 0.0291 -0.0591 -0.0382 740 GLN A O 5901 C CB . GLN A 747 ? 0.2554 0.2129 0.2812 0.0163 -0.0548 -0.0315 740 GLN A CB 5902 C CG . GLN A 747 ? 0.2649 0.2160 0.2877 0.0204 -0.0598 -0.0353 740 GLN A CG 5903 C CD . GLN A 747 ? 0.3038 0.2517 0.3342 0.0213 -0.0666 -0.0413 740 GLN A CD 5904 O OE1 . GLN A 747 ? 0.2956 0.2454 0.3373 0.0176 -0.0676 -0.0420 740 GLN A OE1 5905 N NE2 . GLN A 747 ? 0.2990 0.2418 0.3233 0.0265 -0.0716 -0.0459 740 GLN A NE2 5906 N N . ALA A 748 ? 0.2394 0.2041 0.2423 0.0232 -0.0493 -0.0296 741 ALA A N 5907 C CA . ALA A 748 ? 0.2393 0.2042 0.2314 0.0277 -0.0479 -0.0292 741 ALA A CA 5908 C C . ALA A 748 ? 0.2425 0.2089 0.2293 0.0313 -0.0492 -0.0318 741 ALA A C 5909 O O . ALA A 748 ? 0.2558 0.2197 0.2343 0.0366 -0.0507 -0.0340 741 ALA A O 5910 C CB . ALA A 748 ? 0.2331 0.2017 0.2225 0.0254 -0.0421 -0.0241 741 ALA A CB 5911 N N . ALA A 749 ? 0.2383 0.2086 0.2296 0.0288 -0.0484 -0.0316 742 ALA A N 5912 C CA . ALA A 749 ? 0.2408 0.2120 0.2273 0.0324 -0.0501 -0.0339 742 ALA A CA 5913 C C . ALA A 749 ? 0.2664 0.2330 0.2522 0.0364 -0.0571 -0.0394 742 ALA A C 5914 O O . ALA A 749 ? 0.2612 0.2256 0.2373 0.0420 -0.0588 -0.0415 742 ALA A O 5915 C CB . ALA A 749 ? 0.2370 0.2131 0.2302 0.0289 -0.0485 -0.0330 742 ALA A CB 5916 N N . ALA A 750 ? 0.2603 0.2251 0.2562 0.0337 -0.0609 -0.0418 743 ALA A N 5917 C CA . ALA A 750 ? 0.2784 0.2382 0.2747 0.0374 -0.0685 -0.0477 743 ALA A CA 5918 C C . ALA A 750 ? 0.2841 0.2389 0.2688 0.0430 -0.0696 -0.0493 743 ALA A C 5919 O O . ALA A 750 ? 0.2840 0.2353 0.2606 0.0487 -0.0740 -0.0535 743 ALA A O 5920 C CB . ALA A 750 ? 0.2735 0.2317 0.2837 0.0331 -0.0718 -0.0495 743 ALA A CB 5921 N N . GLU A 751 ? 0.2679 0.2219 0.2512 0.0417 -0.0656 -0.0460 744 GLU A N 5922 C CA . GLU A 751 ? 0.2834 0.2325 0.2576 0.0469 -0.0665 -0.0477 744 GLU A CA 5923 C C . GLU A 751 ? 0.2798 0.2296 0.2407 0.0523 -0.0637 -0.0470 744 GLU A C 5924 O O . GLU A 751 ? 0.2952 0.2405 0.2473 0.0580 -0.0652 -0.0497 744 GLU A O 5925 C CB . GLU A 751 ? 0.2815 0.2297 0.2589 0.0442 -0.0633 -0.0443 744 GLU A CB 5926 C CG . GLU A 751 ? 0.3076 0.2525 0.2965 0.0404 -0.0673 -0.0461 744 GLU A CG 5927 C CD . GLU A 751 ? 0.3608 0.3038 0.3531 0.0378 -0.0647 -0.0426 744 GLU A CD 5928 O OE1 . GLU A 751 ? 0.3777 0.3228 0.3643 0.0385 -0.0599 -0.0387 744 GLU A OE1 5929 O OE2 . GLU A 751 ? 0.3613 0.3005 0.3626 0.0351 -0.0676 -0.0437 744 GLU A OE2 5930 N N . THR A 752 ? 0.2800 0.2349 0.2396 0.0509 -0.0594 -0.0436 745 THR A N 5931 C CA . THR A 752 ? 0.2797 0.2348 0.2272 0.0561 -0.0566 -0.0428 745 THR A CA 5932 C C . THR A 752 ? 0.2928 0.2438 0.2330 0.0619 -0.0623 -0.0477 745 THR A C 5933 O O . THR A 752 ? 0.3044 0.2535 0.2327 0.0676 -0.0607 -0.0477 745 THR A O 5934 C CB . THR A 752 ? 0.2687 0.2297 0.2167 0.0534 -0.0509 -0.0381 745 THR A CB 5935 O OG1 . THR A 752 ? 0.2724 0.2353 0.2249 0.0517 -0.0536 -0.0394 745 THR A OG1 5936 C CG2 . THR A 752 ? 0.2724 0.2374 0.2275 0.0477 -0.0461 -0.0336 745 THR A CG2 5937 N N . LEU A 753 ? 0.2871 0.2368 0.2348 0.0604 -0.0689 -0.0518 746 LEU A N 5938 C CA . LEU A 753 ? 0.2976 0.2433 0.2394 0.0658 -0.0758 -0.0573 746 LEU A CA 5939 C C . LEU A 753 ? 0.3192 0.2581 0.2580 0.0697 -0.0818 -0.0629 746 LEU A C 5940 O O . LEU A 753 ? 0.3323 0.2667 0.2640 0.0753 -0.0882 -0.0680 746 LEU A O 5941 C CB . LEU A 753 ? 0.2880 0.2366 0.2407 0.0624 -0.0801 -0.0591 746 LEU A CB 5942 C CG . LEU A 753 ? 0.3020 0.2569 0.2579 0.0590 -0.0749 -0.0544 746 LEU A CG 5943 C CD1 . LEU A 753 ? 0.3168 0.2745 0.2853 0.0557 -0.0796 -0.0569 746 LEU A CD1 5944 C CD2 . LEU A 753 ? 0.3365 0.2909 0.2783 0.0644 -0.0721 -0.0526 746 LEU A CD2 5945 N N . SER A 754 ? 0.3130 0.2507 0.2573 0.0670 -0.0805 -0.0622 747 SER A N 5946 C CA . SER A 754 ? 0.3264 0.2570 0.2671 0.0712 -0.0855 -0.0673 747 SER A CA 5947 C C . SER A 754 ? 0.3457 0.2724 0.2687 0.0794 -0.0838 -0.0684 747 SER A C 5948 O O . SER A 754 ? 0.3483 0.2780 0.2635 0.0809 -0.0771 -0.0638 747 SER A O 5949 C CB . SER A 754 ? 0.3344 0.2646 0.2837 0.0668 -0.0832 -0.0652 747 SER A CB 5950 O OG . SER A 754 ? 0.3650 0.2977 0.3300 0.0598 -0.0848 -0.0645 747 SER A OG 5951 N N . GLU A 755 ? 0.3571 0.2767 0.2738 0.0849 -0.0896 -0.0744 748 GLU A N 5952 C CA . GLU A 755 ? 0.3933 0.3088 0.2935 0.0927 -0.0867 -0.0751 748 GLU A CA 5953 C C . GLU A 755 ? 0.3770 0.2959 0.2774 0.0909 -0.0775 -0.0690 748 GLU A C 5954 O O . GLU A 755 ? 0.3685 0.2893 0.2803 0.0855 -0.0762 -0.0670 748 GLU A O 5955 C CB . GLU A 755 ? 0.4219 0.3290 0.3167 0.0983 -0.0940 -0.0827 748 GLU A CB 5956 C CG . GLU A 755 ? 0.4798 0.3837 0.3722 0.1012 -0.1033 -0.0888 748 GLU A CG 5957 C CD . GLU A 755 ? 0.6119 0.5068 0.4950 0.1084 -0.1109 -0.0969 748 GLU A CD 5958 O OE1 . GLU A 755 ? 0.6519 0.5435 0.5451 0.1062 -0.1166 -0.1014 748 GLU A OE1 5959 O OE2 . GLU A 755 ? 0.6602 0.5512 0.5256 0.1164 -0.1112 -0.0988 748 GLU A OE2 5960 N N . VAL A 756 ? 0.3795 0.2994 0.2678 0.0955 -0.0713 -0.0659 749 VAL A N 5961 C CA . VAL A 756 ? 0.3807 0.3055 0.2709 0.0933 -0.0623 -0.0596 749 VAL A CA 5962 C C . VAL A 756 ? 0.3933 0.3151 0.2834 0.0955 -0.0608 -0.0606 749 VAL A C 5963 O O . VAL A 756 ? 0.3821 0.3081 0.2781 0.0924 -0.0551 -0.0560 749 VAL A O 5964 C CB . VAL A 756 ? 0.3832 0.3105 0.2631 0.0967 -0.0553 -0.0554 749 VAL A CB 5965 C CG1 . VAL A 756 ? 0.3774 0.3077 0.2589 0.0941 -0.0568 -0.0541 749 VAL A CG1 5966 C CG2 . VAL A 756 ? 0.3879 0.3088 0.2506 0.1064 -0.0548 -0.0585 749 VAL A CG2 5967 N N . ALA A 757 ? 0.4028 0.3172 0.2862 0.1011 -0.0663 -0.0669 750 ALA A N 5968 C CA . ALA A 757 ? 0.4345 0.3449 0.3165 0.1044 -0.0655 -0.0689 750 ALA A CA 5969 C C . ALA A 757 ? 0.4657 0.3675 0.3419 0.1096 -0.0739 -0.0770 750 ALA A C 5970 O O . ALA A 757 ? 0.5137 0.4108 0.3895 0.1124 -0.0749 -0.0800 750 ALA A O 5971 C CB . ALA A 757 ? 0.4264 0.3378 0.2978 0.1100 -0.0572 -0.0659 750 ALA A CB 5972 O OXT . ALA A 757 ? 0.4793 0.3785 0.3508 0.1115 -0.0798 -0.0810 750 ALA A OXT 5973 ZN ZN . ZN B . ? 0.2381 0.2441 0.2716 0.0201 0.0157 -0.0309 801 ZN A ZN 5974 ZN ZN . ZN C . ? 0.2567 0.2575 0.2824 0.0257 0.0093 -0.0231 802 ZN A ZN 5975 CA CA . CA D . ? 0.2044 0.2210 0.2165 0.0000 0.0041 -0.0132 803 CA A CA 5976 CL CL . CL E . ? 0.2914 0.2942 0.3062 0.0398 -0.0142 -0.0211 804 CL A CL 5977 C C1 . NAG F . ? 0.4652 0.3535 0.4756 0.0650 0.0416 0.0434 805 NAG A C1 5978 C C2 . NAG F . ? 0.5225 0.4043 0.5441 0.0630 0.0448 0.0443 805 NAG A C2 5979 C C3 . NAG F . ? 0.5396 0.4167 0.5651 0.0597 0.0522 0.0500 805 NAG A C3 5980 C C4 . NAG F . ? 0.5310 0.4031 0.5437 0.0643 0.0561 0.0586 805 NAG A C4 5981 C C5 . NAG F . ? 0.5176 0.3967 0.5184 0.0668 0.0518 0.0564 805 NAG A C5 5982 C C6 . NAG F . ? 0.5433 0.4169 0.5286 0.0727 0.0547 0.0642 805 NAG A C6 5983 C C7 . NAG F . ? 0.5968 0.4838 0.6339 0.0601 0.0386 0.0321 805 NAG A C7 5984 C C8 . NAG F . ? 0.5858 0.4793 0.6334 0.0550 0.0367 0.0234 805 NAG A C8 5985 N N2 . NAG F . ? 0.5579 0.4460 0.5909 0.0580 0.0422 0.0359 805 NAG A N2 5986 O O3 . NAG F . ? 0.5474 0.4167 0.5823 0.0590 0.0548 0.0516 805 NAG A O3 5987 O O4 . NAG F . ? 0.5519 0.4231 0.5704 0.0599 0.0629 0.0622 805 NAG A O4 5988 O O5 . NAG F . ? 0.4760 0.3580 0.4743 0.0699 0.0445 0.0513 805 NAG A O5 5989 O O6 . NAG F . ? 0.5926 0.4561 0.5718 0.0790 0.0547 0.0695 805 NAG A O6 5990 O O7 . NAG F . ? 0.6423 0.5234 0.6746 0.0661 0.0369 0.0353 805 NAG A O7 5991 C C1 . NAG G . ? 0.6111 0.4714 0.6268 0.0631 0.0694 0.0715 806 NAG A C1 5992 C C2 . NAG G . ? 0.6288 0.4901 0.6471 0.0596 0.0768 0.0760 806 NAG A C2 5993 C C3 . NAG G . ? 0.6754 0.5253 0.6938 0.0618 0.0852 0.0861 806 NAG A C3 5994 C C4 . NAG G . ? 0.6983 0.5401 0.7271 0.0612 0.0856 0.0868 806 NAG A C4 5995 C C5 . NAG G . ? 0.6969 0.5387 0.7206 0.0652 0.0773 0.0816 806 NAG A C5 5996 C C6 . NAG G . ? 0.7133 0.5477 0.7480 0.0646 0.0771 0.0811 806 NAG A C6 5997 C C7 . NAG G . ? 0.6079 0.4852 0.6162 0.0578 0.0736 0.0708 806 NAG A C7 5998 C C8 . NAG G . ? 0.5504 0.4345 0.5747 0.0503 0.0713 0.0631 806 NAG A C8 5999 N N2 . NAG G . ? 0.6006 0.4674 0.6064 0.0619 0.0761 0.0765 806 NAG A N2 6000 O O3 . NAG G . ? 0.6854 0.5382 0.7125 0.0567 0.0918 0.0883 806 NAG A O3 6001 O O4 . NAG G . ? 0.7473 0.5772 0.7732 0.0645 0.0932 0.0971 806 NAG A O4 6002 O O5 . NAG G . ? 0.6467 0.5003 0.6735 0.0617 0.0708 0.0719 806 NAG A O5 6003 O O6 . NAG G . ? 0.7169 0.5571 0.7683 0.0570 0.0760 0.0736 806 NAG A O6 6004 O O7 . NAG G . ? 0.6109 0.4918 0.6082 0.0602 0.0732 0.0715 806 NAG A O7 6005 C C1 . NAG H . ? 0.6018 0.5494 0.6234 -0.0020 -0.0208 -0.1247 807 NAG A C1 6006 C C2 . NAG H . ? 0.6313 0.5814 0.6561 -0.0047 -0.0272 -0.1245 807 NAG A C2 6007 C C3 . NAG H . ? 0.6794 0.6248 0.7126 -0.0061 -0.0347 -0.1325 807 NAG A C3 6008 C C4 . NAG H . ? 0.7136 0.6526 0.7385 -0.0031 -0.0363 -0.1419 807 NAG A C4 6009 C C5 . NAG H . ? 0.7155 0.6526 0.7398 -0.0009 -0.0285 -0.1400 807 NAG A C5 6010 C C6 . NAG H . ? 0.7623 0.6923 0.7813 0.0021 -0.0294 -0.1493 807 NAG A C6 6011 C C7 . NAG H . ? 0.6521 0.6122 0.6830 -0.0078 -0.0243 -0.1104 807 NAG A C7 6012 C C8 . NAG H . ? 0.6510 0.6127 0.6649 -0.0058 -0.0270 -0.1132 807 NAG A C8 6013 N N2 . NAG H . ? 0.6306 0.5850 0.6664 -0.0073 -0.0245 -0.1159 807 NAG A N2 6014 O O3 . NAG H . ? 0.6867 0.6350 0.7167 -0.0071 -0.0410 -0.1336 807 NAG A O3 6015 O O4 . NAG H . ? 0.7465 0.6805 0.7828 -0.0048 -0.0429 -0.1490 807 NAG A O4 6016 O O5 . NAG H . ? 0.6715 0.6138 0.6852 0.0007 -0.0225 -0.1334 807 NAG A O5 6017 O O6 . NAG H . ? 0.8245 0.7546 0.8244 0.0062 -0.0270 -0.1523 807 NAG A O6 6018 O O7 . NAG H . ? 0.6865 0.6500 0.7258 -0.0096 -0.0219 -0.1034 807 NAG A O7 6019 C C1 . NAG I . ? 0.5865 0.5240 0.5195 0.0500 0.0574 -0.1645 808 NAG A C1 6020 C C2 . NAG I . ? 0.6209 0.5524 0.5520 0.0550 0.0601 -0.1736 808 NAG A C2 6021 C C3 . NAG I . ? 0.6473 0.5708 0.5616 0.0569 0.0551 -0.1823 808 NAG A C3 6022 C C4 . NAG I . ? 0.6550 0.5751 0.5712 0.0526 0.0442 -0.1827 808 NAG A C4 6023 C C5 . NAG I . ? 0.6044 0.5316 0.5257 0.0475 0.0425 -0.1725 808 NAG A C5 6024 C C6 . NAG I . ? 0.5849 0.5095 0.5133 0.0430 0.0325 -0.1721 808 NAG A C6 6025 C C7 . NAG I . ? 0.6758 0.6144 0.6189 0.0604 0.0752 -0.1720 808 NAG A C7 6026 C C8 . NAG I . ? 0.6797 0.6231 0.6205 0.0645 0.0862 -0.1718 808 NAG A C8 6027 N N2 . NAG I . ? 0.6430 0.5786 0.5711 0.0589 0.0704 -0.1732 808 NAG A N2 6028 O O3 . NAG I . ? 0.6503 0.5675 0.5649 0.0614 0.0565 -0.1912 808 NAG A O3 6029 O O4 . NAG I . ? 0.7327 0.6473 0.6302 0.0548 0.0404 -0.1896 808 NAG A O4 6030 O O5 . NAG I . ? 0.5888 0.5224 0.5245 0.0464 0.0478 -0.1653 808 NAG A O5 6031 O O6 . NAG I . ? 0.5724 0.4933 0.5174 0.0420 0.0295 -0.1742 808 NAG A O6 6032 O O7 . NAG I . ? 0.6912 0.6288 0.6499 0.0588 0.0711 -0.1708 808 NAG A O7 6033 C C1 . NAG J . ? 0.7829 0.6897 0.6840 0.0541 0.0312 -0.1973 809 NAG A C1 6034 C C2 . NAG J . ? 0.8082 0.7113 0.6910 0.0546 0.0246 -0.2017 809 NAG A C2 6035 C C3 . NAG J . ? 0.8546 0.7492 0.7403 0.0542 0.0144 -0.2110 809 NAG A C3 6036 C C4 . NAG J . ? 0.8746 0.7628 0.7644 0.0582 0.0167 -0.2194 809 NAG A C4 6037 C C5 . NAG J . ? 0.8572 0.7498 0.7658 0.0572 0.0237 -0.2133 809 NAG A C5 6038 C C6 . NAG J . ? 0.8727 0.7591 0.7874 0.0612 0.0261 -0.2210 809 NAG A C6 6039 C C7 . NAG J . ? 0.7861 0.6997 0.6541 0.0515 0.0276 -0.1882 809 NAG A C7 6040 C C8 . NAG J . ? 0.7529 0.6719 0.6220 0.0470 0.0242 -0.1798 809 NAG A C8 6041 N N2 . NAG J . ? 0.7859 0.6950 0.6678 0.0504 0.0222 -0.1932 809 NAG A N2 6042 O O3 . NAG J . ? 0.8827 0.7734 0.7490 0.0561 0.0088 -0.2164 809 NAG A O3 6043 O O4 . NAG J . ? 0.9183 0.7984 0.8128 0.0574 0.0069 -0.2280 809 NAG A O4 6044 O O5 . NAG J . ? 0.8197 0.7204 0.7237 0.0580 0.0329 -0.2055 809 NAG A O5 6045 O O6 . NAG J . ? 0.8897 0.7768 0.7907 0.0669 0.0349 -0.2237 809 NAG A O6 6046 O O7 . NAG J . ? 0.7852 0.6984 0.6402 0.0561 0.0353 -0.1899 809 NAG A O7 6047 C C1 . NAG K . ? 0.9249 0.8813 0.6685 0.0294 0.1297 -0.0110 810 NAG A C1 6048 C C2 . NAG K . ? 1.0022 0.9535 0.7356 0.0291 0.1311 -0.0023 810 NAG A C2 6049 C C3 . NAG K . ? 1.0191 0.9648 0.7367 0.0310 0.1185 -0.0040 810 NAG A C3 6050 C C4 . NAG K . ? 1.0410 0.9804 0.7349 0.0369 0.1169 -0.0101 810 NAG A C4 6051 C C5 . NAG K . ? 1.0169 0.9605 0.7191 0.0375 0.1171 -0.0189 810 NAG A C5 6052 C C6 . NAG K . ? 1.0464 0.9829 0.7234 0.0439 0.1208 -0.0232 810 NAG A C6 6053 C C7 . NAG K . ? 1.0201 0.9783 0.7835 0.0220 0.1446 0.0100 810 NAG A C7 6054 C C8 . NAG K . ? 1.0034 0.9667 0.7893 0.0165 0.1433 0.0148 810 NAG A C8 6055 N N2 . NAG K . ? 1.0009 0.9573 0.7556 0.0238 0.1328 0.0038 810 NAG A N2 6056 O O3 . NAG K . ? 1.0488 0.9895 0.7573 0.0309 0.1193 0.0042 810 NAG A O3 6057 O O4 . NAG K . ? 1.0639 0.9985 0.7446 0.0387 0.1044 -0.0122 810 NAG A O4 6058 O O5 . NAG K . ? 0.9763 0.9272 0.6996 0.0345 0.1264 -0.0177 810 NAG A O5 6059 O O6 . NAG K . ? 1.0499 0.9881 0.7299 0.0454 0.1165 -0.0329 810 NAG A O6 6060 O O7 . NAG K . ? 1.0475 1.0036 0.8023 0.0246 0.1561 0.0117 810 NAG A O7 6061 C C1 . NAG L . ? 0.4628 0.5027 0.6387 0.0853 -0.0525 -0.0555 811 NAG A C1 6062 C C2 . NAG L . ? 0.4515 0.4974 0.6354 0.0788 -0.0419 -0.0572 811 NAG A C2 6063 C C3 . NAG L . ? 0.4934 0.5475 0.6989 0.0799 -0.0400 -0.0613 811 NAG A C3 6064 C C4 . NAG L . ? 0.5132 0.5739 0.7346 0.0829 -0.0488 -0.0645 811 NAG A C4 6065 C C5 . NAG L . ? 0.5203 0.5742 0.7312 0.0891 -0.0599 -0.0628 811 NAG A C5 6066 C C6 . NAG L . ? 0.5151 0.5755 0.7414 0.0920 -0.0697 -0.0666 811 NAG A C6 6067 C C7 . NAG L . ? 0.3744 0.4134 0.5364 0.0709 -0.0288 -0.0529 811 NAG A C7 6068 C C8 . NAG L . ? 0.3463 0.3785 0.4957 0.0690 -0.0224 -0.0504 811 NAG A C8 6069 N N2 . NAG L . ? 0.4236 0.4627 0.5937 0.0768 -0.0349 -0.0542 811 NAG A N2 6070 O O3 . NAG L . ? 0.5088 0.5692 0.7213 0.0738 -0.0309 -0.0629 811 NAG A O3 6071 O O4 . NAG L . ? 0.5192 0.5870 0.7610 0.0852 -0.0478 -0.0681 811 NAG A O4 6072 O O5 . NAG L . ? 0.4764 0.5230 0.6667 0.0875 -0.0602 -0.0592 811 NAG A O5 6073 O O6 . NAG L . ? 0.5426 0.6088 0.7740 0.0864 -0.0688 -0.0681 811 NAG A O6 6074 O O7 . NAG L . ? 0.3394 0.3834 0.5045 0.0670 -0.0283 -0.0539 811 NAG A O7 6075 C C1 . NAG M . ? 0.4139 0.3646 0.3463 0.1131 -0.1471 -0.0795 812 NAG A C1 6076 C C2 . NAG M . ? 0.4260 0.3715 0.3428 0.1140 -0.1412 -0.0774 812 NAG A C2 6077 C C3 . NAG M . ? 0.4334 0.3763 0.3526 0.1148 -0.1495 -0.0845 812 NAG A C3 6078 C C4 . NAG M . ? 0.4619 0.4001 0.3756 0.1228 -0.1632 -0.0913 812 NAG A C4 6079 C C5 . NAG M . ? 0.4496 0.3938 0.3798 0.1215 -0.1684 -0.0927 812 NAG A C5 6080 C C6 . NAG M . ? 0.5174 0.4572 0.4423 0.1300 -0.1828 -0.0993 812 NAG A C6 6081 C C7 . NAG M . ? 0.5099 0.4583 0.4215 0.1065 -0.1198 -0.0656 812 NAG A C7 6082 C C8 . NAG M . ? 0.4657 0.4196 0.3865 0.0982 -0.1090 -0.0607 812 NAG A C8 6083 N N2 . NAG M . ? 0.4404 0.3911 0.3652 0.1058 -0.1295 -0.0719 812 NAG A N2 6084 O O3 . NAG M . ? 0.4727 0.4102 0.3764 0.1167 -0.1446 -0.0829 812 NAG A O3 6085 O O4 . NAG M . ? 0.5091 0.4462 0.4300 0.1219 -0.1709 -0.0984 812 NAG A O4 6086 O O5 . NAG M . ? 0.4444 0.3904 0.3706 0.1211 -0.1598 -0.0854 812 NAG A O5 6087 O O6 . NAG M . ? 0.5603 0.4907 0.4575 0.1397 -0.1836 -0.0973 812 NAG A O6 6088 O O7 . NAG M . ? 0.5994 0.5411 0.4916 0.1139 -0.1196 -0.0636 812 NAG A O7 6089 C C1 . NAG N . ? 0.5584 0.4859 0.4585 0.1315 -0.1789 -0.1029 813 NAG A C1 6090 C C2 . NAG N . ? 0.6037 0.5309 0.5166 0.1299 -0.1892 -0.1117 813 NAG A C2 6091 C C3 . NAG N . ? 0.6568 0.5737 0.5485 0.1398 -0.1984 -0.1178 813 NAG A C3 6092 C C4 . NAG N . ? 0.6523 0.5627 0.5194 0.1437 -0.1886 -0.1125 813 NAG A C4 6093 C C5 . NAG N . ? 0.6407 0.5526 0.4985 0.1442 -0.1777 -0.1032 813 NAG A C5 6094 C C6 . NAG N . ? 0.6550 0.5614 0.4914 0.1473 -0.1672 -0.0977 813 NAG A C6 6095 C C7 . NAG N . ? 0.6342 0.5761 0.5957 0.1176 -0.1955 -0.1165 813 NAG A C7 6096 C C8 . NAG N . ? 0.6097 0.5541 0.5776 0.1096 -0.1847 -0.1125 813 NAG A C8 6097 N N2 . NAG N . ? 0.6355 0.5691 0.5706 0.1270 -0.1975 -0.1160 813 NAG A N2 6098 O O3 . NAG N . ? 0.6492 0.5656 0.5536 0.1377 -0.2071 -0.1259 813 NAG A O3 6099 O O4 . NAG N . ? 0.7160 0.6164 0.5609 0.1543 -0.1969 -0.1177 813 NAG A O4 6100 O O5 . NAG N . ? 0.5631 0.4849 0.4428 0.1343 -0.1705 -0.0987 813 NAG A O5 6101 O O6 . NAG N . ? 0.6988 0.6088 0.5456 0.1399 -0.1603 -0.0966 813 NAG A O6 6102 O O7 . NAG N . ? 0.6883 0.6358 0.6691 0.1156 -0.2022 -0.1200 813 NAG A O7 6103 C C1 . NAG O . ? 0.4420 0.3770 0.5132 0.0135 -0.0801 -0.0501 814 NAG A C1 6104 C C2 . NAG O . ? 0.4485 0.3832 0.5148 0.0112 -0.0729 -0.0427 814 NAG A C2 6105 C C3 . NAG O . ? 0.5306 0.4578 0.6038 0.0096 -0.0743 -0.0421 814 NAG A C3 6106 C C4 . NAG O . ? 0.5349 0.4557 0.6040 0.0150 -0.0817 -0.0488 814 NAG A C4 6107 C C5 . NAG O . ? 0.5714 0.4931 0.6442 0.0172 -0.0886 -0.0562 814 NAG A C5 6108 C C6 . NAG O . ? 0.6057 0.5207 0.6710 0.0236 -0.0955 -0.0629 814 NAG A C6 6109 C C7 . NAG O . ? 0.4474 0.3912 0.5072 0.0066 -0.0603 -0.0320 814 NAG A C7 6110 C C8 . NAG O . ? 0.4382 0.3874 0.5023 0.0018 -0.0539 -0.0270 814 NAG A C8 6111 N N2 . NAG O . ? 0.4070 0.3475 0.4769 0.0065 -0.0661 -0.0371 814 NAG A N2 6112 O O3 . NAG O . ? 0.5234 0.4500 0.5899 0.0087 -0.0686 -0.0357 814 NAG A O3 6113 O O4 . NAG O . ? 0.6204 0.5337 0.6985 0.0133 -0.0842 -0.0494 814 NAG A O4 6114 O O5 . NAG O . ? 0.5058 0.4344 0.5712 0.0187 -0.0865 -0.0557 814 NAG A O5 6115 O O6 . NAG O . ? 0.7466 0.6602 0.8176 0.0254 -0.1036 -0.0704 814 NAG A O6 6116 O O7 . NAG O . ? 