data_1R1H # _entry.id 1R1H # _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 1R1H RCSB RCSB020322 WWPDB D_1000020322 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1DMT . unspecified PDB 1R1I . unspecified PDB 1R1J . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1R1H _pdbx_database_status.recvd_initial_deposition_date 2003-09-24 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.SG_entry . _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Oefner, C.' 1 'Roques, B.P.' 2 'Fournie-Zaluski, M.C.' 3 'Dale, G.E.' 4 # _citation.id primary _citation.title 'Structural analysis of neprilysin with various specific and potent inhibitors.' _citation.journal_abbrev 'Acta Crystallogr.,Sect.D' _citation.journal_volume 60 _citation.page_first 392 _citation.page_last 396 _citation.year 2004 _citation.journal_id_ASTM ABCRE6 _citation.country DK _citation.journal_id_ISSN 0907-4449 _citation.journal_id_CSD 0766 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 14747736 _citation.pdbx_database_id_DOI 10.1107/S0907444903027410 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Oefner, C.' 1 primary 'Roques, B.P.' 2 primary 'Fournie-Zaluski, M.C.' 3 primary 'Dale, G.E.' 4 # _cell.entry_id 1R1H _cell.length_a 107.791 _cell.length_b 107.791 _cell.length_c 113.090 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 6 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1R1H _symmetry.space_group_name_H-M 'P 32 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 154 _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 Neprilysin 79525.508 1 3.4.24.11 ? 'EXTRACELLULAR DOMAIN, (residues 54-749)' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 3 non-polymer syn 'ZINC ION' 65.409 1 ? ? ? ? 4 non-polymer syn "N-[3-[(1-AMINOETHYL)(HYDROXY)PHOSPHORYL]-2-(1,1'-BIPHENYL-4-YLMETHYL)PROPANOYL]ALANINE" 418.423 1 ? ? ? ? 5 water nat water 18.015 295 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Neutral endopeptidase, NEP, Enkephalinase, Common acute lymphocytic leukemia antigen, CALLA, Neutral endopeptidase 24.11, CD10' # _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 ;GICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQ KAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVN HVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRN DPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWR FIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQT LDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDE WISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSASN FKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVW CGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW ; _entity_poly.pdbx_seq_one_letter_code_can ;GICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQ KAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVN HVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRN DPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWR FIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQT LDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDE WISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSASN FKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVW CGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW ; _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 GLY n 1 2 ILE n 1 3 CYS n 1 4 LYS n 1 5 SER n 1 6 SER n 1 7 ASP n 1 8 CYS n 1 9 ILE n 1 10 LYS n 1 11 SER n 1 12 ALA n 1 13 ALA n 1 14 ARG n 1 15 LEU n 1 16 ILE n 1 17 GLN n 1 18 ASN n 1 19 MET n 1 20 ASP n 1 21 ALA n 1 22 THR n 1 23 THR n 1 24 GLU n 1 25 PRO n 1 26 CYS n 1 27 THR n 1 28 ASP n 1 29 PHE n 1 30 PHE n 1 31 LYS n 1 32 TYR n 1 33 ALA n 1 34 CYS n 1 35 GLY n 1 36 GLY n 1 37 TRP n 1 38 LEU n 1 39 LYS n 1 40 ARG n 1 41 ASN n 1 42 VAL n 1 43 ILE n 1 44 PRO n 1 45 GLU n 1 46 THR n 1 47 SER n 1 48 SER n 1 49 ARG n 1 50 TYR n 1 51 GLY n 1 52 ASN n 1 53 PHE n 1 54 ASP n 1 55 ILE n 1 56 LEU n 1 57 ARG n 1 58 ASP n 1 59 GLU n 1 60 LEU n 1 61 GLU n 1 62 VAL n 1 63 VAL n 1 64 LEU n 1 65 LYS n 1 66 ASP n 1 67 VAL n 1 68 LEU n 1 69 GLN n 1 70 GLU n 1 71 PRO n 1 72 LYS n 1 73 THR n 1 74 GLU n 1 75 ASP n 1 76 ILE n 1 77 VAL n 1 78 ALA n 1 79 VAL n 1 80 GLN n 1 81 LYS n 1 82 ALA n 1 83 LYS n 1 84 ALA n 1 85 LEU n 1 86 TYR n 1 87 ARG n 1 88 SER n 1 89 CYS n 1 90 ILE n 1 91 ASN n 1 92 GLU n 1 93 SER n 1 94 ALA n 1 95 ILE n 1 96 ASP n 1 97 SER n 1 98 ARG n 1 99 GLY n 1 100 GLY n 1 101 GLU n 1 102 PRO n 1 103 LEU n 1 104 LEU n 1 105 LYS n 1 106 LEU n 1 107 LEU n 1 108 PRO n 1 109 ASP n 1 110 ILE n 1 111 TYR n 1 112 GLY n 1 113 TRP n 1 114 PRO n 1 115 VAL n 1 116 ALA n 1 117 THR n 1 118 GLU n 1 119 ASN n 1 120 TRP n 1 121 GLU n 1 122 GLN n 1 123 LYS n 1 124 TYR n 1 125 GLY n 1 126 ALA n 1 127 SER n 1 128 TRP n 1 129 THR n 1 130 ALA n 1 131 GLU n 1 132 LYS n 1 133 ALA n 1 134 ILE n 1 135 ALA n 1 136 GLN n 1 137 LEU n 1 138 ASN n 1 139 SER n 1 140 LYS n 1 141 TYR n 1 142 GLY n 1 143 LYS n 1 144 LYS n 1 145 VAL n 1 146 LEU n 1 147 ILE n 1 148 ASN n 1 149 LEU n 1 150 PHE n 1 151 VAL n 1 152 GLY n 1 153 THR n 1 154 ASP n 1 155 ASP n 1 156 LYS n 1 157 ASN n 1 158 SER n 1 159 VAL n 1 160 ASN n 1 161 HIS n 1 162 VAL n 1 163 ILE n 1 164 HIS n 1 165 ILE n 1 166 ASP n 1 167 GLN n 1 168 PRO n 1 169 ARG n 1 170 LEU n 1 171 GLY n 1 172 LEU n 1 173 PRO n 1 174 SER n 1 175 ARG n 1 176 ASP n 1 177 TYR n 1 178 TYR n 1 179 GLU n 1 180 CYS n 1 181 THR n 1 182 GLY n 1 183 ILE n 1 184 TYR n 1 185 LYS n 1 186 GLU n 1 187 ALA n 1 188 CYS n 1 189 THR n 1 190 ALA n 1 191 TYR n 1 192 VAL n 1 193 ASP n 1 194 PHE n 1 195 MET n 1 196 ILE n 1 197 SER n 1 198 VAL n 1 199 ALA n 1 200 ARG n 1 201 LEU n 1 202 ILE n 1 203 ARG n 1 204 GLN n 1 205 GLU n 1 206 GLU n 1 207 ARG n 1 208 LEU n 1 209 PRO n 1 210 ILE n 1 211 ASP n 1 212 GLU n 1 213 ASN n 1 214 GLN n 1 215 LEU n 1 216 ALA n 1 217 LEU n 1 218 GLU n 1 219 MET n 1 220 ASN n 1 221 LYS n 1 222 VAL n 1 223 MET n 1 224 GLU n 1 225 LEU n 1 226 GLU n 1 227 LYS n 1 228 GLU n 1 229 ILE n 1 230 ALA n 1 231 ASN n 1 232 ALA n 1 233 THR n 1 234 ALA n 1 235 LYS n 1 236 PRO n 1 237 GLU n 1 238 ASP n 1 239 ARG n 1 240 ASN n 1 241 ASP n 1 242 PRO n 1 243 MET n 1 244 LEU n 1 245 LEU n 1 246 TYR n 1 247 ASN n 1 248 LYS n 1 249 MET n 1 250 THR n 1 251 LEU n 1 252 ALA n 1 253 GLN n 1 254 ILE n 1 255 GLN n 1 256 ASN n 1 257 ASN n 1 258 PHE n 1 259 SER n 1 260 LEU n 1 261 GLU n 1 262 ILE n 1 263 ASN n 1 264 GLY n 1 265 LYS n 1 266 PRO n 1 267 PHE n 1 268 SER n 1 269 TRP n 1 270 LEU n 1 271 ASN n 1 272 PHE n 1 273 THR n 1 274 ASN n 1 275 GLU n 1 276 ILE n 1 277 MET n 1 278 SER n 1 279 THR n 1 280 VAL n 1 281 ASN n 1 282 ILE n 1 283 SER n 1 284 ILE n 1 285 THR n 1 286 ASN n 1 287 GLU n 1 288 GLU n 1 289 ASP n 1 290 VAL n 1 291 VAL n 1 292 VAL n 1 293 TYR n 1 294 ALA n 1 295 PRO n 1 296 GLU n 1 297 TYR n 1 298 LEU n 1 299 THR n 1 300 LYS n 1 301 LEU n 1 302 LYS n 1 303 PRO n 1 304 ILE n 1 305 LEU n 1 306 THR n 1 307 LYS n 1 308 TYR n 1 309 SER n 1 310 ALA n 1 311 ARG n 1 312 ASP n 1 313 LEU n 1 314 GLN n 1 315 ASN n 1 316 LEU n 1 317 MET n 1 318 SER n 1 319 TRP n 1 320 ARG n 1 321 PHE n 1 322 ILE n 1 323 MET n 1 324 ASP n 1 325 LEU n 1 326 VAL n 1 327 SER n 1 328 SER n 1 329 LEU n 1 330 SER n 1 331 ARG n 1 332 THR n 1 333 TYR n 1 334 LYS n 1 335 GLU n 1 336 SER n 1 337 ARG n 1 338 ASN n 1 339 ALA n 1 340 PHE n 1 341 ARG n 1 342 LYS n 1 343 ALA n 1 344 LEU n 1 345 TYR n 1 346 GLY n 1 347 THR n 1 348 THR n 1 349 SER n 1 350 GLU n 1 351 THR n 1 352 ALA n 1 353 THR n 1 354 TRP n 1 355 ARG n 1 356 ARG n 1 357 CYS n 1 358 ALA n 1 359 ASN n 1 360 TYR n 1 361 VAL n 1 362 ASN n 1 363 GLY n 1 364 ASN n 1 365 MET n 1 366 GLU n 1 367 ASN n 1 368 ALA n 1 369 VAL n 1 370 GLY n 1 371 ARG n 1 372 LEU n 1 373 TYR n 1 374 VAL n 1 375 GLU n 1 376 ALA n 1 377 ALA n 1 378 PHE n 1 379 ALA n 1 380 GLY n 1 381 GLU n 1 382 SER n 1 383 LYS n 1 384 HIS n 1 385 VAL n 1 386 VAL n 1 387 GLU n 1 388 ASP n 1 389 LEU n 1 390 ILE n 1 391 ALA n 1 392 GLN n 1 393 ILE n 1 394 ARG n 1 395 GLU n 1 396 VAL n 1 397 PHE n 1 398 ILE n 1 399 GLN n 1 400 THR n 1 401 LEU n 1 402 ASP n 1 403 ASP n 1 404 LEU n 1 405 THR n 1 406 TRP n 1 407 MET n 1 408 ASP n 1 409 ALA n 1 410 GLU n 1 411 THR n 1 412 LYS n 1 413 LYS n 1 414 ARG n 1 415 ALA n 1 416 GLU n 1 417 GLU n 1 418 LYS n 1 419 ALA n 1 420 LEU n 1 421 ALA n 1 422 ILE n 1 423 LYS n 1 424 GLU n 1 425 ARG n 1 426 ILE n 1 427 GLY n 1 428 TYR n 1 429 PRO n 1 430 ASP n 1 431 ASP n 1 432 ILE n 1 433 VAL n 1 434 SER n 1 435 ASN n 1 436 ASP n 1 437 ASN n 1 438 LYS n 1 439 LEU n 1 440 ASN n 1 441 ASN n 1 442 GLU n 1 443 TYR n 1 444 LEU n 1 445 GLU n 1 446 LEU n 1 447 ASN n 1 448 TYR n 1 449 LYS n 1 450 GLU n 1 451 ASP n 1 452 GLU n 1 453 TYR n 1 454 PHE n 1 455 GLU n 1 456 ASN n 1 457 ILE n 1 458 ILE n 1 459 GLN n 1 460 ASN n 1 461 LEU n 1 462 LYS n 1 463 PHE n 1 464 SER n 1 465 GLN n 1 466 SER n 1 467 LYS n 1 468 GLN n 1 469 LEU n 1 470 LYS n 1 471 LYS n 1 472 LEU n 1 473 ARG n 1 474 GLU n 1 475 LYS n 1 476 VAL n 1 477 ASP n 1 478 LYS n 1 479 ASP n 1 480 GLU n 1 481 TRP n 1 482 ILE n 1 483 SER n 1 484 GLY n 1 485 ALA n 1 486 ALA n 1 487 VAL n 1 488 VAL n 1 489 ASN n 1 490 ALA n 1 491 PHE n 1 492 TYR n 1 493 SER n 1 494 SER n 1 495 GLY n 1 496 ARG n 1 497 ASN n 1 498 GLN n 1 499 ILE n 1 500 VAL n 1 501 PHE n 1 502 PRO n 1 503 ALA n 1 504 GLY n 1 505 ILE n 1 506 LEU n 1 507 GLN n 1 508 PRO n 1 509 PRO n 1 510 PHE n 1 511 PHE n 1 512 SER n 1 513 ALA n 1 514 GLN n 1 515 GLN n 1 516 SER n 1 517 ASN n 1 518 SER n 1 519 LEU n 1 520 ASN n 1 521 TYR n 1 522 GLY n 1 523 GLY n 1 524 ILE n 1 525 GLY n 1 526 MET n 1 527 VAL n 1 528 ILE n 1 529 GLY n 1 530 HIS n 1 531 GLU n 1 532 ILE n 1 533 THR n 1 534 HIS n 1 535 GLY n 1 536 PHE n 1 537 ASP n 1 538 ASP n 1 539 ASN n 1 540 GLY n 1 541 ARG n 1 542 ASN n 1 543 PHE n 1 544 ASN n 1 545 LYS n 1 546 ASP n 1 547 GLY n 1 548 ASP n 1 549 LEU n 1 550 VAL n 1 551 ASP n 1 552 TRP n 1 553 TRP n 1 554 THR n 1 555 GLN n 1 556 GLN n 1 557 SER n 1 558 ALA n 1 559 SER n 1 560 ASN n 1 561 PHE n 1 562 LYS n 1 563 GLU n 1 564 GLN n 1 565 SER n 1 566 GLN n 1 567 CYS n 1 568 MET n 1 569 VAL n 1 570 TYR n 1 571 GLN n 1 572 TYR n 1 573 GLY n 1 574 ASN n 1 575 PHE n 1 576 SER n 1 577 TRP n 1 578 ASP n 1 579 LEU n 1 580 ALA n 1 581 GLY n 1 582 GLY n 1 583 GLN n 1 584 HIS n 1 585 LEU n 1 586 ASN n 1 587 GLY n 1 588 ILE n 1 589 ASN n 1 590 THR n 1 591 LEU n 1 592 GLY n 1 593 GLU n 1 594 ASN n 1 595 ILE n 1 596 ALA n 1 597 ASP n 1 598 ASN n 1 599 GLY n 1 600 GLY n 1 601 LEU n 1 602 GLY n 1 603 GLN n 1 604 ALA n 1 605 TYR n 1 606 ARG n 1 607 ALA n 1 608 TYR n 1 609 GLN n 1 610 ASN n 1 611 TYR n 1 612 ILE n 1 613 LYS n 1 614 LYS n 1 615 ASN n 1 616 GLY n 1 617 GLU n 1 618 GLU n 1 619 LYS n 1 620 LEU n 1 621 LEU n 1 622 PRO n 1 623 GLY n 1 624 LEU n 1 625 ASP n 1 626 LEU n 1 627 ASN n 1 628 HIS n 1 629 LYS n 1 630 GLN n 1 631 LEU n 1 632 PHE n 1 633 PHE n 1 634 LEU n 1 635 ASN n 1 636 PHE n 1 637 ALA n 1 638 GLN n 1 639 VAL n 1 640 TRP n 1 641 CYS n 1 642 GLY n 1 643 THR n 1 644 TYR n 1 645 ARG n 1 646 PRO n 1 647 GLU n 1 648 TYR n 1 649 ALA n 1 650 VAL n 1 651 ASN n 1 652 SER n 1 653 ILE n 1 654 LYS n 1 655 THR n 1 656 ASP n 1 657 VAL n 1 658 HIS n 1 659 SER n 1 660 PRO n 1 661 GLY n 1 662 ASN n 1 663 PHE n 1 664 ARG n 1 665 ILE n 1 666 ILE n 1 667 GLY n 1 668 THR n 1 669 LEU n 1 670 GLN n 1 671 ASN n 1 672 SER n 1 673 ALA n 1 674 GLU n 1 675 PHE n 1 676 SER n 1 677 GLU n 1 678 ALA n 1 679 PHE n 1 680 HIS n 1 681 CYS n 1 682 ARG n 1 683 LYS n 1 684 ASN n 1 685 SER n 1 686 TYR n 1 687 MET n 1 688 ASN n 1 689 PRO n 1 690 GLU n 1 691 LYS n 1 692 LYS n 1 693 CYS n 1 694 ARG n 1 695 VAL n 1 696 TRP n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name human _entity_src_gen.gene_src_genus Homo _entity_src_gen.pdbx_gene_src_gene 'MME, EPN' _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 ;baker's yeast ; _entity_src_gen.pdbx_host_org_scientific_name 'Saccharomyces cerevisiae' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 4932 _entity_src_gen.host_org_genus Saccharomyces _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type 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 PPICZ-ALPHA _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code NEP_HUMAN _struct_ref.pdbx_db_accession P08473 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;GICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQ KAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVN HVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRN DPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWR FIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQT LDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDE WISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSASN FKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVW CGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW ; _struct_ref.pdbx_align_begin 54 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1R1H _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 696 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P08473 _struct_ref_seq.db_align_beg 54 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 749 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 54 _struct_ref_seq.pdbx_auth_seq_align_end 749 # 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 BIR non-polymer . "N-[3-[(1-AMINOETHYL)(HYDROXY)PHOSPHORYL]-2-(1,1'-BIPHENYL-4-YLMETHYL)PROPANOYL]ALANINE" ? 'C21 H27 N2 O5 P' 418.423 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 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 1R1H _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.38 _exptl_crystal.density_percent_sol 48.42 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 2001-08-09 _diffrn_detector.details OSMIC # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator OSMIC _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.54 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'ROTATING ANODE' _diffrn_source.type 'ENRAF-NONIUS FR591' _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.54 # _reflns.entry_id 1R1H _reflns.observed_criterion_sigma_F 0 _reflns.observed_criterion_sigma_I 0 _reflns.d_resolution_high 1.95 _reflns.d_resolution_low 20.0 _reflns.number_all 53437 _reflns.number_obs 53437 _reflns.percent_possible_obs 95.9 _reflns.pdbx_Rmerge_I_obs 0.062 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 26.2 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.95 _reflns_shell.d_res_low 2.07 _reflns_shell.percent_possible_all 93.4 _reflns_shell.Rmerge_I_obs 0.463 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.5 _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 1R1H _refine.ls_number_reflns_obs 50726 _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 1.95 _refine.ls_percent_reflns_obs 95.99 _refine.ls_R_factor_obs 0.21143 _refine.ls_R_factor_all 0.2114 _refine.ls_R_factor_R_work 0.20885 _refine.ls_R_factor_R_free 0.26024 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 2707 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.941 _refine.correlation_coeff_Fo_to_Fc_free 0.911 _refine.B_iso_mean 25.996 _refine.aniso_B[1][1] 0.19 _refine.aniso_B[2][2] 0.19 _refine.aniso_B[3][3] -0.28 _refine.aniso_B[1][2] 0.09 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.198 _refine.pdbx_overall_ESU_R_Free 0.179 _refine.overall_SU_ML 0.183 _refine.overall_SU_B 6.310 _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_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_phase_error ? _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 5595 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 72 _refine_hist.number_atoms_solvent 295 _refine_hist.number_atoms_total 5962 _refine_hist.d_res_high 1.95 _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 0.007 0.021 ? 5794 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 5063 'X-RAY DIFFRACTION' ? r_angle_refined_deg 0.856 1.956 ? 7845 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.569 3.000 ? 11822 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 8.000 3.000 ? 695 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 22.144 15.000 ? 1037 'X-RAY DIFFRACTION' ? r_chiral_restr 0.049 0.200 ? 843 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.003 0.020 ? 6441 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 1162 'X-RAY DIFFRACTION' ? r_nbd_refined 0.286 0.300 ? 1554 'X-RAY DIFFRACTION' ? r_nbd_other 0.254 0.300 ? 5293 'X-RAY DIFFRACTION' ? r_nbtor_other 0.775 0.500 ? 3 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.240 0.500 ? 363 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other 0.233 0.500 ? 4 'X-RAY DIFFRACTION' ? r_metal_ion_refined 0.072 0.500 ? 3 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.846 0.300 ? 43 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other 0.503 0.300 ? 43 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.688 0.500 ? 11 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 2.472 2.000 ? 3461 'X-RAY DIFFRACTION' ? r_mcangle_it 3.537 3.000 ? 5572 'X-RAY DIFFRACTION' ? r_scbond_it 2.693 2.000 ? 2333 'X-RAY DIFFRACTION' ? r_scangle_it 3.973 3.000 ? 2273 '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 10 _refine_ls_shell.d_res_high 1.950 _refine_ls_shell.d_res_low 2.054 _refine_ls_shell.number_reflns_R_work 7061 _refine_ls_shell.R_factor_R_work 0.251 _refine_ls_shell.percent_reflns_obs ? _refine_ls_shell.R_factor_R_free 0.319 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 385 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.R_factor_all ? # _struct.entry_id 1R1H _struct.title 'STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS' _struct.pdbx_descriptor 'Neprilysin (E.C.3.4.24.11)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1R1H _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'ENKEPHALINASE, glycoprotein, metalloprotease, hydrolase' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 2 ? E N N 3 ? F N N 4 ? G N N 5 ? # _struct_biol.id 1 _struct_biol.pdbx_parent_biol_id ? _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 5 ? MET A 19 ? SER A 58 MET A 72 1 ? 15 HELX_P HELX_P2 2 ASP A 28 ? ASN A 41 ? ASP A 81 ASN A 94 1 ? 14 HELX_P HELX_P3 3 ASN A 52 ? GLN A 69 ? ASN A 105 GLN A 122 1 ? 18 HELX_P HELX_P4 4 ILE A 76 ? ASN A 91 ? ILE A 129 ASN A 144 1 ? 16 HELX_P HELX_P5 5 ASN A 91 ? ARG A 98 ? ASN A 144 ARG A 151 1 ? 8 HELX_P HELX_P6 6 GLY A 100 ? LYS A 105 ? GLY A 153 LYS A 158 1 ? 6 HELX_P HELX_P7 7 LEU A 106 ? TYR A 111 ? LEU A 159 TYR A 164 5 ? 6 HELX_P HELX_P8 8 TRP A 113 ? THR A 117 ? TRP A 166 THR A 170 5 ? 5 HELX_P HELX_P9 9 ASN A 119 ? TYR A 124 ? ASN A 172 TYR A 177 1 ? 6 HELX_P HELX_P10 10 THR A 129 ? GLY A 142 ? THR A 182 GLY A 195 1 ? 14 HELX_P HELX_P11 11 SER A 174 ? CYS A 180 ? SER A 227 CYS A 233 5 ? 7 HELX_P HELX_P12 12 THR A 181 ? ILE A 183 ? THR A 234 ILE A 236 5 ? 3 HELX_P HELX_P13 13 TYR A 184 ? GLU A 206 ? TYR A 237 GLU A 259 1 ? 23 HELX_P HELX_P14 14 ASP A 211 ? THR A 233 ? ASP A 264 THR A 286 1 ? 23 HELX_P HELX_P15 15 LYS A 235 ? ARG A 239 ? LYS A 288 ARG A 292 5 ? 5 HELX_P HELX_P16 16 ASP A 241 ? TYR A 246 ? ASP A 294 TYR A 299 1 ? 6 HELX_P HELX_P17 17 LEU A 251 ? PHE A 258 ? LEU A 304 PHE A 311 1 ? 8 HELX_P HELX_P18 18 SER A 268 ? SER A 278 ? SER A 321 SER A 331 1 ? 11 HELX_P HELX_P19 19 THR A 279 ? ASN A 281 ? THR A 332 ASN A 334 5 ? 3 HELX_P HELX_P20 20 ALA A 294 ? THR A 306 ? ALA A 347 THR A 359 1 ? 13 HELX_P HELX_P21 21 SER A 309 ? VAL A 326 ? SER A 362 VAL A 379 1 ? 18 HELX_P HELX_P22 22 SER A 327 ? LEU A 329 ? SER A 380 LEU A 382 5 ? 3 HELX_P HELX_P23 23 SER A 330 ? SER A 336 ? SER A 383 SER A 389 1 ? 7 HELX_P HELX_P24 24 ARG A 337 ? GLY A 346 ? ARG A 390 GLY A 399 1 ? 10 HELX_P HELX_P25 25 ALA A 352 ? MET A 365 ? ALA A 405 MET A 418 1 ? 14 HELX_P HELX_P26 26 MET A 365 ? PHE A 378 ? MET A 418 PHE A 431 1 ? 14 HELX_P HELX_P27 27 GLU A 381 ? LEU A 401 ? GLU A 434 LEU A 454 1 ? 21 HELX_P HELX_P28 28 ASP A 402 ? LEU A 404 ? ASP A 455 LEU A 457 5 ? 3 HELX_P HELX_P29 29 ASP A 408 ? ALA A 421 ? ASP A 461 ALA A 474 1 ? 14 HELX_P HELX_P30 30 ASP A 430 ? ASN A 435 ? ASP A 483 ASN A 488 1 ? 6 HELX_P HELX_P31 31 ASN A 435 ? TYR A 443 ? ASN A 488 TYR A 496 1 ? 9 HELX_P HELX_P32 32 GLU A 452 ? LYS A 470 ? GLU A 505 LYS A 523 1 ? 19 HELX_P HELX_P33 33 GLY A 504 ? LEU A 506 ? GLY A 557 LEU A 559 5 ? 3 HELX_P HELX_P34 34 SER A 516 ? GLY A 523 ? SER A 569 GLY A 576 1 ? 8 HELX_P HELX_P35 35 GLY A 523 ? HIS A 534 ? GLY A 576 HIS A 587 1 ? 12 HELX_P HELX_P36 36 GLY A 535 ? ASP A 537 ? GLY A 588 ASP A 590 5 ? 3 HELX_P HELX_P37 37 THR A 554 ? ASN A 574 ? THR A 607 ASN A 627 1 ? 21 HELX_P HELX_P38 38 TRP A 577 ? GLY A 581 ? TRP A 630 GLY A 634 5 ? 5 HELX_P HELX_P39 39 THR A 590 ? GLY A 616 ? THR A 643 GLY A 669 1 ? 27 HELX_P HELX_P40 40 ASN A 627 ? VAL A 639 ? ASN A 680 VAL A 692 1 ? 13 HELX_P HELX_P41 41 ARG A 645 ? ASP A 656 ? ARG A 698 ASP A 709 1 ? 12 HELX_P HELX_P42 42 PRO A 660 ? ASN A 671 ? PRO A 713 ASN A 724 1 ? 12 HELX_P HELX_P43 43 SER A 672 ? PHE A 679 ? SER A 725 PHE A 732 1 ? 8 # _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 disulf1 disulf ? ? A CYS 3 SG ? ? ? 1_555 A CYS 8 SG ? ? A CYS 56 A CYS 61 1_555 ? ? ? ? ? ? ? 2.028 ? disulf2 disulf ? ? A CYS 26 SG ? ? ? 1_555 A CYS 681 SG ? ? A CYS 79 A CYS 734 1_555 ? ? ? ? ? ? ? 2.015 ? disulf3 disulf ? ? A CYS 34 SG ? ? ? 1_555 A CYS 641 SG ? ? A CYS 87 A CYS 694 1_555 ? ? ? ? ? ? ? 2.033 ? disulf4 disulf ? ? A CYS 89 SG ? ? ? 1_555 A CYS 357 SG ? ? A CYS 142 A CYS 410 1_555 ? ? ? ? ? ? ? 2.038 ? disulf5 disulf ? ? A CYS 180 SG ? ? ? 1_555 A CYS 188 SG ? ? A CYS 233 A CYS 241 1_555 ? ? ? ? ? ? ? 2.024 ? disulf6 disulf ? ? A CYS 567 SG ? ? ? 1_555 A CYS 693 SG ? ? A CYS 620 A CYS 746 1_555 ? ? ? ? ? ? ? 2.042 ? covale1 covale ? ? A ASN 91 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 144 A NAG 752 1_555 ? ? ? ? ? ? ? 1.445 ? covale2 covale ? ? A ASN 271 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 324 A NAG 753 1_555 ? ? ? ? ? ? ? 1.440 ? covale3 covale ? ? A ASN 574 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 627 A NAG 754 1_555 ? ? ? ? ? ? ? 1.435 ? metalc1 metalc ? ? A HIS 530 NE2 ? ? ? 1_555 E ZN . ZN ? ? A HIS 583 A ZN 1001 1_555 ? ? ? ? ? ? ? 1.968 ? metalc2 metalc ? ? A HIS 534 NE2 ? ? ? 1_555 E ZN . ZN ? ? A HIS 587 A ZN 1001 1_555 ? ? ? ? ? ? ? 2.116 ? metalc3 metalc ? ? A GLU 593 OE1 ? ? ? 1_555 E ZN . ZN ? ? A GLU 646 A ZN 1001 1_555 ? ? ? ? ? ? ? 1.984 ? metalc4 metalc ? ? E ZN . ZN ? ? ? 1_555 F BIR . O6 ? ? A ZN 1001 A BIR 2001 1_555 ? ? ? ? ? ? ? 1.945 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? 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 LYS 265 A . ? LYS 318 A PRO 266 A ? PRO 319 A 1 5.23 2 PRO 508 A . ? PRO 561 A PRO 509 A ? PRO 562 A 1 12.57 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 2 ? B ? 4 ? C ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? parallel B 3 4 ? anti-parallel C 1 2 ? parallel C 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 ARG A 49 ? GLY A 51 ? ARG A 102 GLY A 104 A 2 GLY A 642 ? TYR A 644 ? GLY A 695 TYR A 697 B 1 ASN A 148 ? ASP A 154 ? ASN A 201 ASP A 207 B 2 ASN A 157 ? ASP A 166 ? ASN A 210 ASP A 219 B 3 ASP A 289 ? VAL A 292 ? ASP A 342 VAL A 345 B 4 LYS A 248 ? THR A 250 ? LYS A 301 THR A 303 C 1 LYS A 423 ? GLY A 427 ? LYS A 476 GLY A 480 C 2 GLN A 498 ? PRO A 502 ? GLN A 551 PRO A 555 C 3 PHE A 491 ? SER A 493 ? PHE A 544 SER A 546 # 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 50 ? N TYR A 103 O THR A 643 ? O THR A 696 B 1 2 N ASN A 148 ? N ASN A 201 O ASP A 166 ? O ASP A 219 B 2 3 N ILE A 165 ? N ILE A 218 O VAL A 291 ? O VAL A 344 B 3 4 O VAL A 290 ? O VAL A 343 N MET A 249 ? N MET A 302 C 1 2 N GLY A 427 ? N GLY A 480 O PHE A 501 ? O PHE A 554 C 2 3 O VAL A 500 ? O VAL A 553 N PHE A 491 ? N PHE A 544 # 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 ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 752' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 753' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 754' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 1001' AC5 Software ? ? ? ? 21 'BINDING SITE FOR RESIDUE BIR A 2001' # 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 2 ASN A 91 ? ASN A 144 . ? 1_555 ? 2 AC1 2 ALA A 94 ? ALA A 147 . ? 1_555 ? 3 AC2 2 ASN A 271 ? ASN A 324 . ? 1_555 ? 4 AC2 2 GLU A 275 ? GLU A 328 . ? 1_555 ? 5 AC3 3 TYR A 570 ? TYR A 623 . ? 1_555 ? 6 AC3 3 GLY A 573 ? GLY A 626 . ? 1_555 ? 7 AC3 3 ASN A 574 ? ASN A 627 . ? 1_555 ? 8 AC4 4 HIS A 530 ? HIS A 583 . ? 1_555 ? 9 AC4 4 HIS A 534 ? HIS A 587 . ? 1_555 ? 10 AC4 4 GLU A 593 ? GLU A 646 . ? 1_555 ? 11 AC4 4 BIR F . ? BIR A 2001 . ? 1_555 ? 12 AC5 21 PHE A 53 ? PHE A 106 . ? 1_555 ? 13 AC5 21 ASN A 489 ? ASN A 542 . ? 1_555 ? 14 AC5 21 ALA A 490 ? ALA A 543 . ? 1_555 ? 15 AC5 21 PHE A 491 ? PHE A 544 . ? 1_555 ? 16 AC5 21 HIS A 530 ? HIS A 583 . ? 1_555 ? 17 AC5 21 GLU A 531 ? GLU A 584 . ? 1_555 ? 18 AC5 21 HIS A 534 ? HIS A 587 . ? 1_555 ? 19 AC5 21 GLU A 593 ? GLU A 646 . ? 1_555 ? 20 AC5 21 PHE A 636 ? PHE A 689 . ? 1_555 ? 21 AC5 21 VAL A 639 ? VAL A 692 . ? 1_555 ? 22 AC5 21 TRP A 640 ? TRP A 693 . ? 1_555 ? 23 AC5 21 HIS A 658 ? HIS A 711 . ? 1_555 ? 24 AC5 21 ARG A 664 ? ARG A 717 . ? 1_555 ? 25 AC5 21 ZN E . ? ZN A 1001 . ? 1_555 ? 26 AC5 21 HOH G . ? HOH A 2010 . ? 1_555 ? 27 AC5 21 HOH G . ? HOH A 2011 . ? 1_555 ? 28 AC5 21 HOH G . ? HOH A 2012 . ? 1_555 ? 29 AC5 21 HOH G . ? HOH A 2197 . ? 1_555 ? 30 AC5 21 HOH G . ? HOH A 2207 . ? 1_555 ? 31 AC5 21 HOH G . ? HOH A 2208 . ? 1_555 ? 32 AC5 21 HOH G . ? HOH A 2251 . ? 1_555 ? # _database_PDB_matrix.entry_id 1R1H _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 1R1H _atom_sites.fract_transf_matrix[1][1] 0.009277 _atom_sites.fract_transf_matrix[1][2] 0.005356 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.010712 _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] 0.008843 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O P 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 . GLY A 1 1 ? 45.362 72.123 50.922 1.00 38.68 ? 54 GLY A N 1 ATOM 2 C CA . GLY A 1 1 ? 44.446 71.796 49.786 1.00 38.62 ? 54 GLY A CA 1 ATOM 3 C C . GLY A 1 1 ? 43.773 70.448 49.984 1.00 36.25 ? 54 GLY A C 1 ATOM 4 O O . GLY A 1 1 ? 43.616 69.684 49.037 1.00 35.91 ? 54 GLY A O 1 ATOM 5 N N . ILE A 1 2 ? 43.400 70.156 51.227 1.00 37.64 ? 55 ILE A N 1 ATOM 6 C CA . ILE A 1 2 ? 42.449 69.084 51.544 1.00 37.57 ? 55 ILE A CA 1 ATOM 7 C C . ILE A 1 2 ? 40.975 69.487 51.403 1.00 38.40 ? 55 ILE A C 1 ATOM 8 O O . ILE A 1 2 ? 40.505 70.416 52.066 1.00 40.99 ? 55 ILE A O 1 ATOM 9 C CB . ILE A 1 2 ? 42.702 68.605 52.975 1.00 37.55 ? 55 ILE A CB 1 ATOM 10 C CG1 . ILE A 1 2 ? 44.202 68.389 53.194 1.00 38.13 ? 55 ILE A CG1 1 ATOM 11 C CG2 . ILE A 1 2 ? 41.929 67.338 53.254 1.00 36.29 ? 55 ILE A CG2 1 ATOM 12 C CD1 . ILE A 1 2 ? 44.915 67.865 51.978 1.00 39.08 ? 55 ILE A CD1 1 ATOM 13 N N . CYS A 1 3 ? 40.248 68.761 50.556 1.00 33.91 ? 56 CYS A N 1 ATOM 14 C CA . CYS A 1 3 ? 38.786 68.788 50.542 1.00 33.31 ? 56 CYS A CA 1 ATOM 15 C C . CYS A 1 3 ? 38.158 68.311 51.855 1.00 35.52 ? 56 CYS A C 1 ATOM 16 O O . CYS A 1 3 ? 38.435 67.199 52.328 1.00 36.00 ? 56 CYS A O 1 ATOM 17 C CB . CYS A 1 3 ? 38.260 67.927 49.389 1.00 33.67 ? 56 CYS A CB 1 ATOM 18 S SG . CYS A 1 3 ? 36.457 67.843 49.295 1.00 30.46 ? 56 CYS A SG 1 ATOM 19 N N . LYS A 1 4 ? 37.293 69.144 52.427 1.00 35.21 ? 57 LYS A N 1 ATOM 20 C CA . LYS A 1 4 ? 36.699 68.854 53.731 1.00 36.03 ? 57 LYS A CA 1 ATOM 21 C C . LYS A 1 4 ? 35.173 68.748 53.674 1.00 33.78 ? 57 LYS A C 1 ATOM 22 O O . LYS A 1 4 ? 34.503 68.828 54.705 1.00 36.24 ? 57 LYS A O 1 ATOM 23 C CB . LYS A 1 4 ? 37.098 69.927 54.747 1.00 38.32 ? 57 LYS A CB 1 ATOM 24 C CG . LYS A 1 4 ? 36.704 71.347 54.344 1.00 42.28 ? 57 LYS A CG 1 ATOM 25 C CD . LYS A 1 4 ? 37.720 72.387 54.822 1.00 45.61 ? 57 LYS A CD 1 ATOM 26 C CE . LYS A 1 4 ? 37.056 73.469 55.665 1.00 47.20 ? 57 LYS A CE 1 ATOM 27 N NZ . LYS A 1 4 ? 37.905 74.698 55.793 1.00 50.11 ? 57 LYS A NZ 1 ATOM 28 N N . SER A 1 5 ? 34.626 68.567 52.478 1.00 33.59 ? 58 SER A N 1 ATOM 29 C CA . SER A 1 5 ? 33.174 68.473 52.304 1.00 31.00 ? 58 SER A CA 1 ATOM 30 C C . SER A 1 5 ? 32.649 67.154 52.868 1.00 32.46 ? 58 SER A C 1 ATOM 31 O O . SER A 1 5 ? 33.407 66.200 53.004 1.00 24.98 ? 58 SER A O 1 ATOM 32 C CB . SER A 1 5 ? 32.817 68.560 50.825 1.00 33.03 ? 58 SER A CB 1 ATOM 33 O OG . SER A 1 5 ? 33.124 67.344 50.156 1.00 34.54 ? 58 SER A OG 1 ATOM 34 N N . SER A 1 6 ? 31.359 67.092 53.189 1.00 26.95 ? 59 SER A N 1 ATOM 35 C CA . SER A 1 6 ? 30.774 65.851 53.688 1.00 30.74 ? 59 SER A CA 1 ATOM 36 C C . SER A 1 6 ? 30.897 64.747 52.660 1.00 27.92 ? 59 SER A C 1 ATOM 37 O O . SER A 1 6 ? 31.084 63.586 53.001 1.00 23.39 ? 59 SER A O 1 ATOM 38 C CB . SER A 1 6 ? 29.299 66.032 54.055 1.00 33.36 ? 59 SER A CB 1 ATOM 39 O OG . SER A 1 6 ? 29.151 66.197 55.453 1.00 40.66 ? 59 SER A OG 1 ATOM 40 N N . ASP A 1 7 ? 30.781 65.098 51.389 1.00 29.88 ? 60 ASP A N 1 ATOM 41 C CA . ASP A 1 7 ? 30.884 64.085 50.356 1.00 32.70 ? 60 ASP A CA 1 ATOM 42 C C . ASP A 1 7 ? 32.315 63.560 50.276 1.00 30.41 ? 60 ASP A C 1 ATOM 43 O O . ASP A 1 7 ? 32.539 62.374 50.011 1.00 22.31 ? 60 ASP A O 1 ATOM 44 C CB . ASP A 1 7 ? 30.413 64.640 49.020 1.00 35.64 ? 60 ASP A CB 1 ATOM 45 C CG . ASP A 1 7 ? 28.973 65.111 49.073 1.00 39.20 ? 60 ASP A CG 1 ATOM 46 O OD1 . ASP A 1 7 ? 28.078 64.266 49.273 1.00 41.61 ? 60 ASP A OD1 1 ATOM 47 O OD2 . ASP A 1 7 ? 28.641 66.307 48.943 1.00 43.15 ? 60 ASP A OD2 1 ATOM 48 N N . CYS A 1 8 ? 33.284 64.436 50.527 1.00 26.52 ? 61 CYS A N 1 ATOM 49 C CA . CYS A 1 8 ? 34.674 64.006 50.574 1.00 26.82 ? 61 CYS A CA 1 ATOM 50 C C . CYS A 1 8 ? 34.930 63.136 51.788 1.00 22.94 ? 61 CYS A C 1 ATOM 51 O O . CYS A 1 8 ? 35.711 62.199 51.717 1.00 25.97 ? 61 CYS A O 1 ATOM 52 C CB . CYS A 1 8 ? 35.626 65.200 50.593 1.00 28.17 ? 61 CYS A CB 1 ATOM 53 S SG . CYS A 1 8 ? 35.913 65.917 48.967 1.00 32.64 ? 61 CYS A SG 1 ATOM 54 N N . ILE A 1 9 ? 34.282 63.470 52.897 1.00 22.85 ? 62 ILE A N 1 ATOM 55 C CA . ILE A 1 9 ? 34.404 62.709 54.127 1.00 21.06 ? 62 ILE A CA 1 ATOM 56 C C . ILE A 1 9 ? 33.818 61.308 53.949 1.00 22.17 ? 62 ILE A C 1 ATOM 57 O O . ILE A 1 9 ? 34.328 60.342 54.519 1.00 21.37 ? 62 ILE A O 1 ATOM 58 C CB . ILE A 1 9 ? 33.692 63.440 55.284 1.00 24.69 ? 62 ILE A CB 1 ATOM 59 C CG1 . ILE A 1 9 ? 34.626 64.487 55.894 1.00 26.41 ? 62 ILE A CG1 1 ATOM 60 C CG2 . ILE A 1 9 ? 33.221 62.442 56.339 1.00 23.93 ? 62 ILE A CG2 1 ATOM 61 C CD1 . ILE A 1 9 ? 35.952 64.595 55.178 1.00 28.68 ? 62 ILE A CD1 1 ATOM 62 N N . LYS A 1 10 ? 32.754 61.193 53.162 1.00 20.81 ? 63 LYS A N 1 ATOM 63 C CA . LYS A 1 10 ? 32.124 59.891 52.929 1.00 23.77 ? 63 LYS A CA 1 ATOM 64 C C . LYS A 1 10 ? 33.002 59.011 52.056 1.00 22.65 ? 63 LYS A C 1 ATOM 65 O O . LYS A 1 10 ? 33.218 57.842 52.365 1.00 18.43 ? 63 LYS A O 1 ATOM 66 C CB . LYS A 1 10 ? 30.753 60.054 52.279 1.00 27.58 ? 63 LYS A CB 1 ATOM 67 C CG . LYS A 1 10 ? 29.694 60.686 53.173 1.00 32.56 ? 63 LYS A CG 1 ATOM 68 C CD . LYS A 1 10 ? 28.469 61.071 52.354 1.00 35.14 ? 63 LYS A CD 1 ATOM 69 C CE . LYS A 1 10 ? 27.185 60.903 53.145 1.00 38.25 ? 63 LYS A CE 1 ATOM 70 N NZ . LYS A 1 10 ? 26.013 61.484 52.426 1.00 38.15 ? 63 LYS A NZ 1 ATOM 71 N N . SER A 1 11 ? 33.499 59.577 50.960 1.00 26.87 ? 64 SER A N 1 ATOM 72 C CA . SER A 1 11 ? 34.371 58.844 50.055 1.00 26.10 ? 64 SER A CA 1 ATOM 73 C C . SER A 1 11 ? 35.565 58.373 50.845 1.00 24.56 ? 64 SER A C 1 ATOM 74 O O . SER A 1 11 ? 35.873 57.184 50.860 1.00 22.47 ? 64 SER A O 1 ATOM 75 C CB . SER A 1 11 ? 34.840 59.731 48.901 1.00 26.29 ? 64 SER A CB 1 ATOM 76 O OG . SER A 1 11 ? 33.803 60.578 48.474 1.00 31.63 ? 64 SER A OG 1 ATOM 77 N N . ALA A 1 12 ? 36.232 59.310 51.518 1.00 23.05 ? 65 ALA A N 1 ATOM 78 C CA . ALA A 1 12 ? 37.505 58.994 52.160 1.00 24.14 ? 65 ALA A CA 1 ATOM 79 C C . ALA A 1 12 ? 37.311 57.870 53.160 1.00 20.12 ? 65 ALA A C 1 ATOM 80 O O . ALA A 1 12 ? 38.072 56.911 53.169 1.00 20.77 ? 65 ALA A O 1 ATOM 81 C CB . ALA A 1 12 ? 38.088 60.215 52.840 1.00 26.48 ? 65 ALA A CB 1 ATOM 82 N N . ALA A 1 13 ? 36.276 57.981 53.987 1.00 20.96 ? 66 ALA A N 1 ATOM 83 C CA . ALA A 1 13 ? 36.005 56.991 55.022 1.00 20.12 ? 66 ALA A CA 1 ATOM 84 C C . ALA A 1 13 ? 35.882 55.596 54.417 1.00 21.41 ? 66 ALA A C 1 ATOM 85 O O . ALA A 1 13 ? 36.398 54.620 54.965 1.00 18.26 ? 66 ALA A O 1 ATOM 86 C CB . ALA A 1 13 ? 34.720 57.329 55.768 1.00 20.61 ? 66 ALA A CB 1 ATOM 87 N N . ARG A 1 14 ? 35.176 55.503 53.297 1.00 22.12 ? 67 ARG A N 1 ATOM 88 C CA . ARG A 1 14 ? 34.943 54.211 52.644 1.00 21.78 ? 67 ARG A CA 1 ATOM 89 C C . ARG A 1 14 ? 36.241 53.622 52.101 1.00 21.40 ? 67 ARG A C 1 ATOM 90 O O . ARG A 1 14 ? 36.494 52.428 52.233 1.00 23.34 ? 67 ARG A O 1 ATOM 91 C CB . ARG A 1 14 ? 33.920 54.357 51.516 1.00 26.38 ? 67 ARG A CB 1 ATOM 92 C CG . ARG A 1 14 ? 33.575 53.057 50.822 1.00 24.25 ? 67 ARG A CG 1 ATOM 93 C CD . ARG A 1 14 ? 34.286 52.865 49.497 1.00 24.49 ? 67 ARG A CD 1 ATOM 94 N NE . ARG A 1 14 ? 34.018 53.952 48.559 1.00 23.43 ? 67 ARG A NE 1 ATOM 95 C CZ . ARG A 1 14 ? 34.634 54.092 47.399 1.00 26.76 ? 67 ARG A CZ 1 ATOM 96 N NH1 . ARG A 1 14 ? 35.548 53.187 47.021 1.00 21.94 ? 67 ARG A NH1 1 ATOM 97 N NH2 . ARG A 1 14 ? 34.331 55.127 46.608 1.00 26.00 ? 67 ARG A NH2 1 ATOM 98 N N . LEU A 1 15 ? 37.068 54.468 51.507 1.00 18.05 ? 68 LEU A N 1 ATOM 99 C CA . LEU A 1 15 ? 38.332 54.025 50.942 1.00 17.07 ? 68 LEU A CA 1 ATOM 100 C C . LEU A 1 15 ? 39.237 53.538 52.057 1.00 19.77 ? 68 LEU A C 1 ATOM 101 O O . LEU A 1 15 ? 39.874 52.482 51.939 1.00 17.62 ? 68 LEU A O 1 ATOM 102 C CB . LEU A 1 15 ? 38.985 55.168 50.177 1.00 17.31 ? 68 LEU A CB 1 ATOM 103 C CG . LEU A 1 15 ? 38.208 55.586 48.927 1.00 21.77 ? 68 LEU A CG 1 ATOM 104 C CD1 . LEU A 1 15 ? 38.627 56.957 48.440 1.00 20.40 ? 68 LEU A CD1 1 ATOM 105 C CD2 . LEU A 1 15 ? 38.387 54.559 47.820 1.00 23.94 ? 68 LEU A CD2 1 ATOM 106 N N . ILE A 1 16 ? 39.275 54.301 53.150 1.00 16.97 ? 69 ILE A N 1 ATOM 107 C CA . ILE A 1 16 ? 40.122 53.966 54.282 1.00 23.19 ? 69 ILE A CA 1 ATOM 108 C C . ILE A 1 16 ? 39.747 52.591 54.833 1.00 23.41 ? 69 ILE A C 1 ATOM 109 O O . ILE A 1 16 ? 40.602 51.722 55.005 1.00 20.64 ? 69 ILE A O 1 ATOM 110 C CB . ILE A 1 16 ? 40.024 55.053 55.377 1.00 22.76 ? 69 ILE A CB 1 ATOM 111 C CG1 . ILE A 1 16 ? 40.631 56.366 54.874 1.00 22.26 ? 69 ILE A CG1 1 ATOM 112 C CG2 . ILE A 1 16 ? 40.730 54.596 56.647 1.00 25.45 ? 69 ILE A CG2 1 ATOM 113 C CD1 . ILE A 1 16 ? 40.283 57.570 55.725 1.00 22.61 ? 69 ILE A CD1 1 ATOM 114 N N . GLN A 1 17 ? 38.461 52.392 55.092 1.00 19.56 ? 70 GLN A N 1 ATOM 115 C CA . GLN A 1 17 ? 38.015 51.227 55.846 1.00 26.07 ? 70 GLN A CA 1 ATOM 116 C C . GLN A 1 17 ? 38.202 49.916 55.062 1.00 22.98 ? 70 GLN A C 1 ATOM 117 O O . GLN A 1 17 ? 38.395 48.857 55.657 1.00 24.05 ? 70 GLN A O 1 ATOM 118 C CB . GLN A 1 17 ? 36.546 51.383 56.257 1.00 28.77 ? 70 GLN A CB 1 ATOM 119 C CG . GLN A 1 17 ? 36.335 52.306 57.459 1.00 35.23 ? 70 GLN A CG 1 ATOM 120 C CD . GLN A 1 17 ? 34.945 52.927 57.491 1.00 41.86 ? 70 GLN A CD 1 ATOM 121 O OE1 . GLN A 1 17 ? 33.986 52.331 57.007 1.00 44.33 ? 70 GLN A OE1 1 ATOM 122 N NE2 . GLN A 1 17 ? 34.835 54.126 58.060 1.00 42.33 ? 70 GLN A NE2 1 ATOM 123 N N . ASN A 1 18 ? 38.164 49.999 53.733 1.00 18.85 ? 71 ASN A N 1 ATOM 124 C CA . ASN A 1 18 ? 38.344 48.820 52.879 1.00 17.02 ? 71 ASN A CA 1 ATOM 125 C C . ASN A 1 18 ? 39.792 48.352 52.731 1.00 19.26 ? 71 ASN A C 1 ATOM 126 O O . ASN A 1 18 ? 40.060 47.154 52.580 1.00 16.54 ? 71 ASN A O 1 ATOM 127 C CB . ASN A 1 18 ? 37.731 49.073 51.503 1.00 17.31 ? 71 ASN A CB 1 ATOM 128 C CG . ASN A 1 18 ? 