data_3FEC # _entry.id 3FEC # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3FEC RCSB RCSB050484 WWPDB D_1000050484 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3FF3 . unspecified PDB 3FED . unspecified PDB 3FEE . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3FEC _pdbx_database_status.recvd_initial_deposition_date 2008-11-28 _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.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Barinka, C.' 1 'Lubkowski, J.' 2 'Hlouchova, K.' 3 # _citation.id primary _citation.title 'Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III' _citation.journal_abbrev 'Febs J.' _citation.journal_volume 276 _citation.page_first 4448 _citation.page_last 4462 _citation.year 2009 _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 19678840 _citation.pdbx_database_id_DOI 10.1111/j.1742-4658.2009.07152.x # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Hlouchova, K.' 1 primary 'Barinka, C.' 2 primary 'Konvalinka, J.' 3 primary 'Lubkowski, J.' 4 # _cell.entry_id 3FEC _cell.length_a 122.767 _cell.length_b 104.322 _cell.length_c 78.008 _cell.angle_alpha 90.00 _cell.angle_beta 107.69 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _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 3FEC _symmetry.space_group_name_H-M 'C 1 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 5 _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 III' 79940.578 1 3.4.17.21 ? 'Extracellular domain' ? 2 non-polymer syn 'GLUTAMIC ACID' 147.129 1 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 5 ? ? ? ? 4 non-polymer syn 'ZINC ION' 65.409 2 ? ? ? ? 5 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 6 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 7 non-polymer syn GLYCEROL 92.094 2 ? ? ? ? 8 non-polymer syn '3[N-MORPHOLINO]PROPANE SULFONIC ACID' 209.263 1 ? ? ? ? 9 water nat water 18.015 727 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'GCPIII, N-acetylated-alpha-linked acidic dipeptidase 2, N-acetylated-alpha-linked acidic dipeptidase II, NAALADase II' # _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 ;RSETTTSVRYHQSIRWKLVSEMKAENIKSFLRSFTKLPHLAGTEQNFLLAKKIQTQWKKFGLDSAKLVHYDVLLSYPNET NANYISIVDEHETEIFKTSYLEPPPDGYENVTNIVPPYNAFSAQGMPEGDLVYVNYARTEDFFKLEREMGINCTGKIVIA RYGKIFRGNKVKNAMLAGAIGIILYSDPADYFAPEVQPYPKGWNLPGTAAQRGNVLNLNGAGDPLTPGYPAKEYTFRLDV EEGVGIPRIPVHPIGYNDAEILLRYLGGIAPPDKSWKGALNVSYSIGPGFTGSDSFRKVRMHVYNINKITRIYNVVGTIR GSVEPDRYVILGGHRDSWVFGAIDPTSGVAVLQEIARSFGKLMSKGWRPRRTIIFASWDAEEFGLLGSTEWAEENVKILQ ERSIAYINSDSSIEGNYTLRVDCTPLLYQLVYKLTKEIPSPDDGFESKSLYESWLEKDPSPENKNLPRINKLGSGSDFEA YFQRLGIASGRARYTKNKKTDKYSSYPVYHTIYETFELVEKFYDPTFKKQLSVAQLRGALVYELVDSKIIPFNIQDYAEA LKNYAASIYNLSKKHDQQLTDHGVSFDSLFSAVKNFSEAASDFHKRLIQVDLNNPIAVRMMNDQLMLLERAFIDPLGLPG KLFYRHIIFAPSSHNKYAGESFPGIYDAIFDIENKANSRLAWKEVKKHISIAAFTIQAAAGTLKEVL ; _entity_poly.pdbx_seq_one_letter_code_can ;RSETTTSVRYHQSIRWKLVSEMKAENIKSFLRSFTKLPHLAGTEQNFLLAKKIQTQWKKFGLDSAKLVHYDVLLSYPNET NANYISIVDEHETEIFKTSYLEPPPDGYENVTNIVPPYNAFSAQGMPEGDLVYVNYARTEDFFKLEREMGINCTGKIVIA RYGKIFRGNKVKNAMLAGAIGIILYSDPADYFAPEVQPYPKGWNLPGTAAQRGNVLNLNGAGDPLTPGYPAKEYTFRLDV EEGVGIPRIPVHPIGYNDAEILLRYLGGIAPPDKSWKGALNVSYSIGPGFTGSDSFRKVRMHVYNINKITRIYNVVGTIR GSVEPDRYVILGGHRDSWVFGAIDPTSGVAVLQEIARSFGKLMSKGWRPRRTIIFASWDAEEFGLLGSTEWAEENVKILQ ERSIAYINSDSSIEGNYTLRVDCTPLLYQLVYKLTKEIPSPDDGFESKSLYESWLEKDPSPENKNLPRINKLGSGSDFEA YFQRLGIASGRARYTKNKKTDKYSSYPVYHTIYETFELVEKFYDPTFKKQLSVAQLRGALVYELVDSKIIPFNIQDYAEA LKNYAASIYNLSKKHDQQLTDHGVSFDSLFSAVKNFSEAASDFHKRLIQVDLNNPIAVRMMNDQLMLLERAFIDPLGLPG KLFYRHIIFAPSSHNKYAGESFPGIYDAIFDIENKANSRLAWKEVKKHISIAAFTIQAAAGTLKEVL ; _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 ARG n 1 2 SER n 1 3 GLU n 1 4 THR n 1 5 THR n 1 6 THR n 1 7 SER n 1 8 VAL n 1 9 ARG n 1 10 TYR n 1 11 HIS n 1 12 GLN n 1 13 SER n 1 14 ILE n 1 15 ARG n 1 16 TRP n 1 17 LYS n 1 18 LEU n 1 19 VAL n 1 20 SER n 1 21 GLU n 1 22 MET n 1 23 LYS n 1 24 ALA n 1 25 GLU n 1 26 ASN n 1 27 ILE n 1 28 LYS n 1 29 SER n 1 30 PHE n 1 31 LEU n 1 32 ARG n 1 33 SER n 1 34 PHE n 1 35 THR n 1 36 LYS n 1 37 LEU n 1 38 PRO n 1 39 HIS n 1 40 LEU n 1 41 ALA n 1 42 GLY n 1 43 THR n 1 44 GLU n 1 45 GLN n 1 46 ASN n 1 47 PHE n 1 48 LEU n 1 49 LEU n 1 50 ALA n 1 51 LYS n 1 52 LYS n 1 53 ILE n 1 54 GLN n 1 55 THR n 1 56 GLN n 1 57 TRP n 1 58 LYS n 1 59 LYS n 1 60 PHE n 1 61 GLY n 1 62 LEU n 1 63 ASP n 1 64 SER n 1 65 ALA n 1 66 LYS n 1 67 LEU n 1 68 VAL n 1 69 HIS n 1 70 TYR n 1 71 ASP n 1 72 VAL n 1 73 LEU n 1 74 LEU n 1 75 SER n 1 76 TYR n 1 77 PRO n 1 78 ASN n 1 79 GLU n 1 80 THR n 1 81 ASN n 1 82 ALA n 1 83 ASN n 1 84 TYR n 1 85 ILE n 1 86 SER n 1 87 ILE n 1 88 VAL n 1 89 ASP n 1 90 GLU n 1 91 HIS n 1 92 GLU n 1 93 THR n 1 94 GLU n 1 95 ILE n 1 96 PHE n 1 97 LYS n 1 98 THR n 1 99 SER n 1 100 TYR n 1 101 LEU n 1 102 GLU n 1 103 PRO n 1 104 PRO n 1 105 PRO n 1 106 ASP n 1 107 GLY n 1 108 TYR n 1 109 GLU n 1 110 ASN n 1 111 VAL n 1 112 THR n 1 113 ASN n 1 114 ILE n 1 115 VAL n 1 116 PRO n 1 117 PRO n 1 118 TYR n 1 119 ASN n 1 120 ALA n 1 121 PHE n 1 122 SER n 1 123 ALA n 1 124 GLN n 1 125 GLY n 1 126 MET n 1 127 PRO n 1 128 GLU n 1 129 GLY n 1 130 ASP n 1 131 LEU n 1 132 VAL n 1 133 TYR n 1 134 VAL n 1 135 ASN n 1 136 TYR n 1 137 ALA n 1 138 ARG n 1 139 THR n 1 140 GLU n 1 141 ASP n 1 142 PHE n 1 143 PHE n 1 144 LYS n 1 145 LEU n 1 146 GLU n 1 147 ARG n 1 148 GLU n 1 149 MET n 1 150 GLY n 1 151 ILE n 1 152 ASN n 1 153 CYS n 1 154 THR n 1 155 GLY n 1 156 LYS n 1 157 ILE n 1 158 VAL n 1 159 ILE n 1 160 ALA n 1 161 ARG n 1 162 TYR n 1 163 GLY n 1 164 LYS n 1 165 ILE n 1 166 PHE n 1 167 ARG n 1 168 GLY n 1 169 ASN n 1 170 LYS n 1 171 VAL n 1 172 LYS n 1 173 ASN n 1 174 ALA n 1 175 MET n 1 176 LEU n 1 177 ALA n 1 178 GLY n 1 179 ALA n 1 180 ILE n 1 181 GLY n 1 182 ILE n 1 183 ILE n 1 184 LEU n 1 185 TYR n 1 186 SER n 1 187 ASP n 1 188 PRO n 1 189 ALA n 1 190 ASP n 1 191 TYR n 1 192 PHE n 1 193 ALA n 1 194 PRO n 1 195 GLU n 1 196 VAL n 1 197 GLN n 1 198 PRO n 1 199 TYR n 1 200 PRO n 1 201 LYS n 1 202 GLY n 1 203 TRP n 1 204 ASN n 1 205 LEU n 1 206 PRO n 1 207 GLY n 1 208 THR n 1 209 ALA n 1 210 ALA n 1 211 GLN n 1 212 ARG n 1 213 GLY n 1 214 ASN n 1 215 VAL n 1 216 LEU n 1 217 ASN n 1 218 LEU n 1 219 ASN n 1 220 GLY n 1 221 ALA n 1 222 GLY n 1 223 ASP n 1 224 PRO n 1 225 LEU n 1 226 THR n 1 227 PRO n 1 228 GLY n 1 229 TYR n 1 230 PRO n 1 231 ALA n 1 232 LYS n 1 233 GLU n 1 234 TYR n 1 235 THR n 1 236 PHE n 1 237 ARG n 1 238 LEU n 1 239 ASP n 1 240 VAL n 1 241 GLU n 1 242 GLU n 1 243 GLY n 1 244 VAL n 1 245 GLY n 1 246 ILE n 1 247 PRO n 1 248 ARG n 1 249 ILE n 1 250 PRO n 1 251 VAL n 1 252 HIS n 1 253 PRO n 1 254 ILE n 1 255 GLY n 1 256 TYR n 1 257 ASN n 1 258 ASP n 1 259 ALA n 1 260 GLU n 1 261 ILE n 1 262 LEU n 1 263 LEU n 1 264 ARG n 1 265 TYR n 1 266 LEU n 1 267 GLY n 1 268 GLY n 1 269 ILE n 1 270 ALA n 1 271 PRO n 1 272 PRO n 1 273 ASP n 1 274 LYS n 1 275 SER n 1 276 TRP n 1 277 LYS n 1 278 GLY n 1 279 ALA n 1 280 LEU n 1 281 ASN n 1 282 VAL n 1 283 SER n 1 284 TYR n 1 285 SER n 1 286 ILE n 1 287 GLY n 1 288 PRO n 1 289 GLY n 1 290 PHE n 1 291 THR n 1 292 GLY n 1 293 SER n 1 294 ASP n 1 295 SER n 1 296 PHE n 1 297 ARG n 1 298 LYS n 1 299 VAL n 1 300 ARG n 1 301 MET n 1 302 HIS n 1 303 VAL n 1 304 TYR n 1 305 ASN n 1 306 ILE n 1 307 ASN n 1 308 LYS n 1 309 ILE n 1 310 THR n 1 311 ARG n 1 312 ILE n 1 313 TYR n 1 314 ASN n 1 315 VAL n 1 316 VAL n 1 317 GLY n 1 318 THR n 1 319 ILE n 1 320 ARG n 1 321 GLY n 1 322 SER n 1 323 VAL n 1 324 GLU n 1 325 PRO n 1 326 ASP n 1 327 ARG n 1 328 TYR n 1 329 VAL n 1 330 ILE n 1 331 LEU n 1 332 GLY n 1 333 GLY n 1 334 HIS n 1 335 ARG n 1 336 ASP n 1 337 SER n 1 338 TRP n 1 339 VAL n 1 340 PHE n 1 341 GLY n 1 342 ALA n 1 343 ILE n 1 344 ASP n 1 345 PRO n 1 346 THR n 1 347 SER n 1 348 GLY n 1 349 VAL n 1 350 ALA n 1 351 VAL n 1 352 LEU n 1 353 GLN n 1 354 GLU n 1 355 ILE n 1 356 ALA n 1 357 ARG n 1 358 SER n 1 359 PHE n 1 360 GLY n 1 361 LYS n 1 362 LEU n 1 363 MET n 1 364 SER n 1 365 LYS n 1 366 GLY n 1 367 TRP n 1 368 ARG n 1 369 PRO n 1 370 ARG n 1 371 ARG n 1 372 THR n 1 373 ILE n 1 374 ILE n 1 375 PHE n 1 376 ALA n 1 377 SER n 1 378 TRP n 1 379 ASP n 1 380 ALA n 1 381 GLU n 1 382 GLU n 1 383 PHE n 1 384 GLY n 1 385 LEU n 1 386 LEU n 1 387 GLY n 1 388 SER n 1 389 THR n 1 390 GLU n 1 391 TRP n 1 392 ALA n 1 393 GLU n 1 394 GLU n 1 395 ASN n 1 396 VAL n 1 397 LYS n 1 398 ILE n 1 399 LEU n 1 400 GLN n 1 401 GLU n 1 402 ARG n 1 403 SER n 1 404 ILE n 1 405 ALA n 1 406 TYR n 1 407 ILE n 1 408 ASN n 1 409 SER n 1 410 ASP n 1 411 SER n 1 412 SER n 1 413 ILE n 1 414 GLU n 1 415 GLY n 1 416 ASN n 1 417 TYR n 1 418 THR n 1 419 LEU n 1 420 ARG n 1 421 VAL n 1 422 ASP n 1 423 CYS n 1 424 THR n 1 425 PRO n 1 426 LEU n 1 427 LEU n 1 428 TYR n 1 429 GLN n 1 430 LEU n 1 431 VAL n 1 432 TYR n 1 433 LYS n 1 434 LEU n 1 435 THR n 1 436 LYS n 1 437 GLU n 1 438 ILE n 1 439 PRO n 1 440 SER n 1 441 PRO n 1 442 ASP n 1 443 ASP n 1 444 GLY n 1 445 PHE n 1 446 GLU n 1 447 SER n 1 448 LYS n 1 449 SER n 1 450 LEU n 1 451 TYR n 1 452 GLU n 1 453 SER n 1 454 TRP n 1 455 LEU n 1 456 GLU n 1 457 LYS n 1 458 ASP n 1 459 PRO n 1 460 SER n 1 461 PRO n 1 462 GLU n 1 463 ASN n 1 464 LYS n 1 465 ASN n 1 466 LEU n 1 467 PRO n 1 468 ARG n 1 469 ILE n 1 470 ASN n 1 471 LYS n 1 472 LEU n 1 473 GLY n 1 474 SER n 1 475 GLY n 1 476 SER n 1 477 ASP n 1 478 PHE n 1 479 GLU n 1 480 ALA n 1 481 TYR n 1 482 PHE n 1 483 GLN n 1 484 ARG n 1 485 LEU n 1 486 GLY n 1 487 ILE n 1 488 ALA n 1 489 SER n 1 490 GLY n 1 491 ARG n 1 492 ALA n 1 493 ARG n 1 494 TYR n 1 495 THR n 1 496 LYS n 1 497 ASN n 1 498 LYS n 1 499 LYS n 1 500 THR n 1 501 ASP n 1 502 LYS n 1 503 TYR n 1 504 SER n 1 505 SER n 1 506 TYR n 1 507 PRO n 1 508 VAL n 1 509 TYR n 1 510 HIS n 1 511 THR n 1 512 ILE n 1 513 TYR n 1 514 GLU n 1 515 THR n 1 516 PHE n 1 517 GLU n 1 518 LEU n 1 519 VAL n 1 520 GLU n 1 521 LYS n 1 522 PHE n 1 523 TYR n 1 524 ASP n 1 525 PRO n 1 526 THR n 1 527 PHE n 1 528 LYS n 1 529 LYS n 1 530 GLN n 1 531 LEU n 1 532 SER n 1 533 VAL n 1 534 ALA n 1 535 GLN n 1 536 LEU n 1 537 ARG n 1 538 GLY n 1 539 ALA n 1 540 LEU n 1 541 VAL n 1 542 TYR n 1 543 GLU n 1 544 LEU n 1 545 VAL n 1 546 ASP n 1 547 SER n 1 548 LYS n 1 549 ILE n 1 550 ILE n 1 551 PRO n 1 552 PHE n 1 553 ASN n 1 554 ILE n 1 555 GLN n 1 556 ASP n 1 557 TYR n 1 558 ALA n 1 559 GLU n 1 560 ALA n 1 561 LEU n 1 562 LYS n 1 563 ASN n 1 564 TYR n 1 565 ALA n 1 566 ALA n 1 567 SER n 1 568 ILE n 1 569 TYR n 1 570 ASN n 1 571 LEU n 1 572 SER n 1 573 LYS n 1 574 LYS n 1 575 HIS n 1 576 ASP n 1 577 GLN n 1 578 GLN n 1 579 LEU n 1 580 THR n 1 581 ASP n 1 582 HIS n 1 583 GLY n 1 584 VAL n 1 585 SER n 1 586 PHE n 1 587 ASP n 1 588 SER n 1 589 LEU n 1 590 PHE n 1 591 SER n 1 592 ALA n 1 593 VAL n 1 594 LYS n 1 595 ASN n 1 596 PHE n 1 597 SER n 1 598 GLU n 1 599 ALA n 1 600 ALA n 1 601 SER n 1 602 ASP n 1 603 PHE n 1 604 HIS n 1 605 LYS n 1 606 ARG n 1 607 LEU n 1 608 ILE n 1 609 GLN n 1 610 VAL n 1 611 ASP n 1 612 LEU n 1 613 ASN n 1 614 ASN n 1 615 PRO n 1 616 ILE n 1 617 ALA n 1 618 VAL n 1 619 ARG n 1 620 MET n 1 621 MET n 1 622 ASN n 1 623 ASP n 1 624 GLN n 1 625 LEU n 1 626 MET n 1 627 LEU n 1 628 LEU n 1 629 GLU n 1 630 ARG n 1 631 ALA n 1 632 PHE n 1 633 ILE n 1 634 ASP n 1 635 PRO n 1 636 LEU n 1 637 GLY n 1 638 LEU n 1 639 PRO n 1 640 GLY n 1 641 LYS n 1 642 LEU n 1 643 PHE n 1 644 TYR n 1 645 ARG n 1 646 HIS n 1 647 ILE n 1 648 ILE n 1 649 PHE n 1 650 ALA n 1 651 PRO n 1 652 SER n 1 653 SER n 1 654 HIS n 1 655 ASN n 1 656 LYS n 1 657 TYR n 1 658 ALA n 1 659 GLY n 1 660 GLU n 1 661 SER n 1 662 PHE n 1 663 PRO n 1 664 GLY n 1 665 ILE n 1 666 TYR n 1 667 ASP n 1 668 ALA n 1 669 ILE n 1 670 PHE n 1 671 ASP n 1 672 ILE n 1 673 GLU n 1 674 ASN n 1 675 LYS n 1 676 ALA n 1 677 ASN n 1 678 SER n 1 679 ARG n 1 680 LEU n 1 681 ALA n 1 682 TRP n 1 683 LYS n 1 684 GLU n 1 685 VAL n 1 686 LYS n 1 687 LYS n 1 688 HIS n 1 689 ILE n 1 690 SER n 1 691 ILE n 1 692 ALA n 1 693 ALA n 1 694 PHE n 1 695 THR n 1 696 ILE n 1 697 GLN n 1 698 ALA n 1 699 ALA n 1 700 ALA n 1 701 GLY n 1 702 THR n 1 703 LEU n 1 704 LYS n 1 705 GLU n 1 706 VAL n 1 707 LEU 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 man _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene NAALAD2 _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 NALD2_HUMAN _struct_ref.pdbx_db_accession Q9Y3Q0 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;ETTTSVRYHQSIRWKLVSEMKAENIKSFLRSFTKLPHLAGTEQNFLLAKKIQTQWKKFGLDSAKLVHYDVLLSYPNETNA NYISIVDEHETEIFKTSYLEPPPDGYENVTNIVPPYNAFSAQGMPEGDLVYVNYARTEDFFKLEREMGINCTGKIVIARY GKIFRGNKVKNAMLAGAIGIILYSDPADYFAPEVQPYPKGWNLPGTAAQRGNVLNLNGAGDPLTPGYPAKEYTFRLDVEE GVGIPRIPVHPIGYNDAEILLRYLGGIAPPDKSWKGALNVSYSIGPGFTGSDSFRKVRMHVYNINKITRIYNVVGTIRGS VEPDRYVILGGHRDSWVFGAIDPTSGVAVLQEIARSFGKLMSKGWRPRRTIIFASWDAEEFGLLGSTEWAEENVKILQER SIAYINSDSSIEGNYTLRVDCTPLLYQLVYKLTKEIPSPDDGFESKSLYESWLEKDPSPENKNLPRINKLGSGSDFEAYF QRLGIASGRARYTKNKKTDKYSSYPVYHTIYETFELVEKFYDPTFKKQLSVAQLRGALVYELVDSKIIPFNIQDYAEALK NYAASIYNLSKKHDQQLTDHGVSFDSLFSAVKNFSEAASDFHKRLIQVDLNNPIAVRMMNDQLMLLERAFIDPLGLPGKL FYRHIIFAPSSHNKYAGESFPGIYDAIFDIENKANSRLAWKEVKKHISIAAFTIQAAAGTLKEVL ; _struct_ref.pdbx_align_begin 36 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3FEC _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 3 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 707 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q9Y3Q0 _struct_ref_seq.db_align_beg 36 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 740 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 36 _struct_ref_seq.pdbx_auth_seq_align_end 740 # 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 3FEC ARG A 1 ? UNP Q9Y3Q0 ? ? 'EXPRESSION TAG' 34 1 1 3FEC SER A 2 ? UNP Q9Y3Q0 ? ? 'EXPRESSION TAG' 35 2 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 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 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 MPO non-polymer . '3[N-MORPHOLINO]PROPANE SULFONIC ACID' ? 'C7 H15 N O4 S' 209.263 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 3FEC _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.98 _exptl_crystal.density_percent_sol 58.68 _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 7.5 _exptl_crystal_grow.pdbx_details '0.1 M HEPES-Na, 10% (w/v) PEG6000, 5% (v/v) MPD, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K' _exptl_crystal_grow.pdbx_pH_range . # _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 2006-11-01 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.00 _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.entry_id 3FEC _reflns.observed_criterion_sigma_F -3 _reflns.observed_criterion_sigma_I -3 _reflns.d_resolution_high 1.49 _reflns.d_resolution_low 20 _reflns.number_all 148978 _reflns.number_obs 148978 _reflns.percent_possible_obs 98.7 _reflns.pdbx_Rmerge_I_obs 0.079 _reflns.pdbx_Rsym_value ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 4.9 _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.pdbx_netI_over_sigmaI ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.49 _reflns_shell.d_res_low 1.54 _reflns_shell.percent_possible_all 93.6 _reflns_shell.Rmerge_I_obs 0.525 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.0 _reflns_shell.pdbx_redundancy 3.4 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 14188 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 3FEC _refine.ls_number_reflns_obs 145908 _refine.ls_number_reflns_all ? _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 20.00 _refine.ls_d_res_high 1.49 _refine.ls_percent_reflns_obs 97.26 _refine.ls_R_factor_obs 0.15902 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.15852 _refine.ls_R_factor_R_free 0.18320 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 2.0 _refine.ls_number_reflns_R_free 2983 _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 0.964 _refine.B_iso_mean 24.402 _refine.aniso_B[1][1] -0.13 _refine.aniso_B[2][2] -0.29 _refine.aniso_B[3][3] 0.85 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.70 _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 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 'PDB entry 2OR4' _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 0.057 _refine.pdbx_overall_ESU_R_Free 0.059 _refine.overall_SU_ML 0.039 _refine.overall_SU_B 2.051 _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _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.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_TLS_residual_ADP_flag 'LIKELY RESIDUAL' _refine.pdbx_diffrn_id 1 _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 5497 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 109 _refine_hist.number_atoms_solvent 727 _refine_hist.number_atoms_total 6333 _refine_hist.d_res_high 1.49 _refine_hist.d_res_low 20.00 # 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 0.020 0.022 ? 6134 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.884 1.977 ? 8307 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.986 5.000 ? 723 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.643 23.912 ? 294 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 14.500 15.000 ? 1082 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 17.267 15.000 ? 40 'X-RAY DIFFRACTION' ? r_chiral_restr 0.140 0.200 ? 896 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.013 0.021 ? 4655 '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 1.117 1.500 ? 3589 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.809 2.000 ? 5855 'X-RAY DIFFRACTION' ? r_scbond_it 2.743 3.000 ? 2545 'X-RAY DIFFRACTION' ? r_scangle_it 4.289 4.500 ? 2447 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.49 _refine_ls_shell.d_res_low 1.526 _refine_ls_shell.number_reflns_R_work 9562 _refine_ls_shell.R_factor_R_work 0.218 _refine_ls_shell.percent_reflns_obs 86.77 _refine_ls_shell.R_factor_R_free 0.245 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 188 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 3FEC _struct.title 'Crystal structure of human Glutamate Carboxypeptidase III (GCPIII/NAALADase II), pseudo-unliganded' _struct.pdbx_descriptor 'Glutamate carboxypeptidase III (E.C.3.4.17.21)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3FEC _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text ;metallopeptidase; bimetallic active site; N-glycosylation; calcium cation; chloride anion; zinc ions;, Carboxypeptidase, Dipeptidase, Glycoprotein, Hydrolase, Membrane, Metal-binding, Metalloprotease, Multifunctional enzyme, Protease, Signal-anchor, Transmembrane ; # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 4 ? I N N 4 ? J N N 5 ? K N N 6 ? L N N 7 ? M N N 7 ? N N N 8 ? O 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 SER A 13 ? MET A 22 ? SER A 46 MET A 55 1 ? 10 HELX_P HELX_P2 2 LYS A 23 ? THR A 35 ? LYS A 56 THR A 68 1 ? 13 HELX_P HELX_P3 3 THR A 43 ? GLY A 61 ? THR A 76 GLY A 94 1 ? 19 HELX_P HELX_P4 4 ARG A 138 ? ARG A 147 ? ARG A 171 ARG A 180 1 ? 10 HELX_P HELX_P5 5 PHE A 166 ? ALA A 177 ? PHE A 199 ALA A 210 1 ? 12 HELX_P HELX_P6 6 ASP A 187 ? PHE A 192 ? ASP A 220 PHE A 225 1 ? 6 HELX_P HELX_P7 7 ASP A 239 ? GLY A 243 ? ASP A 272 GLY A 276 5 ? 5 HELX_P HELX_P8 8 GLY A 255 ? ARG A 264 ? GLY A 288 ARG A 297 1 ? 10 HELX_P HELX_P9 9 ASP A 273 ? LYS A 277 ? ASP A 306 LYS A 310 5 ? 5 HELX_P HELX_P10 10 PRO A 345 ? LYS A 365 ? PRO A 378 LYS A 398 1 ? 21 HELX_P HELX_P11 11 ALA A 380 ? GLY A 384 ? ALA A 413 GLY A 417 5 ? 5 HELX_P HELX_P12 12 LEU A 385 ? ARG A 402 ? LEU A 418 ARG A 435 1 ? 18 HELX_P HELX_P13 13 LEU A 427 ? LYS A 436 ? LEU A 460 LYS A 469 1 ? 10 HELX_P HELX_P14 14 SER A 449 ? ASP A 458 ? SER A 482 ASP A 491 1 ? 10 HELX_P HELX_P15 15 PHE A 478 ? ARG A 484 ? PHE A 511 ARG A 517 1 ? 7 HELX_P HELX_P16 16 THR A 515 ? TYR A 523 ? THR A 548 TYR A 556 1 ? 9 HELX_P HELX_P17 17 PHE A 527 ? SER A 547 ? PHE A 560 SER A 580 1 ? 21 HELX_P HELX_P18 18 ASN A 553 ? LYS A 573 ? ASN A 586 LYS A 606 1 ? 21 HELX_P HELX_P19 19 HIS A 575 ? HIS A 582 ? HIS A 608 HIS A 615 1 ? 8 HELX_P HELX_P20 20 PHE A 586 ? ILE A 608 ? PHE A 619 ILE A 641 1 ? 23 HELX_P HELX_P21 21 ASN A 614 ? PHE A 632 ? ASN A 647 PHE A 665 1 ? 19 HELX_P HELX_P22 22 PHE A 662 ? PHE A 670 ? PHE A 695 PHE A 703 1 ? 9 HELX_P HELX_P23 23 ASP A 671 ? LYS A 675 ? ASP A 704 LYS A 708 5 ? 5 HELX_P HELX_P24 24 ASN A 677 ? LYS A 704 ? ASN A 710 LYS A 737 1 ? 28 # _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 78 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 111 A NAG 1756 1_555 ? ? ? ? ? ? ? 1.461 ? covale2 covale ? ? A ASN 152 ND2 A ? ? 1_555 G NAG . C1 ? ? A ASN 185 A NAG 1766 1_555 ? ? ? ? ? ? ? 1.388 ? covale3 covale ? ? A ASN 152 ND2 B ? ? 1_555 G NAG . C1 ? ? A ASN 185 A NAG 1766 1_555 ? ? ? ? ? ? ? 1.525 ? metalc1 metalc ? ? A THR 226 O ? ? ? 1_555 K CA . CA ? ? A THR 259 A CA 1755 1_555 ? ? ? ? ? ? ? 2.478 ? metalc2 metalc ? ? A THR 226 OG1 ? ? ? 1_555 K CA . CA ? ? A THR 259 A CA 1755 1_555 ? ? ? ? ? ? ? 2.485 ? metalc3 metalc ? ? A TYR 229 O ? ? ? 1_555 K CA . CA ? ? A TYR 262 A CA 1755 1_555 ? ? ? ? ? ? ? 2.356 ? metalc4 metalc ? ? A HIS 334 NE2 ? ? ? 1_555 I ZN . ZN A ? A HIS 367 A ZN 1752 1_555 ? ? ? ? ? ? ? 2.151 ? metalc5 metalc ? ? A HIS 334 NE2 ? ? ? 1_555 I ZN . ZN B ? A HIS 367 A ZN 1752 1_555 ? ? ? ? ? ? ? 2.013 ? metalc6 metalc ? ? A ASP 344 OD1 ? ? ? 1_555 I ZN . ZN A ? A ASP 377 A ZN 1752 1_555 ? ? ? ? ? ? ? 2.064 ? metalc7 metalc ? ? A ASP 344 OD1 ? ? ? 1_555 I ZN . ZN B ? A ASP 377 A ZN 1752 1_555 ? ? ? ? ? ? ? 1.966 ? metalc8 metalc ? ? A ASP 344 OD2 ? ? ? 1_555 H ZN . ZN A ? A ASP 377 A ZN 1751 1_555 ? ? ? ? ? ? ? 2.073 ? metalc9 metalc ? ? A ASP 344 OD2 ? ? ? 1_555 H ZN . ZN B ? A ASP 377 A ZN 1751 1_555 ? ? ? ? ? ? ? 1.953 ? metalc10 metalc ? ? A GLU 382 OE2 ? ? ? 1_555 H ZN . ZN A ? A GLU 415 A ZN 1751 1_555 ? ? ? ? ? ? ? 2.274 ? metalc11 metalc ? ? A GLU 382 OE2 ? ? ? 1_555 H ZN . ZN B ? A GLU 415 A ZN 1751 1_555 ? ? ? ? ? ? ? 1.921 ? metalc12 metalc ? ? A GLU 390 OE1 ? ? ? 1_555 K CA . CA ? ? A GLU 423 A CA 1755 1_555 ? ? ? ? ? ? ? 2.438 ? metalc13 metalc ? ? A GLU 390 OE2 ? ? ? 1_555 K CA . CA ? ? A GLU 423 A CA 1755 1_555 ? ? ? ? ? ? ? 2.445 ? metalc14 metalc ? ? A GLU 393 OE2 ? ? ? 1_555 K CA . CA ? ? A GLU 426 A CA 1755 1_555 ? ? ? ? ? ? ? 2.286 ? metalc15 metalc ? ? A ASP 410 OD1 ? ? ? 1_555 I ZN . ZN A ? A ASP 443 A ZN 1752 1_555 ? ? ? ? ? ? ? 2.031 ? metalc16 metalc ? ? A ASP 410 OD1 ? ? ? 1_555 I ZN . ZN B ? A ASP 443 A ZN 1752 1_555 ? ? ? ? ? ? ? 2.292 ? metalc17 metalc ? ? A ASP 410 OD2 ? ? ? 1_555 I ZN . ZN A ? A ASP 443 A ZN 1752 1_555 ? ? ? ? ? ? ? 2.374 ? covale4 covale ? ? A ASN 416 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 449 A NAG 1758 1_555 ? ? ? ? ? ? ? 1.433 ? metalc18 metalc ? ? A HIS 510 NE2 ? ? ? 1_555 H ZN . ZN A ? A HIS 543 A ZN 1751 1_555 ? ? ? ? ? ? ? 2.096 ? metalc19 metalc ? ? A HIS 510 NE2 ? ? ? 1_555 H ZN . ZN B ? A HIS 543 A ZN 1751 1_555 ? ? ? ? ? ? ? 2.016 ? covale5 covale ? ? A ASN 595 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 628 A NAG 1759 1_555 ? ? ? ? ? ? ? 1.466 ? covale6 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 1759 A NAG 1760 1_555 ? ? ? ? ? ? ? 1.440 ? metalc20 metalc ? ? H ZN . ZN A ? ? 1_555 O HOH . O ? ? A ZN 1751 A HOH 802 1_555 ? ? ? ? ? ? ? 1.827 ? metalc21 metalc ? ? H ZN . ZN A ? ? 1_555 O HOH . O ? ? A ZN 1751 A HOH 801 1_555 ? ? ? ? ? ? ? 2.143 ? metalc22 metalc ? ? H ZN . ZN B ? ? 1_555 O HOH . O ? ? A ZN 1751 A HOH 802 1_555 ? ? ? ? ? ? ? 2.267 ? metalc23 metalc ? ? H ZN . ZN B ? ? 1_555 O HOH . O ? ? A ZN 1751 A HOH 801 1_555 ? ? ? ? ? ? ? 2.330 ? metalc24 metalc ? ? I ZN . ZN A ? ? 1_555 O HOH . O ? ? A ZN 1752 A HOH 805 1_555 ? ? ? ? ? ? ? 1.915 ? metalc25 metalc ? ? I ZN . ZN A ? ? 1_555 O HOH . O ? ? A ZN 1752 A HOH 801 1_555 ? ? ? ? ? ? ? 2.328 ? metalc26 metalc ? ? I ZN . ZN B ? ? 1_555 O HOH . O ? ? A ZN 1752 A HOH 805 1_555 ? ? ? ? ? ? ? 1.996 ? metalc27 metalc ? ? I ZN . ZN B ? ? 1_555 O HOH . O ? ? A ZN 1752 A HOH 801 1_555 ? ? ? ? ? ? ? 2.087 ? metalc28 metalc ? ? K CA . CA ? ? ? 1_555 O HOH . O ? ? A CA 1755 A HOH 816 1_555 ? ? ? ? ? ? ? 2.383 ? metalc29 metalc ? ? H ZN . ZN A ? ? 1_555 N MPO . S1 A ? A ZN 1751 A MPO 741 1_555 ? ? ? ? ? ? ? 2.692 ? metalc30 metalc ? ? H ZN . ZN A ? ? 1_555 N MPO . O1 A ? A ZN 1751 A MPO 741 1_555 ? ? ? ? ? ? ? 1.838 ? metalc31 metalc ? ? I ZN . ZN A ? ? 1_555 N MPO . O3 A ? A ZN 1752 A MPO 741 1_555 ? ? ? ? ? ? ? 2.052 ? # 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 199 A . ? TYR 232 A PRO 200 A ? PRO 233 A 1 10.88 2 GLY 287 A . ? GLY 320 A PRO 288 A ? PRO 321 A 1 -3.83 3 ASP 344 A . ? ASP 377 A PRO 345 A ? PRO 378 A 1 2.51 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 7 ? B ? 4 ? C ? 4 ? D ? 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 C 2 3 ? parallel C 3 4 ? parallel D 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 64 ? TYR A 76 ? SER A 97 TYR A 109 A 2 ILE A 306 ? ILE A 319 ? ILE A 339 ILE A 352 A 3 ARG A 371 ? TRP A 378 ? ARG A 404 TRP A 411 A 4 GLU A 324 ? HIS A 334 ? GLU A 357 HIS A 367 A 5 SER A 403 ? ASN A 408 ? SER A 436 ASN A 441 A 6 SER A 489 ? THR A 495 ? SER A 522 THR A 528 A 7 THR A 418 ? CYS A 423 ? THR A 451 CYS A 456 B 1 GLU A 94 ? LYS A 97 ? GLU A 127 LYS A 130 B 2 TYR A 84 ? VAL A 88 ? TYR A 117 VAL A 121 B 3 LYS A 298 ? HIS A 302 ? LYS A 331 HIS A 335 B 4 GLU A 128 ? GLY A 129 ? GLU A 161 GLY A 162 C 1 LEU A 131 ? TYR A 133 ? LEU A 164 TYR A 166 C 2 ILE A 157 ? ARG A 161 ? ILE A 190 ARG A 194 C 3 GLY A 181 ? TYR A 185 ? GLY A 214 TYR A 218 C 4 VAL A 251 ? ILE A 254 ? VAL A 284 ILE A 287 D 1 PRO A 459 ? SER A 460 ? PRO A 492 SER A 493 D 2 ASN A 463 ? PRO A 467 ? ASN A 496 PRO A 500 # 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 TYR A 76 ? N TYR A 109 O ILE A 306 ? O ILE A 339 A 2 3 N GLY A 317 ? N GLY A 350 O PHE A 375 ? O PHE A 408 A 3 4 O ILE A 374 ? O ILE A 407 N LEU A 331 ? N LEU A 364 A 4 5 N ILE A 330 ? N ILE A 363 O ILE A 407 ? O ILE A 440 A 5 6 N ASN A 408 ? N ASN A 441 O GLY A 490 ? O GLY A 523 A 6 7 O THR A 495 ? O THR A 528 N THR A 418 ? N THR A 451 B 1 2 O ILE A 95 ? O ILE A 128 N ILE A 87 ? N ILE A 120 B 2 3 N SER A 86 ? N SER A 119 O ARG A 300 ? O ARG A 333 B 3 4 O VAL A 299 ? O VAL A 332 N GLY A 129 ? N GLY A 162 C 1 2 N VAL A 132 ? N VAL A 165 O ILE A 159 ? O ILE A 192 C 2 3 N ALA A 160 ? N ALA A 193 O ILE A 183 ? O ILE A 216 C 3 4 N LEU A 184 ? N LEU A 217 O ILE A 254 ? O ILE A 287 D 1 2 N SER A 460 ? N SER A 493 O LEU A 466 ? O LEU A 499 # 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 ? ? ? ? 16 'BINDING SITE FOR RESIDUE GLU A 742' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 1756' AC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 1758' AC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 1759' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 1760' AC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 1766' AC7 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE ZN A 1751' AC8 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE ZN A 1752' AC9 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CL A 1754' BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 1755' BC2 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL A 1' BC3 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE GOL A 2' BC4 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE MPO A 741' # 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 16 GOL L . ? GOL A 1 . ? 1_555 ? 2 AC1 16 ARG A 167 ? ARG A 200 . ? 1_555 ? 3 AC1 16 ASN A 214 ? ASN A 247 . ? 1_555 ? 4 AC1 16 GLU A 381 ? GLU A 414 . ? 1_555 ? 5 AC1 16 GLU A 382 ? GLU A 415 . ? 1_555 ? 6 AC1 16 GLY A 384 ? GLY A 417 . ? 1_555 ? 7 AC1 16 GLY A 475 ? GLY A 508 . ? 1_555 ? 8 AC1 16 TYR A 509 ? TYR A 542 . ? 1_555 ? 9 AC1 16 HIS A 510 ? HIS A 543 . ? 1_555 ? 10 AC1 16 LYS A 656 ? LYS A 689 . ? 1_555 ? 11 AC1 16 TYR A 657 ? TYR A 690 . ? 1_555 ? 12 AC1 16 HOH O . ? HOH A 801 . ? 1_555 ? 13 AC1 16 HOH O . ? HOH A 802 . ? 1_555 ? 14 AC1 16 HOH O . ? HOH A 806 . ? 1_555 ? 15 AC1 16 HOH O . ? HOH A 1170 . ? 1_555 ? 16 AC1 16 HOH O . ? HOH A 1250 . ? 1_555 ? 17 AC2 6 ASN A 78 ? ASN A 111 . ? 1_555 ? 18 AC2 6 THR A 80 ? THR A 113 . ? 1_555 ? 19 AC2 6 ASN A 81 ? ASN A 114 . ? 1_555 ? 20 AC2 6 ILE A 306 ? ILE A 339 . ? 1_555 ? 21 AC2 6 HOH O . ? HOH A 1065 . ? 1_555 ? 22 AC2 6 HOH O . ? HOH A 1320 . ? 1_555 ? 23 AC3 8 TRP A 203 ? TRP A 236 . ? 1_555 ? 24 AC3 8 ASN A 416 ? ASN A 449 . ? 1_555 ? 25 AC3 8 PHE A 522 ? PHE A 555 . ? 1_555 ? 26 AC3 8 TYR A 523 ? TYR A 556 . ? 1_555 ? 27 AC3 8 HOH O . ? HOH A 882 . ? 1_555 ? 28 AC3 8 HOH O . ? HOH A 1046 . ? 1_555 ? 29 AC3 8 HOH O . ? HOH A 1112 . ? 1_555 ? 30 AC3 8 HOH O . ? HOH A 1274 . ? 1_555 ? 31 AC4 7 SER A 588 ? SER A 621 . ? 1_555 ? 32 AC4 7 SER A 591 ? SER A 624 . ? 1_555 ? 33 AC4 7 ASN A 595 ? ASN A 628 . ? 1_555 ? 34 AC4 7 GLN A 697 ? GLN A 730 . ? 1_555 ? 35 AC4 7 HOH O . ? HOH A 931 . ? 2_555 ? 36 AC4 7 HOH O . ? HOH A 1405 . ? 1_555 ? 37 AC4 7 NAG F . ? NAG A 1760 . ? 1_555 ? 38 AC5 4 GLU A 233 ? GLU A 266 . ? 2_555 ? 39 AC5 4 HOH O . ? HOH A 927 . ? 2_555 ? 40 AC5 4 HOH O . ? HOH A 1405 . ? 1_555 ? 41 AC5 4 NAG E . ? NAG A 1759 . ? 1_555 ? 42 AC6 2 ASN A 152 ? ASN A 185 . ? 1_555 ? 43 AC6 2 THR A 154 ? THR A 187 . ? 1_555 ? 44 AC7 8 ASP A 344 ? ASP A 377 . ? 1_555 ? 45 AC7 8 GLU A 382 ? GLU A 415 . ? 1_555 ? 46 AC7 8 HIS A 510 ? HIS A 543 . ? 1_555 ? 47 AC7 8 MPO N . ? MPO A 741 . ? 1_555 ? 48 AC7 8 HOH O . ? HOH A 801 . ? 1_555 ? 49 AC7 8 HOH O . ? HOH A 802 . ? 1_555 ? 50 AC7 8 HOH O . ? HOH A 806 . ? 1_555 ? 51 AC7 8 ZN I . ? ZN A 1752 . ? 1_555 ? 52 AC8 7 HIS A 334 ? HIS A 367 . ? 1_555 ? 53 AC8 7 ASP A 344 ? ASP A 377 . ? 1_555 ? 54 AC8 7 ASP A 410 ? ASP A 443 . ? 1_555 ? 55 AC8 7 MPO N . ? MPO A 741 . ? 1_555 ? 56 AC8 7 HOH O . ? HOH A 801 . ? 1_555 ? 57 AC8 7 HOH O . ? HOH A 805 . ? 1_555 ? 58 AC8 7 ZN H . ? ZN A 1751 . ? 1_555 ? 59 AC9 6 ASN A 408 ? ASN A 441 . ? 1_555 ? 60 AC9 6 ASP A 410 ? ASP A 443 . ? 1_555 ? 61 AC9 6 ARG A 491 ? ARG A 524 . ? 1_555 ? 62 AC9 6 ARG A 493 ? ARG A 526 . ? 1_555 ? 63 AC9 6 ARG A 537 ? ARG A 570 . ? 1_555 ? 64 AC9 6 HOH O . ? HOH A 818 . ? 1_555 ? 65 BC1 5 THR A 226 ? THR A 259 . ? 1_555 ? 66 BC1 5 TYR A 229 ? TYR A 262 . ? 1_555 ? 67 BC1 5 GLU A 390 ? GLU A 423 . ? 1_555 ? 68 BC1 5 GLU A 393 ? GLU A 426 . ? 1_555 ? 69 BC1 5 HOH O . ? HOH A 816 . ? 1_555 ? 70 BC2 8 PHE A 166 ? PHE A 199 . ? 1_555 ? 71 BC2 8 ARG A 167 ? ARG A 200 . ? 1_555 ? 72 BC2 8 TYR A 509 ? TYR A 542 . ? 1_555 ? 73 BC2 8 TYR A 657 ? TYR A 690 . ? 1_555 ? 74 BC2 8 GLU B . ? GLU A 742 . ? 1_555 ? 75 BC2 8 HOH O . ? HOH A 1202 . ? 1_555 ? 76 BC2 8 HOH O . ? HOH A 1260 . ? 1_555 ? 77 BC2 8 HOH O . ? HOH A 1344 . ? 1_555 ? 78 BC3 10 LEU A 636 ? LEU A 669 . ? 1_555 ? 79 BC3 10 GLY A 637 ? GLY A 670 . ? 1_555 ? 80 BC3 10 LEU A 638 ? LEU A 671 . ? 1_555 ? 81 BC3 10 PRO A 639 ? PRO A 672 . ? 1_555 ? 82 BC3 10 LYS A 687 ? LYS A 720 . ? 1_555 ? 83 BC3 10 HIS A 688 ? HIS A 721 . ? 1_555 ? 84 BC3 10 HOH O . ? HOH A 840 . ? 1_555 ? 85 BC3 10 HOH O . ? HOH A 913 . ? 1_555 ? 86 BC3 10 HOH O . ? HOH A 974 . ? 1_555 ? 87 BC3 10 HOH O . ? HOH A 1427 . ? 1_555 ? 88 BC4 16 PHE A 166 ? PHE A 199 . ? 1_555 ? 89 BC4 16 ASN A 214 ? ASN A 247 . ? 1_555 ? 90 BC4 16 ASP A 344 ? ASP A 377 . ? 1_555 ? 91 BC4 16 GLU A 381 ? GLU A 414 . ? 1_555 ? 92 BC4 16 GLU A 382 ? GLU A 415 . ? 1_555 ? 93 BC4 16 GLY A 384 ? GLY A 417 . ? 1_555 ? 94 BC4 16 ASP A 410 ? ASP A 443 . ? 1_555 ? 95 BC4 16 GLY A 475 ? GLY A 508 . ? 1_555 ? 96 BC4 16 TYR A 509 ? TYR A 542 . ? 1_555 ? 97 BC4 16 HOH O . ? HOH A 801 . ? 1_555 ? 98 BC4 16 HOH O . ? HOH A 802 . ? 1_555 ? 99 BC4 16 HOH O . ? HOH A 805 . ? 1_555 ? 100 BC4 16 HOH O . ? HOH A 806 . ? 1_555 ? 101 BC4 16 HOH O . ? HOH A 1250 . ? 1_555 ? 102 BC4 16 ZN H . ? ZN A 1751 . ? 1_555 ? 103 BC4 16 ZN I . ? ZN A 1752 . ? 1_555 ? # _database_PDB_matrix.entry_id 3FEC _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 3FEC _atom_sites.fract_transf_matrix[1][1] 0.008146 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.002598 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.009586 _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] 0.013455 _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 . SER A 1 13 ? 22.993 80.212 14.027 1.00 29.33 ? 46 SER A N 1 ATOM 2 C CA . SER A 1 13 ? 21.699 79.601 13.482 1.00 26.64 ? 46 SER A CA 1 ATOM 3 C C . SER A 1 13 ? 20.985 78.793 14.549 1.00 25.53 ? 46 SER A C 1 ATOM 4 O O . SER A 1 13 ? 21.556 78.451 15.583 1.00 23.10 ? 46 SER A O 1 ATOM 5 C CB . SER A 1 13 ? 22.018 78.693 12.283 1.00 28.25 ? 46 SER A CB 1 ATOM 6 O OG . SER A 1 13 ? 22.768 77.530 12.684 1.00 29.79 ? 46 SER A OG 1 ATOM 7 N N . ILE A 1 14 ? 19.736 78.442 14.254 1.00 24.49 ? 47 ILE A N 1 ATOM 8 C CA . ILE A 1 14 ? 18.964 77.592 15.168 1.00 23.95 ? 47 ILE A CA 1 ATOM 9 C C . ILE A 1 14 ? 19.631 76.213 15.280 1.00 22.56 ? 47 ILE A C 1 ATOM 10 O O . ILE A 1 14 ? 19.754 75.650 16.393 1.00 22.31 ? 47 ILE A O 1 ATOM 11 C CB . ILE A 1 14 ? 17.516 77.478 14.689 1.00 23.85 ? 47 ILE A CB 1 ATOM 12 C CG1 . ILE A 1 14 ? 16.827 78.875 14.809 1.00 26.30 ? 47 ILE A CG1 1 ATOM 13 C CG2 . ILE A 1 14 ? 16.739 76.436 15.545 1.00 23.94 ? 47 ILE A CG2 1 ATOM 14 C CD1 . ILE A 1 14 ? 16.464 79.323 16.223 1.00 29.63 ? 47 ILE A CD1 1 ATOM 15 N N . ARG A 1 15 ? 20.093 75.677 14.151 1.00 22.46 ? 48 ARG A N 1 ATOM 16 C CA . ARG A 1 15 ? 20.783 74.398 14.180 1.00 22.20 ? 48 ARG A CA 1 ATOM 17 C C . ARG A 1 15 ? 22.028 74.463 15.054 1.00 21.32 ? 48 ARG A C 1 ATOM 18 O O . ARG A 1 15 ? 22.319 73.531 15.810 1.00 21.76 ? 48 ARG A O 1 ATOM 19 C CB . ARG A 1 15 ? 21.164 73.895 12.778 1.00 21.47 ? 48 ARG A CB 1 ATOM 20 C CG . ARG A 1 15 ? 21.925 72.533 12.884 1.00 24.52 ? 48 ARG A CG 1 ATOM 21 C CD . ARG A 1 15 ? 22.109 71.811 11.609 1.00 34.89 ? 48 ARG A CD 1 ATOM 22 N NE . ARG A 1 15 ? 22.282 72.695 10.468 1.00 35.78 ? 48 ARG A NE 1 ATOM 23 C CZ . ARG A 1 15 ? 23.409 72.915 9.816 1.00 39.98 ? 48 ARG A CZ 1 ATOM 24 N NH1 . ARG A 1 15 ? 23.366 73.749 8.788 1.00 43.50 ? 48 ARG A NH1 1 ATOM 25 N NH2 . ARG A 1 15 ? 24.556 72.324 10.174 1.00 39.23 ? 48 ARG A NH2 1 ATOM 26 N N . TRP A 1 16 ? 22.813 75.561 14.986 1.00 21.26 ? 49 TRP A N 1 ATOM 27 C CA . TRP A 1 16 ? 23.966 75.635 15.848 1.00 21.09 ? 49 TRP A CA 1 ATOM 28 C C . TRP A 1 16 ? 23.562 75.691 17.340 1.00 20.11 ? 49 TRP A C 1 ATOM 29 O O . TRP A 1 16 ? 24.219 75.091 18.202 1.00 20.69 ? 49 TRP A O 1 ATOM 30 C CB . TRP A 1 16 ? 24.798 76.866 15.472 1.00 23.24 ? 49 TRP A CB 1 ATOM 31 C CG . TRP A 1 16 ? 26.029 77.065 16.355 1.00 28.53 ? 49 TRP A CG 1 ATOM 32 C CD1 . TRP A 1 16 ? 27.290 76.632 16.078 1.00 35.88 ? 49 TRP A CD1 1 ATOM 33 C CD2 . TRP A 1 16 ? 26.124 77.778 17.610 1.00 30.28 ? 49 TRP A CD2 1 ATOM 34 N NE1 . TRP A 1 16 ? 28.160 77.009 17.085 1.00 35.79 ? 49 TRP A NE1 1 ATOM 35 C CE2 . TRP A 1 16 ? 27.463 77.689 18.041 1.00 33.20 ? 49 TRP A CE2 1 ATOM 36 C CE3 . TRP A 1 16 ? 25.192 78.420 18.438 1.00 33.54 ? 49 TRP A CE3 1 ATOM 37 C CZ2 . TRP A 1 16 ? 27.913 78.254 19.247 1.00 36.43 ? 49 TRP A CZ2 1 ATOM 38 C CZ3 . TRP A 1 16 ? 25.636 78.982 19.652 1.00 37.12 ? 49 TRP A CZ3 1 ATOM 39 C CH2 . TRP A 1 16 ? 26.989 78.899 20.035 1.00 36.42 ? 49 TRP A CH2 1 ATOM 40 N N . LYS A 1 17 ? 22.473 76.390 17.655 1.00 19.74 ? 50 LYS A N 1 ATOM 41 C CA . LYS A 1 17 ? 21.993 76.448 19.044 1.00 20.46 ? 50 LYS A CA 1 ATOM 42 C C . LYS A 1 17 ? 21.533 75.060 19.525 1.00 19.25 ? 50 LYS A C 1 ATOM 43 O O . LYS A 1 17 ? 21.725 74.694 20.710 1.00 21.30 ? 50 LYS A O 1 ATOM 44 C CB . LYS A 1 17 ? 20.826 77.427 19.151 1.00 21.20 ? 50 LYS A CB 1 ATOM 45 C CG . LYS A 1 17 ? 21.258 78.907 18.981 1.00 26.50 ? 50 LYS A CG 1 ATOM 46 C CD . LYS A 1 17 ? 20.014 79.810 19.018 1.00 32.32 ? 50 LYS A CD 1 ATOM 47 C CE . LYS A 1 17 ? 20.363 81.344 18.852 1.00 37.99 ? 50 LYS A CE 1 ATOM 48 N NZ . LYS A 1 17 ? 19.748 81.897 17.557 1.00 42.47 ? 50 LYS A NZ 1 ATOM 49 N N . LEU A 1 18 ? 20.874 74.326 18.629 1.00 19.15 ? 51 LEU A N 1 ATOM 50 C CA . LEU A 1 18 ? 20.441 72.953 18.971 1.00 18.97 ? 51 LEU A CA 1 ATOM 51 C C . LEU A 1 18 ? 21.648 72.060 19.317 1.00 18.48 ? 51 LEU A C 1 ATOM 52 O O . LEU A 1 18 ? 21.684 71.363 20.356 1.00 18.60 ? 51 LEU A O 1 ATOM 53 C CB . LEU A 1 18 ? 19.692 72.345 17.830 1.00 19.51 ? 51 LEU A CB 1 ATOM 54 C CG . LEU A 1 18 ? 19.265 70.911 18.073 1.00 19.05 ? 51 LEU A CG 1 ATOM 55 C CD1 . LEU A 1 18 ? 18.059 70.868 19.005 1.00 21.51 ? 51 LEU A CD1 1 ATOM 56 C CD2 . LEU A 1 18 ? 18.893 70.317 16.695 1.00 22.98 ? 51 LEU A CD2 1 ATOM 57 N N . VAL A 1 19 ? 22.631 72.084 18.434 1.00 19.07 ? 52 VAL A N 1 ATOM 58 C CA . VAL A 1 19 ? 23.817 71.264 18.579 1.00 17.85 ? 52 VAL A CA 1 ATOM 59 C C . VAL A 1 19 ? 24.695 71.702 19.767 1.00 18.44 ? 52 VAL A C 1 ATOM 60 O O . VAL A 1 19 ? 25.128 70.857 20.571 1.00 19.99 ? 52 VAL A O 1 ATOM 61 C CB . VAL A 1 19 ? 24.595 71.356 17.238 1.00 20.32 ? 52 VAL A CB 1 ATOM 62 C CG1 . VAL A 1 19 ? 26.033 70.870 17.374 1.00 20.71 ? 52 VAL A CG1 1 ATOM 63 C CG2 . VAL A 1 19 ? 23.832 70.583 16.147 1.00 19.86 ? 52 VAL A CG2 1 ATOM 64 N N . SER A 1 20 ? 24.933 73.002 19.932 1.00 18.49 ? 53 SER A N 1 ATOM 65 C CA . SER A 1 20 ? 25.840 73.498 20.982 1.00 19.22 ? 53 SER A CA 1 ATOM 66 C C . SER A 1 20 ? 25.276 73.420 22.411 1.00 18.29 ? 53 SER A C 1 ATOM 67 O O . SER A 1 20 ? 26.031 73.332 23.414 1.00 20.51 ? 53 SER A O 1 ATOM 68 C CB . SER A 1 20 ? 26.249 74.915 20.616 1.00 19.69 ? 53 SER A CB 1 ATOM 69 O OG A SER A 1 20 ? 25.156 75.803 20.739 0.45 19.44 ? 53 SER A OG 1 ATOM 70 O OG B SER A 1 20 ? 26.876 74.951 19.365 0.25 18.95 ? 53 SER A OG 1 ATOM 71 O OG C SER A 1 20 ? 27.146 75.438 21.574 0.30 19.34 ? 53 SER A OG 1 ATOM 72 N N . GLU A 1 21 ? 23.930 73.378 22.488 1.00 18.35 ? 54 GLU A N 1 ATOM 73 C CA . GLU A 1 21 ? 23.237 73.200 23.754 1.00 19.85 ? 54 GLU A CA 1 ATOM 74 C C . GLU A 1 21 ? 23.442 71.797 24.350 1.00 18.37 ? 54 GLU A C 1 ATOM 75 O O . GLU A 1 21 ? 23.409 71.647 25.573 1.00 19.17 ? 54 GLU A O 1 ATOM 76 C CB . GLU A 1 21 ? 21.725 73.551 23.609 1.00 19.67 ? 54 GLU A CB 1 ATOM 77 C CG . GLU A 1 21 ? 20.855 73.363 24.884 1.00 21.21 ? 54 GLU A CG 1 ATOM 78 C CD . GLU A 1 21 ? 21.354 74.149 26.095 1.00 23.43 ? 54 GLU A CD 1 ATOM 79 O OE1 . GLU A 1 21 ? 21.874 75.276 25.931 1.00 23.49 ? 54 GLU A OE1 1 ATOM 80 O OE2 . GLU A 1 21 ? 21.252 73.644 27.235 1.00 21.25 ? 54 GLU A OE2 1 ATOM 81 N N . MET A 1 22 ? 23.614 70.781 23.494 1.00 18.18 ? 55 MET A N 1 ATOM 82 C CA . MET A 1 22 ? 23.798 69.410 24.022 1.00 17.53 ? 55 MET A CA 1 ATOM 83 C C . MET A 1 22 ? 25.135 69.289 24.746 1.00 18.61 ? 55 MET A C 1 ATOM 84 O O . MET A 1 22 ? 26.128 69.873 24.288 1.00 19.94 ? 55 MET A O 1 ATOM 85 C CB . MET A 1 22 ? 23.735 68.416 22.863 1.00 18.34 ? 55 MET A CB 1 ATOM 86 C CG . MET A 1 22 ? 22.392 68.470 22.117 1.00 18.89 ? 55 MET A CG 1 ATOM 87 S SD . MET A 1 22 ? 22.436 67.154 20.887 1.00 19.37 ? 55 MET A SD 1 ATOM 88 C CE . MET A 1 22 ? 21.212 67.743 19.721 1.00 19.51 ? 55 MET A CE 1 ATOM 89 N N . LYS A 1 23 ? 25.164 68.540 25.846 1.00 17.48 ? 56 LYS A N 1 ATOM 90 C CA . LYS A 1 23 ? 26.384 68.460 26.679 1.00 17.70 ? 56 LYS A CA 1 ATOM 91 C C . LYS A 1 23 ? 26.739 67.017 27.015 1.00 18.42 ? 56 LYS A C 1 ATOM 92 O O . LYS A 1 23 ? 25.846 66.226 27.398 1.00 17.67 ? 56 LYS A O 1 ATOM 93 C CB . LYS A 1 23 ? 26.251 69.212 28.045 1.00 17.56 ? 56 LYS A CB 1 ATOM 94 C CG . LYS A 1 23 ? 25.930 70.693 27.957 1.00 19.99 ? 56 LYS A CG 1 ATOM 95 C CD . LYS A 1 23 ? 27.022 71.391 27.158 1.00 26.93 ? 56 LYS A CD 1 ATOM 96 C CE . LYS A 1 23 ? 26.940 72.908 27.267 1.00 33.85 ? 56 LYS A CE 1 ATOM 97 N NZ . LYS A 1 23 ? 26.000 73.518 26.282 1.00 29.71 ? 56 LYS A NZ 1 ATOM 98 N N . ALA A 1 24 ? 28.030 66.690 26.894 1.00 17.45 ? 57 ALA A N 1 ATOM 99 C CA . ALA A 1 24 ? 28.552 65.360 27.260 1.00 18.36 ? 57 ALA A CA 1 ATOM 100 C C . ALA A 1 24 ? 28.163 65.009 28.695 1.00 19.08 ? 57 ALA A C 1 ATOM 101 O O . ALA A 1 24 ? 27.707 63.884 28.928 1.00 19.22 ? 57 ALA A O 1 ATOM 102 C CB . ALA A 1 24 ? 30.081 65.312 27.079 1.00 18.48 ? 57 ALA A CB 1 ATOM 103 N N . GLU A 1 25 ? 28.298 65.960 29.637 1.00 19.33 ? 58 GLU A N 1 ATOM 104 C CA . GLU A 1 25 ? 28.002 65.681 31.028 1.00 19.50 ? 58 GLU A CA 1 ATOM 105 C C . GLU A 1 25 ? 26.515 65.327 31.217 1.00 19.46 ? 58 GLU A C 1 ATOM 106 O O . GLU A 1 25 ? 26.182 64.525 32.072 1.00 19.82 ? 58 GLU A O 1 ATOM 107 C CB . GLU A 1 25 ? 28.428 66.859 31.935 1.00 19.17 ? 58 GLU A CB 1 ATOM 108 C CG . GLU A 1 25 ? 28.239 66.571 33.418 1.00 26.68 ? 58 GLU A CG 1 ATOM 109 C CD . GLU A 1 25 ? 28.924 65.273 33.877 1.00 35.31 ? 58 GLU A CD 1 ATOM 110 O OE1 . GLU A 1 25 ? 30.157 65.121 33.644 1.00 32.80 ? 58 GLU A OE1 1 ATOM 111 O OE2 . GLU A 1 25 ? 28.181 64.384 34.414 1.00 41.47 ? 58 GLU A OE2 1 ATOM 112 N N . ASN A 1 26 ? 25.622 65.914 30.427 1.00 17.98 ? 59 ASN A N 1 ATOM 113 C CA . ASN A 1 26 ? 24.224 65.520 30.528 1.00 18.68 ? 59 ASN A CA 1 ATOM 114 C C . ASN A 1 26 ? 23.968 64.112 30.036 1.00 18.58 ? 59 ASN A C 1 ATOM 115 O O . ASN A 1 26 ? 23.183 63.396 30.628 1.00 18.61 ? 59 ASN A O 1 ATOM 116 C CB . ASN A 1 26 ? 23.335 66.489 29.731 1.00 18.63 ? 59 ASN A CB 1 ATOM 117 C CG . ASN A 1 26 ? 23.302 67.884 30.367 1.00 18.67 ? 59 ASN A CG 1 ATOM 118 O OD1 . ASN A 1 26 ? 23.592 68.067 31.576 1.00 20.94 ? 59 ASN A OD1 1 ATOM 119 N ND2 . ASN A 1 26 ? 23.020 68.876 29.543 1.00 20.36 ? 59 ASN A ND2 1 ATOM 120 N N . ILE A 1 27 ? 24.576 63.737 28.908 1.00 17.68 ? 60 ILE A N 1 ATOM 121 C CA . ILE A 1 27 ? 24.437 62.361 28.416 1.00 18.62 ? 60 ILE A CA 1 ATOM 122 C C . ILE A 1 27 ? 24.933 61.370 29.489 1.00 17.43 ? 60 ILE A C 1 ATOM 123 O O . ILE A 1 27 ? 24.292 60.352 29.761 1.00 17.69 ? 60 ILE A O 1 ATOM 124 C CB . ILE A 1 27 ? 25.155 62.237 27.098 1.00 17.25 ? 60 ILE A CB 1 ATOM 125 C CG1 . ILE A 1 27 ? 24.448 63.097 26.036 1.00 19.67 ? 60 ILE A CG1 1 ATOM 126 C CG2 . ILE A 1 27 ? 25.147 60.775 26.616 1.00 17.60 ? 60 ILE A CG2 1 ATOM 127 C CD1 . ILE A 1 27 ? 25.287 63.242 24.804 1.00 20.85 ? 60 ILE A CD1 1 ATOM 128 N N . LYS A 1 28 ? 26.053 61.710 30.124 1.00 18.00 ? 61 LYS A N 1 ATOM 129 C CA . LYS A 1 28 ? 26.624 60.893 31.171 1.00 18.30 ? 61 LYS A CA 1 ATOM 130 C C . LYS A 1 28 ? 25.646 60.756 32.340 1.00 18.33 ? 61 LYS A C 1 ATOM 131 O O . LYS A 1 28 ? 25.403 59.636 32.809 1.00 18.75 ? 61 LYS A O 1 ATOM 132 C CB . LYS A 1 28 ? 27.914 61.547 31.635 1.00 18.37 ? 61 LYS A CB 1 ATOM 133 C CG . LYS A 1 28 ? 28.683 60.673 32.622 1.00 20.28 ? 61 LYS A CG 1 ATOM 134 C CD . LYS A 1 28 ? 29.964 61.382 33.085 1.00 21.20 ? 61 LYS A CD 1 ATOM 135 C CE . LYS A 1 28 ? 30.724 60.592 34.128 1.00 27.28 ? 61 LYS A CE 1 ATOM 136 N NZ . LYS A 1 28 ? 32.053 61.289 34.440 1.00 27.41 ? 61 LYS A NZ 1 ATOM 137 N N . SER A 1 29 ? 25.080 61.863 32.833 1.00 18.08 ? 62 SER A N 1 ATOM 138 C CA . SER A 1 29 ? 24.115 61.772 33.940 1.00 18.40 ? 62 SER A CA 1 ATOM 139 C C . SER A 1 29 ? 22.878 60.990 33.548 1.00 17.51 ? 62 SER A C 1 ATOM 140 O O . SER A 1 29 ? 22.416 60.175 34.337 1.00 17.58 ? 62 SER A O 1 ATOM 141 C CB . SER A 1 29 ? 23.689 63.143 34.428 1.00 17.51 ? 62 SER A CB 1 ATOM 142 O OG A SER A 1 29 ? 24.849 63.823 34.831 0.55 20.96 ? 62 SER A OG 1 ATOM 143 O OG B SER A 1 29 ? 23.530 64.106 33.422 0.15 14.08 ? 62 SER A OG 1 ATOM 144 O OG C SER A 1 29 ? 23.045 63.053 35.688 0.30 21.59 ? 62 SER A OG 1 ATOM 145 N N . PHE A 1 30 ? 22.335 61.195 32.341 1.00 17.35 ? 63 PHE A N 1 ATOM 146 C CA . PHE A 1 30 ? 21.184 60.381 31.914 1.00 18.82 ? 63 PHE A CA 1 ATOM 147 C C . PHE A 1 30 ? 21.590 58.911 31.915 1.00 18.28 ? 63 PHE A C 1 ATOM 148 O O . PHE A 1 30 ? 20.882 58.069 32.492 1.00 19.32 ? 63 PHE A O 1 ATOM 149 C CB . PHE A 1 30 ? 20.702 60.759 30.510 1.00 17.81 ? 63 PHE A CB 1 ATOM 150 C CG . PHE A 1 30 ? 19.888 62.033 30.465 1.00 16.39 ? 63 PHE A CG 1 ATOM 151 C CD1 . PHE A 1 30 ? 18.750 62.184 31.251 1.00 18.63 ? 63 PHE A CD1 1 ATOM 152 C CD2 . PHE A 1 30 ? 20.268 63.074 29.581 1.00 16.11 ? 63 PHE A CD2 1 ATOM 153 C CE1 . PHE A 1 30 ? 18.021 63.431 31.193 1.00 19.32 ? 63 PHE A CE1 1 ATOM 154 C CE2 . PHE A 1 30 ? 19.528 64.272 29.469 1.00 17.33 ? 63 PHE A CE2 1 ATOM 155 C CZ . PHE A 1 30 ? 18.406 64.421 30.277 1.00 18.17 ? 63 PHE A CZ 1 ATOM 156 N N . LEU A 1 31 ? 22.725 58.585 31.291 1.00 17.72 ? 64 LEU A N 1 ATOM 157 C CA . LEU A 1 31 ? 23.126 57.139 31.207 1.00 17.43 ? 64 LEU A CA 1 ATOM 158 C C . LEU A 1 31 ? 23.266 56.509 32.614 1.00 17.01 ? 64 LEU A C 1 ATOM 159 O O . LEU A 1 31 ? 22.755 55.401 32.868 1.00 17.94 ? 64 LEU A O 1 ATOM 160 C CB . LEU A 1 31 ? 24.412 56.980 30.418 1.00 19.25 ? 64 LEU A CB 1 ATOM 161 C CG . LEU A 1 31 ? 24.848 55.546 30.143 1.00 19.11 ? 64 LEU A CG 1 ATOM 162 C CD1 . LEU A 1 31 ? 23.792 54.819 29.274 1.00 18.00 ? 64 LEU A CD1 1 ATOM 163 C CD2 . LEU A 1 31 ? 26.196 55.484 29.442 1.00 21.10 ? 64 LEU A CD2 1 ATOM 164 N N . ARG A 1 32 ? 23.899 57.260 33.532 1.00 17.90 ? 65 ARG A N 1 ATOM 165 C CA . ARG A 1 32 ? 24.099 56.684 34.824 1.00 17.45 ? 65 ARG A CA 1 ATOM 166 C C . ARG A 1 32 ? 22.730 56.449 35.465 1.00 17.89 ? 65 ARG A C 1 ATOM 167 O O . ARG A 1 32 ? 22.525 55.438 36.135 1.00 19.32 ? 65 ARG A O 1 ATOM 168 C CB . ARG A 1 32 ? 24.922 57.640 35.710 1.00 16.91 ? 65 ARG A CB 1 ATOM 169 C CG . ARG A 1 32 ? 24.940 57.260 37.218 1.00 19.04 ? 65 ARG A CG 1 ATOM 170 C CD . ARG A 1 32 ? 25.796 56.024 37.544 1.00 20.82 ? 65 ARG A CD 1 ATOM 171 N NE . ARG A 1 32 ? 25.133 54.788 37.096 1.00 19.47 ? 65 ARG A NE 1 ATOM 172 C CZ . ARG A 1 32 ? 25.643 53.580 37.251 1.00 23.31 ? 65 ARG A CZ 1 ATOM 173 N NH1 . ARG A 1 32 ? 24.986 52.523 36.773 1.00 22.08 ? 65 ARG A NH1 1 ATOM 174 N NH2 . ARG A 1 32 ? 26.804 53.444 37.883 1.00 22.66 ? 65 ARG A NH2 1 ATOM 175 N N . SER A 1 33 ? 21.779 57.375 35.283 1.00 17.27 ? 66 SER A N 1 ATOM 176 C CA . SER A 1 33 ? 20.461 57.245 35.955 1.00 17.90 ? 66 SER A CA 1 ATOM 177 C C . SER A 1 33 ? 19.617 56.080 35.408 1.00 18.70 ? 66 SER A C 1 ATOM 178 O O . SER A 1 33 ? 18.691 55.639 36.071 1.00 19.47 ? 66 SER A O 1 ATOM 179 C CB . SER A 1 33 ? 19.644 58.559 35.821 1.00 19.23 ? 66 SER A CB 1 ATOM 180 O OG . SER A 1 33 ? 19.152 58.730 34.514 1.00 22.52 ? 66 SER A OG 1 ATOM 181 N N . PHE A 1 34 ? 19.878 55.654 34.167 1.00 17.30 ? 67 PHE A N 1 ATOM 182 C CA . PHE A 1 34 ? 19.038 54.619 33.526 1.00 16.58 ? 67 PHE A CA 1 ATOM 183 C C . PHE A 1 34 ? 19.667 53.233 33.535 1.00 17.17 ? 67 PHE A C 1 ATOM 184 O O . PHE A 1 34 ? 19.073 52.288 32.944 1.00 19.35 ? 67 PHE A O 1 ATOM 185 C CB . PHE A 1 34 ? 18.787 55.022 32.072 1.00 17.37 ? 67 PHE A CB 1 ATOM 186 C CG . PHE A 1 34 ? 18.077 56.354 31.874 1.00 19.67 ? 67 PHE A CG 1 ATOM 187 C CD1 . PHE A 1 34 ? 17.146 56.841 32.795 1.00 21.97 ? 67 PHE A CD1 1 ATOM 188 C CD2 . PHE A 1 34 ? 18.325 57.088 30.707 1.00 21.15 ? 67 PHE A CD2 1 ATOM 189 C CE1 . PHE A 1 34 ? 16.494 58.073 32.553 1.00 21.00 ? 67 PHE A CE1 1 ATOM 190 C CE2 . PHE A 1 34 ? 17.674 58.299 30.454 1.00 19.82 ? 67 PHE A CE2 1 ATOM 191 C CZ . PHE A 1 34 ? 16.725 58.754 31.357 1.00 17.70 ? 67 PHE A CZ 1 ATOM 192 N N . THR A 1 35 ? 20.852 53.099 34.158 1.00 18.21 ? 68 THR A N 1 ATOM 193 C CA . THR A 1 35 ? 21.592 51.826 34.102 1.00 18.32 ? 68 THR A CA 1 ATOM 194 C C . THR A 1 35 ? 21.882 51.227 35.454 1.00 18.94 ? 68 THR A C 1 ATOM 195 O O . THR A 1 35 ? 22.744 50.350 35.546 1.00 20.23 ? 68 THR A O 1 ATOM 196 C CB . THR A 1 35 ? 22.937 51.986 33.364 1.00 18.77 ? 68 THR A CB 1 ATOM 197 O OG1 . THR A 1 35 ? 23.670 53.067 33.965 1.00 19.19 ? 68 THR A OG1 1 ATOM 198 C CG2 . THR A 1 35 ? 22.745 52.298 31.857 1.00 17.37 ? 68 THR A CG2 1 ATOM 199 N N . LYS A 1 36 ? 21.205 51.714 36.494 1.00 19.53 ? 69 LYS A N 1 ATOM 200 C CA . LYS A 1 36 ? 21.435 51.172 37.856 1.00 19.95 ? 69 LYS A CA 1 ATOM 201 C C . LYS A 1 36 ? 20.756 49.822 38.035 1.00 20.20 ? 69 LYS A C 1 ATOM 202 O O . LYS A 1 36 ? 21.219 49.005 38.846 1.00 20.58 ? 69 LYS A O 1 ATOM 203 C CB A LYS A 1 36 ? 21.049 52.158 38.956 0.65 20.66 ? 69 LYS A CB 1 ATOM 204 C CB B LYS A 1 36 ? 20.883 52.146 38.922 0.35 20.21 ? 69 LYS A CB 1 ATOM 205 C CG A LYS A 1 36 ? 21.998 53.370 38.962 0.65 22.32 ? 69 LYS A CG 1 ATOM 206 C CG B LYS A 1 36 ? 21.275 53.630 38.717 0.35 22.00 ? 69 LYS A CG 1 ATOM 207 C CD A LYS A 1 36 ? 21.642 54.307 40.113 0.65 26.42 ? 69 LYS A CD 1 ATOM 208 C CD B LYS A 1 36 ? 20.640 54.577 39.781 0.35 20.65 ? 69 LYS A CD 1 ATOM 209 C CE A LYS A 1 36 ? 22.224 55.684 39.859 0.65 31.70 ? 69 LYS A CE 1 ATOM 210 C CE B LYS A 1 36 ? 21.233 54.369 41.169 0.35 23.66 ? 69 LYS A CE 1 ATOM 211 N NZ A LYS A 1 36 ? 22.517 56.457 41.095 0.65 33.98 ? 69 LYS A NZ 1 ATOM 212 N NZ B LYS A 1 36 ? 20.994 55.562 42.062 0.35 24.79 ? 69 LYS A NZ 1 ATOM 213 N N . LEU A 1 37 ? 19.636 49.618 37.328 1.00 18.90 ? 70 LEU A N 1 ATOM 214 C CA . LEU A 1 37 ? 18.889 48.405 37.508 1.00 19.41 ? 70 LEU A CA 1 ATOM 215 C C . LEU A 1 37 ? 18.547 47.822 36.128 1.00 20.19 ? 70 LEU A C 1 ATOM 216 O O . LEU A 1 37 ? 18.533 48.559 35.115 1.00 20.42 ? 70 LEU A O 1 ATOM 217 C CB . LEU A 1 37 ? 17.602 48.670 38.273 1.00 20.88 ? 70 LEU A CB 1 ATOM 218 C CG . LEU A 1 37 ? 17.780 49.199 39.697 1.00 21.62 ? 70 LEU A CG 1 ATOM 219 C CD1 . LEU A 1 37 ? 16.404 49.681 40.154 1.00 24.70 ? 70 LEU A CD1 1 ATOM 220 C CD2 . LEU A 1 37 ? 18.295 48.062 40.523 1.00 20.62 ? 70 LEU A CD2 1 ATOM 221 N N . PRO A 1 38 ? 18.274 46.510 36.068 1.00 19.32 ? 71 PRO A N 1 ATOM 222 C CA . PRO A 1 38 ? 17.883 45.919 34.757 1.00 20.87 ? 71 PRO A CA 1 ATOM 223 C C . PRO A 1 38 ? 16.558 46.469 34.290 1.00 20.31 ? 71 PRO A C 1 ATOM 224 O O . PRO A 1 38 ? 15.725 46.902 35.076 1.00 21.27 ? 71 PRO A O 1 ATOM 225 C CB . PRO A 1 38 ? 17.755 44.416 35.078 1.00 22.38 ? 71 PRO A CB 1 ATOM 226 C CG . PRO A 1 38 ? 18.532 44.196 36.439 1.00 24.01 ? 71 PRO A CG 1 ATOM 227 C CD . PRO A 1 38 ? 18.342 45.511 37.163 1.00 22.00 ? 71 PRO A CD 1 ATOM 228 N N . HIS A 1 39 ? 16.365 46.511 32.959 1.00 19.00 ? 72 HIS A N 1 ATOM 229 C CA . HIS A 1 39 ? 15.119 47.088 32.451 1.00 18.70 ? 72 HIS A CA 1 ATOM 230 C C . HIS A 1 39 ? 14.698 46.263 31.220 1.00 17.82 ? 72 HIS A C 1 ATOM 231 O O . HIS A 1 39 ? 14.574 46.756 30.104 1.00 17.56 ? 72 HIS A O 1 ATOM 232 C CB . HIS A 1 39 ? 15.189 48.609 32.175 1.00 18.37 ? 72 HIS A CB 1 ATOM 233 C CG . HIS A 1 39 ? 16.414 49.076 31.445 1.00 19.63 ? 72 HIS A CG 1 ATOM 234 N ND1 . HIS A 1 39 ? 16.408 49.435 30.110 1.00 19.26 ? 72 HIS A ND1 1 ATOM 235 C CD2 . HIS A 1 39 ? 17.686 49.271 31.888 1.00 21.61 ? 72 HIS A CD2 1 ATOM 236 C CE1 . HIS A 1 39 ? 17.624 49.837 29.763 1.00 20.53 ? 72 HIS A CE1 1 ATOM 237 N NE2 . HIS A 1 39 ? 18.426 49.717 30.822 1.00 19.82 ? 72 HIS A NE2 1 ATOM 238 N N . LEU A 1 40 ? 14.375 45.044 31.524 1.00 18.53 ? 73 LEU A N 1 ATOM 239 C CA . LEU A 1 40 ? 13.961 44.033 30.529 1.00 17.14 ? 73 LEU A CA 1 ATOM 240 C C . LEU A 1 40 ? 12.496 44.347 30.100 1.00 17.18 ? 73 LEU A C 1 ATOM 241 O O . LEU A 1 40 ? 11.656 44.740 30.950 1.00 17.53 ? 73 LEU A O 1 ATOM 242 C CB . LEU A 1 40 ? 14.023 42.659 31.226 1.00 17.32 ? 73 LEU A CB 1 ATOM 243 C CG . LEU A 1 40 ? 13.612 41.450 30.399 1.00 16.54 ? 73 LEU A CG 1 ATOM 244 C CD1 . LEU A 1 40 ? 14.561 41.157 29.225 1.00 19.65 ? 73 LEU A CD1 1 ATOM 245 C CD2 . LEU A 1 40 ? 13.585 40.252 31.351 1.00 17.28 ? 73 LEU A CD2 1 ATOM 246 N N . ALA A 1 41 ? 12.171 44.121 28.820 1.00 16.33 ? 74 ALA A N 1 ATOM 247 C CA . ALA A 1 41 ? 10.816 44.458 28.375 1.00 16.85 ? 74 ALA A CA 1 ATOM 248 C C . ALA A 1 41 ? 9.811 43.641 29.153 1.00 16.67 ? 74 ALA A C 1 ATOM 249 O O . ALA A 1 41 ? 10.032 42.458 29.469 1.00 18.04 ? 74 ALA A O 1 ATOM 250 C CB . ALA A 1 41 ? 10.725 44.124 26.908 1.00 18.16 ? 74 ALA A CB 1 ATOM 251 N N . GLY A 1 42 ? 8.681 44.310 29.447 1.00 17.59 ? 75 GLY A N 1 ATOM 252 C CA . GLY A 1 42 ? 7.590 43.633 30.115 1.00 19.16 ? 75 GLY A CA 1 ATOM 253 C C . GLY A 1 42 ? 7.703 43.578 31.623 1.00 20.87 ? 75 GLY A C 1 ATOM 254 O O . GLY A 1 42 ? 6.817 43.025 32.276 1.00 24.50 ? 75 GLY A O 1 ATOM 255 N N . THR A 1 43 ? 8.795 44.106 32.190 1.00 19.17 ? 76 THR A N 1 ATOM 256 C CA . THR A 1 43 ? 8.991 44.060 33.619 1.00 18.41 ? 76 THR A CA 1 ATOM 257 C C . THR A 1 43 ? 8.670 45.444 34.229 1.00 18.77 ? 76 THR A C 1 ATOM 258 O O . THR A 1 43 ? 8.639 46.480 33.543 1.00 19.08 ? 76 THR A O 1 ATOM 259 C CB . THR A 1 43 ? 10.416 43.686 34.008 1.00 18.97 ? 76 THR A CB 1 ATOM 260 O OG1 . THR A 1 43 ? 11.339 44.722 33.596 1.00 19.12 ? 76 THR A OG1 1 ATOM 261 C CG2 . THR A 1 43 ? 10.806 42.285 33.411 1.00 19.72 ? 76 THR A CG2 1 ATOM 262 N N . GLU A 1 44 ? 8.436 45.457 35.533 1.00 19.66 ? 77 GLU A N 1 ATOM 263 C CA . GLU A 1 44 ? 8.086 46.714 36.210 1.00 19.13 ? 77 GLU A CA 1 ATOM 264 C C . GLU A 1 44 ? 9.163 47.796 36.009 1.00 19.12 ? 77 GLU A C 1 ATOM 265 O O . GLU A 1 44 ? 8.813 48.969 35.794 1.00 17.73 ? 77 GLU A O 1 ATOM 266 C CB . GLU A 1 44 ? 7.927 46.425 37.691 1.00 20.97 ? 77 GLU A CB 1 ATOM 267 C CG . GLU A 1 44 ? 7.655 47.688 38.467 1.00 24.82 ? 77 GLU A CG 1 ATOM 268 C CD . GLU A 1 44 ? 6.285 48.329 38.201 1.00 31.28 ? 77 GLU A CD 1 ATOM 269 O OE1 . GLU A 1 44 ? 6.056 49.452 38.749 1.00 35.17 ? 77 GLU A OE1 1 ATOM 270 O OE2 . GLU A 1 44 ? 5.405 47.744 37.502 1.00 33.21 ? 77 GLU A OE2 1 ATOM 271 N N . GLN A 1 45 ? 10.438 47.421 36.070 1.00 19.13 ? 78 GLN A N 1 ATOM 272 C CA . GLN A 1 45 ? 11.490 48.437 35.962 1.00 18.92 ? 78 GLN A CA 1 ATOM 273 C C . GLN A 1 45 ? 11.462 49.154 34.600 1.00 18.31 ? 78 GLN A C 1 ATOM 274 O O . GLN A 1 45 ? 11.684 50.395 34.533 1.00 18.11 ? 78 GLN A O 1 ATOM 275 C CB . GLN A 1 45 ? 12.872 47.882 36.267 1.00 20.73 ? 78 GLN A CB 1 ATOM 276 C CG A GLN A 1 45 ? 13.976 48.961 36.326 0.65 24.21 ? 78 GLN A CG 1 ATOM 277 C CG B GLN A 1 45 ? 12.978 47.407 37.713 0.35 16.84 ? 78 GLN A CG 1 ATOM 278 C CD A GLN A 1 45 ? 13.785 49.972 37.450 0.65 29.06 ? 78 GLN A CD 1 ATOM 279 C CD B GLN A 1 45 ? 14.071 46.370 38.006 0.35 21.43 ? 78 GLN A CD 1 ATOM 280 O OE1 A GLN A 1 45 ? 14.149 51.131 37.300 0.65 33.54 ? 78 GLN A OE1 1 ATOM 281 O OE1 B GLN A 1 45 ? 14.357 45.464 37.212 0.35 18.23 ? 78 GLN A OE1 1 ATOM 282 N NE2 A GLN A 1 45 ? 13.200 49.536 38.554 0.65 30.13 ? 78 GLN A NE2 1 ATOM 283 N NE2 B GLN A 1 45 ? 14.653 46.488 39.191 0.35 19.99 ? 78 GLN A NE2 1 ATOM 284 N N . ASN A 1 46 ? 11.126 48.416 33.525 1.00 17.38 ? 79 ASN A N 1 ATOM 285 C CA . ASN A 1 46 ? 11.105 49.095 32.249 1.00 16.81 ? 79 ASN A CA 1 ATOM 286 C C . ASN A 1 46 ? 9.840 49.961 32.082 1.00 17.23 ? 79 ASN A C 1 ATOM 287 O O . ASN A 1 46 ? 9.817 50.897 31.227 1.00 17.93 ? 79 ASN A O 1 ATOM 288 C CB . ASN A 1 46 ? 11.227 48.131 31.074 1.00 17.48 ? 79 ASN A CB 1 ATOM 289 C CG . ASN A 1 46 ? 11.746 48.840 29.847 1.00 18.37 ? 79 ASN A CG 1 ATOM 290 O OD1 . ASN A 1 46 ? 12.681 49.696 29.917 1.00 20.22 ? 79 ASN A OD1 1 ATOM 291 N ND2 . ASN A 1 46 ? 11.125 48.518 28.685 1.00 19.34 ? 79 ASN A ND2 1 ATOM 292 N N . PHE A 1 47 ? 8.783 49.662 32.840 1.00 17.13 ? 80 PHE A N 1 ATOM 293 C CA . PHE A 1 47 ? 7.610 50.568 32.876 1.00 16.71 ? 80 PHE A CA 1 ATOM 294 C C . PHE A 1 47 ? 7.965 51.819 33.664 1.00 17.26 ? 80 PHE A C 1 ATOM 295 O O . PHE A 1 47 ? 7.620 52.944 33.228 1.00 17.57 ? 80 PHE A O 1 ATOM 296 C CB . PHE A 1 47 ? 6.393 49.828 33.466 1.00 17.39 ? 80 PHE A CB 1 ATOM 297 C CG . PHE A 1 47 ? 5.172 50.704 33.759 1.00 20.28 ? 80 PHE A CG 1 ATOM 298 C CD1 . PHE A 1 47 ? 4.440 51.287 32.757 1.00 21.41 ? 80 PHE A CD1 1 ATOM 299 C CD2 . PHE A 1 47 ? 4.758 50.874 35.071 1.00 27.40 ? 80 PHE A CD2 1 ATOM 300 C CE1 . PHE A 1 47 ? 3.315 52.044 33.011 1.00 24.25 ? 80 PHE A CE1 1 ATOM 301 C CE2 . PHE A 1 47 ? 3.641 51.648 35.350 1.00 31.58 ? 80 PHE A CE2 1 ATOM 302 C CZ . PHE A 1 47 ? 2.919 52.230 34.307 1.00 27.04 ? 80 PHE A CZ 1 ATOM 303 N N . LEU A 1 48 ? 8.640 51.628 34.786 1.00 17.84 ? 81 LEU A N 1 ATOM 304 C CA . LEU A 1 48 ? 9.094 52.804 35.565 1.00 17.78 ? 81 LEU A CA 1 ATOM 305 C C . LEU A 1 48 ? 10.005 53.707 34.716 1.00 18.29 ? 81 LEU A C 1 ATOM 306 O O . LEU A 1 48 ? 9.899 54.908 34.760 1.00 19.67 ? 81 LEU A O 1 ATOM 307 C CB . LEU A 1 48 ? 9.791 52.397 36.896 1.00 17.73 ? 81 LEU A CB 1 ATOM 308 C CG . LEU A 1 48 ? 8.931 51.650 37.885 1.00 19.99 ? 81 LEU A CG 1 ATOM 309 C CD1 . LEU A 1 48 ? 9.916 51.254 38.936 1.00 22.32 ? 81 LEU A CD1 1 ATOM 310 C CD2 . LEU A 1 48 ? 7.876 52.668 38.421 1.00 21.09 ? 81 LEU A CD2 1 ATOM 311 N N . LEU A 1 49 ? 10.898 53.117 33.920 1.00 17.35 ? 82 LEU A N 1 ATOM 312 C CA . LEU A 1 49 ? 11.765 53.907 33.070 1.00 17.19 ? 82 LEU A CA 1 ATOM 313 C C . LEU A 1 49 ? 10.922 54.667 32.027 1.00 17.40 ? 82 LEU A C 1 ATOM 314 O O . LEU A 1 49 ? 11.209 55.844 31.690 1.00 17.52 ? 82 LEU A O 1 ATOM 315 C CB . LEU A 1 49 ? 12.802 52.965 32.406 1.00 18.44 ? 82 LEU A CB 1 ATOM 316 C CG . LEU A 1 49 ? 13.765 53.686 31.499 1.00 20.18 ? 82 LEU A CG 1 ATOM 317 C CD1 . LEU A 1 49 ? 14.637 54.694 32.240 1.00 22.60 ? 82 LEU A CD1 1 ATOM 318 C CD2 . LEU A 1 49 ? 14.684 52.620 30.904 1.00 21.26 ? 82 LEU A CD2 1 ATOM 319 N N . ALA A 1 50 ? 9.876 54.016 31.481 1.00 16.73 ? 83 ALA A N 1 ATOM 320 C CA . ALA A 1 50 ? 8.964 54.776 30.556 1.00 16.72 ? 83 ALA A CA 1 ATOM 321 C C . ALA A 1 50 ? 8.364 56.005 31.218 1.00 17.26 ? 83 ALA A C 1 ATOM 322 O O . ALA A 1 50 ? 8.317 57.070 30.624 1.00 18.78 ? 83 ALA A O 1 ATOM 323 C CB . ALA A 1 50 ? 7.795 53.871 30.080 1.00 17.67 ? 83 ALA A CB 1 ATOM 324 N N . LYS A 1 51 ? 7.877 55.809 32.436 1.00 16.87 ? 84 LYS A N 1 ATOM 325 C CA . LYS A 1 51 ? 7.265 56.926 33.172 1.00 16.57 ? 84 LYS A CA 1 ATOM 326 C C . LYS A 1 51 ? 8.288 58.044 33.421 1.00 17.44 ? 84 LYS A C 1 ATOM 327 O O . LYS A 1 51 ? 7.926 59.251 33.365 1.00 18.88 ? 84 LYS A O 1 ATOM 328 C CB . LYS A 1 51 ? 6.622 56.440 34.509 1.00 17.35 ? 84 LYS A CB 1 ATOM 329 C CG . LYS A 1 51 ? 5.318 55.701 34.167 1.00 21.57 ? 84 LYS A CG 1 ATOM 330 C CD . LYS A 1 51 ? 4.444 55.383 35.323 1.00 32.11 ? 84 LYS A CD 1 ATOM 331 C CE . LYS A 1 51 ? 5.049 54.258 36.138 1.00 33.89 ? 84 LYS A CE 1 ATOM 332 N NZ . LYS A 1 51 ? 4.345 54.170 37.449 1.00 39.64 ? 84 LYS A NZ 1 ATOM 333 N N . LYS A 1 52 ? 9.528 57.685 33.733 1.00 17.01 ? 85 LYS A N 1 ATOM 334 C CA . LYS A 1 52 ? 10.581 58.712 33.970 1.00 17.57 ? 85 LYS A CA 1 ATOM 335 C C . LYS A 1 52 ? 10.866 59.504 32.687 1.00 16.95 ? 85 LYS A C 1 ATOM 336 O O . LYS A 1 52 ? 10.953 60.745 32.681 1.00 17.58 ? 85 LYS A O 1 ATOM 337 C CB . LYS A 1 52 ? 11.839 58.027 34.487 1.00 17.87 ? 85 LYS A CB 1 ATOM 338 C CG . LYS A 1 52 ? 13.036 58.937 34.765 1.00 19.85 ? 85 LYS A CG 1 ATOM 339 C CD . LYS A 1 52 ? 14.114 58.074 35.400 1.00 23.88 ? 85 LYS A CD 1 ATOM 340 C CE . LYS A 1 52 ? 15.207 58.867 35.996 1.00 29.38 ? 85 LYS A CE 1 ATOM 341 N NZ . LYS A 1 52 ? 15.015 59.170 37.458 1.00 25.59 ? 85 LYS A NZ 1 ATOM 342 N N . ILE A 1 53 ? 10.964 58.775 31.554 1.00 16.58 ? 86 ILE A N 1 ATOM 343 C CA . ILE A 1 53 ? 11.177 59.435 30.258 1.00 17.49 ? 86 ILE A CA 1 ATOM 344 C C . ILE A 1 53 ? 10.016 60.366 29.923 1.00 17.34 ? 86 ILE A C 1 ATOM 345 O O . ILE A 1 53 ? 10.236 61.471 29.489 1.00 18.23 ? 86 ILE A O 1 ATOM 346 C CB . ILE A 1 53 ? 11.373 58.352 29.145 1.00 17.10 ? 86 ILE A CB 1 ATOM 347 C CG1 . ILE A 1 53 ? 12.773 57.764 29.381 1.00 18.54 ? 86 ILE A CG1 1 ATOM 348 C CG2 . ILE A 1 53 ? 11.228 58.948 27.721 1.00 17.26 ? 86 ILE A CG2 1 ATOM 349 C CD1 . ILE A 1 53 ? 13.050 56.531 28.484 1.00 18.59 ? 86 ILE A CD1 1 ATOM 350 N N . GLN A 1 54 ? 8.782 59.892 30.158 1.00 17.45 ? 87 GLN A N 1 ATOM 351 C CA . GLN A 1 54 ? 7.612 60.723 29.881 1.00 16.84 ? 87 GLN A CA 1 ATOM 352 C C . GLN A 1 54 ? 7.658 62.005 30.789 1.00 17.60 ? 87 GLN A C 1 ATOM 353 O O . GLN A 1 54 ? 7.371 63.100 30.298 1.00 17.08 ? 87 GLN A O 1 ATOM 354 C CB . GLN A 1 54 ? 6.357 59.888 30.234 1.00 18.13 ? 87 GLN A CB 1 ATOM 355 C CG . GLN A 1 54 ? 5.023 60.679 30.182 1.00 18.85 ? 87 GLN A CG 1 ATOM 356 C CD . GLN A 1 54 ? 3.865 59.842 30.610 1.00 22.27 ? 87 GLN A CD 1 ATOM 357 O OE1 . GLN A 1 54 ? 3.961 59.085 31.569 1.00 22.28 ? 87 GLN A OE1 1 ATOM 358 N NE2 . GLN A 1 54 ? 2.780 59.948 29.892 1.00 20.14 ? 87 GLN A NE2 1 ATOM 359 N N . THR A 1 55 ? 7.965 61.868 32.092 1.00 16.75 ? 88 THR A N 1 ATOM 360 C CA . THR A 1 55 ? 8.022 63.044 32.981 1.00 17.19 ? 88 THR A CA 1 ATOM 361 C C . THR A 1 55 ? 9.057 64.001 32.429 1.00 17.59 ? 88 THR A C 1 ATOM 362 O O . THR A 1 55 ? 8.845 65.221 32.385 1.00 18.45 ? 88 THR A O 1 ATOM 363 C CB . THR A 1 55 ? 8.360 62.591 34.362 1.00 17.38 ? 88 THR A CB 1 ATOM 364 O OG1 . THR A 1 55 ? 7.262 61.810 34.858 1.00 20.72 ? 88 THR A OG1 1 ATOM 365 C CG2 . THR A 1 55 ? 8.570 63.778 35.311 1.00 18.69 ? 88 THR A CG2 1 ATOM 366 N N . GLN A 1 56 ? 10.198 63.456 32.002 1.00 16.93 ? 89 GLN A N 1 ATOM 367 C CA . GLN A 1 56 ? 11.244 64.341 31.472 1.00 16.11 ? 89 GLN A CA 1 ATOM 368 C C . GLN A 1 56 ? 10.803 65.076 30.205 1.00 16.86 ? 89 GLN A C 1 ATOM 369 O O . GLN A 1 56 ? 10.990 66.286 30.075 1.00 16.88 ? 89 GLN A O 1 ATOM 370 C CB . GLN A 1 56 ? 12.556 63.581 31.208 1.00 17.53 ? 89 GLN A CB 1 ATOM 371 C CG . GLN A 1 56 ? 13.211 63.148 32.542 1.00 16.94 ? 89 GLN A CG 1 ATOM 372 C CD . GLN A 1 56 ? 14.450 62.282 32.373 1.00 18.40 ? 89 GLN A CD 1 ATOM 373 O OE1 . GLN A 1 56 ? 14.758 61.817 31.284 1.00 19.41 ? 89 GLN A OE1 1 ATOM 374 N NE2 . GLN A 1 56 ? 15.182 62.067 33.468 1.00 17.82 ? 89 GLN A NE2 1 ATOM 375 N N . TRP A 1 57 ? 10.153 64.362 29.295 1.00 16.85 ? 90 TRP A N 1 ATOM 376 C CA . TRP A 1 57 ? 9.724 65.025 28.072 1.00 15.98 ? 90 TRP A CA 1 ATOM 377 C C . TRP A 1 57 ? 8.721 66.133 28.355 1.00 17.03 ? 90 TRP A C 1 ATOM 378 O O . TRP A 1 57 ? 8.778 67.196 27.712 1.00 16.78 ? 90 TRP A O 1 ATOM 379 C CB . TRP A 1 57 ? 9.041 64.021 27.094 1.00 16.29 ? 90 TRP A CB 1 ATOM 380 C CG . TRP A 1 57 ? 10.020 63.095 26.448 1.00 15.91 ? 90 TRP A CG 1 ATOM 381 C CD1 . TRP A 1 57 ? 11.400 63.090 26.599 1.00 18.02 ? 90 TRP A CD1 1 ATOM 382 C CD2 . TRP A 1 57 ? 9.698 62.048 25.504 1.00 15.81 ? 90 TRP A CD2 1 ATOM 383 N NE1 . TRP A 1 57 ? 11.948 62.080 25.801 1.00 17.89 ? 90 TRP A NE1 1 ATOM 384 C CE2 . TRP A 1 57 ? 10.925 61.431 25.137 1.00 15.84 ? 90 TRP A CE2 1 ATOM 385 C CE3 . TRP A 1 57 ? 8.486 61.556 24.940 1.00 17.03 ? 90 TRP A CE3 1 ATOM 386 C CZ2 . TRP A 1 57 ? 10.978 60.344 24.241 1.00 16.73 ? 90 TRP A CZ2 1 ATOM 387 C CZ3 . TRP A 1 57 ? 8.547 60.479 24.072 1.00 19.75 ? 90 TRP A CZ3 1 ATOM 388 C CH2 . TRP A 1 57 ? 9.766 59.870 23.739 1.00 19.08 ? 90 TRP A CH2 1 ATOM 389 N N . LYS A 1 58 ? 7.833 65.936 29.327 1.00 16.92 ? 91 LYS A N 1 ATOM 390 C CA . LYS A 1 58 ? 6.908 67.021 29.679 1.00 17.55 ? 91 LYS A CA 1 ATOM 391 C C . LYS A 1 58 ? 7.707 68.205 30.253 1.00 17.70 ? 91 LYS A C 1 ATOM 392 O O . LYS A 1 58 ? 7.397 69.372 29.930 1.00 19.48 ? 91 LYS A O 1 ATOM 393 C CB . LYS A 1 58 ? 5.863 66.516 30.702 1.00 18.41 ? 91 LYS A CB 1 ATOM 394 C CG . LYS A 1 58 ? 4.824 65.609 29.985 1.00 19.81 ? 91 LYS A CG 1 ATOM 395 C CD . LYS A 1 58 ? 3.828 64.978 30.962 1.00 24.77 ? 91 LYS A CD 1 ATOM 396 C CE . LYS A 1 58 ? 2.876 64.103 30.106 1.00 28.28 ? 91 LYS A CE 1 ATOM 397 N NZ . LYS A 1 58 ? 1.777 63.671 31.057 1.00 33.39 ? 91 LYS A NZ 1 ATOM 398 N N . LYS A 1 59 ? 8.679 67.901 31.114 1.00 17.78 ? 92 LYS A N 1 ATOM 399 C CA . LYS A 1 59 ? 9.502 68.962 31.710 1.00 17.86 ? 92 LYS A CA 1 ATOM 400 C C . LYS A 1 59 ? 10.259 69.746 30.630 1.00 18.66 ? 92 LYS A C 1 ATOM 401 O O . LYS A 1 59 ? 10.385 70.978 30.686 1.00 18.31 ? 92 LYS A O 1 ATOM 402 C CB . LYS A 1 59 ? 10.486 68.368 32.718 1.00 19.83 ? 92 LYS A CB 1 ATOM 403 C CG . LYS A 1 59 ? 11.409 69.385 33.408 1.00 22.50 ? 92 LYS A CG 1 ATOM 404 C CD . LYS A 1 59 ? 12.301 68.623 34.454 1.00 27.41 ? 92 LYS A CD 1 ATOM 405 C CE . LYS A 1 59 ? 13.360 67.739 33.820 1.00 28.50 ? 92 LYS A CE 1 ATOM 406 N NZ . LYS A 1 59 ? 14.087 66.945 34.864 1.00 35.31 ? 92 LYS A NZ 1 ATOM 407 N N . PHE A 1 60 ? 10.750 69.034 29.621 1.00 18.40 ? 93 PHE A N 1 ATOM 408 C CA . PHE A 1 60 ? 11.467 69.675 28.524 1.00 19.28 ? 93 PHE A CA 1 ATOM 409 C C . PHE A 1 60 ? 10.580 70.577 27.674 1.00 18.28 ? 93 PHE A C 1 ATOM 410 O O . PHE A 1 60 ? 11.102 71.407 26.953 1.00 21.65 ? 93 PHE A O 1 ATOM 411 C CB . PHE A 1 60 ? 12.059 68.604 27.579 1.00 18.29 ? 93 PHE A CB 1 ATOM 412 C CG . PHE A 1 60 ? 13.055 67.688 28.223 1.00 19.10 ? 93 PHE A CG 1 ATOM 413 C CD1 . PHE A 1 60 ? 13.762 68.017 29.409 1.00 21.64 ? 93 PHE A CD1 1 ATOM 414 C CD2 . PHE A 1 60 ? 13.342 66.474 27.586 1.00 19.58 ? 93 PHE A CD2 1 ATOM 415 C CE1 . PHE A 1 60 ? 14.698 67.120 29.963 1.00 19.45 ? 93 PHE A CE1 1 ATOM 416 C CE2 . PHE A 1 60 ? 14.269 65.583 28.155 1.00 20.57 ? 93 PHE A CE2 1 ATOM 417 C CZ . PHE A 1 60 ? 14.936 65.919 29.360 1.00 19.05 ? 93 PHE A CZ 1 ATOM 418 N N . GLY A 1 61 ? 9.269 70.414 27.745 1.00 19.14 ? 94 GLY A N 1 ATOM 419 C CA . GLY A 1 61 ? 8.343 71.327 27.026 1.00 19.57 ? 94 GLY A CA 1 ATOM 420 C C . GLY A 1 61 ? 7.725 70.706 25.794 1.00 20.89 ? 94 GLY A C 1 ATOM 421 O O . GLY A 1 61 ? 7.162 71.415 24.982 1.00 21.30 ? 94 GLY A O 1 ATOM 422 N N . LEU A 1 62 ? 7.842 69.395 25.615 1.00 19.72 ? 95 LEU A N 1 ATOM 423 C CA . LEU A 1 62 ? 7.155 68.786 24.470 1.00 18.85 ? 95 LEU A CA 1 ATOM 424 C C . LEU A 1 62 ? 5.646 69.000 24.541 1.00 18.92 ? 95 LEU A C 1 ATOM 425 O O . LEU A 1 62 ? 5.069 69.126 25.675 1.00 20.48 ? 95 LEU A O 1 ATOM 426 C CB A LEU A 1 62 ? 7.430 67.261 24.406 0.65 19.60 ? 95 LEU A CB 1 ATOM 427 C CB B LEU A 1 62 ? 7.492 67.288 24.349 0.35 18.16 ? 95 LEU A CB 1 ATOM 428 C CG A LEU A 1 62 ? 8.871 66.728 24.250 0.65 25.23 ? 95 LEU A CG 1 ATOM 429 C CG B LEU A 1 62 ? 8.719 66.942 23.484 0.35 13.71 ? 95 LEU A CG 1 ATOM 430 C CD1 A LEU A 1 62 ? 8.880 65.337 23.580 0.65 23.06 ? 95 LEU A CD1 1 ATOM 431 C CD1 B LEU A 1 62 ? 9.982 67.533 24.096 0.35 16.65 ? 95 LEU A CD1 1 ATOM 432 C CD2 A LEU A 1 62 ? 9.814 67.659 23.570 0.65 25.96 ? 95 LEU A CD2 1 ATOM 433 C CD2 B LEU A 1 62 ? 8.834 65.410 23.424 0.35 15.18 ? 95 LEU A CD2 1 ATOM 434 N N . ASP A 1 63 ? 5.008 69.012 23.372 1.00 18.73 ? 96 ASP A N 1 ATOM 435 C CA . ASP A 1 63 ? 3.552 69.245 23.367 1.00 19.55 ? 96 ASP A CA 1 ATOM 436 C C . ASP A 1 63 ? 2.742 68.095 23.940 1.00 20.35 ? 96 ASP A C 1 ATOM 437 O O . ASP A 1 63 ? 1.663 68.287 24.480 1.00 22.84 ? 96 ASP A O 1 ATOM 438 C CB . ASP A 1 63 ? 3.049 69.457 21.945 1.00 20.13 ? 96 ASP A CB 1 ATOM 439 C CG . ASP A 1 63 ? 3.603 70.697 21.294 1.00 21.20 ? 96 ASP A CG 1 ATOM 440 O OD1 . ASP A 1 63 ? 3.944 71.684 21.993 1.00 26.30 ? 96 ASP A OD1 1 ATOM 441 O OD2 . ASP A 1 63 ? 3.531 70.787 20.084 1.00 24.85 ? 96 ASP A OD2 1 ATOM 442 N N . SER A 1 64 ? 3.241 66.867 23.772 1.00 18.88 ? 97 SER A N 1 ATOM 443 C CA . SER A 1 64 ? 2.564 65.728 24.338 1.00 19.02 ? 97 SER A CA 1 ATOM 444 C C . SER A 1 64 ? 3.661 64.700 24.702 1.00 18.97 ? 97 SER A C 1 ATOM 445 O O . SER A 1 64 ? 4.800 64.753 24.143 1.00 18.70 ? 97 SER A O 1 ATOM 446 C CB . SER A 1 64 ? 1.619 65.108 23.312 1.00 20.29 ? 97 SER A CB 1 ATOM 447 O OG . SER A 1 64 ? 2.344 64.565 22.205 1.00 21.25 ? 97 SER A OG 1 ATOM 448 N N . ALA A 1 65 ? 3.311 63.759 25.584 1.00 19.39 ? 98 ALA A N 1 ATOM 449 C CA . ALA A 1 65 ? 4.194 62.592 25.890 1.00 20.10 ? 98 ALA A CA 1 ATOM 450 C C . ALA A 1 65 ? 3.296 61.559 26.543 1.00 19.10 ? 98 ALA A C 1 ATOM 451 O O . ALA A 1 65 ? 2.845 61.727 27.706 1.00 20.28 ? 98 ALA A O 1 ATOM 452 C CB . ALA A 1 65 ? 5.307 63.022 26.803 1.00 20.06 ? 98 ALA A CB 1 ATOM 453 N N . LYS A 1 66 ? 2.942 60.552 25.760 1.00 18.34 ? 99 LYS A N 1 ATOM 454 C CA . LYS A 1 66 ? 1.941 59.575 26.203 1.00 19.51 ? 99 LYS A CA 1 ATOM 455 C C . LYS A 1 66 ? 2.506 58.164 26.212 1.00 18.17 ? 99 LYS A C 1 ATOM 456 O O . LYS A 1 66 ? 3.394 57.837 25.385 1.00 19.62 ? 99 LYS A O 1 ATOM 457 C CB . LYS A 1 66 ? 0.724 59.571 25.251 1.00 20.78 ? 99 LYS A CB 1 ATOM 458 C CG A LYS A 1 66 ? -0.090 60.878 25.240 0.65 23.72 ? 99 LYS A CG 1 ATOM 459 C CG B LYS A 1 66 ? 0.927 59.013 23.878 0.35 23.94 ? 99 LYS A CG 1 ATOM 460 C CD A LYS A 1 66 ? -1.190 60.776 24.135 0.65 26.27 ? 99 LYS A CD 1 ATOM 461 C CD B LYS A 1 66 ? 0.685 60.010 22.750 0.35 27.12 ? 99 LYS A CD 1 ATOM 462 C CE A LYS A 1 66 ? -1.462 62.140 23.559 0.65 33.22 ? 99 LYS A CE 1 ATOM 463 C CE B LYS A 1 66 ? 0.487 59.287 21.417 0.35 24.73 ? 99 LYS A CE 1 ATOM 464 N NZ A LYS A 1 66 ? -1.811 63.115 24.631 0.65 36.67 ? 99 LYS A NZ 1 ATOM 465 N NZ B LYS A 1 66 ? -0.738 58.468 21.415 0.35 22.19 ? 99 LYS A NZ 1 ATOM 466 N N . LEU A 1 67 ? 1.971 57.303 27.079 1.00 18.95 ? 100 LEU A N 1 ATOM 467 C CA . LEU A 1 67 ? 2.296 55.861 27.004 1.00 19.56 ? 100 LEU A CA 1 ATOM 468 C C . LEU A 1 67 ? 1.294 55.195 26.105 1.00 20.99 ? 100 LEU A C 1 ATOM 469 O O . LEU A 1 67 ? 0.069 55.421 26.217 1.00 22.53 ? 100 LEU A O 1 ATOM 470 C CB A LEU A 1 67 ? 2.296 55.205 28.398 0.65 20.44 ? 100 LEU A CB 1 ATOM 471 C CB B LEU A 1 67 ? 2.199 55.257 28.404 0.35 19.07 ? 100 LEU A CB 1 ATOM 472 C CG A LEU A 1 67 ? 3.691 55.185 29.082 0.65 24.14 ? 100 LEU A CG 1 ATOM 473 C CG B LEU A 1 67 ? 3.062 55.902 29.498 0.35 16.96 ? 100 LEU A CG 1 ATOM 474 C CD1 A LEU A 1 67 ? 4.203 56.590 29.351 0.65 25.59 ? 100 LEU A CD1 1 ATOM 475 C CD1 B LEU A 1 67 ? 2.874 55.114 30.780 0.35 17.85 ? 100 LEU A CD1 1 ATOM 476 C CD2 A LEU A 1 67 ? 3.736 54.360 30.345 0.65 25.24 ? 100 LEU A CD2 1 ATOM 477 C CD2 B LEU A 1 67 ? 4.537 55.902 29.066 0.35 17.71 ? 100 LEU A CD2 1 ATOM 478 N N . VAL A 1 68 ? 1.813 54.440 25.163 1.00 19.17 ? 101 VAL A N 1 ATOM 479 C CA . VAL A 1 68 ? 0.993 53.705 24.203 1.00 18.97 ? 101 VAL A CA 1 ATOM 480 C C . VAL A 1 68 ? 1.321 52.226 24.400 1.00 19.25 ? 101 VAL A C 1 ATOM 481 O O . VAL A 1 68 ? 2.468 51.826 24.173 1.00 19.39 ? 101 VAL A O 1 ATOM 482 C CB . VAL A 1 68 ? 1.303 54.127 22.775 1.00 19.71 ? 101 VAL A CB 1 ATOM 483 C CG1 . VAL A 1 68 ? 0.462 53.323 21.808 1.00 21.91 ? 101 VAL A CG1 1 ATOM 484 C CG2 . VAL A 1 68 ? 1.051 55.630 22.595 1.00 20.51 ? 101 VAL A CG2 1 ATOM 485 N N . HIS A 1 69 ? 0.326 51.423 24.774 1.00 18.22 ? 102 HIS A N 1 ATOM 486 C CA . HIS A 1 69 ? 0.618 50.016 25.072 1.00 19.24 ? 102 HIS A CA 1 ATOM 487 C C . HIS A 1 69 ? 0.052 49.050 24.045 1.00 19.87 ? 102 HIS A C 1 ATOM 488 O O . HIS A 1 69 ? -0.827 49.344 23.237 1.00 19.33 ? 102 HIS A O 1 ATOM 489 C CB . HIS A 1 69 ? 0.065 49.683 26.456 1.00 20.01 ? 102 HIS A CB 1 ATOM 490 C CG . HIS A 1 69 ? -1.429 49.688 26.533 1.00 19.53 ? 102 HIS A CG 1 ATOM 491 N ND1 . HIS A 1 69 ? -2.160 50.770 26.983 1.00 25.35 ? 102 HIS A ND1 1 ATOM 492 C CD2 . HIS A 1 69 ? -2.331 48.711 26.244 1.00 23.28 ? 102 HIS A CD2 1 ATOM 493 C CE1 . HIS A 1 69 ? -3.447 50.460 26.965 1.00 25.88 ? 102 HIS A CE1 1 ATOM 494 N NE2 . HIS A 1 69 ? -3.581 49.224 26.516 1.00 24.92 ? 102 HIS A NE2 1 ATOM 495 N N . TYR A 1 70 ? 0.681 47.867 24.093 1.00 17.72 ? 103 TYR A N 1 ATOM 496 C CA . TYR A 1 70 ? 0.269 46.709 23.274 1.00 18.63 ? 103 TYR A CA 1 ATOM 497 C C . TYR A 1 70 ? 0.460 45.483 24.124 1.00 18.31 ? 103 TYR A C 1 ATOM 498 O O . TYR A 1 70 ? 1.228 45.506 25.119 1.00 18.99 ? 103 TYR A O 1 ATOM 499 C CB . TYR A 1 70 ? 1.145 46.512 22.004 1.00 18.72 ? 103 TYR A CB 1 ATOM 500 C CG . TYR A 1 70 ? 1.061 47.733 21.138 1.00 18.81 ? 103 TYR A CG 1 ATOM 501 C CD1 . TYR A 1 70 ? -0.040 47.957 20.296 1.00 19.57 ? 103 TYR A CD1 1 ATOM 502 C CD2 . TYR A 1 70 ? 2.062 48.704 21.207 1.00 19.52 ? 103 TYR A CD2 1 ATOM 503 C CE1 . TYR A 1 70 ? -0.139 49.116 19.544 1.00 17.78 ? 103 TYR A CE1 1 ATOM 504 C CE2 . TYR A 1 70 ? 1.972 49.893 20.456 1.00 19.56 ? 103 TYR A CE2 1 ATOM 505 C CZ . TYR A 1 70 ? 0.861 50.117 19.657 1.00 18.67 ? 103 TYR A CZ 1 ATOM 506 O OH . TYR A 1 70 ? 0.772 51.267 18.925 1.00 20.14 ? 103 TYR A OH 1 ATOM 507 N N . ASP A 1 71 ? -0.254 44.399 23.813 1.00 17.59 ? 104 ASP A N 1 ATOM 508 C CA . ASP A 1 71 ? -0.114 43.150 24.590 1.00 17.51 ? 104 ASP A CA 1 ATOM 509 C C . ASP A 1 71 ? 0.436 42.109 23.610 1.00 17.97 ? 104 ASP A C 1 ATOM 510 O O . ASP A 1 71 ? -0.287 41.714 22.661 1.00 17.38 ? 104 ASP A O 1 ATOM 511 C CB . ASP A 1 71 ? -1.495 42.689 25.126 1.00 17.83 ? 104 ASP A CB 1 ATOM 512 C CG . ASP A 1 71 ? -2.026 43.658 26.184 1.00 18.50 ? 104 ASP A CG 1 ATOM 513 O OD1 . ASP A 1 71 ? -1.275 43.927 27.130 1.00 20.63 ? 104 ASP A OD1 1 ATOM 514 O OD2 . ASP A 1 71 ? -3.178 44.132 26.068 1.00 22.14 ? 104 ASP A OD2 1 ATOM 515 N N . VAL A 1 72 ? 1.707 41.752 23.783 1.00 16.06 ? 105 VAL A N 1 ATOM 516 C CA . VAL A 1 72 ? 2.425 40.993 22.765 1.00 16.97 ? 105 VAL A CA 1 ATOM 517 C C . VAL A 1 72 ? 3.037 39.750 23.384 1.00 18.17 ? 105 VAL A C 1 ATOM 518 O O . VAL A 1 72 ? 3.222 39.684 24.613 1.00 17.53 ? 105 VAL A O 1 ATOM 519 C CB . VAL A 1 72 ? 3.578 41.854 22.130 1.00 16.53 ? 105 VAL A CB 1 ATOM 520 C CG1 . VAL A 1 72 ? 3.020 43.174 21.423 1.00 18.03 ? 105 VAL A CG1 1 ATOM 521 C CG2 . VAL A 1 72 ? 4.659 42.223 23.152 1.00 16.77 ? 105 VAL A CG2 1 ATOM 522 N N . LEU A 1 73 ? 3.385 38.771 22.544 1.00 16.67 ? 106 LEU A N 1 ATOM 523 C CA . LEU A 1 73 ? 3.997 37.557 23.120 1.00 15.70 ? 106 LEU A CA 1 ATOM 524 C C . LEU A 1 73 ? 5.453 37.824 23.473 1.00 17.66 ? 106 LEU A C 1 ATOM 525 O O . LEU A 1 73 ? 6.246 38.195 22.586 1.00 17.38 ? 106 LEU A O 1 ATOM 526 C CB . LEU A 1 73 ? 3.955 36.445 22.050 1.00 16.99 ? 106 LEU A CB 1 ATOM 527 C CG . LEU A 1 73 ? 4.286 35.059 22.654 1.00 16.71 ? 106 LEU A CG 1 ATOM 528 C CD1 . LEU A 1 73 ? 3.116 34.551 23.566 1.00 19.27 ? 106 LEU A CD1 1 ATOM 529 C CD2 . LEU A 1 73 ? 4.496 34.055 21.473 1.00 17.82 ? 106 LEU A CD2 1 ATOM 530 N N . LEU A 1 74 ? 5.783 37.683 24.780 1.00 17.59 ? 107 LEU A N 1 ATOM 531 C CA . LEU A 1 74 ? 7.181 37.709 25.241 1.00 15.45 ? 107 LEU A CA 1 ATOM 532 C C . LEU A 1 74 ? 7.562 36.334 25.756 1.00 16.60 ? 107 LEU A C 1 ATOM 533 O O . LEU A 1 74 ? 6.737 35.411 25.755 1.00 18.01 ? 107 LEU A O 1 ATOM 534 C CB . LEU A 1 74 ? 7.408 38.801 26.318 1.00 16.99 ? 107 LEU A CB 1 ATOM 535 C CG . LEU A 1 74 ? 7.022 40.240 25.880 1.00 16.81 ? 107 LEU A CG 1 ATOM 536 C CD1 . LEU A 1 74 ? 7.439 41.205 26.972 1.00 17.02 ? 107 LEU A CD1 1 ATOM 537 C CD2 . LEU A 1 74 ? 7.772 40.623 24.550 1.00 19.88 ? 107 LEU A CD2 1 ATOM 538 N N . SER A 1 75 ? 8.809 36.195 26.185 1.00 17.08 ? 108 SER A N 1 ATOM 539 C CA . SER A 1 75 ? 9.351 34.871 26.565 1.00 16.10 ? 108 SER A CA 1 ATOM 540 C C . SER A 1 75 ? 10.374 35.076 27.650 1.00 16.81 ? 108 SER A C 1 ATOM 541 O O . SER A 1 75 ? 11.222 35.950 27.528 1.00 18.07 ? 108 SER A O 1 ATOM 542 C CB . SER A 1 75 ? 10.016 34.236 25.330 1.00 17.56 ? 108 SER A CB 1 ATOM 543 O OG . SER A 1 75 ? 10.792 33.097 25.730 1.00 18.00 ? 108 SER A OG 1 ATOM 544 N N . TYR A 1 76 ? 10.253 34.272 28.718 1.00 15.74 ? 109 TYR A N 1 ATOM 545 C CA . TYR A 1 76 ? 11.138 34.403 29.866 1.00 17.57 ? 109 TYR A CA 1 ATOM 546 C C . TYR A 1 76 ? 11.484 33.023 30.423 1.00 17.76 ? 109 TYR A C 1 ATOM 547 O O . TYR A 1 76 ? 10.707 32.082 30.250 1.00 17.98 ? 109 TYR A O 1 ATOM 548 C CB . TYR A 1 76 ? 10.387 35.133 30.990 1.00 17.07 ? 109 TYR A CB 1 ATOM 549 C CG . TYR A 1 76 ? 9.900 36.517 30.679 1.00 17.29 ? 109 TYR A CG 1 ATOM 550 C CD1 . TYR A 1 76 ? 10.784 37.637 30.638 1.00 19.09 ? 109 TYR A CD1 1 ATOM 551 C CD2 . TYR A 1 76 ? 8.556 36.731 30.398 1.00 21.42 ? 109 TYR A CD2 1 ATOM 552 C CE1 . TYR A 1 76 ? 10.291 38.933 30.354 1.00 21.33 ? 109 TYR A CE1 1 ATOM 553 C CE2 . TYR A 1 76 ? 8.078 37.991 30.108 1.00 20.22 ? 109 TYR A CE2 1 ATOM 554 C CZ . TYR A 1 76 ? 8.939 39.126 30.141 1.00 20.02 ? 109 TYR A CZ 1 ATOM 555 O OH . TYR A 1 76 ? 8.389 40.386 29.913 1.00 19.94 ? 109 TYR A OH 1 ATOM 556 N N . PRO A 1 77 ? 12.654 32.892 31.095 1.00 18.36 ? 110 PRO A N 1 ATOM 557 C CA . PRO A 1 77 ? 12.948 31.622 31.793 1.00 18.08 ? 110 PRO A CA 1 ATOM 558 C C . PRO A 1 77 ? 11.913 31.340 32.893 1.00 19.13 ? 110 PRO A C 1 ATOM 559 O O . PRO A 1 77 ? 11.310 32.278 33.435 1.00 20.22 ? 110 PRO A O 1 ATOM 560 C CB . PRO A 1 77 ? 14.326 31.861 32.443 1.00 20.02 ? 110 PRO A CB 1 ATOM 561 C CG . PRO A 1 77 ? 14.959 32.944 31.626 1.00 21.80 ? 110 PRO A CG 1 ATOM 562 C CD . PRO A 1 77 ? 13.759 33.863 31.202 1.00 17.15 ? 110 PRO A CD 1 ATOM 563 N N . ASN A 1 78 ? 11.729 30.054 33.171 1.00 19.39 ? 111 ASN A N 1 ATOM 564 C CA . ASN A 1 78 ? 10.857 29.664 34.298 1.00 20.79 ? 111 ASN A CA 1 ATOM 565 C C . ASN A 1 78 ? 11.761 29.711 35.531 1.00 22.62 ? 111 ASN A C 1 ATOM 566 O O . ASN A 1 78 ? 12.743 28.979 35.649 1.00 22.59 ? 111 ASN A O 1 ATOM 567 C CB . ASN A 1 78 ? 10.290 28.291 34.015 1.00 20.73 ? 111 ASN A CB 1 ATOM 568 C CG . ASN A 1 78 ? 9.359 27.818 35.106 1.00 24.92 ? 111 ASN A CG 1 ATOM 569 O OD1 . ASN A 1 78 ? 9.484 28.253 36.235 1.00 26.13 ? 111 ASN A OD1 1 ATOM 570 N ND2 . ASN A 1 78 ? 8.420 26.968 34.751 1.00 28.11 ? 111 ASN A ND2 1 ATOM 571 N N . GLU A 1 79 ? 11.394 30.613 36.446 1.00 26.02 ? 112 GLU A N 1 ATOM 572 C CA . GLU A 1 79 ? 12.165 30.788 37.685 1.00 29.70 ? 112 GLU A CA 1 ATOM 573 C C . GLU A 1 79 ? 12.227 29.512 38.527 1.00 29.86 ? 112 GLU A C 1 ATOM 574 O O . GLU A 1 79 ? 13.145 29.372 39.338 1.00 32.90 ? 112 GLU A O 1 ATOM 575 C CB . GLU A 1 79 ? 11.591 31.971 38.506 1.00 29.20 ? 112 GLU A CB 1 ATOM 576 C CG . GLU A 1 79 ? 11.567 33.329 37.745 1.00 35.01 ? 112 GLU A CG 1 ATOM 577 C CD . GLU A 1 79 ? 10.826 34.431 38.497 1.00 43.60 ? 112 GLU A CD 1 ATOM 578 O OE1 . GLU A 1 79 ? 10.615 34.293 39.730 1.00 47.84 ? 112 GLU A OE1 1 ATOM 579 O OE2 . GLU A 1 79 ? 10.451 35.439 37.838 1.00 47.88 ? 112 GLU A OE2 1 ATOM 580 N N . THR A 1 80 ? 11.309 28.563 38.341 1.00 29.87 ? 113 THR A N 1 ATOM 581 C CA . THR A 1 80 ? 11.342 27.314 39.125 1.00 30.07 ? 113 THR A CA 1 ATOM 582 C C . THR A 1 80 ? 11.643 26.052 38.303 1.00 30.65 ? 113 THR A C 1 ATOM 583 O O . THR A 1 80 ? 11.469 24.914 38.788 1.00 31.87 ? 113 THR A O 1 ATOM 584 C CB . THR A 1 80 ? 10.043 27.105 39.938 1.00 30.52 ? 113 THR A CB 1 ATOM 585 O OG1 . THR A 1 80 ? 8.916 26.942 39.069 1.00 29.81 ? 113 THR A OG1 1 ATOM 586 C CG2 . THR A 1 80 ? 9.802 28.268 40.867 1.00 33.17 ? 113 THR A CG2 1 ATOM 587 N N . ASN A 1 81 ? 12.128 26.232 37.054 1.00 28.30 ? 114 ASN A N 1 ATOM 588 C CA . ASN A 1 81 ? 12.606 25.112 36.245 1.00 26.95 ? 114 ASN A CA 1 ATOM 589 C C . ASN A 1 81 ? 13.724 25.694 35.370 1.00 25.95 ? 114 ASN A C 1 ATOM 590 O O . ASN A 1 81 ? 13.486 26.062 34.193 1.00 26.74 ? 114 ASN A O 1 ATOM 591 C CB . ASN A 1 81 ? 11.483 24.488 35.411 1.00 26.62 ? 114 ASN A CB 1 ATOM 592 C CG . ASN A 1 81 ? 11.840 23.126 34.842 1.00 27.39 ? 114 ASN A CG 1 ATOM 593 O OD1 . ASN A 1 81 ? 12.850 22.529 35.217 1.00 31.45 ? 114 ASN A OD1 1 ATOM 594 N ND2 . ASN A 1 81 ? 10.988 22.601 33.969 1.00 29.74 ? 114 ASN A ND2 1 ATOM 595 N N . ALA A 1 82 ? 14.913 25.783 35.958 1.00 25.29 ? 115 ALA A N 1 ATOM 596 C CA . ALA A 1 82 ? 16.042 26.509 35.327 1.00 24.30 ? 115 ALA A CA 1 ATOM 597 C C . ALA A 1 82 ? 16.587 25.723 34.148 1.00 22.23 ? 115 ALA A C 1 ATOM 598 O O . ALA A 1 82 ? 16.581 24.503 34.141 1.00 23.07 ? 115 ALA A O 1 ATOM 599 C CB . ALA A 1 82 ? 17.141 26.745 36.329 1.00 26.09 ? 115 ALA A CB 1 ATOM 600 N N . ASN A 1 83 ? 16.987 26.479 33.111 1.00 19.92 ? 116 ASN A N 1 ATOM 601 C CA . ASN A 1 83 ? 17.556 25.822 31.918 1.00 18.49 ? 116 ASN A CA 1 ATOM 602 C C . ASN A 1 83 ? 18.988 25.346 32.210 1.00 19.20 ? 116 ASN A C 1 ATOM 603 O O . ASN A 1 83 ? 19.751 26.060 32.929 1.00 21.38 ? 116 ASN A O 1 ATOM 604 C CB . ASN A 1 83 ? 17.645 26.900 30.853 1.00 19.65 ? 116 ASN A CB 1 ATOM 605 C CG . ASN A 1 83 ? 16.311 27.479 30.501 1.00 19.77 ? 116 ASN A CG 1 ATOM 606 O OD1 . ASN A 1 83 ? 15.294 26.772 30.475 1.00 20.51 ? 116 ASN A OD1 1 ATOM 607 N ND2 . ASN A 1 83 ? 16.291 28.786 30.193 1.00 17.56 ? 116 ASN A ND2 1 ATOM 608 N N . TYR A 1 84 ? 19.402 24.287 31.509 1.00 18.52 ? 117 TYR A N 1 ATOM 609 C CA . TYR A 1 84 ? 20.819 23.919 31.566 1.00 18.84 ? 117 TYR A CA 1 ATOM 610 C C . TYR A 1 84 ? 21.137 22.964 30.425 1.00 18.37 ? 117 TYR A C 1 ATOM 611 O O . TYR A 1 84 ? 20.219 22.472 29.714 1.00 18.88 ? 117 TYR A O 1 ATOM 612 C CB . TYR A 1 84 ? 21.180 23.231 32.924 1.00 21.21 ? 117 TYR A CB 1 ATOM 613 C CG . TYR A 1 84 ? 