0.4221 0.3648 0.4707 0.0102 -0.0600 -0.0315 814 NAG A O7 6117 C C1 . NAG P . ? 0.6186 0.5289 0.6907 0.0134 -0.0799 -0.0441 815 NAG A C1 6118 C C2 . NAG P . ? 0.6496 0.5510 0.7217 0.0168 -0.0852 -0.0481 815 NAG A C2 6119 C C3 . NAG P . ? 0.6528 0.5502 0.7221 0.0160 -0.0810 -0.0419 815 NAG A C3 6120 C C4 . NAG P . ? 0.6509 0.5492 0.7300 0.0092 -0.0754 -0.0347 815 NAG A C4 6121 C C5 . NAG P . ? 0.6561 0.5637 0.7322 0.0069 -0.0705 -0.0316 815 NAG A C5 6122 C C6 . NAG P . ? 0.7276 0.6366 0.8115 0.0007 -0.0642 -0.0245 815 NAG A C6 6123 C C7 . NAG P . ? 0.7120 0.6093 0.7734 0.0271 -0.0967 -0.0619 815 NAG A C7 6124 C C8 . NAG P . ? 0.6960 0.5903 0.7743 0.0231 -0.1019 -0.0656 815 NAG A C8 6125 N N2 . NAG P . ? 0.6589 0.5594 0.7188 0.0238 -0.0893 -0.0539 815 NAG A N2 6126 O O3 . NAG P . ? 0.7059 0.5946 0.7770 0.0190 -0.0860 -0.0459 815 NAG A O3 6127 O O4 . NAG P . ? 0.6801 0.5752 0.7543 0.0090 -0.0714 -0.0284 815 NAG A O4 6128 O O5 . NAG P . ? 0.6312 0.5420 0.7124 0.0073 -0.0747 -0.0376 815 NAG A O5 6129 O O6 . NAG P . ? 0.8040 0.7084 0.9037 -0.0028 -0.0670 -0.0266 815 NAG A O6 6130 O O7 . NAG P . ? 0.7727 0.6694 0.8219 0.0334 -0.0993 -0.0662 815 NAG A O7 6131 C C1 . BMA Q . ? 0.6666 0.5525 0.7478 0.0088 -0.0742 -0.0289 816 BMA A C1 6132 C C2 . BMA Q . ? 0.6812 0.5647 0.7641 0.0048 -0.0682 -0.0199 816 BMA A C2 6133 C C3 . BMA Q . ? 0.7115 0.5848 0.8004 0.0049 -0.0705 -0.0190 816 BMA A C3 6134 C C4 . BMA Q . ? 0.7401 0.6098 0.8203 0.0117 -0.0753 -0.0242 816 BMA A C4 6135 C C5 . BMA Q . ? 0.7421 0.6145 0.8204 0.0154 -0.0809 -0.0333 816 BMA A C5 6136 C C6 . BMA Q . ? 0.7540 0.6233 0.8224 0.0227 -0.0849 -0.0387 816 BMA A C6 6137 O O2 . BMA Q . ? 0.6575 0.5451 0.7268 0.0074 -0.0644 -0.0157 816 BMA A O2 6138 O O3 . BMA Q . ? 0.6962 0.5680 0.7826 0.0024 -0.0645 -0.0101 816 BMA A O3 6139 O O4 . BMA Q . ? 0.7624 0.6220 0.8493 0.0118 -0.0780 -0.0242 816 BMA A O4 6140 O O5 . BMA Q . ? 0.6925 0.5746 0.7648 0.0149 -0.0778 -0.0326 816 BMA A O5 6141 O O6 . BMA Q . ? 0.7464 0.6183 0.8112 0.0261 -0.0894 -0.0464 816 BMA A O6 6142 C C1 . MAN R . ? 0.7736 0.6374 0.8722 -0.0018 -0.0637 -0.0065 817 MAN A C1 6143 C C2 . MAN R . ? 0.7748 0.6348 0.8668 -0.0021 -0.0589 0.0023 817 MAN A C2 6144 C C3 . MAN R . ? 0.7881 0.6549 0.8743 -0.0051 -0.0518 0.0090 817 MAN A C3 6145 C C4 . MAN R . ? 0.8135 0.6831 0.9121 -0.0110 -0.0487 0.0097 817 MAN A C4 6146 C C5 . MAN R . ? 0.7948 0.6683 0.9005 -0.0103 -0.0542 0.0005 817 MAN A C5 6147 C C6 . MAN R . ? 0.8391 0.7168 0.9582 -0.0158 -0.0517 0.0003 817 MAN A C6 6148 O O2 . MAN R . ? 0.8029 0.6539 0.9066 -0.0056 -0.0584 0.0055 817 MAN A O2 6149 O O3 . MAN R . ? 0.8347 0.6967 0.9155 -0.0056 -0.0477 0.0174 817 MAN A O3 6150 O O4 . MAN R . ? 0.8116 0.6884 0.9032 -0.0130 -0.0423 0.0147 817 MAN A O4 6151 O O5 . MAN R . ? 0.7632 0.6291 0.8744 -0.0078 -0.0609 -0.0051 817 MAN A O5 6152 O O6 . MAN R . ? 0.8792 0.7498 1.0129 -0.0205 -0.0498 0.0038 817 MAN A O6 6153 O O4 . 28Z S . ? 0.6666 0.7175 0.7877 0.0258 0.0005 -0.0441 818 28Z A O4 6154 C C4 . 28Z S . ? 0.6781 0.7305 0.8037 0.0253 -0.0044 -0.0444 818 28Z A C4 6155 C C4A . 28Z S . ? 0.6601 0.7138 0.7853 0.0211 -0.0021 -0.0432 818 28Z A C4A 6156 N N3 . 28Z S . ? 0.7028 0.7552 0.8335 0.0293 -0.0120 -0.0459 818 28Z A N3 6157 C C8A . 28Z S . ? 0.6670 0.7217 0.7977 0.0211 -0.0080 -0.0440 818 28Z A C8A 6158 N N5 . 28Z S . ? 0.6407 0.6941 0.7600 0.0173 0.0050 -0.0416 818 28Z A N5 6159 C C2 . 28Z S . ? 0.6988 0.7524 0.8341 0.0294 -0.0178 -0.0468 818 28Z A C2 6160 N N8 . 28Z S . ? 0.6662 0.7216 0.7972 0.0172 -0.0062 -0.0428 818 28Z A N8 6161 N N1 . 28Z S . ? 0.6868 0.7415 0.8225 0.0252 -0.0158 -0.0459 818 28Z A N1 6162 C C6 . 28Z S . ? 0.6073 0.6612 0.7260 0.0137 0.0067 -0.0401 818 28Z A C6 6163 N N2 . 28Z S . ? 0.7157 0.7689 0.8551 0.0338 -0.0259 -0.0486 818 28Z A N2 6164 C C7 . 28Z S . ? 0.6333 0.6882 0.7584 0.0136 0.0011 -0.0407 818 28Z A C7 6165 C C9 . 28Z S . ? 0.5626 0.6158 0.6740 0.0098 0.0142 -0.0380 818 28Z A C9 6166 N N10 . 28Z S . ? 0.5238 0.5740 0.6242 0.0103 0.0179 -0.0376 818 28Z A N10 6167 C CBH . 28Z S . ? 0.4657 0.5109 0.5541 0.0118 0.0149 -0.0366 818 28Z A CBH 6168 C CAL . 28Z S . ? 0.4330 0.4754 0.5168 0.0129 0.0088 -0.0354 818 28Z A CAL 6169 C CAK . 28Z S . ? 0.4465 0.4892 0.5274 0.0123 0.0181 -0.0368 818 28Z A CAK 6170 C CAN . 28Z S . ? 0.3996 0.4371 0.4719 0.0146 0.0064 -0.0341 818 28Z A CAN 6171 C CAM . 28Z S . ? 0.3947 0.4324 0.4650 0.0137 0.0152 -0.0355 818 28Z A CAM 6172 C CBI . 28Z S . ? 0.3727 0.4080 0.4389 0.0148 0.0098 -0.0340 818 28Z A CBI 6173 C CBF . 28Z S . ? 0.3713 0.4015 0.4268 0.0163 0.0076 -0.0323 818 28Z A CBF 6174 O OAF . 28Z S . ? 0.4007 0.4288 0.4520 0.0173 0.0036 -0.0308 818 28Z A OAF 6175 N NBA . 28Z S . ? 0.3441 0.3720 0.3959 0.0168 0.0101 -0.0325 818 28Z A NBA 6176 C CBO . 28Z S . ? 0.3290 0.3521 0.3719 0.0180 0.0084 -0.0305 818 28Z A CBO 6177 C CBD . 28Z S . ? 0.3824 0.4032 0.4257 0.0221 0.0037 -0.0297 818 28Z A CBD 6178 O OAI . 28Z S . ? 0.4490 0.4669 0.4852 0.0228 0.0015 -0.0275 818 28Z A OAI 6179 C CAS . 28Z S . ? 0.2884 0.3092 0.3289 0.0176 0.0118 -0.0312 818 28Z A CAS 6180 C CAQ . 28Z S . ? 0.2951 0.3110 0.3289 0.0189 0.0105 -0.0291 818 28Z A CAQ 6181 C CBE . 28Z S . ? 0.3051 0.3196 0.3358 0.0165 0.0140 -0.0300 818 28Z A CBE 6182 O OAE . 28Z S . ? 0.2760 0.2899 0.3099 0.0170 0.0160 -0.0321 818 28Z A OAE 6183 O OAD . 28Z S . ? 0.4237 0.4456 0.4739 0.0246 0.0025 -0.0313 818 28Z A OAD 6184 N N . 28Z S . ? 0.2832 0.2970 0.3080 0.0141 0.0143 -0.0288 818 28Z A N 6185 C CA . 28Z S . ? 0.2847 0.2974 0.3068 0.0118 0.0169 -0.0304 818 28Z A CA 6186 C C . 28Z S . ? 0.2957 0.3115 0.3200 0.0106 0.0199 -0.0332 818 28Z A C 6187 O OXT . 28Z S . ? 0.2973 0.3164 0.3246 0.0105 0.0201 -0.0330 818 28Z A OXT 6188 C CB . 28Z S . ? 0.2848 0.2971 0.3008 0.0095 0.0163 -0.0288 818 28Z A CB 6189 C CG . 28Z S . ? 0.2845 0.2998 0.2989 0.0082 0.0160 -0.0280 818 28Z A CG 6190 C CD . 28Z S . ? 0.3154 0.3303 0.3237 0.0059 0.0155 -0.0268 818 28Z A CD 6191 O OE1 . 28Z S . ? 0.2860 0.2995 0.2916 0.0047 0.0161 -0.0279 818 28Z A OE1 6192 O OE2 . 28Z S . ? 0.2745 0.2906 0.2814 0.0055 0.0142 -0.0251 818 28Z A OE2 6193 O O . 28Z S . ? 0.3015 0.3162 0.3248 0.0099 0.0222 -0.0357 818 28Z A O 6194 O O . HOH T . ? 0.2091 0.2075 0.2145 0.0147 0.0142 -0.0112 901 HOH A O 6195 O O . HOH T . ? 0.2314 0.2439 0.2039 -0.0022 0.0024 -0.0105 902 HOH A O 6196 O O . HOH T . ? 0.2804 0.2434 0.2125 0.0602 -0.0465 -0.0355 903 HOH A O 6197 O O . HOH T . ? 0.2756 0.2701 0.2771 0.0301 0.0047 -0.0119 904 HOH A O 6198 O O . HOH T . ? 0.2164 0.2235 0.2094 0.0147 0.0055 -0.0122 905 HOH A O 6199 O O . HOH T . ? 0.2053 0.2210 0.2066 -0.0012 0.0018 -0.0166 906 HOH A O 6200 O O . HOH T . ? 0.2236 0.2342 0.2225 0.0033 -0.0052 -0.0126 907 HOH A O 6201 O O . HOH T . ? 0.2715 0.2359 0.3306 0.0173 0.0247 -0.0466 908 HOH A O 6202 O O . HOH T . ? 0.2410 0.2490 0.2607 0.0092 0.0220 -0.0376 909 HOH A O 6203 O O . HOH T . ? 0.2587 0.2387 0.1974 0.0528 -0.0274 -0.0192 910 HOH A O 6204 O O . HOH T . ? 0.2243 0.2096 0.2576 0.0118 0.0203 -0.0289 911 HOH A O 6205 O O . HOH T . ? 0.2770 0.2655 0.2137 0.0653 0.0370 0.0133 912 HOH A O 6206 O O . HOH T . ? 0.3214 0.2434 0.3674 0.0464 0.0291 0.0067 913 HOH A O 6207 O O . HOH T . ? 0.2738 0.2595 0.2636 0.0096 -0.0227 -0.0075 914 HOH A O 6208 O O . HOH T . ? 0.2811 0.2576 0.2309 0.0452 -0.0311 -0.0232 915 HOH A O 6209 O O . HOH T . ? 0.2294 0.2212 0.2686 0.0245 0.0178 -0.0305 916 HOH A O 6210 O O . HOH T . ? 0.2804 0.2819 0.2450 0.0428 0.0110 0.0019 917 HOH A O 6211 O O . HOH T . ? 0.2507 0.2761 0.3703 0.0485 0.0107 -0.0504 918 HOH A O 6212 O O . HOH T . ? 0.3147 0.2547 0.2396 0.0720 -0.0625 -0.0517 919 HOH A O 6213 O O . HOH T . ? 0.3020 0.2779 0.2106 0.0753 0.0314 0.0102 920 HOH A O 6214 O O . HOH T . ? 0.2695 0.2640 0.2688 0.0513 -0.0255 -0.0198 921 HOH A O 6215 O O . HOH T . ? 0.3672 0.3094 0.2406 0.0925 -0.0382 -0.0382 922 HOH A O 6216 O O . HOH T . ? 0.2349 0.2569 0.2636 -0.0132 0.0266 -0.0082 923 HOH A O 6217 O O . HOH T . ? 0.2450 0.2606 0.2710 0.0220 0.0363 0.0149 924 HOH A O 6218 O O . HOH T . ? 0.2679 0.2781 0.2743 0.0091 0.0388 -0.0559 925 HOH A O 6219 O O . HOH T . ? 0.3144 0.2857 0.2722 0.0772 -0.0912 -0.0535 926 HOH A O 6220 O O . HOH T . ? 0.2810 0.2765 0.2339 0.0530 0.0271 0.0096 927 HOH A O 6221 O O . HOH T . ? 0.2569 0.2437 0.2349 0.0117 -0.0209 -0.0009 928 HOH A O 6222 O O . HOH T . ? 0.2876 0.3425 0.3844 0.0177 0.0745 -0.0572 929 HOH A O 6223 O O . HOH T . ? 0.2516 0.2892 0.3017 0.0076 0.0476 -0.0427 930 HOH A O 6224 O O . HOH T . ? 0.2888 0.2794 0.2676 0.0102 0.0330 -0.0777 931 HOH A O 6225 O O . HOH T . ? 0.2708 0.2539 0.3246 0.0301 0.0203 -0.0359 932 HOH A O 6226 O O . HOH T . ? 0.2957 0.3232 0.3892 0.0355 0.0645 -0.0778 933 HOH A O 6227 O O . HOH T . ? 0.3144 0.2763 0.2825 0.0409 -0.0455 -0.0303 934 HOH A O 6228 O O . HOH T . ? 0.2703 0.2697 0.2374 0.0271 -0.0081 -0.0077 935 HOH A O 6229 O O . HOH T . ? 0.2631 0.2226 0.3045 0.0347 0.0208 -0.0135 936 HOH A O 6230 O O . HOH T . ? 0.2617 0.2344 0.3138 0.0069 0.0279 -0.0111 937 HOH A O 6231 O O . HOH T . ? 0.2947 0.3084 0.2832 0.0126 0.0023 -0.0039 938 HOH A O 6232 O O . HOH T . ? 0.3865 0.3408 0.3374 0.0566 0.0617 0.0452 939 HOH A O 6233 O O . HOH T . ? 0.2685 0.2671 0.2840 0.0079 0.0262 -0.0534 940 HOH A O 6234 O O . HOH T . ? 0.3768 0.2971 0.5243 -0.0571 0.0484 0.0621 941 HOH A O 6235 O O . HOH T . ? 0.2744 0.2942 0.3502 -0.0273 0.0462 0.0056 942 HOH A O 6236 O O . HOH T . ? 0.2667 0.2869 0.3734 -0.0153 -0.0065 -0.0198 943 HOH A O 6237 O O . HOH T . ? 0.2313 0.2589 0.2639 0.0073 0.0344 -0.0394 944 HOH A O 6238 O O . HOH T . ? 0.2763 0.2969 0.3276 0.0221 0.0552 -0.0667 945 HOH A O 6239 O O . HOH T . ? 0.2445 0.2668 0.2435 -0.0056 0.0257 -0.0183 946 HOH A O 6240 O O . HOH T . ? 0.2649 0.2886 0.3479 0.0286 0.0369 -0.0564 947 HOH A O 6241 O O . HOH T . ? 0.2859 0.2390 0.3537 0.0129 0.0266 -0.0294 948 HOH A O 6242 O O . HOH T . ? 0.3399 0.3494 0.4015 0.0388 0.0751 -0.0955 949 HOH A O 6243 O O . HOH T . ? 0.3282 0.2755 0.3951 0.0557 0.0142 -0.0206 950 HOH A O 6244 O O . HOH T . ? 0.3747 0.3384 0.3694 0.0077 0.0106 -0.1033 951 HOH A O 6245 O O . HOH T . ? 0.4098 0.4321 0.5156 0.0473 -0.0978 -0.0676 952 HOH A O 6246 O O . HOH T . ? 0.2337 0.2524 0.2530 -0.0091 0.0151 -0.0103 953 HOH A O 6247 O O . HOH T . ? 0.2564 0.2513 0.3071 0.0279 0.0192 -0.0367 954 HOH A O 6248 O O . HOH T . ? 0.3083 0.2860 0.3745 0.0363 0.0211 -0.0397 955 HOH A O 6249 O O . HOH T . ? 0.2351 0.2478 0.2287 0.0028 0.0084 -0.0185 956 HOH A O 6250 O O . HOH T . ? 0.2568 0.2698 0.2963 -0.0095 -0.0026 -0.0297 957 HOH A O 6251 O O . HOH T . ? 0.3897 0.3279 0.2270 0.1046 -0.0229 -0.0154 958 HOH A O 6252 O O . HOH T . ? 0.2628 0.2660 0.2267 -0.0013 -0.0052 -0.0001 959 HOH A O 6253 O O . HOH T . ? 0.3230 0.2774 0.3743 -0.0221 -0.0031 0.0189 960 HOH A O 6254 O O . HOH T . ? 0.2312 0.2432 0.2181 0.0076 0.0023 -0.0112 961 HOH A O 6255 O O . HOH T . ? 0.2720 0.2456 0.2634 0.0457 0.0059 -0.0011 962 HOH A O 6256 O O . HOH T . ? 0.3636 0.2752 0.3945 0.0490 0.0379 0.0248 963 HOH A O 6257 O O . HOH T . ? 0.2529 0.2855 0.3042 0.0112 0.0380 -0.0434 964 HOH A O 6258 O O . HOH T . ? 0.3102 0.3087 0.3019 -0.0144 0.0177 0.0080 965 HOH A O 6259 O O . HOH T . ? 0.2874 0.2774 0.2514 0.0314 -0.0194 -0.0132 966 HOH A O 6260 O O . HOH T . ? 0.2985 0.2892 0.2699 0.0248 -0.0204 -0.0110 967 HOH A O 6261 O O . HOH T . ? 0.2892 0.3003 0.2849 0.0280 0.0240 0.0091 968 HOH A O 6262 O O . HOH T . ? 0.3434 0.3539 0.3247 0.0155 -0.0011 -0.0042 969 HOH A O 6263 O O . HOH T . ? 0.2943 0.2612 0.3660 0.0021 0.0314 -0.0100 970 HOH A O 6264 O O . HOH T . ? 0.3017 0.3209 0.3026 0.0154 0.0049 -0.0003 971 HOH A O 6265 O O . HOH T . ? 0.3541 0.3308 0.2971 0.0544 -0.0409 -0.0283 972 HOH A O 6266 O O . HOH T . ? 0.2943 0.3295 0.3984 0.0413 -0.0560 -0.0498 973 HOH A O 6267 O O . HOH T . ? 0.2616 0.2540 0.2814 -0.0098 -0.0052 -0.0007 974 HOH A O 6268 O O . HOH T . ? 0.2898 0.2587 0.3526 0.0267 0.0342 -0.0764 975 HOH A O 6269 O O . HOH T . ? 0.4382 0.3645 0.3887 0.0747 -0.1085 -0.0826 976 HOH A O 6270 O O . HOH T . ? 0.3715 0.4215 0.5382 0.0629 -0.0359 -0.0547 977 HOH A O 6271 O O . HOH T . ? 0.2763 0.3086 0.3578 0.0242 0.0452 -0.0575 978 HOH A O 6272 O O . HOH T . ? 0.3115 0.3244 0.2987 0.0220 0.0051 0.0003 979 HOH A O 6273 O O . HOH T . ? 0.4238 0.3436 0.2977 0.1016 -0.0837 -0.0703 980 HOH A O 6274 O O . HOH T . ? 0.3534 0.3535 0.3919 0.0319 0.0644 -0.0925 981 HOH A O 6275 O O . HOH T . ? 0.4249 0.3731 0.2860 0.0929 -0.0225 -0.0186 982 HOH A O 6276 O O . HOH T . ? 0.3481 0.3238 0.3572 0.0127 0.0278 -0.0876 983 HOH A O 6277 O O . HOH T . ? 0.3096 0.2603 0.3136 0.0460 0.0216 0.0104 984 HOH A O 6278 O O . HOH T . ? 0.4054 0.3610 0.3975 0.0453 0.0223 0.0131 985 HOH A O 6279 O O . HOH T . ? 0.3284 0.3094 0.3213 0.0638 -0.0929 -0.0585 986 HOH A O 6280 O O . HOH T . ? 0.3768 0.3249 0.4793 -0.0042 0.0250 -0.0338 987 HOH A O 6281 O O . HOH T . ? 0.3081 0.3224 0.3423 0.0200 -0.0299 -0.0305 988 HOH A O 6282 O O . HOH T . ? 0.2780 0.3020 0.3210 0.0193 -0.0110 -0.0286 989 HOH A O 6283 O O . HOH T . ? 0.2970 0.3380 0.4337 0.0491 -0.0050 -0.0498 990 HOH A O 6284 O O . HOH T . ? 0.3581 0.3097 0.3286 0.0437 -0.0515 -0.0342 991 HOH A O 6285 O O . HOH T . ? 0.3799 0.3588 0.4498 0.1135 -0.0724 -0.0285 992 HOH A O 6286 O O . HOH T . ? 0.2897 0.3202 0.3452 -0.0143 0.0314 -0.0117 993 HOH A O 6287 O O . HOH T . ? 0.3157 0.2956 0.3001 -0.0231 0.0453 0.0322 994 HOH A O 6288 O O . HOH T . ? 0.5277 0.4224 0.2836 0.1575 -0.0891 -0.0388 995 HOH A O 6289 O O . HOH T . ? 0.2710 0.3073 0.4727 -0.0181 -0.0294 -0.0399 996 HOH A O 6290 O O . HOH T . ? 0.2810 0.2977 0.2804 0.0128 0.0067 -0.0017 997 HOH A O 6291 O O . HOH T . ? 0.5005 0.4103 0.3756 0.1478 -0.0820 0.0030 998 HOH A O 6292 O O . HOH T . ? 0.4343 0.3529 0.2255 0.1277 -0.0271 -0.0222 999 HOH A O 6293 O O . HOH T . ? 0.3935 0.3451 0.3282 0.0808 -0.0993 -0.0659 1000 HOH A O 6294 O O . HOH T . ? 0.4991 0.3896 0.4070 0.1508 -0.0625 0.0240 1001 HOH A O 6295 O O . HOH T . ? 0.3549 0.3815 0.3574 0.0042 -0.0194 -0.0090 1002 HOH A O 6296 O O . HOH T . ? 0.4955 0.4003 0.2817 0.1456 -0.0989 -0.0524 1003 HOH A O 6297 O O . HOH T . ? 0.4153 0.3338 0.4438 0.0376 0.0815 0.0613 1004 HOH A O 6298 O O . HOH T . ? 0.3543 0.3758 0.3377 -0.0077 0.0488 -0.0174 1005 HOH A O 6299 O O . HOH T . ? 0.2975 0.2926 0.2860 -0.0011 -0.0092 -0.0011 1006 HOH A O 6300 O O . HOH T . ? 0.3064 0.2946 0.2871 0.0060 0.0227 -0.0753 1007 HOH A O 6301 O O . HOH T . ? 0.3127 0.2859 0.3981 -0.0056 0.0266 -0.0176 1008 HOH A O 6302 O O . HOH T . ? 0.3448 0.3716 0.4593 0.0859 -0.1039 -0.0607 1009 HOH A O 6303 O O . HOH T . ? 0.3757 0.3294 0.4535 -0.0303 0.0056 0.0228 1010 HOH A O 6304 O O . HOH T . ? 0.3418 0.3432 0.3691 -0.0082 -0.0054 -0.0071 1011 HOH A O 6305 O O . HOH T . ? 0.3321 0.2882 0.3958 0.0220 0.0294 -0.0797 1012 HOH A O 6306 O O . HOH T . ? 0.2992 0.3350 0.3275 -0.0087 0.0622 -0.0197 1013 HOH A O 6307 O O . HOH T . ? 0.4386 0.3919 0.5383 -0.0260 -0.0161 0.0046 1014 HOH A O 6308 O O . HOH T . ? 0.3338 0.3209 0.4573 0.0127 -0.0917 -0.0665 1015 HOH A O 6309 O O . HOH T . ? 0.3146 0.3384 0.4124 -0.0184 0.0087 -0.0136 1016 HOH A O 6310 O O . HOH T . ? 0.3222 0.3341 0.3152 0.0069 0.0063 -0.0146 1017 HOH A O 6311 O O . HOH T . ? 0.3628 0.3670 0.4821 0.0531 0.0596 -0.0926 1018 HOH A O 6312 O O . HOH T . ? 0.3906 0.3753 0.3519 0.0000 -0.0021 -0.0800 1019 HOH A O 6313 O O . HOH T . ? 0.4770 0.4238 0.4178 0.0874 -0.1205 -0.0790 1020 HOH A O 6314 O O . HOH T . ? 0.3911 0.3542 0.4410 0.0474 -0.1228 -0.0856 1021 HOH A O 6315 O O . HOH T . ? 0.3154 0.2982 0.4162 -0.0144 0.0156 -0.0299 1022 HOH A O 6316 O O . HOH T . ? 0.3738 0.3056 0.4093 0.0312 -0.0890 -0.0607 1023 HOH A O 6317 O O . HOH T . ? 0.4717 0.3750 0.3782 0.1502 -0.0756 0.0125 1024 HOH A O 6318 O O . HOH T . ? 0.3885 0.3655 0.4666 0.0396 -0.1191 -0.0829 1025 HOH A O 6319 O O . HOH T . ? 0.4387 0.4078 0.3333 0.0790 0.0171 0.0018 1026 HOH A O 6320 O O . HOH T . ? 0.5500 0.4169 0.3783 0.1268 0.0334 0.0729 1027 HOH A O 6321 O O . HOH T . ? 0.2844 0.3017 0.2699 -0.0068 0.0214 -0.0136 1028 HOH A O 6322 O O . HOH T . ? 0.3646 0.3290 0.3778 0.0137 0.0239 -0.0989 1029 HOH A O 6323 O O . HOH T . ? 0.3575 0.3146 0.4234 0.0119 0.0240 -0.0433 1030 HOH A O 6324 O O . HOH T . ? 0.3329 0.2978 0.3087 0.0500 0.0112 0.0082 1031 HOH A O 6325 O O . HOH T . ? 0.3734 0.3888 0.3846 -0.0180 0.0455 0.0025 1032 HOH A O 6326 O O . HOH T . ? 0.3067 0.3242 0.2914 -0.0032 0.0179 -0.0211 1033 HOH A O 6327 O O . HOH T . ? 0.3889 0.4242 0.4632 0.0084 -0.0065 -0.0310 1034 HOH A O 6328 O O . HOH T . ? 0.3330 0.3490 0.3880 0.0231 -0.0438 -0.0388 1035 HOH A O 6329 O O . HOH T . ? 0.4446 0.4262 0.4681 0.0464 0.0789 -0.1238 1036 HOH A O 6330 O O . HOH T . ? 0.3462 0.3935 0.4302 -0.0067 0.0371 -0.0251 1037 HOH A O 6331 O O . HOH T . ? 0.4141 0.3971 0.4127 0.0264 0.0537 -0.1013 1038 HOH A O 6332 O O . HOH T . ? 0.3514 0.3959 0.4829 0.0440 -0.0587 -0.0543 1039 HOH A O 6333 O O . HOH T . ? 0.4961 0.4082 0.3564 0.1092 -0.0776 -0.0719 1040 HOH A O 6334 O O . HOH T . ? 0.6029 0.4875 0.3259 0.1622 -0.0419 -0.0062 1041 HOH A O 6335 O O . HOH T . ? 0.3683 0.3614 0.3880 0.0253 0.0542 -0.0896 1042 HOH A O 6336 O O . HOH T . ? 