36.215 49.054 51.547 1.00 19.23 ? 71 ASN A CG 1 ATOM 129 O OD1 . ASN A 1 18 ? 35.635 48.419 52.421 1.00 23.99 ? 71 ASN A OD1 1 ATOM 130 N ND2 . ASN A 1 18 ? 35.573 49.745 50.621 1.00 18.89 ? 71 ASN A ND2 1 ATOM 131 N N . MET A 1 19 ? 40.717 49.300 52.754 1.00 19.14 ? 72 MET A N 1 ATOM 132 C CA . MET A 1 19 ? 42.081 49.047 52.315 1.00 21.80 ? 72 MET A CA 1 ATOM 133 C C . MET A 1 19 ? 42.883 48.444 53.459 1.00 25.50 ? 72 MET A C 1 ATOM 134 O O . MET A 1 19 ? 42.493 48.551 54.610 1.00 22.80 ? 72 MET A O 1 ATOM 135 C CB . MET A 1 19 ? 42.732 50.343 51.813 1.00 20.42 ? 72 MET A CB 1 ATOM 136 C CG . MET A 1 19 ? 42.939 51.403 52.858 1.00 21.87 ? 72 MET A CG 1 ATOM 137 S SD . MET A 1 19 ? 43.516 52.960 52.129 1.00 26.41 ? 72 MET A SD 1 ATOM 138 C CE . MET A 1 19 ? 45.040 52.442 51.373 1.00 27.25 ? 72 MET A CE 1 ATOM 139 N N . ASP A 1 20 ? 43.994 47.791 53.142 1.00 26.25 ? 73 ASP A N 1 ATOM 140 C CA . ASP A 1 20 ? 44.978 47.477 54.165 1.00 27.30 ? 73 ASP A CA 1 ATOM 141 C C . ASP A 1 20 ? 46.340 48.050 53.831 1.00 28.46 ? 73 ASP A C 1 ATOM 142 O O . ASP A 1 20 ? 47.105 47.463 53.059 1.00 24.99 ? 73 ASP A O 1 ATOM 143 C CB . ASP A 1 20 ? 45.120 45.982 54.373 1.00 29.61 ? 73 ASP A CB 1 ATOM 144 C CG . ASP A 1 20 ? 46.086 45.664 55.497 1.00 32.71 ? 73 ASP A CG 1 ATOM 145 O OD1 . ASP A 1 20 ? 46.504 46.621 56.188 1.00 31.58 ? 73 ASP A OD1 1 ATOM 146 O OD2 . ASP A 1 20 ? 46.482 44.511 55.766 1.00 37.67 ? 73 ASP A OD2 1 ATOM 147 N N . ALA A 1 21 ? 46.642 49.199 54.426 1.00 28.86 ? 74 ALA A N 1 ATOM 148 C CA . ALA A 1 21 ? 47.892 49.888 54.152 1.00 32.68 ? 74 ALA A CA 1 ATOM 149 C C . ALA A 1 21 ? 49.116 49.114 54.650 1.00 32.53 ? 74 ALA A C 1 ATOM 150 O O . ALA A 1 21 ? 50.241 49.523 54.383 1.00 35.02 ? 74 ALA A O 1 ATOM 151 C CB . ALA A 1 21 ? 47.870 51.288 54.765 1.00 34.27 ? 74 ALA A CB 1 ATOM 152 N N . THR A 1 22 ? 48.911 48.008 55.367 1.00 35.46 ? 75 THR A N 1 ATOM 153 C CA . THR A 1 22 ? 50.045 47.210 55.842 1.00 36.72 ? 75 THR A CA 1 ATOM 154 C C . THR A 1 22 ? 50.639 46.388 54.702 1.00 35.43 ? 75 THR A C 1 ATOM 155 O O . THR A 1 22 ? 51.743 45.856 54.815 1.00 34.45 ? 75 THR A O 1 ATOM 156 C CB . THR A 1 22 ? 49.647 46.279 57.012 1.00 36.38 ? 75 THR A CB 1 ATOM 157 O OG1 . THR A 1 22 ? 48.526 45.473 56.640 1.00 43.60 ? 75 THR A OG1 1 ATOM 158 C CG2 . THR A 1 22 ? 49.147 47.065 58.208 1.00 38.84 ? 75 THR A CG2 1 ATOM 159 N N . THR A 1 23 ? 49.893 46.283 53.608 1.00 32.44 ? 76 THR A N 1 ATOM 160 C CA . THR A 1 23 ? 50.347 45.555 52.431 1.00 32.26 ? 76 THR A CA 1 ATOM 161 C C . THR A 1 23 ? 50.938 46.513 51.405 1.00 28.56 ? 76 THR A C 1 ATOM 162 O O . THR A 1 23 ? 50.407 47.596 51.175 1.00 28.64 ? 76 THR A O 1 ATOM 163 C CB . THR A 1 23 ? 49.175 44.762 51.803 1.00 34.94 ? 76 THR A CB 1 ATOM 164 O OG1 . THR A 1 23 ? 48.758 43.711 52.685 1.00 36.22 ? 76 THR A OG1 1 ATOM 165 C CG2 . THR A 1 23 ? 49.625 44.024 50.545 1.00 35.17 ? 76 THR A CG2 1 ATOM 166 N N . GLU A 1 24 ? 52.042 46.103 50.787 1.00 26.00 ? 77 GLU A N 1 ATOM 167 C CA . GLU A 1 24 ? 52.653 46.857 49.695 1.00 27.66 ? 77 GLU A CA 1 ATOM 168 C C . GLU A 1 24 ? 51.784 46.814 48.452 1.00 22.51 ? 77 GLU A C 1 ATOM 169 O O . GLU A 1 24 ? 51.476 45.751 47.945 1.00 25.88 ? 77 GLU A O 1 ATOM 170 C CB . GLU A 1 24 ? 54.036 46.286 49.367 1.00 30.91 ? 77 GLU A CB 1 ATOM 171 C CG . GLU A 1 24 ? 54.650 46.828 48.089 1.00 32.14 ? 77 GLU A CG 1 ATOM 172 C CD . GLU A 1 24 ? 54.736 48.336 48.089 1.00 33.88 ? 77 GLU A CD 1 ATOM 173 O OE1 . GLU A 1 24 ? 54.320 48.956 47.091 1.00 32.47 ? 77 GLU A OE1 1 ATOM 174 O OE2 . GLU A 1 24 ? 55.206 48.900 49.098 1.00 36.10 ? 77 GLU A OE2 1 ATOM 175 N N . PRO A 1 25 ? 51.390 47.978 47.961 1.00 25.50 ? 78 PRO A N 1 ATOM 176 C CA . PRO A 1 25 ? 50.578 48.060 46.743 1.00 25.40 ? 78 PRO A CA 1 ATOM 177 C C . PRO A 1 25 ? 51.158 47.243 45.590 1.00 29.02 ? 78 PRO A C 1 ATOM 178 O O . PRO A 1 25 ? 50.410 46.745 44.739 1.00 26.99 ? 78 PRO A O 1 ATOM 179 C CB . PRO A 1 25 ? 50.603 49.547 46.418 1.00 24.99 ? 78 PRO A CB 1 ATOM 180 C CG . PRO A 1 25 ? 50.784 50.201 47.713 1.00 24.98 ? 78 PRO A CG 1 ATOM 181 C CD . PRO A 1 25 ? 51.651 49.304 48.539 1.00 26.79 ? 78 PRO A CD 1 ATOM 182 N N . CYS A 1 26 ? 52.483 47.118 45.558 1.00 28.27 ? 79 CYS A N 1 ATOM 183 C CA . CYS A 1 26 ? 53.166 46.590 44.384 1.00 26.17 ? 79 CYS A CA 1 ATOM 184 C C . CYS A 1 26 ? 53.353 45.076 44.532 1.00 23.91 ? 79 CYS A C 1 ATOM 185 O O . CYS A 1 26 ? 53.707 44.383 43.582 1.00 24.01 ? 79 CYS A O 1 ATOM 186 C CB . CYS A 1 26 ? 54.517 47.294 44.191 1.00 25.16 ? 79 CYS A CB 1 ATOM 187 S SG . CYS A 1 26 ? 54.388 49.056 43.809 1.00 28.88 ? 79 CYS A SG 1 ATOM 188 N N . THR A 1 27 ? 53.107 44.575 45.737 1.00 25.75 ? 80 THR A N 1 ATOM 189 C CA . THR A 1 27 ? 53.110 43.138 45.999 1.00 25.18 ? 80 THR A CA 1 ATOM 190 C C . THR A 1 27 ? 51.755 42.504 45.674 1.00 24.25 ? 80 THR A C 1 ATOM 191 O O . THR A 1 27 ? 51.684 41.428 45.101 1.00 23.84 ? 80 THR A O 1 ATOM 192 C CB . THR A 1 27 ? 53.472 42.883 47.479 1.00 27.47 ? 80 THR A CB 1 ATOM 193 O OG1 . THR A 1 27 ? 54.802 43.339 47.733 1.00 29.68 ? 80 THR A OG1 1 ATOM 194 C CG2 . THR A 1 27 ? 53.518 41.388 47.802 1.00 27.90 ? 80 THR A CG2 1 ATOM 195 N N . ASP A 1 28 ? 50.676 43.183 46.042 1.00 25.99 ? 81 ASP A N 1 ATOM 196 C CA . ASP A 1 28 ? 49.337 42.668 45.782 1.00 22.22 ? 81 ASP A CA 1 ATOM 197 C C . ASP A 1 28 ? 48.352 43.797 45.971 1.00 20.73 ? 81 ASP A C 1 ATOM 198 O O . ASP A 1 28 ? 47.955 44.096 47.093 1.00 21.26 ? 81 ASP A O 1 ATOM 199 C CB . ASP A 1 28 ? 49.008 41.529 46.739 1.00 19.59 ? 81 ASP A CB 1 ATOM 200 C CG . ASP A 1 28 ? 47.645 40.920 46.483 1.00 24.80 ? 81 ASP A CG 1 ATOM 201 O OD1 . ASP A 1 28 ? 46.722 41.650 46.053 1.00 25.59 ? 81 ASP A OD1 1 ATOM 202 O OD2 . ASP A 1 28 ? 47.397 39.717 46.705 1.00 22.65 ? 81 ASP A OD2 1 ATOM 203 N N . PHE A 1 29 ? 47.987 44.456 44.881 1.00 22.41 ? 82 PHE A N 1 ATOM 204 C CA . PHE A 1 29 ? 47.154 45.638 44.999 1.00 20.79 ? 82 PHE A CA 1 ATOM 205 C C . PHE A 1 29 ? 45.732 45.304 45.426 1.00 17.35 ? 82 PHE A C 1 ATOM 206 O O . PHE A 1 29 ? 45.039 46.151 45.997 1.00 21.44 ? 82 PHE A O 1 ATOM 207 C CB . PHE A 1 29 ? 47.117 46.432 43.705 1.00 20.26 ? 82 PHE A CB 1 ATOM 208 C CG . PHE A 1 29 ? 46.613 47.825 43.889 1.00 21.51 ? 82 PHE A CG 1 ATOM 209 C CD1 . PHE A 1 29 ? 47.427 48.800 44.443 1.00 21.84 ? 82 PHE A CD1 1 ATOM 210 C CD2 . PHE A 1 29 ? 45.311 48.155 43.553 1.00 19.65 ? 82 PHE A CD2 1 ATOM 211 C CE1 . PHE A 1 29 ? 46.961 50.077 44.625 1.00 20.57 ? 82 PHE A CE1 1 ATOM 212 C CE2 . PHE A 1 29 ? 44.843 49.436 43.735 1.00 18.06 ? 82 PHE A CE2 1 ATOM 213 C CZ . PHE A 1 29 ? 45.652 50.397 44.270 1.00 18.09 ? 82 PHE A CZ 1 ATOM 214 N N . PHE A 1 30 ? 45.285 44.080 45.165 1.00 19.55 ? 83 PHE A N 1 ATOM 215 C CA . PHE A 1 30 ? 43.956 43.677 45.631 1.00 18.89 ? 83 PHE A CA 1 ATOM 216 C C . PHE A 1 30 ? 43.898 43.644 47.160 1.00 17.64 ? 83 PHE A C 1 ATOM 217 O O . PHE A 1 30 ? 42.948 44.138 47.772 1.00 17.52 ? 83 PHE A O 1 ATOM 218 C CB . PHE A 1 30 ? 43.545 42.329 45.054 1.00 19.52 ? 83 PHE A CB 1 ATOM 219 C CG . PHE A 1 30 ? 42.176 41.879 45.489 1.00 21.13 ? 83 PHE A CG 1 ATOM 220 C CD1 . PHE A 1 30 ? 42.028 40.847 46.391 1.00 19.76 ? 83 PHE A CD1 1 ATOM 221 C CD2 . PHE A 1 30 ? 41.035 42.500 44.993 1.00 21.83 ? 83 PHE A CD2 1 ATOM 222 C CE1 . PHE A 1 30 ? 40.757 40.432 46.796 1.00 21.85 ? 83 PHE A CE1 1 ATOM 223 C CE2 . PHE A 1 30 ? 39.771 42.089 45.389 1.00 20.95 ? 83 PHE A CE2 1 ATOM 224 C CZ . PHE A 1 30 ? 39.634 41.054 46.291 1.00 21.87 ? 83 PHE A CZ 1 ATOM 225 N N . LYS A 1 31 ? 44.925 43.077 47.777 1.00 21.89 ? 84 LYS A N 1 ATOM 226 C CA . LYS A 1 31 ? 44.991 42.996 49.234 1.00 22.74 ? 84 LYS A CA 1 ATOM 227 C C . LYS A 1 31 ? 45.172 44.383 49.850 1.00 16.70 ? 84 LYS A C 1 ATOM 228 O O . LYS A 1 31 ? 44.540 44.720 50.842 1.00 20.21 ? 84 LYS A O 1 ATOM 229 C CB . LYS A 1 31 ? 46.152 42.082 49.650 1.00 25.76 ? 84 LYS A CB 1 ATOM 230 C CG . LYS A 1 31 ? 46.145 41.707 51.119 1.00 31.00 ? 84 LYS A CG 1 ATOM 231 C CD . LYS A 1 31 ? 47.374 40.864 51.490 1.00 34.70 ? 84 LYS A CD 1 ATOM 232 C CE . LYS A 1 31 ? 47.253 40.274 52.883 1.00 36.27 ? 84 LYS A CE 1 ATOM 233 N NZ . LYS A 1 31 ? 48.094 39.050 53.018 1.00 41.81 ? 84 LYS A NZ 1 ATOM 234 N N . TYR A 1 32 ? 46.041 45.188 49.252 1.00 21.13 ? 85 TYR A N 1 ATOM 235 C CA . TYR A 1 32 ? 46.172 46.590 49.648 1.00 23.06 ? 85 TYR A CA 1 ATOM 236 C C . TYR A 1 32 ? 44.831 47.331 49.599 1.00 20.54 ? 85 TYR A C 1 ATOM 237 O O . TYR A 1 32 ? 44.476 48.047 50.534 1.00 19.78 ? 85 TYR A O 1 ATOM 238 C CB . TYR A 1 32 ? 47.165 47.294 48.732 1.00 21.25 ? 85 TYR A CB 1 ATOM 239 C CG . TYR A 1 32 ? 47.325 48.786 48.978 1.00 22.20 ? 85 TYR A CG 1 ATOM 240 C CD1 . TYR A 1 32 ? 48.140 49.268 49.997 1.00 23.37 ? 85 TYR A CD1 1 ATOM 241 C CD2 . TYR A 1 32 ? 46.697 49.711 48.158 1.00 23.52 ? 85 TYR A CD2 1 ATOM 242 C CE1 . TYR A 1 32 ? 48.310 50.638 50.198 1.00 26.15 ? 85 TYR A CE1 1 ATOM 243 C CE2 . TYR A 1 32 ? 46.853 51.070 48.352 1.00 24.83 ? 85 TYR A CE2 1 ATOM 244 C CZ . TYR A 1 32 ? 47.655 51.534 49.367 1.00 25.89 ? 85 TYR A CZ 1 ATOM 245 O OH . TYR A 1 32 ? 47.796 52.895 49.538 1.00 24.49 ? 85 TYR A OH 1 ATOM 246 N N . ALA A 1 33 ? 44.113 47.179 48.494 1.00 19.82 ? 86 ALA A N 1 ATOM 247 C CA . ALA A 1 33 ? 42.871 47.931 48.267 1.00 20.49 ? 86 ALA A CA 1 ATOM 248 C C . ALA A 1 33 ? 41.722 47.423 49.144 1.00 22.45 ? 86 ALA A C 1 ATOM 249 O O . ALA A 1 33 ? 40.808 48.184 49.478 1.00 17.31 ? 86 ALA A O 1 ATOM 250 C CB . ALA A 1 33 ? 42.467 47.845 46.813 1.00 18.31 ? 86 ALA A CB 1 ATOM 251 N N . CYS A 1 34 ? 41.764 46.139 49.495 1.00 18.17 ? 87 CYS A N 1 ATOM 252 C CA . CYS A 1 34 ? 40.563 45.404 49.892 1.00 19.23 ? 87 CYS A CA 1 ATOM 253 C C . CYS A 1 34 ? 40.770 44.604 51.181 1.00 20.55 ? 87 CYS A C 1 ATOM 254 O O . CYS A 1 34 ? 39.844 44.006 51.711 1.00 16.74 ? 87 CYS A O 1 ATOM 255 C CB . CYS A 1 34 ? 40.116 44.479 48.754 1.00 21.57 ? 87 CYS A CB 1 ATOM 256 S SG . CYS A 1 34 ? 39.350 45.388 47.396 1.00 16.59 ? 87 CYS A SG 1 ATOM 257 N N . GLY A 1 35 ? 41.985 44.606 51.706 1.00 22.63 ? 88 GLY A N 1 ATOM 258 C CA . GLY A 1 35 ? 42.308 43.721 52.815 1.00 23.19 ? 88 GLY A CA 1 ATOM 259 C C . GLY A 1 35 ? 41.541 44.069 54.077 1.00 24.57 ? 88 GLY A C 1 ATOM 260 O O . GLY A 1 35 ? 41.293 43.207 54.918 1.00 27.13 ? 88 GLY A O 1 ATOM 261 N N . GLY A 1 36 ? 41.175 45.341 54.219 1.00 22.88 ? 89 GLY A N 1 ATOM 262 C CA . GLY A 1 36 ? 40.350 45.772 55.331 1.00 21.40 ? 89 GLY A CA 1 ATOM 263 C C . GLY A 1 36 ? 38.982 45.124 55.249 1.00 21.14 ? 89 GLY A C 1 ATOM 264 O O . GLY A 1 36 ? 38.495 44.522 56.208 1.00 19.91 ? 89 GLY A O 1 ATOM 265 N N . TRP A 1 37 ? 38.364 45.240 54.080 1.00 17.90 ? 90 TRP A N 1 ATOM 266 C CA . TRP A 1 37 ? 37.060 44.661 53.843 1.00 18.29 ? 90 TRP A CA 1 ATOM 267 C C . TRP A 1 37 ? 37.102 43.162 54.114 1.00 17.07 ? 90 TRP A C 1 ATOM 268 O O . TRP A 1 37 ? 36.241 42.605 54.801 1.00 13.96 ? 90 TRP A O 1 ATOM 269 C CB . TRP A 1 37 ? 36.625 44.934 52.392 1.00 17.90 ? 90 TRP A CB 1 ATOM 270 C CG . TRP A 1 37 ? 35.218 44.526 52.128 1.00 20.34 ? 90 TRP A CG 1 ATOM 271 C CD1 . TRP A 1 37 ? 34.121 45.338 52.108 1.00 23.71 ? 90 TRP A CD1 1 ATOM 272 C CD2 . TRP A 1 37 ? 34.738 43.201 51.870 1.00 16.41 ? 90 TRP A CD2 1 ATOM 273 N NE1 . TRP A 1 37 ? 32.989 44.601 51.852 1.00 20.10 ? 90 TRP A NE1 1 ATOM 274 C CE2 . TRP A 1 37 ? 33.343 43.285 51.702 1.00 20.72 ? 90 TRP A CE2 1 ATOM 275 C CE3 . TRP A 1 37 ? 35.346 41.947 51.767 1.00 20.10 ? 90 TRP A CE3 1 ATOM 276 C CZ2 . TRP A 1 37 ? 32.550 42.166 51.450 1.00 18.84 ? 90 TRP A CZ2 1 ATOM 277 C CZ3 . TRP A 1 37 ? 34.559 40.841 51.496 1.00 20.56 ? 90 TRP A CZ3 1 ATOM 278 C CH2 . TRP A 1 37 ? 33.177 40.960 51.332 1.00 19.88 ? 90 TRP A CH2 1 ATOM 279 N N . LEU A 1 38 ? 38.105 42.503 53.556 1.00 20.33 ? 91 LEU A N 1 ATOM 280 C CA . LEU A 1 38 ? 38.197 41.056 53.646 1.00 25.85 ? 91 LEU A CA 1 ATOM 281 C C . LEU A 1 38 ? 38.132 40.617 55.109 1.00 28.93 ? 91 LEU A C 1 ATOM 282 O O . LEU A 1 38 ? 37.410 39.682 55.449 1.00 26.71 ? 91 LEU A O 1 ATOM 283 C CB . LEU A 1 38 ? 39.494 40.561 53.006 1.00 27.71 ? 91 LEU A CB 1 ATOM 284 C CG . LEU A 1 38 ? 39.436 40.018 51.576 1.00 31.81 ? 91 LEU A CG 1 ATOM 285 C CD1 . LEU A 1 38 ? 38.017 39.883 51.056 1.00 30.54 ? 91 LEU A CD1 1 ATOM 286 C CD2 . LEU A 1 38 ? 40.259 40.874 50.646 1.00 31.90 ? 91 LEU A CD2 1 ATOM 287 N N . LYS A 1 39 ? 38.884 41.299 55.970 1.00 28.23 ? 92 LYS A N 1 ATOM 288 C CA . LYS A 1 39 ? 39.019 40.889 57.365 1.00 29.83 ? 92 LYS A CA 1 ATOM 289 C C . LYS A 1 39 ? 37.731 41.128 58.143 1.00 28.89 ? 92 LYS A C 1 ATOM 290 O O . LYS A 1 39 ? 37.422 40.398 59.078 1.00 27.75 ? 92 LYS A O 1 ATOM 291 C CB . LYS A 1 39 ? 40.165 41.637 58.044 1.00 34.10 ? 92 LYS A CB 1 ATOM 292 C CG . LYS A 1 39 ? 40.311 41.301 59.529 1.00 37.79 ? 92 LYS A CG 1 ATOM 293 C CD . LYS A 1 39 ? 40.605 42.539 60.365 1.00 41.06 ? 92 LYS A CD 1 ATOM 294 C CE . LYS A 1 39 ? 41.185 42.172 61.733 1.00 43.74 ? 92 LYS A CE 1 ATOM 295 N NZ . LYS A 1 39 ? 41.047 40.715 62.037 1.00 42.85 ? 92 LYS A NZ 1 ATOM 296 N N . ARG A 1 40 ? 36.984 42.154 57.762 1.00 27.52 ? 93 ARG A N 1 ATOM 297 C CA . ARG A 1 40 ? 35.819 42.560 58.533 1.00 29.83 ? 93 ARG A CA 1 ATOM 298 C C . ARG A 1 40 ? 34.567 41.790 58.112 1.00 28.98 ? 93 ARG A C 1 ATOM 299 O O . ARG A 1 40 ? 33.630 41.650 58.885 1.00 27.03 ? 93 ARG A O 1 ATOM 300 C CB . ARG A 1 40 ? 35.590 44.071 58.405 1.00 36.58 ? 93 ARG A CB 1 ATOM 301 C CG . ARG A 1 40 ? 36.441 44.888 59.374 1.00 41.42 ? 93 ARG A CG 1 ATOM 302 C CD . ARG A 1 40 ? 36.380 46.394 59.168 1.00 46.50 ? 93 ARG A CD 1 ATOM 303 N NE . ARG A 1 40 ? 37.593 46.900 58.530 1.00 50.62 ? 93 ARG A NE 1 ATOM 304 C CZ . ARG A 1 40 ? 38.141 48.086 58.778 1.00 53.13 ? 93 ARG A CZ 1 ATOM 305 N NH1 . ARG A 1 40 ? 37.591 48.910 59.665 1.00 54.15 ? 93 ARG A NH1 1 ATOM 306 N NH2 . ARG A 1 40 ? 39.245 48.450 58.137 1.00 51.74 ? 93 ARG A NH2 1 ATOM 307 N N . ASN A 1 41 ? 34.554 41.275 56.888 1.00 25.25 ? 94 ASN A N 1 ATOM 308 C CA . ASN A 1 41 ? 33.334 40.676 56.355 1.00 22.70 ? 94 ASN A CA 1 ATOM 309 C C . ASN A 1 41 ? 33.408 39.164 56.230 1.00 24.77 ? 94 ASN A C 1 ATOM 310 O O . ASN A 1 41 ? 34.430 38.600 55.844 1.00 23.16 ? 94 ASN A O 1 ATOM 311 C CB . ASN A 1 41 ? 32.982 41.315 55.012 1.00 23.21 ? 94 ASN A CB 1 ATOM 312 C CG . ASN A 1 41 ? 32.466 42.736 55.168 1.00 24.61 ? 94 ASN A CG 1 ATOM 313 O OD1 . ASN A 1 41 ? 31.289 42.946 55.463 1.00 26.79 ? 94 ASN A OD1 1 ATOM 314 N ND2 . ASN A 1 41 ? 33.349 43.720 54.984 1.00 24.47 ? 94 ASN A ND2 1 ATOM 315 N N . VAL A 1 42 ? 32.296 38.517 56.570 1.00 24.52 ? 95 VAL A N 1 ATOM 316 C CA . VAL A 1 42 ? 32.088 37.096 56.315 1.00 21.76 ? 95 VAL A CA 1 ATOM 317 C C . VAL A 1 42 ? 30.899 36.928 55.375 1.00 22.67 ? 95 VAL A C 1 ATOM 318 O O . VAL A 1 42 ? 29.856 37.555 55.563 1.00 25.51 ? 95 VAL A O 1 ATOM 319 C CB . VAL A 1 42 ? 31.804 36.328 57.624 1.00 20.11 ? 95 VAL A CB 1 ATOM 320 C CG1 . VAL A 1 42 ? 31.568 34.854 57.345 1.00 24.25 ? 95 VAL A CG1 1 ATOM 321 C CG2 . VAL A 1 42 ? 32.938 36.500 58.608 1.00 22.20 ? 95 VAL A CG2 1 ATOM 322 N N . ILE A 1 43 ? 31.061 36.083 54.362 1.00 16.21 ? 96 ILE A N 1 ATOM 323 C CA . ILE A 1 43 ? 30.015 35.856 53.365 1.00 17.29 ? 96 ILE A CA 1 ATOM 324 C C . ILE A 1 43 ? 28.738 35.352 54.015 1.00 14.81 ? 96 ILE A C 1 ATOM 325 O O . ILE A 1 43 ? 28.739 34.299 54.649 1.00 16.00 ? 96 ILE A O 1 ATOM 326 C CB . ILE A 1 43 ? 30.468 34.802 52.349 1.00 20.29 ? 96 ILE A CB 1 ATOM 327 C CG1 . ILE A 1 43 ? 31.792 35.187 51.718 1.00 22.14 ? 96 ILE A CG1 1 ATOM 328 C CG2 . ILE A 1 43 ? 29.384 34.584 51.291 1.00 20.92 ? 96 ILE A CG2 1 ATOM 329 C CD1 . ILE A 1 43 ? 32.341 34.112 50.767 1.00 25.51 ? 96 ILE A CD1 1 ATOM 330 N N . PRO A 1 44 ? 27.638 36.079 53.846 1.00 16.94 ? 97 PRO A N 1 ATOM 331 C CA . PRO A 1 44 ? 26.359 35.654 54.420 1.00 17.45 ? 97 PRO A CA 1 ATOM 332 C C . PRO A 1 44 ? 25.993 34.240 53.985 1.00 15.59 ? 97 PRO A C 1 ATOM 333 O O . PRO A 1 44 ? 26.423 33.788 52.914 1.00 17.90 ? 97 PRO A O 1 ATOM 334 C CB . PRO A 1 44 ? 25.366 36.687 53.875 1.00 16.90 ? 97 PRO A CB 1 ATOM 335 C CG . PRO A 1 44 ? 26.177 37.867 53.554 1.00 18.74 ? 97 PRO A CG 1 ATOM 336 C CD . PRO A 1 44 ? 27.511 37.337 53.093 1.00 19.64 ? 97 PRO A CD 1 ATOM 337 N N . GLU A 1 45 ? 25.222 33.542 54.815 1.00 15.04 ? 98 GLU A N 1 ATOM 338 C CA . GLU A 1 45 ? 24.761 32.192 54.489 1.00 13.48 ? 98 GLU A CA 1 ATOM 339 C C . GLU A 1 45 ? 23.874 32.152 53.232 1.00 16.45 ? 98 GLU A C 1 ATOM 340 O O . GLU A 1 45 ? 23.783 31.121 52.557 1.00 14.53 ? 98 GLU A O 1 ATOM 341 C CB . GLU A 1 45 ? 24.023 31.579 55.685 1.00 17.83 ? 98 GLU A CB 1 ATOM 342 C CG . GLU A 1 45 ? 24.865 31.484 56.953 1.00 20.00 ? 98 GLU A CG 1 ATOM 343 C CD . GLU A 1 45 ? 26.035 30.536 56.806 1.00 18.43 ? 98 GLU A CD 1 ATOM 344 O OE1 . GLU A 1 45 ? 25.790 29.348 56.523 1.00 22.02 ? 98 GLU A OE1 1 ATOM 345 O OE2 . GLU A 1 45 ? 27.194 30.950 56.964 1.00 25.84 ? 98 GLU A OE2 1 ATOM 346 N N . THR A 1 46 ? 23.252 33.278 52.902 1.00 14.88 ? 99 THR A N 1 ATOM 347 C CA . THR A 1 46 ? 22.389 33.353 51.724 1.00 16.85 ? 99 THR A CA 1 ATOM 348 C C . THR A 1 46 ? 23.119 33.860 50.467 1.00 21.28 ? 99 THR A C 1 ATOM 349 O O . THR A 1 46 ? 22.482 34.053 49.427 1.00 19.23 ? 99 THR A O 1 ATOM 350 C CB . THR A 1 46 ? 21.227 34.316 51.989 1.00 17.11 ? 99 THR A CB 1 ATOM 351 O OG1 . THR A 1 46 ? 21.767 35.595 52.314 1.00 15.75 ? 99 THR A OG1 1 ATOM 352 C CG2 . THR A 1 46 ? 20.411 33.937 53.239 1.00 18.22 ? 99 THR A CG2 1 ATOM 353 N N . SER A 1 47 ? 24.425 34.113 50.569 1.00 17.05 ? 100 SER A N 1 ATOM 354 C CA . SER A 1 47 ? 25.205 34.664 49.451 1.00 16.92 ? 100 SER A CA 1 ATOM 355 C C . SER A 1 47 ? 26.201 33.630 48.903 1.00 17.40 ? 100 SER A C 1 ATOM 356 O O . SER A 1 47 ? 26.850 32.934 49.673 1.00 16.17 ? 100 SER A O 1 ATOM 357 C CB . SER A 1 47 ? 25.997 35.909 49.908 1.00 19.36 ? 100 SER A CB 1 ATOM 358 O OG . SER A 1 47 ? 25.149 36.973 50.339 1.00 22.18 ? 100 SER A OG 1 ATOM 359 N N . SER A 1 48 ? 26.338 33.553 47.581 1.00 15.94 ? 101 SER A N 1 ATOM 360 C CA . SER A 1 48 ? 27.361 32.722 46.955 1.00 19.98 ? 101 SER A CA 1 ATOM 361 C C . SER A 1 48 ? 28.602 33.549 46.639 1.00 16.67 ? 101 SER A C 1 ATOM 362 O O . SER A 1 48 ? 29.695 33.030 46.586 1.00 14.26 ? 101 SER A O 1 ATOM 363 C CB . SER A 1 48 ? 26.816 32.074 45.681 1.00 19.65 ? 101 SER A CB 1 ATOM 364 O OG . SER A 1 48 ? 26.284 33.055 44.817 1.00 24.24 ? 101 SER A OG 1 ATOM 365 N N . ARG A 1 49 ? 28.407 34.848 46.461 1.00 16.88 ? 102 ARG A N 1 ATOM 366 C CA . ARG A 1 49 ? 29.495 35.795 46.292 1.00 20.95 ? 102 ARG A CA 1 ATOM 367 C C . ARG A 1 49 ? 29.079 37.031 47.045 1.00 19.86 ? 102 ARG A C 1 ATOM 368 O O . ARG A 1 49 ? 27.906 37.367 47.069 1.00 17.99 ? 102 ARG A O 1 ATOM 369 C CB . ARG A 1 49 ? 29.698 36.132 44.822 1.00 21.69 ? 102 ARG A CB 1 ATOM 370 C CG . ARG A 1 49 ? 30.877 37.049 44.534 1.00 23.53 ? 102 ARG A CG 1 ATOM 371 C CD . ARG A 1 49 ? 30.943 37.567 43.092 1.00 22.03 ? 102 ARG A CD 1 ATOM 372 N NE . ARG A 1 49 ? 29.833 38.462 42.793 1.00 21.20 ? 102 ARG A NE 1 ATOM 373 C CZ . ARG A 1 49 ? 29.447 38.816 41.571 1.00 25.28 ? 102 ARG A CZ 1 ATOM 374 N NH1 . ARG A 1 49 ? 30.067 38.346 40.491 1.00 21.53 ? 102 ARG A NH1 1 ATOM 375 N NH2 . ARG A 1 49 ? 28.416 39.628 41.429 1.00 24.49 ? 102 ARG A NH2 1 ATOM 376 N N . TYR A 1 50 ? 30.031 37.698 47.676 1.00 17.02 ? 103 TYR A N 1 ATOM 377 C CA . TYR A 1 50 ? 29.713 38.857 48.488 1.00 18.15 ? 103 TYR A CA 1 ATOM 378 C C . TYR A 1 50 ? 30.864 39.832 48.401 1.00 17.17 ? 103 TYR A C 1 ATOM 379 O O . TYR A 1 50 ? 32.013 39.422 48.287 1.00 17.60 ? 103 TYR A O 1 ATOM 380 C CB . TYR A 1 50 ? 29.484 38.440 49.936 1.00 19.15 ? 103 TYR A CB 1 ATOM 381 C CG . TYR A 1 50 ? 28.833 39.490 50.790 1.00 19.74 ? 103 TYR A CG 1 ATOM 382 C CD1 . TYR A 1 50 ? 27.546 39.927 50.516 1.00 19.94 ? 103 TYR A CD1 1 ATOM 383 C CD2 . TYR A 1 50 ? 29.486 40.026 51.889 1.00 21.82 ? 103 TYR A CD2 1 ATOM 384 C CE1 . TYR A 1 50 ? 26.940 40.877 51.298 1.00 19.16 ? 103 TYR A CE1 1 ATOM 385 C CE2 . TYR A 1 50 ? 28.881 40.978 52.682 1.00 21.55 ? 103 TYR A CE2 1 ATOM 386 C CZ . TYR A 1 50 ? 27.603 41.401 52.378 1.00 23.14 ? 103 TYR A CZ 1 ATOM 387 O OH . TYR A 1 50 ? 26.973 42.351 53.158 1.00 22.02 ? 103 TYR A OH 1 ATOM 388 N N . GLY A 1 51 ? 30.551 41.123 48.418 1.00 13.66 ? 104 GLY A N 1 ATOM 389 C CA . GLY A 1 51 ? 31.513 42.145 48.061 1.00 14.85 ? 104 GLY A CA 1 ATOM 390 C C . GLY A 1 51 ? 30.822 43.481 47.850 1.00 19.27 ? 104 GLY A C 1 ATOM 391 O O . GLY A 1 51 ? 29.595 43.541 47.854 1.00 17.76 ? 104 GLY A O 1 ATOM 392 N N . ASN A 1 52 ? 31.601 44.547 47.654 1.00 16.54 ? 105 ASN A N 1 ATOM 393 C CA . ASN A 1 52 ? 31.029 45.881 47.550 1.00 15.56 ? 105 ASN A CA 1 ATOM 394 C C . ASN A 1 52 ? 29.966 45.899 46.459 1.00 17.66 ? 105 ASN A C 1 ATOM 395 O O . ASN A 1 52 ? 28.935 46.545 46.598 1.00 16.66 ? 105 ASN A O 1 ATOM 396 C CB . ASN A 1 52 ? 32.106 46.933 47.271 1.00 16.01 ? 105 ASN A CB 1 ATOM 397 C CG . ASN A 1 52 ? 32.976 47.240 48.497 1.00 20.26 ? 105 ASN A CG 1 ATOM 398 O OD1 . ASN A 1 52 ? 34.155 47.618 48.367 1.00 20.25 ? 105 ASN A OD1 1 ATOM 399 N ND2 . ASN A 1 52 ? 32.392 47.110 49.683 1.00 15.77 ? 105 ASN A ND2 1 ATOM 400 N N . PHE A 1 53 ? 30.227 45.185 45.371 1.00 17.03 ? 106 PHE A N 1 ATOM 401 C CA . PHE A 1 53 ? 29.347 45.204 44.222 1.00 13.00 ? 106 PHE A CA 1 ATOM 402 C C . PHE A 1 53 ? 28.017 44.524 44.545 1.00 17.70 ? 106 PHE A C 1 ATOM 403 O O . PHE A 1 53 ? 26.942 45.041 44.223 1.00 12.86 ? 106 PHE A O 1 ATOM 404 C CB . PHE A 1 53 ? 30.028 44.522 43.047 1.00 18.44 ? 106 PHE A CB 1 ATOM 405 C CG . PHE A 1 53 ? 29.246 44.587 41.775 1.00 17.27 ? 106 PHE A CG 1 ATOM 406 C CD1 . PHE A 1 53 ? 29.185 45.762 41.040 1.00 20.77 ? 106 PHE A CD1 1 ATOM 407 C CD2 . PHE A 1 53 ? 28.558 43.486 41.326 1.00 20.09 ? 106 PHE A CD2 1 ATOM 408 C CE1 . PHE A 1 53 ? 28.455 45.834 39.879 1.00 15.87 ? 106 PHE A CE1 1 ATOM 409 C CE2 . PHE A 1 53 ? 27.833 43.541 40.150 1.00 20.74 ? 106 PHE A CE2 1 ATOM 410 C CZ . PHE A 1 53 ? 27.775 44.728 39.432 1.00 20.71 ? 106 PHE A CZ 1 ATOM 411 N N . ASP A 1 54 ? 28.091 43.362 45.188 1.00 15.68 ? 107 ASP A N 1 ATOM 412 C CA . ASP A 1 54 ? 26.902 42.639 45.589 1.00 16.07 ? 107 ASP A CA 1 ATOM 413 C C . ASP A 1 54 ? 26.111 43.391 46.658 1.00 15.36 ? 107 ASP A C 1 ATOM 414 O O . ASP A 1 54 ? 24.881 43.297 46.709 1.00 14.53 ? 107 ASP A O 1 ATOM 415 C CB . ASP A 1 54 ? 27.275 41.243 46.085 1.00 18.11 ? 107 ASP A CB 1 ATOM 416 C CG . ASP A 1 54 ? 27.910 40.400 44.994 1.00 22.86 ? 107 ASP A CG 1 ATOM 417 O OD1 . ASP A 1 54 ? 27.238 40.143 43.980 1.00 24.20 ? 107 ASP A OD1 1 ATOM 418 O OD2 . ASP A 1 54 ? 29.082 39.994 45.047 1.00 23.40 ? 107 ASP A OD2 1 ATOM 419 N N . ILE A 1 55 ? 26.817 44.141 47.491 1.00 15.29 ? 108 ILE A N 1 ATOM 420 C CA . ILE A 1 55 ? 26.172 44.986 48.482 1.00 15.81 ? 108 ILE A CA 1 ATOM 421 C C . ILE A 1 55 ? 25.306 46.051 47.795 1.00 17.67 ? 108 ILE A C 1 ATOM 422 O O . ILE A 1 55 ? 24.182 46.319 48.230 1.00 14.77 ? 108 ILE A O 1 ATOM 423 C CB . ILE A 1 55 ? 27.232 45.591 49.424 1.00 16.66 ? 108 ILE A CB 1 ATOM 424 C CG1 . ILE A 1 55 ? 27.841 44.481 50.287 1.00 19.69 ? 108 ILE A CG1 1 ATOM 425 C CG2 . ILE A 1 55 ? 26.630 46.671 50.295 1.00 18.63 ? 108 ILE A CG2 1 ATOM 426 C CD1 . ILE A 1 55 ? 28.914 44.937 51.188 1.00 19.91 ? 108 ILE A CD1 1 ATOM 427 N N . LEU A 1 56 ? 25.794 46.637 46.706 1.00 17.53 ? 109 LEU A N 1 ATOM 428 C CA . LEU A 1 56 ? 24.964 47.592 45.950 1.00 19.67 ? 109 LEU A CA 1 ATOM 429 C C . LEU A 1 56 ? 23.664 46.947 45.485 1.00 16.95 ? 109 LEU A C 1 ATOM 430 O O . LEU A 1 56 ? 22.597 47.565 45.530 1.00 15.15 ? 109 LEU A O 1 ATOM 431 C CB . LEU A 1 56 ? 25.698 48.117 44.725 1.00 20.51 ? 109 LEU A CB 1 ATOM 432 C CG . LEU A 1 56 ? 26.722 49.208 44.946 1.00 25.55 ? 109 LEU A CG 1 ATOM 433 C CD1 . LEU A 1 56 ? 27.374 49.535 43.625 1.00 26.79 ? 109 LEU A CD1 1 ATOM 434 C CD2 . LEU A 1 56 ? 26.084 50.455 45.566 1.00 27.65 ? 109 LEU A CD2 1 ATOM 435 N N . ARG A 1 57 ? 23.757 45.702 45.027 1.00 12.17 ? 110 ARG A N 1 ATOM 436 C CA . ARG A 1 57 ? 22.569 44.964 44.621 1.00 13.03 ? 110 ARG A CA 1 ATOM 437 C C . ARG A 1 57 ? 21.633 44.748 45.795 1.00 17.29 ? 110 ARG A C 1 ATOM 438 O O . ARG A 1 57 ? 20.427 44.978 45.679 1.00 16.74 ? 110 ARG A O 1 ATOM 439 C CB . ARG A 1 57 ? 22.947 43.635 43.966 1.00 14.92 ? 110 ARG A CB 1 ATOM 440 C CG . ARG A 1 57 ? 23.760 43.825 42.709 1.00 19.89 ? 110 ARG A CG 1 ATOM 441 C CD . ARG A 1 57 ? 23.849 42.605 41.815 1.00 24.97 ? 110 ARG A CD 1 ATOM 442 N NE . ARG A 1 57 ? 24.342 42.985 40.491 1.00 26.04 ? 110 ARG A NE 1 ATOM 443 C CZ . ARG A 1 57 ? 24.852 42.142 39.612 1.00 28.83 ? 110 ARG A CZ 1 ATOM 444 N NH1 . ARG A 1 57 ? 24.941 40.847 39.904 1.00 25.55 ? 110 ARG A NH1 1 ATOM 445 N NH2 . ARG A 1 57 ? 25.278 42.590 38.439 1.00 31.21 ? 110 ARG A NH2 1 ATOM 446 N N . ASP A 1 58 ? 22.180 44.327 46.934 1.00 18.16 ? 111 ASP A N 1 ATOM 447 C CA . ASP A 1 58 ? 21.375 44.183 48.142 1.00 16.86 ? 111 ASP A CA 1 ATOM 448 C C . ASP A 1 58 ? 20.662 45.486 48.493 1.00 16.82 ? 111 ASP A C 1 ATOM 449 O O . ASP A 1 58 ? 19.501 45.479 48.886 1.00 16.86 ? 111 ASP A O 1 ATOM 450 C CB . ASP A 1 58 ? 22.240 43.732 49.317 1.00 17.13 ? 111 ASP A CB 1 ATOM 451 C CG . ASP A 1 58 ? 22.678 42.280 49.193 1.00 19.46 ? 111 ASP A CG 1 ATOM 452 O OD1 . ASP A 1 58 ? 23.476 41.834 50.034 1.00 20.06 ? 111 ASP A OD1 1 ATOM 453 O OD2 . ASP A 1 58 ? 22.275 41.516 48.297 1.00 14.07 ? 111 ASP A OD2 1 ATOM 454 N N . GLU A 1 59 ? 21.371 46.599 48.362 1.00 16.37 ? 112 GLU A N 1 ATOM 455 C CA . GLU A 1 59 ? 20.837 47.893 48.752 1.00 16.36 ? 112 GLU A CA 1 ATOM 456 C C . GLU A 1 59 ? 19.749 48.376 47.791 1.00 17.06 ? 112 GLU A C 1 ATOM 457 O O . GLU A 1 59 ? 18.811 49.062 48.204 1.00 15.34 ? 112 GLU A O 1 ATOM 458 C CB . GLU A 1 59 ? 21.968 48.918 48.881 1.00 14.13 ? 112 GLU A CB 1 ATOM 459 C CG . GLU A 1 59 ? 22.759 48.715 50.173 1.00 16.98 ? 112 GLU A CG 1 ATOM 460 C CD . GLU A 1 59 ? 24.039 49.532 50.278 1.00 19.43 ? 112 GLU A CD 1 ATOM 461 O OE1 . GLU A 1 59 ? 24.432 50.196 49.298 1.00 22.89 ? 112 GLU A OE1 1 ATOM 462 O OE2 . GLU A 1 59 ? 24.663 49.487 51.356 1.00 15.71 ? 112 GLU A OE2 1 ATOM 463 N N . LEU A 1 60 ? 19.863 47.996 46.525 1.00 14.39 ? 113 LEU A N 1 ATOM 464 C CA . LEU A 1 60 ? 18.840 48.320 45.538 1.00 14.23 ? 113 LEU A CA 1 ATOM 465 C C . LEU A 1 60 ? 17.548 47.586 45.864 1.00 17.70 ? 113 LEU A C 1 ATOM 466 O O . LEU A 1 60 ? 16.461 48.151 45.750 1.00 17.20 ? 113 LEU A O 1 ATOM 467 C CB . LEU A 1 60 ? 19.316 47.971 44.124 1.00 17.08 ? 113 LEU A CB 1 ATOM 468 C CG . LEU A 1 60 ? 18.333 48.391 43.023 1.00 18.16 ? 113 LEU A CG 1 ATOM 469 C CD1 . LEU A 1 60 ? 19.039 48.896 41.772 1.00 19.06 ? 113 LEU A CD1 1 ATOM 470 C CD2 . LEU A 1 60 ? 17.421 47.237 42.706 1.00 21.10 ? 113 LEU A CD2 1 ATOM 471 N N . GLU A 1 61 ? 17.664 46.331 46.287 1.00 17.53 ? 114 GLU A N 1 ATOM 472 C CA . GLU A 1 61 ? 16.483 45.561 46.673 1.00 15.70 ? 114 GLU A CA 1 ATOM 473 C C . GLU A 1 61 ? 15.714 46.269 47.795 1.00 16.49 ? 114 GLU A C 1 ATOM 474 O O . GLU A 1 61 ? 14.484 46.224 47.848 1.00 13.74 ? 114 GLU A O 1 ATOM 475 C CB . GLU A 1 61 ? 16.880 44.141 47.081 1.00 17.65 ? 114 GLU A CB 1 ATOM 476 C CG . GLU A 1 61 ? 17.467 43.340 45.930 1.00 15.58 ? 114 GLU A CG 1 ATOM 477 C CD . GLU A 1 61 ? 18.121 42.036 46.360 1.00 18.93 ? 114 GLU A CD 1 ATOM 478 O OE1 . GLU A 1 61 ? 18.235 41.782 47.572 1.00 17.93 ? 114 GLU A OE1 1 ATOM 479 O OE2 . GLU A 1 61 ? 18.496 41.251 45.467 1.00 18.81 ? 114 GLU A OE2 1 ATOM 480 N N . VAL A 1 62 ? 16.439 46.928 48.690 1.00 16.84 ? 115 VAL A N 1 ATOM 481 C CA . VAL A 1 62 ? 15.797 47.630 49.803 1.00 16.33 ? 115 VAL A CA 1 ATOM 482 C C . VAL A 1 62 ? 14.910 48.755 49.267 1.00 17.39 ? 115 VAL A C 1 ATOM 483 O O . VAL A 1 62 ? 13.805 48.976 49.779 1.00 17.10 ? 115 VAL A O 1 ATOM 484 C CB . VAL A 1 62 ? 16.836 48.224 50.790 1.00 14.91 ? 115 VAL A CB 1 ATOM 485 C CG1 . VAL A 1 62 ? 16.174 49.218 51.729 1.00 17.61 ? 115 VAL A CG1 1 ATOM 486 C CG2 . VAL A 1 62 ? 17.526 47.121 51.577 1.00 14.43 ? 115 VAL A CG2 1 ATOM 487 N N . VAL A 1 63 ? 15.380 49.438 48.220 1.00 14.80 ? 116 VAL A N 1 ATOM 488 C CA . VAL A 1 63 ? 14.575 50.448 47.536 1.00 17.86 ? 116 VAL A CA 1 ATOM 489 C C . VAL A 1 63 ? 13.325 49.854 46.897 1.00 16.28 ? 116 VAL A C 1 ATOM 490 O O . VAL A 1 63 ? 12.220 50.388 47.057 1.00 16.30 ? 116 VAL A O 1 ATOM 491 C CB . VAL A 1 63 ? 15.384 51.217 46.467 1.00 17.74 ? 116 VAL A CB 1 ATOM 492 C CG1 . VAL A 1 63 ? 14.493 52.244 45.753 1.00 17.57 ? 116 VAL A CG1 1 ATOM 493 C CG2 . VAL A 1 63 ? 16.577 51.928 47.099 1.00 19.57 ? 116 VAL A CG2 1 ATOM 494 N N . LEU A 1 64 ? 13.498 48.743 46.192 1.00 14.32 ? 117 LEU A N 1 ATOM 495 C CA . LEU A 1 64 ? 12.392 48.059 45.548 1.00 15.28 ? 117 LEU A CA 1 ATOM 496 C C . LEU A 1 64 ? 11.306 47.699 46.563 1.00 18.23 ? 117 LEU A C 1 ATOM 497 O O . LEU A 1 64 ? 10.118 47.898 46.300 1.00 14.02 ? 117 LEU A O 1 ATOM 498 C CB . LEU A 1 64 ? 12.878 46.789 44.843 1.00 18.82 ? 117 LEU A CB 1 ATOM 499 C CG . LEU A 1 64 ? 13.897 46.975 43.715 1.00 20.41 ? 117 LEU A CG 1 ATOM 500 C CD1 . LEU A 1 64 ? 13.980 45.708 42.881 1.00 22.52 ? 117 LEU A CD1 1 ATOM 501 C CD2 . LEU A 1 64 ? 13.552 48.181 42.857 1.00 19.20 ? 117 LEU A CD2 1 ATOM 502 N N . LYS A 1 65 ? 11.710 47.158 47.713 1.00 17.19 ? 118 LYS A N 1 ATOM 503 C CA . LYS A 1 65 ? 10.760 46.853 48.790 1.00 13.93 ? 118 LYS A CA 1 ATOM 504 C C . LYS A 1 65 ? 9.959 48.110 49.163 1.00 14.92 ? 118 LYS A C 1 ATOM 505 O O . LYS A 1 65 ? 8.739 48.069 49.275 1.00 16.68 ? 118 LYS A O 1 ATOM 506 C CB . LYS A 1 65 ? 11.503 46.303 50.018 1.00 18.82 ? 118 LYS A CB 1 ATOM 507 C CG . LYS A 1 65 ? 10.620 46.007 51.236 1.00 23.12 ? 118 LYS A CG 1 ATOM 508 C CD . LYS A 1 65 ? 11.453 45.704 52.489 1.00 25.87 ? 118 LYS A CD 1 ATOM 509 C CE . LYS A 1 65 ? 10.567 45.131 53.602 1.00 31.00 ? 118 LYS A CE 1 ATOM 510 N NZ . LYS A 1 65 ? 10.907 45.671 54.948 1.00 39.41 ? 118 LYS A NZ 1 ATOM 511 N N . ASP A 1 66 ? 10.651 49.222 49.360 1.00 15.60 ? 119 ASP A N 1 ATOM 512 C CA . ASP A 1 66 ? 10.006 50.456 49.779 1.00 19.22 ? 119 ASP A CA 1 ATOM 513 C C . ASP A 1 66 ? 8.959 50.895 48.752 1.00 20.28 ? 119 ASP A C 1 ATOM 514 O O . ASP A 1 66 ? 7.873 51.350 49.127 1.00 22.10 ? 119 ASP A O 1 ATOM 515 C CB . ASP A 1 66 ? 11.034 51.564 49.941 1.00 23.47 ? 119 ASP A CB 1 ATOM 516 C CG . ASP A 1 66 ? 11.854 51.427 51.204 1.00 32.85 ? 119 ASP A CG 1 ATOM 517 O OD1 . ASP A 1 66 ? 11.491 50.611 52.087 1.00 34.58 ? 119 ASP A OD1 1 ATOM 518 O OD2 . ASP A 1 66 ? 12.887 52.106 51.392 1.00 35.71 ? 119 ASP A OD2 1 ATOM 519 N N . VAL A 1 67 ? 9.275 50.766 47.463 1.00 17.82 ? 120 VAL A N 1 ATOM 520 C CA . VAL A 1 67 ? 8.398 51.326 46.432 1.00 18.74 ? 120 VAL A CA 1 ATOM 521 C C . VAL A 1 67 ? 7.329 50.332 46.005 1.00 20.56 ? 120 VAL A C 1 ATOM 522 O O . VAL A 1 67 ? 6.355 50.726 45.373 1.00 23.50 ? 120 VAL A O 1 ATOM 523 C CB . VAL A 1 67 ? 9.154 51.817 45.162 1.00 17.81 ? 120 VAL A CB 1 ATOM 524 C CG1 . VAL A 1 67 ? 10.190 52.861 45.510 1.00 20.32 ? 120 VAL A CG1 1 ATOM 525 C CG2 . VAL A 1 67 ? 9.771 50.651 44.388 1.00 18.63 ? 120 VAL A CG2 1 ATOM 526 N N . LEU A 1 68 ? 7.493 49.055 46.347 1.00 16.76 ? 121 LEU A N 1 ATOM 527 C CA . LEU A 1 68 ? 6.481 48.061 45.987 1.00 17.57 ? 121 LEU A CA 1 ATOM 528 C C . LEU A 1 68 ? 5.469 47.758 47.093 1.00 17.90 ? 121 LEU A C 1 ATOM 529 O O . LEU A 1 68 ? 4.358 47.316 46.805 1.00 22.34 ? 121 LEU A O 1 ATOM 530 C CB . LEU A 1 68 ? 7.132 46.764 45.536 1.00 16.89 ? 121 LEU A CB 1 ATOM 531 C CG . LEU A 1 68 ? 7.934 46.923 44.258 1.00 18.18 ? 121 LEU A CG 1 ATOM 532 C CD1 . LEU A 1 68 ? 8.744 45.693 43.999 1.00 18.68 ? 121 LEU A CD1 1 ATOM 533 C CD2 . LEU A 1 68 ? 6.994 47.223 43.105 1.00 21.02 ? 121 LEU A CD2 1 ATOM 534 N N . GLN A 1 69 ? 5.846 47.954 48.348 1.00 20.04 ? 122 GLN A N 1 ATOM 535 C CA . GLN A 1 69 ? 5.132 47.296 49.437 1.00 21.10 ? 122 GLN A CA 1 ATOM 536 C C . GLN A 1 69 ? 3.901 48.082 49.907 1.00 22.77 ? 122 GLN A C 1 ATOM 537 O O . GLN A 1 69 ? 3.110 47.574 50.700 1.00 24.77 ? 122 GLN A O 1 ATOM 538 C CB . GLN A 1 69 ? 6.064 47.032 50.630 1.00 19.52 ? 122 GLN A CB 1 ATOM 539 C CG . GLN A 1 69 ? 6.552 48.286 51.364 1.00 16.63 ? 122 GLN A CG 1 ATOM 540 C CD . GLN A 1 69 ? 7.494 47.970 52.535 1.00 18.96 ? 122 GLN A CD 1 ATOM 541 O OE1 . GLN A 1 69 ? 7.732 46.806 52.860 1.00 19.07 ? 122 GLN A OE1 1 ATOM 542 N NE2 . GLN A 1 69 ? 8.016 49.010 53.169 1.00 18.27 ? 122 GLN A NE2 1 ATOM 543 N N . GLU A 1 70 ? 3.748 49.318 49.443 1.00 26.42 ? 123 GLU A N 1 ATOM 544 C CA . GLU A 1 70 ? 2.615 50.145 49.879 1.00 30.79 ? 123 GLU A CA 1 ATOM 545 C C . GLU A 1 70 ? 1.805 50.652 48.693 1.00 25.58 ? 123 GLU A C 1 ATOM 546 O O . GLU A 1 70 ? 2.314 51.397 47.856 1.00 20.33 ? 123 GLU A O 1 ATOM 547 C CB . GLU A 1 70 ? 3.107 51.336 50.713 1.00 37.45 ? 123 GLU A CB 1 ATOM 548 C CG . GLU A 1 70 ? 2.564 51.379 52.139 1.00 42.65 ? 123 GLU A CG 1 ATOM 549 C CD . GLU A 1 70 ? 2.722 52.747 52.789 1.00 46.62 ? 123 GLU A CD 1 ATOM 550 O OE1 . GLU A 1 70 ? 3.718 52.955 53.524 1.00 52.18 ? 123 GLU A OE1 1 ATOM 551 O OE2 . GLU A 1 70 ? 1.854 53.618 52.565 1.00 47.91 ? 123 GLU A OE2 1 ATOM 552 N N . PRO A 1 71 ? 0.545 50.245 48.623 1.00 28.15 ? 124 PRO A N 1 ATOM 553 C CA . PRO A 1 71 ? -0.413 50.843 47.686 1.00 27.86 ? 124 PRO A CA 1 ATOM 554 C C . PRO A 1 71 ? -0.485 52.352 47.856 1.00 27.32 ? 124 PRO A C 1 ATOM 555 O O . PRO A 1 71 ? -0.426 52.839 48.982 1.00 27.50 ? 124 PRO A O 1 ATOM 556 C CB . PRO A 1 71 ? -1.740 50.190 48.077 1.00 29.43 ? 124 PRO A CB 1 ATOM 557 C CG . PRO A 1 71 ? -1.346 48.891 48.704 1.00 31.06 ? 124 PRO A CG 1 ATOM 558 C CD . PRO A 1 71 ? -0.059 49.161 49.415 1.00 29.52 ? 124 PRO A CD 1 ATOM 559 N N . LYS A 1 72 ? -0.573 53.074 46.748 1.00 28.18 ? 125 LYS A N 1 ATOM 560 C CA . LYS A 1 72 ? -0.846 54.509 46.775 1.00 33.53 ? 125 LYS A CA 1 ATOM 561 C C . LYS A 1 72 ? -2.002 54.815 45.829 1.00 32.51 ? 125 LYS A C 1 ATOM 562 O O . LYS A 1 72 ? -2.133 54.186 44.786 1.00 30.02 ? 125 LYS A O 1 ATOM 563 C CB . LYS A 1 72 ? 0.390 55.302 46.352 1.00 34.67 ? 125 LYS A CB 1 ATOM 564 C CG . LYS A 1 72 ? 1.384 55.559 47.478 1.00 41.86 ? 125 LYS A CG 1 ATOM 565 C CD . LYS A 1 72 ? 1.728 57.042 47.610 1.00 44.98 ? 125 LYS A CD 1 ATOM 566 C CE . LYS A 1 72 ? 2.452 57.351 48.930 1.00 46.84 ? 125 LYS A CE 1 ATOM 567 N NZ . LYS A 1 72 ? 3.623 58.278 48.750 1.00 47.26 ? 125 LYS A NZ 1 ATOM 568 N N . THR A 1 73 ? -2.836 55.783 46.193 1.00 35.82 ? 126 THR A N 1 ATOM 569 C CA . THR A 1 73 ? -4.164 55.900 45.592 1.00 35.47 ? 126 THR A CA 1 ATOM 570 C C . THR A 1 73 ? -4.042 56.310 44.124 1.00 32.79 ? 126 THR A C 1 ATOM 571 O O . THR A 1 73 ? -4.895 55.976 43.308 1.00 35.13 ? 126 THR A O 1 ATOM 572 C CB . THR A 1 73 ? -5.032 56.917 46.380 1.00 37.12 ? 126 THR A CB 1 ATOM 573 O OG1 . THR A 1 73 ? -5.526 56.319 47.588 1.00 38.74 ? 126 THR A OG1 1 ATOM 574 C CG2 . THR A 1 73 ? -6.297 57.264 45.618 1.00 38.83 ? 126 THR A CG2 1 ATOM 575 N N . GLU A 1 74 ? -2.970 57.017 43.787 1.00 33.52 ? 127 GLU A N 1 ATOM 576 C CA . GLU A 1 74 ? -2.814 57.561 42.438 1.00 38.83 ? 127 GLU A CA 1 ATOM 577 C C . GLU A 1 74 ? -2.131 56.587 41.483 1.00 33.32 ? 127 GLU A C 1 ATOM 578 O O . GLU A 1 74 ? -1.939 56.909 40.309 1.00 31.91 ? 127 GLU A O 1 ATOM 579 C CB . GLU A 1 74 ? -2.019 58.869 42.473 1.00 43.03 ? 127 GLU A CB 1 ATOM 580 C CG . GLU A 1 74 ? -0.585 58.723 42.958 1.00 47.37 ? 127 GLU A CG 1 ATOM 581 C CD . GLU A 1 74 ? 0.319 58.023 41.956 1.00 53.22 ? 127 GLU A CD 1 ATOM 582 O OE1 . GLU A 1 74 ? 0.988 57.039 42.352 1.00 53.66 ? 127 GLU A OE1 1 ATOM 583 O OE2 . GLU A 1 74 ? 0.373 58.458 40.778 1.00 56.26 ? 127 GLU A OE2 1 ATOM 584 N N . ASP A 1 75 ? -1.771 55.405 41.987 1.00 30.46 ? 128 ASP A N 1 ATOM 585 C CA . ASP A 1 75 ? -1.062 54.404 41.186 1.00 25.86 ? 128 ASP A CA 1 ATOM 586 C C . ASP A 1 75 ? -1.818 54.085 39.904 1.00 24.15 ? 