20.385 21.956 33.186 1.00 22.44 ? 117 TYR A CG 1 ATOM 614 C CD1 . TYR A 1 84 ? 20.801 20.708 32.678 1.00 27.07 ? 117 TYR A CD1 1 ATOM 615 C CD2 . TYR A 1 84 ? 19.194 22.001 33.940 1.00 25.38 ? 117 TYR A CD2 1 ATOM 616 C CE1 . TYR A 1 84 ? 20.042 19.531 32.927 1.00 27.19 ? 117 TYR A CE1 1 ATOM 617 C CE2 . TYR A 1 84 ? 18.434 20.819 34.184 1.00 26.45 ? 117 TYR A CE2 1 ATOM 618 C CZ . TYR A 1 84 ? 18.869 19.611 33.675 1.00 28.03 ? 117 TYR A CZ 1 ATOM 619 O OH . TYR A 1 84 ? 18.102 18.469 33.940 1.00 31.07 ? 117 TYR A OH 1 ATOM 620 N N . ILE A 1 85 ? 22.450 22.721 30.259 1.00 18.25 ? 118 ILE A N 1 ATOM 621 C CA . ILE A 1 85 ? 22.915 21.689 29.342 1.00 18.26 ? 118 ILE A CA 1 ATOM 622 C C . ILE A 1 85 ? 23.766 20.750 30.187 1.00 17.38 ? 118 ILE A C 1 ATOM 623 O O . ILE A 1 85 ? 24.456 21.205 31.094 1.00 18.27 ? 118 ILE A O 1 ATOM 624 C CB . ILE A 1 85 ? 23.783 22.330 28.212 1.00 19.23 ? 118 ILE A CB 1 ATOM 625 C CG1 . ILE A 1 85 ? 22.884 23.234 27.324 1.00 21.86 ? 118 ILE A CG1 1 ATOM 626 C CG2 . ILE A 1 85 ? 24.554 21.278 27.392 1.00 19.58 ? 118 ILE A CG2 1 ATOM 627 C CD1 . ILE A 1 85 ? 23.725 24.314 26.797 1.00 23.92 ? 118 ILE A CD1 1 ATOM 628 N N . SER A 1 86 ? 23.706 19.461 29.875 1.00 16.64 ? 119 SER A N 1 ATOM 629 C CA . SER A 1 86 ? 24.501 18.505 30.643 1.00 15.92 ? 119 SER A CA 1 ATOM 630 C C . SER A 1 86 ? 25.138 17.476 29.729 1.00 16.71 ? 119 SER A C 1 ATOM 631 O O . SER A 1 86 ? 24.750 17.317 28.521 1.00 16.58 ? 119 SER A O 1 ATOM 632 C CB . SER A 1 86 ? 23.612 17.798 31.698 1.00 18.81 ? 119 SER A CB 1 ATOM 633 O OG . SER A 1 86 ? 22.626 16.950 31.104 1.00 18.50 ? 119 SER A OG 1 ATOM 634 N N . ILE A 1 87 ? 26.127 16.784 30.282 1.00 14.75 ? 120 ILE A N 1 ATOM 635 C CA . ILE A 1 87 ? 26.738 15.633 29.626 1.00 15.65 ? 120 ILE A CA 1 ATOM 636 C C . ILE A 1 87 ? 26.482 14.439 30.530 1.00 16.90 ? 120 ILE A C 1 ATOM 637 O O . ILE A 1 87 ? 26.713 14.546 31.725 1.00 17.58 ? 120 ILE A O 1 ATOM 638 C CB . ILE A 1 87 ? 28.236 15.818 29.466 1.00 15.44 ? 120 ILE A CB 1 ATOM 639 C CG1 . ILE A 1 87 ? 28.440 17.052 28.532 1.00 19.17 ? 120 ILE A CG1 1 ATOM 640 C CG2 . ILE A 1 87 ? 28.833 14.524 28.908 1.00 19.22 ? 120 ILE A CG2 1 ATOM 641 C CD1 . ILE A 1 87 ? 29.876 17.435 28.397 1.00 22.39 ? 120 ILE A CD1 1 ATOM 642 N N . VAL A 1 88 ? 26.035 13.331 29.954 1.00 16.80 ? 121 VAL A N 1 ATOM 643 C CA . VAL A 1 88 ? 25.850 12.104 30.727 1.00 17.61 ? 121 VAL A CA 1 ATOM 644 C C . VAL A 1 88 ? 26.694 10.993 30.184 1.00 18.00 ? 121 VAL A C 1 ATOM 645 O O . VAL A 1 88 ? 27.136 11.002 29.007 1.00 18.98 ? 121 VAL A O 1 ATOM 646 C CB . VAL A 1 88 ? 24.388 11.650 30.748 1.00 18.89 ? 121 VAL A CB 1 ATOM 647 C CG1 . VAL A 1 88 ? 23.501 12.711 31.468 1.00 21.50 ? 121 VAL A CG1 1 ATOM 648 C CG2 . VAL A 1 88 ? 23.894 11.366 29.325 1.00 19.98 ? 121 VAL A CG2 1 ATOM 649 N N . ASP A 1 89 ? 26.976 10.018 31.068 1.00 17.03 ? 122 ASP A N 1 ATOM 650 C CA . ASP A 1 89 ? 27.661 8.788 30.656 1.00 18.01 ? 122 ASP A CA 1 ATOM 651 C C . ASP A 1 89 ? 26.627 7.765 30.148 1.00 17.16 ? 122 ASP A C 1 ATOM 652 O O . ASP A 1 89 ? 25.423 8.076 30.025 1.00 21.11 ? 122 ASP A O 1 ATOM 653 C CB . ASP A 1 89 ? 28.592 8.239 31.769 1.00 16.44 ? 122 ASP A CB 1 ATOM 654 C CG . ASP A 1 89 ? 27.827 7.643 32.941 1.00 18.42 ? 122 ASP A CG 1 ATOM 655 O OD1 . ASP A 1 89 ? 28.560 7.297 33.911 1.00 20.94 ? 122 ASP A OD1 1 ATOM 656 O OD2 . ASP A 1 89 ? 26.599 7.593 32.864 1.00 18.06 ? 122 ASP A OD2 1 ATOM 657 N N . GLU A 1 90 ? 27.105 6.570 29.838 1.00 20.51 ? 123 GLU A N 1 ATOM 658 C CA . GLU A 1 90 ? 26.220 5.577 29.277 1.00 23.23 ? 123 GLU A CA 1 ATOM 659 C C . GLU A 1 90 ? 25.297 4.971 30.351 1.00 24.75 ? 123 GLU A C 1 ATOM 660 O O . GLU A 1 90 ? 24.378 4.229 30.015 1.00 27.26 ? 123 GLU A O 1 ATOM 661 C CB . GLU A 1 90 ? 27.028 4.481 28.603 1.00 24.10 ? 123 GLU A CB 1 ATOM 662 C CG . GLU A 1 90 ? 27.830 3.626 29.571 1.00 23.79 ? 123 GLU A CG 1 ATOM 663 C CD . GLU A 1 90 ? 29.272 4.098 29.811 1.00 30.86 ? 123 GLU A CD 1 ATOM 664 O OE1 . GLU A 1 90 ? 29.533 5.335 29.927 1.00 25.96 ? 123 GLU A OE1 1 ATOM 665 O OE2 . GLU A 1 90 ? 30.181 3.210 29.889 1.00 29.00 ? 123 GLU A OE2 1 ATOM 666 N N . HIS A 1 91 ? 25.498 5.336 31.622 1.00 23.93 ? 124 HIS A N 1 ATOM 667 C CA . HIS A 1 91 ? 24.617 4.863 32.682 1.00 24.26 ? 124 HIS A CA 1 ATOM 668 C C . HIS A 1 91 ? 23.637 5.950 33.089 1.00 25.45 ? 124 HIS A C 1 ATOM 669 O O . HIS A 1 91 ? 23.037 5.877 34.178 1.00 26.89 ? 124 HIS A O 1 ATOM 670 C CB . HIS A 1 91 ? 25.484 4.458 33.889 1.00 23.92 ? 124 HIS A CB 1 ATOM 671 C CG . HIS A 1 91 ? 26.613 3.566 33.517 1.00 22.82 ? 124 HIS A CG 1 ATOM 672 N ND1 . HIS A 1 91 ? 26.416 2.301 32.994 1.00 23.55 ? 124 HIS A ND1 1 ATOM 673 C CD2 . HIS A 1 91 ? 27.953 3.754 33.543 1.00 22.26 ? 124 HIS A CD2 1 ATOM 674 C CE1 . HIS A 1 91 ? 27.587 1.760 32.709 1.00 24.96 ? 124 HIS A CE1 1 ATOM 675 N NE2 . HIS A 1 91 ? 28.537 2.624 33.034 1.00 22.92 ? 124 HIS A NE2 1 ATOM 676 N N . GLU A 1 92 ? 23.475 6.976 32.232 1.00 25.38 ? 125 GLU A N 1 ATOM 677 C CA . GLU A 1 92 ? 22.677 8.161 32.522 1.00 25.21 ? 125 GLU A CA 1 ATOM 678 C C . GLU A 1 92 ? 23.095 9.019 33.708 1.00 23.83 ? 125 GLU A C 1 ATOM 679 O O . GLU A 1 92 ? 22.320 9.827 34.198 1.00 25.79 ? 125 GLU A O 1 ATOM 680 C CB . GLU A 1 92 ? 21.208 7.790 32.616 1.00 28.11 ? 125 GLU A CB 1 ATOM 681 C CG . GLU A 1 92 ? 20.681 7.233 31.323 1.00 33.72 ? 125 GLU A CG 1 ATOM 682 C CD . GLU A 1 92 ? 19.160 7.200 31.311 1.00 41.70 ? 125 GLU A CD 1 ATOM 683 O OE1 . GLU A 1 92 ? 18.547 8.087 30.663 1.00 46.42 ? 125 GLU A OE1 1 ATOM 684 O OE2 . GLU A 1 92 ? 18.577 6.309 31.977 1.00 43.58 ? 125 GLU A OE2 1 ATOM 685 N N . THR A 1 93 ? 24.325 8.885 34.135 1.00 21.51 ? 126 THR A N 1 ATOM 686 C CA . THR A 1 93 ? 24.797 9.705 35.233 1.00 21.42 ? 126 THR A CA 1 ATOM 687 C C . THR A 1 93 ? 25.281 11.031 34.684 1.00 20.84 ? 126 THR A C 1 ATOM 688 O O . THR A 1 93 ? 26.073 11.060 33.729 1.00 20.99 ? 126 THR A O 1 ATOM 689 C CB . THR A 1 93 ? 25.938 9.002 35.920 1.00 20.69 ? 126 THR A CB 1 ATOM 690 O OG1 . THR A 1 93 ? 25.471 7.701 36.356 1.00 21.23 ? 126 THR A OG1 1 ATOM 691 C CG2 . THR A 1 93 ? 26.406 9.775 37.182 1.00 20.88 ? 126 THR A CG2 1 ATOM 692 N N . GLU A 1 94 ? 24.871 12.100 35.340 1.00 19.60 ? 127 GLU A N 1 ATOM 693 C CA . GLU A 1 94 ? 25.307 13.434 34.989 1.00 20.10 ? 127 GLU A CA 1 ATOM 694 C C . GLU A 1 94 ? 26.752 13.623 35.374 1.00 21.17 ? 127 GLU A C 1 ATOM 695 O O . GLU A 1 94 ? 27.146 13.474 36.578 1.00 21.02 ? 127 GLU A O 1 ATOM 696 C CB . GLU A 1 94 ? 24.469 14.443 35.717 1.00 20.80 ? 127 GLU A CB 1 ATOM 697 C CG A GLU A 1 94 ? 24.319 15.744 35.039 0.65 25.69 ? 127 GLU A CG 1 ATOM 698 C CG B GLU A 1 94 ? 23.067 14.471 35.288 0.35 15.75 ? 127 GLU A CG 1 ATOM 699 C CD A GLU A 1 94 ? 23.382 16.633 35.821 0.65 28.19 ? 127 GLU A CD 1 ATOM 700 C CD B GLU A 1 94 ? 22.265 15.558 35.965 0.35 17.06 ? 127 GLU A CD 1 ATOM 701 O OE1 A GLU A 1 94 ? 23.822 17.202 36.852 0.65 33.85 ? 127 GLU A OE1 1 ATOM 702 O OE1 B GLU A 1 94 ? 21.243 15.924 35.364 0.35 20.06 ? 127 GLU A OE1 1 ATOM 703 O OE2 A GLU A 1 94 ? 22.207 16.750 35.406 0.65 33.12 ? 127 GLU A OE2 1 ATOM 704 O OE2 B GLU A 1 94 ? 22.627 16.021 37.080 0.35 19.12 ? 127 GLU A OE2 1 ATOM 705 N N . ILE A 1 95 ? 27.593 13.918 34.369 1.00 18.27 ? 128 ILE A N 1 ATOM 706 C CA . ILE A 1 95 ? 29.016 14.121 34.579 1.00 18.82 ? 128 ILE A CA 1 ATOM 707 C C . ILE A 1 95 ? 29.347 15.608 34.628 1.00 19.81 ? 128 ILE A C 1 ATOM 708 O O . ILE A 1 95 ? 30.282 16.013 35.315 1.00 21.86 ? 128 ILE A O 1 ATOM 709 C CB . ILE A 1 95 ? 29.862 13.478 33.462 1.00 19.44 ? 128 ILE A CB 1 ATOM 710 C CG1 . ILE A 1 95 ? 29.389 12.029 33.228 1.00 21.37 ? 128 ILE A CG1 1 ATOM 711 C CG2 . ILE A 1 95 ? 31.373 13.626 33.736 1.00 20.77 ? 128 ILE A CG2 1 ATOM 712 C CD1 . ILE A 1 95 ? 29.534 11.103 34.538 1.00 18.57 ? 128 ILE A CD1 1 ATOM 713 N N . PHE A 1 96 ? 28.602 16.409 33.856 1.00 17.52 ? 129 PHE A N 1 ATOM 714 C CA . PHE A 1 96 ? 28.836 17.861 33.832 1.00 18.06 ? 129 PHE A CA 1 ATOM 715 C C . PHE A 1 96 ? 27.509 18.583 33.589 1.00 17.37 ? 129 PHE A C 1 ATOM 716 O O . PHE A 1 96 ? 26.652 18.034 32.858 1.00 18.11 ? 129 PHE A O 1 ATOM 717 C CB . PHE A 1 96 ? 29.763 18.186 32.618 1.00 19.62 ? 129 PHE A CB 1 ATOM 718 C CG . PHE A 1 96 ? 29.850 19.676 32.278 1.00 21.97 ? 129 PHE A CG 1 ATOM 719 C CD1 . PHE A 1 96 ? 30.617 20.552 33.067 1.00 26.15 ? 129 PHE A CD1 1 ATOM 720 C CD2 . PHE A 1 96 ? 29.192 20.180 31.177 1.00 25.10 ? 129 PHE A CD2 1 ATOM 721 C CE1 . PHE A 1 96 ? 30.701 21.910 32.757 1.00 27.92 ? 129 PHE A CE1 1 ATOM 722 C CE2 . PHE A 1 96 ? 29.262 21.542 30.875 1.00 27.70 ? 129 PHE A CE2 1 ATOM 723 C CZ . PHE A 1 96 ? 30.028 22.400 31.663 1.00 27.76 ? 129 PHE A CZ 1 ATOM 724 N N . LYS A 1 97 ? 27.315 19.754 34.164 1.00 18.42 ? 130 LYS A N 1 ATOM 725 C CA . LYS A 1 97 ? 26.068 20.490 34.023 1.00 23.31 ? 130 LYS A CA 1 ATOM 726 C C . LYS A 1 97 ? 26.437 21.959 34.039 1.00 27.32 ? 130 LYS A C 1 ATOM 727 O O . LYS A 1 97 ? 27.301 22.393 34.810 1.00 29.24 ? 130 LYS A O 1 ATOM 728 C CB . LYS A 1 97 ? 25.111 20.117 35.167 1.00 24.10 ? 130 LYS A CB 1 ATOM 729 C CG . LYS A 1 97 ? 23.750 20.729 35.120 1.00 26.73 ? 130 LYS A CG 1 ATOM 730 C CD . LYS A 1 97 ? 22.906 20.174 36.280 1.00 29.96 ? 130 LYS A CD 1 ATOM 731 C CE . LYS A 1 97 ? 21.678 21.023 36.399 1.00 30.17 ? 130 LYS A CE 1 ATOM 732 N NZ . LYS A 1 97 ? 20.675 20.518 37.423 1.00 33.94 ? 130 LYS A NZ 1 ATOM 733 N N . THR A 1 98 ? 25.790 22.752 33.194 1.00 29.41 ? 131 THR A N 1 ATOM 734 C CA . THR A 1 98 ? 25.965 24.204 33.321 1.00 32.81 ? 131 THR A CA 1 ATOM 735 C C . THR A 1 98 ? 25.299 24.756 34.576 1.00 35.33 ? 131 THR A C 1 ATOM 736 O O . THR A 1 98 ? 24.346 24.156 35.135 1.00 35.51 ? 131 THR A O 1 ATOM 737 C CB . THR A 1 98 ? 25.480 24.914 32.090 1.00 32.75 ? 131 THR A CB 1 ATOM 738 O OG1 . THR A 1 98 ? 24.104 24.567 31.850 1.00 33.83 ? 131 THR A OG1 1 ATOM 739 C CG2 . THR A 1 98 ? 26.330 24.482 30.888 1.00 28.68 ? 131 THR A CG2 1 ATOM 740 N N . SER A 1 99 ? 25.864 25.869 35.066 1.00 38.80 ? 132 SER A N 1 ATOM 741 C CA . SER A 1 99 ? 25.362 26.616 36.228 1.00 41.24 ? 132 SER A CA 1 ATOM 742 C C . SER A 1 99 ? 24.666 27.863 35.705 1.00 40.87 ? 132 SER A C 1 ATOM 743 O O . SER A 1 99 ? 23.493 27.826 35.341 1.00 40.90 ? 132 SER A O 1 ATOM 744 C CB . SER A 1 99 ? 26.539 27.017 37.118 1.00 41.85 ? 132 SER A CB 1 ATOM 745 O OG . SER A 1 99 ? 26.117 27.814 38.220 1.00 46.43 ? 132 SER A OG 1 ATOM 746 N N . PRO A 1 104 ? 27.072 38.566 39.167 1.00 33.77 ? 137 PRO A N 1 ATOM 747 C CA . PRO A 1 104 ? 26.703 39.986 38.850 1.00 32.57 ? 137 PRO A CA 1 ATOM 748 C C . PRO A 1 104 ? 27.943 40.855 38.831 1.00 31.31 ? 137 PRO A C 1 ATOM 749 O O . PRO A 1 104 ? 28.894 40.561 39.566 1.00 31.80 ? 137 PRO A O 1 ATOM 750 C CB . PRO A 1 104 ? 25.766 40.404 39.981 1.00 32.95 ? 137 PRO A CB 1 ATOM 751 C CG . PRO A 1 104 ? 25.634 39.215 40.897 1.00 34.38 ? 137 PRO A CG 1 ATOM 752 C CD . PRO A 1 104 ? 26.683 38.186 40.530 1.00 34.86 ? 137 PRO A CD 1 ATOM 753 N N . PRO A 1 105 ? 27.961 41.913 38.012 1.00 29.15 ? 138 PRO A N 1 ATOM 754 C CA . PRO A 1 105 ? 29.187 42.721 37.984 1.00 28.11 ? 138 PRO A CA 1 ATOM 755 C C . PRO A 1 105 ? 29.485 43.403 39.317 1.00 27.63 ? 138 PRO A C 1 ATOM 756 O O . PRO A 1 105 ? 28.579 43.677 40.102 1.00 25.73 ? 138 PRO A O 1 ATOM 757 C CB . PRO A 1 105 ? 28.914 43.773 36.915 1.00 27.31 ? 138 PRO A CB 1 ATOM 758 C CG . PRO A 1 105 ? 27.664 43.302 36.206 1.00 26.99 ? 138 PRO A CG 1 ATOM 759 C CD . PRO A 1 105 ? 26.900 42.452 37.129 1.00 28.64 ? 138 PRO A CD 1 ATOM 760 N N . ASP A 1 106 ? 30.761 43.697 39.553 1.00 28.37 ? 139 ASP A N 1 ATOM 761 C CA . ASP A 1 106 ? 31.142 44.366 40.786 1.00 27.81 ? 139 ASP A CA 1 ATOM 762 C C . ASP A 1 106 ? 30.346 45.653 40.938 1.00 27.48 ? 139 ASP A C 1 ATOM 763 O O . ASP A 1 106 ? 30.196 46.416 39.975 1.00 28.89 ? 139 ASP A O 1 ATOM 764 C CB . ASP A 1 106 ? 32.624 44.705 40.765 1.00 29.03 ? 139 ASP A CB 1 ATOM 765 C CG . ASP A 1 106 ? 33.515 43.467 40.804 1.00 31.77 ? 139 ASP A CG 1 ATOM 766 O OD1 . ASP A 1 106 ? 34.599 43.511 40.191 1.00 35.85 ? 139 ASP A OD1 1 ATOM 767 O OD2 . ASP A 1 106 ? 33.144 42.458 41.439 1.00 35.28 ? 139 ASP A OD2 1 ATOM 768 N N . GLY A 1 107 ? 29.791 45.848 42.128 1.00 26.36 ? 140 GLY A N 1 ATOM 769 C CA . GLY A 1 107 ? 29.003 47.008 42.476 1.00 26.91 ? 140 GLY A CA 1 ATOM 770 C C . GLY A 1 107 ? 27.507 46.781 42.325 1.00 26.88 ? 140 GLY A C 1 ATOM 771 O O . GLY A 1 107 ? 26.717 47.628 42.714 1.00 28.50 ? 140 GLY A O 1 ATOM 772 N N . TYR A 1 108 ? 27.127 45.642 41.741 1.00 27.08 ? 141 TYR A N 1 ATOM 773 C CA . TYR A 1 108 ? 25.711 45.294 41.511 1.00 27.04 ? 141 TYR A CA 1 ATOM 774 C C . TYR A 1 108 ? 25.319 43.974 42.181 1.00 28.28 ? 141 TYR A C 1 ATOM 775 O O . TYR A 1 108 ? 24.374 43.274 41.758 1.00 27.92 ? 141 TYR A O 1 ATOM 776 C CB . TYR A 1 108 ? 25.491 45.186 40.007 1.00 25.15 ? 141 TYR A CB 1 ATOM 777 C CG . TYR A 1 108 ? 25.795 46.447 39.269 1.00 24.20 ? 141 TYR A CG 1 ATOM 778 C CD1 . TYR A 1 108 ? 24.796 47.360 39.029 1.00 24.42 ? 141 TYR A CD1 1 ATOM 779 C CD2 . TYR A 1 108 ? 27.072 46.719 38.802 1.00 22.59 ? 141 TYR A CD2 1 ATOM 780 C CE1 . TYR A 1 108 ? 25.050 48.542 38.352 1.00 22.20 ? 141 TYR A CE1 1 ATOM 781 C CE2 . TYR A 1 108 ? 27.351 47.886 38.102 1.00 24.22 ? 141 TYR A CE2 1 ATOM 782 C CZ . TYR A 1 108 ? 26.324 48.790 37.887 1.00 26.10 ? 141 TYR A CZ 1 ATOM 783 O OH . TYR A 1 108 ? 26.577 49.932 37.199 1.00 22.90 ? 141 TYR A OH 1 ATOM 784 N N . GLU A 1 109 ? 26.070 43.644 43.243 1.00 28.69 ? 142 GLU A N 1 ATOM 785 C CA . GLU A 1 109 ? 25.811 42.448 44.017 1.00 28.98 ? 142 GLU A CA 1 ATOM 786 C C . GLU A 1 109 ? 24.407 42.425 44.623 1.00 28.83 ? 142 GLU A C 1 ATOM 787 O O . GLU A 1 109 ? 23.870 41.332 44.834 1.00 31.05 ? 142 GLU A O 1 ATOM 788 C CB . GLU A 1 109 ? 26.836 42.332 45.153 1.00 28.68 ? 142 GLU A CB 1 ATOM 789 C CG . GLU A 1 109 ? 28.280 42.197 44.634 1.00 30.43 ? 142 GLU A CG 1 ATOM 790 C CD . GLU A 1 109 ? 28.947 43.545 44.369 1.00 28.33 ? 142 GLU A CD 1 ATOM 791 O OE1 . GLU A 1 109 ? 28.334 44.599 44.642 1.00 31.60 ? 142 GLU A OE1 1 ATOM 792 O OE2 . GLU A 1 109 ? 30.099 43.537 43.901 1.00 31.40 ? 142 GLU A OE2 1 ATOM 793 N N . ASN A 1 110 ? 23.825 43.585 44.914 1.00 28.49 ? 143 ASN A N 1 ATOM 794 C CA . ASN A 1 110 ? 22.479 43.591 45.511 1.00 29.78 ? 143 ASN A CA 1 ATOM 795 C C . ASN A 1 110 ? 21.280 43.572 44.547 1.00 29.36 ? 143 ASN A C 1 ATOM 796 O O . ASN A 1 110 ? 20.119 43.656 44.967 1.00 29.17 ? 143 ASN A O 1 ATOM 797 C CB . ASN A 1 110 ? 22.324 44.709 46.553 1.00 30.35 ? 143 ASN A CB 1 ATOM 798 C CG A ASN A 1 110 ? 22.308 46.111 45.950 0.70 33.11 ? 143 ASN A CG 1 ATOM 799 C CG B ASN A 1 110 ? 23.210 44.496 47.783 0.30 30.52 ? 143 ASN A CG 1 ATOM 800 O OD1 A ASN A 1 110 ? 22.401 46.285 44.728 0.70 34.67 ? 143 ASN A OD1 1 ATOM 801 O OD1 B ASN A 1 110 ? 23.659 43.376 48.072 0.30 32.32 ? 143 ASN A OD1 1 ATOM 802 N ND2 A ASN A 1 110 ? 22.173 47.134 46.823 0.70 34.82 ? 143 ASN A ND2 1 ATOM 803 N ND2 B ASN A 1 110 ? 23.472 45.575 48.503 0.30 32.27 ? 143 ASN A ND2 1 ATOM 804 N N . VAL A 1 111 ? 21.568 43.519 43.245 1.00 27.48 ? 144 VAL A N 1 ATOM 805 C CA . VAL A 1 111 ? 20.511 43.589 42.231 1.00 27.27 ? 144 VAL A CA 1 ATOM 806 C C . VAL A 1 111 ? 19.922 42.191 42.099 1.00 26.91 ? 144 VAL A C 1 ATOM 807 O O . VAL A 1 111 ? 20.653 41.226 41.876 1.00 28.51 ? 144 VAL A O 1 ATOM 808 C CB . VAL A 1 111 ? 21.115 44.033 40.921 1.00 26.18 ? 144 VAL A CB 1 ATOM 809 C CG1 . VAL A 1 111 ? 20.044 43.948 39.797 1.00 25.62 ? 144 VAL A CG1 1 ATOM 810 C CG2 . VAL A 1 111 ? 21.677 45.455 41.028 1.00 25.98 ? 144 VAL A CG2 1 ATOM 811 N N . THR A 1 112 ? 18.603 42.075 42.232 1.00 28.13 ? 145 THR A N 1 ATOM 812 C CA . THR A 1 112 ? 17.996 40.762 42.458 1.00 30.42 ? 145 THR A CA 1 ATOM 813 C C . THR A 1 112 ? 17.271 40.107 41.239 1.00 31.55 ? 145 THR A C 1 ATOM 814 O O . THR A 1 112 ? 16.925 38.896 41.270 1.00 34.64 ? 145 THR A O 1 ATOM 815 C CB . THR A 1 112 ? 17.001 40.798 43.668 1.00 31.31 ? 145 THR A CB 1 ATOM 816 O OG1 A THR A 1 112 ? 16.577 39.467 43.968 0.56 34.91 ? 145 THR A OG1 1 ATOM 817 O OG1 B THR A 1 112 ? 15.962 41.745 43.397 0.14 29.58 ? 145 THR A OG1 1 ATOM 818 O OG1 C THR A 1 112 ? 17.389 41.834 44.580 0.30 28.88 ? 145 THR A OG1 1 ATOM 819 C CG2 A THR A 1 112 ? 15.805 41.634 43.315 0.56 28.18 ? 145 THR A CG2 1 ATOM 820 C CG2 B THR A 1 112 ? 17.724 41.177 44.956 0.14 30.15 ? 145 THR A CG2 1 ATOM 821 C CG2 C THR A 1 112 ? 17.061 39.486 44.443 0.30 31.51 ? 145 THR A CG2 1 ATOM 822 N N . ASN A 1 113 ? 17.016 40.891 40.208 1.00 29.75 ? 146 ASN A N 1 ATOM 823 C CA . ASN A 1 113 ? 16.125 40.450 39.120 1.00 28.84 ? 146 ASN A CA 1 ATOM 824 C C . ASN A 1 113 ? 16.884 40.467 37.799 1.00 28.02 ? 146 ASN A C 1 ATOM 825 O O . ASN A 1 113 ? 16.333 40.877 36.742 1.00 28.00 ? 146 ASN A O 1 ATOM 826 C CB . ASN A 1 113 ? 14.934 41.402 39.020 1.00 29.42 ? 146 ASN A CB 1 ATOM 827 C CG A ASN A 1 113 ? 15.368 42.781 38.763 0.60 28.69 ? 146 ASN A CG 1 ATOM 828 C CG B ASN A 1 113 ? 13.792 41.025 39.950 0.40 30.75 ? 146 ASN A CG 1 ATOM 829 O OD1 A ASN A 1 113 ? 16.465 43.170 39.165 0.60 31.45 ? 146 ASN A OD1 1 ATOM 830 O OD1 B ASN A 1 113 ? 13.375 41.822 40.800 0.40 35.17 ? 146 ASN A OD1 1 ATOM 831 N ND2 A ASN A 1 113 ? 14.552 43.536 38.047 0.60 33.24 ? 146 ASN A ND2 1 ATOM 832 N ND2 B ASN A 1 113 ? 13.289 39.800 39.808 0.40 33.31 ? 146 ASN A ND2 1 ATOM 833 N N . ILE A 1 114 ? 18.144 40.070 37.827 1.00 24.97 ? 147 ILE A N 1 ATOM 834 C CA . ILE A 1 114 ? 18.871 39.862 36.553 1.00 22.95 ? 147 ILE A CA 1 ATOM 835 C C . ILE A 1 114 ? 18.378 38.552 35.952 1.00 22.87 ? 147 ILE A C 1 ATOM 836 O O . ILE A 1 114 ? 18.415 37.503 36.617 1.00 21.71 ? 147 ILE A O 1 ATOM 837 C CB . ILE A 1 114 ? 20.385 39.828 36.766 1.00 24.56 ? 147 ILE A CB 1 ATOM 838 C CG1 . ILE A 1 114 ? 20.899 41.187 37.315 1.00 26.11 ? 147 ILE A CG1 1 ATOM 839 C CG2 . ILE A 1 114 ? 21.127 39.317 35.524 1.00 24.10 ? 147 ILE A CG2 1 ATOM 840 C CD1 . ILE A 1 114 ? 22.341 41.112 37.727 1.00 30.27 ? 147 ILE A CD1 1 ATOM 841 N N . VAL A 1 115 ? 17.903 38.618 34.679 1.00 20.97 ? 148 VAL A N 1 ATOM 842 C CA . VAL A 1 115 ? 17.349 37.414 34.030 1.00 21.21 ? 148 VAL A CA 1 ATOM 843 C C . VAL A 1 115 ? 18.523 36.542 33.670 1.00 21.00 ? 148 VAL A C 1 ATOM 844 O O . VAL A 1 115 ? 19.533 37.021 33.131 1.00 21.80 ? 148 VAL A O 1 ATOM 845 C CB . VAL A 1 115 ? 16.504 37.818 32.769 1.00 22.63 ? 148 VAL A CB 1 ATOM 846 C CG1 . VAL A 1 115 ? 17.413 38.273 31.572 1.00 23.35 ? 148 VAL A CG1 1 ATOM 847 C CG2 . VAL A 1 115 ? 15.635 36.652 32.370 1.00 20.73 ? 148 VAL A CG2 1 ATOM 848 N N . PRO A 1 116 ? 18.438 35.245 33.976 1.00 20.21 ? 149 PRO A N 1 ATOM 849 C CA . PRO A 1 116 ? 19.600 34.446 33.597 1.00 21.13 ? 149 PRO A CA 1 ATOM 850 C C . PRO A 1 116 ? 19.717 34.319 32.070 1.00 19.17 ? 149 PRO A C 1 ATOM 851 O O . PRO A 1 116 ? 18.736 34.598 31.352 1.00 19.89 ? 149 PRO A O 1 ATOM 852 C CB . PRO A 1 116 ? 19.327 33.064 34.219 1.00 22.32 ? 149 PRO A CB 1 ATOM 853 C CG . PRO A 1 116 ? 17.994 33.040 34.479 1.00 23.18 ? 149 PRO A CG 1 ATOM 854 C CD . PRO A 1 116 ? 17.527 34.478 34.831 1.00 21.52 ? 149 PRO A CD 1 ATOM 855 N N . PRO A 1 117 ? 20.895 33.900 31.591 1.00 19.48 ? 150 PRO A N 1 ATOM 856 C CA A PRO A 1 117 ? 21.010 33.827 30.131 0.70 18.18 ? 150 PRO A CA 1 ATOM 857 C CA B PRO A 1 117 ? 21.110 33.708 30.142 0.30 17.98 ? 150 PRO A CA 1 ATOM 858 C C . PRO A 1 117 ? 20.052 32.791 29.548 1.00 18.21 ? 150 PRO A C 1 ATOM 859 O O . PRO A 1 117 ? 19.768 31.740 30.138 1.00 19.57 ? 150 PRO A O 1 ATOM 860 C CB A PRO A 1 117 ? 22.498 33.478 29.879 0.70 19.13 ? 150 PRO A CB 1 ATOM 861 C CB B PRO A 1 117 ? 22.457 32.969 30.070 0.30 18.19 ? 150 PRO A CB 1 ATOM 862 C CG A PRO A 1 117 ? 23.218 33.846 31.219 0.70 21.49 ? 150 PRO A CG 1 ATOM 863 C CG B PRO A 1 117 ? 22.677 32.433 31.434 0.30 16.00 ? 150 PRO A CG 1 ATOM 864 C CD A PRO A 1 117 ? 22.192 33.634 32.274 0.70 20.60 ? 150 PRO A CD 1 ATOM 865 C CD B PRO A 1 117 ? 21.950 33.263 32.405 0.30 19.32 ? 150 PRO A CD 1 ATOM 866 N N . TYR A 1 118 ? 19.463 33.176 28.397 1.00 16.80 ? 151 TYR A N 1 ATOM 867 C CA . TYR A 1 118 ? 18.506 32.297 27.704 1.00 16.34 ? 151 TYR A CA 1 ATOM 868 C C . TYR A 1 118 ? 18.356 32.869 26.334 1.00 17.18 ? 151 TYR A C 1 ATOM 869 O O . TYR A 1 118 ? 18.760 34.022 26.118 1.00 16.45 ? 151 TYR A O 1 ATOM 870 C CB . TYR A 1 118 ? 17.150 32.216 28.406 1.00 16.21 ? 151 TYR A CB 1 ATOM 871 C CG . TYR A 1 118 ? 16.256 33.403 28.307 1.00 16.16 ? 151 TYR A CG 1 ATOM 872 C CD1 . TYR A 1 118 ? 16.615 34.638 28.906 1.00 15.77 ? 151 TYR A CD1 1 ATOM 873 C CD2 . TYR A 1 118 ? 15.032 33.329 27.615 1.00 16.72 ? 151 TYR A CD2 1 ATOM 874 C CE1 . TYR A 1 118 ? 15.745 35.748 28.860 1.00 16.22 ? 151 TYR A CE1 1 ATOM 875 C CE2 . TYR A 1 118 ? 14.150 34.435 27.612 1.00 16.07 ? 151 TYR A CE2 1 ATOM 876 C CZ . TYR A 1 118 ? 14.510 35.653 28.213 1.00 15.50 ? 151 TYR A CZ 1 ATOM 877 O OH . TYR A 1 118 ? 13.662 36.758 28.225 1.00 16.97 ? 151 TYR A OH 1 ATOM 878 N N . ASN A 1 119 ? 17.741 32.079 25.447 1.00 15.53 ? 152 ASN A N 1 ATOM 879 C CA . ASN A 1 119 ? 17.374 32.618 24.115 1.00 15.58 ? 152 ASN A CA 1 ATOM 880 C C . ASN A 1 119 ? 15.876 32.686 24.048 1.00 15.67 ? 152 ASN A C 1 ATOM 881 O O . ASN A 1 119 ? 15.174 31.645 23.947 1.00 16.61 ? 152 ASN A O 1 ATOM 882 C CB . ASN A 1 119 ? 17.915 31.702 23.021 1.00 16.10 ? 152 ASN A CB 1 ATOM 883 C CG . ASN A 1 119 ? 19.420 31.868 22.862 1.00 16.48 ? 152 ASN A CG 1 ATOM 884 O OD1 . ASN A 1 119 ? 19.908 32.985 22.478 1.00 19.98 ? 152 ASN A OD1 1 ATOM 885 N ND2 . ASN A 1 119 ? 20.152 30.826 23.057 1.00 13.95 ? 152 ASN A ND2 1 ATOM 886 N N . ALA A 1 120 ? 15.353 33.929 24.086 1.00 15.15 ? 153 ALA A N 1 ATOM 887 C CA . ALA A 1 120 ? 13.910 34.131 24.055 1.00 15.31 ? 153 ALA A CA 1 ATOM 888 C C . ALA A 1 120 ? 13.253 33.445 22.825 1.00 16.08 ? 153 ALA A C 1 ATOM 889 O O . ALA A 1 120 ? 13.719 33.631 21.680 1.00 16.22 ? 153 ALA A O 1 ATOM 890 C CB . ALA A 1 120 ? 13.588 35.607 24.041 1.00 16.37 ? 153 ALA A CB 1 ATOM 891 N N . PHE A 1 121 ? 12.133 32.760 23.113 1.00 15.17 ? 154 PHE A N 1 ATOM 892 C CA . PHE A 1 121 ? 11.232 32.051 22.195 1.00 15.32 ? 154 PHE A CA 1 ATOM 893 C C . PHE A 1 121 ? 11.757 30.666 21.820 1.00 17.00 ? 154 PHE A C 1 ATOM 894 O O . PHE A 1 121 ? 11.146 29.990 21.016 1.00 17.81 ? 154 PHE A O 1 ATOM 895 C CB . PHE A 1 121 ? 10.873 32.877 20.934 1.00 14.72 ? 154 PHE A CB 1 ATOM 896 C CG . PHE A 1 121 ? 10.207 34.160 21.284 1.00 15.43 ? 154 PHE A CG 1 ATOM 897 C CD1 . PHE A 1 121 ? 8.873 34.177 21.669 1.00 17.09 ? 154 PHE A CD1 1 ATOM 898 C CD2 . PHE A 1 121 ? 10.934 35.361 21.233 1.00 17.00 ? 154 PHE A CD2 1 ATOM 899 C CE1 . PHE A 1 121 ? 8.263 35.447 21.943 1.00 17.56 ? 154 PHE A CE1 1 ATOM 900 C CE2 . PHE A 1 121 ? 10.341 36.611 21.524 1.00 17.20 ? 154 PHE A CE2 1 ATOM 901 C CZ . PHE A 1 121 ? 9.017 36.636 21.911 1.00 16.36 ? 154 PHE A CZ 1 ATOM 902 N N . SER A 1 122 ? 12.860 30.227 22.427 1.00 15.74 ? 155 SER A N 1 ATOM 903 C CA . SER A 1 122 ? 13.252 28.803 22.277 1.00 15.86 ? 155 SER A CA 1 ATOM 904 C C . SER A 1 122 ? 12.057 27.887 22.498 1.00 16.64 ? 155 SER A C 1 ATOM 905 O O . SER A 1 122 ? 11.261 28.153 23.410 1.00 17.99 ? 155 SER A O 1 ATOM 906 C CB . SER A 1 122 ? 14.276 28.489 23.376 1.00 16.36 ? 155 SER A CB 1 ATOM 907 O OG . SER A 1 122 ? 14.570 27.080 23.341 1.00 16.48 ? 155 SER A OG 1 ATOM 908 N N . ALA A 1 123 ? 12.001 26.766 21.782 1.00 16.89 ? 156 ALA A N 1 ATOM 909 C CA . ALA A 1 123 ? 11.005 25.737 22.120 1.00 16.73 ? 156 ALA A CA 1 ATOM 910 C C . ALA A 1 123 ? 11.421 25.155 23.473 1.00 18.89 ? 156 ALA A C 1 ATOM 911 O O . ALA A 1 123 ? 12.581 25.244 23.918 1.00 18.31 ? 156 ALA A O 1 ATOM 912 C CB . ALA A 1 123 ? 10.988 24.619 21.031 1.00 18.24 ? 156 ALA A CB 1 ATOM 913 N N . GLN A 1 124 ? 10.461 24.488 24.122 1.00 19.04 ? 157 GLN A N 1 ATOM 914 C CA . GLN A 1 124 ? 10.757 23.726 25.314 1.00 19.28 ? 157 GLN A CA 1 ATOM 915 C C . GLN A 1 124 ? 11.163 22.318 24.967 1.00 20.08 ? 157 GLN A C 1 ATOM 916 O O . GLN A 1 124 ? 10.689 21.762 23.950 1.00 21.41 ? 157 GLN A O 1 ATOM 917 C CB . GLN A 1 124 ? 9.500 23.652 26.211 1.00 20.63 ? 157 GLN A CB 1 ATOM 918 C CG . GLN A 1 124 ? 8.964 24.985 26.634 1.00 19.09 ? 157 GLN A CG 1 ATOM 919 C CD . GLN A 1 124 ? 7.907 24.874 27.705 1.00 21.37 ? 157 GLN A CD 1 ATOM 920 O OE1 . GLN A 1 124 ? 7.248 23.842 27.816 1.00 26.37 ? 157 GLN A OE1 1 ATOM 921 N NE2 . GLN A 1 124 ? 7.755 25.908 28.491 1.00 20.60 ? 157 GLN A NE2 1 ATOM 922 N N . GLY A 1 125 ? 12.059 21.750 25.763 1.00 18.40 ? 158 GLY A N 1 ATOM 923 C CA . GLY A 1 125 ? 12.413 20.332 25.581 1.00 20.55 ? 158 GLY A CA 1 ATOM 924 C C . GLY A 1 125 ? 13.574 19.847 26.367 1.00 21.01 ? 158 GLY A C 1 ATOM 925 O O . GLY A 1 125 ? 14.318 20.651 26.961 1.00 20.13 ? 158 GLY A O 1 ATOM 926 N N . MET A 1 126 ? 13.719 18.515 26.343 1.00 22.48 ? 159 MET A N 1 ATOM 927 C CA . MET A 1 126 ? 14.838 17.867 26.980 1.00 20.80 ? 159 MET A CA 1 ATOM 928 C C . MET A 1 126 ? 15.495 16.884 25.985 1.00 20.90 ? 159 MET A C 1 ATOM 929 O O . MET A 1 126 ? 15.671 15.683 26.278 1.00 20.93 ? 159 MET A O 1 ATOM 930 C CB . MET A 1 126 ? 14.352 17.133 28.216 1.00 23.91 ? 159 MET A CB 1 ATOM 931 C CG A MET A 1 126 ? 13.138 16.251 27.900 0.70 25.76 ? 159 MET A CG 1 ATOM 932 C CG B MET A 1 126 ? 14.704 17.817 29.533 0.30 25.20 ? 159 MET A CG 1 ATOM 933 S SD A MET A 1 126 ? 12.537 15.350 29.363 0.70 36.12 ? 159 MET A SD 1 ATOM 934 S SD B MET A 1 126 ? 14.955 16.739 31.002 0.30 31.60 ? 159 MET A SD 1 ATOM 935 C CE A MET A 1 126 ? 12.881 16.616 30.603 0.70 27.67 ? 159 MET A CE 1 ATOM 936 C CE B MET A 1 126 ? 13.295 16.837 31.654 0.30 30.96 ? 159 MET A CE 1 ATOM 937 N N . PRO A 1 127 ? 15.882 17.365 24.807 1.00 19.39 ? 160 PRO A N 1 ATOM 938 C CA . PRO A 1 127 ? 16.506 16.444 23.845 1.00 19.53 ? 160 PRO A CA 1 ATOM 939 C C . PRO A 1 127 ? 17.851 15.887 24.362 1.00 19.72 ? 160 PRO A C 1 ATOM 940 O O . PRO A 1 127 ? 18.580 16.577 25.100 1.00 19.55 ? 160 PRO A O 1 ATOM 941 C CB . PRO A 1 127 ? 16.800 17.336 22.633 1.00 20.55 ? 160 PRO A CB 1 ATOM 942 C CG . PRO A 1 127 ? 16.964 18.732 23.240 1.00 19.73 ? 160 PRO A CG 1 ATOM 943 C CD . PRO A 1 127 ? 15.875 18.771 24.314 1.00 19.58 ? 160 PRO A CD 1 ATOM 944 N N . GLU A 1 128 ? 18.212 14.695 23.903 1.00 19.84 ? 161 GLU A N 1 ATOM 945 C CA . GLU A 1 128 ? 19.471 14.056 24.279 1.00 19.70 ? 161 GLU A CA 1 ATOM 946 C C . GLU A 1 128 ? 20.021 13.436 23.004 1.00 20.16 ? 161 GLU A C 1 ATOM 947 O O . GLU A 1 128 ? 19.277 12.855 22.193 1.00 21.16 ? 161 GLU A O 1 ATOM 948 C CB . GLU A 1 128 ? 19.233 12.934 25.329 1.00 21.04 ? 161 GLU A CB 1 ATOM 949 C CG . GLU A 1 128 ? 20.546 12.138 25.627 1.00 24.72 ? 161 GLU A CG 1 ATOM 950 C CD . GLU A 1 128 ? 20.437 11.085 26.739 1.00 34.06 ? 161 GLU A CD 1 ATOM 951 O OE1 . GLU A 1 128 ? 21.113 10.055 26.618 1.00 40.69 ? 161 GLU A OE1 1 ATOM 952 O OE2 . GLU A 1 128 ? 19.729 11.310 27.726 1.00 37.38 ? 161 GLU A OE2 1 ATOM 953 N N . GLY A 1 129 ? 21.327 13.555 22.778 1.00 17.41 ? 162 GLY A N 1 ATOM 954 C CA . GLY A 1 129 ? 21.873 12.961 21.562 1.00 18.03 ? 162 GLY A CA 1 ATOM 955 C C . GLY A 1 129 ? 23.360 13.155 21.455 1.00 18.62 ? 162 GLY A C 1 ATOM 956 O O . GLY A 1 129 ? 23.978 13.689 22.392 1.00 17.94 ? 162 GLY A O 1 ATOM 957 N N . ASP A 1 130 ? 23.935 12.739 20.336 1.00 18.39 ? 163 ASP A N 1 ATOM 958 C CA . ASP A 1 130 ? 25.329 13.032 20.047 1.00 18.32 ? 163 ASP A CA 1 ATOM 959 C C . ASP A 1 130 ? 25.470 14.490 19.623 1.00 16.92 ? 163 ASP A C 1 ATOM 960 O O . ASP A 1 130 ? 24.569 15.081 19.011 1.00 17.42 ? 163 ASP A O 1 ATOM 961 C CB . ASP A 1 130 ? 25.817 12.156 18.912 1.00 18.24 ? 163 ASP A CB 1 ATOM 962 C CG . ASP A 1 130 ? 25.957 10.693 19.331 1.00 26.13 ? 163 ASP A CG 1 ATOM 963 O OD1 . ASP A 1 130 ? 26.352 10.447 20.484 1.00 28.69 ? 163 ASP A OD1 1 ATOM 964 O OD2 . ASP A 1 130 ? 25.623 9.838 18.467 1.00 34.50 ? 163 ASP A OD2 1 ATOM 965 N N . LEU A 1 131 ? 26.637 15.054 19.950 1.00 16.88 ? 164 LEU A N 1 ATOM 966 C CA . LEU A 1 131 ? 26.940 16.446 19.662 1.00 17.13 ? 164 LEU A CA 1 ATOM 967 C C . LEU A 1 131 ? 27.691 16.577 18.340 1.00 16.22 ? 164 LEU A C 1 ATOM 968 O O . LEU A 1 131 ? 28.564 15.728 18.046 1.00 16.34 ? 164 LEU A O 1 ATOM 969 C CB . LEU A 1 131 ? 27.827 17.001 20.796 1.00 18.03 ? 164 LEU A CB 1 ATOM 970 C CG . LEU A 1 131 ? 28.133 18.495 20.803 1.00 15.82 ? 164 LEU A CG 1 ATOM 971 C CD1 . LEU A 1 131 ? 26.828 19.316 20.968 1.00 15.83 ? 164 LEU A CD1 1 ATOM 972 C CD2 . LEU A 1 131 ? 29.201 18.811 21.880 1.00 17.07 ? 164 LEU A CD2 1 ATOM 973 N N . VAL A 1 132 ? 27.339 17.622 17.580 1.00 16.65 ? 165 VAL A N 1 ATOM 974 C CA . VAL A 1 132 ? 28.048 17.969 16.308 1.00 16.53 ? 165 VAL A CA 1 ATOM 975 C C . VAL A 1 132 ? 28.356 19.451 16.336 1.00 15.42 ? 165 VAL A C 1 ATOM 976 O O . VAL A 1 132 ? 27.477 20.242 16.644 1.00 15.45 ? 165 VAL A O 1 ATOM 977 C CB . VAL A 1 132 ? 27.177 17.674 15.093 1.00 18.47 ? 165 VAL A CB 1 ATOM 978 C CG1 . VAL A 1 132 ? 27.920 18.051 13.787 1.00 21.34 ? 165 VAL A CG1 1 ATOM 979 C CG2 . VAL A 1 132 ? 26.861 16.205 15.010 1.00 20.63 ? 165 VAL A CG2 1 ATOM 980 N N . TYR A 1 133 ? 29.608 19.806 16.056 1.00 16.18 ? 166 TYR A N 1 ATOM 981 C CA . TYR A 1 133 ? 29.987 21.190 15.933 1.00 15.89 ? 166 TYR A CA 1 ATOM 982 C C . TYR A 1 133 ? 29.754 21.691 14.496 1.00 16.19 ? 166 TYR A C 1 ATOM 983 O O . TYR A 1 133 ? 30.211 21.031 13.527 1.00 17.79 ? 166 TYR A O 1 ATOM 984 C CB . TYR A 1 133 ? 31.450 21.359 16.320 1.00 13.69 ? 166 TYR A CB 1 ATOM 985 C CG . TYR A 1 133 ? 32.074 22.711 15.994 1.00 15.54 ? 166 TYR A CG 1 ATOM 986 C CD1 . TYR A 1 133 ? 31.631 23.895 16.599 1.00 16.80 ? 166 TYR A CD1 1 ATOM 987 C CD2 . TYR A 1 133 ? 33.157 22.800 15.141 1.00 17.31 ? 166 TYR A CD2 1 ATOM 988 C CE1 . TYR A 1 133 ? 32.233 25.124 16.326 1.00 18.57 ? 166 TYR A CE1 1 ATOM 989 C CE2 . TYR A 1 133 ? 33.722 24.011 14.845 1.00 17.46 ? 166 TYR A CE2 1 ATOM 990 C CZ . TYR A 1 133 ? 33.251 25.169 15.408 1.00 17.96 ? 166 TYR A CZ 1 ATOM 991 O OH . TYR A 1 133 ? 33.846 26.384 15.149 1.00 18.05 ? 166 TYR A OH 1 ATOM 992 N N . VAL A 1 134 ? 29.043 22.810 14.389 1.00 16.01 ? 167 VAL A N 1 ATOM 993 C CA . VAL A 1 134 ? 28.577 23.293 13.080 1.00 17.87 ? 167 VAL A CA 1 ATOM 994 C C . VAL A 1 134 ? 29.083 24.681 12.718 1.00 18.16 ? 167 VAL A C 1 ATOM 995 O O . VAL A 1 134 ? 28.463 25.393 11.882 1.00 17.90 ? 167 VAL A O 1 ATOM 996 C CB . VAL A 1 134 ? 27.045 23.144 12.958 1.00 18.39 ? 167 VAL A CB 1 ATOM 997 C CG1 . VAL A 1 134 ? 26.633 21.732 13.207 1.00 18.96 ? 167 VAL A CG1 1 ATOM 998 C CG2 . VAL A 1 134 ? 26.337 24.144 13.943 1.00 18.48 ? 167 VAL A CG2 1 ATOM 999 N N . ASN A 1 135 ? 30.176 25.111 13.310 1.00 16.93 ? 168 ASN A N 1 ATOM 1000 C CA . ASN A 1 135 ? 30.816 26.396 13.064 1.00 17.15 ? 168 ASN A CA 1 ATOM 1001 C C . ASN A 1 135 ? 29.829 27.492 13.354 1.00 18.38 ? 168 ASN A C 1 ATOM 1002 O O . ASN A 1 135 ? 29.299 27.478 14.462 1.00 17.88 ? 168 ASN A O 1 ATOM 1003 C CB . ASN A 1 135 ? 31.348 26.434 11.612 1.00 18.18 ? 168 ASN A CB 1 ATOM 1004 C CG . ASN A 1 135 ? 32.451 27.395 11.435 1.00 17.92 ? 168 ASN A CG 1 ATOM 1005 O OD1 . ASN A 1 135 ? 33.084 27.872 12.318 1.00 18.18 ? 168 ASN A OD1 1 ATOM 1006 N ND2 . ASN A 1 135 ? 32.690 27.717 10.127 1.00 22.54 ? 168 ASN A ND2 1 ATOM 1007 N N A TYR A 1 136 ? 29.336 28.176 12.317 0.60 16.78 ? 169 TYR A N 1 ATOM 1008 N N B TYR A 1 136 ? 29.738 28.580 12.554 0.40 15.76 ? 169 TYR A N 1 ATOM 1009 C CA A TYR A 1 136 ? 28.370 29.235 12.513 0.60 15.96 ? 169 TYR A CA 1 ATOM 1010 C CA B TYR A 1 136 ? 28.830 29.722 12.921 0.40 14.10 ? 169 TYR A CA 1 ATOM 1011 C C A TYR A 1 136 ? 26.911 28.830 12.231 0.60 15.24 ? 169 TYR A C 1 ATOM 1012 C C B TYR A 1 136 ? 27.366 29.449 12.577 0.40 12.29 ? 169 TYR A C 1 ATOM 1013 O O A TYR A 1 136 ? 26.012 29.635 12.343 0.60 15.23 ? 169 TYR A O 1 ATOM 1014 O O B TYR A 1 136 ? 26.510 30.344 12.658 0.40 13.48 ? 169 TYR A O 1 ATOM 1015 C CB A TYR A 1 136 ? 28.761 30.407 11.599 0.60 15.23 ? 169 TYR A CB 1 ATOM 1016 C CB B TYR A 1 136 ? 29.206 31.039 12.203 0.40 11.95 ? 169 TYR A CB 1 ATOM 1017 C CG A TYR A 1 136 ? 30.098 31.016 11.920 0.60 15.52 ? 169 TYR A CG 1 ATOM 1018 C CG B TYR A 1 136 ? 30.531 31.628 12.601 0.40 13.76 ? 169 TYR A CG 1 ATOM 1019 C CD1 A TYR A 1 136 ? 30.263 31.836 13.032 0.60 14.68 ? 169 TYR A CD1 1 ATOM 1020 C CD1 B TYR A 1 136 ? 30.636 32.465 13.718 0.40 12.00 ? 169 TYR A CD1 1 ATOM 1021 C CD2 A TYR A 1 136 ? 31.211 30.755 11.116 0.60 17.19 ? 169 TYR A CD2 1 ATOM 1022 C CD2 B TYR A 1 136 ? 31.643 31.461 11.787 0.40 13.87 ? 169 TYR A CD2 1 ATOM 1023 C CE1 A TYR A 1 136 ? 31.512 32.402 13.304 0.60 15.10 ? 169 TYR A CE1 1 ATOM 1024 C CE1 B TYR A 1 136 ? 31.850 33.047 14.066 0.40 12.48 ? 169 TYR A CE1 1 ATOM 1025 C CE2 A TYR A 1 136 ? 32.464 31.318 11.400 0.60 18.73 ? 169 TYR A CE2 1 ATOM 1026 C CE2 B TYR A 1 136 ? 32.863 32.002 12.119 0.40 14.01 ? 169 TYR A CE2 1 ATOM 1027 C CZ A TYR A 1 136 ? 32.600 32.141 12.494 0.60 17.41 ? 169 TYR A CZ 1 ATOM 1028 C CZ B TYR A 1 136 ? 32.970 32.827 13.252 0.40 12.77 ? 169 TYR A CZ 1 ATOM 1029 O OH A TYR A 1 136 ? 33.844 32.704 12.799 0.60 17.46 ? 169 TYR A OH 1 ATOM 1030 O OH B TYR A 1 136 ? 34.196 33.406 13.576 0.40 19.17 ? 169 TYR A OH 1 ATOM 1031 N N A ALA A 1 137 ? 26.710 27.552 11.917 0.60 15.15 ? 170 ALA A N 1 ATOM 1032 N N B ALA A 1 137 ? 27.082 28.228 12.130 0.40 14.59 ? 170 ALA A N 1 ATOM 1033 C CA A ALA A 1 137 ? 25.367 27.061 11.560 0.60 15.62 ? 170 ALA A CA 1 ATOM 1034 C CA B ALA A 1 137 ? 25.728 27.901 11.768 0.40 14.58 ? 170 ALA A CA 1 ATOM 1035 C C A ALA A 1 137 ? 24.737 27.839 10.394 0.60 16.02 ? 170 ALA A C 1 ATOM 1036 C C B ALA A 1 137 ? 25.181 28.769 10.633 0.40 15.86 ? 170 ALA A C 1 ATOM 1037 O O A ALA A 1 137 ? 23.509 27.974 10.299 0.60 18.07 ? 170 ALA A O 1 ATOM 1038 O O B ALA A 1 137 ? 23.992 28.964 10.562 0.40 16.62 ? 170 ALA A O 1 ATOM 1039 C CB A ALA A 1 137 ? 24.404 27.111 12.798 0.60 16.22 ? 170 ALA A CB 1 ATOM 1040 C CB B ALA A 1 137 ? 24.831 28.018 12.976 0.40 14.39 ? 170 ALA A CB 1 ATOM 1041 N N A ARG A 1 138 ? 25.606 28.308 9.494 0.60 16.37 ? 171 ARG A N 1 ATOM 1042 N N B ARG A 1 138 ? 26.090 29.281 9.792 0.40 16.08 ? 171 ARG A N 1 ATOM 1043 C CA A ARG A 1 138 ? 25.106 28.971 8.273 0.60 16.30 ? 171 ARG A CA 1 ATOM 1044 C CA B ARG A 1 138 ? 25.727 30.036 8.596 0.40 17.74 ? 171 ARG A CA 1 ATOM 1045 C C A ARG A 1 138 ? 24.652 27.913 7.321 0.60 16.33 ? 171 ARG A C 1 ATOM 1046 C C B ARG A 1 138 ? 25.285 29.045 7.532 0.40 18.00 ? 171 ARG A C 1 ATOM 1047 O O A ARG A 1 138 ? 25.040 26.745 7.408 0.60 18.75 ? 171 ARG A O 1 ATOM 1048 O O B ARG A 1 138 ? 25.645 27.880 7.557 0.40 17.24 ? 171 ARG A O 1 ATOM 1049 C CB A ARG A 1 138 ? 26.257 29.704 7.585 0.60 15.62 ? 171 ARG A CB 1 ATOM 1050 C CB B ARG A 1 138 ? 26.967 30.753 8.089 0.40 16.95 ? 171 ARG A CB 1 ATOM 1051 C CG A ARG A 1 138 ? 26.771 30.862 8.374 0.60 16.73 ? 171 ARG A CG 1 ATOM 1052 C CG B ARG A 1 138 ? 27.401 31.905 8.979 0.40 17.49 ? 171 ARG A CG 1 ATOM 1053 C CD A ARG A 1 138 ? 28.118 31.400 7.887 0.60 17.18 ? 171 ARG A CD 1 ATOM 1054 C CD B ARG A 1 138 ? 28.685 32.469 8.500 0.40 17.21 ? 171 ARG A CD 1 ATOM 1055 N NE A ARG A 1 138 ? 29.191 30.394 7.981 0.60 16.27 ? 171 ARG A NE 1 ATOM 1056 N NE B ARG A 1 138 ? 29.748 31.460 8.539 0.40 17.64 ? 171 ARG A NE 1 ATOM 1057 C CZ A ARG A 1 138 ? 30.455 30.580 7.587 0.60 18.87 ? 171 ARG A CZ 1 ATOM 1058 C CZ B ARG A 1 138 ? 31.002 31.671 8.149 0.40 23.71 ? 171 ARG A CZ 1 ATOM 1059 N NH1 A ARG A 1 138 ? 30.815 31.771 7.116 0.60 23.71 ? 171 ARG A NH1 1 ATOM 1060 N NH1 B ARG A 1 138 ? 31.375 32.859 7.710 0.40 23.41 ? 171 ARG A NH1 1 ATOM 1061 N NH2 A ARG A 1 138 ? 31.359 29.611 7.708 0.60 19.91 ? 171 ARG A NH2 1 ATOM 1062 N NH2 B ARG A 1 138 ? 31.898 30.688 8.234 0.40 24.20 ? 171 ARG A NH2 1 ATOM 1063 N N A THR A 1 139 ? 23.904 28.390 6.319 0.60 18.96 ? 172 THR A N 1 ATOM 1064 N N B THR A 1 139 ? 24.561 29.538 6.539 0.40 18.80 ? 172 THR A N 1 ATOM 1065 C CA A THR A 1 139 ? 23.504 27.505 5.255 0.60 20.66 ? 172 THR A CA 1 ATOM 1066 C CA B THR A 1 139 ? 24.169 28.758 5.397 0.40 19.09 ? 172 THR A CA 1 ATOM 1067 C C A THR A 1 139 ? 24.726 26.746 4.683 0.60 20.38 ? 172 THR A C 1 ATOM 1068 C C B THR A 1 139 ? 25.367 28.016 4.771 0.40 17.76 ? 172 THR A C 1 ATOM 1069 O O A THR A 1 139 ? 24.666 25.531 4.491 0.60 20.41 ? 172 THR A O 1 ATOM 1070 O O B THR A 1 139 ? 25.307 26.798 4.468 0.40 18.20 ? 172 THR A O 1 ATOM 1071 C CB A THR A 1 139 ? 22.732 28.280 4.153 0.60 20.95 ? 172 THR A CB 1 ATOM 1072 C CB B THR A 1 139 ? 23.542 29.674 4.330 0.40 20.30 ? 172 THR A CB 1 ATOM 1073 O OG1 A THR A 1 139 ? 21.529 28.840 4.701 0.60 24.26 ? 172 THR A OG1 1 ATOM 1074 O OG1 B THR A 1 139 ? 22.300 30.199 4.838 0.40 22.43 ? 172 THR A OG1 1 ATOM 1075 C CG2 A THR A 1 139 ? 22.372 27.348 2.977 0.60 23.38 ? 172 THR A CG2 1 ATOM 1076 C CG2 B THR A 1 139 ? 23.308 28.922 3.070 0.40 20.47 ? 172 THR A CG2 1 ATOM 1077 N N A GLU A 1 140 ? 25.848 27.453 4.460 0.60 19.96 ? 173 GLU A N 1 ATOM 1078 N N B GLU A 1 140 ? 26.461 28.742 4.621 0.40 18.48 ? 173 GLU A N 1 ATOM 1079 C CA A GLU A 1 140 ? 27.007 26.760 3.890 0.60 21.22 ? 173 GLU A CA 1 ATOM 1080 C CA B GLU A 1 140 ? 27.632 28.185 3.947 0.40 19.75 ? 173 GLU A CA 1 ATOM 1081 C C A GLU A 1 140 ? 27.708 25.754 4.821 0.60 20.36 ? 173 GLU A C 1 ATOM 1082 C C B GLU A 1 140 ? 28.370 27.189 4.860 0.40 19.98 ? 173 GLU A C 1 ATOM 1083 O O A GLU A 1 140 ? 28.360 24.809 4.362 0.60 22.24 ? 173 GLU A O 1 ATOM 1084 O O B GLU A 1 140 ? 29.148 26.349 4.399 0.40 21.43 ? 173 GLU A O 1 ATOM 1085 C CB A GLU A 1 140 ? 28.013 27.740 3.288 0.60 22.96 ? 173 GLU A CB 1 ATOM 1086 C CB B GLU A 1 140 ? 28.563 29.272 3.396 0.40 20.83 ? 173 GLU A CB 1 ATOM 1087 C CG A GLU A 1 140 ? 28.624 28.681 4.300 0.60 25.83 ? 173 GLU A CG 1 ATOM 1088 C CG B GLU A 1 140 ? 29.318 30.115 4.422 0.40 20.23 ? 173 GLU A CG 1 ATOM 1089 C CD A GLU A 1 140 ? 27.955 30.031 4.288 0.60 33.30 ? 173 GLU A CD 1 ATOM 1090 C CD B GLU A 1 140 ? 28.634 31.482 4.756 0.40 23.52 ? 173 GLU A CD 1 ATOM 1091 O OE1 A GLU A 1 140 ? 26.687 30.100 4.305 0.60 35.16 ? 173 GLU A OE1 1 ATOM 1092 O OE1 B GLU A 1 140 ? 27.390 31.630 4.662 0.40 26.24 ? 173 GLU A OE1 1 ATOM 1093 O OE2 A GLU A 1 140 ? 28.720 31.030 4.230 0.60 38.20 ? 173 GLU A OE2 1 ATOM 1094 O OE2 B GLU A 1 140 ? 29.366 32.414 5.132 0.40 27.42 ? 173 GLU A OE2 1 ATOM 1095 N N A ASP A 1 141 ? 27.543 25.935 6.139 0.60 18.54 ? 174 ASP A N 1 ATOM 1096 N N B ASP A 1 141 ? 28.100 27.261 6.163 0.40 19.25 ? 174 ASP A N 1 ATOM 1097 C CA A ASP A 1 141 ? 28.163 25.025 7.092 0.60 18.48 ? 174 ASP A CA 1 ATOM 1098 C CA B ASP A 1 141 ? 28.637 26.249 7.067 0.40 18.70 ? 174 ASP A CA 1 ATOM 1099 C C A ASP A 1 141 ? 27.409 23.675 7.045 0.60 16.60 ? 174 ASP A C 1 ATOM 1100 C C B ASP A 1 141 ? 27.866 24.935 6.928 0.40 18.39 ? 174 ASP A C 1 ATOM 1101 O O A ASP A 1 141 ? 28.018 22.628 7.007 0.60 18.61 ? 174 ASP A O 1 ATOM 1102 O O B ASP A 1 141 ? 28.468 23.881 6.938 0.40 17.73 ? 174 ASP A O 1 ATOM 1103 C CB A ASP A 1 141 ? 28.106 25.666 8.498 0.60 16.60 ? 174 ASP A CB 1 ATOM 1104 C CB B ASP A 1 141 ? 28.608 26.717 8.541 0.40 18.24 ? 174 ASP A CB 1 ATOM 1105 C CG A ASP A 1 141 ? 28.975 26.931 8.611 0.60 15.76 ? 174 ASP A CG 1 ATOM 1106 C CG B ASP A 1 141 ? 29.530 27.908 8.806 0.40 16.73 ? 174 ASP A CG 1 ATOM 1107 O OD1 A ASP A 1 141 ? 30.088 26.916 8.019 0.60 18.29 ? 174 ASP A OD1 1 ATOM 1108 O OD1 B ASP A 1 141 ? 30.647 27.958 8.244 0.40 16.33 ? 174 ASP A OD1 1 ATOM 1109 O OD2 A ASP A 1 141 ? 28.540 27.908 9.268 0.60 16.45 ? 174 ASP A OD2 1 ATOM 1110 O OD2 B ASP A 1 141 ? 29.118 28.843 9.548 0.40 17.49 ? 174 ASP A OD2 1 ATOM 1111 N N A PHE A 1 142 ? 26.081 23.760 7.076 0.60 19.35 ? 175 PHE A N 1 ATOM 1112 N N B PHE A 1 142 ? 26.537 24.995 6.854 0.40 16.25 ? 175 PHE A N 1 ATOM 1113 C CA A PHE A 1 142 ? 25.268 22.575 6.932 0.60 19.60 ? 175 PHE A CA 1 ATOM 1114 C CA B PHE A 1 142 ? 25.709 23.812 6.642 0.40 17.24 ? 175 PHE A CA 1 ATOM 1115 C C A PHE A 1 142 ? 25.393 21.898 5.570 0.60 20.81 ? 175 PHE A C 1 ATOM 1116 C C B PHE A 1 142 ? 25.912 23.223 5.223 0.40 16.37 ? 175 PHE A C 1 ATOM 1117 O O A PHE A 1 142 ? 25.446 20.686 5.524 0.60 21.15 ? 175 PHE A O 1 ATOM 1118 O O B PHE A 1 142 ? 25.935 22.006 5.080 0.40 16.91 ? 175 PHE A O 1 ATOM 1119 C CB A PHE A 1 142 ? 23.801 22.855 7.263 0.60 19.97 ? 175 PHE A CB 1 ATOM 1120 C CB B PHE A 1 142 ? 24.217 24.031 6.987 0.40 16.38 ? 175 PHE A CB 1 ATOM 1121 C CG A PHE A 1 142 ? 23.547 23.024 8.744 0.60 19.73 ? 175 PHE A CG 1 ATOM 1122 C CG B PHE A 1 142 ? 23.960 24.170 8.463 0.40 17.19 ? 175 PHE A CG 1 ATOM 1123 C CD1 A PHE A 1 142 ? 23.292 24.268 9.297 0.60 18.22 ? 175 PHE A CD1 1 ATOM 1124 C CD1 B PHE A 1 142 ? 23.679 25.413 9.010 0.40 15.04 ? 175 PHE A CD1 1 ATOM 1125 C CD2 A PHE A 1 142 ? 23.579 21.923 9.566 0.60 18.45 ? 175 PHE A CD2 1 ATOM 1126 C CD2 B PHE A 1 142 ? 24.012 23.074 9.284 0.40 14.14 ? 175 PHE A CD2 1 ATOM 1127 C CE1 A PHE A 1 142 ? 23.097 24.382 10.682 0.60 18.82 ? 175 PHE A CE1 1 ATOM 1128 C CE1 B PHE A 1 142 ? 23.464 25.554 10.383 0.40 15.91 ? 175 PHE A CE1 1 ATOM 1129 C CE2 A PHE A 1 142 ? 23.394 22.028 10.928 0.60 18.98 ? 175 PHE A CE2 1 ATOM 1130 C CE2 B PHE A 1 142 ? 23.792 23.206 10.673 0.40 15.39 ? 175 PHE A CE2 1 ATOM 1131 C CZ A PHE A 1 142 ? 23.120 23.259 11.477 0.60 17.98 ? 175 PHE A CZ 1 ATOM 1132 C CZ B PHE A 1 142 ? 23.499 24.449 11.188 0.40 15.08 ? 175 PHE A CZ 1 ATOM 1133 N N A PHE A 1 143 ? 25.464 22.696 4.493 0.60 22.25 ? 176 PHE A N 1 ATOM 1134 N N B PHE A 1 143 ? 26.044 24.077 4.200 0.40 18.68 ? 176 PHE A N 1 ATOM 1135 C CA A PHE A 1 143 ? 25.764 22.153 3.130 0.60 24.08 ? 176 PHE A CA 1 ATOM 1136 C CA B PHE A 1 143 ? 26.381 23.596 2.871 0.40 18.89 ? 176 PHE A CA 1 ATOM 1137 C C A PHE A 1 143 ? 27.034 21.279 3.205 0.60 23.64 ? 176 PHE A C 1 ATOM 1138 C C B PHE A 1 143 ? 27.641 22.728 2.944 0.40 18.29 ? 176 PHE A C 1 ATOM 1139 O O A PHE A 1 143 ? 27.060 20.108 2.774 0.60 24.24 ? 176 PHE A O 1 ATOM 1140 O O B PHE A 1 143 ? 27.741 21.650 2.323 0.40 19.77 ? 176 PHE A O 1 ATOM 1141 C CB A PHE A 1 143 ? 26.007 23.267 2.095 0.60 26.73 ? 176 PHE A CB 1 ATOM 1142 C CB B PHE A 1 143 ? 26.725 24.745 1.917 0.40 19.57 ? 176 PHE A CB 1 ATOM 1143 C CG A PHE A 1 143 ? 24.751 23.931 1.516 0.60 31.58 ? 176 PHE A CG 1 ATOM 1144 C CG B PHE A 1 143 ? 25.540 25.512 1.342 0.40 19.70 ? 176 PHE A CG 1 ATOM 1145 C CD1 A PHE A 1 143 ? 23.469 23.453 1.755 0.60 36.69 ? 176 PHE A CD1 1 ATOM 1146 C CD1 B PHE A 1 143 ? 24.227 25.056 1.473 0.40 21.84 ? 176 PHE A CD1 1 ATOM 1147 C CD2 A PHE A 1 143 ? 24.891 25.036 0.653 0.60 36.13 ? 176 PHE A CD2 1 ATOM 1148 C CD2 B PHE A 1 143 ? 25.782 26.654 0.629 0.40 17.62 ? 176 PHE A CD2 1 ATOM 1149 C CE1 A PHE A 1 143 ? 22.320 24.090 1.180 0.60 36.59 ? 176 PHE A CE1 1 ATOM 1150 C CE1 B PHE A 1 143 ? 23.147 25.785 0.939 0.40 24.91 ? 176 PHE A CE1 1 ATOM 1151 C CE2 A PHE A 1 143 ? 23.769 25.647 0.059 0.60 38.10 ? 176 PHE A CE2 1 ATOM 1152 C CE2 B PHE A 1 143 ? 24.720 27.384 0.059 0.40 23.45 ? 176 PHE A CE2 1 ATOM 1153 C CZ A PHE A 1 143 ? 22.485 25.176 0.344 0.60 37.45 ? 176 PHE A CZ 1 ATOM 1154 C CZ B PHE A 1 143 ? 23.407 26.937 0.223 0.40 20.98 ? 176 PHE A CZ 1 ATOM 1155 N N A LYS A 1 144 ? 28.102 21.844 3.765 0.60 22.03 ? 177 LYS A N 1 ATOM 1156 N N B LYS A 1 144 ? 28.636 23.262 3.648 0.40 17.17 ? 177 LYS A N 1 ATOM 1157 C CA A LYS A 1 144 ? 29.358 21.126 3.880 0.60 20.47 ? 177 LYS A CA 1 ATOM 1158 C CA B LYS A 1 144 ? 29.923 22.601 3.758 0.40 17.07 ? 177 LYS A CA 1 ATOM 1159 C C A LYS A 1 144 ? 29.241 19.836 4.686 0.60 20.73 ? 177 LYS A C 1 ATOM 1160 C C B LYS A 1 144 ? 29.804 21.253 4.471 0.40 17.79 ? 177 LYS A C 1 ATOM 1161 O O A LYS A 1 144 ? 29.750 18.792 4.298 0.60 21.25 ? 177 LYS A O 1 ATOM 1162 O O B LYS A 1 144 ? 30.410 20.300 4.050 0.40 17.45 ? 177 LYS A O 1 ATOM 1163 C CB A LYS A 1 144 ? 30.462 22.050 4.438 0.60 20.32 ? 177 LYS A CB 1 ATOM 1164 C CB B LYS A 1 144 ? 30.968 23.499 4.398 0.40 17.35 ? 177 LYS A CB 1 ATOM 1165 C CG A LYS A 1 144 ? 31.856 21.510 4.193 0.60 22.40 ? 177 LYS A CG 1 ATOM 1166 C CG B LYS A 1 144 ? 32.396 22.997 4.144 0.40 17.53 ? 177 LYS A CG 1 ATOM 1167 C CD A LYS A 1 144 ? 32.933 22.286 4.974 0.60 23.33 ? 177 LYS A CD 1 ATOM 1168 C CD B LYS A 1 144 ? 33.362 23.812 4.942 0.40 18.19 ? 177 LYS A CD 1 ATOM 1169 C CE A LYS A 1 144 ? 34.315 21.920 4.498 0.60 22.66 ? 177 LYS A CE 1 ATOM 1170 C CE B LYS A 1 144 ? 34.777 23.378 4.718 0.40 19.46 ? 177 LYS A CE 1 ATOM 1171 N NZ A LYS A 1 144 ? 34.552 22.306 3.081 0.60 23.75 ? 177 LYS A NZ 1 ATOM 1172 N NZ B LYS A 1 144 ? 35.179 23.486 3.290 0.40 20.49 ? 177 LYS A NZ 1 ATOM 1173 N N A LEU A 1 145 ? 28.553 19.894 5.826 0.60 20.08 ? 178 LEU A N 1 ATOM 1174 N N B LEU A 1 145 ? 29.033 21.195 5.560 0.40 17.60 ? 178 LEU A N 1 ATOM 1175 C CA A LEU A 1 145 ? 28.411 18.723 6.697 0.60 20.47 ? 178 LEU A CA 1 ATOM 1176 C CA B LEU A 1 145 ? 28.850 19.932 6.278 0.40 18.46 ? 178 LEU A CA 1 ATOM 1177 C C A LEU A 1 145 ? 27.653 17.605 5.995 0.60 20.31 ? 178 LEU A C 1 ATOM 1178 C C B LEU A 1 145 ? 28.192 18.855 5.435 0.40 19.47 ? 178 LEU A C 1 ATOM 1179 O O A LEU A 1 145 ? 28.050 16.442 6.049 0.60 21.02 ? 178 LEU A O 1 ATOM 1180 O O B LEU A 1 145 ? 28.667 17.715 5.367 0.40 19.35 ? 178 LEU A O 1 ATOM 1181 C CB A LEU A 1 145 ? 27.646 19.096 7.968 0.60 19.92 ? 178 LEU A CB 1 ATOM 1182 C CB B LEU A 1 145 ? 28.015 20.173 7.526 0.40 18.80 ? 178 LEU A CB 1 ATOM 1183 C CG A LEU A 1 145 ? 28.346 19.949 9.007 0.60 20.93 ? 178 LEU A CG 1 ATOM 1184 C CG B LEU A 1 145 ? 28.711 20.991 8.606 0.40 15.97 ? 178 LEU A CG 1 ATOM 1185 C CD1 A LEU A 1 145 ? 27.284 20.572 9.941 0.60 21.43 ? 178 LEU A CD1 1 ATOM 1186 C CD1 B LEU A 1 145 ? 27.681 21.683 9.512 0.40 15.95 ? 178 LEU A CD1 1 ATOM 1187 C CD2 A LEU A 1 145 ? 29.332 19.114 9.736 0.60 24.08 ? 178 LEU A CD2 1 ATOM 1188 C CD2 B LEU A 1 145 ? 29.642 20.096 9.441 0.40 13.70 ? 178 LEU A CD2 1 ATOM 1189 N N A GLU A 1 146 ? 26.556 17.987 5.352 0.60 21.75 ? 179 GLU A N 1 ATOM 1190 N N B GLU A 1 146 ? 27.102 19.214 4.769 0.40 20.10 ? 179 GLU A N 1 ATOM 1191 C CA A GLU A 1 146 ? 25.618 17.023 4.753 0.60 23.77 ? 179 GLU A CA 1 ATOM 1192 C CA B GLU A 1 146 ? 26.355 18.245 4.001 0.40 21.59 ? 179 GLU A CA 1 ATOM 1193 C C A GLU A 1 146 ? 26.036 16.584 3.351 0.60 23.23 ? 179 GLU A C 1 ATOM 1194 C C B GLU A 1 146 ? 26.961 17.888 2.635 0.40 22.02 ? 179 GLU A C 1 ATOM 1195 O O A GLU A 1 146 ? 26.073 15.371 3.077 0.60 25.27 ? 179 GLU A O 1 ATOM 1196 O O B GLU A 1 146 ? 26.869 16.728 2.200 0.40 22.65 ? 179 GLU A O 1 ATOM 1197 C CB A GLU A 1 146 ? 24.207 17.624 4.708 0.60 23.59 ? 179 GLU A CB 1 ATOM 1198 C CB B GLU A 1 146 ? 24.896 18.696 3.858 0.40 22.95 ? 179 GLU A CB 1 ATOM 1199 C CG A GLU A 1 146 ? 23.440 17.495 6.040 0.60 28.75 ? 179 GLU A CG 1 ATOM 1200 C CG B GLU A 1 146 ? 24.159 18.726 5.206 0.40 25.59 ? 179 GLU A CG 1 ATOM 1201 C CD A GLU A 1 146 ? 23.792 18.540 7.077 0.60 36.88 ? 179 GLU A CD 1 ATOM 1202 C CD B GLU A 1 146 ? 22.649 18.893 5.067 0.40 30.42 ? 179 GLU A CD 1 ATOM 1203 O OE1 A GLU A 1 146 ? 24.402 18.155 8.101 0.60 39.73 ? 179 GLU A OE1 1 ATOM 1204 O OE1 B GLU A 1 146 ? 22.042 19.479 5.993 0.40 29.18 ? 179 GLU A OE1 1 ATOM 1205 O OE2 A GLU A 1 146 ? 23.440 19.742 6.899 0.60 37.95 ? 179 GLU A OE2 1 ATOM 1206 O OE2 B GLU A 1 146 ? 22.086 18.439 4.028 0.40 32.24 ? 179 GLU A OE2 1 ATOM 1207 N N A ARG A 1 147 ? 26.333 17.553 2.477 0.60 24.85 ? 180 ARG A N 1 ATOM 1208 N N B ARG A 1 147 ? 27.587 18.873 1.982 0.40 22.03 ? 180 ARG A N 1 ATOM 1209 C CA A ARG A 1 147 ? 26.606 17.286 1.039 0.60 25.77 ? 180 ARG A CA 1 ATOM 1210 C CA B ARG A 1 147 ? 28.078 18.703 0.593 0.40 22.38 ? 180 ARG A CA 1 ATOM 1211 C C A ARG A 1 147 ? 28.014 16.704 0.888 0.60 25.76 ? 180 ARG A C 1 ATOM 1212 C C B ARG A 1 147 ? 29.552 18.325 0.477 0.40 22.60 ? 180 ARG A C 1 ATOM 1213 O O A ARG A 1 147 ? 28.231 15.674 0.225 0.60 25.28 ? 180 ARG A O 1 ATOM 1214 O O B ARG A 1 147 ? 29.994 17.819 -0.561 0.40 22.65 ? 180 ARG A O 1 ATOM 1215 C CB A ARG A 1 147 ? 26.504 18.562 0.168 0.60 27.00 ? 180 ARG A CB 1 ATOM 1216 C CB B ARG A 1 147 ? 27.836 19.977 -0.241 0.40 22.94 ? 180 ARG A CB 1 ATOM 1217 C CG A ARG A 1 147 ? 25.137 19.304 0.080 0.60 29.31 ? 180 ARG A CG 1 ATOM 1218 C CG B ARG A 1 147 ? 26.379 20.398 -0.361 0.40 24.26 ? 180 ARG A CG 1 ATOM 1219 C CD A ARG A 1 147 ? 25.226 20.673 -0.687 0.60 33.41 ? 180 ARG A CD 1 ATOM 1220 C CD B ARG A 1 147 ? 26.206 21.650 -1.214 0.40 23.50 ? 180 ARG A CD 1 ATOM 1221 N NE A ARG A 1 147 ? 23.891 21.157 -1.088 0.60 31.29 ? 180 ARG A NE 1 ATOM 1222 N NE B ARG A 1 147 ? 24.825 22.085 -1.091 0.40 24.83 ? 180 ARG A NE 1 ATOM 1223 C CZ A ARG A 1 147 ? 23.605 22.334 -1.666 0.60 35.10 ? 180 ARG A CZ 1 ATOM 1224 C CZ B ARG A 1 147 ? 24.319 23.247 -1.513 0.40 25.72 ? 180 ARG A CZ 1 ATOM 1225 N NH1 A ARG A 1 147 ? 24.551 23.227 -1.933 0.60 34.35 ? 180 ARG A NH1 1 ATOM 1226 N NH1 B ARG A 1 147 ? 25.082 24.163 -2.099 0.40 26.91 ? 180 ARG A NH1 1 ATOM 1227 N NH2 A ARG A 1 147 ? 22.339 22.627 -1.976 0.60 34.40 ? 180 ARG A NH2 1 ATOM 1228 N NH2 B ARG A 1 147 ? 23.029 23.490 -1.321 0.40 30.78 ? 180 ARG A NH2 1 ATOM 1229 N N A GLU A 1 148 ? 28.990 17.393 1.457 0.60 25.22 ? 181 GLU A N 1 ATOM 1230 N N B GLU A 1 148 ? 30.331 18.569 1.518 0.40 22.30 ? 181 GLU A N 1 ATOM 1231 C CA A GLU A 1 148 ? 30.370 16.987 1.279 0.60 25.45 ? 181 GLU A CA 1 ATOM 1232 C CA B GLU A 1 148 ? 31.783 18.495 1.390 0.40 22.41 ? 181 GLU A CA 1 ATOM 1233 C C A GLU A 1 148 ? 30.724 15.844 2.179 0.60 25.25 ? 181 GLU A C 1 ATOM 1234 C C B GLU A 1 148 ? 32.366 17.608 2.473 0.40 21.38 ? 181 GLU A C 1 ATOM 1235 O O A GLU A 1 148 ? 31.302 14.861 1.723 0.60 26.03 ? 181 GLU A O 1 ATOM 1236 O O B GLU A 1 148 ? 33.334 16.897 2.235 0.40 20.57 ? 181 GLU A O 1 ATOM 1237 C CB A GLU A 1 148 ? 31.336 18.144 1.513 0.60 25.32 ? 181 GLU A CB 1 ATOM 1238 C CB B GLU A 1 148 ? 32.408 19.896 1.524 0.40 23.19 ? 181 GLU A CB 1 ATOM 1239 C CG A GLU A 1 148 ? 31.129 19.327 0.597 0.60 26.60 ? 181 GLU A CG 1 ATOM 1240 C CG B GLU A 1 148 ? 32.420 20.766 0.269 0.40 25.66 ? 181 GLU A CG 1 ATOM 1241 C CD A GLU A 1 148 ? 32.193 20.415 0.708 0.60 28.80 ? 181 GLU A CD 1 ATOM 1242 C CD B GLU A 1 148 ? 33.227 22.054 0.453 0.40 29.46 ? 181 GLU A CD 1 ATOM 1243 O OE1 A GLU A 1 148 ? 31.894 21.517 0.175 0.60 30.87 ? 181 GLU A OE1 1 ATOM 1244 O OE1 B GLU A 1 148 ? 32.747 23.139 0.030 0.40 30.90 ? 181 GLU A OE1 1 ATOM 1245 O OE2 A GLU A 1 148 ? 33.287 20.186 1.306 0.60 26.88 ? 181 GLU A OE2 1 ATOM 1246 O OE2 B GLU A 1 148 ? 34.337 21.984 1.019 0.40 29.73 ? 181 GLU A OE2 1 ATOM 1247 N N A MET A 1 149 ? 30.438 15.976 3.473 0.60 25.62 ? 182 MET A N 1 ATOM 1248 N N B MET A 1 149 ? 31.767 17.691 3.662 0.40 19.28 ? 182 MET A N 1 ATOM 1249 C CA A MET A 1 149 ? 30.909 15.002 4.449 0.60 25.79 ? 182 MET A CA 1 ATOM 1250 C CA B MET A 1 149 ? 32.307 17.056 4.859 0.40 18.27 ? 182 MET A CA 1 ATOM 1251 C C A MET A 1 149 ? 29.996 13.809 4.674 0.60 25.42 ? 182 MET A C 1 ATOM 1252 C C B MET A 1 149 ? 31.679 15.703 5.231 0.40 19.18 ? 182 MET A C 1 ATOM 1253 O O A MET A 1 149 ? 30.412 12.810 5.250 0.60 25.96 ? 182 MET A O 1 ATOM 1254 O O B MET A 1 149 ? 32.216 14.976 6.053 0.40 19.16 ? 182 MET A O 1 ATOM 1255 C CB A MET A 1 149 ? 31.203 15.704 5.758 0.60 26.81 ? 182 MET A CB 1 ATOM 1256 C CB B MET A 1 149 ? 32.220 18.045 6.003 0.40 16.18 ? 182 MET A CB 1 ATOM 1257 C CG A MET A 1 149 ? 32.418 16.626 5.656 0.60 28.30 ? 182 MET A CG 1 ATOM 1258 C CG B MET A 1 149 ? 33.121 19.251 5.833 0.40 16.90 ? 182 MET A CG 1 ATOM 1259 S SD A MET A 1 149 ? 32.646 17.493 7.214 0.60 30.48 ? 182 MET A SD 1 ATOM 1260 S SD B MET A 1 149 ? 32.682 20.645 6.893 0.40 19.91 ? 182 MET A SD 1 ATOM 1261 C CE A MET A 1 149 ? 32.089 19.147 6.765 0.60 29.66 ? 182 MET A CE 1 ATOM 1262 C CE B MET A 1 149 ? 33.159 19.994 8.512 0.40 17.84 ? 182 MET A CE 1 ATOM 1263 N N A GLY A 1 150 ? 28.756 13.909 4.210 0.60 25.10 ? 183 GLY A N 1 ATOM 1264 N N B GLY A 1 150 ? 30.562 15.344 4.621 0.40 19.60 ? 183 GLY A N 1 ATOM 1265 C CA A GLY A 1 150 ? 27.775 12.847 4.403 0.60 25.09 ? 183 GLY A CA 1 ATOM 1266 C CA B GLY A 1 150 ? 29.910 14.069 4.948 0.40 19.67 ? 183 GLY A CA 1 ATOM 1267 C C A GLY A 1 150 ? 27.378 12.636 5.857 0.60 25.53 ? 183 GLY A C 1 ATOM 1268 C C B GLY A 1 150 ? 29.150 13.992 6.274 0.40 19.92 ? 183 GLY A C 1 ATOM 1269 O O A GLY A 1 150 ? 26.983 11.524 6.244 0.60 25.85 ? 183 GLY A O 1 ATOM 1270 O O B GLY A 1 150 ? 28.920 12.901 6.809 0.40 18.73 ? 183 GLY A O 1 ATOM 1271 N N A ILE A 1 151 ? 27.504 13.705 6.656 0.60 25.62 ? 184 ILE A N 1 ATOM 1272 N N B ILE A 1 151 ? 28.716 15.142 6.793 0.40 19.97 ? 184 ILE A N 1 ATOM 1273 C CA A ILE A 1 151 ? 27.112 13.696 8.082 0.60 27.03 ? 184 ILE A CA 1 ATOM 1274 C CA B ILE A 1 151 ? 28.017 15.187 8.093 0.40 21.65 ? 184 ILE A CA 1 ATOM 1275 C C A ILE A 1 151 ? 25.624 13.969 8.230 0.60 27.00 ? 184 ILE A C 1 ATOM 1276 C C B ILE A 1 151 ? 26.493 15.338 7.962 0.40 22.06 ? 184 ILE A C 1 ATOM 1277 O O A ILE A 1 151 ? 25.055 14.866 7.589 0.60 26.19 ? 184 ILE A O 1 ATOM 1278 O O B ILE A 1 151 ? 26.052 16.275 7.304 0.40 23.49 ? 184 ILE A O 1 ATOM 1279 C CB A ILE A 1 151 ? 27.906 14.721 8.922 0.60 27.42 ? 184 ILE A CB 1 ATOM 1280 C CB B ILE A 1 151 ? 28.606 16.315 8.959 0.40 21.07 ? 184 ILE A CB 1 ATOM 1281 C CG1 A ILE A 1 151 ? 29.362 14.257 9.038 0.60 29.27 ? 184 ILE A CG1 1 ATOM 1282 C CG1 B ILE A 1 151 ? 30.071 16.043 9.253 0.40 21.11 ? 184 ILE A CG1 1 ATOM 1283 C CG2 A ILE A 1 151 ? 27.212 15.011 10.304 0.60 28.24 ? 184 ILE A CG2 1 ATOM 1284 C CG2 B ILE A 1 151 ? 27.850 16.470 10.274 0.40 20.56 ? 184 ILE A CG2 1 ATOM 1285 C CD1 A ILE A 1 151 ? 30.368 15.359 9.282 0.60 33.54 ? 184 ILE A CD1 1 ATOM 1286 C CD1 B ILE A 1 151 ? 30.264 14.932 10.278 0.40 21.04 ? 184 ILE A CD1 1 ATOM 1287 N N A ASN A 1 152 ? 25.014 13.169 9.088 0.60 27.45 ? 185 ASN A N 1 ATOM 1288 N N B ASN A 1 152 ? 25.711 14.393 8.527 0.40 22.66 ? 185 ASN A N 1 ATOM 1289 C CA A ASN A 1 152 ? 23.616 13.277 9.331 0.60 27.92 ? 185 ASN A CA 1 ATOM 1290 C CA B ASN A 1 152 ? 24.214 14.453 8.644 0.40 23.51 ? 185 ASN A CA 1 ATOM 1291 C C A ASN A 1 152 ? 23.265 13.920 10.649 0.60 26.08 ? 185 ASN A C 1 ATOM 1292 C C B ASN A 1 152 ? 23.907 15.041 10.028 0.40 22.70 ? 185 ASN A C 1 ATOM 1293 O O A ASN A 1 152 ? 23.512 13.328 11.694 0.60 27.63 ? 185 ASN A O 1 ATOM 1294 O O B ASN A 1 152 ? 24.159 14.399 11.037 0.40 21.86 ? 185 ASN A O 1 ATOM 1295 C CB A ASN A 1 152 ? 23.031 11.907 9.347 0.60 28.29 ? 185 ASN A CB 1 ATOM 1296 C CB B ASN A 1 152 ? 23.521 13.042 8.436 0.40 24.81 ? 185 ASN A CB 1 ATOM 1297 C CG A ASN A 1 152 ? 21.590 11.954 9.162 0.60 32.98 ? 185 ASN A CG 1 ATOM 1298 C CG B ASN A 1 152 ? 21.924 13.091 8.394 0.40 30.29 ? 185 ASN A CG 1 ATOM 1299 O OD1 A ASN A 1 152 ? 20.860 12.732 9.818 0.60 32.81 ? 185 ASN A OD1 1 ATOM 1300 O OD1 B ASN A 1 152 ? 21.359 14.182 8.467 0.40 30.84 ? 185 ASN A OD1 1 ATOM 1301 N ND2 A ASN A 1 152 ? 21.126 11.176 8.243 0.60 39.46 ? 185 ASN A ND2 1 ATOM 1302 N ND2 B ASN A 1 152 ? 21.215 11.865 8.285 0.40 36.74 ? 185 ASN A ND2 1 ATOM 1303 N N A CYS A 1 153 ? 22.644 15.092 10.596 0.60 25.62 ? 186 CYS A N 1 ATOM 1304 N N B CYS A 1 153 ? 23.379 16.265 10.095 0.40 21.44 ? 186 CYS A N 1 ATOM 1305 C CA A CYS A 1 153 ? 22.362 15.827 11.815 0.60 24.09 ? 186 CYS A CA 1 ATOM 1306 C CA B CYS A 1 153 ? 22.963 16.819 11.396 0.40 20.95 ? 186 CYS A CA 1 ATOM 1307 C C A CYS A 1 153 ? 21.049 15.428 12.455 0.60 23.69 ? 186 CYS A C 1 ATOM 1308 C C B CYS A 1 153 ? 21.582 16.353 11.870 0.40 20.63 ? 186 CYS A C 1 ATOM 1309 O O A CYS A 1 153 ? 20.727 15.909 13.546 0.60 22.13 ? 186 CYS A O 1 ATOM 1310 O O B CYS A 1 153 ? 21.119 16.772 12.930 0.40 18.24 ? 186 CYS A O 1 ATOM 1311 C CB A CYS A 1 153 ? 22.394 17.336 11.582 0.60 23.98 ? 186 CYS A CB 1 ATOM 1312 C CB B CYS A 1 153 ? 23.005 18.366 11.409 0.40 21.29 ? 186 CYS A CB 1 ATOM 1313 S SG A CYS A 1 153 ? 24.061 17.959 11.183 0.60 29.00 ? 186 CYS A SG 1 ATOM 1314 S SG B CYS A 1 153 ? 24.609 19.157 11.253 0.40 21.30 ? 186 CYS A SG 1 ATOM 1315 N N A THR A 1 154 ? 20.292 14.561 11.781 0.60 22.24 ? 187 THR A N 1 ATOM 1316 N N B THR A 1 154 ? 20.912 15.500 11.102 0.40 20.03 ? 187 THR A N 1 ATOM 1317 C CA A THR A 1 154 ? 19.058 14.040 12.340 0.60 21.99 ? 187 THR A CA 1 ATOM 1318 C CA B THR A 1 154 ? 19.592 15.001 11.516 0.40 21.44 ? 187 THR A CA 1 ATOM 1319 C C A THR A 1 154 ? 19.274 13.343 13.688 0.60 20.38 ? 187 THR A C 1 ATOM 1320 C C B THR A 1 154 ? 19.561 14.229 12.875 0.40 21.70 ? 187 THR A C 1 ATOM 1321 O O A THR A 1 154 ? 19.999 12.383 13.841 0.60 21.54 ? 187 THR A O 1 ATOM 1322 O O B THR A 1 154 ? 20.317 13.253 13.012 0.40 22.06 ? 187 THR A O 1 ATOM 1323 C CB A THR A 1 154 ? 18.244 13.156 11.363 0.60 22.46 ? 187 THR A CB 1 ATOM 1324 C CB B THR A 1 154 ? 18.956 14.107 10.399 0.40 21.40 ? 187 THR A CB 1 ATOM 1325 O OG1 A THR A 1 154 ? 18.064 13.863 10.134 0.60 24.68 ? 187 THR A OG1 1 ATOM 1326 O OG1 B THR A 1 154 ? 18.927 14.801 9.131 0.40 22.60 ? 187 THR A OG1 1 ATOM 1327 C CG2 A THR A 1 154 ? 16.864 12.876 11.944 0.60 24.15 ? 187 THR A CG2 1 ATOM 1328 C CG2 B THR A 1 154 ? 17.537 13.730 10.797 0.40 20.38 ? 187 THR A CG2 1 ATOM 1329 N N A GLY A 1 155 ? 18.628 13.910 14.700 0.40 18.60 ? 188 GLY A N 1 ATOM 1330 N N B GLY A 1 155 ? 18.727 14.656 13.856 0.60 22.58 ? 188 GLY A N 1 ATOM 1331 C CA A GLY A 1 155 ? 18.683 13.379 16.064 0.40 17.91 ? 188 GLY A CA 1 ATOM 1332 C CA B GLY A 1 155 ? 18.577 13.982 15.162 0.60 21.49 ? 188 GLY A CA 1 ATOM 1333 C C A GLY A 1 155 ? 19.909 13.788 16.876 0.40 18.70 ? 188 GLY A C 1 ATOM 1334 C C B GLY A 1 155 ? 19.766 14.250 16.085 0.60 21.81 ? 188 GLY A C 1 ATOM 1335 O O A GLY A 1 155 ? 20.082 13.316 18.032 0.40 16.98 ? 188 GLY A O 1 ATOM 1336 O O B GLY A 1 155 ? 19.860 13.655 17.166 0.60 23.29 ? 188 GLY A O 1 ATOM 1337 N N A LYS A 1 156 ? 20.744 14.651 16.289 0.60 19.71 ? 189 LYS A N 1 ATOM 1338 N N B LYS A 1 156 ? 20.663 15.159 15.657 0.40 19.83 ? 189 LYS A N 1 ATOM 1339 C CA A LYS A 1 156 ? 21.867 15.255 16.984 0.60 20.27 ? 189 LYS A CA 1 ATOM 1340 C CA B LYS A 1 156 ? 21.862 15.602 16.451 0.40 19.06 ? 189 LYS A CA 1 ATOM 1341 C C A LYS A 1 156 ? 21.449 16.560 17.649 0.60 19.65 ? 189 LYS A C 1 ATOM 1342 C C B LYS A 1 156 ? 21.610 16.814 17.371 0.40 18.95 ? 189 LYS A C 1 ATOM 1343 O O A LYS A 1 156 ? 20.489 17.237 17.322 0.60 20.11 ? 189 LYS A O 1 ATOM 1344 O O B LYS A 1 156 ? 20.818 17.681 16.945 0.40 17.19 ? 189 LYS A O 1 ATOM 1345 C CB A LYS A 1 156 ? 23.006 15.599 16.010 0.60 21.10 ? 189 LYS A CB 1 ATOM 1346 C CB B LYS A 1 156 ? 23.024 16.005 15.523 0.40 18.37 ? 189 LYS A CB 1 ATOM 1347 C CG A LYS A 1 156 ? 23.502 14.419 15.157 0.60 19.86 ? 189 LYS A CG 1 ATOM 1348 C CG B LYS A 1 156 ? 23.427 14.960 14.446 0.40 19.07 ? 189 LYS A CG 1 ATOM 1349 C CD A LYS A 1 156 ? 24.027 13.245 15.969 0.60 17.96 ? 189 LYS A CD 1 ATOM 1350 C CD B LYS A 1 156 ? 23.889 13.641 15.068 0.40 17.84 ? 189 LYS A CD 1 ATOM 1351 C CE A LYS A 1 156 ? 24.635 12.177 15.013 0.60 19.10 ? 189 LYS A CE 1 ATOM 1352 C CE B LYS A 1 156 ? 24.544 12.706 14.064 0.40 18.84 ? 189 LYS A CE 1 ATOM 1353 N NZ A LYS A 1 156 ? 23.580 11.617 14.123 0.60 20.29 ? 189 LYS A NZ 1 ATOM 1354 N NZ B LYS A 1 156 ? 23.643 12.386 12.917 0.40 22.76 ? 189 LYS A NZ 1 ATOM 1355 N N . ILE A 1 157 ? 22.307 16.939 18.542 1.00 18.92 ? 190 ILE A N 1 ATOM 1356 C CA . ILE A 1 157 ? 22.352 18.277 19.174 1.00 18.25 ? 190 ILE A CA 1 ATOM 1357 C C . ILE A 1 157 ? 23.533 19.002 18.529 1.00 16.73 ? 190 ILE A C 1 ATOM 1358 O O . ILE A 1 157 ? 24.647 18.405 18.450 1.00 17.02 ? 190 ILE A O 1 ATOM 1359 C CB . ILE A 1 157 ? 22.552 18.150 20.662 1.00 18.93 ? 190 ILE A CB 1 ATOM 1360 C CG1 . ILE A 1 157 ? 21.276 17.446 21.239 1.00 22.79 ? 190 ILE A CG1 1 ATOM 1361 C CG2 . ILE A 1 157 ? 22.872 19.566 21.274 1.00 17.79 ? 190 ILE A CG2 1 ATOM 1362 C CD1 A ILE A 1 157 ? 20.246 18.254 21.753 0.60 25.48 ? 190 ILE A CD1 1 ATOM 1363 C CD1 B ILE A 1 157 ? 21.264 17.260 22.696 0.40 19.17 ? 190 ILE A CD1 1 ATOM 1364 N N . VAL A 1 158 ? 23.322 20.196 17.991 1.00 16.88 ? 191 VAL A N 1 ATOM 1365 C CA . VAL A 1 158 ? 24.441 20.914 17.379 1.00 15.86 ? 191 VAL A CA 1 ATOM 1366 C C . VAL A 1 158 ? 24.905 22.011 18.260 1.00 15.13 ? 191 VAL A C 1 ATOM 1367 O O . VAL A 1 158 ? 24.119 22.605 19.050 1.00 16.11 ? 191 VAL A O 1 ATOM 1368 C CB . VAL A 1 158 ? 24.070 21.445 15.961 1.00 15.80 ? 191 VAL A CB 1 ATOM 1369 C CG1 . VAL A 1 158 ? 23.688 20.238 15.034 1.00 18.43 ? 191 VAL A CG1 1 ATOM 1370 C CG2 . VAL A 1 158 ? 22.906 22.418 15.995 1.00 17.18 ? 191 VAL A CG2 1 ATOM 1371 N N . ILE A 1 159 ? 26.205 22.295 18.194 1.00 14.25 ? 192 ILE A N 1 ATOM 1372 C CA . ILE A 1 159 ? 26.779 23.454 18.874 1.00 14.39 ? 192 ILE A CA 1 ATOM 1373 C C . ILE A 1 159 ? 27.344 24.394 17.838 1.00 14.21 ? 192 ILE A C 1 ATOM 1374 O O . ILE A 1 159 ? 28.162 23.954 17.006 1.00 15.64 ? 192 ILE A O 1 ATOM 1375 C CB . ILE A 1 159 ? 27.804 23.022 20.010 1.00 14.56 ? 192 ILE A CB 1 ATOM 1376 C CG1 . ILE A 1 159 ? 28.332 24.258 20.732 1.00 13.65 ? 192 ILE A CG1 1 ATOM 1377 C CG2 . ILE A 1 159 ? 28.947 22.069 19.483 1.00 14.05 ? 192 ILE A CG2 1 ATOM 1378 C CD1 . ILE A 1 159 ? 29.099 23.972 22.054 1.00 16.55 ? 192 ILE A CD1 1 ATOM 1379 N N . ALA A 1 160 ? 26.958 25.646 17.977 1.00 15.26 ? 193 ALA A N 1 ATOM 1380 C CA . ALA A 1 160 ? 27.369 26.698 16.999 1.00 14.74 ? 193 ALA A CA 1 ATOM 1381 C C . ALA A 1 160 ? 27.925 27.860 17.701 1.00 16.10 ? 193 ALA A C 1 ATOM 1382 O O . ALA A 1 160 ? 27.401 28.273 18.741 1.00 16.18 ? 193 ALA A O 1 ATOM 1383 C CB . ALA A 1 160 ? 26.171 27.139 16.125 1.00 17.95 ? 193 ALA A CB 1 ATOM 1384 N N . ARG A 1 161 ? 28.957 28.473 17.133 1.00 16.36 ? 194 ARG A N 1 ATOM 1385 C CA . ARG A 1 161 ? 29.441 29.764 17.651 1.00 16.81 ? 194 ARG A CA 1 ATOM 1386 C C . ARG A 1 161 ? 28.608 30.934 17.126 1.00 17.66 ? 194 ARG A C 1 ATOM 1387 O O . ARG A 1 161 ? 28.181 30.910 15.957 1.00 17.54 ? 194 ARG A O 1 ATOM 1388 C CB . ARG A 1 161 ? 30.924 29.994 17.348 1.00 20.29 ? 194 ARG A CB 1 ATOM 1389 C CG . ARG A 1 161 ? 31.355 29.696 15.940 1.00 19.92 ? 194 ARG A CG 1 ATOM 1390 C CD . ARG A 1 161 ? 32.850 30.055 15.918 1.00 24.32 ? 194 ARG A CD 1 ATOM 1391 N NE . ARG A 1 161 ? 33.512 29.608 14.700 1.00 19.25 ? 194 ARG A NE 1 ATOM 1392 C CZ . ARG A 1 161 ? 34.710 30.076 14.359 1.00 19.09 ? 194 ARG A CZ 1 ATOM 1393 N NH1 . ARG A 1 161 ? 35.324 30.951 15.148 1.00 20.09 ? 194 ARG A NH1 1 ATOM 1394 N NH2 . ARG A 1 161 ? 35.271 29.614 13.254 1.00 21.73 ? 194 ARG A NH2 1 ATOM 1395 N N . TYR A 1 162 ? 28.403 31.904 18.006 1.00 17.71 ? 195 TYR A N 1 ATOM 1396 C CA . TYR A 1 162 ? 27.719 33.121 17.612 1.00 20.83 ? 195 TYR A CA 1 ATOM 1397 C C . TYR A 1 162 ? 28.588 33.857 16.544 1.00 23.26 ? 195 TYR A C 1 ATOM 1398 O O . TYR A 1 162 ? 29.815 33.656 16.502 1.00 22.57 ? 195 TYR A O 1 ATOM 1399 C CB . TYR A 1 162 ? 27.564 33.958 18.849 1.00 20.88 ? 195 TYR A CB 1 ATOM 1400 C CG . TYR A 1 162 ? 26.294 33.783 19.643 1.00 19.25 ? 195 TYR A CG 1 ATOM 1401 C CD1 . TYR A 1 162 ? 26.364 33.496 21.014 1.00 18.54 ? 195 TYR A CD1 1 ATOM 1402 C CD2 . TYR A 1 162 ? 25.080 34.068 19.099 1.00 20.04 ? 195 TYR A CD2 1 ATOM 1403 C CE1 . TYR A 1 162 ? 25.221 33.393 21.798 1.00 18.88 ? 195 TYR A CE1 1 ATOM 1404 C CE2 . TYR A 1 162 ? 23.903 34.045 19.909 1.00 21.04 ? 195 TYR A CE2 1 ATOM 1405 C CZ . TYR A 1 162 ? 23.995 33.712 21.223 1.00 21.04 ? 195 TYR A CZ 1 ATOM 1406 O OH . TYR A 1 162 ? 22.825 33.764 22.033 1.00 19.59 ? 195 TYR A OH 1 ATOM 1407 N N . GLY A 1 163 ? 27.908 34.625 15.694 1.00 24.04 ? 196 GLY A N 1 ATOM 1408 C CA . GLY A 1 163 ? 28.562 35.472 14.631 1.00 24.68 ? 196 GLY A CA 1 ATOM 1409 C C . GLY A 1 163 ? 28.122 35.198 13.244 1.00 24.51 ? 196 GLY A C 1 ATOM 1410 O O . GLY A 1 163 ? 27.487 34.171 12.932 1.00 24.83 ? 196 GLY A O 1 ATOM 1411 N N . LYS A 1 164 ? 28.494 36.151 12.359 1.00 27.69 ? 197 LYS A N 1 ATOM 1412 C CA . LYS A 1 164 ? 28.279 36.050 10.881 1.00 29.48 ? 197 LYS A CA 1 ATOM 1413 C C . LYS A 1 164 ? 26.838 36.149 10.380 1.00 30.48 ? 197 LYS A C 1 ATOM 1414 O O . LYS A 1 164 ? 26.579 36.687 9.283 1.00 30.91 ? 197 LYS A O 1 ATOM 1415 C CB . LYS A 1 164 ? 28.865 34.793 10.261 1.00 29.91 ? 197 LYS A CB 1 ATOM 1416 C CG . LYS A 1 164 ? 30.343 34.503 10.645 1.00 32.24 ? 197 LYS A CG 1 ATOM 1417 C CD . LYS A 1 164 ? 31.316 35.578 10.213 1.00 34.43 ? 197 LYS A CD 1 ATOM 1418 C CE . LYS A 1 164 ? 32.697 34.929 10.076 1.00 34.49 ? 197 LYS A CE 1 ATOM 1419 N NZ . LYS A 1 164 ? 33.699 36.028 9.864 1.00 39.93 ? 197 LYS A NZ 1 ATOM 1420 N N . ILE A 1 165 ? 25.895 35.547 11.104 1.00 28.65 ? 198 ILE A N 1 ATOM 1421 C CA . ILE A 1 165 ? 24.493 35.618 10.763 1.00 25.31 ? 198 ILE A CA 1 ATOM 1422 C C . ILE A 1 165 ? 23.672 35.803 12.036 1.00 27.05 ? 198 ILE A C 1 ATOM 1423 O O . ILE A 1 165 ? 24.139 35.571 13.157 1.00 25.94 ? 198 ILE A O 1 ATOM 1424 C CB . ILE A 1 165 ? 23.987 34.374 9.997 1.00 26.95 ? 198 ILE A CB 1 ATOM 1425 C CG1 . ILE A 1 165 ? 24.235 33.084 10.760 1.00 23.98 ? 198 ILE A CG1 1 ATOM 1426 C CG2 . ILE A 1 165 ? 24.656 34.243 8.569 1.00 26.76 ? 198 ILE A CG2 1 ATOM 1427 C CD1 . ILE A 1 165 ? 23.479 31.937 10.245 1.00 27.04 ? 198 ILE A CD1 1 ATOM 1428 N N . PHE A 1 166 ? 22.460 36.288 11.866 1.00 26.72 ? 199 PHE A N 1 ATOM 1429 C CA . PHE A 1 166 ? 21.626 36.556 13.026 1.00 26.49 ? 199 PHE A CA 1 ATOM 1430 C C . PHE A 1 166 ? 21.365 35.202 13.675 1.00 22.65 ? 199 PHE A C 1 ATOM 1431 O O . PHE A 1 166 ? 21.140 34.201 12.993 1.00 24.18 ? 199 PHE A O 1 ATOM 1432 C CB . PHE A 1 166 ? 20.348 37.251 12.513 1.00 26.58 ? 199 PHE A CB 1 ATOM 1433 C CG . PHE A 1 166 ? 19.196 37.269 13.516 1.00 27.43 ? 199 PHE A CG 1 ATOM 1434 C CD1 . PHE A 1 166 ? 19.313 37.968 14.703 1.00 28.47 ? 199 PHE A CD1 1 ATOM 1435 C CD2 . PHE A 1 166 ? 18.048 36.548 13.242 1.00 30.78 ? 199 PHE A CD2 1 ATOM 1436 C CE1 . PHE A 1 166 ? 18.226 37.943 15.652 1.00 29.31 ? 199 PHE A CE1 1 ATOM 1437 C CE2 . PHE A 1 166 ? 16.991 36.544 14.149 1.00 29.25 ? 199 PHE A CE2 1 ATOM 1438 C CZ . PHE A 1 166 ? 17.097 37.216 15.311 1.00 26.31 ? 199 PHE A CZ 1 ATOM 1439 N N . ARG A 1 167 ? 21.278 35.241 15.024 1.00 23.63 ? 200 ARG A N 1 ATOM 1440 C CA . ARG A 1 167 ? 21.140 33.963 15.745 1.00 21.66 ? 200 ARG A CA 1 ATOM 1441 C C . ARG A 1 167 ? 19.873 33.206 15.393 1.00 20.27 ? 200 ARG A C 1 ATOM 1442 O O . ARG A 1 167 ? 19.852 31.995 15.426 1.00 20.46 ? 200 ARG A O 1 ATOM 1443 C CB . ARG A 1 167 ? 21.269 34.176 17.278 1.00 20.50 ? 200 ARG A CB 1 ATOM 1444 C CG . ARG A 1 167 ? 20.069 34.919 17.903 1.00 20.96 ? 200 ARG A CG 1 ATOM 1445 C CD . ARG A 1 167 ? 20.305 35.143 19.427 1.00 22.37 ? 200 ARG A CD 1 ATOM 1446 N NE . ARG A 1 167 ? 21.176 36.291 19.727 1.00 23.24 ? 200 ARG A NE 1 ATOM 1447 C CZ . ARG A 1 167 ? 20.832 37.567 19.525 1.00 25.81 ? 200 ARG A CZ 1 ATOM 1448 N NH1 . ARG A 1 167 ? 19.589 37.849 19.073 1.00 21.90 ? 200 ARG A NH1 1 ATOM 1449 N NH2 . ARG A 1 167 ? 21.688 38.545 19.849 1.00 25.58 ? 200 ARG A NH2 1 ATOM 1450 N N . GLY A 1 168 ? 18.760 33.917 15.057 1.00 21.15 ? 201 GLY A N 1 ATOM 1451 C CA . GLY A 1 168 ? 17.575 33.232 14.620 1.00 21.90 ? 201 GLY A CA 1 ATOM 1452 C C . GLY A 1 168 ? 17.715 32.386 13.328 1.00 20.60 ? 201 GLY A C 1 ATOM 1453 O O . GLY A 1 168 ? 17.080 31.373 13.128 1.00 23.62 ? 201 GLY A O 1 ATOM 1454 N N . ASN A 1 169 ? 18.580 32.867 12.455 1.00 25.02 ? 202 ASN A N 1 ATOM 1455 C CA . ASN A 1 169 ? 18.856 32.110 11.244 1.00 26.25 ? 202 ASN A CA 1 ATOM 1456 C C . ASN A 1 169 ? 19.700 30.857 11.512 1.00 24.34 ? 202 ASN A C 1 ATOM 1457 O O . ASN A 1 169 ? 19.494 29.791 10.909 1.00 25.88 ? 202 ASN A O 1 ATOM 1458 C CB . ASN A 1 169 ? 19.604 32.999 10.267 1.00 28.17 ? 202 ASN A CB 1 ATOM 1459 C CG . ASN A 1 169 ? 18.681 33.996 9.592 1.00 30.95 ? 202 ASN A CG 1 ATOM 1460 O OD1 . ASN A 1 169 ? 18.819 35.182 9.782 1.00 40.83 ? 202 ASN A OD1 1 ATOM 1461 N ND2 . ASN A 1 169 ? 17.701 33.486 8.885 1.00 39.12 ? 202 ASN A ND2 1 ATOM 1462 N N . LYS A 1 170 ? 20.574 30.962 12.537 1.00 22.10 ? 203 LYS A N 1 ATOM 1463 C CA . LYS A 1 170 ? 21.285 29.724 12.937 1.00 20.84 ? 203 LYS A CA 1 ATOM 1464 C C . LYS A 1 170 ? 20.329 28.623 13.381 1.00 19.09 ? 203 LYS A C 1 ATOM 1465 O O . LYS A 1 170 ? 20.450 27.443 13.070 1.00 19.60 ? 203 LYS A O 1 ATOM 1466 C CB . LYS A 1 170 ? 22.230 30.015 14.121 1.00 18.62 ? 203 LYS A CB 1 ATOM 1467 C CG . LYS A 1 170 ? 23.309 31.011 13.809 1.00 18.02 ? 203 LYS A CG 1 ATOM 1468 C CD . LYS A 1 170 ? 24.113 31.382 15.092 1.00 19.96 ? 203 LYS A CD 1 ATOM 1469 C CE . LYS A 1 170 ? 25.021 32.570 14.906 1.00 18.91 ? 203 LYS A CE 1 ATOM 1470 N NZ . LYS A 1 170 ? 26.331 32.075 14.193 1.00 20.92 ? 203 LYS A NZ 1 ATOM 1471 N N . VAL A 1 171 ? 19.326 29.059 14.159 1.00 18.53 ? 204 VAL A N 1 ATOM 1472 C CA . VAL A 1 171 ? 18.368 28.083 14.646 1.00 20.18 ? 204 VAL A CA 1 ATOM 1473 C C . VAL A 1 171 ? 17.493 27.498 13.514 1.00 20.72 ? 204 VAL A C 1 ATOM 1474 O O . VAL A 1 171 ? 17.232 26.312 13.484 1.00 22.93 ? 204 VAL A O 1 ATOM 1475 C CB . VAL A 1 171 ? 17.469 28.796 15.714 1.00 19.77 ? 204 VAL A CB 1 ATOM 1476 C CG1 . VAL A 1 171 ? 16.398 27.874 16.167 1.00 20.47 ? 204 VAL A CG1 1 ATOM 1477 C CG2 . VAL A 1 171 ? 18.357 29.269 16.908 1.00 19.51 ? 204 VAL A CG2 1 ATOM 1478 N N . LYS A 1 172 ? 17.042 28.407 12.632 1.00 23.09 ? 205 LYS A N 1 ATOM 1479 C CA . LYS A 1 172 ? 16.233 27.922 11.491 1.00 25.13 ? 205 LYS A CA 1 ATOM 1480 C C . LYS A 1 172 ? 17.037 26.924 10.628 1.00 23.73 ? 205 LYS A C 1 ATOM 1481 O O . LYS A 1 172 ? 16.536 25.850 10.233 1.00 25.61 ? 205 LYS A O 1 ATOM 1482 C CB . LYS A 1 172 ? 15.826 29.096 10.650 1.00 26.49 ? 205 LYS A CB 1 ATOM 1483 C CG . LYS A 1 172 ? 14.854 28.670 9.493 1.00 32.20 ? 205 LYS A CG 1 ATOM 1484 C CD . LYS A 1 172 ? 14.795 29.789 8.473 1.00 41.79 ? 205 LYS A CD 1 ATOM 1485 C CE . LYS A 1 172 ? 13.877 29.378 7.312 1.00 47.24 ? 205 LYS A CE 1 ATOM 1486 N NZ . LYS A 1 172 ? 14.415 29.928 6.049 1.00 50.74 ? 205 LYS A NZ 1 ATOM 1487 N N . ASN A 1 173 ? 18.301 27.278 10.448 1.00 23.78 ? 206 ASN A N 1 ATOM 1488 C CA . ASN A 1 173 ? 19.210 26.370 9.702 1.00 24.44 ? 206 ASN A CA 1 ATOM 1489 C C . ASN A 1 173 ? 19.397 25.029 10.371 1.00 25.04 ? 206 ASN A C 1 ATOM 1490 O O . ASN A 1 173 ? 19.372 23.989 9.742 1.00 25.17 ? 206 ASN A O 1 ATOM 1491 C CB . ASN A 1 173 ? 20.547 27.021 9.441 1.00 23.45 ? 206 ASN A CB 1 ATOM 1492 C CG . ASN A 1 173 ? 20.449 28.223 8.546 1.00 27.36 ? 206 ASN A CG 1 ATOM 1493 O OD1 . ASN A 1 173 ? 19.381 28.429 7.909 1.00 29.92 ? 206 ASN A OD1 1 ATOM 1494 N ND2 . ASN A 1 173 ? 21.453 29.069 8.551 1.00 25.31 ? 206 ASN A ND2 1 ATOM 1495 N N . ALA A 1 174 ? 19.536 25.010 11.708 1.00 23.08 ? 207 ALA A N 1 ATOM 1496 C CA . ALA A 1 174 ? 19.676 23.765 12.368 1.00 21.98 ? 207 ALA A CA 1 ATOM 1497 C C . ALA A 1 174 ? 18.410 22.924 12.305 1.00 22.72 ? 207 ALA A C 1 ATOM 1498 O O . ALA A 1 174 ? 18.429 21.698 12.233 1.00 23.77 ? 207 ALA A O 1 ATOM 1499 C CB . ALA A 1 174 ? 20.080 24.027 13.893 1.00 22.84 ? 207 ALA A CB 1 ATOM 1500 N N . MET A 1 175 ? 17.248 23.618 12.386 1.00 23.49 ? 208 MET A N 1 ATOM 1501 C CA . MET A 1 175 ? 15.978 22.931 12.286 1.00 25.59 ? 208 MET A CA 1 ATOM 1502 C C . MET A 1 175 ? 15.913 22.237 10.911 1.00 25.72 ? 208 MET A C 1 ATOM 1503 O O . MET A 1 175 ? 15.514 21.087 10.830 1.00 26.89 ? 208 MET A O 1 ATOM 1504 C CB . MET A 1 175 ? 14.822 23.957 12.394 1.00 25.94 ? 208 MET A CB 1 ATOM 1505 C CG . MET A 1 175 ? 14.575 24.450 13.823 1.00 26.48 ? 208 MET A CG 1 ATOM 1506 S SD . MET A 1 175 ? 13.361 25.812 13.994 1.00 28.02 ? 208 MET A SD 1 ATOM 1507 C CE . MET A 1 175 ? 11.981 25.335 12.945 1.00 36.40 ? 208 MET A CE 1 ATOM 1508 N N . LEU A 1 176 ? 16.288 22.980 9.893 1.00 27.52 ? 209 LEU A N 1 ATOM 1509 C CA . LEU A 1 176 ? 16.195 22.410 8.511 1.00 29.46 ? 209 LEU A CA 1 ATOM 1510 C C . LEU A 1 176 ? 17.038 21.152 8.395 1.00 30.13 ? 209 LEU A C 1 ATOM 1511 O O . LEU A 1 176 ? 16.682 20.189 7.690 1.00 29.69 ? 209 LEU A O 1 ATOM 1512 C CB . LEU A 1 176 ? 16.608 23.445 7.500 1.00 29.67 ? 209 LEU A CB 1 ATOM 1513 C CG . LEU A 1 176 ? 15.582 24.572 7.289 1.00 35.26 ? 209 LEU A CG 1 ATOM 1514 C CD1 . LEU A 1 176 ? 16.208 25.775 6.558 1.00 37.30 ? 209 LEU A CD1 1 ATOM 1515 C CD2 . LEU A 1 176 ? 14.322 24.059 6.517 1.00 38.68 ? 209 LEU A CD2 1 ATOM 1516 N N . ALA A 1 177 ? 18.101 21.091 9.198 1.00 28.70 ? 210 ALA A N 1 ATOM 1517 C CA . ALA A 1 177 ? 19.044 19.960 9.161 1.00 26.84 ? 210 ALA A CA 1 ATOM 1518 C C . ALA A 1 177 ? 18.668 18.737 9.998 1.00 26.43 ? 210 ALA A C 1 ATOM 1519 O O . ALA A 1 177 ? 19.370 17.714 9.998 1.00 26.12 ? 210 ALA A O 1 ATOM 1520 C CB . ALA A 1 177 ? 20.437 20.516 9.506 1.00 26.86 ? 210 ALA A CB 1 ATOM 1521 N N . GLY A 1 178 ? 17.567 18.801 10.738 1.00 23.67 ? 211 GLY A N 1 ATOM 1522 C CA . GLY A 1 178 ? 17.078 17.683 11.480 1.00 25.19 ? 211 GLY A CA 1 ATOM 1523 C C . GLY A 1 178 ? 17.665 17.657 12.881 1.00 21.34 ? 211 GLY A C 1 ATOM 1524 O O . GLY A 1 178 ? 17.389 16.748 13.638 1.00 25.19 ? 211 GLY A O 1 ATOM 1525 N N . ALA A 1 179 ? 18.346 18.754 13.242 1.00 23.90 ? 212 ALA A N 1 ATOM 1526 C CA . ALA A 1 179 ? 18.891 18.783 14.601 1.00 22.89 ? 212 ALA A CA 1 ATOM 1527 C C . ALA A 1 179 ? 17.748 18.853 15.591 1.00 21.49 ? 212 ALA A C 1 ATOM 1528 O O . ALA A 1 179 ? 16.685 19.470 15.315 1.00 22.33 ? 212 ALA A O 1 ATOM 1529 C CB . ALA A 1 179 ? 19.791 19.997 14.793 1.00 22.50 ? 212 ALA A CB 1 ATOM 1530 N N . ILE A 1 180 ? 17.961 18.314 16.765 1.00 20.04 ? 213 ILE A N 1 ATOM 1531 C CA . ILE A 1 180 ? 16.905 18.343 17.791 1.00 19.74 ? 213 ILE A CA 1 ATOM 1532 C C . ILE A 1 180 ? 17.125 19.339 18.909 1.00 18.26 ? 213 ILE A C 1 ATOM 1533 O O . ILE A 1 180 ? 16.278 19.501 19.800 1.00 19.30 ? 213 ILE A O 1 ATOM 1534 C CB . ILE A 1 180 ? 16.646 16.935 18.387 1.00 20.16 ? 213 ILE A CB 1 ATOM 1535 C CG1 . ILE A 1 180 ? 17.927 16.326 19.000 1.00 20.99 ? 213 ILE A CG1 1 ATOM 1536 C CG2 . ILE A 1 180 ? 16.141 15.990 17.272 1.00 22.61 ? 213 ILE A CG2 1 ATOM 1537 C CD1 . ILE A 1 180 ? 17.694 15.068 19.880 1.00 24.49 ? 213 ILE A CD1 1 ATOM 1538 N N . GLY A 1 181 ? 18.258 20.059 18.828 1.00 18.31 ? 214 GLY A N 1 ATOM 1539 C CA . GLY A 1 181 ? 18.520 21.201 19.732 1.00 17.71 ? 214 GLY A CA 1 ATOM 1540 C C . GLY A 1 181 ? 19.736 21.908 19.192 1.00 15.06 ? 214 GLY A C 1 ATOM 1541 O O . GLY A 1 181 ? 20.560 21.278 18.510 1.00 17.48 ? 214 GLY A O 1 ATOM 1542 N N . ILE A 1 182 ? 19.904 23.159 19.612 1.00 15.50 ? 215 ILE A N 1 ATOM 1543 C CA . ILE A 1 182 ? 21.130 23.898 19.275 1.00 15.71 ? 215 ILE A CA 1 ATOM 1544 C C . ILE A 1 182 ? 21.619 24.686 20.493 1.00 15.26 ? 215 ILE A C 1 ATOM 1545 O O . ILE A 1 182 ? 20.853 25.430 21.123 1.00 14.40 ? 215 ILE A O 1 ATOM 1546 C CB . ILE A 1 182 ? 20.926 24.799 18.004 1.00 15.95 ? 215 ILE A CB 1 ATOM 1547 C CG1 . ILE A 1 182 ? 22.128 25.706 17.788 1.00 17.13 ? 215 ILE A CG1 1 ATOM 1548 C CG2 . ILE A 1 182 ? 19.675 25.664 18.135 1.00 16.96 ? 215 ILE A CG2 1 ATOM 1549 C CD1 . ILE A 1 182 ? 22.155 26.416 16.391 1.00 17.71 ? 215 ILE A CD1 1 ATOM 1550 N N . ILE A 1 183 ? 22.911 24.477 20.784 1.00 14.33 ? 216 ILE A N 1 ATOM 1551 C CA . ILE A 1 183 ? 23.650 25.239 21.788 1.00 14.22 ? 216 ILE A CA 1 ATOM 1552 C C . ILE A 1 183 ? 24.418 26.365 21.081 1.00 15.83 ? 216 ILE A C 1 ATOM 1553 O O . ILE A 1 183 ? 25.140 26.081 20.105 1.00 16.10 ? 216 ILE A O 1 ATOM 1554 C CB . ILE A 1 183 ? 24.616 24.287 22.495 1.00 14.13 ? 216 ILE A CB 1 ATOM 1555 C CG1 . ILE A 1 183 ? 23.848 23.132 23.191 1.00 15.51 ? 216 ILE A CG1 1 ATOM 1556 C CG2 . ILE A 1 183 ? 25.473 25.061 23.458 1.00 15.54 ? 216 ILE A CG2 1 ATOM 1557 C CD1 . ILE A 1 183 ? 24.742 21.971 23.630 1.00 16.97 ? 216 ILE A CD1 1 ATOM 1558 N N . LEU A 1 184 ? 24.255 27.604 21.540 1.00 14.84 ? 217 LEU A N 1 ATOM 1559 C CA . LEU A 1 184 ? 24.996 28.765 21.000 1.00 15.24 ? 217 LEU A CA 1 ATOM 1560 C C . LEU A 1 184 ? 26.030 29.171 21.967 1.00 15.98 ? 217 LEU A C 1 ATOM 1561 O O . LEU A 1 184 ? 25.767 29.132 23.215 1.00 15.91 ? 217 LEU A O 1 ATOM 1562 C CB . LEU A 1 184 ? 24.051 29.959 20.760 1.00 14.88 ? 217 LEU A CB 1 ATOM 1563 C CG . LEU A 1 184 ? 22.917 29.601 19.805 1.00 15.10 ? 217 LEU A CG 1 ATOM 1564 C CD1 . LEU A 1 184 ? 21.915 30.748 19.773 1.00 16.95 ? 217 LEU A CD1 1 ATOM 1565 C CD2 . LEU A 1 184 ? 23.462 29.396 18.378 1.00 18.77 ? 217 LEU A CD2 1 ATOM 1566 N N . TYR A 1 185 ? 27.233 29.541 21.531 1.00 14.93 ? 218 TYR A N 1 ATOM 1567 C CA . TYR A 1 185 ? 28.248 30.054 22.482 1.00 14.46 ? 218 TYR A CA 1 ATOM 1568 C C . TYR A 1 185 ? 29.118 31.087 21.827 1.00 16.43 ? 218 TYR A C 1 ATOM 1569 O O . TYR A 1 185 ? 29.107 31.206 20.607 1.00 17.19 ? 218 TYR A O 1 ATOM 1570 C CB . TYR A 1 185 ? 29.114 28.877 22.993 1.00 15.30 ? 218 TYR A CB 1 ATOM 1571 C CG . TYR A 1 185 ? 30.238 28.454 22.020 1.00 14.66 ? 218 TYR A CG 1 ATOM 1572 C CD1 . TYR A 1 185 ? 31.540 28.952 22.152 1.00 16.30 ? 218 TYR A CD1 1 ATOM 1573 C CD2 . TYR A 1 185 ? 29.942 27.640 20.934 1.00 16.10 ? 218 TYR A CD2 1 ATOM 1574 C CE1 . TYR A 1 185 ? 32.545 28.592 21.190 1.00 15.40 ? 218 TYR A CE1 1 ATOM 1575 C CE2 . TYR A 1 185 ? 30.959 27.280 19.978 1.00 15.40 ? 218 TYR A CE2 1 ATOM 1576 C CZ . TYR A 1 185 ? 32.212 27.806 20.143 1.00 15.50 ? 218 TYR A CZ 1 ATOM 1577 O OH . TYR A 1 185 ? 33.200 27.499 19.205 1.00 16.37 ? 218 TYR A OH 1 ATOM 1578 N N . SER A 1 186 ? 29.740 31.887 22.673 1.00 17.50 ? 219 SER A N 1 ATOM 1579 C CA . SER A 1 186 ? 30.589 32.997 22.210 1.00 18.64 ? 219 SER A CA 1 ATOM 1580 C C . SER A 1 186 ? 32.055 32.531 22.131 1.00 19.66 ? 219 SER A C 1 ATOM 1581 O O . SER A 1 186 ? 32.675 32.331 23.168 1.00 19.47 ? 219 SER A O 1 ATOM 1582 C CB . SER A 1 186 ? 30.495 34.090 23.269 1.00 20.05 ? 219 SER A CB 1 ATOM 1583 O OG . SER A 1 186 ? 29.116 34.467 23.468 1.00 23.83 ? 219 SER A OG 1 ATOM 1584 N N . ASP A 1 187 ? 32.552 32.316 20.915 1.00 18.99 ? 220 ASP A N 1 ATOM 1585 C CA . ASP A 1 187 ? 33.990 31.905 20.802 1.00 19.87 ? 220 ASP A CA 1 ATOM 1586 C C . ASP A 1 187 ? 34.916 33.144 20.991 1.00 21.23 ? 220 ASP A C 1 ATOM 1587 O O . ASP A 1 187 ? 34.625 34.195 20.382 1.00 22.70 ? 220 ASP A O 1 ATOM 1588 C CB . ASP A 1 187 ? 34.215 31.256 19.444 1.00 19.05 ? 220 ASP A CB 1 ATOM 1589 C CG . ASP A 1 187 ? 35.461 30.382 19.435 1.00 21.19 ? 220 ASP A CG 1 ATOM 1590 O OD1 . ASP A 1 187 ? 35.308 29.125 19.381 1.00 20.31 ? 220 ASP A OD1 1 ATOM 1591 O OD2 . ASP A 1 187 ? 36.577 30.929 19.561 1.00 19.14 ? 220 ASP A OD2 1 ATOM 1592 N N . PRO A 1 188 ? 35.989 33.024 21.780 1.00 21.70 ? 221 PRO A N 1 ATOM 1593 C CA . PRO A 1 188 ? 36.911 34.179 21.870 1.00 22.14 ? 221 PRO A CA 1 ATOM 1594 C C . PRO A 1 188 ? 37.466 34.617 20.504 1.00 24.93 ? 221 PRO A C 1 ATOM 1595 O O . PRO A 1 188 ? 37.874 35.783 20.383 1.00 25.61 ? 221 PRO A O 1 ATOM 1596 C CB . PRO A 1 188 ? 38.052 33.649 22.740 1.00 23.28 ? 221 PRO A CB 1 ATOM 1597 C CG . PRO A 1 188 ? 37.426 32.623 23.604 1.00 24.89 ? 221 PRO A CG 1 ATOM 1598 C CD . PRO A 1 188 ? 36.386 31.957 22.714 1.00 19.90 ? 221 PRO A CD 1 ATOM 1599 N N . ALA A 1 189 ? 37.467 33.740 19.483 1.00 24.40 ? 222 ALA A N 1 ATOM 1600 C CA . ALA A 1 189 ? 37.913 34.120 18.152 1.00 24.78 ? 222 ALA A CA 1 ATOM 1601 C C . ALA A 1 189 ? 37.076 35.297 17.675 1.00 27.57 ? 222 ALA A C 1 ATOM 1602 O O . ALA A 1 189 ? 37.580 36.192 16.991 1.00 28.84 ? 222 ALA A O 1 ATOM 1603 C CB . ALA A 1 189 ? 37.821 32.997 17.169 1.00 24.48 ? 222 ALA A CB 1 ATOM 1604 N N . ASP A 1 190 ? 35.809 35.289 18.061 1.00 26.28 ? 223 ASP A N 1 ATOM 1605 C CA . ASP A 1 190 ? 34.862 36.272 17.526 1.00 28.37 ? 223 ASP A CA 1 ATOM 1606 C C . ASP A 1 190 ? 34.512 37.381 18.476 1.00 29.39 ? 223 ASP A C 1 ATOM 1607 O O . ASP A 1 190 ? 34.047 38.450 17.988 1.00 30.65 ? 223 ASP A O 1 ATOM 1608 C CB . ASP A 1 190 ? 33.601 35.531 17.116 1.00 27.54 ? 223 ASP A CB 1 ATOM 1609 C CG . ASP A 1 190 ? 33.904 34.432 16.137 1.00 26.75 ? 223 ASP A CG 1 ATOM 1610 O OD1 . ASP A 1 190 ? 34.151 34.699 14.946 1.00 28.94 ? 223 ASP A OD1 1 ATOM 1611 O OD2 . ASP A 1 190 ? 33.825 33.228 16.486 1.00 23.74 ? 223 ASP A OD2 1 ATOM 1612 N N . TYR A 1 191 ? 