0.3324 0.3462 0.4262 -0.0368 0.0719 0.0216 1043 HOH A O 6337 O O . HOH T . ? 0.3833 0.3754 0.3780 -0.0250 0.0626 0.0284 1044 HOH A O 6338 O O . HOH T . ? 0.3550 0.3340 0.5080 -0.0082 -0.0709 -0.0507 1045 HOH A O 6339 O O . HOH T . ? 0.4074 0.4377 0.4816 -0.0141 -0.0309 -0.0406 1046 HOH A O 6340 O O . HOH T . ? 0.4239 0.3788 0.4042 0.1281 -0.0963 -0.0223 1047 HOH A O 6341 O O . HOH T . ? 0.4416 0.3966 0.4705 0.0101 0.0163 -0.1010 1048 HOH A O 6342 O O . HOH T . ? 0.3371 0.3657 0.4439 0.0115 -0.0432 -0.0435 1049 HOH A O 6343 O O . HOH T . ? 0.3744 0.3412 0.3876 0.0198 0.0335 -0.1021 1050 HOH A O 6344 O O . HOH T . ? 0.5157 0.4153 0.4315 0.1002 -0.1371 -0.1087 1051 HOH A O 6345 O O . HOH T . ? 0.4900 0.4582 0.5259 -0.0055 -0.0025 -0.0853 1052 HOH A O 6346 O O . HOH T . ? 0.5164 0.4697 0.5749 -0.0174 -0.0167 0.0079 1053 HOH A O 6347 O O . HOH T . ? 0.4506 0.3626 0.3914 0.0793 -0.1040 -0.0843 1054 HOH A O 6348 O O . HOH T . ? 0.5087 0.4147 0.2663 0.1436 -0.0201 -0.0217 1055 HOH A O 6349 O O . HOH T . ? 0.3507 0.3789 0.4304 0.0076 0.0361 0.0117 1056 HOH A O 6350 O O . HOH T . ? 0.4144 0.3688 0.5791 -0.0229 -0.0548 -0.0316 1057 HOH A O 6351 O O . HOH T . ? 0.5285 0.4575 0.6281 0.0349 0.0297 -0.0686 1058 HOH A O 6352 O O . HOH T . ? 0.4017 0.4395 0.5031 0.0307 -0.0392 -0.0447 1059 HOH A O 6353 O O . HOH T . ? 0.3777 0.3672 0.3605 -0.0010 0.0067 -0.0693 1060 HOH A O 6354 O O . HOH T . ? 0.4381 0.5106 0.5964 0.0501 0.1325 -0.0951 1061 HOH A O 6355 O O . HOH T . ? 0.4996 0.3893 0.2168 0.1613 -0.0198 -0.0182 1062 HOH A O 6356 O O . HOH T . ? 0.4109 0.3804 0.5174 -0.0084 0.0334 -0.0098 1063 HOH A O 6357 O O . HOH T . ? 0.4128 0.4345 0.5203 -0.0035 0.0361 0.0074 1064 HOH A O 6358 O O . HOH T . ? 0.3525 0.4153 0.4702 -0.0069 0.0614 -0.0289 1065 HOH A O 6359 O O . HOH T . ? 0.2556 0.2693 0.2513 0.0010 0.0165 -0.0292 1066 HOH A O 6360 O O . HOH T . ? 0.2890 0.3055 0.2784 0.0087 -0.0024 -0.0050 1067 HOH A O 6361 O O . HOH T . ? 0.4266 0.4430 0.3920 -0.0101 0.0952 -0.0015 1068 HOH A O 6362 O O . HOH T . ? 0.5131 0.4444 0.4784 0.0598 0.0971 0.0739 1069 HOH A O 6363 O O . HOH T . ? 0.4310 0.3825 0.4042 0.0558 0.0165 0.0162 1070 HOH A O 6364 O O . HOH T . ? 0.3354 0.3589 0.4107 -0.0309 0.0799 0.0151 1071 HOH A O 6365 O O . HOH T . ? 0.6597 0.6225 0.5470 -0.0125 0.0861 0.0474 1072 HOH A O 6366 O O . HOH T . ? 0.3772 0.3838 0.3561 -0.0091 0.0130 -0.0011 1073 HOH A O 6367 O O . HOH T . ? 0.4752 0.5092 0.5923 -0.0190 0.0146 -0.0165 1074 HOH A O 6368 O O . HOH T . ? 0.4170 0.4788 0.5082 -0.0102 0.1276 -0.0160 1075 HOH A O 6369 O O . HOH T . ? 0.3519 0.3310 0.3682 0.0208 0.0404 -0.0921 1076 HOH A O 6370 O O . HOH T . ? 0.3838 0.3770 0.5054 0.0543 0.0479 -0.0854 1077 HOH A O 6371 O O . HOH T . ? 0.6334 0.5510 0.5525 -0.0241 0.0914 0.0930 1078 HOH A O 6372 O O . HOH T . ? 0.3443 0.3046 0.4230 0.0328 0.0332 -0.0732 1079 HOH A O 6373 O O . HOH T . ? 0.4865 0.4264 0.4077 0.1442 -0.1230 -0.0310 1080 HOH A O 6374 O O . HOH T . ? 0.5975 0.4846 0.3504 0.1685 -0.0923 -0.0192 1081 HOH A O 6375 O O . HOH T . ? 0.5146 0.4949 0.5913 -0.0133 0.0037 -0.0515 1082 HOH A O 6376 O O . HOH T . ? 0.5630 0.5279 0.5484 0.0565 0.0881 -0.1482 1083 HOH A O 6377 O O . HOH T . ? 0.3767 0.3600 0.4091 0.0265 0.0474 -0.0919 1084 HOH A O 6378 O O . HOH T . ? 0.3876 0.3773 0.3623 -0.0150 0.0215 0.0163 1085 HOH A O 6379 O O . HOH T . ? 0.3960 0.3893 0.4531 0.0357 0.0586 -0.0939 1086 HOH A O 6380 O O . HOH T . ? 0.4044 0.3764 0.5893 -0.0394 -0.0166 -0.0081 1087 HOH A O 6381 O O . HOH T . ? 0.5125 0.4977 0.6765 -0.0618 0.1183 0.0637 1088 HOH A O 6382 O O . HOH T . ? 0.3882 0.3079 0.4386 0.0377 0.0376 0.0127 1089 HOH A O 6383 O O . HOH T . ? 0.4783 0.4588 0.4047 0.0034 -0.0109 -0.0867 1090 HOH A O 6384 O O . HOH T . ? 0.4084 0.4412 0.5537 0.0937 -0.0935 -0.0581 1091 HOH A O 6385 O O . HOH T . ? 0.4865 0.4808 0.5507 0.1369 -0.2036 -0.0933 1092 HOH A O 6386 O O . HOH T . ? 0.3421 0.3346 0.3298 -0.0061 -0.0033 0.0041 1093 HOH A O 6387 O O . HOH T . ? 0.4878 0.4472 0.4527 0.0908 -0.1345 -0.0812 1094 HOH A O 6388 O O . HOH T . ? 0.4877 0.4356 0.4113 0.1334 -0.1620 -0.0748 1095 HOH A O 6389 O O . HOH T . ? 0.3749 0.3447 0.3549 -0.0033 -0.0120 0.0159 1096 HOH A O 6390 O O . HOH T . ? 0.3964 0.4476 0.5929 0.1001 -0.1166 -0.0721 1097 HOH A O 6391 O O . HOH T . ? 0.5465 0.4699 0.6928 0.0717 0.0319 -0.0785 1098 HOH A O 6392 O O . HOH T . ? 0.4091 0.4237 0.5806 0.0046 -0.0818 -0.0647 1099 HOH A O 6393 O O . HOH T . ? 0.4784 0.4383 0.4660 0.0010 -0.0156 -0.1146 1100 HOH A O 6394 O O . HOH T . ? 0.4516 0.4927 0.5190 -0.0189 0.0785 -0.0061 1101 HOH A O 6395 O O . HOH T . ? 0.4648 0.4477 0.4544 0.0351 0.0476 0.0269 1102 HOH A O 6396 O O . HOH T . ? 0.5435 0.4239 0.4956 0.0730 0.0981 0.0943 1103 HOH A O 6397 O O . HOH T . ? 0.5131 0.4701 0.5187 0.0410 0.0574 -0.1345 1104 HOH A O 6398 O O . HOH T . ? 0.3644 0.4001 0.4319 -0.0174 0.0465 -0.0098 1105 HOH A O 6399 O O . HOH T . ? 0.4792 0.4299 0.4248 -0.0156 0.0270 0.0478 1106 HOH A O 6400 O O . HOH T . ? 0.4326 0.3837 0.5468 0.0690 0.0156 -0.0448 1107 HOH A O 6401 O O . HOH T . ? 0.5992 0.5634 0.3723 0.0425 0.1109 -0.0770 1108 HOH A O 6402 O O . HOH T . ? 0.4888 0.4477 0.5294 0.0268 0.0787 0.0491 1109 HOH A O 6403 O O . HOH T . ? 0.7475 0.6540 0.5672 0.1373 -0.1265 -0.0806 1110 HOH A O 6404 O O . HOH T . ? 0.3009 0.3094 0.2527 -0.0018 0.0241 -0.0374 1111 HOH A O 6405 O O . HOH T . ? 0.5193 0.5157 0.4668 -0.0034 -0.0030 0.0057 1112 HOH A O 6406 O O . HOH T . ? 0.3942 0.3920 0.4494 -0.0160 -0.0186 -0.0618 1113 HOH A O 6407 O O . HOH T . ? 0.4405 0.4221 0.5884 0.0023 -0.0881 -0.0638 1114 HOH A O 6408 O O . HOH T . ? 0.5107 0.4748 0.4923 -0.0316 0.0996 0.0630 1115 HOH A O 6409 O O . HOH T . ? 0.2144 0.2294 0.2068 0.0018 0.0095 -0.0195 1116 HOH A O 6410 O O . HOH T . ? 0.4879 0.4546 0.7221 -0.0775 0.1175 0.0745 1117 HOH A O 6411 O O . HOH T . ? 0.4079 0.4131 0.3825 0.0224 -0.0060 -0.0041 1118 HOH A O 6412 O O . HOH T . ? 0.4296 0.4502 0.4809 -0.0296 0.1093 0.0240 1119 HOH A O 6413 O O . HOH T . ? 0.3706 0.3948 0.3786 -0.0026 -0.0135 -0.0178 1120 HOH A O 6414 O O . HOH T . ? 0.5210 0.4828 0.4930 0.1234 -0.1064 -0.0324 1121 HOH A O 6415 O O . HOH T . ? 0.4375 0.3744 0.4478 0.0281 -0.0621 -0.0350 1122 HOH A O 6416 O O . HOH T . ? 0.4923 0.5175 0.5700 0.0550 0.1165 -0.1137 1123 HOH A O 6417 O O . HOH T . ? 0.3317 0.3518 0.3213 -0.0033 0.0257 -0.0241 1124 HOH A O 6418 O O . HOH T . ? 0.5245 0.4035 0.5300 0.0798 0.0295 0.0420 1125 HOH A O 6419 O O . HOH T . ? 0.7018 0.5570 0.4230 0.1589 0.0596 0.0779 1126 HOH A O 6420 O O . HOH T . ? 0.6622 0.5402 0.3781 0.1625 -0.0132 0.0182 1127 HOH A O 6421 O O . HOH T . ? 0.4686 0.4693 0.4475 -0.0199 0.0636 0.0183 1128 HOH A O 6422 O O . HOH T . ? 0.5764 0.4286 0.4121 0.1511 -0.0142 0.0622 1129 HOH A O 6423 O O . HOH T . ? 0.5333 0.5169 0.3774 0.0121 0.0527 -0.0425 1130 HOH A O 6424 O O . HOH T . ? 0.4104 0.4156 0.3979 -0.0182 0.0477 0.0105 1131 HOH A O 6425 O O . HOH T . ? 0.4555 0.3653 0.4971 0.1085 -0.0183 0.0067 1132 HOH A O 6426 O O . HOH T . ? 0.4055 0.4456 0.5947 -0.0324 0.0215 -0.0146 1133 HOH A O 6427 O O . HOH T . ? 0.4455 0.3546 0.5051 0.0296 0.0650 0.0421 1134 HOH A O 6428 O O . HOH T . ? 0.5680 0.4993 0.5614 -0.0290 0.0456 0.0656 1135 HOH A O 6429 O O . HOH T . ? 0.4486 0.4715 0.4447 -0.0030 -0.0219 -0.0216 1136 HOH A O 6430 O O . HOH T . ? 0.6148 0.5470 0.5997 0.0856 -0.1630 -0.1130 1137 HOH A O 6431 O O . HOH T . ? 0.4203 0.3494 0.6078 -0.0364 -0.0402 -0.0120 1138 HOH A O 6432 O O . HOH T . ? 0.5982 0.5749 0.6742 0.0080 0.0584 0.0257 1139 HOH A O 6433 O O . HOH T . ? 0.4618 0.4679 0.4548 -0.0117 0.0155 0.0007 1140 HOH A O 6434 O O . HOH T . ? 0.3928 0.4438 0.5589 0.0556 -0.0136 -0.0547 1141 HOH A O 6435 O O . HOH T . ? 0.2644 0.2803 0.2533 -0.0010 0.0171 -0.0265 1142 HOH A O 6436 O O . HOH T . ? 0.4761 0.4807 0.4465 0.0602 0.1461 -0.1252 1143 HOH A O 6437 O O . HOH T . ? 0.3253 0.3716 0.3946 -0.0192 0.1317 0.0035 1144 HOH A O 6438 O O . HOH T . ? 0.5824 0.5542 0.4172 0.0208 0.0351 -0.0797 1145 HOH A O 6439 O O . HOH T . ? 0.4146 0.4334 0.5045 -0.0367 0.0917 0.0251 1146 HOH A O 6440 O O . HOH T . ? 0.4568 0.4530 0.5165 0.0093 0.0475 0.0183 1147 HOH A O 6441 O O . HOH T . ? 0.4773 0.5452 0.6806 0.0581 -0.0353 -0.0612 1148 HOH A O 6442 O O . HOH T . ? 0.4451 0.4416 0.4564 0.0247 0.0426 0.0201 1149 HOH A O 6443 O O . HOH T . ? 0.5625 0.4758 0.5705 0.0467 0.0932 0.0742 1150 HOH A O 6444 O O . HOH T . ? 0.6939 0.5903 0.6119 0.1063 -0.1581 -0.1214 1151 HOH A O 6445 O O . HOH T . ? 0.4492 0.4586 0.5535 -0.0026 0.0443 0.0122 1152 HOH A O 6446 O O . HOH T . ? 0.4933 0.5004 0.4167 -0.0031 0.0835 -0.0113 1153 HOH A O 6447 O O . HOH T . ? 0.5272 0.5730 0.5433 0.0282 0.1578 -0.0652 1154 HOH A O 6448 O O . HOH T . ? 0.5358 0.4571 0.6059 0.0692 0.0130 -0.0098 1155 HOH A O 6449 O O . HOH T . ? 0.4322 0.3804 0.5673 0.0662 0.0327 -0.0759 1156 HOH A O 6450 O O . HOH T . ? 0.5050 0.4425 0.4887 0.0422 -0.0598 -0.0377 1157 HOH A O 6451 O O . HOH T . ? 0.4931 0.4545 0.5449 0.0009 0.0121 -0.0755 1158 HOH A O 6452 O O . HOH T . ? 0.4302 0.3360 0.2070 0.1336 0.0686 0.0502 1159 HOH A O 6453 O O . HOH T . ? 0.2496 0.2620 0.2380 0.0072 0.0003 -0.0125 1160 HOH A O 6454 O O . HOH T . ? 0.5049 0.4768 0.5392 -0.0399 0.1001 0.0606 1161 HOH A O 6455 O O . HOH T . ? 0.4430 0.4373 0.4091 -0.0021 -0.0064 0.0057 1162 HOH A O 6456 O O . HOH T . ? 0.4959 0.5406 0.6848 0.0887 -0.1687 -0.0988 1163 HOH A O 6457 O O . HOH T . ? 0.7054 0.5499 0.3877 0.1985 -0.1460 -0.1100 1164 HOH A O 6458 O O . HOH T . ? 0.5167 0.4381 0.4891 0.0637 -0.1018 -0.0782 1165 HOH A O 6459 O O . HOH T . ? 0.5522 0.4365 0.4233 0.0999 0.0912 0.0915 1166 HOH A O 6460 O O . HOH T . ? 0.6209 0.4674 0.4431 0.1405 0.0224 0.0797 1167 HOH A O 6461 O O . HOH T . ? 0.6388 0.4875 0.3750 0.1871 -0.0597 0.0367 1168 HOH A O 6462 O O . HOH T . ? 0.7189 0.5628 0.4060 0.2100 -0.1015 0.0075 1169 HOH A O 6463 O O . HOH T . ? 0.2987 0.3116 0.2666 -0.0031 0.0024 -0.0143 1170 HOH A O 6464 O O . HOH T . ? 0.3700 0.4075 0.4478 -0.0090 0.0193 -0.0205 1171 HOH A O 6465 O O . HOH T . ? 0.3846 0.4247 0.6117 -0.0290 -0.0114 -0.0316 1172 HOH A O 6466 O O . HOH T . ? 0.6894 0.5587 0.4373 0.1646 -0.1054 -0.0959 1173 HOH A O 6467 O O . HOH T . ? 0.4757 0.4618 0.4544 -0.0044 -0.0141 -0.0800 1174 HOH A O 6468 O O . HOH T . ? 0.4767 0.5320 0.6740 0.0861 -0.0861 -0.0660 1175 HOH A O 6469 O O . HOH T . ? 0.3947 0.3510 0.6236 -0.0480 -0.0226 -0.0088 1176 HOH A O 6470 O O . HOH T . ? 0.5141 0.5256 0.4704 -0.0064 0.0235 -0.0154 1177 HOH A O 6471 O O . HOH T . ? 0.6115 0.5445 0.6216 -0.0425 0.1155 0.0935 1178 HOH A O 6472 O O . HOH T . ? 0.3878 0.4038 0.3599 -0.0060 0.0262 -0.0184 1179 HOH A O 6473 O O . HOH T . ? 0.2904 0.3494 0.4028 -0.0020 0.0434 -0.0327 1180 HOH A O 6474 O O . HOH T . ? 0.5141 0.4311 0.5890 0.0885 0.0002 -0.0078 1181 HOH A O 6475 O O . HOH T . ? 0.4042 0.4094 0.4897 0.0345 -0.0914 -0.0650 1182 HOH A O 6476 O O . HOH T . ? 0.3940 0.3448 0.4373 0.0201 0.0277 -0.1036 1183 HOH A O 6477 O O . HOH T . ? 0.4829 0.4774 0.4321 -0.0009 0.0025 -0.0632 1184 HOH A O 6478 O O . HOH T . ? 0.5594 0.5290 0.5721 0.1529 -0.1650 -0.0549 1185 HOH A O 6479 O O . HOH T . ? 0.4884 0.3941 0.3339 0.1181 -0.0970 -0.0815 1186 HOH A O 6480 O O . HOH T . ? 0.4859 0.4170 0.5192 0.0203 -0.0665 -0.0363 1187 HOH A O 6481 O O . HOH T . ? 0.2091 0.2425 0.3250 -0.0071 -0.0118 -0.0293 1188 HOH A O 6482 O O . HOH T . ? 0.4178 0.4601 0.4746 -0.0118 0.0633 -0.0172 1189 HOH A O 6483 O O . HOH T . ? 0.4360 0.5055 0.6885 0.0579 -0.1368 -0.0959 1190 HOH A O 6484 O O . HOH T . ? 0.4471 0.4566 0.3957 -0.0047 0.0129 -0.0207 1191 HOH A O 6485 O O . HOH T . ? 0.5329 0.4999 0.6026 0.0421 0.0521 -0.1074 1192 HOH A O 6486 O O . HOH T . ? 0.5534 0.5473 0.4813 0.0004 -0.0003 -0.0608 1193 HOH A O 6487 O O . HOH T . ? 0.4604 0.3454 0.4526 0.0904 0.0161 0.0380 1194 HOH A O 6488 O O . HOH T . ? 0.4518 0.4601 0.4254 0.0050 -0.0089 -0.0034 1195 HOH A O 6489 O O . HOH T . ? 0.5885 0.5959 0.5228 -0.0069 0.1096 0.0036 1196 HOH A O 6490 O O . HOH T . ? 0.5819 0.5864 0.5713 -0.0082 -0.0434 -0.0676 1197 HOH A O 6491 O O . HOH T . ? 0.3567 0.3118 0.3953 0.0386 0.0501 -0.1239 1198 HOH A O 6492 O O . HOH T . ? 0.4685 0.4236 0.6319 -0.0140 -0.0734 -0.0476 1199 HOH A O 6493 O O . HOH T . ? 0.6233 0.5891 0.8218 -0.0332 -0.0430 -0.0265 1200 HOH A O 6494 O O . HOH T . ? 0.3405 0.3165 0.3732 0.0670 -0.1345 -0.0868 1201 HOH A O 6495 O O . HOH T . ? 0.4812 0.4946 0.5045 -0.0118 -0.0326 -0.0536 1202 HOH A O 6496 O O . HOH T . ? 0.2488 0.2892 0.3657 -0.0265 0.0538 -0.0046 1203 HOH A O 6497 O O . HOH T . ? 0.4333 0.3760 0.3299 0.1015 -0.1054 -0.0634 1204 HOH A O 6498 O O . HOH T . ? 0.4708 0.5519 0.6304 -0.0065 0.0922 -0.0316 1205 HOH A O 6499 O O . HOH T . ? 0.3419 0.3375 0.3064 0.0299 -0.0123 -0.0091 1206 HOH A O 6500 O O . HOH T . ? 0.4529 0.4361 0.4126 0.0004 -0.0125 0.0131 1207 HOH A O 6501 O O . HOH T . ? 0.4874 0.4444 0.5550 0.0059 0.0205 -0.0546 1208 HOH A O 6502 O O . HOH T . ? 0.5191 0.4672 0.5790 0.0195 0.0267 -0.0928 1209 HOH A O 6503 O O . HOH T . ? 0.4073 0.4140 0.3838 0.0265 -0.0033 -0.0022 1210 HOH A O 6504 O O . HOH T . ? 0.4870 0.4807 0.5901 0.0528 0.0653 -0.1032 1211 HOH A O 6505 O O . HOH T . ? 0.4307 0.4618 0.5041 -0.0282 0.0925 0.0117 1212 HOH A O 6506 O O . HOH T . ? 0.3776 0.4024 0.4746 -0.0320 0.0627 0.0098 1213 HOH A O 6507 O O . HOH T . ? 0.5043 0.5492 0.6956 -0.0144 -0.0212 -0.0386 1214 HOH A O 6508 O O . HOH T . ? 0.5495 0.5472 0.6581 0.1126 -0.0789 -0.0395 1215 HOH A O 6509 O O . HOH T . ? 0.4272 0.4443 0.3879 -0.0074 0.0822 -0.0102 1216 HOH A O 6510 O O . HOH T . ? 0.4352 0.3545 0.3744 0.1500 -0.0912 -0.0007 1217 HOH A O 6511 O O . HOH T . ? 0.5178 0.4567 0.4832 0.1428 -0.1006 -0.0144 1218 HOH A O 6512 O O . HOH T . ? 0.5367 0.4558 0.5100 0.0690 -0.1173 -0.0896 1219 HOH A O 6513 O O . HOH T . ? 0.4618 0.2901 0.1143 0.2128 -0.1501 -0.1217 1220 HOH A O 6514 O O . HOH T . ? 0.2462 0.3347 0.4241 0.0054 0.0848 -0.0452 1221 HOH A O 6515 O O . HOH T . ? 0.6330 0.6860 0.7770 0.0342 -0.0383 -0.0511 1222 HOH A O 6516 O O . HOH T . ? 0.7921 0.6272 0.4468 0.2137 -0.1634 -0.1120 1223 HOH A O 6517 O O . HOH T . ? 0.4487 0.4523 0.3837 -0.0028 -0.0012 -0.0380 1224 HOH A O 6518 O O . HOH T . ? 0.5315 0.4782 0.5548 0.0740 -0.1623 -0.1108 1225 HOH A O 6519 O O . HOH T . ? 0.5083 0.5629 0.6874 -0.0169 -0.0008 -0.0169 1226 HOH A O 6520 O O . HOH T . ? 0.4196 0.3889 0.3940 0.0455 0.0596 0.0386 1227 HOH A O 6521 O O . HOH T . ? 0.5127 0.4908 0.6350 -0.0086 0.0475 0.0084 1228 HOH A O 6522 O O . HOH T . ? 0.4399 0.4463 0.3738 -0.0011 0.0315 -0.0352 1229 HOH A O 6523 O O . HOH T . ? 0.4931 0.5098 0.4690 -0.0106 0.0497 -0.0088 1230 HOH A O 6524 O O . HOH T . ? 0.5626 0.4191 0.2899 0.1878 -0.1753 -0.1193 1231 HOH A O 6525 O O . HOH T . ? 0.6603 0.5907 0.7051 0.0354 -0.1048 -0.0745 1232 HOH A O 6526 O O . HOH T . ? 0.5926 0.5606 0.4385 0.0206 0.0224 -0.0927 1233 HOH A O 6527 O O . HOH T . ? 0.6812 0.5879 0.4792 0.1519 -0.1013 -0.0318 1234 HOH A O 6528 O O . HOH T . ? 0.5372 0.5207 0.6601 0.0292 -0.1234 -0.0872 1235 HOH A O 6529 O O . HOH T . ? 0.5416 0.4959 0.5138 0.1367 -0.1153 -0.0297 1236 HOH A O 6530 O O . HOH T . ? 0.4395 0.4713 0.5071 -0.0282 0.1242 0.0197 1237 HOH A O 6531 O O . HOH T . ? 0.4808 0.4724 0.6264 0.0157 -0.1064 -0.0772 1238 HOH A O 6532 O O . HOH T . ? 0.5189 0.5388 0.6026 0.0042 0.0398 0.0124 1239 HOH A O 6533 O O . HOH T . ? 0.4513 0.4891 0.5105 -0.0168 0.0613 -0.0094 1240 HOH A O 6534 O O . HOH T . ? 0.5234 0.5244 0.4736 -0.0026 -0.0468 -0.0648 1241 HOH A O 6535 O O . HOH T . ? 0.5404 0.5710 0.6544 -0.0170 -0.0092 -0.0283 1242 HOH A O 6536 O O . HOH T . ? 0.5364 0.5368 0.4973 0.0028 -0.0132 0.0031 1243 HOH A O 6537 O O . HOH T . ? 0.5046 0.5199 0.4804 -0.0039 -0.0433 -0.0436 1244 HOH A O 6538 O O . HOH T . ? 0.5423 0.4758 0.4675 0.1479 -0.1134 -0.0199 1245 HOH A O 6539 O O . HOH T . ? 0.4695 0.4871 0.4415 -0.0102 0.0675 -0.0081 1246 HOH A O 6540 O O . HOH T . ? 0.6692 0.5529 0.4319 0.1599 -0.1258 -0.0856 1247 HOH A O 6541 O O . HOH T . ? 0.2877 0.3632 0.4218 -0.0094 0.1205 -0.0229 1248 HOH A O 6542 O O . HOH T . ? 0.5353 0.5318 0.6755 0.0613 0.0413 -0.0803 1249 HOH A O 6543 O O . HOH T . ? 0.5095 0.5207 0.6558 0.1025 -0.0580 -0.0456 1250 HOH A O 6544 O O . HOH T . ? 0.4041 0.3970 0.5019 0.1501 -0.1505 -0.0538 1251 HOH A O 6545 O O . HOH T . ? 0.4011 0.4082 0.3405 -0.0039 0.0039 -0.0244 1252 HOH A O 6546 O O . HOH T . ? 0.4350 0.4436 0.4135 0.0215 -0.0001 -0.0025 1253 HOH A O 6547 O O . HOH T . ? 0.5153 0.4747 0.4710 -0.0131 0.0144 0.0370 1254 HOH A O 6548 O O . HOH T . ? 0.5565 0.4378 0.2644 0.1653 -0.0245 -0.0012 1255 HOH A O 6549 O O . HOH T . ? 0.5902 0.4702 0.3004 0.1627 -0.0031 0.0164 1256 HOH A O 6550 O O . HOH T . ? 0.5848 0.5910 0.5161 -0.0029 0.0264 -0.0275 1257 HOH A O 6551 O O . HOH T . ? 0.4612 0.5013 0.6055 0.0255 -0.0680 -0.0590 1258 HOH A O 6552 O O . HOH T . ? 0.2908 0.3838 0.4759 0.0126 0.0991 -0.0527 1259 HOH A O 6553 O O . HOH T . ? 0.5091 0.5119 0.4617 -0.0017 -0.0064 0.0002 1260 HOH A O 6554 O O . HOH T . ? 0.2644 0.2844 0.2927 0.0059 -0.0061 -0.0214 1261 HOH A O 6555 O O . HOH T . ? 