128 ASP A C 1 ATOM 587 O O . ASP A 1 75 ? -2.958 53.624 39.944 1.00 22.25 ? 128 ASP A O 1 ATOM 588 C CB . ASP A 1 75 ? -0.891 53.108 41.974 1.00 24.43 ? 128 ASP A CB 1 ATOM 589 C CG . ASP A 1 75 ? 0.217 53.176 42.996 1.00 23.66 ? 128 ASP A CG 1 ATOM 590 O OD1 . ASP A 1 75 ? 0.993 54.155 43.016 1.00 23.91 ? 128 ASP A OD1 1 ATOM 591 O OD2 . ASP A 1 75 ? 0.395 52.274 43.824 1.00 25.99 ? 128 ASP A OD2 1 ATOM 592 N N . ILE A 1 76 ? -1.175 54.323 38.767 1.00 23.52 ? 129 ILE A N 1 ATOM 593 C CA . ILE A 1 76 ? -1.670 53.823 37.492 1.00 26.17 ? 129 ILE A CA 1 ATOM 594 C C . ILE A 1 76 ? -1.598 52.305 37.459 1.00 27.42 ? 129 ILE A C 1 ATOM 595 O O . ILE A 1 76 ? -0.918 51.695 38.279 1.00 24.70 ? 129 ILE A O 1 ATOM 596 C CB . ILE A 1 76 ? -0.844 54.417 36.361 1.00 26.48 ? 129 ILE A CB 1 ATOM 597 C CG1 . ILE A 1 76 ? 0.592 53.885 36.434 1.00 25.91 ? 129 ILE A CG1 1 ATOM 598 C CG2 . ILE A 1 76 ? -0.861 55.950 36.458 1.00 26.79 ? 129 ILE A CG2 1 ATOM 599 C CD1 . ILE A 1 76 ? 1.436 54.285 35.275 1.00 25.33 ? 129 ILE A CD1 1 ATOM 600 N N . VAL A 1 77 ? -2.310 51.703 36.514 1.00 23.85 ? 130 VAL A N 1 ATOM 601 C CA . VAL A 1 77 ? -2.578 50.272 36.544 1.00 22.09 ? 130 VAL A CA 1 ATOM 602 C C . VAL A 1 77 ? -1.276 49.479 36.447 1.00 22.07 ? 130 VAL A C 1 ATOM 603 O O . VAL A 1 77 ? -1.137 48.448 37.081 1.00 22.67 ? 130 VAL A O 1 ATOM 604 C CB . VAL A 1 77 ? -3.519 49.842 35.395 1.00 19.84 ? 130 VAL A CB 1 ATOM 605 C CG1 . VAL A 1 77 ? -3.438 48.354 35.166 1.00 20.33 ? 130 VAL A CG1 1 ATOM 606 C CG2 . VAL A 1 77 ? -4.960 50.235 35.709 1.00 22.74 ? 130 VAL A CG2 1 ATOM 607 N N . ALA A 1 78 ? -0.326 49.965 35.661 1.00 22.12 ? 131 ALA A N 1 ATOM 608 C CA . ALA A 1 78 ? 0.960 49.286 35.535 1.00 21.59 ? 131 ALA A CA 1 ATOM 609 C C . ALA A 1 78 ? 1.615 49.123 36.911 1.00 20.98 ? 131 ALA A C 1 ATOM 610 O O . ALA A 1 78 ? 2.211 48.092 37.213 1.00 20.07 ? 131 ALA A O 1 ATOM 611 C CB . ALA A 1 78 ? 1.871 50.048 34.607 1.00 21.57 ? 131 ALA A CB 1 ATOM 612 N N . VAL A 1 79 ? 1.510 50.144 37.743 1.00 18.63 ? 132 VAL A N 1 ATOM 613 C CA . VAL A 1 79 ? 2.134 50.076 39.054 1.00 24.54 ? 132 VAL A CA 1 ATOM 614 C C . VAL A 1 79 ? 1.299 49.207 39.993 1.00 25.17 ? 132 VAL A C 1 ATOM 615 O O . VAL A 1 79 ? 1.846 48.387 40.730 1.00 20.83 ? 132 VAL A O 1 ATOM 616 C CB . VAL A 1 79 ? 2.358 51.469 39.653 1.00 24.21 ? 132 VAL A CB 1 ATOM 617 C CG1 . VAL A 1 79 ? 2.469 51.404 41.156 1.00 25.59 ? 132 VAL A CG1 1 ATOM 618 C CG2 . VAL A 1 79 ? 3.602 52.115 39.061 1.00 25.49 ? 132 VAL A CG2 1 ATOM 619 N N . GLN A 1 80 ? -0.021 49.353 39.937 1.00 23.18 ? 133 GLN A N 1 ATOM 620 C CA . GLN A 1 80 ? -0.914 48.480 40.696 1.00 22.66 ? 133 GLN A CA 1 ATOM 621 C C . GLN A 1 80 ? -0.630 47.028 40.384 1.00 21.41 ? 133 GLN A C 1 ATOM 622 O O . GLN A 1 80 ? -0.744 46.162 41.250 1.00 17.39 ? 133 GLN A O 1 ATOM 623 C CB . GLN A 1 80 ? -2.382 48.773 40.375 1.00 23.46 ? 133 GLN A CB 1 ATOM 624 C CG . GLN A 1 80 ? -2.863 50.131 40.819 1.00 22.31 ? 133 GLN A CG 1 ATOM 625 C CD . GLN A 1 80 ? -4.257 50.431 40.313 1.00 27.74 ? 133 GLN A CD 1 ATOM 626 O OE1 . GLN A 1 80 ? -5.136 49.571 40.375 1.00 29.43 ? 133 GLN A OE1 1 ATOM 627 N NE2 . GLN A 1 80 ? -4.461 51.639 39.795 1.00 23.89 ? 133 GLN A NE2 1 ATOM 628 N N . LYS A 1 81 ? -0.293 46.751 39.130 1.00 16.75 ? 134 LYS A N 1 ATOM 629 C CA . LYS A 1 81 ? -0.117 45.369 38.702 1.00 18.32 ? 134 LYS A CA 1 ATOM 630 C C . LYS A 1 81 ? 1.184 44.797 39.245 1.00 20.63 ? 134 LYS A C 1 ATOM 631 O O . LYS A 1 81 ? 1.268 43.605 39.533 1.00 21.86 ? 134 LYS A O 1 ATOM 632 C CB . LYS A 1 81 ? -0.142 45.236 37.175 1.00 22.93 ? 134 LYS A CB 1 ATOM 633 C CG . LYS A 1 81 ? -1.552 45.021 36.617 1.00 19.92 ? 134 LYS A CG 1 ATOM 634 C CD . LYS A 1 81 ? -1.565 44.913 35.095 1.00 22.30 ? 134 LYS A CD 1 ATOM 635 C CE . LYS A 1 81 ? -3.000 44.841 34.553 1.00 20.64 ? 134 LYS A CE 1 ATOM 636 N NZ . LYS A 1 81 ? -3.009 44.753 33.049 1.00 22.67 ? 134 LYS A NZ 1 ATOM 637 N N . ALA A 1 82 ? 2.195 45.647 39.387 1.00 18.70 ? 135 ALA A N 1 ATOM 638 C CA . ALA A 1 82 ? 3.483 45.201 39.915 1.00 21.89 ? 135 ALA A CA 1 ATOM 639 C C . ALA A 1 82 ? 3.375 45.019 41.422 1.00 17.86 ? 135 ALA A C 1 ATOM 640 O O . ALA A 1 82 ? 3.892 44.056 41.975 1.00 17.55 ? 135 ALA A O 1 ATOM 641 C CB . ALA A 1 82 ? 4.567 46.210 39.579 1.00 21.72 ? 135 ALA A CB 1 ATOM 642 N N . LYS A 1 83 ? 2.680 45.935 42.089 1.00 17.53 ? 136 LYS A N 1 ATOM 643 C CA . LYS A 1 83 ? 2.451 45.786 43.533 1.00 19.30 ? 136 LYS A CA 1 ATOM 644 C C . LYS A 1 83 ? 1.614 44.564 43.890 1.00 20.75 ? 136 LYS A C 1 ATOM 645 O O . LYS A 1 83 ? 1.879 43.877 44.887 1.00 16.17 ? 136 LYS A O 1 ATOM 646 C CB . LYS A 1 83 ? 1.847 47.064 44.119 1.00 18.58 ? 136 LYS A CB 1 ATOM 647 C CG . LYS A 1 83 ? 2.842 48.235 44.127 1.00 18.23 ? 136 LYS A CG 1 ATOM 648 C CD . LYS A 1 83 ? 2.268 49.509 44.735 1.00 20.77 ? 136 LYS A CD 1 ATOM 649 C CE . LYS A 1 83 ? 3.213 50.681 44.545 1.00 19.13 ? 136 LYS A CE 1 ATOM 650 N NZ . LYS A 1 83 ? 2.843 51.853 45.369 1.00 18.58 ? 136 LYS A NZ 1 ATOM 651 N N . ALA A 1 84 ? 0.613 44.258 43.074 1.00 21.00 ? 137 ALA A N 1 ATOM 652 C CA . ALA A 1 84 ? -0.173 43.055 43.299 1.00 20.31 ? 137 ALA A CA 1 ATOM 653 C C . ALA A 1 84 ? 0.689 41.806 43.063 1.00 19.76 ? 137 ALA A C 1 ATOM 654 O O . ALA A 1 84 ? 0.555 40.788 43.737 1.00 17.54 ? 137 ALA A O 1 ATOM 655 C CB . ALA A 1 84 ? -1.387 43.047 42.383 1.00 24.16 ? 137 ALA A CB 1 ATOM 656 N N . LEU A 1 85 ? 1.567 41.879 42.086 1.00 19.61 ? 138 LEU A N 1 ATOM 657 C CA . LEU A 1 85 ? 2.414 40.747 41.782 1.00 18.62 ? 138 LEU A CA 1 ATOM 658 C C . LEU A 1 85 ? 3.340 40.518 42.970 1.00 18.21 ? 138 LEU A C 1 ATOM 659 O O . LEU A 1 85 ? 3.469 39.403 43.457 1.00 16.33 ? 138 LEU A O 1 ATOM 660 C CB . LEU A 1 85 ? 3.236 41.035 40.530 1.00 18.48 ? 138 LEU A CB 1 ATOM 661 C CG . LEU A 1 85 ? 4.221 39.934 40.159 1.00 16.77 ? 138 LEU A CG 1 ATOM 662 C CD1 . LEU A 1 85 ? 3.547 38.566 40.100 1.00 19.26 ? 138 LEU A CD1 1 ATOM 663 C CD2 . LEU A 1 85 ? 4.887 40.267 38.833 1.00 16.08 ? 138 LEU A CD2 1 ATOM 664 N N . TYR A 1 86 ? 3.957 41.600 43.433 1.00 20.08 ? 139 TYR A N 1 ATOM 665 C CA . TYR A 1 86 ? 4.732 41.589 44.679 1.00 19.01 ? 139 TYR A CA 1 ATOM 666 C C . TYR A 1 86 ? 3.971 40.937 45.837 1.00 16.44 ? 139 TYR A C 1 ATOM 667 O O . TYR A 1 86 ? 4.487 40.041 46.528 1.00 17.08 ? 139 TYR A O 1 ATOM 668 C CB . TYR A 1 86 ? 5.114 43.017 45.060 1.00 16.09 ? 139 TYR A CB 1 ATOM 669 C CG . TYR A 1 86 ? 5.998 43.072 46.285 1.00 18.47 ? 139 TYR A CG 1 ATOM 670 C CD1 . TYR A 1 86 ? 7.326 42.671 46.221 1.00 17.62 ? 139 TYR A CD1 1 ATOM 671 C CD2 . TYR A 1 86 ? 5.502 43.496 47.504 1.00 17.26 ? 139 TYR A CD2 1 ATOM 672 C CE1 . TYR A 1 86 ? 8.133 42.712 47.331 1.00 16.25 ? 139 TYR A CE1 1 ATOM 673 C CE2 . TYR A 1 86 ? 6.305 43.549 48.621 1.00 20.19 ? 139 TYR A CE2 1 ATOM 674 C CZ . TYR A 1 86 ? 7.616 43.141 48.534 1.00 16.25 ? 139 TYR A CZ 1 ATOM 675 O OH . TYR A 1 86 ? 8.428 43.167 49.642 1.00 18.73 ? 139 TYR A OH 1 ATOM 676 N N . ARG A 1 87 ? 2.747 41.408 46.067 1.00 15.67 ? 140 ARG A N 1 ATOM 677 C CA . ARG A 1 87 ? 1.981 40.961 47.210 1.00 19.12 ? 140 ARG A CA 1 ATOM 678 C C . ARG A 1 87 ? 1.703 39.472 47.132 1.00 17.41 ? 140 ARG A C 1 ATOM 679 O O . ARG A 1 87 ? 1.720 38.807 48.147 1.00 16.95 ? 140 ARG A O 1 ATOM 680 C CB . ARG A 1 87 ? 0.684 41.768 47.350 1.00 20.70 ? 140 ARG A CB 1 ATOM 681 C CG . ARG A 1 87 ? 0.900 43.102 48.020 1.00 21.46 ? 140 ARG A CG 1 ATOM 682 C CD . ARG A 1 87 ? -0.378 43.841 48.405 1.00 23.98 ? 140 ARG A CD 1 ATOM 683 N NE . ARG A 1 87 ? -1.369 43.826 47.331 1.00 23.41 ? 140 ARG A NE 1 ATOM 684 C CZ . ARG A 1 87 ? -1.520 44.795 46.451 1.00 22.53 ? 140 ARG A CZ 1 ATOM 685 N NH1 . ARG A 1 87 ? -0.753 45.880 46.505 1.00 22.22 ? 140 ARG A NH1 1 ATOM 686 N NH2 . ARG A 1 87 ? -2.454 44.687 45.522 1.00 23.85 ? 140 ARG A NH2 1 ATOM 687 N N . SER A 1 88 ? 1.453 38.958 45.930 1.00 18.47 ? 141 SER A N 1 ATOM 688 C CA . SER A 1 88 ? 1.096 37.554 45.739 1.00 16.89 ? 141 SER A CA 1 ATOM 689 C C . SER A 1 88 ? 2.308 36.680 46.007 1.00 20.00 ? 141 SER A C 1 ATOM 690 O O . SER A 1 88 ? 2.191 35.534 46.431 1.00 20.84 ? 141 SER A O 1 ATOM 691 C CB . SER A 1 88 ? 0.587 37.314 44.314 1.00 18.97 ? 141 SER A CB 1 ATOM 692 O OG . SER A 1 88 ? 1.647 37.240 43.370 1.00 20.24 ? 141 SER A OG 1 ATOM 693 N N . CYS A 1 89 ? 3.478 37.255 45.772 1.00 18.83 ? 142 CYS A N 1 ATOM 694 C CA . CYS A 1 89 ? 4.732 36.528 45.903 1.00 20.47 ? 142 CYS A CA 1 ATOM 695 C C . CYS A 1 89 ? 5.176 36.430 47.358 1.00 17.32 ? 142 CYS A C 1 ATOM 696 O O . CYS A 1 89 ? 5.757 35.425 47.770 1.00 20.02 ? 142 CYS A O 1 ATOM 697 C CB . CYS A 1 89 ? 5.791 37.217 45.043 1.00 18.32 ? 142 CYS A CB 1 ATOM 698 S SG . CYS A 1 89 ? 7.413 36.456 45.059 1.00 18.70 ? 142 CYS A SG 1 ATOM 699 N N . ILE A 1 90 ? 4.892 37.454 48.150 1.00 19.01 ? 143 ILE A N 1 ATOM 700 C CA . ILE A 1 90 ? 5.349 37.446 49.529 1.00 22.36 ? 143 ILE A CA 1 ATOM 701 C C . ILE A 1 90 ? 4.324 36.800 50.468 1.00 20.07 ? 143 ILE A C 1 ATOM 702 O O . ILE A 1 90 ? 4.598 36.623 51.650 1.00 22.76 ? 143 ILE A O 1 ATOM 703 C CB . ILE A 1 90 ? 5.720 38.859 50.015 1.00 21.72 ? 143 ILE A CB 1 ATOM 704 C CG1 . ILE A 1 90 ? 4.497 39.777 50.057 1.00 21.34 ? 143 ILE A CG1 1 ATOM 705 C CG2 . ILE A 1 90 ? 6.803 39.468 49.132 1.00 23.24 ? 143 ILE A CG2 1 ATOM 706 C CD1 . ILE A 1 90 ? 4.674 40.988 50.954 1.00 25.33 ? 143 ILE A CD1 1 ATOM 707 N N . ASN A 1 91 ? 3.155 36.434 49.952 1.00 18.81 ? 144 ASN A N 1 ATOM 708 C CA . ASN A 1 91 ? 2.170 35.758 50.804 1.00 20.82 ? 144 ASN A CA 1 ATOM 709 C C . ASN A 1 91 ? 2.448 34.251 50.904 1.00 17.20 ? 144 ASN A C 1 ATOM 710 O O . ASN A 1 91 ? 1.891 33.461 50.161 1.00 18.06 ? 144 ASN A O 1 ATOM 711 C CB . ASN A 1 91 ? 0.749 36.024 50.313 1.00 22.22 ? 144 ASN A CB 1 ATOM 712 C CG . ASN A 1 91 ? -0.312 35.723 51.375 1.00 26.32 ? 144 ASN A CG 1 ATOM 713 O OD1 . ASN A 1 91 ? -0.122 34.861 52.247 1.00 24.51 ? 144 ASN A OD1 1 ATOM 714 N ND2 . ASN A 1 91 ? -1.433 36.446 51.304 1.00 30.73 ? 144 ASN A ND2 1 ATOM 715 N N . GLU A 1 92 ? 3.328 33.871 51.822 1.00 21.43 ? 145 GLU A N 1 ATOM 716 C CA . GLU A 1 92 ? 3.787 32.487 51.928 1.00 27.41 ? 145 GLU A CA 1 ATOM 717 C C . GLU A 1 92 ? 2.683 31.587 52.477 1.00 24.81 ? 145 GLU A C 1 ATOM 718 O O . GLU A 1 92 ? 2.659 30.386 52.206 1.00 24.56 ? 145 GLU A O 1 ATOM 719 C CB . GLU A 1 92 ? 5.032 32.373 52.820 1.00 31.14 ? 145 GLU A CB 1 ATOM 720 C CG . GLU A 1 92 ? 6.088 33.441 52.587 1.00 37.56 ? 145 GLU A CG 1 ATOM 721 C CD . GLU A 1 92 ? 7.423 33.114 53.243 1.00 43.39 ? 145 GLU A CD 1 ATOM 722 O OE1 . GLU A 1 92 ? 8.200 34.057 53.510 1.00 46.61 ? 145 GLU A OE1 1 ATOM 723 O OE2 . GLU A 1 92 ? 7.704 31.918 53.488 1.00 46.88 ? 145 GLU A OE2 1 ATOM 724 N N . SER A 1 93 ? 1.771 32.169 53.247 1.00 27.09 ? 146 SER A N 1 ATOM 725 C CA . SER A 1 93 ? 0.669 31.406 53.809 1.00 28.39 ? 146 SER A CA 1 ATOM 726 C C . SER A 1 93 ? -0.230 30.893 52.698 1.00 26.64 ? 146 SER A C 1 ATOM 727 O O . SER A 1 93 ? -0.588 29.708 52.656 1.00 23.41 ? 146 SER A O 1 ATOM 728 C CB . SER A 1 93 ? -0.142 32.271 54.773 1.00 33.20 ? 146 SER A CB 1 ATOM 729 O OG . SER A 1 93 ? -1.176 32.962 54.092 1.00 39.46 ? 146 SER A OG 1 ATOM 730 N N . ALA A 1 94 ? -0.596 31.790 51.792 1.00 23.50 ? 147 ALA A N 1 ATOM 731 C CA . ALA A 1 94 ? -1.399 31.419 50.635 1.00 23.08 ? 147 ALA A CA 1 ATOM 732 C C . ALA A 1 94 ? -0.705 30.354 49.777 1.00 25.81 ? 147 ALA A C 1 ATOM 733 O O . ALA A 1 94 ? -1.344 29.424 49.286 1.00 23.00 ? 147 ALA A O 1 ATOM 734 C CB . ALA A 1 94 ? -1.718 32.658 49.810 1.00 23.04 ? 147 ALA A CB 1 ATOM 735 N N . ILE A 1 95 ? 0.606 30.483 49.601 1.00 22.41 ? 148 ILE A N 1 ATOM 736 C CA . ILE A 1 95 ? 1.355 29.509 48.815 1.00 23.15 ? 148 ILE A CA 1 ATOM 737 C C . ILE A 1 95 ? 1.440 28.157 49.532 1.00 18.24 ? 148 ILE A C 1 ATOM 738 O O . ILE A 1 95 ? 1.161 27.122 48.938 1.00 24.22 ? 148 ILE A O 1 ATOM 739 C CB . ILE A 1 95 ? 2.760 30.053 48.480 1.00 20.68 ? 148 ILE A CB 1 ATOM 740 C CG1 . ILE A 1 95 ? 2.639 31.214 47.483 1.00 19.66 ? 148 ILE A CG1 1 ATOM 741 C CG2 . ILE A 1 95 ? 3.653 28.945 47.932 1.00 21.74 ? 148 ILE A CG2 1 ATOM 742 C CD1 . ILE A 1 95 ? 3.832 32.149 47.488 1.00 21.55 ? 148 ILE A CD1 1 ATOM 743 N N . ASP A 1 96 ? 1.815 28.163 50.807 1.00 20.96 ? 149 ASP A N 1 ATOM 744 C CA . ASP A 1 96 ? 1.949 26.909 51.542 1.00 21.42 ? 149 ASP A CA 1 ATOM 745 C C . ASP A 1 96 ? 0.623 26.154 51.548 1.00 24.08 ? 149 ASP A C 1 ATOM 746 O O . ASP A 1 96 ? 0.595 24.930 51.511 1.00 21.55 ? 149 ASP A O 1 ATOM 747 C CB . ASP A 1 96 ? 2.422 27.165 52.974 1.00 23.88 ? 149 ASP A CB 1 ATOM 748 C CG . ASP A 1 96 ? 3.914 27.407 53.057 1.00 24.30 ? 149 ASP A CG 1 ATOM 749 O OD1 . ASP A 1 96 ? 4.374 27.969 54.072 1.00 28.71 ? 149 ASP A OD1 1 ATOM 750 O OD2 . ASP A 1 96 ? 4.706 27.058 52.151 1.00 30.09 ? 149 ASP A OD2 1 ATOM 751 N N . SER A 1 97 ? -0.476 26.898 51.582 1.00 22.21 ? 150 SER A N 1 ATOM 752 C CA . SER A 1 97 ? -1.802 26.296 51.657 1.00 29.42 ? 150 SER A CA 1 ATOM 753 C C . SER A 1 97 ? -2.131 25.488 50.398 1.00 29.03 ? 150 SER A C 1 ATOM 754 O O . SER A 1 97 ? -2.984 24.599 50.427 1.00 31.61 ? 150 SER A O 1 ATOM 755 C CB . SER A 1 97 ? -2.855 27.391 51.891 1.00 29.19 ? 150 SER A CB 1 ATOM 756 O OG . SER A 1 97 ? -4.165 26.874 51.825 1.00 39.61 ? 150 SER A OG 1 ATOM 757 N N . ARG A 1 98 ? -1.463 25.787 49.287 1.00 26.64 ? 151 ARG A N 1 ATOM 758 C CA . ARG A 1 98 ? -1.807 25.129 48.031 1.00 26.12 ? 151 ARG A CA 1 ATOM 759 C C . ARG A 1 98 ? -0.994 23.846 47.791 1.00 26.07 ? 151 ARG A C 1 ATOM 760 O O . ARG A 1 98 ? -1.241 23.102 46.831 1.00 25.61 ? 151 ARG A O 1 ATOM 761 C CB . ARG A 1 98 ? -1.674 26.109 46.866 1.00 25.33 ? 151 ARG A CB 1 ATOM 762 C CG . ARG A 1 98 ? -2.705 27.226 46.923 1.00 30.23 ? 151 ARG A CG 1 ATOM 763 C CD . ARG A 1 98 ? -2.398 28.417 46.055 1.00 34.99 ? 151 ARG A CD 1 ATOM 764 N NE . ARG A 1 98 ? -2.612 28.153 44.634 1.00 45.11 ? 151 ARG A NE 1 ATOM 765 C CZ . ARG A 1 98 ? -3.752 27.721 44.108 1.00 48.48 ? 151 ARG A CZ 1 ATOM 766 N NH1 . ARG A 1 98 ? -4.800 27.491 44.885 1.00 52.22 ? 151 ARG A NH1 1 ATOM 767 N NH2 . ARG A 1 98 ? -3.846 27.518 42.801 1.00 50.12 ? 151 ARG A NH2 1 ATOM 768 N N . GLY A 1 99 ? -0.037 23.572 48.669 1.00 25.84 ? 152 GLY A N 1 ATOM 769 C CA . GLY A 1 99 ? 0.849 22.438 48.468 1.00 26.84 ? 152 GLY A CA 1 ATOM 770 C C . GLY A 1 99 ? 1.497 22.456 47.094 1.00 26.33 ? 152 GLY A C 1 ATOM 771 O O . GLY A 1 99 ? 2.079 23.465 46.701 1.00 25.24 ? 152 GLY A O 1 ATOM 772 N N . GLY A 1 100 ? 1.406 21.339 46.372 1.00 24.90 ? 153 GLY A N 1 ATOM 773 C CA . GLY A 1 100 ? 1.912 21.258 45.014 1.00 26.31 ? 153 GLY A CA 1 ATOM 774 C C . GLY A 1 100 ? 0.815 21.290 43.967 1.00 27.22 ? 153 GLY A C 1 ATOM 775 O O . GLY A 1 100 ? 1.073 21.125 42.772 1.00 25.46 ? 153 GLY A O 1 ATOM 776 N N . GLU A 1 101 ? -0.413 21.519 44.420 1.00 28.69 ? 154 GLU A N 1 ATOM 777 C CA . GLU A 1 101 ? -1.581 21.407 43.565 1.00 28.05 ? 154 GLU A CA 1 ATOM 778 C C . GLU A 1 101 ? -1.423 22.200 42.274 1.00 26.37 ? 154 GLU A C 1 ATOM 779 O O . GLU A 1 101 ? -1.791 21.731 41.203 1.00 27.45 ? 154 GLU A O 1 ATOM 780 C CB . GLU A 1 101 ? -2.823 21.881 44.327 1.00 36.01 ? 154 GLU A CB 1 ATOM 781 C CG . GLU A 1 101 ? -4.092 21.922 43.493 1.00 40.14 ? 154 GLU A CG 1 ATOM 782 C CD . GLU A 1 101 ? -4.629 20.540 43.179 1.00 45.52 ? 154 GLU A CD 1 ATOM 783 O OE1 . GLU A 1 101 ? -5.294 20.393 42.130 1.00 49.76 ? 154 GLU A OE1 1 ATOM 784 O OE2 . GLU A 1 101 ? -4.389 19.600 43.978 1.00 47.60 ? 154 GLU A OE2 1 ATOM 785 N N . PRO A 1 102 ? -0.885 23.408 42.357 1.00 23.88 ? 155 PRO A N 1 ATOM 786 C CA . PRO A 1 102 ? -0.733 24.232 41.162 1.00 23.24 ? 155 PRO A CA 1 ATOM 787 C C . PRO A 1 102 ? 0.243 23.591 40.166 1.00 27.42 ? 155 PRO A C 1 ATOM 788 O O . PRO A 1 102 ? 0.119 23.819 38.965 1.00 26.50 ? 155 PRO A O 1 ATOM 789 C CB . PRO A 1 102 ? -0.191 25.555 41.707 1.00 27.03 ? 155 PRO A CB 1 ATOM 790 C CG . PRO A 1 102 ? -0.484 25.527 43.188 1.00 25.35 ? 155 PRO A CG 1 ATOM 791 C CD . PRO A 1 102 ? -0.381 24.077 43.569 1.00 25.63 ? 155 PRO A CD 1 ATOM 792 N N . LEU A 1 103 ? 1.189 22.796 40.656 1.00 24.96 ? 156 LEU A N 1 ATOM 793 C CA . LEU A 1 103 ? 2.044 22.001 39.771 1.00 25.50 ? 156 LEU A CA 1 ATOM 794 C C . LEU A 1 103 ? 1.282 20.824 39.163 1.00 24.71 ? 156 LEU A C 1 ATOM 795 O O . LEU A 1 103 ? 1.378 20.558 37.962 1.00 27.82 ? 156 LEU A O 1 ATOM 796 C CB . LEU A 1 103 ? 3.281 21.479 40.512 1.00 26.33 ? 156 LEU A CB 1 ATOM 797 C CG . LEU A 1 103 ? 4.330 20.857 39.582 1.00 29.02 ? 156 LEU A CG 1 ATOM 798 C CD1 . LEU A 1 103 ? 5.445 20.196 40.367 1.00 28.37 ? 156 LEU A CD1 1 ATOM 799 C CD2 . LEU A 1 103 ? 3.684 19.860 38.632 1.00 35.27 ? 156 LEU A CD2 1 ATOM 800 N N . LEU A 1 104 ? 0.524 20.122 39.996 1.00 27.94 ? 157 LEU A N 1 ATOM 801 C CA . LEU A 1 104 ? -0.164 18.920 39.551 1.00 29.85 ? 157 LEU A CA 1 ATOM 802 C C . LEU A 1 104 ? -1.141 19.266 38.430 1.00 34.55 ? 157 LEU A C 1 ATOM 803 O O . LEU A 1 104 ? -1.312 18.489 37.492 1.00 29.97 ? 157 LEU A O 1 ATOM 804 C CB . LEU A 1 104 ? -0.912 18.267 40.712 1.00 30.07 ? 157 LEU A CB 1 ATOM 805 C CG . LEU A 1 104 ? -0.086 17.834 41.926 1.00 31.83 ? 157 LEU A CG 1 ATOM 806 C CD1 . LEU A 1 104 ? -0.980 17.329 43.064 1.00 34.45 ? 157 LEU A CD1 1 ATOM 807 C CD2 . LEU A 1 104 ? 0.917 16.770 41.539 1.00 32.31 ? 157 LEU A CD2 1 ATOM 808 N N . LYS A 1 105 ? -1.777 20.433 38.519 1.00 35.45 ? 158 LYS A N 1 ATOM 809 C CA . LYS A 1 105 ? -2.743 20.839 37.502 1.00 40.23 ? 158 LYS A CA 1 ATOM 810 C C . LYS A 1 105 ? -2.048 21.178 36.194 1.00 36.51 ? 158 LYS A C 1 ATOM 811 O O . LYS A 1 105 ? -2.655 21.161 35.130 1.00 38.83 ? 158 LYS A O 1 ATOM 812 C CB . LYS A 1 105 ? -3.560 22.032 37.983 1.00 43.35 ? 158 LYS A CB 1 ATOM 813 C CG . LYS A 1 105 ? -4.970 21.656 38.418 1.00 49.14 ? 158 LYS A CG 1 ATOM 814 C CD . LYS A 1 105 ? -5.090 20.156 38.656 1.00 51.89 ? 158 LYS A CD 1 ATOM 815 C CE . LYS A 1 105 ? -4.958 19.817 40.130 1.00 54.13 ? 158 LYS A CE 1 ATOM 816 N NZ . LYS A 1 105 ? -4.405 18.426 40.315 1.00 55.35 ? 158 LYS A NZ 1 ATOM 817 N N . LEU A 1 106 ? -0.763 21.484 36.284 1.00 34.12 ? 159 LEU A N 1 ATOM 818 C CA . LEU A 1 106 ? 0.011 21.863 35.117 1.00 32.13 ? 159 LEU A CA 1 ATOM 819 C C . LEU A 1 106 ? 0.451 20.613 34.384 1.00 25.78 ? 159 LEU A C 1 ATOM 820 O O . LEU A 1 106 ? 0.531 20.600 33.165 1.00 26.42 ? 159 LEU A O 1 ATOM 821 C CB . LEU A 1 106 ? 1.244 22.668 35.535 1.00 32.95 ? 159 LEU A CB 1 ATOM 822 C CG . LEU A 1 106 ? 1.887 23.521 34.446 1.00 36.13 ? 159 LEU A CG 1 ATOM 823 C CD1 . LEU A 1 106 ? 0.828 24.066 33.507 1.00 38.96 ? 159 LEU A CD1 1 ATOM 824 C CD2 . LEU A 1 106 ? 2.682 24.659 35.069 1.00 36.66 ? 159 LEU A CD2 1 ATOM 825 N N . LEU A 1 107 ? 0.756 19.571 35.143 1.00 25.76 ? 160 LEU A N 1 ATOM 826 C CA . LEU A 1 107 ? 1.533 18.448 34.628 1.00 31.28 ? 160 LEU A CA 1 ATOM 827 C C . LEU A 1 107 ? 0.900 17.860 33.362 1.00 33.71 ? 160 LEU A C 1 ATOM 828 O O . LEU A 1 107 ? 1.583 17.607 32.368 1.00 38.59 ? 160 LEU A O 1 ATOM 829 C CB . LEU A 1 107 ? 1.669 17.373 35.708 1.00 32.03 ? 160 LEU A CB 1 ATOM 830 C CG . LEU A 1 107 ? 3.070 17.199 36.287 1.00 33.17 ? 160 LEU A CG 1 ATOM 831 C CD1 . LEU A 1 107 ? 3.990 18.298 35.783 1.00 34.30 ? 160 LEU A CD1 1 ATOM 832 C CD2 . LEU A 1 107 ? 3.046 17.152 37.798 1.00 35.75 ? 160 LEU A CD2 1 ATOM 833 N N . PRO A 1 108 ? -0.408 17.648 33.388 1.00 35.66 ? 161 PRO A N 1 ATOM 834 C CA . PRO A 1 108 ? -1.099 17.102 32.219 1.00 35.99 ? 161 PRO A CA 1 ATOM 835 C C . PRO A 1 108 ? -0.868 17.951 30.971 1.00 34.24 ? 161 PRO A C 1 ATOM 836 O O . PRO A 1 108 ? -0.993 17.449 29.858 1.00 36.33 ? 161 PRO A O 1 ATOM 837 C CB . PRO A 1 108 ? -2.576 17.105 32.641 1.00 36.69 ? 161 PRO A CB 1 ATOM 838 C CG . PRO A 1 108 ? -2.550 17.103 34.130 1.00 38.17 ? 161 PRO A CG 1 ATOM 839 C CD . PRO A 1 108 ? -1.322 17.895 34.517 1.00 35.24 ? 161 PRO A CD 1 ATOM 840 N N . ASP A 1 109 ? -0.513 19.219 31.146 1.00 34.10 ? 162 ASP A N 1 ATOM 841 C CA . ASP A 1 109 ? -0.398 20.120 30.001 1.00 34.39 ? 162 ASP A CA 1 ATOM 842 C C . ASP A 1 109 ? 0.961 20.058 29.308 1.00 31.99 ? 162 ASP A C 1 ATOM 843 O O . ASP A 1 109 ? 1.167 20.701 28.284 1.00 34.70 ? 162 ASP A O 1 ATOM 844 C CB . ASP A 1 109 ? -0.672 21.563 30.410 1.00 37.18 ? 162 ASP A CB 1 ATOM 845 C CG . ASP A 1 109 ? -0.933 22.457 29.216 1.00 37.09 ? 162 ASP A CG 1 ATOM 846 O OD1 . ASP A 1 109 ? -0.307 23.538 29.117 1.00 34.89 ? 162 ASP A OD1 1 ATOM 847 O OD2 . ASP A 1 109 ? -1.733 22.139 28.310 1.00 35.84 ? 162 ASP A OD2 1 ATOM 848 N N . ILE A 1 110 ? 1.896 19.306 29.869 1.00 32.73 ? 163 ILE A N 1 ATOM 849 C CA . ILE A 1 110 ? 3.201 19.146 29.236 1.00 32.43 ? 163 ILE A CA 1 ATOM 850 C C . ILE A 1 110 ? 3.480 17.679 28.928 1.00 30.79 ? 163 ILE A C 1 ATOM 851 O O . ILE A 1 110 ? 4.633 17.276 28.757 1.00 29.08 ? 163 ILE A O 1 ATOM 852 C CB . ILE A 1 110 ? 4.303 19.718 30.143 1.00 29.74 ? 163 ILE A CB 1 ATOM 853 C CG1 . ILE A 1 110 ? 4.210 19.095 31.535 1.00 29.57 ? 163 ILE A CG1 1 ATOM 854 C CG2 . ILE A 1 110 ? 4.167 21.229 30.254 1.00 29.54 ? 163 ILE A CG2 1 ATOM 855 C CD1 . ILE A 1 110 ? 5.271 19.584 32.485 1.00 28.96 ? 163 ILE A CD1 1 ATOM 856 N N . TYR A 1 111 ? 2.416 16.888 28.850 1.00 30.77 ? 164 TYR A N 1 ATOM 857 C CA . TYR A 1 111 ? 2.525 15.465 28.528 1.00 33.17 ? 164 TYR A CA 1 ATOM 858 C C . TYR A 1 111 ? 3.045 14.661 29.714 1.00 34.82 ? 164 TYR A C 1 ATOM 859 O O . TYR A 1 111 ? 3.482 13.522 29.560 1.00 35.08 ? 164 TYR A O 1 ATOM 860 C CB . TYR A 1 111 ? 3.431 15.253 27.315 1.00 37.04 ? 164 TYR A CB 1 ATOM 861 C CG . TYR A 1 111 ? 2.818 15.735 26.025 1.00 39.30 ? 164 TYR A CG 1 ATOM 862 C CD1 . TYR A 1 111 ? 3.140 16.979 25.507 1.00 39.96 ? 164 TYR A CD1 1 ATOM 863 C CD2 . TYR A 1 111 ? 1.905 14.949 25.328 1.00 40.50 ? 164 TYR A CD2 1 ATOM 864 C CE1 . TYR A 1 111 ? 2.576 17.429 24.332 1.00 42.92 ? 164 TYR A CE1 1 ATOM 865 C CE2 . TYR A 1 111 ? 1.334 15.392 24.151 1.00 41.03 ? 164 TYR A CE2 1 ATOM 866 C CZ . TYR A 1 111 ? 1.671 16.631 23.657 1.00 43.56 ? 164 TYR A CZ 1 ATOM 867 O OH . TYR A 1 111 ? 1.106 17.087 22.485 1.00 46.16 ? 164 TYR A OH 1 ATOM 868 N N . GLY A 1 112 ? 2.970 15.248 30.904 1.00 30.23 ? 165 GLY A N 1 ATOM 869 C CA . GLY A 1 112 ? 3.113 14.487 32.124 1.00 28.28 ? 165 GLY A CA 1 ATOM 870 C C . GLY A 1 112 ? 4.559 14.430 32.558 1.00 26.67 ? 165 GLY A C 1 ATOM 871 O O . GLY A 1 112 ? 5.451 14.836 31.811 1.00 26.64 ? 165 GLY A O 1 ATOM 872 N N . TRP A 1 113 ? 4.782 13.926 33.767 1.00 23.80 ? 166 TRP A N 1 ATOM 873 C CA . TRP A 1 113 ? 6.096 13.452 34.193 1.00 26.85 ? 166 TRP A CA 1 ATOM 874 C C . TRP A 1 113 ? 6.030 11.959 34.518 1.00 24.97 ? 166 TRP A C 1 ATOM 875 O O . TRP A 1 113 ? 5.582 11.572 35.596 1.00 23.80 ? 166 TRP A O 1 ATOM 876 C CB . TRP A 1 113 ? 6.549 14.238 35.430 1.00 26.65 ? 166 TRP A CB 1 ATOM 877 C CG . TRP A 1 113 ? 8.009 14.137 35.729 1.00 25.85 ? 166 TRP A CG 1 ATOM 878 C CD1 . TRP A 1 113 ? 9.017 13.908 34.837 1.00 27.50 ? 166 TRP A CD1 1 ATOM 879 C CD2 . TRP A 1 113 ? 8.636 14.292 37.005 1.00 23.48 ? 166 TRP A CD2 1 ATOM 880 N NE1 . TRP A 1 113 ? 10.229 13.898 35.483 1.00 26.07 ? 166 TRP A NE1 1 ATOM 881 C CE2 . TRP A 1 113 ? 10.023 14.125 36.816 1.00 24.86 ? 166 TRP A CE2 1 ATOM 882 C CE3 . TRP A 1 113 ? 8.165 14.537 38.301 1.00 22.14 ? 166 TRP A CE3 1 ATOM 883 C CZ2 . TRP A 1 113 ? 10.937 14.207 37.862 1.00 26.48 ? 166 TRP A CZ2 1 ATOM 884 C CZ3 . TRP A 1 113 ? 9.079 14.611 39.340 1.00 25.34 ? 166 TRP A CZ3 1 ATOM 885 C CH2 . TRP A 1 113 ? 10.447 14.446 39.113 1.00 24.55 ? 166 TRP A CH2 1 ATOM 886 N N . PRO A 1 114 ? 6.472 11.119 33.583 1.00 24.29 ? 167 PRO A N 1 ATOM 887 C CA . PRO A 1 114 ? 6.250 9.670 33.675 1.00 26.22 ? 167 PRO A CA 1 ATOM 888 C C . PRO A 1 114 ? 6.573 9.082 35.044 1.00 26.06 ? 167 PRO A C 1 ATOM 889 O O . PRO A 1 114 ? 5.710 8.442 35.649 1.00 29.11 ? 167 PRO A O 1 ATOM 890 C CB . PRO A 1 114 ? 7.182 9.105 32.601 1.00 25.53 ? 167 PRO A CB 1 ATOM 891 C CG . PRO A 1 114 ? 7.281 10.196 31.585 1.00 23.74 ? 167 PRO A CG 1 ATOM 892 C CD . PRO A 1 114 ? 7.188 11.488 32.354 1.00 24.55 ? 167 PRO A CD 1 ATOM 893 N N . VAL A 1 115 ? 7.793 9.298 35.530 1.00 27.64 ? 168 VAL A N 1 ATOM 894 C CA . VAL A 1 115 ? 8.170 8.880 36.868 1.00 28.46 ? 168 VAL A CA 1 ATOM 895 C C . VAL A 1 115 ? 7.020 9.076 37.835 1.00 28.76 ? 168 VAL A C 1 ATOM 896 O O . VAL A 1 115 ? 6.746 8.241 38.683 1.00 29.41 ? 168 VAL A O 1 ATOM 897 C CB . VAL A 1 115 ? 9.358 9.697 37.392 1.00 34.65 ? 168 VAL A CB 1 ATOM 898 C CG1 . VAL A 1 115 ? 9.800 10.715 36.356 1.00 37.57 ? 168 VAL A CG1 1 ATOM 899 C CG2 . VAL A 1 115 ? 8.984 10.401 38.692 1.00 36.06 ? 168 VAL A CG2 1 ATOM 900 N N . ALA A 1 116 ? 6.343 10.205 37.733 1.00 30.91 ? 169 ALA A N 1 ATOM 901 C CA . ALA A 1 116 ? 5.395 10.552 38.769 1.00 32.56 ? 169 ALA A CA 1 ATOM 902 C C . ALA A 1 116 ? 3.967 10.332 38.291 1.00 36.73 ? 169 ALA A C 1 ATOM 903 O O . ALA A 1 116 ? 3.045 10.981 38.774 1.00 36.20 ? 169 ALA A O 1 ATOM 904 C CB . ALA A 1 116 ? 5.598 11.990 39.199 1.00 33.50 ? 169 ALA A CB 1 ATOM 905 N N . THR A 1 117 ? 3.778 9.415 37.348 1.00 38.96 ? 170 THR A N 1 ATOM 906 C CA . THR A 1 117 ? 2.432 8.979 37.005 1.00 39.70 ? 170 THR A CA 1 ATOM 907 C C . THR A 1 117 ? 2.285 7.465 36.990 1.00 42.38 ? 170 THR A C 1 ATOM 908 O O . THR A 1 117 ? 3.271 6.725 36.969 1.00 41.88 ? 170 THR A O 1 ATOM 909 C CB . THR A 1 117 ? 2.013 9.542 35.643 1.00 40.52 ? 170 THR A CB 1 ATOM 910 O OG1 . THR A 1 117 ? 2.782 10.709 35.337 1.00 41.08 ? 170 THR A OG1 1 ATOM 911 C CG2 . THR A 1 117 ? 0.577 10.051 35.692 1.00 43.02 ? 170 THR A CG2 1 ATOM 912 N N . GLU A 1 118 ? 1.033 7.015 36.993 1.00 43.80 ? 171 GLU A N 1 ATOM 913 C CA . GLU A 1 118 ? 0.696 5.660 36.572 1.00 44.04 ? 171 GLU A CA 1 ATOM 914 C C . GLU A 1 118 ? 0.409 5.595 35.073 1.00 42.94 ? 171 GLU A C 1 ATOM 915 O O . GLU A 1 118 ? -0.109 6.541 34.476 1.00 41.64 ? 171 GLU A O 1 ATOM 916 C CB . GLU A 1 118 ? -0.522 5.160 37.346 1.00 44.95 ? 171 GLU A CB 1 ATOM 917 C CG . GLU A 1 118 ? -1.706 6.113 37.288 1.00 44.99 ? 171 GLU A CG 1 ATOM 918 C CD . GLU A 1 118 ? -2.632 5.971 38.480 1.00 42.82 ? 171 GLU A CD 1 ATOM 919 O OE1 . GLU A 1 118 ? -3.454 6.876 38.698 1.00 43.53 ? 171 GLU A OE1 1 ATOM 920 O OE2 . GLU A 1 118 ? -2.538 4.951 39.195 1.00 45.30 ? 171 GLU A OE2 1 ATOM 921 N N . ASN A 1 119 ? 0.751 4.464 34.471 1.00 41.79 ? 172 ASN A N 1 ATOM 922 C CA . ASN A 1 119 ? 0.270 4.136 33.140 1.00 42.53 ? 172 ASN A CA 1 ATOM 923 C C . ASN A 1 119 ? 0.506 5.280 32.159 1.00 39.79 ? 172 ASN A C 1 ATOM 924 O O . ASN A 1 119 ? -0.331 5.575 31.307 1.00 37.38 ? 172 ASN A O 1 ATOM 925 C CB . ASN A 1 119 ? -1.213 3.764 33.208 1.00 43.14 ? 172 ASN A CB 1 ATOM 926 C CG . ASN A 1 119 ? -1.438 2.415 33.863 1.00 42.83 ? 172 ASN A CG 1 ATOM 927 O OD1 . ASN A 1 119 ? -0.940 1.396 33.383 1.00 44.92 ? 172 ASN A OD1 1 ATOM 928 N ND2 . ASN A 1 119 ? -2.177 2.401 34.970 1.00 40.15 ? 172 ASN A ND2 1 ATOM 929 N N . TRP A 1 120 ? 1.673 5.910 32.273 1.00 37.33 ? 173 TRP A N 1 ATOM 930 C CA . TRP A 1 120 ? 1.989 7.075 31.463 1.00 34.78 ? 173 TRP A CA 1 ATOM 931 C C . TRP A 1 120 ? 1.921 6.730 29.987 1.00 31.87 ? 173 TRP A C 1 ATOM 932 O O . TRP A 1 120 ? 1.539 7.554 29.158 1.00 31.00 ? 173 TRP A O 1 ATOM 933 C CB . TRP A 1 120 ? 3.386 7.607 31.798 1.00 33.85 ? 173 TRP A CB 1 ATOM 934 C CG . TRP A 1 120 ? 3.769 8.783 30.965 1.00 31.34 ? 173 TRP A CG 1 ATOM 935 C CD1 . TRP A 1 120 ? 3.563 10.103 31.266 1.00 28.44 ? 173 TRP A CD1 1 ATOM 936 C CD2 . TRP A 1 120 ? 4.409 8.763 29.686 1.00 30.28 ? 173 TRP A CD2 1 ATOM 937 N NE1 . TRP A 1 120 ? 4.035 10.896 30.252 1.00 28.70 ? 173 TRP A NE1 1 ATOM 938 C CE2 . TRP A 1 120 ? 4.566 10.099 29.272 1.00 29.33 ? 173 TRP A CE2 1 ATOM 939 C CE3 . TRP A 1 120 ? 4.880 7.748 28.849 1.00 31.23 ? 173 TRP A CE3 1 ATOM 940 C CZ2 . TRP A 1 120 ? 5.167 10.446 28.060 1.00 32.11 ? 173 TRP A CZ2 1 ATOM 941 C CZ3 . TRP A 1 120 ? 5.478 8.095 27.643 1.00 31.68 ? 173 TRP A CZ3 1 ATOM 942 C CH2 . TRP A 1 120 ? 5.611 9.430 27.260 1.00 31.18 ? 173 TRP A CH2 1 ATOM 943 N N . GLU A 1 121 ? 2.322 5.513 29.653 1.00 32.66 ? 174 GLU A N 1 ATOM 944 C CA . GLU A 1 121 ? 2.367 5.114 28.260 1.00 36.75 ? 174 GLU A CA 1 ATOM 945 C C . GLU A 1 121 ? 0.950 5.113 27.695 1.00 35.54 ? 174 GLU A C 1 ATOM 946 O O . GLU A 1 121 ? 0.731 5.501 26.549 1.00 33.59 ? 174 GLU A O 1 ATOM 947 C CB . GLU A 1 121 ? 3.010 3.735 28.115 1.00 39.05 ? 174 GLU A CB 1 ATOM 948 C CG . GLU A 1 121 ? 4.520 3.740 28.293 1.00 40.74 ? 174 GLU A CG 1 ATOM 949 C CD . GLU A 1 121 ? 4.932 3.796 29.754 1.00 42.11 ? 174 GLU A CD 1 ATOM 950 O OE1 . GLU A 1 121 ? 4.042 3.781 30.628 1.00 43.09 ? 174 GLU A OE1 1 ATOM 951 O OE2 . GLU A 1 121 ? 6.149 3.846 30.027 1.00 42.59 ? 174 GLU A OE2 1 ATOM 952 N N . GLN A 1 122 ? -0.011 4.699 28.512 1.00 39.21 ? 175 GLN A N 1 ATOM 953 C CA . GLN A 1 122 ? -1.404 4.644 28.069 1.00 45.11 ? 175 GLN A CA 1 ATOM 954 C C . GLN A 1 122 ? -1.986 6.050 27.922 1.00 42.78 ? 175 GLN A C 1 ATOM 955 O O . GLN A 1 122 ? -2.610 6.369 26.912 1.00 44.44 ? 175 GLN A O 1 ATOM 956 C CB . GLN A 1 122 ? -2.253 3.824 29.044 1.00 48.11 ? 175 GLN A CB 1 ATOM 957 C CG . GLN A 1 122 ? -3.506 3.215 28.414 1.00 53.17 ? 175 GLN A CG 1 ATOM 958 C CD . GLN A 1 122 ? -4.771 3.987 28.757 1.00 56.28 ? 175 GLN A CD 1 ATOM 959 O OE1 . GLN A 1 122 ? -4.947 4.427 29.898 1.00 59.25 ? 175 GLN A OE1 1 ATOM 960 N NE2 . GLN A 1 122 ? -5.655 4.151 27.774 1.00 56.57 ? 175 GLN A NE2 1 ATOM 961 N N . LYS A 1 123 ? -1.783 6.893 28.928 1.00 42.88 ? 176 LYS A N 1 ATOM 962 C CA . LYS A 1 123 ? -2.391 8.223 28.920 1.00 42.76 ? 176 LYS A CA 1 ATOM 963 C C . LYS A 1 123 ? -1.784 9.076 27.815 1.00 42.12 ? 176 LYS A C 1 ATOM 964 O O . LYS A 1 123 ? -2.496 9.703 27.035 1.00 39.81 ? 176 LYS A O 1 ATOM 965 C CB . LYS A 1 123 ? -2.207 8.909 30.270 1.00 41.44 ? 176 LYS A CB 1 ATOM 966 C CG . LYS A 1 123 ? -2.765 8.122 31.436 1.00 42.93 ? 176 LYS A CG 1 ATOM 967 C CD . LYS A 1 123 ? -2.792 8.954 32.712 1.00 44.23 ? 176 LYS A CD 1 ATOM 968 C CE . LYS A 1 123 ? -3.068 8.086 33.933 1.00 43.82 ? 176 LYS A CE 1 ATOM 969 N NZ . LYS A 1 123 ? -4.468 7.552 33.906 1.00 45.82 ? 176 LYS A NZ 1 ATOM 970 N N . TYR A 1 124 ? -0.457 9.084 27.753 1.00 43.37 ? 177 TYR A N 1 ATOM 971 C CA . TYR A 1 124 ? 0.282 10.185 27.152 1.00 41.80 ? 177 TYR A CA 1 ATOM 972 C C . TYR A 1 124 ? 1.126 9.676 25.996 1.00 42.20 ? 177 TYR A C 1 ATOM 973 O O . TYR A 1 124 ? 1.223 10.318 24.956 1.00 45.86 ? 177 TYR A O 1 ATOM 974 C CB . TYR A 1 124 ? 1.197 10.833 28.188 1.00 40.99 ? 177 TYR A CB 1 ATOM 975 C CG . TYR A 1 124 ? 0.472 11.582 29.280 1.00 39.53 ? 177 TYR A CG 1 ATOM 976 C CD1 . TYR A 1 124 ? -0.187 12.774 29.011 1.00 38.91 ? 177 TYR A CD1 1 ATOM 977 C CD2 . TYR A 1 124 ? 0.467 11.109 30.585 1.00 37.89 ? 177 TYR A CD2 1 ATOM 978 C CE1 . TYR A 1 124 ? -0.842 13.466 30.010 1.00 39.05 ? 177 TYR A CE1 1 ATOM 979 C CE2 . TYR A 1 124 ? -0.187 11.795 31.592 1.00 37.57 ? 177 TYR A CE2 1 ATOM 980 C CZ . TYR A 1 124 ? -0.839 12.976 31.299 1.00 39.37 ? 177 TYR A CZ 1 ATOM 981 O OH . TYR A 1 124 ? -1.496 13.664 32.298 1.00 39.57 ? 177 TYR A OH 1 ATOM 982 N N . GLY A 1 125 ? 1.735 8.513 26.191 1.00 44.87 ? 178 GLY A N 1 ATOM 983 C CA . GLY A 1 125 ? 2.613 7.933 25.192 1.00 44.13 ? 178 GLY A CA 1 ATOM 984 C C . GLY A 1 125 ? 1.925 7.778 23.850 1.00 45.60 ? 178 GLY A C 1 ATOM 985 O O . GLY A 1 125 ? 2.537 7.982 22.800 1.00 41.88 ? 178 GLY A O 1 ATOM 986 N N . ALA A 1 126 ? 0.644 7.423 23.882 1.00 48.79 ? 179 ALA A N 1 ATOM 987 C CA . ALA A 1 126 ? -0.148 7.328 22.663 1.00 50.69 ? 179 ALA A CA 1 ATOM 988 C C . ALA A 1 126 ? 0.062 8.564 21.800 1.00 52.84 ? 179 ALA A C 1 ATOM 989 O O . ALA A 1 126 ? 0.579 8.475 20.689 1.00 54.32 ? 179 ALA A O 1 ATOM 990 C CB . ALA A 1 126 ? -1.618 7.165 23.001 1.00 53.19 ? 179 ALA A CB 1 ATOM 991 N N . SER A 1 127 ? -0.341 9.720 22.322 1.00 54.63 ? 180 SER A N 1 ATOM 992 C CA . SER A 1 127 ? -0.372 10.950 21.536 1.00 54.54 ? 180 SER A CA 1 ATOM 993 C C . SER A 1 127 ? 0.984 11.661 21.530 1.00 53.67 ? 180 SER A C 1 ATOM 994 O O . SER A 1 127 ? 1.249 12.501 20.671 1.00 55.55 ? 180 SER A O 1 ATOM 995 C CB . SER A 1 127 ? -1.452 11.894 22.073 1.00 54.06 ? 180 SER A CB 1 ATOM 996 O OG . SER A 1 127 ? -1.299 12.117 23.463 1.00 53.64 ? 180 SER A OG 1 ATOM 997 N N . TRP A 1 128 ? 1.833 11.325 22.497 1.00 51.58 ? 181 TRP A N 1 ATOM 998 C CA . TRP A 1 128 ? 3.219 11.795 22.521 1.00 47.35 ? 181 TRP A CA 1 ATOM 999 C C . TRP A 1 128 ? 3.870 11.748 21.144 1.00 44.92 ? 181 TRP A C 1 ATOM 1000 O O . TRP A 1 128 ? 3.884 10.705 20.493 1.00 45.91 ? 181 TRP A O 1 ATOM 1001 C CB . TRP A 1 128 ? 4.032 10.935 23.492 1.00 48.59 ? 181 TRP A CB 1 ATOM 1002 C CG . TRP A 1 128 ? 5.273 11.594 23.996 1.00 46.20 ? 181 TRP A CG 1 ATOM 1003 C CD1 . TRP A 1 128 ? 5.399 12.345 25.125 1.00 46.16 ? 181 TRP A CD1 1 ATOM 1004 C CD2 . TRP A 1 128 ? 6.573 11.555 23.395 1.00 45.79 ? 181 TRP A CD2 1 ATOM 1005 N NE1 . TRP A 1 128 ? 6.694 12.782 25.261 1.00 42.50 ? 181 TRP A NE1 1 ATOM 1006 C CE2 . TRP A 1 128 ? 7.436 12.308 24.212 1.00 43.59 ? 181 TRP A CE2 1 ATOM 1007 C CE3 . TRP A 1 128 ? 7.097 10.958 22.244 1.00 46.12 ? 181 TRP A CE3 1 ATOM 1008 C CZ2 . TRP A 1 128 ? 8.785 12.480 23.918 1.00 43.48 ? 181 TRP A CZ2 1 ATOM 1009 C CZ3 . TRP A 1 128 ? 8.433 11.129 21.955 1.00 45.37 ? 181 TRP A CZ3 1 ATOM 1010 C CH2 . TRP A 1 128 ? 9.262 11.886 22.786 1.00 45.15 ? 181 TRP A CH2 1 ATOM 1011 N N . THR A 1 129 ? 4.428 12.873 20.710 1.00 42.82 ? 182 THR A N 1 ATOM 1012 C CA . THR A 1 129 ? 5.669 12.855 19.946 1.00 40.66 ? 182 THR A CA 1 ATOM 1013 C C . THR A 1 129 ? 6.618 13.984 20.352 1.00 40.52 ? 182 THR A C 1 ATOM 1014 O O . THR A 1 129 ? 6.211 14.976 20.970 1.00 37.86 ? 182 THR A O 1 ATOM 1015 C CB . THR A 1 129 ? 5.364 12.945 18.448 1.00 42.88 ? 182 THR A CB 1 ATOM 1016 O OG1 . THR A 1 129 ? 5.034 14.294 18.098 1.00 39.79 ? 182 THR A OG1 1 ATOM 1017 C CG2 . THR A 1 129 ? 4.097 12.167 18.108 1.00 43.71 ? 182 THR A CG2 1 ATOM 1018 N N . ALA A 1 130 ? 7.890 13.824 19.997 1.00 37.21 ? 183 ALA A N 1 ATOM 1019 C CA . ALA A 1 130 ? 8.927 14.725 20.473 1.00 35.99 ? 183 ALA A CA 1 ATOM 1020 C C . ALA A 1 130 ? 8.709 16.108 19.874 1.00 33.56 ? 183 ALA A C 1 ATOM 1021 O O . ALA A 1 130 ? 8.963 17.131 20.521 1.00 32.26 ? 183 ALA A O 1 ATOM 1022 C CB . ALA A 1 130 ? 10.302 14.193 20.097 1.00 36.45 ? 183 ALA A CB 1 ATOM 1023 N N . GLU A 1 131 ? 8.242 16.138 18.630 1.00 28.24 ? 184 GLU A N 1 ATOM 1024 C CA . GLU A 1 131 ? 7.831 17.392 18.019 1.00 31.80 ? 184 GLU A CA 1 ATOM 1025 C C . GLU A 1 131 ? 6.852 18.094 18.959 1.00 32.79 ? 184 GLU A C 1 ATOM 1026 O O . GLU A 1 131 ? 7.037 19.255 19.287 1.00 33.67 ? 184 GLU A O 1 ATOM 1027 C CB . GLU A 1 131 ? 7.172 17.159 16.653 1.00 34.61 ? 184 GLU A CB 1 ATOM 1028 C CG . GLU A 1 131 ? 7.947 16.235 15.728 1.00 35.11 ? 184 GLU A CG 1 ATOM 1029 C CD . GLU A 1 131 ? 7.965 14.810 16.233 1.00 37.18 ? 184 GLU A CD 1 ATOM 1030 O OE1 . GLU A 1 131 ? 7.431 14.563 17.335 1.00 45.98 ? 184 GLU A OE1 1 ATOM 1031 O OE2 . GLU A 1 131 ? 8.505 13.937 15.535 1.00 42.28 ? 184 GLU A OE2 1 ATOM 1032 N N . LYS A 1 132 ? 5.819 17.379 19.397 1.00 34.52 ? 185 LYS A N 1 ATOM 1033 C CA . LYS A 1 132 ? 4.713 18.003 20.126 1.00 34.70 ? 185 LYS A CA 1 ATOM 1034 C C . LYS A 1 132 ? 5.167 18.385 21.528 1.00 32.21 ? 185 LYS A C 1 ATOM 1035 O O . LYS A 1 132 ? 4.899 19.483 21.998 1.00 33.28 ? 185 LYS A O 1 ATOM 1036 C CB . LYS A 1 132 ? 3.510 17.056 20.215 1.00 34.20 ? 185 LYS A CB 1 ATOM 1037 C CG . LYS A 1 132 ? 2.698 16.934 18.924 1.00 36.92 ? 185 LYS A CG 1 ATOM 1038 C CD . LYS A 1 132 ? 1.349 16.265 19.159 1.00 38.41 ? 185 LYS A CD 1 ATOM 1039 C CE . LYS A 1 132 ? 1.488 14.785 19.504 1.00 38.84 ? 185 LYS A CE 1 ATOM 1040 N NZ . LYS A 1 132 ? 0.154 14.117 19.643 1.00 39.23 ? 185 LYS A NZ 1 ATOM 1041 N N . ALA A 1 133 ? 5.860 17.465 22.193 1.00 31.96 ? 186 ALA A N 1 ATOM 1042 C CA . ALA A 1 133 ? 6.224 17.653 23.590 1.00 32.15 ? 186 ALA A CA 1 ATOM 1043 C C . ALA A 1 133 ? 