34.660 37.170 19.786 1.00 28.20 ? 224 TYR A N 1 ATOM 1613 C CA . TYR A 1 191 ? 34.190 38.130 20.781 1.00 30.11 ? 224 TYR A CA 1 ATOM 1614 C C . TYR A 1 191 ? 35.254 38.510 21.795 1.00 31.21 ? 224 TYR A C 1 ATOM 1615 O O . TYR A 1 191 ? 34.961 39.076 22.846 1.00 32.74 ? 224 TYR A O 1 ATOM 1616 C CB . TYR A 1 191 ? 32.959 37.581 21.518 1.00 30.32 ? 224 TYR A CB 1 ATOM 1617 C CG . TYR A 1 191 ? 31.765 37.502 20.620 1.00 29.95 ? 224 TYR A CG 1 ATOM 1618 C CD1 . TYR A 1 191 ? 31.481 36.323 19.921 1.00 26.98 ? 224 TYR A CD1 1 ATOM 1619 C CD2 . TYR A 1 191 ? 30.872 38.597 20.492 1.00 30.29 ? 224 TYR A CD2 1 ATOM 1620 C CE1 . TYR A 1 191 ? 30.434 36.240 19.042 1.00 23.61 ? 224 TYR A CE1 1 ATOM 1621 C CE2 . TYR A 1 191 ? 29.809 38.527 19.656 1.00 30.33 ? 224 TYR A CE2 1 ATOM 1622 C CZ . TYR A 1 191 ? 29.533 37.353 18.963 1.00 26.65 ? 224 TYR A CZ 1 ATOM 1623 O OH . TYR A 1 191 ? 28.471 37.266 18.078 1.00 28.72 ? 224 TYR A OH 1 ATOM 1624 N N . PHE A 1 192 ? 36.505 38.119 21.560 1.00 29.00 ? 225 PHE A N 1 ATOM 1625 C CA . PHE A 1 192 ? 37.525 38.491 22.508 1.00 28.86 ? 225 PHE A CA 1 ATOM 1626 C C . PHE A 1 192 ? 38.569 39.312 21.742 1.00 29.66 ? 225 PHE A C 1 ATOM 1627 O O . PHE A 1 192 ? 39.216 38.803 20.806 1.00 29.86 ? 225 PHE A O 1 ATOM 1628 C CB . PHE A 1 192 ? 38.163 37.229 23.122 1.00 28.63 ? 225 PHE A CB 1 ATOM 1629 C CG . PHE A 1 192 ? 39.016 37.481 24.326 1.00 26.92 ? 225 PHE A CG 1 ATOM 1630 C CD1 . PHE A 1 192 ? 38.461 37.492 25.602 1.00 26.62 ? 225 PHE A CD1 1 ATOM 1631 C CD2 . PHE A 1 192 ? 40.402 37.599 24.194 1.00 24.74 ? 225 PHE A CD2 1 ATOM 1632 C CE1 . PHE A 1 192 ? 39.245 37.697 26.739 1.00 25.33 ? 225 PHE A CE1 1 ATOM 1633 C CE2 . PHE A 1 192 ? 41.200 37.808 25.314 1.00 22.31 ? 225 PHE A CE2 1 ATOM 1634 C CZ . PHE A 1 192 ? 40.643 37.860 26.603 1.00 25.85 ? 225 PHE A CZ 1 ATOM 1635 N N . ALA A 1 193 ? 38.727 40.580 22.139 1.00 28.74 ? 226 ALA A N 1 ATOM 1636 C CA . ALA A 1 193 ? 39.644 41.462 21.449 1.00 28.39 ? 226 ALA A CA 1 ATOM 1637 C C . ALA A 1 193 ? 41.083 41.161 21.872 1.00 29.30 ? 226 ALA A C 1 ATOM 1638 O O . ALA A 1 193 ? 41.356 40.924 23.050 1.00 28.10 ? 226 ALA A O 1 ATOM 1639 C CB . ALA A 1 193 ? 39.271 42.929 21.722 1.00 29.02 ? 226 ALA A CB 1 ATOM 1640 N N . PRO A 1 194 ? 42.021 41.170 20.910 1.00 30.83 ? 227 PRO A N 1 ATOM 1641 C CA . PRO A 1 194 ? 43.415 40.841 21.258 1.00 32.91 ? 227 PRO A CA 1 ATOM 1642 C C . PRO A 1 194 ? 44.010 41.842 22.241 1.00 33.69 ? 227 PRO A C 1 ATOM 1643 O O . PRO A 1 194 ? 43.765 43.052 22.119 1.00 34.63 ? 227 PRO A O 1 ATOM 1644 C CB . PRO A 1 194 ? 44.162 40.914 19.921 1.00 32.91 ? 227 PRO A CB 1 ATOM 1645 C CG . PRO A 1 194 ? 43.306 41.701 19.021 1.00 32.98 ? 227 PRO A CG 1 ATOM 1646 C CD . PRO A 1 194 ? 41.865 41.509 19.485 1.00 31.62 ? 227 PRO A CD 1 ATOM 1647 N N . GLU A 1 195 ? 44.748 41.303 23.208 1.00 34.74 ? 228 GLU A N 1 ATOM 1648 C CA . GLU A 1 195 ? 45.413 42.017 24.305 1.00 35.33 ? 228 GLU A CA 1 ATOM 1649 C C . GLU A 1 195 ? 44.573 43.006 25.088 1.00 34.18 ? 228 GLU A C 1 ATOM 1650 O O . GLU A 1 195 ? 45.049 44.075 25.496 1.00 33.89 ? 228 GLU A O 1 ATOM 1651 C CB . GLU A 1 195 ? 46.768 42.633 23.929 1.00 36.91 ? 228 GLU A CB 1 ATOM 1652 C CG . GLU A 1 195 ? 46.806 43.333 22.622 1.00 42.33 ? 228 GLU A CG 1 ATOM 1653 C CD . GLU A 1 195 ? 47.598 42.549 21.604 1.00 49.61 ? 228 GLU A CD 1 ATOM 1654 O OE1 . GLU A 1 195 ? 47.143 42.455 20.432 1.00 53.28 ? 228 GLU A OE1 1 ATOM 1655 O OE2 . GLU A 1 195 ? 48.682 42.031 21.978 1.00 51.37 ? 228 GLU A OE2 1 ATOM 1656 N N . VAL A 1 196 ? 43.329 42.636 25.340 1.00 31.14 ? 229 VAL A N 1 ATOM 1657 C CA . VAL A 1 196 ? 42.605 43.372 26.337 1.00 29.52 ? 229 VAL A CA 1 ATOM 1658 C C . VAL A 1 196 ? 42.092 42.446 27.405 1.00 28.27 ? 229 VAL A C 1 ATOM 1659 O O . VAL A 1 196 ? 41.758 41.287 27.116 1.00 28.76 ? 229 VAL A O 1 ATOM 1660 C CB . VAL A 1 196 ? 41.574 44.405 25.711 1.00 30.15 ? 229 VAL A CB 1 ATOM 1661 C CG1 . VAL A 1 196 ? 41.659 44.534 24.227 1.00 30.44 ? 229 VAL A CG1 1 ATOM 1662 C CG2 . VAL A 1 196 ? 40.220 44.291 26.276 1.00 29.45 ? 229 VAL A CG2 1 ATOM 1663 N N . GLN A 1 197 ? 42.055 42.932 28.636 1.00 27.03 ? 230 GLN A N 1 ATOM 1664 C CA . GLN A 1 197 ? 41.673 42.115 29.770 1.00 27.74 ? 230 GLN A CA 1 ATOM 1665 C C . GLN A 1 197 ? 40.136 41.925 29.813 1.00 26.74 ? 230 GLN A C 1 ATOM 1666 O O . GLN A 1 197 ? 39.396 42.825 29.381 1.00 25.59 ? 230 GLN A O 1 ATOM 1667 C CB . GLN A 1 197 ? 42.153 42.772 31.064 1.00 28.67 ? 230 GLN A CB 1 ATOM 1668 C CG . GLN A 1 197 ? 43.680 42.975 31.127 1.00 32.36 ? 230 GLN A CG 1 ATOM 1669 C CD . GLN A 1 197 ? 44.096 43.706 32.398 1.00 38.40 ? 230 GLN A CD 1 ATOM 1670 O OE1 . GLN A 1 197 ? 44.367 43.079 33.420 1.00 43.44 ? 230 GLN A OE1 1 ATOM 1671 N NE2 . GLN A 1 197 ? 44.108 45.043 32.349 1.00 42.46 ? 230 GLN A NE2 1 ATOM 1672 N N . PRO A 1 198 ? 39.658 40.784 30.363 1.00 26.87 ? 231 PRO A N 1 ATOM 1673 C CA . PRO A 1 198 ? 38.203 40.608 30.591 1.00 26.55 ? 231 PRO A CA 1 ATOM 1674 C C . PRO A 1 198 ? 37.677 41.559 31.677 1.00 26.89 ? 231 PRO A C 1 ATOM 1675 O O . PRO A 1 198 ? 38.413 41.978 32.598 1.00 26.49 ? 231 PRO A O 1 ATOM 1676 C CB . PRO A 1 198 ? 38.074 39.144 31.035 1.00 26.24 ? 231 PRO A CB 1 ATOM 1677 C CG . PRO A 1 198 ? 39.449 38.823 31.622 1.00 28.91 ? 231 PRO A CG 1 ATOM 1678 C CD . PRO A 1 198 ? 40.437 39.586 30.770 1.00 27.36 ? 231 PRO A CD 1 ATOM 1679 N N . TYR A 1 199 ? 36.423 41.961 31.520 1.00 25.85 ? 232 TYR A N 1 ATOM 1680 C CA . TYR A 1 199 ? 35.729 42.757 32.520 1.00 26.45 ? 232 TYR A CA 1 ATOM 1681 C C . TYR A 1 199 ? 35.930 42.052 33.869 1.00 27.46 ? 232 TYR A C 1 ATOM 1682 O O . TYR A 1 199 ? 35.840 40.817 33.916 1.00 29.33 ? 232 TYR A O 1 ATOM 1683 C CB . TYR A 1 199 ? 34.229 42.810 32.124 1.00 25.30 ? 232 TYR A CB 1 ATOM 1684 C CG . TYR A 1 199 ? 33.474 43.846 32.945 1.00 24.69 ? 232 TYR A CG 1 ATOM 1685 C CD1 . TYR A 1 199 ? 33.247 45.101 32.434 1.00 25.80 ? 232 TYR A CD1 1 ATOM 1686 C CD2 . TYR A 1 199 ? 33.019 43.568 34.229 1.00 25.05 ? 232 TYR A CD2 1 ATOM 1687 C CE1 . TYR A 1 199 ? 32.555 46.069 33.171 1.00 23.86 ? 232 TYR A CE1 1 ATOM 1688 C CE2 . TYR A 1 199 ? 32.330 44.549 35.015 1.00 26.33 ? 232 TYR A CE2 1 ATOM 1689 C CZ . TYR A 1 199 ? 32.095 45.792 34.439 1.00 25.28 ? 232 TYR A CZ 1 ATOM 1690 O OH . TYR A 1 199 ? 31.428 46.788 35.149 1.00 24.08 ? 232 TYR A OH 1 ATOM 1691 N N . PRO A 1 200 ? 36.207 42.792 34.974 1.00 27.84 ? 233 PRO A N 1 ATOM 1692 C CA . PRO A 1 200 ? 36.138 44.255 35.128 1.00 27.88 ? 233 PRO A CA 1 ATOM 1693 C C . PRO A 1 200 ? 37.443 45.006 34.850 1.00 27.15 ? 233 PRO A C 1 ATOM 1694 O O . PRO A 1 200 ? 37.429 46.247 34.791 1.00 26.14 ? 233 PRO A O 1 ATOM 1695 C CB . PRO A 1 200 ? 35.737 44.425 36.584 1.00 28.28 ? 233 PRO A CB 1 ATOM 1696 C CG . PRO A 1 200 ? 36.474 43.301 37.289 1.00 28.11 ? 233 PRO A CG 1 ATOM 1697 C CD . PRO A 1 200 ? 36.356 42.129 36.285 1.00 28.10 ? 233 PRO A CD 1 ATOM 1698 N N . LYS A 1 201 ? 38.522 44.267 34.618 1.00 26.35 ? 234 LYS A N 1 ATOM 1699 C CA . LYS A 1 201 ? 39.829 44.902 34.410 1.00 27.43 ? 234 LYS A CA 1 ATOM 1700 C C . LYS A 1 201 ? 39.950 45.554 33.032 1.00 26.86 ? 234 LYS A C 1 ATOM 1701 O O . LYS A 1 201 ? 40.655 46.552 32.858 1.00 25.87 ? 234 LYS A O 1 ATOM 1702 C CB . LYS A 1 201 ? 40.962 43.917 34.685 1.00 28.88 ? 234 LYS A CB 1 ATOM 1703 C CG . LYS A 1 201 ? 41.030 43.499 36.145 1.00 32.72 ? 234 LYS A CG 1 ATOM 1704 C CD . LYS A 1 201 ? 42.427 43.084 36.580 1.00 40.01 ? 234 LYS A CD 1 ATOM 1705 C CE . LYS A 1 201 ? 42.728 41.607 36.267 1.00 44.16 ? 234 LYS A CE 1 ATOM 1706 N NZ . LYS A 1 201 ? 43.881 41.088 37.110 1.00 47.17 ? 234 LYS A NZ 1 ATOM 1707 N N . GLY A 1 202 ? 39.245 44.993 32.045 1.00 25.74 ? 235 GLY A N 1 ATOM 1708 C CA . GLY A 1 202 ? 39.205 45.574 30.705 1.00 23.43 ? 235 GLY A CA 1 ATOM 1709 C C . GLY A 1 202 ? 37.801 45.343 30.149 1.00 22.70 ? 235 GLY A C 1 ATOM 1710 O O . GLY A 1 202 ? 36.877 44.990 30.894 1.00 23.35 ? 235 GLY A O 1 ATOM 1711 N N . TRP A 1 203 ? 37.669 45.560 28.860 1.00 21.44 ? 236 TRP A N 1 ATOM 1712 C CA . TRP A 1 203 ? 36.342 45.546 28.240 1.00 22.01 ? 236 TRP A CA 1 ATOM 1713 C C . TRP A 1 203 ? 36.058 44.240 27.504 1.00 22.53 ? 236 TRP A C 1 ATOM 1714 O O . TRP A 1 203 ? 35.112 44.137 26.746 1.00 21.93 ? 236 TRP A O 1 ATOM 1715 C CB . TRP A 1 203 ? 36.153 46.747 27.324 1.00 21.72 ? 236 TRP A CB 1 ATOM 1716 C CG . TRP A 1 203 ? 37.288 47.048 26.393 1.00 22.39 ? 236 TRP A CG 1 ATOM 1717 C CD1 . TRP A 1 203 ? 38.417 47.786 26.685 1.00 24.64 ? 236 TRP A CD1 1 ATOM 1718 C CD2 . TRP A 1 203 ? 37.395 46.695 25.012 1.00 20.37 ? 236 TRP A CD2 1 ATOM 1719 N NE1 . TRP A 1 203 ? 39.219 47.873 25.577 1.00 24.63 ? 236 TRP A NE1 1 ATOM 1720 C CE2 . TRP A 1 203 ? 38.628 47.213 24.537 1.00 22.66 ? 236 TRP A CE2 1 ATOM 1721 C CE3 . TRP A 1 203 ? 36.580 45.981 24.125 1.00 22.81 ? 236 TRP A CE3 1 ATOM 1722 C CZ2 . TRP A 1 203 ? 39.047 47.056 23.218 1.00 23.68 ? 236 TRP A CZ2 1 ATOM 1723 C CZ3 . TRP A 1 203 ? 37.003 45.821 22.820 1.00 24.93 ? 236 TRP A CZ3 1 ATOM 1724 C CH2 . TRP A 1 203 ? 38.245 46.362 22.372 1.00 25.50 ? 236 TRP A CH2 1 ATOM 1725 N N . ASN A 1 204 ? 36.839 43.208 27.800 1.00 22.05 ? 237 ASN A N 1 ATOM 1726 C CA . ASN A 1 204 ? 36.629 41.966 27.070 1.00 21.77 ? 237 ASN A CA 1 ATOM 1727 C C . ASN A 1 204 ? 35.610 41.035 27.734 1.00 21.08 ? 237 ASN A C 1 ATOM 1728 O O . ASN A 1 204 ? 35.283 41.154 28.931 1.00 21.86 ? 237 ASN A O 1 ATOM 1729 C CB . ASN A 1 204 ? 37.961 41.196 26.918 1.00 22.56 ? 237 ASN A CB 1 ATOM 1730 C CG . ASN A 1 204 ? 38.367 41.019 25.476 1.00 23.84 ? 237 ASN A CG 1 ATOM 1731 O OD1 . ASN A 1 204 ? 37.544 41.061 24.544 1.00 25.67 ? 237 ASN A OD1 1 ATOM 1732 N ND2 . ASN A 1 204 ? 39.677 40.737 25.274 1.00 25.86 ? 237 ASN A ND2 1 ATOM 1733 N N . LEU A 1 205 ? 35.135 40.078 26.928 1.00 22.84 ? 238 LEU A N 1 ATOM 1734 C CA . LEU A 1 205 ? 34.186 39.087 27.403 1.00 22.73 ? 238 LEU A CA 1 ATOM 1735 C C . LEU A 1 205 ? 34.817 38.028 28.345 1.00 22.36 ? 238 LEU A C 1 ATOM 1736 O O . LEU A 1 205 ? 35.739 37.333 27.917 1.00 23.11 ? 238 LEU A O 1 ATOM 1737 C CB . LEU A 1 205 ? 33.622 38.364 26.175 1.00 22.70 ? 238 LEU A CB 1 ATOM 1738 C CG . LEU A 1 205 ? 32.596 37.306 26.508 1.00 23.23 ? 238 LEU A CG 1 ATOM 1739 C CD1 . LEU A 1 205 ? 31.287 37.918 27.085 1.00 23.62 ? 238 LEU A CD1 1 ATOM 1740 C CD2 . LEU A 1 205 ? 32.353 36.572 25.182 1.00 26.09 ? 238 LEU A CD2 1 ATOM 1741 N N . PRO A 1 206 ? 34.325 37.887 29.589 1.00 22.69 ? 239 PRO A N 1 ATOM 1742 C CA . PRO A 1 206 ? 34.792 36.768 30.435 1.00 22.66 ? 239 PRO A CA 1 ATOM 1743 C C . PRO A 1 206 ? 34.221 35.416 29.994 1.00 22.54 ? 239 PRO A C 1 ATOM 1744 O O . PRO A 1 206 ? 33.164 35.384 29.338 1.00 22.44 ? 239 PRO A O 1 ATOM 1745 C CB . PRO A 1 206 ? 34.260 37.096 31.823 1.00 23.96 ? 239 PRO A CB 1 ATOM 1746 C CG . PRO A 1 206 ? 33.798 38.541 31.730 1.00 23.51 ? 239 PRO A CG 1 ATOM 1747 C CD . PRO A 1 206 ? 33.492 38.839 30.357 1.00 23.52 ? 239 PRO A CD 1 ATOM 1748 N N . GLY A 1 207 ? 34.927 34.334 30.348 1.00 21.42 ? 240 GLY A N 1 ATOM 1749 C CA . GLY A 1 207 ? 34.505 32.969 29.961 1.00 21.73 ? 240 GLY A CA 1 ATOM 1750 C C . GLY A 1 207 ? 33.227 32.487 30.601 1.00 21.87 ? 240 GLY A C 1 ATOM 1751 O O . GLY A 1 207 ? 32.674 31.477 30.195 1.00 21.25 ? 240 GLY A O 1 ATOM 1752 N N . THR A 1 208 ? 32.729 33.229 31.592 1.00 20.82 ? 241 THR A N 1 ATOM 1753 C CA . THR A 1 208 ? 31.540 32.850 32.354 1.00 21.72 ? 241 THR A CA 1 ATOM 1754 C C . THR A 1 208 ? 30.248 33.451 31.733 1.00 22.10 ? 241 THR A C 1 ATOM 1755 O O . THR A 1 208 ? 29.162 33.072 32.143 1.00 25.34 ? 241 THR A O 1 ATOM 1756 C CB . THR A 1 208 ? 31.652 33.418 33.780 1.00 23.00 ? 241 THR A CB 1 ATOM 1757 O OG1 . THR A 1 208 ? 31.879 34.820 33.652 1.00 24.97 ? 241 THR A OG1 1 ATOM 1758 C CG2 . THR A 1 208 ? 32.890 32.807 34.471 1.00 24.69 ? 241 THR A CG2 1 ATOM 1759 N N . ALA A 1 209 ? 30.359 34.358 30.764 1.00 20.72 ? 242 ALA A N 1 ATOM 1760 C CA . ALA A 1 209 ? 29.222 35.188 30.359 1.00 21.38 ? 242 ALA A CA 1 ATOM 1761 C C . ALA A 1 209 ? 28.618 34.682 29.074 1.00 21.06 ? 242 ALA A C 1 ATOM 1762 O O . ALA A 1 209 ? 29.319 34.530 28.046 1.00 23.90 ? 242 ALA A O 1 ATOM 1763 C CB . ALA A 1 209 ? 29.689 36.599 30.111 1.00 22.58 ? 242 ALA A CB 1 ATOM 1764 N N . ALA A 1 210 ? 27.310 34.548 29.054 1.00 19.69 ? 243 ALA A N 1 ATOM 1765 C CA . ALA A 1 210 ? 26.620 34.129 27.829 1.00 20.17 ? 243 ALA A CA 1 ATOM 1766 C C . ALA A 1 210 ? 25.848 35.304 27.239 1.00 20.99 ? 243 ALA A C 1 ATOM 1767 O O . ALA A 1 210 ? 25.397 36.196 27.997 1.00 20.33 ? 243 ALA A O 1 ATOM 1768 C CB . ALA A 1 210 ? 25.664 32.980 28.153 1.00 21.49 ? 243 ALA A CB 1 ATOM 1769 N N . GLN A 1 211 ? 25.728 35.299 25.918 1.00 18.49 ? 244 GLN A N 1 ATOM 1770 C CA . GLN A 1 211 ? 24.993 36.326 25.121 1.00 19.64 ? 244 GLN A CA 1 ATOM 1771 C C . GLN A 1 211 ? 23.520 35.949 25.047 1.00 20.55 ? 244 GLN A C 1 ATOM 1772 O O . GLN A 1 211 ? 23.167 34.893 24.472 1.00 20.82 ? 244 GLN A O 1 ATOM 1773 C CB . GLN A 1 211 ? 25.643 36.423 23.749 1.00 20.46 ? 244 GLN A CB 1 ATOM 1774 C CG . GLN A 1 211 ? 24.842 37.342 22.826 1.00 23.10 ? 244 GLN A CG 1 ATOM 1775 C CD . GLN A 1 211 ? 25.158 37.238 21.344 1.00 24.05 ? 244 GLN A CD 1 ATOM 1776 O OE1 . GLN A 1 211 ? 24.239 37.306 20.496 1.00 28.22 ? 244 GLN A OE1 1 ATOM 1777 N NE2 . GLN A 1 211 ? 26.425 37.093 21.004 1.00 25.85 ? 244 GLN A NE2 1 ATOM 1778 N N . ARG A 1 212 ? 22.665 36.811 25.608 1.00 19.57 ? 245 ARG A N 1 ATOM 1779 C CA . ARG A 1 212 ? 21.207 36.638 25.485 1.00 19.53 ? 245 ARG A CA 1 ATOM 1780 C C . ARG A 1 212 ? 20.775 37.083 24.059 1.00 18.84 ? 245 ARG A C 1 ATOM 1781 O O . ARG A 1 212 ? 21.496 37.756 23.317 1.00 19.24 ? 245 ARG A O 1 ATOM 1782 C CB . ARG A 1 212 ? 20.511 37.531 26.536 1.00 19.34 ? 245 ARG A CB 1 ATOM 1783 C CG . ARG A 1 212 ? 20.638 36.987 27.991 1.00 24.19 ? 245 ARG A CG 1 ATOM 1784 C CD . ARG A 1 212 ? 20.522 38.130 29.070 1.00 24.36 ? 245 ARG A CD 1 ATOM 1785 N NE . ARG A 1 212 ? 20.814 37.663 30.421 1.00 25.74 ? 245 ARG A NE 1 ATOM 1786 C CZ . ARG A 1 212 ? 22.046 37.477 30.845 1.00 24.28 ? 245 ARG A CZ 1 ATOM 1787 N NH1 . ARG A 1 212 ? 23.069 37.666 29.995 1.00 24.53 ? 245 ARG A NH1 1 ATOM 1788 N NH2 . ARG A 1 212 ? 22.252 37.059 32.115 1.00 25.29 ? 245 ARG A NH2 1 ATOM 1789 N N . GLY A 1 213 ? 19.549 36.718 23.709 1.00 18.41 ? 246 GLY A N 1 ATOM 1790 C CA . GLY A 1 213 ? 18.947 37.281 22.477 1.00 19.15 ? 246 GLY A CA 1 ATOM 1791 C C . GLY A 1 213 ? 17.826 36.415 21.963 1.00 18.23 ? 246 GLY A C 1 ATOM 1792 O O . GLY A 1 213 ? 17.829 35.197 22.078 1.00 18.54 ? 246 GLY A O 1 ATOM 1793 N N . ASN A 1 214 ? 16.858 37.073 21.318 1.00 16.39 ? 247 ASN A N 1 ATOM 1794 C CA . ASN A 1 214 ? 15.763 36.272 20.754 1.00 16.46 ? 247 ASN A CA 1 ATOM 1795 C C . ASN A 1 214 ? 16.187 35.477 19.495 1.00 17.34 ? 247 ASN A C 1 ATOM 1796 O O . ASN A 1 214 ? 17.143 35.834 18.785 1.00 18.47 ? 247 ASN A O 1 ATOM 1797 C CB . ASN A 1 214 ? 14.532 37.177 20.451 1.00 17.62 ? 247 ASN A CB 1 ATOM 1798 C CG . ASN A 1 214 ? 14.583 37.798 19.076 1.00 21.28 ? 247 ASN A CG 1 ATOM 1799 O OD1 . ASN A 1 214 ? 14.382 37.109 18.049 1.00 20.53 ? 247 ASN A OD1 1 ATOM 1800 N ND2 . ASN A 1 214 ? 14.886 39.117 19.025 1.00 21.48 ? 247 ASN A ND2 1 ATOM 1801 N N . VAL A 1 215 ? 15.458 34.378 19.328 1.00 16.68 ? 248 VAL A N 1 ATOM 1802 C CA . VAL A 1 215 ? 15.761 33.470 18.228 1.00 17.17 ? 248 VAL A CA 1 ATOM 1803 C C . VAL A 1 215 ? 14.550 33.308 17.303 1.00 18.04 ? 248 VAL A C 1 ATOM 1804 O O . VAL A 1 215 ? 14.397 32.260 16.632 1.00 18.64 ? 248 VAL A O 1 ATOM 1805 C CB . VAL A 1 215 ? 16.285 32.059 18.718 1.00 18.25 ? 248 VAL A CB 1 ATOM 1806 C CG1 . VAL A 1 215 ? 17.673 32.187 19.252 1.00 20.04 ? 248 VAL A CG1 1 ATOM 1807 C CG2 . VAL A 1 215 ? 15.364 31.490 19.805 1.00 18.63 ? 248 VAL A CG2 1 ATOM 1808 N N . LEU A 1 216 ? 13.699 34.334 17.222 1.00 18.00 ? 249 LEU A N 1 ATOM 1809 C CA . LEU A 1 216 ? 12.584 34.287 16.244 1.00 18.84 ? 249 LEU A CA 1 ATOM 1810 C C . LEU A 1 216 ? 13.132 34.517 14.833 1.00 19.26 ? 249 LEU A C 1 ATOM 1811 O O . LEU A 1 216 ? 14.255 35.062 14.676 1.00 21.70 ? 249 LEU A O 1 ATOM 1812 C CB . LEU A 1 216 ? 11.638 35.442 16.477 1.00 19.00 ? 249 LEU A CB 1 ATOM 1813 C CG . LEU A 1 216 ? 10.844 35.330 17.760 1.00 19.85 ? 249 LEU A CG 1 ATOM 1814 C CD1 . LEU A 1 216 ? 10.094 36.703 18.027 1.00 21.72 ? 249 LEU A CD1 1 ATOM 1815 C CD2 . LEU A 1 216 ? 9.866 34.204 17.755 1.00 19.13 ? 249 LEU A CD2 1 ATOM 1816 N N . ASN A 1 217 ? 12.386 34.018 13.833 1.00 19.60 ? 250 ASN A N 1 ATOM 1817 C CA . ASN A 1 217 ? 12.613 34.440 12.410 1.00 21.24 ? 250 ASN A CA 1 ATOM 1818 C C . ASN A 1 217 ? 11.349 35.140 11.910 1.00 19.50 ? 250 ASN A C 1 ATOM 1819 O O . ASN A 1 217 ? 10.518 34.550 11.248 1.00 20.62 ? 250 ASN A O 1 ATOM 1820 C CB . ASN A 1 217 ? 12.904 33.154 11.675 1.00 20.97 ? 250 ASN A CB 1 ATOM 1821 C CG A ASN A 1 217 ? 13.161 33.326 10.203 0.65 25.25 ? 250 ASN A CG 1 ATOM 1822 C CG B ASN A 1 217 ? 14.309 32.709 11.919 0.35 20.91 ? 250 ASN A CG 1 ATOM 1823 O OD1 A ASN A 1 217 ? 12.775 32.465 9.415 0.65 34.87 ? 250 ASN A OD1 1 ATOM 1824 O OD1 B ASN A 1 217 ? 15.248 33.472 11.741 0.35 22.95 ? 250 ASN A OD1 1 ATOM 1825 N ND2 A ASN A 1 217 ? 13.876 34.356 9.840 0.65 29.51 ? 250 ASN A ND2 1 ATOM 1826 N ND2 B ASN A 1 217 ? 14.466 31.484 12.348 0.35 25.15 ? 250 ASN A ND2 1 ATOM 1827 N N . LEU A 1 218 ? 11.192 36.404 12.317 1.00 19.33 ? 251 LEU A N 1 ATOM 1828 C CA . LEU A 1 218 ? 9.962 37.148 12.076 1.00 19.15 ? 251 LEU A CA 1 ATOM 1829 C C . LEU A 1 218 ? 9.885 37.729 10.695 1.00 20.22 ? 251 LEU A C 1 ATOM 1830 O O . LEU A 1 218 ? 8.732 38.027 10.250 1.00 20.31 ? 251 LEU A O 1 ATOM 1831 C CB . LEU A 1 218 ? 9.823 38.354 13.033 1.00 20.65 ? 251 LEU A CB 1 ATOM 1832 C CG . LEU A 1 218 ? 9.513 37.985 14.464 1.00 21.42 ? 251 LEU A CG 1 ATOM 1833 C CD1 . LEU A 1 218 ? 9.714 39.222 15.365 1.00 19.94 ? 251 LEU A CD1 1 ATOM 1834 C CD2 . LEU A 1 218 ? 8.115 37.317 14.564 1.00 18.76 ? 251 LEU A CD2 1 ATOM 1835 N N . ASN A 1 219 ? 11.044 37.996 10.056 1.00 20.00 ? 252 ASN A N 1 ATOM 1836 C CA . ASN A 1 219 ? 10.996 38.680 8.747 1.00 19.16 ? 252 ASN A CA 1 ATOM 1837 C C . ASN A 1 219 ? 10.089 39.927 8.793 1.00 20.32 ? 252 ASN A C 1 ATOM 1838 O O . ASN A 1 219 ? 9.321 40.204 7.849 1.00 20.38 ? 252 ASN A O 1 ATOM 1839 C CB . ASN A 1 219 ? 10.563 37.766 7.640 1.00 20.97 ? 252 ASN A CB 1 ATOM 1840 C CG . ASN A 1 219 ? 11.582 36.648 7.435 1.00 23.53 ? 252 ASN A CG 1 ATOM 1841 O OD1 . ASN A 1 219 ? 12.795 36.877 7.454 1.00 26.68 ? 252 ASN A OD1 1 ATOM 1842 N ND2 . ASN A 1 219 ? 11.072 35.480 7.243 1.00 26.10 ? 252 ASN A ND2 1 ATOM 1843 N N . GLY A 1 220 ? 10.224 40.718 9.858 1.00 18.40 ? 253 GLY A N 1 ATOM 1844 C CA . GLY A 1 220 ? 9.561 42.021 9.875 1.00 18.54 ? 253 GLY A CA 1 ATOM 1845 C C . GLY A 1 220 ? 8.170 41.977 10.402 1.00 18.30 ? 253 GLY A C 1 ATOM 1846 O O . GLY A 1 220 ? 7.520 43.030 10.439 1.00 20.47 ? 253 GLY A O 1 ATOM 1847 N N . ALA A 1 221 ? 7.647 40.825 10.841 1.00 18.93 ? 254 ALA A N 1 ATOM 1848 C CA . ALA A 1 221 ? 6.254 40.727 11.240 1.00 17.48 ? 254 ALA A CA 1 ATOM 1849 C C . ALA A 1 221 ? 5.844 41.445 12.521 1.00 18.42 ? 254 ALA A C 1 ATOM 1850 O O . ALA A 1 221 ? 4.656 41.785 12.649 1.00 18.68 ? 254 ALA A O 1 ATOM 1851 C CB . ALA A 1 221 ? 5.822 39.276 11.313 1.00 18.45 ? 254 ALA A CB 1 ATOM 1852 N N . GLY A 1 222 ? 6.770 41.673 13.455 1.00 17.06 ? 255 GLY A N 1 ATOM 1853 C CA . GLY A 1 222 ? 6.319 42.245 14.767 1.00 16.95 ? 255 GLY A CA 1 ATOM 1854 C C . GLY A 1 222 ? 5.850 41.131 15.716 1.00 17.30 ? 255 GLY A C 1 ATOM 1855 O O . GLY A 1 222 ? 6.346 40.003 15.652 1.00 17.83 ? 255 GLY A O 1 ATOM 1856 N N . ASP A 1 223 ? 4.922 41.470 16.606 1.00 16.78 ? 256 ASP A N 1 ATOM 1857 C CA . ASP A 1 223 ? 4.425 40.439 17.551 1.00 16.89 ? 256 ASP A CA 1 ATOM 1858 C C . ASP A 1 223 ? 4.056 39.175 16.797 1.00 18.33 ? 256 ASP A C 1 ATOM 1859 O O . ASP A 1 223 ? 3.280 39.231 15.838 1.00 17.65 ? 256 ASP A O 1 ATOM 1860 C CB . ASP A 1 223 ? 3.150 41.049 18.161 1.00 16.68 ? 256 ASP A CB 1 ATOM 1861 C CG . ASP A 1 223 ? 2.345 40.035 18.954 1.00 17.99 ? 256 ASP A CG 1 ATOM 1862 O OD1 . ASP A 1 223 ? 2.945 39.197 19.697 1.00 17.76 ? 256 ASP A OD1 1 ATOM 1863 O OD2 . ASP A 1 223 ? 1.106 40.081 18.874 1.00 18.44 ? 256 ASP A OD2 1 ATOM 1864 N N . PRO A 1 224 ? 4.584 38.009 17.247 1.00 17.63 ? 257 PRO A N 1 ATOM 1865 C CA . PRO A 1 224 ? 4.258 36.759 16.536 1.00 16.78 ? 257 PRO A CA 1 ATOM 1866 C C . PRO A 1 224 ? 2.803 36.408 16.393 1.00 16.53 ? 257 PRO A C 1 ATOM 1867 O O . PRO A 1 224 ? 2.497 35.681 15.446 1.00 18.04 ? 257 PRO A O 1 ATOM 1868 C CB . PRO A 1 224 ? 4.955 35.672 17.455 1.00 18.66 ? 257 PRO A CB 1 ATOM 1869 C CG . PRO A 1 224 ? 6.078 36.359 18.103 1.00 19.69 ? 257 PRO A CG 1 ATOM 1870 C CD . PRO A 1 224 ? 5.650 37.857 18.272 1.00 18.24 ? 257 PRO A CD 1 ATOM 1871 N N . LEU A 1 225 ? 1.932 36.912 17.292 1.00 16.20 ? 258 LEU A N 1 ATOM 1872 C CA . LEU A 1 225 ? 0.550 36.449 17.258 1.00 15.81 ? 258 LEU A CA 1 ATOM 1873 C C . LEU A 1 225 ? -0.345 37.373 16.391 1.00 16.14 ? 258 LEU A C 1 ATOM 1874 O O . LEU A 1 225 ? -1.496 36.988 16.128 1.00 17.58 ? 258 LEU A O 1 ATOM 1875 C CB . LEU A 1 225 ? -0.033 36.405 18.666 1.00 17.58 ? 258 LEU A CB 1 ATOM 1876 C CG . LEU A 1 225 ? 0.779 35.524 19.639 1.00 18.44 ? 258 LEU A CG 1 ATOM 1877 C CD1 . LEU A 1 225 ? 0.003 35.551 20.943 1.00 21.97 ? 258 LEU A CD1 1 ATOM 1878 C CD2 . LEU A 1 225 ? 0.953 34.120 19.087 1.00 21.10 ? 258 LEU A CD2 1 ATOM 1879 N N . THR A 1 226 ? 0.148 38.556 15.973 1.00 16.60 ? 259 THR A N 1 ATOM 1880 C CA . THR A 1 226 ? -0.750 39.525 15.305 1.00 16.94 ? 259 THR A CA 1 ATOM 1881 C C . THR A 1 226 ? -0.112 40.135 14.037 1.00 17.93 ? 259 THR A C 1 ATOM 1882 O O . THR A 1 226 ? -0.194 41.340 13.818 1.00 17.36 ? 259 THR A O 1 ATOM 1883 C CB . THR A 1 226 ? -1.110 40.653 16.277 1.00 15.42 ? 259 THR A CB 1 ATOM 1884 O OG1 . THR A 1 226 ? 0.111 41.287 16.693 1.00 17.50 ? 259 THR A OG1 1 ATOM 1885 C CG2 . THR A 1 226 ? -1.866 40.117 17.478 1.00 17.14 ? 259 THR A CG2 1 ATOM 1886 N N . PRO A 1 227 ? 0.450 39.298 13.149 1.00 16.59 ? 260 PRO A N 1 ATOM 1887 C CA . PRO A 1 227 ? 1.138 39.878 11.966 1.00 17.37 ? 260 PRO A CA 1 ATOM 1888 C C . PRO A 1 227 ? 0.158 40.716 11.153 1.00 18.18 ? 260 PRO A C 1 ATOM 1889 O O . PRO A 1 227 ? -0.931 40.230 10.765 1.00 18.51 ? 260 PRO A O 1 ATOM 1890 C CB . PRO A 1 227 ? 1.599 38.624 11.160 1.00 17.18 ? 260 PRO A CB 1 ATOM 1891 C CG . PRO A 1 227 ? 0.642 37.487 11.611 1.00 17.43 ? 260 PRO A CG 1 ATOM 1892 C CD . PRO A 1 227 ? 0.413 37.797 13.111 1.00 17.79 ? 260 PRO A CD 1 ATOM 1893 N N . GLY A 1 228 ? 0.583 41.934 10.858 1.00 16.54 ? 261 GLY A N 1 ATOM 1894 C CA . GLY A 1 228 ? -0.191 42.864 9.984 1.00 16.68 ? 261 GLY A CA 1 ATOM 1895 C C . GLY A 1 228 ? -1.005 43.886 10.742 1.00 19.03 ? 261 GLY A C 1 ATOM 1896 O O . GLY A 1 228 ? -1.388 44.899 10.145 1.00 18.38 ? 261 GLY A O 1 ATOM 1897 N N . TYR A 1 229 ? -1.315 43.663 12.028 1.00 17.08 ? 262 TYR A N 1 ATOM 1898 C CA . TYR A 1 229 ? -2.286 44.491 12.780 1.00 17.37 ? 262 TYR A CA 1 ATOM 1899 C C . TYR A 1 229 ? -1.780 44.747 14.180 1.00 17.55 ? 262 TYR A C 1 ATOM 1900 O O . TYR A 1 229 ? -1.127 43.891 14.779 1.00 17.42 ? 262 TYR A O 1 ATOM 1901 C CB . TYR A 1 229 ? -3.636 43.727 12.867 1.00 18.45 ? 262 TYR A CB 1 ATOM 1902 C CG . TYR A 1 229 ? -4.089 43.333 11.478 1.00 16.30 ? 262 TYR A CG 1 ATOM 1903 C CD1 . TYR A 1 229 ? -4.634 44.285 10.618 1.00 18.37 ? 262 TYR A CD1 1 ATOM 1904 C CD2 . TYR A 1 229 ? -3.837 42.072 10.974 1.00 17.01 ? 262 TYR A CD2 1 ATOM 1905 C CE1 . TYR A 1 229 ? -4.933 43.949 9.247 1.00 19.04 ? 262 TYR A CE1 1 ATOM 1906 C CE2 . TYR A 1 229 ? -4.083 41.714 9.619 1.00 17.35 ? 262 TYR A CE2 1 ATOM 1907 C CZ . TYR A 1 229 ? -4.661 42.671 8.762 1.00 17.68 ? 262 TYR A CZ 1 ATOM 1908 O OH . TYR A 1 229 ? -4.921 42.312 7.441 1.00 19.24 ? 262 TYR A OH 1 ATOM 1909 N N . PRO A 1 230 ? -2.085 45.910 14.768 1.00 16.80 ? 263 PRO A N 1 ATOM 1910 C CA . PRO A 1 230 ? -1.550 46.202 16.111 1.00 17.35 ? 263 PRO A CA 1 ATOM 1911 C C . PRO A 1 230 ? -2.196 45.308 17.138 1.00 16.82 ? 263 PRO A C 1 ATOM 1912 O O . PRO A 1 230 ? -3.405 45.039 17.067 1.00 16.93 ? 263 PRO A O 1 ATOM 1913 C CB . PRO A 1 230 ? -1.920 47.681 16.310 1.00 17.56 ? 263 PRO A CB 1 ATOM 1914 C CG . PRO A 1 230 ? -3.210 47.816 15.477 1.00 17.48 ? 263 PRO A CG 1 ATOM 1915 C CD . PRO A 1 230 ? -2.917 47.003 14.222 1.00 16.66 ? 263 PRO A CD 1 ATOM 1916 N N . ALA A 1 231 ? -1.395 44.967 18.146 1.00 16.20 ? 264 ALA A N 1 ATOM 1917 C CA . ALA A 1 231 ? -1.825 44.035 19.172 1.00 16.67 ? 264 ALA A CA 1 ATOM 1918 C C . ALA A 1 231 ? -2.568 44.763 20.277 1.00 18.18 ? 264 ALA A C 1 ATOM 1919 O O . ALA A 1 231 ? -2.030 45.000 21.365 1.00 18.27 ? 264 ALA A O 1 ATOM 1920 C CB . ALA A 1 231 ? -0.562 43.339 19.713 1.00 18.44 ? 264 ALA A CB 1 ATOM 1921 N N . LYS A 1 232 ? -3.832 45.132 19.988 1.00 18.28 ? 265 LYS A N 1 ATOM 1922 C CA . LYS A 1 232 ? -4.747 45.875 20.955 1.00 18.17 ? 265 LYS A CA 1 ATOM 1923 C C . LYS A 1 232 ? -5.493 44.819 21.750 1.00 18.81 ? 265 LYS A C 1 ATOM 1924 O O . LYS A 1 232 ? -5.360 43.604 21.494 1.00 20.26 ? 265 LYS A O 1 ATOM 1925 C CB . LYS A 1 232 ? -5.728 46.737 20.162 1.00 21.04 ? 265 LYS A CB 1 ATOM 1926 C CG . LYS A 1 232 ? -5.029 47.697 19.129 1.00 24.72 ? 265 LYS A CG 1 ATOM 1927 C CD . LYS A 1 232 ? -4.380 48.838 19.738 1.00 32.52 ? 265 LYS A CD 1 ATOM 1928 C CE . LYS A 1 232 ? -5.427 49.857 20.177 1.00 34.02 ? 265 LYS A CE 1 ATOM 1929 N NZ . LYS A 1 232 ? -4.738 51.075 20.614 1.00 35.50 ? 265 LYS A NZ 1 ATOM 1930 N N . GLU A 1 233 ? -6.351 45.267 22.654 1.00 19.87 ? 266 GLU A N 1 ATOM 1931 C CA . GLU A 1 233 ? -7.015 44.288 23.521 1.00 21.47 ? 266 GLU A CA 1 ATOM 1932 C C . GLU A 1 233 ? -8.012 43.364 22.774 1.00 22.10 ? 266 GLU A C 1 ATOM 1933 O O . GLU A 1 233 ? -8.184 42.192 23.148 1.00 23.86 ? 266 GLU A O 1 ATOM 1934 C CB . GLU A 1 233 ? -7.764 45.071 24.625 1.00 23.50 ? 266 GLU A CB 1 ATOM 1935 C CG . GLU A 1 233 ? -6.812 45.856 25.560 1.00 25.88 ? 266 GLU A CG 1 ATOM 1936 C CD . GLU A 1 233 ? -6.481 47.287 25.049 1.00 31.52 ? 266 GLU A CD 1 ATOM 1937 O OE1 . GLU A 1 233 ? -6.099 48.136 25.905 1.00 31.03 ? 266 GLU A OE1 1 ATOM 1938 O OE2 . GLU A 1 233 ? -6.627 47.634 23.813 1.00 31.48 ? 266 GLU A OE2 1 ATOM 1939 N N . TYR A 1 234 ? -8.673 43.898 21.741 1.00 21.49 ? 267 TYR A N 1 ATOM 1940 C CA . TYR A 1 234 ? -9.718 43.177 21.038 1.00 21.56 ? 267 TYR A CA 1 ATOM 1941 C C . TYR A 1 234 ? -9.146 42.300 19.938 1.00 21.34 ? 267 TYR A C 1 ATOM 1942 O O . TYR A 1 234 ? -9.881 41.519 19.304 1.00 21.77 ? 267 TYR A O 1 ATOM 1943 C CB . TYR A 1 234 ? -10.759 44.168 20.403 1.00 21.01 ? 267 TYR A CB 1 ATOM 1944 C CG . TYR A 1 234 ? -10.093 45.017 19.338 1.00 20.72 ? 267 TYR A CG 1 ATOM 1945 C CD1 . TYR A 1 234 ? -9.899 44.528 18.016 1.00 20.19 ? 267 TYR A CD1 1 ATOM 1946 C CD2 . TYR A 1 234 ? -9.570 46.281 19.635 1.00 24.28 ? 267 TYR A CD2 1 ATOM 1947 C CE1 . TYR A 1 234 ? -9.202 45.255 17.034 1.00 21.27 ? 267 TYR A CE1 1 ATOM 1948 C CE2 . TYR A 1 234 ? -8.902 47.030 18.656 1.00 22.94 ? 267 TYR A CE2 1 ATOM 1949 C CZ . TYR A 1 234 ? -8.705 46.496 17.345 1.00 22.75 ? 267 TYR A CZ 1 ATOM 1950 O OH . TYR A 1 234 ? -7.980 47.172 16.388 1.00 24.10 ? 267 TYR A OH 1 ATOM 1951 N N . THR A 1 235 ? -7.842 42.441 19.652 1.00 18.44 ? 268 THR A N 1 ATOM 1952 C CA . THR A 1 235 ? -7.286 41.975 18.391 1.00 17.99 ? 268 THR A CA 1 ATOM 1953 C C . THR A 1 235 ? -7.241 40.450 18.288 1.00 19.42 ? 268 THR A C 1 ATOM 1954 O O . THR A 1 235 ? -6.910 39.743 19.269 1.00 19.62 ? 268 THR A O 1 ATOM 1955 C CB . THR A 1 235 ? -5.843 42.517 18.255 1.00 19.04 ? 268 THR A CB 1 ATOM 1956 O OG1 . THR A 1 235 ? -5.967 43.934 18.356 1.00 18.65 ? 268 THR A OG1 1 ATOM 1957 C CG2 . THR A 1 235 ? -5.193 42.166 16.906 1.00 18.78 ? 268 THR A CG2 1 ATOM 1958 N N . PHE A 1 236 ? -7.599 39.923 17.123 1.00 19.37 ? 269 PHE A N 1 ATOM 1959 C CA . PHE A 1 236 ? -7.435 38.514 16.868 1.00 19.73 ? 269 PHE A CA 1 ATOM 1960 C C . PHE A 1 236 ? -5.962 38.086 17.005 1.00 17.78 ? 269 PHE A C 1 ATOM 1961 O O . PHE A 1 236 ? -5.055 38.770 16.516 1.00 19.14 ? 269 PHE A O 1 ATOM 1962 C CB . PHE A 1 236 ? -7.883 38.243 15.420 1.00 20.48 ? 269 PHE A CB 1 ATOM 1963 C CG . PHE A 1 236 ? -7.476 36.868 14.917 1.00 21.18 ? 269 PHE A CG 1 ATOM 1964 C CD1 . PHE A 1 236 ? -6.317 36.699 14.183 1.00 22.36 ? 269 PHE A CD1 1 ATOM 1965 C CD2 . PHE A 1 236 ? -8.264 35.789 15.208 1.00 22.18 ? 269 PHE A CD2 1 ATOM 1966 C CE1 . PHE A 1 236 ? -5.935 35.420 13.716 1.00 24.50 ? 269 PHE A CE1 1 ATOM 1967 C CE2 . PHE A 1 236 ? -7.876 34.474 14.737 1.00 23.20 ? 269 PHE A CE2 1 ATOM 1968 C CZ . PHE A 1 236 ? -6.722 34.319 14.009 1.00 20.97 ? 269 PHE A CZ 1 ATOM 1969 N N . ARG A 1 237 ? -5.755 36.917 17.668 1.00 18.37 ? 270 ARG A N 1 ATOM 1970 C CA . ARG A 1 237 ? -4.413 36.374 17.821 1.00 18.95 ? 270 ARG A CA 1 ATOM 1971 C C . ARG A 1 237 ? -4.365 34.984 17.252 1.00 18.36 ? 270 ARG A C 1 ATOM 1972 O O . ARG A 1 237 ? -5.257 34.166 17.529 1.00 20.23 ? 270 ARG A O 1 ATOM 1973 C CB . ARG A 1 237 ? -4.025 36.365 19.304 1.00 19.71 ? 270 ARG A CB 1 ATOM 1974 C CG . ARG A 1 237 ? -3.668 37.802 19.748 1.00 23.74 ? 270 ARG A CG 1 ATOM 1975 C CD . ARG A 1 237 ? -3.651 38.099 21.182 1.00 28.21 ? 270 ARG A CD 1 ATOM 1976 N NE . ARG A 1 237 ? -3.124 39.457 21.439 1.00 23.13 ? 270 ARG A NE 1 ATOM 1977 C CZ . ARG A 1 237 ? -3.825 40.578 21.621 1.00 20.19 ? 270 ARG A CZ 1 ATOM 1978 N NH1 . ARG A 1 237 ? -5.166 40.671 21.483 1.00 20.94 ? 270 ARG A NH1 1 ATOM 1979 N NH2 . ARG A 1 237 ? -3.149 41.683 21.969 1.00 19.04 ? 270 ARG A NH2 1 ATOM 1980 N N . LEU A 1 238 ? -3.304 34.706 16.522 1.00 18.78 ? 271 LEU A N 1 ATOM 1981 C CA . LEU A 1 238 ? -2.955 33.338 16.144 1.00 19.31 ? 271 LEU A CA 1 ATOM 1982 C C . LEU A 1 238 ? -2.813 32.478 17.398 1.00 20.25 ? 271 LEU A C 1 ATOM 1983 O O . LEU A 1 238 ? -2.424 32.962 18.474 1.00 19.85 ? 271 LEU A O 1 ATOM 1984 C CB . LEU A 1 238 ? -1.612 33.329 15.405 1.00 18.99 ? 271 LEU A CB 1 ATOM 1985 C CG . LEU A 1 238 ? -1.610 34.030 14.045 1.00 19.45 ? 271 LEU A CG 1 ATOM 1986 C CD1 . LEU A 1 238 ? -0.210 34.143 13.527 1.00 19.80 ? 271 LEU A CD1 1 ATOM 1987 C CD2 . LEU A 1 238 ? -2.510 33.149 13.090 1.00 22.56 ? 271 LEU A CD2 1 ATOM 1988 N N . ASP A 1 239 ? -3.118 31.196 17.219 1.00 21.10 ? 272 ASP A N 1 ATOM 1989 C CA . ASP A 1 239 ? -2.777 30.270 18.271 1.00 23.61 ? 272 ASP A CA 1 ATOM 1990 C C . ASP A 1 239 ? -1.269 30.305 18.445 1.00 24.37 ? 272 ASP A C 1 ATOM 1991 O O . ASP A 1 239 ? -0.494 30.475 17.471 1.00 24.89 ? 272 ASP A O 1 ATOM 1992 C CB . ASP A 1 239 ? -3.204 28.839 17.853 1.00 24.86 ? 272 ASP A CB 1 ATOM 1993 C CG . ASP A 1 239 ? -4.744 28.656 17.700 1.00 29.88 ? 272 ASP A CG 1 ATOM 1994 O OD1 . ASP A 1 239 ? -5.566 29.501 18.168 1.00 30.36 ? 272 ASP A OD1 1 ATOM 1995 O OD2 . ASP A 1 239 ? -5.125 27.613 17.074 1.00 33.02 ? 272 ASP A OD2 1 ATOM 1996 N N . VAL A 1 240 ? -0.841 30.141 19.697 1.00 26.14 ? 273 VAL A N 1 ATOM 1997 C CA . VAL A 1 240 ? 0.604 30.267 19.967 1.00 28.54 ? 273 VAL A CA 1 ATOM 1998 C C . VAL A 1 240 ? 1.447 29.303 19.148 1.00 31.11 ? 273 VAL A C 1 ATOM 1999 O O . VAL A 1 240 ? 2.546 29.624 18.680 1.00 28.80 ? 273 VAL A O 1 ATOM 2000 C CB . VAL A 1 240 ? 0.985 30.247 21.471 1.00 29.71 ? 273 VAL A CB 1 ATOM 2001 C CG1 A VAL A 1 240 ? 0.850 28.822 22.063 0.65 27.54 ? 273 VAL A CG1 1 ATOM 2002 C CG1 B VAL A 1 240 ? 2.490 30.450 21.638 0.35 29.79 ? 273 VAL A CG1 1 ATOM 2003 C CG2 A VAL A 1 240 ? 2.378 30.825 21.680 0.65 30.28 ? 273 VAL A CG2 1 ATOM 2004 C CG2 B VAL A 1 240 ? 0.241 31.291 22.228 0.35 29.44 ? 273 VAL A CG2 1 ATOM 2005 N N . GLU A 1 241 ? 0.926 28.098 18.937 1.00 31.85 ? 274 GLU A N 1 ATOM 2006 C CA . GLU A 1 241 ? 1.616 27.103 18.115 1.00 33.24 ? 274 GLU A CA 1 ATOM 2007 C C . GLU A 1 241 ? 1.866 27.577 16.681 1.00 32.92 ? 274 GLU A C 1 ATOM 2008 O O . GLU A 1 241 ? 2.756 27.048 15.983 1.00 34.63 ? 274 GLU A O 1 ATOM 2009 C CB . GLU A 1 241 ? 0.828 25.758 18.153 1.00 34.78 ? 274 GLU A CB 1 ATOM 2010 C CG A GLU A 1 241 ? -0.653 25.856 17.780 0.50 35.30 ? 274 GLU A CG 1 ATOM 2011 C CG B GLU A 1 241 ? 0.740 25.140 19.561 0.50 34.00 ? 274 GLU A CG 1 ATOM 2012 C CD A GLU A 1 241 ? -1.595 25.915 18.987 0.50 35.52 ? 274 GLU A CD 1 ATOM 2013 C CD B GLU A 1 241 ? -0.400 25.681 20.444 0.50 36.76 ? 274 GLU A CD 1 ATOM 2014 O OE1 A GLU A 1 241 ? -1.333 26.659 19.965 0.50 33.07 ? 274 GLU A OE1 1 ATOM 2015 O OE1 B GLU A 1 241 ? -1.120 26.640 20.060 0.50 33.36 ? 274 GLU A OE1 1 ATOM 2016 O OE2 A GLU A 1 241 ? -2.631 25.209 18.947 0.50 38.85 ? 274 GLU A OE2 1 ATOM 2017 O OE2 B GLU A 1 241 ? -0.577 25.135 21.559 0.50 36.39 ? 274 GLU A OE2 1 ATOM 2018 N N . GLU A 1 242 ? 1.081 28.567 16.237 1.00 30.28 ? 275 GLU A N 1 ATOM 2019 C CA . GLU A 1 242 ? 1.185 29.094 14.906 1.00 29.30 ? 275 GLU A CA 1 ATOM 2020 C C . GLU A 1 242 ? 1.878 30.480 14.887 1.00 24.84 ? 275 GLU A C 1 ATOM 2021 O O . GLU A 1 242 ? 1.897 31.107 13.838 1.00 25.48 ? 275 GLU A O 1 ATOM 2022 C CB . GLU A 1 242 ? -0.168 29.216 14.232 1.00 31.03 ? 275 GLU A CB 1 ATOM 2023 C CG . GLU A 1 242 ? -0.743 27.857 13.735 1.00 38.63 ? 275 GLU A CG 1 ATOM 2024 C CD . GLU A 1 242 ? -2.072 28.000 12.961 1.00 46.42 ? 275 GLU A CD 1 ATOM 2025 O OE1 . GLU A 1 242 ? -2.477 29.140 12.633 1.00 45.08 ? 275 GLU A OE1 1 ATOM 2026 O OE2 . GLU A 1 242 ? -2.714 26.948 12.662 1.00 52.91 ? 275 GLU A OE2 1 ATOM 2027 N N . GLY A 1 243 ? 2.371 30.934 16.034 1.00 23.76 ? 276 GLY A N 1 ATOM 2028 C CA . GLY A 1 243 ? 3.061 32.239 16.126 1.00 21.73 ? 276 GLY A CA 1 ATOM 2029 C C . GLY A 1 243 ? 4.122 32.368 15.086 1.00 21.61 ? 276 GLY A C 1 ATOM 2030 O O . GLY A 1 243 ? 4.924 31.445 14.872 1.00 22.85 ? 276 GLY A O 1 ATOM 2031 N N . VAL A 1 244 ? 4.163 33.513 14.402 1.00 19.16 ? 277 VAL A N 1 ATOM 2032 C CA . VAL A 1 244 ? 5.143 33.703 13.357 1.00 19.37 ? 277 VAL A CA 1 ATOM 2033 C C . VAL A 1 244 ? 6.582 33.626 13.874 1.00 19.04 ? 277 VAL A C 1 ATOM 2034 O O . VAL A 1 244 ? 6.895 34.288 14.860 1.00 20.88 ? 277 VAL A O 1 ATOM 2035 C CB . VAL A 1 244 ? 4.911 35.078 12.643 1.00 20.85 ? 277 VAL A CB 1 ATOM 2036 C CG1 . VAL A 1 244 ? 6.031 35.364 11.570 1.00 21.21 ? 277 VAL A CG1 1 ATOM 2037 C CG2 . VAL A 1 244 ? 3.501 35.085 11.981 1.00 23.25 ? 277 VAL A CG2 1 ATOM 2038 N N . GLY A 1 245 ? 7.397 32.785 13.188 1.00 19.91 ? 278 GLY A N 1 ATOM 2039 C CA . GLY A 1 245 ? 8.878 32.761 13.409 1.00 20.44 ? 278 GLY A CA 1 ATOM 2040 C C . GLY A 1 245 ? 9.313 32.030 14.660 1.00 18.29 ? 278 GLY A C 1 ATOM 2041 O O . GLY A 1 245 ? 10.519 32.021 14.931 1.00 18.86 ? 278 GLY A O 1 ATOM 2042 N N . ILE A 1 246 ? 8.395 31.391 15.374 1.00 18.78 ? 279 ILE A N 1 ATOM 2043 C CA . ILE A 1 246 ? 8.794 30.682 16.613 1.00 18.39 ? 279 ILE A CA 1 ATOM 2044 C C . ILE A 1 246 ? 9.488 29.367 16.271 1.00 19.01 ? 279 ILE A C 1 ATOM 2045 O O . ILE A 1 246 ? 8.954 28.568 15.499 1.00 19.66 ? 279 ILE A O 1 ATOM 2046 C CB . ILE A 1 246 ? 7.565 30.433 17.478 1.00 19.16 ? 279 ILE A CB 1 ATOM 2047 C CG1 . ILE A 1 246 ? 7.008 31.795 17.928 1.00 20.19 ? 279 ILE A CG1 1 ATOM 2048 C CG2 . ILE A 1 246 ? 7.976 29.692 18.760 1.00 21.39 ? 279 ILE A CG2 1 ATOM 2049 C CD1 . ILE A 1 246 ? 5.704 31.613 18.798 1.00 23.17 ? 279 ILE A CD1 1 ATOM 2050 N N . PRO A 1 247 ? 10.680 29.159 16.833 1.00 17.50 ? 280 PRO A N 1 ATOM 2051 C CA . PRO A 1 247 ? 11.420 27.920 16.440 1.00 18.22 ? 280 PRO A CA 1 ATOM 2052 C C . PRO A 1 247 ? 10.843 26.689 17.107 1.00 18.73 ? 280 PRO A C 1 ATOM 2053 O O . PRO A 1 247 ? 10.096 26.797 18.073 1.00 20.22 ? 280 PRO A O 1 ATOM 2054 C CB . PRO A 1 247 ? 12.841 28.200 16.957 1.00 19.79 ? 280 PRO A CB 1 ATOM 2055 C CG . PRO A 1 247 ? 12.639 29.153 18.180 1.00 20.13 ? 280 PRO A CG 1 ATOM 2056 C CD . PRO A 1 247 ? 11.502 30.085 17.655 1.00 19.14 ? 280 PRO A CD 1 ATOM 2057 N N . ARG A 1 248 ? 11.206 25.531 16.582 1.00 19.14 ? 281 ARG A N 1 ATOM 2058 C CA . ARG A 1 248 ? 10.562 24.305 17.035 1.00 20.24 ? 281 ARG A CA 1 ATOM 2059 C C . ARG A 1 248 ? 11.535 23.345 17.698 1.00 20.50 ? 281 ARG A C 1 ATOM 2060 O O . ARG A 1 248 ? 11.186 22.204 17.975 1.00 22.54 ? 281 ARG A O 1 ATOM 2061 C CB A ARG A 1 248 ? 10.073 23.586 15.790 0.70 21.12 ? 281 ARG A CB 1 ATOM 2062 C CB B ARG A 1 248 ? 9.699 23.633 15.967 0.30 20.59 ? 281 ARG A CB 1 ATOM 2063 C CG A ARG A 1 248 ? 9.101 24.476 15.003 0.70 25.37 ? 281 ARG A CG 1 ATOM 2064 C CG B ARG A 1 248 ? 8.354 24.374 15.715 0.30 19.91 ? 281 ARG A CG 1 ATOM 2065 C CD A ARG A 1 248 ? 8.325 23.716 13.966 0.70 31.72 ? 281 ARG A CD 1 ATOM 2066 C CD B ARG A 1 248 ? 7.376 23.446 15.033 0.30 24.05 ? 281 ARG A CD 1 ATOM 2067 N NE A ARG A 1 248 ? 7.221 24.541 13.491 0.70 40.47 ? 281 ARG A NE 1 ATOM 2068 N NE B ARG A 1 248 ? 7.392 22.136 15.699 0.30 29.08 ? 281 ARG A NE 1 ATOM 2069 C CZ A ARG A 1 248 ? 7.310 25.416 12.490 0.70 42.31 ? 281 ARG A CZ 1 ATOM 2070 C CZ B ARG A 1 248 ? 7.377 20.958 15.081 0.30 30.48 ? 281 ARG A CZ 1 ATOM 2071 N NH1 A ARG A 1 248 ? 6.233 26.110 12.133 0.70 45.22 ? 281 ARG A NH1 1 ATOM 2072 N NH1 B ARG A 1 248 ? 7.414 19.843 15.798 0.30 31.48 ? 281 ARG A NH1 1 ATOM 2073 N NH2 A ARG A 1 248 ? 8.460 25.583 11.831 0.70 43.11 ? 281 ARG A NH2 1 ATOM 2074 N NH2 B ARG A 1 248 ? 7.340 20.881 13.755 0.30 32.69 ? 281 ARG A NH2 1 ATOM 2075 N N . ILE A 1 249 ? 12.748 23.850 17.983 1.00 18.49 ? 282 ILE A N 1 ATOM 2076 C CA . ILE A 1 249 ? 13.715 23.057 18.773 1.00 17.61 ? 282 ILE A CA 1 ATOM 2077 C C . ILE A 1 249 ? 14.233 23.972 19.905 1.00 18.30 ? 282 ILE A C 1 ATOM 2078 O O . ILE A 1 249 ? 14.223 25.211 19.812 1.00 17.87 ? 282 ILE A O 1 ATOM 2079 C CB . ILE A 1 249 ? 14.886 22.542 17.939 1.00 18.08 ? 282 ILE A CB 1 ATOM 2080 C CG1 . ILE A 1 249 ? 15.711 23.677 17.358 1.00 17.56 ? 282 ILE A CG1 1 ATOM 2081 C CG2 . ILE A 1 249 ? 14.378 21.542 16.894 1.00 19.33 ? 282 ILE A CG2 1 ATOM 2082 C CD1 . ILE A 1 249 ? 16.924 23.172 16.493 1.00 18.28 ? 282 ILE A CD1 1 ATOM 2083 N N . PRO A 1 250 ? 14.744 23.353 20.978 1.00 16.25 ? 283 PRO A N 1 ATOM 2084 C CA . PRO A 1 250 ? 15.331 24.159 22.069 1.00 17.14 ? 283 PRO A CA 1 ATOM 2085 C C . PRO A 1 250 ? 16.637 24.811 21.648 1.00 16.13 ? 283 PRO A C 1 ATOM 2086 O O . PRO A 1 250 ? 17.437 24.183 20.857 1.00 16.54 ? 283 PRO A O 1 ATOM 2087 C CB . PRO A 1 250 ? 15.614 23.111 23.156 1.00 17.01 ? 283 PRO A CB 1 ATOM 2088 C CG . PRO A 1 250 ? 14.615 22.013 22.821 1.00 19.13 ? 283 PRO A CG 1 ATOM 2089 C CD . PRO A 1 250 ? 14.609 21.913 21.335 1.00 17.12 ? 283 PRO A CD 1 ATOM 2090 N N . VAL A 1 251 ? 16.866 25.978 22.219 1.00 16.07 ? 284 VAL A N 1 ATOM 2091 C CA . VAL A 1 251 ? 18.045 26.758 21.939 1.00 15.99 ? 284 VAL A CA 1 ATOM 2092 C C . VAL A 1 251 ? 18.487 27.382 23.231 1.00 15.96 ? 284 VAL A C 1 ATOM 2093 O O . VAL A 1 251 ? 17.621 27.893 23.967 1.00 16.46 ? 284 VAL A O 1 ATOM 2094 C CB . VAL A 1 251 ? 17.748 27.960 21.003 1.00 19.24 ? 284 VAL A CB 1 ATOM 2095 C CG1 . VAL A 1 251 ? 19.076 28.673 20.570 1.00 19.26 ? 284 VAL A CG1 1 ATOM 2096 C CG2 . VAL A 1 251 ? 16.855 27.508 19.861 1.00 21.59 ? 284 VAL A CG2 1 ATOM 2097 N N . HIS A 1 252 ? 19.783 27.331 23.516 1.00 15.64 ? 285 HIS A N 1 ATOM 2098 C CA . HIS A 1 252 ? 20.251 27.947 24.766 1.00 15.21 ? 285 HIS A CA 1 ATOM 2099 C C . HIS A 1 252 ? 21.679 28.412 24.622 1.00 14.10 ? 285 HIS A C 1 ATOM 2100 O O . HIS A 1 252 ? 22.462 27.720 23.976 1.00 14.63 ? 285 HIS A O 1 ATOM 2101 C CB . HIS A 1 252 ? 20.138 26.861 25.888 1.00 15.40 ? 285 HIS A CB 1 ATOM 2102 C CG . HIS A 1 252 ? 20.366 27.414 27.265 1.00 16.36 ? 285 HIS A CG 1 ATOM 2103 N ND1 . HIS A 1 252 ? 19.468 28.295 27.843 1.00 17.99 ? 285 HIS A ND1 1 ATOM 2104 C CD2 . HIS A 1 252 ? 21.397 27.265 28.138 1.00 17.48 ? 285 HIS A CD2 1 ATOM 2105 C CE1 . HIS A 1 252 ? 19.956 28.682 29.030 1.00 18.96 ? 285 HIS A CE1 1 ATOM 2106 N NE2 . HIS A 1 252 ? 21.105 28.065 29.236 1.00 18.52 ? 285 HIS A NE2 1 ATOM 2107 N N . PRO A 1 253 ? 22.067 29.516 25.265 1.00 14.77 ? 286 PRO A N 1 ATOM 2108 C CA . PRO A 1 253 ? 23.421 30.056 25.111 1.00 14.92 ? 286 PRO A CA 1 ATOM 2109 C C . PRO A 1 253 ? 24.278 29.854 26.332 1.00 15.33 ? 286 PRO A C 1 ATOM 2110 O O . PRO A 1 253 ? 23.771 29.841 27.457 1.00 17.73 ? 286 PRO A O 1 ATOM 2111 C CB . PRO A 1 253 ? 23.130 31.567 24.894 1.00 17.10 ? 286 PRO A CB 1 ATOM 2112 C CG . PRO A 1 253 ? 21.990 31.857 25.891 1.00 16.56 ? 286 PRO A CG 1 ATOM 2113 C CD . PRO A 1 253 ? 21.183 30.503 25.926 1.00 14.81 ? 286 PRO A CD 1 ATOM 2114 N N . ILE A 1 254 ? 25.557 29.619 26.048 1.00 15.37 ? 287 ILE A N 1 ATOM 2115 C CA . ILE A 1 254 ? 26.548 29.393 27.082 1.00 15.73 ? 287 ILE A CA 1 ATOM 2116 C C . ILE A 1 254 ? 27.819 30.197 26.829 1.00 15.97 ? 287 ILE A C 1 ATOM 2117 O O . ILE A 1 254 ? 28.106 30.668 25.727 1.00 16.68 ? 287 ILE A O 1 ATOM 2118 C CB . ILE A 1 254 ? 26.930 27.899 27.223 1.00 15.65 ? 287 ILE A CB 1 ATOM 2119 C CG1 . ILE A 1 254 ? 27.612 27.392 25.930 1.00 15.09 ? 287 ILE A CG1 1 ATOM 2120 C CG2 . ILE A 1 254 ? 25.674 27.022 27.585 1.00 16.69 ? 287 ILE A CG2 1 ATOM 2121 C CD1 . ILE A 1 254 ? 28.053 25.908 25.979 1.00 15.92 ? 287 ILE A CD1 1 ATOM 2122 N N . GLY A 1 255 ? 28.571 30.360 27.917 1.00 15.95 ? 288 GLY A N 1 ATOM 2123 C CA . GLY A 1 255 ? 29.840 31.074 27.784 1.00 15.95 ? 288 GLY A CA 1 ATOM 2124 C C . GLY A 1 255 ? 30.948 30.152 27.304 1.00 17.81 ? 288 GLY A C 1 ATOM 2125 O O . GLY A 1 255 ? 30.764 28.950 27.150 1.00 18.19 ? 288 GLY A O 1 ATOM 2126 N N . TYR A 1 256 ? 32.111 30.735 27.030 1.00 17.29 ? 289 TYR A N 1 ATOM 2127 C CA . TYR A 1 256 ? 33.132 29.884 26.415 1.00 17.31 ? 289 TYR A CA 1 ATOM 2128 C C . TYR A 1 256 ? 33.800 28.927 27.378 1.00 17.53 ? 289 TYR A C 1 ATOM 2129 O O . TYR A 1 256 ? 34.402 27.916 26.919 1.00 18.33 ? 289 TYR A O 1 ATOM 2130 C CB . TYR A 1 256 ? 34.116 30.687 25.597 1.00 19.74 ? 289 TYR A CB 1 ATOM 2131 C CG . TYR A 1 256 ? 34.908 31.789 26.273 1.00 19.26 ? 289 TYR A CG 1 ATOM 2132 C CD1 . TYR A 1 256 ? 34.509 33.128 26.050 1.00 19.49 ? 289 TYR A CD1 1 ATOM 2133 C CD2 . TYR A 1 256 ? 36.080 31.540 26.975 1.00 19.28 ? 289 TYR A CD2 1 ATOM 2134 C CE1 . TYR A 1 256 ? 35.257 34.193 26.593 1.00 20.66 ? 289 TYR A CE1 1 ATOM 2135 C CE2 . TYR A 1 256 ? 36.838 32.599 27.526 1.00 18.12 ? 289 TYR A CE2 1 ATOM 2136 C CZ . TYR A 1 256 ? 36.391 33.916 27.323 1.00 20.67 ? 289 TYR A CZ 1 ATOM 2137 O OH . TYR A 1 256 ? 37.102 34.989 27.838 1.00 23.68 ? 289 TYR A OH 1 ATOM 2138 N N . ASN A 1 257 ? 33.782 29.192 28.680 1.00 18.36 ? 290 ASN A N 1 ATOM 2139 C CA . ASN A 1 257 ? 34.337 28.182 29.586 1.00 17.17 ? 290 ASN A CA 1 ATOM 2140 C C . ASN A 1 257 ? 33.520 26.896 29.490 1.00 18.05 ? 290 ASN A C 1 ATOM 2141 O O . ASN A 1 257 ? 34.088 25.804 29.390 1.00 18.24 ? 290 ASN A O 1 ATOM 2142 C CB . ASN A 1 257 ? 34.343 28.608 31.069 1.00 18.76 ? 290 ASN A CB 1 ATOM 2143 C CG . ASN A 1 257 ? 35.308 29.763 31.359 1.00 19.67 ? 290 ASN A CG 1 ATOM 2144 O OD1 . ASN A 1 257 ? 36.200 30.058 30.548 1.00 22.29 ? 290 ASN A OD1 1 ATOM 2145 N ND2 . ASN A 1 257 ? 35.075 30.453 32.518 1.00 20.82 ? 290 ASN A ND2 1 ATOM 2146 N N . ASP A 1 258 ? 32.194 27.041 29.491 1.00 17.90 ? 291 ASP A N 1 ATOM 2147 C CA . ASP A 1 258 ? 31.315 25.848 29.351 1.00 17.11 ? 291 ASP A CA 1 ATOM 2148 C C . ASP A 1 258 ? 31.472 25.223 27.956 1.00 16.07 ? 291 ASP A C 1 ATOM 2149 O O . ASP A 1 258 ? 31.519 23.990 27.827 1.00 16.72 ? 291 ASP A O 1 ATOM 2150 C CB . ASP A 1 258 ? 29.845 26.141 29.647 1.00 17.65 ? 291 ASP A CB 1 ATOM 2151 C CG . ASP A 1 258 ? 29.538 26.347 31.146 1.00 19.91 ? 291 ASP A CG 1 ATOM 2152 O OD1 . ASP A 1 258 ? 30.338 25.860 31.974 1.00 22.18 ? 291 ASP A OD1 1 ATOM 2153 O OD2 . ASP A 1 258 ? 28.491 26.984 31.376 1.00 22.32 ? 291 ASP A OD2 1 ATOM 2154 N N . ALA A 1 259 ? 31.570 26.072 26.914 1.00 15.77 ? 292 ALA A N 1 ATOM 2155 C CA . ALA A 1 259 ? 31.691 25.523 25.552 1.00 15.12 ? 292 ALA A CA 1 ATOM 2156 C C . ALA A 1 259 ? 32.941 24.709 25.405 1.00 15.41 ? 292 ALA A C 1 ATOM 2157 O O . ALA A 1 259 ? 32.958 23.672 24.769 1.00 15.71 ? 292 ALA A O 1 ATOM 2158 C CB . ALA A 1 259 ? 31.682 26.655 24.517 1.00 16.64 ? 292 ALA A CB 1 ATOM 2159 N N . GLU A 1 260 ? 34.025 25.173 26.022 1.00 16.59 ? 293 GLU A N 1 ATOM 2160 C CA . GLU A 1 260 ? 35.293 24.438 25.936 1.00 16.74 ? 293 GLU A CA 1 ATOM 2161 C C . GLU A 1 260 ? 35.145 22.986 26.431 1.00 15.21 ? 293 GLU A C 1 ATOM 2162 O O . GLU A 1 260 ? 35.695 22.034 25.860 1.00 16.04 ? 293 GLU A O 1 ATOM 2163 C CB . GLU A 1 260 ? 36.377 25.187 26.744 1.00 17.34 ? 293 GLU A CB 1 ATOM 2164 C CG . GLU A 1 260 ? 37.767 24.609 26.538 1.00 20.52 ? 293 GLU A CG 1 ATOM 2165 C CD . GLU A 1 260 ? 38.790 25.656 26.964 1.00 29.79 ? 293 GLU A CD 1 ATOM 2166 O OE1 . GLU A 1 260 ? 39.639 26.040 26.135 1.00 34.23 ? 293 GLU A OE1 1 ATOM 2167 O OE2 . GLU A 1 260 ? 38.670 26.132 28.108 1.00 29.68 ? 293 GLU A OE2 1 ATOM 2168 N N . ILE A 1 261 ? 34.430 22.840 27.559 1.00 16.47 ? 294 ILE A N 1 ATOM 2169 C CA . ILE A 1 261 ? 34.198 21.539 28.150 1.00 16.36 ? 294 ILE A CA 1 ATOM 2170 C C . ILE A 1 261 ? 33.400 20.631 27.182 1.00 14.71 ? 294 ILE A C 1 ATOM 2171 O O . ILE A 1 261 ? 33.738 19.452 27.053 1.00 14.93 ? 294 ILE A O 1 ATOM 2172 C CB . ILE A 1 261 ? 33.466 21.701 29.488 1.00 16.54 ? 294 ILE A CB 1 ATOM 2173 C CG1 . ILE A 1 261 ? 34.493 22.265 30.481 1.00 20.23 ? 294 ILE A CG1 1 ATOM 2174 C CG2 . ILE A 1 261 ? 33.005 20.297 29.969 1.00 18.42 ? 294 ILE A CG2 1 ATOM 2175 C CD1 . ILE A 1 261 ? 33.888 22.902 31.695 1.00 24.96 ? 294 ILE A CD1 1 ATOM 2176 N N . LEU A 1 262 ? 32.375 21.202 26.515 1.00 15.45 ? 295 LEU A N 1 ATOM 2177 C CA . LEU A 1 262 ? 31.553 20.439 25.565 1.00 15.19 ? 295 LEU A CA 1 ATOM 2178 C C . LEU A 1 262 ? 32.338 20.075 24.302 1.00 16.43 ? 295 LEU A C 1 ATOM 2179 O O . LEU A 1 262 ? 32.130 19.001 23.741 1.00 16.33 ? 295 LEU A O 1 ATOM 2180 C CB . LEU A 1 262 ? 30.302 21.237 25.156 1.00 14.93 ? 295 LEU A CB 1 ATOM 2181 C CG . LEU A 1 262 ? 29.308 21.339 26.320 1.00 18.17 ? 295 LEU A CG 1 ATOM 2182 C CD1 . LEU A 1 262 ? 28.295 22.457 26.058 1.00 19.32 ? 295 LEU A CD1 1 ATOM 2183 C CD2 . LEU A 1 262 ? 28.558 20.021 26.298 1.00 24.35 ? 295 LEU A CD2 1 ATOM 2184 N N . LEU A 1 263 ? 33.216 20.993 23.850 1.00 15.41 ? 296 LEU A N 1 ATOM 2185 C CA . LEU A 1 263 ? 33.931 20.773 22.572 1.00 16.22 ? 296 LEU A CA 1 ATOM 2186 C C . LEU A 1 263 ? 35.113 19.836 22.692 1.00 15.93 ? 296 LEU A C 1 ATOM 2187 O O . LEU A 1 263 ? 35.519 19.179 21.711 1.00 16.86 ? 296 LEU A O 1 ATOM 2188 C CB . LEU A 1 263 ? 34.454 22.093 21.980 1.00 14.70 ? 296 LEU A CB 1 ATOM 2189 C CG . LEU A 1 263 ? 33.356 23.088 21.559 1.00 16.51 ? 296 LEU A CG 1 ATOM 2190 C CD1 . LEU A 1 263 ? 34.003 24.463 21.273 1.00 18.69 ? 296 LEU A CD1 1 ATOM 2191 C CD2 . LEU A 1 263 ? 32.632 22.530 20.348 1.00 18.06 ? 296 LEU A CD2 1 ATOM 2192 N N . ARG A 1 264 ? 35.678 19.767 23.897 1.00 15.61 ? 297 ARG A N 1 ATOM 2193 C CA . ARG A 1 264 ? 37.002 19.186 24.068 1.00 16.38 ? 297 ARG A CA 1 ATOM 2194 C C . ARG A 1 264 ? 37.126 17.767 23.502 1.00 15.55 ? 297 ARG A C 1 ATOM 2195 O O . ARG A 1 264 ? 38.180 17.420 22.895 1.00 17.36 ? 297 ARG A O 1 ATOM 2196 C CB . ARG A 1 264 ? 37.408 19.252 25.563 1.00 16.86 ? 297 ARG A CB 1 ATOM 2197 C CG . ARG A 1 264 ? 38.720 18.521 25.828 1.00 19.08 ? 297 ARG A CG 1 ATOM 2198 C CD . ARG A 1 264 ? 39.179 18.686 27.256 1.00 25.70 ? 297 ARG A CD 1 ATOM 2199 N NE . ARG A 1 264 ? 39.722 20.037 27.393 1.00 26.89 ? 297 ARG A NE 1 ATOM 2200 C CZ . ARG A 1 264 ? 39.234 20.984 28.194 1.00 31.10 ? 297 ARG A CZ 1 ATOM 2201 N NH1 . ARG A 1 264 ? 39.841 22.169 28.231 1.00 34.69 ? 297 ARG A NH1 1 ATOM 2202 N NH2 . ARG A 1 264 ? 38.144 20.777 28.945 1.00 30.39 ? 297 ARG A NH2 1 ATOM 2203 N N . TYR A 1 265 ? 36.148 16.906 23.758 1.00 16.14 ? 298 TYR A N 1 ATOM 2204 C CA . TYR A 1 265 ? 36.299 15.491 23.393 1.00 16.31 ? 298 TYR A CA 1 ATOM 2205 C C . TYR A 1 265 ? 35.498 15.106 22.167 1.00 16.09 ? 298 TYR A C 1 ATOM 2206 O O . TYR A 1 265 ? 35.393 13.915 21.863 1.00 17.04 ? 298 TYR A O 1 ATOM 2207 C CB . TYR A 1 265 ? 35.884 14.574 24.582 1.00 16.45 ? 298 TYR A CB 1 ATOM 2208 C CG . TYR A 1 265 ? 36.786 14.742 25.752 1.00 19.92 ? 298 TYR A CG 1 ATOM 2209 C CD1 . TYR A 1 265 ? 38.016 14.140 25.745 1.00 21.77 ? 298 TYR A CD1 1 ATOM 2210 C CD2 . TYR A 1 265 ? 36.430 15.528 26.835 1.00 20.90 ? 298 TYR A CD2 1 ATOM 2211 C CE1 . TYR A 1 265 ? 38.900 14.291 26.805 1.00 25.13 ? 298 TYR A CE1 1 ATOM 2212 C CE2 . TYR A 1 265 ? 37.304 15.667 27.926 1.00 25.01 ? 298 TYR A CE2 1 ATOM 2213 C CZ . TYR A 1 265 ? 38.533 15.051 27.862 1.00 23.65 ? 298 TYR A CZ 1 ATOM 2214 O OH . TYR A 1 265 ? 39.452 15.163 28.875 1.00 31.14 ? 298 TYR A OH 1 ATOM 2215 N N . LEU A 1 266 ? 35.069 16.087 21.367 1.00 16.92 ? 299 LEU A N 1 ATOM 2216 C CA . LEU A 1 266 ? 34.455 15.742 20.067 1.00 15.79 ? 299 LEU A CA 1 ATOM 2217 C C . LEU A 1 266 ? 35.443 14.929 19.237 1.00 16.64 ? 299 LEU A C 1 ATOM 2218 O O . LEU A 1 266 ? 36.638 15.259 19.163 1.00 18.33 ? 299 LEU A O 1 ATOM 2219 C CB . LEU A 1 266 ? 34.064 17.013 19.311 1.00 15.45 ? 299 LEU A CB 1 ATOM 2220 C CG . LEU A 1 266 ? 32.746 17.589 19.768 1.00 16.71 ? 299 LEU A CG 1 ATOM 2221 C CD1 . LEU A 1 266 ? 32.486 18.894 19.091 1.00 15.33 ? 299 LEU A CD1 1 ATOM 2222 C CD2 . LEU A 1 266 ? 31.561 16.629 19.456 1.00 19.41 ? 299 LEU A CD2 1 ATOM 2223 N N . GLY A 1 267 ? 34.927 13.890 18.598 1.00 15.83 ? 300 GLY A N 1 ATOM 2224 C CA . GLY A 1 267 ? 35.762 13.022 17.756 1.00 16.26 ? 300 GLY A CA 1 ATOM 2225 C C . GLY A 1 267 ? 35.413 13.218 16.308 1.00 14.67 ? 300 GLY A C 1 ATOM 2226 O O . GLY A 1 267 ? 35.082 14.307 15.895 1.00 16.61 ? 300 GLY A O 1 ATOM 2227 N N . GLY A 1 268 ? 35.504 12.128 15.538 1.00 15.29 ? 301 GLY A N 1 ATOM 2228 C CA . GLY A 1 268 ? 35.163 12.213 14.119 1.00 16.59 ? 301 GLY A CA 1 ATOM 2229 C C . GLY A 1 268 ? 36.147 13.055 13.328 1.00 16.16 ? 301 GLY A C 1 ATOM 2230 O O . GLY A 1 268 ? 37.394 12.956 13.527 1.00 17.07 ? 301 GLY A O 1 ATOM 2231 N N . ILE A 1 269 ? 35.604 13.730 12.327 1.00 17.22 ? 302 ILE A N 1 ATOM 2232 C CA . ILE A 1 269 ? 36.500 14.398 11.398 1.00 18.60 ? 302 ILE A CA 1 ATOM 2233 C C . ILE A 1 269 ? 37.130 15.620 11.994 1.00 16.66 ? 302 ILE A C 1 ATOM 2234 O O . ILE A 1 269 ? 36.510 16.374 12.763 1.00 16.00 ? 302 ILE A O 1 ATOM 2235 C CB . ILE A 1 269 ? 35.871 14.742 10.034 1.00 21.91 ? 302 ILE A CB 1 ATOM 2236 C CG1 . ILE A 1 269 ? 34.752 15.682 10.221 1.00 23.43 ? 302 ILE A CG1 1 ATOM 2237 C CG2 . ILE A 1 269 ? 35.436 13.456 9.284 1.00 24.39 ? 302 ILE A CG2 1 ATOM 2238 C CD1 . ILE A 1 269 ? 34.366 16.314 8.837 1.00 29.76 ? 302 ILE A CD1 1 ATOM 2239 N N . ALA A 1 270 ? 38.385 15.828 11.616 1.00 15.26 ? 303 ALA A N 1 ATOM 2240 C CA . ALA A 1 270 ? 39.136 17.015 12.012 1.00 14.93 ? 303 ALA A CA 1 ATOM 2241 C C . ALA A 1 270 ? 38.496 18.286 11.443 1.00 14.45 ? 303 ALA A C 1 ATOM 2242 O O . ALA A 1 270 ? 37.776 18.230 10.444 1.00 15.61 ? 303 ALA A O 1 ATOM 2243 C CB . ALA A 1 270 ? 40.562 16.888 11.497 1.00 15.47 ? 303 ALA A CB 1 ATOM 2244 N N . PRO A 1 271 ? 38.731 19.469 12.068 1.00 14.30 ? 304 PRO A N 1 ATOM 2245 C CA . PRO A 1 271 ? 38.210 20.702 11.437 1.00 14.88 ? 304 PRO A CA 1 ATOM 2246 C C . PRO A 1 271 ? 38.731 20.757 9.987 1.00 14.60 ? 304 PRO A C 1 ATOM 2247 O O . PRO A 1 271 ? 39.887 20.457 9.736 1.00 15.94 ? 304 PRO A O 1 ATOM 2248 C CB . PRO A 1 271 ? 38.813 21.803 12.315 1.00 16.78 ? 304 PRO A CB 1 ATOM 2249 C CG . PRO A 1 271 ? 40.022 21.187 12.923 1.00 17.47 ? 304 PRO A CG 1 ATOM 2250 C CD . PRO A 1 271 ? 39.617 19.746 13.216 1.00 16.21 ? 304 PRO A CD 1 ATOM 2251 N N . PRO A 1 272 ? 37.838 21.155 9.062 1.00 15.31 ? 305 PRO A N 1 ATOM 2252 C CA . PRO A 1 272 ? 38.207 20.976 7.648 1.00 17.80 ? 305 PRO A CA 1 ATOM 2253 C C . PRO A 1 272 ? 39.237 21.985 7.173 1.00 18.85 ? 305 PRO A C 1 ATOM 2254 O O . PRO A 1 272 ? 39.948 21.676 6.201 1.00 19.16 ? 305 PRO A O 1 ATOM 2255 C CB . PRO A 1 272 ? 36.880 21.221 6.913 1.00 18.51 ? 305 PRO A CB 1 ATOM 2256 C CG . PRO A 1 272 ? 36.005 21.909 7.851 1.00 22.43 ? 305 PRO A CG 1 ATOM 2257 C CD . PRO A 1 272 ? 36.384 21.316 9.202 1.00 17.87 ? 305 PRO A CD 1 ATOM 2258 N N . ASP A 1 273 ? 39.276 23.156 7.802 1.00 17.67 ? 306 ASP A N 1 ATOM 2259 C CA . ASP A 1 273 ? 40.254 24.181 7.503 1.00 19.97 ? 306 ASP A CA 1 ATOM 2260 C C . ASP A 1 273 ? 40.222 25.161 8.667 1.00 19.07 ? 306 ASP A C 1 ATOM 2261 O O . ASP A 1 273 ? 39.364 25.044 9.581 1.00 17.76 ? 306 ASP A O 1 ATOM 2262 C CB . ASP A 1 273 ? 39.935 24.865 6.147 1.00 18.92 ? 306 ASP A CB 1 ATOM 2263 C CG . ASP A 1 273 ? 38.598 25.591 6.159 1.00 23.40 ? 306 ASP A CG 1 ATOM 2264 O OD1 . ASP A 1 273 ? 38.430 26.488 6.988 1.00 27.96 ? 306 ASP A OD1 1 ATOM 2265 O OD2 . ASP A 1 273 ? 37.725 25.184 5.378 1.00 28.07 ? 306 ASP A OD2 1 ATOM 2266 N N . LYS A 1 274 ? 41.141 26.119 8.672 1.00 20.14 ? 307 LYS A N 1 ATOM 2267 C CA . LYS A 1 274 ? 41.258 27.102 9.746 1.00 21.87 ? 307 LYS A CA 1 ATOM 2268 C C . LYS A 1 274 ? 40.004 27.932 9.957 1.00 21.49 ? 307 LYS A C 1 ATOM 2269 O O . LYS A 1 274 ? 39.843 28.439 11.119 1.00 22.73 ? 307 LYS A O 1 ATOM 2270 C CB . LYS A 1 274 ? 42.463 28.017 9.505 1.00 23.75 ? 307 LYS A CB 1 ATOM 2271 C CG . LYS A 1 274 ? 43.749 27.333 9.728 1.00 24.19 ? 307 LYS A CG 1 ATOM 2272 C CD . LYS A 1 274 ? 44.974 28.255 9.609 1.00 31.05 ? 307 LYS A CD 1 ATOM 2273 C CE . LYS A 1 274 ? 44.960 29.002 8.313 1.00 36.63 ? 307 LYS A CE 1 ATOM 2274 N NZ . LYS A 1 274 ? 46.367 29.485 7.990 1.00 38.35 ? 307 LYS A NZ 1 ATOM 2275 N N . SER A 1 275 ? 39.139 28.029 8.944 1.00 20.14 ? 308 SER A N 1 ATOM 2276 C CA . SER A 1 275 ? 37.889 28.835 9.064 1.00 21.53 ? 308 SER A CA 1 ATOM 2277 C C . SER A 1 275 ? 36.848 28.180 9.962 1.00 22.19 ? 308 SER A C 1 ATOM 2278 O O . SER A 1 275 ? 35.809 28.796 10.282 1.00 23.76 ? 308 SER A O 1 ATOM 2279 C CB . SER A 1 275 ? 37.234 29.116 7.712 1.00 18.92 ? 308 SER A CB 1 ATOM 2280 O OG . SER A 1 275 ? 36.469 28.065 7.121 1.00 25.09 ? 308 SER A OG 1 ATOM 2281 N N . TRP A 1 276 ? 37.128 26.941 10.373 1.00 20.51 ? 309 TRP A N 1 ATOM 2282 C CA . TRP A 1 276 ? 36.255 26.218 11.343 1.00 19.61 ? 309 TRP A CA 1 ATOM 2283 C C . TRP A 1 276 ? 36.842 26.254 12.725 1.00 19.92 ? 309 TRP A C 1 ATOM 2284 O O . TRP A 1 276 ? 36.151 25.840 13.671 1.00 19.12 ? 309 TRP A O 1 ATOM 2285 C CB . TRP A 1 276 ? 36.088 24.754 10.883 1.00 19.20 ? 309 TRP A CB 1 ATOM 2286 C CG . TRP A 1 276 ? 34.988 24.636 9.829 1.00 19.99 ? 309 TRP A CG 1 ATOM 2287 C CD1 . TRP A 1 276 ? 35.003 25.190 8.536 1.00 22.19 ? 309 TRP A CD1 1 ATOM 2288 C CD2 . TRP A 1 276 ? 33.695 24.009 9.951 1.00 18.70 ? 309 TRP A CD2 1 ATOM 2289 N NE1 . TRP A 1 276 ? 33.813 24.914 7.878 1.00 24.37 ? 309 TRP A NE1 1 ATOM 2290 C CE2 . TRP A 1 276 ? 32.990 24.199 8.723 1.00 24.37 ? 309 TRP A CE2 1 ATOM 2291 C CE3 . TRP A 1 276 ? 33.061 23.273 10.973 1.00 20.01 ? 309 TRP A CE3 1 ATOM 2292 C CZ2 . TRP A 1 276 ? 31.690 23.710 8.525 1.00 23.31 ? 309 TRP A CZ2 1 ATOM 2293 C CZ3 . TRP A 1 276 ? 31.786 22.787 10.774 1.00 20.15 ? 309 TRP A CZ3 1 ATOM 2294 C CH2 . TRP A 1 276 ? 31.105 22.996 9.551 1.00 23.43 ? 309 TRP A CH2 1 ATOM 2295 N N . LYS A 1 277 ? 38.072 26.716 12.902 1.00 19.61 ? 310 LYS A N 1 ATOM 2296 C CA . LYS A 1 277 ? 38.773 26.573 14.173 1.00 20.99 ? 310 LYS A CA 1 ATOM 2297 C C . LYS A 1 277 ? 38.708 27.900 14.905 1.00 23.12 ? 310 LYS A C 1 ATOM 2298 O O . LYS A 1 277 ? 39.148 28.936 14.379 1.00 25.95 ? 310 LYS A O 1 ATOM 2299 C CB . LYS A 1 277 ? 40.233 26.084 14.003 1.00 20.78 ? 310 LYS A CB 1 ATOM 2300 C CG . LYS A 1 277 ? 40.913 25.721 15.321 1.00 24.43 ? 310 LYS A CG 1 ATOM 2301 C CD . LYS A 1 277 ? 42.183 24.916 15.071 1.00 24.50 ? 310 LYS A CD 1 ATOM 2302 C CE . LYS A 1 277 ? 42.825 24.370 16.319 1.00 28.78 ? 310 LYS A CE 1 ATOM 2303 N NZ . LYS A 1 277 ? 43.418 25.395 17.184 1.00 36.65 ? 310 LYS A NZ 1 ATOM 2304 N N . GLY A 1 278 ? 38.080 27.921 16.084 1.00 20.57 ? 311 GLY A N 1 ATOM 2305 C CA . GLY A 1 278 ? 38.102 29.108 16.930 1.00 20.12 ? 311 GLY A CA 1 ATOM 2306 C C . GLY A 1 278 ? 39.340 29.180 17.804 1.00 20.77 ? 311 GLY A C 1 ATOM 2307 O O . GLY A 1 278 ? 40.381 28.605 17.475 1.00 21.56 ? 311 GLY A O 1 ATOM 2308 N N . ALA A 1 279 ? 39.241 29.853 18.954 1.00 20.14 ? 312 ALA A N 1 ATOM 2309 C CA . ALA A 1 279 ? 40.412 30.188 19.753 1.00 20.23 ? 312 ALA A CA 1 ATOM 2310 C C . ALA A 1 279 ? 40.571 29.418 21.061 1.00 18.30 ? 312 ALA A C 1 ATOM 2311 O O . ALA A 1 279 ? 41.561 29.605 21.780 1.00 21.18 ? 312 ALA A O 1 ATOM 2312 C CB . ALA A 1 279 ? 40.412 31.699 20.016 1.00 21.42 ? 312 ALA A CB 1 ATOM 2313 N N . LEU A 1 280 ? 39.602 28.552 21.381 1.00 18.96 ? 313 LEU A N 1 ATOM 2314 C CA . LEU A 1 280 ? 39.720 27.772 22.611 1.00 17.10 ? 313 LEU A CA 1 ATOM 2315 C C . LEU A 1 280 ? 40.788 26.686 22.447 1.00 18.47 ? 313 LEU A C 1 ATOM 2316 O O . LEU A 1 280 ? 41.180 26.328 21.334 1.00 17.76 ? 313 LEU A O 1 ATOM 2317 C CB . LEU A 1 280 ? 38.365 27.116 22.923 1.00 16.94 ? 313 LEU A CB 1 ATOM 2318 C CG . LEU A 1 280 ? 37.260 28.181 23.220 1.00 16.65 ? 313 LEU A CG 1 ATOM 2319 C CD1 . LEU A 1 280 ? 35.898 27.524 23.276 1.00 18.34 ? 313 LEU A CD1 1 ATOM 2320 C CD2 . LEU A 1 280 ? 37.562 28.886 24.553 1.00 20.54 ? 313 LEU A CD2 1 ATOM 2321 N N . ASN A 1 281 ? 41.197 26.141 23.582 1.00 18.68 ? 314 ASN A N 1 ATOM 2322 C CA . ASN A 1 281 ? 42.274 25.130 23.581 1.00 20.01 ? 314 ASN A CA 1 ATOM 2323 C C . ASN A 1 281 ? 41.686 23.743 23.344 1.00 19.21 ? 314 ASN A C 1 ATOM 2324 O O . ASN A 1 281 ? 41.884 22.811 24.161 1.00 19.57 ? 314 ASN A O 1 ATOM 2325 C CB . ASN A 1 281 ? 43.045 25.184 24.907 1.00 20.82 ? 314 ASN A CB 1 ATOM 2326 C CG . ASN A 1 281 ? 44.229 24.295 24.921 1.00 24.05 ? 314 ASN A CG 1 ATOM 2327 O OD1 . ASN A 1 281 ? 44.809 24.030 23.878 1.00 26.69 ? 314 ASN A OD1 1 ATOM 2328 N ND2 . ASN A 1 281 ? 44.556 23.771 26.092 1.00 27.16 ? 314 ASN A ND2 1 ATOM 2329 N N . VAL A 1 282 ? 40.991 23.592 22.213 1.00 17.86 ? 315 VAL A N 1 ATOM 2330 C CA . VAL A 1 282 ? 40.367 22.318 21.825 1.00 17.50 ? 315 VAL A CA 1 ATOM 2331 C C . VAL A 1 282 ? 40.591 22.111 20.340 1.00 17.30 ? 315 VAL A C 1 ATOM 2332 O O . VAL A 1 282 ? 40.997 23.065 19.614 1.00 16.59 ? 315 VAL A O 1 ATOM 2333 C CB . VAL A 1 282 ? 38.860 22.252 22.110 1.00 15.96 ? 315 VAL A CB 1 ATOM 2334 C CG1 . VAL A 1 282 ? 38.607 22.361 23.684 1.00 18.70 ? 315 VAL A CG1 1 ATOM 2335 C CG2 . VAL A 1 282 ? 38.117 23.347 21.336 1.00 18.04 ? 315 VAL A CG2 1 ATOM 2336 N N . SER A 1 283 ? 40.290 20.901 19.862 1.00 15.89 ? 316 SER A N 1 ATOM 2337 C CA . SER A 1 283 ? 40.647 20.545 18.468 1.00 16.15 ? 316 SER A CA 1 ATOM 2338 C C . SER A 1 283 ? 39.719 21.167 17.433 1.00 16.79 ? 316 SER A C 1 ATOM 2339 O O . SER A 1 283 ? 40.133 21.322 16.268 1.00 16.81 ? 316 SER A O 1 ATOM 2340 C CB . SER A 1 283 ? 40.655 19.028 18.287 1.00 16.53 ? 316 SER A CB 1 ATOM 2341 O OG . SER A 1 283 ? 39.377 18.476 18.310 1.00 19.79 ? 316 SER A OG 1 ATOM 2342 N N . TYR A 1 284 ? 38.481 21.466 17.786 1.00 14.30 ? 317 TYR A N 1 ATOM 2343 C CA . TYR A 1 284 ? 37.478 21.915 16.823 1.00 14.75 ? 317 TYR A CA 1 ATOM 2344 C C . TYR A 1 284 ? 37.155 20.784 15.836 1.00 14.90 ? 317 TYR A C 1 ATOM 2345 O O . TYR A 1 284 ? 36.653 21.030 14.695 1.00 16.46 ? 317 TYR A O 1 ATOM 2346 C CB . TYR A 1 284 ? 37.774 23.267 16.148 1.00 16.02 ? 317 TYR A CB 1 ATOM 2347 C CG . TYR A 1 284 ? 37.626 24.402 17.145 1.00 15.16 ? 317 TYR A CG 1 ATOM 2348 C CD1 . TYR A 1 284 ? 36.413 25.092 17.332 1.00 15.82 ? 317 TYR A CD1 1 ATOM 2349 C CD2 . TYR A 1 284 ? 38.724 24.799 17.896 1.00 16.30 ? 317 TYR A CD2 1 ATOM 2350 C CE1 . TYR A 1 284 ? 36.322 26.104 18.311 1.00 16.20 ? 317 TYR A CE1 1 ATOM 2351 C CE2 . TYR A 1 284 ? 38.641 25.809 18.882 1.00 16.10 ? 317 TYR A CE2 1 ATOM 2352 C CZ . TYR A 1 284 ? 37.454 26.486 19.033 1.00 14.66 ? 317 TYR A CZ 1 ATOM 2353 O OH . TYR A 1 284 ? 37.321 27.503 19.991 1.00 16.36 ? 317 TYR A OH 1 ATOM 2354 N N . SER A 1 285 ? 37.344 19.529 16.280 1.00 15.83 ? 318 SER A N 1 ATOM 2355 C CA . SER A 1 285 ? 36.759 18.393 15.531 1.00 14.93 ? 318 SER A CA 1 ATOM 2356 C C . SER A 1 285 ? 35.257 18.476 15.492 1.00 15.44 ? 318 SER A C 1 ATOM 2357 O O . SER A 1 285 ? 34.612 19.137 16.362 1.00 16.41 ? 318 SER A O 1 ATOM 2358 C CB . SER A 1 285 ? 37.176 17.061 16.170 1.00 14.38 ? 318 SER A CB 1 ATOM 2359 O OG . SER A 1 285 ? 38.597 16.899 16.044 1.00 15.91 ? 318 SER A OG 1 ATOM 2360 N N . ILE A 1 286 ? 34.660 17.809 14.507 1.00 15.34 ? 319 ILE A N 1 ATOM 2361 C CA . ILE A 1 286 ? 33.266 18.009 14.219 1.00 17.17 ? 319 ILE A CA 1 ATOM 2362 C C . ILE A 1 286 ? 32.313 17.086 14.972 1.00 17.53 ? 319 ILE A C 1 ATOM 2363 O O . ILE A 1 286 ? 31.143 17.480 15.195 1.00 17.40 ? 319 ILE A O 1 ATOM 2364 C CB . ILE A 1 286 ? 33.037 17.799 12.662 1.00 17.98 ? 319 ILE A CB 1 ATOM 2365 C CG1 . ILE A 1 286 ? 33.849 18.817 11.834 1.00 23.82 ? 319 ILE A CG1 1 ATOM 2366 C CG2 . ILE A 1 286 ? 31.555 17.934 12.236 1.00 20.19 ? 319 ILE A CG2 1 ATOM 2367 C CD1 . ILE A 1 286 ? 33.957 20.220 12.392 1.00 26.35 ? 319 ILE A CD1 1 ATOM 2368 N N . GLY A 1 287 ? 32.783 15.914 15.343 1.00 17.71 ? 320 GLY A N 1 ATOM 2369 C CA . GLY A 1 287 ? 31.873 14.867 15.754 1.00 19.18 ? 320 GLY A CA 1 ATOM 2370 C C . GLY A 1 287 ? 31.325 14.164 14.530 1.00 21.22 ? 320 GLY A C 1 ATOM 2371 O O . GLY A 1 287 ? 32.043 14.037 13.516 1.00 24.75 ? 320 GLY A O 1 ATOM 2372 N N . PRO A 1 288 ? 30.156 13.547 14.667 1.00 21.20 ? 321 PRO A N 1 ATOM 2373 C CA . PRO A 1 288 ? 29.350 13.391 15.887 1.00 21.70 ? 321 PRO A CA 1 ATOM 2374 C C . PRO A 1 288 ? 30.030 12.534 16.929 1.00 21.12 ? 321 PRO A C 1 ATOM 2375 O O . PRO A 1 288 ? 30.828 11.630 16.581 1.00 22.88 ? 321 PRO A O 1 ATOM 2376 C CB . PRO A 1 288 ? 28.056 12.679 15.417 1.00 21.33 ? 321 PRO A CB 1 ATOM 2377 C CG . PRO A 1 288 ? 28.298 12.234 14.071 1.00 26.15 ? 321 PRO A CG 1 ATOM 2378 C CD . PRO A 1 288 ? 29.537 12.915 13.489 1.00 23.46 ? 321 PRO A CD 1 ATOM 2379 N N . GLY A 1 289 ? 29.666 12.806 18.185 1.00 22.18 ? 322 GLY A N 1 ATOM 2380 C CA . GLY A 1 289 ? 30.087 12.008 19.314 1.00 22.49 ? 322 GLY A CA 1 ATOM 2381 C C . GLY A 1 289 ? 31.432 12.368 19.877 1.00 22.58 ? 322 GLY A C 1 ATOM 2382 O O . GLY A 1 289 ? 32.188 13.145 19.294 1.00 20.70 ? 322 GLY A O 1 ATOM 2383 N N . PHE A 1 290 ? 31.742 11.736 21.005 1.00 20.98 ? 323 PHE A N 1 ATOM 2384 C CA . PHE A 1 290 ? 32.965 11.995 21.745 1.00 20.56 ? 323 PHE A CA 1 ATOM 2385 C C . PHE A 1 290 ? 33.924 10.868 21.611 1.00 22.94 ? 323 PHE A C 1 ATOM 2386 O O . PHE A 1 290 ? 33.528 9.728 21.344 1.00 25.86 ? 323 PHE A O 1 ATOM 2387 C CB . PHE A 1 290 ? 32.635 12.156 23.226 1.00 19.75 ? 323 PHE A CB 1 ATOM 2388 C CG . PHE A 1 290 ? 31.707 13.327 23.519 1.00 18.74 ? 323 PHE A CG 1 ATOM 2389 C CD1 . PHE A 1 290 ? 30.521 13.159 24.268 1.00 20.84 ? 323 PHE A CD1 1 ATOM 2390 C CD2 . PHE A 1 290 ? 32.029 14.617 23.097 1.00 18.36 ? 323 PHE A CD2 1 ATOM 2391 C CE1 . PHE A 1 290 ? 29.713 14.211 24.596 1.00 23.18 ? 323 PHE A CE1 1 ATOM 2392 C CE2 . PHE A 1 290 ? 31.206 15.722 23.401 1.00 18.81 ? 323 PHE A CE2 1 ATOM 2393 C CZ . PHE A 1 290 ? 30.028 15.534 24.146 1.00 19.25 ? 323 PHE A CZ 1 ATOM 2394 N N . THR A 1 291 ? 35.189 11.184 21.837 1.00 21.63 ? 324 THR A N 1 ATOM 2395 C CA . THR A 1 291 ? 36.229 10.157 21.887 1.00 24.51 ? 324 THR A CA 1 ATOM 2396 C C . THR A 1 291 ? 37.226 10.519 22.974 1.00 25.14 ? 324 THR A C 1 ATOM 2397 O O . THR A 1 291 ? 37.458 11.678 23.265 1.00 26.17 ? 324 THR A O 1 ATOM 2398 C CB . THR A 1 291 ? 36.908 10.047 20.518 1.00 24.83 ? 324 THR A CB 1 ATOM 2399 O OG1 . THR A 1 291 ? 37.766 8.902 20.530 1.00 29.87 ? 324 THR A OG1 1 ATOM 2400 C CG2 . THR A 1 291 ? 37.786 11.265 20.251 1.00 25.85 ? 324 THR A CG2 1 ATOM 2401 N N . GLY A 1 292 ? 37.862 9.523 23.602 1.00 26.07 ? 325 GLY A N 1 ATOM 2402 C CA . GLY A 1 292 ? 38.925 9.852 24.543 1.00 26.55 ? 325 GLY A CA 1 ATOM 2403 C C . GLY A 1 292 ? 38.505 10.279 25.943 1.00 28.11 ? 325 GLY A C 1 ATOM 2404 O O . GLY A 1 292 ? 39.338 10.771 26.721 1.00 29.00 ? 325 GLY A O 1 ATOM 2405 N N . SER A 1 293 ? 37.225 10.097 26.282 1.00 27.40 ? 326 SER A N 1 ATOM 2406 C CA . SER A 1 293 ? 36.735 10.461 27.617 1.00 28.91 ? 326 SER A CA 1 ATOM 2407 C C . SER A 1 293 ? 36.363 9.182 28.364 1.00 29.43 ? 326 SER A C 1 ATOM 2408 O O . SER A 1 293 ? 35.519 8.410 27.891 1.00 29.04 ? 326 SER A O 1 ATOM 2409 C CB . SER A 1 293 ? 35.506 11.353 27.525 1.00 28.48 ? 326 SER A CB 1 ATOM 2410 O OG . SER A 1 293 ? 35.077 11.821 28.813 1.00 30.96 ? 326 SER A OG 1 ATOM 2411 N N . SER A 1 295 ? 33.933 9.218 30.473 1.00 24.57 ? 328 SER A N 1 ATOM 2412 C CA . SER A 1 295 ? 32.574 9.384 30.941 1.00 22.64 ? 328 SER A CA 1 ATOM 2413 C C . SER A 1 295 ? 31.673 10.210 30.019 1.00 22.71 ? 328 SER A C 1 ATOM 2414 O O . SER A 1 295 ? 30.468 10.242 30.197 1.00 23.27 ? 328 SER A O 1 ATOM 2415 C CB . SER A 1 295 ? 32.593 10.062 32.290 1.00 22.68 ? 328 SER A CB 1 ATOM 2416 O OG . SER A 1 295 ? 32.965 9.083 33.284 1.00 28.48 ? 328 SER A OG 1 ATOM 2417 N N . PHE A 1 296 ? 32.235 10.956 29.066 1.00 22.15 ? 329 PHE A N 1 ATOM 2418 C CA . PHE A 1 296 ? 31.372 11.801 28.224 1.00 22.15 ? 329 PHE A CA 1 ATOM 2419 C C . PHE A 1 296 ? 30.772 10.966 27.136 1.00 20.41 ? 329 PHE A C 1 ATOM 2420 O O . PHE A 1 296 ? 31.505 10.435 26.262 1.00 21.68 ? 329 PHE A O 1 ATOM 2421 C CB . PHE A 1 296 ? 32.201 12.933 27.577 1.00 22.10 ? 329 PHE A CB 1 ATOM 2422 C CG . PHE A 1 296 ? 32.489 14.117 28.507 1.00 25.64 ? 329 PHE A CG 1 ATOM 2423 C CD1 . PHE A 1 296 ? 32.550 13.988 29.902 1.00 28.48 ? 329 PHE A CD1 1 ATOM 2424 C CD2 . PHE A 1 296 ? 32.732 15.375 27.970 1.00 26.54 ? 329 PHE A CD2 1 ATOM 2425 C CE1 . PHE A 1 296 ? 32.833 15.098 30.727 1.00 27.73 ? 329 PHE A CE1 1 ATOM 2426 C CE2 . PHE A 1 296 ? 33.036 16.454 28.785 1.00 26.48 ? 329 PHE A CE2 1 ATOM 2427 C CZ . PHE A 1 296 ? 33.067 16.318 30.180 1.00 30.30 ? 329 PHE A CZ 1 ATOM 2428 N N . ARG A 1 297 ? 29.445 10.844 27.146 1.00 18.93 ? 330 ARG A N 1 ATOM 2429 C CA . ARG A 1 297 ? 28.786 9.962 26.152 1.00 18.48 ? 330 ARG A CA 1 ATOM 2430 C C . ARG A 1 297 ? 27.715 10.649 25.357 1.00 19.35 ? 330 ARG A C 1 ATOM 2431 O O . ARG A 1 297 ? 27.674 10.516 24.121 1.00 22.28 ? 330 ARG A O 1 ATOM 2432 C CB . ARG A 1 297 ? 28.205 8.693 26.763 1.00 20.42 ? 330 ARG A CB 1 ATOM 2433 C CG A ARG A 1 297 ? 29.248 7.625 27.091 0.65 23.31 ? 330 ARG A CG 1 ATOM 2434 C CG B ARG A 1 297 ? 29.253 7.846 27.488 0.35 16.61 ? 330 ARG A CG 1 ATOM 2435 C CD A ARG A 1 297 ? 29.807 6.906 25.834 0.65 27.13 ? 330 ARG A CD 1 ATOM 2436 C CD B ARG A 1 297 ? 30.249 7.249 26.476 0.35 12.94 ? 330 ARG A CD 1 ATOM 2437 N NE A ARG A 1 297 ? 30.650 5.768 26.229 0.65 34.33 ? 330 ARG A NE 1 ATOM 2438 N NE B ARG A 1 297 ? 31.228 6.343 27.098 0.35 15.09 ? 330 ARG A NE 1 ATOM 2439 C CZ A ARG A 1 297 ? 30.280 4.484 26.203 0.65 35.51 ? 330 ARG A CZ 1 ATOM 2440 C CZ B ARG A 1 297 ? 32.400 6.739 27.572 0.35 17.44 ? 330 ARG A CZ 1 ATOM 2441 N NH1 A ARG A 1 297 ? 29.076 4.122 25.765 0.65 37.80 ? 330 ARG A NH1 1 ATOM 2442 N NH1 B ARG A 1 297 ? 33.250 5.862 28.105 0.35 18.46 ? 330 ARG A NH1 1 ATOM 2443 N NH2 A ARG A 1 297 ? 31.135 3.555 26.603 0.65 36.57 ? 330 ARG A NH2 1 ATOM 2444 N NH2 B ARG A 1 297 ? 32.716 8.020 27.532 0.35 15.69 ? 330 ARG A NH2 1 ATOM 2445 N N . LYS A 1 298 ? 26.829 11.349 26.047 1.00 16.88 ? 331 LYS A N 1 ATOM 2446 C CA . LYS A 1 298 ? 25.740 12.054 25.328 1.00 17.00 ? 331 LYS A CA 1 ATOM 2447 C C . LYS A 1 298 ? 25.550 13.412 25.880 1.00 16.25 ? 331 LYS A C 1 ATOM 2448 O O . LYS A 1 298 ? 25.851 13.678 27.055 1.00 17.71 ? 331 LYS A O 1 ATOM 2449 C CB . LYS A 1 298 ? 24.369 11.318 25.422 1.00 18.26 ? 331 LYS A CB 1 ATOM 2450 C CG . LYS A 1 298 ? 24.326 9.922 24.774 1.00 21.80 ? 331 LYS A CG 1 ATOM 2451 C CD . LYS A 1 298 ? 24.074 10.007 23.277 1.00 25.81 ? 331 LYS A CD 1 ATOM 2452 C CE . LYS A 1 298 ? 24.249 8.605 22.689 1.00 31.65 ? 331 LYS A CE 1 ATOM 2453 N NZ . LYS A 1 298 ? 24.043 8.608 21.197 1.00 35.41 ? 331 LYS A NZ 1 ATOM 2454 N N . VAL A 1 299 ? 25.010 14.324 25.074 1.00 15.33 ? 332 VAL A N 1 ATOM 2455 C CA . VAL A 1 299 ? 24.650 15.643 25.572 1.00 15.61 ? 332 VAL A CA 1 ATOM 2456 C C . VAL A 1 299 ? 23.134 15.795 25.727 1.00 16.33 ? 332 VAL A C 1 ATOM 2457 O O . VAL A 1 299 ? 22.389 15.212 24.932 1.00 17.31 ? 332 VAL A O 1 ATOM 2458 C CB . VAL A 1 299 ? 25.218 16.751 24.563 1.00 16.04 ? 332 VAL A CB 1 ATOM 2459 C CG1 A VAL A 1 299 ? 24.692 18.154 24.921 0.34 10.23 ? 332 VAL A CG1 1 ATOM 2460 C CG1 B VAL A 1 299 ? 26.716 16.766 24.684 0.33 15.61 ? 332 VAL A CG1 1 ATOM 2461 C CG1 C VAL A 1 299 ? 24.399 16.793 23.288 0.33 18.96 ? 332 VAL A CG1 1 ATOM 2462 C CG2 A VAL A 1 299 ? 26.727 16.631 24.518 0.34 13.28 ? 332 VAL A CG2 1 ATOM 2463 C CG2 B VAL A 1 299 ? 24.852 16.433 23.121 0.33 18.69 ? 332 VAL A CG2 1 ATOM 2464 C CG2 C VAL A 1 299 ? 25.226 18.110 25.184 0.33 14.39 ? 332 VAL A CG2 1 ATOM 2465 N N . ARG A 1 300 ? 22.717 16.484 26.775 1.00 16.04 ? 333 ARG A N 1 ATOM 2466 C CA . ARG A 1 300 ? 21.320 16.781 26.984 1.00 16.72 ? 333 ARG A CA 1 ATOM 2467 C C . ARG A 1 300 ? 21.095 18.296 27.072 1.00 17.21 ? 333 ARG A C 1 ATOM 2468 O O . ARG A 1 300 ? 21.893 19.028 27.633 1.00 19.13 ? 333 ARG A O 1 ATOM 2469 C CB A ARG A 1 300 ? 20.837 16.064 28.257 0.65 17.99 ? 333 ARG A CB 1 ATOM 2470 C CB B ARG A 1 300 ? 20.848 16.179 28.313 0.35 16.88 ? 333 ARG A CB 1 ATOM 2471 C CG A ARG A 1 300 ? 20.805 14.567 28.136 0.65 23.74 ? 333 ARG A CG 1 ATOM 2472 C CG B ARG A 1 300 ? 21.063 14.720 28.487 0.35 16.92 ? 333 ARG A CG 1 ATOM 2473 C CD A ARG A 1 300 ? 20.467 13.944 29.464 0.65 32.23 ? 333 ARG A CD 1 ATOM 2474 C CD B ARG A 1 300 ? 20.574 14.292 29.850 0.35 14.68 ? 333 ARG A CD 1 ATOM 2475 N NE A ARG A 1 300 ? 19.063 14.066 29.828 0.65 34.76 ? 333 ARG A NE 1 ATOM 2476 N NE B ARG A 1 300 ? 20.211 12.878 29.829 0.35 12.33 ? 333 ARG A NE 1 ATOM 2477 C CZ A ARG A 1 300 ? 18.572 13.580 30.970 0.65 40.09 ? 333 ARG A CZ 1 ATOM 2478 C CZ B ARG A 1 300 ? 19.960 12.175 30.922 0.35 13.41 ? 333 ARG A CZ 1 ATOM 2479 N NH1 A ARG A 1 300 ? 19.387 12.972 31.833 0.65 37.47 ? 333 ARG A NH1 1 ATOM 2480 N NH1 B ARG A 1 300 ? 20.094 12.751 32.115 0.35 15.91 ? 333 ARG A NH1 1 ATOM 2481 N NH2 A ARG A 1 300 ? 17.277 13.715 31.261 0.65 42.51 ? 333 ARG A NH2 1 ATOM 2482 N NH2 B ARG A 1 300 ? 19.637 10.908 30.810 0.35 14.62 ? 333 ARG A NH2 1 ATOM 2483 N N . MET A 1 301 ? 19.997 18.751 26.521 1.00 16.85 ? 334 MET A N 1 ATOM 2484 C CA . MET A 1 301 ? 19.550 20.098 26.871 1.00 15.61 ? 334 MET A CA 1 ATOM 2485 C C . MET A 1 301 ? 18.312 20.035 27.737 1.00 17.57 ? 334 MET A C 1 ATOM 2486 O O . MET A 1 301 ? 17.532 19.042 27.621 1.00 19.06 ? 334 MET A O 1 ATOM 2487 C CB . MET A 1 301 ? 19.219 20.923 25.593 1.00 16.12 ? 334 MET A CB 1 ATOM 2488 C CG . MET A 1 301 ? 20.336 20.936 24.591 1.00 15.02 ? 334 MET A CG 1 ATOM 2489 S SD . MET A 1 301 ? 19.952 21.837 23.080 1.00 17.89 ? 334 MET A SD 1 ATOM 2490 C CE . MET A 1 301 ? 19.842 23.529 23.744 1.00 17.15 ? 334 MET A CE 1 ATOM 2491 N N . HIS A 1 302 ? 18.092 21.106 28.544 1.00 17.04 ? 335 HIS A N 1 ATOM 2492 C CA . HIS A 1 302 ? 16.883 21.172 29.361 1.00 18.16 ? 335 HIS A CA 1 ATOM 2493 C C . HIS A 1 302 ? 16.466 22.627 29.287 1.00 16.66 ? 335 HIS A C 1 ATOM 2494 O O . HIS A 1 302 ? 17.070 23.462 29.931 1.00 17.54 ? 335 HIS A O 1 ATOM 2495 C CB . HIS A 1 302 ? 17.215 20.742 30.814 1.00 19.75 ? 335 HIS A CB 1 ATOM 2496 C CG . HIS A 1 302 ? 16.045 20.784 31.744 1.00 21.74 ? 335 HIS A CG 1 ATOM 2497 N ND1 . HIS A 1 302 ? 15.265 19.666 32.010 1.00 27.14 ? 335 HIS A ND1 1 ATOM 2498 C CD2 . HIS A 1 302 ? 15.519 21.799 32.464 1.00 24.54 ? 335 HIS A CD2 1 ATOM 2499 C CE1 . HIS A 1 302 ? 14.297 20.010 32.836 1.00 25.29 ? 335 HIS A CE1 1 ATOM 2500 N NE2 . HIS A 1 302 ? 14.448 21.282 33.157 1.00 28.94 ? 335 HIS A NE2 1 ATOM 2501 N N . VAL A 1 303 ? 15.445 22.928 28.476 1.00 16.78 ? 336 VAL A N 1 ATOM 2502 C CA . VAL A 1 303 ? 15.065 24.334 28.244 1.00 17.47 ? 336 VAL A CA 1 ATOM 2503 C C . VAL A 1 303 ? 13.572 24.459 28.376 1.00 16.75 ? 336 VAL A C 1 ATOM 2504 O O . VAL A 1 303 ? 12.824 23.752 27.685 1.00 17.73 ? 336 VAL A O 1 ATOM 2505 C CB . VAL A 1 303 ? 15.466 24.750 26.822 1.00 17.32 ? 336 VAL A CB 1 ATOM 2506 C CG1 . VAL A 1 303 ? 15.115 26.248 26.642 1.00 18.46 ? 336 VAL A CG1 1 ATOM 2507 C CG2 . VAL A 1 303 ? 16.993 24.545 26.622 1.00 18.17 ? 336 VAL A CG2 1 ATOM 2508 N N . TYR A 1 304 ? 13.131 25.333 29.271 1.00 17.11 ? 337 TYR A N 1 ATOM 2509 C CA . TYR A 1 304 ? 11.696 25.414 29.644 1.00 19.33 ? 337 TYR A CA 1 ATOM 2510 C C . TYR A 1 304 ? 11.289 26.858 29.841 1.00 19.24 ? 337 TYR A C 1 ATOM 2511 O O . TYR A 1 304 ? 10.444 27.196 30.651 1.00 20.37 ? 337 TYR A O 1 ATOM 2512 C CB . TYR A 1 304 ? 11.317 24.481 30.861 1.00 20.57 ? 337 TYR A CB 1 ATOM 2513 C CG . TYR A 1 304 ? 11.303 23.039 30.410 1.00 22.94 ? 337 TYR A CG 1 ATOM 2514 C CD1 . TYR A 1 304 ? 12.464 22.251 30.541 1.00 23.85 ? 337 TYR A CD1 1 ATOM 2515 C CD2 . TYR A 1 304 ? 10.179 22.478 29.756 1.00 22.34 ? 337 TYR A CD2 1 ATOM 2516 C CE1 . TYR A 1 304 ? 12.492 20.966 30.043 1.00 26.23 ? 337 TYR A CE1 1 ATOM 2517 C CE2 . TYR A 1 304 ? 10.190 21.183 29.268 1.00 25.42 ? 337 TYR A CE2 1 ATOM 2518 C CZ . TYR A 1 304 ? 11.349 20.452 29.401 1.00 25.21 ? 337 TYR A CZ 1 ATOM 2519 O OH . TYR A 1 304 ? 11.364 19.160 28.931 1.00 32.15 ? 337 TYR A OH 1 ATOM 2520 N N . ASN A 1 305 ? 11.790 27.746 28.979 1.00 18.45 ? 338 ASN A N 1 ATOM 2521 C CA . ASN A 1 305 ? 11.288 29.129 28.995 1.00 18.48 ? 338 ASN A CA 1 ATOM 2522 C C . ASN A 1 305 ? 9.830 29.128 28.640 1.00 20.65 ? 338 ASN A C 1 ATOM 2523 O O . ASN A 1 305 ? 9.322 28.234 27.917 1.00 20.50 ? 338 ASN A O 1 ATOM 2524 C CB . ASN A 1 305 ? 12.019 29.921 27.896 1.00 19.18 ? 338 ASN A CB 1 ATOM 2525 C CG . ASN A 1 305 ? 13.510 29.862 28.067 1.00 20.35 ? 338 ASN A CG 1 ATOM 2526 O OD1 . ASN A 1 305 ? 14.029 30.154 29.110 1.00 19.84 ? 338 ASN A OD1 1 ATOM 2527 N ND2 . ASN A 1 305 ? 14.242 29.585 26.975 1.00 21.41 ? 338 ASN A ND2 1 ATOM 2528 N N . ILE A 1 306 ? 9.149 30.136 29.139 1.00 19.70 ? 339 ILE A N 1 ATOM 2529 C CA . ILE A 1 306 ? 7.705 30.254 28.922 1.00 21.33 ? 339 ILE A CA 1 ATOM 2530 C C . ILE A 1 306 ? 7.395 31.407 27.965 1.00 21.91 ? 339 ILE A C 1 ATOM 2531 O O . ILE A 1 306 ? 7.988 32.475 28.110 1.00 24.75 ? 339 ILE A O 1 ATOM 2532 C CB . ILE A 1 306 ? 7.025 30.558 30.240 1.00 21.96 ? 339 ILE A CB 1 ATOM 2533 C CG1 A ILE A 1 306 ? 7.325 29.500 31.304 0.65 20.91 ? 339 ILE A CG1 1 ATOM 2534 C CG1 B ILE A 1 306 ? 5.596 31.073 30.100 0.35 23.55 ? 339 ILE A CG1 1 ATOM 2535 C CG2 A ILE A 1 306 ? 5.481 30.628 30.095 0.65 25.06 ? 339 ILE A CG2 1 ATOM 2536 C CG2 B ILE A 1 306 ? 7.695 31.666 30.986 0.35 21.06 ? 339 ILE A CG2 1 ATOM 2537 C CD1 A ILE A 1 306 ? 7.401 30.185 32.682 0.65 24.78 ? 339 ILE A CD1 1 ATOM 2538 C CD1 B ILE A 1 306 ? 5.252 31.937 31.242 0.35 24.42 ? 339 ILE A CD1 1 ATOM 2539 N N . ASN A 1 307 ? 6.434 31.208 27.083 1.00 20.14 ? 340 ASN A N 1 ATOM 2540 C CA . ASN A 1 307 ? 5.957 32.342 26.253 1.00 19.25 ? 340 ASN A CA 1 ATOM 2541 C C . ASN A 1 307 ? 4.670 32.847 26.934 1.00 20.31 ? 340 ASN A C 1 ATOM 2542 O O . ASN A 1 307 ? 3.789 32.020 27.265 1.00 21.21 ? 340 ASN A O 1 ATOM 2543 C CB . ASN A 1 307 ? 5.637 31.885 24.832 1.00 19.28 ? 340 ASN A CB 1 ATOM 2544 C CG . ASN A 1 307 ? 6.844 31.347 24.070 1.00 19.62 ? 340 ASN A CG 1 ATOM 2545 O OD1 . ASN A 1 307 ? 7.966 31.753 24.315 1.00 22.89 ? 340 ASN A OD1 1 ATOM 2546 N ND2 . ASN A 1 307 ? 6.600 30.426 23.141 1.00 22.41 ? 340 ASN A ND2 1 ATOM 2547 N N . LYS A 1 308 ? 4.514 34.174 27.072 1.00 19.07 ? 341 LYS A N 1 ATOM 2548 C CA . LYS A 1 308 ? 3.339 34.717 27.735 1.00 19.38 ? 341 LYS A CA 1 ATOM 2549 C C . LYS A 1 308 ? 3.015 36.063 27.110 1.00 18.66 ? 341 LYS A C 1 ATOM 2550 O O . LYS A 1 308 ? 3.910 36.867 26.878 1.00 18.31 ? 341 LYS A O 1 ATOM 2551 C CB . LYS A 1 308 ? 3.649 34.902 29.227 1.00 22.47 ? 341 LYS A CB 1 ATOM 2552 C CG . LYS A 1 308 ? 2.618 35.689 30.013 1.00 31.02 ? 341 LYS A CG 1 ATOM 2553 C CD . LYS A 1 308 ? 1.279 34.942 30.196 1.00 38.32 ? 341 LYS A CD 1 ATOM 2554 C CE . LYS A 1 308 ? 0.074 35.511 29.347 1.00 42.09 ? 341 LYS A CE 1 ATOM 2555 N NZ . LYS A 1 308 ? -0.647 36.703 29.903 1.00 37.93 ? 341 LYS A NZ 1 ATOM 2556 N N . ILE A 1 309 ? 1.727 36.304 26.880 1.00 18.62 ? 342 ILE A N 1 ATOM 2557 C CA . ILE A 1 309 ? 1.272 37.618 26.384 1.00 17.87 ? 342 ILE A CA 1 ATOM 2558 C C . ILE A 1 309 ? 1.494 38.604 27.530 1.00 17.07 ? 342 ILE A C 1 ATOM 2559 O O . ILE A 1 309 ? 1.034 38.375 28.673 1.00 19.58 ? 342 ILE A O 1 ATOM 2560 C CB . ILE A 1 309 ? -0.171 37.579 25.949 1.00 17.27 ? 342 ILE A CB 1 ATOM 2561 C CG1 . ILE A 1 309 ? -0.242 36.719 24.669 1.00 19.55 ? 342 ILE A CG1 1 ATOM 2562 C CG2 . ILE A 1 309 ? -0.681 39.023 25.592 1.00 19.03 ? 342 ILE A CG2 1 ATOM 2563 C CD1 . ILE A 1 309 ? -1.671 36.363 24.208 1.00 23.57 ? 342 ILE A CD1 1 ATOM 2564 N N . THR A 1 310 ? 2.210 39.699 27.234 1.00 17.85 ? 343 THR A N 1 ATOM 2565 C CA . THR A 1 310 ? 2.669 40.662 28.269 1.00 17.84 ? 343 THR A CA 1 ATOM 2566 C C . THR A 1 310 ? 2.495 42.071 27.731 1.00 17.03 ? 343 THR A C 1 ATOM 2567 O O . THR A 1 310 ? 2.702 42.325 26.510 1.00 17.52 ? 343 THR A O 1 ATOM 2568 C CB . THR A 1 310 ? 4.140 40.411 28.520 1.00 18.06 ? 343 THR A CB 1 ATOM 2569 O OG1 . THR A 1 310 ? 4.326 39.013 28.844 1.00 19.79 ? 343 THR A OG1 1 ATOM 2570 C CG2 . THR A 1 310 ? 4.695 41.281 29.624 1.00 18.69 ? 343 THR A CG2 1 ATOM 2571 N N . ARG A 1 311 ? 2.075 42.996 28.612 1.00 17.13 ? 344 ARG A N 1 ATOM 2572 C CA . ARG A 1 311 ? 1.882 44.382 28.186 1.00 17.14 ? 344 ARG A CA 1 ATOM 2573 C C . ARG A 1 311 ? 3.238 45.084 28.057 1.00 17.47 ? 344 ARG A C 1 ATOM 2574 O O . ARG A 1 311 ? 4.156 44.905 28.866 1.00 18.46 ? 344 ARG A O 1 ATOM 2575 C CB . ARG A 1 311 ? 0.970 45.165 29.171 1.00 18.16 ? 344 ARG A CB 1 ATOM 2576 C CG . ARG A 1 311 ? 0.610 46.561 28.584 1.00 18.18 ? 344 ARG A CG 1 ATOM 2577 C CD . ARG A 1 311 ? -0.686 47.002 29.274 1.00 19.92 ? 344 ARG A CD 1 ATOM 2578 N NE . ARG A 1 311 ? -1.798 46.265 28.655 1.00 20.41 ? 344 ARG A NE 1 ATOM 2579 C CZ . ARG A 1 311 ? -3.076 46.602 28.820 1.00 23.75 ? 344 ARG A CZ 1 ATOM 2580 N NH1 . ARG A 1 311 ? -3.409 47.611 29.649 1.00 24.50 ? 344 ARG A NH1 1 ATOM 2581 N NH2 . ARG A 1 311 ? -4.015 45.955 28.168 1.00 22.63 ? 344 ARG A NH2 1 ATOM 2582 N N . ILE A 1 312 ? 3.384 45.803 26.946 1.00 15.56 ? 345 ILE A N 1 ATOM 2583 C CA . ILE A 1 312 ? 4.580 46.641 26.712 1.00 15.85 ? 345 ILE A CA 1 ATOM 2584 C C . ILE A 1 312 ? 4.127 48.085 26.478 1.00 16.79 ? 345 ILE A C 1 ATOM 2585 O O . ILE A 1 312 ? 2.978 48.339 26.158 1.00 17.83 ? 345 ILE A O 1 ATOM 2586 C CB . ILE A 1 312 ? 5.419 46.166 25.474 1.00 16.37 ? 345 ILE A CB 1 ATOM 2587 C CG1 . ILE A 1 312 ? 4.549 46.147 24.206 1.00 17.50 ? 345 ILE A CG1 1 ATOM 2588 C CG2 . ILE A 1 312 ? 5.940 44.718 25.791 1.00 18.52 ? 345 ILE A CG2 1 ATOM 2589 C CD1 . ILE A 1 312 ? 5.395 45.969 22.876 1.00 19.04 ? 345 ILE A CD1 1 ATOM 2590 N N . TYR A 1 313 ? 5.068 49.010 26.668 1.00 16.48 ? 346 TYR A N 1 ATOM 2591 C CA . TYR A 1 313 ? 4.725 50.471 26.657 1.00 16.91 ? 346 TYR A CA 1 ATOM 2592 C C . TYR A 1 313 ? 5.719 51.266 25.866 1.00 17.25 ? 346 TYR A C 1 ATOM 2593 O O . TYR A 1 313 ? 6.908 51.339 26.233 1.00 17.23 ? 346 TYR A O 1 ATOM 2594 C CB . TYR A 1 313 ? 4.745 51.037 28.092 1.00 17.75 ? 346 TYR A CB 1 ATOM 2595 C CG . TYR A 1 313 ? 3.792 50.340 29.032 1.00 18.58 ? 346 TYR A CG 1 ATOM 2596 C CD1 . TYR A 1 313 ? 2.493 50.810 29.193 1.00 19.06 ? 346 TYR A CD1 1 ATOM 2597 C CD2 . TYR A 1 313 ? 4.225 49.220 29.750 1.00 18.90 ? 346 TYR A CD2 1 ATOM 2598 C CE1 . TYR A 1 313 ? 1.634 50.163 30.144 1.00 21.64 ? 346 TYR A CE1 1 ATOM 2599 C CE2 . TYR A 1 313 ? 3.381 48.564 30.670 1.00 19.63 ? 346 TYR A CE2 1 ATOM 2600 C CZ . TYR A 1 313 ? 2.090 49.075 30.823 1.00 21.37 ? 346 TYR A CZ 1 ATOM 2601 O OH . TYR A 1 313 ? 1.229 48.451 31.753 1.00 23.74 ? 346 TYR A OH 1 ATOM 2602 N N . ASN A 1 314 ? 5.236 51.893 24.816 1.00 16.29 ? 347 ASN A N 1 ATOM 2603 C CA . ASN A 1 314 ? 6.021 52.913 24.114 1.00 15.93 ? 