0.5360 0.4447 0.3286 0.1428 -0.0767 -0.0240 1262 HOH A O 6556 O O . HOH T . ? 0.6584 0.5707 0.6321 0.1334 -0.0549 0.0119 1263 HOH A O 6557 O O . HOH T . ? 0.5779 0.5103 0.6228 0.1217 -0.0465 -0.0044 1264 HOH A O 6558 O O . HOH T . ? 0.6215 0.5101 0.5914 0.0802 0.0344 0.0504 1265 HOH A O 6559 O O . HOH T . ? 0.3790 0.3169 0.3937 0.0421 0.0991 0.0706 1266 HOH A O 6560 O O . HOH T . ? 0.6084 0.6182 0.6710 0.0080 0.0413 0.0142 1267 HOH A O 6561 O O . HOH T . ? 0.4362 0.4534 0.5353 -0.0141 0.0075 -0.0199 1268 HOH A O 6562 O O . HOH T . ? 0.5297 0.5392 0.6155 -0.0073 0.0232 -0.0061 1269 HOH A O 6563 O O . HOH T . ? 0.5038 0.6047 0.7850 0.0604 0.0598 -0.0854 1270 HOH A O 6564 O O . HOH T . ? 0.4815 0.5270 0.5965 0.0482 0.1091 -0.0975 1271 HOH A O 6565 O O . HOH T . ? 0.3694 0.4068 0.4611 0.0248 0.0244 -0.0462 1272 HOH A O 6566 O O . HOH T . ? 0.2296 0.2595 0.2866 0.0157 0.0200 -0.0370 1273 HOH A O 6567 O O . HOH T . ? 0.4023 0.3624 0.5053 0.0655 0.0126 -0.0402 1274 HOH A O 6568 O O . HOH T . ? 0.4710 0.5147 0.6825 0.0728 0.0428 -0.0847 1275 HOH A O 6569 O O . HOH T . ? 0.7032 0.6436 0.6487 0.1063 -0.1638 -0.1017 1276 HOH A O 6570 O O . HOH T . ? 0.3698 0.4136 0.4806 -0.0128 -0.0207 -0.0274 1277 HOH A O 6571 O O . HOH T . ? 0.2984 0.3357 0.3658 0.0133 0.0303 -0.0409 1278 HOH A O 6572 O O . HOH T . ? 0.3673 0.4109 0.4394 0.0082 0.0361 -0.0388 1279 HOH A O 6573 O O . HOH T . ? 0.5156 0.5056 0.3738 0.0460 0.1449 -0.0898 1280 HOH A O 6574 O O . HOH T . ? 0.6482 0.5297 0.4012 0.1807 -0.1136 -0.0213 1281 HOH A O 6575 O O . HOH T . ? 0.3990 0.4192 0.4294 0.0174 0.0015 -0.0259 1282 HOH A O 6576 O O . HOH T . ? 0.5206 0.4886 0.4174 0.0765 0.0023 -0.0074 1283 HOH A O 6577 O O . HOH T . ? 0.4371 0.4771 0.5189 0.0177 0.0330 -0.0455 1284 HOH A O 6578 O O . HOH T . ? 0.5391 0.5919 0.5746 0.0351 0.1724 -0.0728 1285 HOH A O 6579 O O . HOH T . ? 0.4394 0.3720 0.3036 0.1142 -0.1030 -0.0593 1286 HOH A O 6580 O O . HOH T . ? 0.4469 0.5330 0.6124 -0.0009 0.1009 -0.0377 1287 HOH A O 6581 O O . HOH T . ? 0.3855 0.4163 0.4572 0.0222 0.0162 -0.0395 1288 HOH A O 6582 O O . HOH T . ? 0.5876 0.5294 0.5112 0.0252 0.0114 -0.1450 1289 HOH A O 6583 O O . HOH T . ? 0.3327 0.3618 0.3831 0.0145 -0.0004 -0.0293 1290 HOH A O 6584 O O . HOH T . ? 0.5605 0.6217 0.6804 0.0105 0.0437 -0.0440 1291 HOH A O 6585 O O . HOH T . ? 0.5171 0.3622 0.6110 -0.0125 -0.0409 0.0312 1292 HOH A O 6586 O O . HOH T . ? 0.5556 0.5686 0.5131 0.0513 0.1524 -0.1062 1293 HOH A O 6587 O O . HOH T . ? 0.6966 0.6639 0.6818 -0.0029 -0.0285 -0.1105 1294 HOH A O 6588 O O . HOH T . ? 0.6226 0.5461 0.6380 0.0735 -0.1650 -0.1193 1295 HOH A O 6589 O O . HOH T . ? 0.4586 0.4988 0.5706 0.0087 -0.0237 -0.0388 1296 HOH A O 6590 O O . HOH T . ? 0.5336 0.6047 0.7484 0.0294 -0.0614 -0.0656 1297 HOH A O 6591 O O . HOH T . ? 0.9081 0.8948 0.7788 0.0008 0.1319 0.0157 1298 HOH A O 6592 O O . HOH T . ? 0.3504 0.3751 0.4931 -0.0415 0.0712 0.0164 1299 HOH A O 6593 O O . HOH T . ? 0.4119 0.4528 0.5219 -0.0169 0.0252 -0.0172 1300 HOH A O 6594 O O . HOH T . ? 0.4800 0.5753 0.6646 0.0066 0.1133 -0.0462 1301 HOH A O 6595 O O . HOH T . ? 0.6492 0.6213 0.6696 -0.0396 0.1382 0.0731 1302 HOH A O 6596 O O . HOH T . ? 0.5603 0.5744 0.6923 0.0950 -0.0586 -0.0447 1303 HOH A O 6597 O O . HOH T . ? 0.4217 0.4695 0.6452 -0.0312 0.0077 -0.0248 1304 HOH A O 6598 O O . HOH T . ? 0.5681 0.5913 0.8131 -0.0390 -0.0120 -0.0257 1305 HOH A O 6599 O O . HOH T . ? 0.6463 0.5796 0.5489 0.0342 0.0184 -0.1587 1306 HOH A O 6600 O O . HOH T . ? 0.4194 0.4508 0.5746 0.0576 0.0669 -0.0913 1307 HOH A O 6601 O O . HOH T . ? 0.2180 0.2379 0.2138 -0.0028 0.0172 -0.0190 1308 HOH A O 6602 O O . HOH T . ? 0.5246 0.4794 0.6417 0.0207 -0.1184 -0.0841 1309 HOH A O 6603 O O . HOH T . ? 0.7532 0.6910 0.6358 0.1256 -0.1282 -0.0613 1310 HOH A O 6604 O O . HOH T . ? 0.6153 0.5578 0.5747 0.0219 0.0135 -0.1402 1311 HOH A O 6605 O O . HOH T . ? 0.6305 0.4891 0.7799 -0.0170 -0.0649 -0.0101 1312 HOH A O 6606 O O . HOH T . ? 0.5034 0.5931 0.7177 0.0322 0.0543 -0.0650 1313 HOH A O 6607 O O . HOH T . ? 0.5151 0.5546 0.6119 0.0253 -0.0242 -0.0406 1314 HOH A O 6608 O O . HOH T . ? 0.5487 0.5585 0.5224 -0.0107 0.0256 -0.0031 1315 HOH A O 6609 O O A HOH T . ? 0.3062 0.3153 0.3702 0.0026 0.0324 0.0058 1316 HOH A O 6610 O O B HOH T . ? 0.3649 0.3736 0.4460 -0.0017 0.0334 0.0046 1316 HOH A O 6611 O O . HOH T . ? 0.4743 0.4970 0.6806 -0.0093 -0.0652 -0.0571 1317 HOH A O 6612 O O . HOH T . ? 0.5324 0.6270 0.6681 0.0264 0.2163 -0.0529 1318 HOH A O 6613 O O . HOH T . ? 0.6232 0.5269 0.6667 0.0408 0.0519 0.0350 1319 HOH A O 6614 O O . HOH T . ? 0.5240 0.6271 0.7207 0.0308 0.1519 -0.0707 1320 HOH A O 6615 O O . HOH T . ? 0.5643 0.4864 0.5731 0.1308 -0.0559 0.0037 1321 HOH A O 6616 O O . HOH T . ? 0.6300 0.5952 0.6133 0.1433 -0.1960 -0.0871 1322 HOH A O 6617 O O . HOH T . ? 0.7093 0.6593 0.4814 0.0397 0.0492 -0.1049 1323 HOH A O 6618 O O . HOH T . ? 0.4557 0.4926 0.5356 0.0182 -0.0108 -0.0353 1324 HOH A O 6619 O O . HOH T . ? 0.4683 0.4388 0.5982 0.0806 0.0035 -0.0453 1325 HOH A O 6620 O O . HOH T . ? 0.6659 0.4869 0.3844 0.1745 0.0292 0.0914 1326 HOH A O 6621 O O . HOH T . ? 0.5305 0.5547 0.6751 0.0145 -0.0749 -0.0607 1327 HOH A O 6622 O O . HOH T . ? 0.4617 0.4894 0.5216 0.0250 -0.0061 -0.0327 1328 HOH A O 6623 O O . HOH T . ? 0.7422 0.7172 0.6142 0.0136 0.0117 -0.0855 1329 HOH A O 6624 O O . HOH T . ? 0.7039 0.6610 0.6075 0.0157 -0.0046 -0.1223 1330 HOH A O 6625 O O . HOH T . ? 0.5117 0.5427 0.6851 0.0851 -0.0341 -0.0538 1331 HOH A O 6626 O O . HOH T . ? 0.3750 0.2239 0.1775 0.1662 -0.0314 0.0568 1332 HOH A O 6627 O O . HOH T . ? 0.6757 0.6645 0.7169 0.0753 -0.1367 -0.0828 1333 HOH A O 6628 O O . HOH T . ? 0.6041 0.5896 0.5322 0.0656 0.1406 -0.1385 1334 HOH A O 6629 O O . HOH T . ? 0.6269 0.6159 0.6700 0.1230 -0.1865 -0.0906 1335 HOH A O 6630 O O . HOH T . ? 0.5830 0.6837 0.7572 0.0294 0.1768 -0.0662 1336 HOH A O 6631 O O . HOH T . ? 0.5449 0.5552 0.5017 -0.0048 0.0068 -0.0129 1337 HOH A O 6632 O O . HOH T . ? 0.6341 0.6454 0.5172 0.0303 0.2182 -0.0245 1338 HOH A O 6633 O O . HOH T . ? 0.5953 0.5457 0.6143 -0.0424 0.1207 0.0834 1339 HOH A O 6634 O O . HOH T . ? 0.5887 0.6012 0.6373 0.0303 0.0050 -0.0308 1340 HOH A O 6635 O O . HOH T . ? 0.5329 0.6178 0.8228 0.0801 0.0324 -0.0876 1341 HOH A O 6636 O O . HOH T . ? 0.6511 0.5640 0.5840 0.0800 -0.0883 -0.0746 1342 HOH A O 6637 O O . HOH T . ? 0.5463 0.5160 0.6961 0.0095 -0.1091 -0.0780 1343 HOH A O 6638 O O . HOH T . ? 0.4471 0.4655 0.5689 0.0273 -0.0881 -0.0658 1344 HOH A O 6639 O O . HOH T . ? 0.2253 0.2309 0.2527 0.0207 0.0123 -0.0265 1345 HOH A O 6640 O O . HOH T . ? 0.7073 0.5397 0.3968 0.1923 -0.0279 0.0535 1346 HOH A O 6641 O O . HOH T . ? 0.6658 0.5072 0.3945 0.1795 -0.0251 0.0555 1347 HOH A O 6642 O O . HOH T . ? 0.7477 0.6167 0.4524 0.1740 -0.0408 0.0112 1348 HOH A O 6643 O O . HOH T . ? 0.7365 0.6433 0.5893 0.1610 -0.1067 -0.0089 1349 HOH A O 6644 O O . HOH T . ? 0.5854 0.4499 0.4570 0.1613 -0.0515 0.0423 1350 HOH A O 6645 O O . HOH T . ? 0.7392 0.6079 0.7191 0.1045 0.0114 0.0464 1351 HOH A O 6646 O O . HOH T . ? 0.3841 0.3033 0.4785 0.0249 0.0308 -0.0304 1352 HOH A O 6647 O O . HOH T . ? 0.9248 0.7722 0.5632 0.1963 -0.0204 0.0162 1353 HOH A O 6648 O O . HOH T . ? 0.8167 0.7540 0.6950 0.1285 -0.1177 -0.0485 1354 HOH A O 6649 O O . HOH T . ? 0.5309 0.4226 0.5205 0.0579 0.1041 0.0904 1355 HOH A O 6650 O O . HOH T . ? 0.4857 0.4147 0.3184 0.0491 0.0372 -0.1644 1356 HOH A O 6651 O O . HOH T . ? 0.7810 0.7376 0.7204 0.0088 -0.0171 -0.1243 1357 HOH A O 6652 O O . HOH T . ? 0.5620 0.5739 0.5390 -0.0156 0.0721 0.0058 1358 HOH A O 6653 O O . HOH T . ? 0.6264 0.6360 0.5806 -0.0115 0.0819 0.0030 1359 HOH A O 6654 O O . HOH T . ? 0.4299 0.4115 0.6022 0.0805 0.0338 -0.0823 1360 HOH A O 6655 O O . HOH T . ? 0.6108 0.6066 0.6721 0.0432 0.0718 -0.1051 1361 HOH A O 6656 O O . HOH T . ? 0.4566 0.4765 0.5118 0.0077 0.0297 0.0077 1362 HOH A O 6657 O O . HOH T . ? 0.5466 0.6695 0.8000 -0.0054 0.1924 -0.0258 1363 HOH A O 6658 O O . HOH T . ? 0.7479 0.7239 0.6356 0.0841 0.1714 -0.1551 1364 HOH A O 6659 O O . HOH T . ? 0.7814 0.7243 0.5553 0.0932 0.1638 -0.1644 1365 HOH A O 6660 O O . HOH T . ? 0.5180 0.5772 0.7199 0.0772 -0.0630 -0.0632 1366 HOH A O 6661 O O . HOH T . ? 0.5122 0.6024 0.7785 0.0634 -0.0580 -0.0733 1367 HOH A O 6662 O O . HOH T . ? 0.5604 0.6236 0.7378 0.0425 -0.0448 -0.0577 1368 HOH A O 6663 O O . HOH T . ? 0.5783 0.5596 0.6606 0.0471 -0.1313 -0.0896 1369 HOH A O 6664 O O . HOH T . ? 0.5724 0.5892 0.8257 -0.0234 -0.0635 -0.0560 1370 HOH A O 6665 O O . HOH T . ? 0.4150 0.4559 0.5128 -0.0015 0.0007 -0.0292 1371 HOH A O 6666 O O . HOH T . ? 0.3114 0.3487 0.4165 -0.0090 0.0032 -0.0247 1372 HOH A O 6667 O O . HOH T . ? 0.9208 0.7505 0.5506 0.2023 -0.0056 0.0460 1373 HOH A O 6668 O O . HOH T . ? 0.6948 0.5542 0.5752 0.1274 0.0098 0.0659 1374 HOH A O 6669 O O . HOH T . ? 0.4660 0.3324 0.3590 0.1140 0.0250 0.0677 1375 HOH A O 6670 O O . HOH T . ? 0.4056 0.3614 0.5160 -0.0064 0.0355 -0.0110 1376 HOH A O 6671 O O . HOH T . ? 0.4091 0.3597 0.4990 0.0104 0.0741 0.0398 1377 HOH A O 6672 O O . HOH T . ? 0.4470 0.3848 0.5645 0.0049 0.0797 0.0422 1378 HOH A O 6673 O O . HOH T . ? 0.5285 0.5205 0.5022 -0.0055 -0.0190 -0.0730 1379 HOH A O 6674 O O . HOH T . ? 0.5327 0.5327 0.4610 -0.0018 -0.0097 -0.0463 1380 HOH A O 6675 O O . HOH T . ? 0.3727 0.3375 0.4296 0.0017 0.0161 -0.0609 1381 HOH A O 6676 O O . HOH T . ? 0.4915 0.4553 0.5626 -0.0041 0.0136 -0.0551 1382 HOH A O 6677 O O . HOH T . ? 0.3858 0.3395 0.4349 0.0080 0.0168 -0.0885 1383 HOH A O 6678 O O . HOH T . ? 0.4115 0.4246 0.3922 -0.0136 0.0461 -0.0014 1384 HOH A O 6679 O O . HOH T . ? 0.4021 0.4107 0.3673 -0.0117 0.0367 -0.0013 1385 HOH A O 6680 O O . HOH T . ? 0.3946 0.3946 0.3611 -0.0131 0.0265 0.0077 1386 HOH A O 6681 O O . HOH T . ? 0.3659 0.3516 0.3356 -0.0182 0.0360 0.0238 1387 HOH A O 6682 O O . HOH T . ? 0.3657 0.3581 0.3368 -0.0188 0.0456 0.0206 1388 HOH A O 6683 O O . HOH T . ? 0.4333 0.3898 0.3501 -0.0171 0.0631 0.0527 1389 HOH A O 6684 O O . HOH T . ? 0.4157 0.3698 0.3094 -0.0141 0.0727 0.0546 1390 HOH A O 6685 O O . HOH T . ? 0.4052 0.4070 0.3687 -0.0176 0.0812 0.0180 1391 HOH A O 6686 O O . HOH T . ? 0.4565 0.4991 0.5358 -0.0242 0.1155 0.0071 1392 HOH A O 6687 O O . HOH T . ? 0.3291 0.3677 0.3998 -0.0232 0.0927 0.0028 1393 HOH A O 6688 O O . HOH T . ? 0.4158 0.4767 0.5213 -0.0173 0.1283 -0.0065 1394 HOH A O 6689 O O . HOH T . ? 0.3840 0.4511 0.5167 -0.0157 0.0905 -0.0182 1395 HOH A O 6690 O O . HOH T . ? 0.4397 0.4453 0.3738 -0.0030 0.0151 -0.0303 1396 HOH A O 6691 O O . HOH T . ? 0.6527 0.6506 0.5593 0.0004 0.0148 -0.0386 1397 HOH A O 6692 O O . HOH T . ? 0.4144 0.4173 0.3381 -0.0024 0.0069 -0.0302 1398 HOH A O 6693 O O . HOH T . ? 0.3749 0.3826 0.3139 -0.0047 0.0213 -0.0202 1399 HOH A O 6694 O O . HOH T . ? 0.5085 0.5100 0.4214 -0.0026 0.0299 -0.0215 1400 HOH A O 6695 O O . HOH T . ? 0.3133 0.3505 0.3865 0.0105 -0.0009 -0.0318 1401 HOH A O 6696 O O . HOH T . ? 0.2973 0.3425 0.4050 0.0147 -0.0141 -0.0389 1402 HOH A O 6697 O O . HOH T . ? 0.4063 0.4516 0.5566 0.0156 -0.0495 -0.0523 1403 HOH A O 6698 O O . HOH T . ? 0.7701 0.6862 0.6232 0.0648 0.0574 -0.1917 1404 HOH A O 6699 O O . HOH T . ? 0.7064 0.5973 0.8390 0.0432 0.0303 -0.0791 1405 HOH A O 6700 O O . HOH T . ? 0.5069 0.4631 0.3334 0.0267 0.0143 -0.1099 1406 HOH A O 6701 O O . HOH T . ? 0.6004 0.5995 0.4622 0.0229 0.2301 0.0046 1407 HOH A O 6702 O O . HOH T . ? 0.7269 0.7121 0.5425 0.0292 0.1827 -0.0184 1408 HOH A O 6703 O O . HOH T . ? 0.8107 0.7691 0.5552 0.0332 0.1744 -0.0015 1409 HOH A O 6704 O O . HOH T . ? 0.4370 0.4257 0.2857 0.0117 0.1191 -0.0138 1410 HOH A O 6705 O O . HOH T . ? 0.3665 0.4390 0.5162 0.0140 0.0534 -0.0495 1411 HOH A O 6706 O O . HOH T . ? 0.2588 0.3513 0.4832 0.0398 0.0739 -0.0740 1412 HOH A O 6707 O O . HOH T . ? 0.5387 0.5165 0.7303 0.0971 0.0142 -0.0706 1413 HOH A O 6708 O O . HOH T . ? 0.4091 0.4487 0.5777 -0.0198 0.0068 -0.0166 1414 HOH A O 6709 O O . HOH T . ? 0.4074 0.4274 0.4578 0.0142 0.0372 0.0138 1415 HOH A O 6710 O O . HOH T . ? 0.5396 0.5833 0.6742 -0.0193 -0.0778 -0.0703 1416 HOH A O 6711 O O . HOH T . ? 0.3157 0.3393 0.3998 -0.0172 -0.0247 -0.0435 1417 HOH A O 6712 O O . HOH T . ? 0.5254 0.5275 0.4469 -0.0015 -0.0113 -0.0329 1418 HOH A O 6713 O O . HOH T . ? 0.2867 0.3285 0.4623 0.0662 0.0894 -0.1055 1419 HOH A O 6714 O O . HOH T . ? 0.2681 0.2695 0.3154 0.0506 0.0953 -0.1179 1420 HOH A O 6715 O O . HOH T . ? 0.7203 0.7746 0.7298 0.0212 0.2606 -0.0152 1421 HOH A O 6716 O O . HOH T . ? 0.6461 0.7116 0.7043 0.0089 0.2353 -0.0118 1422 HOH A O 6717 O O . HOH T . ? 0.3927 0.4908 0.5450 0.0098 0.2286 -0.0276 1423 HOH A O 6718 O O . HOH T . ? 0.3822 0.4631 0.4667 0.0312 0.2400 -0.0492 1424 HOH A O 6719 O O . HOH T . ? 0.6582 0.6129 0.4141 0.0917 0.1964 -0.1373 1425 HOH A O 6720 O O . HOH T . ? 0.5170 0.5347 0.6551 0.1053 -0.0818 -0.0492 1426 HOH A O 6721 O O . HOH T . ? 0.2814 0.3493 0.4835 0.0553 -0.0171 -0.0606 1427 HOH A O 6722 O O . HOH T . ? 0.4323 0.4243 0.5027 0.1394 -0.1505 -0.0569 1428 HOH A O 6723 O O . HOH T . ? 0.7507 0.7817 0.9403 0.1502 -0.1753 -0.0773 1429 HOH A O 6724 O O . HOH T . ? 0.3434 0.3596 0.4830 0.1561 -0.2171 -0.0923 1430 HOH A O 6725 O O . HOH T . ? 0.5334 0.6226 0.7963 0.0487 -0.0716 -0.0752 1431 HOH A O 6726 O O . HOH T . ? 0.3778 0.4053 0.5583 0.0079 -0.0799 -0.0656 1432 HOH A O 6727 O O . HOH T . ? 0.3896 0.3955 0.5680 0.0092 -0.1015 -0.0761 1433 HOH A O 6728 O O . HOH T . ? 0.3924 0.4048 0.5789 0.0183 -0.1172 -0.0860 1434 HOH A O 6729 O O . HOH T . ? 0.3793 0.4094 0.5468 0.0850 -0.1823 -0.1075 1435 HOH A O 6730 O O . HOH T . ? 0.5236 0.5518 0.6749 0.0945 -0.1798 -0.1014 1436 HOH A O 6731 O O . HOH T . ? 0.4284 0.4906 0.6688 0.0734 -0.1620 -0.1035 1437 HOH A O 6732 O O . HOH T . ? 0.3512 0.3104 0.4518 0.1164 -0.0458 -0.0237 1438 HOH A O 6733 O O . HOH T . ? 0.2720 0.2769 0.4226 0.1041 -0.0491 -0.0446 1439 HOH A O 6734 O O . HOH T . ? 0.6419 0.5801 0.7121 -0.0532 0.1186 0.0921 1440 HOH A O 6735 O O . HOH T . ? 0.8117 0.6981 0.5114 0.1685 0.0373 0.0160 1441 HOH A O 6736 O O . HOH T . ? 0.4280 0.4187 0.4016 -0.0056 -0.0025 0.0079 1442 HOH A O 6737 O O . HOH T . ? 0.7761 0.7733 0.7183 -0.0097 0.0224 0.0063 1443 HOH A O 6738 O O . HOH T . ? 0.3755 0.3038 0.3811 0.0406 -0.0815 -0.0563 1444 HOH A O 6739 O O . HOH T . ? 0.6345 0.4629 0.3923 0.1733 -0.0060 0.0765 1445 HOH A O 6740 O O . HOH T . ? 0.5719 0.4508 0.2978 0.1707 -0.0687 -0.0083 1446 HOH A O 6741 O O . HOH T . ? 0.8756 0.7535 0.6040 0.1808 -0.1301 -0.0589 1447 HOH A O 6742 O O . HOH T . ? 0.5915 0.4386 0.3051 0.2046 -0.0969 0.0161 1448 HOH A O 6743 O O . HOH T . ? 0.3881 0.3443 0.3748 0.1482 -0.1349 -0.0362 1449 HOH A O 6744 O O . HOH T . ? 0.3797 0.2973 0.2910 0.1597 -0.1112 -0.0088 1450 HOH A O 6745 O O . HOH T . ? 0.4539 0.2977 0.2965 0.1590 -0.0227 0.0639 1451 HOH A O 6746 O O . HOH T . ? 0.4989 0.3978 0.5391 0.0392 0.0736 0.0573 1452 HOH A O 6747 O O . HOH T . ? 0.7201 0.5407 0.5059 0.1432 0.0914 0.1235 1453 HOH A O 6748 O O . HOH T . ? 0.4927 0.3612 0.4074 0.0882 0.1067 0.1065 1454 HOH A O 6749 O O . HOH T . ? 0.4658 0.4006 0.3618 0.0833 0.0796 0.0607 1455 HOH A O 6750 O O . HOH T . ? 0.8215 0.7836 0.7532 0.0633 0.0569 0.0387 1456 HOH A O 6751 O O . HOH T . ? 0.5321 0.5289 0.5461 0.0423 0.0795 0.0422 1457 HOH A O 6752 O O . HOH T . ? 0.6719 0.6637 0.6853 0.0328 0.0625 0.0339 1458 HOH A O 6753 O O . HOH T . ? 0.4771 0.4535 0.4754 0.0348 0.0569 0.0338 1459 HOH A O 6754 O O . HOH T . ? 0.4423 0.4271 0.4688 0.0245 0.0578 0.0308 1460 HOH A O 6755 O O . HOH T . ? 0.5053 0.4672 0.4478 0.0628 0.0727 0.0477 1461 HOH A O 6756 O O . HOH T . ? 0.3342 0.3133 0.4869 -0.0181 0.0395 -0.0034 1462 HOH A O 6757 O O . HOH T . ? 0.5625 0.5383 0.7416 -0.0218 0.0470 0.0020 1463 HOH A O 6758 O O . HOH T . ? 0.3956 0.4015 0.4584 -0.0174 -0.0256 -0.0596 1464 HOH A O 6759 O O . HOH T . ? 0.3922 0.3864 0.3106 0.0003 -0.0093 -0.0575 1465 HOH A O 6760 O O . HOH T . ? 0.3135 0.3213 0.2548 -0.0036 -0.0024 -0.0191 1466 HOH A O 6761 O O . HOH T . ? 0.3298 0.3365 0.2752 -0.0034 -0.0024 -0.0085 1467 HOH A O 6762 O O . HOH T . ? 0.2883 0.2927 0.2336 -0.0022 -0.0064 -0.0034 1468 HOH A O 6763 O O . HOH T . ? 0.5692 0.5837 0.5378 -0.0010 -0.0108 -0.0116 1469 HOH A O 6764 O O . HOH T . ? 0.4464 0.4548 0.4145 0.0037 -0.0122 -0.0018 1470 HOH A O 6765 O O . HOH T . ? 0.3216 0.3347 0.2864 -0.0026 -0.0052 -0.0140 1471 HOH A O 6766 O O . HOH T . ? 0.5666 0.5290 0.6361 -0.0067 0.0067 -0.0686 1472 HOH A O 6767 O O . HOH T . ? 0.4153 0.3731 0.4691 0.0059 0.0170 -0.0772 1473 HOH A O 6768 O O . HOH T . ? 0.3935 0.3446 0.4628 0.0081 0.0202 -0.0674 1474 HOH A O 6769 O O . HOH T . ? 0.4526 0.4180 0.4309 0.0663 0.1047 -0.1580 1475 HOH A O 6770 O O . HOH T . ? 0.3597 0.3373 0.3810 0.0556 0.0902 -0.1372 1476 HOH A O 6771 O O . HOH T . ? 0.7421 0.6505 0.6542 0.0408 0.0068 -0.1901 1477 HOH A O 6772 O O . HOH T . ? 0.3754 0.2916 0.1938 0.0593 0.0418 -0.1836 1478 HOH A O 6773 O O . HOH T . ? 0.4819 0.3883 0.3569 0.0684 0.0550 -0.2054 1479 HOH A O 6774 O O . HOH T . ? 0.5843 0.5265 0.5618 0.0044 -0.0354 -0.1449 1480 HOH A O 6775 O O . HOH T . ? 