7.264 18.774 23.746 1.00 31.26 ? 186 ALA A C 1 ATOM 1044 O O . ALA A 1 133 ? 7.060 19.698 24.531 1.00 29.30 ? 186 ALA A O 1 ATOM 1045 C CB . ALA A 1 133 ? 6.734 16.356 24.173 1.00 34.21 ? 186 ALA A CB 1 ATOM 1046 N N . ILE A 1 134 ? 8.349 18.717 22.974 1.00 30.44 ? 187 ILE A N 1 ATOM 1047 C CA . ILE A 1 134 ? 9.366 19.767 23.012 1.00 28.32 ? 187 ILE A CA 1 ATOM 1048 C C . ILE A 1 134 ? 8.748 21.119 22.713 1.00 30.03 ? 187 ILE A C 1 ATOM 1049 O O . ILE A 1 134 ? 9.072 22.119 23.355 1.00 27.78 ? 187 ILE A O 1 ATOM 1050 C CB . ILE A 1 134 ? 10.492 19.508 21.986 1.00 30.10 ? 187 ILE A CB 1 ATOM 1051 C CG1 . ILE A 1 134 ? 11.169 18.169 22.228 1.00 32.21 ? 187 ILE A CG1 1 ATOM 1052 C CG2 . ILE A 1 134 ? 11.544 20.603 22.058 1.00 29.94 ? 187 ILE A CG2 1 ATOM 1053 C CD1 . ILE A 1 134 ? 12.124 17.796 21.116 1.00 31.32 ? 187 ILE A CD1 1 ATOM 1054 N N . ALA A 1 135 ? 7.872 21.156 21.713 1.00 28.42 ? 188 ALA A N 1 ATOM 1055 C CA . ALA A 1 135 ? 7.239 22.408 21.312 1.00 28.33 ? 188 ALA A CA 1 ATOM 1056 C C . ALA A 1 135 ? 6.318 22.982 22.394 1.00 22.33 ? 188 ALA A C 1 ATOM 1057 O O . ALA A 1 135 ? 6.278 24.189 22.589 1.00 27.96 ? 188 ALA A O 1 ATOM 1058 C CB . ALA A 1 135 ? 6.476 22.222 20.003 1.00 28.47 ? 188 ALA A CB 1 ATOM 1059 N N . GLN A 1 136 ? 5.577 22.128 23.087 1.00 27.30 ? 189 GLN A N 1 ATOM 1060 C CA . GLN A 1 136 ? 4.684 22.583 24.154 1.00 29.11 ? 189 GLN A CA 1 ATOM 1061 C C . GLN A 1 136 ? 5.462 23.353 25.211 1.00 32.24 ? 189 GLN A C 1 ATOM 1062 O O . GLN A 1 136 ? 5.133 24.498 25.540 1.00 34.22 ? 189 GLN A O 1 ATOM 1063 C CB . GLN A 1 136 ? 4.008 21.399 24.836 1.00 31.34 ? 189 GLN A CB 1 ATOM 1064 C CG . GLN A 1 136 ? 2.533 21.237 24.566 1.00 36.59 ? 189 GLN A CG 1 ATOM 1065 C CD . GLN A 1 136 ? 1.732 22.502 24.781 1.00 36.98 ? 189 GLN A CD 1 ATOM 1066 O OE1 . GLN A 1 136 ? 1.802 23.425 23.976 1.00 40.75 ? 189 GLN A OE1 1 ATOM 1067 N NE2 . GLN A 1 136 ? 0.948 22.537 25.850 1.00 38.07 ? 189 GLN A NE2 1 ATOM 1068 N N . LEU A 1 137 ? 6.487 22.701 25.751 1.00 29.41 ? 190 LEU A N 1 ATOM 1069 C CA . LEU A 1 137 ? 7.329 23.287 26.786 1.00 29.38 ? 190 LEU A CA 1 ATOM 1070 C C . LEU A 1 137 ? 7.962 24.569 26.292 1.00 27.44 ? 190 LEU A C 1 ATOM 1071 O O . LEU A 1 137 ? 8.064 25.552 27.031 1.00 30.29 ? 190 LEU A O 1 ATOM 1072 C CB . LEU A 1 137 ? 8.434 22.307 27.185 1.00 30.40 ? 190 LEU A CB 1 ATOM 1073 C CG . LEU A 1 137 ? 8.083 21.269 28.250 1.00 31.76 ? 190 LEU A CG 1 ATOM 1074 C CD1 . LEU A 1 137 ? 9.163 20.199 28.319 1.00 28.69 ? 190 LEU A CD1 1 ATOM 1075 C CD2 . LEU A 1 137 ? 7.891 21.935 29.606 1.00 30.52 ? 190 LEU A CD2 1 ATOM 1076 N N . ASN A 1 138 ? 8.407 24.552 25.040 1.00 27.30 ? 191 ASN A N 1 ATOM 1077 C CA . ASN A 1 138 ? 9.025 25.725 24.432 1.00 28.45 ? 191 ASN A CA 1 ATOM 1078 C C . ASN A 1 138 ? 8.038 26.885 24.299 1.00 29.01 ? 191 ASN A C 1 ATOM 1079 O O . ASN A 1 138 ? 8.326 28.006 24.712 1.00 30.73 ? 191 ASN A O 1 ATOM 1080 C CB . ASN A 1 138 ? 9.605 25.360 23.063 1.00 26.42 ? 191 ASN A CB 1 ATOM 1081 C CG . ASN A 1 138 ? 10.229 26.536 22.363 1.00 28.69 ? 191 ASN A CG 1 ATOM 1082 O OD1 . ASN A 1 138 ? 9.598 27.572 22.185 1.00 32.38 ? 191 ASN A OD1 1 ATOM 1083 N ND2 . ASN A 1 138 ? 11.478 26.379 21.938 1.00 32.27 ? 191 ASN A ND2 1 ATOM 1084 N N . SER A 1 139 ? 6.873 26.615 23.725 1.00 31.36 ? 192 SER A N 1 ATOM 1085 C CA . SER A 1 139 ? 6.036 27.686 23.187 1.00 30.01 ? 192 SER A CA 1 ATOM 1086 C C . SER A 1 139 ? 5.135 28.234 24.276 1.00 26.45 ? 192 SER A C 1 ATOM 1087 O O . SER A 1 139 ? 4.833 29.417 24.303 1.00 23.34 ? 192 SER A O 1 ATOM 1088 C CB . SER A 1 139 ? 5.183 27.182 22.021 1.00 29.95 ? 192 SER A CB 1 ATOM 1089 O OG . SER A 1 139 ? 4.118 26.378 22.487 1.00 25.71 ? 192 SER A OG 1 ATOM 1090 N N . LYS A 1 140 ? 4.707 27.361 25.178 1.00 27.39 ? 193 LYS A N 1 ATOM 1091 C CA . LYS A 1 140 ? 3.814 27.773 26.249 1.00 31.01 ? 193 LYS A CA 1 ATOM 1092 C C . LYS A 1 140 ? 4.591 28.324 27.447 1.00 30.64 ? 193 LYS A C 1 ATOM 1093 O O . LYS A 1 140 ? 4.156 29.285 28.078 1.00 32.33 ? 193 LYS A O 1 ATOM 1094 C CB . LYS A 1 140 ? 2.924 26.604 26.676 1.00 34.04 ? 193 LYS A CB 1 ATOM 1095 C CG . LYS A 1 140 ? 1.599 27.027 27.297 1.00 37.02 ? 193 LYS A CG 1 ATOM 1096 C CD . LYS A 1 140 ? 0.587 25.886 27.280 1.00 39.05 ? 193 LYS A CD 1 ATOM 1097 C CE . LYS A 1 140 ? -0.840 26.391 27.338 1.00 38.52 ? 193 LYS A CE 1 ATOM 1098 N NZ . LYS A 1 140 ? -1.578 25.862 28.526 1.00 37.56 ? 193 LYS A NZ 1 ATOM 1099 N N . TYR A 1 141 ? 5.732 27.712 27.760 1.00 30.09 ? 194 TYR A N 1 ATOM 1100 C CA . TYR A 1 141 ? 6.372 27.887 29.067 1.00 26.19 ? 194 TYR A CA 1 ATOM 1101 C C . TYR A 1 141 ? 7.817 28.390 28.950 1.00 25.35 ? 194 TYR A C 1 ATOM 1102 O O . TYR A 1 141 ? 8.501 28.586 29.950 1.00 26.45 ? 194 TYR A O 1 ATOM 1103 C CB . TYR A 1 141 ? 6.325 26.576 29.861 1.00 22.94 ? 194 TYR A CB 1 ATOM 1104 C CG . TYR A 1 141 ? 4.913 26.090 30.137 1.00 26.53 ? 194 TYR A CG 1 ATOM 1105 C CD1 . TYR A 1 141 ? 4.099 26.752 31.036 1.00 27.16 ? 194 TYR A CD1 1 ATOM 1106 C CD2 . TYR A 1 141 ? 4.392 24.983 29.485 1.00 27.64 ? 194 TYR A CD2 1 ATOM 1107 C CE1 . TYR A 1 141 ? 2.814 26.324 31.296 1.00 26.63 ? 194 TYR A CE1 1 ATOM 1108 C CE2 . TYR A 1 141 ? 3.097 24.550 29.732 1.00 28.90 ? 194 TYR A CE2 1 ATOM 1109 C CZ . TYR A 1 141 ? 2.315 25.227 30.644 1.00 30.91 ? 194 TYR A CZ 1 ATOM 1110 O OH . TYR A 1 141 ? 1.026 24.815 30.906 1.00 29.18 ? 194 TYR A OH 1 ATOM 1111 N N . GLY A 1 142 ? 8.276 28.605 27.725 1.00 27.79 ? 195 GLY A N 1 ATOM 1112 C CA . GLY A 1 142 ? 9.615 29.124 27.492 1.00 27.69 ? 195 GLY A CA 1 ATOM 1113 C C . GLY A 1 142 ? 10.731 28.184 27.914 1.00 27.75 ? 195 GLY A C 1 ATOM 1114 O O . GLY A 1 142 ? 11.888 28.593 28.054 1.00 28.36 ? 195 GLY A O 1 ATOM 1115 N N . LYS A 1 143 ? 10.393 26.918 28.117 1.00 26.54 ? 196 LYS A N 1 ATOM 1116 C CA . LYS A 1 143 ? 11.372 25.939 28.570 1.00 24.64 ? 196 LYS A CA 1 ATOM 1117 C C . LYS A 1 143 ? 11.916 25.148 27.374 1.00 25.55 ? 196 LYS A C 1 ATOM 1118 O O . LYS A 1 143 ? 11.163 24.489 26.665 1.00 23.47 ? 196 LYS A O 1 ATOM 1119 C CB . LYS A 1 143 ? 10.723 25.005 29.588 1.00 25.07 ? 196 LYS A CB 1 ATOM 1120 C CG . LYS A 1 143 ? 11.656 23.979 30.186 1.00 27.55 ? 196 LYS A CG 1 ATOM 1121 C CD . LYS A 1 143 ? 13.045 24.553 30.383 1.00 26.87 ? 196 LYS A CD 1 ATOM 1122 C CE . LYS A 1 143 ? 13.145 25.304 31.687 1.00 25.51 ? 196 LYS A CE 1 ATOM 1123 N NZ . LYS A 1 143 ? 14.347 24.901 32.451 1.00 27.54 ? 196 LYS A NZ 1 ATOM 1124 N N . LYS A 1 144 ? 13.218 25.255 27.134 1.00 23.38 ? 197 LYS A N 1 ATOM 1125 C CA . LYS A 1 144 ? 13.828 24.742 25.918 1.00 26.80 ? 197 LYS A CA 1 ATOM 1126 C C . LYS A 1 144 ? 14.661 23.513 26.270 1.00 24.46 ? 197 LYS A C 1 ATOM 1127 O O . LYS A 1 144 ? 15.686 23.622 26.950 1.00 23.66 ? 197 LYS A O 1 ATOM 1128 C CB . LYS A 1 144 ? 14.723 25.802 25.255 1.00 30.17 ? 197 LYS A CB 1 ATOM 1129 C CG . LYS A 1 144 ? 14.216 27.259 25.340 1.00 35.50 ? 197 LYS A CG 1 ATOM 1130 C CD . LYS A 1 144 ? 13.070 27.520 24.379 1.00 34.93 ? 197 LYS A CD 1 ATOM 1131 C CE . LYS A 1 144 ? 12.971 28.991 23.958 1.00 32.24 ? 197 LYS A CE 1 ATOM 1132 N NZ . LYS A 1 144 ? 13.815 29.899 24.785 1.00 38.20 ? 197 LYS A NZ 1 ATOM 1133 N N . VAL A 1 145 ? 14.195 22.345 25.848 1.00 25.04 ? 198 VAL A N 1 ATOM 1134 C CA . VAL A 1 145 ? 14.856 21.084 26.178 1.00 27.38 ? 198 VAL A CA 1 ATOM 1135 C C . VAL A 1 145 ? 15.163 20.262 24.909 1.00 28.88 ? 198 VAL A C 1 ATOM 1136 O O . VAL A 1 145 ? 14.412 20.314 23.933 1.00 29.34 ? 198 VAL A O 1 ATOM 1137 C CB . VAL A 1 145 ? 14.010 20.269 27.169 1.00 29.57 ? 198 VAL A CB 1 ATOM 1138 C CG1 . VAL A 1 145 ? 13.711 21.109 28.416 1.00 27.29 ? 198 VAL A CG1 1 ATOM 1139 C CG2 . VAL A 1 145 ? 12.712 19.809 26.524 1.00 30.09 ? 198 VAL A CG2 1 ATOM 1140 N N . LEU A 1 146 ? 16.284 19.535 24.942 1.00 27.40 ? 199 LEU A N 1 ATOM 1141 C CA . LEU A 1 146 ? 16.784 18.724 23.822 1.00 26.32 ? 199 LEU A CA 1 ATOM 1142 C C . LEU A 1 146 ? 17.224 19.542 22.613 1.00 24.38 ? 199 LEU A C 1 ATOM 1143 O O . LEU A 1 146 ? 18.341 19.384 22.107 1.00 25.02 ? 199 LEU A O 1 ATOM 1144 C CB . LEU A 1 146 ? 15.752 17.686 23.397 1.00 25.71 ? 199 LEU A CB 1 ATOM 1145 C CG . LEU A 1 146 ? 15.436 16.598 24.422 1.00 28.12 ? 199 LEU A CG 1 ATOM 1146 C CD1 . LEU A 1 146 ? 14.468 15.583 23.816 1.00 29.81 ? 199 LEU A CD1 1 ATOM 1147 C CD2 . LEU A 1 146 ? 16.707 15.913 24.898 1.00 29.19 ? 199 LEU A CD2 1 ATOM 1148 N N . ILE A 1 147 ? 16.352 20.416 22.136 1.00 19.88 ? 200 ILE A N 1 ATOM 1149 C CA . ILE A 1 147 ? 16.678 21.244 20.991 1.00 21.41 ? 200 ILE A CA 1 ATOM 1150 C C . ILE A 1 147 ? 16.194 22.661 21.226 1.00 26.11 ? 200 ILE A C 1 ATOM 1151 O O . ILE A 1 147 ? 15.008 22.875 21.457 1.00 27.72 ? 200 ILE A O 1 ATOM 1152 C CB . ILE A 1 147 ? 16.004 20.673 19.729 1.00 26.48 ? 200 ILE A CB 1 ATOM 1153 C CG1 . ILE A 1 147 ? 16.532 19.266 19.442 1.00 27.63 ? 200 ILE A CG1 1 ATOM 1154 C CG2 . ILE A 1 147 ? 16.235 21.589 18.538 1.00 28.52 ? 200 ILE A CG2 1 ATOM 1155 C CD1 . ILE A 1 147 ? 15.589 18.428 18.608 1.00 33.02 ? 200 ILE A CD1 1 ATOM 1156 N N . ASN A 1 148 ? 17.111 23.620 21.177 1.00 27.57 ? 201 ASN A N 1 ATOM 1157 C CA . ASN A 1 148 ? 16.829 24.996 21.592 1.00 30.84 ? 201 ASN A CA 1 ATOM 1158 C C . ASN A 1 148 ? 16.476 25.856 20.393 1.00 29.99 ? 201 ASN A C 1 ATOM 1159 O O . ASN A 1 148 ? 17.361 26.351 19.695 1.00 36.17 ? 201 ASN A O 1 ATOM 1160 C CB . ASN A 1 148 ? 18.048 25.584 22.315 1.00 29.10 ? 201 ASN A CB 1 ATOM 1161 C CG . ASN A 1 148 ? 17.813 26.992 22.848 1.00 32.00 ? 201 ASN A CG 1 ATOM 1162 O OD1 . ASN A 1 148 ? 16.691 27.504 22.864 1.00 27.21 ? 201 ASN A OD1 1 ATOM 1163 N ND2 . ASN A 1 148 ? 18.892 27.627 23.290 1.00 35.46 ? 201 ASN A ND2 1 ATOM 1164 N N . LEU A 1 149 ? 15.176 26.012 20.160 1.00 29.59 ? 202 LEU A N 1 ATOM 1165 C CA . LEU A 1 149 ? 14.654 26.848 19.085 1.00 31.34 ? 202 LEU A CA 1 ATOM 1166 C C . LEU A 1 149 ? 14.103 28.154 19.651 1.00 28.21 ? 202 LEU A C 1 ATOM 1167 O O . LEU A 1 149 ? 13.233 28.132 20.516 1.00 27.20 ? 202 LEU A O 1 ATOM 1168 C CB . LEU A 1 149 ? 13.545 26.096 18.345 1.00 33.65 ? 202 LEU A CB 1 ATOM 1169 C CG . LEU A 1 149 ? 12.962 26.750 17.091 1.00 35.72 ? 202 LEU A CG 1 ATOM 1170 C CD1 . LEU A 1 149 ? 12.015 27.888 17.456 1.00 36.71 ? 202 LEU A CD1 1 ATOM 1171 C CD2 . LEU A 1 149 ? 14.071 27.237 16.178 1.00 38.91 ? 202 LEU A CD2 1 ATOM 1172 N N . PHE A 1 150 ? 14.616 29.286 19.175 1.00 30.08 ? 203 PHE A N 1 ATOM 1173 C CA . PHE A 1 150 ? 14.124 30.595 19.608 1.00 32.20 ? 203 PHE A CA 1 ATOM 1174 C C . PHE A 1 150 ? 14.072 31.565 18.434 1.00 32.46 ? 203 PHE A C 1 ATOM 1175 O O . PHE A 1 150 ? 14.929 31.517 17.548 1.00 30.18 ? 203 PHE A O 1 ATOM 1176 C CB . PHE A 1 150 ? 15.017 31.173 20.713 1.00 32.12 ? 203 PHE A CB 1 ATOM 1177 C CG . PHE A 1 150 ? 16.467 31.311 20.322 1.00 30.43 ? 203 PHE A CG 1 ATOM 1178 C CD1 . PHE A 1 150 ? 16.969 32.521 19.899 1.00 27.34 ? 203 PHE A CD1 1 ATOM 1179 C CD2 . PHE A 1 150 ? 17.324 30.225 20.382 1.00 29.70 ? 203 PHE A CD2 1 ATOM 1180 C CE1 . PHE A 1 150 ? 18.288 32.647 19.542 1.00 28.83 ? 203 PHE A CE1 1 ATOM 1181 C CE2 . PHE A 1 150 ? 18.649 30.355 20.028 1.00 26.34 ? 203 PHE A CE2 1 ATOM 1182 C CZ . PHE A 1 150 ? 19.128 31.558 19.607 1.00 28.15 ? 203 PHE A CZ 1 ATOM 1183 N N . VAL A 1 151 ? 13.090 32.461 18.435 1.00 32.24 ? 204 VAL A N 1 ATOM 1184 C CA . VAL A 1 151 ? 13.196 33.687 17.651 1.00 31.41 ? 204 VAL A CA 1 ATOM 1185 C C . VAL A 1 151 ? 14.149 34.697 18.287 1.00 31.17 ? 204 VAL A C 1 ATOM 1186 O O . VAL A 1 151 ? 13.992 35.080 19.446 1.00 28.00 ? 204 VAL A O 1 ATOM 1187 C CB . VAL A 1 151 ? 11.815 34.329 17.467 1.00 32.18 ? 204 VAL A CB 1 ATOM 1188 C CG1 . VAL A 1 151 ? 11.919 35.619 16.677 1.00 34.58 ? 204 VAL A CG1 1 ATOM 1189 C CG2 . VAL A 1 151 ? 10.887 33.355 16.775 1.00 36.06 ? 204 VAL A CG2 1 ATOM 1190 N N . GLY A 1 152 ? 15.149 35.120 17.516 1.00 28.15 ? 205 GLY A N 1 ATOM 1191 C CA . GLY A 1 152 ? 15.999 36.225 17.914 1.00 31.05 ? 205 GLY A CA 1 ATOM 1192 C C . GLY A 1 152 ? 16.388 37.120 16.753 1.00 33.14 ? 205 GLY A C 1 ATOM 1193 O O . GLY A 1 152 ? 15.920 36.949 15.628 1.00 33.92 ? 205 GLY A O 1 ATOM 1194 N N . THR A 1 153 ? 17.252 38.085 17.037 1.00 32.54 ? 206 THR A N 1 ATOM 1195 C CA . THR A 1 153 ? 17.768 38.984 16.016 1.00 31.94 ? 206 THR A CA 1 ATOM 1196 C C . THR A 1 153 ? 18.668 38.233 15.021 1.00 34.24 ? 206 THR A C 1 ATOM 1197 O O . THR A 1 153 ? 19.380 37.295 15.392 1.00 30.81 ? 206 THR A O 1 ATOM 1198 C CB . THR A 1 153 ? 18.552 40.115 16.687 1.00 31.06 ? 206 THR A CB 1 ATOM 1199 O OG1 . THR A 1 153 ? 17.695 40.855 17.566 1.00 31.15 ? 206 THR A OG1 1 ATOM 1200 C CG2 . THR A 1 153 ? 19.017 41.149 15.676 1.00 33.25 ? 206 THR A CG2 1 ATOM 1201 N N . ASP A 1 154 ? 18.645 38.662 13.763 1.00 32.01 ? 207 ASP A N 1 ATOM 1202 C CA . ASP A 1 154 ? 19.526 38.089 12.739 1.00 31.90 ? 207 ASP A CA 1 ATOM 1203 C C . ASP A 1 154 ? 20.905 38.729 12.765 1.00 30.46 ? 207 ASP A C 1 ATOM 1204 O O . ASP A 1 154 ? 21.058 39.902 12.419 1.00 32.39 ? 207 ASP A O 1 ATOM 1205 C CB . ASP A 1 154 ? 18.906 38.265 11.351 1.00 32.26 ? 207 ASP A CB 1 ATOM 1206 C CG . ASP A 1 154 ? 19.583 37.408 10.295 1.00 34.67 ? 207 ASP A CG 1 ATOM 1207 O OD1 . ASP A 1 154 ? 18.922 37.072 9.283 1.00 33.34 ? 207 ASP A OD1 1 ATOM 1208 O OD2 . ASP A 1 154 ? 20.768 37.020 10.402 1.00 28.38 ? 207 ASP A OD2 1 ATOM 1209 N N . ASP A 1 155 ? 21.915 37.959 13.168 1.00 29.81 ? 208 ASP A N 1 ATOM 1210 C CA . ASP A 1 155 ? 23.274 38.490 13.300 1.00 27.34 ? 208 ASP A CA 1 ATOM 1211 C C . ASP A 1 155 ? 23.724 39.240 12.054 1.00 26.95 ? 208 ASP A C 1 ATOM 1212 O O . ASP A 1 155 ? 24.461 40.215 12.147 1.00 25.66 ? 208 ASP A O 1 ATOM 1213 C CB . ASP A 1 155 ? 24.273 37.374 13.567 1.00 28.86 ? 208 ASP A CB 1 ATOM 1214 C CG . ASP A 1 155 ? 24.080 36.741 14.911 1.00 31.87 ? 208 ASP A CG 1 ATOM 1215 O OD1 . ASP A 1 155 ? 24.414 35.542 15.050 1.00 26.64 ? 208 ASP A OD1 1 ATOM 1216 O OD2 . ASP A 1 155 ? 23.583 37.369 15.872 1.00 30.66 ? 208 ASP A OD2 1 ATOM 1217 N N . LYS A 1 156 ? 23.303 38.767 10.887 1.00 30.01 ? 209 LYS A N 1 ATOM 1218 C CA . LYS A 1 156 ? 23.755 39.368 9.633 1.00 32.07 ? 209 LYS A CA 1 ATOM 1219 C C . LYS A 1 156 ? 22.760 40.372 9.048 1.00 33.95 ? 209 LYS A C 1 ATOM 1220 O O . LYS A 1 156 ? 23.056 41.033 8.051 1.00 34.68 ? 209 LYS A O 1 ATOM 1221 C CB . LYS A 1 156 ? 24.062 38.287 8.601 1.00 30.11 ? 209 LYS A CB 1 ATOM 1222 C CG . LYS A 1 156 ? 25.440 37.672 8.771 1.00 31.43 ? 209 LYS A CG 1 ATOM 1223 C CD . LYS A 1 156 ? 25.876 36.913 7.523 1.00 33.04 ? 209 LYS A CD 1 ATOM 1224 C CE . LYS A 1 156 ? 26.209 35.464 7.842 1.00 36.45 ? 209 LYS A CE 1 ATOM 1225 N NZ . LYS A 1 156 ? 27.667 35.154 7.683 1.00 36.45 ? 209 LYS A NZ 1 ATOM 1226 N N . ASN A 1 157 ? 21.587 40.493 9.655 1.00 31.10 ? 210 ASN A N 1 ATOM 1227 C CA . ASN A 1 157 ? 20.679 41.577 9.295 1.00 33.28 ? 210 ASN A CA 1 ATOM 1228 C C . ASN A 1 157 ? 19.876 42.103 10.477 1.00 30.66 ? 210 ASN A C 1 ATOM 1229 O O . ASN A 1 157 ? 18.815 41.582 10.795 1.00 30.63 ? 210 ASN A O 1 ATOM 1230 C CB . ASN A 1 157 ? 19.725 41.137 8.188 1.00 37.23 ? 210 ASN A CB 1 ATOM 1231 C CG . ASN A 1 157 ? 19.132 42.316 7.435 1.00 41.89 ? 210 ASN A CG 1 ATOM 1232 O OD1 . ASN A 1 157 ? 19.155 43.453 7.918 1.00 43.26 ? 210 ASN A OD1 1 ATOM 1233 N ND2 . ASN A 1 157 ? 18.612 42.054 6.242 1.00 43.06 ? 210 ASN A ND2 1 ATOM 1234 N N . SER A 1 158 ? 20.383 43.163 11.091 1.00 32.65 ? 211 SER A N 1 ATOM 1235 C CA . SER A 1 158 ? 20.112 43.451 12.493 1.00 35.68 ? 211 SER A CA 1 ATOM 1236 C C . SER A 1 158 ? 18.736 44.090 12.684 1.00 36.40 ? 211 SER A C 1 ATOM 1237 O O . SER A 1 158 ? 18.314 44.338 13.806 1.00 32.56 ? 211 SER A O 1 ATOM 1238 C CB . SER A 1 158 ? 21.194 44.369 13.051 1.00 34.06 ? 211 SER A CB 1 ATOM 1239 O OG . SER A 1 158 ? 21.255 45.591 12.339 1.00 36.73 ? 211 SER A OG 1 ATOM 1240 N N . VAL A 1 159 ? 18.040 44.356 11.584 1.00 36.45 ? 212 VAL A N 1 ATOM 1241 C CA . VAL A 1 159 ? 16.688 44.890 11.660 1.00 34.30 ? 212 VAL A CA 1 ATOM 1242 C C . VAL A 1 159 ? 15.663 43.780 11.713 1.00 30.93 ? 212 VAL A C 1 ATOM 1243 O O . VAL A 1 159 ? 14.503 44.017 12.019 1.00 35.08 ? 212 VAL A O 1 ATOM 1244 C CB . VAL A 1 159 ? 16.366 45.766 10.446 1.00 36.62 ? 212 VAL A CB 1 ATOM 1245 C CG1 . VAL A 1 159 ? 17.448 46.802 10.248 1.00 38.54 ? 212 VAL A CG1 1 ATOM 1246 C CG2 . VAL A 1 159 ? 16.201 44.898 9.211 1.00 36.61 ? 212 VAL A CG2 1 ATOM 1247 N N . ASN A 1 160 ? 16.088 42.563 11.395 1.00 30.10 ? 213 ASN A N 1 ATOM 1248 C CA . ASN A 1 160 ? 15.163 41.460 11.229 1.00 31.40 ? 213 ASN A CA 1 ATOM 1249 C C . ASN A 1 160 ? 15.292 40.451 12.357 1.00 29.71 ? 213 ASN A C 1 ATOM 1250 O O . ASN A 1 160 ? 16.328 40.368 13.022 1.00 32.27 ? 213 ASN A O 1 ATOM 1251 C CB . ASN A 1 160 ? 15.402 40.755 9.893 1.00 34.82 ? 213 ASN A CB 1 ATOM 1252 C CG . ASN A 1 160 ? 15.042 41.627 8.701 1.00 38.95 ? 213 ASN A CG 1 ATOM 1253 O OD1 . ASN A 1 160 ? 14.229 42.545 8.813 1.00 35.53 ? 213 ASN A OD1 1 ATOM 1254 N ND2 . ASN A 1 160 ? 15.648 41.337 7.550 1.00 41.96 ? 213 ASN A ND2 1 ATOM 1255 N N . HIS A 1 161 ? 14.239 39.672 12.551 1.00 30.71 ? 214 HIS A N 1 ATOM 1256 C CA . HIS A 1 161 ? 14.316 38.476 13.369 1.00 33.02 ? 214 HIS A CA 1 ATOM 1257 C C . HIS A 1 161 ? 14.358 37.233 12.503 1.00 33.67 ? 214 HIS A C 1 ATOM 1258 O O . HIS A 1 161 ? 13.930 37.256 11.346 1.00 30.81 ? 214 HIS A O 1 ATOM 1259 C CB . HIS A 1 161 ? 13.124 38.415 14.323 1.00 33.32 ? 214 HIS A CB 1 ATOM 1260 C CG . HIS A 1 161 ? 13.024 39.604 15.225 1.00 37.85 ? 214 HIS A CG 1 ATOM 1261 N ND1 . HIS A 1 161 ? 11.948 40.463 15.210 1.00 41.18 ? 214 HIS A ND1 1 ATOM 1262 C CD2 . HIS A 1 161 ? 13.878 40.088 16.157 1.00 41.03 ? 214 HIS A CD2 1 ATOM 1263 C CE1 . HIS A 1 161 ? 12.139 41.422 16.099 1.00 41.17 ? 214 HIS A CE1 1 ATOM 1264 N NE2 . HIS A 1 161 ? 13.304 41.218 16.686 1.00 40.87 ? 214 HIS A NE2 1 ATOM 1265 N N . VAL A 1 162 ? 14.875 36.153 13.079 1.00 29.34 ? 215 VAL A N 1 ATOM 1266 C CA . VAL A 1 162 ? 14.867 34.852 12.443 1.00 32.00 ? 215 VAL A CA 1 ATOM 1267 C C . VAL A 1 162 ? 14.794 33.750 13.487 1.00 34.16 ? 215 VAL A C 1 ATOM 1268 O O . VAL A 1 162 ? 15.191 33.941 14.635 1.00 35.80 ? 215 VAL A O 1 ATOM 1269 C CB . VAL A 1 162 ? 16.145 34.622 11.627 1.00 35.48 ? 215 VAL A CB 1 ATOM 1270 C CG1 . VAL A 1 162 ? 16.060 33.297 10.895 1.00 34.82 ? 215 VAL A CG1 1 ATOM 1271 C CG2 . VAL A 1 162 ? 16.370 35.759 10.657 1.00 36.91 ? 215 VAL A CG2 1 ATOM 1272 N N . ILE A 1 163 ? 14.298 32.591 13.082 1.00 33.68 ? 216 ILE A N 1 ATOM 1273 C CA . ILE A 1 163 ? 14.344 31.413 13.930 1.00 33.26 ? 216 ILE A CA 1 ATOM 1274 C C . ILE A 1 163 ? 15.765 30.866 14.034 1.00 33.24 ? 216 ILE A C 1 ATOM 1275 O O . ILE A 1 163 ? 16.501 30.817 13.046 1.00 32.10 ? 216 ILE A O 1 ATOM 1276 C CB . ILE A 1 163 ? 13.405 30.342 13.385 1.00 33.49 ? 216 ILE A CB 1 ATOM 1277 C CG1 . ILE A 1 163 ? 11.987 30.893 13.280 1.00 35.11 ? 216 ILE A CG1 1 ATOM 1278 C CG2 . ILE A 1 163 ? 13.424 29.103 14.274 1.00 34.65 ? 216 ILE A CG2 1 ATOM 1279 C CD1 . ILE A 1 163 ? 11.000 29.879 12.776 1.00 35.00 ? 216 ILE A CD1 1 ATOM 1280 N N . HIS A 1 164 ? 16.135 30.474 15.252 1.00 31.64 ? 217 HIS A N 1 ATOM 1281 C CA . HIS A 1 164 ? 17.458 29.955 15.565 1.00 27.54 ? 217 HIS A CA 1 ATOM 1282 C C . HIS A 1 164 ? 17.309 28.543 16.074 1.00 27.28 ? 217 HIS A C 1 ATOM 1283 O O . HIS A 1 164 ? 16.315 28.212 16.720 1.00 30.80 ? 217 HIS A O 1 ATOM 1284 C CB . HIS A 1 164 ? 18.102 30.768 16.687 1.00 26.65 ? 217 HIS A CB 1 ATOM 1285 C CG . HIS A 1 164 ? 18.611 32.102 16.262 1.00 24.38 ? 217 HIS A CG 1 ATOM 1286 N ND1 . HIS A 1 164 ? 17.782 33.107 15.812 1.00 25.83 ? 217 HIS A ND1 1 ATOM 1287 C CD2 . HIS A 1 164 ? 19.861 32.613 16.248 1.00 25.27 ? 217 HIS A CD2 1 ATOM 1288 C CE1 . HIS A 1 164 ? 18.503 34.175 15.531 1.00 23.54 ? 217 HIS A CE1 1 ATOM 1289 N NE2 . HIS A 1 164 ? 19.768 33.901 15.782 1.00 27.55 ? 217 HIS A NE2 1 ATOM 1290 N N . ILE A 1 165 ? 18.309 27.711 15.824 1.00 26.96 ? 218 ILE A N 1 ATOM 1291 C CA . ILE A 1 165 ? 18.366 26.406 16.462 1.00 26.26 ? 218 ILE A CA 1 ATOM 1292 C C . ILE A 1 165 ? 19.706 26.263 17.167 1.00 23.37 ? 218 ILE A C 1 ATOM 1293 O O . ILE A 1 165 ? 20.764 26.456 16.562 1.00 23.23 ? 218 ILE A O 1 ATOM 1294 C CB . ILE A 1 165 ? 18.169 25.286 15.410 1.00 28.58 ? 218 ILE A CB 1 ATOM 1295 C CG1 . ILE A 1 165 ? 16.918 25.557 14.583 1.00 30.58 ? 218 ILE A CG1 1 ATOM 1296 C CG2 . ILE A 1 165 ? 18.030 23.930 16.071 1.00 25.11 ? 218 ILE A CG2 1 ATOM 1297 C CD1 . ILE A 1 165 ? 15.711 24.792 15.056 1.00 32.27 ? 218 ILE A CD1 1 ATOM 1298 N N . ASP A 1 166 ? 19.669 25.951 18.457 1.00 22.78 ? 219 ASP A N 1 ATOM 1299 C CA . ASP A 1 166 ? 20.915 25.846 19.217 1.00 23.72 ? 219 ASP A CA 1 ATOM 1300 C C . ASP A 1 166 ? 20.827 24.706 20.216 1.00 21.22 ? 219 ASP A C 1 ATOM 1301 O O . ASP A 1 166 ? 19.750 24.155 20.451 1.00 24.79 ? 219 ASP A O 1 ATOM 1302 C CB . ASP A 1 166 ? 21.212 27.168 19.931 1.00 22.23 ? 219 ASP A CB 1 ATOM 1303 C CG . ASP A 1 166 ? 22.671 27.337 20.282 1.00 25.64 ? 219 ASP A CG 1 ATOM 1304 O OD1 . ASP A 1 166 ? 23.455 26.370 20.114 1.00 26.83 ? 219 ASP A OD1 1 ATOM 1305 O OD2 . ASP A 1 166 ? 23.128 28.418 20.734 1.00 23.18 ? 219 ASP A OD2 1 ATOM 1306 N N . GLN A 1 167 ? 21.961 24.345 20.806 1.00 22.29 ? 220 GLN A N 1 ATOM 1307 C CA . GLN A 1 167 ? 21.976 23.304 21.827 1.00 21.92 ? 220 GLN A CA 1 ATOM 1308 C C . GLN A 1 167 ? 21.284 23.841 23.071 1.00 23.60 ? 220 GLN A C 1 ATOM 1309 O O . GLN A 1 167 ? 21.293 25.037 23.311 1.00 22.72 ? 220 GLN A O 1 ATOM 1310 C CB . GLN A 1 167 ? 23.413 22.881 22.150 1.00 22.07 ? 220 GLN A CB 1 ATOM 1311 C CG . GLN A 1 167 ? 24.280 23.996 22.680 1.00 23.86 ? 220 GLN A CG 1 ATOM 1312 C CD . GLN A 1 167 ? 25.770 23.651 22.678 1.00 24.20 ? 220 GLN A CD 1 ATOM 1313 O OE1 . GLN A 1 167 ? 26.224 22.807 21.906 1.00 24.51 ? 220 GLN A OE1 1 ATOM 1314 N NE2 . GLN A 1 167 ? 26.523 24.314 23.534 1.00 19.93 ? 220 GLN A NE2 1 ATOM 1315 N N . PRO A 1 168 ? 20.679 22.963 23.859 1.00 22.90 ? 221 PRO A N 1 ATOM 1316 C CA . PRO A 1 168 ? 19.940 23.389 25.056 1.00 25.11 ? 221 PRO A CA 1 ATOM 1317 C C . PRO A 1 168 ? 20.844 23.621 26.270 1.00 23.43 ? 221 PRO A C 1 ATOM 1318 O O . PRO A 1 168 ? 21.952 23.103 26.316 1.00 19.30 ? 221 PRO A O 1 ATOM 1319 C CB . PRO A 1 168 ? 18.999 22.219 25.308 1.00 23.29 ? 221 PRO A CB 1 ATOM 1320 C CG . PRO A 1 168 ? 19.762 21.009 24.788 1.00 25.33 ? 221 PRO A CG 1 ATOM 1321 C CD . PRO A 1 168 ? 20.634 21.504 23.668 1.00 26.98 ? 221 PRO A CD 1 ATOM 1322 N N . ARG A 1 169 ? 20.370 24.407 27.230 1.00 24.10 ? 222 ARG A N 1 ATOM 1323 C CA . ARG A 1 169 ? 20.999 24.502 28.541 1.00 26.29 ? 222 ARG A CA 1 ATOM 1324 C C . ARG A 1 169 ? 20.836 23.185 29.303 1.00 24.37 ? 222 ARG A C 1 ATOM 1325 O O . ARG A 1 169 ? 19.950 22.383 29.002 1.00 22.07 ? 222 ARG A O 1 ATOM 1326 C CB . ARG A 1 169 ? 20.360 25.634 29.353 1.00 30.96 ? 222 ARG A CB 1 ATOM 1327 C CG . ARG A 1 169 ? 20.590 27.024 28.793 1.00 37.91 ? 222 ARG A CG 1 ATOM 1328 C CD . ARG A 1 169 ? 20.130 28.150 29.725 1.00 44.26 ? 222 ARG A CD 1 ATOM 1329 N NE . ARG A 1 169 ? 21.235 28.749 30.476 1.00 48.67 ? 222 ARG A NE 1 ATOM 1330 C CZ . ARG A 1 169 ? 21.373 30.053 30.687 1.00 53.86 ? 222 ARG A CZ 1 ATOM 1331 N NH1 . ARG A 1 169 ? 20.475 30.904 30.207 1.00 55.68 ? 222 ARG A NH1 1 ATOM 1332 N NH2 . ARG A 1 169 ? 22.408 30.512 31.379 1.00 57.06 ? 222 ARG A NH2 1 ATOM 1333 N N . LEU A 1 170 ? 21.680 22.983 30.304 1.00 20.81 ? 223 LEU A N 1 ATOM 1334 C CA . LEU A 1 170 ? 21.666 21.757 31.097 1.00 21.63 ? 223 LEU A CA 1 ATOM 1335 C C . LEU A 1 170 ? 21.168 22.046 32.502 1.00 20.75 ? 223 LEU A C 1 ATOM 1336 O O . LEU A 1 170 ? 21.188 23.185 32.947 1.00 17.30 ? 223 LEU A O 1 ATOM 1337 C CB . LEU A 1 170 ? 23.077 21.167 31.175 1.00 24.69 ? 223 LEU A CB 1 ATOM 1338 C CG . LEU A 1 170 ? 23.754 20.932 29.828 1.00 27.07 ? 223 LEU A CG 1 ATOM 1339 C CD1 . LEU A 1 170 ? 25.268 20.838 29.973 1.00 22.73 ? 223 LEU A CD1 1 ATOM 1340 C CD2 . LEU A 1 170 ? 23.190 19.679 29.179 1.00 27.25 ? 223 LEU A CD2 1 ATOM 1341 N N . GLY A 1 171 ? 20.745 21.007 33.208 1.00 16.50 ? 224 GLY A N 1 ATOM 1342 C CA . GLY A 1 171 ? 20.285 21.161 34.578 1.00 17.16 ? 224 GLY A CA 1 ATOM 1343 C C . GLY A 1 171 ? 21.393 21.512 35.549 1.00 18.74 ? 224 GLY A C 1 ATOM 1344 O O . GLY A 1 171 ? 21.154 22.218 36.530 1.00 17.39 ? 224 GLY A O 1 ATOM 1345 N N . LEU A 1 172 ? 22.609 21.034 35.275 1.00 16.52 ? 225 LEU A N 1 ATOM 1346 C CA . LEU A 1 172 ? 23.783 21.458 36.018 1.00 19.16 ? 225 LEU A CA 1 ATOM 1347 C C . LEU A 1 172 ? 24.419 22.657 35.325 1.00 18.25 ? 225 LEU A C 1 ATOM 1348 O O . LEU A 1 172 ? 24.136 22.908 34.164 1.00 15.85 ? 225 LEU A O 1 ATOM 1349 C CB . LEU A 1 172 ? 24.780 20.297 36.134 1.00 22.44 ? 225 LEU A CB 1 ATOM 1350 C CG . LEU A 1 172 ? 24.174 19.012 36.709 1.00 24.76 ? 225 LEU A CG 1 ATOM 1351 C CD1 . LEU A 1 172 ? 25.166 17.875 36.640 1.00 25.18 ? 225 LEU A CD1 1 ATOM 1352 C CD2 . LEU A 1 172 ? 23.708 19.231 38.136 1.00 29.13 ? 225 LEU A CD2 1 ATOM 1353 N N . PRO A 1 173 ? 25.240 23.433 36.032 1.00 16.06 ? 226 PRO A N 1 ATOM 1354 C CA . PRO A 1 173 ? 25.696 24.731 35.503 1.00 14.90 ? 226 PRO A CA 1 ATOM 1355 C C . PRO A 1 173 ? 26.555 24.682 34.227 1.00 17.19 ? 226 PRO A C 1 ATOM 1356 O O . PRO A 1 173 ? 26.473 25.611 33.420 1.00 13.68 ? 226 PRO A O 1 ATOM 1357 C CB . PRO A 1 173 ? 26.465 25.340 36.680 1.00 19.29 ? 226 PRO A CB 1 ATOM 1358 C CG . PRO A 1 173 ? 25.879 24.647 37.879 1.00 18.26 ? 226 PRO A CG 1 ATOM 1359 C CD . PRO A 1 173 ? 25.719 23.201 37.403 1.00 18.09 ? 226 PRO A CD 1 ATOM 1360 N N . SER A 1 174 ? 27.340 23.628 34.020 1.00 16.17 ? 227 SER A N 1 ATOM 1361 C CA . SER A 1 174 ? 28.083 23.486 32.769 1.00 16.45 ? 227 SER A CA 1 ATOM 1362 C C . SER A 1 174 ? 28.274 22.022 32.400 1.00 17.82 ? 227 SER A C 1 ATOM 1363 O O . SER A 1 174 ? 28.043 21.131 33.216 1.00 17.86 ? 227 SER A O 1 ATOM 1364 C CB . SER A 1 174 ? 29.460 24.136 32.873 1.00 19.11 ? 227 SER A CB 1 ATOM 1365 O OG . SER A 1 174 ? 30.309 23.330 33.670 1.00 19.98 ? 227 SER A OG 1 ATOM 1366 N N . ARG A 1 175 ? 28.712 21.775 31.170 1.00 16.78 ? 228 ARG A N 1 ATOM 1367 C CA . ARG A 1 175 ? 28.897 20.411 30.711 1.00 20.68 ? 228 ARG A CA 1 ATOM 1368 C C . ARG A 1 175 ? 29.915 19.676 31.581 1.00 20.30 ? 228 ARG A C 1 ATOM 1369 O O . ARG A 1 175 ? 29.873 18.449 31.713 1.00 16.62 ? 228 ARG A O 1 ATOM 1370 C CB . ARG A 1 175 ? 29.316 20.406 29.241 1.00 21.61 ? 228 ARG A CB 1 ATOM 1371 C CG . ARG A 1 175 ? 30.653 21.062 28.969 1.00 25.08 ? 228 ARG A CG 1 ATOM 1372 C CD . ARG A 1 175 ? 30.841 21.487 27.525 1.00 24.75 ? 228 ARG A CD 1 ATOM 1373 N NE . ARG A 1 175 ? 30.686 20.384 26.577 1.00 23.99 ? 228 ARG A NE 1 ATOM 1374 C CZ . ARG A 1 175 ? 31.572 19.413 26.403 1.00 27.29 ? 228 ARG A CZ 1 ATOM 1375 N NH1 . ARG A 1 175 ? 32.677 19.398 27.128 1.00 24.30 ? 228 ARG A NH1 1 ATOM 1376 N NH2 . ARG A 1 175 ? 31.351 18.452 25.508 1.00 24.18 ? 228 ARG A NH2 1 ATOM 1377 N N . ASP A 1 176 ? 30.829 20.432 32.182 1.00 18.61 ? 229 ASP A N 1 ATOM 1378 C CA . ASP A 1 176 ? 31.876 19.855 33.019 1.00 19.17 ? 229 ASP A CA 1 ATOM 1379 C C . ASP A 1 176 ? 31.343 19.040 34.173 1.00 20.56 ? 229 ASP A C 1 ATOM 1380 O O . ASP A 1 176 ? 31.944 18.040 34.565 1.00 22.71 ? 229 ASP A O 1 ATOM 1381 C CB . ASP A 1 176 ? 32.740 20.964 33.582 1.00 19.33 ? 229 ASP A CB 1 ATOM 1382 C CG . ASP A 1 176 ? 33.196 21.911 32.524 1.00 24.03 ? 229 ASP A CG 1 ATOM 1383 O OD1 . ASP A 1 176 ? 32.456 22.880 32.244 1.00 21.66 ? 229 ASP A OD1 1 ATOM 1384 O OD2 . ASP A 1 176 ? 34.277 21.753 31.913 1.00 22.02 ? 229 ASP A OD2 1 ATOM 1385 N N . TYR A 1 177 ? 30.226 19.487 34.732 1.00 17.27 ? 230 TYR A N 1 ATOM 1386 C CA . TYR A 1 177 ? 29.694 18.908 35.946 1.00 17.70 ? 230 TYR A CA 1 ATOM 1387 C C . TYR A 1 177 ? 29.366 17.451 35.708 1.00 17.09 ? 230 TYR A C 1 ATOM 1388 O O . TYR A 1 177 ? 29.410 16.644 36.627 1.00 17.35 ? 230 TYR A O 1 ATOM 1389 C CB . TYR A 1 177 ? 28.435 19.658 36.382 1.00 20.08 ? 230 TYR A CB 1 ATOM 1390 C CG . TYR A 1 177 ? 28.723 20.826 37.288 1.00 15.27 ? 230 TYR A CG 1 ATOM 1391 C CD1 . TYR A 1 177 ? 29.270 22.005 36.792 1.00 18.47 ? 230 TYR A CD1 1 ATOM 1392 C CD2 . TYR A 1 177 ? 28.431 20.765 38.645 1.00 18.46 ? 230 TYR A CD2 1 ATOM 1393 C CE1 . TYR A 1 177 ? 29.530 23.091 37.634 1.00 17.39 ? 230 TYR A CE1 1 ATOM 1394 C CE2 . TYR A 1 177 ? 28.685 21.837 39.488 1.00 17.71 ? 230 TYR A CE2 1 ATOM 1395 C CZ . TYR A 1 177 ? 29.242 22.993 38.987 1.00 18.72 ? 230 TYR A CZ 1 ATOM 1396 O OH . TYR A 1 177 ? 29.489 24.057 39.846 1.00 18.13 ? 230 TYR A OH 1 ATOM 1397 N N . TYR A 1 178 ? 29.033 17.125 34.465 1.00 18.27 ? 231 TYR A N 1 ATOM 1398 C CA . TYR A 1 178 ? 28.546 15.797 34.129 1.00 18.33 ? 231 TYR A CA 1 ATOM 1399 C C . TYR A 1 178 ? 29.673 14.750 34.119 1.00 19.84 ? 231 TYR A C 1 ATOM 1400 O O . TYR A 1 178 ? 29.415 13.548 33.975 1.00 17.77 ? 231 TYR A O 1 ATOM 1401 C CB . TYR A 1 178 ? 27.777 15.852 32.799 1.00 20.81 ? 231 TYR A CB 1 ATOM 1402 C CG . TYR A 1 178 ? 26.477 16.625 32.976 1.00 20.91 ? 231 TYR A CG 1 ATOM 1403 C CD1 . TYR A 1 178 ? 26.435 18.008 32.827 1.00 18.43 ? 231 TYR A CD1 1 ATOM 1404 C CD2 . TYR A 1 178 ? 25.320 15.981 33.375 1.00 18.94 ? 231 TYR A CD2 1 ATOM 1405 C CE1 . TYR A 1 178 ? 25.253 18.711 33.030 1.00 20.29 ? 231 TYR A CE1 1 ATOM 1406 C CE2 . TYR A 1 178 ? 24.140 16.677 33.586 1.00 21.63 ? 231 TYR A CE2 1 ATOM 1407 C CZ . TYR A 1 178 ? 24.113 18.040 33.412 1.00 20.45 ? 231 TYR A CZ 1 ATOM 1408 O OH . TYR A 1 178 ? 22.929 18.722 33.623 1.00 20.66 ? 231 TYR A OH 1 ATOM 1409 N N . GLU A 1 179 ? 30.910 15.189 34.328 1.00 22.74 ? 232 GLU A N 1 ATOM 1410 C CA . GLU A 1 179 ? 31.973 14.252 34.715 1.00 25.42 ? 232 GLU A CA 1 ATOM 1411 C C . GLU A 1 179 ? 31.599 13.529 35.996 1.00 22.55 ? 232 GLU A C 1 ATOM 1412 O O . GLU A 1 179 ? 31.830 12.333 36.135 1.00 20.15 ? 232 GLU A O 1 ATOM 1413 C CB . GLU A 1 179 ? 33.299 14.977 34.924 1.00 27.42 ? 232 GLU A CB 1 ATOM 1414 C CG . GLU A 1 179 ? 33.917 15.537 33.660 1.00 31.56 ? 232 GLU A CG 1 ATOM 1415 C CD . GLU A 1 179 ? 35.068 16.481 33.958 1.00 36.03 ? 232 GLU A CD 1 ATOM 1416 O OE1 . GLU A 1 179 ? 35.130 17.561 33.329 1.00 37.57 ? 232 GLU A OE1 1 ATOM 1417 O OE2 . GLU A 1 179 ? 35.906 16.142 34.831 1.00 37.46 ? 232 GLU A OE2 1 ATOM 1418 N N . CYS A 1 180 ? 31.040 14.282 36.941 1.00 21.28 ? 233 CYS A N 1 ATOM 1419 C CA . CYS A 1 180 ? 30.441 13.730 38.151 1.00 19.36 ? 233 CYS A CA 1 ATOM 1420 C C . CYS A 1 180 ? 31.467 13.041 39.066 1.00 22.97 ? 233 CYS A C 1 ATOM 1421 O O . CYS A 1 180 ? 31.119 12.199 39.887 1.00 23.90 ? 233 CYS A O 1 ATOM 1422 C CB . CYS A 1 180 ? 29.329 12.757 37.774 1.00 23.47 ? 233 CYS A CB 1 ATOM 1423 S SG . CYS A 1 180 ? 27.898 13.630 37.093 1.00 21.48 ? 233 CYS A SG 1 ATOM 1424 N N . THR A 1 181 ? 32.723 13.451 38.963 1.00 21.48 ? 234 THR A N 1 ATOM 1425 C CA . THR A 1 181 ? 33.731 12.987 39.904 1.00 26.25 ? 234 THR A CA 1 ATOM 1426 C C . THR A 1 181 ? 34.336 14.153 40.669 1.00 26.56 ? 234 THR A C 1 ATOM 1427 O O . THR A 1 181 ? 34.142 15.319 40.308 1.00 25.22 ? 234 THR A O 1 ATOM 1428 C CB . THR A 1 181 ? 34.839 12.239 39.160 1.00 24.07 ? 234 THR A CB 1 ATOM 1429 O OG1 . THR A 1 181 ? 35.358 13.045 38.096 1.00 26.70 ? 234 THR A OG1 1 ATOM 1430 C CG2 . THR A 1 181 ? 34.290 11.002 38.453 1.00 26.03 ? 234 THR A CG2 1 ATOM 1431 N N . GLY A 1 182 ? 35.103 13.835 41.705 1.00 23.85 ? 235 GLY A N 1 ATOM 1432 C CA . GLY A 1 182 ? 35.919 14.837 42.362 1.00 22.73 ? 235 GLY A CA 1 ATOM 1433 C C . GLY A 1 182 ? 35.049 16.013 42.763 1.00 22.41 ? 235 GLY A C 1 ATOM 1434 O O . GLY A 1 182 ? 34.068 15.836 43.477 1.00 20.28 ? 235 GLY A O 1 ATOM 1435 N N . ILE A 1 183 ? 35.410 17.211 42.321 1.00 21.76 ? 236 ILE A N 1 ATOM 1436 C CA . ILE A 1 183 ? 34.733 18.426 42.775 1.00 21.08 ? 236 ILE A CA 1 ATOM 1437 C C . ILE A 1 183 ? 33.294 18.528 42.272 1.00 19.76 ? 236 ILE A C 1 ATOM 1438 O O . ILE A 1 183 ? 32.540 19.397 42.728 1.00 19.97 ? 236 ILE A O 1 ATOM 1439 C CB . ILE A 1 183 ? 35.504 19.683 42.333 1.00 22.10 ? 236 ILE A CB 1 ATOM 1440 C CG1 . ILE A 1 183 ? 35.553 19.754 40.802 1.00 22.39 ? 236 ILE A CG1 1 ATOM 1441 C CG2 . ILE A 1 183 ? 36.907 19.695 42.941 1.00 23.71 ? 236 ILE A CG2 1 ATOM 1442 C CD1 . ILE A 1 183 ? 36.282 20.944 40.278 1.00 22.95 ? 236 ILE A CD1 1 ATOM 1443 N N . TYR A 1 184 ? 32.901 17.638 41.363 1.00 15.96 ? 237 TYR A N 1 ATOM 1444 C CA . TYR A 1 184 ? 31.543 17.656 40.807 1.00 17.70 ? 237 TYR A CA 1 ATOM 1445 C C . TYR A 1 184 ? 30.645 16.567 41.397 1.00 21.02 ? 237 TYR A C 1 ATOM 1446 O O . TYR A 1 184 ? 29.446 16.491 41.095 1.00 21.11 ? 237 TYR A O 1 ATOM 1447 C CB . TYR A 1 184 ? 31.585 17.504 39.285 1.00 20.43 ? 237 TYR A CB 1 ATOM 1448 C CG . TYR A 1 184 ? 32.404 18.563 38.601 1.00 19.21 ? 237 TYR A CG 1 ATOM 1449 C CD1 . TYR A 1 184 ? 31.981 19.903 38.616 1.00 21.17 ? 237 TYR A CD1 1 ATOM 1450 C CD2 . TYR A 1 184 ? 33.581 18.255 37.937 1.00 19.80 ? 237 TYR A CD2 1 ATOM 1451 C CE1 . TYR A 1 184 ? 32.714 20.889 37.999 1.00 20.80 ? 237 TYR A CE1 1 ATOM 1452 C CE2 . TYR A 1 184 ? 34.318 19.238 37.314 1.00 21.90 ? 237 TYR A CE2 1 ATOM 1453 C CZ . TYR A 1 184 ? 33.876 20.560 37.347 1.00 22.56 ? 237 TYR A CZ 1 ATOM 1454 O OH . TYR A 1 184 ? 34.625 21.539 36.735 1.00 20.06 ? 237 TYR A OH 1 ATOM 1455 N N . LYS A 1 185 ? 31.229 15.716 42.232 1.00 23.92 ? 238 LYS A N 1 ATOM 1456 C CA . LYS A 1 185 ? 30.544 14.529 42.713 1.00 25.64 ? 238 LYS A CA 1 ATOM 1457 C C . LYS A 1 185 ? 29.296 14.906 43.502 1.00 24.28 ? 238 LYS A C 1 ATOM 1458 O O . LYS A 1 185 ? 28.216 14.357 43.273 1.00 22.10 ? 238 LYS A O 1 ATOM 1459 C CB . LYS A 1 185 ? 31.481 13.689 43.584 1.00 29.30 ? 238 LYS A CB 1 ATOM 1460 C CG . LYS A 1 185 ? 30.953 12.300 43.914 1.00 32.90 ? 238 LYS A CG 1 ATOM 1461 C CD . LYS A 1 185 ? 32.100 11.296 44.048 1.00 38.11 ? 238 LYS A CD 1 ATOM 1462 C CE . LYS A 1 185 ? 32.178 10.712 45.452 1.00 42.73 ? 238 LYS A CE 1 ATOM 1463 N NZ . LYS A 1 185 ? 32.616 9.275 45.446 1.00 43.24 ? 238 LYS A NZ 1 ATOM 1464 N N . GLU A 1 186 ? 29.436 15.845 44.428 1.00 22.87 ? 239 GLU A N 1 ATOM 1465 C CA . GLU A 1 186 ? 28.318 16.191 45.298 1.00 24.80 ? 239 GLU A CA 1 ATOM 1466 C C . GLU A 1 186 ? 27.156 16.810 44.501 1.00 21.40 ? 239 GLU A C 1 ATOM 1467 O O . GLU A 1 186 ? 26.000 16.573 44.810 1.00 20.07 ? 239 GLU A O 1 ATOM 1468 C CB . GLU A 1 186 ? 28.777 17.124 46.422 1.00 29.34 ? 239 GLU A CB 1 ATOM 1469 C CG . GLU A 1 186 ? 27.644 17.771 47.216 1.00 33.87 ? 239 GLU A CG 1 ATOM 1470 C CD . GLU A 1 186 ? 26.743 16.767 47.929 1.00 37.82 ? 239 GLU A CD 1 ATOM 1471 O OE1 . GLU A 1 186 ? 27.136 15.595 48.098 1.00 41.72 ? 239 GLU A OE1 1 ATOM 1472 O OE2 . GLU A 1 186 ? 25.628 17.156 48.332 1.00 38.79 ? 239 GLU A OE2 1 ATOM 1473 N N . ALA A 1 187 ? 27.454 17.585 43.467 1.00 18.13 ? 240 ALA A N 1 ATOM 1474 C CA . ALA A 1 187 ? 26.393 18.249 42.717 1.00 19.23 ? 240 ALA A CA 1 ATOM 1475 C C . ALA A 1 187 ? 25.605 17.214 41.916 1.00 20.10 ? 240 ALA A C 1 ATOM 1476 O O . ALA A 1 187 ? 24.391 17.305 41.782 1.00 17.15 ? 240 ALA A O 1 ATOM 1477 C CB . ALA A 1 187 ? 26.969 19.285 41.800 1.00 18.24 ? 240 ALA A CB 1 ATOM 1478 N N . CYS A 1 188 ? 26.306 16.225 41.381 1.00 19.76 ? 241 CYS A N 1 ATOM 1479 C CA . CYS A 1 188 ? 25.660 15.217 40.555 1.00 20.12 ? 241 CYS A CA 1 ATOM 1480 C C . CYS A 1 188 ? 24.800 14.337 41.430 1.00 22.57 ? 241 CYS A C 1 ATOM 1481 O O . CYS A 1 188 ? 23.692 13.941 41.052 1.00 22.67 ? 241 CYS A O 1 ATOM 1482 C CB . CYS A 1 188 ? 26.696 14.376 39.815 1.00 21.33 ? 241 CYS A CB 1 ATOM 1483 S SG . CYS A 1 188 ? 27.399 15.141 38.344 1.00 21.58 ? 241 CYS A SG 1 ATOM 1484 N N . THR A 1 189 ? 25.310 14.047 42.615 1.00 21.79 ? 242 THR A N 1 ATOM 1485 C CA . THR A 1 189 ? 24.563 13.297 43.600 1.00 23.48 ? 242 THR A CA 1 ATOM 1486 C C . THR A 1 189 ? 23.335 14.078 44.085 1.00 26.90 ? 242 THR A C 1 ATOM 1487 O O . THR A 1 189 ? 22.245 13.516 44.224 1.00 21.82 ? 242 THR A O 1 ATOM 1488 C CB . THR A 1 189 ? 