347 ASN A CA 1 ATOM 2604 C C . ASN A 1 314 ? 5.762 54.249 24.724 1.00 17.47 ? 347 ASN A C 1 ATOM 2605 O O . ASN A 1 314 ? 4.652 54.508 25.198 1.00 19.99 ? 347 ASN A O 1 ATOM 2606 C CB . ASN A 1 314 ? 5.644 52.967 22.611 1.00 16.84 ? 347 ASN A CB 1 ATOM 2607 C CG . ASN A 1 314 ? 5.963 51.678 21.841 1.00 16.60 ? 347 ASN A CG 1 ATOM 2608 O OD1 . ASN A 1 314 ? 6.923 50.908 22.137 1.00 15.77 ? 347 ASN A OD1 1 ATOM 2609 N ND2 . ASN A 1 314 ? 5.155 51.431 20.747 1.00 18.32 ? 347 ASN A ND2 1 ATOM 2610 N N . VAL A 1 315 ? 6.760 55.120 24.757 1.00 16.35 ? 348 VAL A N 1 ATOM 2611 C CA . VAL A 1 315 ? 6.455 56.523 25.096 1.00 17.10 ? 348 VAL A CA 1 ATOM 2612 C C . VAL A 1 315 ? 6.491 57.278 23.770 1.00 17.72 ? 348 VAL A C 1 ATOM 2613 O O . VAL A 1 315 ? 7.489 57.165 22.994 1.00 16.94 ? 348 VAL A O 1 ATOM 2614 C CB . VAL A 1 315 ? 7.505 57.169 26.057 1.00 15.96 ? 348 VAL A CB 1 ATOM 2615 C CG1 . VAL A 1 315 ? 6.944 58.500 26.580 1.00 18.26 ? 348 VAL A CG1 1 ATOM 2616 C CG2 . VAL A 1 315 ? 7.806 56.253 27.236 1.00 18.34 ? 348 VAL A CG2 1 ATOM 2617 N N . VAL A 1 316 ? 5.398 57.999 23.445 1.00 17.34 ? 349 VAL A N 1 ATOM 2618 C CA . VAL A 1 316 ? 5.317 58.706 22.182 1.00 16.74 ? 349 VAL A CA 1 ATOM 2619 C C . VAL A 1 316 ? 4.996 60.182 22.449 1.00 16.86 ? 349 VAL A C 1 ATOM 2620 O O . VAL A 1 316 ? 3.965 60.481 23.087 1.00 18.62 ? 349 VAL A O 1 ATOM 2621 C CB . VAL A 1 316 ? 4.207 58.087 21.275 1.00 18.29 ? 349 VAL A CB 1 ATOM 2622 C CG1 A VAL A 1 316 ? 4.127 58.899 19.918 0.70 17.12 ? 349 VAL A CG1 1 ATOM 2623 C CG1 B VAL A 1 316 ? 4.694 56.700 20.759 0.30 18.08 ? 349 VAL A CG1 1 ATOM 2624 C CG2 A VAL A 1 316 ? 4.518 56.573 21.028 0.70 19.19 ? 349 VAL A CG2 1 ATOM 2625 C CG2 B VAL A 1 316 ? 2.921 57.983 21.972 0.30 19.57 ? 349 VAL A CG2 1 ATOM 2626 N N . GLY A 1 317 ? 5.841 61.067 21.935 1.00 16.92 ? 350 GLY A N 1 ATOM 2627 C CA . GLY A 1 317 ? 5.707 62.499 22.250 1.00 18.40 ? 350 GLY A CA 1 ATOM 2628 C C . GLY A 1 317 ? 5.782 63.294 20.954 1.00 17.00 ? 350 GLY A C 1 ATOM 2629 O O . GLY A 1 317 ? 6.209 62.784 19.919 1.00 17.54 ? 350 GLY A O 1 ATOM 2630 N N . THR A 1 318 ? 5.350 64.560 21.013 1.00 17.39 ? 351 THR A N 1 ATOM 2631 C CA . THR A 1 318 ? 5.360 65.365 19.812 1.00 17.65 ? 351 THR A CA 1 ATOM 2632 C C . THR A 1 318 ? 5.794 66.783 20.080 1.00 17.22 ? 351 THR A C 1 ATOM 2633 O O . THR A 1 318 ? 5.608 67.295 21.199 1.00 18.15 ? 351 THR A O 1 ATOM 2634 C CB . THR A 1 318 ? 3.973 65.466 19.129 1.00 19.38 ? 351 THR A CB 1 ATOM 2635 O OG1 . THR A 1 318 ? 3.059 66.120 20.057 1.00 20.77 ? 351 THR A OG1 1 ATOM 2636 C CG2 . THR A 1 318 ? 3.422 64.053 18.737 1.00 20.10 ? 351 THR A CG2 1 ATOM 2637 N N . ILE A 1 319 ? 6.341 67.413 19.031 1.00 18.12 ? 352 ILE A N 1 ATOM 2638 C CA . ILE A 1 319 ? 6.343 68.890 18.904 1.00 18.22 ? 352 ILE A CA 1 ATOM 2639 C C . ILE A 1 319 ? 5.655 69.225 17.601 1.00 16.76 ? 352 ILE A C 1 ATOM 2640 O O . ILE A 1 319 ? 6.189 68.863 16.508 1.00 17.52 ? 352 ILE A O 1 ATOM 2641 C CB . ILE A 1 319 ? 7.755 69.480 18.894 1.00 18.21 ? 352 ILE A CB 1 ATOM 2642 C CG1 . ILE A 1 319 ? 8.476 69.121 20.209 1.00 16.93 ? 352 ILE A CG1 1 ATOM 2643 C CG2 . ILE A 1 319 ? 7.687 71.049 18.701 1.00 19.48 ? 352 ILE A CG2 1 ATOM 2644 C CD1 . ILE A 1 319 ? 9.984 69.503 20.258 1.00 18.88 ? 352 ILE A CD1 1 ATOM 2645 N N . ARG A 1 320 ? 4.445 69.793 17.668 1.00 17.67 ? 353 ARG A N 1 ATOM 2646 C CA . ARG A 1 320 ? 3.656 69.974 16.438 1.00 18.37 ? 353 ARG A CA 1 ATOM 2647 C C . ARG A 1 320 ? 4.192 71.061 15.516 1.00 17.20 ? 353 ARG A C 1 ATOM 2648 O O . ARG A 1 320 ? 4.628 72.139 16.012 1.00 19.01 ? 353 ARG A O 1 ATOM 2649 C CB . ARG A 1 320 ? 2.259 70.339 16.877 1.00 20.90 ? 353 ARG A CB 1 ATOM 2650 C CG . ARG A 1 320 ? 1.237 70.397 15.796 1.00 27.57 ? 353 ARG A CG 1 ATOM 2651 C CD . ARG A 1 320 ? -0.092 70.949 16.400 1.00 37.88 ? 353 ARG A CD 1 ATOM 2652 N NE . ARG A 1 320 ? -1.100 71.257 15.379 1.00 40.28 ? 353 ARG A NE 1 ATOM 2653 C CZ . ARG A 1 320 ? -1.716 70.334 14.651 1.00 40.58 ? 353 ARG A CZ 1 ATOM 2654 N NH1 . ARG A 1 320 ? -1.409 69.034 14.803 1.00 36.88 ? 353 ARG A NH1 1 ATOM 2655 N NH2 . ARG A 1 320 ? -2.620 70.728 13.740 1.00 41.22 ? 353 ARG A NH2 1 ATOM 2656 N N . GLY A 1 321 ? 4.142 70.821 14.212 1.00 17.77 ? 354 GLY A N 1 ATOM 2657 C CA . GLY A 1 321 ? 4.644 71.802 13.220 1.00 17.84 ? 354 GLY A CA 1 ATOM 2658 C C . GLY A 1 321 ? 3.771 73.043 13.183 1.00 18.38 ? 354 GLY A C 1 ATOM 2659 O O . GLY A 1 321 ? 2.548 72.921 13.287 1.00 20.43 ? 354 GLY A O 1 ATOM 2660 N N . SER A 1 322 ? 4.431 74.201 12.922 1.00 17.97 ? 355 SER A N 1 ATOM 2661 C CA . SER A 1 322 ? 3.644 75.442 12.810 1.00 19.07 ? 355 SER A CA 1 ATOM 2662 C C . SER A 1 322 ? 3.165 75.668 11.397 1.00 19.46 ? 355 SER A C 1 ATOM 2663 O O . SER A 1 322 ? 2.223 76.479 11.222 1.00 22.38 ? 355 SER A O 1 ATOM 2664 C CB . SER A 1 322 ? 4.502 76.651 13.196 1.00 20.57 ? 355 SER A CB 1 ATOM 2665 O OG A SER A 1 322 ? 5.592 76.750 12.365 0.65 22.44 ? 355 SER A OG 1 ATOM 2666 O OG B SER A 1 322 ? 4.868 76.615 14.537 0.35 20.83 ? 355 SER A OG 1 ATOM 2667 N N . VAL A 1 323 ? 3.726 74.991 10.398 1.00 18.00 ? 356 VAL A N 1 ATOM 2668 C CA . VAL A 1 323 ? 3.361 75.234 9.019 1.00 18.91 ? 356 VAL A CA 1 ATOM 2669 C C . VAL A 1 323 ? 2.765 73.959 8.411 1.00 19.44 ? 356 VAL A C 1 ATOM 2670 O O . VAL A 1 323 ? 1.717 74.038 7.732 1.00 20.04 ? 356 VAL A O 1 ATOM 2671 C CB . VAL A 1 323 ? 4.556 75.653 8.176 1.00 19.29 ? 356 VAL A CB 1 ATOM 2672 C CG1 . VAL A 1 323 ? 4.133 75.962 6.712 1.00 20.98 ? 356 VAL A CG1 1 ATOM 2673 C CG2 . VAL A 1 323 ? 5.223 76.867 8.789 1.00 21.80 ? 356 VAL A CG2 1 ATOM 2674 N N . GLU A 1 324 ? 3.463 72.823 8.626 1.00 17.24 ? 357 GLU A N 1 ATOM 2675 C CA . GLU A 1 324 ? 3.002 71.546 8.042 1.00 17.69 ? 357 GLU A CA 1 ATOM 2676 C C . GLU A 1 324 ? 2.832 70.527 9.158 1.00 18.11 ? 357 GLU A C 1 ATOM 2677 O O . GLU A 1 324 ? 3.638 69.613 9.297 1.00 18.53 ? 357 GLU A O 1 ATOM 2678 C CB . GLU A 1 324 ? 3.994 71.005 6.996 1.00 18.18 ? 357 GLU A CB 1 ATOM 2679 C CG . GLU A 1 324 ? 4.105 71.907 5.797 1.00 18.77 ? 357 GLU A CG 1 ATOM 2680 C CD . GLU A 1 324 ? 5.020 71.294 4.768 1.00 20.52 ? 357 GLU A CD 1 ATOM 2681 O OE1 . GLU A 1 324 ? 4.535 70.562 3.879 1.00 20.27 ? 357 GLU A OE1 1 ATOM 2682 O OE2 . GLU A 1 324 ? 6.266 71.484 4.858 1.00 20.89 ? 357 GLU A OE2 1 ATOM 2683 N N . PRO A 1 325 ? 1.835 70.718 10.010 1.00 16.43 ? 358 PRO A N 1 ATOM 2684 C CA . PRO A 1 325 ? 1.689 69.804 11.168 1.00 16.46 ? 358 PRO A CA 1 ATOM 2685 C C . PRO A 1 325 ? 1.339 68.397 10.729 1.00 18.60 ? 358 PRO A C 1 ATOM 2686 O O . PRO A 1 325 ? 1.468 67.462 11.545 1.00 20.90 ? 358 PRO A O 1 ATOM 2687 C CB . PRO A 1 325 ? 0.513 70.411 11.996 1.00 17.69 ? 358 PRO A CB 1 ATOM 2688 C CG . PRO A 1 325 ? -0.185 71.278 11.005 1.00 15.98 ? 358 PRO A CG 1 ATOM 2689 C CD . PRO A 1 325 ? 0.893 71.871 10.127 1.00 17.00 ? 358 PRO A CD 1 ATOM 2690 N N . ASP A 1 326 ? 0.893 68.227 9.479 1.00 16.85 ? 359 ASP A N 1 ATOM 2691 C CA . ASP A 1 326 ? 0.583 66.904 8.920 1.00 17.11 ? 359 ASP A CA 1 ATOM 2692 C C . ASP A 1 326 ? 1.784 66.257 8.194 1.00 16.54 ? 359 ASP A C 1 ATOM 2693 O O . ASP A 1 326 ? 1.589 65.417 7.309 1.00 17.88 ? 359 ASP A O 1 ATOM 2694 C CB . ASP A 1 326 ? -0.618 66.944 7.951 1.00 17.68 ? 359 ASP A CB 1 ATOM 2695 C CG . ASP A 1 326 ? -0.295 67.632 6.659 1.00 18.39 ? 359 ASP A CG 1 ATOM 2696 O OD1 . ASP A 1 326 ? 0.720 68.378 6.595 1.00 18.08 ? 359 ASP A OD1 1 ATOM 2697 O OD2 . ASP A 1 326 ? -1.058 67.457 5.694 1.00 19.21 ? 359 ASP A OD2 1 ATOM 2698 N N . ARG A 1 327 ? 3.018 66.666 8.542 1.00 17.18 ? 360 ARG A N 1 ATOM 2699 C CA . ARG A 1 327 ? 4.207 66.009 7.989 1.00 16.26 ? 360 ARG A CA 1 ATOM 2700 C C . ARG A 1 327 ? 5.096 65.693 9.204 1.00 16.05 ? 360 ARG A C 1 ATOM 2701 O O . ARG A 1 327 ? 5.230 66.529 10.116 1.00 17.20 ? 360 ARG A O 1 ATOM 2702 C CB . ARG A 1 327 ? 4.947 67.030 7.080 1.00 17.05 ? 360 ARG A CB 1 ATOM 2703 C CG . ARG A 1 327 ? 4.130 67.296 5.763 1.00 16.90 ? 360 ARG A CG 1 ATOM 2704 C CD . ARG A 1 327 ? 4.140 66.066 4.919 1.00 17.59 ? 360 ARG A CD 1 ATOM 2705 N NE . ARG A 1 327 ? 3.395 66.208 3.651 1.00 17.00 ? 360 ARG A NE 1 ATOM 2706 C CZ . ARG A 1 327 ? 2.165 65.681 3.438 1.00 17.33 ? 360 ARG A CZ 1 ATOM 2707 N NH1 . ARG A 1 327 ? 1.407 65.167 4.443 1.00 17.87 ? 360 ARG A NH1 1 ATOM 2708 N NH2 . ARG A 1 327 ? 1.659 65.671 2.192 1.00 18.13 ? 360 ARG A NH2 1 ATOM 2709 N N . TYR A 1 328 ? 5.722 64.493 9.231 1.00 16.99 ? 361 TYR A N 1 ATOM 2710 C CA . TYR A 1 328 ? 6.414 64.004 10.436 1.00 16.90 ? 361 TYR A CA 1 ATOM 2711 C C . TYR A 1 328 ? 7.852 63.649 10.184 1.00 16.69 ? 361 TYR A C 1 ATOM 2712 O O . TYR A 1 328 ? 8.209 63.048 9.158 1.00 18.35 ? 361 TYR A O 1 ATOM 2713 C CB . TYR A 1 328 ? 5.743 62.696 10.896 1.00 17.32 ? 361 TYR A CB 1 ATOM 2714 C CG . TYR A 1 328 ? 4.237 62.751 11.063 1.00 16.69 ? 361 TYR A CG 1 ATOM 2715 C CD1 . TYR A 1 328 ? 3.604 63.867 11.628 1.00 17.17 ? 361 TYR A CD1 1 ATOM 2716 C CD2 . TYR A 1 328 ? 3.449 61.639 10.715 1.00 17.14 ? 361 TYR A CD2 1 ATOM 2717 C CE1 . TYR A 1 328 ? 2.214 63.867 11.798 1.00 18.10 ? 361 TYR A CE1 1 ATOM 2718 C CE2 . TYR A 1 328 ? 2.064 61.620 10.897 1.00 18.09 ? 361 TYR A CE2 1 ATOM 2719 C CZ . TYR A 1 328 ? 1.445 62.735 11.430 1.00 17.45 ? 361 TYR A CZ 1 ATOM 2720 O OH . TYR A 1 328 ? 0.056 62.782 11.607 1.00 19.11 ? 361 TYR A OH 1 ATOM 2721 N N . VAL A 1 329 ? 8.659 63.922 11.193 1.00 16.61 ? 362 VAL A N 1 ATOM 2722 C CA . VAL A 1 329 ? 9.996 63.337 11.264 1.00 17.23 ? 362 VAL A CA 1 ATOM 2723 C C . VAL A 1 329 ? 10.036 62.617 12.616 1.00 17.79 ? 362 VAL A C 1 ATOM 2724 O O . VAL A 1 329 ? 9.712 63.211 13.667 1.00 17.62 ? 362 VAL A O 1 ATOM 2725 C CB . VAL A 1 329 ? 11.080 64.412 11.179 1.00 17.98 ? 362 VAL A CB 1 ATOM 2726 C CG1 . VAL A 1 329 ? 12.523 63.812 11.479 1.00 20.16 ? 362 VAL A CG1 1 ATOM 2727 C CG2 . VAL A 1 329 ? 11.049 65.086 9.772 1.00 20.26 ? 362 VAL A CG2 1 ATOM 2728 N N . ILE A 1 330 ? 10.381 61.335 12.566 1.00 17.91 ? 363 ILE A N 1 ATOM 2729 C CA . ILE A 1 330 ? 10.339 60.457 13.754 1.00 17.33 ? 363 ILE A CA 1 ATOM 2730 C C . ILE A 1 330 ? 11.731 60.270 14.271 1.00 18.18 ? 363 ILE A C 1 ATOM 2731 O O . ILE A 1 330 ? 12.642 59.904 13.478 1.00 18.62 ? 363 ILE A O 1 ATOM 2732 C CB . ILE A 1 330 ? 9.727 59.080 13.391 1.00 18.89 ? 363 ILE A CB 1 ATOM 2733 C CG1 . ILE A 1 330 ? 8.334 59.312 12.757 1.00 20.68 ? 363 ILE A CG1 1 ATOM 2734 C CG2 . ILE A 1 330 ? 9.654 58.241 14.705 1.00 18.42 ? 363 ILE A CG2 1 ATOM 2735 C CD1 . ILE A 1 330 ? 7.884 58.017 11.968 1.00 24.64 ? 363 ILE A CD1 1 ATOM 2736 N N . LEU A 1 331 ? 11.947 60.561 15.552 1.00 17.20 ? 364 LEU A N 1 ATOM 2737 C CA . LEU A 1 331 ? 13.207 60.201 16.235 1.00 16.19 ? 364 LEU A CA 1 ATOM 2738 C C . LEU A 1 331 ? 12.830 59.106 17.237 1.00 17.51 ? 364 LEU A C 1 ATOM 2739 O O . LEU A 1 331 ? 12.132 59.406 18.236 1.00 17.36 ? 364 LEU A O 1 ATOM 2740 C CB . LEU A 1 331 ? 13.795 61.436 16.936 1.00 16.25 ? 364 LEU A CB 1 ATOM 2741 C CG . LEU A 1 331 ? 15.058 61.124 17.765 1.00 16.46 ? 364 LEU A CG 1 ATOM 2742 C CD1 . LEU A 1 331 ? 16.225 60.625 16.910 1.00 17.55 ? 364 LEU A CD1 1 ATOM 2743 C CD2 . LEU A 1 331 ? 15.445 62.395 18.511 1.00 19.35 ? 364 LEU A CD2 1 ATOM 2744 N N . GLY A 1 332 ? 13.255 57.863 16.970 1.00 16.46 ? 365 GLY A N 1 ATOM 2745 C CA . GLY A 1 332 ? 12.786 56.754 17.778 1.00 16.62 ? 365 GLY A CA 1 ATOM 2746 C C . GLY A 1 332 ? 13.933 55.847 18.218 1.00 16.71 ? 365 GLY A C 1 ATOM 2747 O O . GLY A 1 332 ? 14.834 55.575 17.443 1.00 17.48 ? 365 GLY A O 1 ATOM 2748 N N . GLY A 1 333 ? 13.897 55.413 19.462 1.00 17.25 ? 366 GLY A N 1 ATOM 2749 C CA . GLY A 1 333 ? 14.959 54.481 19.941 1.00 17.25 ? 366 GLY A CA 1 ATOM 2750 C C . GLY A 1 333 ? 14.360 53.568 20.985 1.00 17.16 ? 366 GLY A C 1 ATOM 2751 O O . GLY A 1 333 ? 13.477 53.989 21.754 1.00 17.32 ? 366 GLY A O 1 ATOM 2752 N N . HIS A 1 334 ? 14.866 52.339 21.066 1.00 16.68 ? 367 HIS A N 1 ATOM 2753 C CA . HIS A 1 334 ? 14.355 51.448 22.118 1.00 16.37 ? 367 HIS A CA 1 ATOM 2754 C C . HIS A 1 334 ? 14.983 51.683 23.440 1.00 16.86 ? 367 HIS A C 1 ATOM 2755 O O . HIS A 1 334 ? 16.076 52.241 23.528 1.00 16.57 ? 367 HIS A O 1 ATOM 2756 C CB . HIS A 1 334 ? 14.389 49.933 21.713 1.00 17.74 ? 367 HIS A CB 1 ATOM 2757 C CG . HIS A 1 334 ? 15.721 49.245 21.772 1.00 16.88 ? 367 HIS A CG 1 ATOM 2758 N ND1 . HIS A 1 334 ? 16.076 48.349 22.773 1.00 15.79 ? 367 HIS A ND1 1 ATOM 2759 C CD2 . HIS A 1 334 ? 16.728 49.211 20.876 1.00 18.30 ? 367 HIS A CD2 1 ATOM 2760 C CE1 . HIS A 1 334 ? 17.266 47.830 22.492 1.00 16.24 ? 367 HIS A CE1 1 ATOM 2761 N NE2 . HIS A 1 334 ? 17.677 48.328 21.343 1.00 16.59 ? 367 HIS A NE2 1 ATOM 2762 N N . ARG A 1 335 ? 14.275 51.275 24.482 1.00 17.69 ? 368 ARG A N 1 ATOM 2763 C CA . ARG A 1 335 ? 14.822 51.445 25.814 1.00 17.40 ? 368 ARG A CA 1 ATOM 2764 C C . ARG A 1 335 ? 14.909 50.167 26.613 1.00 18.58 ? 368 ARG A C 1 ATOM 2765 O O . ARG A 1 335 ? 15.576 50.129 27.655 1.00 17.37 ? 368 ARG A O 1 ATOM 2766 C CB . ARG A 1 335 ? 14.042 52.485 26.621 1.00 20.27 ? 368 ARG A CB 1 ATOM 2767 C CG . ARG A 1 335 ? 12.751 51.938 27.073 1.00 19.70 ? 368 ARG A CG 1 ATOM 2768 C CD . ARG A 1 335 ? 11.976 52.885 28.161 1.00 19.30 ? 368 ARG A CD 1 ATOM 2769 N NE . ARG A 1 335 ? 10.820 52.106 28.560 1.00 17.33 ? 368 ARG A NE 1 ATOM 2770 C CZ . ARG A 1 335 ? 9.752 51.868 27.784 1.00 15.16 ? 368 ARG A CZ 1 ATOM 2771 N NH1 . ARG A 1 335 ? 9.610 52.525 26.614 1.00 17.19 ? 368 ARG A NH1 1 ATOM 2772 N NH2 . ARG A 1 335 ? 8.833 50.973 28.173 1.00 17.87 ? 368 ARG A NH2 1 ATOM 2773 N N . ASP A 1 336 ? 14.290 49.100 26.089 1.00 17.22 ? 369 ASP A N 1 ATOM 2774 C CA . ASP A 1 336 ? 14.353 47.828 26.820 1.00 16.96 ? 369 ASP A CA 1 ATOM 2775 C C . ASP A 1 336 ? 15.705 47.191 26.584 1.00 16.19 ? 369 ASP A C 1 ATOM 2776 O O . ASP A 1 336 ? 16.267 47.290 25.480 1.00 17.23 ? 369 ASP A O 1 ATOM 2777 C CB . ASP A 1 336 ? 13.247 46.845 26.306 1.00 17.38 ? 369 ASP A CB 1 ATOM 2778 C CG . ASP A 1 336 ? 13.418 46.479 24.848 1.00 17.88 ? 369 ASP A CG 1 ATOM 2779 O OD1 . ASP A 1 336 ? 13.424 47.369 23.964 1.00 16.81 ? 369 ASP A OD1 1 ATOM 2780 O OD2 . ASP A 1 336 ? 13.532 45.267 24.548 1.00 18.40 ? 369 ASP A OD2 1 ATOM 2781 N N . SER A 1 337 ? 16.218 46.542 27.632 1.00 16.54 ? 370 SER A N 1 ATOM 2782 C CA . SER A 1 337 ? 17.553 45.905 27.538 1.00 17.41 ? 370 SER A CA 1 ATOM 2783 C C . SER A 1 337 ? 17.451 44.469 27.999 1.00 18.46 ? 370 SER A C 1 ATOM 2784 O O . SER A 1 337 ? 16.410 44.014 28.523 1.00 18.61 ? 370 SER A O 1 ATOM 2785 C CB . SER A 1 337 ? 18.504 46.702 28.485 1.00 18.30 ? 370 SER A CB 1 ATOM 2786 O OG . SER A 1 337 ? 17.994 46.732 29.814 1.00 20.17 ? 370 SER A OG 1 ATOM 2787 N N . TRP A 1 338 ? 18.530 43.710 27.764 1.00 16.87 ? 371 TRP A N 1 ATOM 2788 C CA . TRP A 1 338 ? 18.587 42.348 28.369 1.00 17.33 ? 371 TRP A CA 1 ATOM 2789 C C . TRP A 1 338 ? 18.913 42.395 29.867 1.00 18.58 ? 371 TRP A C 1 ATOM 2790 O O . TRP A 1 338 ? 18.259 41.710 30.686 1.00 19.06 ? 371 TRP A O 1 ATOM 2791 C CB . TRP A 1 338 ? 19.572 41.418 27.592 1.00 17.60 ? 371 TRP A CB 1 ATOM 2792 C CG . TRP A 1 338 ? 18.937 40.969 26.277 1.00 15.70 ? 371 TRP A CG 1 ATOM 2793 C CD1 . TRP A 1 338 ? 19.262 41.311 25.003 1.00 18.18 ? 371 TRP A CD1 1 ATOM 2794 C CD2 . TRP A 1 338 ? 17.778 40.116 26.216 1.00 16.95 ? 371 TRP A CD2 1 ATOM 2795 N NE1 . TRP A 1 338 ? 18.382 40.723 24.138 1.00 18.78 ? 371 TRP A NE1 1 ATOM 2796 C CE2 . TRP A 1 338 ? 17.438 40.001 24.847 1.00 16.40 ? 371 TRP A CE2 1 ATOM 2797 C CE3 . TRP A 1 338 ? 16.954 39.508 27.181 1.00 17.46 ? 371 TRP A CE3 1 ATOM 2798 C CZ2 . TRP A 1 338 ? 16.290 39.265 24.396 1.00 17.95 ? 371 TRP A CZ2 1 ATOM 2799 C CZ3 . TRP A 1 338 ? 15.827 38.732 26.725 1.00 17.47 ? 371 TRP A CZ3 1 ATOM 2800 C CH2 . TRP A 1 338 ? 15.526 38.629 25.382 1.00 18.38 ? 371 TRP A CH2 1 ATOM 2801 N N . VAL A 1 339 ? 19.923 43.202 30.227 1.00 17.36 ? 372 VAL A N 1 ATOM 2802 C CA . VAL A 1 339 ? 20.239 43.412 31.659 1.00 19.07 ? 372 VAL A CA 1 ATOM 2803 C C . VAL A 1 339 ? 20.309 44.930 31.878 1.00 19.64 ? 372 VAL A C 1 ATOM 2804 O O . VAL A 1 339 ? 19.246 45.554 31.845 1.00 19.22 ? 372 VAL A O 1 ATOM 2805 C CB . VAL A 1 339 ? 21.490 42.617 32.133 1.00 18.94 ? 372 VAL A CB 1 ATOM 2806 C CG1 . VAL A 1 339 ? 21.585 42.727 33.706 1.00 20.97 ? 372 VAL A CG1 1 ATOM 2807 C CG2 . VAL A 1 339 ? 21.404 41.130 31.678 1.00 20.58 ? 372 VAL A CG2 1 ATOM 2808 N N . PHE A 1 340 ? 21.499 45.522 32.112 1.00 18.48 ? 373 PHE A N 1 ATOM 2809 C CA . PHE A 1 340 ? 21.584 46.972 32.258 1.00 18.79 ? 373 PHE A CA 1 ATOM 2810 C C . PHE A 1 340 ? 21.635 47.680 30.895 1.00 17.56 ? 373 PHE A C 1 ATOM 2811 O O . PHE A 1 340 ? 21.238 48.871 30.809 1.00 19.22 ? 373 PHE A O 1 ATOM 2812 C CB . PHE A 1 340 ? 22.784 47.375 33.126 1.00 18.50 ? 373 PHE A CB 1 ATOM 2813 C CG . PHE A 1 340 ? 22.829 46.651 34.440 1.00 19.95 ? 373 PHE A CG 1 ATOM 2814 C CD1 . PHE A 1 340 ? 21.892 46.912 35.425 1.00 20.51 ? 373 PHE A CD1 1 ATOM 2815 C CD2 . PHE A 1 340 ? 23.763 45.619 34.657 1.00 23.55 ? 373 PHE A CD2 1 ATOM 2816 C CE1 . PHE A 1 340 ? 21.921 46.194 36.674 1.00 21.40 ? 373 PHE A CE1 1 ATOM 2817 C CE2 . PHE A 1 340 ? 23.789 44.906 35.885 1.00 24.14 ? 373 PHE A CE2 1 ATOM 2818 C CZ . PHE A 1 340 ? 22.884 45.200 36.879 1.00 20.91 ? 373 PHE A CZ 1 ATOM 2819 N N . GLY A 1 341 ? 22.138 46.976 29.857 1.00 18.49 ? 374 GLY A N 1 ATOM 2820 C CA . GLY A 1 341 ? 22.131 47.540 28.497 1.00 18.97 ? 374 GLY A CA 1 ATOM 2821 C C . GLY A 1 341 ? 22.846 48.875 28.415 1.00 19.22 ? 374 GLY A C 1 ATOM 2822 O O . GLY A 1 341 ? 22.354 49.771 27.729 1.00 19.41 ? 374 GLY A O 1 ATOM 2823 N N . ALA A 1 342 ? 23.952 49.067 29.129 1.00 19.15 ? 375 ALA A N 1 ATOM 2824 C CA . ALA A 1 342 ? 24.602 50.366 29.054 1.00 18.72 ? 375 ALA A CA 1 ATOM 2825 C C . ALA A 1 342 ? 24.980 50.841 27.676 1.00 19.16 ? 375 ALA A C 1 ATOM 2826 O O . ALA A 1 342 ? 24.890 52.053 27.422 1.00 19.91 ? 375 ALA A O 1 ATOM 2827 C CB . ALA A 1 342 ? 25.786 50.489 30.044 1.00 19.08 ? 375 ALA A CB 1 ATOM 2828 N N . ILE A 1 343 ? 25.417 49.954 26.764 1.00 17.20 ? 376 ILE A N 1 ATOM 2829 C CA . ILE A 1 343 ? 25.572 50.341 25.378 1.00 18.08 ? 376 ILE A CA 1 ATOM 2830 C C . ILE A 1 343 ? 24.228 50.163 24.670 1.00 18.41 ? 376 ILE A C 1 ATOM 2831 O O . ILE A 1 343 ? 23.616 51.155 24.219 1.00 18.24 ? 376 ILE A O 1 ATOM 2832 C CB . ILE A 1 343 ? 26.717 49.554 24.661 1.00 17.96 ? 376 ILE A CB 1 ATOM 2833 C CG1 . ILE A 1 343 ? 28.037 50.016 25.340 1.00 19.37 ? 376 ILE A CG1 1 ATOM 2834 C CG2 . ILE A 1 343 ? 26.699 49.811 23.168 1.00 19.38 ? 376 ILE A CG2 1 ATOM 2835 C CD1 . ILE A 1 343 ? 29.276 49.132 24.881 1.00 19.01 ? 376 ILE A CD1 1 ATOM 2836 N N . ASP A 1 344 ? 23.736 48.925 24.643 1.00 17.77 ? 377 ASP A N 1 ATOM 2837 C CA . ASP A 1 344 ? 22.528 48.560 23.876 1.00 18.18 ? 377 ASP A CA 1 ATOM 2838 C C . ASP A 1 344 ? 21.338 48.400 24.823 1.00 17.81 ? 377 ASP A C 1 ATOM 2839 O O . ASP A 1 344 ? 21.271 47.422 25.584 1.00 18.60 ? 377 ASP A O 1 ATOM 2840 C CB . ASP A 1 344 ? 22.804 47.233 23.200 1.00 18.02 ? 377 ASP A CB 1 ATOM 2841 C CG . ASP A 1 344 ? 21.606 46.745 22.468 1.00 19.81 ? 377 ASP A CG 1 ATOM 2842 O OD1 . ASP A 1 344 ? 20.640 47.534 22.176 1.00 19.88 ? 377 ASP A OD1 1 ATOM 2843 O OD2 . ASP A 1 344 ? 21.571 45.551 22.148 1.00 19.99 ? 377 ASP A OD2 1 ATOM 2844 N N . PRO A 1 345 ? 20.362 49.350 24.834 1.00 17.25 ? 378 PRO A N 1 ATOM 2845 C CA . PRO A 1 345 ? 20.232 50.546 24.008 1.00 17.50 ? 378 PRO A CA 1 ATOM 2846 C C . PRO A 1 345 ? 20.510 51.831 24.825 1.00 17.03 ? 378 PRO A C 1 ATOM 2847 O O . PRO A 1 345 ? 20.249 52.936 24.325 1.00 18.05 ? 378 PRO A O 1 ATOM 2848 C CB . PRO A 1 345 ? 18.717 50.567 23.695 1.00 18.54 ? 378 PRO A CB 1 ATOM 2849 C CG . PRO A 1 345 ? 18.109 50.115 25.028 1.00 18.47 ? 378 PRO A CG 1 ATOM 2850 C CD . PRO A 1 345 ? 19.109 49.061 25.553 1.00 18.53 ? 378 PRO A CD 1 ATOM 2851 N N . THR A 1 346 ? 20.942 51.705 26.077 1.00 16.50 ? 379 THR A N 1 ATOM 2852 C CA . THR A 1 346 ? 20.741 52.824 27.012 1.00 16.26 ? 379 THR A CA 1 ATOM 2853 C C . THR A 1 346 ? 21.610 53.992 26.659 1.00 16.61 ? 379 THR A C 1 ATOM 2854 O O . THR A 1 346 ? 21.241 55.107 26.950 1.00 17.19 ? 379 THR A O 1 ATOM 2855 C CB . THR A 1 346 ? 20.889 52.404 28.495 1.00 17.36 ? 379 THR A CB 1 ATOM 2856 O OG1 . THR A 1 346 ? 20.172 51.152 28.687 1.00 16.99 ? 379 THR A OG1 1 ATOM 2857 C CG2 . THR A 1 346 ? 20.228 53.481 29.388 1.00 19.05 ? 379 THR A CG2 1 ATOM 2858 N N . SER A 1 347 ? 22.720 53.756 25.975 1.00 16.59 ? 380 SER A N 1 ATOM 2859 C CA . SER A 1 347 ? 23.518 54.866 25.457 1.00 16.24 ? 380 SER A CA 1 ATOM 2860 C C . SER A 1 347 ? 22.641 55.712 24.487 1.00 16.64 ? 380 SER A C 1 ATOM 2861 O O . SER A 1 347 ? 22.679 56.959 24.521 1.00 17.15 ? 380 SER A O 1 ATOM 2862 C CB . SER A 1 347 ? 24.824 54.330 24.843 1.00 16.40 ? 380 SER A CB 1 ATOM 2863 O OG . SER A 1 347 ? 24.591 53.540 23.664 1.00 17.74 ? 380 SER A OG 1 ATOM 2864 N N . GLY A 1 348 ? 21.787 55.060 23.693 1.00 15.62 ? 381 GLY A N 1 ATOM 2865 C CA . GLY A 1 348 ? 20.875 55.755 22.770 1.00 16.67 ? 381 GLY A CA 1 ATOM 2866 C C . GLY A 1 348 ? 19.717 56.389 23.517 1.00 15.88 ? 381 GLY A C 1 ATOM 2867 O O . GLY A 1 348 ? 19.162 57.378 23.044 1.00 16.50 ? 381 GLY A O 1 ATOM 2868 N N . VAL A 1 349 ? 19.288 55.785 24.620 1.00 17.22 ? 382 VAL A N 1 ATOM 2869 C CA . VAL A 1 349 ? 18.199 56.346 25.461 1.00 16.32 ? 382 VAL A CA 1 ATOM 2870 C C . VAL A 1 349 ? 18.678 57.671 26.019 1.00 15.59 ? 382 VAL A C 1 ATOM 2871 O O . VAL A 1 349 ? 17.944 58.690 25.969 1.00 16.12 ? 382 VAL A O 1 ATOM 2872 C CB . VAL A 1 349 ? 17.889 55.391 26.611 1.00 16.00 ? 382 VAL A CB 1 ATOM 2873 C CG1 . VAL A 1 349 ? 16.886 56.021 27.625 1.00 17.90 ? 382 VAL A CG1 1 ATOM 2874 C CG2 . VAL A 1 349 ? 17.266 54.053 26.085 1.00 16.44 ? 382 VAL A CG2 1 ATOM 2875 N N . ALA A 1 350 ? 19.915 57.670 26.536 1.00 15.60 ? 383 ALA A N 1 ATOM 2876 C CA . ALA A 1 350 ? 20.495 58.906 27.069 1.00 15.80 ? 383 ALA A CA 1 ATOM 2877 C C . ALA A 1 350 ? 20.650 59.985 25.985 1.00 16.49 ? 383 ALA A C 1 ATOM 2878 O O . ALA A 1 350 ? 20.321 61.161 26.191 1.00 17.64 ? 383 ALA A O 1 ATOM 2879 C CB . ALA A 1 350 ? 21.859 58.546 27.677 1.00 16.66 ? 383 ALA A CB 1 ATOM 2880 N N . VAL A 1 351 ? 21.109 59.609 24.816 1.00 16.70 ? 384 VAL A N 1 ATOM 2881 C CA . VAL A 1 351 ? 21.186 60.513 23.711 1.00 17.04 ? 384 VAL A CA 1 ATOM 2882 C C . VAL A 1 351 ? 19.798 61.088 23.344 1.00 18.55 ? 384 VAL A C 1 ATOM 2883 O O . VAL A 1 351 ? 19.657 62.294 23.068 1.00 18.23 ? 384 VAL A O 1 ATOM 2884 C CB . VAL A 1 351 ? 21.843 59.766 22.501 1.00 16.55 ? 384 VAL A CB 1 ATOM 2885 C CG1 . VAL A 1 351 ? 21.504 60.464 21.182 1.00 19.18 ? 384 VAL A CG1 1 ATOM 2886 C CG2 . VAL A 1 351 ? 23.374 59.729 22.714 1.00 20.47 ? 384 VAL A CG2 1 ATOM 2887 N N . LEU A 1 352 ? 18.774 60.240 23.266 1.00 17.56 ? 385 LEU A N 1 ATOM 2888 C CA . LEU A 1 352 ? 17.456 60.730 22.901 1.00 16.63 ? 385 LEU A CA 1 ATOM 2889 C C . LEU A 1 352 ? 16.963 61.788 23.911 1.00 16.78 ? 385 LEU A C 1 ATOM 2890 O O . LEU A 1 352 ? 16.342 62.772 23.534 1.00 17.75 ? 385 LEU A O 1 ATOM 2891 C CB . LEU A 1 352 ? 16.506 59.494 22.781 1.00 18.45 ? 385 LEU A CB 1 ATOM 2892 C CG . LEU A 1 352 ? 15.062 59.750 22.339 1.00 24.43 ? 385 LEU A CG 1 ATOM 2893 C CD1 . LEU A 1 352 ? 14.891 60.725 21.330 1.00 24.10 ? 385 LEU A CD1 1 ATOM 2894 C CD2 . LEU A 1 352 ? 14.372 58.463 21.898 1.00 23.24 ? 385 LEU A CD2 1 ATOM 2895 N N . GLN A 1 353 ? 17.217 61.527 25.186 1.00 15.41 ? 386 GLN A N 1 ATOM 2896 C CA . GLN A 1 353 ? 16.784 62.517 26.212 1.00 15.58 ? 386 GLN A CA 1 ATOM 2897 C C . GLN A 1 353 ? 17.502 63.833 26.012 1.00 16.41 ? 386 GLN A C 1 ATOM 2898 O O . GLN A 1 353 ? 16.877 64.883 26.172 1.00 16.47 ? 386 GLN A O 1 ATOM 2899 C CB . GLN A 1 353 ? 17.017 62.003 27.643 1.00 15.71 ? 386 GLN A CB 1 ATOM 2900 C CG . GLN A 1 353 ? 16.146 60.803 28.048 1.00 16.20 ? 386 GLN A CG 1 ATOM 2901 C CD . GLN A 1 353 ? 14.674 61.001 27.672 1.00 15.32 ? 386 GLN A CD 1 ATOM 2902 O OE1 . GLN A 1 353 ? 14.291 60.723 26.535 1.00 17.76 ? 386 GLN A OE1 1 ATOM 2903 N NE2 . GLN A 1 353 ? 13.871 61.554 28.627 1.00 16.88 ? 386 GLN A NE2 1 ATOM 2904 N N . GLU A 1 354 ? 18.785 63.800 25.671 1.00 17.42 ? 387 GLU A N 1 ATOM 2905 C CA . GLU A 1 354 ? 19.551 65.052 25.550 1.00 17.40 ? 387 GLU A CA 1 ATOM 2906 C C . GLU A 1 354 ? 19.088 65.813 24.301 1.00 17.12 ? 387 GLU A C 1 ATOM 2907 O O . GLU A 1 354 ? 19.033 67.060 24.305 1.00 19.42 ? 387 GLU A O 1 ATOM 2908 C CB . GLU A 1 354 ? 21.068 64.774 25.630 1.00 18.18 ? 387 GLU A CB 1 ATOM 2909 C CG . GLU A 1 354 ? 21.962 66.056 25.545 1.00 16.71 ? 387 GLU A CG 1 ATOM 2910 C CD . GLU A 1 354 ? 21.771 67.028 26.691 1.00 20.74 ? 387 GLU A CD 1 ATOM 2911 O OE1 . GLU A 1 354 ? 20.923 66.815 27.612 1.00 21.42 ? 387 GLU A OE1 1 ATOM 2912 O OE2 . GLU A 1 354 ? 22.559 68.025 26.716 1.00 21.48 ? 387 GLU A OE2 1 ATOM 2913 N N . ILE A 1 355 ? 18.749 65.055 23.253 1.00 16.33 ? 388 ILE A N 1 ATOM 2914 C CA . ILE A 1 355 ? 18.181 65.713 22.103 1.00 14.96 ? 388 ILE A CA 1 ATOM 2915 C C . ILE A 1 355 ? 16.832 66.392 22.415 1.00 16.87 ? 388 ILE A C 1 ATOM 2916 O O . ILE A 1 355 ? 16.596 67.528 21.995 1.00 17.89 ? 388 ILE A O 1 ATOM 2917 C CB . ILE A 1 355 ? 18.055 64.704 20.927 1.00 14.99 ? 388 ILE A CB 1 ATOM 2918 C CG1 . ILE A 1 355 ? 19.440 64.208 20.481 1.00 16.50 ? 388 ILE A CG1 1 ATOM 2919 C CG2 . ILE A 1 355 ? 17.308 65.347 19.741 1.00 15.39 ? 388 ILE A CG2 1 ATOM 2920 C CD1 . ILE A 1 355 ? 19.373 62.967 19.511 1.00 18.62 ? 388 ILE A CD1 1 ATOM 2921 N N . ALA A 1 356 ? 15.926 65.624 23.052 1.00 15.91 ? 389 ALA A N 1 ATOM 2922 C CA . ALA A 1 356 ? 14.632 66.207 23.379 1.00 16.56 ? 389 ALA A CA 1 ATOM 2923 C C . ALA A 1 356 ? 14.858 67.430 24.280 1.00 17.56 ? 389 ALA A C 1 ATOM 2924 O O . ALA A 1 356 ? 14.169 68.459 24.100 1.00 17.56 ? 389 ALA A O 1 ATOM 2925 C CB . ALA A 1 356 ? 13.800 65.108 24.122 1.00 17.13 ? 389 ALA A CB 1 ATOM 2926 N N . ARG A 1 357 ? 15.819 67.366 25.223 1.00 16.35 ? 390 ARG A N 1 ATOM 2927 C CA . ARG A 1 357 ? 16.074 68.528 26.097 1.00 17.03 ? 390 ARG A CA 1 ATOM 2928 C C . ARG A 1 357 ? 16.472 69.735 25.274 1.00 17.80 ? 390 ARG A C 1 ATOM 2929 O O . ARG A 1 357 ? 15.992 70.846 25.522 1.00 18.26 ? 390 ARG A O 1 ATOM 2930 C CB . ARG A 1 357 ? 17.172 68.230 27.137 1.00 16.42 ? 390 ARG A CB 1 ATOM 2931 C CG . ARG A 1 357 ? 17.251 69.304 28.220 1.00 15.60 ? 390 ARG A CG 1 ATOM 2932 C CD . ARG A 1 357 ? 18.464 69.062 29.130 1.00 19.29 ? 390 ARG A CD 1 ATOM 2933 N NE . ARG A 1 357 ? 19.692 69.295 28.361 1.00 20.66 ? 390 ARG A NE 1 ATOM 2934 C CZ . ARG A 1 357 ? 20.162 70.498 28.008 1.00 19.14 ? 390 ARG A CZ 1 ATOM 2935 N NH1 . ARG A 1 357 ? 21.252 70.550 27.268 1.00 20.24 ? 390 ARG A NH1 1 ATOM 2936 N NH2 . ARG A 1 357 ? 19.578 71.665 28.419 1.00 19.91 ? 390 ARG A NH2 1 ATOM 2937 N N . SER A 1 358 ? 17.325 69.524 24.289 1.00 17.82 ? 391 SER A N 1 ATOM 2938 C CA . SER A 1 358 ? 17.814 70.632 23.490 1.00 18.22 ? 391 SER A CA 1 ATOM 2939 C C . SER A 1 358 ? 16.714 71.214 22.579 1.00 17.79 ? 391 SER A C 1 ATOM 2940 O O . SER A 1 358 ? 16.665 72.458 22.442 1.00 19.11 ? 391 SER A O 1 ATOM 2941 C CB . SER A 1 358 ? 19.029 70.185 22.680 1.00 18.17 ? 391 SER A CB 1 ATOM 2942 O OG . SER A 1 358 ? 19.591 71.364 22.054 1.00 19.99 ? 391 SER A OG 1 ATOM 2943 N N . PHE A 1 359 ? 15.844 70.361 21.974 1.00 18.69 ? 392 PHE A N 1 ATOM 2944 C CA . PHE A 1 359 ? 14.687 70.911 21.255 1.00 18.42 ? 392 PHE A CA 1 ATOM 2945 C C . PHE A 1 359 ? 13.798 71.699 22.238 1.00 19.04 ? 392 PHE A C 1 ATOM 2946 O O . PHE A 1 359 ? 13.245 72.746 21.888 1.00 20.17 ? 392 PHE A O 1 ATOM 2947 C CB . PHE A 1 359 ? 13.846 69.824 20.595 1.00 18.61 ? 392 PHE A CB 1 ATOM 2948 C CG . PHE A 1 359 ? 14.417 69.386 19.269 1.00 19.02 ? 392 PHE A CG 1 ATOM 2949 C CD1 . PHE A 1 359 ? 14.360 70.264 18.212 1.00 19.24 ? 392 PHE A CD1 1 ATOM 2950 C CD2 . PHE A 1 359 ? 14.989 68.097 19.071 1.00 16.66 ? 392 PHE A CD2 1 ATOM 2951 C CE1 . PHE A 1 359 ? 14.839 69.904 16.964 1.00 16.32 ? 392 PHE A CE1 1 ATOM 2952 C CE2 . PHE A 1 359 ? 15.497 67.722 17.854 1.00 17.62 ? 392 PHE A CE2 1 ATOM 2953 C CZ . PHE A 1 359 ? 15.434 68.664 16.788 1.00 17.19 ? 392 PHE A CZ 1 ATOM 2954 N N . GLY A 1 360 ? 13.668 71.222 23.474 1.00 19.35 ? 393 GLY A N 1 ATOM 2955 C CA . GLY A 1 360 ? 12.858 71.974 24.481 1.00 20.04 ? 393 GLY A CA 1 ATOM 2956 C C . GLY A 1 360 ? 13.465 73.327 24.769 1.00 19.95 ? 393 GLY A C 1 ATOM 2957 O O . GLY A 1 360 ? 12.734 74.334 24.932 1.00 21.05 ? 393 GLY A O 1 ATOM 2958 N N . LYS A 1 361 ? 14.785 73.411 24.812 1.00 20.31 ? 394 LYS A N 1 ATOM 2959 C CA . LYS A 1 361 ? 15.428 74.740 25.026 1.00 20.64 ? 394 LYS A CA 1 ATOM 2960 C C . LYS A 1 361 ? 15.153 75.688 23.846 1.00 21.20 ? 394 LYS A C 1 ATOM 2961 O O . LYS A 1 361 ? 14.896 76.885 24.050 1.00 21.98 ? 394 LYS A O 1 ATOM 2962 C CB . LYS A 1 361 ? 16.909 74.588 25.188 1.00 23.28 ? 394 LYS A CB 1 ATOM 2963 C CG . LYS A 1 361 ? 17.302 74.014 26.507 1.00 29.14 ? 394 LYS A CG 1 ATOM 2964 C CD . LYS A 1 361 ? 17.642 75.180 27.453 1.00 35.67 ? 394 LYS A CD 1 ATOM 2965 C CE . LYS A 1 361 ? 16.619 75.368 28.552 1.00 41.99 ? 394 LYS A CE 1 ATOM 2966 N NZ . LYS A 1 361 ? 17.113 75.062 29.965 1.00 44.51 ? 394 LYS A NZ 1 ATOM 2967 N N . LEU A 1 362 ? 15.171 75.164 22.609 1.00 20.18 ? 395 LEU A N 1 ATOM 2968 C CA . LEU A 1 362 ? 14.786 76.021 21.459 1.00 20.12 ? 395 LEU A CA 1 ATOM 2969 C C . LEU A 1 362 ? 13.365 76.542 21.675 1.00 20.71 ? 395 LEU A C 1 ATOM 2970 O O . LEU A 1 362 ? 13.077 77.743 21.492 1.00 20.89 ? 395 LEU A O 1 ATOM 2971 C CB . LEU A 1 362 ? 14.817 75.254 20.124 1.00 19.81 ? 395 LEU A CB 1 ATOM 2972 C CG . LEU A 1 362 ? 16.191 74.784 19.575 1.00 20.87 ? 395 LEU A CG 1 ATOM 2973 C CD1 . LEU A 1 362 ? 15.988 74.109 18.199 1.00 20.37 ? 395 LEU A CD1 1 ATOM 2974 C CD2 . LEU A 1 362 ? 17.179 75.961 19.503 1.00 23.12 ? 395 LEU A CD2 1 ATOM 2975 N N . MET A 1 363 ? 12.455 75.643 22.040 1.00 19.27 ? 396 MET A N 1 ATOM 2976 C CA . MET A 1 363 ? 11.065 76.062 22.271 1.00 18.68 ? 396 MET A CA 1 ATOM 2977 C C . MET A 1 363 ? 10.934 77.150 23.327 1.00 19.79 ? 396 MET A C 1 ATOM 2978 O O . MET A 1 363 ? 10.059 78.015 23.205 1.00 19.56 ? 396 MET A O 1 ATOM 2979 C CB . MET A 1 363 ? 10.164 74.865 22.611 1.00 19.33 ? 396 MET A CB 1 ATOM 2980 C CG A MET A 1 363 ? 10.118 73.925 21.373 0.70 19.23 ? 396 MET A CG 1 ATOM 2981 C CG B MET A 1 363 ? 9.989 73.775 21.530 0.30 17.99 ? 396 MET A CG 1 ATOM 2982 S SD A MET A 1 363 ? 8.942 72.644 21.776 0.70 25.40 ? 396 MET A SD 1 ATOM 2983 S SD B MET A 1 363 ? 9.014 72.382 22.204 0.30 15.56 ? 396 MET A SD 1 ATOM 2984 C CE A MET A 1 363 ? 9.835 71.701 23.016 0.70 22.91 ? 396 MET A CE 1 ATOM 2985 C CE B MET A 1 363 ? 7.357 73.053 22.136 0.30 14.25 ? 396 MET A CE 1 ATOM 2986 N N . SER A 1 364 ? 11.765 77.061 24.367 1.00 19.96 ? 397 SER A N 1 ATOM 2987 C CA . SER A 1 364 ? 11.708 78.042 25.474 1.00 21.24 ? 397 SER A CA 1 ATOM 2988 C C . SER A 1 364 ? 11.980 79.467 25.011 1.00 23.71 ? 397 SER A C 1 ATOM 2989 O O . SER A 1 364 ? 11.654 80.427 25.746 1.00 24.55 ? 397 SER A O 1 ATOM 2990 C CB . SER A 1 364 ? 12.684 77.636 26.611 1.00 21.33 ? 397 SER A CB 1 ATOM 2991 O OG . SER A 1 364 ? 14.010 77.989 26.287 1.00 22.83 ? 397 SER A OG 1 ATOM 2992 N N . LYS A 1 365 ? 12.607 79.617 23.847 1.00 23.49 ? 398 LYS A N 1 ATOM 2993 C CA . LYS A 1 365 ? 12.894 80.945 23.282 1.00 25.49 ? 398 LYS A CA 1 ATOM 2994 C C . LYS A 1 365 ? 11.969 81.250 22.103 1.00 25.45 ? 398 LYS A C 1 ATOM 2995 O O . LYS A 1 365 ? 12.232 82.175 21.312 1.00 26.80 ? 398 LYS A O 1 ATOM 2996 C CB . LYS A 1 365 ? 14.376 81.030 22.876 1.00 25.80 ? 398 LYS A CB 1 ATOM 2997 C CG . LYS A 1 365 ? 15.338 80.968 24.093 1.00 29.62 ? 398 LYS A CG 1 ATOM 2998 C CD . LYS A 1 365 ? 15.129 82.212 24.922 1.00 36.19 ? 398 LYS A CD 1 ATOM 2999 C CE . LYS A 1 365 ? 16.087 82.377 26.089 1.00 37.25 ? 398 LYS A CE 1 ATOM 3000 N NZ . LYS A 1 365 ? 15.648 83.657 26.784 1.00 40.87 ? 398 LYS A NZ 1 ATOM 3001 N N . GLY A 1 366 ? 10.902 80.457 21.954 1.00 23.92 ? 399 GLY A N 1 ATOM 3002 C CA . GLY A 1 366 ? 9.858 80.794 21.002 1.00 23.87 ? 399 GLY A CA 1 ATOM 3003 C C . GLY A 1 366 ? 9.908 80.080 19.671 1.00 24.46 ? 399 GLY A C 1 ATOM 3004 O O . GLY A 1 366 ? 9.035 80.310 18.836 1.00 25.55 ? 399 GLY A O 1 ATOM 3005 N N . TRP A 1 367 ? 10.901 79.202 19.462 1.00 22.22 ? 400 TRP A N 1 ATOM 3006 C CA . TRP A 1 367 ? 10.995 78.435 18.200 1.00 20.17 ? 400 TRP A CA 1 ATOM 3007 C C . TRP A 1 367 ? 9.942 77.370 18.159 1.00 19.56 ? 400 TRP A C 1 ATOM 3008 O O . TRP A 1 367 ? 9.609 76.730 19.167 1.00 19.69 ? 400 TRP A O 1 ATOM 3009 C CB . TRP A 1 367 ? 12.365 77.787 18.118 1.00 19.30 ? 400 TRP A CB 1 ATOM 3010 C CG . TRP A 1 367 ? 12.561 76.878 16.944 1.00 20.92 ? 400 TRP A CG 1 ATOM 3011 C CD1 . TRP A 1 367 ? 12.941 77.212 15.665 1.00 19.42 ? 400 TRP A CD1 1 ATOM 3012 C CD2 . TRP A 1 367 ? 12.404 75.458 16.952 1.00 19.99 ? 400 TRP A CD2 1 ATOM 3013 N NE1 . TRP A 1 367 ? 13.030 76.087 14.882 1.00 21.50 ? 400 TRP A NE1 1 ATOM 3014 C CE2 . TRP A 1 367 ? 12.696 74.998 15.652 1.00 20.82 ? 400 TRP A CE2 1 ATOM 3015 C CE3 . TRP A 1 367 ? 12.042 74.537 17.945 1.00 20.59 ? 400 TRP A CE3 1 ATOM 3016 C CZ2 . TRP A 1 367 ? 12.692 73.662 15.321 1.00 20.48 ? 400 TRP A CZ2 1 ATOM 3017 C CZ3 . TRP A 1 367 ? 11.996 73.165 17.590 1.00 19.11 ? 400 TRP A CZ3 1 ATOM 3018 C CH2 . TRP A 1 367 ? 12.331 72.762 16.294 1.00 19.34 ? 400 TRP A CH2 1 ATOM 3019 N N . ARG A 1 368 ? 9.422 77.138 16.953 1.00 19.41 ? 401 ARG A N 1 ATOM 3020 C CA . ARG A 1 368 ? 8.631 75.930 16.702 1.00 19.46 ? 401 ARG A CA 1 ATOM 3021 C C . ARG A 1 368 ? 9.047 75.400 15.337 1.00 19.39 ? 401 ARG A C 1 ATOM 3022 O O . ARG A 1 368 ? 9.338 76.184 14.419 1.00 19.14 ? 401 ARG A O 1 ATOM 3023 C CB . ARG A 1 368 ? 7.166 76.260 16.607 1.00 19.63 ? 401 ARG A CB 1 ATOM 3024 C CG . ARG A 1 368 ? 6.593 76.914 17.838 1.00 22.25 ? 401 ARG A CG 1 ATOM 3025 C CD . ARG A 1 368 ? 6.378 75.933 18.918 1.00 27.01 ? 401 ARG A CD 1 ATOM 3026 N NE . ARG A 1 368 ? 5.485 74.877 18.458 1.00 30.75 ? 401 ARG A NE 1 ATOM 3027 C CZ . ARG A 1 368 ? 4.976 73.928 19.251 1.00 32.04 ? 401 ARG A CZ 1 ATOM 3028 N NH1 . ARG A 1 368 ? 5.196 73.925 20.579 1.00 33.68 ? 401 ARG A NH1 1 ATOM 3029 N NH2 . ARG A 1 368 ? 4.235 73.000 18.713 1.00 24.81 ? 401 ARG A NH2 1 ATOM 3030 N N . PRO A 1 369 ? 9.050 74.075 15.142 1.00 19.27 ? 402 PRO A N 1 ATOM 3031 C CA . PRO A 1 369 ? 9.523 73.540 13.877 1.00 19.49 ? 402 PRO A CA 1 ATOM 3032 C C . PRO A 1 369 ? 8.451 73.741 12.780 1.00 19.41 ? 402 PRO A C 1 ATOM 3033 O O . PRO A 1 369 ? 7.267 73.912 13.067 1.00 19.66 ? 402 PRO A O 1 ATOM 3034 C CB . PRO A 1 369 ? 9.633 72.021 14.156 1.00 19.36 ? 402 PRO A CB 1 ATOM 3035 C CG . PRO A 1 369 ? 8.582 71.769 15.229 1.00 18.87 ? 402 PRO A CG 1 ATOM 3036 C CD . PRO A 1 369 ? 8.621 73.049 16.117 1.00 19.12 ? 402 PRO A CD 1 ATOM 3037 N N . ARG A 1 370 ? 8.865 73.747 11.517 1.00 17.86 ? 403 ARG A N 1 ATOM 3038 C CA . ARG A 1 370 ? 7.928 73.805 10.384 1.00 18.30 ? 403 ARG A CA 1 ATOM 3039 C C . ARG A 1 370 ? 6.973 72.574 10.356 1.00 18.23 ? 403 ARG A C 1 ATOM 3040 O O . ARG A 1 370 ? 5.725 72.723 10.255 1.00 18.12 ? 403 ARG A O 1 ATOM 3041 C CB . ARG A 1 370 ? 8.753 73.893 9.109 1.00 18.70 ? 403 ARG A CB 1 ATOM 3042 C CG . ARG A 1 370 ? 7.867 73.911 7.836 1.00 19.02 ? 403 ARG A CG 1 ATOM 3043 C CD . ARG A 1 370 ? 8.748 73.781 6.608 1.00 19.13 ? 403 ARG A CD 1 ATOM 3044 N NE . ARG A 1 370 ? 7.904 73.724 5.392 1.00 19.81 ? 403 ARG A NE 1 ATOM 3045 C CZ . ARG A 1 370 ? 7.492 74.794 4.704 1.00 20.31 ? 403 ARG A CZ 1 ATOM 3046 N NH1 . ARG A 1 370 ? 7.833 76.036 5.104 1.00 20.98 ? 403 ARG A NH1 1 ATOM 3047 N NH2 . ARG A 1 370 ? 6.689 74.626 3.655 1.00 20.68 ? 403 ARG A NH2 1 ATOM 3048 N N . ARG A 1 371 ? 7.588 71.380 10.380 1.00 17.83 ? 404 ARG A N 1 ATOM 3049 C CA . ARG A 1 371 ? 6.835 70.106 10.396 1.00 17.71 ? 404 ARG A CA 1 ATOM 3050 C C . ARG A 1 371 ? 6.790 69.550 11.804 1.00 18.76 ? 404 ARG A C 1 ATOM 3051 O O . ARG A 1 371 ? 7.355 70.153 12.738 1.00 18.56 ? 404 ARG A O 1 ATOM 3052 C CB . ARG A 1 371 ? 7.567 69.064 9.504 1.00 17.34 ? 404 ARG A CB 1 ATOM 3053 C CG . ARG A 1 371 ? 7.728 69.594 8.065 1.00 16.85 ? 404 ARG A CG 1 ATOM 3054 C CD . ARG A 1 371 ? 8.426 68.513 7.136 1.00 19.60 ? 404 ARG A CD 1 ATOM 3055 N NE . ARG A 1 371 ? 8.497 69.052 5.767 1.00 18.71 ? 404 ARG A NE 1 ATOM 3056 C CZ . ARG A 1 371 ? 9.429 69.941 5.401 1.00 19.61 ? 404 ARG A CZ 1 ATOM 3057 N NH1 . ARG A 1 371 ? 10.577 70.080 6.118 1.00 18.91 ? 404 ARG A NH1 1 ATOM 3058 N NH2 . ARG A 1 371 ? 9.248 70.662 4.303 1.00 19.43 ? 404 ARG A NH2 1 ATOM 3059 N N . THR A 1 372 ? 6.088 68.447 12.007 1.00 16.44 ? 405 THR A N 1 ATOM 3060 C CA . THR A 1 372 ? 5.932 67.869 13.358 1.00 16.76 ? 405 THR A CA 1 ATOM 3061 C C . THR A 1 372 ? 7.046 66.875 13.663 1.00 17.22 ? 405 THR A C 1 ATOM 3062 O O . THR A 1 372 ? 7.389 66.037 12.810 1.00 17.51 ? 405 THR A O 1 ATOM 3063 C CB . THR A 1 372 ? 4.594 67.127 13.376 1.00 16.86 ? 405 THR A CB 1 ATOM 3064 O OG1 . THR A 1 372 ? 3.559 68.131 13.434 1.00 17.58 ? 405 THR A OG1 1 ATOM 3065 C CG2 . THR A 1 372 ? 4.423 66.226 14.632 1.00 17.50 ? 405 THR A CG2 1 ATOM 3066 N N . ILE A 1 373 ? 7.678 66.981 14.846 1.00 16.48 ? 406 ILE A N 1 ATOM 3067 C CA . ILE A 1 373 ? 8.605 65.932 15.314 1.00 16.82 ? 406 ILE A CA 1 ATOM 3068 C C . ILE A 1 373 ? 7.842 64.978 16.212 1.00 17.40 ? 406 ILE A C 1 ATOM 3069 O O . ILE A 1 373 ? 7.088 65.392 17.072 1.00 17.47 ? 406 ILE A O 1 ATOM 3070 C CB . ILE A 1 373 ? 9.761 66.514 16.222 1.00 16.82 ? 406 ILE A CB 1 ATOM 3071 C CG1 . ILE A 1 373 ? 10.511 67.624 15.461 1.00 18.43 ? 406 ILE A CG1 1 ATOM 3072 C CG2 . ILE A 1 373 ? 10.756 65.422 16.606 1.00 18.59 ? 406 ILE A CG2 1 ATOM 3073 C CD1 . ILE A 1 373 ? 11.428 68.418 16.430 1.00 18.57 ? 406 ILE A CD1 1 ATOM 3074 N N . ILE A 1 374 ? 8.027 63.686 15.934 1.00 17.19 ? 407 ILE A N 1 ATOM 3075 C CA . ILE A 1 374 ? 7.517 62.603 16.802 1.00 15.99 ? 407 ILE A CA 1 ATOM 3076 C C . ILE A 1 374 ? 8.706 61.988 17.492 1.00 18.20 ? 407 ILE A C 1 ATOM 3077 O O . ILE A 1 374 ? 9.610 61.492 16.812 1.00 18.34 ? 407 ILE A O 1 ATOM 3078 C CB . ILE A 1 374 ? 6.743 61.523 15.952 1.00 16.98 ? 407 ILE A CB 1 ATOM 3079 C CG1 . ILE A 1 374 ? 5.562 62.181 15.256 1.00 17.27 ? 407 ILE A CG1 1 ATOM 3080 C CG2 . ILE A 1 374 ? 6.250 60.419 16.932 1.00 18.00 ? 407 ILE A CG2 1 ATOM 3081 C CD1 . ILE A 1 374 ? 4.781 61.157 14.341 1.00 19.07 ? 407 ILE A CD1 1 ATOM 3082 N N . PHE A 1 375 ? 8.696 62.021 18.816 1.00 16.93 ? 408 PHE A N 1 ATOM 3083 C CA . PHE A 1 375 ? 9.739 61.327 19.639 1.00 16.96 ? 408 PHE A CA 1 ATOM 3084 C C . PHE A 1 375 ? 9.145 60.031 20.087 1.00 17.50 ? 408 PHE A C 1 ATOM 3085 O O . PHE A 1 375 ? 8.001 59.976 20.573 1.00 16.79 ? 408 PHE A O 1 ATOM 3086 C CB . PHE A 1 375 ? 10.027 62.169 20.881 1.00 16.52 ? 408 PHE A CB 1 ATOM 3087 C CG . PHE A 1 375 ? 10.693 63.482 20.563 1.00 15.89 ? 408 PHE A CG 1 ATOM 3088 C CD1 . PHE A 1 375 ? 12.063 63.627 20.622 1.00 17.53 ? 408 PHE A CD1 1 ATOM 3089 C CD2 . PHE A 1 375 ? 9.888 64.603 20.254 1.00 17.74 ? 408 PHE A CD2 1 ATOM 3090 C CE1 . PHE A 1 375 ? 12.669 64.877 20.334 1.00 18.13 ? 408 PHE A CE1 1 ATOM 3091 C CE2 . PHE A 1 375 ? 10.468 65.849 19.992 1.00 19.33 ? 408 PHE A CE2 1 ATOM 3092 C CZ . PHE A 1 375 ? 11.869 65.984 20.042 1.00 16.22 ? 408 PHE A CZ 1 ATOM 3093 N N . ALA A 1 376 ? 9.940 58.966 20.033 1.00 16.47 ? 409 ALA A N 1 ATOM 3094 C CA . ALA A 1 376 ? 9.416 57.642 20.489 1.00 16.18 ? 409 ALA A CA 1 ATOM 3095 C C . ALA A 1 376 ? 10.467 56.833 21.252 1.00 16.86 ? 409 ALA A C 1 ATOM 3096 O O . ALA A 1 376 ? 11.593 56.680 20.741 1.00 18.07 ? 409 ALA A O 1 ATOM 3097 C CB . ALA A 1 376 ? 8.937 56.828 19.260 1.00 18.34 ? 409 ALA A CB 1 ATOM 3098 N N . SER A 1 377 ? 10.092 56.345 22.435 1.00 16.62 ? 410 SER A N 1 ATOM 3099 C CA . SER A 1 377 ? 10.930 55.438 23.173 1.00 16.54 ? 410 SER A CA 1 ATOM 3100 C C . SER A 1 377 ? 10.256 54.056 23.075 1.00 16.60 ? 410 SER A C 1 ATOM 3101 O O . SER A 1 377 ? 9.161 53.853 23.654 1.00 16.82 ? 410 SER A O 1 ATOM 3102 C CB . SER A 1 377 ? 10.976 55.901 24.638 1.00 17.11 ? 410 SER A CB 1 ATOM 3103 O OG . SER A 1 377 ? 11.685 54.930 25.445 1.00 18.10 ? 410 SER A OG 1 ATOM 3104 N N . TRP A 1 378 ? 10.867 53.131 22.312 1.00 15.55 ? 411 TRP A N 1 ATOM 3105 C CA . TRP A 1 378 ? 10.163 51.886 22.047 1.00 16.65 ? 411 TRP A CA 1 ATOM 3106 C C . TRP A 1 378 ? 10.424 50.832 23.086 1.00 16.87 ? 411 TRP A C 1 ATOM 3107 O O . TRP A 1 378 ? 11.535 50.771 23.695 1.00 17.10 ? 411 TRP A O 1 ATOM 3108 C CB . TRP A 1 378 ? 10.709 51.306 20.749 1.00 15.51 ? 411 TRP A CB 1 ATOM 3109 C CG . TRP A 1 378 ? 10.647 52.202 19.524 1.00 16.61 ? 411 TRP A CG 1 ATOM 3110 C CD1 . TRP A 1 378 ? 11.705 52.527 18.696 1.00 17.85 ? 411 TRP A CD1 1 ATOM 3111 C CD2 . TRP A 1 378 ? 9.477 52.835 18.938 1.00 17.71 ? 411 TRP A CD2 1 ATOM 3112 N NE1 . TRP A 1 378 ? 11.273 53.324 17.642 1.00 16.60 ? 411 TRP A NE1 1 ATOM 3113 C CE2 . TRP A 1 378 ? 9.914 53.499 17.776 1.00 16.19 ? 411 TRP A CE2 1 ATOM 3114 C CE3 . TRP A 1 378 ? 8.115 52.894 19.290 1.00 17.52 ? 411 TRP A CE3 1 ATOM 3115 C CZ2 . TRP A 1 378 ? 9.021 54.192 16.931 1.00 15.85 ? 411 TRP A CZ2 1 ATOM 3116 C CZ3 . TRP A 1 378 ? 7.230 53.603 18.484 1.00 17.80 ? 411 TRP A CZ3 1 ATOM 3117 C CH2 . TRP A 1 378 ? 7.701 54.298 17.351 1.00 17.40 ? 411 TRP A CH2 1 ATOM 3118 N N . ASP A 1 379 ? 9.435 49.955 23.247 1.00 16.32 ? 412 ASP A N 1 ATOM 3119 C CA . ASP A 1 379 ? 9.620 48.826 24.140 1.00 16.59 ? 412 ASP A CA 1 ATOM 3120 C C . ASP A 1 379 ? 9.788 47.520 23.297 1.00 16.11 ? 412 ASP A C 1 ATOM 3121 O O . ASP A 1 379 ? 9.459 47.441 22.099 1.00 16.97 ? 412 ASP A O 1 ATOM 3122 C CB . ASP A 1 379 ? 8.367 48.718 25.027 1.00 17.37 ? 412 ASP A CB 1 ATOM 3123 C CG . ASP A 1 379 ? 8.603 47.955 26.377 1.00 16.78 ? 412 ASP A CG 1 ATOM 3124 O OD1 . ASP A 1 379 ? 9.683 47.351 26.602 1.00 16.91 ? 412 ASP A OD1 1 ATOM 3125 O OD2 . ASP A 1 379 ? 7.642 47.999 27.193 1.00 17.33 ? 412 ASP A OD2 1 ATOM 3126 N N . ALA A 1 380 ? 10.329 46.514 24.016 1.00 16.73 ? 413 ALA A N 1 ATOM 3127 C CA . ALA A 1 380 ? 10.442 45.146 23.479 1.00 17.18 ? 413 ALA A CA 1 ATOM 3128 C C . ALA A 1 380 ? 11.143 45.053 22.121 1.00 16.71 ? 413 ALA A C 1 ATOM 3129 O O . ALA A 1 380 ? 10.873 44.109 21.326 1.00 17.38 ? 413 ALA A O 1 ATOM 3130 C CB . ALA A 1 380 ? 9.045 44.464 23.417 1.00 16.66 ? 413 ALA A CB 1 ATOM 3131 N N . GLU A 1 381 ? 12.074 45.970 21.862 1.00 16.21 ? 414 GLU A N 1 ATOM 3132 C CA . GLU A 1 381 ? 12.883 45.765 20.659 1.00 15.24 ? 414 GLU A CA 1 ATOM 3133 C C . GLU A 1 381 ? 13.665 44.439 20.747 1.00 16.55 ? 414 GLU A C 1 ATOM 3134 O O . GLU A 1 381 ? 13.841 43.762 19.714 1.00 17.12 ? 414 GLU A O 1 ATOM 3135 C CB . GLU A 1 381 ? 13.896 46.911 20.502 1.00 16.62 ? 414 GLU A CB 1 ATOM 3136 C CG . GLU A 1 381 ? 14.675 46.930 19.204 1.00 18.40 ? 414 GLU A CG 1 ATOM 3137 C CD . GLU A 1 381 ? 15.996 46.157 19.248 1.00 23.91 ? 414 GLU A CD 1 ATOM 3138 O OE1 . GLU A 1 381 ? 16.414 45.568 20.275 1.00 20.06 ? 414 GLU A OE1 1 ATOM 3139 O OE2 . GLU A 1 381 ? 16.627 46.144 18.162 1.00 22.77 ? 414 GLU A OE2 1 ATOM 3140 N N . GLU A 1 382 ? 14.088 44.055 21.944 1.00 15.70 ? 415 GLU A N 1 ATOM 3141 C CA . GLU A 1 382 ? 14.968 42.866 22.016 1.00 15.51 ? 415 GLU A CA 1 ATOM 3142 C C . GLU A 1 382 ? 14.199 41.564 21.742 1.00 16.34 ? 415 GLU A C 1 ATOM 3143 O O . GLU A 1 382 ? 14.818 40.492 21.570 1.00 16.97 ? 415 GLU A O 1 ATOM 3144 C CB . GLU A 1 382 ? 15.548 42.762 23.433 1.00 16.38 ? 415 GLU A CB 1 ATOM 3145 C CG . GLU A 1 382 ? 16.554 43.887 23.747 1.00 16.83 ? 415 GLU A CG 1 ATOM 3146 C CD . GLU A 1 382 ? 17.821 43.881 22.902 1.00 18.28 ? 415 GLU A CD 1 ATOM 3147 O OE1 . GLU A 1 382 ? 17.994 43.056 22.012 1.00 19.85 ? 415 GLU A OE1 1 ATOM 3148 O OE2 . GLU A 1 382 ? 18.706 44.742 23.163 1.00 19.55 ? 415 GLU A OE2 1 ATOM 3149 N N . PHE A 1 383 ? 12.862 41.622 21.704 1.00 16.25 ? 416 PHE A N 1 ATOM 3150 C CA . PHE A 1 383 ? 12.007 40.480 21.462 1.00 15.90 ? 416 PHE A CA 1 ATOM 3151 C C . PHE A 1 383 ? 11.478 40.426 20.012 1.00 16.55 ? 416 PHE A C 1 ATOM 3152 O O . PHE A 1 383 ? 10.542 39.669 19.722 1.00 18.62 ? 416 PHE A O 1 ATOM 3153 C CB . PHE A 1 383 ? 10.867 40.502 22.474 1.00 16.93 ? 416 PHE A CB 1 ATOM 3154 C CG . PHE A 1 383 ? 11.322 40.154 23.861 1.00 17.48 ? 416 PHE A CG 1 ATOM 3155 C CD1 . PHE A 1 383 ? 11.246 38.849 24.326 1.00 17.67 ? 416 PHE A CD1 1 ATOM 3156 C CD2 . PHE A 1 383 ? 11.830 41.159 24.686 1.00 17.28 ? 416 PHE A CD2 1 ATOM 3157 C CE1 . PHE A 1 383 ? 11.671 38.523 25.625 1.00 16.81 ? 416 PHE A CE1 1 ATOM 3158 C CE2 . PHE A 1 383 ? 12.324 40.835 25.967 1.00 16.85 ? 416 PHE A CE2 1 ATOM 3159 C CZ . PHE A 1 383 ? 12.181 39.536 26.433 1.00 17.59 ? 416 PHE A CZ 1 ATOM 3160 N N . GLY A 1 384 ? 12.070 41.234 19.143 1.00 16.92 ? 417 GLY A N 1 ATOM 3161 C CA . GLY A 1 384 ? 11.721 41.203 17.703 1.00 16.94 ? 417 GLY A CA 1 ATOM 3162 C C . GLY A 1 384 ? 11.179 42.566 17.182 1.00 17.03 ? 417 GLY A C 1 ATOM 3163 O O . GLY A 1 384 ? 10.295 42.571 16.312 1.00 17.88 ? 417 GLY A O 1 ATOM 3164 N N . LEU A 1 385 ? 11.711 43.669 17.730 1.00 16.94 ? 418 LEU A N 1 ATOM 3165 C CA . LEU A 1 385 ? 11.246 44.997 17.231 1.00 15.89 ? 418 LEU A CA 1 ATOM 3166 C C . LEU A 1 385 ? 9.756 45.168 17.543 1.00 16.33 ? 418 LEU A C 1 ATOM 3167 O O . LEU A 1 385 ? 9.006 45.802 16.761 1.00 17.11 ? 418 LEU A O 1 ATOM 3168 C CB . LEU A 1 385 ? 11.542 45.212 15.728 1.00 17.59 ? 418 LEU A CB 1 ATOM 3169 C CG . LEU A 1 385 ? 12.910 44.677 15.228 1.00 19.13 ? 418 LEU A CG 1 ATOM 3170 C CD1 . LEU A 1 385 ? 13.138 45.006 13.729 1.00 22.11 ? 418 LEU A CD1 1 ATOM 3171 C CD2 . LEU A 1 385 ? 14.013 45.266 16.045 1.00 20.26 ? 418 LEU A CD2 1 ATOM 3172 N N . LEU A 1 386 ? 9.287 44.675 18.680 1.00 15.97 ? 419 LEU A N 1 ATOM 3173 C CA . LEU A 1 386 ? 7.837 44.546 18.828 1.00 15.71 ? 419 LEU A CA 1 ATOM 3174 C C . LEU A 1 386 ? 7.169 45.892 19.052 1.00 16.14 ? 419 LEU A C 1 ATOM 3175 O O . LEU A 1 386 ? 6.160 46.178 18.388 1.00 17.20 ? 419 LEU A O 1 ATOM 3176 C CB . LEU A 1 386 ? 7.489 43.583 19.994 1.00 16.42 ? 419 LEU A CB 1 ATOM 3177 C CG . LEU A 1 386 ? 8.117 42.191 19.829 1.00 16.51 ? 419 LEU A CG 1 ATOM 3178 C CD1 . LEU A 1 386 ? 7.510 41.264 20.908 1.00 18.08 ? 419 LEU A CD1 1 ATOM 3179 C CD2 . LEU A 1 386 ? 7.867 41.518 18.430 1.00 18.45 ? 419 LEU A CD2 1 ATOM 3180 N N . GLY A 1 387 ? 7.674 46.742 19.946 1.00 15.57 ? 420 GLY A N 1 ATOM 3181 C CA . GLY A 1 387 ? 6.959 48.025 20.222 1.00 16.25 ? 420 GLY A CA 1 ATOM 3182 C C . GLY A 1 387 ? 6.974 48.937 18.996 1.00 15.99 ? 420 GLY A C 1 ATOM 3183 O O . GLY A 1 387 ? 5.942 49.601 18.715 1.00 17.19 ? 420 GLY A O 1 ATOM 3184 N N . SER A 1 388 ? 8.111 49.031 18.309 1.00 15.69 ? 421 SER A N 1 ATOM 3185 C CA . SER A 1 388 ? 8.157 49.947 17.169 1.00 15.58 ? 421 SER A CA 1 ATOM 3186 C C . SER A 1 388 ? 7.307 49.392 16.052 1.00 17.29 ? 421 SER A C 1 ATOM 3187 O O . SER A 1 388 ? 6.651 50.168 15.341 1.00 17.65 ? 421 SER A O 1 ATOM 3188 C CB . SER A 1 388 ? 9.574 50.108 16.679 1.00 17.03 ? 421 SER A CB 1 ATOM 3189 O OG . SER A 1 388 ? 10.144 48.886 16.178 1.00 16.94 ? 421 SER A OG 1 ATOM 3190 N N . THR A 1 389 ? 7.282 48.089 15.852 1.00 16.22 ? 422 THR A N 1 ATOM 3191 C CA . THR A 1 389 ? 6.479 47.504 14.760 1.00 16.98 ? 422 THR A CA 1 ATOM 3192 C C . THR A 1 389 ? 4.991 47.581 15.021 1.00 16.49 ? 422 THR A C 1 ATOM 3193 O O . THR A 1 389 ? 4.209 47.912 14.105 1.00 17.20 ? 422 THR A O 1 ATOM 3194 C CB . THR A 1 389 ? 6.971 46.058 14.417 1.00 17.11 ? 422 THR A CB 1 ATOM 3195 O OG1 . THR A 1 389 ? 8.372 46.103 14.185 1.00 17.73 ? 422 THR A OG1 1 ATOM 3196 C CG2 . THR A 1 389 ? 6.221 45.539 13.173 1.00 18.76 ? 422 THR A CG2 1 ATOM 3197 N N . GLU A 1 390 ? 4.563 47.305 16.260 1.00 16.39 ? 423 GLU A N 1 ATOM 3198 C CA . GLU A 1 390 ? 3.119 47.405 16.529 1.00 16.96 ? 423 GLU A CA 1 ATOM 3199 C C . GLU A 1 390 ? 2.620 48.843 16.405 1.00 17.64 ? 423 GLU A C 1 ATOM 3200 O O . GLU A 1 390 ? 1.498 49.046 15.882 1.00 16.89 ? 423 GLU A O 1 ATOM 3201 C CB . GLU A 1 390 ? 2.783 46.872 17.932 1.00 16.95 ? 423 GLU A CB 1 ATOM 3202 C CG . GLU A 1 390 ? 3.065 45.327 18.181 1.00 17.12 ? 423 GLU A CG 1 ATOM 3203 C CD . GLU A 1 390 ? 2.365 44.510 17.120 1.00 16.70 ? 423 GLU A CD 1 ATOM 3204 O OE1 . GLU A 1 390 ? 1.116 44.644 16.984 1.00 17.19 ? 423 GLU A OE1 1 ATOM 3205 O OE2 . GLU A 1 390 ? 3.017 43.706 16.414 1.00 16.46 ? 423 GLU A OE2 1 ATOM 3206 N N . TRP A 1 391 ? 3.467 49.833 16.769 1.00 16.73 ? 424 TRP A N 1 ATOM 3207 C CA . TRP A 1 391 ? 3.017 51.261 16.606 1.00 16.24 ? 424 TRP A CA 1 ATOM 3208 C C . TRP A 1 391 ? 2.982 51.593 15.109 1.00 16.96 ? 424 TRP A C 1 ATOM 3209 O O . TRP A 1 391 ? 2.028 52.298 14.656 1.00 17.67 ? 424 TRP A O 1 ATOM 3210 C CB . TRP A 1 391 ? 3.975 52.168 17.364 1.00 16.53 ? 424 TRP A CB 1 ATOM 3211 C CG . TRP A 1 391 ? 3.440 53.584 17.477 1.00 16.48 ? 424 TRP A CG 1 ATOM 3212 C CD1 . TRP A 1 391 ? 2.557 54.059 18.411 1.00 17.97 ? 424 TRP A CD1 1 ATOM 3213 C CD2 . TRP A 1 391 ? 3.820 54.721 16.653 1.00 17.03 ? 424 TRP A CD2 1 ATOM 3214 N NE1 . TRP A 1 391 ? 2.314 55.414 18.211 1.00 18.09 ? 424 TRP A NE1 1 ATOM 3215 C CE2 . TRP A 1 391 ? 3.101 55.842 17.171 1.00 16.55 ? 424 TRP A CE2 1 ATOM 3216 C CE3 . TRP A 1 391 ? 4.654 54.890 15.532 1.00 18.47 ? 424 TRP A CE3 1 ATOM 3217 C CZ2 . TRP A 1 391 ? 3.193 57.122 16.579 1.00 18.04 ? 424 TRP A CZ2 1 ATOM 3218 C CZ3 . TRP A 1 391 ? 4.777 56.178 14.974 1.00 18.47 ? 424 TRP A CZ3 1 ATOM 3219 C CH2 . TRP A 1 391 ? 4.016 57.264 15.488 1.00 19.74 ? 424 TRP A CH2 1 ATOM 3220 N N . ALA A 1 392 ? 3.887 51.058 14.304 1.00 16.56 ? 425 ALA A N 1 ATOM 3221 C CA . ALA A 1 392 ? 3.819 51.295 12.854 1.00 16.88 ? 425 ALA A CA 1 ATOM 3222 C C . ALA A 1 392 ? 2.547 50.640 12.309 1.00 17.54 ? 425 ALA A C 1 ATOM 3223 O O . ALA A 1 392 ? 1.890 51.202 11.435 1.00 17.62 ? 425 ALA A O 1 ATOM 3224 C CB . ALA A 1 392 ? 5.052 50.675 12.131 1.00 17.22 ? 425 ALA A CB 1 ATOM 3225 N N . GLU A 1 393 ? 2.233 49.424 12.792 1.00 16.40 ? 426 GLU A N 1 ATOM 3226 C CA . GLU A 1 393 ? 1.029 48.748 12.308 1.00 17.02 ? 426 GLU A CA 1 ATOM 3227 C C . GLU A 1 393 ? -0.236 49.521 12.679 1.00 16.99 ? 426 GLU A C 1 ATOM 3228 O O . GLU A 1 393 ? -1.227 49.548 11.896 1.00 18.77 ? 426 GLU A O 1 ATOM 3229 C CB . GLU A 1 393 ? 0.954 47.326 12.823 1.00 16.60 ? 426 GLU A CB 1 ATOM 3230 C CG . GLU A 1 393 ? 1.977 46.458 12.128 1.00 15.59 ? 426 GLU A CG 1 ATOM 3231 C CD . GLU A 1 393 ? 1.868 44.991 12.483 1.00 16.98 ? 426 GLU A CD 1 ATOM 3232 O OE1 . GLU A 1 393 ? 2.214 44.133 11.623 1.00 17.70 ? 426 GLU A OE1 1 ATOM 3233 O OE2 . GLU A 1 393 ? 1.502 44.657 13.642 1.00 17.92 ? 426 GLU A OE2 1 ATOM 3234 N N . GLU A 1 394 ? -0.242 50.134 13.884 1.00 15.28 ? 427 GLU A N 1 ATOM 3235 C CA . GLU A 1 394 ? -1.416 50.905 14.333 1.00 15.98 ? 427 GLU A CA 1 ATOM 3236 C C . GLU A 1 394 ? -1.612 52.145 13.450 1.00 16.58 ? 427 GLU A C 1 ATOM 3237 O O . GLU A 1 394 ? -2.770 52.513 13.144 1.00 17.74 ? 427 GLU A O 1 ATOM 3238 C CB . GLU A 1 394 ? -1.315 51.246 15.820 1.00 16.83 ? 427 GLU A CB 1 ATOM 3239 C CG . GLU A 1 394 ? -2.585 51.966 16.288 1.00 17.15 ? 427 GLU A CG 1 ATOM 3240 C CD . GLU A 1 394 ? -2.742 51.940 17.777 1.00 22.34 ? 427 GLU A CD 1 ATOM 3241 O OE1 . GLU A 1 394 ? -3.909 51.997 18.205 1.00 27.98 ? 427 GLU A OE1 1 ATOM 3242 O OE2 . GLU A 1 394 ? -1.795 51.838 18.533 1.00 22.57 ? 427 GLU A OE2 1 ATOM 3243 N N . ASN A 1 395 ? -0.486 52.811 13.179 1.00 16.61 ? 428 ASN A N 1 ATOM 3244 C CA . ASN A 1 395 ? -0.564 54.168 12.645 1.00 16.22 ? 428 ASN A CA 1 ATOM 3245 C C . ASN A 1 395 ? -0.180 54.199 11.169 1.00 16.99 ? 428 ASN A C 1 ATOM 3246 O O . ASN A 1 395 ? -0.006 55.311 10.596 1.00 17.81 ? 428 ASN A O 1 ATOM 3247 C CB . ASN A 1 395 ? 0.364 55.094 13.496 1.00 17.07 ? 428 ASN A CB 1 ATOM 3248 C CG . ASN A 1 395 ? -0.170 55.288 14.868 1.00 18.35 ? 428 ASN A CG 1 ATOM 3249 O OD1 . ASN A 1 395 ? 0.343 54.638 15.864 1.00 20.87 ? 428 ASN A OD1 1 ATOM 3250 N ND2 . ASN A 1 395 ? -1.244 56.036 14.990 1.00 16.29 ? 428 ASN A ND2 1 ATOM 3251 N N . VAL A 1 396 ? -0.060 53.032 10.522 1.00 17.33 ? 429 VAL A N 1 ATOM 3252 C CA . VAL A 1 396 ? 0.337 52.942 9.153 1.00 16.86 ? 429 VAL A CA 1 ATOM 3253 C C . VAL A 1 396 ? -0.327 53.978 8.207 1.00 16.25 ? 429 VAL A C 1 ATOM 3254 O O . VAL A 1 396 ? 0.356 54.519 7.284 1.00 17.34 ? 429 VAL A O 1 ATOM 3255 C CB . VAL A 1 396 ? 0.146 51.487 8.659 1.00 19.35 ? 429 VAL A CB 1 ATOM 3256 C CG1 . VAL A 1 396 ? -1.324 51.061 8.758 1.00 19.59 ? 429 VAL A CG1 1 ATOM 3257 C CG2 . VAL A 1 396 ? 0.606 51.424 7.197 1.00 20.58 ? 429 VAL A CG2 1 ATOM 3258 N N . LYS A 1 397 ? -1.625 54.187 8.369 1.00 16.22 ? 430 LYS A N 1 ATOM 3259 C CA . LYS A 1 397 ? -2.277 55.050 7.318 1.00 16.93 ? 430 LYS A CA 1 ATOM 3260 C C . LYS A 1 397 ? -1.791 56.480 7.395 1.00 17.78 ? 430 LYS A C 1 ATOM 3261 O O . LYS A 1 397 ? -1.516 57.139 6.365 1.00 19.80 ? 430 LYS A O 1 ATOM 3262 C CB . LYS A 1 397 ? -3.795 55.054 7.470 1.00 17.15 ? 430 LYS A CB 1 ATOM 3263 C CG . LYS A 1 397 ? -4.423 53.671 7.646 1.00 19.93 ? 430 LYS A CG 1 ATOM 3264 C CD . LYS A 1 397 ? -4.194 52.830 6.397 1.00 20.18 ? 430 LYS A CD 1 ATOM 3265 C CE . LYS A 1 397 ? -4.884 51.463 6.658 1.00 22.81 ? 430 LYS A CE 1 ATOM 3266 N NZ . LYS A 1 397 ? -4.923 50.563 5.425 1.00 21.67 ? 430 LYS A NZ 1 ATOM 3267 N N . ILE A 1 398 ? -1.579 56.993 8.609 1.00 16.72 ? 431 ILE A N 1 ATOM 3268 C CA . ILE A 1 398 ? -1.051 58.377 8.717 1.00 16.61 ? 431 ILE A CA 1 ATOM 3269 C C . ILE A 1 398 ? 0.441 58.351 8.442 1.00 17.56 ? 431 ILE A C 1 ATOM 3270 O O . ILE A 1 398 ? 0.990 59.311 7.781 1.00 18.27 ? 431 ILE A O 1 ATOM 3271 C CB . ILE A 1 398 ? -1.393 59.115 10.043 1.00 16.77 ? 431 ILE A CB 1 ATOM 3272 C CG1 . ILE A 1 398 ? -0.875 58.360 11.310 1.00 17.28 ? 431 ILE A CG1 1 ATOM 3273 C CG2 . ILE A 1 398 ? -2.912 59.327 10.167 1.00 17.49 ? 431 ILE A CG2 1 ATOM 3274 C CD1 . ILE A 1 398 ? -1.008 59.215 12.599 1.00 19.65 ? 431 ILE A CD1 1 ATOM 3275 N N . LEU A 1 399 ? 1.180 57.324 8.925 1.00 17.76 ? 432 LEU A N 1 ATOM 3276 C CA . LEU A 1 399 ? 2.623 57.342 8.733 1.00 17.40 ? 432 LEU A CA 1 ATOM 3277 C C . LEU A 1 399 ? 3.013 57.261 7.254 1.00 18.37 ? 432 LEU A C 1 ATOM 3278 O O . LEU A 1 399 ? 3.923 57.995 6.812 1.00 18.67 ? 432 LEU A O 1 ATOM 3279 C CB . LEU A 1 399 ? 3.234 56.143 9.448 1.00 18.23 ? 432 LEU A CB 1 ATOM 3280 C CG . LEU A 1 399 ? 3.103 56.243 10.966 1.00 16.95 ? 432 LEU A CG 1 ATOM 3281 C CD1 . LEU A 1 399 ? 3.649 54.944 11.532 1.00 18.83 ? 432 LEU A CD1 1 ATOM 3282 C CD2 . LEU A 1 399 ? 3.958 57.457 11.539 1.00 22.55 ? 432 LEU A CD2 1 ATOM 3283 N N . GLN A 1 400 ? 2.331 56.417 6.482 1.00 17.45 ? 433 GLN A N 1 ATOM 3284 C CA . GLN A 1 400 ? 2.740 56.269 5.095 1.00 17.05 ? 433 GLN A CA 1 ATOM 3285 C C . GLN A 1 400 ? 2.410 57.472 4.258 1.00 15.76 ? 433 GLN A C 1 ATOM 3286 O O . GLN A 1 400 ? 3.097 57.697 3.218 1.00 18.41 ? 433 GLN A O 1 ATOM 3287 C CB . GLN A 1 400 ? 2.189 54.971 4.479 1.00 18.31 ? 433 GLN A CB 1 ATOM 3288 C CG . GLN A 1 400 ? 0.700 55.007 4.206 1.00 18.37 ? 433 GLN A CG 1 ATOM 3289 C CD . GLN A 1 400 ? 0.027 53.618 4.054 1.00 19.57 ? 433 GLN A CD 1 ATOM 3290 O OE1 . GLN A 1 400 ? -1.168 53.525 4.125 1.00 25.11 ? 433 GLN A OE1 1 ATOM 3291 N NE2 . GLN A 1 400 ? 0.841 52.545 4.007 1.00 20.64 ? 433 GLN A NE2 1 ATOM 3292 N N . GLU A 1 401 ? 1.421 58.251 4.663 1.00 16.94 ? 434 GLU A N 1 ATOM 3293 C CA . GLU A 1 401 ? 1.071 59.396 3.822 1.00 17.77 ? 434 GLU A CA 1 ATOM 3294 C C . GLU A 1 401 ? 1.729 60.661 4.266 1.00 18.21 ? 434 GLU A C 1 ATOM 3295 O O . GLU A 1 401 ? 1.679 61.626 3.486 1.00 18.18 ? 434 GLU A O 1 ATOM 3296 C CB . GLU A 1 401 ? -0.456 59.597 3.857 1.00 18.01 ? 434 GLU A CB 1 ATOM 3297 C CG . GLU A 1 401 ? -1.274 58.393 3.333 1.00 18.72 ? 434 GLU A CG 1 ATOM 3298 C CD . GLU A 1 401 ? -1.034 58.038 1.893 1.00 21.00 ? 434 GLU A CD 1 ATOM 3299 O OE1 . GLU A 1 401 ? -0.264 58.785 1.232 1.00 20.09 ? 434 GLU A OE1 1 ATOM 3300 O OE2 . GLU A 1 401 ? -1.551 56.998 1.426 1.00 21.54 ? 434 GLU A OE2 1 ATOM 3301 N N . ARG A 1 402 ? 2.407 60.641 5.412 1.00 16.82 ? 435 ARG A N 1 ATOM 3302 C CA . ARG A 1 402 ? 2.861 61.937 6.003 1.00 16.33 ? 435 ARG A CA 1 ATOM 3303 C C . ARG A 1 402 ? 4.266 61.993 6.487 1.00 17.05 ? 435 ARG A C 1 ATOM 3304 O O . ARG A 1 402 ? 4.782 63.059 6.802 1.00 16.72 ? 435 ARG A O 1 ATOM 3305 C CB . ARG A 1 402 ? 1.954 62.327 7.229 1.00 17.70 ? 435 ARG A CB 1 ATOM 3306 C CG . ARG A 1 402 ? 0.476 62.409 6.893 1.00 16.62 ? 435 ARG A CG 1 ATOM 3307 C CD . ARG A 1 402 ? -0.317 62.729 8.149 1.00 16.58 ? 435 ARG A CD 1 ATOM 3308 N NE . ARG A 1 402 ? -1.744 62.692 7.816 1.00 16.60 ? 435 ARG A NE 1 ATOM 3309 C CZ . ARG A 1 402 ? -2.701 62.699 8.761 1.00 17.95 ? 435 ARG A CZ 1 ATOM 3310 N NH1 . ARG A 1 402 ? -2.357 62.737 10.052 1.00 17.04 ? 435 ARG A NH1 1 ATOM 3311 N NH2 . ARG A 1 402 ? -3.993 62.639 8.397 1.00 17.43 ? 435 ARG A NH2 1 ATOM 3312 N N . SER A 1 403 ? 4.940 60.827 6.549 1.00 16.57 ? 436 SER A N 1 ATOM 3313 C CA . SER A 1 403 ? 6.284 60.833 7.151 1.00 17.75 ? 436 SER A CA 1 ATOM 3314 C C . SER A 1 403 ? 7.386 61.206 6.182 1.00 17.20 ? 436 SER A C 1 ATOM 3315 O O . SER A 1 403 ? 7.532 60.606 5.109 1.00 18.15 ? 436 SER A O 1 ATOM 3316 C CB . SER A 1 403 ? 6.650 59.446 7.706 1.00 18.32 ? 436 SER A CB 1 ATOM 3317 O OG . SER A 1 403 ? 5.673 59.053 8.679 1.00 19.29 ? 436 SER A OG 1 ATOM 3318 N N . ILE A 1 404 ? 8.197 62.173 6.619 1.00 17.13 ? 437 ILE A N 1 ATOM 3319 C CA . ILE A 1 404 ? 9.380 62.559 5.835 1.00 17.55 ? 437 ILE A CA 1 ATOM 3320 C C . ILE A 1 404 ? 10.488 61.536 6.056 1.00 17.86 ? 437 ILE A C 1 ATOM 3321 O O . ILE A 1 404 ? 11.137 61.060 5.130 1.00 18.46 ? 437 ILE A O 1 ATOM 3322 C CB . ILE A 1 404 ? 9.879 63.938 6.312 1.00 17.17 ? 437 ILE A CB 1 ATOM 3323 C CG1 . ILE A 1 404 ? 8.759 64.998 6.197 1.00 19.72 ? 437 ILE A CG1 1 ATOM 3324 C CG2 . ILE A 1 404 ? 11.165 64.326 5.529 1.00 19.92 ? 437 ILE A CG2 1 ATOM 3325 C CD1 . ILE A 1 404 ? 7.997 64.990 4.933 1.00 20.94 ? 437 ILE A CD1 1 ATOM 3326 N N . ALA A 1 405 ? 10.770 61.200 7.330 1.00 16.54 ? 438 ALA A N 1 ATOM 3327 C CA . ALA A 1 405 ? 11.932 60.372 7.660 1.00 16.85 ? 438 ALA A CA 1 ATOM 3328 C C . ALA A 1 405 ? 11.825 59.793 9.052 1.00 16.52 ? 438 ALA A C 1 ATOM 3329 O O . ALA A 1 405 ? 11.080 60.363 9.867 1.00 17.37 ? 438 ALA A O 1 ATOM 3330 C CB . ALA A 1 405 ? 13.259 61.147 7.515 1.00 17.93 ? 438 ALA A CB 1 ATOM 3331 N N . TYR A 1 406 ? 12.650 58.768 9.280 1.00 16.68 ? 439 TYR A N 1 ATOM 3332 C CA . TYR A 1 406 ? 12.820 58.139 10.589 1.00 17.61 ? 439 TYR A CA 1 ATOM 3333 C C . TYR A 1 406 ? 14.302 58.133 10.929 1.00 17.20 ? 439 TYR A C 1 ATOM 3334 O O . TYR A 1 406 ? 15.129 57.585 10.127 1.00 18.61 ? 439 TYR A O 1 ATOM 3335 C CB . TYR A 1 406 ? 12.262 56.678 10.536 1.00 17.50 ? 439 TYR A CB 1 ATOM 3336 C CG . TYR A 1 406 ? 12.479 55.876 11.803 1.00 16.91 ? 439 TYR A CG 1 ATOM 3337 C CD1 . TYR A 1 406 ? 11.474 55.718 12.756 1.00 17.22 ? 439 TYR A CD1 1 ATOM 3338 C CD2 . TYR A 1 406 ? 13.715 55.308 12.041 1.00 17.96 ? 439 TYR A CD2 1 ATOM 3339 C CE1 . TYR A 1 406 ? 11.705 55.039 13.955 1.00 17.36 ? 439 TYR A CE1 1 ATOM 3340 C CE2 . TYR A 1 406 ? 13.931 54.620 13.239 1.00 16.89 ? 439 TYR A CE2 1 ATOM 3341 C CZ . TYR A 1 406 ? 12.925 54.551 14.197 1.00 17.67 ? 439 TYR A CZ 1 ATOM 3342 O OH . TYR A 1 406 ? 13.159 53.863 15.421 1.00 19.02 ? 439 TYR A OH 1 ATOM 3343 N N . ILE A 1 407 ? 14.676 58.702 12.067 1.00 16.72 ? 440 ILE A N 1 ATOM 3344 C CA . ILE A 1 407 ? 16.046 58.659 12.536 1.00 16.55 ? 440 ILE A CA 1 ATOM 3345 C C . ILE A 1 407 ? 16.080 57.785 13.816 1.00 18.19 ? 440 ILE A C 1 ATOM 3346 O O . ILE A 1 407 ? 15.305 58.028 14.748 1.00 17.05 ? 440 ILE A O 1 ATOM 3347 C CB . ILE A 1 407 ? 16.540 60.088 12.836 1.00 18.23 ? 440 ILE A CB 1 ATOM 3348 C CG1 . ILE A 1 407 ? 16.413 61.051 11.577 1.00 18.02 ? 440 ILE A CG1 1 ATOM 3349 C CG2 . ILE A 1 407 ? 17.944 60.063 13.442 1.00 18.71 ? 440 ILE A CG2 1 ATOM 3350 C CD1 . ILE A 1 407 ? 17.187 60.515 10.300 1.00 19.13 ? 440 ILE A CD1 1 ATOM 3351 N N . ASN A 1 408 ? 16.942 56.762 13.831 1.00 16.56 ? 441 ASN A N 1 ATOM 3352 C CA . ASN A 1 408 ? 16.941 55.862 14.961 1.00 16.18 ? 441 ASN A CA 1 ATOM 3353 C C . ASN A 1 408 ? 17.772 56.444 16.080 1.00 17.81 ? 441 ASN A C 1 ATOM 3354 O O . ASN A 1 408 ? 18.678 57.259 15.859 1.00 18.58 ? 441 ASN A O 1 ATOM 3355 C CB . ASN A 1 408 ? 17.614 54.523 14.532 1.00 18.11 ? 441 ASN A CB 1 ATOM 3356 C CG . ASN A 1 408 ? 17.054 53.283 15.275 1.00 19.51 ? 441 ASN A CG 1 ATOM 3357 O OD1 . ASN A 1 408 ? 15.920 53.188 15.726 1.00 19.95 ? 441 ASN A OD1 1 ATOM 3358 N ND2 . ASN A 1 408 ? 17.929 52.269 15.359 1.00 20.08 ? 441 ASN A ND2 1 ATOM 3359 N N . SER A 1 409 ? 17.569 55.899 17.268 1.00 17.77 ? 442 SER A N 1 ATOM 3360 C CA . SER A 1 409 ? 18.363 56.298 18.428 1.00 17.45 ? 442 SER A CA 1 ATOM 3361 C C . SER A 1 409 ? 18.625 55.107 19.364 1.00 16.74 ? 442 SER A C 1 ATOM 3362 O O . SER A 1 409 ? 18.360 55.146 20.576 1.00 18.42 ? 442 SER A O 1 ATOM 3363 C CB . SER A 1 409 ? 17.773 57.517 19.184 1.00 17.09 ? 442 SER A CB 1 ATOM 3364 O OG . SER A 1 409 ? 18.727 58.036 20.113 1.00 18.02 ? 442 SER A OG 1 ATOM 3365 N N . ASP A 1 410 ? 19.170 54.034 18.753 1.00 17.93 ? 443 ASP A N 1 ATOM 3366 C CA . ASP A 1 410 ? 19.633 52.836 19.482 1.00 17.64 ? 443 ASP A CA 1 ATOM 3367 C C . ASP A 1 410 ? 21.075 53.157 19.943 1.00 17.88 ? 443 ASP A C 1 ATOM 3368 O O . ASP A 1 410 ? 21.515 54.335 20.000 1.00 17.01 ? 443 ASP A O 1 ATOM 3369 C CB . ASP A 1 410 ? 19.570 51.623 18.498 1.00 19.65 ? 443 ASP A CB 1 ATOM 3370 C CG . ASP A 1 410 ? 19.512 50.195 19.202 1.00 21.58 ? 443 ASP A CG 1 ATOM 3371 O OD1 . ASP A 1 410 ? 20.128 49.970 20.298 1.00 20.83 ? 443 ASP A OD1 1 ATOM 3372 O OD2 . ASP A 1 410 ? 18.898 49.245 18.553 1.00 22.12 ? 443 ASP A OD2 1 ATOM 3373 N N . SER A 1 411 ? 21.859 52.111 20.234 1.00 17.96 ? 444 SER A N 1 ATOM 3374 C CA . SER A 1 411 ? 23.203 52.343 20.833 1.00 18.94 ? 444 SER A CA 1 ATOM 3375 C C . SER A 1 411 ? 23.970 53.414 20.095 1.00 17.78 ? 444 SER A C 1 ATOM 3376 O O . SER A 1 411 ? 23.984 53.462 18.852 1.00 17.96 ? 444 SER A O 1 ATOM 3377 C CB . SER A 1 411 ? 24.041 51.081 20.719 1.00 18.83 ? 444 SER A CB 1 ATOM 3378 O OG A SER A 1 411 ? 23.959 50.548 19.466 0.50 22.97 ? 444 SER A OG 1 ATOM 3379 O OG B SER A 1 411 ? 23.299 49.965 21.149 0.50 16.53 ? 444 SER A OG 1 ATOM 3380 N N . SER A 1 412 ? 24.618 54.280 20.888 1.00 17.39 ? 445 SER A N 1 ATOM 3381 C CA . SER A 1 412 ? 25.384 55.371 20.253 1.00 18.35 ? 445 SER A CA 1 ATOM 3382 C C . SER A 1 412 ? 26.880 55.029 20.173 1.00 19.67 ? 445 SER A C 1 ATOM 3383 O O . SER A 1 412 ? 27.620 55.751 19.515 1.00 20.89 ? 445 SER A O 1 ATOM 3384 C CB . SER A 1 412 ? 25.207 56.652 21.070 1.00 18.63 ? 445 SER A CB 1 ATOM 3385 O OG . SER A 1 412 ? 25.712 56.375 22.369 1.00 19.45 ? 445 SER A OG 1 ATOM 3386 N N . ILE A 1 413 ? 27.330 54.025 20.926 1.00 20.87 ? 446 ILE A N 1 ATOM 3387 C CA . ILE A 1 413 ? 28.781 53.835 21.220 1.00 25.09 ? 446 ILE A CA 1 ATOM 3388 C C . ILE A 1 413 ? 29.195 52.342 21.220 1.00 26.76 ? 446 ILE A C 1 ATOM 3389 O O . ILE A 1 413 ? 29.536 51.755 22.287 1.00 29.90 ? 446 ILE A O 1 ATOM 3390 C CB . ILE A 1 413 ? 29.171 54.612 22.541 1.00 24.45 ? 446 ILE A CB 1 ATOM 3391 C CG1 . ILE A 1 413 ? 30.690 54.573 22.898 1.00 28.38 ? 446 ILE A CG1 1 ATOM 3392 C CG2 . ILE A 1 413 ? 28.513 54.050 23.755 1.00 26.39 ? 446 ILE A CG2 1 ATOM 3393 C CD1 . ILE A 1 413 ? 31.568 55.576 22.186 1.00 24.77 ? 446 ILE A CD1 1 ATOM 3394 N N . GLU A 1 414 ? 29.359 51.782 20.024 1.00 25.67 ? 447 GLU A N 1 ATOM 3395 C CA . GLU A 1 414 ? 29.841 50.376 19.904 1.00 26.69 ? 447 GLU A CA 1 ATOM 3396 C C . GLU A 1 414 ? 31.348 50.204 19.755 1.00 26.79 ? 447 GLU A C 1 ATOM 3397 O O . GLU A 1 414 ? 31.861 49.063 19.683 1.00 28.67 ? 447 GLU A O 1 ATOM 3398 C CB . GLU A 1 414 ? 29.098 49.619 18.797 1.00 26.57 ? 447 GLU A CB 1 ATOM 3399 C CG A GLU A 1 414 ? 27.599 49.656 19.035 0.65 28.19 ? 447 GLU A CG 1 ATOM 3400 C CG B GLU A 1 414 ? 29.430 50.085 17.360 0.35 24.57 ? 447 GLU A CG 1 ATOM 3401 C CD A GLU A 1 414 ? 26.841 48.928 17.953 0.65 34.37 ? 447 GLU A CD 1 ATOM 3402 C CD B GLU A 1 414 ? 28.721 49.332 16.235 0.35 25.08 ? 447 GLU A CD 1 ATOM 3403 O OE1 A GLU A 1 414 ? 27.458 48.078 17.281 0.65 36.68 ? 447 GLU A OE1 1 ATOM 3404 O OE1 B GLU A 1 414 ? 27.623 48.798 16.460 0.35 24.37 ? 447 GLU A OE1 1 ATOM 3405 O OE2 A GLU A 1 414 ? 25.634 49.207 17.790 0.65 37.56 ? 447 GLU A OE2 1 ATOM 3406 O OE2 B GLU A 1 414 ? 29.257 49.305 15.106 0.35 24.51 ? 447 GLU A OE2 1 ATOM 3407 N N . GLY A 1 415 ? 32.070 51.310 19.697 1.00 25.11 ? 448 GLY A N 1 ATOM 3408 C CA . GLY A 1 415 ? 33.527 51.312 19.652 1.00 24.19 ? 448 GLY A CA 1 ATOM 3409 C C . GLY A 1 415 ? 33.896 52.765 19.781 1.00 24.76 ? 448 GLY A C 1 ATOM 3410 O O . GLY A 1 415 ? 32.986 53.649 19.901 1.00 24.29 ? 448 GLY A O 1 ATOM 3411 N N . ASN A 1 416 ? 35.187 53.059 19.702 1.00 24.66 ? 449 ASN A N 1 ATOM 3412 C CA . ASN A 1 416 ? 35.586 54.450 19.830 1.00 25.47 ? 449 ASN A CA 1 ATOM 3413 C C . ASN A 1 416 ? 36.532 54.979 18.733 1.00 25.27 ? 449 ASN A C 1 ATOM 3414 O O . ASN A 1 416 ? 37.320 55.912 18.991 1.00 25.88 ? 449 ASN A O 1 ATOM 3415 C CB . ASN A 1 416 ? 36.116 54.714 21.241 1.00 25.45 ? 449 ASN A CB 1 ATOM 3416 C CG . ASN A 1 416 ? 37.382 53.974 21.532 1.00 25.24 ? 449 ASN A CG 1 ATOM 3417 O OD1 . ASN A 1 416 ? 38.016 53.385 20.625 1.00 26.65 ? 449 ASN A OD1 1 ATOM 3418 N ND2 . ASN A 1 416 ? 37.787 53.998 22.823 1.00 24.39 ? 449 ASN A ND2 1 ATOM 3419 N N . TYR A 1 417 ? 36.430 54.411 17.519 1.00 24.58 ? 450 TYR A N 1 ATOM 3420 C CA . TYR A 1 417 ? 37.346 54.783 16.425 1.00 25.48 ? 450 TYR A CA 1 ATOM 3421 C C . TYR A 1 417 ? 36.790 55.904 15.560 1.00 23.51 ? 450 TYR A C 1 ATOM 3422 O O . TYR A 1 417 ? 37.400 56.987 15.441 1.00 23.68 ? 450 TYR A O 1 ATOM 3423 C CB . TYR A 1 417 ? 37.692 53.552 15.567 1.00 25.99 ? 450 TYR A CB 1 ATOM 3424 C CG . TYR A 1 417 ? 38.605 53.852 14.388 1.00 27.02 ? 450 TYR A CG 1 ATOM 3425 C CD1 . TYR A 1 417 ? 39.939 54.264 14.587 1.00 30.35 ? 450 TYR A CD1 1 ATOM 3426 C CD2 . TYR A 1 417 ? 38.149 53.692 13.069 1.00 28.59 ? 450 TYR A CD2 1 ATOM 3427 C CE1 . TYR A 1 417 ? 40.790 54.530 13.495 1.00 30.42 ? 450 TYR A CE1 1 ATOM 3428 C CE2 . TYR A 1 417 ? 39.003 53.956 11.967 1.00 31.98 ? 450 TYR A CE2 1 ATOM 3429 C CZ . TYR A 1 417 ? 40.302 54.377 12.203 1.00 35.02 ? 450 TYR A CZ 1 ATOM 3430 O OH . TYR A 1 417 ? 41.124 54.646 11.131 1.00 36.61 ? 450 TYR A OH 1 ATOM 3431 N N . THR A 1 418 ? 35.583 55.690 15.006 1.00 22.82 ? 451 THR A N 1 ATOM 3432 C CA . THR A 1 418 ? 34.984 56.735 14.189 1.00 22.61 ? 451 THR A CA 1 ATOM 3433 C C . THR A 1 418 ? 33.476 56.515 14.031 1.00 21.54 ? 451 THR A C 1 ATOM 3434 O O . THR A 1 418 ? 32.914 55.563 14.558 1.00 23.43 ? 451 THR A O 1 ATOM 3435 C CB . THR A 1 418 ? 35.651 56.775 12.750 1.00 23.14 ? 451 THR A CB 1 ATOM 3436 O OG1 . THR A 1 418 ? 35.393 58.023 12.077 1.00 24.02 ? 451 THR A OG1 1 ATOM 3437 C CG2 . THR A 1 418 ? 35.220 55.609 11.925 1.00 24.72 ? 451 THR A CG2 1 ATOM 3438 N N . LEU A 1 419 ? 32.887 57.398 13.228 1.00 22.75 ? 452 LEU A N 1 ATOM 3439 C CA . LEU A 1 419 ? 31.429 57.406 12.979 1.00 22.65 ? 452 LEU A CA 1 ATOM 3440 C C . LEU A 1 419 ? 31.091 56.322 11.995 1.00 23.60 ? 452 LEU A C 1 ATOM 3441 O O . LEU A 1 419 ? 31.911 56.054 11.065 1.00 22.97 ? 452 LEU A O 1 ATOM 3442 C CB . LEU A 1 419 ? 31.011 58.762 12.378 1.00 23.68 ? 452 LEU A CB 1 ATOM 3443 C CG . LEU A 1 419 ? 29.493 58.992 12.273 1.00 21.34 ? 452 LEU A CG 1 ATOM 3444 C CD1 . LEU A 1 419 ? 28.917 59.068 13.766 1.00 23.66 ? 452 LEU A CD1 1 ATOM 3445 C CD2 . LEU A 1 419 ? 29.236 60.250 11.440 1.00 25.06 ? 452 LEU A CD2 1 ATOM 3446 N N . ARG A 1 420 ? 29.939 55.690 12.171 1.00 23.69 ? 453 ARG A N 1 ATOM 3447 C CA . ARG A 1 420 ? 29.352 54.857 11.139 1.00 24.09 ? 453 ARG A CA 1 ATOM 3448 C C . ARG A 1 420 ? 27.959 55.386 10.836 1.00 23.86 ? 453 ARG A C 1 ATOM 3449 O O . ARG A 1 420 ? 27.181 55.675 11.779 1.00 24.44 ? 453 ARG A O 1 ATOM 3450 C CB . ARG A 1 420 ? 29.216 53.448 11.659 1.00 24.27 ? 453 ARG A CB 1 ATOM 3451 C CG . ARG A 1 420 ? 28.544 52.467 10.710 1.00 31.69 ? 453 ARG A CG 1 ATOM 3452 C CD . ARG A 1 420 ? 28.065 51.232 11.460 1.00 37.41 ? 453 ARG A CD 1 ATOM 3453 N NE . ARG A 1 420 ? 27.234 50.424 10.560 1.00 45.36 ? 453 ARG A NE 1 ATOM 3454 C CZ . ARG A 1 420 ? 27.687 49.473 9.728 1.00 49.17 ? 453 ARG A CZ 1 ATOM 3455 N NH1 . ARG A 1 420 ? 26.820 48.807 8.951 1.00 49.88 ? 453 ARG A NH1 1 ATOM 3456 N NH2 . ARG A 1 420 ? 28.995 49.183 9.663 1.00 51.19 ? 453 ARG A NH2 1 ATOM 3457 N N . VAL A 1 421 ? 27.620 55.504 9.561 1.00 22.49 ? 454 VAL A N 1 ATOM 3458 C CA . VAL A 1 421 ? 26.278 55.915 9.179 1.00 22.06 ? 454 VAL A CA 1 ATOM 3459 C C . VAL A 1 421 ? 25.696 54.884 8.233 1.00 21.94 ? 454 VAL A C 1 ATOM 3460 O O . VAL A 1 421 ? 26.393 54.477 7.310 1.00 22.75 ? 454 VAL A O 1 ATOM 3461 C CB . VAL A 1 421 ? 26.305 57.251 8.485 1.00 21.85 ? 454 VAL A CB 1 ATOM 3462 C CG1 . VAL A 1 421 ? 24.899 57.624 7.989 1.00 21.49 ? 454 VAL A CG1 1 ATOM 3463 C CG2 . VAL A 1 421 ? 26.797 58.329 9.445 1.00 24.09 ? 454 VAL A CG2 1 ATOM 3464 N N . ASP A 1 422 ? 24.454 54.451 8.474 1.00 21.39 ? 455 ASP A N 1 ATOM 3465 C CA . ASP A 1 422 ? 23.715 53.641 7.516 1.00 21.88 ? 455 ASP A CA 1 ATOM 3466 C C . ASP A 1 422 ? 22.424 54.407 7.175 1.00 21.36 ? 455 ASP A C 1 ATOM 3467 O O . ASP A 1 422 ? 21.674 54.785 8.068 1.00 20.57 ? 455 ASP A O 1 ATOM 3468 C CB . ASP A 1 422 ? 23.250 52.295 8.076 1.00 22.39 ? 455 ASP A CB 1 ATOM 3469 C CG . ASP A 1 422 ? 24.298 51.528 8.872 1.00 28.08 ? 455 ASP A CG 1 ATOM 3470 O OD1 . ASP A 1 422 ? 23.878 50.504 9.465 1.00 34.04 ? 455 ASP A OD1 1 ATOM 3471 O OD2 . ASP A 1 422 ? 25.475 51.855 8.871 1.00 28.03 ? 455 ASP A OD2 1 ATOM 3472 N N . CYS A 1 423 ? 22.148 54.635 5.914 1.00 20.56 ? 456 CYS A N 1 ATOM 3473 C CA . CYS A 1 423 ? 20.923 55.381 5.592 1.00 19.83 ? 456 CYS A CA 1 ATOM 3474 C C . CYS A 1 423 ? 20.594 55.173 4.125 1.00 19.20 ? 456 CYS A C 1 ATOM 3475 O O . CYS A 1 423 ? 21.454 54.770 3.292 1.00 22.76 ? 456 CYS A O 1 ATOM 3476 C CB . CYS A 1 423 ? 21.069 56.872 5.898 1.00 21.34 ? 456 CYS A CB 1 ATOM 3477 S SG . CYS A 1 423 ? 22.290 57.734 4.888 1.00 20.98 ? 456 CYS A SG 1 ATOM 3478 N N . THR A 1 424 ? 19.372 55.529 3.796 1.00 18.32 ? 457 THR A N 1 ATOM 3479 C CA . THR A 1 424 ? 18.952 55.579 2.387 1.00 18.40 ? 457 THR A CA 1 ATOM 3480 C C . THR A 1 424 ? 19.766 56.588 1.595 1.00 19.11 ? 457 THR A C 1 ATOM 3481 O O . THR A 1 424 ? 20.223 57.577 2.133 1.00 18.88 ? 457 THR A O 1 ATOM 3482 C CB . THR A 1 424 ? 17.462 55.948 2.263 1.00 19.14 ? 457 THR A CB 1 ATOM 3483 O OG1 . THR A 1 424 ? 17.182 56.197 0.877 1.00 19.88 ? 457 THR A OG1 1 ATOM 3484 C CG2 . THR A 1 424 ? 17.116 57.228 3.067 1.00 19.25 ? 457 THR A CG2 1 ATOM 3485 N N . PRO A 1 425 ? 20.001 56.351 0.288 1.00 18.24 ? 458 PRO A N 1 ATOM 3486 C CA . PRO A 1 425 ? 20.761 57.339 -0.474 1.00 18.03 ? 458 PRO A CA 1 ATOM 3487 C C . PRO A 1 425 ? 20.146 58.737 -0.485 1.00 18.35 ? 458 PRO A C 1 ATOM 3488 O O . PRO A 1 425 ? 20.875 59.706 -0.668 1.00 19.42 ? 458 PRO A O 1 ATOM 3489 C CB . PRO A 1 425 ? 20.740 56.764 -1.919 1.00 19.35 ? 458 PRO A CB 1 ATOM 3490 C CG . PRO A 1 425 ? 20.619 55.250 -1.722 1.00 19.57 ? 458 PRO A CG 1 ATOM 3491 C CD . PRO A 1 425 ? 19.648 55.135 -0.515 1.00 18.47 ? 458 PRO A CD 1 ATOM 3492 N N . LEU A 1 426 ? 18.836 58.815 -0.271 1.00 18.35 ? 459 LEU A N 1 ATOM 3493 C CA . LEU A 1 426 ? 18.193 60.167 -0.144 1.00 18.22 ? 459 LEU A CA 1 ATOM 3494 C C . LEU A 1 426 ? 18.894 61.089 0.884 1.00 19.40 ? 459 LEU A C 1 ATOM 3495 O O . LEU A 1 426 ? 18.839 62.330 0.709 1.00 21.50 ? 459 LEU A O 1 ATOM 3496 C CB . LEU A 1 426 ? 16.728 60.073 0.236 1.00 19.04 ? 459 LEU A CB 1 ATOM 3497 C CG . LEU A 1 426 ? 15.845 59.427 -0.871 1.00 18.02 ? 459 LEU A CG 1 ATOM 3498 C CD1 . LEU A 1 426 ? 14.429 59.210 -0.341 1.00 18.93 ? 459 LEU A CD1 1 ATOM 3499 C CD2 . LEU A 1 426 ? 15.711 60.307 -2.166 1.00 21.51 ? 459 LEU A CD2 1 ATOM 3500 N N . LEU A 1 427 ? 19.487 60.457 1.917 1.00 19.03 ? 460 LEU A N 1 ATOM 3501 C CA . LEU A 1 427 ? 20.036 61.232 3.044 1.00 18.25 ? 460 LEU A CA 1 ATOM 3502 C C . LEU A 1 427 ? 21.540 61.453 2.942 1.00 18.90 ? 460 LEU A C 1 ATOM 3503 O O . LEU A 1 427 ? 22.117 62.113 3.809 1.00 19.29 ? 460 LEU A O 1 ATOM 3504 C CB . LEU A 1 427 ? 19.691 60.527 4.395 1.00 19.30 ? 460 LEU A CB 1 ATOM 3505 C CG . LEU A 1 427 ? 18.234 60.676 4.819 1.00 19.34 ? 460 LEU A CG 1 ATOM 3506 C CD1 . LEU A 1 427 ? 17.909 59.749 6.001 1.00 21.41 ? 460 LEU A CD1 1 ATOM 3507 C CD2 . LEU A 1 427 ? 17.964 62.136 5.226 1.00 21.08 ? 460 LEU A CD2 1 ATOM 3508 N N . TYR A 1 428 ? 22.226 60.886 1.954 1.00 18.50 ? 461 TYR A N 1 ATOM 3509 C CA . TYR A 1 428 ? 23.697 61.035 1.962 1.00 20.21 ? 461 TYR A CA 1 ATOM 3510 C C . TYR A 1 428 ? 24.169 62.483 2.019 1.00 20.54 ? 461 TYR A C 1 ATOM 3511 O O . TYR A 1 428 ? 25.054 62.840 2.814 1.00 20.70 ? 461 TYR A O 1 ATOM 3512 C CB . TYR A 1 428 ? 24.321 60.432 0.685 1.00 21.91 ? 461 TYR A CB 1 ATOM 3513 C CG . TYR A 1 428 ? 24.221 58.932 0.487 1.00 21.60 ? 461 TYR A CG 1 ATOM 3514 C CD1 . TYR A 1 428 ? 23.859 58.030 1.504 1.00 21.25 ? 461 TYR A CD1 1 ATOM 3515 C CD2 . TYR A 1 428 ? 24.540 58.392 -0.772 1.00 23.14 ? 461 TYR A CD2 1 ATOM 3516 C CE1 . TYR A 1 428 ? 23.805 56.630 1.281 1.00 22.44 ? 461 TYR A CE1 1 ATOM 3517 C CE2 . TYR A 1 428 ? 24.446 57.010 -1.026 1.00 23.41 ? 461 TYR A CE2 1 ATOM 3518 C CZ . TYR A 1 428 ? 24.103 56.150 -0.011 1.00 25.12 ? 461 TYR A CZ 1 ATOM 3519 O OH . TYR A 1 428 ? 24.038 54.794 -0.248 1.00 26.26 ? 461 TYR A OH 1 ATOM 3520 N N . GLN A 1 429 ? 23.605 63.314 1.166 1.00 20.37 ? 462 GLN A N 1 ATOM 3521 C CA . GLN A 1 429 ? 24.084 64.703 1.117 1.00 21.50 ? 462 GLN A CA 1 ATOM 3522 C C . GLN A 1 429 ? 23.864 65.475 2.406 1.00 20.93 ? 462 GLN A C 1 ATOM 3523 O O . GLN A 1 429 ? 24.751 66.229 2.861 1.00 21.52 ? 462 GLN A O 1 ATOM 3524 C CB A GLN A 1 429 ? 23.684 65.432 -0.111 0.65 23.36 ? 462 GLN A CB 1 ATOM 3525 C CB B GLN A 1 429 ? 23.277 65.395 -0.022 0.35 21.22 ? 462 GLN A CB 1 ATOM 3526 C CG A GLN A 1 429 ? 24.725 65.127 -1.159 0.65 24.30 ? 462 GLN A CG 1 ATOM 3527 C CG B GLN A 1 429 ? 23.575 66.918 -0.275 0.35 19.36 ? 462 GLN A CG 1 ATOM 3528 C CD A GLN A 1 429 ? 24.381 65.734 -2.485 0.65 29.06 ? 462 GLN A CD 1 ATOM 3529 C CD B GLN A 1 429 ? 22.961 67.507 -1.588 0.35 20.80 ? 462 GLN A CD 1 ATOM 3530 O OE1 A GLN A 1 429 ? 24.249 66.962 -2.606 0.65 32.21 ? 462 GLN A OE1 1 ATOM 3531 O OE1 B GLN A 1 429 ? 23.702 67.974 -2.449 0.35 24.09 ? 462 GLN A OE1 1 ATOM 3532 N NE2 A GLN A 1 429 ? 24.247 64.886 -3.499 0.65 18.76 ? 462 GLN A NE2 1 ATOM 3533 N NE2 B GLN A 1 429 ? 21.637 67.550 -1.696 0.35 18.69 ? 462 GLN A NE2 1 ATOM 3534 N N . LEU A 1 430 ? 22.716 65.220 3.038 1.00 19.43 ? 463 LEU A N 1 ATOM 3535 C CA . LEU A 1 430 ? 22.438 65.908 4.316 1.00 20.06 ? 463 LEU A CA 1 ATOM 3536 C C . LEU A 1 430 ? 23.437 65.432 5.381 1.00 21.10 ? 463 LEU A C 1 ATOM 3537 O O . LEU A 1 430 ? 23.934 66.270 6.178 1.00 20.30 ? 463 LEU A O 1 ATOM 3538 C CB . LEU A 1 430 ? 21.008 65.568 4.769 1.00 19.63 ? 463 LEU A CB 1 ATOM 3539 C CG . LEU A 1 430 ? 20.629 66.242 6.099 1.00 21.03 ? 463 LEU A CG 1 ATOM 3540 C CD1 . LEU A 1 430 ? 20.751 67.773 6.069 1.00 20.86 ? 463 LEU A CD1 1 ATOM 3541 C CD2 . LEU A 1 430 ? 19.184 65.829 6.485 1.00 18.40 ? 463 LEU A CD2 1 ATOM 3542 N N . VAL A 1 431 ? 23.750 64.147 5.412 1.00 20.06 ? 464 VAL A N 1 ATOM 3543 C CA . VAL A 1 431 ? 24.682 63.601 6.415 1.00 21.08 ? 464 VAL A CA 1 ATOM 3544 C C . VAL A 1 431 ? 26.040 64.277 6.237 1.00 21.51 ? 464 VAL A C 1 ATOM 3545 O O . VAL A 1 431 ? 26.687 64.700 7.211 1.00 21.15 ? 464 VAL A O 1 ATOM 3546 C CB . VAL A 1 431 ? 24.774 62.096 6.326 1.00 21.23 ? 464 VAL A CB 1 ATOM 3547 C CG1 . VAL A 1 431 ? 25.936 61.530 7.192 1.00 23.41 ? 464 VAL A CG1 1 ATOM 3548 C CG2 . VAL A 1 431 ? 23.457 61.399 6.807 1.00 19.30 ? 464 VAL A CG2 1 ATOM 3549 N N . TYR A 1 432 ? 26.479 64.368 4.993 1.00 22.11 ? 465 TYR A N 1 ATOM 3550 C CA . TYR A 1 432 ? 27.822 64.969 4.765 1.00 22.96 ? 465 TYR A CA 1 ATOM 3551 C C . TYR A 1 432 ? 27.799 66.442 5.152 1.00 24.09 ? 465 TYR A C 1 ATOM 3552 O O . TYR A 1 432 ? 28.754 66.959 5.785 1.00 26.86 ? 465 TYR A O 1 ATOM 3553 C CB . TYR A 1 432 ? 28.172 64.824 3.290 1.00 23.89 ? 465 TYR A CB 1 ATOM 3554 C CG . TYR A 1 432 ? 28.411 63.418 2.832 1.00 23.64 ? 465 TYR A CG 1 ATOM 3555 C CD1 . TYR A 1 432 ? 28.084 63.031 1.536 1.00 25.85 ? 465 TYR A CD1 1 ATOM 3556 C CD2 . TYR A 1 432 ? 29.040 62.519 3.658 1.00 25.97 ? 465 TYR A CD2 1 ATOM 3557 C CE1 . TYR A 1 432 ? 28.338 61.726 1.095 1.00 26.53 ? 465 TYR A CE1 1 ATOM 3558 C CE2 . TYR A 1 432 ? 29.334 61.244 3.242 1.00 25.69 ? 465 TYR A CE2 1 ATOM 3559 C CZ . TYR A 1 432 ? 28.960 60.835 1.952 1.00 28.72 ? 465 TYR A CZ 1 ATOM 3560 O OH . TYR A 1 432 ? 29.244 59.537 1.538 1.00 29.73 ? 465 TYR A OH 1 ATOM 3561 N N . LYS A 1 433 ? 26.718 67.141 4.833 1.00 23.03 ? 466 LYS A N 1 ATOM 3562 C CA . LYS A 1 433 ? 26.607 68.542 5.184 1.00 22.77 ? 466 LYS A CA 1 ATOM 3563 C C . LYS A 1 433 ? 26.649 68.764 6.694 1.00 23.50 ? 466 LYS A C 1 ATOM 3564 O O . LYS A 1 433 ? 27.428 69.610 7.195 1.00 22.82 ? 466 LYS A O 1 ATOM 3565 C CB . LYS A 1 433 ? 25.360 69.154 4.568 1.00 23.42 ? 466 LYS A CB 1 ATOM 3566 C CG . LYS A 1 433 ? 25.009 70.498 5.129 1.00 27.34 ? 466 LYS A CG 1 ATOM 3567 C CD . LYS A 1 433 ? 23.863 71.116 4.381 1.00 31.14 ? 466 LYS A CD 1 ATOM 3568 C CE . LYS A 1 433 ? 23.153 72.152 5.272 1.00 36.49 ? 466 LYS A CE 1 ATOM 3569 N NZ . LYS A 1 433 ? 22.246 72.953 4.418 1.00 41.65 ? 466 LYS A NZ 1 ATOM 3570 N N . LEU A 1 434 ? 25.868 67.997 7.459 1.00 21.54 ? 467 LEU A N 1 ATOM 3571 C CA . LEU A 1 434 ? 25.795 68.254 8.913 1.00 21.19 ? 467 LEU A CA 1 ATOM 3572 C C . LEU A 1 434 ? 27.065 67.847 9.637 1.00 22.37 ? 467 LEU A C 1 ATOM 3573 O O . LEU A 1 434 ? 27.447 68.486 10.623 1.00 22.66 ? 467 LEU A O 1 ATOM 3574 C CB . LEU A 1 434 ? 24.623 67.416 9.482 1.00 21.19 ? 467 LEU A CB 1 ATOM 3575 C CG . LEU A 1 434 ? 23.300 67.902 8.979 1.00 21.53 ? 467 LEU A CG 1 ATOM 3576 C CD1 . LEU A 1 434 ? 22.213 66.985 9.611 1.00 21.04 ? 467 LEU A CD1 1 ATOM 3577 C CD2 . LEU A 1 434 ? 23.031 69.370 9.250 1.00 25.67 ? 467 LEU A CD2 1 ATOM 3578 N N . THR A 1 435 ? 27.725 66.766 9.182 1.00 21.49 ? 468 THR A N 1 ATOM 3579 C CA . THR A 1 435 ? 28.906 66.302 9.914 1.00 22.20 ? 468 THR A CA 1 ATOM 3580 C C . THR A 1 435 ? 30.066 67.331 9.775 1.00 22.11 ? 468 THR A C 1 ATOM 3581 O O . THR A 1 435 ? 30.967 67.373 10.618 1.00 22.88 ? 468 THR A O 1 ATOM 3582 C CB . THR A 1 435 ? 29.429 64.950 9.478 1.00 22.91 ? 468 THR A CB 1 ATOM 3583 O OG1 . THR A 1 435 ? 29.533 64.911 8.037 1.00 24.17 ? 468 THR A OG1 1 ATOM 3584 C CG2 . THR A 1 435 ? 28.486 63.769 9.916 1.00 20.01 ? 468 THR A CG2 1 ATOM 3585 N N . LYS A 1 436 ? 30.000 68.155 8.739 1.00 22.80 ? 469 LYS A N 1 ATOM 3586 C CA . LYS A 1 436 ? 30.994 69.245 8.584 1.00 23.74 ? 469 LYS A CA 1 ATOM 3587 C C . LYS A 1 436 ? 30.827 70.375 9.598 1.00 25.12 ? 469 LYS A C 1 ATOM 3588 O O . LYS A 1 436 ? 31.704 71.274 9.705 1.00 25.83 ? 469 LYS A O 1 ATOM 3589 C CB . LYS A 1 436 ? 30.924 69.841 7.166 1.00 23.65 ? 469 LYS A CB 1 ATOM 3590 C CG . LYS A 1 436 ? 31.478 68.923 6.133 1.00 24.41 ? 469 LYS A CG 1 ATOM 3591 C CD . LYS A 1 436 ? 31.243 69.434 4.734 1.00 26.18 ? 469 LYS A CD 1 ATOM 3592 C CE . LYS A 1 436 ? 31.727 68.370 3.794 1.00 33.04 ? 469 LYS A CE 1 ATOM 3593 N NZ . LYS A 1 436 ? 30.824 68.235 2.642 1.00 37.75 ? 469 LYS A NZ 1 ATOM 3594 N N . GLU A 1 437 ? 29.701 70.403 10.292 1.00 24.38 ? 470 GLU A N 1 ATOM 3595 C CA . GLU A 1 437 ? 29.419 71.479 11.226 1.00 26.32 ? 470 GLU A CA 1 ATOM 3596 C C . GLU A 1 437 ? 29.371 70.985 12.643 1.00 26.42 ? 470 GLU A C 1 ATOM 3597 O O . GLU A 1 437 ? 28.963 71.751 13.555 1.00 27.10 ? 470 GLU A O 1 ATOM 3598 C CB . GLU A 1 437 ? 28.147 72.234 10.856 1.00 28.43 ? 