0.5859 0.5601 0.7631 0.0877 0.0235 -0.0742 1481 HOH A O 6776 O O . HOH T . ? 0.4176 0.3387 0.5208 0.0324 0.0295 -0.0802 1482 HOH A O 6777 O O . HOH T . ? 0.6373 0.5599 0.7304 0.0191 0.0322 -0.0246 1483 HOH A O 6778 O O . HOH T . ? 0.4203 0.3295 0.5228 0.0188 0.0386 -0.0114 1484 HOH A O 6779 O O . HOH T . ? 0.5613 0.4434 0.6093 0.0443 0.0656 0.0526 1485 HOH A O 6780 O O . HOH T . ? 0.7569 0.6044 0.7717 0.0750 0.0556 0.0666 1486 HOH A O 6781 O O . HOH T . ? 0.4098 0.3856 0.2625 0.0150 0.0197 -0.0758 1487 HOH A O 6782 O O . HOH T . ? 0.5442 0.4834 0.3316 0.0425 0.0299 -0.1338 1488 HOH A O 6783 O O . HOH T . ? 0.3659 0.4139 0.4474 -0.0107 0.0519 -0.0211 1489 HOH A O 6784 O O . HOH T . ? 0.2892 0.3347 0.3873 -0.0154 0.0409 -0.0170 1490 HOH A O 6785 O O . HOH T . ? 0.2170 0.2621 0.3090 -0.0092 0.0281 -0.0227 1491 HOH A O 6786 O O . HOH T . ? 0.3639 0.4089 0.4560 0.0058 0.0071 -0.0328 1492 HOH A O 6787 O O . HOH T . ? 0.5172 0.5178 0.4202 -0.0012 0.0984 -0.0048 1493 HOH A O 6788 O O . HOH T . ? 0.6362 0.6361 0.5604 -0.0085 0.1219 0.0162 1494 HOH A O 6789 O O . HOH T . ? 0.5005 0.4879 0.3717 -0.0003 0.0919 0.0046 1495 HOH A O 6790 O O . HOH T . ? 0.5360 0.5597 0.5674 -0.0240 0.1388 0.0245 1496 HOH A O 6791 O O . HOH T . ? 0.6880 0.6246 0.4315 0.0896 0.1529 -0.1574 1497 HOH A O 6792 O O . HOH T . ? 0.6794 0.6289 0.4141 0.0424 0.0755 -0.0788 1498 HOH A O 6793 O O . HOH T . ? 0.6810 0.6487 0.4487 0.0335 0.1376 -0.0338 1499 HOH A O 6794 O O . HOH T . ? 0.4359 0.4490 0.4073 -0.0088 0.0265 -0.0092 1500 HOH A O 6795 O O . HOH T . ? 0.5178 0.6224 0.7566 0.0321 0.0858 -0.0700 1501 HOH A O 6796 O O . HOH T . ? 0.2768 0.3754 0.5479 0.0528 0.0129 -0.0723 1502 HOH A O 6797 O O . HOH T . ? 0.5444 0.5637 0.7364 0.0768 0.0358 -0.0821 1503 HOH A O 6798 O O . HOH T . ? 0.3277 0.3540 0.3555 -0.0039 -0.0094 -0.0179 1504 HOH A O 6799 O O . HOH T . ? 0.4294 0.5444 0.6629 0.0108 0.1359 -0.0510 1505 HOH A O 6800 O O . HOH T . ? 0.6099 0.6474 0.6608 -0.0207 0.1502 0.0154 1506 HOH A O 6801 O O . HOH T . ? 0.5349 0.5955 0.5665 0.0535 0.2364 -0.0808 1507 HOH A O 6802 O O . HOH T . ? 0.3844 0.4502 0.4209 0.0462 0.2473 -0.0658 1508 HOH A O 6803 O O . HOH T . ? 0.2754 0.3192 0.2716 0.0526 0.2107 -0.0865 1509 HOH A O 6804 O O . HOH T . ? 0.4433 0.4195 0.2567 0.0549 0.1505 -0.0972 1510 HOH A O 6805 O O . HOH T . ? 0.5579 0.5965 0.6448 0.0236 0.0023 -0.0384 1511 HOH A O 6806 O O . HOH T . ? 0.5281 0.5398 0.5652 0.0304 -0.0011 -0.0268 1512 HOH A O 6807 O O . HOH T . ? 0.4585 0.4322 0.4552 0.0915 -0.1428 -0.0818 1513 HOH A O 6808 O O . HOH T . ? 0.6892 0.6537 0.6810 0.0988 -0.1631 -0.0952 1514 HOH A O 6809 O O . HOH T . ? 0.5287 0.4928 0.5270 0.1097 -0.1851 -0.1047 1515 HOH A O 6810 O O . HOH T . ? 0.3843 0.3828 0.4554 0.0834 -0.1561 -0.0913 1516 HOH A O 6811 O O . HOH T . ? 0.4062 0.4079 0.4809 0.0536 -0.1151 -0.0755 1517 HOH A O 6812 O O . HOH T . ? 0.4700 0.4841 0.5694 0.0447 -0.1034 -0.0710 1518 HOH A O 6813 O O . HOH T . ? 0.4377 0.4017 0.4173 0.1146 -0.1727 -0.0921 1519 HOH A O 6814 O O . HOH T . ? 0.3506 0.3874 0.5161 0.0940 -0.0789 -0.0569 1520 HOH A O 6815 O O . HOH T . ? 0.5500 0.4832 0.5301 0.1409 -0.0862 -0.0064 1521 HOH A O 6816 O O . HOH T . ? 0.7009 0.6293 0.5487 0.1254 -0.1040 -0.0510 1522 HOH A O 6817 O O . HOH T . ? 0.7662 0.6289 0.4354 0.1795 0.0131 0.0278 1523 HOH A O 6818 O O . HOH T . ? 0.7153 0.6188 0.4605 0.1483 0.0486 0.0260 1524 HOH A O 6819 O O . HOH T . ? 0.9110 0.7831 0.5808 0.1801 0.0314 0.0182 1525 HOH A O 6820 O O A HOH T . ? 0.3052 0.3431 0.4543 -0.0068 -0.0237 -0.0372 1526 HOH A O 6821 O O B HOH T . ? 0.2897 0.3291 0.4263 0.0009 -0.0285 -0.0403 1526 HOH A O 6822 O O . HOH T . ? 0.5750 0.6280 0.7822 -0.0217 -0.0007 -0.0318 1527 HOH A O 6823 O O . HOH T . ? 0.5084 0.5429 0.7373 -0.0173 -0.0478 -0.0502 1528 HOH A O 6824 O O . HOH T . ? 0.3918 0.4306 0.6562 -0.0345 -0.0188 -0.0355 1529 HOH A O 6825 O O . HOH T . ? 0.4082 0.4425 0.6585 -0.0529 0.0501 0.0038 1530 HOH A O 6826 O O . HOH T . ? 0.5967 0.6228 0.8675 -0.0549 0.0307 -0.0024 1531 HOH A O 6827 O O . HOH T . ? 0.3975 0.4414 0.6035 -0.0394 0.0423 -0.0062 1532 HOH A O 6828 O O . HOH T . ? 0.5865 0.6320 0.7562 -0.0275 0.0272 -0.0156 1533 HOH A O 6829 O O . HOH T . ? 0.3007 0.3434 0.4347 -0.0228 0.0307 -0.0143 1534 HOH A O 6830 O O . HOH T . ? 0.5017 0.5460 0.6495 -0.0288 0.0458 -0.0079 1535 HOH A O 6831 O O . HOH T . ? 0.5210 0.5575 0.6528 -0.0331 0.0619 0.0033 1536 HOH A O 6832 O O . HOH T . ? 0.3660 0.3766 0.6026 -0.0359 -0.0280 -0.0311 1537 HOH A O 6833 O O . HOH T . ? 0.6392 0.5845 0.8569 -0.0791 0.1256 0.0905 1538 HOH A O 6834 O O . HOH T . ? 0.8777 0.7350 0.8817 0.0987 0.0206 0.0477 1539 HOH A O 6835 O O . HOH T . ? 0.3544 0.3166 0.6706 -0.0906 0.1042 0.0682 1540 HOH A O 6836 O O . HOH T . ? 0.6326 0.6140 0.9350 -0.0821 0.0861 0.0491 1541 HOH A O 6837 O O . HOH T . ? 0.3631 0.2951 0.5539 -0.0296 -0.0584 -0.0291 1542 HOH A O 6838 O O . HOH T . ? 0.4419 0.4021 0.6878 -0.0430 -0.0447 -0.0277 1543 HOH A O 6839 O O . HOH T . ? 0.4048 0.3382 0.5139 -0.0215 -0.0342 -0.0035 1544 HOH A O 6840 O O . HOH T . ? 0.4099 0.3682 0.4666 0.0560 -0.1457 -0.1007 1545 HOH A O 6841 O O . HOH T . ? 0.3420 0.2711 0.3875 0.0555 -0.1482 -0.1077 1546 HOH A O 6842 O O . HOH T . ? 0.3984 0.3492 0.4945 0.0365 -0.1380 -0.0982 1547 HOH A O 6843 O O . HOH T . ? 0.4641 0.3676 0.4127 0.0853 -0.1321 -0.1043 1548 HOH A O 6844 O O . HOH T . ? 0.4716 0.3560 0.3395 0.1276 -0.1621 -0.1256 1549 HOH A O 6845 O O . HOH T . ? 0.4281 0.3123 0.3141 0.1150 -0.1408 -0.1171 1550 HOH A O 6846 O O . HOH T . ? 0.6127 0.5345 0.4672 0.1233 -0.1230 -0.0752 1551 HOH A O 6847 O O . HOH T . ? 0.4208 0.3137 0.2240 0.1541 -0.1577 -0.0989 1552 HOH A O 6848 O O . HOH T . ? 0.2994 0.3057 0.2449 -0.0063 0.0137 -0.0082 1553 HOH A O 6849 O O . HOH T . ? 0.6916 0.5513 0.4049 0.1793 -0.0890 -0.0929 1554 HOH A O 6850 O O . HOH T . ? 0.4443 0.4349 0.3941 -0.0120 0.0230 0.0146 1555 HOH A O 6851 O O . HOH T . ? 0.3589 0.3666 0.3237 -0.0141 0.0573 0.0045 1556 HOH A O 6852 O O . HOH T . ? 0.2666 0.2513 0.3311 0.0520 -0.1247 -0.0836 1557 HOH A O 6853 O O A HOH T . ? 0.5746 0.5309 0.7144 -0.0111 0.0487 0.0045 1558 HOH A O 6854 O O B HOH T . ? 0.4311 0.3867 0.5725 -0.0089 0.0585 0.0161 1558 HOH A O 6855 O O . HOH T . ? 0.4141 0.4048 0.5516 -0.0197 0.0223 -0.0188 1559 HOH A O 6856 O O . HOH T . ? 0.6207 0.6177 0.7335 -0.0177 0.0125 -0.0263 1560 HOH A O 6857 O O . HOH T . ? 0.5747 0.5262 0.6357 -0.0056 -0.0035 -0.0962 1561 HOH A O 6858 O O . HOH T . ? 0.6375 0.5935 0.7255 0.0482 0.0504 -0.1106 1562 HOH A O 6859 O O . HOH T . ? 0.6021 0.6233 0.5863 -0.0007 -0.0239 -0.0171 1563 HOH A O 6860 O O . HOH T . ? 0.6075 0.7005 0.7560 0.0461 0.2030 -0.0827 1564 HOH A O 6861 O O . HOH T . ? 0.4986 0.4697 0.6828 -0.0154 -0.0753 -0.0528 1565 HOH A O 6862 O O . HOH T . ? 0.6273 0.5947 0.8198 -0.0067 -0.1002 -0.0715 1566 HOH A O 6863 O O . HOH T . ? 0.3910 0.4001 0.3684 0.0100 -0.0092 -0.0035 1567 HOH A O 6864 O O . HOH T . ? 0.5548 0.4844 0.4034 -0.0053 0.0563 0.0681 1568 HOH A O # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 MET 1 -6 ? ? ? A . n A 1 2 LYS 2 -5 ? ? ? A . n A 1 3 LEU 3 -4 ? ? ? A . n A 1 4 CYS 4 -3 ? ? ? A . n A 1 5 ILE 5 -2 ? ? ? A . n A 1 6 LEU 6 -1 ? ? ? A . n A 1 7 LEU 7 0 ? ? ? A . n A 1 8 ALA 8 1 ? ? ? A . n A 1 9 VAL 9 2 ? ? ? A . n A 1 10 VAL 10 3 ? ? ? A . n A 1 11 ALA 11 4 ? ? ? A . n A 1 12 PHE 12 5 ? ? ? A . n A 1 13 VAL 13 6 ? ? ? A . n A 1 14 GLY 14 7 ? ? ? A . n A 1 15 LEU 15 8 ? ? ? A . n A 1 16 SER 16 9 ? ? ? A . n A 1 17 LEU 17 10 ? ? ? A . n A 1 18 GLY 18 11 ? ? ? A . n A 1 19 ARG 19 12 ? ? ? A . n A 1 20 SER 20 13 ? ? ? A . n A 1 21 GLY 21 14 ? ? ? A . n A 1 22 LEU 22 15 ? ? ? A . n A 1 23 ASN 23 16 ? ? ? A . n A 1 24 ASP 24 17 ? ? ? A . n A 1 25 ILE 25 18 ? ? ? A . n A 1 26 PHE 26 19 ? ? ? A . n A 1 27 GLU 27 20 ? ? ? A . n A 1 28 ALA 28 21 ? ? ? A . n A 1 29 GLN 29 22 ? ? ? A . n A 1 30 LYS 30 23 ? ? ? A . n A 1 31 ILE 31 24 ? ? ? A . n A 1 32 GLU 32 25 ? ? ? A . n A 1 33 TRP 33 26 ? ? ? A . n A 1 34 HIS 34 27 ? ? ? A . n A 1 35 GLU 35 28 ? ? ? A . n A 1 36 GLY 36 29 ? ? ? A . n A 1 37 SER 37 30 ? ? ? A . n A 1 38 GLY 38 31 ? ? ? A . n A 1 39 SER 39 32 ? ? ? A . n A 1 40 GLY 40 33 ? ? ? A . n A 1 41 SER 41 34 ? ? ? A . n A 1 42 GLU 42 35 ? ? ? A . n A 1 43 ASN 43 36 ? ? ? A . n A 1 44 LEU 44 37 ? ? ? A . n A 1 45 TYR 45 38 ? ? ? A . n A 1 46 PHE 46 39 ? ? ? A . n A 1 47 GLN 47 40 ? ? ? A . n A 1 48 GLY 48 41 ? ? ? A . n A 1 49 ARG 49 42 ? ? ? A . n A 1 50 SER 50 43 ? ? ? A . n A 1 51 LYS 51 44 ? ? ? A . n A 1 52 SER 52 45 ? ? ? A . n A 1 53 SER 53 46 ? ? ? A . n A 1 54 ASN 54 47 ? ? ? A . n A 1 55 GLU 55 48 ? ? ? A . n A 1 56 ALA 56 49 ? ? ? A . n A 1 57 THR 57 50 ? ? ? A . n A 1 58 ASN 58 51 ? ? ? A . n A 1 59 ILE 59 52 ? ? ? A . n A 1 60 THR 60 53 ? ? ? A . n A 1 61 PRO 61 54 ? ? ? A . n A 1 62 LYS 62 55 ? ? ? A . n A 1 63 HIS 63 56 56 HIS HIS A . n A 1 64 ASN 64 57 57 ASN ASN A . n A 1 65 MET 65 58 58 MET MET A . n A 1 66 LYS 66 59 59 LYS LYS A . n A 1 67 ALA 67 60 60 ALA ALA A . n A 1 68 PHE 68 61 61 PHE PHE A . n A 1 69 LEU 69 62 62 LEU LEU A . n A 1 70 ASP 70 63 63 ASP ASP A . n A 1 71 GLU 71 64 64 GLU GLU A . n A 1 72 LEU 72 65 65 LEU LEU A . n A 1 73 LYS 73 66 66 LYS LYS A . n A 1 74 ALA 74 67 67 ALA ALA A . n A 1 75 GLU 75 68 68 GLU GLU A . n A 1 76 ASN 76 69 69 ASN ASN A . n A 1 77 ILE 77 70 70 ILE ILE A . n A 1 78 LYS 78 71 71 LYS LYS A . n A 1 79 LYS 79 72 72 LYS LYS A . n A 1 80 PHE 80 73 73 PHE PHE A . n A 1 81 LEU 81 74 74 LEU LEU A . n A 1 82 TYR 82 75 75 TYR TYR A . n A 1 83 ASN 83 76 76 ASN ASN A . n A 1 84 PHE 84 77 77 PHE PHE A . n A 1 85 THR 85 78 78 THR THR A . n A 1 86 GLN 86 79 79 GLN GLN A . n A 1 87 ILE 87 80 80 ILE ILE A . n A 1 88 PRO 88 81 81 PRO PRO A . n A 1 89 HIS 89 82 82 HIS HIS A . n A 1 90 LEU 90 83 83 LEU LEU A . n A 1 91 ALA 91 84 84 ALA ALA A . n A 1 92 GLY 92 85 85 GLY GLY A . n A 1 93 THR 93 86 86 THR THR A . n A 1 94 GLU 94 87 87 GLU GLU A . n A 1 95 GLN 95 88 88 GLN GLN A . n A 1 96 ASN 96 89 89 ASN ASN A . n A 1 97 PHE 97 90 90 PHE PHE A . n A 1 98 GLN 98 91 91 GLN GLN A . n A 1 99 LEU 99 92 92 LEU LEU A . n A 1 100 ALA 100 93 93 ALA ALA A . n A 1 101 LYS 101 94 94 LYS LYS A . n A 1 102 GLN 102 95 95 GLN GLN A . n A 1 103 ILE 103 96 96 ILE ILE A . n A 1 104 GLN 104 97 97 GLN GLN A . n A 1 105 SER 105 98 98 SER SER A . n A 1 106 GLN 106 99 99 GLN GLN A . n A 1 107 TRP 107 100 100 TRP TRP A . n A 1 108 LYS 108 101 101 LYS LYS A . n A 1 109 GLU 109 102 102 GLU GLU A . n A 1 110 PHE 110 103 103 PHE PHE A . n A 1 111 GLY 111 104 104 GLY GLY A . n A 1 112 LEU 112 105 105 LEU LEU A . n A 1 113 ASP 113 106 106 ASP ASP A . n A 1 114 SER 114 107 107 SER SER A . n A 1 115 VAL 115 108 108 VAL VAL A . n A 1 116 GLU 116 109 109 GLU GLU A . n A 1 117 LEU 117 110 110 LEU LEU A . n A 1 118 ALA 118 111 111 ALA ALA A . n A 1 119 HIS 119 112 112 HIS HIS A . n A 1 120 TYR 120 113 113 TYR TYR A . n A 1 121 ASP 121 114 114 ASP ASP A . n A 1 122 VAL 122 115 115 VAL VAL A . n A 1 123 LEU 123 116 116 LEU LEU A . n A 1 124 LEU 124 117 117 LEU LEU A . n A 1 125 SER 125 118 118 SER SER A . n A 1 126 TYR 126 119 119 TYR TYR A . n A 1 127 PRO 127 120 120 PRO PRO A . n A 1 128 ASN 128 121 121 ASN ASN A . n A 1 129 LYS 129 122 122 LYS LYS A . n A 1 130 THR 130 123 123 THR THR A . n A 1 131 HIS 131 124 124 HIS HIS A . n A 1 132 PRO 132 125 125 PRO PRO A . n A 1 133 ASN 133 126 126 ASN ASN A . n A 1 134 TYR 134 127 127 TYR TYR A . n A 1 135 ILE 135 128 128 ILE ILE A . n A 1 136 SER 136 129 129 SER SER A . n A 1 137 ILE 137 130 130 ILE ILE A . n A 1 138 ILE 138 131 131 ILE ILE A . n A 1 139 ASN 139 132 132 ASN ASN A . n A 1 140 GLU 140 133 133 GLU GLU A . n A 1 141 ASP 141 134 134 ASP ASP A . n A 1 142 GLY 142 135 135 GLY GLY A . n A 1 143 ASN 143 136 136 ASN ASN A . n A 1 144 GLU 144 137 137 GLU GLU A . n A 1 145 ILE 145 138 138 ILE ILE A . n A 1 146 PHE 146 139 139 PHE PHE A . n A 1 147 ASN 147 140 140 ASN ASN A . n A 1 148 THR 148 141 141 THR THR A . n A 1 149 SER 149 142 142 SER SER A . n A 1 150 LEU 150 143 143 LEU LEU A . n A 1 151 PHE 151 144 144 PHE PHE A . n A 1 152 GLU 152 145 145 GLU GLU A . n A 1 153 PRO 153 146 146 PRO PRO A . n A 1 154 PRO 154 147 147 PRO PRO A . n A 1 155 PRO 155 148 148 PRO PRO A . n A 1 156 PRO 156 149 149 PRO PRO A . n A 1 157 GLY 157 150 150 GLY GLY A . n A 1 158 TYR 158 151 151 TYR TYR A . n A 1 159 GLU 159 152 152 GLU GLU A . n A 1 160 ASN 160 153 153 ASN ASN A . n A 1 161 VAL 161 154 154 VAL VAL A . n A 1 162 SER 162 155 155 SER SER A . n A 1 163 ASP 163 156 156 ASP ASP A . n A 1 164 ILE 164 157 157 ILE ILE A . n A 1 165 VAL 165 158 158 VAL VAL A . n A 1 166 PRO 166 159 159 PRO PRO A . n A 1 167 PRO 167 160 160 PRO PRO A . n A 1 168 PHE 168 161 161 PHE PHE A . n A 1 169 SER 169 162 162 SER SER A . n A 1 170 ALA 170 163 163 ALA ALA A . n A 1 171 PHE 171 164 164 PHE PHE A . n A 1 172 SER 172 165 165 SER SER A . n A 1 173 PRO 173 166 166 PRO PRO A . n A 1 174 GLN 174 167 167 GLN GLN A . n A 1 175 GLY 175 168 168 GLY GLY A . n A 1 176 MET 176 169 169 MET MET A . n A 1 177 PRO 177 170 170 PRO PRO A . n A 1 178 GLU 178 171 171 GLU GLU A . n A 1 179 GLY 179 172 172 GLY GLY A . n A 1 180 ASP 180 173 173 ASP ASP A . n A 1 181 LEU 181 174 174 LEU LEU A . n A 1 182 VAL 182 175 175 VAL VAL A . n A 1 183 TYR 183 176 176 TYR TYR A . n A 1 184 VAL 184 177 177 VAL VAL A . n A 1 185 ASN 185 178 178 ASN ASN A . n A 1 186 TYR 186 179 179 TYR TYR A . n A 1 187 ALA 187 180 180 ALA ALA A . n A 1 188 ARG 188 181 181 ARG ARG A . n A 1 189 THR 189 182 182 THR THR A . n A 1 190 GLU 190 183 183 GLU GLU A . n A 1 191 ASP 191 184 184 ASP ASP A . n A 1 192 PHE 192 185 185 PHE PHE A . n A 1 193 PHE 193 186 186 PHE PHE A . n A 1 194 LYS 194 187 187 LYS LYS A . n A 1 195 LEU 195 188 188 LEU LEU A . n A 1 196 GLU 196 189 189 GLU GLU A . n A 1 197 ARG 197 190 190 ARG ARG A . n A 1 198 ASP 198 191 191 ASP ASP A . n A 1 199 MET 199 192 192 MET MET A . n A 1 200 LYS 200 193 193 LYS LYS A . n A 1 201 ILE 201 194 194 ILE ILE A . n A 1 202 ASN 202 195 195 ASN ASN A . n A 1 203 CYS 203 196 196 CYS CYS A . n A 1 204 SER 204 197 197 SER SER A . n A 1 205 GLY 205 198 198 GLY GLY A . n A 1 206 LYS 206 199 199 LYS LYS A . n A 1 207 ILE 207 200 200 ILE ILE A . n A 1 208 VAL 208 201 201 VAL VAL A . n A 1 209 ILE 209 202 202 ILE ILE A . n A 1 210 ALA 210 203 203 ALA ALA A . n A 1 211 ARG 211 204 204 ARG ARG A . n A 1 212 TYR 212 205 205 TYR TYR A . n A 1 213 GLY 213 206 206 GLY GLY A . n A 1 214 LYS 214 207 207 LYS LYS A . n A 1 215 VAL 215 208 208 VAL VAL A . n A 1 216 PHE 216 209 209 PHE PHE A . n A 1 217 ARG 217 210 210 ARG ARG A . n A 1 218 GLY 218 211 211 GLY GLY A . n A 1 219 ASN 219 212 212 ASN ASN A . n A 1 220 LYS 220 213 213 LYS LYS A . n A 1 221 VAL 221 214 214 VAL VAL A . n A 1 222 LYS 222 215 215 LYS LYS A . n A 1 223 ASN 223 216 216 ASN ASN A . n A 1 224 ALA 224 217 217 ALA ALA A . n A 1 225 GLN 225 218 218 GLN GLN A . n A 1 226 LEU 226 219 219 LEU LEU A . n A 1 227 ALA 227 220 220 ALA ALA A . n A 1 228 GLY 228 221 221 GLY GLY A . n A 1 229 ALA 229 222 222 ALA ALA A . n A 1 230 LYS 230 223 223 LYS LYS A . n A 1 231 GLY 231 224 224 GLY GLY A . n A 1 232 VAL 232 225 225 VAL VAL A . n A 1 233 ILE 233 226 226 ILE ILE A . n A 1 234 LEU 234 227 227 LEU LEU A . n A 1 235 TYR 235 228 228 TYR TYR A . n A 1 236 SER 236 229 229 SER SER A . n A 1 237 ASP 237 230 230 ASP ASP A . n A 1 238 PRO 238 231 231 PRO PRO A . n A 1 239 ALA 239 232 232 ALA ALA A . n A 1 240 ASP 240 233 233 ASP ASP A . n A 1 241 TYR 241 234 234 TYR TYR A . n A 1 242 PHE 242 235 235 PHE PHE A . n A 1 243 ALA 243 236 236 ALA ALA A . n A 1 244 PRO 244 237 237 PRO PRO A . n A 1 245 GLY 245 238 238 GLY GLY A . n A 1 246 VAL 246 239 239 VAL VAL A . n A 1 247 LYS 247 240 240 LYS LYS A . n A 1 248 SER 248 241 241 SER SER A . n A 1 249 TYR 249 242 242 TYR TYR A . n A 1 250 PRO 250 243 243 PRO PRO A . n A 1 251 ASP 251 244 244 ASP ASP A . n A 1 252 GLY 252 245 245 GLY GLY A . n A 1 253 TRP 253 246 246 TRP TRP A . n A 1 254 ASN 254 247 247 ASN ASN A . n A 1 255 LEU 255 248 248 LEU LEU A . n A 1 256 PRO 256 249 249 PRO PRO A . n A 1 257 GLY 257 250 250 GLY GLY A . n A 1 258 GLY 258 251 251 GLY GLY A . n A 1 259 GLY 259 252 252 GLY GLY A . n A 1 260 VAL 260 253 253 VAL VAL A . n A 1 261 GLN 261 254 254 GLN GLN A . n A 1 262 ARG 262 255 255 ARG ARG A . n A 1 263 GLY 263 256 256 GLY GLY A . n A 1 264 ASN 264 257 257 ASN ASN A . n A 1 265 ILE 265 258 258 ILE ILE A . n A 1 266 LEU 266 259 259 LEU LEU A . n A 1 267 ASN 267 260 260 ASN ASN A . n A 1 268 LEU 268 261 261 LEU LEU A . n A 1 269 ASN 269 262 262 ASN ASN A . n A 1 270 GLY 270 263 263 GLY GLY A . n A 1 271 ALA 271 264 264 ALA ALA A . n A 1 272 GLY 272 265 265 GLY GLY A . n A 1 273 ASP 273 266 266 ASP ASP A . n A 1 274 PRO 274 267 267 PRO PRO A . n A 1 275 LEU 275 268 268 LEU LEU A . n A 1 276 THR 276 269 269 THR THR A . n A 1 277 PRO 277 270 270 PRO PRO A . n A 1 278 GLY 278 271 271 GLY GLY A . n A 1 279 TYR 279 272 272 TYR TYR A . n A 1 280 PRO 280 273 273 PRO PRO A . n A 1 281 ALA 281 274 274 ALA ALA A . n A 1 282 ASN 282 275 275 ASN ASN A . n A 1 283 GLU 283 276 276 GLU GLU A . n A 1 284 TYR 284 277 277 TYR TYR A . n A 1 285 