25.486 12.934 44.769 1.00 20.80 ? 242 THR A CB 1 ATOM 1489 O OG1 . THR A 1 189 ? 26.460 11.975 44.334 1.00 16.92 ? 242 THR A OG1 1 ATOM 1490 C CG2 . THR A 1 189 ? 24.724 12.232 45.875 1.00 24.68 ? 242 THR A CG2 1 ATOM 1491 N N . ALA A 1 190 ? 23.502 15.373 44.326 1.00 22.51 ? 243 ALA A N 1 ATOM 1492 C CA . ALA A 1 190 ? 22.395 16.186 44.817 1.00 20.96 ? 243 ALA A CA 1 ATOM 1493 C C . ALA A 1 190 ? 21.321 16.375 43.741 1.00 17.78 ? 243 ALA A C 1 ATOM 1494 O O . ALA A 1 190 ? 20.130 16.432 44.046 1.00 18.86 ? 243 ALA A O 1 ATOM 1495 C CB . ALA A 1 190 ? 22.912 17.542 45.320 1.00 19.23 ? 243 ALA A CB 1 ATOM 1496 N N . TYR A 1 191 ? 21.767 16.471 42.495 1.00 20.22 ? 244 TYR A N 1 ATOM 1497 C CA . TYR A 1 191 ? 20.911 16.643 41.322 1.00 16.82 ? 244 TYR A CA 1 ATOM 1498 C C . TYR A 1 191 ? 19.961 15.453 41.185 1.00 21.26 ? 244 TYR A C 1 ATOM 1499 O O . TYR A 1 191 ? 18.744 15.616 41.019 1.00 16.99 ? 244 TYR A O 1 ATOM 1500 C CB . TYR A 1 191 ? 21.797 16.774 40.074 1.00 16.52 ? 244 TYR A CB 1 ATOM 1501 C CG . TYR A 1 191 ? 21.092 17.123 38.771 1.00 20.06 ? 244 TYR A CG 1 ATOM 1502 C CD1 . TYR A 1 191 ? 21.403 16.449 37.589 1.00 16.75 ? 244 TYR A CD1 1 ATOM 1503 C CD2 . TYR A 1 191 ? 20.148 18.143 38.712 1.00 19.85 ? 244 TYR A CD2 1 ATOM 1504 C CE1 . TYR A 1 191 ? 20.777 16.760 36.399 1.00 18.27 ? 244 TYR A CE1 1 ATOM 1505 C CE2 . TYR A 1 191 ? 19.516 18.470 37.517 1.00 19.74 ? 244 TYR A CE2 1 ATOM 1506 C CZ . TYR A 1 191 ? 19.829 17.776 36.365 1.00 21.99 ? 244 TYR A CZ 1 ATOM 1507 O OH . TYR A 1 191 ? 19.201 18.096 35.176 1.00 19.35 ? 244 TYR A OH 1 ATOM 1508 N N . VAL A 1 192 ? 20.511 14.247 41.273 1.00 18.11 ? 245 VAL A N 1 ATOM 1509 C CA . VAL A 1 192 ? 19.674 13.056 41.146 1.00 22.49 ? 245 VAL A CA 1 ATOM 1510 C C . VAL A 1 192 ? 18.782 12.861 42.380 1.00 22.52 ? 245 VAL A C 1 ATOM 1511 O O . VAL A 1 192 ? 17.602 12.513 42.250 1.00 22.78 ? 245 VAL A O 1 ATOM 1512 C CB . VAL A 1 192 ? 20.526 11.811 40.827 1.00 22.63 ? 245 VAL A CB 1 ATOM 1513 C CG1 . VAL A 1 192 ? 19.685 10.552 40.797 1.00 24.70 ? 245 VAL A CG1 1 ATOM 1514 C CG2 . VAL A 1 192 ? 21.220 12.010 39.487 1.00 25.28 ? 245 VAL A CG2 1 ATOM 1515 N N . ASP A 1 193 ? 19.327 13.116 43.567 1.00 22.67 ? 246 ASP A N 1 ATOM 1516 C CA . ASP A 1 193 ? 18.539 13.065 44.798 1.00 23.95 ? 246 ASP A CA 1 ATOM 1517 C C . ASP A 1 193 ? 17.366 14.050 44.727 1.00 23.47 ? 246 ASP A C 1 ATOM 1518 O O . ASP A 1 193 ? 16.273 13.790 45.254 1.00 21.48 ? 246 ASP A O 1 ATOM 1519 C CB . ASP A 1 193 ? 19.416 13.402 46.008 1.00 24.96 ? 246 ASP A CB 1 ATOM 1520 C CG . ASP A 1 193 ? 20.267 12.221 46.483 1.00 28.49 ? 246 ASP A CG 1 ATOM 1521 O OD1 . ASP A 1 193 ? 20.175 11.101 45.917 1.00 28.83 ? 246 ASP A OD1 1 ATOM 1522 O OD2 . ASP A 1 193 ? 21.062 12.342 47.433 1.00 29.08 ? 246 ASP A OD2 1 ATOM 1523 N N . PHE A 1 194 ? 17.611 15.181 44.069 1.00 20.12 ? 247 PHE A N 1 ATOM 1524 C CA . PHE A 1 194 ? 16.620 16.252 43.904 1.00 20.32 ? 247 PHE A CA 1 ATOM 1525 C C . PHE A 1 194 ? 15.497 15.787 42.985 1.00 22.97 ? 247 PHE A C 1 ATOM 1526 O O . PHE A 1 194 ? 14.331 15.864 43.346 1.00 21.71 ? 247 PHE A O 1 ATOM 1527 C CB . PHE A 1 194 ? 17.314 17.500 43.331 1.00 21.21 ? 247 PHE A CB 1 ATOM 1528 C CG . PHE A 1 194 ? 16.422 18.730 43.204 1.00 20.22 ? 247 PHE A CG 1 ATOM 1529 C CD1 . PHE A 1 194 ? 16.778 19.754 42.343 1.00 20.82 ? 247 PHE A CD1 1 ATOM 1530 C CD2 . PHE A 1 194 ? 15.266 18.872 43.953 1.00 20.08 ? 247 PHE A CD2 1 ATOM 1531 C CE1 . PHE A 1 194 ? 15.985 20.904 42.217 1.00 22.14 ? 247 PHE A CE1 1 ATOM 1532 C CE2 . PHE A 1 194 ? 14.460 20.012 43.820 1.00 19.90 ? 247 PHE A CE2 1 ATOM 1533 C CZ . PHE A 1 194 ? 14.829 21.026 42.954 1.00 20.11 ? 247 PHE A CZ 1 ATOM 1534 N N . MET A 1 195 ? 15.849 15.294 41.801 1.00 21.05 ? 248 MET A N 1 ATOM 1535 C CA . MET A 1 195 ? 14.898 14.554 40.975 1.00 24.88 ? 248 MET A CA 1 ATOM 1536 C C . MET A 1 195 ? 14.034 13.641 41.833 1.00 21.75 ? 248 MET A C 1 ATOM 1537 O O . MET A 1 195 ? 12.815 13.712 41.799 1.00 21.64 ? 248 MET A O 1 ATOM 1538 C CB . MET A 1 195 ? 15.622 13.710 39.923 1.00 24.25 ? 248 MET A CB 1 ATOM 1539 C CG . MET A 1 195 ? 16.424 14.518 38.908 1.00 23.38 ? 248 MET A CG 1 ATOM 1540 S SD . MET A 1 195 ? 17.345 13.486 37.736 1.00 23.66 ? 248 MET A SD 1 ATOM 1541 C CE . MET A 1 195 ? 18.377 14.687 36.986 1.00 19.90 ? 248 MET A CE 1 ATOM 1542 N N . ILE A 1 196 ? 14.682 12.763 42.584 1.00 25.74 ? 249 ILE A N 1 ATOM 1543 C CA . ILE A 1 196 ? 13.990 11.689 43.272 1.00 25.89 ? 249 ILE A CA 1 ATOM 1544 C C . ILE A 1 196 ? 13.041 12.271 44.318 1.00 25.63 ? 249 ILE A C 1 ATOM 1545 O O . ILE A 1 196 ? 11.883 11.851 44.412 1.00 20.99 ? 249 ILE A O 1 ATOM 1546 C CB . ILE A 1 196 ? 15.001 10.737 43.931 1.00 24.73 ? 249 ILE A CB 1 ATOM 1547 C CG1 . ILE A 1 196 ? 15.757 9.949 42.858 1.00 26.00 ? 249 ILE A CG1 1 ATOM 1548 C CG2 . ILE A 1 196 ? 14.290 9.775 44.884 1.00 27.46 ? 249 ILE A CG2 1 ATOM 1549 C CD1 . ILE A 1 196 ? 16.860 9.092 43.423 1.00 27.16 ? 249 ILE A CD1 1 ATOM 1550 N N . SER A 1 197 ? 13.527 13.248 45.086 1.00 23.72 ? 250 SER A N 1 ATOM 1551 C CA . SER A 1 197 ? 12.738 13.826 46.174 1.00 25.49 ? 250 SER A CA 1 ATOM 1552 C C . SER A 1 197 ? 11.455 14.471 45.658 1.00 28.30 ? 250 SER A C 1 ATOM 1553 O O . SER A 1 197 ? 10.409 14.416 46.321 1.00 26.08 ? 250 SER A O 1 ATOM 1554 C CB . SER A 1 197 ? 13.549 14.876 46.935 1.00 24.11 ? 250 SER A CB 1 ATOM 1555 O OG . SER A 1 197 ? 14.764 14.334 47.407 1.00 28.51 ? 250 SER A OG 1 ATOM 1556 N N . VAL A 1 198 ? 11.543 15.107 44.492 1.00 24.31 ? 251 VAL A N 1 ATOM 1557 C CA . VAL A 1 198 ? 10.384 15.787 43.934 1.00 27.54 ? 251 VAL A CA 1 ATOM 1558 C C . VAL A 1 198 ? 9.379 14.761 43.430 1.00 24.51 ? 251 VAL A C 1 ATOM 1559 O O . VAL A 1 198 ? 8.183 14.859 43.707 1.00 25.07 ? 251 VAL A O 1 ATOM 1560 C CB . VAL A 1 198 ? 10.778 16.737 42.787 1.00 26.87 ? 251 VAL A CB 1 ATOM 1561 C CG1 . VAL A 1 198 ? 9.544 17.288 42.119 1.00 26.62 ? 251 VAL A CG1 1 ATOM 1562 C CG2 . VAL A 1 198 ? 11.646 17.872 43.326 1.00 27.38 ? 251 VAL A CG2 1 ATOM 1563 N N . ALA A 1 199 ? 9.872 13.770 42.699 1.00 24.19 ? 252 ALA A N 1 ATOM 1564 C CA . ALA A 1 199 ? 9.015 12.711 42.188 1.00 25.52 ? 252 ALA A CA 1 ATOM 1565 C C . ALA A 1 199 ? 8.270 12.072 43.350 1.00 26.04 ? 252 ALA A C 1 ATOM 1566 O O . ALA A 1 199 ? 7.095 11.733 43.233 1.00 32.21 ? 252 ALA A O 1 ATOM 1567 C CB . ALA A 1 199 ? 9.846 11.680 41.444 1.00 27.00 ? 252 ALA A CB 1 ATOM 1568 N N . ARG A 1 200 ? 8.953 11.947 44.482 1.00 28.58 ? 253 ARG A N 1 ATOM 1569 C CA . ARG A 1 200 ? 8.371 11.340 45.666 1.00 31.25 ? 253 ARG A CA 1 ATOM 1570 C C . ARG A 1 200 ? 7.264 12.204 46.265 1.00 32.09 ? 253 ARG A C 1 ATOM 1571 O O . ARG A 1 200 ? 6.191 11.694 46.591 1.00 28.42 ? 253 ARG A O 1 ATOM 1572 C CB . ARG A 1 200 ? 9.437 11.052 46.715 1.00 30.22 ? 253 ARG A CB 1 ATOM 1573 C CG . ARG A 1 200 ? 9.061 9.924 47.670 1.00 33.86 ? 253 ARG A CG 1 ATOM 1574 C CD . ARG A 1 200 ? 10.204 9.470 48.557 1.00 37.57 ? 253 ARG A CD 1 ATOM 1575 N NE . ARG A 1 200 ? 11.109 10.577 48.805 1.00 42.26 ? 253 ARG A NE 1 ATOM 1576 C CZ . ARG A 1 200 ? 12.427 10.510 48.724 1.00 41.35 ? 253 ARG A CZ 1 ATOM 1577 N NH1 . ARG A 1 200 ? 13.032 9.370 48.419 1.00 40.74 ? 253 ARG A NH1 1 ATOM 1578 N NH2 . ARG A 1 200 ? 13.142 11.595 48.961 1.00 44.77 ? 253 ARG A NH2 1 ATOM 1579 N N . LEU A 1 201 ? 7.511 13.507 46.391 1.00 28.16 ? 254 LEU A N 1 ATOM 1580 C CA . LEU A 1 201 ? 6.491 14.415 46.901 1.00 27.30 ? 254 LEU A CA 1 ATOM 1581 C C . LEU A 1 201 ? 5.248 14.383 46.017 1.00 25.25 ? 254 LEU A C 1 ATOM 1582 O O . LEU A 1 201 ? 4.114 14.390 46.508 1.00 24.82 ? 254 LEU A O 1 ATOM 1583 C CB . LEU A 1 201 ? 7.029 15.845 46.997 1.00 29.00 ? 254 LEU A CB 1 ATOM 1584 C CG . LEU A 1 201 ? 8.083 16.116 48.077 1.00 30.13 ? 254 LEU A CG 1 ATOM 1585 C CD1 . LEU A 1 201 ? 8.657 17.531 47.910 1.00 29.88 ? 254 LEU A CD1 1 ATOM 1586 C CD2 . LEU A 1 201 ? 7.506 15.934 49.467 1.00 29.95 ? 254 LEU A CD2 1 ATOM 1587 N N . ILE A 1 202 ? 5.462 14.351 44.710 1.00 26.53 ? 255 ILE A N 1 ATOM 1588 C CA . ILE A 1 202 ? 4.357 14.330 43.762 1.00 26.71 ? 255 ILE A CA 1 ATOM 1589 C C . ILE A 1 202 ? 3.536 13.043 43.901 1.00 29.45 ? 255 ILE A C 1 ATOM 1590 O O . ILE A 1 202 ? 2.304 13.091 43.976 1.00 27.22 ? 255 ILE A O 1 ATOM 1591 C CB . ILE A 1 202 ? 4.892 14.482 42.328 1.00 28.23 ? 255 ILE A CB 1 ATOM 1592 C CG1 . ILE A 1 202 ? 5.567 15.853 42.169 1.00 24.74 ? 255 ILE A CG1 1 ATOM 1593 C CG2 . ILE A 1 202 ? 3.750 14.312 41.316 1.00 31.04 ? 255 ILE A CG2 1 ATOM 1594 C CD1 . ILE A 1 202 ? 5.957 16.182 40.755 1.00 27.27 ? 255 ILE A CD1 1 ATOM 1595 N N . ARG A 1 203 ? 4.220 11.902 43.946 1.00 27.66 ? 256 ARG A N 1 ATOM 1596 C CA . ARG A 1 203 ? 3.553 10.612 44.135 1.00 30.63 ? 256 ARG A CA 1 ATOM 1597 C C . ARG A 1 203 ? 2.789 10.580 45.460 1.00 30.67 ? 256 ARG A C 1 ATOM 1598 O O . ARG A 1 203 ? 1.631 10.165 45.503 1.00 35.98 ? 256 ARG A O 1 ATOM 1599 C CB . ARG A 1 203 ? 4.565 9.455 44.084 1.00 30.91 ? 256 ARG A CB 1 ATOM 1600 C CG . ARG A 1 203 ? 5.209 9.245 42.726 1.00 34.74 ? 256 ARG A CG 1 ATOM 1601 C CD . ARG A 1 203 ? 5.439 7.782 42.348 1.00 39.97 ? 256 ARG A CD 1 ATOM 1602 N NE . ARG A 1 203 ? 5.058 7.555 40.959 1.00 44.59 ? 256 ARG A NE 1 ATOM 1603 C CZ . ARG A 1 203 ? 4.522 6.443 40.494 1.00 43.10 ? 256 ARG A CZ 1 ATOM 1604 N NH1 . ARG A 1 203 ? 4.309 5.416 41.300 1.00 44.49 ? 256 ARG A NH1 1 ATOM 1605 N NH2 . ARG A 1 203 ? 4.198 6.358 39.211 1.00 47.86 ? 256 ARG A NH2 1 ATOM 1606 N N . GLN A 1 204 ? 3.428 11.030 46.537 1.00 30.24 ? 257 GLN A N 1 ATOM 1607 C CA . GLN A 1 204 ? 2.757 11.120 47.832 1.00 32.28 ? 257 GLN A CA 1 ATOM 1608 C C . GLN A 1 204 ? 1.502 11.989 47.734 1.00 33.98 ? 257 GLN A C 1 ATOM 1609 O O . GLN A 1 204 ? 0.444 11.628 48.257 1.00 31.61 ? 257 GLN A O 1 ATOM 1610 C CB . GLN A 1 204 ? 3.710 11.649 48.915 1.00 33.11 ? 257 GLN A CB 1 ATOM 1611 C CG . GLN A 1 204 ? 4.790 10.627 49.322 1.00 33.64 ? 257 GLN A CG 1 ATOM 1612 C CD . GLN A 1 204 ? 5.808 11.169 50.315 1.00 33.95 ? 257 GLN A CD 1 ATOM 1613 O OE1 . GLN A 1 204 ? 6.364 10.407 51.111 1.00 35.09 ? 257 GLN A OE1 1 ATOM 1614 N NE2 . GLN A 1 204 ? 6.064 12.476 50.269 1.00 27.65 ? 257 GLN A NE2 1 ATOM 1615 N N . GLU A 1 205 ? 1.614 13.128 47.059 1.00 31.86 ? 258 GLU A N 1 ATOM 1616 C CA . GLU A 1 205 ? 0.495 14.059 46.983 1.00 31.88 ? 258 GLU A CA 1 ATOM 1617 C C . GLU A 1 205 ? -0.603 13.474 46.102 1.00 32.69 ? 258 GLU A C 1 ATOM 1618 O O . GLU A 1 205 ? -1.782 13.735 46.326 1.00 32.38 ? 258 GLU A O 1 ATOM 1619 C CB . GLU A 1 205 ? 0.938 15.429 46.454 1.00 31.98 ? 258 GLU A CB 1 ATOM 1620 C CG . GLU A 1 205 ? -0.029 16.561 46.788 1.00 33.76 ? 258 GLU A CG 1 ATOM 1621 C CD . GLU A 1 205 ? 0.600 17.947 46.687 1.00 32.88 ? 258 GLU A CD 1 ATOM 1622 O OE1 . GLU A 1 205 ? 1.648 18.093 46.023 1.00 29.61 ? 258 GLU A OE1 1 ATOM 1623 O OE2 . GLU A 1 205 ? 0.034 18.902 47.264 1.00 31.26 ? 258 GLU A OE2 1 ATOM 1624 N N . GLU A 1 206 ? -0.216 12.675 45.110 1.00 31.85 ? 259 GLU A N 1 ATOM 1625 C CA . GLU A 1 206 ? -1.183 12.051 44.216 1.00 33.97 ? 259 GLU A CA 1 ATOM 1626 C C . GLU A 1 206 ? -1.750 10.767 44.821 1.00 35.10 ? 259 GLU A C 1 ATOM 1627 O O . GLU A 1 206 ? -2.509 10.052 44.170 1.00 35.31 ? 259 GLU A O 1 ATOM 1628 C CB . GLU A 1 206 ? -0.545 11.735 42.862 1.00 35.84 ? 259 GLU A CB 1 ATOM 1629 C CG . GLU A 1 206 ? -0.350 12.944 41.961 1.00 38.72 ? 259 GLU A CG 1 ATOM 1630 C CD . GLU A 1 206 ? -1.660 13.507 41.448 1.00 41.97 ? 259 GLU A CD 1 ATOM 1631 O OE1 . GLU A 1 206 ? -1.731 13.875 40.256 1.00 44.68 ? 259 GLU A OE1 1 ATOM 1632 O OE2 . GLU A 1 206 ? -2.616 13.593 42.240 1.00 44.44 ? 259 GLU A OE2 1 ATOM 1633 N N . ARG A 1 207 ? -1.375 10.484 46.062 1.00 35.65 ? 260 ARG A N 1 ATOM 1634 C CA . ARG A 1 207 ? -1.585 9.172 46.668 1.00 39.85 ? 260 ARG A CA 1 ATOM 1635 C C . ARG A 1 207 ? -1.294 8.029 45.706 1.00 39.10 ? 260 ARG A C 1 ATOM 1636 O O . ARG A 1 207 ? -2.155 7.178 45.461 1.00 44.00 ? 260 ARG A O 1 ATOM 1637 C CB . ARG A 1 207 ? -3.013 9.051 47.193 1.00 44.53 ? 260 ARG A CB 1 ATOM 1638 C CG . ARG A 1 207 ? -3.134 9.309 48.686 1.00 48.67 ? 260 ARG A CG 1 ATOM 1639 C CD . ARG A 1 207 ? -3.132 10.789 49.055 1.00 53.10 ? 260 ARG A CD 1 ATOM 1640 N NE . ARG A 1 207 ? -4.382 11.203 49.695 1.00 56.27 ? 260 ARG A NE 1 ATOM 1641 C CZ . ARG A 1 207 ? -5.496 11.494 49.036 1.00 57.95 ? 260 ARG A CZ 1 ATOM 1642 N NH1 . ARG A 1 207 ? -5.525 11.418 47.713 1.00 57.59 ? 260 ARG A NH1 1 ATOM 1643 N NH2 . ARG A 1 207 ? -6.583 11.865 49.698 1.00 58.42 ? 260 ARG A NH2 1 ATOM 1644 N N . LEU A 1 208 ? -0.076 7.997 45.180 1.00 33.45 ? 261 LEU A N 1 ATOM 1645 C CA . LEU A 1 208 ? 0.390 6.854 44.410 1.00 36.20 ? 261 LEU A CA 1 ATOM 1646 C C . LEU A 1 208 ? 1.367 6.009 45.213 1.00 34.83 ? 261 LEU A C 1 ATOM 1647 O O . LEU A 1 208 ? 1.943 6.458 46.201 1.00 35.55 ? 261 LEU A O 1 ATOM 1648 C CB . LEU A 1 208 ? 1.057 7.308 43.111 1.00 34.69 ? 261 LEU A CB 1 ATOM 1649 C CG . LEU A 1 208 ? 0.209 8.201 42.216 1.00 35.96 ? 261 LEU A CG 1 ATOM 1650 C CD1 . LEU A 1 208 ? 1.013 8.700 41.026 1.00 36.74 ? 261 LEU A CD1 1 ATOM 1651 C CD2 . LEU A 1 208 ? -1.028 7.457 41.751 1.00 37.56 ? 261 LEU A CD2 1 ATOM 1652 N N . PRO A 1 209 ? 1.547 4.770 44.780 1.00 38.21 ? 262 PRO A N 1 ATOM 1653 C CA . PRO A 1 209 ? 2.551 3.893 45.384 1.00 38.37 ? 262 PRO A CA 1 ATOM 1654 C C . PRO A 1 209 ? 3.954 4.410 45.096 1.00 36.72 ? 262 PRO A C 1 ATOM 1655 O O . PRO A 1 209 ? 4.208 4.969 44.023 1.00 34.32 ? 262 PRO A O 1 ATOM 1656 C CB . PRO A 1 209 ? 2.308 2.539 44.705 1.00 38.92 ? 262 PRO A CB 1 ATOM 1657 C CG . PRO A 1 209 ? 1.549 2.838 43.458 1.00 40.33 ? 262 PRO A CG 1 ATOM 1658 C CD . PRO A 1 209 ? 0.819 4.129 43.674 1.00 38.28 ? 262 PRO A CD 1 ATOM 1659 N N . ILE A 1 210 ? 4.846 4.244 46.059 1.00 37.93 ? 263 ILE A N 1 ATOM 1660 C CA . ILE A 1 210 ? 6.212 4.717 45.913 1.00 41.03 ? 263 ILE A CA 1 ATOM 1661 C C . ILE A 1 210 ? 7.185 3.558 46.073 1.00 40.47 ? 263 ILE A C 1 ATOM 1662 O O . ILE A 1 210 ? 7.224 2.892 47.106 1.00 37.64 ? 263 ILE A O 1 ATOM 1663 C CB . ILE A 1 210 ? 6.518 5.828 46.936 1.00 41.27 ? 263 ILE A CB 1 ATOM 1664 C CG1 . ILE A 1 210 ? 5.841 7.134 46.516 1.00 40.27 ? 263 ILE A CG1 1 ATOM 1665 C CG2 . ILE A 1 210 ? 8.011 6.048 47.050 1.00 40.10 ? 263 ILE A CG2 1 ATOM 1666 C CD1 . ILE A 1 210 ? 5.475 8.024 47.674 1.00 41.91 ? 263 ILE A CD1 1 ATOM 1667 N N . ASP A 1 211 ? 7.962 3.323 45.025 1.00 41.95 ? 264 ASP A N 1 ATOM 1668 C CA . ASP A 1 211 ? 8.945 2.254 45.020 1.00 40.38 ? 264 ASP A CA 1 ATOM 1669 C C . ASP A 1 211 ? 10.327 2.860 44.831 1.00 36.96 ? 264 ASP A C 1 ATOM 1670 O O . ASP A 1 211 ? 10.718 3.188 43.719 1.00 36.24 ? 264 ASP A O 1 ATOM 1671 C CB . ASP A 1 211 ? 8.627 1.278 43.893 1.00 41.85 ? 264 ASP A CB 1 ATOM 1672 C CG . ASP A 1 211 ? 9.733 0.273 43.654 1.00 43.06 ? 264 ASP A CG 1 ATOM 1673 O OD1 . ASP A 1 211 ? 10.763 0.314 44.364 1.00 41.31 ? 264 ASP A OD1 1 ATOM 1674 O OD2 . ASP A 1 211 ? 9.649 -0.594 42.763 1.00 44.39 ? 264 ASP A OD2 1 ATOM 1675 N N . GLU A 1 212 ? 11.049 3.027 45.932 1.00 40.25 ? 265 GLU A N 1 ATOM 1676 C CA . GLU A 1 212 ? 12.262 3.837 45.944 1.00 39.97 ? 265 GLU A CA 1 ATOM 1677 C C . GLU A 1 212 ? 13.210 3.357 44.861 1.00 39.82 ? 265 GLU A C 1 ATOM 1678 O O . GLU A 1 212 ? 13.828 4.156 44.156 1.00 38.08 ? 265 GLU A O 1 ATOM 1679 C CB . GLU A 1 212 ? 12.947 3.749 47.310 1.00 41.82 ? 265 GLU A CB 1 ATOM 1680 C CG . GLU A 1 212 ? 12.180 4.433 48.430 1.00 41.66 ? 265 GLU A CG 1 ATOM 1681 C CD . GLU A 1 212 ? 12.059 5.934 48.218 1.00 43.00 ? 265 GLU A CD 1 ATOM 1682 O OE1 . GLU A 1 212 ? 11.056 6.524 48.666 1.00 41.62 ? 265 GLU A OE1 1 ATOM 1683 O OE2 . GLU A 1 212 ? 12.969 6.525 47.602 1.00 41.27 ? 265 GLU A OE2 1 ATOM 1684 N N . ASN A 1 213 ? 13.314 2.039 44.724 1.00 40.53 ? 266 ASN A N 1 ATOM 1685 C CA . ASN A 1 213 ? 14.254 1.449 43.791 1.00 39.65 ? 266 ASN A CA 1 ATOM 1686 C C . ASN A 1 213 ? 13.940 1.860 42.369 1.00 38.80 ? 266 ASN A C 1 ATOM 1687 O O . ASN A 1 213 ? 14.843 2.107 41.565 1.00 31.74 ? 266 ASN A O 1 ATOM 1688 C CB . ASN A 1 213 ? 14.226 -0.072 43.906 1.00 45.22 ? 266 ASN A CB 1 ATOM 1689 C CG . ASN A 1 213 ? 15.559 -0.641 44.323 1.00 47.25 ? 266 ASN A CG 1 ATOM 1690 O OD1 . ASN A 1 213 ? 16.183 -1.400 43.579 1.00 51.44 ? 266 ASN A OD1 1 ATOM 1691 N ND2 . ASN A 1 213 ? 16.017 -0.265 45.514 1.00 50.05 ? 266 ASN A ND2 1 ATOM 1692 N N . GLN A 1 214 ? 12.650 1.928 42.060 1.00 36.50 ? 267 GLN A N 1 ATOM 1693 C CA . GLN A 1 214 ? 12.211 2.306 40.726 1.00 35.36 ? 267 GLN A CA 1 ATOM 1694 C C . GLN A 1 214 ? 12.342 3.816 40.529 1.00 31.47 ? 267 GLN A C 1 ATOM 1695 O O . GLN A 1 214 ? 12.637 4.276 39.427 1.00 31.22 ? 267 GLN A O 1 ATOM 1696 C CB . GLN A 1 214 ? 10.767 1.859 40.494 1.00 36.00 ? 267 GLN A CB 1 ATOM 1697 C CG . GLN A 1 214 ? 10.107 2.477 39.278 1.00 38.05 ? 267 GLN A CG 1 ATOM 1698 C CD . GLN A 1 214 ? 10.502 1.811 37.974 1.00 41.13 ? 267 GLN A CD 1 ATOM 1699 O OE1 . GLN A 1 214 ? 10.178 2.315 36.898 1.00 43.75 ? 267 GLN A OE1 1 ATOM 1700 N NE2 . GLN A 1 214 ? 11.196 0.680 38.062 1.00 44.54 ? 267 GLN A NE2 1 ATOM 1701 N N . LEU A 1 215 ? 12.138 4.576 41.603 1.00 31.52 ? 268 LEU A N 1 ATOM 1702 C CA . LEU A 1 215 ? 12.448 6.008 41.596 1.00 32.62 ? 268 LEU A CA 1 ATOM 1703 C C . LEU A 1 215 ? 13.894 6.206 41.193 1.00 29.04 ? 268 LEU A C 1 ATOM 1704 O O . LEU A 1 215 ? 14.191 6.904 40.227 1.00 27.05 ? 268 LEU A O 1 ATOM 1705 C CB . LEU A 1 215 ? 12.225 6.621 42.979 1.00 35.69 ? 268 LEU A CB 1 ATOM 1706 C CG . LEU A 1 215 ? 10.775 6.913 43.373 1.00 36.37 ? 268 LEU A CG 1 ATOM 1707 C CD1 . LEU A 1 215 ? 10.728 8.077 44.343 1.00 36.62 ? 268 LEU A CD1 1 ATOM 1708 C CD2 . LEU A 1 215 ? 9.943 7.196 42.146 1.00 36.78 ? 268 LEU A CD2 1 ATOM 1709 N N . ALA A 1 216 ? 14.788 5.576 41.948 1.00 27.38 ? 269 ALA A N 1 ATOM 1710 C CA . ALA A 1 216 ? 16.218 5.720 41.731 1.00 26.93 ? 269 ALA A CA 1 ATOM 1711 C C . ALA A 1 216 ? 16.580 5.286 40.321 1.00 29.27 ? 269 ALA A C 1 ATOM 1712 O O . ALA A 1 216 ? 17.433 5.892 39.673 1.00 32.95 ? 269 ALA A O 1 ATOM 1713 C CB . ALA A 1 216 ? 16.987 4.907 42.755 1.00 28.73 ? 269 ALA A CB 1 ATOM 1714 N N . LEU A 1 217 ? 15.907 4.247 39.838 1.00 33.50 ? 270 LEU A N 1 ATOM 1715 C CA . LEU A 1 217 ? 16.233 3.658 38.545 1.00 37.63 ? 270 LEU A CA 1 ATOM 1716 C C . LEU A 1 217 ? 15.843 4.592 37.405 1.00 31.62 ? 270 LEU A C 1 ATOM 1717 O O . LEU A 1 217 ? 16.591 4.764 36.451 1.00 31.31 ? 270 LEU A O 1 ATOM 1718 C CB . LEU A 1 217 ? 15.543 2.296 38.386 1.00 41.59 ? 270 LEU A CB 1 ATOM 1719 C CG . LEU A 1 217 ? 16.338 1.172 37.699 1.00 45.81 ? 270 LEU A CG 1 ATOM 1720 C CD1 . LEU A 1 217 ? 17.362 0.503 38.631 1.00 46.89 ? 270 LEU A CD1 1 ATOM 1721 C CD2 . LEU A 1 217 ? 15.388 0.117 37.129 1.00 46.34 ? 270 LEU A CD2 1 ATOM 1722 N N . GLU A 1 218 ? 14.674 5.211 37.511 1.00 30.18 ? 271 GLU A N 1 ATOM 1723 C CA . GLU A 1 218 ? 14.202 6.106 36.460 1.00 26.98 ? 271 GLU A CA 1 ATOM 1724 C C . GLU A 1 218 ? 14.997 7.416 36.442 1.00 24.55 ? 271 GLU A C 1 ATOM 1725 O O . GLU A 1 218 ? 15.334 7.940 35.384 1.00 23.02 ? 271 GLU A O 1 ATOM 1726 C CB . GLU A 1 218 ? 12.698 6.364 36.618 1.00 30.36 ? 271 GLU A CB 1 ATOM 1727 C CG . GLU A 1 218 ? 11.852 5.492 35.701 1.00 33.78 ? 271 GLU A CG 1 ATOM 1728 C CD . GLU A 1 218 ? 10.365 5.710 35.873 1.00 35.38 ? 271 GLU A CD 1 ATOM 1729 O OE1 . GLU A 1 218 ? 9.790 6.510 35.112 1.00 32.40 ? 271 GLU A OE1 1 ATOM 1730 O OE2 . GLU A 1 218 ? 9.767 5.070 36.768 1.00 42.26 ? 271 GLU A OE2 1 ATOM 1731 N N . MET A 1 219 ? 15.339 7.928 37.614 1.00 24.12 ? 272 MET A N 1 ATOM 1732 C CA . MET A 1 219 ? 16.024 9.214 37.683 1.00 23.44 ? 272 MET A CA 1 ATOM 1733 C C . MET A 1 219 ? 17.494 9.053 37.301 1.00 23.61 ? 272 MET A C 1 ATOM 1734 O O . MET A 1 219 ? 18.143 9.989 36.851 1.00 22.13 ? 272 MET A O 1 ATOM 1735 C CB . MET A 1 219 ? 15.896 9.805 39.085 1.00 25.38 ? 272 MET A CB 1 ATOM 1736 C CG . MET A 1 219 ? 14.540 10.439 39.347 1.00 29.70 ? 272 MET A CG 1 ATOM 1737 S SD . MET A 1 219 ? 14.026 11.539 38.009 1.00 31.04 ? 272 MET A SD 1 ATOM 1738 C CE . MET A 1 219 ? 12.799 10.529 37.154 1.00 32.43 ? 272 MET A CE 1 ATOM 1739 N N . ASN A 1 220 ? 18.036 7.859 37.461 1.00 25.58 ? 273 ASN A N 1 ATOM 1740 C CA . ASN A 1 220 ? 19.410 7.660 37.043 1.00 26.31 ? 273 ASN A CA 1 ATOM 1741 C C . ASN A 1 220 ? 19.514 7.616 35.526 1.00 26.88 ? 273 ASN A C 1 ATOM 1742 O O . ASN A 1 220 ? 20.472 8.129 34.958 1.00 25.30 ? 273 ASN A O 1 ATOM 1743 C CB . ASN A 1 220 ? 20.015 6.412 37.693 1.00 29.62 ? 273 ASN A CB 1 ATOM 1744 C CG . ASN A 1 220 ? 20.695 6.729 39.011 1.00 29.72 ? 273 ASN A CG 1 ATOM 1745 O OD1 . ASN A 1 220 ? 21.663 7.488 39.054 1.00 32.98 ? 273 ASN A OD1 1 ATOM 1746 N ND2 . ASN A 1 220 ? 20.192 6.148 40.093 1.00 31.60 ? 273 ASN A ND2 1 ATOM 1747 N N . LYS A 1 221 ? 18.513 7.038 34.869 1.00 25.77 ? 274 LYS A N 1 ATOM 1748 C CA . LYS A 1 221 ? 18.430 7.096 33.411 1.00 28.55 ? 274 LYS A CA 1 ATOM 1749 C C . LYS A 1 221 ? 18.240 8.519 32.886 1.00 24.90 ? 274 LYS A C 1 ATOM 1750 O O . LYS A 1 221 ? 18.733 8.851 31.810 1.00 27.88 ? 274 LYS A O 1 ATOM 1751 C CB . LYS A 1 221 ? 17.297 6.200 32.894 1.00 33.25 ? 274 LYS A CB 1 ATOM 1752 C CG . LYS A 1 221 ? 17.731 4.758 32.618 1.00 39.03 ? 274 LYS A CG 1 ATOM 1753 C CD . LYS A 1 221 ? 18.130 4.557 31.158 1.00 40.32 ? 274 LYS A CD 1 ATOM 1754 C CE . LYS A 1 221 ? 18.888 3.253 30.957 1.00 41.19 ? 274 LYS A CE 1 ATOM 1755 N NZ . LYS A 1 221 ? 19.177 2.992 29.510 1.00 41.33 ? 274 LYS A NZ 1 ATOM 1756 N N . VAL A 1 222 ? 17.527 9.365 33.632 1.00 25.28 ? 275 VAL A N 1 ATOM 1757 C CA . VAL A 1 222 ? 17.517 10.795 33.315 1.00 22.57 ? 275 VAL A CA 1 ATOM 1758 C C . VAL A 1 222 ? 18.925 11.378 33.337 1.00 18.57 ? 275 VAL A C 1 ATOM 1759 O O . VAL A 1 222 ? 19.322 12.070 32.398 1.00 20.49 ? 275 VAL A O 1 ATOM 1760 C CB . VAL A 1 222 ? 16.613 11.605 34.258 1.00 24.38 ? 275 VAL A CB 1 ATOM 1761 C CG1 . VAL A 1 222 ? 16.905 13.095 34.100 1.00 25.35 ? 275 VAL A CG1 1 ATOM 1762 C CG2 . VAL A 1 222 ? 15.147 11.302 33.957 1.00 24.79 ? 275 VAL A CG2 1 ATOM 1763 N N . MET A 1 223 ? 19.691 11.075 34.383 1.00 22.66 ? 276 MET A N 1 ATOM 1764 C CA . MET A 1 223 ? 21.076 11.541 34.456 1.00 20.75 ? 276 MET A CA 1 ATOM 1765 C C . MET A 1 223 ? 21.912 10.962 33.318 1.00 25.11 ? 276 MET A C 1 ATOM 1766 O O . MET A 1 223 ? 22.760 11.646 32.751 1.00 23.67 ? 276 MET A O 1 ATOM 1767 C CB . MET A 1 223 ? 21.715 11.181 35.794 1.00 22.90 ? 276 MET A CB 1 ATOM 1768 C CG . MET A 1 223 ? 23.112 11.773 35.967 1.00 22.51 ? 276 MET A CG 1 ATOM 1769 S SD . MET A 1 223 ? 23.130 13.596 35.668 1.00 27.64 ? 276 MET A SD 1 ATOM 1770 C CE . MET A 1 223 ? 24.189 14.173 36.992 1.00 27.34 ? 276 MET A CE 1 ATOM 1771 N N . GLU A 1 224 ? 21.700 9.693 32.983 1.00 25.41 ? 277 GLU A N 1 ATOM 1772 C CA . GLU A 1 224 ? 22.543 9.085 31.966 1.00 26.10 ? 277 GLU A CA 1 ATOM 1773 C C . GLU A 1 224 ? 22.240 9.757 30.646 1.00 21.87 ? 277 GLU A C 1 ATOM 1774 O O . GLU A 1 224 ? 23.149 10.110 29.896 1.00 24.17 ? 277 GLU A O 1 ATOM 1775 C CB . GLU A 1 224 ? 22.346 7.569 31.877 1.00 31.76 ? 277 GLU A CB 1 ATOM 1776 C CG . GLU A 1 224 ? 23.382 6.906 30.983 1.00 37.43 ? 277 GLU A CG 1 ATOM 1777 C CD . GLU A 1 224 ? 24.780 7.499 31.156 1.00 41.64 ? 277 GLU A CD 1 ATOM 1778 O OE1 . GLU A 1 224 ? 25.251 8.229 30.245 1.00 37.94 ? 277 GLU A OE1 1 ATOM 1779 O OE2 . GLU A 1 224 ? 25.413 7.234 32.208 1.00 44.66 ? 277 GLU A OE2 1 ATOM 1780 N N . LEU A 1 225 ? 20.954 9.975 30.384 1.00 22.41 ? 278 LEU A N 1 ATOM 1781 C CA . LEU A 1 225 ? 20.525 10.775 29.242 1.00 25.15 ? 278 LEU A CA 1 ATOM 1782 C C . LEU A 1 225 ? 21.203 12.132 29.175 1.00 22.88 ? 278 LEU A C 1 ATOM 1783 O O . LEU A 1 225 ? 21.732 12.535 28.126 1.00 18.65 ? 278 LEU A O 1 ATOM 1784 C CB . LEU A 1 225 ? 19.011 10.999 29.295 1.00 27.12 ? 278 LEU A CB 1 ATOM 1785 C CG . LEU A 1 225 ? 18.253 11.040 27.965 1.00 31.51 ? 278 LEU A CG 1 ATOM 1786 C CD1 . LEU A 1 225 ? 17.023 11.929 28.072 1.00 32.23 ? 278 LEU A CD1 1 ATOM 1787 C CD2 . LEU A 1 225 ? 19.127 11.460 26.809 1.00 30.51 ? 278 LEU A CD2 1 ATOM 1788 N N . GLU A 1 226 ? 21.151 12.881 30.269 1.00 23.33 ? 279 GLU A N 1 ATOM 1789 C CA . GLU A 1 226 ? 21.605 14.259 30.192 1.00 19.98 ? 279 GLU A CA 1 ATOM 1790 C C . GLU A 1 226 ? 23.125 14.318 30.157 1.00 17.81 ? 279 GLU A C 1 ATOM 1791 O O . GLU A 1 226 ? 23.690 15.260 29.640 1.00 23.49 ? 279 GLU A O 1 ATOM 1792 C CB . GLU A 1 226 ? 21.068 15.110 31.336 1.00 21.34 ? 279 GLU A CB 1 ATOM 1793 C CG . GLU A 1 226 ? 21.081 16.594 30.978 1.00 18.09 ? 279 GLU A CG 1 ATOM 1794 C CD . GLU A 1 226 ? 20.595 17.487 32.099 1.00 19.86 ? 279 GLU A CD 1 ATOM 1795 O OE1 . GLU A 1 226 ? 20.785 17.116 33.276 1.00 19.40 ? 279 GLU A OE1 1 ATOM 1796 O OE2 . GLU A 1 226 ? 20.030 18.568 31.791 1.00 23.80 ? 279 GLU A OE2 1 ATOM 1797 N N . LYS A 1 227 ? 23.780 13.287 30.674 1.00 25.10 ? 280 LYS A N 1 ATOM 1798 C CA . LYS A 1 227 ? 25.215 13.126 30.467 1.00 20.09 ? 280 LYS A CA 1 ATOM 1799 C C . LYS A 1 227 ? 25.561 13.099 28.986 1.00 22.03 ? 280 LYS A C 1 ATOM 1800 O O . LYS A 1 227 ? 26.434 13.839 28.536 1.00 23.09 ? 280 LYS A O 1 ATOM 1801 C CB . LYS A 1 227 ? 25.719 11.851 31.143 1.00 23.18 ? 280 LYS A CB 1 ATOM 1802 C CG . LYS A 1 227 ? 25.994 11.996 32.639 1.00 25.17 ? 280 LYS A CG 1 ATOM 1803 C CD . LYS A 1 227 ? 26.539 10.706 33.218 1.00 27.88 ? 280 LYS A CD 1 ATOM 1804 C CE . LYS A 1 227 ? 26.815 10.815 34.711 1.00 29.72 ? 280 LYS A CE 1 ATOM 1805 N NZ . LYS A 1 227 ? 27.146 9.494 35.353 1.00 28.08 ? 280 LYS A NZ 1 ATOM 1806 N N . GLU A 1 228 ? 24.878 12.245 28.224 1.00 22.60 ? 281 GLU A N 1 ATOM 1807 C CA . GLU A 1 228 ? 25.105 12.157 26.785 1.00 21.83 ? 281 GLU A CA 1 ATOM 1808 C C . GLU A 1 228 ? 24.871 13.487 26.059 1.00 22.67 ? 281 GLU A C 1 ATOM 1809 O O . GLU A 1 228 ? 25.663 13.895 25.202 1.00 26.01 ? 281 GLU A O 1 ATOM 1810 C CB . GLU A 1 228 ? 24.229 11.045 26.192 1.00 21.83 ? 281 GLU A CB 1 ATOM 1811 C CG . GLU A 1 228 ? 24.608 9.667 26.694 1.00 22.49 ? 281 GLU A CG 1 ATOM 1812 C CD . GLU A 1 228 ? 24.322 8.583 25.681 1.00 24.51 ? 281 GLU A CD 1 ATOM 1813 O OE1 . GLU A 1 228 ? 23.374 7.806 25.908 1.00 26.22 ? 281 GLU A OE1 1 ATOM 1814 O OE2 . GLU A 1 228 ? 25.038 8.534 24.651 1.00 30.07 ? 281 GLU A OE2 1 ATOM 1815 N N . ILE A 1 229 ? 23.786 14.170 26.404 1.00 20.45 ? 282 ILE A N 1 ATOM 1816 C CA . ILE A 1 229 ? 23.509 15.492 25.871 1.00 21.68 ? 282 ILE A CA 1 ATOM 1817 C C . ILE A 1 229 ? 24.635 16.463 26.194 1.00 18.77 ? 282 ILE A C 1 ATOM 1818 O O . ILE A 1 229 ? 25.106 17.220 25.334 1.00 19.04 ? 282 ILE A O 1 ATOM 1819 C CB . ILE A 1 229 ? 22.175 16.004 26.455 1.00 26.13 ? 282 ILE A CB 1 ATOM 1820 C CG1 . ILE A 1 229 ? 21.043 15.046 26.096 1.00 30.44 ? 282 ILE A CG1 1 ATOM 1821 C CG2 . ILE A 1 229 ? 21.854 17.394 25.940 1.00 24.18 ? 282 ILE A CG2 1 ATOM 1822 C CD1 . ILE A 1 229 ? 19.675 15.694 26.150 1.00 33.26 ? 282 ILE A CD1 1 ATOM 1823 N N . ALA A 1 230 ? 25.064 16.445 27.447 1.00 21.55 ? 283 ALA A N 1 ATOM 1824 C CA . ALA A 1 230 ? 26.087 17.364 27.899 1.00 20.42 ? 283 ALA A CA 1 ATOM 1825 C C . ALA A 1 230 ? 27.325 17.129 27.046 1.00 21.53 ? 283 ALA A C 1 ATOM 1826 O O . ALA A 1 230 ? 27.902 18.050 26.478 1.00 24.78 ? 283 ALA A O 1 ATOM 1827 C CB . ALA A 1 230 ? 26.386 17.116 29.350 1.00 22.87 ? 283 ALA A CB 1 ATOM 1828 N N . ASN A 1 231 ? 27.696 15.865 26.932 1.00 21.57 ? 284 ASN A N 1 ATOM 1829 C CA . ASN A 1 231 ? 28.904 15.494 26.219 1.00 23.03 ? 284 ASN A CA 1 ATOM 1830 C C . ASN A 1 231 ? 28.765 15.830 24.737 1.00 17.74 ? 284 ASN A C 1 ATOM 1831 O O . ASN A 1 231 ? 29.747 16.112 24.051 1.00 20.94 ? 284 ASN A O 1 ATOM 1832 C CB . ASN A 1 231 ? 29.184 14.003 26.422 1.00 24.61 ? 284 ASN A CB 1 ATOM 1833 C CG . ASN A 1 231 ? 30.346 13.513 25.587 1.00 26.42 ? 284 ASN A CG 1 ATOM 1834 O OD1 . ASN A 1 231 ? 30.193 12.614 24.747 1.00 32.46 ? 284 ASN A OD1 1 ATOM 1835 N ND2 . ASN A 1 231 ? 31.510 14.100 25.804 1.00 19.89 ? 284 ASN A ND2 1 ATOM 1836 N N . ALA A 1 232 ? 27.537 15.840 24.247 1.00 20.85 ? 285 ALA A N 1 ATOM 1837 C CA . ALA A 1 232 ? 27.303 16.190 22.855 1.00 21.96 ? 285 ALA A CA 1 ATOM 1838 C C . ALA A 1 232 ? 27.352 17.696 22.590 1.00 24.62 ? 285 ALA A C 1 ATOM 1839 O O . ALA A 1 232 ? 27.599 18.113 21.453 1.00 26.44 ? 285 ALA A O 1 ATOM 1840 C CB . ALA A 1 232 ? 25.984 15.614 22.381 1.00 22.10 ? 285 ALA A CB 1 ATOM 1841 N N . THR A 1 233 ? 27.121 18.519 23.613 1.00 22.23 ? 286 THR A N 1 ATOM 1842 C CA . THR A 1 233 ? 27.201 19.958 23.418 1.00 18.08 ? 286 THR A CA 1 ATOM 1843 C C . THR A 1 233 ? 28.612 20.405 23.114 1.00 21.62 ? 286 THR A C 1 ATOM 1844 O O . THR A 1 233 ? 29.604 19.799 23.558 1.00 21.03 ? 286 THR A O 1 ATOM 1845 C CB . THR A 1 233 ? 26.664 20.749 24.628 1.00 19.42 ? 286 THR A CB 1 ATOM 1846 O OG1 . THR A 1 233 ? 27.503 20.559 25.782 1.00 16.35 ? 286 THR A OG1 1 ATOM 1847 C CG2 . THR A 1 233 ? 25.293 20.257 25.028 1.00 18.22 ? 286 THR A CG2 1 ATOM 1848 N N . ALA A 1 234 ? 28.692 21.489 22.363 1.00 20.99 ? 287 ALA A N 1 ATOM 1849 C CA . ALA A 1 234 ? 29.959 22.136 22.082 1.00 23.21 ? 287 ALA A CA 1 ATOM 1850 C C . ALA A 1 234 ? 30.390 23.000 23.250 1.00 24.08 ? 287 ALA A C 1 ATOM 1851 O O . ALA A 1 234 ? 29.560 23.620 23.914 1.00 25.94 ? 287 ALA A O 1 ATOM 1852 C CB . ALA A 1 234 ? 29.847 22.966 20.829 1.00 24.57 ? 287 ALA A CB 1 ATOM 1853 N N . LYS A 1 235 ? 31.695 23.020 23.491 1.00 25.21 ? 288 LYS A N 1 ATOM 1854 C CA . LYS A 1 235 ? 32.311 23.871 24.502 1.00 26.16 ? 288 LYS A CA 1 ATOM 1855 C C . LYS A 1 235 ? 32.183 25.333 24.121 1.00 23.55 ? 288 LYS A C 1 ATOM 1856 O O . LYS A 1 235 ? 32.129 25.664 22.935 1.00 20.93 ? 288 LYS A O 1 ATOM 1857 C CB . LYS A 1 235 ? 33.798 23.540 24.618 1.00 27.35 ? 288 LYS A CB 1 ATOM 1858 C CG . LYS A 1 235 ? 34.109 22.214 25.268 1.00 31.94 ? 288 LYS A CG 1 ATOM 1859 C CD . LYS A 1 235 ? 35.582 21.840 25.090 1.00 34.72 ? 288 LYS A CD 1 ATOM 1860 C CE . LYS A 1 235 ? 35.788 20.325 25.174 1.00 38.14 ? 288 LYS A CE 1 ATOM 1861 N NZ . LYS A 1 235 ? 37.161 19.938 25.625 1.00 38.41 ? 288 LYS A NZ 1 ATOM 1862 N N . PRO A 1 236 ? 32.175 26.204 25.125 1.00 24.30 ? 289 PRO A N 1 ATOM 1863 C CA . PRO A 1 236 ? 32.148 27.653 24.898 1.00 27.28 ? 289 PRO A CA 1 ATOM 1864 C C . PRO A 1 236 ? 33.327 28.096 24.035 1.00 26.48 ? 289 PRO A C 1 ATOM 1865 O O . PRO A 1 236 ? 33.203 29.011 23.221 1.00 27.10 ? 289 PRO A O 1 ATOM 1866 C CB . PRO A 1 236 ? 32.254 28.244 26.309 1.00 26.75 ? 289 PRO A CB 1 ATOM 1867 C CG . PRO A 1 236 ? 31.843 27.140 27.237 1.00 29.03 ? 289 PRO A CG 1 ATOM 1868 C CD . PRO A 1 236 ? 32.204 25.858 26.556 1.00 27.79 ? 289 PRO A CD 1 ATOM 1869 N N . GLU A 1 237 ? 34.463 27.433 24.206 1.00 25.78 ? 290 GLU A N 1 ATOM 1870 C CA . GLU A 1 237 ? 35.669 27.794 23.466 1.00 27.45 ? 290 GLU A CA 1 ATOM 1871 C C . GLU A 1 237 ? 35.509 27.523 21.974 1.00 27.01 ? 290 GLU A C 1 ATOM 1872 O O . GLU A 1 237 ? 36.216 28.102 21.151 1.00 27.35 ? 290 GLU A O 1 ATOM 1873 C CB . GLU A 1 237 ? 36.864 27.006 23.990 1.00 27.24 ? 290 GLU A CB 1 ATOM 1874 C CG . GLU A 1 237 ? 37.240 27.360 25.407 1.00 28.39 ? 290 GLU A CG 1 ATOM 1875 C CD . GLU A 1 237 ? 36.837 26.287 26.391 1.00 29.30 ? 290 GLU A CD 1 ATOM 1876 O OE1 . GLU A 1 237 ? 37.731 25.782 27.096 1.00 29.34 ? 290 GLU A OE1 1 ATOM 1877 O OE2 . GLU A 1 237 ? 35.636 25.943 26.445 1.00 26.49 ? 290 GLU A OE2 1 ATOM 1878 N N . ASP A 1 238 ? 34.583 26.640 21.621 1.00 25.49 ? 291 ASP A N 1 ATOM 1879 C CA . ASP A 1 238 ? 34.332 26.349 20.215 1.00 26.82 ? 291 ASP A CA 1 ATOM 1880 C C . ASP A 1 238 ? 33.092 27.097 19.697 1.00 28.95 ? 291 ASP A C 1 ATOM 1881 O O . ASP A 1 238 ? 32.594 26.804 18.610 1.00 27.02 ? 291 ASP A O 1 ATOM 1882 C CB . ASP A 1 238 ? 34.150 24.842 20.017 1.00 28.84 ? 291 ASP A CB 1 ATOM 1883 C CG . ASP A 1 238 ? 35.403 24.046 20.363 1.00 31.24 ? 291 ASP A CG 1 ATOM 1884 O OD1 . ASP A 1 238 ? 36.528 24.548 20.155 1.00 34.82 ? 291 ASP A OD1 1 ATOM 1885 O OD2 . ASP A 1 238 ? 35.356 22.897 20.836 1.00 27.18 ? 291 ASP A OD2 1 ATOM 1886 N N . ARG A 1 239 ? 32.604 28.057 20.482 1.00 27.08 ? 292 ARG A N 1 ATOM 1887 C CA . ARG A 1 239 ? 31.379 28.791 20.159 1.00 24.48 ? 292 ARG A CA 1 ATOM 1888 C C . ARG A 1 239 ? 31.662 30.291 20.172 1.00 27.60 ? 292 ARG A C 1 ATOM 1889 O O . ARG A 1 239 ? 30.745 31.120 20.119 1.00 27.11 ? 292 ARG A O 1 ATOM 1890 C CB . ARG A 1 239 ? 30.273 28.465 21.168 1.00 25.21 ? 292 ARG A CB 1 ATOM 1891 C CG . ARG A 1 239 ? 29.626 27.103 20.993 1.00 25.93 ? 292 ARG A CG 1 ATOM 1892 C CD . ARG A 1 239 ? 28.708 26.674 22.152 1.00 26.13 ? 292 ARG A CD 1 ATOM 1893 N NE . ARG A 1 239 ? 27.646 27.641 22.419 1.00 27.03 ? 292 ARG A NE 1 ATOM 1894 C CZ . ARG A 1 239 ? 26.444 27.619 21.847 1.00 29.32 ? 292 ARG A CZ 1 ATOM 1895 N NH1 . ARG A 1 239 ? 26.138 26.667 20.966 1.00 28.84 ? 292 ARG A NH1 1 ATOM 1896 N NH2 . ARG A 1 239 ? 25.548 28.552 22.151 1.00 25.20 ? 292 ARG A NH2 1 ATOM 1897 N N . ASN A 1 240 ? 32.944 30.630 20.257 1.00 26.74 ? 293 ASN A N 1 ATOM 1898 C CA . ASN A 1 240 ? 33.363 31.999 20.509 1.00 27.64 ? 293 ASN A CA 1 ATOM 1899 C C . ASN A 1 240 ? 33.591 32.792 19.216 1.00 26.62 ? 293 ASN A C 1 ATOM 1900 O O . ASN A 1 240 ? 33.954 33.966 19.256 1.00 28.20 ? 293 ASN A O 1 ATOM 1901 C CB . ASN A 1 240 ? 34.622 32.021 21.381 1.00 27.94 ? 293 ASN A CB 1 ATOM 1902 C CG . ASN A 1 240 ? 35.820 31.355 20.714 1.00 31.69 ? 293 ASN A CG 1 ATOM 1903 O OD1 . ASN A 1 240 ? 35.676 30.556 19.787 1.00 33.12 ? 293 ASN A OD1 1 ATOM 1904 N ND2 . ASN A 1 240 ? 37.014 31.687 21.189 1.00 32.10 ? 293 ASN A ND2 1 ATOM 1905 N N . ASP A 1 241 ? 33.351 32.159 18.071 1.00 28.42 ? 294 ASP A N 1 ATOM 1906 C CA . ASP A 1 241 ? 33.549 32.828 16.787 1.00 30.14 ? 294 ASP A CA 1 ATOM 1907 C C . ASP A 1 241 ? 32.230 32.981 16.051 1.00 28.10 ? 294 ASP A C 1 ATOM 1908 O O . ASP A 1 241 ? 31.724 32.042 15.443 1.00 26.64 ? 294 ASP A O 1 ATOM 1909 C CB . ASP A 1 241 ? 34.555 32.066 15.920 1.00 30.81 ? 294 ASP A CB 1 ATOM 1910 C CG . ASP A 1 241 ? 34.910 32.812 14.644 1.00 32.56 ? 294 ASP A CG 1 ATOM 1911 O OD1 . ASP A 1 241 ? 34.060 33.575 14.146 1.00 33.20 ? 294 ASP A OD1 1 ATOM 1912 O OD2 . ASP A 1 241 ? 36.013 32.700 14.065 1.00 33.67 ? 294 ASP A OD2 1 ATOM 1913 N N . PRO A 1 242 ? 31.657 34.174 16.121 1.00 29.01 ? 295 PRO A N 1 ATOM 1914 C CA . PRO A 1 242 ? 30.287 34.375 15.655 1.00 27.56 ? 295 PRO A CA 1 ATOM 1915 C C . PRO A 1 242 ? 30.172 34.071 14.164 1.00 27.45 ? 295 PRO A C 1 ATOM 1916 O O . PRO A 1 242 ? 29.133 33.603 13.718 1.00 26.44 ? 295 PRO A O 1 ATOM 1917 C CB . PRO A 1 242 ? 30.019 35.861 15.939 1.00 27.61 ? 295 PRO A CB 1 ATOM 1918 C CG . PRO A 1 242 ? 31.355 36.488 16.118 1.00 28.19 ? 295 PRO A CG 1 ATOM 1919 C CD . PRO A 1 242 ? 32.268 35.408 16.639 1.00 29.71 ? 295 PRO A CD 1 ATOM 1920 N N . MET A 1 243 ? 31.233 34.319 13.407 1.00 31.58 ? 296 MET A N 1 ATOM 1921 C CA . MET A 1 243 ? 31.231 33.983 11.988 1.00 34.38 ? 296 MET A CA 1 ATOM 1922 C C . MET A 1 243 ? 31.136 32.478 11.786 1.00 35.01 ? 296 MET A C 1 ATOM 1923 O O . MET A 1 243 ? 30.463 32.013 10.874 1.00 36.56 ? 296 MET A O 1 ATOM 1924 C CB . MET A 1 243 ? 32.489 34.512 11.301 1.00 36.14 ? 296 MET A CB 1 ATOM 1925 C CG . MET A 1 243 ? 32.423 35.977 10.969 1.00 38.88 ? 296 MET A CG 1 ATOM 1926 S SD . MET A 1 243 ? 31.241 36.342 9.648 1.00 38.34 ? 296 MET A SD 1 ATOM 1927 C CE . MET A 1 243 ? 31.528 38.067 9.499 1.00 38.20 ? 296 MET A CE 1 ATOM 1928 N N . LEU A 1 244 ? 31.816 31.712 12.630 1.00 35.72 ? 297 LEU A N 1 ATOM 1929 C CA . LEU A 1 244 ? 31.733 30.259 12.547 1.00 36.62 ? 297 LEU A CA 1 ATOM 1930 C C . LEU A 1 244 ? 30.389 29.744 13.046 1.00 36.26 ? 297 LEU A C 1 ATOM 1931 O O . LEU A 1 244 ? 29.893 28.716 12.587 1.00 34.62 ? 297 LEU A O 1 ATOM 1932 C CB . LEU A 1 244 ? 32.862 29.613 13.349 1.00 40.29 ? 297 LEU A CB 1 ATOM 1933 C CG . LEU A 1 244 ? 34.258 29.694 12.731 1.00 40.10 ? 297 LEU A CG 1 ATOM 1934 C CD1 . LEU A 1 244 ? 35.196 28.737 13.446 1.00 41.54 ? 297 LEU A CD1 1 ATOM 1935 C CD2 . LEU A 1 244 ? 