470 GLU A CB 1 ATOM 3599 C CG . GLU A 1 437 ? 28.298 73.038 9.567 1.00 36.76 ? 470 GLU A CG 1 ATOM 3600 C CD . GLU A 1 437 ? 26.952 73.353 8.895 1.00 46.38 ? 470 GLU A CD 1 ATOM 3601 O OE1 . GLU A 1 437 ? 26.663 72.801 7.795 1.00 51.86 ? 470 GLU A OE1 1 ATOM 3602 O OE2 . GLU A 1 437 ? 26.176 74.160 9.465 1.00 47.90 ? 470 GLU A OE2 1 ATOM 3603 N N . ILE A 1 438 ? 29.846 69.764 12.854 1.00 22.43 ? 471 ILE A N 1 ATOM 3604 C CA . ILE A 1 438 ? 29.863 69.203 14.226 1.00 22.20 ? 471 ILE A CA 1 ATOM 3605 C C . ILE A 1 438 ? 31.330 68.975 14.589 1.00 22.43 ? 471 ILE A C 1 ATOM 3606 O O . ILE A 1 438 ? 32.072 68.395 13.814 1.00 22.84 ? 471 ILE A O 1 ATOM 3607 C CB . ILE A 1 438 ? 29.041 67.845 14.286 1.00 20.67 ? 471 ILE A CB 1 ATOM 3608 C CG1 . ILE A 1 438 ? 27.566 68.141 14.115 1.00 21.47 ? 471 ILE A CG1 1 ATOM 3609 C CG2 . ILE A 1 438 ? 29.343 67.070 15.565 1.00 22.24 ? 471 ILE A CG2 1 ATOM 3610 C CD1 . ILE A 1 438 ? 26.802 66.816 13.817 1.00 20.19 ? 471 ILE A CD1 1 ATOM 3611 N N . PRO A 1 439 ? 31.778 69.445 15.769 1.00 23.13 ? 472 PRO A N 1 ATOM 3612 C CA . PRO A 1 439 ? 33.174 69.272 16.071 1.00 23.84 ? 472 PRO A CA 1 ATOM 3613 C C . PRO A 1 439 ? 33.528 67.799 16.205 1.00 24.36 ? 472 PRO A C 1 ATOM 3614 O O . PRO A 1 439 ? 32.731 66.994 16.733 1.00 23.47 ? 472 PRO A O 1 ATOM 3615 C CB . PRO A 1 439 ? 33.319 69.965 17.434 1.00 23.77 ? 472 PRO A CB 1 ATOM 3616 C CG . PRO A 1 439 ? 32.258 70.953 17.481 1.00 24.04 ? 472 PRO A CG 1 ATOM 3617 C CD . PRO A 1 439 ? 31.099 70.245 16.797 1.00 23.64 ? 472 PRO A CD 1 ATOM 3618 N N . SER A 1 440 ? 34.695 67.405 15.703 1.00 22.86 ? 473 SER A N 1 ATOM 3619 C CA . SER A 1 440 ? 35.109 66.049 15.889 1.00 21.94 ? 473 SER A CA 1 ATOM 3620 C C . SER A 1 440 ? 35.429 65.775 17.334 1.00 23.03 ? 473 SER A C 1 ATOM 3621 O O . SER A 1 440 ? 36.040 66.655 17.986 1.00 22.49 ? 473 SER A O 1 ATOM 3622 C CB . SER A 1 440 ? 36.316 65.705 15.039 1.00 22.76 ? 473 SER A CB 1 ATOM 3623 O OG . SER A 1 440 ? 36.783 64.405 15.345 1.00 22.56 ? 473 SER A OG 1 ATOM 3624 N N . PRO A 1 441 ? 35.061 64.572 17.841 1.00 22.11 ? 474 PRO A N 1 ATOM 3625 C CA . PRO A 1 441 ? 35.439 64.268 19.236 1.00 22.49 ? 474 PRO A CA 1 ATOM 3626 C C . PRO A 1 441 ? 36.772 63.501 19.345 1.00 23.92 ? 474 PRO A C 1 ATOM 3627 O O . PRO A 1 441 ? 37.173 63.078 20.462 1.00 24.34 ? 474 PRO A O 1 ATOM 3628 C CB . PRO A 1 441 ? 34.280 63.365 19.709 1.00 21.77 ? 474 PRO A CB 1 ATOM 3629 C CG . PRO A 1 441 ? 33.944 62.590 18.430 1.00 21.38 ? 474 PRO A CG 1 ATOM 3630 C CD . PRO A 1 441 ? 34.119 63.560 17.293 1.00 23.20 ? 474 PRO A CD 1 ATOM 3631 N N . ASP A 1 442 ? 37.450 63.316 18.221 1.00 23.96 ? 475 ASP A N 1 ATOM 3632 C CA . ASP A 1 442 ? 38.547 62.371 18.172 1.00 24.82 ? 475 ASP A CA 1 ATOM 3633 C C . ASP A 1 442 ? 39.835 63.044 18.658 1.00 25.66 ? 475 ASP A C 1 ATOM 3634 O O . ASP A 1 442 ? 40.062 64.218 18.394 1.00 26.55 ? 475 ASP A O 1 ATOM 3635 C CB . ASP A 1 442 ? 38.772 61.900 16.760 1.00 24.65 ? 475 ASP A CB 1 ATOM 3636 C CG . ASP A 1 442 ? 37.678 60.972 16.261 1.00 25.97 ? 475 ASP A CG 1 ATOM 3637 O OD1 . ASP A 1 442 ? 36.658 60.732 17.007 1.00 25.82 ? 475 ASP A OD1 1 ATOM 3638 O OD2 . ASP A 1 442 ? 37.865 60.491 15.129 1.00 27.26 ? 475 ASP A OD2 1 ATOM 3639 N N . ASP A 1 443 ? 40.640 62.281 19.371 1.00 26.64 ? 476 ASP A N 1 ATOM 3640 C CA . ASP A 1 443 ? 41.947 62.801 19.860 1.00 27.70 ? 476 ASP A CA 1 ATOM 3641 C C . ASP A 1 443 ? 42.751 63.147 18.624 1.00 28.05 ? 476 ASP A C 1 ATOM 3642 O O . ASP A 1 443 ? 42.734 62.383 17.662 1.00 27.92 ? 476 ASP A O 1 ATOM 3643 C CB . ASP A 1 443 ? 42.656 61.733 20.670 1.00 27.72 ? 476 ASP A CB 1 ATOM 3644 C CG . ASP A 1 443 ? 41.977 61.464 21.994 1.00 31.58 ? 476 ASP A CG 1 ATOM 3645 O OD1 . ASP A 1 443 ? 41.188 62.322 22.463 1.00 33.49 ? 476 ASP A OD1 1 ATOM 3646 O OD2 . ASP A 1 443 ? 42.235 60.388 22.587 1.00 37.75 ? 476 ASP A OD2 1 ATOM 3647 N N . GLY A 1 444 ? 43.417 64.303 18.630 1.00 29.33 ? 477 GLY A N 1 ATOM 3648 C CA . GLY A 1 444 ? 44.119 64.786 17.447 1.00 29.69 ? 477 GLY A CA 1 ATOM 3649 C C . GLY A 1 444 ? 43.319 65.554 16.405 1.00 30.63 ? 477 GLY A C 1 ATOM 3650 O O . GLY A 1 444 ? 43.905 66.092 15.469 1.00 31.83 ? 477 GLY A O 1 ATOM 3651 N N . PHE A 1 445 ? 41.994 65.633 16.554 1.00 29.03 ? 478 PHE A N 1 ATOM 3652 C CA . PHE A 1 445 ? 41.158 66.374 15.600 1.00 28.39 ? 478 PHE A CA 1 ATOM 3653 C C . PHE A 1 445 ? 40.470 67.560 16.266 1.00 29.98 ? 478 PHE A C 1 ATOM 3654 O O . PHE A 1 445 ? 39.371 67.990 15.877 1.00 29.34 ? 478 PHE A O 1 ATOM 3655 C CB . PHE A 1 445 ? 40.123 65.436 14.945 1.00 27.37 ? 478 PHE A CB 1 ATOM 3656 C CG . PHE A 1 445 ? 40.745 64.387 14.056 1.00 25.84 ? 478 PHE A CG 1 ATOM 3657 C CD1 . PHE A 1 445 ? 40.792 64.575 12.686 1.00 24.76 ? 478 PHE A CD1 1 ATOM 3658 C CD2 . PHE A 1 445 ? 41.298 63.232 14.601 1.00 25.94 ? 478 PHE A CD2 1 ATOM 3659 C CE1 . PHE A 1 445 ? 41.384 63.607 11.850 1.00 28.35 ? 478 PHE A CE1 1 ATOM 3660 C CE2 . PHE A 1 445 ? 41.872 62.244 13.790 1.00 29.08 ? 478 PHE A CE2 1 ATOM 3661 C CZ . PHE A 1 445 ? 41.901 62.427 12.394 1.00 28.41 ? 478 PHE A CZ 1 ATOM 3662 N N . GLU A 1 446 ? 41.144 68.134 17.265 1.00 29.37 ? 479 GLU A N 1 ATOM 3663 C CA . GLU A 1 446 ? 40.484 69.149 18.095 1.00 31.13 ? 479 GLU A CA 1 ATOM 3664 C C . GLU A 1 446 ? 40.002 70.407 17.360 1.00 32.15 ? 479 GLU A C 1 ATOM 3665 O O . GLU A 1 446 ? 39.105 71.100 17.854 1.00 34.44 ? 479 GLU A O 1 ATOM 3666 C CB . GLU A 1 446 ? 41.355 69.540 19.310 1.00 31.35 ? 479 GLU A CB 1 ATOM 3667 C CG . GLU A 1 446 ? 41.697 68.375 20.253 1.00 32.22 ? 479 GLU A CG 1 ATOM 3668 C CD . GLU A 1 446 ? 42.739 67.395 19.693 1.00 32.35 ? 479 GLU A CD 1 ATOM 3669 O OE1 . GLU A 1 446 ? 42.939 66.322 20.295 1.00 34.11 ? 479 GLU A OE1 1 ATOM 3670 O OE2 . GLU A 1 446 ? 43.361 67.681 18.650 1.00 32.78 ? 479 GLU A OE2 1 ATOM 3671 N N . SER A 1 447 ? 40.593 70.752 16.223 1.00 31.54 ? 480 SER A N 1 ATOM 3672 C CA . SER A 1 447 ? 40.120 71.959 15.537 1.00 32.52 ? 480 SER A CA 1 ATOM 3673 C C . SER A 1 447 ? 39.420 71.600 14.234 1.00 31.81 ? 480 SER A C 1 ATOM 3674 O O . SER A 1 447 ? 39.242 72.459 13.364 1.00 32.48 ? 480 SER A O 1 ATOM 3675 C CB . SER A 1 447 ? 41.291 72.888 15.224 1.00 32.73 ? 480 SER A CB 1 ATOM 3676 O OG . SER A 1 447 ? 42.259 72.149 14.490 1.00 34.60 ? 480 SER A OG 1 ATOM 3677 N N . LYS A 1 448 ? 38.997 70.335 14.125 1.00 30.18 ? 481 LYS A N 1 ATOM 3678 C CA . LYS A 1 448 ? 38.474 69.786 12.888 1.00 29.00 ? 481 LYS A CA 1 ATOM 3679 C C . LYS A 1 448 ? 37.043 69.295 13.118 1.00 26.70 ? 481 LYS A C 1 ATOM 3680 O O . LYS A 1 448 ? 36.617 69.038 14.251 1.00 27.02 ? 481 LYS A O 1 ATOM 3681 C CB . LYS A 1 448 ? 39.361 68.608 12.433 1.00 28.28 ? 481 LYS A CB 1 ATOM 3682 C CG . LYS A 1 448 ? 40.864 68.988 12.235 1.00 32.40 ? 481 LYS A CG 1 ATOM 3683 C CD . LYS A 1 448 ? 40.950 70.287 11.467 1.00 36.27 ? 481 LYS A CD 1 ATOM 3684 C CE . LYS A 1 448 ? 42.374 70.882 11.464 1.00 40.03 ? 481 LYS A CE 1 ATOM 3685 N NZ . LYS A 1 448 ? 43.095 70.339 10.274 1.00 43.35 ? 481 LYS A NZ 1 ATOM 3686 N N . SER A 1 449 ? 36.308 69.187 12.025 1.00 25.72 ? 482 SER A N 1 ATOM 3687 C CA . SER A 1 449 ? 34.942 68.662 12.097 1.00 24.93 ? 482 SER A CA 1 ATOM 3688 C C . SER A 1 449 ? 34.892 67.135 12.119 1.00 24.58 ? 482 SER A C 1 ATOM 3689 O O . SER A 1 449 ? 35.816 66.432 11.698 1.00 23.44 ? 482 SER A O 1 ATOM 3690 C CB . SER A 1 449 ? 34.142 69.124 10.890 1.00 25.04 ? 482 SER A CB 1 ATOM 3691 O OG . SER A 1 449 ? 34.585 68.443 9.725 1.00 25.92 ? 482 SER A OG 1 ATOM 3692 N N . LEU A 1 450 ? 33.730 66.616 12.544 1.00 23.30 ? 483 LEU A N 1 ATOM 3693 C CA . LEU A 1 450 ? 33.452 65.192 12.479 1.00 23.33 ? 483 LEU A CA 1 ATOM 3694 C C . LEU A 1 450 ? 33.575 64.604 11.063 1.00 24.84 ? 483 LEU A C 1 ATOM 3695 O O . LEU A 1 450 ? 34.043 63.464 10.901 1.00 22.18 ? 483 LEU A O 1 ATOM 3696 C CB . LEU A 1 450 ? 32.019 64.943 13.024 1.00 23.03 ? 483 LEU A CB 1 ATOM 3697 C CG . LEU A 1 450 ? 31.439 63.517 13.059 1.00 25.22 ? 483 LEU A CG 1 ATOM 3698 C CD1 . LEU A 1 450 ? 32.383 62.543 13.883 1.00 22.06 ? 483 LEU A CD1 1 ATOM 3699 C CD2 . LEU A 1 450 ? 30.000 63.594 13.635 1.00 20.98 ? 483 LEU A CD2 1 ATOM 3700 N N . TYR A 1 451 ? 33.145 65.388 10.069 1.00 23.54 ? 484 TYR A N 1 ATOM 3701 C CA . TYR A 1 451 ? 33.313 64.985 8.654 1.00 23.57 ? 484 TYR A CA 1 ATOM 3702 C C . TYR A 1 451 ? 34.777 64.711 8.373 1.00 24.90 ? 484 TYR A C 1 ATOM 3703 O O . TYR A 1 451 ? 35.118 63.655 7.819 1.00 26.06 ? 484 TYR A O 1 ATOM 3704 C CB . TYR A 1 451 ? 32.814 66.061 7.704 1.00 23.05 ? 484 TYR A CB 1 ATOM 3705 C CG . TYR A 1 451 ? 32.968 65.687 6.254 1.00 21.61 ? 484 TYR A CG 1 ATOM 3706 C CD1 . TYR A 1 451 ? 31.978 64.937 5.602 1.00 25.04 ? 484 TYR A CD1 1 ATOM 3707 C CD2 . TYR A 1 451 ? 34.094 66.124 5.519 1.00 23.62 ? 484 TYR A CD2 1 ATOM 3708 C CE1 . TYR A 1 451 ? 32.098 64.612 4.291 1.00 26.28 ? 484 TYR A CE1 1 ATOM 3709 C CE2 . TYR A 1 451 ? 34.216 65.795 4.176 1.00 25.34 ? 484 TYR A CE2 1 ATOM 3710 C CZ . TYR A 1 451 ? 33.221 65.048 3.568 1.00 26.27 ? 484 TYR A CZ 1 ATOM 3711 O OH . TYR A 1 451 ? 33.279 64.661 2.241 1.00 27.45 ? 484 TYR A OH 1 ATOM 3712 N N . GLU A 1 452 ? 35.635 65.646 8.782 1.00 25.67 ? 485 GLU A N 1 ATOM 3713 C CA . GLU A 1 452 ? 37.046 65.470 8.447 1.00 27.34 ? 485 GLU A CA 1 ATOM 3714 C C . GLU A 1 452 ? 37.626 64.219 9.095 1.00 26.50 ? 485 GLU A C 1 ATOM 3715 O O . GLU A 1 452 ? 38.357 63.482 8.434 1.00 26.64 ? 485 GLU A O 1 ATOM 3716 C CB . GLU A 1 452 ? 37.846 66.678 8.837 1.00 27.79 ? 485 GLU A CB 1 ATOM 3717 C CG . GLU A 1 452 ? 37.541 67.881 8.025 1.00 32.71 ? 485 GLU A CG 1 ATOM 3718 C CD . GLU A 1 452 ? 38.284 69.089 8.548 1.00 37.85 ? 485 GLU A CD 1 ATOM 3719 O OE1 . GLU A 1 452 ? 37.825 69.735 9.534 1.00 38.56 ? 485 GLU A OE1 1 ATOM 3720 O OE2 . GLU A 1 452 ? 39.347 69.385 7.957 1.00 41.40 ? 485 GLU A OE2 1 ATOM 3721 N N . SER A 1 453 ? 37.334 63.979 10.385 1.00 24.33 ? 486 SER A N 1 ATOM 3722 C CA . SER A 1 453 ? 37.892 62.780 11.020 1.00 24.02 ? 486 SER A CA 1 ATOM 3723 C C . SER A 1 453 ? 37.319 61.499 10.457 1.00 25.16 ? 486 SER A C 1 ATOM 3724 O O . SER A 1 453 ? 38.027 60.505 10.272 1.00 25.39 ? 486 SER A O 1 ATOM 3725 C CB . SER A 1 453 ? 37.791 62.823 12.567 1.00 24.38 ? 486 SER A CB 1 ATOM 3726 O OG . SER A 1 453 ? 36.444 62.883 13.034 1.00 23.98 ? 486 SER A OG 1 ATOM 3727 N N . TRP A 1 454 ? 36.009 61.526 10.165 1.00 25.42 ? 487 TRP A N 1 ATOM 3728 C CA . TRP A 1 454 ? 35.326 60.396 9.540 1.00 25.42 ? 487 TRP A CA 1 ATOM 3729 C C . TRP A 1 454 ? 35.881 60.117 8.134 1.00 26.24 ? 487 TRP A C 1 ATOM 3730 O O . TRP A 1 454 ? 36.152 58.978 7.840 1.00 25.12 ? 487 TRP A O 1 ATOM 3731 C CB . TRP A 1 454 ? 33.839 60.730 9.512 1.00 24.92 ? 487 TRP A CB 1 ATOM 3732 C CG . TRP A 1 454 ? 32.890 59.712 8.926 1.00 23.59 ? 487 TRP A CG 1 ATOM 3733 C CD1 . TRP A 1 454 ? 32.987 58.341 8.918 1.00 22.82 ? 487 TRP A CD1 1 ATOM 3734 C CD2 . TRP A 1 454 ? 31.639 60.032 8.301 1.00 21.93 ? 487 TRP A CD2 1 ATOM 3735 N NE1 . TRP A 1 454 ? 31.868 57.784 8.296 1.00 26.39 ? 487 TRP A NE1 1 ATOM 3736 C CE2 . TRP A 1 454 ? 31.017 58.800 7.931 1.00 22.37 ? 487 TRP A CE2 1 ATOM 3737 C CE3 . TRP A 1 454 ? 30.979 61.237 8.014 1.00 24.50 ? 487 TRP A CE3 1 ATOM 3738 C CZ2 . TRP A 1 454 ? 29.778 58.748 7.248 1.00 22.72 ? 487 TRP A CZ2 1 ATOM 3739 C CZ3 . TRP A 1 454 ? 29.739 61.167 7.352 1.00 23.72 ? 487 TRP A CZ3 1 ATOM 3740 C CH2 . TRP A 1 454 ? 29.168 59.928 6.983 1.00 22.70 ? 487 TRP A CH2 1 ATOM 3741 N N . LEU A 1 455 ? 36.056 61.147 7.302 1.00 26.74 ? 488 LEU A N 1 ATOM 3742 C CA . LEU A 1 455 ? 36.642 60.952 5.950 1.00 28.39 ? 488 LEU A CA 1 ATOM 3743 C C . LEU A 1 455 ? 38.055 60.323 6.062 1.00 30.28 ? 488 LEU A C 1 ATOM 3744 O O . LEU A 1 455 ? 38.385 59.389 5.331 1.00 31.79 ? 488 LEU A O 1 ATOM 3745 C CB . LEU A 1 455 ? 36.712 62.292 5.207 1.00 28.51 ? 488 LEU A CB 1 ATOM 3746 C CG . LEU A 1 455 ? 37.441 62.269 3.833 1.00 29.41 ? 488 LEU A CG 1 ATOM 3747 C CD1 . LEU A 1 455 ? 36.752 61.275 2.879 1.00 30.02 ? 488 LEU A CD1 1 ATOM 3748 C CD2 . LEU A 1 455 ? 37.490 63.679 3.227 1.00 33.65 ? 488 LEU A CD2 1 ATOM 3749 N N . GLU A 1 456 ? 38.858 60.809 7.010 1.00 30.12 ? 489 GLU A N 1 ATOM 3750 C CA . GLU A 1 456 ? 40.207 60.270 7.153 1.00 31.16 ? 489 GLU A CA 1 ATOM 3751 C C . GLU A 1 456 ? 40.171 58.810 7.559 1.00 31.01 ? 489 GLU A C 1 ATOM 3752 O O . GLU A 1 456 ? 40.970 58.024 7.085 1.00 31.90 ? 489 GLU A O 1 ATOM 3753 C CB . GLU A 1 456 ? 41.027 61.049 8.165 1.00 31.65 ? 489 GLU A CB 1 ATOM 3754 C CG . GLU A 1 456 ? 42.443 60.467 8.285 1.00 34.93 ? 489 GLU A CG 1 ATOM 3755 C CD . GLU A 1 456 ? 43.346 61.314 9.111 1.00 40.17 ? 489 GLU A CD 1 ATOM 3756 O OE1 . GLU A 1 456 ? 43.314 62.559 8.921 1.00 42.62 ? 489 GLU A OE1 1 ATOM 3757 O OE2 . GLU A 1 456 ? 44.092 60.728 9.936 1.00 42.02 ? 489 GLU A OE2 1 ATOM 3758 N N . LYS A 1 457 ? 39.251 58.439 8.453 1.00 30.66 ? 490 LYS A N 1 ATOM 3759 C CA . LYS A 1 457 ? 39.241 57.091 9.046 1.00 28.98 ? 490 LYS A CA 1 ATOM 3760 C C . LYS A 1 457 ? 38.455 56.039 8.298 1.00 31.08 ? 490 LYS A C 1 ATOM 3761 O O . LYS A 1 457 ? 38.678 54.839 8.504 1.00 31.04 ? 490 LYS A O 1 ATOM 3762 C CB . LYS A 1 457 ? 38.765 57.167 10.487 1.00 30.04 ? 490 LYS A CB 1 ATOM 3763 C CG . LYS A 1 457 ? 39.762 57.908 11.403 1.00 26.76 ? 490 LYS A CG 1 ATOM 3764 C CD . LYS A 1 457 ? 39.269 57.914 12.844 1.00 28.47 ? 490 LYS A CD 1 ATOM 3765 C CE . LYS A 1 457 ? 40.337 58.494 13.785 1.00 29.34 ? 490 LYS A CE 1 ATOM 3766 N NZ . LYS A 1 457 ? 39.804 58.651 15.185 1.00 31.92 ? 490 LYS A NZ 1 ATOM 3767 N N . ASP A 1 458 ? 37.505 56.464 7.462 1.00 30.87 ? 491 ASP A N 1 ATOM 3768 C CA . ASP A 1 458 ? 36.687 55.495 6.738 1.00 31.90 ? 491 ASP A CA 1 ATOM 3769 C C . ASP A 1 458 ? 36.213 56.022 5.383 1.00 32.27 ? 491 ASP A C 1 ATOM 3770 O O . ASP A 1 458 ? 35.013 56.281 5.186 1.00 30.28 ? 491 ASP A O 1 ATOM 3771 C CB . ASP A 1 458 ? 35.495 55.030 7.602 1.00 32.29 ? 491 ASP A CB 1 ATOM 3772 C CG . ASP A 1 458 ? 34.850 53.770 7.058 1.00 35.70 ? 491 ASP A CG 1 ATOM 3773 O OD1 . ASP A 1 458 ? 33.734 53.408 7.497 1.00 34.29 ? 491 ASP A OD1 1 ATOM 3774 O OD2 . ASP A 1 458 ? 35.471 53.141 6.165 1.00 37.48 ? 491 ASP A OD2 1 ATOM 3775 N N . PRO A 1 459 ? 37.149 56.242 4.437 1.00 32.28 ? 492 PRO A N 1 ATOM 3776 C CA . PRO A 1 459 ? 36.751 56.784 3.115 1.00 31.99 ? 492 PRO A CA 1 ATOM 3777 C C . PRO A 1 459 ? 35.886 55.778 2.332 1.00 32.61 ? 492 PRO A C 1 ATOM 3778 O O . PRO A 1 459 ? 36.002 54.570 2.573 1.00 31.58 ? 492 PRO A O 1 ATOM 3779 C CB . PRO A 1 459 ? 38.097 57.042 2.403 1.00 31.97 ? 492 PRO A CB 1 ATOM 3780 C CG . PRO A 1 459 ? 39.095 56.265 3.173 1.00 33.33 ? 492 PRO A CG 1 ATOM 3781 C CD . PRO A 1 459 ? 38.612 56.090 4.565 1.00 33.03 ? 492 PRO A CD 1 ATOM 3782 N N . SER A 1 460 ? 34.990 56.258 1.458 1.00 32.02 ? 493 SER A N 1 ATOM 3783 C CA . SER A 1 460 ? 34.135 55.332 0.698 1.00 33.92 ? 493 SER A CA 1 ATOM 3784 C C . SER A 1 460 ? 34.949 54.660 -0.398 1.00 35.57 ? 493 SER A C 1 ATOM 3785 O O . SER A 1 460 ? 35.737 55.330 -1.063 1.00 35.65 ? 493 SER A O 1 ATOM 3786 C CB . SER A 1 460 ? 32.925 56.051 0.099 1.00 33.84 ? 493 SER A CB 1 ATOM 3787 O OG A SER A 1 460 ? 33.295 56.983 -0.905 0.65 36.26 ? 493 SER A OG 1 ATOM 3788 O OG B SER A 1 460 ? 32.288 55.289 -0.899 0.35 31.46 ? 493 SER A OG 1 ATOM 3789 N N . PRO A 1 461 ? 34.758 53.349 -0.576 1.00 37.21 ? 494 PRO A N 1 ATOM 3790 C CA . PRO A 1 461 ? 35.345 52.648 -1.715 1.00 39.45 ? 494 PRO A CA 1 ATOM 3791 C C . PRO A 1 461 ? 34.918 53.244 -3.077 1.00 41.54 ? 494 PRO A C 1 ATOM 3792 O O . PRO A 1 461 ? 35.733 53.241 -3.994 1.00 43.13 ? 494 PRO A O 1 ATOM 3793 C CB . PRO A 1 461 ? 34.810 51.214 -1.566 1.00 39.16 ? 494 PRO A CB 1 ATOM 3794 C CG . PRO A 1 461 ? 33.661 51.316 -0.652 1.00 39.71 ? 494 PRO A CG 1 ATOM 3795 C CD . PRO A 1 461 ? 33.989 52.432 0.274 1.00 36.94 ? 494 PRO A CD 1 ATOM 3796 N N . GLU A 1 462 ? 33.690 53.761 -3.204 1.00 42.59 ? 495 GLU A N 1 ATOM 3797 C CA . GLU A 1 462 ? 33.229 54.327 -4.477 1.00 42.98 ? 495 GLU A CA 1 ATOM 3798 C C . GLU A 1 462 ? 33.806 55.704 -4.774 1.00 42.36 ? 495 GLU A C 1 ATOM 3799 O O . GLU A 1 462 ? 33.829 56.117 -5.938 1.00 43.62 ? 495 GLU A O 1 ATOM 3800 C CB . GLU A 1 462 ? 31.693 54.421 -4.563 1.00 43.90 ? 495 GLU A CB 1 ATOM 3801 C CG . GLU A 1 462 ? 30.907 53.614 -3.525 1.00 48.94 ? 495 GLU A CG 1 ATOM 3802 C CD . GLU A 1 462 ? 30.976 52.115 -3.730 1.00 53.09 ? 495 GLU A CD 1 ATOM 3803 O OE1 . GLU A 1 462 ? 30.212 51.399 -3.054 1.00 56.06 ? 495 GLU A OE1 1 ATOM 3804 O OE2 . GLU A 1 462 ? 31.787 51.650 -4.556 1.00 56.15 ? 495 GLU A OE2 1 ATOM 3805 N N . ASN A 1 463 ? 34.224 56.440 -3.745 1.00 40.53 ? 496 ASN A N 1 ATOM 3806 C CA . ASN A 1 463 ? 34.785 57.797 -3.927 1.00 39.08 ? 496 ASN A CA 1 ATOM 3807 C C . ASN A 1 463 ? 35.637 58.111 -2.711 1.00 38.84 ? 496 ASN A C 1 ATOM 3808 O O . ASN A 1 463 ? 35.120 58.367 -1.618 1.00 38.41 ? 496 ASN A O 1 ATOM 3809 C CB . ASN A 1 463 ? 33.666 58.855 -4.138 1.00 38.69 ? 496 ASN A CB 1 ATOM 3810 C CG . ASN A 1 463 ? 34.209 60.259 -4.515 1.00 39.84 ? 496 ASN A CG 1 ATOM 3811 O OD1 . ASN A 1 463 ? 35.332 60.631 -4.183 1.00 40.64 ? 496 ASN A OD1 1 ATOM 3812 N ND2 . ASN A 1 463 ? 33.393 61.037 -5.219 1.00 38.88 ? 496 ASN A ND2 1 ATOM 3813 N N . LYS A 1 464 ? 36.949 58.067 -2.891 1.00 38.13 ? 497 LYS A N 1 ATOM 3814 C CA . LYS A 1 464 ? 37.885 58.291 -1.803 1.00 37.93 ? 497 LYS A CA 1 ATOM 3815 C C . LYS A 1 464 ? 37.748 59.685 -1.211 1.00 36.72 ? 497 LYS A C 1 ATOM 3816 O O . LYS A 1 464 ? 38.302 59.967 -0.150 1.00 37.78 ? 497 LYS A O 1 ATOM 3817 C CB . LYS A 1 464 ? 39.327 58.091 -2.310 1.00 38.88 ? 497 LYS A CB 1 ATOM 3818 C CG . LYS A 1 464 ? 39.621 56.629 -2.699 1.00 43.85 ? 497 LYS A CG 1 ATOM 3819 C CD . LYS A 1 464 ? 40.454 56.522 -4.003 1.00 48.34 ? 497 LYS A CD 1 ATOM 3820 C CE . LYS A 1 464 ? 39.872 55.441 -4.961 1.00 51.84 ? 497 LYS A CE 1 ATOM 3821 N NZ . LYS A 1 464 ? 38.375 55.558 -5.197 1.00 51.74 ? 497 LYS A NZ 1 ATOM 3822 N N . ASN A 1 465 ? 37.062 60.591 -1.895 1.00 35.19 ? 498 ASN A N 1 ATOM 3823 C CA . ASN A 1 465 ? 36.920 61.939 -1.347 1.00 34.63 ? 498 ASN A CA 1 ATOM 3824 C C . ASN A 1 465 ? 35.671 62.120 -0.474 1.00 32.96 ? 498 ASN A C 1 ATOM 3825 O O . ASN A 1 465 ? 35.386 63.246 -0.019 1.00 32.95 ? 498 ASN A O 1 ATOM 3826 C CB . ASN A 1 465 ? 36.901 62.983 -2.455 1.00 36.14 ? 498 ASN A CB 1 ATOM 3827 C CG . ASN A 1 465 ? 38.265 63.204 -3.067 1.00 41.38 ? 498 ASN A CG 1 ATOM 3828 O OD1 . ASN A 1 465 ? 38.386 63.856 -4.117 1.00 48.05 ? 498 ASN A OD1 1 ATOM 3829 N ND2 . ASN A 1 465 ? 39.314 62.663 -2.416 1.00 43.19 ? 498 ASN A ND2 1 ATOM 3830 N N . LEU A 1 466 ? 34.928 61.037 -0.282 1.00 30.61 ? 499 LEU A N 1 ATOM 3831 C CA . LEU A 1 466 ? 33.659 61.088 0.523 1.00 30.37 ? 499 LEU A CA 1 ATOM 3832 C C . LEU A 1 466 ? 33.735 59.989 1.569 1.00 29.77 ? 499 LEU A C 1 ATOM 3833 O O . LEU A 1 466 ? 34.216 58.897 1.270 1.00 30.13 ? 499 LEU A O 1 ATOM 3834 C CB . LEU A 1 466 ? 32.403 60.878 -0.362 1.00 29.50 ? 499 LEU A CB 1 ATOM 3835 C CG . LEU A 1 466 ? 32.107 61.945 -1.427 1.00 30.79 ? 499 LEU A CG 1 ATOM 3836 C CD1 . LEU A 1 466 ? 30.904 61.523 -2.270 1.00 33.75 ? 499 LEU A CD1 1 ATOM 3837 C CD2 . LEU A 1 466 ? 31.887 63.364 -0.819 1.00 33.02 ? 499 LEU A CD2 1 ATOM 3838 N N . PRO A 1 467 ? 33.223 60.237 2.814 1.00 28.15 ? 500 PRO A N 1 ATOM 3839 C CA . PRO A 1 467 ? 33.228 59.138 3.753 1.00 27.09 ? 500 PRO A CA 1 ATOM 3840 C C . PRO A 1 467 ? 32.248 58.016 3.407 1.00 26.55 ? 500 PRO A C 1 ATOM 3841 O O . PRO A 1 467 ? 31.204 58.226 2.739 1.00 25.59 ? 500 PRO A O 1 ATOM 3842 C CB . PRO A 1 467 ? 32.775 59.796 5.092 1.00 27.05 ? 500 PRO A CB 1 ATOM 3843 C CG . PRO A 1 467 ? 33.010 61.238 4.911 1.00 28.74 ? 500 PRO A CG 1 ATOM 3844 C CD . PRO A 1 467 ? 32.790 61.491 3.445 1.00 29.27 ? 500 PRO A CD 1 ATOM 3845 N N . ARG A 1 468 ? 32.559 56.827 3.911 1.00 24.85 ? 501 ARG A N 1 ATOM 3846 C CA . ARG A 1 468 ? 31.722 55.660 3.687 1.00 25.58 ? 501 ARG A CA 1 ATOM 3847 C C . ARG A 1 468 ? 30.330 55.785 4.350 1.00 24.63 ? 501 ARG A C 1 ATOM 3848 O O . ARG A 1 468 ? 30.232 56.045 5.554 1.00 25.32 ? 501 ARG A O 1 ATOM 3849 C CB . ARG A 1 468 ? 32.426 54.438 4.237 1.00 26.16 ? 501 ARG A CB 1 ATOM 3850 C CG A ARG A 1 468 ? 31.689 53.111 4.040 0.50 25.06 ? 501 ARG A CG 1 ATOM 3851 C CG B ARG A 1 468 ? 31.577 53.174 4.277 0.50 28.58 ? 501 ARG A CG 1 ATOM 3852 C CD A ARG A 1 468 ? 32.281 51.982 4.885 0.50 27.02 ? 501 ARG A CD 1 ATOM 3853 C CD B ARG A 1 468 ? 32.356 52.007 4.826 0.50 34.33 ? 501 ARG A CD 1 ATOM 3854 N NE A ARG A 1 468 ? 33.673 51.692 4.531 0.50 22.70 ? 501 ARG A NE 1 ATOM 3855 N NE B ARG A 1 468 ? 31.553 51.153 5.691 0.50 36.93 ? 501 ARG A NE 1 ATOM 3856 C CZ A ARG A 1 468 ? 34.064 50.829 3.594 0.50 25.34 ? 501 ARG A CZ 1 ATOM 3857 C CZ B ARG A 1 468 ? 31.772 49.853 5.851 0.50 38.01 ? 501 ARG A CZ 1 ATOM 3858 N NH1 A ARG A 1 468 ? 33.181 50.137 2.902 0.50 26.79 ? 501 ARG A NH1 1 ATOM 3859 N NH1 B ARG A 1 468 ? 32.770 49.278 5.192 0.50 40.50 ? 501 ARG A NH1 1 ATOM 3860 N NH2 A ARG A 1 468 ? 35.370 50.651 3.370 0.50 27.48 ? 501 ARG A NH2 1 ATOM 3861 N NH2 B ARG A 1 468 ? 31.018 49.140 6.674 0.50 36.06 ? 501 ARG A NH2 1 ATOM 3862 N N . ILE A 1 469 ? 29.274 55.542 3.574 1.00 24.87 ? 502 ILE A N 1 ATOM 3863 C CA . ILE A 1 469 ? 27.923 55.382 4.205 1.00 24.00 ? 502 ILE A CA 1 ATOM 3864 C C . ILE A 1 469 ? 27.423 54.027 3.780 1.00 25.03 ? 502 ILE A C 1 ATOM 3865 O O . ILE A 1 469 ? 27.459 53.671 2.564 1.00 26.63 ? 502 ILE A O 1 ATOM 3866 C CB . ILE A 1 469 ? 26.931 56.479 3.804 1.00 23.83 ? 502 ILE A CB 1 ATOM 3867 C CG1 . ILE A 1 469 ? 27.399 57.853 4.292 1.00 24.26 ? 502 ILE A CG1 1 ATOM 3868 C CG2 . ILE A 1 469 ? 25.501 56.112 4.309 1.00 22.34 ? 502 ILE A CG2 1 ATOM 3869 C CD1 . ILE A 1 469 ? 26.506 58.957 3.789 1.00 26.86 ? 502 ILE A CD1 1 ATOM 3870 N N . ASN A 1 470 ? 26.936 53.240 4.730 1.00 23.36 ? 503 ASN A N 1 ATOM 3871 C CA . ASN A 1 470 ? 26.403 51.882 4.471 1.00 26.22 ? 503 ASN A CA 1 ATOM 3872 C C . ASN A 1 470 ? 24.927 51.820 4.110 1.00 26.70 ? 503 ASN A C 1 ATOM 3873 O O . ASN A 1 470 ? 24.173 52.768 4.422 1.00 25.20 ? 503 ASN A O 1 ATOM 3874 C CB . ASN A 1 470 ? 26.628 51.021 5.715 1.00 27.97 ? 503 ASN A CB 1 ATOM 3875 C CG . ASN A 1 470 ? 28.026 51.113 6.214 1.00 32.37 ? 503 ASN A CG 1 ATOM 3876 O OD1 . ASN A 1 470 ? 28.932 50.616 5.553 1.00 33.10 ? 503 ASN A OD1 1 ATOM 3877 N ND2 . ASN A 1 470 ? 28.239 51.798 7.359 1.00 33.69 ? 503 ASN A ND2 1 ATOM 3878 N N . LYS A 1 471 ? 24.477 50.705 3.527 1.00 27.39 ? 504 LYS A N 1 ATOM 3879 C CA . LYS A 1 471 ? 23.041 50.523 3.254 1.00 29.32 ? 504 LYS A CA 1 ATOM 3880 C C . LYS A 1 471 ? 22.382 50.293 4.575 1.00 29.93 ? 504 LYS A C 1 ATOM 3881 O O . LYS A 1 471 ? 23.013 49.799 5.500 1.00 29.69 ? 504 LYS A O 1 ATOM 3882 C CB . LYS A 1 471 ? 22.794 49.256 2.416 1.00 30.01 ? 504 LYS A CB 1 ATOM 3883 C CG . LYS A 1 471 ? 23.474 49.333 1.124 1.00 32.69 ? 504 LYS A CG 1 ATOM 3884 C CD . LYS A 1 471 ? 23.322 48.041 0.310 1.00 30.20 ? 504 LYS A CD 1 ATOM 3885 C CE . LYS A 1 471 ? 24.060 48.267 -1.015 1.00 36.88 ? 504 LYS A CE 1 ATOM 3886 N NZ . LYS A 1 471 ? 23.976 47.148 -1.993 1.00 37.02 ? 504 LYS A NZ 1 ATOM 3887 N N . LEU A 1 472 ? 21.112 50.674 4.668 1.00 30.99 ? 505 LEU A N 1 ATOM 3888 C CA . LEU A 1 472 ? 20.295 50.259 5.785 1.00 33.20 ? 505 LEU A CA 1 ATOM 3889 C C . LEU A 1 472 ? 19.812 48.865 5.532 1.00 33.56 ? 505 LEU A C 1 ATOM 3890 O O . LEU A 1 472 ? 19.242 48.546 4.449 1.00 37.25 ? 505 LEU A O 1 ATOM 3891 C CB . LEU A 1 472 ? 19.040 51.140 5.893 1.00 32.50 ? 505 LEU A CB 1 ATOM 3892 C CG . LEU A 1 472 ? 19.043 52.190 6.965 1.00 35.34 ? 505 LEU A CG 1 ATOM 3893 C CD1 . LEU A 1 472 ? 17.648 52.806 7.111 1.00 35.49 ? 505 LEU A CD1 1 ATOM 3894 C CD2 . LEU A 1 472 ? 19.553 51.657 8.309 1.00 32.26 ? 505 LEU A CD2 1 ATOM 3895 N N . GLY A 1 473 ? 20.013 48.013 6.525 1.00 34.49 ? 506 GLY A N 1 ATOM 3896 C CA . GLY A 1 473 ? 19.556 46.652 6.460 1.00 32.23 ? 506 GLY A CA 1 ATOM 3897 C C . GLY A 1 473 ? 18.444 46.331 7.434 1.00 32.00 ? 506 GLY A C 1 ATOM 3898 O O . GLY A 1 473 ? 17.274 46.675 7.216 1.00 33.16 ? 506 GLY A O 1 ATOM 3899 N N . SER A 1 474 ? 18.800 45.660 8.516 1.00 32.88 ? 507 SER A N 1 ATOM 3900 C CA . SER A 1 474 ? 17.781 45.277 9.463 1.00 32.31 ? 507 SER A CA 1 ATOM 3901 C C . SER A 1 474 ? 18.304 45.114 10.885 1.00 30.31 ? 507 SER A C 1 ATOM 3902 O O . SER A 1 474 ? 19.472 45.301 11.139 1.00 29.22 ? 507 SER A O 1 ATOM 3903 C CB . SER A 1 474 ? 17.102 44.037 8.978 1.00 35.13 ? 507 SER A CB 1 ATOM 3904 O OG . SER A 1 474 ? 18.075 43.007 8.905 1.00 38.43 ? 507 SER A OG 1 ATOM 3905 N N . GLY A 1 475 ? 17.413 44.833 11.824 1.00 29.14 ? 508 GLY A N 1 ATOM 3906 C CA . GLY A 1 475 ? 17.832 44.499 13.146 1.00 26.80 ? 508 GLY A CA 1 ATOM 3907 C C . GLY A 1 475 ? 17.690 45.565 14.244 1.00 25.55 ? 508 GLY A C 1 ATOM 3908 O O . GLY A 1 475 ? 18.209 45.413 15.350 1.00 26.51 ? 508 GLY A O 1 ATOM 3909 N N . SER A 1 476 ? 17.098 46.705 13.918 1.00 21.71 ? 509 SER A N 1 ATOM 3910 C CA . SER A 1 476 ? 16.728 47.670 14.949 1.00 18.85 ? 509 SER A CA 1 ATOM 3911 C C . SER A 1 476 ? 15.451 48.334 14.479 1.00 20.09 ? 509 SER A C 1 ATOM 3912 O O . SER A 1 476 ? 14.881 47.947 13.457 1.00 19.10 ? 509 SER A O 1 ATOM 3913 C CB . SER A 1 476 ? 17.849 48.710 15.225 1.00 20.29 ? 509 SER A CB 1 ATOM 3914 O OG . SER A 1 476 ? 17.486 49.562 16.340 1.00 19.55 ? 509 SER A OG 1 ATOM 3915 N N . ASP A 1 477 ? 14.935 49.245 15.283 1.00 18.58 ? 510 ASP A N 1 ATOM 3916 C CA . ASP A 1 477 ? 13.531 49.721 15.127 1.00 17.45 ? 510 ASP A CA 1 ATOM 3917 C C . ASP A 1 477 ? 13.170 50.467 13.860 1.00 19.00 ? 510 ASP A C 1 ATOM 3918 O O . ASP A 1 477 ? 11.988 50.690 13.631 1.00 19.80 ? 510 ASP A O 1 ATOM 3919 C CB . ASP A 1 477 ? 13.167 50.541 16.367 1.00 17.19 ? 510 ASP A CB 1 ATOM 3920 C CG . ASP A 1 477 ? 13.189 49.675 17.638 1.00 18.51 ? 510 ASP A CG 1 ATOM 3921 O OD1 . ASP A 1 477 ? 12.343 48.723 17.671 1.00 18.47 ? 510 ASP A OD1 1 ATOM 3922 O OD2 . ASP A 1 477 ? 14.003 49.957 18.568 1.00 19.76 ? 510 ASP A OD2 1 ATOM 3923 N N . PHE A 1 478 ? 14.176 50.877 13.056 1.00 18.69 ? 511 PHE A N 1 ATOM 3924 C CA . PHE A 1 478 ? 13.855 51.493 11.779 1.00 18.94 ? 511 PHE A CA 1 ATOM 3925 C C . PHE A 1 478 ? 13.239 50.474 10.812 1.00 19.65 ? 511 PHE A C 1 ATOM 3926 O O . PHE A 1 478 ? 12.704 50.891 9.832 1.00 19.34 ? 511 PHE A O 1 ATOM 3927 C CB . PHE A 1 478 ? 15.116 52.042 11.109 1.00 19.76 ? 511 PHE A CB 1 ATOM 3928 C CG . PHE A 1 478 ? 16.117 50.991 10.830 1.00 21.31 ? 511 PHE A CG 1 ATOM 3929 C CD1 . PHE A 1 478 ? 16.029 50.252 9.662 1.00 22.07 ? 511 PHE A CD1 1 ATOM 3930 C CD2 . PHE A 1 478 ? 17.117 50.725 11.759 1.00 22.48 ? 511 PHE A CD2 1 ATOM 3931 C CE1 . PHE A 1 478 ? 16.966 49.178 9.401 1.00 20.84 ? 511 PHE A CE1 1 ATOM 3932 C CE2 . PHE A 1 478 ? 18.038 49.669 11.520 1.00 23.74 ? 511 PHE A CE2 1 ATOM 3933 C CZ . PHE A 1 478 ? 17.942 48.921 10.349 1.00 22.78 ? 511 PHE A CZ 1 ATOM 3934 N N . GLU A 1 479 ? 13.310 49.175 11.103 1.00 19.23 ? 512 GLU A N 1 ATOM 3935 C CA . GLU A 1 479 ? 13.012 48.173 10.057 1.00 19.05 ? 512 GLU A CA 1 ATOM 3936 C C . GLU A 1 479 ? 11.603 48.316 9.508 1.00 20.17 ? 512 GLU A C 1 ATOM 3937 O O . GLU A 1 479 ? 11.425 48.349 8.262 1.00 20.04 ? 512 GLU A O 1 ATOM 3938 C CB A GLU A 1 479 ? 13.076 46.785 10.682 0.50 20.32 ? 512 GLU A CB 1 ATOM 3939 C CB B GLU A 1 479 ? 13.324 46.788 10.606 0.50 20.15 ? 512 GLU A CB 1 ATOM 3940 C CG A GLU A 1 479 ? 14.342 46.088 10.421 0.50 23.63 ? 512 GLU A CG 1 ATOM 3941 C CG B GLU A 1 479 ? 13.139 45.699 9.580 0.50 19.77 ? 512 GLU A CG 1 ATOM 3942 C CD A GLU A 1 479 ? 14.217 44.531 10.503 0.50 19.22 ? 512 GLU A CD 1 ATOM 3943 C CD B GLU A 1 479 ? 12.085 44.693 10.052 0.50 32.29 ? 512 GLU A CD 1 ATOM 3944 O OE1 A GLU A 1 479 ? 13.268 43.841 9.998 0.50 22.64 ? 512 GLU A OE1 1 ATOM 3945 O OE1 B GLU A 1 479 ? 10.841 45.064 10.070 0.50 29.51 ? 512 GLU A OE1 1 ATOM 3946 O OE2 A GLU A 1 479 ? 15.111 43.981 11.108 0.50 20.62 ? 512 GLU A OE2 1 ATOM 3947 O OE2 B GLU A 1 479 ? 12.529 43.554 10.399 0.50 28.80 ? 512 GLU A OE2 1 ATOM 3948 N N . ALA A 1 480 ? 10.582 48.393 10.371 1.00 19.23 ? 513 ALA A N 1 ATOM 3949 C CA . ALA A 1 480 ? 9.235 48.433 9.750 1.00 19.07 ? 513 ALA A CA 1 ATOM 3950 C C . ALA A 1 480 ? 9.053 49.752 8.965 1.00 19.77 ? 513 ALA A C 1 ATOM 3951 O O . ALA A 1 480 ? 8.402 49.797 7.925 1.00 19.62 ? 513 ALA A O 1 ATOM 3952 C CB . ALA A 1 480 ? 8.120 48.337 10.817 1.00 20.60 ? 513 ALA A CB 1 ATOM 3953 N N . TYR A 1 481 ? 9.592 50.844 9.490 1.00 16.89 ? 514 TYR A N 1 ATOM 3954 C CA . TYR A 1 481 ? 9.421 52.134 8.834 1.00 18.21 ? 514 TYR A CA 1 ATOM 3955 C C . TYR A 1 481 ? 10.047 52.142 7.460 1.00 17.64 ? 514 TYR A C 1 ATOM 3956 O O . TYR A 1 481 ? 9.417 52.670 6.519 1.00 18.37 ? 514 TYR A O 1 ATOM 3957 C CB . TYR A 1 481 ? 10.037 53.273 9.721 1.00 17.14 ? 514 TYR A CB 1 ATOM 3958 C CG . TYR A 1 481 ? 9.257 53.261 11.049 1.00 17.84 ? 514 TYR A CG 1 ATOM 3959 C CD1 . TYR A 1 481 ? 9.678 52.422 12.075 1.00 18.04 ? 514 TYR A CD1 1 ATOM 3960 C CD2 . TYR A 1 481 ? 8.071 53.982 11.225 1.00 18.21 ? 514 TYR A CD2 1 ATOM 3961 C CE1 . TYR A 1 481 ? 8.961 52.247 13.251 1.00 16.60 ? 514 TYR A CE1 1 ATOM 3962 C CE2 . TYR A 1 481 ? 7.324 53.810 12.408 1.00 18.61 ? 514 TYR A CE2 1 ATOM 3963 C CZ . TYR A 1 481 ? 7.770 52.964 13.388 1.00 17.35 ? 514 TYR A CZ 1 ATOM 3964 O OH . TYR A 1 481 ? 6.967 52.792 14.483 1.00 18.55 ? 514 TYR A OH 1 ATOM 3965 N N . PHE A 1 482 ? 11.262 51.593 7.331 1.00 17.33 ? 515 PHE A N 1 ATOM 3966 C CA . PHE A 1 482 ? 11.957 51.614 6.025 1.00 17.70 ? 515 PHE A CA 1 ATOM 3967 C C . PHE A 1 482 ? 11.506 50.447 5.115 1.00 18.37 ? 515 PHE A C 1 ATOM 3968 O O . PHE A 1 482 ? 11.090 50.661 3.956 1.00 19.30 ? 515 PHE A O 1 ATOM 3969 C CB . PHE A 1 482 ? 13.481 51.556 6.261 1.00 18.24 ? 515 PHE A CB 1 ATOM 3970 C CG . PHE A 1 482 ? 14.290 51.752 5.025 1.00 19.35 ? 515 PHE A CG 1 ATOM 3971 C CD1 . PHE A 1 482 ? 14.174 52.894 4.276 1.00 19.54 ? 515 PHE A CD1 1 ATOM 3972 C CD2 . PHE A 1 482 ? 15.147 50.785 4.614 1.00 22.51 ? 515 PHE A CD2 1 ATOM 3973 C CE1 . PHE A 1 482 ? 14.943 53.114 3.158 1.00 20.10 ? 515 PHE A CE1 1 ATOM 3974 C CE2 . PHE A 1 482 ? 15.895 50.984 3.434 1.00 24.58 ? 515 PHE A CE2 1 ATOM 3975 C CZ . PHE A 1 482 ? 15.812 52.131 2.730 1.00 23.19 ? 515 PHE A CZ 1 ATOM 3976 N N . GLN A 1 483 ? 11.610 49.216 5.643 1.00 17.51 ? 516 GLN A N 1 ATOM 3977 C CA . GLN A 1 483 ? 11.444 48.026 4.785 1.00 17.94 ? 516 GLN A CA 1 ATOM 3978 C C . GLN A 1 483 ? 9.992 47.639 4.548 1.00 18.09 ? 516 GLN A C 1 ATOM 3979 O O . GLN A 1 483 ? 9.725 46.972 3.544 1.00 18.22 ? 516 GLN A O 1 ATOM 3980 C CB . GLN A 1 483 ? 12.204 46.829 5.442 1.00 19.19 ? 516 GLN A CB 1 ATOM 3981 C CG . GLN A 1 483 ? 13.650 47.083 5.759 1.00 24.48 ? 516 GLN A CG 1 ATOM 3982 C CD . GLN A 1 483 ? 14.536 47.108 4.588 1.00 27.72 ? 516 GLN A CD 1 ATOM 3983 O OE1 . GLN A 1 483 ? 14.063 46.993 3.473 1.00 27.69 ? 516 GLN A OE1 1 ATOM 3984 N NE2 . GLN A 1 483 ? 15.893 47.202 4.817 1.00 23.90 ? 516 GLN A NE2 1 ATOM 3985 N N . ARG A 1 484 ? 9.061 48.058 5.435 1.00 17.74 ? 517 ARG A N 1 ATOM 3986 C CA . ARG A 1 484 ? 7.643 47.816 5.187 1.00 17.53 ? 517 ARG A CA 1 ATOM 3987 C C . ARG A 1 484 ? 6.937 49.043 4.607 1.00 18.72 ? 517 ARG A C 1 ATOM 3988 O O . ARG A 1 484 ? 6.163 48.913 3.688 1.00 19.47 ? 517 ARG A O 1 ATOM 3989 C CB . ARG A 1 484 ? 6.906 47.311 6.479 1.00 18.54 ? 517 ARG A CB 1 ATOM 3990 C CG . ARG A 1 484 ? 5.591 46.601 6.097 1.00 18.00 ? 517 ARG A CG 1 ATOM 3991 C CD . ARG A 1 484 ? 4.646 46.415 7.284 1.00 18.22 ? 517 ARG A CD 1 ATOM 3992 N NE . ARG A 1 484 ? 5.186 45.543 8.351 1.00 18.28 ? 517 ARG A NE 1 ATOM 3993 C CZ . ARG A 1 484 ? 4.368 44.984 9.248 1.00 16.93 ? 517 ARG A CZ 1 ATOM 3994 N NH1 . ARG A 1 484 ? 3.053 45.201 9.265 1.00 17.53 ? 517 ARG A NH1 1 ATOM 3995 N NH2 . ARG A 1 484 ? 4.866 44.202 10.224 1.00 17.53 ? 517 ARG A NH2 1 ATOM 3996 N N . LEU A 1 485 ? 7.200 50.181 5.252 1.00 18.47 ? 518 LEU A N 1 ATOM 3997 C CA . LEU A 1 485 ? 6.430 51.398 4.868 1.00 17.68 ? 518 LEU A CA 1 ATOM 3998 C C . LEU A 1 485 ? 7.156 52.298 3.896 1.00 18.75 ? 518 LEU A C 1 ATOM 3999 O O . LEU A 1 485 ? 6.486 53.192 3.381 1.00 20.13 ? 518 LEU A O 1 ATOM 4000 C CB A LEU A 1 485 ? 6.107 52.224 6.123 0.65 19.20 ? 518 LEU A CB 1 ATOM 4001 C CB B LEU A 1 485 ? 5.990 52.195 6.109 0.35 16.74 ? 518 LEU A CB 1 ATOM 4002 C CG A LEU A 1 485 ? 4.954 51.842 7.065 0.65 24.05 ? 518 LEU A CG 1 ATOM 4003 C CG B LEU A 1 485 ? 5.241 51.401 7.173 0.35 11.22 ? 518 LEU A CG 1 ATOM 4004 C CD1 A LEU A 1 485 ? 4.886 50.360 7.415 0.65 30.69 ? 518 LEU A CD1 1 ATOM 4005 C CD1 B LEU A 1 485 ? 4.548 52.300 8.211 0.35 12.01 ? 518 LEU A CD1 1 ATOM 4006 C CD2 A LEU A 1 485 ? 4.941 52.745 8.329 0.65 22.67 ? 518 LEU A CD2 1 ATOM 4007 C CD2 B LEU A 1 485 ? 4.073 50.606 6.544 0.35 10.72 ? 518 LEU A CD2 1 ATOM 4008 N N . GLY A 1 486 ? 8.457 52.133 3.683 1.00 17.15 ? 519 GLY A N 1 ATOM 4009 C CA . GLY A 1 486 ? 9.134 52.998 2.714 1.00 17.70 ? 519 GLY A CA 1 ATOM 4010 C C . GLY A 1 486 ? 9.338 54.432 3.151 1.00 16.70 ? 519 GLY A C 1 ATOM 4011 O O . GLY A 1 486 ? 9.283 55.385 2.328 1.00 17.18 ? 519 GLY A O 1 ATOM 4012 N N . ILE A 1 487 ? 9.626 54.605 4.435 1.00 17.90 ? 520 ILE A N 1 ATOM 4013 C CA . ILE A 1 487 ? 9.940 55.906 4.975 1.00 17.60 ? 520 ILE A CA 1 ATOM 4014 C C . ILE A 1 487 ? 11.448 56.053 5.066 1.00 19.07 ? 520 ILE A C 1 ATOM 4015 O O . ILE A 1 487 ? 12.139 55.205 5.683 1.00 18.49 ? 520 ILE A O 1 ATOM 4016 C CB . ILE A 1 487 ? 9.293 56.036 6.370 1.00 18.31 ? 520 ILE A CB 1 ATOM 4017 C CG1 . ILE A 1 487 ? 7.775 56.014 6.279 1.00 18.00 ? 520 ILE A CG1 1 ATOM 4018 C CG2 . ILE A 1 487 ? 9.758 57.334 7.055 1.00 18.63 ? 520 ILE A CG2 1 ATOM 4019 C CD1 . ILE A 1 487 ? 7.093 55.763 7.640 1.00 19.66 ? 520 ILE A CD1 1 ATOM 4020 N N . ALA A 1 488 ? 12.024 57.050 4.378 1.00 17.61 ? 521 ALA A N 1 ATOM 4021 C CA . ALA A 1 488 ? 13.447 57.265 4.380 1.00 17.24 ? 521 ALA A CA 1 ATOM 4022 C C . ALA A 1 488 ? 14.006 57.217 5.798 1.00 17.02 ? 521 ALA A C 1 ATOM 4023 O O . ALA A 1 488 ? 13.466 57.899 6.683 1.00 18.12 ? 521 ALA A O 1 ATOM 4024 C CB . ALA A 1 488 ? 13.757 58.623 3.787 1.00 18.54 ? 521 ALA A CB 1 ATOM 4025 N N . SER A 1 489 ? 15.044 56.404 6.048 1.00 17.81 ? 522 SER A N 1 ATOM 4026 C CA . SER A 1 489 ? 15.555 56.164 7.387 1.00 18.33 ? 522 SER A CA 1 ATOM 4027 C C . SER A 1 489 ? 17.047 56.286 7.449 1.00 19.45 ? 522 SER A C 1 ATOM 4028 O O . SER A 1 489 ? 17.774 56.124 6.429 1.00 19.59 ? 522 SER A O 1 ATOM 4029 C CB . SER A 1 489 ? 15.118 54.813 7.908 1.00 19.50 ? 522 SER A CB 1 ATOM 4030 O OG . SER A 1 489 ? 13.693 54.703 7.996 1.00 19.14 ? 522 SER A OG 1 ATOM 4031 N N . GLY A 1 490 ? 17.545 56.518 8.666 1.00 18.58 ? 523 GLY A N 1 ATOM 4032 C CA . GLY A 1 490 ? 18.971 56.752 8.878 1.00 19.01 ? 523 GLY A CA 1 ATOM 4033 C C . GLY A 1 490 ? 19.332 56.341 10.281 1.00 20.03 ? 523 GLY A C 1 ATOM 4034 O O . GLY A 1 490 ? 18.516 56.466 11.239 1.00 19.07 ? 523 GLY A O 1 ATOM 4035 N N . ARG A 1 491 ? 20.592 55.906 10.422 1.00 21.08 ? 524 ARG A N 1 ATOM 4036 C CA . ARG A 1 491 ? 21.156 55.687 11.736 1.00 21.25 ? 524 ARG A CA 1 ATOM 4037 C C . ARG A 1 491 ? 22.619 56.102 11.781 1.00 21.55 ? 524 ARG A C 1 ATOM 4038 O O . ARG A 1 491 ? 23.287 56.034 10.756 1.00 22.71 ? 524 ARG A O 1 ATOM 4039 C CB . ARG A 1 491 ? 20.995 54.272 12.190 1.00 24.48 ? 524 ARG A CB 1 ATOM 4040 C CG . ARG A 1 491 ? 21.712 53.266 11.411 1.00 26.21 ? 524 ARG A CG 1 ATOM 4041 C CD . ARG A 1 491 ? 21.155 51.842 11.740 1.00 31.96 ? 524 ARG A CD 1 ATOM 4042 N NE . ARG A 1 491 ? 21.256 51.467 13.169 1.00 35.46 ? 524 ARG A NE 1 ATOM 4043 C CZ . ARG A 1 491 ? 21.306 50.199 13.606 1.00 35.56 ? 524 ARG A CZ 1 ATOM 4044 N NH1 . ARG A 1 491 ? 21.345 49.948 14.918 1.00 38.17 ? 524 ARG A NH1 1 ATOM 4045 N NH2 . ARG A 1 491 ? 21.293 49.178 12.727 1.00 35.49 ? 524 ARG A NH2 1 ATOM 4046 N N . ALA A 1 492 ? 23.094 56.486 12.949 1.00 18.87 ? 525 ALA A N 1 ATOM 4047 C CA . ALA A 1 492 ? 24.468 56.882 13.121 1.00 20.15 ? 525 ALA A CA 1 ATOM 4048 C C . ALA A 1 492 ? 24.948 56.497 14.512 1.00 19.84 ? 525 ALA A C 1 ATOM 4049 O O . ALA A 1 492 ? 24.200 56.668 15.494 1.00 18.89 ? 525 ALA A O 1 ATOM 4050 C CB . ALA A 1 492 ? 24.621 58.353 12.948 1.00 21.02 ? 525 ALA A CB 1 ATOM 4051 N N . ARG A 1 493 ? 26.194 56.020 14.623 1.00 19.51 ? 526 ARG A N 1 ATOM 4052 C CA . ARG A 1 493 ? 26.743 55.652 15.920 1.00 20.10 ? 526 ARG A CA 1 ATOM 4053 C C . ARG A 1 493 ? 28.254 55.637 15.835 1.00 20.96 ? 526 ARG A C 1 ATOM 4054 O O . ARG A 1 493 ? 28.778 55.586 14.738 1.00 21.37 ? 526 ARG A O 1 ATOM 4055 C CB A ARG A 1 493 ? 26.231 54.310 16.419 0.65 19.94 ? 526 ARG A CB 1 ATOM 4056 C CB B ARG A 1 493 ? 26.249 54.236 16.262 0.35 20.69 ? 526 ARG A CB 1 ATOM 4057 C CG A ARG A 1 493 ? 26.819 53.156 15.634 0.65 22.06 ? 526 ARG A CG 1 ATOM 4058 C CG B ARG A 1 493 ? 26.385 53.291 15.041 0.35 22.69 ? 526 ARG A CG 1 ATOM 4059 C CD A ARG A 1 493 ? 26.446 51.883 16.182 0.65 23.41 ? 526 ARG A CD 1 ATOM 4060 C CD B ARG A 1 493 ? 25.721 51.933 15.153 0.35 28.90 ? 526 ARG A CD 1 ATOM 4061 N NE A ARG A 1 493 ? 25.078 51.922 16.634 0.65 28.61 ? 526 ARG A NE 1 ATOM 4062 N NE B ARG A 1 493 ? 25.591 51.341 13.818 0.35 30.78 ? 526 ARG A NE 1 ATOM 4063 C CZ A ARG A 1 493 ? 24.198 50.935 16.557 0.65 32.01 ? 526 ARG A CZ 1 ATOM 4064 C CZ B ARG A 1 493 ? 24.828 50.299 13.517 0.35 31.97 ? 526 ARG A CZ 1 ATOM 4065 N NH1 A ARG A 1 493 ? 22.990 51.154 17.050 0.65 25.18 ? 526 ARG A NH1 1 ATOM 4066 N NH1 B ARG A 1 493 ? 24.770 49.838 12.264 0.35 30.89 ? 526 ARG A NH1 1 ATOM 4067 N NH2 A ARG A 1 493 ? 24.515 49.769 15.975 0.65 33.53 ? 526 ARG A NH2 1 ATOM 4068 N NH2 B ARG A 1 493 ? 24.115 49.717 14.464 0.35 34.62 ? 526 ARG A NH2 1 ATOM 4069 N N . TYR A 1 494 ? 28.939 55.599 16.970 1.00 19.56 ? 527 TYR A N 1 ATOM 4070 C CA . TYR A 1 494 ? 30.395 55.398 16.933 1.00 20.78 ? 527 TYR A CA 1 ATOM 4071 C C . TYR A 1 494 ? 30.662 53.945 16.904 1.00 21.70 ? 527 TYR A C 1 ATOM 4072 O O . TYR A 1 494 ? 29.966 53.138 17.502 1.00 22.00 ? 527 TYR A O 1 ATOM 4073 C CB . TYR A 1 494 ? 31.128 56.050 18.132 1.00 19.62 ? 527 TYR A CB 1 ATOM 4074 C CG . TYR A 1 494 ? 31.982 57.202 17.666 1.00 21.23 ? 527 TYR A CG 1 ATOM 4075 C CD1 . TYR A 1 494 ? 31.389 58.363 17.175 1.00 19.52 ? 527 TYR A CD1 1 ATOM 4076 C CD2 . TYR A 1 494 ? 33.383 57.104 17.608 1.00 21.25 ? 527 TYR A CD2 1 ATOM 4077 C CE1 . TYR A 1 494 ? 32.161 59.437 16.702 1.00 21.55 ? 527 TYR A CE1 1 ATOM 4078 C CE2 . TYR A 1 494 ? 34.150 58.134 17.113 1.00 21.50 ? 527 TYR A CE2 1 ATOM 4079 C CZ . TYR A 1 494 ? 33.562 59.301 16.671 1.00 20.80 ? 527 TYR A CZ 1 ATOM 4080 O OH . TYR A 1 494 ? 34.331 60.344 16.175 1.00 23.47 ? 527 TYR A OH 1 ATOM 4081 N N . THR A 1 495 ? 31.749 53.618 16.213 1.00 23.73 ? 528 THR A N 1 ATOM 4082 C CA . THR A 1 495 ? 32.089 52.259 15.990 1.00 24.44 ? 528 THR A CA 1 ATOM 4083 C C . THR A 1 495 ? 33.593 52.006 16.052 1.00 25.82 ? 528 THR A C 1 ATOM 4084 O O . THR A 1 495 ? 34.393 52.929 16.199 1.00 24.98 ? 528 THR A O 1 ATOM 4085 C CB . THR A 1 495 ? 31.554 51.891 14.577 1.00 25.15 ? 528 THR A CB 1 ATOM 4086 O OG1 . THR A 1 495 ? 31.585 50.491 14.425 1.00 28.88 ? 528 THR A OG1 1 ATOM 4087 C CG2 . THR A 1 495 ? 32.325 52.556 13.440 1.00 26.75 ? 528 THR A CG2 1 ATOM 4088 N N . LYS A 1 496 ? 33.929 50.728 15.928 1.00 27.15 ? 529 LYS A N 1 ATOM 4089 C CA . LYS A 1 496 ? 35.325 50.253 15.902 1.00 28.95 ? 529 LYS A CA 1 ATOM 4090 C C . LYS A 1 496 ? 36.001 50.441 14.548 1.00 30.94 ? 529 LYS A C 1 ATOM 4091 O O . LYS A 1 496 ? 35.349 50.754 13.566 1.00 30.73 ? 529 LYS A O 1 ATOM 4092 C CB . LYS A 1 496 ? 35.335 48.768 16.286 1.00 28.64 ? 529 LYS A CB 1 ATOM 4093 C CG . LYS A 1 496 ? 34.671 47.886 15.207 1.00 30.34 ? 529 LYS A CG 1 ATOM 4094 C CD . LYS A 1 496 ? 34.843 46.426 15.464 1.00 38.35 ? 529 LYS A CD 1 ATOM 4095 C CE . LYS A 1 496 ? 33.699 45.801 16.141 1.00 38.59 ? 529 LYS A CE 1 ATOM 4096 N NZ . LYS A 1 496 ? 32.955 44.843 15.285 1.00 40.12 ? 529 LYS A NZ 1 ATOM 4097 N N . ASN A 1 497 ? 37.316 50.238 14.507 1.00 32.72 ? 530 ASN A N 1 ATOM 4098 C CA . ASN A 1 497 ? 38.080 50.298 13.265 1.00 35.97 ? 530 ASN A CA 1 ATOM 4099 C C . ASN A 1 497 ? 38.023 48.922 12.608 1.00 38.26 ? 530 ASN A C 1 ATOM 4100 O O . ASN A 1 497 ? 38.705 48.016 13.054 1.00 38.72 ? 530 ASN A O 1 ATOM 4101 C CB . ASN A 1 497 ? 39.547 50.667 13.560 1.00 35.26 ? 530 ASN A CB 1 ATOM 4102 C CG . ASN A 1 497 ? 40.397 50.747 12.295 1.00 37.18 ? 530 ASN A CG 1 ATOM 4103 O OD1 . ASN A 1 497 ? 39.963 50.349 11.211 1.00 39.18 ? 530 ASN A OD1 1 ATOM 4104 N ND2 . ASN A 1 497 ? 41.600 51.278 12.431 1.00 39.22 ? 530 ASN A ND2 1 ATOM 4105 N N . LYS A 1 498 ? 37.244 48.774 11.545 1.00 41.76 ? 531 LYS A N 1 ATOM 4106 C CA . LYS A 1 498 ? 37.025 47.444 10.953 1.00 44.97 ? 531 LYS A CA 1 ATOM 4107 C C . LYS A 1 498 ? 38.234 46.876 10.213 1.00 46.26 ? 531 LYS A C 1 ATOM 4108 O O . LYS A 1 498 ? 38.287 45.670 9.970 1.00 47.61 ? 531 LYS A O 1 ATOM 4109 C CB . LYS A 1 498 ? 35.772 47.382 10.065 1.00 45.48 ? 531 LYS A CB 1 ATOM 4110 C CG . LYS A 1 498 ? 34.976 48.681 9.923 1.00 49.23 ? 531 LYS A CG 1 ATOM 4111 C CD . LYS A 1 498 ? 33.920 48.594 8.795 1.00 53.57 ? 531 LYS A CD 1 ATOM 4112 C CE . LYS A 1 498 ? 33.321 49.981 8.504 1.00 54.77 ? 531 LYS A CE 1 ATOM 4113 N NZ . LYS A 1 498 ? 34.064 50.755 7.471 1.00 54.66 ? 531 LYS A NZ 1 ATOM 4114 N N . LYS A 1 499 ? 39.197 47.723 9.853 1.00 47.80 ? 532 LYS A N 1 ATOM 4115 C CA . LYS A 1 499 ? 40.400 47.212 9.193 1.00 48.64 ? 532 LYS A CA 1 ATOM 4116 C C . LYS A 1 499 ? 41.377 46.520 10.165 1.00 48.45 ? 532 LYS A C 1 ATOM 4117 O O . LYS A 1 499 ? 42.199 45.700 9.737 1.00 49.14 ? 532 LYS A O 1 ATOM 4118 C CB . LYS A 1 499 ? 41.079 48.255 8.268 1.00 49.52 ? 532 LYS A CB 1 ATOM 4119 C CG . LYS A 1 499 ? 41.361 49.655 8.830 1.00 51.21 ? 532 LYS A CG 1 ATOM 4120 C CD . LYS A 1 499 ? 42.748 49.765 9.492 1.00 54.62 ? 532 LYS A CD 1 ATOM 4121 C CE . LYS A 1 499 ? 43.134 51.231 9.824 1.00 54.08 ? 532 LYS A CE 1 ATOM 4122 N NZ . LYS A 1 499 ? 44.295 51.354 10.786 1.00 51.21 ? 532 LYS A NZ 1 ATOM 4123 N N . THR A 1 500 ? 41.255 46.819 11.462 1.00 47.04 ? 533 THR A N 1 ATOM 4124 C CA . THR A 1 500 ? 42.110 46.239 12.500 1.00 45.59 ? 533 THR A CA 1 ATOM 4125 C C . THR A 1 500 ? 41.328 45.425 13.551 1.00 44.99 ? 533 THR A C 1 ATOM 4126 O O . THR A 1 500 ? 41.832 44.445 14.090 1.00 44.54 ? 533 THR A O 1 ATOM 4127 C CB . THR A 1 500 ? 42.928 47.326 13.230 1.00 46.21 ? 533 THR A CB 1 ATOM 4128 O OG1 . THR A 1 500 ? 42.043 48.241 13.901 1.00 47.05 ? 533 THR A OG1 1 ATOM 4129 C CG2 . THR A 1 500 ? 43.830 48.094 12.249 1.00 46.05 ? 533 THR A CG2 1 ATOM 4130 N N . ASP A 1 501 ? 40.104 45.859 13.855 1.00 43.13 ? 534 ASP A N 1 ATOM 4131 C CA . ASP A 1 501 ? 39.260 45.208 14.840 1.00 42.05 ? 534 ASP A CA 1 ATOM 4132 C C . ASP A 1 501 ? 38.325 44.244 14.127 1.00 41.54 ? 534 ASP A C 1 ATOM 4133 O O . ASP A 1 501 ? 37.384 44.661 13.452 1.00 41.68 ? 534 ASP A O 1 ATOM 4134 C CB . ASP A 1 501 ? 38.451 46.252 15.612 1.00 41.69 ? 534 ASP A CB 1 ATOM 4135 C CG . ASP A 1 501 ? 39.337 47.303 16.282 1.00 44.19 ? 534 ASP A CG 1 ATOM 4136 O OD1 . ASP A 1 501 ? 40.543 47.031 16.498 1.00 43.94 ? 534 ASP A OD1 1 ATOM 4137 O OD2 . ASP A 1 501 ? 38.833 48.406 16.588 1.00 45.06 ? 534 ASP A OD2 1 ATOM 4138 N N . LYS A 1 502 ? 38.584 42.952 14.288 1.00 40.23 ? 535 LYS A N 1 ATOM 4139 C CA . LYS A 1 502 ? 37.913 41.925 13.505 1.00 39.65 ? 535 LYS A CA 1 ATOM 4140 C C . LYS A 1 502 ? 36.865 41.131 14.314 1.00 38.31 ? 535 LYS A C 1 ATOM 4141 O O . LYS A 1 502 ? 36.164 40.287 13.739 1.00 38.70 ? 535 LYS A O 1 ATOM 4142 C CB . LYS A 1 502 ? 38.960 40.969 12.897 1.00 40.73 ? 535 LYS A CB 1 ATOM 4143 C CG . LYS A 1 502 ? 40.184 41.671 12.312 1.00 44.22 ? 535 LYS A CG 1 ATOM 4144 C CD . LYS A 1 502 ? 40.239 41.633 10.790 1.00 49.79 ? 535 LYS A CD 1 ATOM 4145 C CE . LYS A 1 502 ? 39.506 42.822 10.175 1.00 52.63 ? 535 LYS A CE 1 ATOM 4146 N NZ . LYS A 1 502 ? 40.312 43.562 9.122 1.00 53.19 ? 535 LYS A NZ 1 ATOM 4147 N N . TYR A 1 503 ? 36.743 41.404 15.621 1.00 35.76 ? 536 TYR A N 1 ATOM 4148 C CA . TYR A 1 503 ? 35.704 40.778 16.455 1.00 34.31 ? 536 TYR A CA 1 ATOM 4149 C C . TYR A 1 503 ? 34.289 41.228 16.018 1.00 32.48 ? 536 TYR A C 1 ATOM 4150 O O . TYR A 1 503 ? 34.127 42.266 15.353 1.00 31.31 ? 536 TYR A O 1 ATOM 4151 C CB . TYR A 1 503 ? 35.934 41.067 17.953 1.00 34.12 ? 536 TYR A CB 1 ATOM 4152 C CG . TYR A 1 503 ? 36.218 42.514 18.265 1.00 35.92 ? 536 TYR A CG 1 ATOM 4153 C CD1 . TYR A 1 503 ? 37.534 43.003 18.259 1.00 37.85 ? 536 TYR A CD1 1 ATOM 4154 C CD2 . TYR A 1 503 ? 35.182 43.400 18.565 1.00 36.26 ? 536 TYR A CD2 1 ATOM 4155 C CE1 . TYR A 1 503 ? 37.812 44.338 18.534 1.00 38.07 ? 536 TYR A CE1 1 ATOM 4156 C CE2 . TYR A 1 503 ? 35.451 44.756 18.845 1.00 38.13 ? 536 TYR A CE2 1 ATOM 4157 C CZ . TYR A 1 503 ? 36.770 45.205 18.827 1.00 39.38 ? 536 TYR A CZ 1 ATOM 4158 O OH . TYR A 1 503 ? 37.053 46.529 19.092 1.00 43.09 ? 536 TYR A OH 1 ATOM 4159 N N . SER A 1 504 ? 33.284 40.409 16.364 1.00 31.42 ? 537 SER A N 1 ATOM 4160 C CA . SER A 1 504 ? 31.869 40.697 16.065 1.00 30.33 ? 537 SER A CA 1 ATOM 4161 C C . SER A 1 504 ? 31.301 41.659 17.128 1.00 29.79 ? 537 SER A C 1 ATOM 4162 O O . SER A 1 504 ? 31.727 41.637 18.282 1.00 30.71 ? 537 SER A O 1 ATOM 4163 C CB . SER A 1 504 ? 31.013 39.390 16.029 1.00 31.30 ? 537 SER A CB 1 ATOM 4164 O OG . SER A 1 504 ? 31.382 38.534 14.928 1.00 30.84 ? 537 SER A OG 1 ATOM 4165 N N . SER A 1 505 ? 30.356 42.509 16.724 1.00 29.32 ? 538 SER A N 1 ATOM 4166 C CA . SER A 1 505 ? 29.655 43.420 17.644 1.00 27.15 ? 538 SER A CA 1 ATOM 4167 C C . SER A 1 505 ? 30.682 44.071 18.557 1.00 25.02 ? 538 SER A C 1 ATOM 4168 O O . SER A 1 505 ? 31.589 44.752 18.110 1.00 27.49 ? 538 SER A O 1 ATOM 4169 C CB . SER A 1 505 ? 28.613 42.674 18.456 1.00 27.50 ? 538 SER A CB 1 ATOM 4170 O OG . SER A 1 505 ? 27.676 42.065 17.541 1.00 32.16 ? 538 SER A OG 1 ATOM 4171 N N . TYR A 1 506 ? 30.513 43.858 19.854 1.00 22.56 ? 539 TYR A N 1 ATOM 4172 C CA . TYR A 1 506 ? 31.525 44.268 20.824 1.00 22.15 ? 539 TYR A CA 1 ATOM 4173 C C . TYR A 1 506 ? 31.531 43.146 21.864 1.00 21.24 ? 539 TYR A C 1 ATOM 4174 O O . TYR A 1 506 ? 30.521 42.447 22.052 1.00 20.72 ? 539 TYR A O 1 ATOM 4175 C CB . TYR A 1 506 ? 31.215 45.651 21.462 1.00 22.43 ? 539 TYR A CB 1 ATOM 4176 C CG . TYR A 1 506 ? 29.804 45.830 21.945 1.00 22.62 ? 539 TYR A CG 1 ATOM 4177 C CD1 . TYR A 1 506 ? 29.459 45.633 23.280 1.00 20.79 ? 539 TYR A CD1 1 ATOM 4178 C CD2 . TYR A 1 506 ? 28.827 46.230 21.042 1.00 22.91 ? 539 TYR A CD2 1 ATOM 4179 C CE1 . TYR A 1 506 ? 28.103 45.795 23.714 1.00 21.98 ? 539 TYR A CE1 1 ATOM 4180 C CE2 . TYR A 1 506 ? 27.492 46.392 21.450 1.00 21.65 ? 539 TYR A CE2 1 ATOM 4181 C CZ . TYR A 1 506 ? 27.148 46.170 22.770 1.00 22.15 ? 539 TYR A CZ 1 ATOM 4182 O OH . TYR A 1 506 ? 25.783 46.355 23.084 1.00 20.38 ? 539 TYR A OH 1 ATOM 4183 N N . PRO A 1 507 ? 32.647 42.943 22.541 1.00 20.83 ? 540 PRO A N 1 ATOM 4184 C CA . PRO A 1 507 ? 32.784 41.748 23.388 1.00 20.59 ? 540 PRO A CA 1 ATOM 4185 C C . PRO A 1 507 ? 31.676 41.435 24.365 1.00 20.67 ? 540 PRO A C 1 ATOM 4186 O O . PRO A 1 507 ? 31.270 40.256 24.437 1.00 21.96 ? 540 PRO A O 1 ATOM 4187 C CB . PRO A 1 507 ? 34.156 41.946 24.079 1.00 20.69 ? 540 PRO A CB 1 ATOM 4188 C CG . PRO A 1 507 ? 34.946 42.668 23.010 1.00 20.94 ? 540 PRO A CG 1 ATOM 4189 C CD . PRO A 1 507 ? 33.924 43.684 22.412 1.00 19.94 ? 540 PRO A CD 1 ATOM 4190 N N . VAL A 1 508 ? 31.175 42.452 25.104 1.00 19.29 ? 541 VAL A N 1 ATOM 4191 C CA . VAL A 1 508 ? 30.218 42.190 26.159 1.00 18.91 ? 541 VAL A CA 1 ATOM 4192 C C . VAL A 1 508 ? 28.743 42.355 25.691 1.00 19.89 ? 541 VAL A C 1 ATOM 4193 O O . VAL A 1 508 ? 27.830 42.297 26.514 1.00 20.74 ? 541 VAL A O 1 ATOM 4194 C CB . VAL A 1 508 ? 30.491 42.978 27.454 1.00 19.93 ? 541 VAL A CB 1 ATOM 4195 C CG1 . VAL A 1 508 ? 31.916 42.632 28.003 1.00 20.25 ? 541 VAL A CG1 1 ATOM 4196 C CG2 . VAL A 1 508 ? 30.276 44.509 27.255 1.00 21.53 ? 541 VAL A CG2 1 ATOM 4197 N N . TYR A 1 509 ? 28.579 42.418 24.381 1.00 19.49 ? 542 TYR A N 1 ATOM 4198 C CA . TYR A 1 509 ? 27.239 42.546 23.758 1.00 19.80 ? 542 TYR A CA 1 ATOM 4199 C C . TYR A 1 509 ? 26.242 41.534 24.342 1.00 20.90 ? 542 TYR A C 1 ATOM 4200 O O . TYR A 1 509 ? 26.473 40.332 24.290 1.00 21.60 ? 542 TYR A O 1 ATOM 4201 C CB . TYR A 1 509 ? 27.370 42.353 22.277 1.00 21.29 ? 542 TYR A CB 1 ATOM 4202 C CG . TYR A 1 509 ? 26.051 42.220 21.535 1.00 20.59 ? 542 TYR A CG 1 ATOM 4203 C CD1 . TYR A 1 509 ? 25.163 43.306 21.435 1.00 22.46 ? 542 TYR A CD1 1 ATOM 4204 C CD2 . TYR A 1 509 ? 25.708 41.018 20.873 1.00 22.07 ? 542 TYR A CD2 1 ATOM 4205 C CE1 . TYR A 1 509 ? 23.967 43.189 20.689 1.00 24.78 ? 542 TYR A CE1 1 ATOM 4206 C CE2 . TYR A 1 509 ? 24.528 40.881 20.169 1.00 21.40 ? 542 TYR A CE2 1 ATOM 4207 C CZ . TYR A 1 509 ? 23.663 41.984 20.098 1.00 23.86 ? 542 TYR A CZ 1 ATOM 4208 O OH . TYR A 1 509 ? 22.477 41.835 19.377 1.00 25.18 ? 542 TYR A OH 1 ATOM 4209 N N . HIS A 1 510 ? 25.127 42.052 24.840 1.00 20.26 ? 543 HIS A N 1 ATOM 4210 C CA . HIS A 1 510 ? 23.994 41.222 25.276 1.00 19.79 ? 543 HIS A CA 1 ATOM 4211 C C . HIS A 1 510 ? 24.347 40.358 26.496 1.00 20.82 ? 543 HIS A C 1 ATOM 4212 O O . HIS A 1 510 ? 23.649 39.345 26.796 1.00 21.60 ? 543 HIS A O 1 ATOM 4213 C CB . HIS A 1 510 ? 23.380 40.394 24.131 1.00 20.58 ? 543 HIS A CB 1 ATOM 4214 C CG . HIS A 1 510 ? 22.375 41.149 23.302 1.00 18.27 ? 543 HIS A CG 1 ATOM 4215 N ND1 . HIS A 1 510 ? 21.458 40.486 22.499 1.00 18.25 ? 543 HIS A ND1 1 ATOM 4216 C CD2 . HIS A 1 510 ? 22.090 42.484 23.216 1.00 20.00 ? 543 HIS A CD2 1 ATOM 4217 C CE1 . HIS A 1 510 ? 20.677 41.416 21.904 1.00 18.96 ? 543 HIS A CE1 1 ATOM 4218 N NE2 . HIS A 1 510 ? 21.080 42.621 22.285 1.00 18.78 ? 543 HIS A NE2 1 ATOM 4219 N N . THR A 1 511 ? 25.357 40.797 27.245 1.00 20.81 ? 544 THR A N 1 ATOM 4220 C CA . THR A 1 511 ? 25.672 40.105 28.495 1.00 20.18 ? 544 THR A CA 1 ATOM 4221 C C . THR A 1 511 ? 25.404 40.993 29.702 1.00 20.48 ? 544 THR A C 1 ATOM 4222 O O . THR A 1 511 ? 25.020 42.206 29.573 1.00 21.92 ? 544 THR A O 1 ATOM 4223 C CB . THR A 1 511 ? 27.174 39.725 28.586 1.00 19.91 ? 544 THR A CB 1 ATOM 4224 O OG1 . THR A 1 511 ? 27.963 40.925 28.776 1.00 19.90 ? 544 THR A OG1 1 ATOM 4225 C CG2 . THR A 1 511 ? 27.624 38.966 27.314 1.00 21.21 ? 544 THR A CG2 1 ATOM 4226 N N . ILE A 1 512 ? 25.595 40.444 30.910 1.00 20.94 ? 545 ILE A N 1 ATOM 4227 C CA . ILE A 1 512 ? 25.408 41.188 32.147 1.00 19.80 ? 545 ILE A CA 1 ATOM 4228 C C . ILE A 1 512 ? 26.452 42.325 32.310 1.00 20.18 ? 545 ILE A C 1 ATOM 4229 O O . ILE A 1 512 ? 26.255 43.245 33.128 1.00 22.55 ? 545 ILE A O 1 ATOM 4230 C CB A ILE A 1 512 ? 25.453 40.343 33.500 0.65 21.14 ? 545 ILE A CB 1 ATOM 4231 C CB B ILE A 1 512 ? 25.531 40.134 33.226 0.35 20.61 ? 545 ILE A CB 1 ATOM 4232 C CG1 A ILE A 1 512 ? 26.777 39.560 33.590 0.65 22.80 ? 545 ILE A CG1 1 ATOM 4233 C CG1 B ILE A 1 512 ? 25.129 40.674 34.562 0.35 15.72 ? 545 ILE A CG1 1 ATOM 4234 C CG2 A ILE A 1 512 ? 24.269 39.395 33.600 0.65 22.58 ? 545 ILE A CG2 1 ATOM 4235 C CG2 B ILE A 1 512 ? 26.933 39.449 33.169 0.35 17.93 ? 545 ILE A CG2 1 ATOM 4236 C CD1 A ILE A 1 512 ? 27.057 38.962 34.998 0.65 25.22 ? 545 ILE A CD1 1 ATOM 4237 C CD1 B ILE A 1 512 ? 25.213 39.589 35.623 0.35 18.53 ? 545 ILE A CD1 1 ATOM 4238 N N . TYR A 1 513 ? 27.523 42.294 31.507 1.00 20.95 ? 546 TYR A N 1 ATOM 4239 C CA . TYR A 1 513 ? 28.653 43.232 31.674 1.00 21.41 ? 546 TYR A CA 1 ATOM 4240 C C . TYR A 1 513 ? 28.525 44.537 30.872 1.00 21.30 ? 546 TYR A C 1 ATOM 4241 O O . TYR A 1 513 ? 29.468 45.374 30.874 1.00 22.08 ? 546 TYR A O 1 ATOM 4242 C CB . TYR A 1 513 ? 29.998 42.530 31.419 1.00 21.87 ? 546 TYR A CB 1 ATOM 4243 C CG . TYR A 1 513 ? 30.207 41.394 32.412 1.00 21.38 ? 546 TYR A CG 1 ATOM 4244 C CD1 . TYR A 1 513 ? 30.320 41.651 33.791 1.00 25.07 ? 546 TYR A CD1 1 ATOM 4245 C CD2 . TYR A 1 513 ? 30.263 40.070 31.983 1.00 22.77 ? 546 TYR A CD2 1 ATOM 4246 C CE1 . TYR A 1 513 ? 30.495 40.629 34.682 1.00 27.32 ? 546 TYR A CE1 1 ATOM 4247 C CE2 . TYR A 1 513 ? 30.437 39.021 32.901 1.00 24.11 ? 546 TYR A CE2 1 ATOM 4248 C CZ . TYR A 1 513 ? 30.556 39.321 34.230 1.00 28.07 ? 546 TYR A CZ 1 ATOM 4249 O OH . TYR A 1 513 ? 30.719 38.331 35.187 1.00 30.13 ? 546 TYR A OH 1 ATOM 4250 N N . GLU A 1 514 ? 27.352 44.779 30.289 1.00 22.26 ? 547 GLU A N 1 ATOM 4251 C CA . GLU A 1 514 ? 27.072 46.096 29.667 1.00 21.32 ? 547 GLU A CA 1 ATOM 4252 C C . GLU A 1 514 ? 26.687 47.042 30.765 1.00 19.98 ? 547 GLU A C 1 ATOM 4253 O O . GLU A 1 514 ? 25.502 47.261 31.050 1.00 19.05 ? 547 GLU A O 1 ATOM 4254 C CB . GLU A 1 514 ? 25.917 46.004 28.645 1.00 21.71 ? 547 GLU A CB 1 ATOM 4255 C CG . GLU A 1 514 ? 26.289 45.307 27.395 1.00 22.66 ? 547 GLU A CG 1 ATOM 4256 C CD . GLU A 1 514 ? 25.422 45.799 26.228 1.00 20.43 ? 547 GLU A CD 1 ATOM 4257 O OE1 . GLU A 1 514 ? 25.091 45.008 25.339 1.00 20.41 ? 547 GLU A OE1 1 ATOM 4258 O OE2 . GLU A 1 514 ? 25.011 47.007 26.264 1.00 21.97 ? 547 GLU A OE2 1 ATOM 4259 N N . THR A 1 515 ? 27.699 47.620 31.439 1.00 18.97 ? 548 THR A N 1 ATOM 4260 C CA . THR A 1 515 ? 27.439 48.474 32.564 1.00 20.14 ? 548 THR A CA 1 ATOM 4261 C C . THR A 1 515 ? 27.892 49.900 32.288 1.00 19.36 ? 548 THR A C 1 ATOM 4262 O O . THR A 1 515 ? 28.647 50.165 31.384 1.00 19.93 ? 548 THR A O 1 ATOM 4263 C CB . THR A 1 515 ? 28.244 48.012 33.767 1.00 19.98 ? 548 THR A CB 1 ATOM 4264 O OG1 . THR A 1 515 ? 29.632 48.087 33.408 1.00 22.06 ? 548 THR A OG1 1 ATOM 4265 C CG2 . THR A 1 515 ? 27.837 46.563 34.183 1.00 21.48 ? 548 THR A CG2 1 ATOM 4266 N N . PHE A 1 516 ? 27.364 50.822 33.070 1.00 18.98 ? 549 PHE A N 1 ATOM 4267 C CA . PHE A 1 516 ? 27.800 52.191 32.987 1.00 19.38 ? 549 PHE A CA 1 ATOM 4268 C C . PHE A 1 516 ? 29.328 52.284 33.114 1.00 19.80 ? 549 PHE A C 1 ATOM 4269 O O . PHE A 1 516 ? 29.974 53.058 32.392 1.00 19.75 ? 549 PHE A O 1 ATOM 4270 C CB . PHE A 1 516 ? 27.134 53.009 34.098 1.00 18.55 ? 549 PHE A CB 1 ATOM 4271 C CG . PHE A 1 516 ? 27.620 54.435 34.168 1.00 17.91 ? 549 PHE A CG 1 ATOM 4272 C CD1 . PHE A 1 516 ? 28.600 54.778 35.077 1.00 17.80 ? 549 PHE A CD1 1 ATOM 4273 C CD2 . PHE A 1 516 ? 27.086 55.402 33.344 1.00 17.31 ? 549 PHE A CD2 1 ATOM 4274 C CE1 . PHE A 1 516 ? 29.079 56.083 35.126 1.00 21.06 ? 549 PHE A CE1 1 ATOM 4275 C CE2 . PHE A 1 516 ? 27.548 56.727 33.373 1.00 17.49 ? 549 PHE A CE2 1 ATOM 4276 C CZ . PHE A 1 516 ? 28.539 57.073 34.297 1.00 19.61 ? 549 PHE A CZ 1 ATOM 4277 N N . GLU A 1 517 ? 29.897 51.505 34.039 1.00 19.77 ? 550 GLU A N 1 ATOM 4278 C CA . GLU A 1 517 ? 31.335 51.553 34.271 1.00 20.10 ? 550 GLU A CA 1 ATOM 4279 C C . GLU A 1 517 ? 32.103 51.136 33.023 1.00 20.86 ? 550 GLU A C 1 ATOM 4280 O O . GLU A 1 517 ? 33.131 51.730 32.648 1.00 20.71 ? 550 GLU A O 1 ATOM 4281 C CB . GLU A 1 517 ? 31.692 50.656 35.479 1.00 20.63 ? 550 GLU A CB 1 ATOM 4282 C CG . GLU A 1 517 ? 31.187 51.151 36.831 1.00 22.74 ? 550 GLU A CG 1 ATOM 4283 C CD . GLU A 1 517 ? 29.697 50.972 37.116 1.00 22.48 ? 550 GLU A CD 1 ATOM 4284 O OE1 . GLU A 1 517 ? 28.982 50.269 36.381 1.00 24.68 ? 550 GLU A OE1 1 ATOM 4285 O OE2 . GLU A 1 517 ? 29.193 51.547 38.091 1.00 26.20 ? 550 GLU A OE2 1 ATOM 4286 N N . LEU A 1 518 ? 31.569 50.146 32.312 1.00 19.52 ? 551 LEU A N 1 ATOM 4287 C CA . LEU A 1 518 ? 32.198 49.733 31.045 1.00 20.24 ? 551 LEU A CA 1 ATOM 4288 C C . LEU A 1 518 ? 32.353 50.918 30.092 1.00 19.84 ? 551 LEU A C 1 ATOM 4289 O O . LEU A 1 518 ? 33.413 51.137 29.477 1.00 20.51 ? 551 LEU A O 1 ATOM 4290 C CB . LEU A 1 518 ? 31.369 48.634 30.339 1.00 20.32 ? 551 LEU A CB 1 ATOM 4291 C CG . LEU A 1 518 ? 31.876 48.100 29.009 1.00 21.29 ? 551 LEU A CG 1 ATOM 4292 C CD1 . LEU A 1 518 ? 32.747 46.805 29.169 1.00 22.38 ? 551 LEU A CD1 1 ATOM 4293 C CD2 . LEU A 1 518 ? 30.736 47.817 28.098 1.00 19.99 ? 551 LEU A CD2 1 ATOM 4294 N N . VAL A 1 519 ? 31.260 51.664 29.917 1.00 19.68 ? 552 VAL A N 1 ATOM 4295 C CA . VAL A 1 519 ? 31.231 52.717 28.918 1.00 19.22 ? 552 VAL A CA 1 ATOM 4296 C C . VAL A 1 519 ? 32.151 53.861 29.393 1.00 19.61 ? 552 VAL A C 1 ATOM 4297 O O . VAL A 1 519 ? 32.951 54.367 28.644 1.00 20.30 ? 552 VAL A O 1 ATOM 4298 C CB . VAL A 1 519 ? 29.805 53.274 28.752 1.00 19.00 ? 552 VAL A CB 1 ATOM 4299 C CG1 . VAL A 1 519 ? 29.806 54.524 27.846 1.00 19.49 ? 552 VAL A CG1 1 ATOM 4300 C CG2 . VAL A 1 519 ? 28.905 52.215 28.101 1.00 17.06 ? 552 VAL A CG2 1 ATOM 4301 N N . GLU A 1 520 ? 32.012 54.234 30.637 1.00 20.41 ? 553 GLU A N 1 ATOM 4302 C CA . GLU A 1 520 ? 32.788 55.356 31.118 1.00 21.06 ? 553 GLU A CA 1 ATOM 4303 C C . GLU A 1 520 ? 34.285 55.042 31.188 1.00 22.46 ? 553 GLU A C 1 ATOM 4304 O O . GLU A 1 520 ? 35.116 55.910 30.824 1.00 23.08 ? 553 GLU A O 1 ATOM 4305 C CB . GLU A 1 520 ? 32.250 55.783 32.454 1.00 22.30 ? 553 GLU A CB 1 ATOM 4306 C CG . GLU A 1 520 ? 32.915 57.012 32.925 1.00 25.94 ? 553 GLU A CG 1 ATOM 4307 C CD . GLU A 1 520 ? 33.083 56.861 34.329 1.00 36.18 ? 553 GLU A CD 1 ATOM 4308 O OE1 . GLU A 1 520 ? 34.099 56.198 34.694 1.00 40.97 ? 553 GLU A OE1 1 ATOM 4309 O OE2 . GLU A 1 520 ? 32.165 57.320 35.044 1.00 38.75 ? 553 GLU A OE2 1 ATOM 4310 N N . LYS A 1 521 ? 34.643 53.840 31.640 1.00 21.52 ? 554 LYS A N 1 ATOM 4311 C CA . LYS A 1 521 ? 36.073 53.530 31.779 1.00 21.82 ? 554 LYS A CA 1 ATOM 4312 C C . LYS A 1 521 ? 36.742 53.224 30.431 1.00 21.40 ? 554 LYS A C 1 ATOM 4313 O O . LYS A 1 521 ? 37.896 53.642 30.199 1.00 21.42 ? 554 LYS A O 1 ATOM 4314 C CB . LYS A 1 521 ? 36.310 52.311 32.683 1.00 22.84 ? 554 LYS A CB 1 ATOM 4315 C CG . LYS A 1 521 ? 35.721 52.268 34.112 1.00 29.05 ? 554 LYS A CG 1 ATOM 4316 C CD . LYS A 1 521 ? 35.461 53.606 34.785 1.00 37.01 ? 554 LYS A CD 1 ATOM 4317 C CE . LYS A 1 521 ? 36.696 54.199 35.502 1.00 39.42 ? 554 LYS A CE 1 ATOM 4318 N NZ . LYS A 1 521 ? 36.354 55.524 36.117 1.00 40.73 ? 554 LYS A NZ 1 ATOM 4319 N N . PHE A 1 522 ? 36.076 52.459 29.564 1.00 19.12 ? 555 PHE A N 1 ATOM 4320 C CA . PHE A 1 522 ? 36.785 51.841 28.465 1.00 20.36 ? 555 PHE A CA 1 ATOM 4321 C C . PHE A 1 522 ? 36.402 52.370 27.122 1.00 20.99 ? 555 PHE A C 1 ATOM 4322 O O . PHE A 1 522 ? 37.182 52.265 26.200 1.00 22.87 ? 555 PHE A O 1 ATOM 4323 C CB . PHE A 1 522 ? 36.569 50.308 28.464 1.00 20.69 ? 555 PHE A CB 1 ATOM 4324 C CG . PHE A 1 522 ? 36.968 49.662 29.743 1.00 21.96 ? 555 PHE A CG 1 ATOM 4325 C CD1 . PHE A 1 522 ? 38.267 49.845 30.231 1.00 23.89 ? 555 PHE A CD1 1 ATOM 4326 C CD2 . PHE A 1 522 ? 36.060 48.917 30.495 1.00 23.56 ? 555 PHE A CD2 1 ATOM 4327 C CE1 . PHE A 1 522 ? 38.673 49.281 31.435 1.00 26.47 ? 555 PHE A CE1 1 ATOM 4328 C CE2 . PHE A 1 522 ? 36.436 48.339 31.706 1.00 24.35 ? 555 PHE A CE2 1 ATOM 4329 C CZ . PHE A 1 522 ? 37.755 48.522 32.188 1.00 24.46 ? 555 PHE A CZ 1 ATOM 4330 N N . TYR A 1 523 ? 35.175 52.901 26.975 1.00 20.90 ? 556 TYR A N 1 ATOM 4331 C CA . TYR A 1 523 ? 34.690 53.376 25.662 1.00 20.21 ? 556 TYR A CA 1 ATOM 4332 C C . TYR A 1 523 ? 34.842 54.888 25.412 1.00 21.92 ? 556 TYR A C 1 ATOM 4333 O O . TYR A 1 523 ? 35.346 55.310 24.343 1.00 22.94 ? 556 TYR A O 1 ATOM 4334 C CB . TYR A 1 523 ? 33.213 52.924 25.420 1.00 21.09 ? 556 TYR A CB 1 ATOM 4335 C CG . TYR A 1 523 ? 33.138 51.490 25.014 1.00 20.62 ? 556 TYR A CG 1 ATOM 4336 C CD1 . TYR A 1 523 ? 33.358 50.469 25.940 1.00 21.60 ? 556 TYR A CD1 1 ATOM 4337 C CD2 . TYR A 1 523 ? 32.946 51.173 23.673 1.00 19.35 ? 556 TYR A CD2 1 ATOM 4338 C CE1 . TYR A 1 523 ? 33.350 49.127 25.536 1.00 22.75 ? 556 TYR A CE1 1 ATOM 4339 C CE2 . TYR A 1 523 ? 32.945 49.827 23.254 1.00 20.28 ? 556 TYR A CE2 1 ATOM 4340 C CZ . TYR A 1 523 ? 33.134 48.836 24.182 1.00 20.61 ? 556 TYR A CZ 1 ATOM 4341 O OH . TYR A 1 523 ? 33.195 47.537 23.752 1.00 22.16 ? 556 TYR A OH 1 ATOM 4342 N N . ASP A 1 524 ? 34.402 55.693 26.384 1.00 19.99 ? 557 ASP A N 1 ATOM 4343 C CA . ASP A 1 524 ? 34.245 57.136 26.093 1.00 19.74 ? 557 ASP A CA 1 ATOM 4344 C C . ASP A 1 524 ? 34.220 57.903 27.407 1.00 20.40 ? 557 ASP A C 1 ATOM 4345 O O . ASP A 1 524 ? 33.186 58.451 27.792 1.00 20.49 ? 557 ASP A O 1 ATOM 4346 C CB . ASP A 1 524 ? 32.924 57.314 25.307 1.00 19.08 ? 557 ASP A CB 1 ATOM 4347 C CG . ASP A 1 524 ? 32.718 58.706 24.750 1.00 19.89 ? 557 ASP A CG 1 ATOM 4348 O OD1 . ASP A 1 524 ? 33.699 59.453 24.496 1.00 19.74 ? 557 ASP A OD1 1 ATOM 4349 O OD2 . ASP A 1 524 ? 31.512 59.022 24.473 1.00 17.97 ? 557 ASP A OD2 1 ATOM 4350 N N . PRO A 1 525 ? 35.354 57.953 28.126 1.00 20.67 ? 558 PRO A N 1 ATOM 4351 C CA . PRO A 1 525 ? 35.361 58.571 29.436 1.00 19.44 ? 558 PRO A CA 1 ATOM 4352 C C . PRO A 1 525 ? 34.884 60.045 29.462 1.00 18.71 ? 558 PRO A C 1 ATOM 4353 O O . PRO A 1 525 ? 34.286 60.493 30.476 1.00 20.95 ? 558 PRO A O 1 ATOM 4354 C CB . PRO A 1 525 ? 36.846 58.533 29.838 1.00 19.95 ? 558 PRO A CB 1 ATOM 4355 C CG . PRO A 1 525 ? 37.548 57.659 28.894 1.00 22.41 ? 558 PRO A CG 1 ATOM 4356 C CD . PRO A 1 525 ? 36.626 57.305 27.775 1.00 19.74 ? 558 PRO A CD 1 ATOM 4357 N N . THR A 1 526 ? 35.164 60.800 28.388 1.00 18.80 ? 559 THR A N 1 ATOM 4358 C CA . THR A 1 526 ? 34.804 62.220 28.339 1.00 19.57 ? 559 THR A CA 1 ATOM 4359 C C . THR A 1 526 ? 33.379 62.382 27.856 1.00 18.57 ? 559 THR A C 1 ATOM 4360 O O . THR A 1 526 ? 32.839 63.489 27.903 1.00 19.43 ? 559 THR A O 1 ATOM 4361 C CB . THR A 1 526 ? 35.666 63.030 27.337 1.00 19.23 ? 559 THR A CB 1 ATOM 4362 O OG1 . THR A 1 526 ? 35.398 62.568 26.007 1.00 19.42 ? 559 THR A OG1 1 ATOM 4363 C CG2 . THR A 1 526 ? 37.167 62.862 27.655 1.00 19.56 ? 559 THR A CG2 1 ATOM 4364 N N . PHE A 1 527 ? 32.765 61.290 27.368 1.00 18.12 ? 560 PHE A N 1 ATOM 4365 C CA . PHE A 1 527 ? 31.414 61.355 26.733 1.00 19.00 ? 560 PHE A CA 1 ATOM 4366 C C . PHE A 1 527 ? 31.342 62.207 25.472 1.00 18.22 ? 560 PHE A C 1 ATOM 4367 O O . PHE A 1 527 ? 30.250 62.490 24.954 1.00 18.82 ? 560 PHE A O 1 ATOM 4368 C CB . PHE A 1 527 ? 30.301 61.678 27.749 1.00 17.63 ? 560 PHE A CB 1 ATOM 4369 C CG . PHE A 1 527 ? 29.914 60.479 28.556 1.00 18.88 ? 560 PHE A CG 1 ATOM 4370 C CD1 . PHE A 1 527 ? 28.718 59.815 28.312 1.00 20.30 ? 560 PHE A CD1 1 ATOM 4371 C CD2 . PHE A 1 527 ? 30.814 59.945 29.503 1.00 22.25 ? 560 PHE A CD2 1 ATOM 4372 C CE1 . PHE A 1 527 ? 28.376 58.686 29.024 1.00 21.08 ? 560 PHE A CE1 1 ATOM 4373 C CE2 . PHE A 1 527 ? 30.494 58.756 30.202 1.00 19.75 ? 560 PHE A CE2 1 ATOM 4374 C CZ . PHE A 1 527 ? 29.268 58.123 29.941 1.00 20.25 ? 560 PHE A CZ 1 ATOM 4375 N N . LYS A 1 528 ? 32.503 62.624 24.979 1.00 19.53 ? 561 LYS A N 1 ATOM 4376 C CA . LYS A 1 528 ? 32.513 63.449 23.757 1.00 18.27 ? 561 LYS A CA 1 ATOM 4377 C C . LYS A 1 528 ? 32.100 62.684 22.511 1.00 18.62 ? 561 LYS A C 1 ATOM 4378 O O . LYS A 1 528 ? 31.495 63.245 21.626 1.00 17.90 ? 561 LYS A O 1 ATOM 4379 C CB . LYS A 1 528 ? 33.895 64.045 23.547 1.00 19.91 ? 561 LYS A CB 1 ATOM 4380 C CG . LYS A 1 528 ? 34.116 65.152 24.545 1.00 21.43 ? 561 LYS A CG 1 ATOM 4381 C CD . LYS A 1 528 ? 35.271 66.053 24.197 1.00 27.51 ? 561 LYS A CD 1 ATOM 4382 C CE . LYS A 1 528 ? 36.550 65.356 24.046 1.00 30.28 ? 561 LYS A CE 1 ATOM 4383 N NZ . LYS A 1 528 ? 37.682 66.389 24.189 1.00 31.87 ? 561 LYS A NZ 1 ATOM 4384 N N . LYS A 1 529 ? 32.390 61.391 22.463 1.00 17.88 ? 562 LYS A N 1 ATOM 4385 C CA . LYS A 1 529 ? 31.984 60.639 21.272 1.00 19.40 ? 562 LYS A CA 1 ATOM 4386 C C . LYS A 1 529 ? 30.470 60.442 21.226 1.00 18.78 ? 562 LYS A C 1 ATOM 4387 O O . LYS A 1 529 ? 29.848 60.668 20.166 1.00 18.62 ? 562 LYS A O 1 ATOM 4388 C CB . LYS A 1 529 ? 32.737 59.313 21.186 1.00 19.44 ? 562 LYS A CB 1 ATOM 4389 C CG . LYS A 1 529 ? 34.278 59.596 20.924 1.00 22.70 ? 562 LYS A CG 1 ATOM 4390 C CD . LYS A 1 529 ? 35.178 58.367 20.963 1.00 23.82 ? 562 LYS A CD 1 ATOM 4391 C CE . LYS A 1 529 ? 36.637 58.768 20.666 1.00 24.33 ? 562 LYS A CE 1 ATOM 4392 N NZ . LYS A 1 529 ? 37.280 59.379 21.852 1.00 27.75 ? 562 LYS A NZ 1 ATOM 4393 N N . GLN A 1 530 ? 29.901 60.106 22.388 1.00 18.18 ? 563 GLN A N 1 ATOM 4394 C CA . GLN A 1 530 ? 28.422 59.998 22.484 1.00 16.95 ? 563 GLN A CA 1 ATOM 4395 C C . GLN A 1 530 ? 27.792 61.372 22.205 1.00 17.50 ? 563 GLN A C 1 ATOM 4396 O O . GLN A 1 530 ? 26.761 61.468 21.525 1.00 17.42 ? 563 GLN A O 1 ATOM 4397 C CB . GLN A 1 530 ? 28.051 59.481 23.887 1.00 18.59 ? 563 GLN A CB 1 ATOM 4398 C CG . GLN A 1 530 ? 28.477 58.020 24.065 1.00 19.77 ? 563 GLN A CG 1 ATOM 4399 C CD . GLN A 1 530 ? 28.431 57.598 25.480 1.00 19.59 ? 563 GLN A CD 1 ATOM 4400 O OE1 . GLN A 1 530 ? 27.379 57.290 26.041 1.00 19.54 ? 563 GLN A OE1 1 ATOM 4401 N NE2 . GLN A 1 530 ? 29.606 57.656 26.122 1.00 17.93 ? 563 GLN A NE2 1 ATOM 4402 N N . LEU A 1 531 ? 28.437 62.449 22.664 1.00 17.41 ? 564 LEU A N 1 ATOM 4403 C CA . LEU A 1 531 ? 27.898 63.798 22.347 1.00 17.29 ? 564 LEU A CA 1 ATOM 4404 C C . LEU A 1 531 ? 27.847 64.026 20.835 1.00 16.96 ? 564 LEU A C 1 ATOM 4405 O O . LEU A 1 531 ? 26.838 64.548 20.289 1.00 17.77 ? 564 LEU A O 1 ATOM 4406 C CB . LEU A 1 531 ? 28.759 64.902 22.981 1.00 16.33 ? 564 LEU A CB 1 ATOM 4407 C CG . LEU A 1 531 ? 28.354 66.315 22.587 1.00 17.79 ? 564 LEU A CG 1 ATOM 4408 C CD1 . LEU A 1 531 ? 26.916 66.644 23.078 1.00 20.25 ? 564 LEU A CD1 1 ATOM 4409 C CD2 . LEU A 1 531 ? 29.407 67.383 23.113 1.00 18.92 ? 564 LEU A CD2 1 ATOM 4410 N N . SER A 1 532 ? 28.916 63.631 20.116 1.00 17.17 ? 565 SER A N 1 ATOM 4411 C CA . SER A 1 532 ? 28.911 63.874 18.682 1.00 17.82 ? 565 SER A CA 1 ATOM 4412 C C . SER A 1 532 ? 27.760 63.130 17.971 1.00 18.67 ? 565 SER A C 1 ATOM 4413 O O . SER A 1 532 ? 27.179 63.684 16.993 1.00 17.60 ? 565 SER A O 1 ATOM 4414 C CB . SER A 1 532 ? 30.247 63.548 18.000 1.00 19.73 ? 565 SER A CB 1 ATOM 4415 O OG . SER A 1 532 ? 30.515 62.163 17.924 1.00 19.97 ? 565 SER A OG 1 ATOM 4416 N N . VAL A 1 533 ? 27.431 61.939 18.484 1.00 17.38 ? 566 VAL A N 1 ATOM 4417 C CA . VAL A 1 533 ? 26.314 61.148 17.900 1.00 18.08 ? 566 VAL A CA 1 ATOM 4418 C C . VAL A 1 533 ? 24.970 61.823 18.212 1.00 17.29 ? 566 VAL A C 1 ATOM 4419 O O . VAL A 1 533 ? 24.103 61.930 17.355 1.00 18.94 ? 566 VAL A O 1 ATOM 4420 C CB . VAL A 1 533 ? 26.409 59.720 18.399 1.00 17.57 ? 566 VAL A CB 1 ATOM 4421 C CG1 . VAL A 1 533 ? 25.155 58.938 17.998 1.00 17.47 ? 566 VAL A CG1 1 ATOM 4422 C CG2 . VAL A 1 533 ? 27.632 59.051 17.828 1.00 18.04 ? 566 VAL A CG2 1 ATOM 4423 N N . ALA A 1 534 ? 24.827 62.366 19.430 1.00 17.83 ? 567 ALA A N 1 ATOM 4424 C CA . ALA A 1 534 ? 23.584 63.076 19.752 1.00 17.59 ? 567 ALA A CA 1 ATOM 4425 C C . ALA A 1 534 ? 23.439 64.317 18.902 1.00 16.87 ? 567 ALA A C 1 ATOM 4426 O O . ALA A 1 534 ? 22.314 64.622 18.422 1.00 17.71 ? 567 ALA A O 1 ATOM 4427 C CB . ALA A 1 534 ? 23.605 63.499 21.226 1.00 16.66 ? 567 ALA A CB 1 ATOM 4428 N N . GLN A 1 535 ? 24.571 65.031 18.689 1.00 16.78 ? 568 GLN A N 1 ATOM 4429 C CA . GLN A 1 535 ? 24.496 66.217 17.830 1.00 16.62 ? 568 GLN A CA 1 ATOM 4430 C C . GLN A 1 535 ? 24.099 65.852 16.398 1.00 16.31 ? 568 GLN A C 1 ATOM 4431 O O . GLN A 1 535 ? 23.259 66.536 15.788 1.00 17.73 ? 568 GLN A O 1 ATOM 4432 C CB . GLN A 1 535 ? 25.807 67.000 17.840 1.00 16.46 ? 568 GLN A CB 1 ATOM 4433 C CG . GLN A 1 535 ? 26.078 67.581 19.186 1.00 16.79 ? 568 GLN A CG 1 ATOM 4434 C CD . GLN A 1 535 ? 27.495 68.118 19.355 1.00 20.80 ? 568 GLN A CD 1 ATOM 4435 O OE1 . GLN A 1 535 ? 28.462 67.554 18.814 1.00 18.83 ? 568 GLN A OE1 1 ATOM 4436 N NE2 . GLN A 1 535 ? 27.633 69.162 20.189 1.00 19.77 ? 568 GLN A NE2 1 ATOM 4437 N N . LEU A 1 536 ? 24.685 64.801 15.831 1.00 17.33 ? 569 LEU A N 1 ATOM 4438 C CA . LEU A 1 536 ? 24.283 64.449 14.496 1.00 17.19 ? 569 LEU A CA 1 ATOM 4439 C C . LEU A 1 536 ? 22.820 63.928 14.381 1.00 16.53 ? 569 LEU A C 1 ATOM 4440 O O . LEU A 1 536 ? 22.090 64.301 13.452 1.00 17.92 ? 569 LEU A O 1 ATOM 4441 C CB . LEU A 1 536 ? 25.235 63.386 13.935 1.00 18.57 ? 569 LEU A CB 1 ATOM 4442 C CG . LEU A 1 536 ? 24.936 62.850 12.540 1.00 19.61 ? 569 LEU A CG 1 ATOM 4443 C CD1 . LEU A 1 536 ? 24.885 64.000 11.504 1.00 21.64 ? 569 LEU A CD1 1 ATOM 4444 C CD2 . LEU A 1 536 ? 25.984 61.745 12.143 1.00 19.96 ? 569 LEU A CD2 1 ATOM 4445 N N . ARG A 1 537 ? 22.391 63.062 15.296 1.00 16.92 ? 570 ARG A N 1 ATOM 4446 C CA . ARG A 1 537 ? 21.004 62.543 15.209 1.00 15.82 ? 570 ARG A CA 1 ATOM 4447 C C . ARG A 1 537 ? 20.054 63.730 15.379 1.00 16.92 ? 570 ARG A C 1 ATOM 4448 O O . ARG A 1 537 ? 19.062 63.842 14.678 1.00 16.41 ? 570 ARG A O 1 ATOM 4449 C CB . ARG A 1 537 ? 20.763 61.559 16.378 1.00 16.43 ? 570 ARG A CB 1 ATOM 4450 C CG . ARG A 1 537 ? 21.523 60.227 16.169 1.00 16.61 ? 570 ARG A CG 1 ATOM 4451 C CD . ARG A 1 537 ? 21.213 59.281 17.334 1.00 17.61 ? 570 ARG A CD 1 ATOM 4452 N NE . ARG A 1 537 ? 22.029 58.060 17.212 1.00 16.03 ? 570 ARG A NE 1 ATOM 4453 C CZ . ARG A 1 537 ? 22.111 57.092 18.135 1.00 17.13 ? 570 ARG A CZ 1 ATOM 4454 N NH1 . ARG A 1 537 ? 21.453 57.155 19.317 1.00 18.12 ? 570 ARG A NH1 1 ATOM 4455 N NH2 . ARG A 1 537 ? 22.853 55.994 17.855 1.00 17.99 ? 570 ARG A NH2 1 ATOM 4456 N N . GLY A 1 538 ? 20.356 64.633 16.322 1.00 16.21 ? 571 GLY A N 1 ATOM 4457 C CA . GLY A 1 538 ? 19.479 65.833 16.512 1.00 17.34 ? 571 GLY A CA 1 ATOM 4458 C C . GLY A 1 538 ? 19.473 66.761 15.295 1.00 16.23 ? 571 GLY A C 1 ATOM 4459 O O . GLY A 1 538 ? 18.405 67.265 14.913 1.00 17.74 ? 571 GLY A O 1 ATOM 4460 N N . ALA A 1 539 ? 20.664 67.005 14.724 1.00 16.56 ? 572 ALA A N 1 ATOM 4461 C CA . ALA A 1 539 ? 20.745 67.923 13.575 1.00 16.48 ? 572 ALA A CA 1 ATOM 4462 C C . ALA A 1 539 ? 20.031 67.333 12.364 1.00 18.24 ? 572 ALA A C 1 ATOM 4463 O O . ALA A 1 539 ? 19.379 68.088 11.635 1.00 17.87 ? 572 ALA A O 1 ATOM 4464 C CB . ALA A 1 539 ? 22.223 68.268 13.232 1.00 17.77 ? 572 ALA A CB 1 ATOM 4465 N N . LEU A 1 540 ? 20.085 66.005 12.207 1.00 17.14 ? 573 LEU A N 1 ATOM 4466 C CA . LEU A 1 540 ? 19.333 65.344 11.107 1.00 17.69 ? 573 LEU A CA 1 ATOM 4467 C C . LEU A 1 540 ? 17.834 65.618 11.290 1.00 18.51 ? 573 LEU A C 1 ATOM 4468 O O . LEU A 1 540 ? 17.165 66.065 10.373 1.00 18.60 ? 573 LEU A O 1 ATOM 4469 C CB . LEU A 1 540 ? 19.549 63.838 11.098 1.00 17.87 ? 573 LEU A CB 1 ATOM 4470 C CG . LEU A 1 540 ? 20.913 63.418 10.499 1.00 19.34 ? 573 LEU A CG 1 ATOM 4471 C CD1 . LEU A 1 540 ? 21.290 62.020 10.883 1.00 18.21 ? 573 LEU A CD1 1 ATOM 4472 C CD2 . LEU A 1 540 ? 20.823 63.545 8.984 1.00 21.68 ? 573 LEU A CD2 1 ATOM 4473 N N . VAL A 1 541 ? 17.301 65.354 12.494 1.00 17.10 ? 574 VAL A N 1 ATOM 4474 C CA . VAL A 1 541 ? 15.889 65.620 12.756 1.00 17.52 ? 574 VAL A CA 1 ATOM 4475 C C . VAL A 1 541 ? 15.576 67.087 12.469 1.00 17.87 ? 574 VAL A C 1 ATOM 4476 O O . VAL A 1 541 ? 14.583 67.425 11.781 1.00 17.20 ? 574 VAL A O 1 ATOM 4477 C CB . VAL A 1 541 ? 15.547 65.197 14.187 1.00 18.69 ? 574 VAL A CB 1 ATOM 4478 C CG1 . VAL A 1 541 ? 14.111 65.636 14.559 1.00 17.89 ? 574 VAL A CG1 1 ATOM 4479 C CG2 . VAL A 1 541 ? 15.742 63.693 14.365 1.00 18.45 ? 574 VAL A CG2 1 ATOM 4480 N N . TYR A 1 542 ? 16.436 67.999 12.976 1.00 16.59 ? 575 TYR A N 1 ATOM 4481 C CA . TYR A 1 542 ? 16.132 69.434 12.826 1.00 17.44 ? 575 TYR A CA 1 ATOM 4482 C C . TYR A 1 542 ? 16.047 69.788 11.337 1.00 17.78 ? 575 TYR A C 1 ATOM 4483 O O . TYR A 1 542 ? 15.108 70.469 10.911 1.00 18.41 ? 575 TYR A O 1 ATOM 4484 C CB . TYR A 1 542 ? 17.247 70.298 13.522 1.00 18.62 ? 575 TYR A CB 1 ATOM 4485 C CG . TYR A 1 542 ? 17.068 71.772 13.179 1.00 18.98 ? 575 TYR A CG 1 ATOM 4486 C CD1 . TYR A 1 542 ? 16.068 72.533 13.781 1.00 20.08 ? 575 TYR A CD1 1 ATOM 4487 C CD2 . TYR A 1 542 ? 17.763 72.309 12.076 1.00 20.01 ? 575 TYR A CD2 1 ATOM 4488 C CE1 . TYR A 1 542 ? 15.842 73.848 13.380 1.00 21.20 ? 575 TYR A CE1 1 ATOM 4489 C CE2 . TYR A 1 542 ? 17.548 73.624 11.677 1.00 21.87 ? 575 TYR A CE2 1 ATOM 4490 C CZ . TYR A 1 542 ? 16.578 74.363 12.321 1.00 22.23 ? 575 TYR A CZ 1 ATOM 4491 O OH . TYR A 1 542 ? 16.322 75.653 11.885 1.00 23.67 ? 575 TYR A OH 1 ATOM 4492 N N . GLU A 1 543 ? 17.034 69.388 10.544 1.00 18.99 ? 576 GLU A N 1 ATOM 4493 C CA . GLU A 1 543 ? 17.016 69.847 9.152 1.00 19.55 ? 576 GLU A CA 1 ATOM 4494 C C . GLU A 1 543 ? 15.845 69.223 8.372 1.00 19.32 ? 576 GLU A C 1 ATOM 4495 O O . GLU A 1 543 ? 15.231 69.892 7.526 1.00 19.90 ? 576 GLU A O 1 ATOM 4496 C CB . GLU A 1 543 ? 18.321 69.450 8.432 1.00 21.13 ? 576 GLU A CB 1 ATOM 4497 C CG . GLU A 1 543 ? 19.547 70.294 8.859 1.00 25.36 ? 576 GLU A CG 1 ATOM 4498 C CD . GLU A 1 543 ? 19.356 71.811 8.593 1.00 25.86 ? 576 GLU A CD 1 ATOM 4499 O OE1 . GLU A 1 543 ? 19.840 72.633 9.391 1.00 29.20 ? 576 GLU A OE1 1 ATOM 4500 O OE2 . GLU A 1 543 ? 18.774 72.197 7.563 1.00 27.82 ? 576 GLU A OE2 1 ATOM 4501 N N . LEU A 1 544 ? 15.481 67.988 8.684 1.00 18.03 ? 577 LEU A N 1 ATOM 4502 C CA . LEU A 1 544 ? 14.379 67.346 7.970 1.00 18.54 ? 577 LEU A CA 1 ATOM 4503 C C . LEU A 1 544 ? 13.056 68.010 8.383 1.00 19.16 ? 577 LEU A C 1 ATOM 4504 O O . LEU A 1 544 ? 12.112 68.072 7.575 1.00 19.33 ? 577 LEU A O 1 ATOM 4505 C CB . LEU A 1 544 ? 14.346 65.844 8.309 1.00 18.28 ? 577 LEU A CB 1 ATOM 4506 C CG . LEU A 1 544 ? 15.548 65.147 7.642 1.00 18.30 ? 577 LEU A CG 1 ATOM 4507 C CD1 . LEU A 1 544 ? 15.837 63.820 8.334 1.00 20.25 ? 577 LEU A CD1 1 ATOM 4508 C CD2 . LEU A 1 544 ? 15.355 64.898 6.139 1.00 18.37 ? 577 LEU A CD2 1 ATOM 4509 N N . VAL A 1 545 ? 12.937 68.445 9.645 1.00 18.34 ? 578 VAL A N 1 ATOM 4510 C CA . VAL A 1 545 ? 11.658 68.967 10.103 1.00 19.45 ? 578 VAL A CA 1 ATOM 4511 C C . VAL A 1 545 ? 11.506 70.430 9.837 1.00 20.56 ? 578 VAL A C 1 ATOM 4512 O O . VAL A 1 545 ? 10.369 70.924 9.828 1.00 22.26 ? 578 VAL A O 1 ATOM 4513 C CB . VAL A 1 545 ? 11.486 68.602 11.610 1.00 20.14 ? 578 VAL A CB 1 ATOM 4514 C CG1 . VAL A 1 545 ? 12.151 69.638 12.548 1.00 19.45 ? 578 VAL A CG1 1 ATOM 4515 C CG2 . VAL A 1 545 ? 10.016 68.375 12.018 1.00 23.32 ? 578 VAL A CG2 1 ATOM 4516 N N . ASP A 1 546 ? 12.613 71.164 9.642 1.00 19.28 ? 579 ASP A N 1 ATOM 4517 C CA . ASP A 1 546 ? 12.522 72.626 9.591 1.00 21.32 ? 579 ASP A CA 1 ATOM 4518 C C . ASP A 1 546 ? 12.797 73.241 8.226 1.00 21.04 ? 579 ASP A C 1 ATOM 4519 O O . ASP A 1 546 ? 12.428 74.396 7.978 1.00 23.82 ? 579 ASP A O 1 ATOM 4520 C CB . ASP A 1 546 ? 13.433 73.278 10.639 1.00 21.66 ? 579 ASP A CB 1 ATOM 4521 C CG . ASP A 1 546 ? 12.809 74.494 11.263 1.00 24.10 ? 579 ASP A CG 1 ATOM 4522 O OD1 . ASP A 1 546 ? 13.543 75.420 11.771 1.00 26.04 ? 579 ASP A OD1 1 ATOM 4523 O OD2 . ASP A 1 546 ? 11.581 74.596 11.370 1.00 21.54 ? 579 ASP A OD2 1 ATOM 4524 N N . SER A 1 547 ? 13.486 72.509 7.376 1.00 19.98 ? 580 SER A N 1 ATOM 4525 C CA . SER A 1 547 ? 13.829 73.074 6.050 1.00 20.48 ? 580 SER A CA 1 ATOM 4526 C C . SER A 1 547 ? 12.590 73.244 5.163 1.00 20.47 ? 580 SER A C 1 ATOM 4527 O O . SER A 1 547 ? 11.750 72.327 5.045 1.00 20.86 ? 580 SER A O 1 ATOM 4528 C CB . SER A 1 547 ? 14.812 72.155 5.313 1.00 19.63 ? 580 SER A CB 1 ATOM 4529 O OG A SER A 1 547 ? 16.002 72.056 6.039 0.65 21.48 ? 580 SER A OG 1 ATOM 4530 O OG B SER A 1 547 ? 15.325 72.751 4.122 0.35 20.06 ? 580 SER A OG 1 ATOM 4531 N N . LYS A 1 548 ? 12.472 74.383 4.501 1.00 19.17 ? 581 LYS A N 1 ATOM 4532 C CA . LYS A 1 548 ? 11.319 74.588 3.638 1.00 18.34 ? 581 LYS A CA 1 ATOM 4533 C C . LYS A 1 548 ? 11.273 73.487 2.573 1.00 17.75 ? 581 LYS A C 1 ATOM 4534 O O . LYS A 1 548 ? 10.216 72.889 2.359 1.00 19.64 ? 581 LYS A O 1 ATOM 4535 C CB . LYS A 1 548 ? 11.439 75.958 2.917 1.00 19.06 ? 581 LYS A CB 1 ATOM 4536 C CG . LYS A 1 548 ? 10.244 76.190 1.934 1.00 20.29 ? 581 LYS A CG 1 ATOM 4537 C CD . LYS A 1 548 ? 10.194 77.610 1.434 1.00 21.16 ? 581 LYS A CD 1 ATOM 4538 C CE . LYS A 1 548 ? 9.508 78.513 2.411 1.00 21.62 ? 581 LYS A CE 1 ATOM 4539 N NZ . LYS A 1 548 ? 9.568 79.969 1.897 1.00 23.53 ? 581 LYS A NZ 1 ATOM 4540 N N . ILE A 1 549 ? 12.402 73.238 1.896 1.00 17.78 ? 582 ILE A N 1 ATOM 4541 C CA . ILE A 1 549 ? 12.509 72.152 0.914 1.00 17.69 ? 582 ILE A CA 1 ATOM 4542 C C . ILE A 1 549 ? 13.155 70.942 1.609 1.00 18.44 ? 582 ILE A C 1 ATOM 4543 O O . ILE A 1 549 ? 14.230 71.045 2.227 1.00 18.25 ? 582 ILE A O 1 ATOM 4544 C CB . ILE A 1 549 ? 13.367 72.552 -0.305 1.00 19.04 ? 582 ILE A CB 1 ATOM 4545 C CG1 . ILE A 1 549 ? 12.669 73.743 -1.018 1.00 21.53 ? 582 ILE A CG1 1 ATOM 4546 C CG2 . ILE A 1 549 ? 13.558 71.319 -1.265 1.00 20.74 ? 582 ILE A CG2 1 ATOM 4547 C CD1 . ILE A 1 549 ? 11.361 73.444 -1.591 1.00 24.13 ? 582 ILE A CD1 1 ATOM 4548 N N . ILE A 1 550 ? 12.467 69.794 1.575 1.00 18.17 ? 583 ILE A N 1 ATOM 4549 C CA . ILE A 1 550 ? 13.026 68.580 2.240 1.00 19.11 ? 583 ILE A CA 1 ATOM 4550 C C . ILE A 1 550 ? 14.430 68.277 1.698 1.00 20.33 ? 583 ILE A C 1 ATOM 4551 O O . ILE A 1 550 ? 14.608 68.178 0.482 1.00 19.12 ? 583 ILE A O 1 ATOM 4552 C CB . ILE A 1 550 ? 12.101 67.391 2.002 1.00 18.53 ? 583 ILE A CB 1 ATOM 4553 C CG1 . ILE A 1 550 ? 10.761 67.612 2.705 1.00 18.24 ? 583 ILE A CG1 1 ATOM 4554 C CG2 . ILE A 1 550 ? 12.777 66.124 2.491 1.00 20.10 ? 583 ILE A CG2 1 ATOM 4555 C CD1 . ILE A 1 550 ? 9.652 66.729 2.169 1.00 19.87 ? 583 ILE A CD1 1 ATOM 4556 N N . PRO A 1 551 ? 15.419 68.066 2.578 1.00 20.61 ? 584 PRO A N 1 ATOM 4557 C CA . PRO A 1 551 ? 16.821 67.937 2.113 1.00 20.30 ? 584 PRO A CA 1 ATOM 4558 C C . PRO A 1 551 ? 17.196 66.527 1.717 1.00 20.47 ? 584 PRO A C 1 ATOM 4559 O O . PRO A 1 551 ? 18.049 65.854 2.383 1.00 22.23 ? 584 PRO A O 1 ATOM 4560 C CB . PRO A 1 551 ? 17.663 68.493 3.334 1.00 20.71 ? 584 PRO A CB 1 ATOM 4561 C CG . PRO A 1 551 ? 16.822 68.162 4.515 1.00 21.46 ? 584 PRO A CG 1 ATOM 4562 C CD . PRO A 1 551 ? 15.375 68.396 4.026 1.00 20.73 ? 584 PRO A CD 1 ATOM 4563 N N . PHE A 1 552 ? 16.533 66.063 0.674 1.00 17.99 ? 585 PHE A N 1 ATOM 4564 C CA . PHE A 1 552 ? 16.914 64.797 0.027 1.00 18.28 ? 585 PHE A CA 1 ATOM 4565 C C . PHE A 1 552 ? 17.543 65.078 -1.325 1.00 18.92 ? 585 PHE A C 1 ATOM 4566 O O . PHE A 1 552 ? 17.190 66.077 -1.988 1.00 21.15 ? 585 PHE A O 1 ATOM 4567 C CB . PHE A 1 552 ? 15.686 63.928 -0.299 1.00 18.55 ? 585 PHE A CB 1 ATOM 4568 C CG . PHE A 1 552 ? 14.909 63.373 0.913 1.00 17.54 ? 585 PHE A CG 1 ATOM 4569 C CD1 . PHE A 1 552 ? 15.519 63.187 2.185 1.00 17.98 ? 585 PHE A CD1 1 ATOM 4570 C CD2 . PHE A 1 552 ? 13.608 62.973 0.738 1.00 18.83 ? 585 PHE A CD2 1 ATOM 4571 C CE1 . PHE A 1 552 ? 14.801 62.671 3.229 1.00 16.83 ? 585 PHE A CE1 1 ATOM 4572 C CE2 . PHE A 1 552 ? 12.911 62.419 1.794 1.00 17.94 ? 585 PHE A CE2 1 ATOM 4573 C CZ . PHE A 1 552 ? 13.494 62.278 3.062 1.00 18.32 ? 585 PHE A CZ 1 ATOM 4574 N N . ASN A 1 553 ? 18.400 64.161 -1.765 1.00 18.24 ? 586 ASN A N 1 ATOM 4575 C CA . ASN A 1 553 ? 18.933 64.267 -3.131 1.00 18.97 ? 586 ASN A CA 1 ATOM 4576 C C . ASN A 1 553 ? 18.642 62.952 -3.878 1.00 19.99 ? 586 ASN A C 1 ATOM 4577 O O . ASN A 1 553 ? 19.074 61.892 -3.467 1.00 19.72 ? 586 ASN A O 1 ATOM 4578 C CB . ASN A 1 553 ? 20.404 64.637 -3.160 1.00 18.22 ? 586 ASN A CB 1 ATOM 4579 C CG . ASN A 1 553 ? 20.848 64.896 -4.585 1.00 21.41 ? 586 ASN A CG 1 ATOM 4580 O OD1 . ASN A 1 553 ? 20.953 63.950 -5.375 1.00 20.73 ? 586 ASN A OD1 1 ATOM 4581 N ND2 . ASN A 1 553 ? 20.998 66.147 -4.946 1.00 22.83 ? 586 ASN A ND2 1 ATOM 4582 N N . ILE A 1 554 ? 17.878 63.074 -4.952 1.00 17.92 ? 587 ILE A N 1 ATOM 4583 C CA . ILE A 1 554 ? 17.399 61.885 -5.686 1.00 19.62 ? 587 ILE A CA 1 ATOM 4584 C C . ILE A 1 554 ? 18.471 61.449 -6.698 1.00 19.02 ? 587 ILE A C 1 ATOM 4585 O O . ILE A 1 554 ? 18.544 60.274 -7.069 1.00 18.44 ? 587 ILE A O 1 ATOM 4586 C CB . ILE A 1 554 ? 16.036 62.136 -6.323 1.00 18.42 ? 587 ILE A CB 1 ATOM 4587 C CG1 . ILE A 1 554 ? 15.049 62.687 -5.257 1.00 21.40 ? 587 ILE A CG1 1 ATOM 4588 C CG2 . ILE A 1 554 ? 15.448 60.775 -6.933 1.00 21.83 ? 587 ILE A CG2 1 ATOM 4589 C CD1 . ILE A 1 554 ? 13.660 62.917 -5.757 1.00 23.16 ? 587 ILE A CD1 1 ATOM 4590 N N . GLN A 1 555 ? 19.332 62.380 -7.142 1.00 18.02 ? 588 GLN A N 1 ATOM 4591 C CA . GLN A 1 555 ? 20.425 61.915 -8.009 1.00 17.24 ? 