ALA 285 278 278 ALA ALA A . n A 1 286 TYR 286 279 279 TYR TYR A . n A 1 287 ARG 287 280 280 ARG ARG A . n A 1 288 ARG 288 281 281 ARG ARG A . n A 1 289 GLY 289 282 282 GLY GLY A . n A 1 290 ILE 290 283 283 ILE ILE A . n A 1 291 ALA 291 284 284 ALA ALA A . n A 1 292 GLU 292 285 285 GLU GLU A . n A 1 293 ALA 293 286 286 ALA ALA A . n A 1 294 VAL 294 287 287 VAL VAL A . n A 1 295 GLY 295 288 288 GLY GLY A . n A 1 296 LEU 296 289 289 LEU LEU A . n A 1 297 PRO 297 290 290 PRO PRO A . n A 1 298 SER 298 291 291 SER SER A . n A 1 299 ILE 299 292 292 ILE ILE A . n A 1 300 PRO 300 293 293 PRO PRO A . n A 1 301 VAL 301 294 294 VAL VAL A . n A 1 302 HIS 302 295 295 HIS HIS A . n A 1 303 PRO 303 296 296 PRO PRO A . n A 1 304 ILE 304 297 297 ILE ILE A . n A 1 305 GLY 305 298 298 GLY GLY A . n A 1 306 TYR 306 299 299 TYR TYR A . n A 1 307 TYR 307 300 300 TYR TYR A . n A 1 308 ASP 308 301 301 ASP ASP A . n A 1 309 ALA 309 302 302 ALA ALA A . n A 1 310 GLN 310 303 303 GLN GLN A . n A 1 311 LYS 311 304 304 LYS LYS A . n A 1 312 LEU 312 305 305 LEU LEU A . n A 1 313 LEU 313 306 306 LEU LEU A . n A 1 314 GLU 314 307 307 GLU GLU A . n A 1 315 LYS 315 308 308 LYS LYS A . n A 1 316 MET 316 309 309 MET MET A . n A 1 317 GLY 317 310 310 GLY GLY A . n A 1 318 GLY 318 311 311 GLY GLY A . n A 1 319 SER 319 312 312 SER SER A . n A 1 320 ALA 320 313 313 ALA ALA A . n A 1 321 PRO 321 314 314 PRO PRO A . n A 1 322 PRO 322 315 315 PRO PRO A . n A 1 323 ASP 323 316 316 ASP ASP A . n A 1 324 SER 324 317 317 SER SER A . n A 1 325 SER 325 318 318 SER SER A . n A 1 326 TRP 326 319 319 TRP TRP A . n A 1 327 ARG 327 320 320 ARG ARG A . n A 1 328 GLY 328 321 321 GLY GLY A . n A 1 329 SER 329 322 322 SER SER A . n A 1 330 LEU 330 323 323 LEU LEU A . n A 1 331 LYS 331 324 324 LYS LYS A . n A 1 332 VAL 332 325 325 VAL VAL A . n A 1 333 PRO 333 326 326 PRO PRO A . n A 1 334 TYR 334 327 327 TYR TYR A . n A 1 335 ASN 335 328 328 ASN ASN A . n A 1 336 VAL 336 329 329 VAL VAL A . n A 1 337 GLY 337 330 330 GLY GLY A . n A 1 338 PRO 338 331 331 PRO PRO A . n A 1 339 GLY 339 332 332 GLY GLY A . n A 1 340 PHE 340 333 333 PHE PHE A . n A 1 341 THR 341 334 334 THR THR A . n A 1 342 GLY 342 335 335 GLY GLY A . n A 1 343 ASN 343 336 336 ASN ASN A . n A 1 344 PHE 344 337 337 PHE PHE A . n A 1 345 SER 345 338 338 SER SER A . n A 1 346 THR 346 339 339 THR THR A . n A 1 347 GLN 347 340 340 GLN GLN A . n A 1 348 LYS 348 341 341 LYS LYS A . n A 1 349 VAL 349 342 342 VAL VAL A . n A 1 350 LYS 350 343 343 LYS LYS A . n A 1 351 MET 351 344 344 MET MET A . n A 1 352 HIS 352 345 345 HIS HIS A . n A 1 353 ILE 353 346 346 ILE ILE A . n A 1 354 HIS 354 347 347 HIS HIS A . n A 1 355 SER 355 348 348 SER SER A . n A 1 356 THR 356 349 349 THR THR A . n A 1 357 ASN 357 350 350 ASN ASN A . n A 1 358 GLU 358 351 351 GLU GLU A . n A 1 359 VAL 359 352 352 VAL VAL A . n A 1 360 THR 360 353 353 THR THR A . n A 1 361 ARG 361 354 354 ARG ARG A . n A 1 362 ILE 362 355 355 ILE ILE A . n A 1 363 TYR 363 356 356 TYR TYR A . n A 1 364 ASN 364 357 357 ASN ASN A . n A 1 365 VAL 365 358 358 VAL VAL A . n A 1 366 ILE 366 359 359 ILE ILE A . n A 1 367 GLY 367 360 360 GLY GLY A . n A 1 368 THR 368 361 361 THR THR A . n A 1 369 LEU 369 362 362 LEU LEU A . n A 1 370 ARG 370 363 363 ARG ARG A . n A 1 371 GLY 371 364 364 GLY GLY A . n A 1 372 ALA 372 365 365 ALA ALA A . n A 1 373 VAL 373 366 366 VAL VAL A . n A 1 374 GLU 374 367 367 GLU GLU A . n A 1 375 PRO 375 368 368 PRO PRO A . n A 1 376 ASP 376 369 369 ASP ASP A . n A 1 377 ARG 377 370 370 ARG ARG A . n A 1 378 TYR 378 371 371 TYR TYR A . n A 1 379 VAL 379 372 372 VAL VAL A . n A 1 380 ILE 380 373 373 ILE ILE A . n A 1 381 LEU 381 374 374 LEU LEU A . n A 1 382 GLY 382 375 375 GLY GLY A . n A 1 383 GLY 383 376 376 GLY GLY A . n A 1 384 HIS 384 377 377 HIS HIS A . n A 1 385 ARG 385 378 378 ARG ARG A . n A 1 386 ASP 386 379 379 ASP ASP A . n A 1 387 SER 387 380 380 SER SER A . n A 1 388 TRP 388 381 381 TRP TRP A . n A 1 389 VAL 389 382 382 VAL VAL A . n A 1 390 PHE 390 383 383 PHE PHE A . n A 1 391 GLY 391 384 384 GLY GLY A . n A 1 392 GLY 392 385 385 GLY GLY A . n A 1 393 ILE 393 386 386 ILE ILE A . n A 1 394 ASP 394 387 387 ASP ASP A . n A 1 395 PRO 395 388 388 PRO PRO A . n A 1 396 GLN 396 389 389 GLN GLN A . n A 1 397 SER 397 390 390 SER SER A . n A 1 398 GLY 398 391 391 GLY GLY A . n A 1 399 ALA 399 392 392 ALA ALA A . n A 1 400 ALA 400 393 393 ALA ALA A . n A 1 401 VAL 401 394 394 VAL VAL A . n A 1 402 VAL 402 395 395 VAL VAL A . n A 1 403 HIS 403 396 396 HIS HIS A . n A 1 404 GLU 404 397 397 GLU GLU A . n A 1 405 ILE 405 398 398 ILE ILE A . n A 1 406 VAL 406 399 399 VAL VAL A . n A 1 407 ARG 407 400 400 ARG ARG A . n A 1 408 SER 408 401 401 SER SER A . n A 1 409 PHE 409 402 402 PHE PHE A . n A 1 410 GLY 410 403 403 GLY GLY A . n A 1 411 THR 411 404 404 THR THR A . n A 1 412 LEU 412 405 405 LEU LEU A . n A 1 413 LYS 413 406 406 LYS LYS A . n A 1 414 LYS 414 407 407 LYS LYS A . n A 1 415 GLU 415 408 408 GLU GLU A . n A 1 416 GLY 416 409 409 GLY GLY A . n A 1 417 TRP 417 410 410 TRP TRP A . n A 1 418 ARG 418 411 411 ARG ARG A . n A 1 419 PRO 419 412 412 PRO PRO A . n A 1 420 ARG 420 413 413 ARG ARG A . n A 1 421 ARG 421 414 414 ARG ARG A . n A 1 422 THR 422 415 415 THR THR A . n A 1 423 ILE 423 416 416 ILE ILE A . n A 1 424 LEU 424 417 417 LEU LEU A . n A 1 425 PHE 425 418 418 PHE PHE A . n A 1 426 ALA 426 419 419 ALA ALA A . n A 1 427 SER 427 420 420 SER SER A . n A 1 428 TRP 428 421 421 TRP TRP A . n A 1 429 ASP 429 422 422 ASP ASP A . n A 1 430 ALA 430 423 423 ALA ALA A . n A 1 431 ALA 431 424 424 ALA ALA A . n A 1 432 GLU 432 425 425 GLU GLU A . n A 1 433 PHE 433 426 426 PHE PHE A . n A 1 434 GLY 434 427 427 GLY GLY A . n A 1 435 LEU 435 428 428 LEU LEU A . n A 1 436 LEU 436 429 429 LEU LEU A . n A 1 437 GLY 437 430 430 GLY GLY A . n A 1 438 SER 438 431 431 SER SER A . n A 1 439 THR 439 432 432 THR THR A . n A 1 440 GLU 440 433 433 GLU GLU A . n A 1 441 TRP 441 434 434 TRP TRP A . n A 1 442 ALA 442 435 435 ALA ALA A . n A 1 443 GLU 443 436 436 GLU GLU A . n A 1 444 GLU 444 437 437 GLU GLU A . n A 1 445 ASN 445 438 438 ASN ASN A . n A 1 446 SER 446 439 439 SER SER A . n A 1 447 ARG 447 440 440 ARG ARG A . n A 1 448 LEU 448 441 441 LEU LEU A . n A 1 449 LEU 449 442 442 LEU LEU A . n A 1 450 GLN 450 443 443 GLN GLN A . n A 1 451 GLU 451 444 444 GLU GLU A . n A 1 452 ARG 452 445 445 ARG ARG A . n A 1 453 GLY 453 446 446 GLY GLY A . n A 1 454 VAL 454 447 447 VAL VAL A . n A 1 455 ALA 455 448 448 ALA ALA A . n A 1 456 TYR 456 449 449 TYR TYR A . n A 1 457 ILE 457 450 450 ILE ILE A . n A 1 458 ASN 458 451 451 ASN ASN A . n A 1 459 ALA 459 452 452 ALA ALA A . n A 1 460 ASP 460 453 453 ASP ASP A . n A 1 461 SER 461 454 454 SER SER A . n A 1 462 SER 462 455 455 SER SER A . n A 1 463 ILE 463 456 456 ILE ILE A . n A 1 464 GLU 464 457 457 GLU GLU A . n A 1 465 GLY 465 458 458 GLY GLY A . n A 1 466 ASN 466 459 459 ASN ASN A . n A 1 467 TYR 467 460 460 TYR TYR A . n A 1 468 THR 468 461 461 THR THR A . n A 1 469 LEU 469 462 462 LEU LEU A . n A 1 470 ARG 470 463 463 ARG ARG A . n A 1 471 VAL 471 464 464 VAL VAL A . n A 1 472 ASP 472 465 465 ASP ASP A . n A 1 473 CYS 473 466 466 CYS CYS A . n A 1 474 THR 474 467 467 THR THR A . n A 1 475 PRO 475 468 468 PRO PRO A . n A 1 476 LEU 476 469 469 LEU LEU A . n A 1 477 MET 477 470 470 MET MET A . n A 1 478 TYR 478 471 471 TYR TYR A . n A 1 479 SER 479 472 472 SER SER A . n A 1 480 LEU 480 473 473 LEU LEU A . n A 1 481 VAL 481 474 474 VAL VAL A . n A 1 482 HIS 482 475 475 HIS HIS A . n A 1 483 ASN 483 476 476 ASN ASN A . n A 1 484 LEU 484 477 477 LEU LEU A . n A 1 485 THR 485 478 478 THR THR A . n A 1 486 LYS 486 479 479 LYS LYS A . n A 1 487 GLU 487 480 480 GLU GLU A . n A 1 488 LEU 488 481 481 LEU LEU A . n A 1 489 LYS 489 482 482 LYS LYS A . n A 1 490 SER 490 483 483 SER SER A . n A 1 491 PRO 491 484 484 PRO PRO A . n A 1 492 ASP 492 485 485 ASP ASP A . n A 1 493 GLU 493 486 486 GLU GLU A . n A 1 494 GLY 494 487 487 GLY GLY A . n A 1 495 PHE 495 488 488 PHE PHE A . n A 1 496 GLU 496 489 489 GLU GLU A . n A 1 497 GLY 497 490 490 GLY GLY A . n A 1 498 LYS 498 491 491 LYS LYS A . n A 1 499 SER 499 492 492 SER SER A . n A 1 500 LEU 500 493 493 LEU LEU A . n A 1 501 TYR 501 494 494 TYR TYR A . n A 1 502 GLU 502 495 495 GLU GLU A . n A 1 503 SER 503 496 496 SER SER A . n A 1 504 TRP 504 497 497 TRP TRP A . n A 1 505 THR 505 498 498 THR THR A . n A 1 506 LYS 506 499 499 LYS LYS A . n A 1 507 LYS 507 500 500 LYS LYS A . n A 1 508 SER 508 501 501 SER SER A . n A 1 509 PRO 509 502 502 PRO PRO A . n A 1 510 SER 510 503 503 SER SER A . n A 1 511 PRO 511 504 504 PRO PRO A . n A 1 512 GLU 512 505 505 GLU GLU A . n A 1 513 PHE 513 506 506 PHE PHE A . n A 1 514 SER 514 507 507 SER SER A . n A 1 515 GLY 515 508 508 GLY GLY A . n A 1 516 MET 516 509 509 MET MET A . n A 1 517 PRO 517 510 510 PRO PRO A . n A 1 518 ARG 518 511 511 ARG ARG A . n A 1 519 ILE 519 512 512 ILE ILE A . n A 1 520 SER 520 513 513 SER SER A . n A 1 521 LYS 521 514 514 LYS LYS A . n A 1 522 LEU 522 515 515 LEU LEU A . n A 1 523 GLY 523 516 516 GLY GLY A . n A 1 524 SER 524 517 517 SER SER A . n A 1 525 GLY 525 518 518 GLY GLY A . n A 1 526 ASN 526 519 519 ASN ASN A . n A 1 527 ASP 527 520 520 ASP ASP A . n A 1 528 PHE 528 521 521 PHE PHE A . n A 1 529 GLU 529 522 522 GLU GLU A . n A 1 530 VAL 530 523 523 VAL VAL A . n A 1 531 PHE 531 524 524 PHE PHE A . n A 1 532 PHE 532 525 525 PHE PHE A . n A 1 533 GLN 533 526 526 GLN GLN A . n A 1 534 ARG 534 527 527 ARG ARG A . n A 1 535 LEU 535 528 528 LEU LEU A . n A 1 536 GLY 536 529 529 GLY GLY A . n A 1 537 ILE 537 530 530 ILE ILE A . n A 1 538 ALA 538 531 531 ALA ALA A . n A 1 539 SER 539 532 532 SER SER A . n A 1 540 GLY 540 533 533 GLY GLY A . n A 1 541 ARG 541 534 534 ARG ARG A . n A 1 542 ALA 542 535 535 ALA ALA A . n A 1 543 ARG 543 536 536 ARG ARG A . n A 1 544 TYR 544 537 537 TYR TYR A . n A 1 545 THR 545 538 538 THR THR A . n A 1 546 LYS 546 539 539 LYS LYS A . n A 1 547 ASN 547 540 540 ASN ASN A . n A 1 548 TRP 548 541 541 TRP TRP A . n A 1 549 GLU 549 542 542 GLU GLU A . n A 1 550 THR 550 543 543 THR THR A . n A 1 551 ASN 551 544 544 ASN ASN A . n A 1 552 LYS 552 545 545 LYS LYS A . n A 1 553 PHE 553 546 546 PHE PHE A . n A 1 554 SER 554 547 547 SER SER A . n A 1 555 GLY 555 548 548 GLY GLY A . n A 1 556 TYR 556 549 549 TYR TYR A . n A 1 557 PRO 557 550 550 PRO PRO A . n A 1 558 LEU 558 551 551 LEU LEU A . n A 1 559 TYR 559 552 552 TYR TYR A . n A 1 560 HIS 560 553 553 HIS HIS A . n A 1 561 SER 561 554 554 SER SER A . n A 1 562 VAL 562 555 555 VAL VAL A . n A 1 563 TYR 563 556 556 TYR TYR A . n A 1 564 GLU 564 557 557 GLU GLU A . n A 1 565 THR 565 558 558 THR THR A . n A 1 566 TYR 566 559 559 TYR TYR A . n A 1 567 GLU 567 560 560 GLU GLU A . n A 1 568 LEU 568 561 561 LEU LEU A . n A 1 569 VAL 569 562 562 VAL VAL A . n A 1 570 GLU 570 563 563 GLU GLU A . n A 1 571 LYS 571 564 564 LYS LYS A . n A 1 572 PHE 572 565 565 PHE PHE A . n A 1 573 TYR 573 566 566 TYR TYR A . n A 1 574 ASP 574 567 567 ASP ASP A . n A 1 575 PRO 575 568 568 PRO PRO A . n A 1 576 MET 576 569 569 MET MET A . n A 1 577 PHE 577 570 570 PHE PHE A . n A 1 578 LYS 578 571 571 LYS LYS A . n A 1 579 TYR 579 572 572 TYR TYR A . n A 1 580 HIS 580 573 573 HIS HIS A . n A 1 581 LEU 581 574 574 LEU LEU A . n A 1 582 THR 582 575 575 THR THR A . n A 1 583 VAL 583 576 576 VAL VAL A . n A 1 584 ALA 584 577 577 ALA ALA A . n A 1 585 GLN 585 578 578 GLN GLN A . n A 1 586 VAL 586 579 579 VAL VAL A . n A 1 587 ARG 587 580 580 ARG ARG A . n A 1 588 GLY 588 581 581 GLY GLY A . n A 1 589 GLY 589 582 582 GLY GLY A . n A 1 590 MET 590 583 583 MET MET A . n A 1 591 VAL 591 584 584 VAL VAL A . n A 1 592 PHE 592 585 585 PHE PHE A . n A 1 593 GLU 593 586 586 GLU GLU A . n A 1 594 LEU 594 587 587 LEU LEU A . n A 1 595 ALA 595 588 588 ALA ALA A . n A 1 596 ASN 596 589 589 ASN ASN A . n A 1 597 SER 597 590 590 SER SER A . n A 1 598 ILE 598 591 591 ILE ILE A . n A 1 599 VAL 599 592 592 VAL VAL A . n A 1 600 LEU 600 593 593 LEU LEU A . n A 1 601 PRO 601 594 594 PRO PRO A . n A 1 602 PHE 602 595 595 PHE PHE A . n A 1 603 ASP 603 596 596 ASP ASP A . n A 1 604 CYS 604 597 597 CYS CYS A . n A 1 605 ARG 605 598 598 ARG ARG A . n A 1 606 ASP 606 599 599 ASP ASP A . n A 1 607 TYR 607 600 600 TYR TYR A . n A 1 608 ALA 608 601 601 ALA ALA A . n A 1 609 VAL 609 602 602 VAL VAL A . n A 1 610 VAL 610 603 603 VAL VAL A . n A 1 611 LEU 611 604 604 LEU LEU A . n A 1 612 ARG 612 605 605 ARG ARG A . n A 1 613 LYS 613 606 606 LYS LYS A . n A 1 614 TYR 614 607 607 TYR TYR A . n A 1 615 ALA 615 608 608 ALA ALA A . n A 1 616 ASP 616 609 609 ASP ASP A . n A 1 617 LYS 617 610 610 LYS LYS A . n A 1 618 ILE 618 611 611 ILE ILE A . n A 1 619 TYR 619 612 612 TYR TYR A . n A 1 620 SER 620 613 613 SER SER A . n A 1 621 ILE 621 614 614 ILE ILE A . n A 1 622 SER 622 615 615 SER SER A . n A 1 623 MET 623 616 616 MET MET A . n A 1 624 LYS 624 617 617 LYS LYS A . n A 1 625 HIS 625 618 618 HIS HIS A . n A 1 626 PRO 626 619 619 PRO PRO A . n A 1 627 GLN 627 620 620 GLN GLN A . n A 1 628 GLU 628 621 621 GLU GLU A . n A 1 629 MET 629 622 622 MET MET A . n A 1 630 LYS 630 623 623 LYS LYS A . n A 1 631 THR 631 624 624 THR THR A . n A 1 632 TYR 632 625 625 TYR TYR A . n A 1 633 SER 633 626 626 SER SER A . n A 1 634 VAL 634 627 627 VAL VAL A . n A 1 635 SER 635 628 628 SER SER A . n A 1 636 PHE 636 629 629 PHE PHE A . n A 1 637 ASP 637 630 630 ASP ASP A . n A 1 638 SER 638 631 631 SER SER A . n A 1 639 LEU 639 632 632 LEU LEU A . n A 1 640 PHE 640 633 633 PHE PHE A . n A 1 641 SER 641 634 634 SER SER A . n A 1 642 ALA 642 635 635 ALA ALA A . n A 1 643 VAL 643 636 636 VAL VAL A . n A 1 644 LYS 644 637 637 LYS LYS A . n A 1 645 ASN 645 638 638 ASN ASN A . n A 1 646 PHE 646 639 639 PHE PHE A . n A 1 647 THR 647 640 640 THR THR A . n A 1 648 GLU 648 641 641 GLU GLU A . n A 1 649 ILE 649 642 642 ILE ILE A . n A 1 650 ALA 650 643 643 ALA ALA A . n A 1 651 SER 651 644 644 SER SER A . n A 1 652 LYS 652 645 645 LYS LYS A . n A 1 653 PHE 653 646 646 PHE PHE A . n A 1 654 SER 654 647 647 SER SER A . n A 1 655 GLU 655 648 648 GLU GLU A . n A 1 656 ARG 656 649 649 ARG ARG A . n A 1 657 LEU 657 650 650 LEU LEU A . n A 1 658 GLN 658 651 651 GLN GLN A . n A 1 659 ASP 659 652 652 ASP ASP A . n A 1 660 PHE 660 653 653 PHE PHE A . n A 1 661 ASP 661 654 ? ? ? A . n A 1 662 LYS 662 655 ? ? ? A . n A 1 663 SER 663 656 656 SER SER A . n A 1 664 ASN 664 657 657 ASN ASN A . n A 1 665 PRO 665 658 658 PRO PRO A . n A 1 666 ILE 666 659 659 ILE ILE A . n A 1 667 VAL 667 660 660 VAL VAL A . n A 1 668 LEU 668 661 661 LEU LEU A . n A 1 669 ARG 669 662 662 ARG ARG A . n A 1 670 MET 670 663 663 MET MET A . n A 1 671 MET 671 664 664 MET MET A . n A 1 672 ASN 672 665 665 ASN ASN A . n A 1 673 ASP 673 666 666 ASP ASP A . n A 1 674 GLN 674 667 667 GLN GLN A . n A 1 675 LEU 675 668 668 LEU LEU A . n A 1 676 MET 676 669 669 MET MET A . n A 1 677 PHE 677 670 670 PHE PHE A . n A 1 678 LEU 678 671 671 LEU LEU A . n A 1 679 GLU 679 672 672 GLU GLU A . n A 1 680 ARG 680 673 673 ARG ARG A . n A 1 681 ALA 681 674 674 ALA ALA A . n A 1 682 PHE 682 675 675 PHE PHE A . n A 1 683 ILE 683 676 676 ILE ILE A . n A 1 684 ASP 684 677 677 ASP ASP A . n A 1 685 PRO 685 678 678 PRO PRO A . n A 1 686 LEU 686 679 679 LEU LEU A . n A 1 687 GLY 687 680 680 GLY GLY A . n A 1 688 LEU 688 681 681 LEU LEU A . n A 1 689 PRO 689 682 682 PRO PRO A . n A 1 690 ASP 690 683 683 ASP ASP A . n A 1 691 ARG 691 684 684 ARG ARG A . n A 1 692 PRO 692 685 685 PRO PRO A . n A 1 693 PHE 693 686 686 PHE PHE A . n A 1 694 TYR 694 687 687 TYR TYR A . n A 1 695 ARG 695 688 688 ARG ARG A . n A 1 696 HIS 696 689 689 HIS HIS A . n A 1 697 VAL 697 690 690 VAL VAL A . n A 1 698 ILE 698 691 691 ILE ILE A . n A 1 699 TYR 699 692 692 TYR TYR A . n A 1 700 ALA 700 693 693 ALA ALA A . n A 1 701 PRO 701 694 694 PRO PRO A . n A 1 702 SER 702 695 695 SER SER A . n A 1 703 SER 703 696 696 SER SER A . n A 1 704 HIS 704 697 697 HIS HIS A . n A 1 705 ASN 705 698 698 ASN ASN A . n A 1 706 LYS 706 699 699 LYS LYS A . n A 1 707 TYR 707 700 700 TYR TYR A . n A 1 708 ALA 708 701 701 ALA ALA A . n A 1 709 GLY 709 702 702 GLY GLY A . n A 1 710 GLU 710 703 703 GLU GLU A . n A 1 711 SER 711 704 704 SER SER A . n A 1 712 PHE 712 705 705 PHE PHE A . n A 1 713 PRO 713 706 706 PRO PRO A . n A 1 714 GLY 714 707 707 GLY GLY A . n A 1 715 ILE 715 708 708 ILE ILE A . n A 1 716 TYR 716 709 709 TYR TYR A . n A 1 717 ASP 717 710 710 ASP ASP A . n A 1 718 ALA 718 711 711 ALA ALA A . n A 1 719 LEU 719 712 712 LEU LEU A . n A 1 720 PHE 720 713 713 PHE PHE A . n A 1 721 ASP 721 714 714 ASP ASP A . n A 1 722 ILE 722 715 715 ILE ILE A . n A 1 723 GLU 723 716 716 GLU GLU A . n A 1 724 SER 724 717 717 SER SER A . n A 1 725 LYS 725 718 718 LYS LYS A . n A 1 726 VAL 726 719 719 VAL VAL A . n A 1 727 ASP 727 720 720 ASP ASP A . n A 1 728 PRO 728 721 721 PRO PRO A . n A 1 729 SER 729 722 722 SER SER A . n A 1 730 LYS 730 723 723 LYS LYS A . n A 1 731 ALA 731 724 724 ALA ALA A . n A 1 732 TRP 732 725 725 TRP TRP A . n A 1 733 GLY 733 726 726 GLY GLY A . n A 1 734 GLU 734 727 727 GLU GLU A . n A 1 735 VAL 735 728 728 VAL VAL A . n A 1 736 LYS 736 729 729 LYS LYS A . n A 1 737 ARG 737 730 730 ARG ARG A . n A 1 738 GLN 738 731 731 GLN GLN A . n A 1 739 ILE 739 732 732 ILE ILE A . n A 1 740 TYR 740 733 733 TYR TYR A . n A 1 741 VAL 741 734 734 VAL VAL A . n A 1 742 ALA 742 735 735 ALA ALA A . n A 1 743 ALA 743 736 736 ALA ALA A . n A 1 744 PHE 744 737 737 PHE PHE A . n A 1 745 THR 745 738 738 THR THR A . n A 1 746 VAL 746 739 739 VAL VAL A . n A 1 747 GLN 747 740 740 GLN GLN A . n A 1 748 ALA 748 741 741 ALA ALA A . n A 1 749 ALA 749 742 742 ALA ALA A . n A 1 750 ALA 750 743 743 ALA ALA A . n A 1 751 GLU 751 744 744 GLU GLU A . n A 1 752 THR 752 745 745 THR THR A . n A 1 753 LEU 753 746 746 LEU LEU A . n A 1 754 SER 754 747 747 SER SER A . n A 1 755 GLU 755 748 748 GLU GLU A . n A 1 756 VAL 756 749 749 VAL VAL A . n A 1 757 ALA 757 750 750 ALA ALA A . n # _pdbx_molecule_features.prd_id PRD_001165 _pdbx_molecule_features.name 'N-(4-{[(2-AMINO-4-OXO-3,4-DIHYDROPTERIDIN-6-YL)METHYL]AMINO}BENZOYL)-L-GAMMA-GLUTAMYL-L-GLUTAMIC ACID' _pdbx_molecule_features.type Peptide-like _pdbx_molecule_features.class Inhibitor _pdbx_molecule_features.details ? # _pdbx_molecule.instance_id 1 _pdbx_molecule.prd_id PRD_001165 _pdbx_molecule.asym_id S # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 645 A ASN 638 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 83 A ASN 76 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 483 A ASN 476 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 147 A ASN 140 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 128 A ASN 121 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 466 A ASN 459 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 202 A ASN 195 ? ASN 'GLYCOSYLATION SITE' # _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 1,2 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T # 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)' 11790 ? 