34.202 29.392 11.239 1.00 40.84 ? 297 LEU A CD2 1 ATOM 1936 N N . LEU A 1 245 ? 29.798 30.445 14.001 1.00 33.73 ? 298 LEU A N 1 ATOM 1937 C CA . LEU A 1 245 ? 28.599 29.937 14.646 1.00 31.15 ? 298 LEU A CA 1 ATOM 1938 C C . LEU A 1 245 ? 27.390 30.121 13.724 1.00 28.82 ? 298 LEU A C 1 ATOM 1939 O O . LEU A 1 245 ? 26.427 29.376 13.809 1.00 28.26 ? 298 LEU A O 1 ATOM 1940 C CB . LEU A 1 245 ? 28.377 30.635 15.994 1.00 31.46 ? 298 LEU A CB 1 ATOM 1941 C CG . LEU A 1 245 ? 28.423 29.721 17.220 1.00 35.07 ? 298 LEU A CG 1 ATOM 1942 C CD1 . LEU A 1 245 ? 27.228 29.968 18.121 1.00 38.08 ? 298 LEU A CD1 1 ATOM 1943 C CD2 . LEU A 1 245 ? 28.491 28.261 16.798 1.00 36.30 ? 298 LEU A CD2 1 ATOM 1944 N N . TYR A 1 246 ? 27.459 31.115 12.842 1.00 31.03 ? 299 TYR A N 1 ATOM 1945 C CA . TYR A 1 246 ? 26.321 31.503 12.010 1.00 28.60 ? 299 TYR A CA 1 ATOM 1946 C C . TYR A 1 246 ? 26.207 30.596 10.784 1.00 31.76 ? 299 TYR A C 1 ATOM 1947 O O . TYR A 1 246 ? 26.947 30.749 9.813 1.00 31.94 ? 299 TYR A O 1 ATOM 1948 C CB . TYR A 1 246 ? 26.470 32.958 11.559 1.00 29.67 ? 299 TYR A CB 1 ATOM 1949 C CG . TYR A 1 246 ? 25.248 33.548 10.868 1.00 31.31 ? 299 TYR A CG 1 ATOM 1950 C CD1 . TYR A 1 246 ? 25.029 33.353 9.508 1.00 33.06 ? 299 TYR A CD1 1 ATOM 1951 C CD2 . TYR A 1 246 ? 24.324 34.319 11.572 1.00 31.69 ? 299 TYR A CD2 1 ATOM 1952 C CE1 . TYR A 1 246 ? 23.919 33.895 8.872 1.00 32.45 ? 299 TYR A CE1 1 ATOM 1953 C CE2 . TYR A 1 246 ? 23.210 34.864 10.940 1.00 32.00 ? 299 TYR A CE2 1 ATOM 1954 C CZ . TYR A 1 246 ? 23.014 34.648 9.591 1.00 31.87 ? 299 TYR A CZ 1 ATOM 1955 O OH . TYR A 1 246 ? 21.917 35.190 8.950 1.00 28.48 ? 299 TYR A OH 1 ATOM 1956 N N . ASN A 1 247 ? 25.268 29.662 10.830 1.00 30.65 ? 300 ASN A N 1 ATOM 1957 C CA . ASN A 1 247 ? 24.985 28.808 9.687 1.00 32.92 ? 300 ASN A CA 1 ATOM 1958 C C . ASN A 1 247 ? 23.520 28.904 9.263 1.00 32.31 ? 300 ASN A C 1 ATOM 1959 O O . ASN A 1 247 ? 22.654 28.264 9.846 1.00 31.87 ? 300 ASN A O 1 ATOM 1960 C CB . ASN A 1 247 ? 25.343 27.361 10.026 1.00 36.56 ? 300 ASN A CB 1 ATOM 1961 C CG . ASN A 1 247 ? 26.733 27.233 10.622 1.00 39.84 ? 300 ASN A CG 1 ATOM 1962 O OD1 . ASN A 1 247 ? 27.737 27.341 9.913 1.00 40.81 ? 300 ASN A OD1 1 ATOM 1963 N ND2 . ASN A 1 247 ? 26.801 27.024 11.933 1.00 38.37 ? 300 ASN A ND2 1 ATOM 1964 N N . LYS A 1 248 ? 23.251 29.713 8.246 1.00 35.03 ? 301 LYS A N 1 ATOM 1965 C CA . LYS A 1 248 ? 21.881 29.942 7.795 1.00 35.79 ? 301 LYS A CA 1 ATOM 1966 C C . LYS A 1 248 ? 21.469 28.915 6.741 1.00 37.97 ? 301 LYS A C 1 ATOM 1967 O O . LYS A 1 248 ? 22.062 28.841 5.660 1.00 40.27 ? 301 LYS A O 1 ATOM 1968 C CB . LYS A 1 248 ? 21.718 31.365 7.253 1.00 34.80 ? 301 LYS A CB 1 ATOM 1969 C CG . LYS A 1 248 ? 20.319 31.683 6.735 1.00 37.98 ? 301 LYS A CG 1 ATOM 1970 C CD . LYS A 1 248 ? 20.146 33.172 6.425 1.00 40.74 ? 301 LYS A CD 1 ATOM 1971 C CE . LYS A 1 248 ? 20.149 33.456 4.919 1.00 43.18 ? 301 LYS A CE 1 ATOM 1972 N NZ . LYS A 1 248 ? 18.948 34.235 4.474 1.00 42.75 ? 301 LYS A NZ 1 ATOM 1973 N N . MET A 1 249 ? 20.456 28.127 7.088 1.00 35.66 ? 302 MET A N 1 ATOM 1974 C CA . MET A 1 249 ? 19.940 27.055 6.251 1.00 37.90 ? 302 MET A CA 1 ATOM 1975 C C . MET A 1 249 ? 18.465 27.318 6.030 1.00 39.24 ? 302 MET A C 1 ATOM 1976 O O . MET A 1 249 ? 17.902 28.208 6.667 1.00 36.32 ? 302 MET A O 1 ATOM 1977 C CB . MET A 1 249 ? 20.069 25.715 6.969 1.00 40.20 ? 302 MET A CB 1 ATOM 1978 C CG . MET A 1 249 ? 21.266 24.894 6.582 1.00 43.04 ? 302 MET A CG 1 ATOM 1979 S SD . MET A 1 249 ? 21.783 23.872 7.958 1.00 45.33 ? 302 MET A SD 1 ATOM 1980 C CE . MET A 1 249 ? 22.900 24.976 8.743 1.00 43.49 ? 302 MET A CE 1 ATOM 1981 N N . THR A 1 250 ? 17.835 26.527 5.159 1.00 37.25 ? 303 THR A N 1 ATOM 1982 C CA . THR A 1 250 ? 16.382 26.372 5.160 1.00 36.46 ? 303 THR A CA 1 ATOM 1983 C C . THR A 1 250 ? 15.969 25.135 5.947 1.00 34.66 ? 303 THR A C 1 ATOM 1984 O O . THR A 1 250 ? 16.736 24.189 6.079 1.00 40.62 ? 303 THR A O 1 ATOM 1985 C CB . THR A 1 250 ? 15.831 26.280 3.700 1.00 36.73 ? 303 THR A CB 1 ATOM 1986 O OG1 . THR A 1 250 ? 16.210 25.034 3.105 1.00 34.63 ? 303 THR A OG1 1 ATOM 1987 C CG2 . THR A 1 250 ? 16.474 27.314 2.794 1.00 37.46 ? 303 THR A CG2 1 ATOM 1988 N N . LEU A 1 251 ? 14.750 25.143 6.468 1.00 36.75 ? 304 LEU A N 1 ATOM 1989 C CA . LEU A 1 251 ? 14.195 23.980 7.145 1.00 37.58 ? 304 LEU A CA 1 ATOM 1990 C C . LEU A 1 251 ? 14.322 22.723 6.292 1.00 42.00 ? 304 LEU A C 1 ATOM 1991 O O . LEU A 1 251 ? 14.449 21.612 6.813 1.00 39.50 ? 304 LEU A O 1 ATOM 1992 C CB . LEU A 1 251 ? 12.722 24.216 7.454 1.00 39.99 ? 304 LEU A CB 1 ATOM 1993 C CG . LEU A 1 251 ? 12.371 24.876 8.782 1.00 41.38 ? 304 LEU A CG 1 ATOM 1994 C CD1 . LEU A 1 251 ? 10.910 24.619 9.094 1.00 42.46 ? 304 LEU A CD1 1 ATOM 1995 C CD2 . LEU A 1 251 ? 13.250 24.357 9.898 1.00 41.80 ? 304 LEU A CD2 1 ATOM 1996 N N . ALA A 1 252 ? 14.256 22.902 4.978 1.00 40.32 ? 305 ALA A N 1 ATOM 1997 C CA . ALA A 1 252 ? 14.526 21.812 4.055 1.00 42.70 ? 305 ALA A CA 1 ATOM 1998 C C . ALA A 1 252 ? 15.943 21.288 4.253 1.00 37.84 ? 305 ALA A C 1 ATOM 1999 O O . ALA A 1 252 ? 16.141 20.120 4.561 1.00 38.97 ? 305 ALA A O 1 ATOM 2000 C CB . ALA A 1 252 ? 14.329 22.275 2.621 1.00 41.39 ? 305 ALA A CB 1 ATOM 2001 N N . GLN A 1 253 ? 16.927 22.158 4.082 1.00 40.10 ? 306 GLN A N 1 ATOM 2002 C CA . GLN A 1 253 ? 18.306 21.766 4.322 1.00 40.99 ? 306 GLN A CA 1 ATOM 2003 C C . GLN A 1 253 ? 18.417 21.059 5.668 1.00 38.90 ? 306 GLN A C 1 ATOM 2004 O O . GLN A 1 253 ? 19.052 20.014 5.779 1.00 39.33 ? 306 GLN A O 1 ATOM 2005 C CB . GLN A 1 253 ? 19.229 22.980 4.281 1.00 43.75 ? 306 GLN A CB 1 ATOM 2006 C CG . GLN A 1 253 ? 18.977 23.912 3.120 1.00 44.54 ? 306 GLN A CG 1 ATOM 2007 C CD . GLN A 1 253 ? 20.200 24.724 2.758 1.00 46.41 ? 306 GLN A CD 1 ATOM 2008 O OE1 . GLN A 1 253 ? 21.258 24.159 2.473 1.00 46.36 ? 306 GLN A OE1 1 ATOM 2009 N NE2 . GLN A 1 253 ? 20.062 26.050 2.758 1.00 44.88 ? 306 GLN A NE2 1 ATOM 2010 N N . ILE A 1 254 ? 17.779 21.626 6.687 1.00 39.70 ? 307 ILE A N 1 ATOM 2011 C CA . ILE A 1 254 ? 17.859 21.088 8.038 1.00 39.64 ? 307 ILE A CA 1 ATOM 2012 C C . ILE A 1 254 ? 17.302 19.683 8.099 1.00 40.74 ? 307 ILE A C 1 ATOM 2013 O O . ILE A 1 254 ? 17.910 18.786 8.684 1.00 42.68 ? 307 ILE A O 1 ATOM 2014 C CB . ILE A 1 254 ? 17.084 21.992 9.024 1.00 39.11 ? 307 ILE A CB 1 ATOM 2015 C CG1 . ILE A 1 254 ? 17.821 23.310 9.234 1.00 37.70 ? 307 ILE A CG1 1 ATOM 2016 C CG2 . ILE A 1 254 ? 16.897 21.287 10.344 1.00 35.89 ? 307 ILE A CG2 1 ATOM 2017 C CD1 . ILE A 1 254 ? 17.124 24.233 10.203 1.00 41.30 ? 307 ILE A CD1 1 ATOM 2018 N N . GLN A 1 255 ? 16.129 19.492 7.507 1.00 43.63 ? 308 GLN A N 1 ATOM 2019 C CA . GLN A 1 255 ? 15.516 18.174 7.457 1.00 44.24 ? 308 GLN A CA 1 ATOM 2020 C C . GLN A 1 255 ? 16.450 17.186 6.775 1.00 45.51 ? 308 GLN A C 1 ATOM 2021 O O . GLN A 1 255 ? 16.512 16.016 7.149 1.00 44.09 ? 308 GLN A O 1 ATOM 2022 C CB . GLN A 1 255 ? 14.187 18.218 6.699 1.00 44.56 ? 308 GLN A CB 1 ATOM 2023 C CG . GLN A 1 255 ? 13.373 16.956 6.861 1.00 44.70 ? 308 GLN A CG 1 ATOM 2024 C CD . GLN A 1 255 ? 13.017 16.686 8.308 1.00 47.13 ? 308 GLN A CD 1 ATOM 2025 O OE1 . GLN A 1 255 ? 12.440 17.543 8.973 1.00 46.78 ? 308 GLN A OE1 1 ATOM 2026 N NE2 . GLN A 1 255 ? 13.353 15.496 8.799 1.00 46.62 ? 308 GLN A NE2 1 ATOM 2027 N N . ASN A 1 256 ? 17.166 17.655 5.764 1.00 49.79 ? 309 ASN A N 1 ATOM 2028 C CA . ASN A 1 256 ? 17.956 16.755 4.935 1.00 54.11 ? 309 ASN A CA 1 ATOM 2029 C C . ASN A 1 256 ? 19.357 16.541 5.500 1.00 53.14 ? 309 ASN A C 1 ATOM 2030 O O . ASN A 1 256 ? 19.989 15.520 5.234 1.00 56.63 ? 309 ASN A O 1 ATOM 2031 C CB . ASN A 1 256 ? 18.008 17.256 3.489 1.00 57.81 ? 309 ASN A CB 1 ATOM 2032 C CG . ASN A 1 256 ? 17.189 16.384 2.545 1.00 61.39 ? 309 ASN A CG 1 ATOM 2033 O OD1 . ASN A 1 256 ? 16.028 16.070 2.818 1.00 61.70 ? 309 ASN A OD1 1 ATOM 2034 N ND2 . ASN A 1 256 ? 17.796 15.981 1.434 1.00 63.47 ? 309 ASN A ND2 1 ATOM 2035 N N . ASN A 1 257 ? 19.828 17.487 6.306 1.00 50.68 ? 310 ASN A N 1 ATOM 2036 C CA . ASN A 1 257 ? 21.193 17.431 6.816 1.00 49.63 ? 310 ASN A CA 1 ATOM 2037 C C . ASN A 1 257 ? 21.274 17.078 8.305 1.00 48.68 ? 310 ASN A C 1 ATOM 2038 O O . ASN A 1 257 ? 22.344 16.728 8.797 1.00 47.15 ? 310 ASN A O 1 ATOM 2039 C CB . ASN A 1 257 ? 21.910 18.757 6.558 1.00 51.47 ? 310 ASN A CB 1 ATOM 2040 C CG . ASN A 1 257 ? 22.328 18.922 5.106 1.00 52.65 ? 310 ASN A CG 1 ATOM 2041 O OD1 . ASN A 1 257 ? 22.559 17.940 4.402 1.00 55.15 ? 310 ASN A OD1 1 ATOM 2042 N ND2 . ASN A 1 257 ? 22.429 20.166 4.655 1.00 51.01 ? 310 ASN A ND2 1 ATOM 2043 N N . PHE A 1 258 ? 20.150 17.167 9.017 1.00 45.96 ? 311 PHE A N 1 ATOM 2044 C CA . PHE A 1 258 ? 20.127 16.858 10.447 1.00 40.31 ? 311 PHE A CA 1 ATOM 2045 C C . PHE A 1 258 ? 18.897 16.066 10.868 1.00 41.53 ? 311 PHE A C 1 ATOM 2046 O O . PHE A 1 258 ? 18.087 16.548 11.666 1.00 43.23 ? 311 PHE A O 1 ATOM 2047 C CB . PHE A 1 258 ? 20.192 18.148 11.276 1.00 38.49 ? 311 PHE A CB 1 ATOM 2048 C CG . PHE A 1 258 ? 21.377 19.001 10.968 1.00 36.81 ? 311 PHE A CG 1 ATOM 2049 C CD1 . PHE A 1 258 ? 22.646 18.600 11.332 1.00 35.38 ? 311 PHE A CD1 1 ATOM 2050 C CD2 . PHE A 1 258 ? 21.224 20.208 10.315 1.00 36.36 ? 311 PHE A CD2 1 ATOM 2051 C CE1 . PHE A 1 258 ? 23.744 19.389 11.044 1.00 35.64 ? 311 PHE A CE1 1 ATOM 2052 C CE2 . PHE A 1 258 ? 22.320 20.993 10.024 1.00 37.95 ? 311 PHE A CE2 1 ATOM 2053 C CZ . PHE A 1 258 ? 23.581 20.580 10.393 1.00 34.06 ? 311 PHE A CZ 1 ATOM 2054 N N . SER A 1 259 ? 18.776 14.841 10.365 1.00 41.80 ? 312 SER A N 1 ATOM 2055 C CA . SER A 1 259 ? 17.643 13.983 10.698 1.00 40.21 ? 312 SER A CA 1 ATOM 2056 C C . SER A 1 259 ? 17.780 13.394 12.098 1.00 39.63 ? 312 SER A C 1 ATOM 2057 O O . SER A 1 259 ? 18.876 13.063 12.546 1.00 36.74 ? 312 SER A O 1 ATOM 2058 C CB . SER A 1 259 ? 17.491 12.858 9.670 1.00 40.10 ? 312 SER A CB 1 ATOM 2059 O OG . SER A 1 259 ? 18.676 12.090 9.560 1.00 41.33 ? 312 SER A OG 1 ATOM 2060 N N . LEU A 1 260 ? 16.652 13.279 12.789 1.00 38.26 ? 313 LEU A N 1 ATOM 2061 C CA . LEU A 1 260 ? 16.594 12.565 14.048 1.00 38.40 ? 313 LEU A CA 1 ATOM 2062 C C . LEU A 1 260 ? 15.485 11.540 13.981 1.00 40.07 ? 313 LEU A C 1 ATOM 2063 O O . LEU A 1 260 ? 14.489 11.744 13.286 1.00 43.24 ? 313 LEU A O 1 ATOM 2064 C CB . LEU A 1 260 ? 16.323 13.534 15.199 1.00 38.29 ? 313 LEU A CB 1 ATOM 2065 C CG . LEU A 1 260 ? 17.389 14.602 15.444 1.00 34.18 ? 313 LEU A CG 1 ATOM 2066 C CD1 . LEU A 1 260 ? 16.810 15.758 16.244 1.00 32.91 ? 313 LEU A CD1 1 ATOM 2067 C CD2 . LEU A 1 260 ? 18.571 14.006 16.160 1.00 35.52 ? 313 LEU A CD2 1 ATOM 2068 N N . GLU A 1 261 ? 15.649 10.447 14.713 1.00 40.13 ? 314 GLU A N 1 ATOM 2069 C CA . GLU A 1 261 ? 14.575 9.481 14.878 1.00 44.33 ? 314 GLU A CA 1 ATOM 2070 C C . GLU A 1 261 ? 14.301 9.233 16.355 1.00 41.51 ? 314 GLU A C 1 ATOM 2071 O O . GLU A 1 261 ? 15.060 8.537 17.030 1.00 42.63 ? 314 GLU A O 1 ATOM 2072 C CB . GLU A 1 261 ? 14.929 8.173 14.162 1.00 48.95 ? 314 GLU A CB 1 ATOM 2073 C CG . GLU A 1 261 ? 14.264 6.937 14.742 1.00 52.83 ? 314 GLU A CG 1 ATOM 2074 C CD . GLU A 1 261 ? 13.998 5.867 13.695 1.00 56.39 ? 314 GLU A CD 1 ATOM 2075 O OE1 . GLU A 1 261 ? 12.830 5.734 13.264 1.00 57.60 ? 314 GLU A OE1 1 ATOM 2076 O OE2 . GLU A 1 261 ? 14.956 5.156 13.309 1.00 58.29 ? 314 GLU A OE2 1 ATOM 2077 N N . ILE A 1 262 ? 13.210 9.808 16.851 1.00 44.36 ? 315 ILE A N 1 ATOM 2078 C CA . ILE A 1 262 ? 12.816 9.643 18.246 1.00 43.82 ? 315 ILE A CA 1 ATOM 2079 C C . ILE A 1 262 ? 11.641 8.683 18.381 1.00 45.32 ? 315 ILE A C 1 ATOM 2080 O O . ILE A 1 262 ? 10.640 8.809 17.669 1.00 45.13 ? 315 ILE A O 1 ATOM 2081 C CB . ILE A 1 262 ? 12.440 11.000 18.857 1.00 42.73 ? 315 ILE A CB 1 ATOM 2082 C CG1 . ILE A 1 262 ? 13.643 11.943 18.849 1.00 43.51 ? 315 ILE A CG1 1 ATOM 2083 C CG2 . ILE A 1 262 ? 11.915 10.809 20.270 1.00 42.60 ? 315 ILE A CG2 1 ATOM 2084 C CD1 . ILE A 1 262 ? 14.610 11.696 17.703 1.00 43.13 ? 315 ILE A CD1 1 ATOM 2085 N N . ASN A 1 263 ? 11.747 7.736 19.308 1.00 46.94 ? 316 ASN A N 1 ATOM 2086 C CA . ASN A 1 263 ? 10.657 6.800 19.544 1.00 50.91 ? 316 ASN A CA 1 ATOM 2087 C C . ASN A 1 263 ? 10.182 6.203 18.227 1.00 53.45 ? 316 ASN A C 1 ATOM 2088 O O . ASN A 1 263 ? 9.074 5.675 18.137 1.00 52.56 ? 316 ASN A O 1 ATOM 2089 C CB . ASN A 1 263 ? 9.488 7.509 20.233 1.00 50.90 ? 316 ASN A CB 1 ATOM 2090 C CG . ASN A 1 263 ? 8.746 6.611 21.207 1.00 52.35 ? 316 ASN A CG 1 ATOM 2091 O OD1 . ASN A 1 263 ? 7.517 6.637 21.279 1.00 51.53 ? 316 ASN A OD1 1 ATOM 2092 N ND2 . ASN A 1 263 ? 9.492 5.819 21.973 1.00 53.97 ? 316 ASN A ND2 1 ATOM 2093 N N . GLY A 1 264 ? 11.029 6.299 17.205 1.00 55.29 ? 317 GLY A N 1 ATOM 2094 C CA . GLY A 1 264 ? 10.686 5.840 15.871 1.00 56.93 ? 317 GLY A CA 1 ATOM 2095 C C . GLY A 1 264 ? 9.658 6.733 15.208 1.00 58.50 ? 317 GLY A C 1 ATOM 2096 O O . GLY A 1 264 ? 8.513 6.326 15.010 1.00 60.77 ? 317 GLY A O 1 ATOM 2097 N N . LYS A 1 265 ? 10.057 7.955 14.866 1.00 58.68 ? 318 LYS A N 1 ATOM 2098 C CA . LYS A 1 265 ? 9.207 8.815 14.052 1.00 58.92 ? 318 LYS A CA 1 ATOM 2099 C C . LYS A 1 265 ? 9.389 8.496 12.574 1.00 57.23 ? 318 LYS A C 1 ATOM 2100 O O . LYS A 1 265 ? 8.679 7.653 12.026 1.00 60.06 ? 318 LYS A O 1 ATOM 2101 C CB . LYS A 1 265 ? 9.500 10.291 14.323 1.00 60.67 ? 318 LYS A CB 1 ATOM 2102 C CG . LYS A 1 265 ? 8.373 11.025 15.059 1.00 59.77 ? 318 LYS A CG 1 ATOM 2103 C CD . LYS A 1 265 ? 7.097 11.113 14.221 1.00 58.19 ? 318 LYS A CD 1 ATOM 2104 C CE . LYS A 1 265 ? 6.814 12.545 13.783 1.00 56.24 ? 318 LYS A CE 1 ATOM 2105 N NZ . LYS A 1 265 ? 5.385 12.926 13.945 1.00 54.31 ? 318 LYS A NZ 1 ATOM 2106 N N . PRO A 1 266 ? 10.336 9.165 11.926 1.00 53.59 ? 319 PRO A N 1 ATOM 2107 C CA . PRO A 1 266 ? 11.259 10.087 12.585 1.00 48.90 ? 319 PRO A CA 1 ATOM 2108 C C . PRO A 1 266 ? 10.784 11.535 12.557 1.00 46.95 ? 319 PRO A C 1 ATOM 2109 O O . PRO A 1 266 ? 9.598 11.799 12.360 1.00 41.37 ? 319 PRO A O 1 ATOM 2110 C CB . PRO A 1 266 ? 12.505 9.964 11.722 1.00 52.61 ? 319 PRO A CB 1 ATOM 2111 C CG . PRO A 1 266 ? 11.953 9.742 10.326 1.00 52.68 ? 319 PRO A CG 1 ATOM 2112 C CD . PRO A 1 266 ? 10.611 9.061 10.483 1.00 52.70 ? 319 PRO A CD 1 ATOM 2113 N N . PHE A 1 267 ? 11.721 12.462 12.738 1.00 42.88 ? 320 PHE A N 1 ATOM 2114 C CA . PHE A 1 267 ? 11.432 13.750 13.357 1.00 40.63 ? 320 PHE A CA 1 ATOM 2115 C C . PHE A 1 267 ? 11.227 14.797 12.277 1.00 40.86 ? 320 PHE A C 1 ATOM 2116 O O . PHE A 1 267 ? 12.045 14.928 11.365 1.00 41.20 ? 320 PHE A O 1 ATOM 2117 C CB . PHE A 1 267 ? 12.590 14.154 14.276 1.00 38.09 ? 320 PHE A CB 1 ATOM 2118 C CG . PHE A 1 267 ? 12.393 15.466 14.986 1.00 32.74 ? 320 PHE A CG 1 ATOM 2119 C CD1 . PHE A 1 267 ? 12.871 16.644 14.439 1.00 31.73 ? 320 PHE A CD1 1 ATOM 2120 C CD2 . PHE A 1 267 ? 11.770 15.516 16.223 1.00 31.27 ? 320 PHE A CD2 1 ATOM 2121 C CE1 . PHE A 1 267 ? 12.718 17.855 15.108 1.00 31.24 ? 320 PHE A CE1 1 ATOM 2122 C CE2 . PHE A 1 267 ? 11.614 16.732 16.898 1.00 30.09 ? 320 PHE A CE2 1 ATOM 2123 C CZ . PHE A 1 267 ? 12.088 17.893 16.342 1.00 26.93 ? 320 PHE A CZ 1 ATOM 2124 N N . SER A 1 268 ? 10.133 15.544 12.374 1.00 39.33 ? 321 SER A N 1 ATOM 2125 C CA . SER A 1 268 ? 9.789 16.499 11.332 1.00 40.12 ? 321 SER A CA 1 ATOM 2126 C C . SER A 1 268 ? 10.038 17.911 11.814 1.00 38.85 ? 321 SER A C 1 ATOM 2127 O O . SER A 1 268 ? 9.299 18.429 12.648 1.00 40.70 ? 321 SER A O 1 ATOM 2128 C CB . SER A 1 268 ? 8.322 16.357 10.907 1.00 38.00 ? 321 SER A CB 1 ATOM 2129 O OG . SER A 1 268 ? 7.967 17.381 9.993 1.00 36.26 ? 321 SER A OG 1 ATOM 2130 N N . TRP A 1 269 ? 11.074 18.531 11.262 1.00 40.02 ? 322 TRP A N 1 ATOM 2131 C CA . TRP A 1 269 ? 11.466 19.878 11.638 1.00 40.12 ? 322 TRP A CA 1 ATOM 2132 C C . TRP A 1 269 ? 10.391 20.896 11.253 1.00 42.74 ? 322 TRP A C 1 ATOM 2133 O O . TRP A 1 269 ? 10.119 21.845 11.994 1.00 40.03 ? 322 TRP A O 1 ATOM 2134 C CB . TRP A 1 269 ? 12.802 20.225 10.974 1.00 39.62 ? 322 TRP A CB 1 ATOM 2135 C CG . TRP A 1 269 ? 13.970 19.525 11.612 1.00 39.63 ? 322 TRP A CG 1 ATOM 2136 C CD1 . TRP A 1 269 ? 14.539 18.347 11.219 1.00 40.94 ? 322 TRP A CD1 1 ATOM 2137 C CD2 . TRP A 1 269 ? 14.699 19.950 12.771 1.00 39.82 ? 322 TRP A CD2 1 ATOM 2138 N NE1 . TRP A 1 269 ? 15.578 18.017 12.059 1.00 41.11 ? 322 TRP A NE1 1 ATOM 2139 C CE2 . TRP A 1 269 ? 15.698 18.986 13.019 1.00 38.44 ? 322 TRP A CE2 1 ATOM 2140 C CE3 . TRP A 1 269 ? 14.611 21.052 13.627 1.00 37.42 ? 322 TRP A CE3 1 ATOM 2141 C CZ2 . TRP A 1 269 ? 16.594 19.090 14.082 1.00 37.66 ? 322 TRP A CZ2 1 ATOM 2142 C CZ3 . TRP A 1 269 ? 15.504 21.153 14.682 1.00 38.29 ? 322 TRP A CZ3 1 ATOM 2143 C CH2 . TRP A 1 269 ? 16.480 20.179 14.898 1.00 35.65 ? 322 TRP A CH2 1 ATOM 2144 N N . LEU A 1 270 ? 9.781 20.696 10.089 1.00 42.12 ? 323 LEU A N 1 ATOM 2145 C CA . LEU A 1 270 ? 8.624 21.487 9.686 1.00 40.10 ? 323 LEU A CA 1 ATOM 2146 C C . LEU A 1 270 ? 7.523 21.446 10.736 1.00 38.07 ? 323 LEU A C 1 ATOM 2147 O O . LEU A 1 270 ? 6.912 22.464 11.055 1.00 39.50 ? 323 LEU A O 1 ATOM 2148 C CB . LEU A 1 270 ? 8.065 20.965 8.366 1.00 41.13 ? 323 LEU A CB 1 ATOM 2149 C CG . LEU A 1 270 ? 7.067 21.909 7.702 1.00 44.54 ? 323 LEU A CG 1 ATOM 2150 C CD1 . LEU A 1 270 ? 7.604 23.336 7.735 1.00 43.34 ? 323 LEU A CD1 1 ATOM 2151 C CD2 . LEU A 1 270 ? 6.772 21.457 6.272 1.00 46.08 ? 323 LEU A CD2 1 ATOM 2152 N N . ASN A 1 271 ? 7.262 20.255 11.254 1.00 37.02 ? 324 ASN A N 1 ATOM 2153 C CA . ASN A 1 271 ? 6.138 20.037 12.142 1.00 36.38 ? 324 ASN A CA 1 ATOM 2154 C C . ASN A 1 271 ? 6.441 20.572 13.536 1.00 37.84 ? 324 ASN A C 1 ATOM 2155 O O . ASN A 1 271 ? 5.650 21.319 14.113 1.00 36.63 ? 324 ASN A O 1 ATOM 2156 C CB . ASN A 1 271 ? 5.829 18.544 12.220 1.00 37.67 ? 324 ASN A CB 1 ATOM 2157 C CG . ASN A 1 271 ? 4.690 18.231 13.161 1.00 39.27 ? 324 ASN A CG 1 ATOM 2158 O OD1 . ASN A 1 271 ? 4.867 17.526 14.159 1.00 39.30 ? 324 ASN A OD1 1 ATOM 2159 N ND2 . ASN A 1 271 ? 3.504 18.747 12.845 1.00 43.45 ? 324 ASN A ND2 1 ATOM 2160 N N . PHE A 1 272 ? 7.593 20.170 14.067 1.00 35.31 ? 325 PHE A N 1 ATOM 2161 C CA . PHE A 1 272 ? 8.142 20.739 15.301 1.00 33.82 ? 325 PHE A CA 1 ATOM 2162 C C . PHE A 1 272 ? 8.045 22.263 15.261 1.00 32.52 ? 325 PHE A C 1 ATOM 2163 O O . PHE A 1 272 ? 7.519 22.875 16.186 1.00 36.10 ? 325 PHE A O 1 ATOM 2164 C CB . PHE A 1 272 ? 9.599 20.264 15.484 1.00 31.51 ? 325 PHE A CB 1 ATOM 2165 C CG . PHE A 1 272 ? 10.386 21.018 16.545 1.00 29.42 ? 325 PHE A CG 1 ATOM 2166 C CD1 . PHE A 1 272 ? 11.594 21.625 16.221 1.00 31.17 ? 325 PHE A CD1 1 ATOM 2167 C CD2 . PHE A 1 272 ? 9.950 21.074 17.857 1.00 30.63 ? 325 PHE A CD2 1 ATOM 2168 C CE1 . PHE A 1 272 ? 12.337 22.294 17.179 1.00 30.94 ? 325 PHE A CE1 1 ATOM 2169 C CE2 . PHE A 1 272 ? 10.691 21.742 18.817 1.00 30.87 ? 325 PHE A CE2 1 ATOM 2170 C CZ . PHE A 1 272 ? 11.873 22.359 18.475 1.00 31.05 ? 325 PHE A CZ 1 ATOM 2171 N N . THR A 1 273 ? 8.523 22.865 14.177 1.00 31.62 ? 326 THR A N 1 ATOM 2172 C CA . THR A 1 273 ? 8.642 24.320 14.083 1.00 29.62 ? 326 THR A CA 1 ATOM 2173 C C . THR A 1 273 ? 7.286 25.016 13.963 1.00 34.61 ? 326 THR A C 1 ATOM 2174 O O . THR A 1 273 ? 7.056 26.068 14.565 1.00 32.43 ? 326 THR A O 1 ATOM 2175 C CB . THR A 1 273 ? 9.502 24.698 12.879 1.00 30.70 ? 326 THR A CB 1 ATOM 2176 O OG1 . THR A 1 273 ? 10.885 24.393 13.135 1.00 35.21 ? 326 THR A OG1 1 ATOM 2177 C CG2 . THR A 1 273 ? 9.495 26.183 12.659 1.00 28.65 ? 326 THR A CG2 1 ATOM 2178 N N . ASN A 1 274 ? 6.387 24.443 13.173 1.00 36.78 ? 327 ASN A N 1 ATOM 2179 C CA . ASN A 1 274 ? 5.019 24.946 13.135 1.00 37.99 ? 327 ASN A CA 1 ATOM 2180 C C . ASN A 1 274 ? 4.267 24.722 14.445 1.00 35.90 ? 327 ASN A C 1 ATOM 2181 O O . ASN A 1 274 ? 3.428 25.537 14.839 1.00 35.61 ? 327 ASN A O 1 ATOM 2182 C CB . ASN A 1 274 ? 4.249 24.330 11.958 1.00 38.38 ? 327 ASN A CB 1 ATOM 2183 C CG . ASN A 1 274 ? 4.525 25.050 10.655 1.00 37.69 ? 327 ASN A CG 1 ATOM 2184 O OD1 . ASN A 1 274 ? 4.447 26.276 10.585 1.00 36.04 ? 327 ASN A OD1 1 ATOM 2185 N ND2 . ASN A 1 274 ? 4.874 24.293 9.618 1.00 41.66 ? 327 ASN A ND2 1 ATOM 2186 N N . GLU A 1 275 ? 4.559 23.620 15.125 1.00 37.38 ? 328 GLU A N 1 ATOM 2187 C CA . GLU A 1 275 ? 3.847 23.302 16.355 1.00 36.56 ? 328 GLU A CA 1 ATOM 2188 C C . GLU A 1 275 ? 4.265 24.259 17.463 1.00 38.94 ? 328 GLU A C 1 ATOM 2189 O O . GLU A 1 275 ? 3.565 24.410 18.464 1.00 39.38 ? 328 GLU A O 1 ATOM 2190 C CB . GLU A 1 275 ? 4.100 21.853 16.775 1.00 38.96 ? 328 GLU A CB 1 ATOM 2191 C CG . GLU A 1 275 ? 3.199 20.847 16.077 1.00 41.90 ? 328 GLU A CG 1 ATOM 2192 C CD . GLU A 1 275 ? 2.053 20.374 16.951 1.00 42.78 ? 328 GLU A CD 1 ATOM 2193 O OE1 . GLU A 1 275 ? 2.012 20.770 18.134 1.00 41.31 ? 328 GLU A OE1 1 ATOM 2194 O OE2 . GLU A 1 275 ? 1.189 19.609 16.459 1.00 41.78 ? 328 GLU A OE2 1 ATOM 2195 N N . ILE A 1 276 ? 5.410 24.908 17.271 1.00 34.76 ? 329 ILE A N 1 ATOM 2196 C CA . ILE A 1 276 ? 5.773 26.067 18.072 1.00 33.75 ? 329 ILE A CA 1 ATOM 2197 C C . ILE A 1 276 ? 5.093 27.326 17.552 1.00 36.82 ? 329 ILE A C 1 ATOM 2198 O O . ILE A 1 276 ? 4.292 27.946 18.258 1.00 36.13 ? 329 ILE A O 1 ATOM 2199 C CB . ILE A 1 276 ? 7.307 26.242 18.059 1.00 32.76 ? 329 ILE A CB 1 ATOM 2200 C CG1 . ILE A 1 276 ? 7.971 25.195 18.958 1.00 31.78 ? 329 ILE A CG1 1 ATOM 2201 C CG2 . ILE A 1 276 ? 7.702 27.647 18.496 1.00 29.28 ? 329 ILE A CG2 1 ATOM 2202 C CD1 . ILE A 1 276 ? 9.497 25.126 18.812 1.00 31.91 ? 329 ILE A CD1 1 ATOM 2203 N N . MET A 1 277 ? 5.374 27.680 16.302 1.00 35.61 ? 330 MET A N 1 ATOM 2204 C CA . MET A 1 277 ? 4.969 28.973 15.763 1.00 36.11 ? 330 MET A CA 1 ATOM 2205 C C . MET A 1 277 ? 3.454 29.086 15.573 1.00 39.46 ? 330 MET A C 1 ATOM 2206 O O . MET A 1 277 ? 2.906 30.183 15.586 1.00 38.99 ? 330 MET A O 1 ATOM 2207 C CB . MET A 1 277 ? 5.671 29.223 14.432 1.00 35.97 ? 330 MET A CB 1 ATOM 2208 C CG . MET A 1 277 ? 7.183 29.336 14.562 1.00 34.44 ? 330 MET A CG 1 ATOM 2209 S SD . MET A 1 277 ? 7.683 30.656 15.700 1.00 32.81 ? 330 MET A SD 1 ATOM 2210 C CE . MET A 1 277 ? 6.705 32.018 15.091 1.00 33.43 ? 330 MET A CE 1 ATOM 2211 N N . SER A 1 278 ? 2.776 27.958 15.398 1.00 41.89 ? 331 SER A N 1 ATOM 2212 C CA . SER A 1 278 ? 1.318 27.971 15.337 1.00 45.44 ? 331 SER A CA 1 ATOM 2213 C C . SER A 1 278 ? 0.762 28.719 16.538 1.00 46.49 ? 331 SER A C 1 ATOM 2214 O O . SER A 1 278 ? -0.397 29.138 16.545 1.00 48.21 ? 331 SER A O 1 ATOM 2215 C CB . SER A 1 278 ? 0.763 26.548 15.296 1.00 47.46 ? 331 SER A CB 1 ATOM 2216 O OG . SER A 1 278 ? 0.818 25.945 16.578 1.00 45.56 ? 331 SER A OG 1 ATOM 2217 N N . THR A 1 279 ? 1.603 28.885 17.554 1.00 47.76 ? 332 THR A N 1 ATOM 2218 C CA . THR A 1 279 ? 1.158 29.354 18.860 1.00 45.39 ? 332 THR A CA 1 ATOM 2219 C C . THR A 1 279 ? 0.883 30.848 18.806 1.00 43.92 ? 332 THR A C 1 ATOM 2220 O O . THR A 1 279 ? 0.175 31.390 19.653 1.00 45.60 ? 332 THR A O 1 ATOM 2221 C CB . THR A 1 279 ? 2.240 29.081 19.926 1.00 46.30 ? 332 THR A CB 1 ATOM 2222 O OG1 . THR A 1 279 ? 1.962 27.858 20.621 1.00 48.18 ? 332 THR A OG1 1 ATOM 2223 C CG2 . THR A 1 279 ? 2.201 30.138 21.022 1.00 46.70 ? 332 THR A CG2 1 ATOM 2224 N N . VAL A 1 280 ? 1.463 31.513 17.815 1.00 42.79 ? 333 VAL A N 1 ATOM 2225 C CA . VAL A 1 280 ? 1.128 32.900 17.537 1.00 44.55 ? 333 VAL A CA 1 ATOM 2226 C C . VAL A 1 280 ? 0.611 33.040 16.114 1.00 42.27 ? 333 VAL A C 1 ATOM 2227 O O . VAL A 1 280 ? 0.932 34.000 15.420 1.00 36.84 ? 333 VAL A O 1 ATOM 2228 C CB . VAL A 1 280 ? 2.342 33.814 17.737 1.00 46.48 ? 333 VAL A CB 1 ATOM 2229 C CG1 . VAL A 1 280 ? 2.004 35.244 17.340 1.00 48.80 ? 333 VAL A CG1 1 ATOM 2230 C CG2 . VAL A 1 280 ? 2.801 33.747 19.181 1.00 47.54 ? 333 VAL A CG2 1 ATOM 2231 N N . ASN A 1 281 ? -0.180 32.064 15.685 1.00 46.86 ? 334 ASN A N 1 ATOM 2232 C CA . ASN A 1 281 ? -0.810 32.119 14.373 1.00 49.97 ? 334 ASN A CA 1 ATOM 2233 C C . ASN A 1 281 ? 0.208 32.537 13.326 1.00 49.15 ? 334 ASN A C 1 ATOM 2234 O O . ASN A 1 281 ? -0.023 33.463 12.551 1.00 51.33 ? 334 ASN A O 1 ATOM 2235 C CB . ASN A 1 281 ? -1.977 33.112 14.387 1.00 52.93 ? 334 ASN A CB 1 ATOM 2236 C CG . ASN A 1 281 ? -2.980 32.855 13.274 1.00 55.28 ? 334 ASN A CG 1 ATOM 2237 O OD1 . ASN A 1 281 ? -3.052 33.607 12.298 1.00 55.94 ? 334 ASN A OD1 1 ATOM 2238 N ND2 . ASN A 1 281 ? -3.764 31.789 13.418 1.00 56.88 ? 334 ASN A ND2 1 ATOM 2239 N N . ILE A 1 282 ? 1.345 31.851 13.313 1.00 45.56 ? 335 ILE A N 1 ATOM 2240 C CA . ILE A 1 282 ? 2.355 32.097 12.300 1.00 45.90 ? 335 ILE A CA 1 ATOM 2241 C C . ILE A 1 282 ? 2.749 30.805 11.599 1.00 47.43 ? 335 ILE A C 1 ATOM 2242 O O . ILE A 1 282 ? 2.900 29.754 12.233 1.00 47.15 ? 335 ILE A O 1 ATOM 2243 C CB . ILE A 1 282 ? 3.589 32.770 12.918 1.00 45.74 ? 335 ILE A CB 1 ATOM 2244 C CG1 . ILE A 1 282 ? 3.226 34.167 13.432 1.00 44.43 ? 335 ILE A CG1 1 ATOM 2245 C CG2 . ILE A 1 282 ? 4.704 32.852 11.898 1.00 45.05 ? 335 ILE A CG2 1 ATOM 2246 C CD1 . ILE A 1 282 ? 4.416 34.995 13.874 1.00 44.01 ? 335 ILE A CD1 1 ATOM 2247 N N . SER A 1 283 ? 2.902 30.901 10.282 1.00 46.81 ? 336 SER A N 1 ATOM 2248 C CA . SER A 1 283 ? 2.986 29.737 9.414 1.00 45.79 ? 336 SER A CA 1 ATOM 2249 C C . SER A 1 283 ? 4.385 29.630 8.824 1.00 43.82 ? 336 SER A C 1 ATOM 2250 O O . SER A 1 283 ? 4.963 30.621 8.377 1.00 43.87 ? 336 SER A O 1 ATOM 2251 C CB . SER A 1 283 ? 1.955 29.844 8.284 1.00 47.85 ? 336 SER A CB 1 ATOM 2252 O OG . SER A 1 283 ? 2.051 31.095 7.617 1.00 47.39 ? 336 SER A OG 1 ATOM 2253 N N . ILE A 1 284 ? 4.921 28.414 8.827 1.00 43.16 ? 337 ILE A N 1 ATOM 2254 C CA . ILE A 1 284 ? 6.325 28.185 8.515 1.00 38.05 ? 337 ILE A CA 1 ATOM 2255 C C . ILE A 1 284 ? 6.475 27.316 7.279 1.00 34.98 ? 337 ILE A C 1 ATOM 2256 O O . ILE A 1 284 ? 6.044 26.171 7.272 1.00 31.20 ? 337 ILE A O 1 ATOM 2257 C CB . ILE A 1 284 ? 7.019 27.488 9.696 1.00 37.76 ? 337 ILE A CB 1 ATOM 2258 C CG1 . ILE A 1 284 ? 6.929 28.358 10.951 1.00 35.86 ? 337 ILE A CG1 1 ATOM 2259 C CG2 . ILE A 1 284 ? 8.468 27.213 9.352 1.00 38.21 ? 337 ILE A CG2 1 ATOM 2260 C CD1 . ILE A 1 284 ? 7.473 29.750 10.741 1.00 33.44 ? 337 ILE A CD1 1 ATOM 2261 N N . THR A 1 285 ? 7.115 27.847 6.245 1.00 39.09 ? 338 THR A N 1 ATOM 2262 C CA . THR A 1 285 ? 7.414 27.047 5.057 1.00 43.99 ? 338 THR A CA 1 ATOM 2263 C C . THR A 1 285 ? 8.699 26.251 5.254 1.00 44.76 ? 338 THR A C 1 ATOM 2264 O O . THR A 1 285 ? 9.761 26.821 5.519 1.00 40.77 ? 338 THR A O 1 ATOM 2265 C CB . THR A 1 285 ? 7.542 27.950 3.811 1.00 44.94 ? 338 THR A CB 1 ATOM 2266 O OG1 . THR A 1 285 ? 6.482 28.921 3.789 1.00 44.71 ? 338 THR A OG1 1 ATOM 2267 C CG2 . THR A 1 285 ? 7.325 27.146 2.536 1.00 47.19 ? 338 THR A CG2 1 ATOM 2268 N N . ASN A 1 286 ? 8.596 24.932 5.115 1.00 47.78 ? 339 ASN A N 1 ATOM 2269 C CA . ASN A 1 286 ? 9.775 24.085 4.965 1.00 49.82 ? 339 ASN A CA 1 ATOM 2270 C C . ASN A 1 286 ? 10.851 24.788 4.150 1.00 45.30 ? 339 ASN A C 1 ATOM 2271 O O . ASN A 1 286 ? 11.967 24.293 4.022 1.00 45.56 ? 339 ASN A O 1 ATOM 2272 C CB . ASN A 1 286 ? 9.407 22.752 4.309 1.00 53.11 ? 339 ASN A CB 1 ATOM 2273 C CG . ASN A 1 286 ? 9.624 21.568 5.236 1.00 57.50 ? 339 ASN A CG 1 ATOM 2274 O OD1 . ASN A 1 286 ? 8.768 20.683 5.354 1.00 58.08 ? 339 ASN A OD1 1 ATOM 2275 N ND2 . ASN A 1 286 ? 10.774 21.548 5.904 1.00 58.15 ? 339 ASN A ND2 1 ATOM 2276 N N . GLU A 1 287 ? 10.510 25.953 3.614 1.00 44.94 ? 340 GLU A N 1 ATOM 2277 C CA . GLU A 1 287 ? 11.485 26.813 2.951 1.00 45.73 ? 340 GLU A CA 1 ATOM 2278 C C . GLU A 1 287 ? 11.825 28.052 3.796 1.00 46.46 ? 340 GLU A C 1 ATOM 2279 O O . GLU A 1 287 ? 12.336 29.050 3.289 1.00 47.92 ? 340 GLU A O 1 ATOM 2280 C CB . GLU A 1 287 ? 10.951 27.219 1.576 1.00 50.04 ? 340 GLU A CB 1 ATOM 2281 C CG . GLU A 1 287 ? 10.242 26.085 0.847 1.00 51.70 ? 340 GLU A CG 1 ATOM 2282 C CD . GLU A 1 287 ? 8.784 26.389 0.562 1.00 54.55 ? 340 GLU A CD 1 ATOM 2283 O OE1 . GLU A 1 287 ? 8.490 27.526 0.122 1.00 57.67 ? 340 GLU A OE1 1 ATOM 2284 O OE2 . GLU A 1 287 ? 7.935 25.488 0.771 1.00 54.13 ? 340 GLU A OE2 1 ATOM 2285 N N . GLU A 1 288 ? 11.554 27.965 5.095 1.00 46.97 ? 341 GLU A N 1 ATOM 2286 C CA . GLU A 1 288 ? 11.929 29.010 6.050 1.00 43.02 ? 341 GLU A CA 1 ATOM 2287 C C . GLU A 1 288 ? 13.439 29.031 6.305 1.00 40.39 ? 341 GLU A C 1 ATOM 2288 O O . GLU A 1 288 ? 14.058 27.988 6.497 1.00 41.83 ? 341 GLU A O 1 ATOM 2289 C CB . GLU A 1 288 ? 11.185 28.779 7.368 1.00 42.17 ? 341 GLU A CB 1 ATOM 2290 C CG . GLU A 1 288 ? 11.507 29.783 8.458 1.00 43.00 ? 341 GLU A CG 1 ATOM 2291 C CD . GLU A 1 288 ? 10.672 31.047 8.369 1.00 41.55 ? 341 GLU A CD 1 ATOM 2292 O OE1 . GLU A 1 288 ? 10.802 31.900 9.266 1.00 37.21 ? 341 GLU A OE1 1 ATOM 2293 O OE2 . GLU A 1 288 ? 9.885 31.189 7.407 1.00 39.82 ? 341 GLU A OE2 1 ATOM 2294 N N . ASP A 1 289 ? 14.021 30.224 6.314 1.00 38.81 ? 342 ASP A N 1 ATOM 2295 C CA . ASP A 1 289 ? 15.428 30.399 6.659 1.00 40.23 ? 342 ASP A CA 1 ATOM 2296 C C . ASP A 1 289 ? 15.657 30.322 8.168 1.00 41.70 ? 342 ASP A C 1 ATOM 2297 O O . ASP A 1 289 ? 14.924 30.931 8.948 1.00 39.67 ? 342 ASP A O 1 ATOM 2298 C CB . ASP A 1 289 ? 15.926 31.745 6.153 1.00 40.66 ? 342 ASP A CB 1 ATOM 2299 C CG . ASP A 1 289 ? 16.425 31.682 4.730 1.00 40.34 ? 342 ASP A CG 1 ATOM 2300 O OD1 . ASP A 1 289 ? 16.613 30.558 4.212 1.00 38.74 ? 342 ASP A OD1 1 ATOM 2301 O OD2 . ASP A 1 289 ? 16.660 32.705 4.059 1.00 35.75 ? 342 ASP A OD2 1 ATOM 2302 N N . VAL A 1 290 ? 16.679 29.571 8.567 1.00 38.86 ? 343 VAL A N 1 ATOM 2303 C CA . VAL A 1 290 ? 16.941 29.304 9.976 1.00 34.91 ? 343 VAL A CA 1 ATOM 2304 C C . VAL A 1 290 ? 18.436 29.430 10.233 1.00 35.55 ? 343 VAL A C 1 ATOM 2305 O O . VAL A 1 290 ? 19.255 29.019 9.409 1.00 33.00 ? 343 VAL A O 1 ATOM 2306 C CB . VAL A 1 290 ? 16.468 27.902 10.374 1.00 33.97 ? 343 VAL A CB 1 ATOM 2307 C CG1 . VAL A 1 290 ? 16.848 27.592 11.819 1.00 35.21 ? 343 VAL A CG1 1 ATOM 2308 C CG2 . VAL A 1 290 ? 14.974 27.765 10.175 1.00 34.38 ? 343 VAL A CG2 1 ATOM 2309 N N . VAL A 1 291 ? 18.791 30.018 11.371 1.00 32.88 ? 344 VAL A N 1 ATOM 2310 C CA . VAL A 1 291 ? 20.184 30.097 11.788 1.00 31.45 ? 344 VAL A CA 1 ATOM 2311 C C . VAL A 1 291 ? 20.504 28.958 12.749 1.00 31.11 ? 344 VAL A C 1 ATOM 2312 O O . VAL A 1 291 ? 19.878 28.808 13.801 1.00 27.62 ? 344 VAL A O 1 ATOM 2313 C CB . VAL A 1 291 ? 20.484 31.444 12.455 1.00 31.31 ? 344 VAL A CB 1 ATOM 2314 C CG1 . VAL A 1 291 ? 21.871 31.440 13.080 1.00 33.31 ? 344 VAL A CG1 1 ATOM 2315 C CG2 . VAL A 1 291 ? 20.359 32.560 11.444 1.00 30.98 ? 344 VAL A CG2 1 ATOM 2316 N N . VAL A 1 292 ? 21.467 28.135 12.373 1.00 29.89 ? 345 VAL A N 1 ATOM 2317 C CA . VAL A 1 292 ? 21.748 26.932 13.135 1.00 30.50 ? 345 VAL A CA 1 ATOM 2318 C C . VAL A 1 292 ? 23.079 27.049 13.840 1.00 27.35 ? 345 VAL A C 1 ATOM 2319 O O . VAL A 1 292 ? 24.123 26.992 13.209 1.00 24.40 ? 345 VAL A O 1 ATOM 2320 C CB . VAL A 1 292 ? 21.785 25.696 12.243 1.00 31.52 ? 345 VAL A CB 1 ATOM 2321 C CG1 . VAL A 1 292 ? 22.144 24.475 13.072 1.00 30.78 ? 345 VAL A CG1 1 ATOM 2322 C CG2 . VAL A 1 292 ? 20.444 25.510 11.546 1.00 32.10 ? 345 VAL A CG2 1 ATOM 2323 N N . TYR A 1 293 ? 23.027 27.209 15.158 1.00 30.45 ? 346 TYR A N 1 ATOM 2324 C CA . TYR A 1 293 ? 24.180 27.616 15.945 1.00 27.75 ? 346 TYR A CA 1 ATOM 2325 C C . TYR A 1 293 ? 25.033 26.413 16.337 1.00 27.95 ? 346 TYR A C 1 ATOM 2326 O O . TYR A 1 293 ? 26.164 26.576 16.783 1.00 27.39 ? 346 TYR A O 1 ATOM 2327 C CB . TYR A 1 293 ? 23.707 28.320 17.220 1.00 28.18 ? 346 TYR A CB 1 ATOM 2328 C CG . TYR A 1 293 ? 23.588 29.826 17.116 1.00 24.72 ? 346 TYR A CG 1 ATOM 2329 C CD1 . TYR A 1 293 ? 24.198 30.523 16.083 1.00 25.24 ? 346 TYR A CD1 1 ATOM 2330 C CD2 . TYR A 1 293 ? 22.864 30.549 18.057 1.00 27.11 ? 346 TYR A CD2 1 ATOM 2331 C CE1 . TYR A 1 293 ? 24.104 31.910 15.993 1.00 23.63 ? 346 TYR A CE1 1 ATOM 2332 C CE2 . TYR A 1 293 ? 22.770 31.926 17.984 1.00 25.21 ? 346 TYR A CE2 1 ATOM 2333 C CZ . TYR A 1 293 ? 23.375 32.605 16.953 1.00 27.26 ? 346 TYR A CZ 1 ATOM 2334 O OH . TYR A 1 293 ? 23.243 33.975 16.895 1.00 23.62 ? 346 TYR A OH 1 ATOM 2335 N N . ALA A 1 294 ? 24.475 25.216 16.197 1.00 27.32 ? 347 ALA A N 1 ATOM 2336 C CA . ALA A 1 294 ? 25.069 24.005 16.766 1.00 26.73 ? 347 ALA A CA 1 ATOM 2337 C C . ALA A 1 294 ? 24.786 22.795 15.863 1.00 25.33 ? 347 ALA A C 1 ATOM 2338 O O . ALA A 1 294 ? 24.181 21.789 16.276 1.00 25.19 ? 347 ALA A O 1 ATOM 2339 C CB . ALA A 1 294 ? 24.541 23.761 18.166 1.00 25.28 ? 347 ALA A CB 1 ATOM 2340 N N . PRO A 1 295 ? 25.247 22.900 14.626 1.00 24.82 ? 348 PRO A N 1 ATOM 2341 C CA . PRO A 1 295 ? 25.174 21.788 13.670 1.00 26.14 ? 348 PRO A CA 1 ATOM 2342 C C . PRO A 1 295 ? 25.753 20.488 14.238 1.00 26.20 ? 348 PRO A C 1 ATOM 2343 O O . PRO A 1 295 ? 25.101 19.443 14.180 1.00 29.53 ? 348 PRO A O 1 ATOM 2344 C CB . PRO A 1 295 ? 26.001 22.282 12.474 1.00 27.36 ? 348 PRO A CB 1 ATOM 2345 C CG . PRO A 1 295 ? 26.683 23.549 12.920 1.00 27.71 ? 348 PRO A CG 1 ATOM 2346 C CD . PRO A 1 295 ? 25.896 24.095 14.071 1.00 24.87 ? 348 PRO A CD 1 ATOM 2347 N N . GLU A 1 296 ? 26.965 20.545 14.778 1.00 28.22 ? 349 GLU A N 1 ATOM 2348 C CA . GLU A 1 296 ? 27.628 19.336 15.249 1.00 29.92 ? 349 GLU A CA 1 ATOM 2349 C C . GLU A 1 296 ? 26.786 18.651 16.318 1.00 27.57 ? 349 GLU A C 1 ATOM 2350 O O . GLU A 1 296 ? 26.813 17.431 16.458 1.00 22.08 ? 349 GLU A O 1 ATOM 2351 C CB . GLU A 1 296 ? 29.019 19.656 15.795 1.00 36.51 ? 349 GLU A CB 1 ATOM 2352 C CG . GLU A 1 296 ? 29.824 20.584 14.901 1.00 42.73 ? 349 GLU A CG 1 ATOM 2353 C CD . GLU A 1 296 ? 31.314 20.296 14.940 1.00 49.06 ? 349 GLU A CD 1 ATOM 2354 O OE1 . GLU A 1 296 ? 32.069 21.033 14.268 1.00 54.16 ? 349 GLU A OE1 1 ATOM 2355 O OE2 . GLU A 1 296 ? 31.731 19.337 15.635 1.00 48.84 ? 349 GLU A OE2 1 ATOM 2356 N N . TYR A 1 297 ? 26.030 19.435 17.077 1.00 26.24 ? 350 TYR A N 1 ATOM 2357 C CA . TYR A 1 297 ? 25.375 18.906 18.260 1.00 23.66 ? 350 TYR A CA 1 ATOM 2358 C C . TYR A 1 297 ? 24.145 18.128 17.823 1.00 20.18 ? 350 TYR A C 1 ATOM 2359 O O . TYR A 1 297 ? 23.828 17.063 18.358 1.00 25.13 ? 350 TYR A O 1 ATOM 2360 C CB . TYR A 1 297 ? 24.948 20.031 19.195 1.00 25.51 ? 350 TYR A CB 1 ATOM 2361 C CG . TYR A 1 297 ? 23.837 19.614 20.125 1.00 25.00 ? 350 TYR A CG 1 ATOM 2362 C CD1 . TYR A 1 297 ? 22.513 19.931 19.849 1.00 26.32 ? 350 TYR A CD1 1 ATOM 2363 C CD2 . TYR A 1 297 ? 24.112 18.894 21.275 1.00 25.29 ? 350 TYR A CD2 1 ATOM 2364 C CE1 . TYR A 1 297 ? 21.496 19.546 20.696 1.00 21.60 ? 350 TYR A CE1 1 ATOM 2365 C CE2 . TYR A 1 297 ? 23.107 18.500 22.125 1.00 28.58 ? 350 TYR A CE2 1 ATOM 2366 C CZ . TYR A 1 297 ? 21.794 18.830 21.830 1.00 26.76 ? 350 TYR A CZ 1 ATOM 2367 O OH . TYR A 1 297 ? 20.803 18.428 22.691 1.00 23.21 ? 350 TYR A OH 1 ATOM 2368 N N . LEU A 1 298 ? 23.443 18.692 16.847 1.00 23.82 ? 351 LEU A N 1 ATOM 2369 C CA . LEU A 1 298 ? 22.326 18.020 16.196 1.00 25.88 ? 351 LEU A CA 1 ATOM 2370 C C . LEU A 1 298 ? 22.796 16.711 15.575 1.00 25.59 ? 351 LEU A C 1 ATOM 2371 O O . LEU A 1 298 ? 22.146 15.670 15.701 1.00 27.52 ? 351 LEU A O 1 ATOM 2372 C CB . LEU A 1 298 ? 21.742 18.918 15.104 1.00 27.15 ? 351 LEU A CB 1 ATOM 2373 C CG . LEU A 1 298 ? 21.087 20.222 15.555 1.00 28.84 ? 351 LEU A CG 1 ATOM 2374 C CD1 . LEU A 1 298 ? 20.611 21.005 14.350 1.00 31.03 ? 351 LEU A CD1 1 ATOM 2375 C CD2 . LEU A 1 298 ? 19.934 19.940 16.499 1.00 28.18 ? 351 LEU A CD2 1 ATOM 2376 N N . THR A 1 299 ? 23.934 16.770 14.902 1.00 30.72 ? 352 THR A N 1 ATOM 2377 C CA . THR A 1 299 ? 24.522 15.574 14.311 1.00 33.22 ? 352 THR A CA 1 ATOM 2378 C C . THR A 1 299 ? 24.754 14.526 15.388 1.00 33.45 ? 352 THR A C 1 ATOM 2379 O O . THR A 1 299 ? 24.375 13.370 15.233 1.00 31.76 ? 352 THR A O 1 ATOM 2380 C CB . THR A 1 299 ? 25.836 15.926 13.614 1.00 33.36 ? 352 THR A CB 1 ATOM 2381 O OG1 . THR A 1 299 ? 25.568 16.694 12.435 1.00 34.06 ? 352 THR A OG1 1 ATOM 2382 C CG2 . THR A 1 299 ? 26.533 14.676 13.092 1.00 35.09 ? 