588 GLN A CA 1 ATOM 4592 C C . GLN A 1 555 ? 21.368 60.945 -7.289 1.00 17.34 ? 588 GLN A C 1 ATOM 4593 O O . GLN A 1 555 ? 21.934 60.035 -7.907 1.00 19.05 ? 588 GLN A O 1 ATOM 4594 C CB . GLN A 1 555 ? 21.217 63.132 -8.596 1.00 19.16 ? 588 GLN A CB 1 ATOM 4595 C CG . GLN A 1 555 ? 20.379 63.972 -9.582 1.00 19.07 ? 588 GLN A CG 1 ATOM 4596 C CD . GLN A 1 555 ? 21.272 64.792 -10.475 1.00 21.43 ? 588 GLN A CD 1 ATOM 4597 O OE1 . GLN A 1 555 ? 21.681 65.880 -10.085 1.00 21.71 ? 588 GLN A OE1 1 ATOM 4598 N NE2 . GLN A 1 555 ? 21.613 64.263 -11.663 1.00 21.39 ? 588 GLN A NE2 1 ATOM 4599 N N . ASP A 1 556 ? 21.561 61.096 -5.967 1.00 18.53 ? 589 ASP A N 1 ATOM 4600 C CA . ASP A 1 556 ? 22.338 60.097 -5.239 1.00 18.91 ? 589 ASP A CA 1 ATOM 4601 C C . ASP A 1 556 ? 21.646 58.716 -5.228 1.00 19.67 ? 589 ASP A C 1 ATOM 4602 O O . ASP A 1 556 ? 22.339 57.678 -5.282 1.00 19.06 ? 589 ASP A O 1 ATOM 4603 C CB . ASP A 1 556 ? 22.486 60.566 -3.789 1.00 19.46 ? 589 ASP A CB 1 ATOM 4604 C CG . ASP A 1 556 ? 23.571 61.646 -3.646 1.00 22.70 ? 589 ASP A CG 1 ATOM 4605 O OD1 . ASP A 1 556 ? 24.392 61.811 -4.579 1.00 24.43 ? 589 ASP A OD1 1 ATOM 4606 O OD2 . ASP A 1 556 ? 23.569 62.364 -2.626 1.00 24.91 ? 589 ASP A OD2 1 ATOM 4607 N N . TYR A 1 557 ? 20.308 58.712 -5.254 1.00 17.87 ? 590 TYR A N 1 ATOM 4608 C CA . TYR A 1 557 ? 19.594 57.424 -5.389 1.00 18.05 ? 590 TYR A CA 1 ATOM 4609 C C . TYR A 1 557 ? 19.857 56.864 -6.774 1.00 17.86 ? 590 TYR A C 1 ATOM 4610 O O . TYR A 1 557 ? 20.060 55.649 -6.936 1.00 18.85 ? 590 TYR A O 1 ATOM 4611 C CB . TYR A 1 557 ? 18.098 57.615 -5.071 1.00 18.56 ? 590 TYR A CB 1 ATOM 4612 C CG . TYR A 1 557 ? 17.467 56.452 -4.286 1.00 17.93 ? 590 TYR A CG 1 ATOM 4613 C CD1 . TYR A 1 557 ? 17.802 55.116 -4.534 1.00 20.39 ? 590 TYR A CD1 1 ATOM 4614 C CD2 . TYR A 1 557 ? 16.619 56.734 -3.217 1.00 19.78 ? 590 TYR A CD2 1 ATOM 4615 C CE1 . TYR A 1 557 ? 17.206 54.058 -3.739 1.00 20.37 ? 590 TYR A CE1 1 ATOM 4616 C CE2 . TYR A 1 557 ? 16.036 55.746 -2.454 1.00 19.34 ? 590 TYR A CE2 1 ATOM 4617 C CZ . TYR A 1 557 ? 16.332 54.426 -2.740 1.00 18.94 ? 590 TYR A CZ 1 ATOM 4618 O OH . TYR A 1 557 ? 15.745 53.442 -1.997 1.00 21.10 ? 590 TYR A OH 1 ATOM 4619 N N . ALA A 1 558 ? 19.819 57.713 -7.797 1.00 18.11 ? 591 ALA A N 1 ATOM 4620 C CA . ALA A 1 558 ? 20.059 57.228 -9.177 1.00 17.91 ? 591 ALA A CA 1 ATOM 4621 C C . ALA A 1 558 ? 21.425 56.581 -9.250 1.00 18.60 ? 591 ALA A C 1 ATOM 4622 O O . ALA A 1 558 ? 21.590 55.537 -9.868 1.00 18.92 ? 591 ALA A O 1 ATOM 4623 C CB . ALA A 1 558 ? 19.944 58.386 -10.128 1.00 18.93 ? 591 ALA A CB 1 ATOM 4624 N N . GLU A 1 559 ? 22.455 57.216 -8.668 1.00 18.92 ? 592 GLU A N 1 ATOM 4625 C CA . GLU A 1 559 ? 23.799 56.588 -8.718 1.00 19.59 ? 592 GLU A CA 1 ATOM 4626 C C . GLU A 1 559 ? 23.891 55.303 -7.942 1.00 20.22 ? 592 GLU A C 1 ATOM 4627 O O . GLU A 1 559 ? 24.546 54.339 -8.367 1.00 21.32 ? 592 GLU A O 1 ATOM 4628 C CB A GLU A 1 559 ? 24.792 57.638 -8.187 0.60 20.15 ? 592 GLU A CB 1 ATOM 4629 C CB B GLU A 1 559 ? 25.042 57.526 -8.425 0.40 21.42 ? 592 GLU A CB 1 ATOM 4630 C CG A GLU A 1 559 ? 24.995 58.842 -9.128 0.60 18.07 ? 592 GLU A CG 1 ATOM 4631 C CG B GLU A 1 559 ? 26.124 57.686 -9.622 0.40 25.14 ? 592 GLU A CG 1 ATOM 4632 C CD A GLU A 1 559 ? 25.274 58.448 -10.593 0.60 21.09 ? 592 GLU A CD 1 ATOM 4633 C CD B GLU A 1 559 ? 27.613 57.498 -9.241 0.40 28.78 ? 592 GLU A CD 1 ATOM 4634 O OE1 A GLU A 1 559 ? 24.467 58.801 -11.461 0.60 23.58 ? 592 GLU A OE1 1 ATOM 4635 O OE1 B GLU A 1 559 ? 28.081 56.341 -9.144 0.40 28.40 ? 592 GLU A OE1 1 ATOM 4636 O OE2 A GLU A 1 559 ? 26.296 57.746 -10.788 0.60 20.15 ? 592 GLU A OE2 1 ATOM 4637 O OE2 B GLU A 1 559 ? 28.341 58.507 -9.076 0.40 26.58 ? 592 GLU A OE2 1 ATOM 4638 N N . ALA A 1 560 ? 23.166 55.217 -6.833 1.00 19.29 ? 593 ALA A N 1 ATOM 4639 C CA . ALA A 1 560 ? 23.158 53.996 -6.052 1.00 19.84 ? 593 ALA A CA 1 ATOM 4640 C C . ALA A 1 560 ? 22.533 52.883 -6.901 1.00 21.50 ? 593 ALA A C 1 ATOM 4641 O O . ALA A 1 560 ? 23.064 51.809 -6.977 1.00 21.05 ? 593 ALA A O 1 ATOM 4642 C CB . ALA A 1 560 ? 22.345 54.193 -4.750 1.00 19.63 ? 593 ALA A CB 1 ATOM 4643 N N . LEU A 1 561 ? 21.408 53.143 -7.560 1.00 20.01 ? 594 LEU A N 1 ATOM 4644 C CA . LEU A 1 561 ? 20.771 52.091 -8.353 1.00 20.03 ? 594 LEU A CA 1 ATOM 4645 C C . LEU A 1 561 ? 21.694 51.650 -9.488 1.00 21.39 ? 594 LEU A C 1 ATOM 4646 O O . LEU A 1 561 ? 21.671 50.467 -9.858 1.00 20.89 ? 594 LEU A O 1 ATOM 4647 C CB . LEU A 1 561 ? 19.477 52.626 -8.985 1.00 20.88 ? 594 LEU A CB 1 ATOM 4648 C CG . LEU A 1 561 ? 18.363 52.956 -7.970 1.00 19.16 ? 594 LEU A CG 1 ATOM 4649 C CD1 . LEU A 1 561 ? 17.162 53.553 -8.714 1.00 21.38 ? 594 LEU A CD1 1 ATOM 4650 C CD2 . LEU A 1 561 ? 17.969 51.732 -7.188 1.00 20.62 ? 594 LEU A CD2 1 ATOM 4651 N N . LYS A 1 562 ? 22.460 52.585 -10.067 1.00 19.34 ? 595 LYS A N 1 ATOM 4652 C CA . LYS A 1 562 ? 23.414 52.124 -11.137 1.00 21.02 ? 595 LYS A CA 1 ATOM 4653 C C . LYS A 1 562 ? 24.426 51.152 -10.534 1.00 22.12 ? 595 LYS A C 1 ATOM 4654 O O . LYS A 1 562 ? 24.764 50.144 -11.139 1.00 22.70 ? 595 LYS A O 1 ATOM 4655 C CB . LYS A 1 562 ? 24.128 53.348 -11.700 1.00 20.17 ? 595 LYS A CB 1 ATOM 4656 C CG . LYS A 1 562 ? 23.253 54.271 -12.494 1.00 22.23 ? 595 LYS A CG 1 ATOM 4657 C CD . LYS A 1 562 ? 23.966 55.574 -12.910 1.00 22.87 ? 595 LYS A CD 1 ATOM 4658 C CE . LYS A 1 562 ? 23.000 56.569 -13.544 1.00 26.89 ? 595 LYS A CE 1 ATOM 4659 N NZ . LYS A 1 562 ? 23.673 57.853 -13.889 1.00 26.74 ? 595 LYS A NZ 1 ATOM 4660 N N . ASN A 1 563 ? 24.922 51.437 -9.334 1.00 22.11 ? 596 ASN A N 1 ATOM 4661 C CA A ASN A 1 563 ? 25.848 50.513 -8.678 0.60 22.56 ? 596 ASN A CA 1 ATOM 4662 C CA B ASN A 1 563 ? 25.846 50.536 -8.626 0.40 23.08 ? 596 ASN A CA 1 ATOM 4663 C C . ASN A 1 563 ? 25.199 49.178 -8.356 1.00 23.67 ? 596 ASN A C 1 ATOM 4664 O O . ASN A 1 563 ? 25.826 48.103 -8.538 1.00 23.74 ? 596 ASN A O 1 ATOM 4665 C CB A ASN A 1 563 ? 26.430 51.123 -7.391 0.60 22.36 ? 596 ASN A CB 1 ATOM 4666 C CB B ASN A 1 563 ? 26.300 51.210 -7.308 0.40 23.45 ? 596 ASN A CB 1 ATOM 4667 C CG A ASN A 1 563 ? 27.219 52.392 -7.655 0.60 25.23 ? 596 ASN A CG 1 ATOM 4668 C CG B ASN A 1 563 ? 27.162 50.315 -6.416 0.40 26.15 ? 596 ASN A CG 1 ATOM 4669 O OD1 A ASN A 1 563 ? 27.714 52.601 -8.763 0.60 30.71 ? 596 ASN A OD1 1 ATOM 4670 O OD1 B ASN A 1 563 ? 26.707 49.293 -5.883 0.40 32.33 ? 596 ASN A OD1 1 ATOM 4671 N ND2 A ASN A 1 563 ? 27.351 53.237 -6.637 0.60 26.25 ? 596 ASN A ND2 1 ATOM 4672 N ND2 B ASN A 1 563 ? 28.404 50.741 -6.196 0.40 29.36 ? 596 ASN A ND2 1 ATOM 4673 N N . TYR A 1 564 ? 23.954 49.189 -7.902 1.00 22.76 ? 597 TYR A N 1 ATOM 4674 C CA . TYR A 1 564 ? 23.348 47.941 -7.494 1.00 23.35 ? 597 TYR A CA 1 ATOM 4675 C C . TYR A 1 564 ? 23.027 47.086 -8.743 1.00 23.17 ? 597 TYR A C 1 ATOM 4676 O O . TYR A 1 564 ? 23.099 45.847 -8.661 1.00 23.30 ? 597 TYR A O 1 ATOM 4677 C CB . TYR A 1 564 ? 22.037 48.198 -6.724 1.00 23.20 ? 597 TYR A CB 1 ATOM 4678 C CG . TYR A 1 564 ? 22.199 49.074 -5.512 1.00 23.80 ? 597 TYR A CG 1 ATOM 4679 C CD1 . TYR A 1 564 ? 23.415 49.194 -4.845 1.00 25.33 ? 597 TYR A CD1 1 ATOM 4680 C CD2 . TYR A 1 564 ? 21.116 49.790 -5.030 1.00 20.91 ? 597 TYR A CD2 1 ATOM 4681 C CE1 . TYR A 1 564 ? 23.537 50.028 -3.719 1.00 25.16 ? 597 TYR A CE1 1 ATOM 4682 C CE2 . TYR A 1 564 ? 21.214 50.612 -3.940 1.00 23.58 ? 597 TYR A CE2 1 ATOM 4683 C CZ . TYR A 1 564 ? 22.434 50.752 -3.289 1.00 23.49 ? 597 TYR A CZ 1 ATOM 4684 O OH . TYR A 1 564 ? 22.487 51.581 -2.174 1.00 24.28 ? 597 TYR A OH 1 ATOM 4685 N N . ALA A 1 565 ? 22.617 47.737 -9.827 1.00 22.13 ? 598 ALA A N 1 ATOM 4686 C CA . ALA A 1 565 ? 22.321 47.018 -11.095 1.00 22.64 ? 598 ALA A CA 1 ATOM 4687 C C . ALA A 1 565 ? 23.625 46.358 -11.572 1.00 25.12 ? 598 ALA A C 1 ATOM 4688 O O . ALA A 1 565 ? 23.607 45.160 -11.904 1.00 24.88 ? 598 ALA A O 1 ATOM 4689 C CB . ALA A 1 565 ? 21.771 47.950 -12.108 1.00 23.49 ? 598 ALA A CB 1 ATOM 4690 N N . ALA A 1 566 ? 24.724 47.118 -11.626 1.00 24.07 ? 599 ALA A N 1 ATOM 4691 C CA . ALA A 1 566 ? 26.004 46.489 -11.998 1.00 25.54 ? 599 ALA A CA 1 ATOM 4692 C C . ALA A 1 566 ? 26.366 45.328 -11.094 1.00 26.71 ? 599 ALA A C 1 ATOM 4693 O O . ALA A 1 566 ? 26.888 44.302 -11.596 1.00 27.09 ? 599 ALA A O 1 ATOM 4694 C CB . ALA A 1 566 ? 27.121 47.534 -11.967 1.00 25.21 ? 599 ALA A CB 1 ATOM 4695 N N . SER A 1 567 ? 26.173 45.447 -9.799 1.00 26.83 ? 600 SER A N 1 ATOM 4696 C CA . SER A 1 567 ? 26.503 44.352 -8.893 1.00 28.64 ? 600 SER A CA 1 ATOM 4697 C C . SER A 1 567 ? 25.693 43.070 -9.100 1.00 30.60 ? 600 SER A C 1 ATOM 4698 O O . SER A 1 567 ? 26.258 41.959 -9.124 1.00 31.00 ? 600 SER A O 1 ATOM 4699 C CB . SER A 1 567 ? 26.447 44.789 -7.436 1.00 29.93 ? 600 SER A CB 1 ATOM 4700 O OG A SER A 1 567 ? 27.366 45.855 -7.254 0.50 30.19 ? 600 SER A OG 1 ATOM 4701 O OG B SER A 1 567 ? 26.532 43.681 -6.535 0.50 30.65 ? 600 SER A OG 1 ATOM 4702 N N . ILE A 1 568 ? 24.381 43.184 -9.266 1.00 29.61 ? 601 ILE A N 1 ATOM 4703 C CA . ILE A 1 568 ? 23.587 41.979 -9.393 1.00 28.99 ? 601 ILE A CA 1 ATOM 4704 C C . ILE A 1 568 ? 23.909 41.357 -10.744 1.00 29.64 ? 601 ILE A C 1 ATOM 4705 O O . ILE A 1 568 ? 23.944 40.114 -10.857 1.00 29.98 ? 601 ILE A O 1 ATOM 4706 C CB . ILE A 1 568 ? 22.066 42.287 -9.219 1.00 28.38 ? 601 ILE A CB 1 ATOM 4707 C CG1 . ILE A 1 568 ? 21.278 40.988 -8.971 1.00 31.80 ? 601 ILE A CG1 1 ATOM 4708 C CG2 . ILE A 1 568 ? 21.544 43.104 -10.382 1.00 27.60 ? 601 ILE A CG2 1 ATOM 4709 C CD1 . ILE A 1 568 ? 21.600 40.322 -7.666 1.00 33.75 ? 601 ILE A CD1 1 ATOM 4710 N N . TYR A 1 569 ? 24.199 42.195 -11.735 1.00 28.72 ? 602 TYR A N 1 ATOM 4711 C CA . TYR A 1 569 ? 24.526 41.705 -13.076 1.00 30.24 ? 602 TYR A CA 1 ATOM 4712 C C . TYR A 1 569 ? 25.844 40.956 -13.035 1.00 31.85 ? 602 TYR A C 1 ATOM 4713 O O . TYR A 1 569 ? 25.959 39.865 -13.640 1.00 31.75 ? 602 TYR A O 1 ATOM 4714 C CB . TYR A 1 569 ? 24.647 42.854 -14.062 1.00 30.55 ? 602 TYR A CB 1 ATOM 4715 C CG . TYR A 1 569 ? 25.047 42.459 -15.475 1.00 33.71 ? 602 TYR A CG 1 ATOM 4716 C CD1 . TYR A 1 569 ? 24.209 41.662 -16.255 1.00 36.16 ? 602 TYR A CD1 1 ATOM 4717 C CD2 . TYR A 1 569 ? 26.239 42.920 -16.029 1.00 37.02 ? 602 TYR A CD2 1 ATOM 4718 C CE1 . TYR A 1 569 ? 24.563 41.294 -17.560 1.00 38.86 ? 602 TYR A CE1 1 ATOM 4719 C CE2 . TYR A 1 569 ? 26.617 42.564 -17.335 1.00 38.91 ? 602 TYR A CE2 1 ATOM 4720 C CZ . TYR A 1 569 ? 25.771 41.755 -18.088 1.00 42.05 ? 602 TYR A CZ 1 ATOM 4721 O OH . TYR A 1 569 ? 26.159 41.402 -19.376 1.00 44.53 ? 602 TYR A OH 1 ATOM 4722 N N . ASN A 1 570 ? 26.832 41.526 -12.327 1.00 32.75 ? 603 ASN A N 1 ATOM 4723 C CA A ASN A 1 570 ? 28.155 40.865 -12.190 0.60 33.85 ? 603 ASN A CA 1 ATOM 4724 C CA B ASN A 1 570 ? 28.142 40.875 -12.207 0.40 32.79 ? 603 ASN A CA 1 ATOM 4725 C C . ASN A 1 570 ? 27.993 39.492 -11.580 1.00 34.12 ? 603 ASN A C 1 ATOM 4726 O O . ASN A 1 570 ? 28.678 38.534 -12.006 1.00 33.97 ? 603 ASN A O 1 ATOM 4727 C CB A ASN A 1 570 ? 29.130 41.665 -11.301 0.60 34.17 ? 603 ASN A CB 1 ATOM 4728 C CB B ASN A 1 570 ? 29.106 41.724 -11.365 0.40 32.27 ? 603 ASN A CB 1 ATOM 4729 C CG A ASN A 1 570 ? 30.240 40.771 -10.680 0.60 36.35 ? 603 ASN A CG 1 ATOM 4730 C CG B ASN A 1 570 ? 29.633 42.931 -12.108 0.40 29.56 ? 603 ASN A CG 1 ATOM 4731 O OD1 A ASN A 1 570 ? 31.269 40.524 -11.306 0.60 40.94 ? 603 ASN A OD1 1 ATOM 4732 O OD1 B ASN A 1 570 ? 29.404 43.088 -13.296 0.40 28.45 ? 603 ASN A OD1 1 ATOM 4733 N ND2 A ASN A 1 570 ? 30.017 40.286 -9.457 0.60 38.55 ? 603 ASN A ND2 1 ATOM 4734 N ND2 B ASN A 1 570 ? 30.358 43.794 -11.401 0.40 30.89 ? 603 ASN A ND2 1 ATOM 4735 N N . LEU A 1 571 ? 27.134 39.391 -10.573 1.00 35.25 ? 604 LEU A N 1 ATOM 4736 C CA . LEU A 1 571 ? 26.853 38.145 -9.879 1.00 37.25 ? 604 LEU A CA 1 ATOM 4737 C C . LEU A 1 571 ? 26.287 37.103 -10.827 1.00 37.51 ? 604 LEU A C 1 ATOM 4738 O O . LEU A 1 571 ? 26.367 35.891 -10.526 1.00 39.28 ? 604 LEU A O 1 ATOM 4739 C CB . LEU A 1 571 ? 25.829 38.321 -8.763 1.00 38.01 ? 604 LEU A CB 1 ATOM 4740 C CG . LEU A 1 571 ? 26.207 38.601 -7.307 1.00 41.26 ? 604 LEU A CG 1 ATOM 4741 C CD1 . LEU A 1 571 ? 25.047 38.212 -6.400 1.00 43.85 ? 604 LEU A CD1 1 ATOM 4742 C CD2 . LEU A 1 571 ? 27.460 37.862 -6.850 1.00 43.99 ? 604 LEU A CD2 1 ATOM 4743 N N . SER A 1 572 ? 25.706 37.554 -11.940 1.00 36.57 ? 605 SER A N 1 ATOM 4744 C CA . SER A 1 572 ? 25.042 36.647 -12.850 1.00 37.11 ? 605 SER A CA 1 ATOM 4745 C C . SER A 1 572 ? 25.995 36.090 -13.878 1.00 37.72 ? 605 SER A C 1 ATOM 4746 O O . SER A 1 572 ? 25.664 35.106 -14.540 1.00 37.64 ? 605 SER A O 1 ATOM 4747 C CB . SER A 1 572 ? 23.881 37.341 -13.592 1.00 37.02 ? 605 SER A CB 1 ATOM 4748 O OG . SER A 1 572 ? 24.368 38.084 -14.715 1.00 37.21 ? 605 SER A OG 1 ATOM 4749 N N . LYS A 1 573 ? 27.155 36.720 -14.051 1.00 37.93 ? 606 LYS A N 1 ATOM 4750 C CA . LYS A 1 573 ? 28.084 36.282 -15.105 1.00 39.39 ? 606 LYS A CA 1 ATOM 4751 C C . LYS A 1 573 ? 28.531 34.815 -14.982 1.00 38.84 ? 606 LYS A C 1 ATOM 4752 O O . LYS A 1 573 ? 28.722 34.164 -16.005 1.00 39.18 ? 606 LYS A O 1 ATOM 4753 C CB . LYS A 1 573 ? 29.289 37.216 -15.218 1.00 39.83 ? 606 LYS A CB 1 ATOM 4754 C CG . LYS A 1 573 ? 28.907 38.614 -15.646 1.00 41.62 ? 606 LYS A CG 1 ATOM 4755 C CD . LYS A 1 573 ? 30.126 39.503 -15.721 1.00 43.53 ? 606 LYS A CD 1 ATOM 4756 C CE . LYS A 1 573 ? 29.757 40.894 -16.182 1.00 46.95 ? 606 LYS A CE 1 ATOM 4757 N NZ . LYS A 1 573 ? 30.936 41.800 -16.076 1.00 48.31 ? 606 LYS A NZ 1 ATOM 4758 N N . LYS A 1 574 ? 28.693 34.299 -13.764 1.00 39.03 ? 607 LYS A N 1 ATOM 4759 C CA . LYS A 1 574 ? 29.079 32.879 -13.590 1.00 38.85 ? 607 LYS A CA 1 ATOM 4760 C C . LYS A 1 574 ? 28.044 31.915 -14.215 1.00 38.37 ? 607 LYS A C 1 ATOM 4761 O O . LYS A 1 574 ? 28.378 30.767 -14.569 1.00 37.16 ? 607 LYS A O 1 ATOM 4762 C CB . LYS A 1 574 ? 29.352 32.518 -12.120 1.00 39.45 ? 607 LYS A CB 1 ATOM 4763 C CG . LYS A 1 574 ? 28.160 32.572 -11.191 1.00 42.21 ? 607 LYS A CG 1 ATOM 4764 C CD . LYS A 1 574 ? 28.116 31.297 -10.344 1.00 47.16 ? 607 LYS A CD 1 ATOM 4765 C CE . LYS A 1 574 ? 28.592 31.500 -8.913 1.00 49.58 ? 607 LYS A CE 1 ATOM 4766 N NZ . LYS A 1 574 ? 28.384 30.235 -8.126 1.00 51.40 ? 607 LYS A NZ 1 ATOM 4767 N N . HIS A 1 575 ? 26.806 32.393 -14.372 1.00 36.06 ? 608 HIS A N 1 ATOM 4768 C CA . HIS A 1 575 ? 25.718 31.605 -14.938 1.00 34.75 ? 608 HIS A CA 1 ATOM 4769 C C . HIS A 1 575 ? 25.385 32.010 -16.362 1.00 34.50 ? 608 HIS A C 1 ATOM 4770 O O . HIS A 1 575 ? 24.303 31.703 -16.870 1.00 34.52 ? 608 HIS A O 1 ATOM 4771 C CB . HIS A 1 575 ? 24.457 31.818 -14.100 1.00 33.64 ? 608 HIS A CB 1 ATOM 4772 C CG . HIS A 1 575 ? 24.613 31.429 -12.672 1.00 33.76 ? 608 HIS A CG 1 ATOM 4773 N ND1 . HIS A 1 575 ? 24.571 32.346 -11.643 1.00 34.53 ? 608 HIS A ND1 1 ATOM 4774 C CD2 . HIS A 1 575 ? 24.832 30.224 -12.095 1.00 29.60 ? 608 HIS A CD2 1 ATOM 4775 C CE1 . HIS A 1 575 ? 24.736 31.720 -10.490 1.00 31.53 ? 608 HIS A CE1 1 ATOM 4776 N NE2 . HIS A 1 575 ? 24.903 30.428 -10.737 1.00 36.78 ? 608 HIS A NE2 1 ATOM 4777 N N . ASP A 1 576 ? 26.308 32.685 -17.035 1.00 35.61 ? 609 ASP A N 1 ATOM 4778 C CA . ASP A 1 576 ? 26.030 33.261 -18.336 1.00 36.33 ? 609 ASP A CA 1 ATOM 4779 C C . ASP A 1 576 ? 25.388 32.296 -19.369 1.00 36.56 ? 609 ASP A C 1 ATOM 4780 O O . ASP A 1 576 ? 24.464 32.691 -20.115 1.00 35.94 ? 609 ASP A O 1 ATOM 4781 C CB . ASP A 1 576 ? 27.301 33.921 -18.885 1.00 38.23 ? 609 ASP A CB 1 ATOM 4782 C CG . ASP A 1 576 ? 27.104 34.514 -20.263 1.00 42.07 ? 609 ASP A CG 1 ATOM 4783 O OD1 . ASP A 1 576 ? 26.398 35.544 -20.402 1.00 47.15 ? 609 ASP A OD1 1 ATOM 4784 O OD2 . ASP A 1 576 ? 27.668 33.938 -21.227 1.00 48.97 ? 609 ASP A OD2 1 ATOM 4785 N N . GLN A 1 577 ? 25.859 31.044 -19.418 1.00 37.03 ? 610 GLN A N 1 ATOM 4786 C CA . GLN A 1 577 ? 25.265 30.065 -20.354 1.00 36.90 ? 610 GLN A CA 1 ATOM 4787 C C . GLN A 1 577 ? 23.788 29.809 -20.036 1.00 35.33 ? 610 GLN A C 1 ATOM 4788 O O . GLN A 1 577 ? 22.962 29.688 -20.957 1.00 35.00 ? 610 GLN A O 1 ATOM 4789 C CB . GLN A 1 577 ? 26.019 28.705 -20.356 1.00 37.67 ? 610 GLN A CB 1 ATOM 4790 C CG . GLN A 1 577 ? 25.556 27.754 -21.476 1.00 40.11 ? 610 GLN A CG 1 ATOM 4791 C CD . GLN A 1 577 ? 25.605 28.418 -22.842 1.00 42.61 ? 610 GLN A CD 1 ATOM 4792 O OE1 . GLN A 1 577 ? 26.662 28.882 -23.273 1.00 47.00 ? 610 GLN A OE1 1 ATOM 4793 N NE2 . GLN A 1 577 ? 24.466 28.481 -23.527 1.00 43.11 ? 610 GLN A NE2 1 ATOM 4794 N N . GLN A 1 578 ? 23.496 29.703 -18.741 1.00 34.33 ? 611 GLN A N 1 ATOM 4795 C CA . GLN A 1 578 ? 22.128 29.432 -18.293 1.00 33.49 ? 611 GLN A CA 1 ATOM 4796 C C . GLN A 1 578 ? 21.222 30.614 -18.598 1.00 32.99 ? 611 GLN A C 1 ATOM 4797 O O . GLN A 1 578 ? 20.061 30.419 -18.993 1.00 29.44 ? 611 GLN A O 1 ATOM 4798 C CB . GLN A 1 578 ? 22.078 29.118 -16.810 1.00 34.37 ? 611 GLN A CB 1 ATOM 4799 C CG . GLN A 1 578 ? 22.533 27.724 -16.500 1.00 38.92 ? 611 GLN A CG 1 ATOM 4800 C CD . GLN A 1 578 ? 23.991 27.563 -16.816 1.00 44.73 ? 611 GLN A CD 1 ATOM 4801 O OE1 . GLN A 1 578 ? 24.848 28.145 -16.140 1.00 47.27 ? 611 GLN A OE1 1 ATOM 4802 N NE2 . GLN A 1 578 ? 24.293 26.811 -17.877 1.00 47.77 ? 611 GLN A NE2 1 ATOM 4803 N N . LEU A 1 579 ? 21.764 31.834 -18.450 1.00 32.29 ? 612 LEU A N 1 ATOM 4804 C CA . LEU A 1 579 ? 21.003 33.043 -18.802 1.00 32.35 ? 612 LEU A CA 1 ATOM 4805 C C . LEU A 1 579 ? 20.599 32.974 -20.256 1.00 31.78 ? 612 LEU A C 1 ATOM 4806 O O . LEU A 1 579 ? 19.449 33.208 -20.612 1.00 31.62 ? 612 LEU A O 1 ATOM 4807 C CB . LEU A 1 579 ? 21.837 34.320 -18.572 1.00 32.06 ? 612 LEU A CB 1 ATOM 4808 C CG . LEU A 1 579 ? 22.340 34.622 -17.158 1.00 34.42 ? 612 LEU A CG 1 ATOM 4809 C CD1 . LEU A 1 579 ? 23.102 35.965 -17.169 1.00 34.47 ? 612 LEU A CD1 1 ATOM 4810 C CD2 . LEU A 1 579 ? 21.170 34.661 -16.224 1.00 32.98 ? 612 LEU A CD2 1 ATOM 4811 N N . THR A 1 580 ? 21.536 32.570 -21.116 1.00 31.71 ? 613 THR A N 1 ATOM 4812 C CA . THR A 1 580 ? 21.225 32.496 -22.520 1.00 32.04 ? 613 THR A CA 1 ATOM 4813 C C . THR A 1 580 ? 20.232 31.374 -22.795 1.00 31.23 ? 613 THR A C 1 ATOM 4814 O O . THR A 1 580 ? 19.265 31.566 -23.532 1.00 31.72 ? 613 THR A O 1 ATOM 4815 C CB . THR A 1 580 ? 22.512 32.271 -23.346 1.00 33.04 ? 613 THR A CB 1 ATOM 4816 O OG1 . THR A 1 580 ? 23.265 33.492 -23.338 1.00 36.18 ? 613 THR A OG1 1 ATOM 4817 C CG2 . THR A 1 580 ? 22.187 31.911 -24.795 1.00 33.76 ? 613 THR A CG2 1 ATOM 4818 N N . ASP A 1 581 ? 20.460 30.224 -22.182 1.00 30.33 ? 614 ASP A N 1 ATOM 4819 C CA . ASP A 1 581 ? 19.610 29.057 -22.459 1.00 30.99 ? 614 ASP A CA 1 ATOM 4820 C C . ASP A 1 581 ? 18.172 29.244 -21.964 1.00 30.96 ? 614 ASP A C 1 ATOM 4821 O O . ASP A 1 581 ? 17.221 28.726 -22.570 1.00 30.96 ? 614 ASP A O 1 ATOM 4822 C CB . ASP A 1 581 ? 20.227 27.825 -21.794 1.00 30.37 ? 614 ASP A CB 1 ATOM 4823 C CG . ASP A 1 581 ? 21.484 27.330 -22.520 1.00 32.47 ? 614 ASP A CG 1 ATOM 4824 O OD1 . ASP A 1 581 ? 21.767 27.797 -23.652 1.00 35.65 ? 614 ASP A OD1 1 ATOM 4825 O OD2 . ASP A 1 581 ? 22.172 26.475 -21.935 1.00 37.21 ? 614 ASP A OD2 1 ATOM 4826 N N . HIS A 1 582 ? 18.006 29.998 -20.862 1.00 29.29 ? 615 HIS A N 1 ATOM 4827 C CA . HIS A 1 582 ? 16.676 30.192 -20.250 1.00 28.87 ? 615 HIS A CA 1 ATOM 4828 C C . HIS A 1 582 ? 16.024 31.554 -20.628 1.00 28.19 ? 615 HIS A C 1 ATOM 4829 O O . HIS A 1 582 ? 14.942 31.908 -20.129 1.00 28.32 ? 615 HIS A O 1 ATOM 4830 C CB . HIS A 1 582 ? 16.765 30.021 -18.740 1.00 28.92 ? 615 HIS A CB 1 ATOM 4831 C CG . HIS A 1 582 ? 17.071 28.617 -18.328 1.00 29.65 ? 615 HIS A CG 1 ATOM 4832 N ND1 . HIS A 1 582 ? 16.085 27.681 -18.073 1.00 31.51 ? 615 HIS A ND1 1 ATOM 4833 C CD2 . HIS A 1 582 ? 18.253 27.975 -18.169 1.00 32.28 ? 615 HIS A CD2 1 ATOM 4834 C CE1 . HIS A 1 582 ? 16.651 26.527 -17.745 1.00 33.65 ? 615 HIS A CE1 1 ATOM 4835 N NE2 . HIS A 1 582 ? 17.964 26.674 -17.806 1.00 32.72 ? 615 HIS A NE2 1 ATOM 4836 N N . GLY A 1 583 ? 16.666 32.257 -21.564 1.00 26.82 ? 616 GLY A N 1 ATOM 4837 C CA . GLY A 1 583 ? 16.211 33.545 -22.082 1.00 26.89 ? 616 GLY A CA 1 ATOM 4838 C C . GLY A 1 583 ? 16.057 34.599 -20.975 1.00 26.63 ? 616 GLY A C 1 ATOM 4839 O O . GLY A 1 583 ? 15.033 35.313 -20.942 1.00 28.09 ? 616 GLY A O 1 ATOM 4840 N N . VAL A 1 584 ? 17.017 34.606 -20.038 1.00 26.10 ? 617 VAL A N 1 ATOM 4841 C CA . VAL A 1 584 ? 17.036 35.583 -18.916 1.00 24.57 ? 617 VAL A CA 1 ATOM 4842 C C . VAL A 1 584 ? 17.868 36.811 -19.339 1.00 26.49 ? 617 VAL A C 1 ATOM 4843 O O . VAL A 1 584 ? 19.011 36.680 -19.738 1.00 26.68 ? 617 VAL A O 1 ATOM 4844 C CB . VAL A 1 584 ? 17.674 34.997 -17.675 1.00 25.65 ? 617 VAL A CB 1 ATOM 4845 C CG1 . VAL A 1 584 ? 17.472 35.989 -16.525 1.00 24.75 ? 617 VAL A CG1 1 ATOM 4846 C CG2 . VAL A 1 584 ? 17.041 33.641 -17.283 1.00 25.72 ? 617 VAL A CG2 1 ATOM 4847 N N . SER A 1 585 ? 17.314 38.009 -19.208 1.00 24.19 ? 618 SER A N 1 ATOM 4848 C CA . SER A 1 585 ? 18.038 39.247 -19.577 1.00 23.80 ? 618 SER A CA 1 ATOM 4849 C C . SER A 1 585 ? 17.877 40.302 -18.465 1.00 24.08 ? 618 SER A C 1 ATOM 4850 O O . SER A 1 585 ? 16.793 40.429 -17.862 1.00 22.90 ? 618 SER A O 1 ATOM 4851 C CB . SER A 1 585 ? 17.448 39.821 -20.842 1.00 24.07 ? 618 SER A CB 1 ATOM 4852 O OG . SER A 1 585 ? 18.084 41.048 -21.247 1.00 25.48 ? 618 SER A OG 1 ATOM 4853 N N . PHE A 1 586 ? 18.941 41.076 -18.240 1.00 22.09 ? 619 PHE A N 1 ATOM 4854 C CA . PHE A 1 586 ? 18.857 42.222 -17.316 1.00 21.39 ? 619 PHE A CA 1 ATOM 4855 C C . PHE A 1 586 ? 18.588 43.518 -18.078 1.00 21.65 ? 619 PHE A C 1 ATOM 4856 O O . PHE A 1 586 ? 18.573 44.586 -17.458 1.00 21.37 ? 619 PHE A O 1 ATOM 4857 C CB . PHE A 1 586 ? 20.173 42.362 -16.500 1.00 22.45 ? 619 PHE A CB 1 ATOM 4858 C CG . PHE A 1 586 ? 20.330 41.325 -15.442 1.00 23.20 ? 619 PHE A CG 1 ATOM 4859 C CD1 . PHE A 1 586 ? 19.920 41.582 -14.130 1.00 22.63 ? 619 PHE A CD1 1 ATOM 4860 C CD2 . PHE A 1 586 ? 20.874 40.064 -15.735 1.00 26.41 ? 619 PHE A CD2 1 ATOM 4861 C CE1 . PHE A 1 586 ? 20.001 40.631 -13.141 1.00 24.42 ? 619 PHE A CE1 1 ATOM 4862 C CE2 . PHE A 1 586 ? 20.970 39.099 -14.708 1.00 27.08 ? 619 PHE A CE2 1 ATOM 4863 C CZ . PHE A 1 586 ? 20.573 39.391 -13.415 1.00 26.75 ? 619 PHE A CZ 1 ATOM 4864 N N . ASP A 1 587 ? 18.303 43.473 -19.369 1.00 21.76 ? 620 ASP A N 1 ATOM 4865 C CA . ASP A 1 587 ? 18.082 44.656 -20.162 1.00 21.57 ? 620 ASP A CA 1 ATOM 4866 C C . ASP A 1 587 ? 17.029 45.606 -19.537 1.00 21.46 ? 620 ASP A C 1 ATOM 4867 O O . ASP A 1 587 ? 17.254 46.797 -19.487 1.00 21.73 ? 620 ASP A O 1 ATOM 4868 C CB . ASP A 1 587 ? 17.687 44.330 -21.609 1.00 23.56 ? 620 ASP A CB 1 ATOM 4869 C CG . ASP A 1 587 ? 18.849 43.825 -22.420 1.00 26.90 ? 620 ASP A CG 1 ATOM 4870 O OD1 . ASP A 1 587 ? 19.988 43.733 -21.905 1.00 30.21 ? 620 ASP A OD1 1 ATOM 4871 O OD2 . ASP A 1 587 ? 18.552 43.502 -23.586 1.00 30.45 ? 620 ASP A OD2 1 ATOM 4872 N N . SER A 1 588 ? 15.899 45.053 -19.077 1.00 20.05 ? 621 SER A N 1 ATOM 4873 C CA . SER A 1 588 ? 14.834 45.934 -18.569 1.00 20.48 ? 621 SER A CA 1 ATOM 4874 C C . SER A 1 588 ? 15.279 46.652 -17.308 1.00 19.79 ? 621 SER A C 1 ATOM 4875 O O . SER A 1 588 ? 14.837 47.772 -17.058 1.00 19.48 ? 621 SER A O 1 ATOM 4876 C CB . SER A 1 588 ? 13.539 45.131 -18.280 1.00 21.17 ? 621 SER A CB 1 ATOM 4877 O OG . SER A 1 588 ? 13.724 44.132 -17.331 1.00 22.87 ? 621 SER A OG 1 ATOM 4878 N N . LEU A 1 589 ? 16.103 45.986 -16.500 1.00 19.39 ? 622 LEU A N 1 ATOM 4879 C CA . LEU A 1 589 ? 16.572 46.579 -15.249 1.00 19.62 ? 622 LEU A CA 1 ATOM 4880 C C . LEU A 1 589 ? 17.471 47.759 -15.599 1.00 19.87 ? 622 LEU A C 1 ATOM 4881 O O . LEU A 1 589 ? 17.325 48.841 -15.008 1.00 21.67 ? 622 LEU A O 1 ATOM 4882 C CB . LEU A 1 589 ? 17.314 45.578 -14.383 1.00 20.16 ? 622 LEU A CB 1 ATOM 4883 C CG . LEU A 1 589 ? 17.817 46.158 -13.066 1.00 22.17 ? 622 LEU A CG 1 ATOM 4884 C CD1 . LEU A 1 589 ? 16.637 46.588 -12.219 1.00 23.30 ? 622 LEU A CD1 1 ATOM 4885 C CD2 . LEU A 1 589 ? 18.649 45.146 -12.369 1.00 24.95 ? 622 LEU A CD2 1 ATOM 4886 N N . PHE A 1 590 ? 18.390 47.556 -16.534 1.00 19.89 ? 623 PHE A N 1 ATOM 4887 C CA . PHE A 1 590 ? 19.310 48.648 -16.869 1.00 19.57 ? 623 PHE A CA 1 ATOM 4888 C C . PHE A 1 590 ? 18.528 49.772 -17.511 1.00 19.49 ? 623 PHE A C 1 ATOM 4889 O O . PHE A 1 590 ? 18.827 50.980 -17.306 1.00 20.25 ? 623 PHE A O 1 ATOM 4890 C CB . PHE A 1 590 ? 20.453 48.146 -17.787 1.00 20.76 ? 623 PHE A CB 1 ATOM 4891 C CG . PHE A 1 590 ? 21.488 47.401 -17.035 1.00 24.64 ? 623 PHE A CG 1 ATOM 4892 C CD1 . PHE A 1 590 ? 22.383 48.105 -16.225 1.00 27.71 ? 623 PHE A CD1 1 ATOM 4893 C CD2 . PHE A 1 590 ? 21.570 46.030 -17.078 1.00 29.06 ? 623 PHE A CD2 1 ATOM 4894 C CE1 . PHE A 1 590 ? 23.355 47.462 -15.507 1.00 29.03 ? 623 PHE A CE1 1 ATOM 4895 C CE2 . PHE A 1 590 ? 22.570 45.336 -16.322 1.00 31.44 ? 623 PHE A CE2 1 ATOM 4896 C CZ . PHE A 1 590 ? 23.438 46.085 -15.521 1.00 30.91 ? 623 PHE A CZ 1 ATOM 4897 N N . SER A 1 591 ? 17.505 49.451 -18.324 1.00 18.06 ? 624 SER A N 1 ATOM 4898 C CA . SER A 1 591 ? 16.728 50.485 -18.938 1.00 17.73 ? 624 SER A CA 1 ATOM 4899 C C . SER A 1 591 ? 15.929 51.359 -17.902 1.00 18.35 ? 624 SER A C 1 ATOM 4900 O O . SER A 1 591 ? 15.865 52.575 -17.993 1.00 19.10 ? 624 SER A O 1 ATOM 4901 C CB . SER A 1 591 ? 15.718 49.817 -19.948 1.00 19.76 ? 624 SER A CB 1 ATOM 4902 O OG . SER A 1 591 ? 14.803 50.762 -20.500 1.00 20.58 ? 624 SER A OG 1 ATOM 4903 N N . ALA A 1 592 ? 15.311 50.656 -16.933 1.00 18.11 ? 625 ALA A N 1 ATOM 4904 C CA . ALA A 1 592 ? 14.634 51.359 -15.847 1.00 17.48 ? 625 ALA A CA 1 ATOM 4905 C C . ALA A 1 592 ? 15.615 52.307 -15.100 1.00 18.23 ? 625 ALA A C 1 ATOM 4906 O O . ALA A 1 592 ? 15.213 53.450 -14.774 1.00 19.04 ? 625 ALA A O 1 ATOM 4907 C CB . ALA A 1 592 ? 14.047 50.330 -14.836 1.00 19.54 ? 625 ALA A CB 1 ATOM 4908 N N . VAL A 1 593 ? 16.809 51.768 -14.768 1.00 18.50 ? 626 VAL A N 1 ATOM 4909 C CA . VAL A 1 593 ? 17.842 52.592 -14.095 1.00 18.87 ? 626 VAL A CA 1 ATOM 4910 C C . VAL A 1 593 ? 18.214 53.817 -14.904 1.00 19.18 ? 626 VAL A C 1 ATOM 4911 O O . VAL A 1 593 ? 18.342 54.920 -14.340 1.00 20.80 ? 626 VAL A O 1 ATOM 4912 C CB . VAL A 1 593 ? 19.029 51.709 -13.714 1.00 20.33 ? 626 VAL A CB 1 ATOM 4913 C CG1 . VAL A 1 593 ? 20.239 52.591 -13.240 1.00 22.71 ? 626 VAL A CG1 1 ATOM 4914 C CG2 . VAL A 1 593 ? 18.645 50.679 -12.592 1.00 19.41 ? 626 VAL A CG2 1 ATOM 4915 N N . LYS A 1 594 ? 18.379 53.644 -16.212 1.00 19.31 ? 627 LYS A N 1 ATOM 4916 C CA . LYS A 1 594 ? 18.653 54.765 -17.105 1.00 19.16 ? 627 LYS A CA 1 ATOM 4917 C C . LYS A 1 594 ? 17.514 55.820 -17.042 1.00 19.36 ? 627 LYS A C 1 ATOM 4918 O O . LYS A 1 594 ? 17.715 57.038 -16.893 1.00 20.24 ? 627 LYS A O 1 ATOM 4919 C CB . LYS A 1 594 ? 18.895 54.243 -18.533 1.00 19.89 ? 627 LYS A CB 1 ATOM 4920 C CG . LYS A 1 594 ? 19.066 55.373 -19.527 1.00 24.83 ? 627 LYS A CG 1 ATOM 4921 C CD . LYS A 1 594 ? 19.288 54.781 -20.947 1.00 26.52 ? 627 LYS A CD 1 ATOM 4922 C CE . LYS A 1 594 ? 19.482 55.929 -21.929 1.00 30.68 ? 627 LYS A CE 1 ATOM 4923 N NZ . LYS A 1 594 ? 18.168 56.615 -22.264 1.00 34.74 ? 627 LYS A NZ 1 ATOM 4924 N N . ASN A 1 595 ? 16.267 55.312 -17.077 1.00 19.14 ? 628 ASN A N 1 ATOM 4925 C CA . ASN A 1 595 ? 15.126 56.249 -17.059 1.00 17.95 ? 628 ASN A CA 1 ATOM 4926 C C . ASN A 1 595 ? 15.032 56.975 -15.696 1.00 17.84 ? 628 ASN A C 1 ATOM 4927 O O . ASN A 1 595 ? 14.631 58.134 -15.654 1.00 19.11 ? 628 ASN A O 1 ATOM 4928 C CB . ASN A 1 595 ? 13.840 55.409 -17.364 1.00 19.22 ? 628 ASN A CB 1 ATOM 4929 C CG . ASN A 1 595 ? 13.814 54.886 -18.793 1.00 20.40 ? 628 ASN A CG 1 ATOM 4930 O OD1 . ASN A 1 595 ? 14.615 55.281 -19.643 1.00 22.40 ? 628 ASN A OD1 1 ATOM 4931 N ND2 . ASN A 1 595 ? 12.812 54.027 -19.076 1.00 19.88 ? 628 ASN A ND2 1 ATOM 4932 N N . PHE A 1 596 ? 15.335 56.226 -14.633 1.00 17.54 ? 629 PHE A N 1 ATOM 4933 C CA . PHE A 1 596 ? 15.295 56.846 -13.270 1.00 17.49 ? 629 PHE A CA 1 ATOM 4934 C C . PHE A 1 596 ? 16.362 57.963 -13.224 1.00 18.02 ? 629 PHE A C 1 ATOM 4935 O O . PHE A 1 596 ? 16.075 59.040 -12.682 1.00 18.74 ? 629 PHE A O 1 ATOM 4936 C CB . PHE A 1 596 ? 15.533 55.787 -12.211 1.00 19.41 ? 629 PHE A CB 1 ATOM 4937 C CG . PHE A 1 596 ? 15.372 56.322 -10.831 1.00 17.27 ? 629 PHE A CG 1 ATOM 4938 C CD1 . PHE A 1 596 ? 14.181 56.150 -10.149 1.00 18.36 ? 629 PHE A CD1 1 ATOM 4939 C CD2 . PHE A 1 596 ? 16.442 56.937 -10.207 1.00 19.00 ? 629 PHE A CD2 1 ATOM 4940 C CE1 . PHE A 1 596 ? 14.044 56.664 -8.859 1.00 20.14 ? 629 PHE A CE1 1 ATOM 4941 C CE2 . PHE A 1 596 ? 16.307 57.479 -8.930 1.00 20.28 ? 629 PHE A CE2 1 ATOM 4942 C CZ . PHE A 1 596 ? 15.111 57.320 -8.245 1.00 21.13 ? 629 PHE A CZ 1 ATOM 4943 N N . SER A 1 597 ? 17.568 57.688 -13.746 1.00 18.25 ? 630 SER A N 1 ATOM 4944 C CA . SER A 1 597 ? 18.633 58.705 -13.638 1.00 18.38 ? 630 SER A CA 1 ATOM 4945 C C . SER A 1 597 ? 18.217 59.967 -14.390 1.00 19.16 ? 630 SER A C 1 ATOM 4946 O O . SER A 1 597 ? 18.438 61.080 -13.888 1.00 20.09 ? 630 SER A O 1 ATOM 4947 C CB . SER A 1 597 ? 19.894 58.109 -14.274 1.00 18.95 ? 630 SER A CB 1 ATOM 4948 O OG . SER A 1 597 ? 20.985 59.082 -14.252 1.00 21.79 ? 630 SER A OG 1 ATOM 4949 N N . GLU A 1 598 ? 17.613 59.813 -15.590 1.00 18.78 ? 631 GLU A N 1 ATOM 4950 C CA . GLU A 1 598 ? 17.100 60.953 -16.351 1.00 18.90 ? 631 GLU A CA 1 ATOM 4951 C C . GLU A 1 598 ? 16.018 61.706 -15.553 1.00 17.98 ? 631 GLU A C 1 ATOM 4952 O O . GLU A 1 598 ? 15.957 62.943 -15.509 1.00 20.69 ? 631 GLU A O 1 ATOM 4953 C CB . GLU A 1 598 ? 16.622 60.541 -17.774 1.00 21.60 ? 631 GLU A CB 1 ATOM 4954 C CG A GLU A 1 598 ? 17.755 59.904 -18.511 0.65 22.15 ? 631 GLU A CG 1 ATOM 4955 C CG B GLU A 1 598 ? 15.988 61.682 -18.498 0.35 21.83 ? 631 GLU A CG 1 ATOM 4956 C CD A GLU A 1 598 ? 17.363 59.303 -19.851 0.65 28.70 ? 631 GLU A CD 1 ATOM 4957 C CD B GLU A 1 598 ? 15.205 61.318 -19.742 0.35 26.19 ? 631 GLU A CD 1 ATOM 4958 O OE1 A GLU A 1 598 ? 18.242 58.677 -20.498 0.65 31.15 ? 631 GLU A OE1 1 ATOM 4959 O OE1 B GLU A 1 598 ? 15.629 61.781 -20.823 0.35 27.51 ? 631 GLU A OE1 1 ATOM 4960 O OE2 A GLU A 1 598 ? 16.202 59.496 -20.238 0.65 31.71 ? 631 GLU A OE2 1 ATOM 4961 O OE2 B GLU A 1 598 ? 14.147 60.637 -19.629 0.35 26.63 ? 631 GLU A OE2 1 ATOM 4962 N N . ALA A 1 599 ? 15.078 60.941 -14.962 1.00 18.09 ? 632 ALA A N 1 ATOM 4963 C CA . ALA A 1 599 ? 13.995 61.608 -14.251 1.00 18.27 ? 632 ALA A CA 1 ATOM 4964 C C . ALA A 1 599 ? 14.529 62.333 -12.994 1.00 18.30 ? 632 ALA A C 1 ATOM 4965 O O . ALA A 1 599 ? 13.999 63.409 -12.608 1.00 18.75 ? 632 ALA A O 1 ATOM 4966 C CB . ALA A 1 599 ? 12.959 60.558 -13.824 1.00 18.39 ? 632 ALA A CB 1 ATOM 4967 N N . ALA A 1 600 ? 15.535 61.750 -12.343 1.00 18.73 ? 633 ALA A N 1 ATOM 4968 C CA . ALA A 1 600 ? 16.067 62.408 -11.147 1.00 19.05 ? 633 ALA A CA 1 ATOM 4969 C C . ALA A 1 600 ? 16.851 63.718 -11.479 1.00 18.80 ? 633 ALA A C 1 ATOM 4970 O O . ALA A 1 600 ? 16.784 64.679 -10.739 1.00 19.36 ? 633 ALA A O 1 ATOM 4971 C CB . ALA A 1 600 ? 16.983 61.422 -10.438 1.00 19.65 ? 633 ALA A CB 1 ATOM 4972 N N . SER A 1 601 ? 17.551 63.686 -12.598 1.00 18.91 ? 634 SER A N 1 ATOM 4973 C CA . SER A 1 601 ? 18.330 64.850 -13.085 1.00 19.00 ? 634 SER A CA 1 ATOM 4974 C C . SER A 1 601 ? 17.316 65.939 -13.428 1.00 19.63 ? 634 SER A C 1 ATOM 4975 O O . SER A 1 601 ? 17.398 67.086 -12.943 1.00 19.49 ? 634 SER A O 1 ATOM 4976 C CB . SER A 1 601 ? 19.092 64.416 -14.329 1.00 18.62 ? 634 SER A CB 1 ATOM 4977 O OG . SER A 1 601 ? 19.610 65.622 -14.930 1.00 23.44 ? 634 SER A OG 1 ATOM 4978 N N . ASP A 1 602 ? 16.266 65.565 -14.173 1.00 19.03 ? 635 ASP A N 1 ATOM 4979 C CA A ASP A 1 602 ? 15.245 66.569 -14.572 0.60 19.01 ? 635 ASP A CA 1 ATOM 4980 C CA B ASP A 1 602 ? 15.262 66.530 -14.567 0.40 20.23 ? 635 ASP A CA 1 ATOM 4981 C C . ASP A 1 602 ? 14.532 67.128 -13.338 1.00 19.57 ? 635 ASP A C 1 ATOM 4982 O O . ASP A 1 602 ? 14.246 68.321 -13.259 1.00 20.09 ? 635 ASP A O 1 ATOM 4983 C CB A ASP A 1 602 ? 14.173 65.966 -15.511 0.60 20.30 ? 635 ASP A CB 1 ATOM 4984 C CB B ASP A 1 602 ? 14.290 65.809 -15.494 0.40 21.94 ? 635 ASP A CB 1 ATOM 4985 C CG A ASP A 1 602 ? 14.665 65.707 -16.897 0.60 21.81 ? 635 ASP A CG 1 ATOM 4986 C CG B ASP A 1 602 ? 13.307 66.722 -16.073 0.40 27.37 ? 635 ASP A CG 1 ATOM 4987 O OD1 A ASP A 1 602 ? 15.749 66.193 -17.284 0.60 21.42 ? 635 ASP A OD1 1 ATOM 4988 O OD1 B ASP A 1 602 ? 13.756 67.687 -16.719 0.40 34.20 ? 635 ASP A OD1 1 ATOM 4989 O OD2 A ASP A 1 602 ? 13.907 65.018 -17.616 0.60 23.37 ? 635 ASP A OD2 1 ATOM 4990 O OD2 B ASP A 1 602 ? 12.093 66.496 -15.878 0.40 33.31 ? 635 ASP A OD2 1 ATOM 4991 N N . PHE A 1 603 ? 14.230 66.245 -12.368 1.00 18.42 ? 636 PHE A N 1 ATOM 4992 C CA . PHE A 1 603 ? 13.563 66.669 -11.134 1.00 18.84 ? 636 PHE A CA 1 ATOM 4993 C C . PHE A 1 603 ? 14.398 67.748 -10.396 1.00 18.16 ? 636 PHE A C 1 ATOM 4994 O O . PHE A 1 603 ? 13.881 68.789 -10.021 1.00 18.63 ? 636 PHE A O 1 ATOM 4995 C CB . PHE A 1 603 ? 13.297 65.462 -10.219 1.00 19.62 ? 636 PHE A CB 1 ATOM 4996 C CG . PHE A 1 603 ? 12.669 65.889 -8.939 1.00 18.73 ? 636 PHE A CG 1 ATOM 4997 C CD1 . PHE A 1 603 ? 11.294 66.161 -8.897 1.00 19.05 ? 636 PHE A CD1 1 ATOM 4998 C CD2 . PHE A 1 603 ? 13.456 66.129 -7.801 1.00 19.92 ? 636 PHE A CD2 1 ATOM 4999 C CE1 . PHE A 1 603 ? 10.676 66.594 -7.678 1.00 19.88 ? 636 PHE A CE1 1 ATOM 5000 C CE2 . PHE A 1 603 ? 12.881 66.564 -6.667 1.00 18.72 ? 636 PHE A CE2 1 ATOM 5001 C CZ . PHE A 1 603 ? 11.513 66.806 -6.591 1.00 19.02 ? 636 PHE A CZ 1 ATOM 5002 N N . HIS A 1 604 ? 15.684 67.479 -10.236 1.00 18.20 ? 637 HIS A N 1 ATOM 5003 C CA . HIS A 1 604 ? 16.540 68.482 -9.539 1.00 17.99 ? 637 HIS A CA 1 ATOM 5004 C C . HIS A 1 604 ? 16.693 69.767 -10.349 1.00 17.70 ? 637 HIS A C 1 ATOM 5005 O O . HIS A 1 604 ? 16.749 70.842 -9.751 1.00 19.61 ? 637 HIS A O 1 ATOM 5006 C CB . HIS A 1 604 ? 17.867 67.803 -9.129 1.00 18.49 ? 637 HIS A CB 1 ATOM 5007 C CG . HIS A 1 604 ? 17.748 67.150 -7.795 1.00 18.45 ? 637 HIS A CG 1 ATOM 5008 N ND1 . HIS A 1 604 ? 17.474 65.819 -7.551 1.00 23.66 ? 637 HIS A ND1 1 ATOM 5009 C CD2 . HIS A 1 604 ? 17.751 67.768 -6.590 1.00 14.83 ? 637 HIS A CD2 1 ATOM 5010 C CE1 . HIS A 1 604 ? 17.304 65.645 -6.239 1.00 17.36 ? 637 HIS A CE1 1 ATOM 5011 N NE2 . HIS A 1 604 ? 17.493 66.806 -5.646 1.00 22.08 ? 637 HIS A NE2 1 ATOM 5012 N N . LYS A 1 605 ? 16.742 69.684 -11.674 1.00 18.33 ? 638 LYS A N 1 ATOM 5013 C CA . LYS A 1 605 ? 16.761 70.911 -12.482 1.00 19.53 ? 638 LYS A CA 1 ATOM 5014 C C . LYS A 1 605 ? 15.502 71.729 -12.210 1.00 19.24 ? 638 LYS A C 1 ATOM 5015 O O . LYS A 1 605 ? 15.583 72.954 -12.148 1.00 21.48 ? 638 LYS A O 1 ATOM 5016 C CB . LYS A 1 605 ? 16.849 70.538 -13.948 1.00 19.41 ? 638 LYS A CB 1 ATOM 5017 C CG . LYS A 1 605 ? 18.165 69.907 -14.350 1.00 21.09 ? 638 LYS A CG 1 ATOM 5018 C CD . LYS A 1 605 ? 18.138 69.388 -15.814 1.00 24.13 ? 638 LYS A CD 1 ATOM 5019 C CE . LYS A 1 605 ? 19.410 68.635 -16.074 1.00 25.36 ? 638 LYS A CE 1 ATOM 5020 N NZ . LYS A 1 605 ? 19.289 67.985 -17.441 1.00 32.22 ? 638 LYS A NZ 1 ATOM 5021 N N . ARG A 1 606 ? 14.345 71.070 -12.084 1.00 18.58 ? 639 ARG A N 1 ATOM 5022 C CA . ARG A 1 606 ? 13.124 71.827 -11.807 1.00 19.64 ? 639 ARG A CA 1 ATOM 5023 C C . ARG A 1 606 ? 13.102 72.332 -10.348 1.00 19.80 ? 639 ARG A C 1 ATOM 5024 O O . ARG A 1 606 ? 12.561 73.403 -10.040 1.00 20.67 ? 639 ARG A O 1 ATOM 5025 C CB . ARG A 1 606 ? 11.887 70.962 -12.098 1.00 20.79 ? 639 ARG A CB 1 ATOM 5026 C CG . ARG A 1 606 ? 11.741 70.684 -13.606 1.00 23.65 ? 639 ARG A CG 1 ATOM 5027 C CD . ARG A 1 606 ? 10.298 70.255 -13.951 1.00 25.98 ? 639 ARG A CD 1 ATOM 5028 N NE . ARG A 1 606 ? 9.810 69.188 -13.027 1.00 26.86 ? 639 ARG A NE 1 ATOM 5029 C CZ . ARG A 1 606 ? 10.162 67.905 -13.130 1.00 28.48 ? 639 ARG A CZ 1 ATOM 5030 N NH1 . ARG A 1 606 ? 10.917 67.495 -14.133 1.00 31.16 ? 639 ARG A NH1 1 ATOM 5031 N NH2 . ARG A 1 606 ? 9.708 67.019 -12.254 1.00 29.77 ? 639 ARG A NH2 1 ATOM 5032 N N . LEU A 1 607 ? 13.627 71.481 -9.455 1.00 18.86 ? 640 LEU A N 1 ATOM 5033 C CA . LEU A 1 607 ? 13.518 71.811 -8.034 1.00 18.81 ? 640 LEU A CA 1 ATOM 5034 C C . LEU A 1 607 ? 14.252 73.144 -7.721 1.00 18.97 ? 640 LEU A C 1 ATOM 5035 O O . LEU A 1 607 ? 13.726 73.975 -6.945 1.00 19.54 ? 640 LEU A O 1 ATOM 5036 C CB . LEU A 1 607 ? 14.098 70.670 -7.187 1.00 17.81 ? 640 LEU A CB 1 ATOM 5037 C CG . LEU A 1 607 ? 14.001 70.857 -5.677 1.00 20.30 ? 640 LEU A CG 1 ATOM 5038 C CD1 . LEU A 1 607 ? 12.528 70.906 -5.156 1.00 20.08 ? 640 LEU A CD1 1 ATOM 5039 C CD2 . LEU A 1 607 ? 14.745 69.713 -5.080 1.00 19.63 ? 640 LEU A CD2 1 ATOM 5040 N N . ILE A 1 608 ? 15.396 73.395 -8.367 1.00 18.73 ? 641 ILE A N 1 ATOM 5041 C CA . ILE A 1 608 ? 16.098 74.690 -8.071 1.00 19.58 ? 641 ILE A CA 1 ATOM 5042 C C . ILE A 1 608 ? 15.304 75.914 -8.566 1.00 19.50 ? 641 ILE A C 1 ATOM 5043 O O . ILE A 1 608 ? 15.614 77.042 -8.163 1.00 20.72 ? 641 ILE A O 1 ATOM 5044 C CB . ILE A 1 608 ? 17.545 74.773 -8.638 1.00 20.43 ? 641 ILE A CB 1 ATOM 5045 C CG1 . ILE A 1 608 ? 17.543 74.830 -10.169 1.00 21.31 ? 641 ILE A CG1 1 ATOM 5046 C CG2 . ILE A 1 608 ? 18.367 73.635 -8.076 1.00 21.40 ? 641 ILE A CG2 1 ATOM 5047 C CD1 . ILE A 1 608 ? 18.926 75.234 -10.769 1.00 21.64 ? 641 ILE A CD1 1 ATOM 5048 N N . GLN A 1 609 ? 14.320 75.693 -9.445 1.00 19.80 ? 642 GLN A N 1 ATOM 5049 C CA . GLN A 1 609 ? 13.504 76.771 -9.977 1.00 20.89 ? 642 GLN A CA 1 ATOM 5050 C C . GLN A 1 609 ? 12.241 77.042 -9.233 1.00 22.52 ? 642 GLN A C 1 ATOM 5051 O O . GLN A 1 609 ? 11.482 77.956 -9.596 1.00 24.00 ? 642 GLN A O 1 ATOM 5052 C CB . GLN A 1 609 ? 13.125 76.504 -11.428 1.00 22.47 ? 642 GLN A CB 1 ATOM 5053 C CG . GLN A 1 609 ? 14.390 76.318 -12.347 1.00 22.63 ? 642 GLN A CG 1 ATOM 5054 C CD . GLN A 1 609 ? 15.292 77.571 -12.492 1.00 25.27 ? 642 GLN A CD 1 ATOM 5055 O OE1 . GLN A 1 609 ? 16.483 77.457 -12.889 1.00 30.52 ? 642 GLN A OE1 1 ATOM 5056 N NE2 . GLN A 1 609 ? 14.725 78.754 -12.260 1.00 24.58 ? 642 GLN A NE2 1 ATOM 5057 N N . VAL A 1 610 ? 11.948 76.225 -8.210 1.00 20.85 ? 643 VAL A N 1 ATOM 5058 C CA . VAL A 1 610 ? 10.658 76.378 -7.547 1.00 21.57 ? 643 VAL A CA 1 ATOM 5059 C C . VAL A 1 610 ? 10.524 77.756 -6.929 1.00 22.22 ? 643 VAL A C 1 ATOM 5060 O O . VAL A 1 610 ? 11.490 78.307 -6.406 1.00 21.19 ? 643 VAL A O 1 ATOM 5061 C CB . VAL A 1 610 ? 10.474 75.267 -6.495 1.00 20.43 ? 643 VAL A CB 1 ATOM 5062 C CG1 . VAL A 1 610 ? 11.313 75.557 -5.264 1.00 22.73 ? 643 VAL A CG1 1 ATOM 5063 C CG2 . VAL A 1 610 ? 8.974 75.120 -6.131 1.00 22.73 ? 643 VAL A CG2 1 ATOM 5064 N N . ASP A 1 611 ? 9.318 78.315 -7.004 1.00 22.08 ? 644 ASP A N 1 ATOM 5065 C CA . ASP A 1 611 ? 9.069 79.617 -6.329 1.00 21.44 ? 644 ASP A CA 1 ATOM 5066 C C . ASP A 1 611 ? 8.837 79.385 -4.829 1.00 21.05 ? 644 ASP A C 1 ATOM 5067 O O . ASP A 1 611 ? 7.812 78.823 -4.401 1.00 20.18 ? 644 ASP A O 1 ATOM 5068 C CB . ASP A 1 611 ? 7.869 80.271 -6.995 1.00 21.89 ? 644 ASP A CB 1 ATOM 5069 C CG . ASP A 1 611 ? 7.488 81.587 -6.339 1.00 22.93 ? 644 ASP A CG 1 ATOM 5070 O OD1 . ASP A 1 611 ? 8.158 82.020 -5.352 1.00 23.05 ? 644 ASP A OD1 1 ATOM 5071 O OD2 . ASP A 1 611 ? 6.493 82.183 -6.822 1.00 28.67 ? 644 ASP A OD2 1 ATOM 5072 N N . LEU A 1 612 ? 9.847 79.711 -4.060 1.00 20.30 ? 645 LEU A N 1 ATOM 5073 C CA . LEU A 1 612 ? 9.833 79.437 -2.646 1.00 21.75 ? 645 LEU A CA 1 ATOM 5074 C C . LEU A 1 612 ? 8.731 80.229 -1.950 1.00 20.58 ? 645 LEU A C 1 ATOM 5075 O O . LEU A 1 612 ? 8.392 79.877 -0.805 1.00 21.71 ? 645 LEU A O 1 ATOM 5076 C CB . LEU A 1 612 ? 11.195 79.724 -1.987 1.00 20.82 ? 645 LEU A CB 1 ATOM 5077 C CG . LEU A 1 612 ? 12.286 78.778 -2.525 1.00 20.34 ? 645 LEU A CG 1 ATOM 5078 C CD1 . LEU A 1 612 ? 13.623 79.375 -2.047 1.00 22.95 ? 645 LEU A CD1 1 ATOM 5079 C CD2 . LEU A 1 612 ? 12.187 77.353 -2.026 1.00 22.41 ? 645 LEU A CD2 1 ATOM 5080 N N . ASN A 1 613 ? 8.206 81.261 -2.613 1.00 21.59 ? 646 ASN A N 1 ATOM 5081 C CA . ASN A 1 613 ? 7.131 82.012 -1.998 1.00 23.28 ? 646 ASN A CA 1 ATOM 5082 C C . ASN A 1 613 ? 5.753 81.548 -2.398 1.00 22.29 ? 646 ASN A C 1 ATOM 5083 O O . ASN A 1 613 ? 4.764 82.238 -2.076 1.00 23.70 ? 646 ASN A O 1 ATOM 5084 C CB . ASN A 1 613 ? 7.237 83.510 -2.352 1.00 24.59 ? 646 ASN A CB 1 ATOM 5085 C CG . ASN A 1 613 ? 8.455 84.134 -1.783 1.00 30.95 ? 646 ASN A CG 1 ATOM 5086 O OD1 . ASN A 1 613 ? 8.802 83.884 -0.620 1.00 35.85 ? 646 ASN A OD1 1 ATOM 5087 N ND2 . ASN A 1 613 ? 9.137 84.956 -2.585 1.00 34.99 ? 646 ASN A ND2 1 ATOM 5088 N N . ASN A 1 614 ? 5.669 80.422 -3.124 1.00 20.58 ? 647 ASN A N 1 ATOM 5089 C CA . ASN A 1 614 ? 4.373 79.876 -3.572 1.00 19.78 ? 647 ASN A CA 1 ATOM 5090 C C . ASN A 1 614 ? 4.159 78.559 -2.789 1.00 20.71 ? 647 ASN A C 1 ATOM 5091 O O . ASN A 1 614 ? 4.803 77.519 -3.113 1.00 19.81 ? 647 ASN A O 1 ATOM 5092 C CB . ASN A 1 614 ? 4.447 79.631 -5.068 1.00 20.18 ? 647 ASN A CB 1 ATOM 5093 C CG . ASN A 1 614 ? 3.182 79.064 -5.625 1.00 23.48 ? 647 ASN A CG 1 ATOM 5094 O OD1 . ASN A 1 614 ? 2.471 78.321 -4.943 1.00 23.18 ? 647 ASN A OD1 1 ATOM 5095 N ND2 . ASN A 1 614 ? 2.934 79.321 -6.903 1.00 25.11 ? 647 ASN A ND2 1 ATOM 5096 N N . PRO A 1 615 ? 3.329 78.610 -1.750 1.00 19.82 ? 648 PRO A N 1 ATOM 5097 C CA . PRO A 1 615 ? 3.294 77.416 -0.871 1.00 19.40 ? 648 PRO A CA 1 ATOM 5098 C C . PRO A 1 615 ? 2.851 76.123 -1.541 1.00 20.86 ? 648 PRO A C 1 ATOM 5099 O O . PRO A 1 615 ? 3.334 75.062 -1.174 1.00 19.74 ? 648 PRO A O 1 ATOM 5100 C CB . PRO A 1 615 ? 2.300 77.794 0.232 1.00 20.05 ? 648 PRO A CB 1 ATOM 5101 C CG . PRO A 1 615 ? 2.320 79.299 0.257 1.00 24.42 ? 648 PRO A CG 1 ATOM 5102 C CD . PRO A 1 615 ? 2.613 79.774 -1.160 1.00 21.79 ? 648 PRO A CD 1 ATOM 5103 N N . ILE A 1 616 ? 1.919 76.214 -2.448 1.00 19.27 ? 649 ILE A N 1 ATOM 5104 C CA . ILE A 1 616 ? 1.483 74.980 -3.134 1.00 19.80 ? 649 ILE A CA 1 ATOM 5105 C C . ILE A 1 616 ? 2.568 74.480 -4.060 1.00 19.63 ? 649 ILE A C 1 ATOM 5106 O O . ILE A 1 616 ? 2.780 73.263 -4.163 1.00 18.13 ? 649 ILE A O 1 ATOM 5107 C CB . ILE A 1 616 ? 0.137 75.174 -3.868 1.00 20.28 ? 649 ILE A CB 1 ATOM 5108 C CG1 . ILE A 1 616 ? -0.945 75.589 -2.870 1.00 22.91 ? 649 ILE A CG1 1 ATOM 5109 C CG2 . ILE A 1 616 ? -0.265 73.864 -4.660 1.00 23.18 ? 649 ILE A CG2 1 ATOM 5110 C CD1 . ILE A 1 616 ? -1.187 74.473 -1.857 1.00 24.55 ? 649 ILE A CD1 1 ATOM 5111 N N . ALA A 1 617 ? 3.292 75.390 -4.745 1.00 18.88 ? 650 ALA A N 1 ATOM 5112 C CA . ALA A 1 617 ? 4.415 74.882 -5.567 1.00 19.05 ? 650 ALA A CA 1 ATOM 5113 C C . ALA A 1 617 ? 5.442 74.135 -4.726 1.00 18.80 ? 650 ALA A C 1 ATOM 5114 O O . ALA A 1 617 ? 5.958 73.094 -5.097 1.00 19.20 ? 650 ALA A O 1 ATOM 5115 C CB . ALA A 1 617 ? 5.070 76.033 -6.310 1.00 20.09 ? 650 ALA A CB 1 ATOM 5116 N N . VAL A 1 618 ? 5.709 74.680 -3.553 1.00 18.34 ? 651 VAL A N 1 ATOM 5117 C CA . VAL A 1 618 ? 6.702 74.088 -2.641 1.00 17.44 ? 651 VAL A CA 1 ATOM 5118 C C . VAL A 1 618 ? 6.144 72.740 -2.127 1.00 17.47 ? 651 VAL A C 1 ATOM 5119 O O . VAL A 1 618 ? 6.860 71.745 -2.128 1.00 18.69 ? 651 VAL A O 1 ATOM 5120 C CB . VAL A 1 618 ? 6.944 75.029 -1.477 1.00 18.91 ? 651 VAL A CB 1 ATOM 5121 C CG1 . VAL A 1 618 ? 7.760 74.343 -0.362 1.00 21.20 ? 651 VAL A CG1 1 ATOM 5122 C CG2 . VAL A 1 618 ? 7.798 76.227 -2.042 1.00 19.51 ? 651 VAL A CG2 1 ATOM 5123 N N . ARG A 1 619 ? 4.896 72.745 -1.708 1.00 17.37 ? 652 ARG A N 1 ATOM 5124 C CA . ARG A 1 619 ? 4.289 71.513 -1.156 1.00 17.24 ? 652 ARG A CA 1 ATOM 5125 C C . ARG A 1 619 ? 4.228 70.386 -2.226 1.00 17.10 ? 652 ARG A C 1 ATOM 5126 O O . ARG A 1 619 ? 4.501 69.190 -1.898 1.00 18.21 ? 652 ARG A O 1 ATOM 5127 C CB . ARG A 1 619 ? 2.842 71.849 -0.731 1.00 17.43 ? 652 ARG A CB 1 ATOM 5128 C CG . ARG A 1 619 ? 2.100 70.651 -0.131 1.00 19.04 ? 652 ARG A CG 1 ATOM 5129 C CD . ARG A 1 619 ? 2.572 70.193 1.280 1.00 21.86 ? 652 ARG A CD 1 ATOM 5130 N NE . ARG A 1 619 ? 1.527 69.232 1.735 1.00 19.28 ? 652 ARG A NE 1 ATOM 5131 C CZ . ARG A 1 619 ? 1.135 69.070 2.981 1.00 18.81 ? 652 ARG A CZ 1 ATOM 5132 N NH1 . ARG A 1 619 ? 0.084 68.254 3.237 1.00 18.22 ? 652 ARG A NH1 1 ATOM 5133 N NH2 . ARG A 1 619 ? 1.771 69.649 4.014 1.00 18.02 ? 652 ARG A NH2 1 ATOM 5134 N N . MET A 1 620 ? 3.937 70.711 -3.501 1.00 17.48 ? 653 MET A N 1 ATOM 5135 C CA . MET A 1 620 ? 3.896 69.644 -4.509 1.00 17.96 ? 653 MET A CA 1 ATOM 5136 C C . MET A 1 620 ? 5.267 69.017 -4.700 1.00 18.37 ? 653 MET A C 1 ATOM 5137 O O . MET A 1 620 ? 5.380 67.782 -4.836 1.00 18.56 ? 653 MET A O 1 ATOM 5138 C CB . MET A 1 620 ? 3.347 70.190 -5.828 1.00 18.66 ? 653 MET A CB 1 ATOM 5139 C CG . MET A 1 620 ? 1.880 70.595 -5.721 1.00 20.16 ? 653 MET A CG 1 ATOM 5140 S SD . MET A 1 620 ? 1.165 71.016 -7.349 1.00 20.75 ? 653 MET A SD 1 ATOM 5141 C CE . MET A 1 620 ? 2.113 72.523 -7.786 1.00 21.26 ? 653 MET A CE 1 ATOM 5142 N N . MET A 1 621 ? 6.345 69.873 -4.714 1.00 18.05 ? 654 MET A N 1 ATOM 5143 C CA . MET A 1 621 ? 7.642 69.267 -4.875 1.00 18.11 ? 654 MET A CA 1 ATOM 5144 C C . MET A 1 621 ? 8.075 68.501 -3.616 1.00 18.75 ? 654 MET A C 1 ATOM 5145 O O . MET A 1 621 ? 8.713 67.453 -3.701 1.00 18.93 ? 654 MET A O 1 ATOM 5146 C CB . MET A 1 621 ? 8.708 70.275 -5.434 1.00 21.84 ? 654 MET A CB 1 ATOM 5147 C CG A MET A 1 621 ? 8.212 71.080 -6.641 0.60 21.11 ? 654 MET A CG 1 ATOM 5148 C CG B MET A 1 621 ? 8.759 70.270 -7.089 0.40 22.79 ? 654 MET A CG 1 ATOM 5149 S SD A MET A 1 621 ? 9.577 71.607 -7.748 0.60 21.72 ? 654 MET A SD 1 ATOM 5150 S SD B MET A 1 621 ? 10.315 70.172 -7.969 0.40 36.65 ? 654 MET A SD 1 ATOM 5151 C CE A MET A 1 621 ? 8.901 71.397 -9.314 0.60 28.74 ? 654 MET A CE 1 ATOM 5152 C CE B MET A 1 621 ? 9.816 69.601 -9.565 0.40 35.16 ? 654 MET A CE 1 ATOM 5153 N N . ASN A 1 622 ? 7.701 69.059 -2.461 1.00 17.06 ? 655 ASN A N 1 ATOM 5154 C CA . ASN A 1 622 ? 8.004 68.309 -1.200 1.00 17.19 ? 655 ASN A CA 1 ATOM 5155 C C . ASN A 1 622 ? 7.287 66.978 -1.184 1.00 18.65 ? 655 ASN A C 1 ATOM 5156 O O . ASN A 1 622 ? 7.858 65.983 -0.703 1.00 18.63 ? 655 ASN A O 1 ATOM 5157 C CB . ASN A 1 622 ? 7.634 69.100 0.037 1.00 16.78 ? 655 ASN A CB 1 ATOM 5158 C CG . ASN A 1 622 ? 8.756 70.090 0.423 1.00 17.85 ? 655 ASN A CG 1 ATOM 5159 O OD1 . ASN A 1 622 ? 9.947 69.788 0.179 1.00 19.28 ? 655 ASN A OD1 1 ATOM 5160 N ND2 . ASN A 1 622 ? 8.399 71.186 1.082 1.00 18.58 ? 655 ASN A ND2 1 ATOM 5161 N N . ASP A 1 623 ? 6.057 66.924 -1.708 1.00 17.88 ? 656 ASP A N 1 ATOM 5162 C CA . ASP A 1 623 ? 5.353 65.615 -1.754 1.00 17.06 ? 656 ASP A CA 1 ATOM 5163 C C . ASP A 1 623 ? 6.121 64.636 -2.611 1.00 17.90 ? 656 ASP A C 1 ATOM 5164 O O . ASP A 1 623 ? 6.211 63.433 -2.296 1.00 18.43 ? 656 ASP A O 1 ATOM 5165 C CB . ASP A 1 623 ? 3.928 65.765 -2.262 1.00 18.62 ? 656 ASP A CB 1 ATOM 5166 C CG . ASP A 1 623 ? 2.948 66.275 -1.185 1.00 19.18 ? 656 ASP A CG 1 ATOM 5167 O OD1 . ASP A 1 623 ? 3.378 66.491 -0.028 1.00 19.40 ? 656 ASP A OD1 1 ATOM 5168 O OD2 . ASP A 1 623 ? 1.738 66.412 -1.553 1.00 21.26 ? 656 ASP A OD2 1 ATOM 5169 N N . GLN A 1 624 ? 6.690 65.137 -3.734 1.00 17.08 ? 657 GLN A N 1 ATOM 5170 C CA . GLN A 1 624 ? 7.450 64.197 -4.592 1.00 15.97 ? 657 GLN A CA 1 ATOM 5171 C C . GLN A 1 624 ? 8.712 63.678 -3.845 1.00 17.39 ? 657 GLN A C 1 ATOM 5172 O O . GLN A 1 624 ? 9.101 62.492 -3.951 1.00 17.66 ? 657 GLN A O 1 ATOM 5173 C CB . GLN A 1 624 ? 7.874 64.871 -5.898 1.00 16.87 ? 657 GLN A CB 1 ATOM 5174 C CG . GLN A 1 624 ? 6.668 65.042 -6.782 1.00 18.33 ? 657 GLN A CG 1 ATOM 5175 C CD . GLN A 1 624 ? 7.048 65.747 -8.062 1.00 19.48 ? 657 GLN A CD 1 ATOM 5176 O OE1 . GLN A 1 624 ? 7.336 66.963 -8.060 1.00 21.76 ? 657 GLN A OE1 1 ATOM 5177 N NE2 . GLN A 1 624 ? 7.049 64.990 -9.185 1.00 19.28 ? 657 GLN A NE2 1 ATOM 5178 N N . LEU A 1 625 ? 9.399 64.614 -3.127 1.00 17.00 ? 658 LEU A N 1 ATOM 5179 C CA . LEU A 1 625 ? 10.591 64.154 -2.353 1.00 17.50 ? 658 LEU A CA 1 ATOM 5180 C C . LEU A 1 625 ? 10.166 63.159 -1.259 1.00 17.41 ? 658 LEU A C 1 ATOM 5181 O O . LEU A 1 625 ? 10.858 62.157 -1.033 1.00 18.34 ? 658 LEU A O 1 ATOM 5182 C CB . LEU A 1 625 ? 11.243 65.397 -1.691 1.00 17.19 ? 658 LEU A CB 1 ATOM 5183 C CG . LEU A 1 625 ? 11.985 66.317 -2.725 1.00 18.66 ? 658 LEU A CG 1 ATOM 5184 C CD1 . LEU A 1 625 ? 12.158 67.745 -2.175 1.00 20.07 ? 658 LEU A CD1 1 ATOM 5185 C CD2 . LEU A 1 625 ? 13.369 65.694 -2.991 1.00 19.82 ? 658 LEU A CD2 1 ATOM 5186 N N . MET A 1 626 ? 9.060 63.447 -0.574 1.00 16.76 ? 659 MET A N 1 ATOM 5187 C CA . MET A 1 626 ? 8.598 62.558 0.524 1.00 17.53 ? 659 MET A CA 1 ATOM 5188 C C . MET A 1 626 ? 8.154 61.180 -0.011 1.00 18.15 ? 659 MET A C 1 ATOM 5189 O O . MET A 1 626 ? 8.353 60.159 0.641 1.00 18.20 ? 659 MET A O 1 ATOM 5190 C CB . MET A 1 626 ? 7.414 63.274 1.217 1.00 16.78 ? 659 MET A CB 1 ATOM 5191 C CG . MET A 1 626 ? 6.801 62.368 2.266 1.00 17.82 ? 659 MET A CG 1 ATOM 5192 S SD . MET A 1 626 ? 5.305 63.219 2.972 1.00 20.01 ? 659 MET A SD 1 ATOM 5193 C CE . MET A 1 626 ? 4.067 62.950 1.659 1.00 20.87 ? 659 MET A CE 1 ATOM 5194 N N . LEU A 1 627 ? 7.518 61.149 -1.184 1.00 16.72 ? 660 LEU A N 1 ATOM 5195 C CA . LEU A 1 627 ? 6.897 59.880 -1.642 1.00 16.96 ? 660 LEU A CA 1 ATOM 5196 C C . LEU A 1 627 ? 7.804 59.030 -2.514 1.00 17.87 ? 660 LEU A C 1 ATOM 5197 O O . LEU A 1 627 ? 7.449 57.941 -2.888 1.00 19.13 ? 660 LEU A O 1 ATOM 5198 C CB . LEU A 1 627 ? 5.609 60.246 -2.347 1.00 17.75 ? 660 LEU A CB 1 ATOM 5199 C CG . LEU A 1 627 ? 4.545 60.806 -1.383 1.00 20.03 ? 660 LEU A CG 1 ATOM 5200 C CD1 . LEU A 1 627 ? 3.412 61.365 -2.212 1.00 22.04 ? 660 LEU A CD1 1 ATOM 5201 C CD2 . LEU A 1 627 ? 3.993 59.659 -0.499 1.00 19.80 ? 660 LEU A CD2 1 ATOM 5202 N N . LEU A 1 628 ? 9.011 59.544 -2.805 1.00 17.65 ? 661 LEU A N 1 ATOM 5203 C CA . LEU A 1 628 ? 9.930 58.782 -3.679 1.00 17.64 ? 661 LEU A CA 1 ATOM 5204 C C . LEU A 1 628 ? 10.289 57.438 -3.022 1.00 18.39 ? 661 LEU A C 1 ATOM 5205 O O . LEU A 1 628 ? 10.192 56.404 -3.693 1.00 18.94 ? 661 LEU A O 1 ATOM 5206 C CB . LEU A 1 628 ? 11.182 59.663 -4.002 1.00 17.65 ? 661 LEU A CB 1 ATOM 5207 C CG . LEU A 1 628 ? 12.160 59.079 -5.043 1.00 18.28 ? 661 LEU A CG 1 ATOM 5208 C CD1 . LEU A 1 628 ? 13.039 58.009 -4.395 1.00 20.37 ? 661 LEU A CD1 1 ATOM 5209 C CD2 . LEU A 1 628 ? 11.436 58.574 -6.316 1.00 19.73 ? 661 LEU A CD2 1 ATOM 5210 N N . GLU A 1 629 ? 10.672 57.431 -1.729 1.00 18.46 ? 662 GLU A N 1 ATOM 5211 C CA . GLU A 1 629 ? 11.068 56.150 -1.099 1.00 18.23 ? 662 GLU A CA 1 ATOM 5212 C C . GLU A 1 629 ? 9.859 55.195 -1.116 1.00 17.67 ? 662 GLU A C 1 ATOM 5213 O O . GLU A 1 629 ? 10.013 53.957 -1.192 1.00 18.96 ? 662 GLU A O 1 ATOM 5214 C CB . GLU A 1 629 ? 11.512 56.436 0.351 1.00 19.09 ? 662 GLU A CB 1 ATOM 5215 C CG . GLU A 1 629 ? 12.260 55.256 0.996 1.00 18.90 ? 662 GLU A CG 1 ATOM 5216 C CD . GLU A 1 629 ? 13.691 55.102 0.479 1.00 18.59 ? 662 GLU A CD 1 ATOM 5217 O OE1 . GLU A 1 629 ? 14.511 55.961 0.826 1.00 20.27 ? 662 GLU A OE1 1 ATOM 5218 O OE2 . GLU A 1 629 ? 13.971 54.083 -0.247 1.00 19.81 ? 662 GLU A OE2 1 ATOM 5219 N N . ARG A 1 630 ? 8.645 55.764 -1.012 1.00 18.17 ? 663 ARG A N 1 ATOM 5220 C CA . ARG A 1 630 ? 7.452 54.926 -0.953 1.00 17.59 ? 663 ARG A CA 1 ATOM 5221 C C . ARG A 1 630 ? 7.257 54.156 -2.246 1.00 17.57 ? 663 ARG A C 1 ATOM 5222 O O . ARG A 1 630 ? 6.561 53.069 -2.301 1.00 18.68 ? 663 ARG A O 1 ATOM 5223 C CB . ARG A 1 630 ? 6.165 55.765 -0.821 1.00 19.50 ? 663 ARG A CB 1 ATOM 5224 C CG . ARG A 1 630 ? 6.133 56.649 0.334 1.00 21.79 ? 663 ARG A CG 1 ATOM 5225 C CD . ARG A 1 630 ? 5.964 55.861 1.695 1.00 18.22 ? 663 ARG A CD 1 ATOM 5226 N NE . ARG A 1 630 ? 5.618 56.892 2.623 1.00 19.86 ? 663 ARG A NE 1 ATOM 5227 C CZ . ARG A 1 630 ? 6.457 57.858 3.008 1.00 18.72 ? 663 ARG A CZ 1 ATOM 5228 N NH1 . ARG A 1 630 ? 7.766 57.835 2.808 1.00 18.31 ? 663 ARG A NH1 1 ATOM 5229 N NH2 . ARG A 1 630 ? 5.912 58.935 3.619 1.00 19.39 ? 663 ARG A NH2 1 ATOM 5230 N N . ALA A 1 631 ? 7.746 54.712 -3.348 1.00 17.77 ? 664 ALA A N 1 ATOM 5231 C CA . ALA A 1 631 ? 7.478 54.077 -4.654 1.00 17.11 ? 664 ALA A CA 1 ATOM 5232 C C . ALA A 1 631 ? 8.135 52.712 -4.722 1.00 19.52 ? 664 ALA A C 1 ATOM 5233 O O . ALA A 1 631 ? 7.722 51.861 -5.472 1.00 20.67 ? 664 ALA A O 1 ATOM 5234 C CB . ALA A 1 631 ? 7.985 54.969 -5.780 1.00 18.16 ? 664 ALA A CB 1 ATOM 5235 N N . PHE A 1 632 ? 9.164 52.466 -3.941 1.00 17.60 ? 665 PHE A N 1 ATOM 5236 C CA . PHE A 1 632 ? 9.874 51.191 -3.955 1.00 17.19 ? 665 PHE A CA 1 ATOM 5237 C C . PHE A 1 632 ? 9.183 50.095 -3.115 1.00 19.10 ? 665 PHE A C 1 ATOM 5238 O O . PHE A 1 632 ? 9.699 48.952 -3.116 1.00 18.55 ? 665 PHE A O 1 ATOM 5239 C CB . PHE A 1 632 ? 11.317 51.410 -3.441 1.00 18.18 ? 665 PHE A CB 1 ATOM 5240 C CG . PHE A 1 632 ? 12.132 52.291 -4.317 1.00 18.50 ? 665 PHE A CG 1 ATOM 5241 C CD1 . PHE A 1 632 ? 12.392 51.904 -5.634 1.00 18.85 ? 665 PHE A CD1 1 ATOM 5242 C CD2 . PHE A 1 632 ? 12.672 53.461 -3.824 1.00 19.97 ? 665 PHE A CD2 1 ATOM 5243 C CE1 . PHE A 1 632 ? 13.117 52.725 -6.523 1.00 18.69 ? 665 PHE A CE1 1 ATOM 5244 C CE2 . PHE A 1 632 ? 13.441 54.280 -4.668 1.00 21.35 ? 665 PHE A CE2 1 ATOM 5245 C CZ . PHE A 1 632 ? 13.670 53.935 -5.987 1.00 21.09 ? 665 PHE A CZ 1 ATOM 5246 N N . ILE A 1 633 ? 8.069 50.411 -2.488 1.00 17.13 ? 666 ILE A N 1 ATOM 5247 C CA . ILE A 1 633 ? 7.351 49.433 -1.650 1.00 17.34 ? 666 ILE A CA 1 ATOM 5248 C C . ILE A 1 633 ? 6.326 48.706 -2.472 1.00 20.13 ? 666 ILE A C 1 ATOM 5249 O O . ILE A 1 633 ? 5.395 49.324 -3.059 1.00 19.85 ? 666 ILE A O 1 ATOM 5250 C CB . ILE A 1 633 ? 6.639 50.220 -0.525 1.00 17.40 ? 666 ILE A CB 1 ATOM 5251 C CG1 . ILE A 1 633 ? 7.653 50.854 0.425 1.00 20.55 ? 666 ILE A CG1 1 ATOM 5252 C CG2 . ILE A 1 633 ? 5.662 49.311 0.297 1.00 20.13 ? 666 ILE A CG2 1 ATOM 5253 C CD1 . ILE A 1 633 ? 8.609 49.846 1.112 1.00 20.68 ? 666 ILE A CD1 1 ATOM 5254 N N . ASP A 1 634 ? 6.425 47.378 -2.486 1.00 18.69 ? 667 ASP A N 1 ATOM 5255 C CA . ASP A 1 634 ? 5.464 46.526 -3.223 1.00 18.65 ? 667 ASP A CA 1 ATOM 5256 C C . ASP A 1 634 ? 4.551 45.844 -2.241 1.00 18.68 ? 667 ASP A C 1 ATOM 5257 O O . ASP A 1 634 ? 5.029 45.118 -1.361 1.00 19.42 ? 667 ASP A O 1 ATOM 5258 C CB . ASP A 1 634 ? 6.303 45.454 -3.982 1.00 17.99 ? 667 ASP A CB 1 ATOM 5259 C CG . ASP A 1 634 ? 5.462 44.608 -4.948 1.00 19.77 ? 667 ASP A CG 1 ATOM 5260 O OD1 . ASP A 1 634 ? 4.211 44.501 -4.742 1.00 19.08 ? 667 ASP A OD1 1 ATOM 5261 O OD2 . ASP A 1 634 ? 6.088 44.014 -5.879 1.00 19.84 ? 667 ASP A OD2 1 ATOM 5262 N N . PRO A 1 635 ? 3.234 46.101 -2.283 1.00 19.51 ? 668 PRO A N 1 ATOM 5263 C CA . PRO A 1 635 ? 2.356 45.541 -1.277 1.00 20.94 ? 668 PRO A CA 1 ATOM 5264 C C . PRO A 1 635 ? 2.311 44.026 -1.336 1.00 20.88 ? 668 PRO A C 1 ATOM 5265 O O . PRO A 1 635 ? 1.819 43.367 -0.373 1.00 23.88 ? 668 PRO A O 1 ATOM 5266 C CB . PRO A 1 635 ? 0.962 46.099 -1.658 1.00 21.42 ? 668 PRO A CB 1 ATOM 5267 C CG . PRO A 1 635 ? 1.048 46.463 -3.063 1.00 21.90 ? 668 PRO A CG 1 ATOM 5268 C CD . PRO A 1 635 ? 2.529 46.910 -3.296 1.00 20.56 ? 668 PRO A CD 1 ATOM 5269 N N . LEU A 1 636 ? 2.773 43.403 -2.453 1.00 19.23 ? 669 LEU A N 1 ATOM 5270 C CA . LEU A 1 636 ? 2.737 41.935 -2.537 1.00 20.03 ? 669 LEU A CA 1 ATOM 5271 C C . LEU A 1 636 ? 3.912 41.366 -1.684 1.00 20.23 ? 669 LEU A C 1 ATOM 5272 O O . LEU A 1 636 ? 3.964 40.161 -1.497 1.00 19.79 ? 669 LEU A O 1 ATOM 5273 C CB . LEU A 1 636 ? 2.764 41.485 -4.002 1.00 20.29 ? 669 LEU A CB 1 ATOM 5274 C CG . LEU A 1 636 ? 1.547 41.961 -4.866 1.00 20.60 ? 669 LEU A CG 1 ATOM 5275 C CD1 . LEU A 1 636 ? 1.679 41.296 -6.200 1.00 20.55 ? 669 LEU A CD1 1 ATOM 5276 C CD2 . LEU A 1 636 ? 0.222 41.560 -4.173 1.00 21.03 ? 669 LEU A CD2 1 ATOM 5277 N N . GLY A 1 637 ? 4.882 42.206 -1.310 1.00 19.79 ? 670 GLY A N 1 ATOM 5278 C CA . GLY A 1 637 ? 6.041 41.674 -0.536 1.00 19.21 ? 670 GLY A CA 1 ATOM 5279 C C . GLY A 1 637 ? 6.984 40.875 -1.371 1.00 21.03 ? 670 GLY A C 1 ATOM 5280 O O . GLY A 1 637 ? 6.918 40.829 -2.603 1.00 22.36 ? 670 GLY A O 1 ATOM 5281 N N . LEU A 1 638 ? 7.872 40.194 -0.641 1.00 20.53 ? 671 LEU A N 1 ATOM 5282 C CA . LEU A 1 638 ? 8.853 39.293 -1.274 1.00 23.07 ? 671 LEU A CA 1 ATOM 5283 C C . LEU A 1 638 ? 8.402 37.864 -1.025 1.00 22.49 ? 671 LEU A C 1 ATOM 5284 O O . LEU A 1 638 ? 7.612 37.590 -0.140 1.00 22.91 ? 671 LEU A O 1 ATOM 5285 C CB . LEU A 1 638 ? 10.251 39.556 -0.676 1.00 22.19 ? 671 LEU A CB 1 ATOM 5286 C CG . LEU A 1 638 ? 10.847 40.878 -1.196 1.00 26.36 ? 671 LEU A CG 1 ATOM 5287 C CD1 . LEU A 1 638 ? 12.032 41.285 -0.337 1.00 31.46 ? 671 LEU A CD1 1 ATOM 5288 C CD2 . LEU A 1 638 ? 11.226 40.842 -2.690 1.00 27.39 ? 671 LEU A CD2 1 ATOM 5289 N N . PRO A 1 639 ? 8.911 36.894 -1.830 1.00 23.85 ? 672 PRO A N 1 ATOM 5290 C CA . PRO A 1 639 ? 8.520 35.513 -1.671 1.00 25.72 ? 672 PRO A CA 1 ATOM 5291 C C . PRO A 1 639 ? 8.621 35.029 -0.229 1.00 24.23 ? 672 PRO A C 1 ATOM 5292 O O . PRO A 1 639 ? 9.699 35.112 0.377 1.00 26.81 ? 672 PRO A O 1 ATOM 5293 C CB . PRO A 1 639 ? 9.572 34.769 -2.552 1.00 25.75 ? 672 PRO A CB 1 ATOM 5294 C CG . PRO A 1 639 ? 9.817 35.815 -3.671 1.00 27.30 ? 672 PRO A CG 1 ATOM 5295 C CD . PRO A 1 639 ? 9.888 37.123 -2.909 1.00 26.25 ? 672 PRO A CD 1 ATOM 5296 N N . GLY A 1 640 ? 7.500 34.599 0.308 1.00 24.17 ? 673 GLY A N 1 ATOM 5297 C CA . GLY A 1 640 ? 7.447 34.052 1.660 1.00 24.39 ? 673 GLY A CA 1 ATOM 5298 C C . GLY A 1 640 ? 7.569 35.126 2.750 1.00 24.59 ? 673 GLY A C 1 ATOM 5299 O O . GLY A 1 640 ? 7.617 34.770 3.935 1.00 24.92 ? 673 GLY A O 1 ATOM 5300 N N . LYS A 1 641 ? 7.588 36.411 2.359 1.00 23.38 ? 674 LYS A N 1 ATOM 5301 C CA . LYS A 1 641 ? 7.854 37.476 3.355 1.00 21.02 ? 674 LYS A CA 1 ATOM 5302 C C . LYS A 1 641 ? 6.941 38.674 3.089 1.00 19.65 ? 674 LYS A C 1 ATOM 5303 O O . LYS A 1 641 ? 7.352 39.672 2.431 1.00 21.27 ? 674 LYS A O 1 ATOM 5304 C CB . LYS A 1 641 ? 9.314 37.864 3.326 1.00 21.29 ? 674 LYS A CB 1 ATOM 5305 C CG . LYS A 1 641 ? 10.256 36.631 3.575 1.00 22.75 ? 674 LYS A CG 1 ATOM 5306 C CD . LYS A 1 641 ? 11.653 37.083 3.600 1.00 26.46 ? 674 LYS A CD 1 ATOM 5307 C CE . LYS A 1 641 ? 12.509 35.848 3.870 1.00 33.98 ? 674 LYS A CE 1 ATOM 5308 N NZ . LYS A 1 641 ? 13.840 36.144 3.255 1.00 43.52 ? 674 LYS A NZ 1 ATOM 5309 N N . LEU A 1 642 ? 5.732 38.580 3.602 1.00 19.15 ? 675 LEU A N 1 ATOM 5310 C CA . LEU A 1 642 ? 4.727 39.619 3.343 1.00 19.51 ? 675 LEU A CA 1 ATOM 5311 C C . LEU A 1 642 ? 5.164 40.987 3.828 1.00 21.77 ? 675 LEU A C 1 ATOM 5312 O O . LEU A 1 642 ? 4.573 42.003 3.376 1.00 21.78 ? 675 LEU A O 1 ATOM 5313 C CB . LEU A 1 642 ? 3.424 39.269 4.092 1.00 20.11 ? 675 LEU A CB 1 ATOM 5314 C CG . LEU A 1 642 ? 2.674 38.066 3.501 1.00 22.05 ? 675 LEU A CG 1 ATOM 5315 C CD1 . LEU A 1 642 ? 1.665 37.525 4.511 1.00 27.01 ? 675 LEU A CD1 1 ATOM 5316 C CD2 . LEU A 1 642 ? 1.985 38.445 2.205 1.00 24.34 ? 675 LEU A CD2 1 ATOM 5317 N N . PHE A 1 643 ? 6.072 41.065 4.811 1.00 19.85 ? 676 PHE A N 1 ATOM 5318 C CA . PHE A 1 643 ? 6.322 42.333 5.504 1.00 19.34 ? 676 PHE A CA 1 ATOM 5319 C C . PHE A 1 643 ? 7.657 42.914 5.085 1.00 19.94 ? 676 PHE A C 1 ATOM 5320 O O . PHE A 1 643 ? 8.038 43.950 5.643 1.00 21.91 ? 676 PHE A O 1 ATOM 5321 C CB . PHE A 1 643 ? 6.209 42.104 7.026 1.00 19.01 ? 676 PHE A CB 1 ATOM 5322 C CG . PHE A 1 643 ? 4.838 41.578 7.391 1.00 18.85 ? 676 PHE A CG 1 ATOM 5323 C CD1 . PHE A 1 643 ? 3.648 42.393 7.231 1.00 19.22 ? 676 PHE A CD1 1 ATOM 5324 C CD2 . PHE A 1 643 ? 4.690 40.293 7.830 1.00 18.59 ? 676 PHE A CD2 1 ATOM 5325 C CE1 . PHE A 1 643 ? 2.415 41.880 7.462 1.00 19.17 ? 676 PHE A CE1 1 ATOM 5326 C CE2 . PHE A 1 643 ? 3.429 39.787 8.058 1.00 20.49 ? 676 PHE A CE2 1 ATOM 5327 C CZ . PHE A 1 643 ? 2.278 40.600 7.900 1.00 19.86 ? 676 PHE A CZ 1 ATOM 5328 N N . TYR A 1 644 ? 8.392 42.261 4.192 1.00 19.03 ? 677 TYR A N 1 ATOM 5329 C CA . TYR A 1 644 ? 9.526 42.907 3.543 1.00 19.75 ? 677 TYR A CA 1 ATOM 5330 C C . TYR A 1 644 ? 9.027 43.331 2.152 1.00 19.89 ? 677 TYR A C 1 ATOM 5331 O O . TYR A 1 644 ? 8.803 42.527 1.216 1.00 20.17 ? 677 TYR A O 1 ATOM 5332 C CB . TYR A 1 644 ? 10.703 41.964 3.494 1.00 21.72 ? 677 TYR A CB 1 ATOM 5333 C CG . TYR A 1 644 ? 11.345 41.813 4.857 1.00 20.85 ? 677 TYR A CG 1 ATOM 5334 C CD1 . TYR A 1 644 ? 11.222 42.788 5.854 1.00 24.06 ? 677 TYR A CD1 1 ATOM 5335 C CD2 . TYR A 1 644 ? 12.143 40.738 5.084 1.00 27.94 ? 677 TYR A CD2 1 ATOM 5336 C CE1 . TYR A 1 644 ? 11.882 42.663 7.135 1.00 25.03 ? 677 TYR A CE1 1 ATOM 5337 C CE2 . TYR A 1 644 ? 12.808 40.616 6.285 1.00 23.52 ? 677 TYR A CE2 1 ATOM 5338 C CZ . TYR A 1 644 ? 12.675 41.551 7.320 1.00 26.17 ? 677 TYR A CZ 1 ATOM 5339 O OH . TYR A 1 644 ? 13.388 41.348 8.572 1.00 26.85 ? 677 TYR A OH 1 ATOM 5340 N N . ARG A 1 645 ? 8.871 44.653 1.998 1.00 19.13 ? 678 ARG A N 1 ATOM 5341 C CA . ARG A 1 645 ? 8.220 45.195 0.794 1.00 19.12 ? 678 ARG A CA 1 ATOM 5342 C C . ARG A 1 645 ? 9.134 46.045 -0.058 1.00 19.01 ? 678 ARG A C 1 ATOM 5343 O O . ARG A 1 645 ? 8.777 46.421 -1.188 1.00 18.51 ? 678 ARG A O 1 ATOM 5344 C CB . ARG A 1 645 ? 6.965 45.960 1.210 1.00 18.09 ? 678 ARG A CB 1 ATOM 5345 C CG . ARG A 1 645 ? 5.956 45.055 1.963 1.00 17.10 ? 678 ARG A CG 1 ATOM 5346 C CD . ARG A 1 645 ? 4.708 45.822 2.273 1.00 18.88 ? 678 ARG A CD 1 ATOM 5347 N NE . ARG A 1 645 ? 3.824 44.910 3.011 1.00 21.48 ? 678 ARG A NE 1 ATOM 5348 C CZ . ARG A 1 645 ? 2.845 45.291 3.814 1.00 21.49 ? 678 ARG A CZ 1 ATOM 5349 N NH1 . ARG A 1 645 ? 2.505 46.548 4.055 1.00 20.60 ? 678 ARG A NH1 1 ATOM 5350 N NH2 . ARG A 1 645 ? 2.149 44.336 4.428 1.00 24.49 ? 678 ARG A NH2 1 ATOM 5351 N N . HIS A 1 646 ? 10.327 46.415 0.438 1.00 18.64 ? 679 HIS A N 1 ATOM 5352 C CA . HIS A 1 646 ? 11.168 47.382 -0.308 1.00 18.09 ? 679 HIS A CA 1 ATOM 5353 C C . HIS A 1 646 ? 11.910 46.628 -1.367 1.00 19.52 ? 679 HIS A C 1 ATOM 5354 O O . HIS A 1 646 ? 12.781 45.757 -1.029 1.00 22.16 ? 679 HIS A O 1 ATOM 5355 C CB . HIS A 1 646 ? 12.139 48.050 0.674 1.00 18.09 ? 679 HIS A CB 1 ATOM 5356 C CG . HIS A 1 646 ? 12.693 49.333 0.161 1.00 17.27 ? 679 HIS A CG 1 ATOM 5357 N ND1 . HIS A 1 646 ? 13.452 49.390 -0.984 1.00 20.09 ? 679 HIS A ND1 1 ATOM 5358 C CD2 . HIS A 1 646 ? 12.572 50.601 0.619 1.00 18.61 ? 679 HIS A CD2 1 ATOM 5359 C CE1 . HIS A 1 646 ? 13.802 50.653 -1.200 1.00 17.84 ? 679 HIS A CE1 1 ATOM 5360 N NE2 . HIS A 1 646 ? 13.291 51.419 -0.243 1.00 18.20 ? 679 HIS A NE2 1 ATOM 5361 N N . ILE A 1 647 ? 11.629 46.882 -2.631 1.00 17.66 ? 680 ILE A N 1 ATOM 5362 C CA . ILE A 1 647 ? 12.240 46.102 -3.682 1.00 18.29 ? 680 ILE A CA 1 ATOM 5363 C C . ILE A 1 647 ? 13.768 46.364 -3.861 1.00 17.36 ? 680 ILE A C 1 ATOM 5364 O O . ILE A 1 647 ? 14.481 45.501 -4.431 1.00 19.16 ? 680 ILE A O 1 ATOM 5365 C CB . ILE A 1 647 ? 11.469 46.479 -5.003 1.00 16.99 ? 680 ILE A CB 1 ATOM 5366 C CG1 . ILE A 1 647 ? 10.015 45.978 -4.859 1.00 18.58 ? 680 ILE A CG1 1 ATOM 5367 C CG2 . ILE A 1 647 ? 12.122 45.847 -6.259 1.00 19.03 ? 680 ILE A CG2 1 ATOM 5368 C CD1 . ILE A 1 647 ? 9.915 44.475 -4.631 1.00 20.84 ? 680 ILE A CD1 1 ATOM 5369 N N A ILE A 1 648 ? 14.306 47.500 -3.395 0.40 14.95 ? 681 ILE A N 1 ATOM 5370 N N B ILE A 1 648 ? 14.278 47.495 -3.350 0.40 15.38 ? 681 ILE A N 1 ATOM 5371 C CA A ILE A 1 648 ? 15.737 47.714 -3.528 0.40 16.18 ? 681 ILE A CA 1 ATOM 5372 C CA B ILE A 1 648 ? 15.678 47.817 -3.504 0.40 16.63 ? 681 ILE A CA 1 ATOM 5373 C C A ILE A 1 648 ? 16.435 47.195 -2.292 0.40 15.74 ? 681 ILE A C 1 ATOM 5374 C C B ILE A 1 648 ? 16.511 47.232 -2.390 0.40 16.93 ? 681 ILE A C 1 ATOM 5375 O O A ILE A 1 648 ? 17.421 46.450 -2.415 0.40 16.01 ? 681 ILE A O 1 ATOM 5376 O O B ILE A 1 648 ? 17.641 46.782 -2.666 0.40 14.22 ? 681 ILE A O 1 ATOM 5377 C CB A ILE A 1 648 ? 16.117 49.197 -3.731 0.40 15.00 ? 681 ILE A CB 1 ATOM 5378 C CB B ILE A 1 648 ? 15.941 49.316 -3.535 0.40 15.32 ? 681 ILE A CB 1 ATOM 5379 C CG1 A ILE A 1 648 ? 15.259 49.860 -4.828 0.40 15.13 ? 681 ILE A CG1 1 ATOM 5380 C CG1 B ILE A 1 648 ? 14.978 50.043 -4.522 0.40 15.40 ? 681 ILE A CG1 1 ATOM 5381 C CG2 A ILE A 1 648 ? 17.607 49.360 -4.083 0.40 15.83 ? 681 ILE A CG2 1 ATOM 5382 C CG2 B ILE A 1 648 ? 17.459 49.568 -3.805 0.40 15.70 ? 681 ILE A CG2 1 ATOM 5383 C CD1 A ILE A 1 648 ? 15.196 49.104 -6.188 0.40 16.01 ? 681 ILE A CD1 1 ATOM 5384 C CD1 B ILE A 1 648 ? 15.010 49.579 -6.028 0.40 15.70 ? 681 ILE A CD1 1 ATOM 5385 N N A PHE A 1 649 ? 15.923 47.527 -1.113 0.40 15.02 ? 682 PHE A N 1 ATOM 5386 N N B PHE A 1 649 ? 15.965 47.219 -1.168 0.40 17.84 ? 682 PHE A N 1 ATOM 5387 C CA A PHE A 1 649 ? 16.708 47.325 0.113 0.40 14.62 ? 682 PHE A CA 1 ATOM 5388 C CA B PHE A 1 649 ? 16.647 46.665 0.027 0.40 19.45 ? 682 PHE A CA 1 ATOM 5389 C C A PHE A 1 649 ? 16.284 46.207 1.093 0.40 15.54 ? 682 PHE A C 1 ATOM 5390 C C B PHE A 1 649 ? 15.795 45.615 0.812 0.40 20.46 ? 682 PHE A C 1 ATOM 5391 O O A PHE A 1 649 ? 16.939 46.064 2.152 0.40 15.82 ? 682 PHE A O 1 ATOM 5392 O O B PHE A 1 649 ? 14.619 45.834 0.997 0.40 20.80 ? 682 PHE A O 1 ATOM 5393 C CB A PHE A 1 649 ? 16.885 48.671 0.872 0.40 14.61 ? 682 PHE A CB 1 ATOM 5394 C CB B PHE A 1 649 ? 17.008 47.817 0.969 0.40 18.83 ? 682 PHE A CB 1 ATOM 5395 C CG A PHE A 1 649 ? 17.809 49.696 0.163 0.40 15.95 ? 682 PHE A CG 1 ATOM 5396 C CG B PHE A 1 649 ? 17.852 48.910 0.320 0.40 17.41 ? 682 PHE A CG 1 ATOM 5397 C CD1 A PHE A 1 649 ? 19.130 49.404 -0.114 0.40 12.29 ? 682 PHE A CD1 1 ATOM 5398 C CD1 B PHE A 1 649 ? 17.276 50.152 -0.008 0.40 18.58 ? 682 PHE A CD1 1 ATOM 5399 C CD2 A PHE A 1 649 ? 17.313 50.933 -0.224 0.40 14.21 ? 682 PHE A CD2 1 ATOM 5400 C CD2 B PHE A 1 649 ? 19.217 48.722 0.073 0.40 17.96 ? 682 PHE A CD2 1 ATOM 5401 C CE1 A PHE A 1 649 ? 19.964 50.331 -0.741 0.40 14.43 ? 682 PHE A CE1 1 ATOM 5402 C CE1 B PHE A 1 649 ? 18.020 51.129 -0.630 0.40 19.03 ? 682 PHE A CE1 1 ATOM 5403 C CE2 A PHE A 1 649 ? 18.149 51.870 -0.857 0.40 13.81 ? 682 PHE A CE2 1 ATOM 5404 C CE2 B PHE A 1 649 ? 19.981 49.741 -0.512 0.40 17.45 ? 682 PHE A CE2 1 ATOM 5405 C CZ A PHE A 1 649 ? 19.462 51.559 -1.102 0.40 16.59 ? 682 PHE A CZ 1 ATOM 5406 C CZ B PHE A 1 649 ? 19.385 50.946 -0.834 0.40 16.68 ? 682 PHE A CZ 1 ATOM 5407 N N A ALA A 1 650 ? 15.213 45.438 0.815 0.40 14.98 ? 683 ALA A N 1 ATOM 5408 N N B ALA A 1 650 ? 16.370 44.509 1.311 0.40 21.82 ? 683 ALA A N 1 ATOM 5409 C CA A ALA A 1 650 ? 14.740 44.491 1.850 0.40 16.77 ? 683 ALA A CA 1 ATOM 5410 C CA B ALA A 1 650 ? 15.740 43.766 2.409 0.40 22.61 ? 683 ALA A CA 1 ATOM 5411 C C A ALA A 1 650 ? 15.846 43.446 2.098 0.40 17.60 ? 683 ALA A C 1 ATOM 5412 C C B ALA A 1 650 ? 16.805 43.276 3.320 0.40 23.76 ? 683 ALA A C 1 ATOM 5413 O O A ALA A 1 650 ? 16.613 43.154 1.191 0.40 17.18 ? 683 ALA A O 1 ATOM 5414 O O B ALA A 1 650 ? 17.963 43.223 2.935 0.40 23.78 ? 683 ALA A O 1 ATOM 5415 C CB A ALA A 1 650 ? 13.485 43.783 1.386 0.40 17.22 ? 683 ALA A CB 1 ATOM 5416 C CB B ALA A 1 650 ? 14.912 42.603 1.933 0.40 23.16 ? 683 ALA A CB 1 ATOM 5417 N N A PRO A 1 651 ? 15.857 42.846 3.302 0.40 19.64 ? 684 PRO A N 1 ATOM 5418 N N B PRO A 1 651 ? 16.417 42.944 4.546 0.40 22.67 ? 684 PRO A N 1 ATOM 5419 C CA A PRO A 1 651 ? 16.939 42.051 3.954 0.40 22.28 ? 684 PRO A CA 1 ATOM 5420 C CA B PRO A 1 651 ? 17.368 42.183 5.347 0.40 23.21 ? 684 PRO A CA 1 ATOM 5421 C C A PRO A 1 651 ? 17.867 40.925 3.461 0.40 24.97 ? 684 PRO A C 1 ATOM 5422 C C B PRO A 1 651 ? 17.640 40.871 4.623 0.40 23.74 ? 684 PRO A C 1 ATOM 5423 O O A PRO A 1 651 ? 17.678 40.341 2.368 0.40 25.91 ? 684 PRO A O 1 ATOM 5424 O O B PRO A 1 651 ? 16.727 40.209 4.210 0.40 25.76 ? 684 PRO A O 1 ATOM 5425 C CB A PRO A 1 651 ? 16.247 41.548 5.211 0.40 21.62 ? 684 PRO A CB 1 ATOM 5426 C CB B PRO A 1 651 ? 16.619 41.955 6.651 0.40 22.76 ? 684 PRO A CB 1 ATOM 5427 C CG A PRO A 1 651 ? 15.590 42.754 5.663 0.40 22.10 ? 684 PRO A CG 1 ATOM 5428 C CG B PRO A 1 651 ? 15.549 43.006 6.650 0.40 19.89 ? 684 PRO A CG 1 ATOM 5429 C CD A PRO A 1 651 ? 14.934 43.309 4.356 0.40 18.41 ? 684 PRO A CD 1 ATOM 5430 C CD B PRO A 1 651 ? 15.146 43.193 5.234 0.40 23.70 ? 684 PRO A CD 1 ATOM 5431 N N . SER A 1 652 ? 18.901 40.627 4.294 0.40 24.78 ? 685 SER A N 1 ATOM 5432 C CA . SER A 1 652 ? 19.511 39.338 3.994 0.40 24.48 ? 685 SER A CA 1 ATOM 5433 C C . SER A 1 652 ? 18.797 38.164 4.629 0.40 24.62 ? 685 SER A C 1 ATOM 5434 O O . SER A 1 652 ? 18.656 38.072 5.863 0.40 24.87 ? 685 SER A O 1 ATOM 5435 C CB . SER A 1 652 ? 20.997 39.285 4.325 0.40 23.80 ? 685 SER A CB 1 ATOM 5436 O OG . SER A 1 652 ? 21.505 38.047 3.850 0.40 22.59 ? 685 SER A OG 1 ATOM 5437 N N . SER A 1 653 ? 18.350 37.269 3.756 0.40 24.82 ? 686 SER A N 1 ATOM 5438 C CA . SER A 1 653 ? 17.767 35.995 4.176 0.40 25.08 ? 686 SER A CA 1 ATOM 5439 C C . SER A 1 653 ? 18.722 35.130 4.988 0.40 25.21 ? 686 SER A C 1 ATOM 5440 O O . SER A 1 653 ? 18.307 34.137 5.601 0.40 24.89 ? 686 SER A O 1 ATOM 5441 C CB . SER A 1 653 ? 17.283 35.217 2.950 0.40 25.09 ? 686 SER A CB 1 ATOM 5442 O OG . SER A 1 653 ? 16.411 36.031 2.187 0.40 27.72 ? 686 SER A OG 1 ATOM 5443 N N . HIS A 1 654 ? 19.993 35.524 4.990 0.40 25.21 ? 687 HIS A N 1 ATOM 5444 C CA . HIS A 1 654 ? 21.051 34.720 5.593 0.40 24.64 ? 687 HIS A CA 1 ATOM 5445 C C . HIS A 1 654 ? 21.593 35.384 6.843 0.40 24.36 ? 687 HIS A C 1 ATOM 5446 O O . HIS A 1 654 ? 22.320 34.761 7.598 0.40 23.81 ? 687 HIS A O 1 ATOM 5447 C CB . HIS A 1 654 ? 22.172 34.525 4.589 0.40 24.99 ? 687 HIS A CB 1 ATOM 5448 C CG . HIS A 1 654 ? 21.700 33.910 3.306 0.40 26.76 ? 687 HIS A CG 1 ATOM 5449 N ND1 . HIS A 1 654 ? 21.424 32.564 3.179 0.40 28.21 ? 687 HIS A ND1 1 ATOM 5450 C CD2 . HIS A 1 654 ? 21.392 34.474 2.117 0.40 27.45 ? 687 HIS A CD2 1 ATOM 5451 C CE1 . HIS A 1 654 ? 20.984 32.324 1.954 0.40 27.65 ? 687 HIS A CE1 1 ATOM 5452 N NE2 . HIS A 1 654 ? 20.958 33.468 1.291 0.40 26.16 ? 687 HIS A NE2 1 ATOM 5453 N N . ASN A 1 655 ? 21.214 36.636 7.071 0.40 24.57 ? 688 ASN A N 1 ATOM 5454 C CA . ASN A 1 655 ? 21.719 37.423 8.185 0.40 24.27 ? 688 ASN A CA 1 ATOM 5455 C C . ASN A 1 655 ? 20.904 38.694 8.266 0.40 23.70 ? 688 ASN A C 1 ATOM 5456 O O . ASN A 1 655 ? 21.207 39.668 7.569 0.40 23.69 ? 688 ASN A O 1 ATOM 5457 C CB . ASN A 1 655 ? 23.181 37.816 7.946 0.40 23.28 ? 688 ASN A CB 1 ATOM 5458 C CG . ASN A 1 655 ? 23.728 38.748 9.035 0.40 22.98 ? 688 ASN A CG 1 ATOM 5459 O OD1 . ASN A 1 655 ? 23.127 38.918 10.100 0.40 23.55 ? 688 ASN A OD1 1 ATOM 5460 N ND2 . ASN A 1 655 ? 24.872 39.357 8.757 0.40 23.62 ? 688 ASN A ND2 1 ATOM 5461 N N . LYS A 1 656 ? 19.883 38.693 9.113 0.40 22.63 ? 689 LYS A N 1 ATOM 5462 C CA . LYS A 1 656 ? 18.967 39.827 9.192 0.40 24.29 ? 689 LYS A CA 1 ATOM 5463 C C . LYS A 1 656 ? 19.690 41.155 9.504 0.40 23.63 ? 689 LYS A C 1 ATOM 5464 O O . LYS A 1 656 ? 19.230 42.235 9.152 0.40 22.10 ? 689 LYS A O 1 ATOM 5465 C CB . LYS A 1 656 ? 17.875 39.472 10.209 0.40 25.06 ? 689 LYS A CB 1 ATOM 5466 C CG . LYS A 1 656 ? 16.941 40.553 10.641 0.40 27.63 ? 689 LYS A CG 1 ATOM 5467 C CD . LYS A 1 656 ? 16.291 40.177 11.973 0.40 29.56 ? 689 LYS A CD 1 ATOM 5468 C CE . LYS A 1 656 ? 15.121 41.112 12.303 0.40 32.67 ? 689 LYS A CE 1 ATOM 5469 N NZ . LYS A 1 656 ? 14.135 40.321 13.118 0.40 29.93 ? 689 LYS A NZ 1 ATOM 5470 N N . TYR A 1 657 ? 20.832 41.110 10.154 0.40 22.67 ? 690 TYR A N 1 ATOM 5471 C CA . TYR A 1 657 ? 21.559 42.366 10.433 0.40 23.59 ? 690 TYR A CA 1 ATOM 5472 C C . TYR A 1 657 ? 22.076 43.079 9.202 0.40 23.35 ? 690 TYR A C 1 ATOM 5473 O O . TYR A 1 657 ? 22.222 44.320 9.201 0.40 23.54 ? 690 TYR A O 1 ATOM 5474 C CB . TYR A 1 657 ? 22.754 42.096 11.340 0.40 23.62 ? 690 TYR A CB 1 ATOM 5475 C CG . TYR A 1 657 ? 22.376 41.549 12.693 0.40 25.40 ? 690 TYR A CG 1 ATOM 5476 C CD1 . TYR A 1 657 ? 21.343 42.108 13.423 0.40 27.16 ? 690 TYR A CD1 1 ATOM 5477 C CD2 . TYR A 1 657 ? 23.071 40.472 13.241 0.40 26.79 ? 690 TYR A CD2 1 ATOM 5478 C CE1 . TYR A 1 657 ? 20.999 41.595 14.665 0.40 29.92 ? 690 TYR A CE1 1 ATOM 5479 C CE2 . TYR A 1 657 ? 22.751 39.970 14.472 0.40 28.08 ? 690 TYR A CE2 1 ATOM 5480 C CZ . TYR A 1 657 ? 21.722 40.529 15.181 0.40 29.94 ? 690 TYR A CZ 1 ATOM 5481 O OH . TYR A 1 657 ? 21.400 40.012 16.419 0.40 29.22 ? 690 TYR A OH 1 ATOM 5482 N N . ALA A 1 658 ? 22.389 42.295 8.174 0.40 21.98 ? 691 ALA A N 1 ATOM 5483 C CA . ALA A 1 658 ? 22.960 42.820 6.936 0.40 21.85 ? 691 ALA A CA 1 ATOM 5484 C C . ALA A 1 658 ? 21.872 43.208 5.970 0.40 22.54 ? 691 ALA A C 1 ATOM 5485 O O . ALA A 1 658 ? 20.873 42.481 5.814 0.40 22.84 ? 691 ALA A O 1 ATOM 5486 C CB . ALA A 1 658 ? 23.852 41.771 6.259 0.40 22.55 ? 691 ALA A CB 1 ATOM 5487 N N . GLY A 1 659 ? 22.075 44.304 5.256 0.40 21.68 ? 692 GLY A N 1 ATOM 5488 C CA . GLY A 1 659 ? 21.124 44.633 4.187 0.40 23.17 ? 692 GLY A CA 1 ATOM 5489 C C . GLY A 1 659 ? 21.577 44.060 2.863 0.40 23.82 ? 692 GLY A C 1 ATOM 5490 O O . GLY A 1 659 ? 22.782 43.996 2.589 0.40 24.68 ? 692 GLY A O 1 ATOM 5491 N N . GLU A 1 660 ? 20.624 43.641 2.040 0.40 24.16 ? 693 GLU A N 1 ATOM 5492 C CA . GLU A 1 660 ? 20.929 43.087 0.721 0.40 25.02 ? 693 GLU A CA 1 ATOM 5493 C C . GLU A 1 660 ? 20.229 43.888 -0.364 0.40 25.44 ? 693 GLU A C 1 ATOM 5494 O O . GLU A 1 660 ? 19.033 44.156 -0.183 0.40 22.17 ? 693 GLU A O 1 ATOM 5495 C CB . GLU A 1 660 ? 20.403 41.656 0.612 0.40 24.62 ? 693 GLU A CB 1 ATOM 5496 C CG . GLU A 1 660 ? 20.890 40.981 -0.659 0.40 27.00 ? 693 GLU A CG 1 ATOM 5497 C CD . GLU A 1 660 ? 22.388 41.003 -0.701 0.40 28.23 ? 693 GLU A CD 1 ATOM 5498 O OE1 . GLU A 1 660 ? 22.956 40.037 -0.153 0.40 25.80 ? 693 GLU A OE1 1 ATOM 5499 O OE2 . GLU A 1 660 ? 22.995 42.007 -1.199 0.40 29.75 ? 693 GLU A OE2 1 ATOM 5500 N N . SER A 1 661 ? 20.923 44.242 -1.472 1.00 28.76 ? 694 SER A N 1 ATOM 5501 C CA . SER A 1 661 ? 20.236 45.007 -2.610 1.00 26.41 ? 694 SER A CA 1 ATOM 5502 C C . SER A 1 661 ? 19.610 44.099 -3.711 1.00 25.51 ? 694 SER A C 1 ATOM 5503 O O . SER A 1 661 ? 20.145 43.015 -4.031 1.00 29.06 ? 694 SER A O 1 ATOM 5504 C CB . SER A 1 661 ? 21.072 46.077 -3.282 1.00 28.24 ? 694 SER A CB 1 ATOM 5505 O OG A SER A 1 661 ? 21.313 47.147 -2.374 0.50 24.04 ? 694 SER A OG 1 ATOM 5506 O OG B SER A 1 661 ? 22.295 45.405 -3.664 0.50 24.85 ? 694 SER A OG 1 ATOM 5507 N N . PHE A 1 662 ? 18.515 44.594 -4.323 1.00 21.09 ? 695 PHE A N 1 ATOM 5508 C CA . PHE A 1 662 ? 17.637 43.743 -5.165 1.00 21.39 ? 695 PHE A CA 1 ATOM 5509 C C . PHE A 1 662 ? 17.398 42.348 -4.561 1.00 20.60 ? 695 PHE A C 1 ATOM 5510 O O . PHE A 1 662 ? 17.695 41.339 -5.278 1.00 21.66 ? 695 PHE A O 1 ATOM 5511 C CB . PHE A 1 662 ? 18.190 43.647 -6.601 1.00 22.14 ? 695 PHE A CB 1 ATOM 5512 C CG . PHE A 1 662 ? 18.192 44.940 -7.337 1.00 20.76 ? 695 PHE A CG 1 ATOM 5513 C CD1 . PHE A 1 662 ? 17.025 45.715 -7.407 1.00 20.78 ? 695 PHE A CD1 1 ATOM 5514 C CD2 . PHE A 1 662 ? 19.365 45.457 -7.896 1.00 22.48 ? 695 PHE A CD2 1 ATOM 5515 C CE1 . PHE A 1 662 ? 17.007 46.885 -8.082 1.00 23.52 ? 695 PHE A CE1 1 ATOM 5516 C CE2 . PHE A 1 662 ? 19.378 46.687 -8.526 1.00 22.42 ? 695 PHE A CE2 1 ATOM 5517 C CZ . PHE A 1 662 ? 18.209 47.442 -8.619 1.00 22.28 ? 695 PHE A CZ 1 ATOM 5518 N N . PRO A 1 663 ? 16.889 42.270 -3.359 1.00 20.36 ? 696 PRO A N 1 ATOM 5519 C CA . PRO A 1 663 ? 16.775 40.990 -2.626 1.00 20.88 ? 696 PRO A CA 1 ATOM 5520 C C . PRO A 1 663 ? 15.940 39.989 -3.410 1.00 23.28 ? 696 PRO A C 1 ATOM 5521 O O . PRO A 1 663 ? 16.218 38.805 -3.372 1.00 24.61 ? 696 PRO A O 1 ATOM 5522 C CB . PRO A 1 663 ? 16.016 41.361 -1.382 1.00 22.20 ? 696 PRO A CB 1 ATOM 5523 C CG . PRO A 1 663 ? 15.346 42.738 -1.677 1.00 22.04 ? 696 PRO A CG 1 ATOM 5524 C CD . PRO A 1 663 ? 16.362 43.380 -2.530 1.00 20.86 ? 696 PRO A CD 1 ATOM 5525 N N . GLY A 1 664 ? 14.958 40.446 -4.163 1.00 20.64 ? 697 GLY A N 1 ATOM 5526 C CA . GLY A 1 664 ? 14.135 39.444 -4.919 1.00 22.76 ? 697 GLY A CA 1 ATOM 5527 C C . GLY A 1 664 ? 14.984 38.732 -5.965 1.00 21.94 ? 697 GLY A C 1 ATOM 5528 O O . GLY A 1 664 ? 14.827 37.511 -6.202 1.00 22.74 ? 697 GLY A O 1 ATOM 5529 N N . ILE A 1 665 ? 15.872 39.476 -6.635 1.00 20.54 ? 698 ILE A N 1 ATOM 5530 C CA . ILE A 1 665 ? 16.766 38.910 -7.668 1.00 20.50 ? 698 ILE A CA 1 ATOM 5531 C C . ILE A 1 665 ? 17.841 38.094 -6.972 1.00 23.31 ? 698 ILE A C 1 ATOM 5532 O O . ILE A 1 665 ? 18.079 36.928 -7.310 1.00 23.48 ? 698 ILE A O 1 ATOM 5533 C CB . ILE A 1 665 ? 17.397 39.977 -8.575 1.00 20.01 ? 698 ILE A CB 1 ATOM 5534 C CG1 . ILE A 1 665 ? 16.322 40.891 -9.208 1.00 21.96 ? 698 ILE A CG1 1 ATOM 5535 C CG2 . ILE A 1 665 ? 18.239 39.272 -9.679 1.00 20.84 ? 698 ILE A CG2 1 ATOM 5536 C CD1 . ILE A 1 665 ? 16.831 42.068 -10.015 1.00 21.11 ? 698 ILE A CD1 1 ATOM 5537 N N . TYR A 1 666 ? 18.438 38.666 -5.924 1.00 23.78 ? 699 TYR A N 1 ATOM 5538 C CA . TYR A 1 666 ? 19.497 37.923 -5.230 1.00 26.79 ? 699 TYR A CA 1 ATOM 5539 C C . TYR A 1 666 ? 18.995 36.584 -4.687 1.00 26.79 ? 699 TYR A C 1 ATOM 5540 O O . TYR A 1 666 ? 19.648 35.531 -4.873 1.00 27.65 ? 699 TYR A O 1 ATOM 5541 C CB . TYR A 1 666 ? 20.036 38.828 -4.101 1.00 27.98 ? 699 TYR A CB 1 ATOM 5542 C CG . TYR A 1 666 ? 21.196 38.210 -3.382 1.00 29.30 ? 699 TYR A CG 1 ATOM 5543 C CD1 . TYR A 1 666 ? 22.499 38.423 -3.848 1.00 34.15 ? 699 TYR A CD1 1 ATOM 5544 C CD2 . TYR A 1 666 ? 20.992 37.353 -2.322 1.00 31.80 ? 699 TYR A CD2 1 ATOM 5545 C CE1 . TYR A 1 666 ? 23.601 37.802 -3.221 1.00 34.95 ? 699 TYR A CE1 1 ATOM 5546 C CE2 . TYR A 1 666 ? 22.095 36.733 -1.682 1.00 32.71 ? 699 TYR A CE2 1 ATOM 5547 C CZ . TYR A 1 666 ? 23.370 36.990 -2.136 1.00 35.44 ? 699 TYR A CZ 1 ATOM 5548 O OH . TYR A 1 666 ? 24.430 36.336 -1.492 1.00 41.07 ? 699 TYR A OH 1 ATOM 5549 N N . ASP A 1 667 ? 17.861 36.556 -4.039 1.00 26.30 ? 700 ASP A N 1 ATOM 5550 C CA . ASP A 1 667 ? 17.354 35.300 -3.462 1.00 26.20 ? 700 ASP A CA 1 ATOM 5551 C C . ASP A 1 667 ? 17.017 34.279 -4.553 1.00 26.53 ? 700 ASP A C 1 ATOM 5552 O O . ASP A 1 667 ? 17.189 33.046 -4.360 1.00 28.49 ? 700 ASP A O 1 ATOM 5553 C CB . ASP A 1 667 ? 16.136 35.548 -2.603 1.00 27.29 ? 700 ASP A CB 1 ATOM 5554 C CG . ASP A 1 667 ? 16.490 36.125 -1.247 1.00 32.18 ? 700 ASP A CG 1 ATOM 5555 O OD1 . ASP A 1 667 ? 17.672 36.026 -0.829 1.00 37.37 ? 700 ASP A OD1 1 ATOM 5556 O OD2 . ASP A 1 667 ? 15.586 36.673 -0.596 1.00 37.74 ? 700 ASP A OD2 1 ATOM 5557 N N . ALA A 1 668 ? 16.518 34.775 -5.674 1.00 26.16 ? 701 ALA A N 1 ATOM 5558 C CA . ALA A 1 668 ? 16.194 33.903 -6.774 1.00 26.81 ? 701 ALA A CA 1 ATOM 5559 C C . ALA A 1 668 ? 17.412 33.238 -7.397 1.00 28.19 ? 701 ALA A C 1 ATOM 5560 O O . ALA A 1 668 ? 17.363 32.055 -7.801 1.00 27.92 ? 701 ALA A O 1 ATOM 5561 C CB . ALA A 1 668 ? 15.374 34.681 -7.845 1.00 24.99 ? 701 ALA A CB 1 ATOM 5562 N N . ILE A 1 669 ? 18.511 33.966 -7.492 1.00 28.20 ? 702 ILE A N 1 ATOM 5563 C CA . ILE A 1 669 ? 19.728 33.420 -8.100 1.00 30.07 ? 702 ILE A CA 1 ATOM 5564 C C . ILE A 1 669 ? 20.642 32.676 -7.091 1.00 30.81 ? 702 ILE A C 1 ATOM 5565 O O . ILE A 1 669 ? 21.460 31.832 -7.524 1.00 29.65 ? 702 ILE A O 1 ATOM 5566 C CB . ILE A 1 669 ? 20.441 34.520 -8.884 1.00 30.34 ? 702 ILE A CB 1 ATOM 5567 C CG1 . ILE A 1 669 ? 21.231 33.927 -10.057 1.00 35.59 ? 702 ILE A CG1 1 ATOM 5568 C CG2 . ILE A 1 669 ? 21.284 35.358 -7.910 1.00 32.56 ? 702 ILE A CG2 1 ATOM 5569 C CD1 . ILE A 1 669 ? 21.499 34.910 -11.172 1.00 36.15 ? 702 ILE A CD1 1 ATOM 5570 N N . PHE A 1 670 ? 20.495 32.910 -5.782 1.00 31.69 ? 703 PHE A N 1 ATOM 5571 C CA . PHE A 1 670 ? 21.297 32.194 -4.753 1.00 32.85 ? 703 PHE A CA 1 ATOM 5572 C C . PHE A 1 670 ? 21.200 30.649 -4.803 1.00 33.43 ? 703 PHE A C 1 ATOM 5573 O O . PHE A 1 670 ? 20.106 30.053 -4.713 1.00 34.25 ? 703 PHE A O 1 ATOM 5574 C CB . PHE A 1 670 ? 20.957 32.689 -3.335 1.00 34.74 ? 703 PHE A CB 1 ATOM 5575 C CG . PHE A 1 670 ? 21.787 32.021 -2.247 1.00 36.26 ? 703 PHE A CG 1 ATOM 5576 C CD1 . PHE A 1 670 ? 23.021 32.540 -1.894 1.00 39.61 ? 703 PHE A CD1 1 ATOM 5577 C CD2 . PHE A 1 670 ? 21.323 30.869 -1.610 1.00 38.18 ? 703 PHE A CD2 1 ATOM 5578 C CE1 . PHE A 1 670 ? 23.807 31.889 -0.902 1.00 39.48 ? 703 PHE A CE1 1 ATOM 5579 C CE2 . PHE A 1 670 ? 22.078 30.213 -0.617 1.00 40.73 ? 703 PHE A CE2 1 ATOM 5580 C CZ . PHE A 1 670 ? 23.311 30.742 -0.255 1.00 39.68 ? 