1 MORE -57 ? 1 'SSA (A^2)' 49820 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_565 -x,-y+1,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 130.1760000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? T HOH . ? A HOH 1345 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD2 ? A ASP 460 ? A ASP 453 ? 1_555 114.3 ? 2 O ? T HOH . ? A HOH 1345 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD1 ? A ASP 394 ? A ASP 387 ? 1_555 105.7 ? 3 OD2 ? A ASP 460 ? A ASP 453 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD1 ? A ASP 394 ? A ASP 387 ? 1_555 120.1 ? 4 O ? T HOH . ? A HOH 1345 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 NE2 ? A HIS 384 ? A HIS 377 ? 1_555 108.4 ? 5 OD2 ? A ASP 460 ? A ASP 453 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 NE2 ? A HIS 384 ? A HIS 377 ? 1_555 100.8 ? 6 OD1 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 NE2 ? A HIS 384 ? A HIS 377 ? 1_555 106.8 ? 7 O ? T HOH . ? A HOH 1345 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 162.9 ? 8 O ? T HOH . ? A HOH 1345 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 96.2 ? 9 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 91.3 ? 10 O ? T HOH . ? A HOH 1345 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 94.3 ? 11 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 99.6 ? 12 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 99.3 ? 13 O ? T HOH . ? A HOH 1345 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 89.6 ? 14 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 89.8 ? 15 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 155.6 ? 16 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 56.6 ? 17 O ? T HOH . ? A HOH 1345 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAE ? S 28Z . ? A 28Z 818 ? 1_555 77.7 ? 18 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAE ? S 28Z . ? A 28Z 818 ? 1_555 85.4 ? 19 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAE ? S 28Z . ? A 28Z 818 ? 1_555 106.9 ? 20 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAE ? S 28Z . ? A 28Z 818 ? 1_555 153.2 ? 21 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAE ? S 28Z . ? A 28Z 818 ? 1_555 97.5 ? 22 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A TYR 279 ? A TYR 272 ? 1_555 81.5 ? 23 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 97.2 ? 24 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 145.8 ? 25 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A THR 276 ? A THR 269 ? 1_555 103.8 ? 26 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A THR 276 ? A THR 269 ? 1_555 73.5 ? 27 O ? T HOH . ? A HOH 906 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A THR 276 ? A THR 269 ? 1_555 73.7 ? 28 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 92.6 ? 29 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 86.2 ? 30 O ? T HOH . ? A HOH 906 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 127.9 ? 31 O ? A THR 276 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 151.3 ? 32 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 172.5 ? 33 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 91.0 ? 34 O ? T HOH . ? A HOH 906 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 88.6 ? 35 O ? A THR 276 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 73.3 ? 36 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 87.4 ? 37 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 88.0 ? 38 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 137.4 ? 39 O ? T HOH . ? A HOH 906 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 76.3 ? 40 O ? A THR 276 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 148.9 ? 41 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 53.0 ? 42 OG1 ? A THR 276 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 98.0 ? # 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 2014-06-18 2 'Structure model' 1 1 2014-08-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 17.6674 _pdbx_refine_tls.origin_y 49.7597 _pdbx_refine_tls.origin_z 44.5849 _pdbx_refine_tls.T[1][1] 0.0228 _pdbx_refine_tls.T[2][2] 0.0422 _pdbx_refine_tls.T[3][3] 0.0480 _pdbx_refine_tls.T[1][2] 0.0147 _pdbx_refine_tls.T[1][3] 0.0047 _pdbx_refine_tls.T[2][3] -0.0250 _pdbx_refine_tls.L[1][1] 0.5685 _pdbx_refine_tls.L[2][2] 0.8945 _pdbx_refine_tls.L[3][3] 0.3011 _pdbx_refine_tls.L[1][2] -0.2929 _pdbx_refine_tls.L[1][3] 0.0228 _pdbx_refine_tls.L[2][3] 0.0623 _pdbx_refine_tls.S[1][1] -0.0647 _pdbx_refine_tls.S[2][2] 0.0717 _pdbx_refine_tls.S[3][3] -0.0071 _pdbx_refine_tls.S[1][2] 0.0216 _pdbx_refine_tls.S[1][3] -0.0357 _pdbx_refine_tls.S[2][3] -0.1622 _pdbx_refine_tls.S[2][1] 0.0206 _pdbx_refine_tls.S[3][1] 0.0288 _pdbx_refine_tls.S[3][2] 0.0574 # 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.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection_details _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection 'X-RAY DIFFRACTION' 1 1 A 56 A 750 ? . . . . ? 'X-RAY DIFFRACTION' 2 1 A 801 A 818 ? . . . . ? 'X-RAY DIFFRACTION' 3 1 A 901 A 1568 ? . . . . ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal SERGUI 'data collection' . ? 1 REFMAC refinement . ? 2 HKL-2000 'data reduction' . ? 3 HKL-2000 'data scaling' . ? 4 REFMAC phasing . ? 5 # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 NH1 _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 ARG _pdbx_validate_close_contact.auth_seq_id_1 688 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 B _pdbx_validate_close_contact.auth_atom_id_2 O _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 HOH _pdbx_validate_close_contact.auth_seq_id_2 969 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.05 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 OE2 _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 GLU _pdbx_validate_symm_contact.auth_seq_id_1 276 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 D _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O2 _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 BMA _pdbx_validate_symm_contact.auth_seq_id_2 816 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 2_565 _pdbx_validate_symm_contact.dist 2.10 # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 CB _pdbx_validate_rmsd_bond.auth_asym_id_1 A _pdbx_validate_rmsd_bond.auth_comp_id_1 GLU _pdbx_validate_rmsd_bond.auth_seq_id_1 557 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 CG _pdbx_validate_rmsd_bond.auth_asym_id_2 A _pdbx_validate_rmsd_bond.auth_comp_id_2 GLU _pdbx_validate_rmsd_bond.auth_seq_id_2 557 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.401 _pdbx_validate_rmsd_bond.bond_target_value 1.517 _pdbx_validate_rmsd_bond.bond_deviation -0.116 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.019 _pdbx_validate_rmsd_bond.linker_flag N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 NE A ARG 440 ? ? CZ A ARG 440 ? ? NH2 A ARG 440 ? ? 117.25 120.30 -3.05 0.50 N 2 1 NE A ARG 688 ? B CZ A ARG 688 ? B NH2 A ARG 688 ? B 123.44 120.30 3.14 0.50 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 PHE A 164 ? ? 86.55 5.80 2 1 ASN A 178 ? ? 57.35 -126.22 3 1 LYS A 207 ? ? 71.93 -47.59 4 1 VAL A 382 ? ? -130.86 -107.22 5 1 ALA A 452 ? ? -155.78 57.91 6 1 ASP A 453 ? ? -83.60 -158.10 7 1 SER A 454 ? ? -35.83 124.71 8 1 SER A 454 ? ? -37.08 125.40 9 1 PHE A 525 ? ? -90.37 -65.52 10 1 PHE A 525 ? ? -90.37 -63.60 11 1 TRP A 541 ? ? -78.48 39.48 12 1 GLU A 542 ? ? -141.40 -45.61 13 1 SER A 547 ? ? 55.44 135.18 14 1 ASP A 567 ? ? -153.29 66.46 15 1 ASN A 698 ? ? -169.56 98.56 16 1 PHE A 705 ? ? 38.77 56.41 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A MET -6 ? A MET 1 2 1 Y 1 A LYS -5 ? A LYS 2 3 1 Y 1 A LEU -4 ? A LEU 3 4 1 Y 1 A CYS -3 ? A CYS 4 5 1 Y 1 A ILE -2 ? A ILE 5 6 1 Y 1 A LEU -1 ? A LEU 6 7 1 Y 1 A LEU 0 ? A LEU 7 8 1 Y 1 A ALA 1 ? A ALA 8 9 1 Y 1 A VAL 2 ? A VAL 9 10 1 Y 1 A VAL 3 ? A VAL 10 11 1 Y 1 A ALA 4 ? A ALA 11 12 1 Y 1 A PHE 5 ? A PHE 12 13 1 Y 1 A VAL 6 ? A VAL 13 14 1 Y 1 A GLY 7 ? A GLY 14 15 1 Y 1 A LEU 8 ? A LEU 15 16 1 Y 1 A SER 9 ? A SER 16 17 1 Y 1 A LEU 10 ? A LEU 17 18 1 Y 1 A GLY 11 ? A GLY 18 19 1 Y 1 A ARG 12 ? A ARG 19 20 1 Y 1 A SER 13 ? A SER 20 21 1 Y 1 A GLY 14 ? A GLY 21 22 1 Y 1 A LEU 15 ? A LEU 22 23 1 Y 1 A ASN 16 ? A ASN 23 24 1 Y 1 A ASP 17 ? A ASP 24 25 1 Y 1 A ILE 18 ? A ILE 25 26 1 Y 1 A PHE 19 ? A PHE 26 27 1 Y 1 A GLU 20 ? A GLU 27 28 1 Y 1 A ALA 21 ? A ALA 28 29 1 Y 1 A GLN 22 ? A GLN 29 30 1 Y 1 A LYS 23 ? A LYS 30 31 1 Y 1 A ILE 24 ? A ILE 31 32 1 Y 1 A GLU 25 ? A GLU 32 33 1 Y 1 A TRP 26 ? A TRP 33 34 1 Y 1 A HIS 27 ? A HIS 34 35 1 Y 1 A GLU 28 ? A GLU 35 36 1 Y 1 A GLY 29 ? A GLY 36 37 1 Y 1 A SER 30 ? A SER 37 38 1 Y 1 A GLY 31 ? A GLY 38 39 1 Y 1 A SER 32 ? A SER 39 40 1 Y 1 A GLY 33 ? A GLY 40 41 1 Y 1 A SER 34 ? A SER 41 42 1 Y 1 A GLU 35 ? A GLU 42 43 1 Y 1 A ASN 36 ? A ASN 43 44 1 Y 1 A LEU 37 ? A LEU 44 45 1 Y 1 A TYR 38 ? A TYR 45 46 1 Y 1 A PHE 39 ? A PHE 46 47 1 Y 1 A GLN 40 ? A GLN 47 48 1 Y 1 A GLY 41 ? A GLY 48 49 1 Y 1 A ARG 42 ? A ARG 49 50 1 Y 1 A SER 43 ? A SER 50 51 1 Y 1 A LYS 44 ? A LYS 51 52 1 Y 1 A SER 45 ? A SER 52 53 1 Y 1 A SER 46 ? A SER 53 54 1 Y 1 A ASN 47 ? A ASN 54 55 1 Y 1 A GLU 48 ? A GLU 55 56 1 Y 1 A ALA 49 ? A ALA 56 57 1 Y 1 A THR 50 ? A THR 57 58 1 Y 1 A ASN 51 ? A ASN 58 59 1 Y 1 A ILE 52 ? A ILE 59 60 1 Y 1 A THR 53 ? A THR 60 61 1 Y 1 A PRO 54 ? A PRO 61 62 1 Y 1 A LYS 55 ? A LYS 62 63 1 Y 1 A ASP 654 ? A ASP 661 64 1 Y 1 A LYS 655 ? A LYS 662 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'ZINC ION' ZN 3 'CALCIUM ION' CA 4 'CHLORIDE ION' CL 5 N-ACETYL-D-GLUCOSAMINE NAG 6 BETA-D-MANNOSE BMA 7 ALPHA-D-MANNOSE MAN 8 'N-(4-{[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino}benzoyl)-L-gamma-glutamyl-L-glutamic acid' 28Z 9 water HOH # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 ZN 1 801 1751 ZN ZN A . C 2 ZN 1 802 1752 ZN ZN A . D 3 CA 1 803 1753 CA CA A . E 4 CL 1 804 1754 CL CL A . F 5 NAG 1 805 1755 NAG NAG A . G 5 NAG 2 806 1756 NAG NAG A . H 5 NAG 1 807 1757 NAG NAG A . I 5 NAG 1 808 1758 NAG NAG A . J 5 NAG 2 809 1767 NAG NAG A . K 5 NAG 1 810 1759 NAG NAG A . L 5 NAG 1 811 1760 NAG NAG A . M 5 NAG 1 812 1761 NAG NAG A . N 5 NAG 2 813 1762 NAG NAG A . O 5 NAG 1 814 1763 NAG NAG A . P 5 NAG 2 815 1764 NAG NAG A . Q 6 BMA 3 816 1765 BMA BMA A . R 7 MAN 4 817 1766 MAN MAN A . S 8 28Z 1 818 1 28Z DRG A . T 9 HOH 1 901 1 HOH HOH A . T 9 HOH 2 902 2 HOH HOH A . T 9 HOH 3 903 3 HOH HOH A . T 9 HOH 4 904 4 HOH HOH A . T 9 HOH 5 905 5 HOH HOH A . T 9 HOH 6 906 6 HOH HOH A . T 9 HOH 7 907 7 HOH HOH A . T 9 HOH 8 908 8 HOH HOH A . T 9 HOH 9 909 9 HOH HOH A . T 9 HOH 10 910 10 HOH HOH A . T 9 HOH 11 911 11 HOH HOH A . T 9 HOH 12 912 12 HOH HOH A . T 9 HOH 13 913 13 HOH HOH A . T 9 HOH 14 914 14 HOH HOH A . T 9 HOH 15 915 15 HOH HOH A . T 9 HOH 16 916 16 HOH HOH A . T 9 HOH 17 917 17 HOH HOH A . T 9 HOH 18 918 18 HOH HOH A . T 9 HOH 19 919 19 HOH HOH A . T 9 HOH 20 920 20 HOH HOH A . T 9 HOH 21 921 21 HOH HOH A . T 9 HOH 22 922 22 HOH HOH A . T 9 HOH 23 923 23 HOH HOH A . T 9 HOH 24 924 24 HOH HOH A . T 9 HOH 25 925 25 HOH HOH A . T 9 HOH 26 926 26 HOH HOH A . T 9 HOH 27 927 27 HOH HOH A . T 9 HOH 28 928 28 HOH HOH A . T 9 HOH 29 929 29 HOH HOH A . T 9 HOH 30 930 30 HOH HOH A . T 9 HOH 31 931 31 HOH HOH A . T 9 HOH 32 932 32 HOH HOH A . T 9 HOH 33 933 33 HOH HOH A . T 9 HOH 34 934 34 HOH HOH A . T 9 HOH 35 935 35 HOH HOH A . T 9 HOH 36 936 36 HOH HOH A . T 9 HOH 37 937 37 HOH HOH A . T 9 HOH 38 938 38 HOH HOH A . T 9 HOH 39 939 40 HOH HOH A . T 9 HOH 40 940 41 HOH HOH A . T 9 HOH 41 941 42 HOH HOH A . T 9 HOH 42 942 43 HOH HOH A . T 9 HOH 43 943 44 HOH HOH A . T 9 HOH 44 944 45 HOH HOH A . T 9 HOH 45 945 46 HOH HOH A . T 9 HOH 46 946 47 HOH HOH A . T 9 HOH 47 947 48 HOH HOH A . T 9 HOH 48 948 49 HOH HOH A . T 9 HOH 49 949 50 HOH HOH A . T 9 HOH 50 950 51 HOH HOH A . T 9 HOH 51 951 52 HOH HOH A . T 9 HOH 52 952 53 HOH HOH A . T 9 HOH 53 953 54 HOH HOH A . T 9 HOH 54 954 55 HOH HOH A . T 9 HOH 55 955 56 HOH HOH A . T 9 HOH 56 956 57 HOH HOH A . T 9 HOH 57 957 58 HOH HOH A . T 9 HOH 58 958 59 HOH HOH A . T 9 HOH 59 959 60 HOH HOH A . T 9 HOH 60 960 61 HOH HOH A . T 9 HOH 61 961 62 HOH HOH A . T 9 HOH 62 962 63 HOH HOH A . T 9 HOH 63 963 64 HOH HOH A . T 9 HOH 64 964 65 HOH HOH A . T 9 HOH 65 965 66 HOH HOH A . T 9 HOH 66 966 67 HOH HOH A . T 9 HOH 67 967 68 HOH HOH A . T 9 HOH 68 968 69 HOH HOH A . T 9 HOH 69 969 70 HOH HOH A . T 9 HOH 70 970 71 HOH HOH A . T 9 HOH 71 971 72 HOH HOH A . T 9 HOH 72 972 73 HOH HOH A . T 9 HOH 73 973 74 HOH HOH A . T 9 HOH 74 974 75 HOH HOH A . T 9 HOH 75 975 76 HOH HOH A . T 9 HOH 76 976 77 HOH HOH A . T 9 HOH 77 977 78 HOH HOH A . T 9 HOH 78 978 79 HOH HOH A . T 9 HOH 79 979 80 HOH HOH A . T 9 HOH 80 980 81 HOH HOH A . T 9 HOH 81 981 82 HOH HOH A . T 9 HOH 82 982 83 HOH HOH A . T 9 HOH 83 983 84 HOH HOH A . T 9 HOH 84 984 85 HOH HOH A . T 9 HOH 85 985 86 HOH HOH A . T 9 HOH 86 986 87 HOH HOH A . T 9 HOH 87 987 88 HOH HOH A . T 9 HOH 88 988 90 HOH HOH A . T 9 HOH 89 989 91 HOH HOH A . T 9 HOH 90 990 92 HOH HOH A . T 9 HOH 91 991 93 HOH HOH A . T 9 HOH 92 992 94 HOH HOH A . T 9 HOH 93 993 95 HOH HOH A . T 9 HOH 94 994 96 HOH HOH A . T 9 HOH 95 995 97 HOH HOH A . T 9 HOH 96 996 98 HOH HOH A . T 9 HOH 97 997 99 HOH HOH A . T 9 HOH 98 998 100 HOH HOH A . T 9 HOH 99 999 101 HOH HOH A . T 9 HOH 100 1000 102 HOH HOH A . T 9 HOH 101 1001 103 HOH HOH A . T 9 HOH 102 1002 104 HOH HOH A . T 9 HOH 103 1003 105 HOH HOH A . T 9 HOH 104 1004 106 HOH HOH A . T 9 HOH 105 1005 107 HOH HOH A . T 9 HOH 106 1006 108 HOH HOH A . T 9 HOH 107 1007 109 HOH HOH A . T 9 HOH 108 1008 110 HOH HOH A . T 9 HOH 109 1009 112 HOH HOH A . T 9 HOH 110 1010 113 HOH HOH A . T 9 HOH 111 1011 114 HOH HOH A . T 9 HOH 112 1012 115 HOH HOH A . T 9 HOH 113 1013 116 HOH HOH A . T 9 HOH 114 1014 117 HOH HOH A . T 9 HOH 115 1015 118 HOH HOH A . T 9 HOH 116 1016 119 HOH HOH A . T 9 HOH 117 1017 120 HOH HOH A . T 9 HOH 118 1018 121 HOH HOH A . T 9 HOH 119 1019 122 HOH HOH A . T 9 HOH 120 1020 123 HOH HOH A . T 9 HOH 121 1021 125 HOH HOH A . T 9 HOH 122 1022 126 HOH HOH A . T 9 HOH 123 1023 127 HOH HOH A . T 9 HOH 124 1024 128 HOH HOH A . T 9 HOH 125 1025 129 HOH HOH A . T 9 HOH 126 1026 130 HOH HOH A . T 9 HOH 127 1027 131 HOH HOH A . T 9 HOH 128 1028 132 HOH HOH A . T 9 HOH 129 1029 133 HOH HOH A . T 9 HOH 130 1030 135 HOH HOH A . T 9 HOH 131 1031 136 HOH HOH A . T 9 HOH 132 1032 137 HOH HOH A . T 9 HOH 133 1033 138 HOH HOH A . T 9 HOH 134 1034 139 HOH HOH A . T 9 HOH 135 1035 140 HOH HOH A . T 9 HOH 136 1036 141 HOH HOH A . T 9 HOH 137 1037 142 HOH HOH A . T 9 HOH 138 1038 143 HOH HOH A . T 9 HOH 139 1039 144 HOH HOH A . T 9 HOH 140 1040 145 HOH HOH A . T 9 HOH 141 1041 146 HOH HOH A . T 9 HOH 142 1042 147 HOH HOH A . T 9 HOH 143 1043 148 HOH HOH A . T 9 HOH 144 1044 149 HOH HOH A . T 9 HOH 145 1045 150 HOH HOH A . T 9 HOH 146 1046 151 HOH HOH A . T 9 HOH 147 1047 152 HOH HOH A . T 9 HOH 148 1048 153 HOH HOH A . T 9 HOH 149 1049 154 HOH HOH A . T 9 HOH 150 1050 155 HOH HOH A . T 9 HOH 151 1051 156 HOH HOH A . T 9 HOH 152 1052 157 HOH HOH A . T 9 HOH 153 1053 158 HOH HOH A . T 9 