352 THR A CG2 1 ATOM 2383 N N . LYS A 1 300 ? 25.370 14.929 16.496 1.00 31.45 ? 353 LYS A N 1 ATOM 2384 C CA . LYS A 1 300 ? 25.694 13.972 17.553 1.00 29.33 ? 353 LYS A CA 1 ATOM 2385 C C . LYS A 1 300 ? 24.416 13.444 18.223 1.00 25.58 ? 353 LYS A C 1 ATOM 2386 O O . LYS A 1 300 ? 24.357 12.305 18.689 1.00 21.97 ? 353 LYS A O 1 ATOM 2387 C CB . LYS A 1 300 ? 26.642 14.609 18.575 1.00 30.89 ? 353 LYS A CB 1 ATOM 2388 C CG . LYS A 1 300 ? 28.025 14.930 17.994 1.00 32.69 ? 353 LYS A CG 1 ATOM 2389 C CD . LYS A 1 300 ? 28.972 15.522 19.028 1.00 35.67 ? 353 LYS A CD 1 ATOM 2390 C CE . LYS A 1 300 ? 29.543 16.854 18.566 1.00 38.16 ? 353 LYS A CE 1 ATOM 2391 N NZ . LYS A 1 300 ? 30.926 17.085 19.092 1.00 40.32 ? 353 LYS A NZ 1 ATOM 2392 N N . LEU A 1 301 ? 23.381 14.274 18.239 1.00 28.17 ? 354 LEU A N 1 ATOM 2393 C CA . LEU A 1 301 ? 22.112 13.934 18.887 1.00 27.69 ? 354 LEU A CA 1 ATOM 2394 C C . LEU A 1 301 ? 21.459 12.677 18.295 1.00 27.92 ? 354 LEU A C 1 ATOM 2395 O O . LEU A 1 301 ? 20.834 11.886 19.011 1.00 34.45 ? 354 LEU A O 1 ATOM 2396 C CB . LEU A 1 301 ? 21.153 15.110 18.737 1.00 29.30 ? 354 LEU A CB 1 ATOM 2397 C CG . LEU A 1 301 ? 20.165 15.351 19.871 1.00 29.79 ? 354 LEU A CG 1 ATOM 2398 C CD1 . LEU A 1 301 ? 20.894 15.441 21.183 1.00 28.98 ? 354 LEU A CD1 1 ATOM 2399 C CD2 . LEU A 1 301 ? 19.346 16.626 19.611 1.00 28.22 ? 354 LEU A CD2 1 ATOM 2400 N N . LYS A 1 302 ? 21.598 12.507 16.983 1.00 29.56 ? 355 LYS A N 1 ATOM 2401 C CA . LYS A 1 302 ? 20.876 11.468 16.250 1.00 30.01 ? 355 LYS A CA 1 ATOM 2402 C C . LYS A 1 302 ? 21.097 10.100 16.866 1.00 29.78 ? 355 LYS A C 1 ATOM 2403 O O . LYS A 1 302 ? 20.147 9.414 17.236 1.00 28.55 ? 355 LYS A O 1 ATOM 2404 C CB . LYS A 1 302 ? 21.307 11.465 14.774 1.00 29.76 ? 355 LYS A CB 1 ATOM 2405 C CG . LYS A 1 302 ? 20.502 10.514 13.884 1.00 33.20 ? 355 LYS A CG 1 ATOM 2406 C CD . LYS A 1 302 ? 21.288 10.116 12.647 1.00 35.06 ? 355 LYS A CD 1 ATOM 2407 C CE . LYS A 1 302 ? 20.500 9.168 11.759 1.00 35.84 ? 355 LYS A CE 1 ATOM 2408 N NZ . LYS A 1 302 ? 19.543 9.898 10.890 1.00 36.72 ? 355 LYS A NZ 1 ATOM 2409 N N . PRO A 1 303 ? 22.358 9.700 16.980 1.00 32.61 ? 356 PRO A N 1 ATOM 2410 C CA . PRO A 1 303 ? 22.733 8.461 17.674 1.00 33.32 ? 356 PRO A CA 1 ATOM 2411 C C . PRO A 1 303 ? 22.255 8.357 19.126 1.00 32.06 ? 356 PRO A C 1 ATOM 2412 O O . PRO A 1 303 ? 21.997 7.249 19.591 1.00 29.97 ? 356 PRO A O 1 ATOM 2413 C CB . PRO A 1 303 ? 24.273 8.484 17.628 1.00 34.67 ? 356 PRO A CB 1 ATOM 2414 C CG . PRO A 1 303 ? 24.639 9.890 17.278 1.00 34.92 ? 356 PRO A CG 1 ATOM 2415 C CD . PRO A 1 303 ? 23.527 10.400 16.426 1.00 34.42 ? 356 PRO A CD 1 ATOM 2416 N N . ILE A 1 304 ? 22.146 9.475 19.839 1.00 30.58 ? 357 ILE A N 1 ATOM 2417 C CA . ILE A 1 304 ? 21.829 9.406 21.261 1.00 28.77 ? 357 ILE A CA 1 ATOM 2418 C C . ILE A 1 304 ? 20.351 9.107 21.440 1.00 28.38 ? 357 ILE A C 1 ATOM 2419 O O . ILE A 1 304 ? 19.970 8.186 22.157 1.00 30.20 ? 357 ILE A O 1 ATOM 2420 C CB . ILE A 1 304 ? 22.195 10.717 21.976 1.00 29.59 ? 357 ILE A CB 1 ATOM 2421 C CG1 . ILE A 1 304 ? 23.708 10.934 21.930 1.00 31.42 ? 357 ILE A CG1 1 ATOM 2422 C CG2 . ILE A 1 304 ? 21.711 10.687 23.416 1.00 28.55 ? 357 ILE A CG2 1 ATOM 2423 C CD1 . ILE A 1 304 ? 24.142 12.308 22.396 1.00 30.44 ? 357 ILE A CD1 1 ATOM 2424 N N . LEU A 1 305 ? 19.524 9.900 20.778 1.00 32.91 ? 358 LEU A N 1 ATOM 2425 C CA . LEU A 1 305 ? 18.094 9.896 21.033 1.00 34.97 ? 358 LEU A CA 1 ATOM 2426 C C . LEU A 1 305 ? 17.491 8.550 20.653 1.00 36.84 ? 358 LEU A C 1 ATOM 2427 O O . LEU A 1 305 ? 16.504 8.123 21.235 1.00 35.62 ? 358 LEU A O 1 ATOM 2428 C CB . LEU A 1 305 ? 17.425 11.025 20.247 1.00 36.53 ? 358 LEU A CB 1 ATOM 2429 C CG . LEU A 1 305 ? 17.106 12.301 21.038 1.00 39.04 ? 358 LEU A CG 1 ATOM 2430 C CD1 . LEU A 1 305 ? 17.795 12.318 22.397 1.00 38.06 ? 358 LEU A CD1 1 ATOM 2431 C CD2 . LEU A 1 305 ? 17.481 13.534 20.238 1.00 37.54 ? 358 LEU A CD2 1 ATOM 2432 N N . THR A 1 306 ? 18.107 7.868 19.691 1.00 41.14 ? 359 THR A N 1 ATOM 2433 C CA . THR A 1 306 ? 17.535 6.646 19.143 1.00 42.64 ? 359 THR A CA 1 ATOM 2434 C C . THR A 1 306 ? 17.525 5.544 20.187 1.00 41.98 ? 359 THR A C 1 ATOM 2435 O O . THR A 1 306 ? 16.855 4.525 20.023 1.00 42.60 ? 359 THR A O 1 ATOM 2436 C CB . THR A 1 306 ? 18.318 6.188 17.898 1.00 43.36 ? 359 THR A CB 1 ATOM 2437 O OG1 . THR A 1 306 ? 19.617 5.717 18.277 1.00 44.93 ? 359 THR A OG1 1 ATOM 2438 C CG2 . THR A 1 306 ? 18.603 7.357 16.969 1.00 45.63 ? 359 THR A CG2 1 ATOM 2439 N N . LYS A 1 307 ? 18.271 5.748 21.265 1.00 40.53 ? 360 LYS A N 1 ATOM 2440 C CA . LYS A 1 307 ? 18.477 4.700 22.255 1.00 38.08 ? 360 LYS A CA 1 ATOM 2441 C C . LYS A 1 307 ? 17.484 4.787 23.413 1.00 38.76 ? 360 LYS A C 1 ATOM 2442 O O . LYS A 1 307 ? 17.452 3.900 24.268 1.00 39.18 ? 360 LYS A O 1 ATOM 2443 C CB . LYS A 1 307 ? 19.909 4.764 22.794 1.00 41.31 ? 360 LYS A CB 1 ATOM 2444 C CG . LYS A 1 307 ? 20.962 4.962 21.705 1.00 43.11 ? 360 LYS A CG 1 ATOM 2445 C CD . LYS A 1 307 ? 22.373 4.793 22.253 1.00 45.09 ? 360 LYS A CD 1 ATOM 2446 C CE . LYS A 1 307 ? 22.995 6.139 22.610 1.00 44.53 ? 360 LYS A CE 1 ATOM 2447 N NZ . LYS A 1 307 ? 24.007 6.017 23.694 1.00 46.12 ? 360 LYS A NZ 1 ATOM 2448 N N . TYR A 1 308 ? 16.682 5.852 23.446 1.00 34.82 ? 361 TYR A N 1 ATOM 2449 C CA . TYR A 1 308 ? 15.868 6.160 24.625 1.00 33.21 ? 361 TYR A CA 1 ATOM 2450 C C . TYR A 1 308 ? 14.369 6.108 24.310 1.00 28.78 ? 361 TYR A C 1 ATOM 2451 O O . TYR A 1 308 ? 13.949 6.430 23.210 1.00 31.84 ? 361 TYR A O 1 ATOM 2452 C CB . TYR A 1 308 ? 16.232 7.544 25.177 1.00 32.20 ? 361 TYR A CB 1 ATOM 2453 C CG . TYR A 1 308 ? 17.584 7.592 25.840 1.00 26.69 ? 361 TYR A CG 1 ATOM 2454 C CD1 . TYR A 1 308 ? 17.735 7.287 27.179 1.00 26.50 ? 361 TYR A CD1 1 ATOM 2455 C CD2 . TYR A 1 308 ? 18.716 7.935 25.117 1.00 27.73 ? 361 TYR A CD2 1 ATOM 2456 C CE1 . TYR A 1 308 ? 18.983 7.318 27.786 1.00 27.64 ? 361 TYR A CE1 1 ATOM 2457 C CE2 . TYR A 1 308 ? 19.970 7.974 25.718 1.00 23.03 ? 361 TYR A CE2 1 ATOM 2458 C CZ . TYR A 1 308 ? 20.097 7.663 27.041 1.00 22.86 ? 361 TYR A CZ 1 ATOM 2459 O OH . TYR A 1 308 ? 21.342 7.720 27.628 1.00 25.96 ? 361 TYR A OH 1 ATOM 2460 N N . SER A 1 309 ? 13.570 5.702 25.287 1.00 30.66 ? 362 SER A N 1 ATOM 2461 C CA . SER A 1 309 ? 12.117 5.716 25.136 1.00 32.43 ? 362 SER A CA 1 ATOM 2462 C C . SER A 1 309 ? 11.559 7.138 25.154 1.00 32.77 ? 362 SER A C 1 ATOM 2463 O O . SER A 1 309 ? 12.205 8.068 25.645 1.00 25.64 ? 362 SER A O 1 ATOM 2464 C CB . SER A 1 309 ? 11.463 4.899 26.246 1.00 31.57 ? 362 SER A CB 1 ATOM 2465 O OG . SER A 1 309 ? 11.835 5.385 27.520 1.00 32.46 ? 362 SER A OG 1 ATOM 2466 N N . ALA A 1 310 ? 10.351 7.302 24.624 1.00 31.03 ? 363 ALA A N 1 ATOM 2467 C CA . ALA A 1 310 ? 9.595 8.527 24.840 1.00 30.74 ? 363 ALA A CA 1 ATOM 2468 C C . ALA A 1 310 ? 9.501 8.807 26.335 1.00 31.52 ? 363 ALA A C 1 ATOM 2469 O O . ALA A 1 310 ? 9.619 9.955 26.782 1.00 30.41 ? 363 ALA A O 1 ATOM 2470 C CB . ALA A 1 310 ? 8.211 8.410 24.225 1.00 30.55 ? 363 ALA A CB 1 ATOM 2471 N N . ARG A 1 311 ? 9.300 7.748 27.104 1.00 29.71 ? 364 ARG A N 1 ATOM 2472 C CA . ARG A 1 311 ? 9.162 7.865 28.549 1.00 32.89 ? 364 ARG A CA 1 ATOM 2473 C C . ARG A 1 311 ? 10.454 8.385 29.181 1.00 34.68 ? 364 ARG A C 1 ATOM 2474 O O . ARG A 1 311 ? 10.417 9.203 30.105 1.00 26.28 ? 364 ARG A O 1 ATOM 2475 C CB . ARG A 1 311 ? 8.803 6.520 29.154 1.00 32.11 ? 364 ARG A CB 1 ATOM 2476 C CG . ARG A 1 311 ? 9.507 6.232 30.469 1.00 36.43 ? 364 ARG A CG 1 ATOM 2477 C CD . ARG A 1 311 ? 9.023 4.987 31.186 1.00 34.41 ? 364 ARG A CD 1 ATOM 2478 N NE . ARG A 1 311 ? 8.759 5.280 32.589 1.00 33.48 ? 364 ARG A NE 1 ATOM 2479 C CZ . ARG A 1 311 ? 7.549 5.340 33.118 1.00 31.24 ? 364 ARG A CZ 1 ATOM 2480 N NH1 . ARG A 1 311 ? 6.488 5.090 32.365 1.00 32.61 ? 364 ARG A NH1 1 ATOM 2481 N NH2 . ARG A 1 311 ? 7.398 5.636 34.402 1.00 30.67 ? 364 ARG A NH2 1 ATOM 2482 N N . ASP A 1 312 ? 11.586 7.908 28.671 1.00 32.68 ? 365 ASP A N 1 ATOM 2483 C CA . ASP A 1 312 ? 12.892 8.388 29.110 1.00 33.99 ? 365 ASP A CA 1 ATOM 2484 C C . ASP A 1 312 ? 13.023 9.882 28.828 1.00 30.69 ? 365 ASP A C 1 ATOM 2485 O O . ASP A 1 312 ? 13.468 10.659 29.681 1.00 30.10 ? 365 ASP A O 1 ATOM 2486 C CB . ASP A 1 312 ? 14.018 7.638 28.386 1.00 33.77 ? 365 ASP A CB 1 ATOM 2487 C CG . ASP A 1 312 ? 14.062 6.154 28.725 1.00 36.70 ? 365 ASP A CG 1 ATOM 2488 O OD1 . ASP A 1 312 ? 13.757 5.777 29.879 1.00 39.48 ? 365 ASP A OD1 1 ATOM 2489 O OD2 . ASP A 1 312 ? 14.405 5.288 27.893 1.00 36.50 ? 365 ASP A OD2 1 ATOM 2490 N N . LEU A 1 313 ? 12.666 10.273 27.613 1.00 28.28 ? 366 LEU A N 1 ATOM 2491 C CA . LEU A 1 313 ? 12.943 11.617 27.139 1.00 30.44 ? 366 LEU A CA 1 ATOM 2492 C C . LEU A 1 313 ? 12.082 12.603 27.920 1.00 29.73 ? 366 LEU A C 1 ATOM 2493 O O . LEU A 1 313 ? 12.535 13.691 28.294 1.00 26.34 ? 366 LEU A O 1 ATOM 2494 C CB . LEU A 1 313 ? 12.661 11.717 25.641 1.00 32.39 ? 366 LEU A CB 1 ATOM 2495 C CG . LEU A 1 313 ? 13.473 10.734 24.796 1.00 31.18 ? 366 LEU A CG 1 ATOM 2496 C CD1 . LEU A 1 313 ? 12.956 10.686 23.363 1.00 31.63 ? 366 LEU A CD1 1 ATOM 2497 C CD2 . LEU A 1 313 ? 14.935 11.118 24.810 1.00 30.65 ? 366 LEU A CD2 1 ATOM 2498 N N . GLN A 1 314 ? 10.846 12.200 28.199 1.00 29.15 ? 367 GLN A N 1 ATOM 2499 C CA . GLN A 1 314 ? 9.903 13.091 28.852 1.00 27.45 ? 367 GLN A CA 1 ATOM 2500 C C . GLN A 1 314 ? 10.178 13.173 30.346 1.00 26.69 ? 367 GLN A C 1 ATOM 2501 O O . GLN A 1 314 ? 9.883 14.182 30.979 1.00 23.94 ? 367 GLN A O 1 ATOM 2502 C CB . GLN A 1 314 ? 8.464 12.636 28.613 1.00 30.09 ? 367 GLN A CB 1 ATOM 2503 C CG . GLN A 1 314 ? 7.441 13.675 29.054 1.00 29.32 ? 367 GLN A CG 1 ATOM 2504 C CD . GLN A 1 314 ? 7.482 14.900 28.177 1.00 29.62 ? 367 GLN A CD 1 ATOM 2505 O OE1 . GLN A 1 314 ? 7.473 14.781 26.953 1.00 33.35 ? 367 GLN A OE1 1 ATOM 2506 N NE2 . GLN A 1 314 ? 7.544 16.082 28.790 1.00 28.08 ? 367 GLN A NE2 1 ATOM 2507 N N . ASN A 1 315 ? 10.743 12.114 30.915 1.00 22.61 ? 368 ASN A N 1 ATOM 2508 C CA . ASN A 1 315 ? 11.249 12.192 32.279 1.00 24.98 ? 368 ASN A CA 1 ATOM 2509 C C . ASN A 1 315 ? 12.291 13.318 32.444 1.00 20.58 ? 368 ASN A C 1 ATOM 2510 O O . ASN A 1 315 ? 12.248 14.039 33.428 1.00 22.15 ? 368 ASN A O 1 ATOM 2511 C CB . ASN A 1 315 ? 11.825 10.845 32.735 1.00 25.19 ? 368 ASN A CB 1 ATOM 2512 C CG . ASN A 1 315 ? 10.815 9.992 33.512 1.00 28.20 ? 368 ASN A CG 1 ATOM 2513 O OD1 . ASN A 1 315 ? 11.061 8.811 33.778 1.00 28.98 ? 368 ASN A OD1 1 ATOM 2514 N ND2 . ASN A 1 315 ? 9.681 10.582 33.869 1.00 22.14 ? 368 ASN A ND2 1 ATOM 2515 N N . LEU A 1 316 ? 13.215 13.459 31.488 1.00 25.59 ? 369 LEU A N 1 ATOM 2516 C CA . LEU A 1 316 ? 14.181 14.568 31.485 1.00 24.75 ? 369 LEU A CA 1 ATOM 2517 C C . LEU A 1 316 ? 13.502 15.892 31.173 1.00 25.95 ? 369 LEU A C 1 ATOM 2518 O O . LEU A 1 316 ? 13.756 16.907 31.821 1.00 21.84 ? 369 LEU A O 1 ATOM 2519 C CB . LEU A 1 316 ? 15.290 14.346 30.449 1.00 21.77 ? 369 LEU A CB 1 ATOM 2520 C CG . LEU A 1 316 ? 16.166 15.576 30.150 1.00 21.24 ? 369 LEU A CG 1 ATOM 2521 C CD1 . LEU A 1 316 ? 16.777 16.133 31.428 1.00 22.79 ? 369 LEU A CD1 1 ATOM 2522 C CD2 . LEU A 1 316 ? 17.273 15.265 29.130 1.00 19.14 ? 369 LEU A CD2 1 ATOM 2523 N N . MET A 1 317 ? 12.661 15.877 30.147 1.00 25.96 ? 370 MET A N 1 ATOM 2524 C CA . MET A 1 317 ? 12.085 17.097 29.607 1.00 27.46 ? 370 MET A CA 1 ATOM 2525 C C . MET A 1 317 ? 11.268 17.804 30.673 1.00 25.44 ? 370 MET A C 1 ATOM 2526 O O . MET A 1 317 ? 11.460 18.992 30.928 1.00 23.94 ? 370 MET A O 1 ATOM 2527 C CB . MET A 1 317 ? 11.199 16.775 28.414 1.00 28.53 ? 370 MET A CB 1 ATOM 2528 C CG . MET A 1 317 ? 11.950 16.709 27.088 1.00 33.46 ? 370 MET A CG 1 ATOM 2529 S SD . MET A 1 317 ? 10.958 15.854 25.852 1.00 40.87 ? 370 MET A SD 1 ATOM 2530 C CE . MET A 1 317 ? 12.179 14.775 25.106 1.00 43.58 ? 370 MET A CE 1 ATOM 2531 N N . SER A 1 318 ? 10.362 17.061 31.302 1.00 25.79 ? 371 SER A N 1 ATOM 2532 C CA . SER A 1 318 ? 9.504 17.621 32.335 1.00 22.96 ? 371 SER A CA 1 ATOM 2533 C C . SER A 1 318 ? 10.267 17.948 33.631 1.00 23.70 ? 371 SER A C 1 ATOM 2534 O O . SER A 1 318 ? 9.980 18.947 34.288 1.00 22.35 ? 371 SER A O 1 ATOM 2535 C CB . SER A 1 318 ? 8.348 16.675 32.615 1.00 26.77 ? 371 SER A CB 1 ATOM 2536 O OG . SER A 1 318 ? 7.408 16.741 31.555 1.00 29.14 ? 371 SER A OG 1 ATOM 2537 N N . TRP A 1 319 ? 11.249 17.129 33.996 1.00 20.26 ? 372 TRP A N 1 ATOM 2538 C CA . TRP A 1 319 ? 12.116 17.488 35.114 1.00 21.06 ? 372 TRP A CA 1 ATOM 2539 C C . TRP A 1 319 ? 12.763 18.854 34.904 1.00 16.76 ? 372 TRP A C 1 ATOM 2540 O O . TRP A 1 319 ? 12.964 19.603 35.852 1.00 20.01 ? 372 TRP A O 1 ATOM 2541 C CB . TRP A 1 319 ? 13.215 16.450 35.326 1.00 20.81 ? 372 TRP A CB 1 ATOM 2542 C CG . TRP A 1 319 ? 14.269 16.919 36.279 1.00 19.28 ? 372 TRP A CG 1 ATOM 2543 C CD1 . TRP A 1 319 ? 15.603 17.090 36.012 1.00 22.04 ? 372 TRP A CD1 1 ATOM 2544 C CD2 . TRP A 1 319 ? 14.086 17.285 37.649 1.00 17.96 ? 372 TRP A CD2 1 ATOM 2545 N NE1 . TRP A 1 319 ? 16.258 17.529 37.137 1.00 20.22 ? 372 TRP A NE1 1 ATOM 2546 C CE2 . TRP A 1 319 ? 15.353 17.649 38.160 1.00 20.70 ? 372 TRP A CE2 1 ATOM 2547 C CE3 . TRP A 1 319 ? 12.984 17.320 38.513 1.00 18.63 ? 372 TRP A CE3 1 ATOM 2548 C CZ2 . TRP A 1 319 ? 15.540 18.059 39.482 1.00 20.04 ? 372 TRP A CZ2 1 ATOM 2549 C CZ3 . TRP A 1 319 ? 13.171 17.735 39.828 1.00 20.08 ? 372 TRP A CZ3 1 ATOM 2550 C CH2 . TRP A 1 319 ? 14.443 18.094 40.297 1.00 20.56 ? 372 TRP A CH2 1 ATOM 2551 N N . ARG A 1 320 ? 13.124 19.164 33.671 1.00 20.81 ? 373 ARG A N 1 ATOM 2552 C CA . ARG A 1 320 ? 13.912 20.362 33.407 1.00 21.14 ? 373 ARG A CA 1 ATOM 2553 C C . ARG A 1 320 ? 13.049 21.616 33.596 1.00 22.29 ? 373 ARG A C 1 ATOM 2554 O O . ARG A 1 320 ? 13.563 22.706 33.822 1.00 28.48 ? 373 ARG A O 1 ATOM 2555 C CB . ARG A 1 320 ? 14.512 20.321 32.009 1.00 21.06 ? 373 ARG A CB 1 ATOM 2556 C CG . ARG A 1 320 ? 15.787 19.461 31.905 1.00 25.02 ? 373 ARG A CG 1 ATOM 2557 C CD . ARG A 1 320 ? 17.016 20.085 32.563 1.00 23.98 ? 373 ARG A CD 1 ATOM 2558 N NE . ARG A 1 320 ? 17.435 21.273 31.843 1.00 23.85 ? 373 ARG A NE 1 ATOM 2559 C CZ . ARG A 1 320 ? 17.349 22.493 32.325 1.00 22.13 ? 373 ARG A CZ 1 ATOM 2560 N NH1 . ARG A 1 320 ? 16.909 22.690 33.556 1.00 25.61 ? 373 ARG A NH1 1 ATOM 2561 N NH2 . ARG A 1 320 ? 17.741 23.513 31.588 1.00 21.38 ? 373 ARG A NH2 1 ATOM 2562 N N . PHE A 1 321 ? 11.738 21.442 33.509 1.00 21.04 ? 374 PHE A N 1 ATOM 2563 C CA . PHE A 1 321 ? 10.790 22.501 33.828 1.00 21.65 ? 374 PHE A CA 1 ATOM 2564 C C . PHE A 1 321 ? 10.463 22.462 35.309 1.00 17.11 ? 374 PHE A C 1 ATOM 2565 O O . PHE A 1 321 ? 10.519 23.475 35.982 1.00 19.20 ? 374 PHE A O 1 ATOM 2566 C CB . PHE A 1 321 ? 9.511 22.318 33.018 1.00 22.20 ? 374 PHE A CB 1 ATOM 2567 C CG . PHE A 1 321 ? 8.541 23.478 33.103 1.00 20.57 ? 374 PHE A CG 1 ATOM 2568 C CD1 . PHE A 1 321 ? 8.983 24.775 33.313 1.00 22.44 ? 374 PHE A CD1 1 ATOM 2569 C CD2 . PHE A 1 321 ? 7.183 23.257 32.943 1.00 19.41 ? 374 PHE A CD2 1 ATOM 2570 C CE1 . PHE A 1 321 ? 8.082 25.829 33.374 1.00 22.27 ? 374 PHE A CE1 1 ATOM 2571 C CE2 . PHE A 1 321 ? 6.283 24.292 33.000 1.00 16.62 ? 374 PHE A CE2 1 ATOM 2572 C CZ . PHE A 1 321 ? 6.719 25.578 33.213 1.00 20.96 ? 374 PHE A CZ 1 ATOM 2573 N N . ILE A 1 322 ? 10.093 21.289 35.809 1.00 19.42 ? 375 ILE A N 1 ATOM 2574 C CA . ILE A 1 322 ? 9.675 21.161 37.200 1.00 20.36 ? 375 ILE A CA 1 ATOM 2575 C C . ILE A 1 322 ? 10.776 21.685 38.104 1.00 22.29 ? 375 ILE A C 1 ATOM 2576 O O . ILE A 1 322 ? 10.517 22.395 39.079 1.00 22.36 ? 375 ILE A O 1 ATOM 2577 C CB . ILE A 1 322 ? 9.336 19.692 37.546 1.00 20.64 ? 375 ILE A CB 1 ATOM 2578 C CG1 . ILE A 1 322 ? 8.023 19.282 36.868 1.00 21.23 ? 375 ILE A CG1 1 ATOM 2579 C CG2 . ILE A 1 322 ? 9.227 19.515 39.046 1.00 21.39 ? 375 ILE A CG2 1 ATOM 2580 C CD1 . ILE A 1 322 ? 7.961 17.821 36.481 1.00 23.06 ? 375 ILE A CD1 1 ATOM 2581 N N . MET A 1 323 ? 12.008 21.349 37.749 1.00 20.38 ? 376 MET A N 1 ATOM 2582 C CA . MET A 1 323 ? 13.181 21.934 38.365 1.00 25.44 ? 376 MET A CA 1 ATOM 2583 C C . MET A 1 323 ? 12.934 23.380 38.795 1.00 24.87 ? 376 MET A C 1 ATOM 2584 O O . MET A 1 323 ? 13.181 23.733 39.947 1.00 25.27 ? 376 MET A O 1 ATOM 2585 C CB . MET A 1 323 ? 14.326 21.892 37.372 1.00 25.54 ? 376 MET A CB 1 ATOM 2586 C CG . MET A 1 323 ? 15.606 21.530 37.942 1.00 29.99 ? 376 MET A CG 1 ATOM 2587 S SD . MET A 1 323 ? 16.602 21.213 36.556 1.00 22.58 ? 376 MET A SD 1 ATOM 2588 C CE . MET A 1 323 ? 17.884 22.411 36.890 1.00 26.71 ? 376 MET A CE 1 ATOM 2589 N N . ASP A 1 324 ? 12.461 24.211 37.866 1.00 22.90 ? 377 ASP A N 1 ATOM 2590 C CA . ASP A 1 324 ? 12.369 25.671 38.086 1.00 26.33 ? 377 ASP A CA 1 ATOM 2591 C C . ASP A 1 324 ? 11.164 26.095 38.945 1.00 21.39 ? 377 ASP A C 1 ATOM 2592 O O . ASP A 1 324 ? 11.143 27.195 39.500 1.00 28.34 ? 377 ASP A O 1 ATOM 2593 C CB . ASP A 1 324 ? 12.306 26.419 36.747 1.00 23.98 ? 377 ASP A CB 1 ATOM 2594 C CG . ASP A 1 324 ? 13.524 26.179 35.877 1.00 28.20 ? 377 ASP A CG 1 ATOM 2595 O OD1 . ASP A 1 324 ? 13.463 26.519 34.675 1.00 25.97 ? 377 ASP A OD1 1 ATOM 2596 O OD2 . ASP A 1 324 ? 14.583 25.664 36.298 1.00 22.81 ? 377 ASP A OD2 1 ATOM 2597 N N . LEU A 1 325 ? 10.167 25.219 39.041 1.00 20.27 ? 378 LEU A N 1 ATOM 2598 C CA . LEU A 1 325 ? 8.857 25.581 39.573 1.00 19.37 ? 378 LEU A CA 1 ATOM 2599 C C . LEU A 1 325 ? 8.760 25.327 41.070 1.00 22.08 ? 378 LEU A C 1 ATOM 2600 O O . LEU A 1 325 ? 7.965 25.953 41.765 1.00 21.76 ? 378 LEU A O 1 ATOM 2601 C CB . LEU A 1 325 ? 7.772 24.776 38.870 1.00 19.83 ? 378 LEU A CB 1 ATOM 2602 C CG . LEU A 1 325 ? 7.663 25.061 37.379 1.00 23.69 ? 378 LEU A CG 1 ATOM 2603 C CD1 . LEU A 1 325 ? 6.642 24.150 36.736 1.00 22.10 ? 378 LEU A CD1 1 ATOM 2604 C CD2 . LEU A 1 325 ? 7.302 26.518 37.160 1.00 22.88 ? 378 LEU A CD2 1 ATOM 2605 N N . VAL A 1 326 ? 9.570 24.398 41.562 1.00 20.12 ? 379 VAL A N 1 ATOM 2606 C CA . VAL A 1 326 ? 9.441 23.897 42.916 1.00 21.13 ? 379 VAL A CA 1 ATOM 2607 C C . VAL A 1 326 ? 9.593 24.990 43.976 1.00 24.59 ? 379 VAL A C 1 ATOM 2608 O O . VAL A 1 326 ? 8.942 24.941 45.018 1.00 22.96 ? 379 VAL A O 1 ATOM 2609 C CB . VAL A 1 326 ? 10.486 22.801 43.171 1.00 26.38 ? 379 VAL A CB 1 ATOM 2610 C CG1 . VAL A 1 326 ? 10.709 22.629 44.644 1.00 34.04 ? 379 VAL A CG1 1 ATOM 2611 C CG2 . VAL A 1 326 ? 10.041 21.497 42.536 1.00 21.86 ? 379 VAL A CG2 1 ATOM 2612 N N . SER A 1 327 ? 10.452 25.976 43.730 1.00 18.95 ? 380 SER A N 1 ATOM 2613 C CA . SER A 1 327 ? 10.675 27.005 44.733 1.00 24.34 ? 380 SER A CA 1 ATOM 2614 C C . SER A 1 327 ? 9.494 27.977 44.780 1.00 22.32 ? 380 SER A C 1 ATOM 2615 O O . SER A 1 327 ? 9.442 28.865 45.617 1.00 24.19 ? 380 SER A O 1 ATOM 2616 C CB . SER A 1 327 ? 12.021 27.721 44.506 1.00 23.49 ? 380 SER A CB 1 ATOM 2617 O OG . SER A 1 327 ? 11.928 28.768 43.558 1.00 24.02 ? 380 SER A OG 1 ATOM 2618 N N . SER A 1 328 ? 8.516 27.775 43.909 1.00 23.43 ? 381 SER A N 1 ATOM 2619 C CA . SER A 1 328 ? 7.325 28.611 43.913 1.00 23.56 ? 381 SER A CA 1 ATOM 2620 C C . SER A 1 328 ? 6.125 27.871 44.511 1.00 25.77 ? 381 SER A C 1 ATOM 2621 O O . SER A 1 328 ? 5.000 28.363 44.458 1.00 25.87 ? 381 SER A O 1 ATOM 2622 C CB . SER A 1 328 ? 7.004 29.072 42.491 1.00 23.51 ? 381 SER A CB 1 ATOM 2623 O OG . SER A 1 328 ? 8.122 29.730 41.913 1.00 24.02 ? 381 SER A OG 1 ATOM 2624 N N . LEU A 1 329 ? 6.370 26.681 45.051 1.00 23.87 ? 382 LEU A N 1 ATOM 2625 C CA . LEU A 1 329 ? 5.335 25.894 45.716 1.00 23.44 ? 382 LEU A CA 1 ATOM 2626 C C . LEU A 1 329 ? 5.511 25.908 47.231 1.00 23.22 ? 382 LEU A C 1 ATOM 2627 O O . LEU A 1 329 ? 6.200 26.769 47.780 1.00 23.01 ? 382 LEU A O 1 ATOM 2628 C CB . LEU A 1 329 ? 5.359 24.447 45.204 1.00 25.18 ? 382 LEU A CB 1 ATOM 2629 C CG . LEU A 1 329 ? 5.061 24.302 43.707 1.00 26.81 ? 382 LEU A CG 1 ATOM 2630 C CD1 . LEU A 1 329 ? 5.245 22.871 43.207 1.00 23.53 ? 382 LEU A CD1 1 ATOM 2631 C CD2 . LEU A 1 329 ? 3.664 24.799 43.395 1.00 26.85 ? 382 LEU A CD2 1 ATOM 2632 N N . SER A 1 330 ? 4.892 24.950 47.919 1.00 23.55 ? 383 SER A N 1 ATOM 2633 C CA . SER A 1 330 ? 4.897 24.978 49.376 1.00 23.42 ? 383 SER A CA 1 ATOM 2634 C C . SER A 1 330 ? 6.261 24.550 49.935 1.00 26.87 ? 383 SER A C 1 ATOM 2635 O O . SER A 1 330 ? 7.162 24.135 49.192 1.00 20.58 ? 383 SER A O 1 ATOM 2636 C CB . SER A 1 330 ? 3.780 24.096 49.942 1.00 22.06 ? 383 SER A CB 1 ATOM 2637 O OG . SER A 1 330 ? 3.923 22.748 49.528 1.00 22.45 ? 383 SER A OG 1 ATOM 2638 N N . ARG A 1 331 ? 6.406 24.656 51.251 1.00 29.85 ? 384 ARG A N 1 ATOM 2639 C CA . ARG A 1 331 ? 7.716 24.562 51.883 1.00 32.53 ? 384 ARG A CA 1 ATOM 2640 C C . ARG A 1 331 ? 8.360 23.212 51.589 1.00 28.55 ? 384 ARG A C 1 ATOM 2641 O O . ARG A 1 331 ? 9.546 23.133 51.281 1.00 28.49 ? 384 ARG A O 1 ATOM 2642 C CB . ARG A 1 331 ? 7.602 24.780 53.395 1.00 36.64 ? 384 ARG A CB 1 ATOM 2643 C CG . ARG A 1 331 ? 8.918 24.615 54.152 1.00 39.40 ? 384 ARG A CG 1 ATOM 2644 C CD . ARG A 1 331 ? 10.010 25.643 53.786 1.00 43.30 ? 384 ARG A CD 1 ATOM 2645 N NE . ARG A 1 331 ? 9.562 27.029 53.911 1.00 46.47 ? 384 ARG A NE 1 ATOM 2646 C CZ . ARG A 1 331 ? 10.174 28.066 53.351 1.00 48.59 ? 384 ARG A CZ 1 ATOM 2647 N NH1 . ARG A 1 331 ? 11.266 27.884 52.620 1.00 49.40 ? 384 ARG A NH1 1 ATOM 2648 N NH2 . ARG A 1 331 ? 9.692 29.289 53.517 1.00 50.31 ? 384 ARG A NH2 1 ATOM 2649 N N . THR A 1 332 ? 7.570 22.148 51.661 1.00 27.06 ? 385 THR A N 1 ATOM 2650 C CA . THR A 1 332 ? 8.083 20.815 51.393 1.00 31.65 ? 385 THR A CA 1 ATOM 2651 C C . THR A 1 332 ? 8.734 20.749 50.016 1.00 27.30 ? 385 THR A C 1 ATOM 2652 O O . THR A 1 332 ? 9.777 20.127 49.842 1.00 28.01 ? 385 THR A O 1 ATOM 2653 C CB . THR A 1 332 ? 6.946 19.781 51.500 1.00 36.18 ? 385 THR A CB 1 ATOM 2654 O OG1 . THR A 1 332 ? 6.499 19.698 52.859 1.00 37.76 ? 385 THR A OG1 1 ATOM 2655 C CG2 . THR A 1 332 ? 7.457 18.396 51.212 1.00 39.99 ? 385 THR A CG2 1 ATOM 2656 N N . TYR A 1 333 ? 8.117 21.405 49.039 1.00 25.79 ? 386 TYR A N 1 ATOM 2657 C CA . TYR A 1 333 ? 8.677 21.458 47.702 1.00 23.09 ? 386 TYR A CA 1 ATOM 2658 C C . TYR A 1 333 ? 9.897 22.374 47.659 1.00 22.19 ? 386 TYR A C 1 ATOM 2659 O O . TYR A 1 333 ? 10.910 22.037 47.054 1.00 20.71 ? 386 TYR A O 1 ATOM 2660 C CB . TYR A 1 333 ? 7.619 21.927 46.707 1.00 23.01 ? 386 TYR A CB 1 ATOM 2661 C CG . TYR A 1 333 ? 6.661 20.827 46.320 1.00 20.74 ? 386 TYR A CG 1 ATOM 2662 C CD1 . TYR A 1 333 ? 7.021 19.867 45.396 1.00 22.81 ? 386 TYR A CD1 1 ATOM 2663 C CD2 . TYR A 1 333 ? 5.413 20.733 46.908 1.00 22.07 ? 386 TYR A CD2 1 ATOM 2664 C CE1 . TYR A 1 333 ? 6.157 18.848 45.049 1.00 23.77 ? 386 TYR A CE1 1 ATOM 2665 C CE2 . TYR A 1 333 ? 4.536 19.713 46.572 1.00 22.45 ? 386 TYR A CE2 1 ATOM 2666 C CZ . TYR A 1 333 ? 4.910 18.780 45.639 1.00 22.60 ? 386 TYR A CZ 1 ATOM 2667 O OH . TYR A 1 333 ? 4.045 17.769 45.296 1.00 25.46 ? 386 TYR A OH 1 ATOM 2668 N N . LYS A 1 334 ? 9.789 23.530 48.305 1.00 25.80 ? 387 LYS A N 1 ATOM 2669 C CA . LYS A 1 334 ? 10.916 24.451 48.444 1.00 27.25 ? 387 LYS A CA 1 ATOM 2670 C C . LYS A 1 334 ? 12.109 23.720 49.026 1.00 26.29 ? 387 LYS A C 1 ATOM 2671 O O . LYS A 1 334 ? 13.232 23.825 48.526 1.00 24.25 ? 387 LYS A O 1 ATOM 2672 C CB . LYS A 1 334 ? 10.539 25.598 49.376 1.00 30.08 ? 387 LYS A CB 1 ATOM 2673 C CG . LYS A 1 334 ? 9.737 26.717 48.729 1.00 32.46 ? 387 LYS A CG 1 ATOM 2674 C CD . LYS A 1 334 ? 9.437 27.814 49.753 1.00 35.91 ? 387 LYS A CD 1 ATOM 2675 C CE . LYS A 1 334 ? 9.183 29.153 49.087 1.00 36.76 ? 387 LYS A CE 1 ATOM 2676 N NZ . LYS A 1 334 ? 9.683 29.166 47.689 1.00 41.70 ? 387 LYS A NZ 1 ATOM 2677 N N . GLU A 1 335 ? 11.833 22.991 50.104 1.00 24.26 ? 388 GLU A N 1 ATOM 2678 C CA . GLU A 1 335 ? 12.814 22.230 50.865 1.00 26.48 ? 388 GLU A CA 1 ATOM 2679 C C . GLU A 1 335 ? 13.642 21.302 50.002 1.00 25.28 ? 388 GLU A C 1 ATOM 2680 O O . GLU A 1 335 ? 14.830 21.081 50.260 1.00 24.34 ? 388 GLU A O 1 ATOM 2681 C CB . GLU A 1 335 ? 12.062 21.349 51.860 1.00 33.30 ? 388 GLU A CB 1 ATOM 2682 C CG . GLU A 1 335 ? 12.416 21.525 53.319 1.00 38.00 ? 388 GLU A CG 1 ATOM 2683 C CD . GLU A 1 335 ? 11.560 20.639 54.220 1.00 43.18 ? 388 GLU A CD 1 ATOM 2684 O OE1 . GLU A 1 335 ? 11.173 19.517 53.800 1.00 43.45 ? 388 GLU A OE1 1 ATOM 2685 O OE2 . GLU A 1 335 ? 11.267 21.073 55.353 1.00 49.37 ? 388 GLU A OE2 1 ATOM 2686 N N . SER A 1 336 ? 12.996 20.696 49.013 1.00 21.27 ? 389 SER A N 1 ATOM 2687 C CA . SER A 1 336 ? 13.604 19.578 48.303 1.00 22.47 ? 389 SER A CA 1 ATOM 2688 C C . SER A 1 336 ? 14.824 20.045 47.528 1.00 21.40 ? 389 SER A C 1 ATOM 2689 O O . SER A 1 336 ? 15.634 19.230 47.088 1.00 21.28 ? 389 SER A O 1 ATOM 2690 C CB . SER A 1 336 ? 12.600 18.932 47.343 1.00 22.12 ? 389 SER A CB 1 ATOM 2691 O OG . SER A 1 336 ? 12.270 19.805 46.276 1.00 21.16 ? 389 SER A OG 1 ATOM 2692 N N . ARG A 1 337 ? 14.951 21.358 47.356 1.00 20.25 ? 390 ARG A N 1 ATOM 2693 C CA . ARG A 1 337 ? 16.027 21.930 46.546 1.00 20.35 ? 390 ARG A CA 1 ATOM 2694 C C . ARG A 1 337 ? 17.293 22.234 47.363 1.00 20.71 ? 390 ARG A C 1 ATOM 2695 O O . ARG A 1 337 ? 18.313 22.702 46.818 1.00 17.16 ? 390 ARG A O 1 ATOM 2696 C CB . ARG A 1 337 ? 15.533 23.205 45.862 1.00 21.47 ? 390 ARG A CB 1 ATOM 2697 C CG . ARG A 1 337 ? 16.457 23.727 44.807 1.00 21.97 ? 390 ARG A CG 1 ATOM 2698 C CD . ARG A 1 337 ? 15.853 24.827 43.960 1.00 22.79 ? 390 ARG A CD 1 ATOM 2699 N NE . ARG A 1 337 ? 16.781 25.247 42.921 1.00 23.61 ? 390 ARG A NE 1 ATOM 2700 C CZ . ARG A 1 337 ? 17.651 26.229 43.069 1.00 23.23 ? 390 ARG A CZ 1 ATOM 2701 N NH1 . ARG A 1 337 ? 17.703 26.895 44.217 1.00 22.02 ? 390 ARG A NH1 1 ATOM 2702 N NH2 . ARG A 1 337 ? 18.472 26.549 42.072 1.00 25.37 ? 390 ARG A NH2 1 ATOM 2703 N N . ASN A 1 338 ? 17.228 21.979 48.664 1.00 19.72 ? 391 ASN A N 1 ATOM 2704 C CA . ASN A 1 338 ? 18.247 22.468 49.601 1.00 21.08 ? 391 ASN A CA 1 ATOM 2705 C C . ASN A 1 338 ? 19.659 22.008 49.247 1.00 18.47 ? 391 ASN A C 1 ATOM 2706 O O . ASN A 1 338 ? 20.568 22.818 49.091 1.00 18.61 ? 391 ASN A O 1 ATOM 2707 C CB . ASN A 1 338 ? 17.922 22.004 51.024 1.00 29.91 ? 391 ASN A CB 1 ATOM 2708 C CG . ASN A 1 338 ? 17.085 23.005 51.796 1.00 36.15 ? 391 ASN A CG 1 ATOM 2709 O OD1 . ASN A 1 338 ? 17.459 24.168 51.937 1.00 45.75 ? 391 ASN A OD1 1 ATOM 2710 N ND2 . ASN A 1 338 ? 15.957 22.549 52.325 1.00 39.20 ? 391 ASN A ND2 1 ATOM 2711 N N . ALA A 1 339 ? 19.848 20.702 49.135 1.00 19.07 ? 392 ALA A N 1 ATOM 2712 C CA . ALA A 1 339 ? 21.182 20.146 48.911 1.00 22.65 ? 392 ALA A CA 1 ATOM 2713 C C . ALA A 1 339 ? 21.712 20.551 47.542 1.00 18.47 ? 392 ALA A C 1 ATOM 2714 O O . ALA A 1 339 ? 22.903 20.814 47.387 1.00 20.98 ? 392 ALA A O 1 ATOM 2715 C CB . ALA A 1 339 ? 21.160 18.627 49.048 1.00 21.33 ? 392 ALA A CB 1 ATOM 2716 N N . PHE A 1 340 ? 20.815 20.600 46.562 1.00 18.77 ? 393 PHE A N 1 ATOM 2717 C CA . PHE A 1 340 ? 21.160 20.991 45.197 1.00 19.77 ? 393 PHE A CA 1 ATOM 2718 C C . PHE A 1 340 ? 21.686 22.426 45.166 1.00 19.39 ? 393 PHE A C 1 ATOM 2719 O O . PHE A 1 340 ? 22.752 22.702 44.609 1.00 19.17 ? 393 PHE A O 1 ATOM 2720 C CB . PHE A 1 340 ? 19.935 20.871 44.301 1.00 20.78 ? 393 PHE A CB 1 ATOM 2721 C CG . PHE A 1 340 ? 20.188 21.193 42.846 1.00 20.33 ? 393 PHE A CG 1 ATOM 2722 C CD1 . PHE A 1 340 ? 19.587 22.286 42.258 1.00 21.77 ? 393 PHE A CD1 1 ATOM 2723 C CD2 . PHE A 1 340 ? 20.999 20.384 42.064 1.00 17.90 ? 393 PHE A CD2 1 ATOM 2724 C CE1 . PHE A 1 340 ? 19.796 22.575 40.919 1.00 23.29 ? 393 PHE A CE1 1 ATOM 2725 C CE2 . PHE A 1 340 ? 21.208 20.672 40.734 1.00 18.71 ? 393 PHE A CE2 1 ATOM 2726 C CZ . PHE A 1 340 ? 20.613 21.766 40.162 1.00 21.24 ? 393 PHE A CZ 1 ATOM 2727 N N . ARG A 1 341 ? 20.954 23.355 45.758 1.00 18.37 ? 394 ARG A N 1 ATOM 2728 C CA . ARG A 1 341 ? 21.433 24.729 45.712 1.00 18.07 ? 394 ARG A CA 1 ATOM 2729 C C . ARG A 1 341 ? 22.721 24.915 46.535 1.00 18.69 ? 394 ARG A C 1 ATOM 2730 O O . ARG A 1 341 ? 23.607 25.662 46.130 1.00 16.30 ? 394 ARG A O 1 ATOM 2731 C CB . ARG A 1 341 ? 20.331 25.725 46.079 1.00 23.08 ? 394 ARG A CB 1 ATOM 2732 C CG . ARG A 1 341 ? 20.021 25.843 47.499 1.00 29.95 ? 394 ARG A CG 1 ATOM 2733 C CD . ARG A 1 341 ? 19.953 27.290 47.995 1.00 30.67 ? 394 ARG A CD 1 ATOM 2734 N NE . ARG A 1 341 ? 20.238 27.278 49.414 1.00 31.27 ? 394 ARG A NE 1 ATOM 2735 C CZ . ARG A 1 341 ? 19.436 26.746 50.313 1.00 34.58 ? 394 ARG A CZ 1 ATOM 2736 N NH1 . ARG A 1 341 ? 18.275 26.241 49.936 1.00 32.46 ? 394 ARG A NH1 1 ATOM 2737 N NH2 . ARG A 1 341 ? 19.775 26.750 51.597 1.00 39.18 ? 394 ARG A NH2 1 ATOM 2738 N N . LYS A 1 342 ? 22.854 24.198 47.650 1.00 18.08 ? 395 LYS A N 1 ATOM 2739 C CA . LYS A 1 342 ? 24.112 24.187 48.387 1.00 18.88 ? 395 LYS A CA 1 ATOM 2740 C C . LYS A 1 342 ? 25.275 23.697 47.522 1.00 16.78 ? 395 LYS A C 1 ATOM 2741 O O . LYS A 1 342 ? 26.331 24.305 47.501 1.00 20.60 ? 395 LYS A O 1 ATOM 2742 C CB . LYS A 1 342 ? 23.995 23.343 49.661 1.00 22.10 ? 395 LYS A CB 1 ATOM 2743 C CG . LYS A 1 342 ? 25.253 23.381 50.524 1.00 23.75 ? 395 LYS A CG 1 ATOM 2744 C CD . LYS A 1 342 ? 25.007 22.845 51.928 1.00 31.69 ? 395 LYS A CD 1 ATOM 2745 C CE . LYS A 1 342 ? 26.310 22.708 52.715 1.00 35.22 ? 395 LYS A CE 1 ATOM 2746 N NZ . LYS A 1 342 ? 27.189 21.632 52.148 1.00 39.57 ? 395 LYS A NZ 1 ATOM 2747 N N . ALA A 1 343 ? 25.084 22.601 46.796 1.00 18.46 ? 396 ALA A N 1 ATOM 2748 C CA . ALA A 1 343 ? 26.148 22.061 45.950 1.00 16.77 ? 396 ALA A CA 1 ATOM 2749 C C . ALA A 1 343 ? 26.614 23.070 44.888 1.00 18.82 ? 396 ALA A C 1 ATOM 2750 O O . ALA A 1 343 ? 27.796 23.119 44.546 1.00 20.06 ? 396 ALA A O 1 ATOM 2751 C CB . ALA A 1 343 ? 25.689 20.757 45.284 1.00 15.69 ? 396 ALA A CB 1 ATOM 2752 N N . LEU A 1 344 ? 25.684 23.865 44.369 1.00 16.84 ? 397 LEU A N 1 ATOM 2753 C CA . LEU A 1 344 ? 25.963 24.739 43.226 1.00 18.96 ? 397 LEU A CA 1 ATOM 2754 C C . LEU A 1 344 ? 26.429 26.129 43.671 1.00 17.63 ? 397 LEU A C 1 ATOM 2755 O O . LEU A 1 344 ? 27.178 26.801 42.953 1.00 17.85 ? 397 LEU A O 1 ATOM 2756 C CB . LEU A 1 344 ? 24.728 24.896 42.345 1.00 17.10 ? 397 LEU A CB 1 ATOM 2757 C CG . LEU A 1 344 ? 24.084 23.674 41.699 1.00 22.40 ? 397 LEU A CG 1 ATOM 2758 C CD1 . LEU A 1 344 ? 23.390 24.099 40.425 1.00 22.54 ? 397 LEU A CD1 1 ATOM 2759 C CD2 . LEU A 1 344 ? 25.072 22.585 41.431 1.00 23.57 ? 397 LEU A CD2 1 ATOM 2760 N N . TYR A 1 345 ? 25.985 26.552 44.854 1.00 19.65 ? 398 TYR A N 1 ATOM 2761 C CA . TYR A 1 345 ? 26.067 27.947 45.260 1.00 19.03 ? 398 TYR A CA 1 ATOM 2762 C C . TYR A 1 345 ? 26.704 28.100 46.634 1.00 20.70 ? 398 TYR A C 1 ATOM 2763 O O . TYR A 1 345 ? 27.193 29.171 46.983 1.00 20.96 ? 398 TYR A O 1 ATOM 2764 C CB . TYR A 1 345 ? 24.669 28.561 45.256 1.00 19.14 ? 398 TYR A CB 1 ATOM 2765 C CG . TYR A 1 345 ? 24.074 28.614 43.869 1.00 20.17 ? 398 TYR A CG 1 ATOM 2766 C CD1 . TYR A 1 345 ? 24.625 29.437 42.889 1.00 22.33 ? 398 TYR A CD1 1 ATOM 2767 C CD2 . TYR A 1 345 ? 22.999 27.815 43.523 1.00 22.10 ? 398 TYR A CD2 1 ATOM 2768 C CE1 . TYR A 1 345 ? 24.093 29.480 41.603 1.00 21.97 ? 398 TYR A CE1 1 ATOM 2769 C CE2 . TYR A 1 345 ? 22.457 27.850 42.240 1.00 24.93 ? 398 TYR A CE2 1 ATOM 2770 C CZ . TYR A 1 345 ? 23.008 28.682 41.290 1.00 22.74 ? 398 TYR A CZ 1 ATOM 2771 O OH . TYR A 1 345 ? 22.479 28.710 40.025 1.00 24.12 ? 398 TYR A OH 1 ATOM 2772 N N . GLY A 1 346 ? 26.704 27.020 47.406 1.00 17.96 ? 399 GLY A N 1 ATOM 2773 C CA . GLY A 1 346 ? 27.324 27.014 48.711 1.00 16.77 ? 399 GLY A CA 1 ATOM 2774 C C . GLY A 1 346 ? 26.423 27.591 49.794 1.00 17.75 ? 399 GLY A C 1 ATOM 2775 O O . GLY A 1 346 ? 26.774 27.553 50.982 1.00 16.03 ? 399 GLY A O 1 ATOM 2776 N N . THR A 1 347 ? 25.263 28.108 49.387 1.00 14.70 ? 400 THR A N 1 ATOM 2777 C CA . THR A 1 347 ? 24.338 28.769 50.307 1.00 15.64 ? 400 THR A CA 1 ATOM 2778 C C . THR A 1 347 ? 23.583 27.753 51.178 1.00 18.03 ? 400 THR A C 1 ATOM 2779 O O . THR A 1 347 ? 23.220 26.685 50.706 1.00 22.35 ? 400 THR A O 1 ATOM 2780 C CB . THR A 1 347 ? 23.322 29.622 49.510 1.00 16.35 ? 400 THR A CB 1 ATOM 2781 O OG1 . THR A 1 347 ? 22.819 28.877 48.380 1.00 13.84 ? 400 THR A OG1 1 ATOM 2782 C CG2 . THR A 1 347 ? 24.004 30.829 48.892 1.00 15.31 ? 400 THR A CG2 1 ATOM 2783 N N . THR A 1 348 ? 23.321 28.117 52.433 1.00 18.36 ? 401 THR A N 1 ATOM 2784 C CA . THR A 1 348 ? 22.647 27.231 53.380 1.00 20.70 ? 401 THR A CA 1 ATOM 2785 C C . THR A 1 348 ? 21.214 27.677 53.674 1.00 21.87 ? 401 THR A C 1 ATOM 2786 O O . THR A 1 348 ? 20.475 26.982 54.379 1.00 20.46 ? 401 THR A O 1 ATOM 2787 C CB . THR A 1 348 ? 23.424 27.184 54.706 1.00 21.33 ? 401 THR A CB 1 ATOM 2788 O OG1 . THR A 1 348 ? 23.538 28.505 55.253 1.00 19.61 ? 401 THR A OG1 1 ATOM 2789 C CG2 . THR A 1 348 ? 24.869 26.758 54.486 1.00 20.19 ? 401 THR A CG2 1 ATOM 2790 N N . SER A 1 349 ? 20.835 28.833 53.142 1.00 20.46 ? 402 SER A N 1 ATOM 2791 C CA . SER A 1 349 ? 19.491 29.379 53.324 1.00 25.79 ? 402 SER A CA 1 ATOM 2792 C C . SER A 1 349 ? 19.096 30.113 52.047 1.00 22.52 ? 402 SER A C 1 ATOM 2793 O O . SER A 1 349 ? 19.961 30.583 51.322 1.00 15.50 ? 402 SER A O 1 ATOM 2794 C CB . SER A 1 349 ? 19.459 30.349 54.518 1.00 26.54 ? 402 SER A CB 1 ATOM 2795 O OG . SER A 1 349 ? 18.389 31.269 54.393 1.00 34.40 ? 402 SER A OG 1 ATOM 2796 N N . GLU A 1 350 ? 17.802 30.239 51.775 1.00 24.59 ? 403 GLU A N 1 ATOM 2797 C CA . GLU A 1 350 ? 17.379 31.107 50.681 1.00 28.11 ? 403 GLU A CA 1 ATOM 2798 C C . GLU A 1 350 ? 17.394 32.548 51.154 1.00 24.16 ? 403 GLU A C 1 ATOM 2799 O O . GLU A 1 350 ? 17.265 32.808 52.350 1.00 16.27 ? 403 GLU A O 1 ATOM 2800 C CB . GLU A 1 350 ? 16.003 30.708 50.127 1.00 36.16 ? 403 GLU A CB 1 ATOM 2801 C CG . GLU A 1 350 ? 15.998 30.586 48.604 1.00 43.42 ? 403 GLU A CG 1 ATOM 2802 C CD . GLU A 1 350 ? 14.733 29.961 48.032 1.00 50.11 ? 403 GLU A CD 1 ATOM 2803 O OE1 . GLU A 1 350 ? 13.887 29.463 48.811 1.00 54.03 ? 403 GLU A OE1 1 ATOM 2804 O OE2 . GLU A 1 350 ? 14.586 29.969 46.786 1.00 52.39 ? 403 GLU A OE2 1 ATOM 2805 N N . THR A 1 351 ? 17.579 33.467 50.209 1.00 17.46 ? 404 THR A N 1 ATOM 2806 C CA . THR A 1 351 ? 17.397 34.891 50.436 1.00 24.58 ? 404 THR A CA 1 ATOM 2807 C C . THR A 1 351 ? 16.004 35.191 50.979 1.00 18.04 ? 404 THR A C 1 ATOM 2808 O O . THR A 1 351 ? 15.068 34.452 50.719 1.00 17.71 ? 404 THR A O 1 ATOM 2809 C CB . THR A 1 351 ? 17.632 35.665 49.113 1.00 28.29 ? 404 THR A CB 1 ATOM 2810 O OG1 . THR A 1 351 ? 17.930 37.035 49.386 1.00 31.35 ? 404 THR A OG1 1 ATOM 2811 C CG2 . THR A 1 351 ? 16.372 35.742 48.293 1.00 32.05 ? 404 THR A CG2 1 ATOM 2812 N N . ALA A 1 352 ? 15.892 36.269 51.741 1.00 16.29 ? 405 ALA A N 1 ATOM 2813 C CA . ALA A 1 352 ? 14.607 36.722 52.262 1.00 17.70 ? 405 ALA A CA 1 ATOM 2814 C C . ALA A 1 352 ? 13.568 36.736 51.152 1.00 17.94 ? 405 ALA A C 1 ATOM 2815 O O . ALA A 1 352 ? 13.842 37.144 50.012 1.00 15.79 ? 405 ALA A O 1 ATOM 2816 C CB . ALA A 1 352 ? 14.733 38.096 52.853 1.00 15.93 ? 405 ALA A CB 1 ATOM 2817 N N . THR A 1 353 ? 12.366 36.316 51.503 1.00 19.08 ? 406 THR A N 1 ATOM 2818 C CA . THR A 1 353 ? 11.286 36.243 50.548 1.00 17.82 ? 406 THR A CA 1 ATOM 2819 C C . THR A 1 353 ? 11.033 37.583 49.857 1.00 16.00 ? 406 THR A C 1 ATOM 2820 O O . THR A 1 353 ? 10.894 37.630 48.633 1.00 13.61 ? 406 THR A O 1 ATOM 2821 C CB . THR A 1 353 ? 10.031 35.722 51.227 1.00 20.62 ? 406 THR A CB 1 ATOM 2822 O OG1 . THR A 1 353 ? 10.259 34.378 51.680 1.00 19.05 ? 406 THR A OG1 1 ATOM 2823 C CG2 . THR A 1 353 ? 8.904 35.592 50.216 1.00 20.84 ? 406 THR A CG2 1 ATOM 2824 N N . TRP A 1 354 ? 10.974 38.670 50.618 1.00 17.22 ? 407 TRP A N 1 ATOM 2825 C CA . TRP A 1 354 ? 10.698 39.972 50.014 1.00 16.88 ? 407 TRP A CA 1 ATOM 2826 C C . TRP A 1 354 ? 11.757 40.338 48.971 1.00 15.42 ? 407 TRP A C 1 ATOM 2827 O O . TRP A 1 354 ? 11.454 41.015 47.994 1.00 14.67 ? 407 TRP A O 1 ATOM 2828 C CB . TRP A 1 354 ? 10.549 41.082 51.066 1.00 17.13 ? 407 TRP A CB 1 ATOM 2829 C CG . TRP A 1 354 ? 