703 PHE A CZ 1 ATOM 5581 N N . ASP A 1 671 ? 22.375 29.993 -4.863 1.00 32.90 ? 704 ASP A N 1 ATOM 5582 C CA . ASP A 1 671 ? 22.482 28.509 -4.894 1.00 33.00 ? 704 ASP A CA 1 ATOM 5583 C C . ASP A 1 671 ? 21.681 27.899 -6.030 1.00 32.32 ? 704 ASP A C 1 ATOM 5584 O O . ASP A 1 671 ? 21.236 26.751 -5.939 1.00 31.54 ? 704 ASP A O 1 ATOM 5585 C CB . ASP A 1 671 ? 22.037 27.872 -3.545 1.00 33.90 ? 704 ASP A CB 1 ATOM 5586 C CG . ASP A 1 671 ? 22.552 26.442 -3.356 1.00 36.26 ? 704 ASP A CG 1 ATOM 5587 O OD1 . ASP A 1 671 ? 23.692 26.157 -3.788 1.00 36.60 ? 704 ASP A OD1 1 ATOM 5588 O OD2 . ASP A 1 671 ? 21.814 25.594 -2.792 1.00 35.45 ? 704 ASP A OD2 1 ATOM 5589 N N . ILE A 1 672 ? 21.509 28.648 -7.119 1.00 30.47 ? 705 ILE A N 1 ATOM 5590 C CA . ILE A 1 672 ? 20.565 28.210 -8.151 1.00 30.00 ? 705 ILE A CA 1 ATOM 5591 C C . ILE A 1 672 ? 21.055 26.918 -8.813 1.00 30.42 ? 705 ILE A C 1 ATOM 5592 O O . ILE A 1 672 ? 20.254 26.106 -9.312 1.00 30.02 ? 705 ILE A O 1 ATOM 5593 C CB . ILE A 1 672 ? 20.289 29.340 -9.199 1.00 29.69 ? 705 ILE A CB 1 ATOM 5594 C CG1 . ILE A 1 672 ? 19.201 28.916 -10.217 1.00 25.74 ? 705 ILE A CG1 1 ATOM 5595 C CG2 . ILE A 1 672 ? 21.563 29.728 -9.976 1.00 29.99 ? 705 ILE A CG2 1 ATOM 5596 C CD1 . ILE A 1 672 ? 18.423 30.172 -10.855 1.00 23.99 ? 705 ILE A CD1 1 ATOM 5597 N N . GLU A 1 673 ? 22.369 26.748 -8.849 1.00 31.61 ? 706 GLU A N 1 ATOM 5598 C CA . GLU A 1 673 ? 22.926 25.565 -9.531 1.00 33.80 ? 706 GLU A CA 1 ATOM 5599 C C . GLU A 1 673 ? 22.502 24.257 -8.842 1.00 34.75 ? 706 GLU A C 1 ATOM 5600 O O . GLU A 1 673 ? 22.527 23.167 -9.462 1.00 34.76 ? 706 GLU A O 1 ATOM 5601 C CB . GLU A 1 673 ? 24.442 25.688 -9.688 1.00 34.42 ? 706 GLU A CB 1 ATOM 5602 C CG . GLU A 1 673 ? 25.222 25.573 -8.371 1.00 37.69 ? 706 GLU A CG 1 ATOM 5603 C CD . GLU A 1 673 ? 25.392 26.894 -7.610 1.00 41.71 ? 706 GLU A CD 1 ATOM 5604 O OE1 . GLU A 1 673 ? 24.632 27.889 -7.850 1.00 39.51 ? 706 GLU A OE1 1 ATOM 5605 O OE2 . GLU A 1 673 ? 26.301 26.917 -6.732 1.00 43.89 ? 706 GLU A OE2 1 ATOM 5606 N N . ASN A 1 674 ? 22.063 24.369 -7.590 1.00 35.49 ? 707 ASN A N 1 ATOM 5607 C CA . ASN A 1 674 ? 21.604 23.211 -6.843 1.00 36.75 ? 707 ASN A CA 1 ATOM 5608 C C . ASN A 1 674 ? 20.085 23.045 -6.730 1.00 37.38 ? 707 ASN A C 1 ATOM 5609 O O . ASN A 1 674 ? 19.595 22.117 -6.071 1.00 37.84 ? 707 ASN A O 1 ATOM 5610 C CB . ASN A 1 674 ? 22.273 23.196 -5.474 1.00 36.96 ? 707 ASN A CB 1 ATOM 5611 C CG . ASN A 1 674 ? 23.770 22.917 -5.577 1.00 37.55 ? 707 ASN A CG 1 ATOM 5612 O OD1 . ASN A 1 674 ? 24.185 21.851 -6.061 1.00 40.22 ? 707 ASN A OD1 1 ATOM 5613 N ND2 . ASN A 1 674 ? 24.585 23.884 -5.174 1.00 33.13 ? 707 ASN A ND2 1 ATOM 5614 N N . LYS A 1 675 ? 19.332 23.925 -7.389 1.00 37.38 ? 708 LYS A N 1 ATOM 5615 C CA . LYS A 1 675 ? 17.875 23.796 -7.410 1.00 37.04 ? 708 LYS A CA 1 ATOM 5616 C C . LYS A 1 675 ? 17.490 22.577 -8.208 1.00 37.18 ? 708 LYS A C 1 ATOM 5617 O O . LYS A 1 675 ? 18.069 22.325 -9.261 1.00 37.49 ? 708 LYS A O 1 ATOM 5618 C CB . LYS A 1 675 ? 17.229 25.052 -8.011 1.00 37.07 ? 708 LYS A CB 1 ATOM 5619 C CG . LYS A 1 675 ? 17.268 26.254 -7.069 1.00 38.74 ? 708 LYS A CG 1 ATOM 5620 C CD . LYS A 1 675 ? 16.213 26.133 -5.983 1.00 42.59 ? 708 LYS A CD 1 ATOM 5621 C CE . LYS A 1 675 ? 16.445 27.146 -4.854 1.00 44.56 ? 708 LYS A CE 1 ATOM 5622 N NZ . LYS A 1 675 ? 15.915 28.487 -5.207 1.00 45.47 ? 708 LYS A NZ 1 ATOM 5623 N N . ALA A 1 676 ? 16.526 21.813 -7.708 1.00 37.09 ? 709 ALA A N 1 ATOM 5624 C CA . ALA A 1 676 ? 16.121 20.579 -8.376 1.00 37.78 ? 709 ALA A CA 1 ATOM 5625 C C . ALA A 1 676 ? 15.632 20.831 -9.807 1.00 37.59 ? 709 ALA A C 1 ATOM 5626 O O . ALA A 1 676 ? 16.003 20.124 -10.743 1.00 37.20 ? 709 ALA A O 1 ATOM 5627 C CB . ALA A 1 676 ? 15.052 19.865 -7.551 1.00 38.24 ? 709 ALA A CB 1 ATOM 5628 N N . ASN A 1 677 ? 14.812 21.866 -9.970 1.00 37.24 ? 710 ASN A N 1 ATOM 5629 C CA . ASN A 1 677 ? 14.199 22.189 -11.253 1.00 36.61 ? 710 ASN A CA 1 ATOM 5630 C C . ASN A 1 677 ? 14.755 23.500 -11.823 1.00 35.72 ? 710 ASN A C 1 ATOM 5631 O O . ASN A 1 677 ? 14.305 24.573 -11.436 1.00 33.23 ? 710 ASN A O 1 ATOM 5632 C CB . ASN A 1 677 ? 12.682 22.356 -11.048 1.00 37.66 ? 710 ASN A CB 1 ATOM 5633 C CG . ASN A 1 677 ? 11.896 22.357 -12.360 1.00 40.04 ? 710 ASN A CG 1 ATOM 5634 O OD1 . ASN A 1 677 ? 10.807 21.777 -12.405 1.00 46.31 ? 710 ASN A OD1 1 ATOM 5635 N ND2 . ASN A 1 677 ? 12.414 22.992 -13.417 1.00 34.51 ? 710 ASN A ND2 1 ATOM 5636 N N . SER A 1 678 ? 15.685 23.410 -12.761 1.00 34.75 ? 711 SER A N 1 ATOM 5637 C CA . SER A 1 678 ? 16.323 24.619 -13.327 1.00 34.15 ? 711 SER A CA 1 ATOM 5638 C C . SER A 1 678 ? 15.369 25.518 -14.131 1.00 33.70 ? 711 SER A C 1 ATOM 5639 O O . SER A 1 678 ? 15.464 26.754 -14.021 1.00 32.02 ? 711 SER A O 1 ATOM 5640 C CB . SER A 1 678 ? 17.534 24.251 -14.189 1.00 34.95 ? 711 SER A CB 1 ATOM 5641 O OG . SER A 1 678 ? 17.111 23.761 -15.463 1.00 37.14 ? 711 SER A OG 1 ATOM 5642 N N . ARG A 1 679 ? 14.477 24.934 -14.939 1.00 31.33 ? 712 ARG A N 1 ATOM 5643 C CA A ARG A 1 679 ? 13.560 25.741 -15.749 0.60 31.59 ? 712 ARG A CA 1 ATOM 5644 C CA B ARG A 1 679 ? 13.528 25.718 -15.747 0.40 31.09 ? 712 ARG A CA 1 ATOM 5645 C C . ARG A 1 679 ? 12.687 26.600 -14.832 1.00 30.15 ? 712 ARG A C 1 ATOM 5646 O O . ARG A 1 679 ? 12.504 27.790 -15.092 1.00 30.02 ? 712 ARG A O 1 ATOM 5647 C CB A ARG A 1 679 ? 12.716 24.891 -16.716 0.60 32.35 ? 712 ARG A CB 1 ATOM 5648 C CB B ARG A 1 679 ? 12.613 24.820 -16.596 0.40 31.45 ? 712 ARG A CB 1 ATOM 5649 C CG A ARG A 1 679 ? 13.526 24.232 -17.838 0.60 35.44 ? 712 ARG A CG 1 ATOM 5650 C CG B ARG A 1 679 ? 11.697 25.586 -17.563 0.40 32.22 ? 712 ARG A CG 1 ATOM 5651 C CD A ARG A 1 679 ? 12.629 23.858 -19.035 0.60 40.67 ? 712 ARG A CD 1 ATOM 5652 C CD B ARG A 1 679 ? 12.447 26.020 -18.818 0.40 35.16 ? 712 ARG A CD 1 ATOM 5653 N NE A ARG A 1 679 ? 13.299 22.992 -20.017 0.60 44.65 ? 712 ARG A NE 1 ATOM 5654 N NE B ARG A 1 679 ? 11.849 27.192 -19.450 0.40 34.37 ? 712 ARG A NE 1 ATOM 5655 C CZ A ARG A 1 679 ? 14.272 23.372 -20.856 0.60 47.11 ? 712 ARG A CZ 1 ATOM 5656 C CZ B ARG A 1 679 ? 12.342 27.783 -20.535 0.40 37.42 ? 712 ARG A CZ 1 ATOM 5657 N NH1 A ARG A 1 679 ? 14.783 22.484 -21.698 0.60 46.68 ? 712 ARG A NH1 1 ATOM 5658 N NH1 B ARG A 1 679 ? 11.734 28.842 -21.060 0.40 37.22 ? 712 ARG A NH1 1 ATOM 5659 N NH2 A ARG A 1 679 ? 14.742 24.625 -20.863 0.60 47.87 ? 712 ARG A NH2 1 ATOM 5660 N NH2 B ARG A 1 679 ? 13.439 27.297 -21.116 0.40 38.17 ? 712 ARG A NH2 1 ATOM 5661 N N . LEU A 1 680 ? 12.191 26.007 -13.742 1.00 29.59 ? 713 LEU A N 1 ATOM 5662 C CA . LEU A 1 680 ? 11.396 26.760 -12.757 1.00 27.62 ? 713 LEU A CA 1 ATOM 5663 C C . LEU A 1 680 ? 12.262 27.823 -12.060 1.00 27.70 ? 713 LEU A C 1 ATOM 5664 O O . LEU A 1 680 ? 11.822 28.972 -11.849 1.00 27.22 ? 713 LEU A O 1 ATOM 5665 C CB . LEU A 1 680 ? 10.828 25.831 -11.701 1.00 30.53 ? 713 LEU A CB 1 ATOM 5666 C CG . LEU A 1 680 ? 9.708 24.868 -12.121 1.00 33.65 ? 713 LEU A CG 1 ATOM 5667 C CD1 . LEU A 1 680 ? 9.239 24.085 -10.872 1.00 40.17 ? 713 LEU A CD1 1 ATOM 5668 C CD2 . LEU A 1 680 ? 8.533 25.644 -12.753 1.00 38.13 ? 713 LEU A CD2 1 ATOM 5669 N N . ALA A 1 681 ? 13.490 27.439 -11.684 1.00 26.40 ? 714 ALA A N 1 ATOM 5670 C CA . ALA A 1 681 ? 14.340 28.365 -10.929 1.00 25.10 ? 714 ALA A CA 1 ATOM 5671 C C . ALA A 1 681 ? 14.634 29.595 -11.754 1.00 24.27 ? 714 ALA A C 1 ATOM 5672 O O . ALA A 1 681 ? 14.547 30.717 -11.196 1.00 23.48 ? 714 ALA A O 1 ATOM 5673 C CB . ALA A 1 681 ? 15.656 27.673 -10.534 1.00 26.37 ? 714 ALA A CB 1 ATOM 5674 N N . TRP A 1 682 ? 15.008 29.443 -13.020 1.00 23.15 ? 715 TRP A N 1 ATOM 5675 C CA . TRP A 1 682 ? 15.308 30.598 -13.869 1.00 22.75 ? 715 TRP A CA 1 ATOM 5676 C C . TRP A 1 682 ? 14.087 31.519 -14.162 1.00 23.59 ? 715 TRP A C 1 ATOM 5677 O O . TRP A 1 682 ? 14.251 32.740 -14.349 1.00 23.40 ? 715 TRP A O 1 ATOM 5678 C CB . TRP A 1 682 ? 16.035 30.200 -15.138 1.00 23.70 ? 715 TRP A CB 1 ATOM 5679 C CG . TRP A 1 682 ? 17.454 29.823 -14.816 1.00 24.76 ? 715 TRP A CG 1 ATOM 5680 C CD1 . TRP A 1 682 ? 18.020 28.565 -14.910 1.00 27.96 ? 715 TRP A CD1 1 ATOM 5681 C CD2 . TRP A 1 682 ? 18.502 30.710 -14.392 1.00 25.75 ? 715 TRP A CD2 1 ATOM 5682 N NE1 . TRP A 1 682 ? 19.355 28.626 -14.536 1.00 27.78 ? 715 TRP A NE1 1 ATOM 5683 C CE2 . TRP A 1 682 ? 19.669 29.925 -14.207 1.00 29.43 ? 715 TRP A CE2 1 ATOM 5684 C CE3 . TRP A 1 682 ? 18.567 32.098 -14.132 1.00 25.62 ? 715 TRP A CE3 1 ATOM 5685 C CZ2 . TRP A 1 682 ? 20.873 30.476 -13.770 1.00 28.54 ? 715 TRP A CZ2 1 ATOM 5686 C CZ3 . TRP A 1 682 ? 19.768 32.631 -13.680 1.00 26.50 ? 715 TRP A CZ3 1 ATOM 5687 C CH2 . TRP A 1 682 ? 20.892 31.816 -13.506 1.00 29.79 ? 715 TRP A CH2 1 ATOM 5688 N N . LYS A 1 683 ? 12.900 30.911 -14.248 1.00 22.26 ? 716 LYS A N 1 ATOM 5689 C CA . LYS A 1 683 ? 11.701 31.746 -14.430 1.00 21.66 ? 716 LYS A CA 1 ATOM 5690 C C . LYS A 1 683 ? 11.506 32.638 -13.215 1.00 21.59 ? 716 LYS A C 1 ATOM 5691 O O . LYS A 1 683 ? 11.015 33.767 -13.373 1.00 20.81 ? 716 LYS A O 1 ATOM 5692 C CB . LYS A 1 683 ? 10.448 30.873 -14.700 1.00 22.00 ? 716 LYS A CB 1 ATOM 5693 C CG . LYS A 1 683 ? 10.442 30.335 -16.111 1.00 25.72 ? 716 LYS A CG 1 ATOM 5694 C CD . LYS A 1 683 ? 9.268 29.351 -16.347 1.00 29.11 ? 716 LYS A CD 1 ATOM 5695 C CE . LYS A 1 683 ? 9.267 28.915 -17.802 1.00 30.42 ? 716 LYS A CE 1 ATOM 5696 N NZ . LYS A 1 683 ? 8.072 28.061 -18.115 1.00 31.83 ? 716 LYS A NZ 1 ATOM 5697 N N . GLU A 1 684 ? 11.832 32.150 -12.017 1.00 21.46 ? 717 GLU A N 1 ATOM 5698 C CA . GLU A 1 684 ? 11.749 32.984 -10.799 1.00 21.27 ? 717 GLU A CA 1 ATOM 5699 C C . GLU A 1 684 ? 12.745 34.162 -10.891 1.00 22.04 ? 717 GLU A C 1 ATOM 5700 O O . GLU A 1 684 ? 12.433 35.274 -10.501 1.00 20.82 ? 717 GLU A O 1 ATOM 5701 C CB . GLU A 1 684 ? 11.914 32.134 -9.522 1.00 23.80 ? 717 GLU A CB 1 ATOM 5702 C CG A GLU A 1 684 ? 11.715 32.880 -8.186 0.50 24.92 ? 717 GLU A CG 1 ATOM 5703 C CG B GLU A 1 684 ? 10.775 31.131 -9.314 0.50 22.97 ? 717 GLU A CG 1 ATOM 5704 C CD A GLU A 1 684 ? 10.233 33.047 -7.747 0.50 25.43 ? 717 GLU A CD 1 ATOM 5705 C CD B GLU A 1 684 ? 9.403 31.718 -9.571 0.50 28.15 ? 717 GLU A CD 1 ATOM 5706 O OE1 A GLU A 1 684 ? 9.951 33.696 -6.681 0.50 22.99 ? 717 GLU A OE1 1 ATOM 5707 O OE1 B GLU A 1 684 ? 8.625 31.134 -10.372 0.50 31.23 ? 717 GLU A OE1 1 ATOM 5708 O OE2 A GLU A 1 684 ? 9.360 32.512 -8.470 0.50 29.12 ? 717 GLU A OE2 1 ATOM 5709 O OE2 B GLU A 1 684 ? 9.100 32.793 -9.008 0.50 29.90 ? 717 GLU A OE2 1 ATOM 5710 N N . VAL A 1 685 ? 13.938 33.921 -11.423 1.00 22.14 ? 718 VAL A N 1 ATOM 5711 C CA . VAL A 1 685 ? 14.863 35.019 -11.666 1.00 20.40 ? 718 VAL A CA 1 ATOM 5712 C C . VAL A 1 685 ? 14.264 36.035 -12.614 1.00 20.56 ? 718 VAL A C 1 ATOM 5713 O O . VAL A 1 685 ? 14.240 37.250 -12.299 1.00 21.88 ? 718 VAL A O 1 ATOM 5714 C CB . VAL A 1 685 ? 16.236 34.484 -12.176 1.00 21.02 ? 718 VAL A CB 1 ATOM 5715 C CG1 . VAL A 1 685 ? 17.185 35.659 -12.417 1.00 21.79 ? 718 VAL A CG1 1 ATOM 5716 C CG2 . VAL A 1 685 ? 16.826 33.528 -11.130 1.00 23.57 ? 718 VAL A CG2 1 ATOM 5717 N N . LYS A 1 686 ? 13.665 35.571 -13.705 1.00 20.10 ? 719 LYS A N 1 ATOM 5718 C CA . LYS A 1 686 ? 12.999 36.473 -14.655 1.00 19.25 ? 719 LYS A CA 1 ATOM 5719 C C . LYS A 1 686 ? 11.886 37.269 -13.970 1.00 19.16 ? 719 LYS A C 1 ATOM 5720 O O . LYS A 1 686 ? 11.765 38.450 -14.211 1.00 19.34 ? 719 LYS A O 1 ATOM 5721 C CB . LYS A 1 686 ? 12.403 35.654 -15.830 1.00 20.63 ? 719 LYS A CB 1 ATOM 5722 C CG . LYS A 1 686 ? 13.496 35.088 -16.724 1.00 24.16 ? 719 LYS A CG 1 ATOM 5723 C CD . LYS A 1 686 ? 12.862 34.331 -17.882 1.00 28.46 ? 719 LYS A CD 1 ATOM 5724 C CE . LYS A 1 686 ? 12.228 35.248 -18.875 1.00 31.66 ? 719 LYS A CE 1 ATOM 5725 N NZ . LYS A 1 686 ? 12.089 34.480 -20.177 1.00 35.59 ? 719 LYS A NZ 1 ATOM 5726 N N . LYS A 1 687 ? 11.124 36.614 -13.126 1.00 18.02 ? 720 LYS A N 1 ATOM 5727 C CA . LYS A 1 687 ? 10.047 37.304 -12.416 1.00 18.29 ? 720 LYS A CA 1 ATOM 5728 C C . LYS A 1 687 ? 10.606 38.498 -11.626 1.00 19.02 ? 720 LYS A C 1 ATOM 5729 O O . LYS A 1 687 ? 10.040 39.617 -11.662 1.00 19.28 ? 720 LYS A O 1 ATOM 5730 C CB . LYS A 1 687 ? 9.349 36.310 -11.496 1.00 19.21 ? 720 LYS A CB 1 ATOM 5731 C CG . LYS A 1 687 ? 8.280 37.001 -10.594 1.00 21.45 ? 720 LYS A CG 1 ATOM 5732 C CD A LYS A 1 687 ? 7.550 35.969 -9.737 0.50 22.76 ? 720 LYS A CD 1 ATOM 5733 C CD B LYS A 1 687 ? 7.751 36.021 -9.560 0.50 21.82 ? 720 LYS A CD 1 ATOM 5734 C CE A LYS A 1 687 ? 6.588 36.661 -8.754 0.50 25.39 ? 720 LYS A CE 1 ATOM 5735 C CE B LYS A 1 687 ? 6.962 34.899 -10.215 0.50 24.93 ? 720 LYS A CE 1 ATOM 5736 N NZ A LYS A 1 687 ? 5.601 35.760 -7.957 0.50 27.80 ? 720 LYS A NZ 1 ATOM 5737 N NZ B LYS A 1 687 ? 6.546 33.863 -9.187 0.50 27.33 ? 720 LYS A NZ 1 ATOM 5738 N N . HIS A 1 688 ? 11.640 38.244 -10.828 1.00 19.42 ? 721 HIS A N 1 ATOM 5739 C CA . HIS A 1 688 ? 12.157 39.277 -9.942 1.00 17.51 ? 721 HIS A CA 1 ATOM 5740 C C . HIS A 1 688 ? 12.903 40.389 -10.691 1.00 18.89 ? 721 HIS A C 1 ATOM 5741 O O . HIS A 1 688 ? 12.880 41.565 -10.235 1.00 18.33 ? 721 HIS A O 1 ATOM 5742 C CB . HIS A 1 688 ? 12.849 38.631 -8.743 1.00 18.81 ? 721 HIS A CB 1 ATOM 5743 C CG . HIS A 1 688 ? 11.850 37.973 -7.883 1.00 21.53 ? 721 HIS A CG 1 ATOM 5744 N ND1 . HIS A 1 688 ? 11.620 36.602 -7.809 1.00 25.30 ? 721 HIS A ND1 1 ATOM 5745 C CD2 . HIS A 1 688 ? 10.871 38.562 -7.158 1.00 18.39 ? 721 HIS A CD2 1 ATOM 5746 C CE1 . HIS A 1 688 ? 10.582 36.378 -7.011 1.00 19.91 ? 721 HIS A CE1 1 ATOM 5747 N NE2 . HIS A 1 688 ? 10.090 37.557 -6.633 1.00 25.61 ? 721 HIS A NE2 1 ATOM 5748 N N . ILE A 1 689 ? 13.553 40.066 -11.808 1.00 18.75 ? 722 ILE A N 1 ATOM 5749 C CA . ILE A 1 689 ? 14.117 41.092 -12.638 1.00 17.77 ? 722 ILE A CA 1 ATOM 5750 C C . ILE A 1 689 ? 12.994 42.046 -13.144 1.00 19.09 ? 722 ILE A C 1 ATOM 5751 O O . ILE A 1 689 ? 13.096 43.281 -13.071 1.00 19.19 ? 722 ILE A O 1 ATOM 5752 C CB . ILE A 1 689 ? 14.905 40.490 -13.820 1.00 19.10 ? 722 ILE A CB 1 ATOM 5753 C CG1 . ILE A 1 689 ? 16.181 39.827 -13.319 1.00 19.25 ? 722 ILE A CG1 1 ATOM 5754 C CG2 . ILE A 1 689 ? 15.206 41.590 -14.813 1.00 19.09 ? 722 ILE A CG2 1 ATOM 5755 C CD1 . ILE A 1 689 ? 16.872 38.928 -14.381 1.00 20.50 ? 722 ILE A CD1 1 ATOM 5756 N N . SER A 1 690 ? 11.909 41.420 -13.603 1.00 18.03 ? 723 SER A N 1 ATOM 5757 C CA . SER A 1 690 ? 10.792 42.182 -14.177 1.00 17.61 ? 723 SER A CA 1 ATOM 5758 C C . SER A 1 690 ? 10.168 43.134 -13.090 1.00 18.33 ? 723 SER A C 1 ATOM 5759 O O . SER A 1 690 ? 9.827 44.284 -13.359 1.00 18.25 ? 723 SER A O 1 ATOM 5760 C CB . SER A 1 690 ? 9.729 41.155 -14.670 1.00 18.10 ? 723 SER A CB 1 ATOM 5761 O OG . SER A 1 690 ? 8.619 41.850 -15.252 1.00 19.35 ? 723 SER A OG 1 ATOM 5762 N N . ILE A 1 691 ? 9.977 42.597 -11.891 1.00 17.54 ? 724 ILE A N 1 ATOM 5763 C CA . ILE A 1 691 ? 9.415 43.383 -10.760 1.00 16.45 ? 724 ILE A CA 1 ATOM 5764 C C . ILE A 1 691 ? 10.365 44.586 -10.449 1.00 17.75 ? 724 ILE A C 1 ATOM 5765 O O . ILE A 1 691 ? 9.920 45.733 -10.214 1.00 17.80 ? 724 ILE A O 1 ATOM 5766 C CB . ILE A 1 691 ? 9.168 42.522 -9.554 1.00 17.16 ? 724 ILE A CB 1 ATOM 5767 C CG1 . ILE A 1 691 ? 7.986 41.604 -9.842 1.00 17.36 ? 724 ILE A CG1 1 ATOM 5768 C CG2 . ILE A 1 691 ? 8.808 43.385 -8.322 1.00 18.67 ? 724 ILE A CG2 1 ATOM 5769 C CD1 . ILE A 1 691 ? 7.826 40.467 -8.820 1.00 20.79 ? 724 ILE A CD1 1 ATOM 5770 N N . ALA A 1 692 ? 11.683 44.308 -10.402 1.00 17.68 ? 725 ALA A N 1 ATOM 5771 C CA . ALA A 1 692 ? 12.622 45.401 -10.067 1.00 17.87 ? 725 ALA A CA 1 ATOM 5772 C C . ALA A 1 692 ? 12.623 46.502 -11.135 1.00 17.99 ? 725 ALA A C 1 ATOM 5773 O O . ALA A 1 692 ? 12.598 47.712 -10.829 1.00 18.55 ? 725 ALA A O 1 ATOM 5774 C CB . ALA A 1 692 ? 14.032 44.777 -9.916 1.00 19.44 ? 725 ALA A CB 1 ATOM 5775 N N . ALA A 1 693 ? 12.573 46.078 -12.392 1.00 17.75 ? 726 ALA A N 1 ATOM 5776 C CA . ALA A 1 693 ? 12.495 47.036 -13.516 1.00 15.94 ? 726 ALA A CA 1 ATOM 5777 C C . ALA A 1 693 ? 11.249 47.914 -13.446 1.00 17.50 ? 726 ALA A C 1 ATOM 5778 O O . ALA A 1 693 ? 11.296 49.122 -13.509 1.00 18.48 ? 726 ALA A O 1 ATOM 5779 C CB . ALA A 1 693 ? 12.574 46.265 -14.877 1.00 18.45 ? 726 ALA A CB 1 ATOM 5780 N N . PHE A 1 694 ? 10.120 47.221 -13.252 1.00 17.02 ? 727 PHE A N 1 ATOM 5781 C CA . PHE A 1 694 ? 8.889 47.995 -13.089 1.00 16.00 ? 727 PHE A CA 1 ATOM 5782 C C . PHE A 1 694 ? 8.975 48.968 -11.930 1.00 17.00 ? 727 PHE A C 1 ATOM 5783 O O . PHE A 1 694 ? 8.512 50.131 -12.060 1.00 17.51 ? 727 PHE A O 1 ATOM 5784 C CB . PHE A 1 694 ? 7.672 47.041 -12.861 1.00 17.26 ? 727 PHE A CB 1 ATOM 5785 C CG . PHE A 1 694 ? 6.496 47.755 -12.210 1.00 16.77 ? 727 PHE A CG 1 ATOM 5786 C CD1 . PHE A 1 694 ? 5.731 48.638 -12.965 1.00 20.63 ? 727 PHE A CD1 1 ATOM 5787 C CD2 . PHE A 1 694 ? 6.194 47.488 -10.861 1.00 19.30 ? 727 PHE A CD2 1 ATOM 5788 C CE1 . PHE A 1 694 ? 4.673 49.334 -12.322 1.00 18.83 ? 727 PHE A CE1 1 ATOM 5789 C CE2 . PHE A 1 694 ? 5.126 48.212 -10.224 1.00 18.82 ? 727 PHE A CE2 1 ATOM 5790 C CZ . PHE A 1 694 ? 4.408 49.072 -10.952 1.00 18.93 ? 727 PHE A CZ 1 ATOM 5791 N N . THR A 1 695 ? 9.451 48.493 -10.782 1.00 15.63 ? 728 THR A N 1 ATOM 5792 C CA . THR A 1 695 ? 9.364 49.342 -9.605 1.00 16.32 ? 728 THR A CA 1 ATOM 5793 C C . THR A 1 695 ? 10.222 50.592 -9.804 1.00 17.74 ? 728 THR A C 1 ATOM 5794 O O . THR A 1 695 ? 9.813 51.674 -9.377 1.00 17.18 ? 728 THR A O 1 ATOM 5795 C CB . THR A 1 695 ? 9.835 48.557 -8.378 1.00 17.50 ? 728 THR A CB 1 ATOM 5796 O OG1 . THR A 1 695 ? 9.075 47.316 -8.279 1.00 18.76 ? 728 THR A OG1 1 ATOM 5797 C CG2 . THR A 1 695 ? 9.676 49.345 -7.035 1.00 18.92 ? 728 THR A CG2 1 ATOM 5798 N N . ILE A 1 696 ? 11.410 50.426 -10.376 1.00 17.72 ? 729 ILE A N 1 ATOM 5799 C CA . ILE A 1 696 ? 12.284 51.602 -10.586 1.00 16.64 ? 729 ILE A CA 1 ATOM 5800 C C . ILE A 1 696 ? 11.662 52.524 -11.638 1.00 18.00 ? 729 ILE A C 1 ATOM 5801 O O . ILE A 1 696 ? 11.668 53.766 -11.459 1.00 18.62 ? 729 ILE A O 1 ATOM 5802 C CB . ILE A 1 696 ? 13.647 51.069 -11.051 1.00 16.62 ? 729 ILE A CB 1 ATOM 5803 C CG1 . ILE A 1 696 ? 14.333 50.441 -9.826 1.00 19.17 ? 729 ILE A CG1 1 ATOM 5804 C CG2 . ILE A 1 696 ? 14.455 52.250 -11.664 1.00 17.51 ? 729 ILE A CG2 1 ATOM 5805 C CD1 . ILE A 1 696 ? 15.563 49.638 -10.184 1.00 20.49 ? 729 ILE A CD1 1 ATOM 5806 N N . GLN A 1 697 ? 11.038 51.948 -12.664 1.00 17.20 ? 730 GLN A N 1 ATOM 5807 C CA . GLN A 1 697 ? 10.375 52.812 -13.623 1.00 17.23 ? 730 GLN A CA 1 ATOM 5808 C C . GLN A 1 697 ? 9.199 53.579 -12.990 1.00 17.87 ? 730 GLN A C 1 ATOM 5809 O O . GLN A 1 697 ? 8.986 54.751 -13.277 1.00 19.06 ? 730 GLN A O 1 ATOM 5810 C CB . GLN A 1 697 ? 9.868 51.929 -14.809 1.00 18.69 ? 730 GLN A CB 1 ATOM 5811 C CG . GLN A 1 697 ? 9.210 52.720 -15.960 1.00 19.62 ? 730 GLN A CG 1 ATOM 5812 C CD . GLN A 1 697 ? 10.223 53.669 -16.628 1.00 22.70 ? 730 GLN A CD 1 ATOM 5813 O OE1 . GLN A 1 697 ? 11.363 53.321 -16.810 1.00 21.99 ? 730 GLN A OE1 1 ATOM 5814 N NE2 . GLN A 1 697 ? 9.776 54.864 -16.977 1.00 26.29 ? 730 GLN A NE2 1 ATOM 5815 N N . ALA A 1 698 ? 8.427 52.884 -12.134 1.00 17.16 ? 731 ALA A N 1 ATOM 5816 C CA . ALA A 1 698 ? 7.308 53.556 -11.470 1.00 17.27 ? 731 ALA A CA 1 ATOM 5817 C C . ALA A 1 698 ? 7.803 54.682 -10.574 1.00 18.33 ? 731 ALA A C 1 ATOM 5818 O O . ALA A 1 698 ? 7.213 55.755 -10.510 1.00 17.62 ? 731 ALA A O 1 ATOM 5819 C CB . ALA A 1 698 ? 6.532 52.489 -10.649 1.00 18.55 ? 731 ALA A CB 1 ATOM 5820 N N . ALA A 1 699 ? 8.883 54.394 -9.851 1.00 18.03 ? 732 ALA A N 1 ATOM 5821 C CA . ALA A 1 699 ? 9.474 55.450 -9.013 1.00 17.12 ? 732 ALA A CA 1 ATOM 5822 C C . ALA A 1 699 ? 9.901 56.668 -9.864 1.00 17.39 ? 732 ALA A C 1 ATOM 5823 O O . ALA A 1 699 ? 9.653 57.827 -9.479 1.00 17.90 ? 732 ALA A O 1 ATOM 5824 C CB . ALA A 1 699 ? 10.668 54.855 -8.224 1.00 18.65 ? 732 ALA A CB 1 ATOM 5825 N N . ALA A 1 700 ? 10.547 56.384 -10.995 1.00 17.26 ? 733 ALA A N 1 ATOM 5826 C CA . ALA A 1 700 ? 10.898 57.498 -11.927 1.00 17.54 ? 733 ALA A CA 1 ATOM 5827 C C . ALA A 1 700 ? 9.660 58.279 -12.319 1.00 19.37 ? 733 ALA A C 1 ATOM 5828 O O . ALA A 1 700 ? 9.672 59.493 -12.435 1.00 18.51 ? 733 ALA A O 1 ATOM 5829 C CB . ALA A 1 700 ? 11.575 56.908 -13.158 1.00 18.00 ? 733 ALA A CB 1 ATOM 5830 N N . GLY A 1 701 ? 8.571 57.541 -12.580 1.00 18.33 ? 734 GLY A N 1 ATOM 5831 C CA . GLY A 1 701 ? 7.316 58.217 -12.986 1.00 18.68 ? 734 GLY A CA 1 ATOM 5832 C C . GLY A 1 701 ? 6.796 59.170 -11.948 1.00 17.81 ? 734 GLY A C 1 ATOM 5833 O O . GLY A 1 701 ? 6.078 60.138 -12.319 1.00 19.88 ? 734 GLY A O 1 ATOM 5834 N N . THR A 1 702 ? 7.100 58.926 -10.660 1.00 17.64 ? 735 THR A N 1 ATOM 5835 C CA . THR A 1 702 ? 6.543 59.841 -9.639 1.00 16.93 ? 735 THR A CA 1 ATOM 5836 C C . THR A 1 702 ? 7.247 61.202 -9.672 1.00 17.71 ? 735 THR A C 1 ATOM 5837 O O . THR A 1 702 ? 6.732 62.185 -9.085 1.00 18.77 ? 735 THR A O 1 ATOM 5838 C CB . THR A 1 702 ? 6.658 59.269 -8.192 1.00 16.69 ? 735 THR A CB 1 ATOM 5839 O OG1 . THR A 1 702 ? 8.027 59.296 -7.743 1.00 18.21 ? 735 THR A OG1 1 ATOM 5840 C CG2 . THR A 1 702 ? 6.028 57.856 -8.057 1.00 18.75 ? 735 THR A CG2 1 ATOM 5841 N N . LEU A 1 703 ? 8.402 61.255 -10.334 1.00 19.23 ? 736 LEU A N 1 ATOM 5842 C CA . LEU A 1 703 ? 9.223 62.486 -10.360 1.00 18.71 ? 736 LEU A CA 1 ATOM 5843 C C . LEU A 1 703 ? 8.816 63.379 -11.538 1.00 19.54 ? 736 LEU A C 1 ATOM 5844 O O . LEU A 1 703 ? 9.158 64.609 -11.558 1.00 21.52 ? 736 LEU A O 1 ATOM 5845 C CB . LEU A 1 703 ? 10.678 62.123 -10.475 1.00 18.94 ? 736 LEU A CB 1 ATOM 5846 C CG . LEU A 1 703 ? 11.214 61.315 -9.315 1.00 21.18 ? 736 LEU A CG 1 ATOM 5847 C CD1 . LEU A 1 703 ? 12.739 60.930 -9.582 1.00 23.12 ? 736 LEU A CD1 1 ATOM 5848 C CD2 . LEU A 1 703 ? 11.004 61.999 -7.981 1.00 23.17 ? 736 LEU A CD2 1 ATOM 5849 N N . LYS A 1 704 ? 8.130 62.799 -12.525 1.00 19.62 ? 737 LYS A N 1 ATOM 5850 C CA . LYS A 1 704 ? 7.818 63.528 -13.764 1.00 20.83 ? 737 LYS A CA 1 ATOM 5851 C C . LYS A 1 704 ? 6.866 64.689 -13.526 1.00 21.92 ? 737 LYS A C 1 ATOM 5852 O O . LYS A 1 704 ? 6.029 64.689 -12.643 1.00 22.23 ? 737 LYS A O 1 ATOM 5853 C CB . LYS A 1 704 ? 7.209 62.570 -14.765 1.00 22.56 ? 737 LYS A CB 1 ATOM 5854 C CG . LYS A 1 704 ? 8.264 61.564 -15.130 1.00 28.63 ? 737 LYS A CG 1 ATOM 5855 C CD . LYS A 1 704 ? 7.785 60.551 -16.159 1.00 30.17 ? 737 LYS A CD 1 ATOM 5856 C CE . LYS A 1 704 ? 9.004 59.690 -16.539 1.00 35.70 ? 737 LYS A CE 1 ATOM 5857 N NZ . LYS A 1 704 ? 8.554 58.465 -17.192 1.00 32.99 ? 737 LYS A NZ 1 ATOM 5858 N N . GLU A 1 705 ? 7.055 65.707 -14.373 1.00 22.94 ? 738 GLU A N 1 ATOM 5859 C CA . GLU A 1 705 ? 6.303 66.911 -14.266 1.00 25.89 ? 738 GLU A CA 1 ATOM 5860 C C . GLU A 1 705 ? 4.911 66.720 -14.832 1.00 27.51 ? 738 GLU A C 1 ATOM 5861 O O . GLU A 1 705 ? 3.931 67.302 -14.354 1.00 28.85 ? 738 GLU A O 1 ATOM 5862 C CB . GLU A 1 705 ? 7.052 68.026 -15.057 1.00 26.36 ? 738 GLU A CB 1 ATOM 5863 C CG . GLU A 1 705 ? 6.360 69.350 -14.989 1.00 31.04 ? 738 GLU A CG 1 ATOM 5864 C CD . GLU A 1 705 ? 7.126 70.426 -15.772 1.00 36.07 ? 738 GLU A CD 1 ATOM 5865 O OE1 . GLU A 1 705 ? 7.949 70.100 -16.671 1.00 36.33 ? 738 GLU A OE1 1 ATOM 5866 O OE2 . GLU A 1 705 ? 6.891 71.593 -15.449 1.00 41.08 ? 738 GLU A OE2 1 ATOM 5867 N N . VAL A 1 706 ? 4.782 65.944 -15.887 1.00 30.26 ? 739 VAL A N 1 ATOM 5868 C CA . VAL A 1 706 ? 3.404 65.821 -16.424 1.00 36.12 ? 739 VAL A CA 1 ATOM 5869 C C . VAL A 1 706 ? 3.056 64.365 -16.618 1.00 36.51 ? 739 VAL A C 1 ATOM 5870 O O . VAL A 1 706 ? 3.971 63.560 -16.809 1.00 38.14 ? 739 VAL A O 1 ATOM 5871 C CB . VAL A 1 706 ? 3.199 66.658 -17.724 1.00 36.65 ? 739 VAL A CB 1 ATOM 5872 C CG1 . VAL A 1 706 ? 1.810 66.504 -18.216 1.00 40.38 ? 739 VAL A CG1 1 ATOM 5873 C CG2 . VAL A 1 706 ? 3.484 68.155 -17.484 1.00 34.35 ? 739 VAL A CG2 1 HETATM 5874 N N B GLU B 2 . ? 18.214 44.052 18.192 0.40 22.69 ? 742 GLU A N 1 HETATM 5875 C CA B GLU B 2 . ? 17.832 42.727 18.804 0.40 22.43 ? 742 GLU A CA 1 HETATM 5876 C C B GLU B 2 . ? 18.927 41.674 18.563 0.40 22.74 ? 742 GLU A C 1 HETATM 5877 O O B GLU B 2 . ? 18.966 40.635 19.163 0.40 21.14 ? 742 GLU A O 1 HETATM 5878 C CB B GLU B 2 . ? 16.521 42.246 18.187 0.40 23.57 ? 742 GLU A CB 1 HETATM 5879 C CG B GLU B 2 . ? 16.658 42.214 16.654 0.40 21.25 ? 742 GLU A CG 1 HETATM 5880 C CD B GLU B 2 . ? 15.535 41.440 15.976 0.40 23.82 ? 742 GLU A CD 1 HETATM 5881 O OE1 B GLU B 2 . ? 14.879 40.618 16.647 0.40 22.07 ? 742 GLU A OE1 1 HETATM 5882 O OE2 B GLU B 2 . ? 15.317 41.631 14.773 0.40 26.96 ? 742 GLU A OE2 1 HETATM 5883 O OXT B GLU B 2 . ? 19.834 41.808 17.726 0.40 23.37 ? 742 GLU A OXT 1 HETATM 5884 C C1 . NAG C 3 . ? 7.523 26.413 35.762 1.00 29.64 ? 1756 NAG A C1 1 HETATM 5885 C C2 . NAG C 3 . ? 6.089 26.331 35.263 1.00 32.71 ? 1756 NAG A C2 1 HETATM 5886 C C3 . NAG C 3 . ? 5.256 25.478 36.253 1.00 35.39 ? 1756 NAG A C3 1 HETATM 5887 C C4 . NAG C 3 . ? 5.897 24.116 36.449 1.00 37.24 ? 1756 NAG A C4 1 HETATM 5888 C C5 . NAG C 3 . ? 7.342 24.327 36.942 1.00 35.18 ? 1756 NAG A C5 1 HETATM 5889 C C6 . NAG C 3 . ? 8.148 23.059 37.093 1.00 37.04 ? 1756 NAG A C6 1 HETATM 5890 C C7 . NAG C 3 . ? 4.787 27.817 33.887 1.00 37.28 ? 1756 NAG A C7 1 HETATM 5891 C C8 . NAG C 3 . ? 4.090 29.128 33.619 1.00 39.22 ? 1756 NAG A C8 1 HETATM 5892 N N2 . NAG C 3 . ? 5.451 27.619 35.045 1.00 34.06 ? 1756 NAG A N2 1 HETATM 5893 O O3 . NAG C 3 . ? 3.964 25.319 35.713 1.00 42.67 ? 1756 NAG A O3 1 HETATM 5894 O O4 . NAG C 3 . ? 5.109 23.317 37.349 1.00 41.10 ? 1756 NAG A O4 1 HETATM 5895 O O5 . NAG C 3 . ? 8.015 25.093 35.912 1.00 31.51 ? 1756 NAG A O5 1 HETATM 5896 O O6 . NAG C 3 . ? 8.029 22.388 35.846 1.00 40.01 ? 1756 NAG A O6 1 HETATM 5897 O O7 . NAG C 3 . ? 4.731 26.947 33.010 1.00 41.82 ? 1756 NAG A O7 1 HETATM 5898 C C1 . NAG D 3 . ? 39.000 53.389 23.282 1.00 28.65 ? 1758 NAG A C1 1 HETATM 5899 C C2 . NAG D 3 . ? 39.311 51.911 23.018 1.00 27.20 ? 1758 NAG A C2 1 HETATM 5900 C C3 . NAG D 3 . ? 40.665 51.508 23.608 1.00 30.96 ? 1758 NAG A C3 1 HETATM 5901 C C4 . NAG D 3 . ? 41.744 52.506 23.158 1.00 32.68 ? 1758 NAG A C4 1 HETATM 5902 C C5 . NAG D 3 . ? 41.260 53.937 23.501 1.00 33.98 ? 1758 NAG A C5 1 HETATM 5903 C C6 . NAG D 3 . ? 42.225 55.069 23.137 1.00 35.01 ? 1758 NAG A C6 1 HETATM 5904 C C7 . NAG D 3 . ? 37.494 50.322 22.952 1.00 26.84 ? 1758 NAG A C7 1 HETATM 5905 C C8 . NAG D 3 . ? 36.393 49.650 23.710 1.00 25.88 ? 1758 NAG A C8 1 HETATM 5906 N N2 . NAG D 3 . ? 38.228 51.175 23.648 1.00 26.64 ? 1758 NAG A N2 1 HETATM 5907 O O3 . NAG D 3 . ? 40.912 50.202 23.135 1.00 28.65 ? 1758 NAG A O3 1 HETATM 5908 O O4 . NAG D 3 . ? 42.966 52.209 23.850 1.00 33.51 ? 1758 NAG A O4 1 HETATM 5909 O O5 . NAG D 3 . ? 40.046 54.194 22.809 1.00 31.74 ? 1758 NAG A O5 1 HETATM 5910 O O6 . NAG D 3 . ? 42.572 54.912 21.777 1.00 39.04 ? 1758 NAG A O6 1 HETATM 5911 O O7 . NAG D 3 . ? 37.692 50.097 21.765 1.00 26.25 ? 1758 NAG A O7 1 HETATM 5912 C C1 . NAG E 3 . ? 12.701 53.453 -20.420 1.00 21.33 ? 1759 NAG A C1 1 HETATM 5913 C C2 . NAG E 3 . ? 11.695 52.272 -20.397 1.00 19.56 ? 1759 NAG A C2 1 HETATM 5914 C C3 . NAG E 3 . ? 11.715 51.776 -21.866 1.00 23.96 ? 1759 NAG A C3 1 HETATM 5915 C C4 . NAG E 3 . ? 11.377 52.862 -22.864 1.00 27.88 ? 1759 NAG A C4 1 HETATM 5916 C C5 . NAG E 3 . ? 12.222 54.120 -22.584 1.00 27.94 ? 1759 NAG A C5 1 HETATM 5917 C C6 . NAG E 3 . ? 11.769 55.338 -23.382 1.00 29.62 ? 1759 NAG A C6 1 HETATM 5918 C C7 . NAG E 3 . ? 11.227 50.569 -18.733 1.00 19.93 ? 1759 NAG A C7 1 HETATM 5919 C C8 . NAG E 3 . ? 11.796 49.449 -17.945 1.00 21.79 ? 1759 NAG A C8 1 HETATM 5920 N N2 . NAG E 3 . ? 12.114 51.229 -19.535 1.00 18.99 ? 1759 NAG A N2 1 HETATM 5921 O O3 . NAG E 3 . ? 10.759 50.714 -21.945 1.00 25.99 ? 1759 NAG A O3 1 HETATM 5922 O O4 . NAG E 3 . ? 11.742 52.453 -24.207 1.00 30.52 ? 1759 NAG A O4 1 HETATM 5923 O O5 . NAG E 3 . ? 12.133 54.481 -21.187 1.00 23.80 ? 1759 NAG A O5 1 HETATM 5924 O O6 . NAG E 3 . ? 10.423 55.625 -23.043 1.00 40.61 ? 1759 NAG A O6 1 HETATM 5925 O O7 . NAG E 3 . ? 10.029 50.896 -18.637 1.00 22.45 ? 1759 NAG A O7 1 HETATM 5926 C C1 . NAG F 3 . ? 10.729 51.777 -24.975 1.00 34.33 ? 1760 NAG A C1 1 HETATM 5927 C C2 . NAG F 3 . ? 10.983 52.121 -26.435 1.00 39.01 ? 1760 NAG A C2 1 HETATM 5928 C C3 . NAG F 3 . ? 9.935 51.396 -27.262 1.00 40.54 ? 1760 NAG A C3 1 HETATM 5929 C C4 . NAG F 3 . ? 9.937 49.900 -26.979 1.00 41.50 ? 1760 NAG A C4 1 HETATM 5930 C C5 . NAG F 3 . ? 9.928 49.586 -25.492 1.00 39.97 ? 1760 NAG A C5 1 HETATM 5931 C C6 . NAG F 3 . ? 10.368 48.154 -25.279 1.00 40.87 ? 1760 NAG A C6 1 HETATM 5932 C C7 . NAG F 3 . ? 12.149 54.221 -26.937 1.00 44.56 ? 1760 NAG A C7 1 HETATM 5933 C C8 . NAG F 3 . ? 12.015 55.691 -27.273 1.00 42.04 ? 1760 NAG A C8 1 HETATM 5934 N N2 . NAG F 3 . ? 10.989 53.548 -26.754 1.00 41.97 ? 1760 NAG A N2 1 HETATM 5935 O O3 . NAG F 3 . ? 10.276 51.604 -28.620 1.00 41.26 ? 1760 NAG A O3 1 HETATM 5936 O O4 . NAG F 3 . ? 8.759 49.333 -27.552 1.00 45.81 ? 1760 NAG A O4 1 HETATM 5937 O O5 . NAG F 3 . ? 10.892 50.402 -24.824 1.00 34.41 ? 1760 NAG A O5 1 HETATM 5938 O O6 . NAG F 3 . ? 10.213 47.808 -23.912 1.00 45.03 ? 1760 NAG A O6 1 HETATM 5939 O O7 . NAG F 3 . ? 13.281 53.700 -26.804 1.00 44.73 ? 1760 NAG A O7 1 HETATM 5940 C C1 . NAG G 3 . ? 19.759 11.415 8.221 0.60 42.24 ? 1766 NAG A C1 1 HETATM 5941 C C2 . NAG G 3 . ? 18.851 10.500 9.099 0.60 46.56 ? 1766 NAG A C2 1 HETATM 5942 C C3 . NAG G 3 . ? 17.962 9.526 8.328 0.60 48.51 ? 1766 NAG A C3 1 HETATM 5943 C C4 . NAG G 3 . ? 17.348 10.179 7.102 0.60 49.09 ? 1766 NAG A C4 1 HETATM 5944 C C5 . NAG G 3 . ? 18.441 10.807 6.243 0.60 48.87 ? 1766 NAG A C5 1 HETATM 5945 C C6 . NAG G 3 . ? 17.822 11.559 5.073 0.60 51.13 ? 1766 NAG A C6 1 HETATM 5946 C C7 . NAG G 3 . ? 19.214 9.034 11.118 0.60 49.32 ? 1766 NAG A C7 1 HETATM 5947 C C8 . NAG G 3 . ? 20.296 8.425 11.968 0.60 51.05 ? 1766 NAG A C8 1 HETATM 5948 N N2 . NAG G 3 . ? 19.649 9.773 10.087 0.60 47.36 ? 1766 NAG A N2 1 HETATM 5949 O O3 . NAG G 3 . ? 16.936 9.047 9.176 0.60 48.47 ? 1766 NAG A O3 1 HETATM 5950 O O4 . NAG G 3 . ? 16.675 9.176 6.373 0.60 51.76 ? 1766 NAG A O4 1 HETATM 5951 O O5 . NAG G 3 . ? 19.208 11.758 6.960 0.60 46.66 ? 1766 NAG A O5 1 HETATM 5952 O O6 . NAG G 3 . ? 17.346 12.806 5.545 0.60 54.72 ? 1766 NAG A O6 1 HETATM 5953 O O7 . NAG G 3 . ? 18.027 8.825 11.407 0.60 49.75 ? 1766 NAG A O7 1 HETATM 5954 ZN ZN A ZN H 4 . ? 20.106 44.270 21.434 0.50 21.52 ? 1751 ZN A ZN 1 HETATM 5955 ZN ZN B ZN H 4 . ? 20.076 44.322 21.883 0.45 16.33 ? 1751 ZN A ZN 1 HETATM 5956 ZN ZN A ZN I 4 . ? 19.610 48.012 20.453 0.40 20.18 ? 1752 ZN A ZN 1 HETATM 5957 ZN ZN B ZN I 4 . ? 19.476 47.796 20.614 0.40 18.49 ? 1752 ZN A ZN 1 HETATM 5958 CL CL . CL J 5 . ? 20.938 53.648 15.968 1.00 25.40 ? 1754 CL A CL 1 HETATM 5959 CA CA . CA K 6 . ? 1.028 43.021 15.167 1.00 16.82 ? 1755 CA A CA 1 HETATM 5960 C C1 . GOL L 7 . ? 23.372 40.085 14.405 0.35 22.83 ? 1 GOL A C1 1 HETATM 5961 O O1 . GOL L 7 . ? 23.951 40.753 13.304 0.35 26.82 ? 1 GOL A O1 1 HETATM 5962 C C2 . GOL L 7 . ? 22.001 40.672 14.686 0.35 20.21 ? 1 GOL A C2 1 HETATM 5963 O O2 . GOL L 7 . ? 22.188 42.000 15.124 0.35 22.87 ? 1 GOL A O2 1 HETATM 5964 C C3 . GOL L 7 . ? 21.452 39.930 15.886 0.35 23.26 ? 1 GOL A C3 1 HETATM 5965 O O3 . GOL L 7 . ? 22.027 40.654 16.934 0.30 22.58 ? 1 GOL A O3 1 HETATM 5966 C C1 . GOL M 7 . ? 5.802 35.761 -4.058 0.80 42.47 ? 2 GOL A C1 1 HETATM 5967 O O1 . GOL M 7 . ? 4.602 35.989 -3.364 0.80 38.80 ? 2 GOL A O1 1 HETATM 5968 C C2 . GOL M 7 . ? 6.573 37.073 -4.049 0.80 42.19 ? 2 GOL A C2 1 HETATM 5969 O O2 . GOL M 7 . ? 5.903 38.088 -3.315 0.80 40.39 ? 2 GOL A O2 1 HETATM 5970 C C3 . GOL M 7 . ? 6.872 37.496 -5.471 0.80 43.06 ? 2 GOL A C3 1 HETATM 5971 O O3 . GOL M 7 . ? 7.141 38.874 -5.465 0.80 32.89 ? 2 GOL A O3 1 HETATM 5972 S S1 A MPO N 8 . ? 19.860 45.283 18.952 0.40 30.13 ? 741 MPO A S1 1 HETATM 5973 O O1 A MPO N 8 . ? 19.043 45.030 20.142 0.40 26.18 ? 741 MPO A O1 1 HETATM 5974 O O2 A MPO N 8 . ? 21.062 44.408 18.996 0.40 29.19 ? 741 MPO A O2 1 HETATM 5975 O O4 A MPO N 8 . ? 15.425 41.140 16.573 0.40 30.85 ? 741 MPO A O4 1 HETATM 5976 N N1 A MPO N 8 . ? 17.168 42.007 18.499 0.40 30.33 ? 741 MPO A N1 1 HETATM 5977 C C1 A MPO N 8 . ? 18.873 44.940 17.677 0.40 22.65 ? 741 MPO A C1 1 HETATM 5978 O O3 A MPO N 8 . ? 20.223 46.734 18.969 0.40 30.61 ? 741 MPO A O3 1 HETATM 5979 C C2 A MPO N 8 . ? 18.715 43.417 17.583 0.40 28.35 ? 741 MPO A C2 1 HETATM 5980 C C3 A MPO N 8 . ? 18.340 42.742 18.906 0.40 27.60 ? 741 MPO A C3 1 HETATM 5981 C C4 A MPO N 8 . ? 15.914 42.718 18.379 0.40 27.56 ? 741 MPO A C4 1 HETATM 5982 C C5 A MPO N 8 . ? 14.946 41.724 17.775 0.40 25.68 ? 741 MPO A C5 1 HETATM 5983 C C6 A MPO N 8 . ? 16.667 40.442 16.736 0.40 31.61 ? 741 MPO A C6 1 HETATM 5984 C C7 A MPO N 8 . ? 17.262 40.594 18.138 0.40 31.42 ? 741 MPO A C7 1 HETATM 5985 O O . HOH O 9 . ? 14.454 42.894 -5.573 1.00 17.30 ? 3 HOH A O 1 HETATM 5986 O O . HOH O 9 . ? 11.036 59.613 0.247 1.00 14.87 ? 4 HOH A O 1 HETATM 5987 O O . HOH O 9 . ? -2.894 63.572 5.268 1.00 15.26 ? 5 HOH A O 1 HETATM 5988 O O . HOH O 9 . ? 27.018 33.065 24.551 1.00 19.58 ? 6 HOH A O 1 HETATM 5989 O O . HOH O 9 . ? 0.000 67.559 0.000 0.50 15.05 ? 7 HOH A O 1 HETATM 5990 O O . HOH O 9 . ? 16.010 51.713 18.369 1.00 17.05 ? 8 HOH A O 1 HETATM 5991 O O . HOH O 9 . ? -0.397 39.394 21.035 1.00 16.71 ? 9 HOH A O 1 HETATM 5992 O O . HOH O 9 . ? 10.404 59.155 3.169 1.00 15.03 ? 10 HOH A O 1 HETATM 5993 O O . HOH O 9 . ? 4.482 56.201 -11.127 1.00 15.56 ? 11 HOH A O 1 HETATM 5994 O O . HOH O 9 . ? -4.779 61.526 5.820 1.00 14.93 ? 12 HOH A O 1 HETATM 5995 O O . HOH O 9 . ? -1.089 47.607 9.788 1.00 15.11 ? 13 HOH A O 1 HETATM 5996 O O . HOH O 9 . ? 17.084 36.022 25.213 1.00 16.95 ? 14 HOH A O 1 HETATM 5997 O O . HOH O 9 . ? 4.974 38.178 0.184 1.00 19.86 ? 15 HOH A O 1 HETATM 5998 O O . HOH O 9 . ? 31.677 33.062 18.299 1.00 21.29 ? 16 HOH A O 1 HETATM 5999 O O . HOH O 9 . ? 23.047 11.488 37.988 1.00 17.37 ? 17 HOH A O 1 HETATM 6000 O O . HOH O 9 . ? 26.007 37.341 30.742 1.00 25.72 ? 18 HOH A O 1 HETATM 6001 O O . HOH O 9 . ? 0.329 44.784 6.656 1.00 15.70 ? 19 HOH A O 1 HETATM 6002 O O . HOH O 9 . ? 4.748 62.438 -11.569 1.00 17.67 ? 21 HOH A O 1 HETATM 6003 O O . HOH O 9 . ? -5.905 45.305 15.828 1.00 17.97 ? 22 HOH A O 1 HETATM 6004 O O . HOH O 9 . ? 33.753 17.215 25.231 1.00 19.66 ? 23 HOH A O 1 HETATM 6005 O O . HOH O 9 . ? 15.104 30.784 -8.567 1.00 26.91 ? 24 HOH A O 1 HETATM 6006 O O . HOH O 9 . ? 12.573 39.413 -16.692 1.00 20.64 ? 25 HOH A O 1 HETATM 6007 O O . HOH O 9 . ? 25.271 35.542 15.945 1.00 23.32 ? 26 HOH A O 1 HETATM 6008 O O . HOH O 9 . ? -3.562 56.829 13.761 1.00 17.91 ? 27 HOH A O 1 HETATM 6009 O O . HOH O 9 . ? 6.574 68.717 3.571 1.00 17.09 ? 28 HOH A O 1 HETATM 6010 O O . HOH O 9 . ? 32.915 45.069 25.280 1.00 23.28 ? 29 HOH A O 1 HETATM 6011 O O . HOH O 9 . ? 21.621 62.459 -0.850 1.00 20.05 ? 30 HOH A O 1 HETATM 6012 O O . HOH O 9 . ? 13.972 44.321 34.476 1.00 21.42 ? 31 HOH A O 1 HETATM 6013 O O . HOH O 9 . ? 22.078 66.817 -7.566 1.00 21.22 ? 32 HOH A O 1 HETATM 6014 O O . HOH O 9 . ? 28.828 38.969 24.023 1.00 23.99 ? 33 HOH A O 1 HETATM 6015 O O . HOH O 9 . ? 12.313 27.272 -8.059 1.00 48.05 ? 743 HOH A O 1 HETATM 6016 O O . HOH O 9 . ? 7.211 28.492 -13.521 1.00 44.93 ? 744 HOH A O 1 HETATM 6017 O O . HOH O 9 . ? 5.928 62.425 -18.852 1.00 38.13 ? 745 HOH A O 1 HETATM 6018 O O . HOH O 9 . ? 17.187 29.389 26.306 1.00 17.31 ? 746 HOH A O 1 HETATM 6019 O O . HOH O 9 . ? 10.485 47.809 19.361 1.00 16.21 ? 747 HOH A O 1 HETATM 6020 O O . HOH O 9 . ? 11.514 64.429 -13.713 1.00 22.54 ? 748 HOH A O 1 HETATM 6021 O O . HOH O 9 . ? 14.189 55.631 24.648 1.00 18.82 ? 749 HOH A O 1 HETATM 6022 O O . HOH O 9 . ? 31.783 33.627 27.560 1.00 23.87 ? 750 HOH A O 1 HETATM 6023 O O . HOH O 9 . ? 25.313 57.959 24.575 1.00 19.60 ? 751 HOH A O 1 HETATM 6024 O O . HOH O 9 . ? 1.499 38.840 -1.621 1.00 19.25 ? 752 HOH A O 1 HETATM 6025 O O . HOH O 9 . ? 25.271 49.697 34.662 1.00 24.59 ? 753 HOH A O 1 HETATM 6026 O O . HOH O 9 . ? 22.008 11.610 18.470 1.00 28.72 ? 754 HOH A O 1 HETATM 6027 O O . HOH O 9 . ? 4.370 74.511 1.305 1.00 18.74 ? 755 HOH A O 1 HETATM 6028 O O . HOH O 9 . ? 5.199 36.283 5.318 1.00 23.02 ? 756 HOH A O 1 HETATM 6029 O O . HOH O 9 . ? 5.210 56.924 -4.426 1.00 16.37 ? 757 HOH A O 1 HETATM 6030 O O . HOH O 9 . ? 17.799 61.146 34.451 1.00 24.11 ? 758 HOH A O 1 HETATM 6031 O O . HOH O 9 . ? 20.455 61.606 -11.916 1.00 23.24 ? 759 HOH A O 1 HETATM 6032 O O . HOH O 9 . ? 11.915 27.165 26.100 1.00 22.58 ? 760 HOH A O 1 HETATM 6033 O O . HOH O 9 . ? 40.333 18.905 21.938 1.00 23.26 ? 761 HOH A O 1 HETATM 6034 O O . HOH O 9 . ? 30.824 29.446 30.528 1.00 24.82 ? 762 HOH A O 1 HETATM 6035 O O . HOH O 9 . ? -6.556 31.847 16.880 1.00 23.97 ? 763 HOH A O 1 HETATM 6036 O O . HOH O 9 . ? 20.322 64.542 1.541 1.00 21.06 ? 764 HOH A O 1 HETATM 6037 O O . HOH O 9 . ? 13.498 27.982 32.359 1.00 22.19 ? 765 HOH A O 1 HETATM 6038 O O . HOH O 9 . ? 15.038 42.232 -19.211 1.00 23.50 ? 766 HOH A O 1 HETATM 6039 O O . HOH O 9 . ? -5.393 52.842 14.174 1.00 19.81 ? 767 HOH A O 1 HETATM 6040 O O . HOH O 9 . ? 3.478 49.059 3.002 1.00 22.36 ? 768 HOH A O 1 HETATM 6041 O O . HOH O 9 . ? 0.276 78.718 -3.481 1.00 23.49 ? 769 HOH A O 1 HETATM 6042 O O . HOH O 9 . ? 21.415 40.580 -19.492 1.00 30.57 ? 770 HOH A O 1 HETATM 6043 O O . HOH O 9 . ? 30.044 68.864 26.479 1.00 26.57 ? 771 HOH A O 1 HETATM 6044 O O . HOH O 9 . ? -2.782 38.783 12.389 1.00 19.38 ? 772 HOH A O 1 HETATM 6045 O O . HOH O 9 . ? 10.907 57.400 -18.097 1.00 26.25 ? 773 HOH A O 1 HETATM 6046 O O . HOH O 9 . ? 18.906 74.331 22.064 1.00 25.13 ? 774 HOH A O 1 HETATM 6047 O O . HOH O 9 . ? 6.461 41.283 -13.279 1.00 20.86 ? 775 HOH A O 1 HETATM 6048 O O . HOH O 9 . ? 22.494 44.179 29.019 1.00 21.84 ? 776 HOH A O 1 HETATM 6049 O O . HOH O 9 . ? 14.543 71.662 27.751 1.00 28.84 ? 777 HOH A O 1 HETATM 6050 O O A HOH O 9 . ? 31.749 26.081 5.876 0.50 20.14 ? 778 HOH A O 1 HETATM 6051 O O B HOH O 9 . ? 32.329 27.148 6.179 0.50 23.75 ? 778 HOH A O 1 HETATM 6052 O O . HOH O 9 . ? 4.432 36.016 8.039 1.00 27.65 ? 779 HOH A O 1 HETATM 6053 O O . HOH O 9 . ? 0.663 64.210 26.793 1.00 29.25 ? 780 HOH A O 1 HETATM 6054 O O . HOH O 9 . ? 27.657 29.376 30.353 1.00 28.59 ? 781 HOH A O 1 HETATM 6055 O O . HOH O 9 . ? 24.359 29.599 30.070 1.00 23.80 ? 782 HOH A O 1 HETATM 6056 O O A HOH O 9 . ? -0.914 54.622 18.458 0.50 14.80 ? 783 HOH A O 1 HETATM 6057 O O B HOH O 9 . ? -1.217 55.514 18.752 0.50 39.75 ? 783 HOH A O 1 HETATM 6058 O O . HOH O 9 . ? 28.145 72.062 6.029 1.00 26.91 ? 784 HOH A O 1 HETATM 6059 O O . HOH O 9 . ? 13.833 18.508 19.884 1.00 26.78 ? 785 HOH A O 1 HETATM 6060 O O . HOH O 9 . ? 18.940 48.068 -21.315 1.00 28.25 ? 786 HOH A O 1 HETATM 6061 O O . HOH O 9 . ? 14.149 78.004 -5.895 1.00 21.44 ? 787 HOH A O 1 HETATM 6062 O O . HOH O 9 . ? 16.490 54.951 22.886 1.00 18.49 ? 788 HOH A O 1 HETATM 6063 O O . HOH O 9 . ? 1.986 61.894 21.849 1.00 35.04 ? 789 HOH A O 1 HETATM 6064 O O . HOH O 9 . ? 22.117 66.667 -14.835 1.00 29.59 ? 790 HOH A O 1 HETATM 6065 O O . HOH O 9 . ? 0.422 48.006 5.788 1.00 22.76 ? 791 HOH A O 1 HETATM 6066 O O . HOH O 9 . ? 36.301 20.364 19.283 1.00 29.63 ? 792 HOH A O 1 HETATM 6067 O O . HOH O 9 . ? 6.043 78.959 0.428 1.00 26.00 ? 793 HOH A O 1 HETATM 6068 O O . HOH O 9 . ? 26.582 67.568 1.280 1.00 27.31 ? 794 HOH A O 1 HETATM 6069 O O . HOH O 9 . ? 3.683 52.248 2.837 1.00 23.00 ? 795 HOH A O 1 HETATM 6070 O O . HOH O 9 . ? 18.023 77.924 -6.813 1.00 25.14 ? 796 HOH A O 1 HETATM 6071 O O . HOH O 9 . ? 21.496 51.840 -17.005 1.00 26.88 ? 797 HOH A O 1 HETATM 6072 O O . HOH O 9 . ? 31.087 67.212 18.934 1.00 27.81 ? 798 HOH A O 1 HETATM 6073 O O . HOH O 9 . ? 10.375 76.866 12.035 1.00 24.73 ? 799 HOH A O 1 HETATM 6074 O O . HOH O 9 . ? 10.016 74.334 -10.649 1.00 30.25 ? 800 HOH A O 1 HETATM 6075 O O . HOH O 9 . ? 18.929 45.786 20.480 0.40 13.89 ? 801 HOH A O 1 HETATM 6076 O O . HOH O 9 . ? 20.489 43.678 19.749 0.40 17.18 ? 802 HOH A O 1 HETATM 6077 O O . HOH O 9 . ? 20.916 46.520 12.979 0.40 25.25 ? 803 HOH A O 1 HETATM 6078 O O . HOH O 9 . ? 23.241 47.980 19.195 0.40 21.55 ? 804 HOH A O 1 HETATM 6079 O O . HOH O 9 . ? 20.737 46.977 19.302 0.40 15.57 ? 805 HOH A O 1 HETATM 6080 O O . HOH O 9 . ? 20.224 45.389 18.706 0.40 12.74 ? 806 HOH A O 1 HETATM 6081 O O . HOH O 9 . ? 20.854 34.054 7.083 0.40 29.44 ? 807 HOH A O 1 HETATM 6082 O O . HOH O 9 . ? 21.689 36.842 9.081 0.40 23.20 ? 808 HOH A O 1 HETATM 6083 O O . HOH O 9 . ? 18.779 37.696 9.162 0.40 36.59 ? 809 HOH A O 1 HETATM 6084 O O . HOH O 9 . ? -2.053 56.052 -1.007 1.00 23.83 ? 810 HOH A O 1 HETATM 6085 O O . HOH O 9 . ? 13.491 28.637 -17.461 1.00 32.44 ? 811 HOH A O 1 HETATM 6086 O O . HOH O 9 . ? 8.441 28.004 24.987 1.00 29.25 ? 812 HOH A O 1 HETATM 6087 O O . HOH O 9 . ? 25.010 57.391 -4.459 1.00 30.28 ? 813 HOH A O 1 HETATM 6088 O O . HOH O 9 . ? 7.589 39.011 6.097 1.00 17.37 ? 814 HOH A O 1 HETATM 6089 O O . HOH O 9 . ? 14.122 43.677 26.738 1.00 16.45 ? 815 HOH A O 1 HETATM 6090 O O . HOH O 9 . ? 2.663 41.446 14.442 1.00 15.26 ? 816 HOH A O 1 HETATM 6091 O O . HOH O 9 . ? 7.457 60.854 -5.456 1.00 16.09 ? 817 HOH A O 1 HETATM 6092 O O . HOH O 9 . ? 21.070 56.496 14.894 1.00 18.13 ? 818 HOH A O 1 HETATM 6093 O O . HOH O 9 . ? 12.642 42.332 -7.426 1.00 19.50 ? 819 HOH A O 1 HETATM 6094 O O . HOH O 9 . ? -3.335 66.215 6.006 1.00 15.96 ? 820 HOH A O 1 HETATM 6095 O O . HOH O 9 . ? 17.615 41.257 33.359 1.00 21.22 ? 821 HOH A O 1 HETATM 6096 O O . HOH O 9 . ? 1.236 47.183 8.138 1.00 15.42 ? 822 HOH A O 1 HETATM 6097 O O . HOH O 9 . ? -3.249 53.784 10.647 1.00 15.43 ? 823 HOH A O 1 HETATM 6098 O O . HOH O 9 . ? 10.482 48.297 13.253 1.00 18.61 ? 824 HOH A O 1 HETATM 6099 O O . HOH O 9 . ? -1.018 64.227 3.221 1.00 17.76 ? 825 HOH A O 1 HETATM 6100 O O . HOH O 9 . ? 2.499 44.727 -6.913 1.00 16.35 ? 826 HOH A O 1 HETATM 6101 O O . HOH O 9 . ? 15.071 58.181 25.677 1.00 18.91 ? 827 HOH A O 1 HETATM 6102 O O . HOH O 9 . ? -4.195 40.116 14.291 1.00 20.10 ? 828 HOH A O 1 HETATM 6103 O O . HOH O 9 . ? 24.806 37.504 17.800 1.00 27.43 ? 829 HOH A O 1 HETATM 6104 O O . HOH O 9 . ? -3.734 58.948 5.635 1.00 16.33 ? 830 HOH A O 1 HETATM 6105 O O . HOH O 9 . ? 17.121 74.584 -13.764 1.00 21.15 ? 831 HOH A O 1 HETATM 6106 O O . HOH O 9 . ? 5.521 66.713 1.708 1.00 17.25 ? 832 HOH A O 1 HETATM 6107 O O . HOH O 9 . ? 20.084 44.991 25.588 1.00 18.48 ? 833 HOH A O 1 HETATM 6108 O O . HOH O 9 . ? 9.498 44.540 12.259 1.00 20.36 ? 834 HOH A O 1 HETATM 6109 O O . HOH O 9 . ? 1.162 36.240 -0.752 1.00 20.98 ? 835 HOH A O 1 HETATM 6110 O O . HOH O 9 . ? 38.597 17.271 7.961 1.00 23.10 ? 836 HOH A O 1 HETATM 6111 O O . HOH O 9 . ? 6.610 46.981 31.575 1.00 20.93 ? 837 HOH A O 1 HETATM 6112 O O . HOH O 9 . ? 8.410 47.042 29.472 1.00 19.58 ? 838 HOH A O 1 HETATM 6113 O O . HOH O 9 . ? 6.923 37.128 8.242 1.00 21.76 ? 839 HOH A O 1 HETATM 6114 O O . HOH O 9 . ? 7.712 41.623 -5.131 1.00 19.86 ? 840 HOH A O 1 HETATM 6115 O O . HOH O 9 . ? 28.875 36.915 22.530 1.00 30.78 ? 841 HOH A O 1 HETATM 6116 O O . HOH O 9 . ? 5.725 72.119 1.792 1.00 18.13 ? 842 HOH A O 1 HETATM 6117 O O A HOH O 9 . ? 8.166 44.957 8.391 0.50 12.97 ? 843 HOH A O 1 HETATM 6118 O O B HOH O 9 . ? 7.919 45.514 9.339 0.25 8.15 ? 843 HOH A O 1 HETATM 6119 O O C HOH O 9 . ? 9.758 44.921 7.484 0.25 12.35 ? 843 HOH A O 1 HETATM 6120 O O . HOH O 9 . ? 4.415 45.041 31.545 1.00 23.92 ? 844 HOH A O 1 HETATM 6121 O O . HOH O 9 . ? -3.172 55.430 3.105 1.00 17.50 ? 845 HOH A O 1 HETATM 6122 O O . HOH O 9 . ? -10.458 38.855 18.359 1.00 24.28 ? 846 HOH A O 1 HETATM 6123 O O . HOH O 9 . ? 19.291 55.602 -11.794 1.00 23.40 ? 847 HOH A O 1 HETATM 6124 O O . HOH O 9 . ? 22.578 44.067 26.292 1.00 20.72 ? 848 HOH A O 1 HETATM 6125 O O A HOH O 9 . ? 18.539 70.426 -6.121 0.60 20.84 ? 849 HOH A O 1 HETATM 6126 O O B HOH O 9 . ? 17.895 70.540 -7.163 0.40 18.58 ? 849 HOH A O 1 HETATM 6127 O O . HOH O 9 . ? 3.619 35.823 0.417 1.00 24.49 ? 850 HOH A O 1 HETATM 6128 O O . HOH O 9 . ? -0.338 34.227 27.196 1.00 26.16 ? 851 HOH A O 1 HETATM 6129 O O . HOH O 9 . ? 15.074 41.736 34.588 1.00 24.07 ? 852 HOH A O 1 HETATM 6130 O O . HOH O 9 . ? 8.718 28.770 22.042 1.00 20.66 ? 853 HOH A O 1 HETATM 6131 O O . HOH O 9 . ? 41.064 18.488 8.151 1.00 25.05 ? 854 HOH A O 1 HETATM 6132 O O . HOH O 9 . ? 5.586 77.003 2.309 1.00 22.23 ? 855 HOH A O 1 HETATM 6133 O O . HOH O 9 . ? 2.205 47.428 -7.211 1.00 17.66 ? 856 HOH A O 1 HETATM 6134 O O . HOH O 9 . ? 12.919 59.177 -17.598 1.00 26.80 ? 857 HOH A O 1 HETATM 6135 O O . HOH O 9 . ? 5.163 59.906 33.858 1.00 23.83 ? 858 HOH A O 1 HETATM 6136 O O . HOH O 9 . ? 0.393 76.327 7.239 1.00 29.30 ? 859 HOH A O 1 HETATM 6137 O O . HOH O 9 . ? 24.179 44.724 31.484 1.00 24.03 ? 860 HOH A O 1 HETATM 6138 O O . HOH O 9 . ? 7.371 77.290 -8.865 1.00 25.40 ? 861 HOH A O 1 HETATM 6139 O O . HOH O 9 . ? 33.838 47.542 21.097 1.00 26.34 ? 862 HOH A O 1 HETATM 6140 O O . HOH O 9 . ? 29.811 68.495 29.247 1.00 26.36 ? 863 HOH A O 1 HETATM 6141 O O . HOH O 9 . ? 13.261 35.988 -4.503 1.00 25.90 ? 864 HOH A O 1 HETATM 6142 O O . HOH O 9 . ? 6.926 43.884 -13.787 1.00 22.10 ? 865 HOH A O 1 HETATM 6143 O O . HOH O 9 . ? 10.524 41.148 -6.217 1.00 19.63 ? 866 HOH A O 1 HETATM 6144 O O . HOH O 9 . ? 10.291 30.414 24.999 1.00 23.71 ? 867 HOH A O 1 HETATM 6145 O O A HOH O 9 . ? 0.667 57.528 19.329 0.50 18.72 ? 868 HOH A O 1 HETATM 6146 O O B HOH O 9 . ? 0.082 57.137 19.028 0.50 29.89 ? 868 HOH A O 1 HETATM 6147 O O . HOH O 9 . ? 7.788 24.360 22.992 1.00 25.76 ? 869 HOH A O 1 HETATM 6148 O O . HOH O 9 . ? 24.179 65.732 -6.273 1.00 29.14 ? 870 HOH A O 1 HETATM 6149 O O . HOH O 9 . ? 14.894 15.558 13.714 1.00 38.46 ? 871 HOH A O 1 HETATM 6150 O O . HOH O 9 . ? 36.611 25.492 30.448 1.00 28.08 ? 872 HOH A O 1 HETATM 6151 O O . HOH O 9 . ? 32.153 66.008 21.057 1.00 26.92 ? 873 HOH A O 1 HETATM 6152 O O . HOH O 9 . ? 12.198 41.955 -17.660 1.00 29.80 ? 874 HOH A O 1 HETATM 6153 O O . HOH O 9 . ? 5.763 72.578 -7.852 1.00 26.68 ? 875 HOH A O 1 HETATM 6154 O O . HOH O 9 . ? 8.072 77.669 21.236 1.00 28.05 ? 876 HOH A O 1 HETATM 6155 O O . HOH O 9 . ? 16.090 68.588 -1.824 1.00 25.97 ? 877 HOH A O 1 HETATM 6156 O O . HOH O 9 . ? 11.595 63.696 -16.419 1.00 31.53 ? 878 HOH A O 1 HETATM 6157 O O . HOH O 9 . ? 1.468 42.199 31.307 1.00 27.16 ? 879 HOH A O 1 HETATM 6158 O O . HOH O 9 . ? -3.592 30.029 14.641 1.00 27.37 ? 880 HOH A O 1 HETATM 6159 O O . HOH O 9 . ? 35.988 59.981 25.673 1.00 26.90 ? 881 HOH A O 1 HETATM 6160 O O . HOH O 9 . ? 36.722 50.890 18.940 1.00 29.52 ? 882 HOH A O 1 HETATM 6161 O O . HOH O 9 . ? 12.085 81.616 -4.914 1.00 26.87 ? 883 HOH A O 1 HETATM 6162 O O . HOH O 9 . ? 29.874 54.662 7.890 1.00 31.67 ? 884 HOH A O 1 HETATM 6163 O O . HOH O 9 . ? -0.033 40.702 -0.541 0.50 17.05 ? 885 HOH A O 1 HETATM 6164 O O . HOH O 9 . ? 31.621 26.442 3.177 1.00 39.12 ? 886 HOH A O 1 HETATM 6165 O O . HOH O 9 . ? 7.670 56.053 -15.486 1.00 23.18 ? 887 HOH A O 1 HETATM 6166 O O . HOH O 9 . ? 42.271 27.104 18.886 1.00 28.41 ? 888 HOH A O 1 HETATM 6167 O O . HOH O 9 . ? 18.473 52.623 36.606 1.00 29.43 ? 889 HOH A O 1 HETATM 6168 O O . HOH O 9 . ? 14.851 74.869 2.195 1.00 26.68 ? 890 HOH A O 1 HETATM 6169 O O A HOH O 9 . ? -4.243 59.403 14.528 0.50 15.78 ? 891 HOH A O 1 HETATM 6170 O O B HOH O 9 . ? -3.866 59.487 16.883 0.50 32.99 ? 891 HOH A O 1 HETATM 6171 O O . HOH O 9 . ? 18.057 29.712 -6.416 1.00 38.95 ? 892 HOH A O 1 HETATM 6172 O O . HOH O 9 . ? 1.599 36.223 8.402 1.00 27.90 ? 893 HOH A O 1 HETATM 6173 O O . HOH O 9 . ? 6.671 46.427 -7.292 1.00 18.02 ? 894 HOH A O 1 HETATM 6174 O O . HOH O 9 . ? 8.489 25.926 32.134 1.00 25.53 ? 895 HOH A O 1 HETATM 6175 O O . HOH O 9 . ? 12.049 65.122 35.362 1.00 29.98 ? 896 HOH A O 1 HETATM 6176 O O . HOH O 9 . ? -4.801 48.053 6.279 1.00 18.06 ? 897 HOH A O 1 HETATM 6177 O O . HOH O 9 . ? 20.310 23.708 7.171 1.00 34.88 ? 898 HOH A O 1 HETATM 6178 O O . HOH O 9 . ? 7.443 66.800 34.194 1.00 28.60 ? 899 HOH A O 1 HETATM 6179 O O . HOH O 9 . ? -0.094 58.367 28.988 1.00 29.52 ? 900 HOH A O 1 HETATM 6180 O O . HOH O 9 . ? 8.236 77.129 10.180 1.00 29.78 ? 901 HOH A O 1 HETATM 6181 O O . HOH O 9 . ? 28.515 69.265 2.250 1.00 25.29 ? 902 HOH A O 1 HETATM 6182 O O . HOH O 9 . ? 3.834 52.991 -1.777 1.00 20.17 ? 903 HOH A O 1 HETATM 6183 O O . HOH O 9 . ? 27.787 24.424 -1.789 1.00 49.58 ? 904 HOH A O 1 HETATM 6184 O O . HOH O 9 . ? 9.234 65.393 -16.483 1.00 26.56 ? 905 HOH A O 1 HETATM 6185 O O . HOH O 9 . ? 23.666 27.056 31.085 1.00 32.61 ? 906 HOH A O 1 HETATM 6186 O O . HOH O 9 . ? 9.908 79.441 15.076 1.00 32.70 ? 907 HOH A O 1 HETATM 6187 O O . HOH O 9 . ? 35.754 60.313 13.525 1.00 29.97 ? 908 HOH A O 1 HETATM 6188 O O . HOH O 9 . ? -8.023 35.530 18.940 1.00 27.34 ? 909 HOH A O 1 HETATM 6189 O O . HOH O 9 . ? 38.255 17.048 20.154 1.00 31.38 ? 910 HOH A O 1 HETATM 6190 O O . HOH O 9 . ? 14.985 73.951 -4.328 1.00 25.25 ? 911 HOH A O 1 HETATM 6191 O O . HOH O 9 . ? 32.789 12.690 11.764 1.00 33.12 ? 912 HOH A O 1 HETATM 6192 O O . HOH O 9 . ? 5.158 34.185 -1.111 1.00 31.54 ? 913 HOH A O 1 HETATM 6193 O O . HOH O 9 . ? 22.272 49.466 41.262 1.00 35.99 ? 914 HOH A O 1 HETATM 6194 O O . HOH O 9 . ? 24.588 62.951 -7.199 1.00 31.01 ? 915 HOH A O 1 HETATM 6195 O O . HOH O 9 . ? 33.774 28.340 6.757 1.00 36.51 ? 916 HOH A O 1 HETATM 6196 O O . HOH O 9 . ? 14.592 30.707 14.437 1.00 25.38 ? 917 HOH A O 1 HETATM 6197 O O . HOH O 9 . ? 22.755 60.482 37.164 1.00 28.29 ? 918 HOH A O 1 HETATM 6198 O O . HOH O 9 . ? -3.279 46.124 23.943 1.00 32.01 ? 919 HOH A O 1 HETATM 6199 O O . HOH O 9 . ? 3.850 34.552 3.227 1.00 36.45 ? 920 HOH A O 1 HETATM 6200 O O . HOH O 9 . ? 29.316 20.192 36.328 1.00 35.25 ? 921 HOH A O 1 HETATM 6201 O O . HOH O 9 . ? 11.466 44.929 37.194 1.00 27.54 ? 922 HOH A O 1 HETATM 6202 O O . HOH O 9 . ? -2.363 52.631 24.301 1.00 30.05 ? 923 HOH A O 1 HETATM 6203 O O . HOH O 9 . ? 25.015 50.257 -13.956 1.00 31.41 ? 924 HOH A O 1 HETATM 6204 O O . HOH O 9 . ? 15.484 76.592 -3.852 1.00 26.58 ? 925 HOH A O 1 HETATM 6205 O O . HOH O 9 . ? 5.195 28.597 26.870 1.00 31.91 ? 926 HOH A O 1 HETATM 6206 O O . HOH O 9 . ? -6.462 48.035 28.489 1.00 35.19 ? 927 HOH A O 1 HETATM 6207 O O . HOH O 9 . ? 18.383 30.360 31.759 1.00 33.52 ? 928 HOH A O 1 HETATM 6208 O O . HOH O 9 . ? 8.116 42.930 36.815 1.00 29.70 ? 929 HOH A O 1 HETATM 6209 O O . HOH O 9 . ? 16.944 29.380 33.685 1.00 30.50 ? 930 HOH A O 1 HETATM 6210 O O . HOH O 9 . ? -8.035 49.742 16.976 1.00 30.53 ? 931 HOH A O 1 HETATM 6211 O O . HOH O 9 . ? 20.986 64.600 32.642 1.00 27.99 ? 932 HOH A O 1 HETATM 6212 O O . HOH O 9 . ? 43.227 24.584 4.345 1.00 28.14 ? 933 HOH A O 1 HETATM 6213 O O . HOH O 9 . ? 18.933 11.464 19.834 1.00 40.58 ? 934 HOH A O 1 HETATM 6214 O O . HOH O 9 . ? 27.789 6.366 36.351 1.00 26.73 ? 935 HOH A O 1 HETATM 6215 O O A HOH O 9 . ? 7.824 25.498 18.963 0.34 15.80 ? 936 HOH A O 1 HETATM 6216 O O B HOH O 9 . ? 7.366 26.571 21.353 0.33 17.57 ? 936 HOH A O 1 HETATM 6217 O O C HOH O 9 . ? 7.948 26.457 20.083 0.33 18.76 ? 936 HOH A O 1 HETATM 6218 O O . HOH O 9 . ? 35.110 15.079 5.505 1.00 37.55 ? 937 HOH A O 1 HETATM 6219 O O . HOH O 9 . ? 33.131 62.703 31.802 1.00 32.77 ? 938 HOH A O 1 HETATM 6220 O O . HOH O 9 . ? 14.814 19.840 13.296 1.00 36.28 ? 939 HOH A O 1 HETATM 6221 O O . HOH O 9 . ? 16.430 22.757 36.178 1.00 28.94 ? 940 HOH A O 1 HETATM 6222 O O . HOH O 9 . ? 32.369 28.805 3.927 1.00 64.33 ? 941 HOH A O 1 HETATM 6223 O O . HOH O 9 . ? 21.014 60.430 -16.638 1.00 29.14 ? 942 HOH A O 1 HETATM 6224 O O . HOH O 9 . ? 21.804 58.549 38.803 1.00 30.12 ? 943 HOH A O 1 HETATM 6225 O O . HOH O 9 . ? 20.996 15.647 32.860 1.00 29.23 ? 944 HOH A O 1 HETATM 6226 O O . HOH O 9 . ? 33.518 66.144 27.933 1.00 30.87 ? 945 HOH A O 1 HETATM 6227 O O . HOH O 9 . ? 24.917 31.444 -4.815 1.00 42.15 ? 946 HOH A O 1 HETATM 6228 O O . HOH O 9 . ? 1.885 37.466 -4.234 1.00 29.18 ? 947 HOH A O 1 HETATM 6229 O O A HOH O 9 . ? 19.472 50.755 -20.875 0.60 23.77 ? 948 HOH A O 1 HETATM 6230 O O B HOH O 9 . ? 18.767 51.151 -21.815 0.40 25.22 ? 948 HOH A O 1 HETATM 6231 O O . HOH O 9 . ? 42.106 22.105 4.496 1.00 25.40 ? 949 HOH A O 1 HETATM 6232 O O . HOH O 9 . ? -3.462 32.939 21.004 1.00 34.55 ? 950 HOH A O 1 HETATM 6233 O O . HOH O 9 . ? 15.886 13.183 22.747 1.00 32.26 ? 951 HOH A O 1 HETATM 6234 O O . HOH O 9 . ? 38.583 66.603 19.191 1.00 34.11 ? 952 HOH A O 1 HETATM 6235 O O . HOH O 9 . ? 8.932 77.186 7.584 1.00 27.18 ? 953 HOH A O 1 HETATM 6236 O O . HOH O 9 . ? 8.104 35.024 6.918 1.00 31.69 ? 954 HOH A O 1 HETATM 6237 O O . HOH O 9 . ? 7.739 59.553 36.499 1.00 27.58 ? 955 HOH A O 1 HETATM 6238 O O . HOH O 9 . ? 42.841 45.681 29.062 1.00 37.07 ? 956 HOH A O 1 HETATM 6239 O O . HOH O 9 . ? 15.894 52.152 -22.553 1.00 34.37 ? 957 HOH A O 1 HETATM 6240 O O . HOH O 9 . ? 22.249 54.285 -16.201 1.00 34.24 ? 958 HOH A O 1 HETATM 6241 O O . HOH O 9 . ? 2.305 42.172 1.935 1.00 30.54 ? 959 HOH A O 1 HETATM 6242 O O . HOH O 9 . ? 0.372 81.218 2.534 1.00 29.98 ? 960 HOH A O 1 HETATM 6243 O O . HOH O 9 . ? 20.187 58.187 -17.933 1.00 36.89 ? 961 HOH A O 1 HETATM 6244 O O . HOH O 9 . ? 19.821 39.250 40.101 1.00 35.68 ? 962 HOH A O 1 HETATM 6245 O O . HOH O 9 . ? 6.682 78.771 4.943 1.00 31.48 ? 963 HOH A O 1 HETATM 6246 O O . HOH O 9 . ? 22.918 60.817 -11.226 1.00 31.81 ? 964 HOH A O 1 HETATM 6247 O O . HOH O 9 . ? 4.049 74.912 16.250 1.00 36.15 ? 965 HOH A O 1 HETATM 6248 O O A HOH O 9 . ? -1.999 38.508 8.912 0.50 20.70 ? 966 HOH A O 1 HETATM 6249 O O B HOH O 9 . ? -0.503 38.355 8.290 0.50 26.77 ? 966 HOH A O 1 HETATM 6250 O O . HOH O 9 . ? 20.668 26.228 -13.814 1.00 45.15 ? 967 HOH A O 1 HETATM 6251 O O . HOH O 9 . ? -1.072 65.118 12.455 1.00 31.17 ? 968 HOH A O 1 HETATM 6252 O O . HOH O 9 . ? 28.276 71.882 3.247 1.00 32.62 ? 969 HOH A O 1 HETATM 6253 O O . HOH O 9 . ? 2.252 46.138 32.908 1.00 30.09 ? 970 HOH A O 1 HETATM 6254 O O . HOH O 9 . ? 32.671 68.014 25.980 1.00 37.60 ? 971 HOH A O 1 HETATM 6255 O O . HOH O 9 . ? 31.255 64.460 31.065 1.00 37.59 ? 972 HOH A O 1 HETATM 6256 O O . HOH O 9 . ? 12.339 32.819 6.361 1.00 36.55 ? 973 HOH A O 1 HETATM 6257 O O A HOH O 9 . ? 4.967 39.487 -6.926 0.50 19.46 ? 974 HOH A O 1 HETATM 6258 O O B HOH O 9 . ? 4.632 38.196 -8.410 0.50 27.13 ? 974 HOH A O 1 HETATM 6259 O O . HOH O 9 . ? 37.720 32.225 13.791 1.00 39.84 ? 975 HOH A O 1 HETATM 6260 O O . HOH O 9 . ? 4.671 81.173 -8.429 1.00 32.43 ? 976 HOH A O 1 HETATM 6261 O O A HOH O 9 . ? 28.103 13.301 21.939 0.70 22.93 ? 977 HOH A O 1 HETATM 6262 O O B HOH O 9 . ? 28.695 13.510 20.602 0.30 26.93 ? 977 HOH A O 1 HETATM 6263 O O . HOH O 9 . ? 2.179 48.581 0.695 1.00 29.01 ? 978 HOH A O 1 HETATM 6264 O O . HOH O 9 . ? 41.057 27.877 26.277 1.00 36.90 ? 979 HOH A O 1 HETATM 6265 O O . HOH O 9 . ? 13.813 69.759 -16.172 1.00 43.09 ? 980 HOH A O 1 HETATM 6266 O O . HOH O 9 . ? 37.546 34.798 31.611 1.00 38.64 ? 981 HOH A O 1 HETATM 6267 O O . HOH O 9 . ? 31.635 46.485 37.640 1.00 33.94 ? 982 HOH A O 1 HETATM 6268 O O . HOH O 9 . ? 15.272 30.142 35.602 1.00 28.40 ? 983 HOH A O 1 HETATM 6269 O O . HOH O 9 . ? 24.143 32.048 -7.693 1.00 47.86 ? 984 HOH A O 1 HETATM 6270 O O A HOH O 9 . ? 12.502 34.551 34.440 0.50 27.31 ? 985 HOH A O 1 HETATM 6271 O O B HOH O 9 . ? 14.064 34.837 35.485 0.50 36.80 ? 985 HOH A O 1 HETATM 6272 O O . HOH O 9 . ? 9.384 56.028 37.337 1.00 27.18 ? 986 HOH A O 1 HETATM 6273 O O . HOH O 9 . ? 9.011 31.892 36.547 1.00 36.46 ? 987 HOH A O 1 HETATM 6274 O O . HOH O 9 . ? 5.274 81.460 1.413 1.00 30.76 ? 988 HOH A O 1 HETATM 6275 O O . HOH O 9 . ? 19.201 25.071 -11.620 1.00 45.28 ? 989 HOH A O 1 HETATM 6276 O O A HOH O 9 . ? 29.806 54.784 0.690 0.50 26.63 ? 990 HOH A O 1 HETATM 6277 O O B HOH O 9 . ? 29.002 55.977 0.413 0.50 42.70 ? 990 HOH A O 1 HETATM 6278 O O . HOH O 9 . ? 14.664 38.301 -18.066 1.00 31.32 ? 991 HOH A O 1 HETATM 6279 O O . HOH O 9 . ? 6.746 31.647 10.679 1.00 38.02 ? 992 HOH A O 1 HETATM 6280 O O . HOH O 9 . ? 17.484 72.286 30.329 1.00 37.65 ? 993 HOH A O 1 HETATM 6281 O O . HOH O 9 . ? 10.636 32.055 -19.552 1.00 33.67 ? 994 HOH A O 1 HETATM 6282 O O . HOH O 9 . ? 3.500 65.883 -11.556 1.00 31.33 ? 995 HOH A O 1 HETATM 6283 O O . HOH O 9 . ? -8.958 33.237 17.731 1.00 32.54 ? 996 HOH A O 1 HETATM 6284 O O . HOH O 9 . ? 29.778 25.519 1.769 1.00 48.04 ? 997 HOH A O 1 HETATM 6285 O O . HOH O 9 . ? 28.603 55.276 39.178 1.00 39.36 ? 998 HOH A O 1 HETATM 6286 O O . HOH O 9 . ? 31.203 7.144 33.880 1.00 31.34 ? 999 HOH A O 1 HETATM 6287 O O . HOH O 9 . ? 5.844 69.319 -8.303 1.00 31.67 ? 1000 HOH A O 1 HETATM 6288 O O . HOH O 9 . ? 39.749 59.720 20.004 1.00 35.89 ? 1001 HOH A O 1 HETATM 6289 O O . HOH O 9 . ? -5.247 55.314 15.245 1.00 27.99 ? 1002 HOH A O 1 HETATM 6290 O O . HOH O 9 . ? 0.184 62.657 1.380 1.00 22.92 ? 1003 HOH A O 1 HETATM 6291 O O . HOH O 9 . ? 36.732 61.895 22.779 1.00 30.70 ? 1004 HOH A O 1 HETATM 6292 O O . HOH O 9 . ? 15.004 79.251 19.894 1.00 34.20 ? 1005 HOH A O 1 HETATM 6293 O O . HOH O 9 . ? 3.103 50.170 -1.652 1.00 30.11 ? 1006 HOH A O 1 HETATM 6294 O O . HOH O 9 . ? 29.581 35.715 -11.268 1.00 45.43 ? 1007 HOH A O 1 HETATM 6295 O O . HOH O 9 . ? -6.259 30.708 14.294 1.00 32.38 ? 1008 HOH A O 1 HETATM 6296 O O . HOH O 9 . ? 10.449 74.556 26.508 1.00 34.79 ? 1009 HOH A O 1 HETATM 6297 O O . HOH O 9 . ? 41.616 29.574 12.712 1.00 38.74 ? 1010 HOH A O 1 HETATM 6298 O O . HOH O 9 . ? 5.348 70.120 28.241 1.00 33.27 ? 1011 HOH A O 1 HETATM 6299 O O . HOH O 9 . ? 28.625 41.448 -7.524 1.00 39.84 ? 1012 HOH A O 1 HETATM 6300 O O . HOH O 9 . ? 33.601 37.371 14.262 1.00 47.18 ? 1013 HOH A O 1 HETATM 6301 O O . HOH O 9 . ? 7.289 74.562 -9.362 1.00 32.96 ? 1014 HOH A O 1 HETATM 6302 O O A HOH O 9 . ? -7.376 38.133 21.362 0.50 23.34 ? 1015 HOH A O 1 HETATM 6303 O O B HOH O 9 . ? -9.352 39.498 22.862 0.50 33.18 ? 1015 HOH A O 1 HETATM 6304 O O . HOH O 9 . ? 15.959 54.754 -21.940 1.00 36.71 ? 1016 HOH A O 1 HETATM 6305 O O . HOH O 9 . ? 22.729 71.712 30.459 1.00 34.27 ? 1017 HOH A O 1 HETATM 6306 O O . HOH O 9 . ? 34.017 32.074 7.262 1.00 43.63 ? 1018 HOH A O 1 HETATM 6307 O O A HOH O 9 . ? 14.384 76.582 5.089 0.50 21.69 ? 1019 HOH A O 1 HETATM 6308 O O B HOH O 9 . ? 15.501 75.889 4.642 0.50 33.38 ? 1019 HOH A O 1 HETATM 6309 O O . HOH O 9 . ? 25.221 53.259 11.839 1.00 41.60 ? 1020 HOH A O 1 HETATM 6310 O O . HOH O 9 . ? 27.165 39.485 17.205 1.00 32.80 ? 1021 HOH A O 1 HETATM 6311 O O . HOH O 9 . ? 7.307 74.169 25.057 1.00 36.57 ? 1022 HOH A O 1 HETATM 6312 O O . HOH O 9 . ? 30.992 65.981 1.114 1.00 29.61 ? 1023 HOH A O 1 HETATM 6313 O O . HOH O 9 . ? 4.831 28.836 14.467 1.00 31.73 ? 1024 HOH A O 1 HETATM 6314 O O . HOH O 9 . ? 5.899 27.191 25.334 1.00 42.41 ? 1025 HOH A O 1 HETATM 6315 O O . HOH O 9 . ? 32.776 42.468 37.811 1.00 37.83 ? 1026 HOH A O 1 HETATM 6316 O O . HOH O 9 . ? -2.810 29.855 21.789 1.00 44.04 ? 1027 HOH A O 1 HETATM 6317 O O . HOH O 9 . ? 35.508 31.598 9.688 1.00 38.39 ? 1028 HOH A O 1 HETATM 6318 O O . HOH O 9 . ? 29.674 71.145 21.037 1.00 31.57 ? 1029 HOH A O 1 HETATM 6319 O O . HOH O 9 . ? -3.541 48.388 22.950 1.00 34.12 ? 1030 HOH A O 1 HETATM 6320 O O . HOH O 9 . ? 16.525 72.366 1.794 1.00 35.37 ? 1031 HOH A O 1 HETATM 6321 O O . HOH O 9 . ? 4.703 72.566 24.269 1.00 37.27 ? 1032 HOH A O 1 HETATM 6322 O O . HOH O 9 . ? 21.575 10.922 15.622 1.00 54.75 ? 1033 HOH A O 1 HETATM 6323 O O . HOH O 9 . ? 17.366 14.585 28.132 1.00 36.50 ? 1034 HOH A O 1 HETATM 6324 O O . HOH O 9 . ? 39.121 34.763 30.029 1.00 57.63 ? 1035 HOH A O 1 HETATM 6325 O O . HOH O 9 . ? 24.071 8.046 27.585 1.00 43.20 ? 1036 HOH A O 1 HETATM 6326 O O . HOH O 9 . ? 16.576 61.280 37.004 1.00 31.88 ? 1037 HOH A O 1 HETATM 6327 O O . HOH O 9 . ? 27.031 17.501 37.148 1.00 44.39 ? 1038 HOH A O 1 HETATM 6328 O O . HOH O 9 . ? 38.027 23.233 30.624 1.00 39.72 ? 1039 HOH A O 1 HETATM 6329 O O . HOH O 9 . ? 29.938 9.924 22.345 1.00 35.44 ? 1040 HOH A O 1 HETATM 6330 O O . HOH O 9 . ? 4.068 66.991 -8.594 1.00 26.41 ? 1041 HOH A O 1 HETATM 6331 O O . HOH O 9 . ? 37.721 23.165 3.404 1.00 43.60 ? 1042 HOH A O 1 HETATM 6332 O O . HOH O 9 . ? -2.154 51.131 21.368 1.00 29.92 ? 1043 HOH A O 1 HETATM 6333 O O . HOH O 9 . ? 32.716 26.024 33.086 1.00 41.22 ? 1044 HOH A O 1 HETATM 6334 O O . HOH O 9 . ? 6.640 51.165 -14.240 1.00 53.72 ? 1045 HOH A O 1 HETATM 6335 O O . HOH O 9 . ? 36.257 48.444 20.436 1.00 34.59 ? 1046 HOH A O 1 HETATM 6336 O O . HOH O 9 . ? 37.794 28.733 28.312 1.00 36.70 ? 1047 HOH A O 1 HETATM 6337 O O . HOH O 9 . ? 10.895 19.964 16.030 1.00 42.32 ? 1048 HOH A O 1 HETATM 6338 O O . HOH O 9 . ? 40.556 28.536 5.990 1.00 44.97 ? 1049 HOH A O 1 HETATM 6339 O O . HOH O 9 . ? 26.888 54.915 -9.757 1.00 38.26 ? 1050 HOH A O 1 HETATM 6340 O O . HOH O 9 . ? 34.735 69.957 3.034 1.00 63.70 ? 1051 HOH A O 1 HETATM 6341 O O . HOH O 9 . ? 9.097 78.401 -10.727 1.00 38.25 ? 1052 HOH A O 1 HETATM 6342 O O . HOH O 9 . ? 28.128 71.400 23.244 1.00 31.88 ? 1053 HOH A O 1 HETATM 6343 O O . HOH O 9 . ? 34.734 70.091 7.726 1.00 46.38 ? 1054 HOH A O 1 HETATM 6344 O O . HOH O 9 . ? 19.823 62.959 34.622 1.00 35.91 ? 1055 HOH A O 1 HETATM 6345 O O . HOH O 9 . ? 37.219 52.918 4.209 1.00 39.26 ? 1056 HOH A O 1 HETATM 6346 O O . HOH O 9 . ? 25.291 70.196 11.884 1.00 39.32 ? 1057 HOH A O 1 HETATM 6347 O O . HOH O 9 . ? 15.512 30.805 -4.188 1.00 43.53 ? 1058 HOH A O 1 HETATM 6348 O O . HOH O 9 . ? 35.376 26.111 5.102 1.00 40.94 ? 1059 HOH A O 1 HETATM 6349 O O . HOH O 9 . ? 42.977 28.237 5.540 1.00 44.41 ? 1060 HOH A O 1 HETATM 6350 O O . HOH O 9 . ? 21.754 47.074 -20.999 1.00 44.61 ? 1061 HOH A O 1 HETATM 6351 O O . HOH O 9 . ? 12.704 18.901 22.386 1.00 35.88 ? 1062 HOH A O 1 HETATM 6352 O O . HOH O 9 . ? 6.631 27.254 15.353 1.00 35.36 ? 1063 HOH A O 1 HETATM 6353 O O . HOH O 9 . ? 36.519 32.409 33.668 1.00 44.86 ? 1064 HOH A O 1 HETATM 6354 O O . HOH O 9 . ? 8.559 23.562 33.281 1.00 37.80 ? 1065 HOH A O 1 HETATM 6355 O O . HOH O 9 . ? 9.408 18.123 27.584 1.00 42.28 ? 1066 HOH A O 1 HETATM 6356 O O . HOH O 9 . ? 8.205 22.427 19.234 1.00 53.77 ? 1067 HOH A O 1 HETATM 6357 O O . HOH O 9 . ? 26.725 61.683 -1.806 1.00 45.29 ? 1068 HOH A O 1 HETATM 6358 O O . HOH O 9 . ? 18.939 76.951 22.779 1.00 33.67 ? 1069 HOH A O 1 HETATM 6359 O O . HOH O 9 . ? 9.058 32.888 9.641 1.00 41.74 ? 1070 HOH A O 1 HETATM 6360 O O . HOH O 9 . ? 12.336 33.433 -5.366 1.00 39.63 ? 1071 HOH A O 1 HETATM 6361 O O . HOH O 9 . ? 0.198 73.834 13.892 1.00 49.05 ? 1072 HOH A O 1 HETATM 6362 O O . HOH O 9 . ? 23.674 58.436 40.939 1.00 55.22 ? 1073 HOH A O 1 HETATM 6363 O O . HOH O 9 . ? 11.788 68.684 -16.635 1.00 36.01 ? 1074 HOH A O 1 HETATM 6364 O O . HOH O 9 . ? 13.639 38.413 -20.794 1.00 47.11 ? 1075 HOH A O 1 HETATM 6365 O O . HOH O 9 . ? 2.513 53.285 0.621 1.00 24.76 ? 1076 HOH A O 1 HETATM 6366 O O . HOH O 9 . ? 16.968 17.388 7.175 1.00 49.96 ? 1077 HOH A O 1 HETATM 6367 O O . HOH O 9 . ? 22.512 23.638 3.849 1.00 39.05 ? 1078 HOH A O 1 HETATM 6368 O O . HOH O 9 . ? 25.369 10.592 11.631 1.00 53.81 ? 1079 HOH A O 1 HETATM 6369 O O . HOH O 9 . ? -0.069 62.542 28.940 1.00 38.35 ? 1080 HOH A O 1 HETATM 6370 O O . HOH O 9 . ? 41.861 59.955 17.047 1.00 48.36 ? 1081 HOH A O 1 HETATM 6371 O O . HOH O 9 . ? 11.191 20.800 21.653 1.00 47.03 ? 1082 HOH A O 1 HETATM 6372 O O . HOH O 9 . ? 2.313 31.093 29.558 1.00 38.82 ? 1083 HOH A O 1 HETATM 6373 O O . HOH O 9 . ? 36.044 18.644 28.700 1.00 30.62 ? 1084 HOH A O 1 HETATM 6374 O O . HOH O 9 . ? 25.727 30.214 -6.963 1.00 46.90 ? 1085 HOH A O 1 HETATM 6375 O O . HOH O 9 . ? 37.078 69.199 17.191 1.00 39.15 ? 1086 HOH A O 1 HETATM 6376 O O . HOH O 9 . ? 41.430 49.421 26.618 1.00 38.32 ? 1087 HOH A O 1 HETATM 6377 O O . HOH O 9 . ? 35.848 33.537 11.111 1.00 41.73 ? 1088 HOH A O 1 HETATM 6378 O O . HOH O 9 . ? 11.946 16.862 24.742 1.00 44.62 ? 1089 HOH A O 1 HETATM 6379 O O . HOH O 9 . ? 19.749 27.339 5.245 1.00 40.79 ? 1090 HOH A O 1 HETATM 6380 O O . HOH O 9 . ? 31.282 14.267 37.366 1.00 40.31 ? 1091 HOH A O 1 HETATM 6381 O O . HOH O 9 . ? 20.445 40.126 -22.363 1.00 36.49 ? 1092 HOH A O 1 HETATM 6382 O O . HOH O 9 . ? 31.280 58.631 36.958 1.00 46.56 ? 1093 HOH A O 1 HETATM 6383 O O . HOH O 9 . ? 21.881 51.489 -19.846 1.00 44.74 ? 1094 HOH A O 1 HETATM 6384 O O . HOH O 9 . ? -1.827 49.193 31.331 1.00 41.95 ? 1095 HOH A O 1 HETATM 6385 O O . HOH O 9 . ? 11.222 79.190 12.650 1.00 36.62 ? 1096 HOH A O 1 HETATM 6386 O O . HOH O 9 . ? -5.313 42.611 26.331 1.00 38.82 ? 1097 HOH A O 1 HETATM 6387 O O . HOH O 9 . ? 6.322 76.058 22.414 1.00 40.44 ? 1098 HOH A O 1 HETATM 6388 O O . HOH O 9 . ? -0.076 49.941 3.884 1.00 32.51 ? 1099 HOH A O 1 HETATM 6389 O O . HOH O 9 . ? 18.200 65.576 -17.309 1.00 37.31 ? 1100 HOH A O 1 HETATM 6390 O O . HOH O 9 . ? 1.592 31.456 11.260 1.00 45.01 ? 1101 HOH A O 1 HETATM 6391 O O . HOH O 9 . ? 17.210 74.319 7.723 1.00 42.28 ? 1102 HOH A O 1 HETATM 6392 O O . HOH O 9 . ? 24.134 66.634 34.117 1.00 41.78 ? 1103 HOH A O 1 HETATM 6393 O O . HOH O 9 . ? 2.098 30.579 25.474 1.00 48.41 ? 1104 HOH A O 1 HETATM 6394 O O . HOH O 9 . ? 10.160 74.722 -13.316 1.00 54.35 ? 1105 HOH A O 1 HETATM 6395 O O . HOH O 9 . ? 16.159 65.708 33.247 1.00 39.05 ? 1106 HOH A O 1 HETATM 6396 O O . HOH O 9 . ? 14.930 71.417 30.419 1.00 36.45 ? 1107 HOH A O 1 HETATM 6397 O O . HOH O 9 . ? 25.890 54.766 -3.992 1.00 51.25 ? 1108 HOH A O 1 HETATM 6398 O O . HOH O 9 . ? 40.607 59.698 3.698 1.00 42.02 ? 1109 HOH A O 1 HETATM 6399 O O . HOH O 9 . ? 8.761 84.661 -5.275 1.00 44.27 ? 1110 HOH A O 1 HETATM 6400 O O . HOH O 9 . ? 34.389 59.950 33.146 1.00 47.09 ? 1111 HOH A O 1 HETATM 6401 O O . HOH O 9 . ? 40.270 49.404 20.546 1.00 42.28 ? 1112 HOH A O 1 HETATM 6402 O O . HOH O 9 . ? 41.702 30.117 15.386 1.00 46.30 ? 1113 HOH A O 1 HETATM 6403 O O . HOH O 9 . ? 32.624 54.306 35.994 1.00 40.16 ? 1114 HOH A O 1 HETATM 6404 O O . HOH O 9 . ? 23.909 73.306 28.236 1.00 41.72 ? 1115 HOH A O 1 HETATM 6405 O O A HOH O 9 . ? 28.475 57.950 -0.607 0.50 26.02 ? 1116 HOH A O 1 HETATM 6406 O O B HOH O 9 . ? 27.617 55.394 -0.116 0.50 30.30 ? 1116 HOH A O 1 HETATM 6407 O O . HOH O 9 . ? 13.780 74.248 28.185 1.00 43.38 ? 1117 HOH A O 1 HETATM 6408 O O . HOH O 9 . ? 39.138 55.537 31.775 1.00 40.09 ? 1118 HOH A O 1 HETATM 6409 O O . HOH O 9 . ? 35.178 66.047 0.843 1.00 40.80 ? 1119 HOH A O 1 HETATM 6410 O O . HOH O 9 . ? 16.109 41.657 -23.909 1.00 46.52 ? 1120 HOH A O 1 HETATM 6411 O O . HOH O 9 . ? 15.473 78.905 28.094 1.00 49.65 ? 1121 HOH A O 1 HETATM 6412 O O . HOH O 9 . ? 14.000 46.892 -21.755 1.00 40.06 ? 1122 HOH A O 1 HETATM 6413 O O . HOH O 9 . ? -1.418 57.652 17.158 1.00 36.13 ? 1123 HOH A O 1 HETATM 6414 O O . HOH O 9 . ? 35.355 47.930 35.715 1.00 45.75 ? 1124 HOH A O 1 HETATM 6415 O O . HOH O 9 . ? -3.031 36.242 10.835 1.00 37.03 ? 1125 HOH A O 1 HETATM 6416 O O A HOH O 9 . ? -1.686 57.029 24.180 0.50 25.30 ? 1126 HOH A O 1 HETATM 6417 O O B HOH O 9 . ? -2.933 54.954 22.700 0.50 30.84 ? 1126 HOH A O 1 HETATM 6418 O O . HOH O 9 . ? 12.665 17.758 17.247 1.00 51.09 ? 1127 HOH A O 1 HETATM 6419 O O . HOH O 9 . ? 25.572 57.014 -15.914 1.00 45.14 ? 1128 HOH A O 1 HETATM 6420 O O . HOH O 9 . ? 30.302 45.932 -9.267 1.00 47.78 ? 1129 HOH A O 1 HETATM 6421 O O . HOH O 9 . ? 10.053 36.912 -19.947 1.00 42.19 ? 1130 HOH A O 1 HETATM 6422 O O . HOH O 9 . ? 37.747 30.631 11.991 1.00 40.87 ? 1131 HOH A O 1 HETATM 6423 O O . HOH O 9 . ? 38.822 58.194 17.931 1.00 37.26 ? 1132 HOH A O 1 HETATM 6424 O O . HOH O 9 . ? 31.607 5.612 31.749 1.00 41.56 ? 1133 HOH A O 1 HETATM 6425 O O . HOH O 9 . ? 1.608 78.147 5.361 1.00 32.66 ? 1134 HOH A O 1 HETATM 6426 O O . HOH O 9 . ? 21.387 77.275 24.009 1.00 34.31 ? 1135 HOH A O 1 HETATM 6427 O O . HOH O 9 . ? 27.028 60.685 36.163 1.00 41.52 ? 1136 HOH A O 1 HETATM 6428 O O . HOH O 9 . ? -0.868 52.863 28.263 1.00 41.86 ? 1137 HOH A O 1 HETATM 6429 O O . HOH O 9 . ? 30.830 57.323 -2.416 1.00 49.80 ? 1138 HOH A O 1 HETATM 6430 O O . HOH O 9 . ? 35.489 9.505 16.620 1.00 45.40 ? 1139 HOH A O 1 HETATM 6431 O O . HOH O 9 . ? 18.070 72.216 4.266 1.00 39.03 ? 1140 HOH A O 1 HETATM 6432 O O . HOH O 9 . ? 33.315 36.322 35.343 1.00 43.88 ? 1141 HOH A O 1 HETATM 6433 O O . HOH O 9 . ? 34.302 9.547 25.066 1.00 44.67 ? 1142 HOH A O 1 HETATM 6434 O O . HOH O 9 . ? 13.800 37.403 10.532 1.00 29.91 ? 1143 HOH A O 1 HETATM 6435 O O . HOH O 9 . ? 9.771 42.166 13.572 1.00 17.85 ? 1144 HOH A O 1 HETATM 6436 O O . HOH O 9 . ? 15.535 64.810 35.698 1.00 51.95 ? 1145 HOH A O 1 HETATM 6437 O O . HOH O 9 . ? 42.821 21.014 15.595 1.00 21.55 ? 1146 HOH A O 1 HETATM 6438 O O . HOH O 9 . ? 44.329 20.593 17.692 1.00 33.08 ? 1147 HOH A O 1 HETATM 6439 O O . HOH O 9 . ? 32.104 66.976 30.147 1.00 32.11 ? 1148 HOH A O 1 HETATM 6440 O O . HOH O 9 . ? 25.243 61.189 37.827 1.00 39.23 ? 1149 HOH A O 1 HETATM 6441 O O . HOH O 9 . ? 24.495 51.625 40.890 1.00 43.57 ? 1150 HOH A O 1 HETATM 6442 O O . HOH O 9 . ? 4.495 38.314 31.538 1.00 32.88 ? 1151 HOH A O 1 HETATM 6443 O O . HOH O 9 . ? 13.004 39.929 35.274 1.00 41.61 ? 1152 HOH A O 1 HETATM 6444 O O . HOH O 9 . ? 6.612 55.925 38.283 1.00 33.88 ? 1153 HOH A O 1 HETATM 6445 O O A HOH O 9 . ? 0.606 66.511 18.809 0.50 22.68 ? 1154 HOH A O 1 HETATM 6446 O O B HOH O 9 . ? 1.349 67.688 19.180 0.50 22.88 ? 1154 HOH A O 1 HETATM 6447 O O . HOH O 9 . ? 0.299 66.393 16.274 1.00 52.42 ? 1155 HOH A O 1 HETATM 6448 O O . HOH O 9 . ? -0.218 69.515 19.963 1.00 55.53 ? 1156 HOH A O 1 HETATM 6449 O O . HOH O 9 . ? 14.815 32.809 36.151 1.00 35.57 ? 1157 HOH A O 1 HETATM 6450 O O . HOH O 9 . ? 31.883 6.204 36.379 1.00 31.67 ? 1158 HOH A O 1 HETATM 6451 O O . HOH O 9 . ? 29.564 38.809 12.870 1.00 40.40 ? 1159 HOH A O 1 HETATM 6452 O O . HOH O 9 . ? 28.985 41.681 13.737 1.00 54.23 ? 1160 HOH A O 1 HETATM 6453 O O . HOH O 9 . ? 11.515 22.344 11.646 1.00 55.35 ? 1161 HOH A O 1 HETATM 6454 O O . HOH O 9 . ? 33.266 29.124 34.217 1.00 43.63 ? 1162 HOH A O 1 HETATM 6455 O O . HOH O 9 . ? 19.818 51.791 2.415 1.00 24.00 ? 1163 HOH A O 1 HETATM 6456 O O . HOH O 9 . ? 33.990 47.487 38.161 1.00 39.12 ? 1164 HOH A O 1 HETATM 6457 O O . HOH O 9 . ? 39.731 30.181 27.343 1.00 44.66 ? 1165 HOH A O 1 HETATM 6458 O O . HOH O 9 . ? 15.234 24.919 38.781 1.00 48.94 ? 1166 HOH A O 1 HETATM 6459 O O . HOH O 9 . ? 22.818 44.604 -6.213 1.00 32.05 ? 1167 HOH A O 1 HETATM 6460 O O . HOH O 9 . ? -5.946 51.012 16.277 1.00 28.11 ? 1168 HOH A O 1 HETATM 6461 O O . HOH O 9 . ? 7.867 68.003 -10.574 1.00 28.76 ? 1169 HOH A O 1 HETATM 6462 O O . HOH O 9 . ? 17.456 39.914 21.214 1.00 17.53 ? 1170 HOH A O 1 HETATM 6463 O O . HOH O 9 . ? 11.942 41.195 12.190 1.00 21.98 ? 1171 HOH A O 1 HETATM 6464 O O . HOH O 9 . ? 19.431 76.727 11.375 1.00 32.08 ? 1172 HOH A O 1 HETATM 6465 O O . HOH O 9 . ? 18.727 79.871 11.823 1.00 44.38 ? 1173 HOH A O 1 HETATM 6466 O O . HOH O 9 . ? 15.920 75.819 8.705 1.00 47.43 ? 1174 HOH A O 1 HETATM 6467 O O . HOH O 9 . ? 25.694 79.477 13.216 1.00 53.24 ? 1175 HOH A O 1 HETATM 6468 O O . HOH O 9 . ? 27.444 74.254 16.503 1.00 57.02 ? 1176 HOH A O 1 HETATM 6469 O O . HOH O 9 . ? 26.026 72.298 13.780 1.00 38.13 ? 1177 HOH A O 1 HETATM 6470 O O . HOH O 9 . ? 23.212 77.075 22.461 1.00 43.64 ? 1178 HOH A O 1 HETATM 6471 O O . HOH O 9 . ? 29.925 71.235 25.118 1.00 36.62 ? 1179 HOH A O 1 HETATM 6472 O O . HOH O 9 . ? 33.168 68.084 22.682 1.00 36.84 ? 1180 HOH A O 1 HETATM 6473 O O . HOH O 9 . ? 37.991 67.227 21.595 1.00 44.55 ? 1181 HOH A O 1 HETATM 6474 O O . HOH O 9 . ? 36.293 66.458 28.431 1.00 49.40 ? 1182 HOH A O 1 HETATM 6475 O O . HOH O 9 . ? 39.596 64.729 25.498 1.00 43.35 ? 1183 HOH A O 1 HETATM 6476 O O . HOH O 9 . ? 29.066 70.434 30.982 1.00 40.67 ? 1184 HOH A O 1 HETATM 6477 O O . HOH O 9 . ? 17.541 67.641 32.239 1.00 39.45 ? 1185 HOH A O 1 HETATM 6478 O O . HOH O 9 . ? 20.915 62.514 37.035 1.00 35.06 ? 1186 HOH A O 1 HETATM 6479 O O . HOH O 9 . ? 27.118 50.669 40.724 1.00 60.18 ? 1187 HOH A O 1 HETATM 6480 O O . HOH O 9 . ? 24.868 54.269 40.945 1.00 64.58 ? 1188 HOH A O 1 HETATM 6481 O O . HOH O 9 . ? 19.264 58.899 39.459 1.00 37.85 ? 1189 HOH A O 1 HETATM 6482 O O . HOH O 9 . ? 18.763 61.372 38.625 1.00 38.72 ? 1190 HOH A O 1 HETATM 6483 O O . HOH O 9 . ? 18.220 52.208 41.706 1.00 49.90 ? 1191 HOH A O 1 HETATM 6484 O O . HOH O 9 . ? 20.395 50.983 42.713 1.00 43.03 ? 1192 HOH A O 1 HETATM 6485 O O . HOH O 9 . ? 17.795 45.477 42.843 1.00 47.60 ? 1193 HOH A O 1 HETATM 6486 O O . HOH O 9 . ? 6.619 40.145 32.831 1.00 38.46 ? 1194 HOH A O 1 HETATM 6487 O O . HOH O 9 . ? 4.388 46.468 35.377 1.00 62.36 ? 1195 HOH A O 1 HETATM 6488 O O . HOH O 9 . ? 4.447 51.330 38.707 1.00 44.10 ? 1196 HOH A O 1 HETATM 6489 O O . HOH O 9 . ? 17.251 57.174 38.347 1.00 39.02 ? 1197 HOH A O 1 HETATM 6490 O O . HOH O 9 . ? 2.011 57.883 32.953 1.00 39.04 ? 1198 HOH A O 1 HETATM 6491 O O . HOH O 9 . ? 9.075 67.569 36.194 1.00 36.92 ? 1199 HOH A O 1 HETATM 6492 O O . HOH O 9 . ? 0.700 72.518 19.767 1.00 65.17 ? 1200 HOH A O 1 HETATM 6493 O O . HOH O 9 . ? -1.920 42.461 29.386 1.00 40.41 ? 1201 HOH A O 1 HETATM 6494 O O . HOH O 9 . ? 22.260 37.509 16.601 1.00 25.79 ? 1202 HOH A O 1 HETATM 6495 O O . HOH O 9 . ? 12.142 30.027 13.754 1.00 30.26 ? 1203 HOH A O 1 HETATM 6496 O O . HOH O 9 . ? 25.466 74.883 12.420 1.00 49.92 ? 1204 HOH A O 1 HETATM 6497 O O . HOH O 9 . ? 27.014 69.824 32.820 1.00 61.15 ? 1205 HOH A O 1 HETATM 6498 O O . HOH O 9 . ? 22.816 64.950 37.554 1.00 52.50 ? 1206 HOH A O 1 HETATM 6499 O O . HOH O 9 . ? 17.562 53.341 39.139 1.00 47.94 ? 1207 HOH A O 1 HETATM 6500 O O . HOH O 9 . ? 17.106 50.986 34.655 1.00 35.39 ? 1208 HOH A O 1 HETATM 6501 O O . HOH O 9 . ? 4.085 42.494 33.076 1.00 41.26 ? 1209 HOH A O 1 HETATM 6502 O O . HOH O 9 . ? 0.260 44.220 32.946 1.00 44.03 ? 1210 HOH A O 1 HETATM 6503 O O . HOH O 9 . ? 2.726 48.691 37.209 1.00 60.34 ? 1211 HOH A O 1 HETATM 6504 O O . HOH O 9 . ? -0.354 50.540 35.762 1.00 59.82 ? 1212 HOH A O 1 HETATM 6505 O O . HOH O 9 . ? 1.447 54.099 36.815 1.00 55.34 ? 1213 HOH A O 1 HETATM 6506 O O . HOH O 9 . ? 12.453 54.984 37.458 1.00 45.25 ? 1214 HOH A O 1 HETATM 6507 O O . HOH O 9 . ? 4.199 62.440 33.349 1.00 44.14 ? 1215 HOH A O 1 HETATM 6508 O O . HOH O 9 . ? 5.693 63.396 36.523 1.00 51.62 ? 1216 HOH A O 1 HETATM 6509 O O . HOH O 9 . ? 3.663 69.252 32.087 1.00 48.80 ? 1217 HOH A O 1 HETATM 6510 O O . HOH O 9 . ? 26.772 20.335 38.910 1.00 43.95 ? 1218 HOH A O 1 HETATM 6511 O O . HOH O 9 . ? 16.471 69.752 32.133 1.00 48.96 ? 1219 HOH A O 1 HETATM 6512 O O . HOH O 9 . ? 15.483 70.050 35.270 1.00 42.69 ? 1220 HOH A O 1 HETATM 6513 O O . HOH O 9 . ? 15.737 75.292 32.342 1.00 77.69 ? 1221 HOH A O 1 HETATM 6514 O O . HOH O 9 . ? 7.536 72.754 30.263 1.00 61.17 ? 1222 HOH A O 1 HETATM 6515 O O . HOH O 9 . ? 4.480 72.706 28.377 1.00 58.19 ? 1223 HOH A O 1 HETATM 6516 O O . HOH O 9 . ? 18.410 16.412 32.286 1.00 46.51 ? 1224 HOH A O 1 HETATM 6517 O O . HOH O 9 . ? 17.420 16.923 29.660 1.00 37.88 ? 1225 HOH A O 1 HETATM 6518 O O . HOH O 9 . ? 20.362 11.398 34.432 1.00 42.32 ? 1226 HOH A O 1 HETATM 6519 O O . HOH O 9 . ? 23.440 18.202 42.080 1.00 71.52 ? 1227 HOH A O 1 HETATM 6520 O O . HOH O 9 . ? 24.371 19.605 39.900 1.00 49.49 ? 1228 HOH A O 1 HETATM 6521 O O . HOH O 9 . ? 20.074 17.906 36.699 1.00 43.94 ? 1229 HOH A O 1 HETATM 6522 O O . HOH O 9 . ? 25.966 22.669 38.197 1.00 49.16 ? 1230 HOH A O 1 HETATM 6523 O O . HOH O 9 . ? 22.371 21.475 39.795 1.00 43.95 ? 1231 HOH A O 1 HETATM 6524 O O . HOH O 9 . ? 19.437 22.916 37.437 1.00 40.24 ? 1232 HOH A O 1 HETATM 6525 O O . HOH O 9 . ? 32.064 39.802 37.809 1.00 59.01 ? 1233 HOH A O 1 HETATM 6526 O O . HOH O 9 . ? 30.340 49.544 40.119 1.00 53.96 ? 1234 HOH A O 1 HETATM 6527 O O . HOH O 9 . ? 18.792 43.837 47.082 1.00 62.34 ? 1235 HOH A O 1 HETATM 6528 O O . HOH O 9 . ? 20.462 35.780 37.108 1.00 36.32 ? 1236 HOH A O 1 HETATM 6529 O O . HOH O 9 . ? 5.954 69.187 33.363 1.00 46.67 ? 1237 HOH A O 1 HETATM 6530 O O . HOH O 9 . ? 29.567 34.410 6.389 1.00 34.15 ? 1238 HOH A O 1 HETATM 6531 O O . HOH O 9 . ? 23.014 31.528 6.635 1.00 46.71 ? 1239 HOH A O 1 HETATM 6532 O O . HOH O 9 . ? 32.678 36.906 7.336 1.00 56.39 ? 1240 HOH A O 1 HETATM 6533 O O . HOH O 9 . ? 34.159 25.444 2.357 1.00 47.09 ? 1241 HOH A O 1 HETATM 6534 O O . HOH O 9 . ? 30.600 20.512 -2.502 1.00 44.25 ? 1242 HOH A O 1 HETATM 6535 O O . HOH O 9 . ? 33.555 14.339 0.743 1.00 41.10 ? 1243 HOH A O 1 HETATM 6536 O O . HOH O 9 . ? 22.802 21.042 3.725 1.00 42.85 ? 1244 HOH A O 1 HETATM 6537 O O . HOH O 9 . ? 19.859 20.984 5.865 1.00 40.35 ? 1245 HOH A O 1 HETATM 6538 O O A HOH O 9 . ? 21.539 17.378 7.866 0.33 25.30 ? 1246 HOH A O 1 HETATM 6539 O O B HOH O 9 . ? 21.407 17.883 6.481 0.33 23.04 ? 1246 HOH A O 1 HETATM 6540 O O C HOH O 9 . ? 21.160 16.142 8.447 0.33 25.99 ? 1246 HOH A O 1 HETATM 6541 O O . HOH O 9 . ? 27.301 12.301 10.890 1.00 56.79 ? 1247 HOH A O 1 HETATM 6542 O O . HOH O 9 . ? 16.362 15.826 8.690 0.50 32.32 ? 1248 HOH A O 1 HETATM 6543 O O . HOH O 9 . ? 13.377 37.928 13.674 1.00 27.47 ? 1249 HOH A O 1 HETATM 6544 O O . HOH O 9 . ? 13.762 38.810 15.866 1.00 30.49 ? 1250 HOH A O 1 HETATM 6545 O O . HOH O 9 . ? 11.155 29.570 11.441 1.00 38.37 ? 1251 HOH A O 1 HETATM 6546 O O . HOH O 9 . ? 4.698 33.245 8.308 1.00 36.11 ? 1252 HOH A O 1 HETATM 6547 O O . HOH O 9 . ? 34.962 18.944 2.038 1.00 51.39 ? 1253 HOH A O 1 HETATM 6548 O O . HOH O 9 . ? -6.096 33.396 20.331 1.00 37.80 ? 1254 HOH A O 1 HETATM 6549 O O . HOH O 9 . ? -5.752 30.673 20.980 1.00 50.30 ? 1255 HOH A O 1 HETATM 6550 O O . HOH O 9 . ? 0.181 32.721 24.986 1.00 46.10 ? 1256 HOH A O 1 HETATM 6551 O O . HOH O 9 . ? 3.840 28.856 24.169 1.00 43.58 ? 1257 HOH A O 1 HETATM 6552 O O . HOH O 9 . ? -5.846 32.182 11.273 1.00 41.81 ? 1258 HOH A O 1 HETATM 6553 O O . HOH O 9 . ? 0.457 34.369 9.777 1.00 32.21 ? 1259 HOH A O 1 HETATM 6554 O O . HOH O 9 . ? 24.914 38.942 11.973 1.00 44.20 ? 1260 HOH A O 1 HETATM 6555 O O . HOH O 9 . ? 21.570 48.970 9.101 1.00 43.41 ? 1261 HOH A O 1 HETATM 6556 O O . HOH O 9 . ? 13.150 37.127 -1.920 1.00 33.57 ? 1262 HOH A O 1 HETATM 6557 O O . HOH O 9 . ? 12.162 35.577 -0.328 1.00 45.30 ? 1263 HOH A O 1 HETATM 6558 O O . HOH O 9 . ? 28.616 44.927 -14.169 0.50 34.75 ? 1264 HOH A O 1 HETATM 6559 O O . HOH O 9 . ? 24.554 42.330 -6.091 1.00 51.24 ? 1265 HOH A O 1 HETATM 6560 O O . HOH O 9 . ? 28.840 47.763 -8.596 1.00 46.02 ? 1266 HOH A O 1 HETATM 6561 O O . HOH O 9 . ? 22.026 53.057 1.213 1.00 32.95 ? 1267 HOH A O 1 HETATM 6562 O O . HOH O 9 . ? 32.013 10.651 14.113 1.00 54.06 ? 1268 HOH A O 1 HETATM 6563 O O . HOH O 9 . ? 28.062 11.163 21.751 0.50 24.59 ? 1269 HOH A O 1 HETATM 6564 O O . HOH O 9 . ? 37.174 57.314 23.861 1.00 31.96 ? 1270 HOH A O 1 HETATM 6565 O O . HOH O 9 . ? 40.276 54.050 19.151 1.00 44.65 ? 1271 HOH A O 1 HETATM 6566 O O . HOH O 9 . ? 34.828 8.650 13.650 1.00 45.79 ? 1272 HOH A O 1 HETATM 6567 O O . HOH O 9 . ? 31.519 63.647 35.698 1.00 49.65 ? 1273 HOH A O 1 HETATM 6568 O O . HOH O 9 . ? 39.673 56.383 21.016 1.00 49.01 ? 1274 HOH A O 1 HETATM 6569 O O . HOH O 9 . ? 40.079 64.160 6.334 1.00 40.56 ? 1275 HOH A O 1 HETATM 6570 O O A HOH O 9 . ? 12.080 80.896 1.616 0.50 25.75 ? 1276 HOH A O 1 HETATM 6571 O O B HOH O 9 . ? 13.888 79.398 1.805 0.50 31.03 ? 1276 HOH A O 1 HETATM 6572 O O . HOH O 9 . ? 14.159 77.016 0.810 1.00 45.03 ? 1277 HOH A O 1 HETATM 6573 O O . HOH O 9 . ? 15.907 76.583 -1.089 1.00 36.99 ? 1278 HOH A O 1 HETATM 6574 O O . HOH O 9 . ? -3.142 68.619 11.992 1.00 42.20 ? 1279 HOH A O 1 HETATM 6575 O O . HOH O 9 . ? 12.728 83.358 -2.871 1.00 40.07 ? 1280 HOH A O 1 HETATM 6576 O O . HOH O 9 . ? 21.520 9.474 20.404 1.00 45.08 ? 1281 HOH A O 1 HETATM 6577 O O . HOH O 9 . ? 36.765 10.446 10.310 1.00 41.07 ? 1282 HOH A O 1 HETATM 6578 O O . HOH O 9 . ? -5.792 51.288 29.054 1.00 45.30 ? 1283 HOH A O 1 HETATM 6579 O O . HOH O 9 . ? -1.985 45.211 32.304 1.00 49.15 ? 