HOH 154 1054 159 HOH HOH A . T 9 HOH 155 1055 160 HOH HOH A . T 9 HOH 156 1056 161 HOH HOH A . T 9 HOH 157 1057 162 HOH HOH A . T 9 HOH 158 1058 163 HOH HOH A . T 9 HOH 159 1059 164 HOH HOH A . T 9 HOH 160 1060 166 HOH HOH A . T 9 HOH 161 1061 167 HOH HOH A . T 9 HOH 162 1062 168 HOH HOH A . T 9 HOH 163 1063 169 HOH HOH A . T 9 HOH 164 1064 173 HOH HOH A . T 9 HOH 165 1065 175 HOH HOH A . T 9 HOH 166 1066 176 HOH HOH A . T 9 HOH 167 1067 177 HOH HOH A . T 9 HOH 168 1068 178 HOH HOH A . T 9 HOH 169 1069 179 HOH HOH A . T 9 HOH 170 1070 180 HOH HOH A . T 9 HOH 171 1071 181 HOH HOH A . T 9 HOH 172 1072 182 HOH HOH A . T 9 HOH 173 1073 183 HOH HOH A . T 9 HOH 174 1074 184 HOH HOH A . T 9 HOH 175 1075 185 HOH HOH A . T 9 HOH 176 1076 186 HOH HOH A . T 9 HOH 177 1077 187 HOH HOH A . T 9 HOH 178 1078 188 HOH HOH A . T 9 HOH 179 1079 189 HOH HOH A . T 9 HOH 180 1080 190 HOH HOH A . T 9 HOH 181 1081 191 HOH HOH A . T 9 HOH 182 1082 193 HOH HOH A . T 9 HOH 183 1083 195 HOH HOH A . T 9 HOH 184 1084 197 HOH HOH A . T 9 HOH 185 1085 198 HOH HOH A . T 9 HOH 186 1086 199 HOH HOH A . T 9 HOH 187 1087 202 HOH HOH A . T 9 HOH 188 1088 203 HOH HOH A . T 9 HOH 189 1089 204 HOH HOH A . T 9 HOH 190 1090 205 HOH HOH A . T 9 HOH 191 1091 206 HOH HOH A . T 9 HOH 192 1092 207 HOH HOH A . T 9 HOH 193 1093 208 HOH HOH A . T 9 HOH 194 1094 209 HOH HOH A . T 9 HOH 195 1095 210 HOH HOH A . T 9 HOH 196 1096 211 HOH HOH A . T 9 HOH 197 1097 213 HOH HOH A . T 9 HOH 198 1098 214 HOH HOH A . T 9 HOH 199 1099 215 HOH HOH A . T 9 HOH 200 1100 217 HOH HOH A . T 9 HOH 201 1101 220 HOH HOH A . T 9 HOH 202 1102 222 HOH HOH A . T 9 HOH 203 1103 223 HOH HOH A . T 9 HOH 204 1104 224 HOH HOH A . T 9 HOH 205 1105 226 HOH HOH A . T 9 HOH 206 1106 227 HOH HOH A . T 9 HOH 207 1107 228 HOH HOH A . T 9 HOH 208 1108 229 HOH HOH A . T 9 HOH 209 1109 230 HOH HOH A . T 9 HOH 210 1110 231 HOH HOH A . T 9 HOH 211 1111 232 HOH HOH A . T 9 HOH 212 1112 233 HOH HOH A . T 9 HOH 213 1113 234 HOH HOH A . T 9 HOH 214 1114 235 HOH HOH A . T 9 HOH 215 1115 236 HOH HOH A . T 9 HOH 216 1116 237 HOH HOH A . T 9 HOH 217 1117 238 HOH HOH A . T 9 HOH 218 1118 239 HOH HOH A . T 9 HOH 219 1119 240 HOH HOH A . T 9 HOH 220 1120 244 HOH HOH A . T 9 HOH 221 1121 245 HOH HOH A . T 9 HOH 222 1122 246 HOH HOH A . T 9 HOH 223 1123 247 HOH HOH A . T 9 HOH 224 1124 248 HOH HOH A . T 9 HOH 225 1125 249 HOH HOH A . T 9 HOH 226 1126 250 HOH HOH A . T 9 HOH 227 1127 251 HOH HOH A . T 9 HOH 228 1128 252 HOH HOH A . T 9 HOH 229 1129 253 HOH HOH A . T 9 HOH 230 1130 254 HOH HOH A . T 9 HOH 231 1131 258 HOH HOH A . T 9 HOH 232 1132 262 HOH HOH A . T 9 HOH 233 1133 263 HOH HOH A . T 9 HOH 234 1134 264 HOH HOH A . T 9 HOH 235 1135 265 HOH HOH A . T 9 HOH 236 1136 267 HOH HOH A . T 9 HOH 237 1137 268 HOH HOH A . T 9 HOH 238 1138 271 HOH HOH A . T 9 HOH 239 1139 272 HOH HOH A . T 9 HOH 240 1140 276 HOH HOH A . T 9 HOH 241 1141 277 HOH HOH A . T 9 HOH 242 1142 278 HOH HOH A . T 9 HOH 243 1143 279 HOH HOH A . T 9 HOH 244 1144 280 HOH HOH A . T 9 HOH 245 1145 282 HOH HOH A . T 9 HOH 246 1146 283 HOH HOH A . T 9 HOH 247 1147 284 HOH HOH A . T 9 HOH 248 1148 285 HOH HOH A . T 9 HOH 249 1149 288 HOH HOH A . T 9 HOH 250 1150 292 HOH HOH A . T 9 HOH 251 1151 293 HOH HOH A . T 9 HOH 252 1152 294 HOH HOH A . T 9 HOH 253 1153 295 HOH HOH A . T 9 HOH 254 1154 296 HOH HOH A . T 9 HOH 255 1155 297 HOH HOH A . T 9 HOH 256 1156 301 HOH HOH A . T 9 HOH 257 1157 304 HOH HOH A . T 9 HOH 258 1158 305 HOH HOH A . T 9 HOH 259 1159 306 HOH HOH A . T 9 HOH 260 1160 309 HOH HOH A . T 9 HOH 261 1161 310 HOH HOH A . T 9 HOH 262 1162 311 HOH HOH A . T 9 HOH 263 1163 314 HOH HOH A . T 9 HOH 264 1164 315 HOH HOH A . T 9 HOH 265 1165 316 HOH HOH A . T 9 HOH 266 1166 317 HOH HOH A . T 9 HOH 267 1167 321 HOH HOH A . T 9 HOH 268 1168 324 HOH HOH A . T 9 HOH 269 1169 325 HOH HOH A . T 9 HOH 270 1170 326 HOH HOH A . T 9 HOH 271 1171 329 HOH HOH A . T 9 HOH 272 1172 330 HOH HOH A . T 9 HOH 273 1173 331 HOH HOH A . T 9 HOH 274 1174 333 HOH HOH A . T 9 HOH 275 1175 336 HOH HOH A . T 9 HOH 276 1176 339 HOH HOH A . T 9 HOH 277 1177 340 HOH HOH A . T 9 HOH 278 1178 342 HOH HOH A . T 9 HOH 279 1179 345 HOH HOH A . T 9 HOH 280 1180 346 HOH HOH A . T 9 HOH 281 1181 350 HOH HOH A . T 9 HOH 282 1182 351 HOH HOH A . T 9 HOH 283 1183 352 HOH HOH A . T 9 HOH 284 1184 357 HOH HOH A . T 9 HOH 285 1185 358 HOH HOH A . T 9 HOH 286 1186 365 HOH HOH A . T 9 HOH 287 1187 366 HOH HOH A . T 9 HOH 288 1188 370 HOH HOH A . T 9 HOH 289 1189 371 HOH HOH A . T 9 HOH 290 1190 373 HOH HOH A . T 9 HOH 291 1191 375 HOH HOH A . T 9 HOH 292 1192 376 HOH HOH A . T 9 HOH 293 1193 377 HOH HOH A . T 9 HOH 294 1194 379 HOH HOH A . T 9 HOH 295 1195 381 HOH HOH A . T 9 HOH 296 1196 383 HOH HOH A . T 9 HOH 297 1197 384 HOH HOH A . T 9 HOH 298 1198 385 HOH HOH A . T 9 HOH 299 1199 391 HOH HOH A . T 9 HOH 300 1200 396 HOH HOH A . T 9 HOH 301 1201 402 HOH HOH A . T 9 HOH 302 1202 405 HOH HOH A . T 9 HOH 303 1203 406 HOH HOH A . T 9 HOH 304 1204 407 HOH HOH A . T 9 HOH 305 1205 412 HOH HOH A . T 9 HOH 306 1206 416 HOH HOH A . T 9 HOH 307 1207 418 HOH HOH A . T 9 HOH 308 1208 419 HOH HOH A . T 9 HOH 309 1209 420 HOH HOH A . T 9 HOH 310 1210 421 HOH HOH A . T 9 HOH 311 1211 422 HOH HOH A . T 9 HOH 312 1212 423 HOH HOH A . T 9 HOH 313 1213 424 HOH HOH A . T 9 HOH 314 1214 426 HOH HOH A . T 9 HOH 315 1215 430 HOH HOH A . T 9 HOH 316 1216 433 HOH HOH A . T 9 HOH 317 1217 435 HOH HOH A . T 9 HOH 318 1218 436 HOH HOH A . T 9 HOH 319 1219 437 HOH HOH A . T 9 HOH 320 1220 438 HOH HOH A . T 9 HOH 321 1221 439 HOH HOH A . T 9 HOH 322 1222 442 HOH HOH A . T 9 HOH 323 1223 443 HOH HOH A . T 9 HOH 324 1224 444 HOH HOH A . T 9 HOH 325 1225 446 HOH HOH A . T 9 HOH 326 1226 450 HOH HOH A . T 9 HOH 327 1227 451 HOH HOH A . T 9 HOH 328 1228 455 HOH HOH A . T 9 HOH 329 1229 456 HOH HOH A . T 9 HOH 330 1230 462 HOH HOH A . T 9 HOH 331 1231 465 HOH HOH A . T 9 HOH 332 1232 468 HOH HOH A . T 9 HOH 333 1233 475 HOH HOH A . T 9 HOH 334 1234 480 HOH HOH A . T 9 HOH 335 1235 482 HOH HOH A . T 9 HOH 336 1236 485 HOH HOH A . T 9 HOH 337 1237 487 HOH HOH A . T 9 HOH 338 1238 493 HOH HOH A . T 9 HOH 339 1239 494 HOH HOH A . T 9 HOH 340 1240 495 HOH HOH A . T 9 HOH 341 1241 497 HOH HOH A . T 9 HOH 342 1242 505 HOH HOH A . T 9 HOH 343 1243 509 HOH HOH A . T 9 HOH 344 1244 510 HOH HOH A . T 9 HOH 345 1245 517 HOH HOH A . T 9 HOH 346 1246 519 HOH HOH A . T 9 HOH 347 1247 529 HOH HOH A . T 9 HOH 348 1248 536 HOH HOH A . T 9 HOH 349 1249 543 HOH HOH A . T 9 HOH 350 1250 549 HOH HOH A . T 9 HOH 351 1251 566 HOH HOH A . T 9 HOH 352 1252 582 HOH HOH A . T 9 HOH 353 1253 583 HOH HOH A . T 9 HOH 354 1254 584 HOH HOH A . T 9 HOH 355 1255 586 HOH HOH A . T 9 HOH 356 1256 587 HOH HOH A . T 9 HOH 357 1257 589 HOH HOH A . T 9 HOH 358 1258 590 HOH HOH A . T 9 HOH 359 1259 599 HOH HOH A . T 9 HOH 360 1260 611 HOH HOH A . T 9 HOH 361 1261 635 HOH HOH A . T 9 HOH 362 1262 668 HOH HOH A . T 9 HOH 363 1263 671 HOH HOH A . T 9 HOH 364 1264 672 HOH HOH A . T 9 HOH 365 1265 673 HOH HOH A . T 9 HOH 366 1266 679 HOH HOH A . T 9 HOH 367 1267 680 HOH HOH A . T 9 HOH 368 1268 681 HOH HOH A . T 9 HOH 369 1269 682 HOH HOH A . T 9 HOH 370 1270 691 HOH HOH A . T 9 HOH 371 1271 694 HOH HOH A . T 9 HOH 372 1272 695 HOH HOH A . T 9 HOH 373 1273 697 HOH HOH A . T 9 HOH 374 1274 698 HOH HOH A . T 9 HOH 375 1275 699 HOH HOH A . T 9 HOH 376 1276 701 HOH HOH A . T 9 HOH 377 1277 702 HOH HOH A . T 9 HOH 378 1278 703 HOH HOH A . T 9 HOH 379 1279 705 HOH HOH A . T 9 HOH 380 1280 706 HOH HOH A . T 9 HOH 381 1281 707 HOH HOH A . T 9 HOH 382 1282 709 HOH HOH A . T 9 HOH 383 1283 710 HOH HOH A . T 9 HOH 384 1284 711 HOH HOH A . T 9 HOH 385 1285 712 HOH HOH A . T 9 HOH 386 1286 714 HOH HOH A . T 9 HOH 387 1287 715 HOH HOH A . T 9 HOH 388 1288 716 HOH HOH A . T 9 HOH 389 1289 717 HOH HOH A . T 9 HOH 390 1290 718 HOH HOH A . T 9 HOH 391 1291 719 HOH HOH A . T 9 HOH 392 1292 720 HOH HOH A . T 9 HOH 393 1293 721 HOH HOH A . T 9 HOH 394 1294 723 HOH HOH A . T 9 HOH 395 1295 726 HOH HOH A . T 9 HOH 396 1296 727 HOH HOH A . T 9 HOH 397 1297 728 HOH HOH A . T 9 HOH 398 1298 729 HOH HOH A . T 9 HOH 399 1299 730 HOH HOH A . T 9 HOH 400 1300 732 HOH HOH A . T 9 HOH 401 1301 733 HOH HOH A . T 9 HOH 402 1302 734 HOH HOH A . T 9 HOH 403 1303 738 HOH HOH A . T 9 HOH 404 1304 739 HOH HOH A . T 9 HOH 405 1305 740 HOH HOH A . T 9 HOH 406 1306 741 HOH HOH A . T 9 HOH 407 1307 742 HOH HOH A . T 9 HOH 408 1308 743 HOH HOH A . T 9 HOH 409 1309 744 HOH HOH A . T 9 HOH 410 1310 745 HOH HOH A . T 9 HOH 411 1311 747 HOH HOH A . T 9 HOH 412 1312 749 HOH HOH A . T 9 HOH 413 1313 750 HOH HOH A . T 9 HOH 414 1314 751 HOH HOH A . T 9 HOH 415 1315 752 HOH HOH A . T 9 HOH 416 1316 755 HOH HOH A . T 9 HOH 417 1317 758 HOH HOH A . T 9 HOH 418 1318 759 HOH HOH A . T 9 HOH 419 1319 760 HOH HOH A . T 9 HOH 420 1320 761 HOH HOH A . T 9 HOH 421 1321 762 HOH HOH A . T 9 HOH 422 1322 763 HOH HOH A . T 9 HOH 423 1323 764 HOH HOH A . T 9 HOH 424 1324 765 HOH HOH A . T 9 HOH 425 1325 766 HOH HOH A . T 9 HOH 426 1326 767 HOH HOH A . T 9 HOH 427 1327 768 HOH HOH A . T 9 HOH 428 1328 769 HOH HOH A . T 9 HOH 429 1329 771 HOH HOH A . T 9 HOH 430 1330 772 HOH HOH A . T 9 HOH 431 1331 773 HOH HOH A . T 9 HOH 432 1332 774 HOH HOH A . T 9 HOH 433 1333 775 HOH HOH A . T 9 HOH 434 1334 776 HOH HOH A . T 9 HOH 435 1335 777 HOH HOH A . T 9 HOH 436 1336 779 HOH HOH A . T 9 HOH 437 1337 780 HOH HOH A . T 9 HOH 438 1338 781 HOH HOH A . T 9 HOH 439 1339 782 HOH HOH A . T 9 HOH 440 1340 783 HOH HOH A . T 9 HOH 441 1341 784 HOH HOH A . T 9 HOH 442 1342 785 HOH HOH A . T 9 HOH 443 1343 786 HOH HOH A . T 9 HOH 444 1344 787 HOH HOH A . T 9 HOH 445 1345 788 HOH HOH A . T 9 HOH 446 1346 789 HOH HOH A . T 9 HOH 447 1347 790 HOH HOH A . T 9 HOH 448 1348 791 HOH HOH A . T 9 HOH 449 1349 792 HOH HOH A . T 9 HOH 450 1350 793 HOH HOH A . T 9 HOH 451 1351 794 HOH HOH A . T 9 HOH 452 1352 796 HOH HOH A . T 9 HOH 453 1353 798 HOH HOH A . T 9 HOH 454 1354 799 HOH HOH A . T 9 HOH 455 1355 800 HOH HOH A . T 9 HOH 456 1356 801 HOH HOH A . T 9 HOH 457 1357 802 HOH HOH A . T 9 HOH 458 1358 803 HOH HOH A . T 9 HOH 459 1359 804 HOH HOH A . T 9 HOH 460 1360 807 HOH HOH A . T 9 HOH 461 1361 808 HOH HOH A . T 9 HOH 462 1362 809 HOH HOH A . T 9 HOH 463 1363 810 HOH HOH A . T 9 HOH 464 1364 811 HOH HOH A . T 9 HOH 465 1365 812 HOH HOH A . T 9 HOH 466 1366 813 HOH HOH A . T 9 HOH 467 1367 814 HOH HOH A . T 9 HOH 468 1368 815 HOH HOH A . T 9 HOH 469 1369 817 HOH HOH A . T 9 HOH 470 1370 818 HOH HOH A . T 9 HOH 471 1371 819 HOH HOH A . T 9 HOH 472 1372 820 HOH HOH A . T 9 HOH 473 1373 821 HOH HOH A . T 9 HOH 474 1374 822 HOH HOH A . T 9 HOH 475 1375 823 HOH HOH A . T 9 HOH 476 1376 824 HOH HOH A . T 9 HOH 477 1377 825 HOH HOH A . T 9 HOH 478 1378 826 HOH HOH A . T 9 HOH 479 1379 828 HOH HOH A . T 9 HOH 480 1380 829 HOH HOH A . T 9 HOH 481 1381 830 HOH HOH A . T 9 HOH 482 1382 831 HOH HOH A . T 9 HOH 483 1383 832 HOH HOH A . T 9 HOH 484 1384 834 HOH HOH A . T 9 HOH 485 1385 835 HOH HOH A . T 9 HOH 486 1386 836 HOH HOH A . T 9 HOH 487 1387 837 HOH HOH A . T 9 HOH 488 1388 838 HOH HOH A . T 9 HOH 489 1389 839 HOH HOH A . T 9 HOH 490 1390 840 HOH HOH A . T 9 HOH 491 1391 841 HOH HOH A . T 9 HOH 492 1392 842 HOH HOH A . T 9 HOH 493 1393 843 HOH HOH A . T 9 HOH 494 1394 844 HOH HOH A . T 9 HOH 495 1395 846 HOH HOH A . T 9 HOH 496 1396 847 HOH HOH A . T 9 HOH 497 1397 848 HOH HOH A . T 9 HOH 498 1398 849 HOH HOH A . T 9 HOH 499 1399 850 HOH HOH A . T 9 HOH 500 1400 851 HOH HOH A . T 9 HOH 501 1401 853 HOH HOH A . T 9 HOH 502 1402 854 HOH HOH A . T 9 HOH 503 1403 855 HOH HOH A . T 9 HOH 504 1404 857 HOH HOH A . T 9 HOH 505 1405 858 HOH HOH A . T 9 HOH 506 1406 859 HOH HOH A . T 9 HOH 507 1407 860 HOH HOH A . T 9 HOH 508 1408 862 HOH HOH A . T 9 HOH 509 1409 863 HOH HOH A . T 9 HOH 510 1410 865 HOH HOH A . T 9 HOH 511 1411 866 HOH HOH A . T 9 HOH 512 1412 867 HOH HOH A . T 9 HOH 513 1413 868 HOH HOH A . T 9 HOH 514 1414 869 HOH HOH A . T 9 HOH 515 1415 870 HOH HOH A . T 9 HOH 516 1416 871 HOH HOH A . T 9 HOH 517 1417 872 HOH HOH A . T 9 HOH 518 1418 873 HOH HOH A . T 9 HOH 519 1419 875 HOH HOH A . T 9 HOH 520 1420 877 HOH HOH A . T 9 HOH 521 1421 878 HOH HOH A . T 9 HOH 522 1422 879 HOH HOH A . T 9 HOH 523 1423 880 HOH HOH A . T 9 HOH 524 1424 881 HOH HOH A . T 9 HOH 525 1425 882 HOH HOH A . T 9 HOH 526 1426 883 HOH HOH A . T 9 HOH 527 1427 884 HOH HOH A . T 9 HOH 528 1428 885 HOH HOH A . T 9 HOH 529 1429 886 HOH HOH A . T 9 HOH 530 1430 888 HOH HOH A . T 9 HOH 531 1431 889 HOH HOH A . T 9 HOH 532 1432 890 HOH HOH A . T 9 HOH 533 1433 891 HOH HOH A . T 9 HOH 534 1434 892 HOH HOH A . T 9 HOH 535 1435 893 HOH HOH A . T 9 HOH 536 1436 894 HOH HOH A . T 9 HOH 537 1437 895 HOH HOH A . T 9 HOH 538 1438 897 HOH HOH A . T 9 HOH 539 1439 898 HOH HOH A . T 9 HOH 540 1440 899 HOH HOH A . T 9 HOH 541 1441 900 HOH HOH A . T 9 HOH 542 1442 901 HOH HOH A . T 9 HOH 543 1443 902 HOH HOH A . T 9 HOH 544 1444 903 HOH HOH A . T 9 HOH 545 1445 904 HOH HOH A . T 9 HOH 546 1446 905 HOH HOH A . T 9 HOH 547 1447 906 HOH HOH A . T 9 HOH 548 1448 907 HOH HOH A . T 9 HOH 549 1449 908 HOH HOH A . T 9 HOH 550 1450 909 HOH HOH A . T 9 HOH 551 1451 910 HOH HOH A . T 9 HOH 552 1452 911 HOH HOH A . T 9 HOH 553 1453 912 HOH HOH A . T 9 HOH 554 1454 913 HOH HOH A . T 9 HOH 555 1455 914 HOH HOH A . T 9 HOH 556 1456 915 HOH HOH A . T 9 HOH 557 1457 916 HOH HOH A . T 9 HOH 558 1458 917 HOH HOH A . T 9 HOH 559 1459 918 HOH HOH A . T 9 HOH 560 1460 919 HOH HOH A . T 9 HOH 561 1461 920 HOH HOH A . T 9 HOH 562 1462 922 HOH HOH A . T 9 HOH 563 1463 923 HOH HOH A . T 9 HOH 564 1464 924 HOH HOH A . T 9 HOH 565 1465 926 HOH HOH A . T 9 HOH 566 1466 927 HOH HOH A . T 9 HOH 567 1467 928 HOH HOH A . T 9 HOH 568 1468 929 HOH HOH A . T 9 HOH 569 1469 930 HOH HOH A . T 9 HOH 570 1470 931 HOH HOH A . T 9 HOH 571 1471 932 HOH HOH A . T 9 HOH 572 1472 933 HOH HOH A . T 9 HOH 573 1473 934 HOH HOH A . T 9 HOH 574 1474 935 HOH HOH A . T 9 HOH 575 1475 937 HOH HOH A . T 9 HOH 576 1476 938 HOH HOH A . T 9 HOH 577 1477 939 HOH HOH A . T 9 HOH 578 1478 942 HOH HOH A . T 9 HOH 579 1479 943 HOH HOH A . T 9 HOH 580 1480 945 HOH HOH A . T 9 HOH 581 1481 949 HOH HOH A . T 9 HOH 582 1482 952 HOH HOH A . T 9 HOH 583 1483 953 HOH HOH A . T 9 HOH 584 1484 954 HOH HOH A . T 9 HOH 585 1485 955 HOH HOH A . T 9 HOH 586 1486 956 HOH HOH A . T 9 HOH 587 1487 958 HOH HOH A . T 9 HOH 588 1488 959 HOH HOH A . T 9 HOH 589 1489 960 HOH HOH A . T 9 HOH 590 1490 961 HOH HOH A . T 9 HOH 591 1491 962 HOH HOH A . T 9 HOH 592 1492 963 HOH HOH A . T 9 HOH 593 1493 966 HOH HOH A . T 9 HOH 594 1494 967 HOH HOH A . T 9 HOH 595 1495 968 HOH HOH A . T 9 HOH 596 1496 969 HOH HOH A . T 9 HOH 597 1497 970 HOH HOH A . T 9 HOH 598 1498 971 HOH HOH A . T 9 HOH 599 1499 972 HOH HOH A . T 9 HOH 600 1500 973 HOH HOH A . T 9 HOH 601 1501 974 HOH HOH A . T 9 HOH 602 1502 975 HOH HOH A . T 9 HOH 603 1503 976 HOH HOH A . T 9 HOH 604 1504 977 HOH HOH A . T 9 HOH 605 1505 978 HOH HOH A . T 9 HOH 606 1506 980 HOH HOH A . T 9 HOH 607 1507 982 HOH HOH A . T 9 HOH 608 1508 983 HOH HOH A . T 9 HOH 609 1509 984 HOH HOH A . T 9 HOH 610 1510 988 HOH HOH A . T 9 HOH 611 1511 989 HOH HOH A . T 9 HOH 612 1512 991 HOH HOH A . T 9 HOH 613 1513 992 HOH HOH A . T 9 HOH 614 1514 993 HOH HOH A . T 9 HOH 615 1515 994 HOH HOH A . T 9 HOH 616 1516 995 HOH HOH A . T 9 HOH 617 1517 996 HOH HOH A . T 9 HOH 618 1518 997 HOH HOH A . T 9 HOH 619 1519 998 HOH HOH A . T 9 HOH 620 1520 1000 HOH HOH A . T 9 HOH 621 1521 1003 HOH HOH A . T 9 HOH 622 1522 1004 HOH HOH A . T 9 HOH 623 1523 1005 HOH HOH A . T 9 HOH 624 1524 1006 HOH HOH A . T 9 HOH 625 1525 1007 HOH HOH A . T 9 HOH 626 1526 1008 HOH HOH A . T 9 HOH 627 1527 1009 HOH HOH A . T 9 HOH 628 1528 1010 HOH HOH A . T 9 HOH 629 1529 1011 HOH HOH A . T 9 HOH 630 1530 1012 HOH HOH A . T 9 HOH 631 1531 1013 HOH HOH A . T 9 HOH 632 1532 1014 HOH HOH A . T 9 HOH 633 1533 1015 HOH HOH A . T 9 HOH 634 1534 1016 HOH HOH A . T 9 HOH 635 1535 1017 HOH HOH A . T 9 HOH 636 1536 1018 HOH HOH A . T 9 HOH 637 1537 1019 HOH HOH A . T 9 HOH 638 1538 1020 HOH HOH A . T 9 HOH 639 1539 1021 HOH HOH A . T 9 HOH 640 1540 1022 HOH HOH A . T 9 HOH 641 1541 1023 HOH HOH A . T 9 HOH 642 1542 1024 HOH HOH A . T 9 HOH 643 1543 1025 HOH HOH A . T 9 HOH 644 1544 1026 HOH HOH A . T 9 HOH 645 1545 1027 HOH HOH A . T 9 HOH 646 1546 1028 HOH HOH A . T 9 HOH 647 1547 1029 HOH HOH A . T 9 HOH 648 1548 1030 HOH HOH A . T 9 HOH 649 1549 1031 HOH HOH A . T 9 HOH 650 1550 1032 HOH HOH A . T 9 HOH 651 1551 1033 HOH HOH A . T 9 HOH 652 1552 1034 HOH HOH A . T 9 HOH 653 1553 1036 HOH HOH A . T 9 HOH 654 1554 1037 HOH HOH A . T 9 HOH 655 1555 1038 HOH HOH A . T 9 HOH 656 1556 1039 HOH HOH A . T 9 HOH 657 1557 1040 HOH HOH A . T 9 HOH 658 1558 1041 HOH HOH A . T 9 HOH 659 1559 1042 HOH HOH A . T 9 HOH 660 1560 1043 HOH HOH A . T 9 HOH 661 1561 1044 HOH HOH A . T 9 HOH 662 1562 1045 HOH HOH A . T 9 HOH 663 1563 1046 HOH HOH A . T 9 HOH 664 1564 1047 HOH HOH A . T 9 HOH 665 1565 1048 HOH HOH A . T 9 HOH 666 1566 1049 HOH HOH A . T 9 HOH 667 1567 1050 HOH HOH A . T 9 HOH 668 1568 1051 HOH HOH A . #