1284 HOH A O 1 HETATM 6580 O O . HOH O 9 . ? -3.320 43.457 31.103 1.00 46.52 ? 1285 HOH A O 1 HETATM 6581 O O . HOH O 9 . ? -6.512 46.140 30.484 1.00 47.41 ? 1286 HOH A O 1 HETATM 6582 O O . HOH O 9 . ? -4.527 39.035 24.839 1.00 40.13 ? 1287 HOH A O 1 HETATM 6583 O O . HOH O 9 . ? 37.377 56.997 33.338 1.00 46.17 ? 1288 HOH A O 1 HETATM 6584 O O . HOH O 9 . ? 20.005 62.840 -17.616 1.00 39.15 ? 1289 HOH A O 1 HETATM 6585 O O . HOH O 9 . ? 17.519 70.729 -2.311 1.00 36.95 ? 1290 HOH A O 1 HETATM 6586 O O . HOH O 9 . ? -0.197 32.438 29.243 1.00 43.75 ? 1291 HOH A O 1 HETATM 6587 O O . HOH O 9 . ? 38.779 59.830 25.410 1.00 36.17 ? 1292 HOH A O 1 HETATM 6588 O O . HOH O 9 . ? 11.145 76.795 7.040 1.00 48.40 ? 1293 HOH A O 1 HETATM 6589 O O . HOH O 9 . ? 21.078 8.515 28.571 1.00 61.12 ? 1294 HOH A O 1 HETATM 6590 O O . HOH O 9 . ? 2.341 31.870 32.129 1.00 56.46 ? 1295 HOH A O 1 HETATM 6591 O O . HOH O 9 . ? 21.604 68.860 2.316 1.00 34.75 ? 1296 HOH A O 1 HETATM 6592 O O . HOH O 9 . ? 38.830 62.282 24.280 1.00 49.41 ? 1297 HOH A O 1 HETATM 6593 O O . HOH O 9 . ? 36.347 71.640 15.986 1.00 48.59 ? 1298 HOH A O 1 HETATM 6594 O O . HOH O 9 . ? 19.977 46.668 2.747 1.00 43.28 ? 1299 HOH A O 1 HETATM 6595 O O . HOH O 9 . ? 20.416 70.910 3.548 1.00 44.17 ? 1300 HOH A O 1 HETATM 6596 O O . HOH O 9 . ? 41.301 66.214 22.563 1.00 53.79 ? 1301 HOH A O 1 HETATM 6597 O O A HOH O 9 . ? 10.560 82.581 -8.716 0.50 36.77 ? 1302 HOH A O 1 HETATM 6598 O O B HOH O 9 . ? 11.524 82.715 -7.247 0.50 43.53 ? 1302 HOH A O 1 HETATM 6599 O O . HOH O 9 . ? 21.335 3.606 31.176 1.00 66.94 ? 1303 HOH A O 1 HETATM 6600 O O . HOH O 9 . ? 17.933 11.630 17.914 1.00 50.10 ? 1304 HOH A O 1 HETATM 6601 O O . HOH O 9 . ? 43.780 28.230 13.203 1.00 43.64 ? 1305 HOH A O 1 HETATM 6602 O O . HOH O 9 . ? 21.029 25.221 5.502 1.00 74.52 ? 1306 HOH A O 1 HETATM 6603 O O . HOH O 9 . ? 16.604 36.768 38.427 1.00 49.46 ? 1307 HOH A O 1 HETATM 6604 O O . HOH O 9 . ? 5.826 24.340 24.890 1.00 50.56 ? 1308 HOH A O 1 HETATM 6605 O O . HOH O 9 . ? 7.659 80.929 3.750 1.00 43.84 ? 1309 HOH A O 1 HETATM 6606 O O . HOH O 9 . ? 29.586 10.838 8.944 1.00 65.13 ? 1310 HOH A O 1 HETATM 6607 O O . HOH O 9 . ? 7.389 78.438 13.733 1.00 44.49 ? 1311 HOH A O 1 HETATM 6608 O O . HOH O 9 . ? 3.994 78.593 4.010 1.00 30.21 ? 1312 HOH A O 1 HETATM 6609 O O A HOH O 9 . ? 26.194 33.781 31.560 0.50 30.70 ? 1313 HOH A O 1 HETATM 6610 O O B HOH O 9 . ? 26.488 35.811 32.526 0.50 36.66 ? 1313 HOH A O 1 HETATM 6611 O O . HOH O 9 . ? 29.365 35.856 33.940 1.00 36.82 ? 1314 HOH A O 1 HETATM 6612 O O . HOH O 9 . ? 24.116 37.614 37.535 1.00 44.13 ? 1315 HOH A O 1 HETATM 6613 O O . HOH O 9 . ? 15.584 44.025 45.232 1.00 63.20 ? 1316 HOH A O 1 HETATM 6614 O O . HOH O 9 . ? 38.441 31.627 30.933 1.00 43.90 ? 1317 HOH A O 1 HETATM 6615 O O . HOH O 9 . ? 12.495 21.514 13.862 1.00 39.26 ? 1318 HOH A O 1 HETATM 6616 O O . HOH O 9 . ? 12.747 23.296 9.306 1.00 45.51 ? 1319 HOH A O 1 HETATM 6617 O O . HOH O 9 . ? 5.791 25.742 30.823 1.00 37.27 ? 1320 HOH A O 1 HETATM 6618 O O . HOH O 9 . ? 5.836 22.701 29.849 1.00 49.55 ? 1321 HOH A O 1 HETATM 6619 O O . HOH O 9 . ? 11.150 19.443 33.221 1.00 53.60 ? 1322 HOH A O 1 HETATM 6620 O O . HOH O 9 . ? 36.561 17.665 5.995 1.00 34.32 ? 1323 HOH A O 1 HETATM 6621 O O . HOH O 9 . ? 34.542 9.905 11.544 1.00 38.29 ? 1324 HOH A O 1 HETATM 6622 O O . HOH O 9 . ? 33.057 10.164 17.637 1.00 48.69 ? 1325 HOH A O 1 HETATM 6623 O O . HOH O 9 . ? -3.706 37.949 27.469 1.00 46.29 ? 1326 HOH A O 1 HETATM 6624 O O . HOH O 9 . ? -2.990 35.381 27.679 1.00 43.51 ? 1327 HOH A O 1 HETATM 6625 O O . HOH O 9 . ? 0.287 66.890 13.882 1.00 40.64 ? 1328 HOH A O 1 HETATM 6626 O O . HOH O 9 . ? 14.191 81.315 18.675 1.00 41.33 ? 1329 HOH A O 1 HETATM 6627 O O . HOH O 9 . ? 29.677 72.674 29.767 1.00 54.96 ? 1330 HOH A O 1 HETATM 6628 O O . HOH O 9 . ? 46.842 28.473 5.525 1.00 30.11 ? 1331 HOH A O 1 HETATM 6629 O O . HOH O 9 . ? 43.644 24.048 19.503 1.00 36.88 ? 1332 HOH A O 1 HETATM 6630 O O . HOH O 9 . ? 40.807 42.052 16.113 1.00 43.12 ? 1333 HOH A O 1 HETATM 6631 O O . HOH O 9 . ? 41.106 47.689 28.901 1.00 37.27 ? 1334 HOH A O 1 HETATM 6632 O O . HOH O 9 . ? 20.319 67.262 31.847 1.00 53.63 ? 1335 HOH A O 1 HETATM 6633 O O . HOH O 9 . ? 46.437 24.178 28.132 1.00 54.66 ? 1336 HOH A O 1 HETATM 6634 O O . HOH O 9 . ? 35.568 45.992 39.927 1.00 43.29 ? 1337 HOH A O 1 HETATM 6635 O O . HOH O 9 . ? 31.120 35.416 37.648 1.00 54.27 ? 1338 HOH A O 1 HETATM 6636 O O . HOH O 9 . ? -7.014 35.547 21.876 1.00 42.49 ? 1339 HOH A O 1 HETATM 6637 O O . HOH O 9 . ? 42.294 44.587 20.314 1.00 53.63 ? 1340 HOH A O 1 HETATM 6638 O O . HOH O 9 . ? 44.812 46.193 27.184 1.00 52.34 ? 1341 HOH A O 1 HETATM 6639 O O . HOH O 9 . ? 42.583 24.468 28.272 1.00 53.27 ? 1342 HOH A O 1 HETATM 6640 O O . HOH O 9 . ? 11.920 27.437 9.333 1.00 52.67 ? 1343 HOH A O 1 HETATM 6641 O O . HOH O 9 . ? 20.735 40.850 13.042 0.40 33.76 ? 1344 HOH A O 1 HETATM 6642 O O . HOH O 9 . ? 44.980 38.667 23.821 1.00 49.59 ? 1345 HOH A O 1 HETATM 6643 O O . HOH O 9 . ? 19.441 47.531 43.977 1.00 56.13 ? 1346 HOH A O 1 HETATM 6644 O O . HOH O 9 . ? -3.231 53.037 21.006 1.00 41.03 ? 1347 HOH A O 1 HETATM 6645 O O . HOH O 9 . ? 40.144 35.742 15.709 1.00 41.69 ? 1348 HOH A O 1 HETATM 6646 O O . HOH O 9 . ? 21.917 44.739 8.110 0.40 34.54 ? 1349 HOH A O 1 HETATM 6647 O O . HOH O 9 . ? 29.988 73.179 27.371 1.00 59.12 ? 1350 HOH A O 1 HETATM 6648 O O . HOH O 9 . ? 34.137 5.771 13.218 1.00 43.45 ? 1351 HOH A O 1 HETATM 6649 O O . HOH O 9 . ? 25.101 38.697 44.363 1.00 57.30 ? 1352 HOH A O 1 HETATM 6650 O O . HOH O 9 . ? 30.075 31.720 36.919 1.00 55.31 ? 1353 HOH A O 1 HETATM 6651 O O . HOH O 9 . ? 6.612 79.410 11.044 1.00 50.49 ? 1354 HOH A O 1 HETATM 6652 O O . HOH O 9 . ? -0.852 78.444 8.614 1.00 43.90 ? 1355 HOH A O 1 HETATM 6653 O O . HOH O 9 . ? -1.039 74.891 10.843 1.00 45.75 ? 1356 HOH A O 1 HETATM 6654 O O . HOH O 9 . ? 3.130 62.423 -14.224 1.00 35.07 ? 1357 HOH A O 1 HETATM 6655 O O . HOH O 9 . ? -2.523 51.074 3.950 1.00 26.46 ? 1358 HOH A O 1 HETATM 6656 O O . HOH O 9 . ? -0.127 49.755 1.415 1.00 33.86 ? 1359 HOH A O 1 HETATM 6657 O O . HOH O 9 . ? 0.001 51.989 0.000 0.50 24.05 ? 1360 HOH A O 1 HETATM 6658 O O . HOH O 9 . ? 31.501 47.707 17.383 1.00 53.51 ? 1361 HOH A O 1 HETATM 6659 O O . HOH O 9 . ? 40.851 56.249 17.760 1.00 45.51 ? 1362 HOH A O 1 HETATM 6660 O O . HOH O 9 . ? 43.392 55.830 11.495 1.00 55.22 ? 1363 HOH A O 1 HETATM 6661 O O . HOH O 9 . ? 32.141 54.201 9.039 1.00 40.10 ? 1364 HOH A O 1 HETATM 6662 O O . HOH O 9 . ? 20.219 67.264 0.559 1.00 36.58 ? 1365 HOH A O 1 HETATM 6663 O O . HOH O 9 . ? 17.410 72.290 -4.637 1.00 25.07 ? 1366 HOH A O 1 HETATM 6664 O O . HOH O 9 . ? 39.084 19.676 4.281 1.00 50.30 ? 1367 HOH A O 1 HETATM 6665 O O . HOH O 9 . ? 41.198 21.882 1.782 1.00 44.93 ? 1368 HOH A O 1 HETATM 6666 O O . HOH O 9 . ? 25.965 72.624 2.005 1.00 58.21 ? 1369 HOH A O 1 HETATM 6667 O O . HOH O 9 . ? 41.636 25.988 2.660 1.00 54.24 ? 1370 HOH A O 1 HETATM 6668 O O . HOH O 9 . ? 30.393 73.347 6.347 1.00 48.10 ? 1371 HOH A O 1 HETATM 6669 O O . HOH O 9 . ? 33.247 72.172 13.277 1.00 63.09 ? 1372 HOH A O 1 HETATM 6670 O O . HOH O 9 . ? 45.527 63.248 14.682 1.00 60.46 ? 1373 HOH A O 1 HETATM 6671 O O . HOH O 9 . ? 43.014 69.638 14.844 1.00 65.71 ? 1374 HOH A O 1 HETATM 6672 O O . HOH O 9 . ? 19.291 24.186 -17.027 1.00 48.19 ? 1375 HOH A O 1 HETATM 6673 O O . HOH O 9 . ? 40.709 59.240 1.006 1.00 47.25 ? 1376 HOH A O 1 HETATM 6674 O O . HOH O 9 . ? 26.392 48.579 2.774 1.00 38.43 ? 1377 HOH A O 1 HETATM 6675 O O . HOH O 9 . ? 38.850 50.426 17.118 0.70 35.10 ? 1378 HOH A O 1 HETATM 6676 O O . HOH O 9 . ? 41.616 44.291 17.543 1.00 53.53 ? 1379 HOH A O 1 HETATM 6677 O O . HOH O 9 . ? 38.458 38.509 18.281 1.00 45.44 ? 1380 HOH A O 1 HETATM 6678 O O . HOH O 9 . ? 31.161 55.349 37.967 1.00 54.70 ? 1381 HOH A O 1 HETATM 6679 O O . HOH O 9 . ? 26.114 59.572 -5.103 1.00 43.78 ? 1382 HOH A O 1 HETATM 6680 O O . HOH O 9 . ? 24.916 53.020 -2.036 1.00 41.20 ? 1383 HOH A O 1 HETATM 6681 O O . HOH O 9 . ? 22.182 56.612 -17.389 1.00 39.56 ? 1384 HOH A O 1 HETATM 6682 O O . HOH O 9 . ? 23.400 51.900 -15.166 1.00 43.72 ? 1385 HOH A O 1 HETATM 6683 O O . HOH O 9 . ? 24.907 53.685 -16.041 1.00 42.54 ? 1386 HOH A O 1 HETATM 6684 O O . HOH O 9 . ? 31.156 4.899 12.345 1.00 68.83 ? 1387 HOH A O 1 HETATM 6685 O O . HOH O 9 . ? 27.199 54.506 -14.273 1.00 52.70 ? 1388 HOH A O 1 HETATM 6686 O O . HOH O 9 . ? 27.171 46.456 -15.752 1.00 56.32 ? 1389 HOH A O 1 HETATM 6687 O O . HOH O 9 . ? 21.635 43.392 -19.686 1.00 50.25 ? 1390 HOH A O 1 HETATM 6688 O O . HOH O 9 . ? 23.825 45.054 -20.715 1.00 60.75 ? 1391 HOH A O 1 HETATM 6689 O O . HOH O 9 . ? 26.733 49.038 -15.466 1.00 46.80 ? 1392 HOH A O 1 HETATM 6690 O O . HOH O 9 . ? 26.085 46.515 -19.247 1.00 64.01 ? 1393 HOH A O 1 HETATM 6691 O O . HOH O 9 . ? 23.353 49.268 -20.293 1.00 56.67 ? 1394 HOH A O 1 HETATM 6692 O O . HOH O 9 . ? 32.823 42.080 -8.118 1.00 63.16 ? 1395 HOH A O 1 HETATM 6693 O O . HOH O 9 . ? 24.907 34.216 -5.420 1.00 52.39 ? 1396 HOH A O 1 HETATM 6694 O O . HOH O 9 . ? 20.952 37.567 -21.398 1.00 60.00 ? 1397 HOH A O 1 HETATM 6695 O O . HOH O 9 . ? 18.802 36.040 -22.751 1.00 56.82 ? 1398 HOH A O 1 HETATM 6696 O O . HOH O 9 . ? 18.596 33.887 -24.736 1.00 56.21 ? 1399 HOH A O 1 HETATM 6697 O O . HOH O 9 . ? 12.803 30.745 -19.005 1.00 47.10 ? 1400 HOH A O 1 HETATM 6698 O O . HOH O 9 . ? 14.179 41.940 -21.742 1.00 43.93 ? 1401 HOH A O 1 HETATM 6699 O O . HOH O 9 . ? 13.935 44.325 -22.590 1.00 40.12 ? 1402 HOH A O 1 HETATM 6700 O O A HOH O 9 . ? 11.416 44.723 -24.068 0.60 28.71 ? 1403 HOH A O 1 HETATM 6701 O O B HOH O 9 . ? 11.628 43.239 -23.653 0.40 29.40 ? 1404 HOH A O 1 HETATM 6702 O O . HOH O 9 . ? 14.570 51.898 -25.117 1.00 53.94 ? 1405 HOH A O 1 HETATM 6703 O O . HOH O 9 . ? 7.162 65.052 -17.948 1.00 48.78 ? 1406 HOH A O 1 HETATM 6704 O O . HOH O 9 . ? 11.750 61.509 -17.735 1.00 43.50 ? 1407 HOH A O 1 HETATM 6705 O O . HOH O 9 . ? 9.786 61.451 -19.375 1.00 51.23 ? 1408 HOH A O 1 HETATM 6706 O O . HOH O 9 . ? 6.862 55.068 -19.164 1.00 63.23 ? 1409 HOH A O 1 HETATM 6707 O O . HOH O 9 . ? 23.551 60.862 -14.030 1.00 45.14 ? 1410 HOH A O 1 HETATM 6708 O O . HOH O 9 . ? 22.669 62.965 -14.624 1.00 40.48 ? 1411 HOH A O 1 HETATM 6709 O O . HOH O 9 . ? 17.761 69.453 -19.083 1.00 51.76 ? 1412 HOH A O 1 HETATM 6710 O O . HOH O 9 . ? 7.793 70.826 -11.571 1.00 50.95 ? 1413 HOH A O 1 HETATM 6711 O O . HOH O 9 . ? 12.780 80.344 -11.599 1.00 52.97 ? 1414 HOH A O 1 HETATM 6712 O O . HOH O 9 . ? 4.940 78.330 -9.298 1.00 49.30 ? 1415 HOH A O 1 HETATM 6713 O O . HOH O 9 . ? 5.273 84.202 -5.713 1.00 42.51 ? 1416 HOH A O 1 HETATM 6714 O O . HOH O 9 . ? 3.317 83.791 -3.893 1.00 48.74 ? 1417 HOH A O 1 HETATM 6715 O O . HOH O 9 . ? 1.450 81.941 -4.557 1.00 42.91 ? 1418 HOH A O 1 HETATM 6716 O O . HOH O 9 . ? 2.942 82.557 -9.874 1.00 58.74 ? 1419 HOH A O 1 HETATM 6717 O O . HOH O 9 . ? 3.352 83.485 -0.120 1.00 54.15 ? 1420 HOH A O 1 HETATM 6718 O O . HOH O 9 . ? 0.634 82.096 -7.024 1.00 58.14 ? 1421 HOH A O 1 HETATM 6719 O O . HOH O 9 . ? 3.991 82.950 5.344 1.00 52.87 ? 1422 HOH A O 1 HETATM 6720 O O . HOH O 9 . ? -1.420 79.923 -7.321 1.00 51.73 ? 1423 HOH A O 1 HETATM 6721 O O . HOH O 9 . ? 0.126 82.311 0.084 0.50 38.58 ? 1424 HOH A O 1 HETATM 6722 O O . HOH O 9 . ? 3.255 81.095 3.307 1.00 32.76 ? 1425 HOH A O 1 HETATM 6723 O O . HOH O 9 . ? 3.017 69.287 -9.534 1.00 34.41 ? 1426 HOH A O 1 HETATM 6724 O O . HOH O 9 . ? 4.129 38.065 -5.067 1.00 45.52 ? 1427 HOH A O 1 HETATM 6725 O O . HOH O 9 . ? 2.902 34.710 -7.140 1.00 49.64 ? 1428 HOH A O 1 HETATM 6726 O O . HOH O 9 . ? 7.422 32.859 -5.087 1.00 46.59 ? 1429 HOH A O 1 HETATM 6727 O O . HOH O 9 . ? 1.321 34.292 6.138 1.00 48.09 ? 1430 HOH A O 1 HETATM 6728 O O . HOH O 9 . ? 0.190 32.027 -0.878 0.50 42.02 ? 1431 HOH A O 1 HETATM 6729 O O . HOH O 9 . ? 0.885 34.926 -4.886 1.00 43.21 ? 1432 HOH A O 1 HETATM 6730 O O . HOH O 9 . ? 0.340 34.403 -2.567 1.00 52.53 ? 1433 HOH A O 1 HETATM 6731 O O . HOH O 9 . ? 19.333 33.565 -0.679 1.00 53.34 ? 1434 HOH A O 1 HETATM 6732 O O . HOH O 9 . ? 17.469 31.970 -1.619 1.00 43.20 ? 1435 HOH A O 1 HETATM 6733 O O . HOH O 9 . ? 19.498 25.488 -4.318 1.00 61.44 ? 1436 HOH A O 1 HETATM 6734 O O . HOH O 9 . ? 26.031 27.783 -4.139 1.00 48.08 ? 1437 HOH A O 1 HETATM 6735 O O . HOH O 9 . ? 9.078 28.997 -11.409 1.00 36.08 ? 1438 HOH A O 1 HETATM 6736 O O . HOH O 9 . ? 13.443 30.941 -6.212 1.00 47.22 ? 1439 HOH A O 1 # 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 ARG 1 34 ? ? ? A . n A 1 2 SER 2 35 ? ? ? A . n A 1 3 GLU 3 36 ? ? ? A . n A 1 4 THR 4 37 ? ? ? A . n A 1 5 THR 5 38 ? ? ? A . n A 1 6 THR 6 39 ? ? ? A . n A 1 7 SER 7 40 ? ? ? A . n A 1 8 VAL 8 41 ? ? ? A . n A 1 9 ARG 9 42 ? ? ? A . n A 1 10 TYR 10 43 ? ? ? A . n A 1 11 HIS 11 44 ? ? ? A . n A 1 12 GLN 12 45 ? ? ? A . n A 1 13 SER 13 46 46 SER SER A . n A 1 14 ILE 14 47 47 ILE ILE A . n A 1 15 ARG 15 48 48 ARG ARG A . n A 1 16 TRP 16 49 49 TRP TRP A . n A 1 17 LYS 17 50 50 LYS LYS A . n A 1 18 LEU 18 51 51 LEU LEU A . n A 1 19 VAL 19 52 52 VAL VAL A . n A 1 20 SER 20 53 53 SER SER A . n A 1 21 GLU 21 54 54 GLU GLU A . n A 1 22 MET 22 55 55 MET MET A . n A 1 23 LYS 23 56 56 LYS LYS A . n A 1 24 ALA 24 57 57 ALA ALA A . n A 1 25 GLU 25 58 58 GLU GLU A . n A 1 26 ASN 26 59 59 ASN ASN A . n A 1 27 ILE 27 60 60 ILE ILE A . n A 1 28 LYS 28 61 61 LYS LYS A . n A 1 29 SER 29 62 62 SER SER A . n A 1 30 PHE 30 63 63 PHE PHE A . n A 1 31 LEU 31 64 64 LEU LEU A . n A 1 32 ARG 32 65 65 ARG ARG A . n A 1 33 SER 33 66 66 SER SER A . n A 1 34 PHE 34 67 67 PHE PHE A . n A 1 35 THR 35 68 68 THR THR A . n A 1 36 LYS 36 69 69 LYS LYS A . n A 1 37 LEU 37 70 70 LEU LEU A . n A 1 38 PRO 38 71 71 PRO PRO A . n A 1 39 HIS 39 72 72 HIS HIS A . n A 1 40 LEU 40 73 73 LEU LEU A . n A 1 41 ALA 41 74 74 ALA ALA A . n A 1 42 GLY 42 75 75 GLY GLY A . n A 1 43 THR 43 76 76 THR THR A . n A 1 44 GLU 44 77 77 GLU GLU A . n A 1 45 GLN 45 78 78 GLN GLN A . n A 1 46 ASN 46 79 79 ASN ASN A . n A 1 47 PHE 47 80 80 PHE PHE A . n A 1 48 LEU 48 81 81 LEU LEU A . n A 1 49 LEU 49 82 82 LEU LEU A . n A 1 50 ALA 50 83 83 ALA ALA A . n A 1 51 LYS 51 84 84 LYS LYS A . n A 1 52 LYS 52 85 85 LYS LYS A . n A 1 53 ILE 53 86 86 ILE ILE A . n A 1 54 GLN 54 87 87 GLN GLN A . n A 1 55 THR 55 88 88 THR THR A . n A 1 56 GLN 56 89 89 GLN GLN A . n A 1 57 TRP 57 90 90 TRP TRP A . n A 1 58 LYS 58 91 91 LYS LYS A . n A 1 59 LYS 59 92 92 LYS LYS A . n A 1 60 PHE 60 93 93 PHE PHE A . n A 1 61 GLY 61 94 94 GLY GLY A . n A 1 62 LEU 62 95 95 LEU LEU A . n A 1 63 ASP 63 96 96 ASP ASP A . n A 1 64 SER 64 97 97 SER SER A . n A 1 65 ALA 65 98 98 ALA ALA A . n A 1 66 LYS 66 99 99 LYS LYS A . n A 1 67 LEU 67 100 100 LEU LEU A . n A 1 68 VAL 68 101 101 VAL VAL A . n A 1 69 HIS 69 102 102 HIS HIS A . n A 1 70 TYR 70 103 103 TYR TYR A . n A 1 71 ASP 71 104 104 ASP ASP A . n A 1 72 VAL 72 105 105 VAL VAL A . n A 1 73 LEU 73 106 106 LEU LEU A . n A 1 74 LEU 74 107 107 LEU LEU A . n A 1 75 SER 75 108 108 SER SER A . n A 1 76 TYR 76 109 109 TYR TYR A . n A 1 77 PRO 77 110 110 PRO PRO A . n A 1 78 ASN 78 111 111 ASN ASN A . n A 1 79 GLU 79 112 112 GLU GLU A . n A 1 80 THR 80 113 113 THR THR A . n A 1 81 ASN 81 114 114 ASN ASN A . n A 1 82 ALA 82 115 115 ALA ALA A . n A 1 83 ASN 83 116 116 ASN ASN A . n A 1 84 TYR 84 117 117 TYR TYR A . n A 1 85 ILE 85 118 118 ILE ILE A . n A 1 86 SER 86 119 119 SER SER A . n A 1 87 ILE 87 120 120 ILE ILE A . n A 1 88 VAL 88 121 121 VAL VAL A . n A 1 89 ASP 89 122 122 ASP ASP A . n A 1 90 GLU 90 123 123 GLU GLU A . n A 1 91 HIS 91 124 124 HIS HIS A . n A 1 92 GLU 92 125 125 GLU GLU A . n A 1 93 THR 93 126 126 THR THR A . n A 1 94 GLU 94 127 127 GLU GLU A . n A 1 95 ILE 95 128 128 ILE ILE A . n A 1 96 PHE 96 129 129 PHE PHE A . n A 1 97 LYS 97 130 130 LYS LYS A . n A 1 98 THR 98 131 131 THR THR A . n A 1 99 SER 99 132 132 SER SER A . n A 1 100 TYR 100 133 ? ? ? A . n A 1 101 LEU 101 134 ? ? ? A . n A 1 102 GLU 102 135 ? ? ? A . n A 1 103 PRO 103 136 ? ? ? A . n A 1 104 PRO 104 137 137 PRO PRO A . n A 1 105 PRO 105 138 138 PRO PRO A . n A 1 106 ASP 106 139 139 ASP ASP A . n A 1 107 GLY 107 140 140 GLY GLY A . n A 1 108 TYR 108 141 141 TYR TYR A . n A 1 109 GLU 109 142 142 GLU GLU A . n A 1 110 ASN 110 143 143 ASN ASN A . n A 1 111 VAL 111 144 144 VAL VAL A . n A 1 112 THR 112 145 145 THR THR A . n A 1 113 ASN 113 146 146 ASN ASN A . n A 1 114 ILE 114 147 147 ILE ILE A . n A 1 115 VAL 115 148 148 VAL VAL A . n A 1 116 PRO 116 149 149 PRO PRO A . n A 1 117 PRO 117 150 150 PRO PRO A . n A 1 118 TYR 118 151 151 TYR TYR A . n A 1 119 ASN 119 152 152 ASN ASN A . n A 1 120 ALA 120 153 153 ALA ALA A . n A 1 121 PHE 121 154 154 PHE PHE A . n A 1 122 SER 122 155 155 SER SER A . n A 1 123 ALA 123 156 156 ALA ALA A . n A 1 124 GLN 124 157 157 GLN GLN A . n A 1 125 GLY 125 158 158 GLY GLY A . n A 1 126 MET 126 159 159 MET MET A . n A 1 127 PRO 127 160 160 PRO PRO A . n A 1 128 GLU 128 161 161 GLU GLU A . n A 1 129 GLY 129 162 162 GLY GLY A . n A 1 130 ASP 130 163 163 ASP ASP A . n A 1 131 LEU 131 164 164 LEU LEU A . n A 1 132 VAL 132 165 165 VAL VAL A . n A 1 133 TYR 133 166 166 TYR TYR A . n A 1 134 VAL 134 167 167 VAL VAL A . n A 1 135 ASN 135 168 168 ASN ASN A . n A 1 136 TYR 136 169 169 TYR TYR A . n A 1 137 ALA 137 170 170 ALA ALA A . n A 1 138 ARG 138 171 171 ARG ARG A . n A 1 139 THR 139 172 172 THR THR A . n A 1 140 GLU 140 173 173 GLU GLU A . n A 1 141 ASP 141 174 174 ASP ASP A . n A 1 142 PHE 142 175 175 PHE PHE A . n A 1 143 PHE 143 176 176 PHE PHE A . n A 1 144 LYS 144 177 177 LYS LYS A . n A 1 145 LEU 145 178 178 LEU LEU A . n A 1 146 GLU 146 179 179 GLU GLU A . n A 1 147 ARG 147 180 180 ARG ARG A . n A 1 148 GLU 148 181 181 GLU GLU A . n A 1 149 MET 149 182 182 MET MET A . n A 1 150 GLY 150 183 183 GLY GLY A . n A 1 151 ILE 151 184 184 ILE ILE A . n A 1 152 ASN 152 185 185 ASN ASN A . n A 1 153 CYS 153 186 186 CYS CYS A . n A 1 154 THR 154 187 187 THR THR A . n A 1 155 GLY 155 188 188 GLY GLY A . n A 1 156 LYS 156 189 189 LYS LYS A . n A 1 157 ILE 157 190 190 ILE ILE A . n A 1 158 VAL 158 191 191 VAL VAL A . n A 1 159 ILE 159 192 192 ILE ILE A . n A 1 160 ALA 160 193 193 ALA ALA A . n A 1 161 ARG 161 194 194 ARG ARG A . n A 1 162 TYR 162 195 195 TYR TYR A . n A 1 163 GLY 163 196 196 GLY GLY A . n A 1 164 LYS 164 197 197 LYS LYS A . n A 1 165 ILE 165 198 198 ILE ILE A . n A 1 166 PHE 166 199 199 PHE PHE A . n A 1 167 ARG 167 200 200 ARG ARG A . n A 1 168 GLY 168 201 201 GLY GLY A . n A 1 169 ASN 169 202 202 ASN ASN A . n A 1 170 LYS 170 203 203 LYS LYS A . n A 1 171 VAL 171 204 204 VAL VAL A . n A 1 172 LYS 172 205 205 LYS LYS A . n A 1 173 ASN 173 206 206 ASN ASN A . n A 1 174 ALA 174 207 207 ALA ALA A . n A 1 175 MET 175 208 208 MET MET A . n A 1 176 LEU 176 209 209 LEU LEU A . n A 1 177 ALA 177 210 210 ALA ALA A . n A 1 178 GLY 178 211 211 GLY GLY A . n A 1 179 ALA 179 212 212 ALA ALA A . n A 1 180 ILE 180 213 213 ILE ILE A . n A 1 181 GLY 181 214 214 GLY GLY A . n A 1 182 ILE 182 215 215 ILE ILE A . n A 1 183 ILE 183 216 216 ILE ILE A . n A 1 184 LEU 184 217 217 LEU LEU A . n A 1 185 TYR 185 218 218 TYR TYR A . n A 1 186 SER 186 219 219 SER SER A . n A 1 187 ASP 187 220 220 ASP ASP A . n A 1 188 PRO 188 221 221 PRO PRO A . n A 1 189 ALA 189 222 222 ALA ALA A . n A 1 190 ASP 190 223 223 ASP ASP A . n A 1 191 TYR 191 224 224 TYR TYR A . n A 1 192 PHE 192 225 225 PHE PHE A . n A 1 193 ALA 193 226 226 ALA ALA A . n A 1 194 PRO 194 227 227 PRO PRO A . n A 1 195 GLU 195 228 228 GLU GLU A . n A 1 196 VAL 196 229 229 VAL VAL A . n A 1 197 GLN 197 230 230 GLN GLN A . n A 1 198 PRO 198 231 231 PRO PRO A . n A 1 199 TYR 199 232 232 TYR TYR A . n A 1 200 PRO 200 233 233 PRO PRO A . n A 1 201 LYS 201 234 234 LYS LYS A . n A 1 202 GLY 202 235 235 GLY GLY A . n A 1 203 TRP 203 236 236 TRP TRP A . n A 1 204 ASN 204 237 237 ASN ASN A . n A 1 205 LEU 205 238 238 LEU LEU A . n A 1 206 PRO 206 239 239 PRO PRO A . n A 1 207 GLY 207 240 240 GLY GLY A . n A 1 208 THR 208 241 241 THR THR A . n A 1 209 ALA 209 242 242 ALA ALA A . n A 1 210 ALA 210 243 243 ALA ALA A . n A 1 211 GLN 211 244 244 GLN GLN A . n A 1 212 ARG 212 245 245 ARG ARG A . n A 1 213 GLY 213 246 246 GLY GLY A . n A 1 214 ASN 214 247 247 ASN ASN A . n A 1 215 VAL 215 248 248 VAL VAL A . n A 1 216 LEU 216 249 249 LEU LEU A . n A 1 217 ASN 217 250 250 ASN ASN A . n A 1 218 LEU 218 251 251 LEU LEU A . n A 1 219 ASN 219 252 252 ASN ASN A . n A 1 220 GLY 220 253 253 GLY GLY A . n A 1 221 ALA 221 254 254 ALA ALA A . n A 1 222 GLY 222 255 255 GLY GLY A . n A 1 223 ASP 223 256 256 ASP ASP A . n A 1 224 PRO 224 257 257 PRO PRO A . n A 1 225 LEU 225 258 258 LEU LEU A . n A 1 226 THR 226 259 259 THR THR A . n A 1 227 PRO 227 260 260 PRO PRO A . n A 1 228 GLY 228 261 261 GLY GLY A . n A 1 229 TYR 229 262 262 TYR TYR A . n A 1 230 PRO 230 263 263 PRO PRO A . n A 1 231 ALA 231 264 264 ALA ALA A . n A 1 232 LYS 232 265 265 LYS LYS A . n A 1 233 GLU 233 266 266 GLU GLU A . n A 1 234 TYR 234 267 267 TYR TYR A . n A 1 235 THR 235 268 268 THR THR A . n A 1 236 PHE 236 269 269 PHE PHE A . n A 1 237 ARG 237 270 270 ARG ARG A . n A 1 238 LEU 238 271 271 LEU LEU A . n A 1 239 ASP 239 272 272 ASP ASP A . n A 1 240 VAL 240 273 273 VAL VAL A . n A 1 241 GLU 241 274 274 GLU GLU A . n A 1 242 GLU 242 275 275 GLU GLU A . n A 1 243 GLY 243 276 276 GLY GLY A . n A 1 244 VAL 244 277 277 VAL VAL A . n A 1 245 GLY 245 278 278 GLY GLY A . n A 1 246 ILE 246 279 279 ILE ILE A . n A 1 247 PRO 247 280 280 PRO PRO A . n A 1 248 ARG 248 281 281 ARG ARG A . n A 1 249 ILE 249 282 282 ILE ILE A . n A 1 250 PRO 250 283 283 PRO PRO A . n A 1 251 VAL 251 284 284 VAL VAL A . n A 1 252 HIS 252 285 285 HIS HIS A . n A 1 253 PRO 253 286 286 PRO PRO A . n A 1 254 ILE 254 287 287 ILE ILE A . n A 1 255 GLY 255 288 288 GLY GLY A . n A 1 256 TYR 256 289 289 TYR TYR A . n A 1 257 ASN 257 290 290 ASN ASN A . n A 1 258 ASP 258 291 291 ASP ASP A . n A 1 259 ALA 259 292 292 ALA ALA A . n A 1 260 GLU 260 293 293 GLU GLU A . n A 1 261 ILE 261 294 294 ILE ILE A . n A 1 262 LEU 262 295 295 LEU LEU A . n A 1 263 LEU 263 296 296 LEU LEU A . n A 1 264 ARG 264 297 297 ARG ARG A . n A 1 265 TYR 265 298 298 TYR TYR A . n A 1 266 LEU 266 299 299 LEU LEU A . n A 1 267 GLY 267 300 300 GLY GLY A . n A 1 268 GLY 268 301 301 GLY GLY A . n A 1 269 ILE 269 302 302 ILE ILE A . n A 1 270 ALA 270 303 303 ALA ALA A . n A 1 271 PRO 271 304 304 PRO PRO A . n A 1 272 PRO 272 305 305 PRO PRO A . n A 1 273 ASP 273 306 306 ASP ASP A . n A 1 274 LYS 274 307 307 LYS LYS A . n A 1 275 SER 275 308 308 SER SER A . n A 1 276 TRP 276 309 309 TRP TRP A . n A 1 277 LYS 277 310 310 LYS LYS A . n A 1 278 GLY 278 311 311 GLY GLY A . n A 1 279 ALA 279 312 312 ALA ALA A . n A 1 280 LEU 280 313 313 LEU LEU A . n A 1 281 ASN 281 314 314 ASN ASN A . n A 1 282 VAL 282 315 315 VAL VAL A . n A 1 283 SER 283 316 316 SER SER A . n A 1 284 TYR 284 317 317 TYR TYR A . n A 1 285 SER 285 318 318 SER SER A . n A 1 286 ILE 286 319 319 ILE ILE A . n A 1 287 GLY 287 320 320 GLY GLY A . n A 1 288 PRO 288 321 321 PRO PRO A . n A 1 289 GLY 289 322 322 GLY GLY A . n A 1 290 PHE 290 323 323 PHE PHE A . n A 1 291 THR 291 324 324 THR THR A . n A 1 292 GLY 292 325 325 GLY GLY A . n A 1 293 SER 293 326 326 SER SER A . n A 1 294 ASP 294 327 ? ? ? A . n A 1 295 SER 295 328 328 SER SER A . n A 1 296 PHE 296 329 329 PHE PHE A . n A 1 297 ARG 297 330 330 ARG ARG A . n A 1 298 LYS 298 331 331 LYS LYS A . n A 1 299 VAL 299 332 332 VAL VAL A . n A 1 300 ARG 300 333 333 ARG ARG A . n A 1 301 MET 301 334 334 MET MET A . n A 1 302 HIS 302 335 335 HIS HIS A . n A 1 303 VAL 303 336 336 VAL VAL A . n A 1 304 TYR 304 337 337 TYR TYR A . n A 1 305 ASN 305 338 338 ASN ASN A . n A 1 306 ILE 306 339 339 ILE ILE A . n A 1 307 ASN 307 340 340 ASN ASN A . n A 1 308 LYS 308 341 341 LYS LYS A . n A 1 309 ILE 309 342 342 ILE ILE A . n A 1 310 THR 310 343 343 THR THR A . n A 1 311 ARG 311 344 344 ARG ARG A . n A 1 312 ILE 312 345 345 ILE ILE A . n A 1 313 TYR 313 346 346 TYR TYR A . n A 1 314 ASN 314 347 347 ASN ASN A . n A 1 315 VAL 315 348 348 VAL VAL A . n A 1 316 VAL 316 349 349 VAL VAL A . n A 1 317 GLY 317 350 350 GLY GLY A . n A 1 318 THR 318 351 351 THR THR A . n A 1 319 ILE 319 352 352 ILE ILE A . n A 1 320 ARG 320 353 353 ARG ARG A . n A 1 321 GLY 321 354 354 GLY GLY A . n A 1 322 SER 322 355 355 SER SER A . n A 1 323 VAL 323 356 356 VAL VAL A . n A 1 324 GLU 324 357 357 GLU GLU A . n A 1 325 PRO 325 358 358 PRO PRO A . n A 1 326 ASP 326 359 359 ASP ASP A . n A 1 327 ARG 327 360 360 ARG ARG A . n A 1 328 TYR 328 361 361 TYR TYR A . n A 1 329 VAL 329 362 362 VAL VAL A . n A 1 330 ILE 330 363 363 ILE ILE A . n A 1 331 LEU 331 364 364 LEU LEU A . n A 1 332 GLY 332 365 365 GLY GLY A . n A 1 333 GLY 333 366 366 GLY GLY A . n A 1 334 HIS 334 367 367 HIS HIS A . n A 1 335 ARG 335 368 368 ARG ARG A . n A 1 336 ASP 336 369 369 ASP ASP A . n A 1 337 SER 337 370 370 SER SER A . n A 1 338 TRP 338 371 371 TRP TRP A . n A 1 339 VAL 339 372 372 VAL VAL A . n A 1 340 PHE 340 373 373 PHE PHE A . n A 1 341 GLY 341 374 374 GLY GLY A . n A 1 342 ALA 342 375 375 ALA ALA A . n A 1 343 ILE 343 376 376 ILE ILE A . n A 1 344 ASP 344 377 377 ASP ASP A . n A 1 345 PRO 345 378 378 PRO PRO A . n A 1 346 THR 346 379 379 THR THR A . n A 1 347 SER 347 380 380 SER SER A . n A 1 348 GLY 348 381 381 GLY GLY A . n A 1 349 VAL 349 382 382 VAL VAL A . n A 1 350 ALA 350 383 383 ALA ALA A . n A 1 351 VAL 351 384 384 VAL VAL A . n A 1 352 LEU 352 385 385 LEU LEU A . n A 1 353 GLN 353 386 386 GLN GLN A . n A 1 354 GLU 354 387 387 GLU GLU A . n A 1 355 ILE 355 388 388 ILE ILE A . n A 1 356 ALA 356 389 389 ALA ALA A . n A 1 357 ARG 357 390 390 ARG ARG A . n A 1 358 SER 358 391 391 SER SER A . n A 1 359 PHE 359 392 392 PHE PHE A . n A 1 360 GLY 360 393 393 GLY GLY A . n A 1 361 LYS 361 394 394 LYS LYS A . n A 1 362 LEU 362 395 395 LEU LEU A . n A 1 363 MET 363 396 396 MET MET A . n A 1 364 SER 364 397 397 SER SER A . n A 1 365 LYS 365 398 398 LYS LYS A . n A 1 366 GLY 366 399 399 GLY GLY A . n A 1 367 TRP 367 400 400 TRP TRP A . n A 1 368 ARG 368 401 401 ARG ARG A . n A 1 369 PRO 369 402 402 PRO PRO A . n A 1 370 ARG 370 403 403 ARG ARG A . n A 1 371 ARG 371 404 404 ARG ARG A . n A 1 372 THR 372 405 405 THR THR A . n A 1 373 ILE 373 406 406 ILE ILE A . n A 1 374 ILE 374 407 407 ILE ILE A . n A 1 375 PHE 375 408 408 PHE PHE A . n A 1 376 ALA 376 409 409 ALA ALA A . n A 1 377 SER 377 410 410 SER SER A . n A 1 378 TRP 378 411 411 TRP TRP A . n A 1 379 ASP 379 412 412 ASP ASP A . n A 1 380 ALA 380 413 413 ALA ALA A . n A 1 381 GLU 381 414 414 GLU GLU A . n A 1 382 GLU 382 415 415 GLU GLU A . n A 1 383 PHE 383 416 416 PHE PHE A . n A 1 384 GLY 384 417 417 GLY GLY A . n A 1 385 LEU 385 418 418 LEU LEU A . n A 1 386 LEU 386 419 419 LEU LEU A . n A 1 387 GLY 387 420 420 GLY GLY A . n A 1 388 SER 388 421 421 SER SER A . n A 1 389 THR 389 422 422 THR THR A . n A 1 390 GLU 390 423 423 GLU GLU A . n A 1 391 TRP 391 424 424 TRP TRP A . n A 1 392 ALA 392 425 425 ALA ALA A . n A 1 393 GLU 393 426 426 GLU GLU A . n A 1 394 GLU 394 427 427 GLU GLU A . n A 1 395 ASN 395 428 428 ASN ASN A . n A 1 396 VAL 396 429 429 VAL VAL A . n A 1 397 LYS 397 430 430 LYS LYS A . n A 1 398 ILE 398 431 431 ILE ILE A . n A 1 399 LEU 399 432 432 LEU LEU A . n A 1 400 GLN 400 433 433 GLN GLN A . n A 1 401 GLU 401 434 434 GLU GLU A . n A 1 402 ARG 402 435 435 ARG ARG A . n A 1 403 SER 403 436 436 SER SER A . n A 1 404 ILE 404 437 437 ILE ILE A . n A 1 405 ALA 405 438 438 ALA ALA A . n A 1 406 TYR 406 439 439 TYR TYR A . n A 1 407 ILE 407 440 440 ILE ILE A . n A 1 408 ASN 408 441 441 ASN ASN A . n A 1 409 SER 409 442 442 SER SER A . n A 1 410 ASP 410 443 443 ASP ASP A . n A 1 411 SER 411 444 444 SER SER A . n A 1 412 SER 412 445 445 SER SER A . n A 1 413 ILE 413 446 446 ILE ILE A . n A 1 414 GLU 414 447 447 GLU GLU A . n A 1 415 GLY 415 448 448 GLY GLY A . n A 1 416 ASN 416 449 449 ASN ASN A . n A 1 417 TYR 417 450 450 TYR TYR A . n A 1 418 THR 418 451 451 THR THR A . n A 1 419 LEU 419 452 452 LEU LEU A . n A 1 420 ARG 420 453 453 ARG ARG A . n A 1 421 VAL 421 454 454 VAL VAL A . n A 1 422 ASP 422 455 455 ASP ASP A . n A 1 423 CYS 423 456 456 CYS CYS A . n A 1 424 THR 424 457 457 THR THR A . n A 1 425 PRO 425 458 458 PRO PRO A . n A 1 426 LEU 426 459 459 LEU LEU A . n A 1 427 LEU 427 460 460 LEU LEU A . n A 1 428 TYR 428 461 461 TYR TYR A . n A 1 429 GLN 429 462 462 GLN GLN A . n A 1 430 LEU 430 463 463 LEU LEU A . n A 1 431 VAL 431 464 464 VAL VAL A . n A 1 432 TYR 432 465 465 TYR TYR A . n A 1 433 LYS 433 466 466 LYS LYS A . n A 1 434 LEU 434 467 467 LEU LEU A . n A 1 435 THR 435 468 468 THR THR A . n A 1 436 LYS 436 469 469 LYS LYS A . n A 1 437 GLU 437 470 470 GLU GLU A . n A 1 438 ILE 438 471 471 ILE ILE A . n A 1 439 PRO 439 472 472 PRO PRO A . n A 1 440 SER 440 473 473 SER SER A . n A 1 441 PRO 441 474 474 PRO PRO A . n A 1 442 ASP 442 475 475 ASP ASP A . n A 1 443 ASP 443 476 476 ASP ASP A . n A 1 444 GLY 444 477 477 GLY GLY A . n A 1 445 PHE 445 478 478 PHE PHE A . n A 1 446 GLU 446 479 479 GLU GLU A . n A 1 447 SER 447 480 480 SER SER A . n A 1 448 LYS 448 481 481 LYS LYS A . n A 1 449 SER 449 482 482 SER SER A . n A 1 450 LEU 450 483 483 LEU LEU A . n A 1 451 TYR 451 484 484 TYR TYR A . n A 1 452 GLU 452 485 485 GLU GLU A . n A 1 453 SER 453 486 486 SER SER A . n A 1 454 TRP 454 487 487 TRP TRP A . n A 1 455 LEU 455 488 488 LEU LEU A . n A 1 456 GLU 456 489 489 GLU GLU A . n A 1 457 LYS 457 490 490 LYS LYS A . n A 1 458 ASP 458 491 491 ASP ASP A . n A 1 459 PRO 459 492 492 PRO PRO A . n A 1 460 SER 460 493 493 SER SER A . n A 1 461 PRO 461 494 494 PRO PRO A . n A 1 462 GLU 462 495 495 GLU GLU A . n A 1 463 ASN 463 496 496 ASN ASN A . n A 1 464 LYS 464 497 497 LYS LYS A . n A 1 465 ASN 465 498 498 ASN ASN A . n A 1 466 LEU 466 499 499 LEU LEU A . n A 1 467 PRO 467 500 500 PRO PRO A . n A 1 468 ARG 468 501 501 ARG ARG A . n A 1 469 ILE 469 502 502 ILE ILE A . n A 1 470 ASN 470 503 503 ASN ASN A . n A 1 471 LYS 471 504 504 LYS LYS A . n A 1 472 LEU 472 505 505 LEU LEU A . n A 1 473 GLY 473 506 506 GLY GLY A . n A 1 474 SER 474 507 507 SER SER A . n A 1 475 GLY 475 508 508 GLY GLY A . n A 1 476 SER 476 509 509 SER SER A . n A 1 477 ASP 477 510 510 ASP ASP A . n A 1 478 PHE 478 511 511 PHE PHE A . n A 1 479 GLU 479 512 512 GLU GLU A . n A 1 480 ALA 480 513 513 ALA ALA A . n A 1 481 TYR 481 514 514 TYR TYR A . n A 1 482 PHE 482 515 515 PHE PHE A . n A 1 483 GLN 483 516 516 GLN GLN A . n A 1 484 ARG 484 517 517 ARG ARG A . n A 1 485 LEU 485 518 518 LEU LEU A . n A 1 486 GLY 486 519 519 GLY GLY A . n A 1 487 ILE 487 520 520 ILE ILE A . n A 1 488 ALA 488 521 521 ALA ALA A . n A 1 489 SER 489 522 522 SER SER A . n A 1 490 GLY 490 523 523 GLY GLY A . n A 1 491 ARG 491 524 524 ARG ARG A . n A 1 492 ALA 492 525 525 ALA ALA A . n A 1 493 ARG 493 526 526 ARG ARG A . n A 1 494 TYR 494 527 527 TYR TYR A . n A 1 495 THR 495 528 528 THR THR A . n A 1 496 LYS 496 529 529 LYS LYS A . n A 1 497 ASN 497 530 530 ASN ASN A . n A 1 498 LYS 498 531 531 LYS LYS A . n A 1 499 LYS 499 532 532 LYS LYS A . n A 1 500 THR 500 533 533 THR THR A . n A 1 501 ASP 501 534 534 ASP ASP A . n A 1 502 LYS 502 535 535 LYS LYS A . n A 1 503 TYR 503 536 536 TYR TYR A . n A 1 504 SER 504 537 537 SER SER A . n A 1 505 SER 505 538 538 SER SER A . n A 1 506 TYR 506 539 539 TYR TYR A . n A 1 507 PRO 507 540 540 PRO PRO A . n A 1 508 VAL 508 541 541 VAL VAL A . n A 1 509 TYR 509 542 542 TYR TYR A . n A 1 510 HIS 510 543 543 HIS HIS A . n A 1 511 THR 511 544 544 THR THR A . n A 1 512 ILE 512 545 545 ILE ILE A . n A 1 513 TYR 513 546 546 TYR TYR A . n A 1 514 GLU 514 547 547 GLU GLU A . n A 1 515 THR 515 548 548 THR THR A . n A 1 516 PHE 516 549 549 PHE PHE A . n A 1 517 GLU 517 550 550 GLU GLU A . n A 1 518 LEU 518 551 551 LEU LEU A . n A 1 519 VAL 519 552 552 VAL VAL A . n A 1 520 GLU 520 553 553 GLU GLU A . n A 1 521 LYS 521 554 554 LYS LYS A . n A 1 522 PHE 522 555 555 PHE PHE A . n A 1 523 TYR 523 556 556 TYR TYR A . n A 1 524 ASP 524 557 557 ASP ASP A . n A 1 525 PRO 525 558 558 PRO PRO A . n A 1 526 THR 526 559 559 THR THR A . n A 1 527 PHE 527 560 560 PHE PHE A . n A 1 528 LYS 528 561 561 LYS LYS A . n A 1 529 LYS 529 562 562 LYS LYS A . n A 1 530 GLN 530 563 563 GLN GLN A . n A 1 531 LEU 531 564 564 LEU LEU A . n A 1 532 SER 532 565 565 SER SER A . n A 1 533 VAL 533 566 566 VAL VAL A . n A 1 534 ALA 534 567 567 ALA ALA A . n A 1 535 GLN 535 568 568 GLN GLN A . n A 1 536 LEU 536 569 569 LEU LEU A . n A 1 537 ARG 537 570 570 ARG ARG A . n A 1 538 GLY 538 571 571 GLY GLY A . n A 1 539 ALA 539 572 572 ALA ALA A . n A 1 540 LEU 540 573 573 LEU LEU A . n A 1 541 VAL 541 574 574 VAL VAL A . n A 1 542 TYR 542 575 575 TYR TYR A . n A 1 543 GLU 543 576 576 GLU GLU A . n A 1 544 LEU 544 577 577 LEU LEU A . n A 1 545 VAL 545 578 578 VAL VAL A . n A 1 546 ASP 546 579 579 ASP ASP A . n A 1 547 SER 547 580 580 SER SER A . n A 1 548 LYS 548 581 581 LYS LYS A . n A 1 549 ILE 549 582 582 ILE ILE A . n A 1 550 ILE 550 583 583 ILE ILE A . n A 1 551 PRO 551 584 584 PRO PRO A . n A 1 552 PHE 552 585 585 PHE PHE A . n A 1 553 ASN 553 586 586 ASN ASN A . n A 1 554 ILE 554 587 587 ILE ILE A . n A 1 555 GLN 555 588 588 GLN GLN A . n A 1 556 ASP 556 589 589 ASP ASP A . n A 1 557 TYR 557 590 590 TYR TYR A . n A 1 558 ALA 558 591 591 ALA ALA A . n A 1 559 GLU 559 592 592 GLU GLU A . n A 1 560 ALA 560 593 593 ALA ALA A . n A 1 561 LEU 561 594 594 LEU LEU A . n A 1 562 LYS 562 595 595 LYS LYS A . n A 1 563 ASN 563 596 596 ASN ASN A . n A 1 564 TYR 564 597 597 TYR TYR A . n A 1 565 ALA 565 598 598 ALA ALA A . n A 1 566 ALA 566 599 599 ALA ALA A . n A 1 567 SER 567 600 600 SER SER A . n A 1 568 ILE 568 601 601 ILE ILE A . n A 1 569 TYR 569 602 602 TYR TYR A . n A 1 570 ASN 570 603 603 ASN ASN A . n A 1 571 LEU 571 604 604 LEU LEU A . n A 1 572 SER 572 605 605 SER SER A . n A 1 573 LYS 573 606 606 LYS LYS A . n A 1 574 LYS 574 607 607 LYS LYS A . n A 1 575 HIS 575 608 608 HIS HIS A . n A 1 576 ASP 576 609 609 ASP ASP A . n A 1 577 GLN 577 610 610 GLN GLN A . n A 1 578 GLN 578 611 611 GLN GLN A . n A 1 579 LEU 579 612 612 LEU LEU A . n A 1 580 THR 580 613 613 THR THR A . n A 1 581 ASP 581 614 614 ASP ASP A . n A 1 582 HIS 582 615 615 HIS HIS A . n A 1 583 GLY 583 616 616 GLY GLY A . n A 1 584 VAL 584 617 617 VAL VAL A . n A 1 585 SER 585 618 618 SER SER A . n A 1 586 PHE 586 619 619 PHE PHE A . n A 1 587 ASP 587 620 620 ASP ASP A . n A 1 588 SER 588 621 621 SER SER A . n A 1 589 LEU 589 622 622 LEU LEU A . n A 1 590 PHE 590 623 623 PHE PHE A . n A 1 591 SER 591 624 624 SER SER A . n A 1 592 ALA 592 625 625 ALA ALA A . n A 1 593 VAL 593 626 626 VAL VAL A . n A 1 594 LYS 594 627 627 LYS LYS A . n A 1 595 ASN 595 628 628 ASN ASN A . n A 1 596 PHE 596 629 629 PHE PHE A . n A 1 597 SER 597 630 630 SER SER A . n A 1 598 GLU 598 631 631 GLU GLU A . n A 1 599 ALA 599 632 632 ALA ALA A . n A 1 600 ALA 600 633 633 ALA ALA A . n A 1 601 SER 601 634 634 SER SER A . n A 1 602 ASP 602 635 635 ASP ASP A . n A 1 603 PHE 603 636 636 PHE PHE A . n A 1 604 HIS 604 637 637 HIS HIS A . n A 1 605 LYS 605 638 638 LYS LYS A . n A 1 606 ARG 606 639 639 ARG ARG A . n A 1 607 LEU 607 640 640 LEU LEU A . n A 1 608 ILE 608 641 641 ILE ILE A . n A 1 609 GLN 609 642 642 GLN GLN A . n A 1 610 VAL 610 643 643 VAL VAL A . n A 1 611 ASP 611 644 644 ASP ASP A . n A 1 612 LEU 612 645 645 LEU LEU A . n A 1 613 ASN 613 646 646 ASN ASN A . n A 1 614 ASN 614 647 647 ASN ASN A . n A 1 615 PRO 615 648 648 PRO PRO A . n A 1 616 ILE 616 649 649 ILE ILE A . n A 1 617 ALA 617 650 650 ALA ALA A . n A 1 618 VAL 618 651 651 VAL VAL A . n A 1 619 ARG 619 652 652 ARG ARG A . n A 1 620 MET 620 653 653 MET MET A . n A 1 621 MET 621 654 654 MET MET A . n A 1 622 ASN 622 655 655 ASN ASN A . n A 1 623 ASP 623 656 656 ASP ASP A . n A 1 624 GLN 624 657 657 GLN GLN A . n A 1 625 LEU 625 658 658 LEU LEU A . n A 1 626 MET 626 659 659 MET MET A . n A 1 627 LEU 627 660 660 LEU LEU A . n A 1 628 LEU 628 661 661 LEU LEU A . n A 1 629 GLU 629 662 662 GLU GLU A . n A 1 630 ARG 630 663 663 ARG ARG A . n A 1 631 ALA 631 664 664 ALA ALA A . n A 1 632 PHE 632 665 665 PHE PHE A . n A 1 633 ILE 633 666 666 ILE ILE A . n A 1 634 ASP 634 667 667 ASP ASP A . n A 1 635 PRO 635 668 668 PRO PRO A . n A 1 636 LEU 636 669 669 LEU LEU A . n A 1 637 GLY 637 670 670 GLY GLY A . n A 1 638 LEU 638 671 671 LEU LEU A . n A 1 639 PRO 639 672 672 PRO PRO A . n A 1 640 GLY 640 673 673 GLY GLY A . n A 1 641 LYS 641 674 674 LYS LYS A . n A 1 642 LEU 642 675 675 LEU LEU A . n A 1 643 PHE 643 676 676 PHE PHE A . n A 1 644 TYR 644 677 677 TYR TYR A . n A 1 645 ARG 645 678 678 ARG ARG A . n A 1 646 HIS 646 679 679 HIS HIS A . n A 1 647 ILE 647 680 680 ILE ILE A . n A 1 648 ILE 648 681 681 ILE ILE A . n A 1 649 PHE 649 682 682 PHE PHE A . n A 1 650 ALA 650 683 683 ALA ALA A . n A 1 651 PRO 651 684 684 PRO PRO A . n A 1 652 SER 652 685 685 SER SER A . n A 1 653 SER 653 686 686 SER SER A . n A 1 654 HIS 654 687 687 HIS HIS A . n A 1 655 ASN 655 688 688 ASN ASN A . n A 1 656 LYS 656 689 689 LYS LYS A . n A 1 657 TYR 657 690 690 TYR TYR A . n A 1 658 ALA 658 691 691 ALA ALA A . n A 1 659 GLY 659 692 692 GLY GLY A . n A 1 660 GLU 660 693 693 GLU GLU A . n A 1 661 SER 661 694 694 SER SER A . n A 1 662 PHE 662 695 695 PHE PHE A . n A 1 663 PRO 663 696 696 PRO PRO A . n A 1 664 GLY 664 697 697 GLY GLY A . n A 1 665 ILE 665 698 698 ILE ILE A . n A 1 666 TYR 666 699 699 TYR TYR A . n A 1 667 ASP 667 700 700 ASP ASP A . n A 1 668 ALA 668 701 701 ALA ALA A . n A 1 669 ILE 669 702 702 ILE ILE A . n A 1 670 PHE 670 703 703 PHE PHE A . n A 1 671 ASP 671 704 704 ASP ASP A . n A 1 672 ILE 672 705 705 ILE ILE A . n A 1 673 GLU 673 706 706 GLU GLU A . n A 1 674 ASN 674 707 707 ASN ASN A . n A 1 675 LYS 675 708 708 LYS LYS A . n A 1 676 ALA 676 709 709 ALA ALA A . n A 1 677 ASN 677 710 710 ASN ASN A . n A 1 678 SER 678 711 711 SER SER A . n A 1 679 ARG 679 712 712 ARG ARG A . n A 1 680 LEU 680 713 713 LEU LEU A . n A 1 681 ALA 681 714 714 ALA ALA A . n A 1 682 TRP 682 715 715 TRP TRP A . n A 1 683 LYS 683 716 716 LYS LYS A . n A 1 684 GLU 684 717 717 GLU GLU A . n A 1 685 VAL 685 718 718 VAL VAL A . n A 1 686 LYS 686 719 719 LYS LYS A . n A 1 687 LYS 687 720 720 LYS LYS A . n A 1 688 HIS 688 721 721 HIS HIS A . n A 1 689 ILE 689 722 722 ILE ILE A . n A 1 690 SER 690 723 723 SER SER A . n A 1 691 ILE 691 724 724 ILE ILE A . n A 1 692 ALA 692 725 725 ALA ALA A . n A 1 693 ALA 693 726 726 ALA ALA A . n A 1 694 PHE 694 727 727 PHE PHE A . n A 1 695 THR 695 728 728 THR THR A . n A 1 696 ILE 696 729 729 ILE ILE A . n A 1 697 GLN 697 730 730 GLN GLN A . n A 1 698 ALA 698 731 731 ALA ALA A . n A 1 699 ALA 699 732 732 ALA ALA A . n A 1 700 ALA 700 733 733 ALA ALA A . n A 1 701 GLY 701 734 734 GLY GLY A . n A 1 702 THR 702 735 735 THR THR A . n A 1 703 LEU 703 736 736 LEU LEU A . n A 1 704 LYS 704 737 737 LYS LYS A . n A 1 705 GLU 705 738 738 GLU GLU A . n A 1 706 VAL 706 739 739 VAL VAL A . n A 1 707 LEU 707 740 ? ? ? A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 GLU 1 742 742 GLU GLU A . C 3 NAG 1 1756 1756 NAG NAG A . D 3 NAG 1 1758 1758 NAG NAG A . E 3 NAG 1 1759 1759 NAG NAG A . F 3 NAG 2 1760 1760 NAG NAG A . G 3 NAG 1 1766 1766 NAG NAG A . H 4 ZN 1 1751 1751 ZN ZN A . I 4 ZN 1 1752 1752 ZN ZN A . J 5 CL 1 1754 1754 CL CL A . K 6 CA 1 1755 1755 CA CA A . L 7 GOL 1 1 1 GOL GOL A . M 7 GOL 1 2 2 GOL GOL A . N 8 MPO 1 741 741 MPO MPO A . O 9 HOH 1 3 3 HOH HOH A . O 9 HOH 2 4 4 HOH HOH A . O 9 HOH 3 5 5 HOH HOH A . O 9 HOH 4 6 6 HOH HOH A . O 9 HOH 5 7 7 HOH HOH A . O 9 HOH 6 8 8 HOH HOH A . O 9 HOH 7 9 9 HOH HOH A . O 9 HOH 8 10 10 HOH HOH A . O 9 HOH 9 11 11 HOH HOH A . O 9 HOH 10 12 12 HOH HOH A . O 9 HOH 11 13 13 HOH HOH A . O 9 HOH 12 14 14 HOH HOH A . O 9 HOH 13 15 15 HOH HOH A . O 9 HOH 14 16 16 HOH HOH A . O 9 HOH 15 17 17 HOH HOH A . O 9 HOH 16 18 18 HOH HOH A . O 9 HOH 17 19 19 HOH HOH A . O 9 HOH 18 21 21 HOH HOH A . O 9 HOH 19 22 22 HOH HOH A . O 9 HOH 20 23 23 HOH HOH A . O 9 HOH 21 24 24 HOH HOH A . O 9 HOH 22 25 25 HOH HOH A . O 9 HOH 23 26 26 HOH HOH A . O 9 HOH 24 27 27 HOH HOH A . O 9 HOH 25 28 28 HOH HOH A . O 9 HOH 26 29 29 HOH HOH A . O 9 HOH 27 30 30 HOH HOH A . O 9 HOH 28 31 31 HOH HOH A . O 9 HOH 29 32 32 HOH HOH A . O 9 HOH 30 33 33 HOH HOH A . O 9 HOH 31 743 743 HOH HOH A . O 9 HOH 32 744 744 HOH HOH A . O 9 HOH 33 745 745 HOH HOH A . O 9 HOH 34 746 746 HOH HOH A . O 9 HOH 35 747 747 HOH HOH A . O 9 HOH 36 748 748 HOH HOH A . O 9 HOH 37 749 749 HOH HOH A . O 9 HOH 38 750 750 HOH HOH A . O 9 HOH 39 751 751 HOH HOH A . O 9 HOH 40 752 752 HOH HOH A . O 9 HOH 41 753 753 HOH HOH A . O 9 HOH 42 754 754 HOH HOH A . O 9 HOH 43 755 755 HOH HOH A . O 9 HOH 44 756 756 HOH HOH A . O 9 HOH 45 757 757 HOH HOH A . O 9 HOH 46 758 758 HOH HOH A . O 9 HOH 47 759 759 HOH HOH A . O 9 HOH 48 760 760 HOH HOH A . O 9 HOH 49 761 761 HOH HOH A . O 9 HOH 50 762 762 HOH HOH A . O 9 HOH 51 763 763 HOH HOH A . O 9 HOH 52 764 764 HOH HOH A . O 9 HOH 53 765 765 HOH HOH A . O 9 HOH 54 766 766 HOH HOH A . O 9 HOH 55 767 767 HOH HOH A . O 9 HOH 56 768 768 HOH HOH A . O 9 HOH 57 769 769 HOH HOH A . O 9 HOH 58 770 770 HOH HOH A . O 9 HOH 59 771 771 HOH HOH A . O 9 HOH 60 772 772 HOH HOH A . O 9 HOH 61 773 773 HOH HOH A . O 9 HOH 62 774 774 HOH HOH A . O 9 HOH 63 775 775 HOH HOH A . O 9 HOH 64 776 776 HOH HOH A . O 9 HOH 65 777 777 HOH HOH A . O 9 HOH 66 778 778 HOH HOH A . O 9 HOH 67 779 779 HOH HOH A . O 9 HOH 68 780 780 HOH HOH A . O 9 HOH 69 781 781 HOH HOH A . O 9 HOH 70 782 782 HOH HOH A . O 9 HOH 71 783 783 HOH HOH A . O 9 HOH 72 784 784 HOH HOH A . O 9 HOH 73 785 785 HOH HOH A . O 9 HOH 74 786 786 HOH HOH A . O 9 HOH 75 787 787 HOH HOH A . O 9 HOH 76 788 788 HOH HOH A . O 9 HOH 77 789 789 HOH HOH A . O 9 HOH 78 790 790 HOH HOH A . O 9 HOH 79 791 791 HOH HOH A . O 9 HOH 80 792 792 HOH HOH A . O 9 HOH 81 793 793 HOH HOH A . O 9 HOH 82 794 794 HOH HOH A . O 9 HOH 83 795 795 HOH HOH A . O 9 HOH 84 796 796 HOH HOH A . O 9 HOH 85 797 797 HOH HOH A . O 9 HOH 86 798 798 HOH HOH A . O 9 HOH 87 799 799 HOH HOH A . O 9 HOH 88 800 800 HOH HOH A . O 9 HOH 89 801 801 HOH HOH A . O 9 HOH 90 802 802 HOH HOH A . O 9 HOH 91 803 803 HOH HOH A . O 9 HOH 92 804 804 HOH HOH A . O 9 HOH 93 805 805 HOH HOH A . O 9 HOH 94 806 806 HOH HOH A . O 9 HOH 95 807 807 HOH HOH A . O 9 HOH 96 808 808 HOH HOH A . O 9 HOH 97 809 809 HOH HOH A . O 9 HOH 98 810 810 HOH HOH A . O 9 HOH 99 811 811 HOH HOH A . O 9 HOH 100 812 812 HOH HOH A . O 9 HOH 101 813 813 HOH HOH A . O 9 HOH 102 814 814 HOH HOH A . O 9 HOH 103 815 815 HOH HOH A . O 9 HOH 104 816 816 HOH HOH A . O 9 HOH 105 817 817 HOH HOH A . O 9 HOH 106 818 818 HOH HOH A . O 9 HOH 107 819 819 HOH HOH A . O 9 HOH 108 820 820 HOH HOH A . O 9 HOH 109 821 821 HOH HOH A . O 9 HOH 110 822 822 HOH HOH A . O 9 HOH 111 823 823 HOH HOH A . O 9 HOH 112 824 824 HOH HOH A . O 9 HOH 113 825 825 HOH HOH A . O 9 HOH 114 826 826 HOH HOH A . O 9 HOH 115 827 827 HOH HOH A . O 9 HOH 116 828 828 HOH HOH A . O 9 HOH 117 829 829 HOH HOH A . O 9 HOH 118 830 830 HOH HOH A . O 9 HOH 119 831 831 HOH HOH A . O 9 HOH 120 832 832 HOH HOH A . O 9 HOH 121 833 833 HOH HOH A . O 9 HOH 122 834 834 HOH HOH A . O 9 HOH 123 835 835 HOH HOH A . O 9 HOH 124 836 836 HOH HOH A . O 9 HOH 125 837 837 HOH HOH A . O 9 HOH 126 838 838 HOH HOH A . O 9 HOH 127 839 839 HOH HOH A . O 9 HOH 128 840 840 HOH HOH A . O 9 HOH 129 841 841 HOH HOH A . O 9 HOH 130 842 842 HOH HOH A . O 9 HOH 131 843 843 HOH HOH A . O 9 HOH 132 844 844 HOH HOH A . O 9 HOH 133 845 845 HOH HOH A . O 9 HOH 134 846 846 HOH HOH A . O 9 HOH 135 847 847 HOH HOH A . O 9 HOH 136 848 848 HOH HOH A . O 9 HOH 137 849 849 HOH HOH A . O 9 HOH 138 850 850 HOH HOH A . O 9 HOH 139 851 851 HOH HOH A . O 9 HOH 140 852 852 HOH HOH A . O 9 HOH 141 853 853 HOH HOH A . O 9 HOH 142 854 854 HOH HOH A . O 9 HOH 143 855 855 HOH HOH A . O 9 HOH 144 856 856 HOH HOH A . O 9 HOH 145 857 857 HOH HOH A . O 9 HOH 146 858 858 HOH HOH A . O 9 HOH 147 859 859 HOH HOH A . O 9 HOH 148 860 860 HOH HOH A . O 9 HOH 149 861 861 HOH HOH A . O 9 HOH 150 862 862 HOH HOH A . O 9 HOH 151 863 863 HOH HOH A . O 9 HOH 152 864 864 HOH HOH A . O 9 HOH 153 865 865 HOH HOH A . O 9 HOH 154 866 866 HOH HOH A . O 9 HOH 155 867 867 HOH HOH A . O 9 HOH 156 868 868 HOH HOH A . O 9 HOH 157 869 869 HOH HOH A . O 9 HOH 158 870 870 HOH HOH A . O 9 HOH 159 871 871 HOH HOH A . O 9 HOH 160 872 872 HOH HOH A . O 9 HOH 161 873 873 HOH HOH A . O 9 HOH 162 874 874 HOH HOH A . O 9 HOH 163 875 875 HOH HOH A . O 9 HOH 164 876 876 HOH HOH A . O 9 HOH 165 877 877 HOH HOH A . O 9 HOH 166 878 878 HOH HOH A . O 9 HOH 167 879 879 HOH HOH A . O 9 HOH 168 880 880 HOH HOH A . O 9 HOH 169 881 881 HOH HOH A . O 9 HOH 170 882 882 HOH HOH A . O 9 HOH 171 883 883 HOH HOH A . O 9 HOH 172 884 884 HOH HOH A . O 9 HOH 173 885 885 HOH HOH A . O 9 HOH 174 886 886 HOH HOH A . O 9 HOH 175 887 887 HOH HOH A . O 9 HOH 176 888 888 HOH HOH A . O 9 HOH 177 889 889 HOH HOH A . O 9 HOH 178 890 890 HOH HOH A . O 9 HOH 179 891 891 HOH HOH A . O 9 HOH 180 892 892 HOH HOH A . O 9 HOH 181 893 893 HOH HOH A . O 9 HOH 182 894 894 HOH HOH A . O 9 HOH 183 895 895 HOH HOH A . O 9 HOH 184 896 896 HOH HOH A . O 9 HOH 185 897 897 HOH HOH A . O 9 HOH 186 898 898 HOH HOH A . O 9 HOH 187 899 899 HOH HOH A . O 9 HOH 188 900 900 HOH HOH A . O 9 HOH 189 901 901 HOH HOH A . O 9 HOH 190 902 902 HOH HOH A . O 9 HOH 191 903 903 HOH HOH A . O 9 HOH 192 904 904 HOH HOH A . O 9 HOH 193 905 905 HOH HOH A . O 9 HOH 194 906 906 HOH HOH A . O 9 HOH 195 907 907 HOH HOH A . O 9 HOH 196 908 908 HOH HOH A . O 9 HOH 197 909 909 HOH HOH A . O 9 HOH 198 910 910 HOH HOH A . O 9 HOH 199 911 911 HOH HOH A . O 9 HOH 200 912 912 HOH HOH A . O 9 HOH 201 913 913 HOH HOH A . O 9 HOH 202 914 914 HOH HOH A . O 9 HOH 203 915 915 HOH HOH A . O 9 HOH 204 916 916 HOH HOH A . O 9 HOH 205 917 917 HOH HOH A . O 9 HOH 206 918 918 HOH HOH A . O 9 HOH 207 919 919 HOH HOH A . O 9 HOH 208 920 920 HOH HOH A . O 9 HOH 209 921 921 HOH HOH A . O 9 HOH 210 922 922 HOH HOH A . O 9 HOH 211 923 923 HOH HOH A . O 9 HOH 212 924 924 HOH HOH A . O 9 HOH 213 925 925 HOH HOH A . O 9 HOH 214 926 926 HOH HOH A . O 9 HOH 215 927 927 HOH HOH A . O 9 HOH 216 928 928 HOH HOH A . O 9 HOH 217 929 929 HOH HOH A . O 9 HOH 218 930 930 HOH HOH A . O 9 HOH 219 931 931 HOH HOH A . O 9 HOH 220 932 932 HOH HOH A . O 9 HOH 221 933 933 HOH HOH A . O 9 HOH 222 934 934 HOH HOH A . O 9 HOH 223 935 935 HOH HOH A . O 9 HOH 224 936 936 HOH HOH A . O 9 HOH 225 937 937 HOH HOH A . O 9 HOH 226 938 938 HOH HOH A . O 9 HOH 227 939 939 HOH HOH A . O 9 HOH 228 940 940 HOH HOH A . O 9 HOH 229 941 941 HOH HOH A . O 9 HOH 230 942 942 HOH HOH A . O 9 HOH 231 943 943 HOH HOH A . O 9 HOH 232 944 944 HOH HOH A . O 9 HOH 233 945 945 HOH HOH A . O 9 HOH 234 946 946 HOH HOH A . O 9 HOH 235 947 947 HOH HOH A . O 9 HOH 236 948 948 HOH HOH A . O 9 HOH 237 949 949 HOH HOH A . O 9 HOH 238 950 950 HOH HOH A . O 9 HOH 239 951 951 HOH HOH A . O 9 HOH 240 952 952 HOH HOH A . O 9 HOH 241 953 953 HOH HOH A . O 9 HOH 242 954 954 HOH HOH A . O 9 HOH 243 955 955 HOH HOH A . O 9 HOH 244 956 956 HOH HOH A . O 9 HOH 245 957 957 HOH HOH A . O 9 HOH 246 958 958 HOH HOH A . O 9 HOH 247 959 959 HOH HOH A . O 9 HOH 248 960 960 HOH HOH A . O 9 HOH 249 961 961 HOH HOH A . O 9 HOH 250 962 962 HOH HOH A . O 9 HOH 251 963 963 HOH HOH A . O 9 HOH 252 964 964 HOH HOH A . O 9 HOH 253 965 965 HOH HOH A . O 9 HOH 254 966 966 HOH HOH A . O 9 HOH 255 967 967 HOH HOH A . O 9 HOH 256 968 968 HOH HOH A . O 9 HOH 257 969 969 HOH HOH A . O 9 HOH 258 970 970 HOH HOH A . O 9 HOH 259 971 971 HOH HOH A . O 9 HOH 260 972 972 HOH HOH A . O 9 HOH 261 973 973 HOH HOH A . O 9 HOH 262 974 974 HOH HOH A . O 9 HOH 263 975 975 HOH HOH A . O 9 HOH 264 976 976 HOH HOH A . O 9 HOH 265 977 977 HOH HOH A . O 9 HOH 266 978 978 HOH HOH A . O 9 HOH 267 979 979 HOH HOH A . O 9 HOH 268 980 980 HOH HOH A . O 9 HOH 269 981 981 HOH HOH A . O 9 HOH 270 982 982 HOH HOH A . O 9 HOH 271 983 983 HOH HOH A . O 9 HOH 272 984 984 HOH HOH A . O 9 HOH 273 985 985 HOH HOH A . O 9 HOH 274 986 986 HOH HOH A . O 9 HOH 275 987 987 HOH HOH A . O 9 HOH 276 988 988 HOH HOH A . O 9 HOH 277 989 989 HOH HOH A . O 9 HOH 278 990 990 HOH HOH A . O 9 HOH 279 991 991 HOH HOH A . O 9 HOH 280 992 992 HOH HOH A . O 9 HOH 281 993 993 HOH HOH A . O 9 HOH 282 994 994 HOH HOH A . O 9 HOH 283 995 995 HOH HOH A . O 9 HOH 284 996 996 HOH HOH A . O 9 HOH 285 997 997 HOH HOH A . O 9 HOH 286 998 998 HOH HOH A . O 9 HOH 287 999 999 HOH HOH A . O 9 HOH 288 1000 1000 HOH HOH A . O 9 HOH 289 1001 1001 HOH HOH A . O 9 HOH 290 1002 1002 HOH HOH A . O 9 HOH 291 1003 1003 HOH HOH A . O 9 HOH 292 1004 1004 HOH HOH A . O 9 HOH 293 1005 1005 HOH HOH A . O 9 HOH 294 1006 1006 HOH HOH A . O 9 HOH 295 1007 1007 HOH HOH A . O 9 HOH 296 1008 1008 HOH HOH A . O 9 HOH 297 1009 1009 HOH HOH A . O 9 HOH 298 1010 1010 HOH HOH A . O 9 HOH 299 1011 1011 HOH HOH A . O 9 HOH 300 1012 1012 HOH HOH A . O 9 HOH 301 1013 1013 HOH HOH A . O 9 HOH 302 1014 1014 HOH HOH A . O 9 HOH 303 1015 1015 HOH HOH A . O 9 HOH 304 1016 1016 HOH HOH A . O 9 HOH 305 1017 1017 HOH HOH A . O 9 HOH 306 1018 1018 HOH HOH A . O 9 HOH 307 1019 1019 HOH HOH A . O 9 HOH 308 1020 1020 HOH HOH A . O 9 HOH 309 1021 1021 HOH HOH A . O 9 HOH 310 1022 1022 HOH HOH A . O 9 HOH 311 1023 1023 HOH HOH A . O 9 HOH 312 1024 1024 HOH HOH A . O 9 HOH 313 1025 1025 HOH HOH A . O 9 HOH 314 1026 1026 HOH HOH A . O 9 HOH 315 1027 1027 HOH HOH A . O 9 HOH 316 1028 1028 HOH HOH A . O 9 HOH 317 1029 1029 HOH HOH A . O 9 HOH 318 1030 1030 HOH HOH A . O 9 HOH 319 1031 1031 HOH HOH A . O 9 HOH 320 1032 1032 HOH HOH A . O 9 HOH 321 1033 1033 HOH HOH A . O 9 HOH 322 1034 1034 HOH HOH A . O 9 HOH 323 1035 1035 HOH HOH A . O 9 HOH 324 1036 1036 HOH HOH A . O 9 HOH 325 1037 1037 HOH HOH A . O 9 HOH 326 1038 1038 HOH HOH A . O 9 HOH 327 1039 1039 HOH HOH A . O 9 HOH 328 1040 1040 HOH HOH A . O 9 HOH 329 1041 1041 HOH HOH A . O 9 HOH 330 1042 1042 HOH HOH A . O 9 HOH 331 1043 1043 HOH HOH A . O 9 HOH 332 1044 1044 HOH HOH A . O 9 HOH 333 1045 1045 HOH HOH A . O 9 HOH 334 1046 1046 HOH HOH A . O 9 HOH 335 1047 1047 HOH HOH A . O 9 HOH 336 1048 1048 HOH HOH A . O 9 HOH 337 1049 1049 HOH HOH A . O 9 HOH 338 1050 1050 HOH HOH A . O 9 HOH 339 1051 1051 HOH HOH A . O 9 HOH 340 1052 1052 HOH HOH A . O 9 HOH 341 1053 1053 HOH HOH A . O 9 HOH 342 1054 1054 HOH HOH A . O 9 HOH 343 1055 1055 HOH HOH A . O 9 HOH 344 1056 1056 HOH HOH A . O 9 HOH 345 1057 1057 HOH HOH A . O 9 HOH 346 1058 1058 HOH HOH A . O 9 HOH 347 1059 1059 HOH HOH A . O 9 HOH 348 1060 1060 HOH HOH A . O 9 HOH 349 1061 1061 HOH HOH A . O 9 HOH 350 1062 1062 HOH HOH A . O 9 HOH 351 1063 1063 HOH HOH A . O 9 HOH 352 1064 1064 HOH HOH A . O 9 HOH 353 1065 1065 HOH HOH A . O 9 HOH 354 1066 1066 HOH HOH A . O 9 HOH 355 1067 1067 HOH HOH A . O 9 HOH 356 1068 1068 HOH HOH A . O 9 HOH 357 1069 1069 HOH HOH A . O 9 HOH 358 1070 1070 HOH HOH A . O 9 HOH 359 1071 1071 HOH HOH A . O 9 HOH 360 1072 1072 HOH HOH A . O 9 HOH 361 1073 1073 HOH HOH A . O 9 HOH 362 1074 1074 HOH HOH A . O 9 HOH 363 1075 1075 HOH HOH A . O 9 HOH 364 1076 1076 HOH HOH A . O 9 HOH 365 1077 1077 HOH HOH A . O 9 HOH 366 1078 1078 HOH HOH A . O 9 HOH 367 1079 1079 HOH HOH A . O 9 HOH 368 1080 1080 HOH HOH A . O 9 HOH 369 1081 1081 HOH HOH A . O 9 HOH 370 1082 1082 HOH HOH A . O 9 HOH 371 1083 1083 HOH HOH A . O 9 HOH 372 1084 1084 HOH HOH A . O 9 HOH 373 1085 1085 HOH HOH A . O 9 HOH 374 1086 1086 HOH HOH A . O 9 HOH 375 1087 1087 HOH HOH A . O 9 HOH 376 1088 1088 HOH HOH A . O 9 HOH 377 1089 1089 HOH HOH A . O 9 HOH 378 1090 1090 HOH HOH A . O 9 HOH 379 1091 1091 HOH HOH A . O 9 HOH 380 1092 1092 HOH HOH A . O 9 HOH 381 1093 1093 HOH HOH A . O 9 HOH 382 1094 1094 HOH HOH A . O 9 HOH 383 1095 1095 HOH HOH A . O 9 HOH 384 1096 1096 HOH HOH A . O 9 HOH 385 1097 1097 HOH HOH A . O 9 HOH 386 1098 1098 HOH HOH A . O 9 HOH 387 1099 1099 HOH HOH A . O 9 HOH 388 1100 1100 HOH HOH A . O 9 HOH 389 1101 1101 HOH HOH A . O 9 HOH 390 1102 1102 HOH HOH A . O 9 HOH 391 1103 1103 HOH HOH A . O 9 HOH 392 1104 1104 HOH HOH A . O 9 HOH 393 1105 1105 HOH HOH A . O 9 HOH 394 1106 1106 HOH HOH A . O 9 HOH 395 1107 1107 HOH HOH A . O 9 HOH 396 1108 1108 HOH HOH A . O 9 HOH 397 1109 1109 HOH HOH A . O 9 HOH 398 1110 1110 HOH HOH A . O 9 HOH 399 1111 1111 HOH HOH A . O 9 HOH 400 1112 1112 HOH HOH A . O 9 HOH 401 1113 1113 HOH HOH A . O 9 HOH 402 1114 1114 HOH HOH A . O 9 HOH 403 1115 1115 HOH HOH A . O 9 HOH 404 1116 1116 HOH HOH A . O 9 HOH 405 1117 1117 HOH HOH A . O 9 HOH 406 1118 1118 HOH HOH A . O 9 HOH 407 1119 1119 HOH HOH A . O 9 HOH 408 1120 1120 HOH HOH A . O 9 HOH 409 1121 1121 HOH HOH A . O 9 HOH 410 1122 1122 HOH HOH A . O 9 HOH 411 1123 1123 HOH HOH A . O 9 HOH 412 1124 1124 HOH HOH A . O 9 HOH 413 1125 1125 HOH HOH A . O 9 HOH 414 1126 1126 HOH HOH A . O 9 HOH 415 1127 1127 HOH HOH A . O 9 HOH 416 1128 1128 HOH HOH A . O 9 HOH 417 1129 1129 HOH HOH A . O 9 HOH 418 1130 1130 HOH HOH A . O 9 HOH 419 1131 1131 HOH HOH A . O 9 HOH 420 1132 1132 HOH HOH A . O 9 HOH 421 1133 1133 HOH HOH A . O 9 HOH 422 1134 1134 HOH HOH A . O 9 HOH 423 1135 1135 HOH HOH A . O 9 HOH 424 1136 1136 HOH HOH A . O 9 HOH 425 1137 1137 HOH HOH A . O 9 HOH 426 1138 1138 HOH HOH A . O 9 HOH 427 1139 1139 HOH HOH A . O 9 HOH 428 1140 1140 HOH HOH A . O 9 HOH 429 1141 1141 HOH HOH A . O 9 HOH 430 1142 1142 HOH HOH A . O 9 HOH 431 1143 1143 HOH HOH A . O 9 HOH 432 1144 1144 HOH HOH A . O 9 HOH 433 1145 1145 HOH HOH A . O 9 HOH 434 1146 1146 HOH HOH A . O 9 HOH 435 1147 1147 HOH HOH A . O 9 HOH 436 1148 1148 HOH HOH A . O 9 HOH 437 1149 1149 HOH HOH A . O 9 HOH 438 1150 1150 HOH HOH A . O 9 HOH 439 1151 1151 HOH HOH A . O 9 HOH 440 1152 1152 HOH HOH A . O 9 HOH 441 1153 1153 HOH HOH A . O 9 HOH 442 1154 1154 HOH HOH A . O 9 HOH 443 1155 1155 HOH HOH A . O 9 HOH 444 1156 1156 HOH HOH A . O 9 HOH 445 1157 1157 HOH HOH A . O 9 HOH 446 1158 1158 HOH HOH A . O 9 HOH 447 1159 1159 HOH HOH A . O 9 HOH 448 1160 1160 HOH HOH A . O 9 HOH 449 1161 1161 HOH HOH A . O 9 HOH 450 1162 1162 HOH HOH A . O 9 HOH 451 1163 1163 HOH HOH A . O 9 HOH 452 1164 1164 HOH HOH A . O 9 HOH 453 1165 1165 HOH HOH A . O 9 HOH 454 1166 1166 HOH HOH A . O 9 HOH 455 1167 1167 HOH HOH A . O 9 HOH 456 1168 1168 HOH HOH A . O 9 HOH 457 1169 1169 HOH HOH A . O 9 HOH 458 1170 1170 HOH HOH A . O 9 HOH 459 1171 1171 HOH HOH A . O 9 HOH 460 1172 1172 HOH HOH A . O 9 HOH 461 1173 1173 HOH HOH A . O 9 HOH 462 1174 1174 HOH HOH A . O 9 HOH 463 1175 1175 HOH HOH A . O 9 HOH 464 1176 1176 HOH HOH A . O 9 HOH 465 1177 1177 HOH HOH A . O 9 HOH 466 1178 1178 HOH HOH A . O 9 HOH 467 1179 1179 HOH HOH A . O 9 HOH 468 1180 1180 HOH HOH A . O 9 HOH 469 1181 1181 HOH HOH A . O 9 HOH 470 1182 1182 HOH HOH A . O 9 HOH 471 1183 1183 HOH HOH A . O 9 HOH 472 1184 1184 HOH HOH A . O 9 HOH 473 1185 1185 HOH HOH A . O 9 HOH 474 1186 1186 HOH HOH A . O 9 HOH 475 1187 1187 HOH HOH A . O 9 HOH 476 1188 1188 HOH HOH A . O 9 HOH 477 1189 1189 HOH HOH A . O 9 HOH 478 1190 1190 HOH HOH A . O 9 HOH 479 1191 1191 HOH HOH A . O 9 HOH 480 1192 1192 HOH HOH A . O 9 HOH 481 1193 1193 HOH HOH A . O 9 HOH 482 1194 1194 HOH HOH A . O 9 HOH 483 1195 1195 HOH HOH A . O 9 HOH 484 1196 1196 HOH HOH A . O 9 HOH 485 1197 1197 HOH HOH A . O 9 HOH 486 1198 1198 HOH HOH A . O 9 HOH 487 1199 1199 HOH HOH A . O 9 HOH 488 1200 1200 HOH HOH A . O 9 HOH 489 1201 1201 HOH HOH A . O 9 HOH 490 1202 1202 HOH HOH A . O 9 HOH 491 1203 1203 HOH HOH A . O 9 HOH 492 1204 1204 HOH HOH A . O 9 HOH 493 1205 1205 HOH HOH A . O 9 HOH 494 1206 1206 HOH HOH A . O 9 HOH 495 1207 1207 HOH HOH A . O 9 HOH 496 1208 1208 HOH HOH A . O 9 HOH 497 1209 1209 HOH HOH A . O 9 HOH 498 1210 1210 HOH HOH A . O 9 HOH 499 1211 1211 HOH HOH A . O 9 HOH 500 1212 1212 HOH HOH A . O 9 HOH 501 1213 1213 HOH HOH A . O 9 HOH 502 1214 1214 HOH HOH A . O 9 HOH 503 1215 1215 HOH HOH A . O 9 HOH 504 1216 1216 HOH HOH A . O 9 HOH 505 1217 1217 HOH HOH A . O 9 HOH 506 1218 1218 HOH HOH A . O 9 HOH 507 1219 1219 HOH HOH A . O 9 HOH 508 1220 1220 HOH HOH A . O 9 HOH 509 1221 1221 HOH HOH A . O 9 HOH 510 1222 1222 HOH HOH A . O 9 HOH 511 1223 1223 HOH HOH A . O 9 HOH 512 1224 1224 HOH HOH A . O 9 HOH 513 1225 1225 HOH HOH A . O 9 HOH 514 1226 1226 HOH HOH A . O 9 HOH 515 1227 1227 HOH HOH A . O 9 HOH 516 1228 1228 HOH HOH A . O 9 HOH 517 1229 1229 HOH HOH A . O 9 HOH 518 1230 1230 HOH HOH A . O 9 HOH 519 1231 1231 HOH HOH A . O 9 HOH 520 1232 1232 HOH HOH A . O 9 HOH 521 1233 1233 HOH HOH A . O 9 HOH 522 1234 1234 HOH HOH A . O 9 HOH 523 1235 1235 HOH HOH A . O 9 HOH 524 1236 1236 HOH HOH A . O 9 HOH 525 1237 1237 HOH HOH A . O 9 HOH 526 1238 1238 HOH HOH A . O 9 HOH 527 1239 1239 HOH HOH A . O 9 HOH 528 1240 1240 HOH HOH A . O 9 HOH 529 1241 1241 HOH HOH A . O 9 HOH 530 1242 1242 HOH HOH A . O 9 HOH 531 1243 1243 HOH HOH A . O 9 HOH 532 1244 1244 HOH HOH A . O 9 HOH 533 1245 1245 HOH HOH A . O 9 HOH 534 1246 1246 HOH HOH A . O 9 HOH 535 1247 1247 HOH HOH A . O 9 HOH 536 1248 1248 HOH HOH A . O 9 HOH 537 1249 1249 HOH HOH A . O 9 HOH 538 1250 1250 HOH HOH A . O 9 HOH 539 1251 1251 HOH HOH A . O 9 HOH 540 1252 1252 HOH HOH A . O 9 HOH 541 1253 1253 HOH HOH A . O 9 HOH 542 1254 1254 HOH HOH A . O 9 HOH 543 1255 1255 HOH HOH A . O 9 HOH 544 1256 1256 HOH HOH A . O 9 HOH 545 1257 1257 HOH HOH A . O 9 HOH 546 1258 1258 HOH HOH A . O 9 HOH 547 1259 1259 HOH HOH A . O 9 HOH 548 1260 1260 HOH HOH A . O 9 HOH 549 1261 1261 HOH HOH A . O 9 HOH 550 1262 1262 HOH HOH A . O 9 HOH 551 1263 1263 HOH HOH A . O 9 HOH 552 1264 1264 HOH HOH A . O 9 HOH 553 1265 1265 HOH HOH A . O 9 HOH 554 1266 1266 HOH HOH A . O 9 HOH 555 1267 1267 HOH HOH A . O 9 HOH 556 1268 1268 HOH HOH A . O 9 HOH 557 1269 1269 HOH HOH A . O 9 HOH 558 1270 1270 HOH HOH A . O 9 HOH 559 1271 1271 HOH HOH A . O 9 HOH 560 1272 1272 HOH HOH A . O 9 HOH 561 1273 1273 HOH HOH A . O 9 HOH 562 1274 1274 HOH HOH A . O 9 HOH 563 1275 1275 HOH HOH A . O 9 HOH 564 1276 1276 HOH HOH A . O 9 HOH 565 1277 1277 HOH HOH A . O 9 HOH 566 1278 1278 HOH HOH A . O 9 HOH 567 1279 1279 HOH HOH A . O 9 HOH 568 1280 1280 HOH HOH A . O 9 HOH 569 1281 1281 HOH HOH A . O 9 HOH 570 1282 1282 HOH HOH A . O 9 HOH 571 1283 1283 HOH HOH A . O 9 HOH 572 1284 1284 HOH HOH A . O 9 HOH 573 1285 1285 HOH HOH A . O 9 HOH 574 1286 1286 HOH HOH A . O 9 HOH 575 1287 1287 HOH HOH A . O 9 HOH 576 1288 1288 HOH HOH A . O 9 HOH 577 1289 1289 HOH HOH A . O 9 HOH 578 1290 1290 HOH HOH A . O 9 HOH 579 1291 1291 HOH HOH A . O 9 HOH 580 1292 1292 HOH HOH A . O 9 HOH 581 1293 1293 HOH HOH A . O 9 HOH 582 1294 1294 HOH HOH A . O 9 HOH 583 1295 1295 HOH HOH A . O 9 HOH 584 1296 1296 HOH HOH A . O 9 HOH 585 1297 1297 HOH HOH A . O 9 HOH 586 1298 1298 HOH HOH A . O 9 HOH 587 1299 1299 HOH HOH A . O 9 HOH 588 1300 1300 HOH HOH A . O 9 HOH 589 1301 1301 HOH HOH A . O 9 HOH 590 1302 1302 HOH HOH A . O 9 HOH 591 1303 1303 HOH HOH A . O 9 HOH 592 1304 1304 HOH HOH A . O 9 HOH 593 1305 1305 HOH HOH A . O 9 HOH 594 1306 1306 HOH HOH A . O 9 HOH 595 1307 1307 HOH HOH A . O 9 HOH 596 1308 1308 HOH HOH A . O 9 HOH 597 1309 1309 HOH HOH A . O 9 HOH 598 1310 1310 HOH HOH A . O 9 HOH 599 1311 1311 HOH HOH A . O 9 HOH 600 1312 1312 HOH HOH A . O 9 HOH 601 1313 1313 HOH HOH A . O 9 HOH 602 1314 1314 HOH HOH A . O 9 HOH 603 1315 1315 HOH HOH A . O 9 HOH 604 1316 1316 HOH HOH A . O 9 HOH 605 1317 1317 HOH HOH A . O 9 HOH 606 1318 1318 HOH HOH A . O 9 HOH 607 1319 1319 HOH HOH A . O 9 HOH 608 1320 1320 HOH HOH A . O 9 HOH 609 1321 1321 HOH HOH A . O 9 HOH 610 1322 1322 HOH HOH A . O 9 HOH 611 1323 1323 HOH HOH A . O 9 HOH 612 1324 1324 HOH HOH A . O 9 HOH 613 1325 1325 HOH HOH A . O 9 HOH 614 1326 1326 HOH HOH A . O 9 HOH 615 1327 1327 HOH HOH A . O 9 HOH 616 1328 1328 HOH HOH A . O 9 HOH 617 1329 1329 HOH HOH A . O 9 HOH 618 1330 1330 HOH HOH A . O 9 HOH 619 1331 1331 HOH HOH A . O 9 HOH 620 1332 1332 HOH HOH A . O 9 HOH 621 1333 1333 HOH HOH A . O 9 HOH 622 1334 1334 HOH HOH A . O 9 HOH 623 1335 1335 HOH HOH A . O 9 HOH 624 1336 1336 HOH HOH A . O 9 HOH 625 1337 1337 HOH HOH A . O 9 HOH 626 1338 1338 HOH HOH A . O 9 HOH 627 1339 1339 HOH HOH A . O 9 HOH 628 1340 1340 HOH HOH A . O 9 HOH 629 1341 1341 HOH HOH A . O 9 HOH 630 1342 1342 HOH HOH A . O 9 HOH 631 1343 1343 HOH HOH A . O 9 HOH 632 1344 1344 HOH HOH A . O 9 HOH 633 1345 1345 HOH HOH A . O 9 HOH 634 1346 1346 HOH HOH A . O 9 HOH 635 1347 1347 HOH HOH A . O 9 HOH 636 1348 1348 HOH HOH A . O 9 HOH 637 1349 1349 HOH HOH A . O 9 HOH 638 1350 1350 HOH HOH A . O 9 HOH 639 1351 1351 HOH HOH A . O 9 HOH 640 1352 1352 HOH HOH A . O 9 HOH 641 1353 1353 HOH HOH A . O 9 HOH 642 1354 1354 HOH HOH A . O 9 HOH 643 1355 1355 HOH HOH A . O 9 HOH 644 1356 1356 HOH HOH A . O 9 HOH 645 1357 1357 HOH HOH A . O 9 HOH 646 1358 1358 HOH HOH A . O 9 HOH 647 1359 1359 HOH HOH A . O 9 HOH 648 1360 1360 HOH HOH A . O 9 HOH 649 1361 1361 HOH HOH A . O 9 HOH 650 1362 1362 HOH HOH A . O 9 HOH 651 1363 1363 HOH HOH A . O 9 HOH 652 1364 1364 HOH HOH A . O 9 HOH 653 1365 1365 HOH HOH A . O 9 HOH 654 1366 1366 HOH HOH A . O 9 HOH 655 1367 1367 HOH HOH A . O 9 HOH 656 1368 1368 HOH HOH A . O 9 HOH 657 1369 1369 HOH HOH A . O 9 HOH 658 1370 1370 HOH HOH A . O 9 HOH 659 1371 1371 HOH HOH A . O 9 HOH 660 1372 1372 HOH HOH A . O 9 HOH 661 1373 1373 HOH HOH A . O 9 HOH 662 1374 1374 HOH HOH A . O 9 HOH 663 1375 1375 HOH HOH A . O 9 HOH 664 1376 1376 HOH HOH A . O 9 HOH 665 1377 1377 HOH HOH A . O 9 HOH 666 1378 1378 HOH HOH A . O 9 HOH 667 1379 1379 HOH HOH A . O 9 HOH 668 1380 1380 HOH HOH A . O 9 HOH 669 1381 1381 HOH HOH A . O 9 HOH 670 1382 1382 HOH HOH A . O 9 HOH 671 1383 1383 HOH HOH A . O 9 HOH 672 1384 1384 HOH HOH A . O 9 HOH 673 1385 1385 HOH HOH A . O 9 HOH 674 1386 1386 HOH HOH A . O 9 HOH 675 1387 1387 HOH HOH A . O 9 HOH 676 1388 1388 HOH HOH A . O 9 HOH 677 1389 1389 HOH HOH A . O 9 HOH 678 1390 1390 HOH HOH A . O 9 HOH 679 1391 1391 HOH HOH A . O 9 HOH 680 1392 1392 HOH HOH A . O 9 HOH 681 1393 1393 HOH HOH A . O 9 HOH 682 1394 1394 HOH HOH A . O 9 HOH 683 1395 1395 HOH HOH A . O 9 HOH 684 1396 1396 HOH HOH A . O 9 HOH 685 1397 1397 HOH HOH A . O 9 HOH 686 1398 1398 HOH HOH A . O 9 HOH 687 1399 1399 HOH HOH A . O 9 HOH 688 1400 1400 HOH HOH A . O 9 HOH 689 1401 1401 HOH HOH A . O 9 HOH 690 1402 1402 HOH HOH A . O 9 HOH 691 1403 1403 HOH HOH A . O 9 HOH 692 1404 1404 HOH HOH A . O 9 HOH 693 1405 1405 HOH HOH A . O 9 HOH 694 1406 1406 HOH HOH A . O 9 HOH 695 1407 1407 HOH HOH A . O 9 HOH 696 1408 1408 HOH HOH A . O 9 HOH 697 1409 1409 HOH HOH A . O 9 HOH 698 1410 1410 HOH HOH A . O 9 HOH 699 1411 1411 HOH HOH A . O 9 HOH 700 1412 1412 HOH HOH A . O 9 HOH 701 1413 1413 HOH HOH A . O 9 HOH 702 1414 1414 HOH HOH A . O 9 HOH 703 1415 1415 HOH HOH A . O 9 HOH 704 1416 1416 HOH HOH A . O 9 HOH 705 1417 1417 HOH HOH A . O 9 HOH 706 1418 1418 HOH HOH A . O 9 HOH 707 1419 1419 HOH HOH A . O 9 HOH 708 1420 1420 HOH HOH A . O 9 HOH 709 1421 1421 HOH HOH A . O 9 HOH 710 1422 1422 HOH HOH A . O 9 HOH 711 1423 1423 HOH HOH A . O 9 HOH 712 1424 1424 HOH HOH A . O 9 HOH 713 1425 1425 HOH HOH A . O 9 HOH 714 1426 1426 HOH HOH A . O 9 HOH 715 1427 1427 HOH HOH A . O 9 HOH 716 1428 1428 HOH HOH A . O 9 HOH 717 1429 1429 HOH HOH A . O 9 HOH 718 1430 1430 HOH HOH A . O 9 HOH 719 1431 1431 HOH HOH A . O 9 HOH 720 1432 1432 HOH HOH A . O 9 HOH 721 1433 1433 HOH HOH A . O 9 HOH 722 1434 1434 HOH HOH A . O 9 HOH 723 1435 1435 HOH HOH A . O 9 HOH 724 1436 1436 HOH HOH A . O 9 HOH 725 1437 1437 HOH HOH A . O 9 HOH 726 1438 1438 HOH HOH A . O 9 HOH 727 1439 1439 HOH HOH A . # 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 78 A ASN 111 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 152 A ASN 185 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 416 A ASN 449 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 595 A ASN 628 ? 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 # 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)' 9470 ? 1 MORE -153 ? 1 'SSA (A^2)' 48760 ? # 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_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 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 A HOH 7 ? O HOH . 2 1 A HOH 1360 ? O HOH . # 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 ? A THR 226 ? A THR 259 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 OG1 ? A THR 226 ? A THR 259 ? 1_555 71.3 ? 2 O ? A THR 226 ? A THR 259 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 O ? A TYR 229 ? A TYR 262 ? 1_555 73.1 ? 3 OG1 ? A THR 226 ? A THR 259 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 O ? A TYR 229 ? A TYR 262 ? 1_555 91.2 ? 4 O ? A THR 226 ? A THR 259 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 OE1 ? A GLU 390 ? A GLU 423 ? 1_555 151.1 ? 5 OG1 ? A THR 226 ? A THR 259 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 OE1 ? A GLU 390 ? A GLU 423 ? 1_555 91.2 ? 6 O ? A TYR 229 ? A TYR 262 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 OE1 ? A GLU 390 ? A GLU 423 ? 1_555 84.8 ? 7 O ? A THR 226 ? A THR 259 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 OE2 ? A GLU 390 ? A GLU 423 ? 1_555 150.3 ? 8 OG1 ? A THR 226 ? A THR 259 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 OE2 ? A GLU 390 ? A GLU 423 ? 1_555 100.5 ? 9 O ? A TYR 229 ? A TYR 262 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 OE2 ? A GLU 390 ? A GLU 423 ? 1_555 136.4 ? 10 OE1 ? A GLU 390 ? A GLU 423 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 OE2 ? A GLU 390 ? A GLU 423 ? 1_555 53.4 ? 11 O ? A THR 226 ? A THR 259 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 OE2 ? A GLU 393 ? A GLU 426 ? 1_555 103.0 ? 12 OG1 ? A THR 226 ? A THR 259 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 OE2 ? A GLU 393 ? A GLU 426 ? 1_555 170.2 ? 13 O ? A TYR 229 ? A TYR 262 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 OE2 ? A GLU 393 ? A GLU 426 ? 1_555 79.4 ? 14 OE1 ? A GLU 390 ? A GLU 423 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 OE2 ? A GLU 393 ? A GLU 426 ? 1_555 90.8 ? 15 OE2 ? A GLU 390 ? A GLU 423 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 OE2 ? A GLU 393 ? A GLU 426 ? 1_555 88.3 ? 16 O ? A THR 226 ? A THR 259 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 O ? O HOH . ? A HOH 816 ? 1_555 74.0 ? 17 OG1 ? A THR 226 ? A THR 259 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 O ? O HOH . ? A HOH 816 ? 1_555 88.8 ? 18 O ? A TYR 229 ? A TYR 262 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 O ? O HOH . ? A HOH 816 ? 1_555 145.2 ? 19 OE1 ? A GLU 390 ? A GLU 423 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 O ? O HOH . ? A HOH 816 ? 1_555 129.9 ? 20 OE2 ? A GLU 390 ? A GLU 423 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 O ? O HOH . ? A HOH 816 ? 1_555 77.4 ? 21 OE2 ? A GLU 393 ? A GLU 426 ? 1_555 CA ? K CA . ? A CA 1755 ? 1_555 O ? O HOH . ? A HOH 816 ? 1_555 97.3 ? 22 NE2 ? A HIS 334 ? A HIS 367 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 OD1 ? A ASP 344 ? A ASP 377 ? 1_555 97.9 ? 23 NE2 ? A HIS 334 ? A HIS 367 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 OD1 ? A ASP 410 ? A ASP 443 ? 1_555 96.8 ? 24 OD1 ? A ASP 344 ? A ASP 377 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 OD1 ? A ASP 410 ? A ASP 443 ? 1_555 99.2 ? 25 NE2 ? A HIS 334 ? A HIS 367 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 OD2 ? A ASP 410 ? A ASP 443 ? 1_555 89.2 ? 26 OD1 ? A ASP 344 ? A ASP 377 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 OD2 ? A ASP 410 ? A ASP 443 ? 1_555 159.7 ? 27 OD1 ? A ASP 410 ? A ASP 443 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 OD2 ? A ASP 410 ? A ASP 443 ? 1_555 61.0 ? 28 NE2 ? A HIS 334 ? A HIS 367 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 805 ? 1_555 149.0 ? 29 OD1 ? A ASP 344 ? A ASP 377 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 805 ? 1_555 94.8 ? 30 OD1 ? A ASP 410 ? A ASP 443 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 805 ? 1_555 109.0 ? 31 OD2 ? A ASP 410 ? A ASP 443 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 805 ? 1_555 88.6 ? 32 NE2 ? A HIS 334 ? A HIS 367 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 82.7 ? 33 OD1 ? A ASP 344 ? A ASP 377 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 85.1 ? 34 OD1 ? A ASP 410 ? A ASP 443 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 175.7 ? 35 OD2 ? A ASP 410 ? A ASP 443 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 114.7 ? 36 O ? O HOH . ? A HOH 805 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 70.3 ? 37 NE2 ? A HIS 334 ? A HIS 367 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O3 A N MPO . ? A MPO 741 ? 1_555 131.2 ? 38 OD1 ? A ASP 344 ? A ASP 377 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O3 A N MPO . ? A MPO 741 ? 1_555 108.1 ? 39 OD1 ? A ASP 410 ? A ASP 443 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O3 A N MPO . ? A MPO 741 ? 1_555 118.0 ? 40 OD2 ? A ASP 410 ? A ASP 443 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O3 A N MPO . ? A MPO 741 ? 1_555 80.5 ? 41 O ? O HOH . ? A HOH 805 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O3 A N MPO . ? A MPO 741 ? 1_555 18.7 ? 42 O ? O HOH . ? A HOH 801 ? 1_555 ZN A I ZN . ? A ZN 1752 ? 1_555 O3 A N MPO . ? A MPO 741 ? 1_555 60.0 ? 43 NE2 ? A HIS 334 ? A HIS 367 ? 1_555 ZN B I ZN . ? A ZN 1752 ? 1_555 OD1 ? A ASP 344 ? A ASP 377 ? 1_555 106.1 ? 44 NE2 ? A HIS 334 ? A HIS 367 ? 1_555 ZN B I ZN . ? A ZN 1752 ? 1_555 OD1 ? A ASP 410 ? A ASP 443 ? 1_555 93.1 ? 45 OD1 ? A ASP 344 ? A ASP 377 ? 1_555 ZN B I ZN . ? A ZN 1752 ? 1_555 OD1 ? A ASP 410 ? A ASP 443 ? 1_555 93.9 ? 46 NE2 ? A HIS 334 ? A HIS 367 ? 1_555 ZN B I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 805 ? 1_555 155.7 ? 47 OD1 ? A ASP 344 ? A ASP 377 ? 1_555 ZN B I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 805 ? 1_555 95.4 ? 48 OD1 ? A ASP 410 ? A ASP 443 ? 1_555 ZN B I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 805 ? 1_555 96.8 ? 49 NE2 ? A HIS 334 ? A HIS 367 ? 1_555 ZN B I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 92.5 ? 50 OD1 ? A ASP 344 ? A ASP 377 ? 1_555 ZN B I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 94.5 ? 51 OD1 ? A ASP 410 ? A ASP 443 ? 1_555 ZN B I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 168.3 ? 52 O ? O HOH . ? A HOH 805 ? 1_555 ZN B I ZN . ? A ZN 1752 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 74.2 ? 53 OD2 ? A ASP 344 ? A ASP 377 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 OE2 ? A GLU 382 ? A GLU 415 ? 1_555 92.6 ? 54 OD2 ? A ASP 344 ? A ASP 377 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 NE2 ? A HIS 510 ? A HIS 543 ? 1_555 91.0 ? 55 OE2 ? A GLU 382 ? A GLU 415 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 NE2 ? A HIS 510 ? A HIS 543 ? 1_555 98.1 ? 56 OD2 ? A ASP 344 ? A ASP 377 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 802 ? 1_555 111.7 ? 57 OE2 ? A GLU 382 ? A GLU 415 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 802 ? 1_555 153.9 ? 58 NE2 ? A HIS 510 ? A HIS 543 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 802 ? 1_555 91.3 ? 59 OD2 ? A ASP 344 ? A ASP 377 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 96.0 ? 60 OE2 ? A GLU 382 ? A GLU 415 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 81.6 ? 61 NE2 ? A HIS 510 ? A HIS 543 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 173.0 ? 62 O ? O HOH . ? A HOH 802 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 86.2 ? 63 OD2 ? A ASP 344 ? A ASP 377 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 S1 A N MPO . ? A MPO 741 ? 1_555 98.6 ? 64 OE2 ? A GLU 382 ? A GLU 415 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 S1 A N MPO . ? A MPO 741 ? 1_555 124.5 ? 65 NE2 ? A HIS 510 ? A HIS 543 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 S1 A N MPO . ? A MPO 741 ? 1_555 135.5 ? 66 O ? O HOH . ? A HOH 802 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 S1 A N MPO . ? A MPO 741 ? 1_555 44.8 ? 67 O ? O HOH . ? A HOH 801 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 S1 A N MPO . ? A MPO 741 ? 1_555 43.4 ? 68 OD2 ? A ASP 344 ? A ASP 377 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 O1 A N MPO . ? A MPO 741 ? 1_555 113.3 ? 69 OE2 ? A GLU 382 ? A GLU 415 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 O1 A N MPO . ? A MPO 741 ? 1_555 95.3 ? 70 NE2 ? A HIS 510 ? A HIS 543 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 O1 A N MPO . ? A MPO 741 ? 1_555 151.6 ? 71 O ? O HOH . ? A HOH 802 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 O1 A N MPO . ? A MPO 741 ? 1_555 66.8 ? 72 O ? O HOH . ? A HOH 801 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 O1 A N MPO . ? A MPO 741 ? 1_555 22.6 ? 73 S1 A N MPO . ? A MPO 741 ? 1_555 ZN A H ZN . ? A ZN 1751 ? 1_555 O1 A N MPO . ? A MPO 741 ? 1_555 31.0 ? 74 OD2 ? A ASP 344 ? A ASP 377 ? 1_555 ZN B H ZN . ? A ZN 1751 ? 1_555 OE2 ? A GLU 382 ? A GLU 415 ? 1_555 108.5 ? 75 OD2 ? A ASP 344 ? A ASP 377 ? 1_555 ZN B H ZN . ? A ZN 1751 ? 1_555 NE2 ? A HIS 510 ? A HIS 543 ? 1_555 97.0 ? 76 OE2 ? A GLU 382 ? A GLU 415 ? 1_555 ZN B H ZN . ? A ZN 1751 ? 1_555 NE2 ? A HIS 510 ? A HIS 543 ? 1_555 114.0 ? 77 OD2 ? A ASP 344 ? A ASP 377 ? 1_555 ZN B H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 802 ? 1_555 99.6 ? 78 OE2 ? A GLU 382 ? A GLU 415 ? 1_555 ZN B H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 802 ? 1_555 145.0 ? 79 NE2 ? A HIS 510 ? A HIS 543 ? 1_555 ZN B H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 802 ? 1_555 81.8 ? 80 OD2 ? A ASP 344 ? A ASP 377 ? 1_555 ZN B H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 93.6 ? 81 OE2 ? A GLU 382 ? A GLU 415 ? 1_555 ZN B H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 85.0 ? 82 NE2 ? A HIS 510 ? A HIS 543 ? 1_555 ZN B H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 153.6 ? 83 O ? O HOH . ? A HOH 802 ? 1_555 ZN B H ZN . ? A ZN 1751 ? 1_555 O ? O HOH . ? A HOH 801 ? 1_555 72.6 ? # 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 2009-08-25 2 'Structure model' 1 1 2011-07-13 # _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 ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' Advisory 2 2 'Structure model' 'Version format compliance' # _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 19.3364 _pdbx_refine_tls.origin_y 46.1128 _pdbx_refine_tls.origin_z 13.4340 _pdbx_refine_tls.T[1][1] -0.0459 _pdbx_refine_tls.T[2][2] -0.0169 _pdbx_refine_tls.T[3][3] -0.0262 _pdbx_refine_tls.T[1][2] 0.0016 _pdbx_refine_tls.T[1][3] 0.0003 _pdbx_refine_tls.T[2][3] -0.0249 _pdbx_refine_tls.L[1][1] 0.2155 _pdbx_refine_tls.L[2][2] 0.3720 _pdbx_refine_tls.L[3][3] 0.3724 _pdbx_refine_tls.L[1][2] -0.1225 _pdbx_refine_tls.L[1][3] 0.0408 _pdbx_refine_tls.L[2][3] -0.1958 _pdbx_refine_tls.S[1][1] -0.0158 _pdbx_refine_tls.S[1][2] -0.0424 _pdbx_refine_tls.S[1][3] -0.0015 _pdbx_refine_tls.S[2][1] 0.0537 _pdbx_refine_tls.S[2][2] 0.0251 _pdbx_refine_tls.S[2][3] -0.0647 _pdbx_refine_tls.S[3][1] -0.0078 _pdbx_refine_tls.S[3][2] 0.0905 _pdbx_refine_tls.S[3][3] -0.0092 _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' # _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_auth_asym_id A _pdbx_refine_tls_group.beg_auth_seq_id 46 _pdbx_refine_tls_group.end_auth_asym_id A _pdbx_refine_tls_group.end_auth_seq_id 1760 _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 ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.4.0057 ? 1 MAR345dtb 'data collection' . ? 2 HKL-2000 'data reduction' . ? 3 HKL-2000 'data scaling' . ? 4 PHASER phasing . ? 5 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 OG A SER 507 ? ? O A LYS 689 ? ? 1.41 2 1 OH A TYR 169 ? B OD1 A ASP 223 ? ? 1.88 3 1 OE1 A GLU 592 ? B O A HOH 1050 ? ? 1.96 4 1 OD1 A ASP 635 ? B O A HOH 980 ? ? 2.14 5 1 O A HOH 934 ? ? O A HOH 1304 ? ? 2.17 # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 O A HOH 17 ? ? 1_555 O A HOH 1145 ? ? 4_546 1.60 2 1 O A HOH 767 ? ? 1_555 O A HOH 1045 ? ? 2_555 2.09 3 1 O A HOH 1045 ? ? 1_555 O A HOH 1168 ? ? 2_555 2.16 # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 CG _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_1 553 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 CD _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_2 553 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.422 _pdbx_validate_rmsd_bond.bond_target_value 1.515 _pdbx_validate_rmsd_bond.bond_deviation -0.093 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.015 _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 270 ? ? CZ A ARG 270 ? ? NH1 A ARG 270 ? ? 124.41 120.30 4.11 0.50 N 2 1 NE A ARG 663 ? ? CZ A ARG 663 ? ? NH1 A ARG 663 ? ? 124.37 120.30 4.07 0.50 N 3 1 NE A ARG 663 ? ? CZ A ARG 663 ? ? NH2 A ARG 663 ? ? 116.92 120.30 -3.38 0.50 N 4 1 NE A ARG 678 ? ? CZ A ARG 678 ? ? NH1 A ARG 678 ? ? 125.04 120.30 4.74 0.50 N 5 1 C A ALA 683 ? A N A PRO 684 ? A CA A PRO 684 ? A 129.38 119.30 10.08 1.50 Y 6 1 N A PRO 684 ? A CA A PRO 684 ? A C A PRO 684 ? A 133.34 112.10 21.24 2.60 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 ALA A 98 ? ? -161.83 103.30 2 1 PHE A 154 ? ? 80.94 5.50 3 1 ASN A 168 ? ? 58.26 -108.83 4 1 ASN A 168 ? ? 58.26 -139.13 5 1 LYS A 197 ? ? 69.95 -39.17 6 1 ASN A 250 ? ? -117.09 78.19 7 1 TYR A 337 ? ? -141.51 39.86 8 1 VAL A 372 ? ? -129.14 -109.30 9 1 SER A 442 ? ? -144.82 53.44 10 1 ASP A 443 ? ? -84.87 -158.93 11 1 ASP A 491 ? ? -150.07 66.45 12 1 SER A 538 ? ? 45.28 -120.60 13 1 ASP A 557 ? ? -160.31 68.30 14 1 PRO A 684 ? A -45.94 168.12 15 1 SER A 685 ? ? -25.02 120.72 16 1 ASN A 688 ? ? -170.55 95.60 # _pdbx_validate_planes.id 1 _pdbx_validate_planes.PDB_model_num 1 _pdbx_validate_planes.auth_comp_id ARG _pdbx_validate_planes.auth_asym_id A _pdbx_validate_planes.auth_seq_id 404 _pdbx_validate_planes.PDB_ins_code ? _pdbx_validate_planes.label_alt_id ? _pdbx_validate_planes.rmsd 0.096 _pdbx_validate_planes.type 'SIDE CHAIN' # loop_ _pdbx_validate_chiral.id _pdbx_validate_chiral.PDB_model_num _pdbx_validate_chiral.auth_atom_id _pdbx_validate_chiral.label_alt_id _pdbx_validate_chiral.auth_asym_id _pdbx_validate_chiral.auth_comp_id _pdbx_validate_chiral.auth_seq_id _pdbx_validate_chiral.PDB_ins_code _pdbx_validate_chiral.details _pdbx_validate_chiral.omega 1 1 C1 ? A NAG 1766 ? 'WRONG HAND' . 2 1 C1 ? A NAG 1766 ? PLANAR . # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A ARG 34 ? A ARG 1 2 1 Y 1 A SER 35 ? A SER 2 3 1 Y 1 A GLU 36 ? A GLU 3 4 1 Y 1 A THR 37 ? A THR 4 5 1 Y 1 A THR 38 ? A THR 5 6 1 Y 1 A THR 39 ? A THR 6 7 1 Y 1 A SER 40 ? A SER 7 8 1 Y 1 A VAL 41 ? A VAL 8 9 1 Y 1 A ARG 42 ? A ARG 9 10 1 Y 1 A TYR 43 ? A TYR 10 11 1 Y 1 A HIS 44 ? A HIS 11 12 1 Y 1 A GLN 45 ? A GLN 12 13 1 Y 1 A TYR 133 ? A TYR 100 14 1 Y 1 A LEU 134 ? A LEU 101 15 1 Y 1 A GLU 135 ? A GLU 102 16 1 Y 1 A PRO 136 ? A PRO 103 17 1 Y 1 A ASP 327 ? A ASP 294 18 1 Y 1 A LEU 740 ? A LEU 707 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'GLUTAMIC ACID' GLU 3 N-ACETYL-D-GLUCOSAMINE NAG 4 'ZINC ION' ZN 5 'CHLORIDE ION' CL 6 'CALCIUM ION' CA 7 GLYCEROL GOL 8 '3[N-MORPHOLINO]PROPANE SULFONIC ACID' MPO 9 water HOH #