11.792 41.425 51.878 1.00 19.04 ? 407 TRP A CG 1 ATOM 2830 C CD1 . TRP A 1 354 ? 12.101 40.978 53.136 1.00 18.55 ? 407 TRP A CD1 1 ATOM 2831 C CD2 . TRP A 1 354 ? 12.839 42.336 51.515 1.00 16.05 ? 407 TRP A CD2 1 ATOM 2832 N NE1 . TRP A 1 354 ? 13.288 41.530 53.560 1.00 18.16 ? 407 TRP A NE1 1 ATOM 2833 C CE2 . TRP A 1 354 ? 13.761 42.368 52.586 1.00 17.48 ? 407 TRP A CE2 1 ATOM 2834 C CE3 . TRP A 1 354 ? 13.102 43.117 50.387 1.00 15.46 ? 407 TRP A CE3 1 ATOM 2835 C CZ2 . TRP A 1 354 ? 14.912 43.147 52.560 1.00 16.42 ? 407 TRP A CZ2 1 ATOM 2836 C CZ3 . TRP A 1 354 ? 14.249 43.891 50.365 1.00 17.91 ? 407 TRP A CZ3 1 ATOM 2837 C CH2 . TRP A 1 354 ? 15.139 43.901 51.446 1.00 17.60 ? 407 TRP A CH2 1 ATOM 2838 N N . ARG A 1 355 ? 12.990 39.891 49.178 1.00 15.16 ? 408 ARG A N 1 ATOM 2839 C CA . ARG A 1 355 ? 14.074 40.201 48.243 1.00 14.02 ? 408 ARG A CA 1 ATOM 2840 C C . ARG A 1 355 ? 13.896 39.403 46.951 1.00 15.56 ? 408 ARG A C 1 ATOM 2841 O O . ARG A 1 355 ? 14.017 39.957 45.866 1.00 14.59 ? 408 ARG A O 1 ATOM 2842 C CB . ARG A 1 355 ? 15.444 39.868 48.829 1.00 13.21 ? 408 ARG A CB 1 ATOM 2843 C CG . ARG A 1 355 ? 15.977 40.875 49.834 1.00 16.51 ? 408 ARG A CG 1 ATOM 2844 C CD . ARG A 1 355 ? 17.246 40.403 50.561 1.00 16.92 ? 408 ARG A CD 1 ATOM 2845 N NE . ARG A 1 355 ? 17.637 41.306 51.631 1.00 17.71 ? 408 ARG A NE 1 ATOM 2846 C CZ . ARG A 1 355 ? 18.264 42.459 51.451 1.00 16.84 ? 408 ARG A CZ 1 ATOM 2847 N NH1 . ARG A 1 355 ? 18.570 42.864 50.230 1.00 17.87 ? 408 ARG A NH1 1 ATOM 2848 N NH2 . ARG A 1 355 ? 18.583 43.215 52.495 1.00 18.12 ? 408 ARG A NH2 1 ATOM 2849 N N . ARG A 1 356 ? 13.621 38.105 47.077 1.00 14.21 ? 409 ARG A N 1 ATOM 2850 C CA . ARG A 1 356 ? 13.397 37.252 45.911 1.00 15.08 ? 409 ARG A CA 1 ATOM 2851 C C . ARG A 1 356 ? 12.234 37.812 45.124 1.00 17.58 ? 409 ARG A C 1 ATOM 2852 O O . ARG A 1 356 ? 12.245 37.827 43.889 1.00 13.52 ? 409 ARG A O 1 ATOM 2853 C CB . ARG A 1 356 ? 13.097 35.803 46.331 1.00 20.00 ? 409 ARG A CB 1 ATOM 2854 C CG . ARG A 1 356 ? 14.234 35.115 47.095 1.00 23.07 ? 409 ARG A CG 1 ATOM 2855 C CD . ARG A 1 356 ? 14.052 33.598 47.346 1.00 27.01 ? 409 ARG A CD 1 ATOM 2856 N NE . ARG A 1 356 ? 12.653 33.181 47.497 1.00 26.11 ? 409 ARG A NE 1 ATOM 2857 C CZ . ARG A 1 356 ? 12.075 32.882 48.654 1.00 32.10 ? 409 ARG A CZ 1 ATOM 2858 N NH1 . ARG A 1 356 ? 12.762 32.945 49.787 1.00 28.82 ? 409 ARG A NH1 1 ATOM 2859 N NH2 . ARG A 1 356 ? 10.796 32.516 48.685 1.00 33.03 ? 409 ARG A NH2 1 ATOM 2860 N N . CYS A 1 357 ? 11.233 38.292 45.853 1.00 15.51 ? 410 CYS A N 1 ATOM 2861 C CA . CYS A 1 357 ? 10.002 38.744 45.240 1.00 17.75 ? 410 CYS A CA 1 ATOM 2862 C C . CYS A 1 357 ? 10.219 40.091 44.563 1.00 17.25 ? 410 CYS A C 1 ATOM 2863 O O . CYS A 1 357 ? 9.742 40.314 43.450 1.00 15.20 ? 410 CYS A O 1 ATOM 2864 C CB . CYS A 1 357 ? 8.897 38.816 46.294 1.00 16.45 ? 410 CYS A CB 1 ATOM 2865 S SG . CYS A 1 357 ? 8.248 37.196 46.765 1.00 17.31 ? 410 CYS A SG 1 ATOM 2866 N N . ALA A 1 358 ? 10.969 40.978 45.213 1.00 12.22 ? 411 ALA A N 1 ATOM 2867 C CA . ALA A 1 358 ? 11.290 42.264 44.608 1.00 12.56 ? 411 ALA A CA 1 ATOM 2868 C C . ALA A 1 358 ? 11.999 42.062 43.292 1.00 14.08 ? 411 ALA A C 1 ATOM 2869 O O . ALA A 1 358 ? 11.654 42.691 42.284 1.00 17.64 ? 411 ALA A O 1 ATOM 2870 C CB . ALA A 1 358 ? 12.133 43.090 45.522 1.00 15.71 ? 411 ALA A CB 1 ATOM 2871 N N . ASN A 1 359 ? 12.984 41.173 43.307 1.00 12.16 ? 412 ASN A N 1 ATOM 2872 C CA . ASN A 1 359 ? 13.722 40.811 42.110 1.00 17.16 ? 412 ASN A CA 1 ATOM 2873 C C . ASN A 1 359 ? 12.855 40.194 41.027 1.00 15.87 ? 412 ASN A C 1 ATOM 2874 O O . ASN A 1 359 ? 13.013 40.507 39.847 1.00 14.91 ? 412 ASN A O 1 ATOM 2875 C CB . ASN A 1 359 ? 14.855 39.859 42.481 1.00 19.05 ? 412 ASN A CB 1 ATOM 2876 C CG . ASN A 1 359 ? 15.968 40.559 43.190 1.00 21.66 ? 412 ASN A CG 1 ATOM 2877 O OD1 . ASN A 1 359 ? 16.241 41.730 42.908 1.00 24.95 ? 412 ASN A OD1 1 ATOM 2878 N ND2 . ASN A 1 359 ? 16.631 39.863 44.117 1.00 24.03 ? 412 ASN A ND2 1 ATOM 2879 N N . TYR A 1 360 ? 11.945 39.308 41.418 1.00 17.20 ? 413 TYR A N 1 ATOM 2880 C CA . TYR A 1 360 ? 11.056 38.682 40.448 1.00 17.92 ? 413 TYR A CA 1 ATOM 2881 C C . TYR A 1 360 ? 10.179 39.719 39.723 1.00 15.56 ? 413 TYR A C 1 ATOM 2882 O O . TYR A 1 360 ? 10.070 39.690 38.500 1.00 19.90 ? 413 TYR A O 1 ATOM 2883 C CB . TYR A 1 360 ? 10.159 37.617 41.099 1.00 19.56 ? 413 TYR A CB 1 ATOM 2884 C CG . TYR A 1 360 ? 9.250 36.976 40.072 1.00 19.25 ? 413 TYR A CG 1 ATOM 2885 C CD1 . TYR A 1 360 ? 7.955 37.437 39.895 1.00 21.65 ? 413 TYR A CD1 1 ATOM 2886 C CD2 . TYR A 1 360 ? 9.701 35.954 39.242 1.00 20.19 ? 413 TYR A CD2 1 ATOM 2887 C CE1 . TYR A 1 360 ? 7.120 36.888 38.946 1.00 22.26 ? 413 TYR A CE1 1 ATOM 2888 C CE2 . TYR A 1 360 ? 8.868 35.396 38.282 1.00 21.85 ? 413 TYR A CE2 1 ATOM 2889 C CZ . TYR A 1 360 ? 7.576 35.861 38.145 1.00 20.10 ? 413 TYR A CZ 1 ATOM 2890 O OH . TYR A 1 360 ? 6.706 35.351 37.201 1.00 16.87 ? 413 TYR A OH 1 ATOM 2891 N N . VAL A 1 361 ? 9.550 40.618 40.476 1.00 16.95 ? 414 VAL A N 1 ATOM 2892 C CA . VAL A 1 361 ? 8.735 41.690 39.887 1.00 15.53 ? 414 VAL A CA 1 ATOM 2893 C C . VAL A 1 361 ? 9.554 42.649 39.005 1.00 14.30 ? 414 VAL A C 1 ATOM 2894 O O . VAL A 1 361 ? 9.161 42.963 37.886 1.00 16.46 ? 414 VAL A O 1 ATOM 2895 C CB . VAL A 1 361 ? 8.035 42.490 40.987 1.00 19.31 ? 414 VAL A CB 1 ATOM 2896 C CG1 . VAL A 1 361 ? 7.208 41.562 41.866 1.00 18.74 ? 414 VAL A CG1 1 ATOM 2897 C CG2 . VAL A 1 361 ? 9.065 43.216 41.825 1.00 26.68 ? 414 VAL A CG2 1 ATOM 2898 N N . ASN A 1 362 ? 10.705 43.083 39.509 1.00 16.00 ? 415 ASN A N 1 ATOM 2899 C CA . ASN A 1 362 ? 11.708 43.778 38.697 1.00 16.30 ? 415 ASN A CA 1 ATOM 2900 C C . ASN A 1 362 ? 12.050 43.072 37.368 1.00 17.27 ? 415 ASN A C 1 ATOM 2901 O O . ASN A 1 362 ? 12.087 43.710 36.312 1.00 19.87 ? 415 ASN A O 1 ATOM 2902 C CB . ASN A 1 362 ? 12.976 43.988 39.531 1.00 14.65 ? 415 ASN A CB 1 ATOM 2903 C CG . ASN A 1 362 ? 13.855 45.103 39.002 1.00 20.22 ? 415 ASN A CG 1 ATOM 2904 O OD1 . ASN A 1 362 ? 13.422 45.921 38.194 1.00 20.26 ? 415 ASN A OD1 1 ATOM 2905 N ND2 . ASN A 1 362 ? 15.094 45.154 39.473 1.00 18.98 ? 415 ASN A ND2 1 ATOM 2906 N N . GLY A 1 363 ? 12.290 41.769 37.429 1.00 15.67 ? 416 GLY A N 1 ATOM 2907 C CA . GLY A 1 363 ? 12.670 40.997 36.257 1.00 17.11 ? 416 GLY A CA 1 ATOM 2908 C C . GLY A 1 363 ? 11.577 40.884 35.198 1.00 18.08 ? 416 GLY A C 1 ATOM 2909 O O . GLY A 1 363 ? 11.876 40.751 34.005 1.00 16.38 ? 416 GLY A O 1 ATOM 2910 N N . ASN A 1 364 ? 10.324 40.939 35.638 1.00 16.37 ? 417 ASN A N 1 ATOM 2911 C CA . ASN A 1 364 ? 9.168 40.735 34.775 1.00 19.43 ? 417 ASN A CA 1 ATOM 2912 C C . ASN A 1 364 ? 8.433 42.030 34.389 1.00 19.48 ? 417 ASN A C 1 ATOM 2913 O O . ASN A 1 364 ? 7.723 42.074 33.380 1.00 18.94 ? 417 ASN A O 1 ATOM 2914 C CB . ASN A 1 364 ? 8.216 39.747 35.442 1.00 17.24 ? 417 ASN A CB 1 ATOM 2915 C CG . ASN A 1 364 ? 8.693 38.304 35.304 1.00 19.98 ? 417 ASN A CG 1 ATOM 2916 O OD1 . ASN A 1 364 ? 8.499 37.689 34.267 1.00 20.45 ? 417 ASN A OD1 1 ATOM 2917 N ND2 . ASN A 1 364 ? 9.368 37.778 36.339 1.00 16.27 ? 417 ASN A ND2 1 ATOM 2918 N N . MET A 1 365 ? 8.613 43.081 35.182 1.00 17.28 ? 418 MET A N 1 ATOM 2919 C CA . MET A 1 365 ? 8.055 44.384 34.869 1.00 18.87 ? 418 MET A CA 1 ATOM 2920 C C . MET A 1 365 ? 9.124 45.468 35.005 1.00 17.04 ? 418 MET A C 1 ATOM 2921 O O . MET A 1 365 ? 8.997 46.374 35.813 1.00 16.92 ? 418 MET A O 1 ATOM 2922 C CB . MET A 1 365 ? 6.857 44.689 35.783 1.00 18.90 ? 418 MET A CB 1 ATOM 2923 C CG . MET A 1 365 ? 5.843 43.555 35.911 1.00 20.53 ? 418 MET A CG 1 ATOM 2924 S SD . MET A 1 365 ? 4.315 43.961 36.816 1.00 17.92 ? 418 MET A SD 1 ATOM 2925 C CE . MET A 1 365 ? 3.759 45.407 35.922 1.00 21.59 ? 418 MET A CE 1 ATOM 2926 N N . GLU A 1 366 ? 10.170 45.381 34.189 1.00 15.35 ? 419 GLU A N 1 ATOM 2927 C CA . GLU A 1 366 ? 11.360 46.174 34.403 1.00 19.02 ? 419 GLU A CA 1 ATOM 2928 C C . GLU A 1 366 ? 11.095 47.663 34.224 1.00 18.27 ? 419 GLU A C 1 ATOM 2929 O O . GLU A 1 366 ? 11.740 48.487 34.862 1.00 18.24 ? 419 GLU A O 1 ATOM 2930 C CB . GLU A 1 366 ? 12.481 45.723 33.463 1.00 23.47 ? 419 GLU A CB 1 ATOM 2931 C CG . GLU A 1 366 ? 12.090 45.742 32.003 1.00 30.73 ? 419 GLU A CG 1 ATOM 2932 C CD . GLU A 1 366 ? 13.006 44.894 31.142 1.00 36.19 ? 419 GLU A CD 1 ATOM 2933 O OE1 . GLU A 1 366 ? 12.917 43.641 31.232 1.00 36.09 ? 419 GLU A OE1 1 ATOM 2934 O OE2 . GLU A 1 366 ? 13.807 45.490 30.375 1.00 39.14 ? 419 GLU A OE2 1 ATOM 2935 N N . ASN A 1 367 ? 10.146 48.013 33.360 1.00 17.51 ? 420 ASN A N 1 ATOM 2936 C CA . ASN A 1 367 ? 9.817 49.406 33.150 1.00 19.51 ? 420 ASN A CA 1 ATOM 2937 C C . ASN A 1 367 ? 8.966 49.998 34.266 1.00 16.95 ? 420 ASN A C 1 ATOM 2938 O O . ASN A 1 367 ? 9.203 51.121 34.693 1.00 18.77 ? 420 ASN A O 1 ATOM 2939 C CB . ASN A 1 367 ? 9.145 49.604 31.782 1.00 20.81 ? 420 ASN A CB 1 ATOM 2940 C CG . ASN A 1 367 ? 10.126 49.462 30.634 1.00 22.26 ? 420 ASN A CG 1 ATOM 2941 O OD1 . ASN A 1 367 ? 11.314 49.716 30.798 1.00 23.76 ? 420 ASN A OD1 1 ATOM 2942 N ND2 . ASN A 1 367 ? 9.639 49.023 29.473 1.00 27.48 ? 420 ASN A ND2 1 ATOM 2943 N N . ALA A 1 368 ? 7.971 49.267 34.741 1.00 13.94 ? 421 ALA A N 1 ATOM 2944 C CA . ALA A 1 368 ? 7.174 49.771 35.854 1.00 16.87 ? 421 ALA A CA 1 ATOM 2945 C C . ALA A 1 368 ? 8.049 49.941 37.104 1.00 17.24 ? 421 ALA A C 1 ATOM 2946 O O . ALA A 1 368 ? 7.982 50.967 37.791 1.00 15.86 ? 421 ALA A O 1 ATOM 2947 C CB . ALA A 1 368 ? 6.007 48.841 36.141 1.00 15.65 ? 421 ALA A CB 1 ATOM 2948 N N . VAL A 1 369 ? 8.871 48.932 37.385 1.00 17.05 ? 422 VAL A N 1 ATOM 2949 C CA . VAL A 1 369 ? 9.750 48.967 38.547 1.00 17.46 ? 422 VAL A CA 1 ATOM 2950 C C . VAL A 1 369 ? 10.843 50.011 38.379 1.00 12.39 ? 422 VAL A C 1 ATOM 2951 O O . VAL A 1 369 ? 11.175 50.727 39.323 1.00 20.13 ? 422 VAL A O 1 ATOM 2952 C CB . VAL A 1 369 ? 10.424 47.617 38.802 1.00 20.85 ? 422 VAL A CB 1 ATOM 2953 C CG1 . VAL A 1 369 ? 11.664 47.813 39.652 1.00 23.85 ? 422 VAL A CG1 1 ATOM 2954 C CG2 . VAL A 1 369 ? 9.455 46.655 39.475 1.00 20.67 ? 422 VAL A CG2 1 ATOM 2955 N N . GLY A 1 370 ? 11.400 50.101 37.180 1.00 17.34 ? 423 GLY A N 1 ATOM 2956 C CA . GLY A 1 370 ? 12.390 51.117 36.886 1.00 16.02 ? 423 GLY A CA 1 ATOM 2957 C C . GLY A 1 370 ? 11.864 52.521 37.141 1.00 18.76 ? 423 GLY A C 1 ATOM 2958 O O . GLY A 1 370 ? 12.583 53.383 37.635 1.00 14.98 ? 423 GLY A O 1 ATOM 2959 N N . ARG A 1 371 ? 10.609 52.750 36.778 1.00 18.25 ? 424 ARG A N 1 ATOM 2960 C CA . ARG A 1 371 ? 9.971 54.038 36.989 1.00 16.09 ? 424 ARG A CA 1 ATOM 2961 C C . ARG A 1 371 ? 9.924 54.392 38.481 1.00 15.61 ? 424 ARG A C 1 ATOM 2962 O O . ARG A 1 371 ? 10.375 55.462 38.887 1.00 17.42 ? 424 ARG A O 1 ATOM 2963 C CB . ARG A 1 371 ? 8.569 53.993 36.397 1.00 19.71 ? 424 ARG A CB 1 ATOM 2964 C CG . ARG A 1 371 ? 7.647 55.114 36.790 1.00 20.07 ? 424 ARG A CG 1 ATOM 2965 C CD . ARG A 1 371 ? 6.262 54.951 36.159 1.00 23.00 ? 424 ARG A CD 1 ATOM 2966 N NE . ARG A 1 371 ? 5.303 55.958 36.584 1.00 25.60 ? 424 ARG A NE 1 ATOM 2967 C CZ . ARG A 1 371 ? 4.479 56.566 35.752 1.00 27.61 ? 424 ARG A CZ 1 ATOM 2968 N NH1 . ARG A 1 371 ? 4.524 56.271 34.464 1.00 19.74 ? 424 ARG A NH1 1 ATOM 2969 N NH2 . ARG A 1 371 ? 3.618 57.470 36.198 1.00 30.51 ? 424 ARG A NH2 1 ATOM 2970 N N . LEU A 1 372 ? 9.408 53.471 39.291 1.00 17.57 ? 425 LEU A N 1 ATOM 2971 C CA . LEU A 1 372 ? 9.308 53.674 40.735 1.00 16.48 ? 425 LEU A CA 1 ATOM 2972 C C . LEU A 1 372 ? 10.702 53.844 41.350 1.00 20.22 ? 425 LEU A C 1 ATOM 2973 O O . LEU A 1 372 ? 10.911 54.657 42.257 1.00 16.68 ? 425 LEU A O 1 ATOM 2974 C CB . LEU A 1 372 ? 8.612 52.475 41.373 1.00 19.58 ? 425 LEU A CB 1 ATOM 2975 C CG . LEU A 1 372 ? 7.147 52.231 41.007 1.00 19.16 ? 425 LEU A CG 1 ATOM 2976 C CD1 . LEU A 1 372 ? 6.705 50.833 41.423 1.00 20.36 ? 425 LEU A CD1 1 ATOM 2977 C CD2 . LEU A 1 372 ? 6.291 53.301 41.679 1.00 24.74 ? 425 LEU A CD2 1 ATOM 2978 N N . TYR A 1 373 ? 11.659 53.077 40.840 1.00 15.59 ? 426 TYR A N 1 ATOM 2979 C CA . TYR A 1 373 ? 13.031 53.148 41.332 1.00 15.25 ? 426 TYR A CA 1 ATOM 2980 C C . TYR A 1 373 ? 13.632 54.519 41.085 1.00 16.51 ? 426 TYR A C 1 ATOM 2981 O O . TYR A 1 373 ? 14.179 55.144 41.994 1.00 17.85 ? 426 TYR A O 1 ATOM 2982 C CB . TYR A 1 373 ? 13.907 52.048 40.705 1.00 14.98 ? 426 TYR A CB 1 ATOM 2983 C CG . TYR A 1 373 ? 15.350 52.132 41.129 1.00 12.80 ? 426 TYR A CG 1 ATOM 2984 C CD1 . TYR A 1 373 ? 15.727 51.837 42.427 1.00 15.37 ? 426 TYR A CD1 1 ATOM 2985 C CD2 . TYR A 1 373 ? 16.320 52.577 40.258 1.00 19.17 ? 426 TYR A CD2 1 ATOM 2986 C CE1 . TYR A 1 373 ? 17.051 51.953 42.834 1.00 17.01 ? 426 TYR A CE1 1 ATOM 2987 C CE2 . TYR A 1 373 ? 17.634 52.680 40.644 1.00 19.52 ? 426 TYR A CE2 1 ATOM 2988 C CZ . TYR A 1 373 ? 17.996 52.377 41.940 1.00 15.37 ? 426 TYR A CZ 1 ATOM 2989 O OH . TYR A 1 373 ? 19.312 52.519 42.319 1.00 17.58 ? 426 TYR A OH 1 ATOM 2990 N N . VAL A 1 374 ? 13.566 54.998 39.852 1.00 15.57 ? 427 VAL A N 1 ATOM 2991 C CA . VAL A 1 374 ? 14.271 56.227 39.534 1.00 16.45 ? 427 VAL A CA 1 ATOM 2992 C C . VAL A 1 374 ? 13.578 57.390 40.233 1.00 18.47 ? 427 VAL A C 1 ATOM 2993 O O . VAL A 1 374 ? 14.235 58.349 40.644 1.00 16.53 ? 427 VAL A O 1 ATOM 2994 C CB . VAL A 1 374 ? 14.386 56.467 38.014 1.00 20.56 ? 427 VAL A CB 1 ATOM 2995 C CG1 . VAL A 1 374 ? 15.139 55.319 37.344 1.00 22.71 ? 427 VAL A CG1 1 ATOM 2996 C CG2 . VAL A 1 374 ? 13.020 56.644 37.390 1.00 24.90 ? 427 VAL A CG2 1 ATOM 2997 N N . GLU A 1 375 ? 12.259 57.309 40.377 1.00 17.94 ? 428 GLU A N 1 ATOM 2998 C CA . GLU A 1 375 ? 11.542 58.336 41.137 1.00 22.55 ? 428 GLU A CA 1 ATOM 2999 C C . GLU A 1 375 ? 12.024 58.373 42.599 1.00 23.36 ? 428 GLU A C 1 ATOM 3000 O O . GLU A 1 375 ? 12.136 59.440 43.199 1.00 25.45 ? 428 GLU A O 1 ATOM 3001 C CB . GLU A 1 375 ? 10.026 58.120 41.054 1.00 24.58 ? 428 GLU A CB 1 ATOM 3002 C CG . GLU A 1 375 ? 9.462 58.306 39.655 1.00 26.98 ? 428 GLU A CG 1 ATOM 3003 C CD . GLU A 1 375 ? 7.950 58.208 39.603 1.00 31.72 ? 428 GLU A CD 1 ATOM 3004 O OE1 . GLU A 1 375 ? 7.352 57.537 40.470 1.00 39.23 ? 428 GLU A OE1 1 ATOM 3005 O OE2 . GLU A 1 375 ? 7.357 58.800 38.683 1.00 36.68 ? 428 GLU A OE2 1 ATOM 3006 N N . ALA A 1 376 ? 12.323 57.212 43.163 1.00 21.99 ? 429 ALA A N 1 ATOM 3007 C CA . ALA A 1 376 ? 12.755 57.138 44.555 1.00 21.99 ? 429 ALA A CA 1 ATOM 3008 C C . ALA A 1 376 ? 14.233 57.528 44.721 1.00 23.35 ? 429 ALA A C 1 ATOM 3009 O O . ALA A 1 376 ? 14.599 58.167 45.700 1.00 24.76 ? 429 ALA A O 1 ATOM 3010 C CB . ALA A 1 376 ? 12.513 55.750 45.094 1.00 23.71 ? 429 ALA A CB 1 ATOM 3011 N N . ALA A 1 377 ? 15.084 57.136 43.780 1.00 23.81 ? 430 ALA A N 1 ATOM 3012 C CA . ALA A 1 377 ? 16.506 56.969 44.088 1.00 25.02 ? 430 ALA A CA 1 ATOM 3013 C C . ALA A 1 377 ? 17.444 57.650 43.103 1.00 26.37 ? 430 ALA A C 1 ATOM 3014 O O . ALA A 1 377 ? 18.625 57.794 43.384 1.00 28.88 ? 430 ALA A O 1 ATOM 3015 C CB . ALA A 1 377 ? 16.857 55.474 44.206 1.00 26.18 ? 430 ALA A CB 1 ATOM 3016 N N . PHE A 1 378 ? 16.951 58.078 41.948 1.00 30.16 ? 431 PHE A N 1 ATOM 3017 C CA . PHE A 1 378 ? 17.866 58.538 40.902 1.00 29.77 ? 431 PHE A CA 1 ATOM 3018 C C . PHE A 1 378 ? 17.778 60.050 40.638 1.00 34.24 ? 431 PHE A C 1 ATOM 3019 O O . PHE A 1 378 ? 16.694 60.602 40.449 1.00 31.92 ? 431 PHE A O 1 ATOM 3020 C CB . PHE A 1 378 ? 17.647 57.742 39.609 1.00 30.18 ? 431 PHE A CB 1 ATOM 3021 C CG . PHE A 1 378 ? 18.634 58.068 38.524 1.00 29.37 ? 431 PHE A CG 1 ATOM 3022 C CD1 . PHE A 1 378 ? 18.202 58.546 37.299 1.00 27.22 ? 431 PHE A CD1 1 ATOM 3023 C CD2 . PHE A 1 378 ? 19.993 57.901 38.731 1.00 28.58 ? 431 PHE A CD2 1 ATOM 3024 C CE1 . PHE A 1 378 ? 19.104 58.846 36.304 1.00 27.98 ? 431 PHE A CE1 1 ATOM 3025 C CE2 . PHE A 1 378 ? 20.900 58.205 37.736 1.00 26.06 ? 431 PHE A CE2 1 ATOM 3026 C CZ . PHE A 1 378 ? 20.455 58.675 36.521 1.00 25.83 ? 431 PHE A CZ 1 ATOM 3027 N N . ALA A 1 379 ? 18.928 60.720 40.632 1.00 38.08 ? 432 ALA A N 1 ATOM 3028 C CA . ALA A 1 379 ? 18.962 62.166 40.841 1.00 42.09 ? 432 ALA A CA 1 ATOM 3029 C C . ALA A 1 379 ? 18.137 62.895 39.790 1.00 47.33 ? 432 ALA A C 1 ATOM 3030 O O . ALA A 1 379 ? 17.275 63.714 40.125 1.00 49.62 ? 432 ALA A O 1 ATOM 3031 C CB . ALA A 1 379 ? 20.381 62.673 40.834 1.00 42.89 ? 432 ALA A CB 1 ATOM 3032 N N . GLY A 1 380 ? 18.408 62.619 38.518 1.00 49.09 ? 433 GLY A N 1 ATOM 3033 C CA . GLY A 1 380 ? 17.884 63.458 37.453 1.00 48.78 ? 433 GLY A CA 1 ATOM 3034 C C . GLY A 1 380 ? 18.955 64.124 36.611 1.00 49.16 ? 433 GLY A C 1 ATOM 3035 O O . GLY A 1 380 ? 18.839 64.165 35.392 1.00 54.39 ? 433 GLY A O 1 ATOM 3036 N N . GLU A 1 381 ? 19.997 64.648 37.251 1.00 47.95 ? 434 GLU A N 1 ATOM 3037 C CA . GLU A 1 381 ? 21.069 65.330 36.530 1.00 46.42 ? 434 GLU A CA 1 ATOM 3038 C C . GLU A 1 381 ? 22.373 64.527 36.514 1.00 41.95 ? 434 GLU A C 1 ATOM 3039 O O . GLU A 1 381 ? 23.345 64.910 35.850 1.00 36.22 ? 434 GLU A O 1 ATOM 3040 C CB . GLU A 1 381 ? 21.326 66.701 37.149 1.00 47.80 ? 434 GLU A CB 1 ATOM 3041 C CG . GLU A 1 381 ? 20.259 67.740 36.835 1.00 49.01 ? 434 GLU A CG 1 ATOM 3042 C CD . GLU A 1 381 ? 20.796 68.885 35.995 1.00 49.42 ? 434 GLU A CD 1 ATOM 3043 O OE1 . GLU A 1 381 ? 21.857 69.442 36.355 1.00 50.37 ? 434 GLU A OE1 1 ATOM 3044 O OE2 . GLU A 1 381 ? 20.160 69.220 34.976 1.00 44.63 ? 434 GLU A OE2 1 ATOM 3045 N N . SER A 1 382 ? 22.384 63.417 37.244 1.00 34.82 ? 435 SER A N 1 ATOM 3046 C CA . SER A 1 382 ? 23.309 62.327 36.985 1.00 33.29 ? 435 SER A CA 1 ATOM 3047 C C . SER A 1 382 ? 23.369 62.028 35.501 1.00 31.16 ? 435 SER A C 1 ATOM 3048 O O . SER A 1 382 ? 24.434 61.751 34.952 1.00 32.31 ? 435 SER A O 1 ATOM 3049 C CB . SER A 1 382 ? 22.867 61.068 37.737 1.00 35.52 ? 435 SER A CB 1 ATOM 3050 O OG . SER A 1 382 ? 23.288 61.108 39.091 1.00 37.02 ? 435 SER A OG 1 ATOM 3051 N N . LYS A 1 383 ? 22.219 62.080 34.850 1.00 30.07 ? 436 LYS A N 1 ATOM 3052 C CA . LYS A 1 383 ? 22.132 61.679 33.457 1.00 32.65 ? 436 LYS A CA 1 ATOM 3053 C C . LYS A 1 383 ? 23.041 62.559 32.605 1.00 30.69 ? 436 LYS A C 1 ATOM 3054 O O . LYS A 1 383 ? 23.845 62.057 31.811 1.00 25.64 ? 436 LYS A O 1 ATOM 3055 C CB . LYS A 1 383 ? 20.686 61.781 32.972 1.00 34.88 ? 436 LYS A CB 1 ATOM 3056 C CG . LYS A 1 383 ? 20.465 61.312 31.556 1.00 36.33 ? 436 LYS A CG 1 ATOM 3057 C CD . LYS A 1 383 ? 18.997 60.993 31.304 1.00 38.94 ? 436 LYS A CD 1 ATOM 3058 C CE . LYS A 1 383 ? 18.754 60.602 29.853 1.00 41.03 ? 436 LYS A CE 1 ATOM 3059 N NZ . LYS A 1 383 ? 17.508 61.219 29.297 1.00 42.29 ? 436 LYS A NZ 1 ATOM 3060 N N . HIS A 1 384 ? 22.914 63.874 32.777 1.00 28.15 ? 437 HIS A N 1 ATOM 3061 C CA . HIS A 1 384 ? 23.666 64.827 31.962 1.00 27.89 ? 437 HIS A CA 1 ATOM 3062 C C . HIS A 1 384 ? 25.174 64.686 32.171 1.00 22.72 ? 437 HIS A C 1 ATOM 3063 O O . HIS A 1 384 ? 25.943 64.754 31.224 1.00 22.01 ? 437 HIS A O 1 ATOM 3064 C CB . HIS A 1 384 ? 23.209 66.260 32.251 1.00 32.23 ? 437 HIS A CB 1 ATOM 3065 C CG . HIS A 1 384 ? 21.742 66.467 32.039 1.00 37.41 ? 437 HIS A CG 1 ATOM 3066 N ND1 . HIS A 1 384 ? 20.807 66.227 33.024 1.00 41.05 ? 437 HIS A ND1 1 ATOM 3067 C CD2 . HIS A 1 384 ? 21.045 66.864 30.949 1.00 40.76 ? 437 HIS A CD2 1 ATOM 3068 C CE1 . HIS A 1 384 ? 19.599 66.475 32.551 1.00 41.88 ? 437 HIS A CE1 1 ATOM 3069 N NE2 . HIS A 1 384 ? 19.716 66.869 31.295 1.00 39.85 ? 437 HIS A NE2 1 ATOM 3070 N N . VAL A 1 385 ? 25.590 64.478 33.409 1.00 21.53 ? 438 VAL A N 1 ATOM 3071 C CA . VAL A 1 385 ? 27.007 64.323 33.711 1.00 24.06 ? 438 VAL A CA 1 ATOM 3072 C C . VAL A 1 385 ? 27.548 63.047 33.071 1.00 23.96 ? 438 VAL A C 1 ATOM 3073 O O . VAL A 1 385 ? 28.617 63.038 32.461 1.00 22.04 ? 438 VAL A O 1 ATOM 3074 C CB . VAL A 1 385 ? 27.245 64.289 35.223 1.00 24.49 ? 438 VAL A CB 1 ATOM 3075 C CG1 . VAL A 1 385 ? 28.700 63.999 35.531 1.00 24.06 ? 438 VAL A CG1 1 ATOM 3076 C CG2 . VAL A 1 385 ? 26.804 65.620 35.863 1.00 27.60 ? 438 VAL A CG2 1 ATOM 3077 N N . VAL A 1 386 ? 26.791 61.966 33.189 1.00 23.28 ? 439 VAL A N 1 ATOM 3078 C CA . VAL A 1 386 ? 27.224 60.703 32.632 1.00 23.74 ? 439 VAL A CA 1 ATOM 3079 C C . VAL A 1 386 ? 27.309 60.766 31.100 1.00 22.16 ? 439 VAL A C 1 ATOM 3080 O O . VAL A 1 386 ? 28.237 60.214 30.507 1.00 22.39 ? 439 VAL A O 1 ATOM 3081 C CB . VAL A 1 386 ? 26.313 59.557 33.113 1.00 22.19 ? 439 VAL A CB 1 ATOM 3082 C CG1 . VAL A 1 386 ? 26.625 58.269 32.368 1.00 20.78 ? 439 VAL A CG1 1 ATOM 3083 C CG2 . VAL A 1 386 ? 26.488 59.372 34.639 1.00 20.76 ? 439 VAL A CG2 1 ATOM 3084 N N . GLU A 1 387 ? 26.355 61.453 30.478 1.00 22.28 ? 440 GLU A N 1 ATOM 3085 C CA . GLU A 1 387 ? 26.339 61.667 29.031 1.00 25.13 ? 440 GLU A CA 1 ATOM 3086 C C . GLU A 1 387 ? 27.654 62.280 28.576 1.00 25.61 ? 440 GLU A C 1 ATOM 3087 O O . GLU A 1 387 ? 28.221 61.903 27.559 1.00 28.09 ? 440 GLU A O 1 ATOM 3088 C CB . GLU A 1 387 ? 25.208 62.627 28.644 1.00 26.18 ? 440 GLU A CB 1 ATOM 3089 C CG . GLU A 1 387 ? 23.855 61.986 28.415 1.00 31.74 ? 440 GLU A CG 1 ATOM 3090 C CD . GLU A 1 387 ? 22.719 63.002 28.400 1.00 38.00 ? 440 GLU A CD 1 ATOM 3091 O OE1 . GLU A 1 387 ? 21.537 62.584 28.407 1.00 40.67 ? 440 GLU A OE1 1 ATOM 3092 O OE2 . GLU A 1 387 ? 23.005 64.220 28.379 1.00 42.07 ? 440 GLU A OE2 1 ATOM 3093 N N . ASP A 1 388 ? 28.126 63.249 29.336 1.00 27.03 ? 441 ASP A N 1 ATOM 3094 C CA . ASP A 1 388 ? 29.361 63.930 29.014 1.00 26.32 ? 441 ASP A CA 1 ATOM 3095 C C . ASP A 1 388 ? 30.599 63.052 29.272 1.00 25.72 ? 441 ASP A C 1 ATOM 3096 O O . ASP A 1 388 ? 31.562 63.083 28.512 1.00 24.08 ? 441 ASP A O 1 ATOM 3097 C CB . ASP A 1 388 ? 29.424 65.218 29.824 1.00 27.81 ? 441 ASP A CB 1 ATOM 3098 C CG . ASP A 1 388 ? 30.636 66.019 29.525 1.00 30.37 ? 441 ASP A CG 1 ATOM 3099 O OD1 . ASP A 1 388 ? 30.671 66.642 28.440 1.00 32.82 ? 441 ASP A OD1 1 ATOM 3100 O OD2 . ASP A 1 388 ? 31.603 66.071 30.305 1.00 28.03 ? 441 ASP A OD2 1 ATOM 3101 N N . LEU A 1 389 ? 30.579 62.246 30.324 1.00 22.42 ? 442 LEU A N 1 ATOM 3102 C CA . LEU A 1 389 ? 31.697 61.328 30.555 1.00 23.34 ? 442 LEU A CA 1 ATOM 3103 C C . LEU A 1 389 ? 31.817 60.332 29.398 1.00 18.98 ? 442 LEU A C 1 ATOM 3104 O O . LEU A 1 389 ? 32.915 59.989 28.964 1.00 21.36 ? 442 LEU A O 1 ATOM 3105 C CB . LEU A 1 389 ? 31.525 60.569 31.871 1.00 25.27 ? 442 LEU A CB 1 ATOM 3106 C CG . LEU A 1 389 ? 31.641 61.359 33.174 1.00 29.12 ? 442 LEU A CG 1 ATOM 3107 C CD1 . LEU A 1 389 ? 31.484 60.407 34.350 1.00 28.95 ? 442 LEU A CD1 1 ATOM 3108 C CD2 . LEU A 1 389 ? 32.983 62.091 33.263 1.00 33.76 ? 442 LEU A CD2 1 ATOM 3109 N N . ILE A 1 390 ? 30.676 59.874 28.903 1.00 19.13 ? 443 ILE A N 1 ATOM 3110 C CA . ILE A 1 390 ? 30.647 58.892 27.828 1.00 21.66 ? 443 ILE A CA 1 ATOM 3111 C C . ILE A 1 390 ? 31.171 59.502 26.528 1.00 24.75 ? 443 ILE A C 1 ATOM 3112 O O . ILE A 1 390 ? 31.963 58.880 25.821 1.00 20.82 ? 443 ILE A O 1 ATOM 3113 C CB . ILE A 1 390 ? 29.217 58.369 27.622 1.00 20.34 ? 443 ILE A CB 1 ATOM 3114 C CG1 . ILE A 1 390 ? 28.802 57.456 28.772 1.00 17.25 ? 443 ILE A CG1 1 ATOM 3115 C CG2 . ILE A 1 390 ? 29.106 57.621 26.310 1.00 22.06 ? 443 ILE A CG2 1 ATOM 3116 C CD1 . ILE A 1 390 ? 27.315 57.293 28.871 1.00 19.23 ? 443 ILE A CD1 1 ATOM 3117 N N . ALA A 1 391 ? 30.733 60.724 26.225 1.00 26.49 ? 444 ALA A N 1 ATOM 3118 C CA . ALA A 1 391 ? 31.342 61.512 25.144 1.00 27.96 ? 444 ALA A CA 1 ATOM 3119 C C . ALA A 1 391 ? 32.860 61.539 25.241 1.00 28.44 ? 444 ALA A C 1 ATOM 3120 O O . ALA A 1 391 ? 33.563 61.381 24.237 1.00 28.25 ? 444 ALA A O 1 ATOM 3121 C CB . ALA A 1 391 ? 30.807 62.941 25.152 1.00 27.84 ? 444 ALA A CB 1 ATOM 3122 N N . GLN A 1 392 ? 33.370 61.764 26.445 1.00 27.57 ? 445 GLN A N 1 ATOM 3123 C CA . GLN A 1 392 ? 34.806 61.903 26.634 1.00 27.13 ? 445 GLN A CA 1 ATOM 3124 C C . GLN A 1 392 ? 35.503 60.578 26.310 1.00 28.26 ? 445 GLN A C 1 ATOM 3125 O O . GLN A 1 392 ? 36.509 60.543 25.604 1.00 24.48 ? 445 GLN A O 1 ATOM 3126 C CB . GLN A 1 392 ? 35.125 62.317 28.072 1.00 27.56 ? 445 GLN A CB 1 ATOM 3127 C CG . GLN A 1 392 ? 34.853 63.780 28.415 1.00 25.38 ? 445 GLN A CG 1 ATOM 3128 C CD . GLN A 1 392 ? 34.900 64.033 29.919 1.00 26.69 ? 445 GLN A CD 1 ATOM 3129 O OE1 . GLN A 1 392 ? 35.900 63.736 30.575 1.00 24.12 ? 445 GLN A OE1 1 ATOM 3130 N NE2 . GLN A 1 392 ? 33.814 64.573 30.466 1.00 24.26 ? 445 GLN A NE2 1 ATOM 3131 N N . ILE A 1 393 ? 34.978 59.486 26.849 1.00 25.35 ? 446 ILE A N 1 ATOM 3132 C CA . ILE A 1 393 ? 35.680 58.214 26.781 1.00 25.90 ? 446 ILE A CA 1 ATOM 3133 C C . ILE A 1 393 ? 35.630 57.677 25.353 1.00 24.38 ? 446 ILE A C 1 ATOM 3134 O O . ILE A 1 393 ? 36.589 57.079 24.871 1.00 27.56 ? 446 ILE A O 1 ATOM 3135 C CB . ILE A 1 393 ? 35.062 57.226 27.789 1.00 26.49 ? 446 ILE A CB 1 ATOM 3136 C CG1 . ILE A 1 393 ? 35.525 57.579 29.206 1.00 26.43 ? 446 ILE A CG1 1 ATOM 3137 C CG2 . ILE A 1 393 ? 35.431 55.798 27.464 1.00 26.14 ? 446 ILE A CG2 1 ATOM 3138 C CD1 . ILE A 1 393 ? 34.416 57.562 30.168 1.00 28.99 ? 446 ILE A CD1 1 ATOM 3139 N N . ARG A 1 394 ? 34.513 57.929 24.680 1.00 25.88 ? 447 ARG A N 1 ATOM 3140 C CA . ARG A 1 394 ? 34.366 57.649 23.256 1.00 28.59 ? 447 ARG A CA 1 ATOM 3141 C C . ARG A 1 394 ? 35.426 58.363 22.417 1.00 29.51 ? 447 ARG A C 1 ATOM 3142 O O . ARG A 1 394 ? 35.963 57.791 21.469 1.00 21.53 ? 447 ARG A O 1 ATOM 3143 C CB . ARG A 1 394 ? 32.976 58.066 22.790 1.00 30.37 ? 447 ARG A CB 1 ATOM 3144 C CG . ARG A 1 394 ? 32.631 57.630 21.380 1.00 30.52 ? 447 ARG A CG 1 ATOM 3145 C CD . ARG A 1 394 ? 31.613 58.537 20.695 1.00 29.29 ? 447 ARG A CD 1 ATOM 3146 N NE . ARG A 1 394 ? 30.340 58.535 21.403 1.00 29.71 ? 447 ARG A NE 1 ATOM 3147 C CZ . ARG A 1 394 ? 29.310 57.789 21.055 1.00 31.34 ? 447 ARG A CZ 1 ATOM 3148 N NH1 . ARG A 1 394 ? 29.399 56.986 19.999 1.00 31.05 ? 447 ARG A NH1 1 ATOM 3149 N NH2 . ARG A 1 394 ? 28.184 57.846 21.751 1.00 32.18 ? 447 ARG A NH2 1 ATOM 3150 N N . GLU A 1 395 ? 35.721 59.607 22.778 1.00 29.39 ? 448 GLU A N 1 ATOM 3151 C CA . GLU A 1 395 ? 36.725 60.398 22.081 1.00 33.15 ? 448 GLU A CA 1 ATOM 3152 C C . GLU A 1 395 ? 38.096 59.808 22.324 1.00 31.65 ? 448 GLU A C 1 ATOM 3153 O O . GLU A 1 395 ? 38.931 59.780 21.430 1.00 26.15 ? 448 GLU A O 1 ATOM 3154 C CB . GLU A 1 395 ? 36.711 61.840 22.592 1.00 38.21 ? 448 GLU A CB 1 ATOM 3155 C CG . GLU A 1 395 ? 36.592 62.929 21.530 1.00 42.85 ? 448 GLU A CG 1 ATOM 3156 C CD . GLU A 1 395 ? 37.005 62.492 20.134 1.00 45.08 ? 448 GLU A CD 1 ATOM 3157 O OE1 . GLU A 1 395 ? 36.143 61.972 19.394 1.00 48.88 ? 448 GLU A OE1 1 ATOM 3158 O OE2 . GLU A 1 395 ? 38.181 62.697 19.761 1.00 46.66 ? 448 GLU A OE2 1 ATOM 3159 N N . VAL A 1 396 ? 38.334 59.360 23.553 1.00 28.76 ? 449 VAL A N 1 ATOM 3160 C CA . VAL A 1 396 ? 39.636 58.850 23.934 1.00 25.77 ? 449 VAL A CA 1 ATOM 3161 C C . VAL A 1 396 ? 39.914 57.524 23.217 1.00 27.32 ? 449 VAL A C 1 ATOM 3162 O O . VAL A 1 396 ? 41.045 57.271 22.783 1.00 26.84 ? 449 VAL A O 1 ATOM 3163 C CB . VAL A 1 396 ? 39.732 58.654 25.456 1.00 24.60 ? 449 VAL A CB 1 ATOM 3164 C CG1 . VAL A 1 396 ? 40.954 57.837 25.821 1.00 25.30 ? 449 VAL A CG1 1 ATOM 3165 C CG2 . VAL A 1 396 ? 39.746 59.991 26.167 1.00 26.92 ? 449 VAL A CG2 1 ATOM 3166 N N . PHE A 1 397 ? 38.887 56.687 23.087 1.00 26.23 ? 450 PHE A N 1 ATOM 3167 C CA . PHE A 1 397 ? 38.994 55.484 22.268 1.00 28.89 ? 450 PHE A CA 1 ATOM 3168 C C . PHE A 1 397 ? 39.362 55.821 20.829 1.00 29.30 ? 450 PHE A C 1 ATOM 3169 O O . PHE A 1 397 ? 40.312 55.272 20.283 1.00 28.22 ? 450 PHE A O 1 ATOM 3170 C CB . PHE A 1 397 ? 37.685 54.706 22.251 1.00 28.44 ? 450 PHE A CB 1 ATOM 3171 C CG . PHE A 1 397 ? 37.741 53.445 21.421 1.00 27.56 ? 450 PHE A CG 1 ATOM 3172 C CD1 . PHE A 1 397 ? 37.449 53.472 20.072 1.00 27.02 ? 450 PHE A CD1 1 ATOM 3173 C CD2 . PHE A 1 397 ? 38.084 52.234 21.996 1.00 27.97 ? 450 PHE A CD2 1 ATOM 3174 C CE1 . PHE A 1 397 ? 37.490 52.311 19.310 1.00 26.58 ? 450 PHE A CE1 1 ATOM 3175 C CE2 . PHE A 1 397 ? 38.124 51.075 21.239 1.00 25.35 ? 450 PHE A CE2 1 ATOM 3176 C CZ . PHE A 1 397 ? 37.833 51.116 19.898 1.00 27.40 ? 450 PHE A CZ 1 ATOM 3177 N N . ILE A 1 398 ? 38.581 56.705 20.221 1.00 29.38 ? 451 ILE A N 1 ATOM 3178 C CA . ILE A 1 398 ? 38.859 57.194 18.875 1.00 33.00 ? 451 ILE A CA 1 ATOM 3179 C C . ILE A 1 398 ? 40.306 57.693 18.764 1.00 31.79 ? 451 ILE A C 1 ATOM 3180 O O . ILE A 1 398 ? 41.064 57.290 17.872 1.00 31.96 ? 451 ILE A O 1 ATOM 3181 C CB . ILE A 1 398 ? 37.888 58.335 18.516 1.00 33.97 ? 451 ILE A CB 1 ATOM 3182 C CG1 . ILE A 1 398 ? 36.553 57.767 18.001 1.00 35.17 ? 451 ILE A CG1 1 ATOM 3183 C CG2 . ILE A 1 398 ? 38.531 59.259 17.491 1.00 36.24 ? 451 ILE A CG2 1 ATOM 3184 C CD1 . ILE A 1 398 ? 35.357 58.722 18.109 1.00 34.81 ? 451 ILE A CD1 1 ATOM 3185 N N . GLN A 1 399 ? 40.696 58.569 19.676 1.00 28.48 ? 452 GLN A N 1 ATOM 3186 C CA . GLN A 1 399 ? 41.996 59.199 19.584 1.00 32.47 ? 452 GLN A CA 1 ATOM 3187 C C . GLN A 1 399 ? 43.090 58.143 19.695 1.00 34.91 ? 452 GLN A C 1 ATOM 3188 O O . GLN A 1 399 ? 44.157 58.275 19.094 1.00 35.54 ? 452 GLN A O 1 ATOM 3189 C CB . GLN A 1 399 ? 42.154 60.262 20.672 1.00 38.66 ? 452 GLN A CB 1 ATOM 3190 C CG . GLN A 1 399 ? 41.213 61.454 20.492 1.00 43.83 ? 452 GLN A CG 1 ATOM 3191 C CD . GLN A 1 399 ? 41.643 62.682 21.279 1.00 49.18 ? 452 GLN A CD 1 ATOM 3192 O OE1 . GLN A 1 399 ? 42.557 62.614 22.109 1.00 52.75 ? 452 GLN A OE1 1 ATOM 3193 N NE2 . GLN A 1 399 ? 40.977 63.810 21.029 1.00 52.13 ? 452 GLN A NE2 1 ATOM 3194 N N . THR A 1 400 ? 42.821 57.089 20.462 1.00 29.72 ? 453 THR A N 1 ATOM 3195 C CA . THR A 1 400 ? 43.837 56.094 20.762 1.00 28.66 ? 453 THR A CA 1 ATOM 3196 C C . THR A 1 400 ? 44.127 55.254 19.525 1.00 26.38 ? 453 THR A C 1 ATOM 3197 O O . THR A 1 400 ? 45.186 54.656 19.408 1.00 25.58 ? 453 THR A O 1 ATOM 3198 C CB . THR A 1 400 ? 43.377 55.194 21.927 1.00 28.13 ? 453 THR A CB 1 ATOM 3199 O OG1 . THR A 1 400 ? 43.377 55.946 23.143 1.00 30.42 ? 453 THR A OG1 1 ATOM 3200 C CG2 . THR A 1 400 ? 44.371 54.075 22.191 1.00 26.51 ? 453 THR A CG2 1 ATOM 3201 N N . LEU A 1 401 ? 43.179 55.205 18.603 1.00 28.86 ? 454 LEU A N 1 ATOM 3202 C CA . LEU A 1 401 ? 43.347 54.364 17.433 1.00 28.84 ? 454 LEU A CA 1 ATOM 3203 C C . LEU A 1 401 ? 44.682 54.687 16.782 1.00 34.89 ? 454 LEU A C 1 ATOM 3204 O O . LEU A 1 401 ? 45.303 53.831 16.152 1.00 33.92 ? 454 LEU A O 1 ATOM 3205 C CB . LEU A 1 401 ? 42.223 54.590 16.449 1.00 29.56 ? 454 LEU A CB 1 ATOM 3206 C CG . LEU A 1 401 ? 40.895 54.133 17.063 1.00 31.11 ? 454 LEU A CG 1 ATOM 3207 C CD1 . LEU A 1 401 ? 39.781 54.133 16.055 1.00 27.65 ? 454 LEU A CD1 1 ATOM 3208 C CD2 . LEU A 1 401 ? 41.086 52.747 17.663 1.00 34.77 ? 454 LEU A CD2 1 ATOM 3209 N N . ASP A 1 402 ? 45.122 55.930 16.948 1.00 37.25 ? 455 ASP A N 1 ATOM 3210 C CA . ASP A 1 402 ? 46.220 56.464 16.166 1.00 41.52 ? 455 ASP A CA 1 ATOM 3211 C C . ASP A 1 402 ? 47.540 56.012 16.773 1.00 41.77 ? 455 ASP A C 1 ATOM 3212 O O . ASP A 1 402 ? 48.557 55.968 16.092 1.00 42.65 ? 455 ASP A O 1 ATOM 3213 C CB . ASP A 1 402 ? 46.157 57.992 16.125 1.00 43.06 ? 455 ASP A CB 1 ATOM 3214 C CG . ASP A 1 402 ? 44.854 58.504 15.541 1.00 47.04 ? 455 ASP A CG 1 ATOM 3215 O OD1 . ASP A 1 402 ? 43.912 57.700 15.401 1.00 48.80 ? 455 ASP A OD1 1 ATOM 3216 O OD2 . ASP A 1 402 ? 44.675 59.694 15.198 1.00 48.82 ? 455 ASP A OD2 1 ATOM 3217 N N . ASP A 1 403 ? 47.517 55.669 18.057 1.00 42.07 ? 456 ASP A N 1 ATOM 3218 C CA . ASP A 1 403 ? 48.706 55.180 18.742 1.00 43.53 ? 456 ASP A CA 1 ATOM 3219 C C . ASP A 1 403 ? 48.865 53.655 18.636 1.00 41.02 ? 456 ASP A C 1 ATOM 3220 O O . ASP A 1 403 ? 49.866 53.099 19.092 1.00 42.49 ? 456 ASP A O 1 ATOM 3221 C CB . ASP A 1 403 ? 48.679 55.583 20.218 1.00 46.75 ? 456 ASP A CB 1 ATOM 3222 C CG . ASP A 1 403 ? 48.313 57.041 20.425 1.00 51.26 ? 456 ASP A CG 1 ATOM 3223 O OD1 . ASP A 1 403 ? 49.086 57.929 20.002 1.00 53.73 ? 456 ASP A OD1 1 ATOM 3224 O OD2 . ASP A 1 403 ? 47.272 57.397 21.014 1.00 54.53 ? 456 ASP A OD2 1 ATOM 3225 N N . LEU A 1 404 ? 47.884 52.975 18.053 1.00 37.40 ? 457 LEU A N 1 ATOM 3226 C CA . LEU A 1 404 ? 47.907 51.517 18.022 1.00 35.23 ? 457 LEU A CA 1 ATOM 3227 C C . LEU A 1 404 ? 48.598 50.987 16.766 1.00 35.46 ? 457 LEU A C 1 ATOM 3228 O O . LEU A 1 404 ? 48.124 51.211 15.655 1.00 38.54 ? 457 LEU A O 1 ATOM 3229 C CB . LEU A 1 404 ? 46.489 50.966 18.097 1.00 34.72 ? 457 LEU A CB 1 ATOM 3230 C CG . LEU A 1 404 ? 45.751 51.261 19.405 1.00 32.65 ? 457 LEU A CG 1 ATOM 3231 C CD1 . LEU A 1 404 ? 44.406 50.551 19.433 1.00 30.61 ? 457 LEU A CD1 1 ATOM 3232 C CD2 . LEU A 1 404 ? 46.607 50.874 20.603 1.00 30.23 ? 457 LEU A CD2 1 ATOM 3233 N N . THR A 1 405 ? 49.697 50.264 16.950 1.00 33.98 ? 458 THR A N 1 ATOM 3234 C CA . THR A 1 405 ? 50.621 49.974 15.853 1.00 36.05 ? 458 THR A CA 1 ATOM 3235 C C . THR A 1 405 ? 50.195 48.731 15.078 1.00 35.38 ? 458 THR A C 1 ATOM 3236 O O . THR A 1 405 ? 50.752 48.436 14.023 1.00 33.64 ? 458 THR A O 1 ATOM 3237 C CB . THR A 1 405 ? 52.055 49.781 16.383 1.00 36.20 ? 458 THR A CB 1 ATOM 3238 O OG1 . THR A 1 405 ? 52.121 48.614 17.211 1.00 37.85 ? 458 THR A OG1 1 ATOM 3239 C CG2 . THR A 1 405 ? 52.469 50.922 17.311 1.00 39.57 ? 458 THR A CG2 1 ATOM 3240 N N . TRP A 1 406 ? 49.212 48.004 15.606 1.00 32.64 ? 459 TRP A N 1 ATOM 3241 C CA . TRP A 1 406 ? 48.906 46.667 15.124 1.00 28.87 ? 459 TRP A CA 1 ATOM 3242 C C . TRP A 1 406 ? 47.699 46.653 14.212 1.00 27.84 ? 459 TRP A C 1 ATOM 3243 O O . TRP A 1 406 ? 47.225 45.590 13.830 1.00 27.99 ? 459 TRP A O 1 ATOM 3244 C CB . TRP A 1 406 ? 48.682 45.689 16.289 1.00 28.64 ? 459 TRP A CB 1 ATOM 3245 C CG . TRP A 1 406 ? 47.623 46.105 17.299 1.00 26.80 ? 459 TRP A CG 1 ATOM 3246 C CD1 . TRP A 1 406 ? 47.833 46.811 18.443 1.00 24.37 ? 459 TRP A CD1 1 ATOM 3247 C CD2 . TRP A 1 406 ? 46.219 45.809 17.266 1.00 26.01 ? 459 TRP A CD2 1 ATOM 3248 N NE1 . TRP A 1 406 ? 46.650 46.988 19.118 1.00 28.04 ? 459 TRP A NE1 1 ATOM 3249 C CE2 . TRP A 1 406 ? 45.641 46.383 18.417 1.00 26.28 ? 459 TRP A CE2 1 ATOM 3250 C CE3 . TRP A 1 406 ? 45.390 45.121 16.378 1.00 27.43 ? 459 TRP A CE3 1 ATOM 3251 C CZ2 . TRP A 1 406 ? 44.278 46.294 18.701 1.00 26.42 ? 459 TRP A CZ2 1 ATOM 3252 C CZ3 . TRP A 1 406 ? 44.030 45.035 16.657 1.00 27.70 ? 459 TRP A CZ3 1 ATOM 3253 C CH2 . TRP A 1 406 ? 43.488 45.618 17.810 1.00 27.36 ? 459 TRP A CH2 1 ATOM 3254 N N . MET A 1 407 ? 47.196 47.830 13.858 1.00 31.54 ? 460 MET A N 1 ATOM 3255 C CA . MET A 1 407 ? 46.179 47.929 12.821 1.00 32.52 ? 460 MET A CA 1 ATOM 3256 C C . MET A 1 407 ? 46.659 48.794 11.667 1.00 34.00 ? 460 MET A C 1 ATOM 3257 O O . MET A 1 407 ? 47.475 49.689 11.853 1.00 32.92 ? 460 MET A O 1 ATOM 3258 C CB . MET A 1 407 ? 44.903 48.533 13.391 1.00 34.74 ? 460 MET A CB 1 ATOM 3259 C CG . MET A 1 407 ? 44.369 47.810 14.618 1.00 37.23 ? 460 MET A CG 1 ATOM 3260 S SD . MET A 1 407 ? 42.971 48.686 15.304 1.00 34.64 ? 460 MET A SD 1 ATOM 3261 C CE . MET A 1 407 ? 41.694 47.943 14.426 1.00 35.89 ? 460 MET A CE 1 ATOM 3262 N N . ASP A 1 408 ? 46.131 48.528 10.480 1.00 36.28 ? 461 ASP A N 1 ATOM 3263 C CA . ASP A 1 408 ? 46.374 49.384 9.327 1.00 35.02 ? 461 ASP A CA 1 ATOM 3264 C C . ASP A 1 408 ? 45.352 50.503 9.236 1.00 35.20 ? 461 ASP A C 1 ATOM 3265 O O . ASP A 1 408 ? 44.350 50.523 9.956 1.00 31.28 ? 461 ASP A O 1 ATOM 3266 C CB . ASP A 1 408 ? 46.346 48.565 8.040 1.00 33.40 ? 461 ASP A CB 1 ATOM 3267 C CG . ASP A 1 408 ? 45.156 47.620 7.971 1.00 32.83 ? 461 ASP A CG 1 ATOM 3268 O OD1 . ASP A 1 408 ? 45.381 46.403 7.793 1.00 33.23 ? 461 ASP A OD1 1 ATOM 3269 O OD2 . ASP A 1 408 ? 43.965 47.998 8.054 1.00 29.99 ? 461 ASP A OD2 1 ATOM 3270 N N . ALA A 1 409 ? 45.618 51.433 8.328 1.00 35.81 ? 462 ALA A N 1 ATOM 3271 C CA . ALA A 1 409 ? 44.847 52.657 8.224 1.00 36.13 ? 462 ALA A CA 1 ATOM 3272 C C . ALA A 1 409 ? 43.376 52.362 7.990 1.00 35.85 ? 462 ALA A C 1 ATOM 3273 O O . ALA A 1 409 ? 42.518 52.942 8.656 1.00 41.28 ? 462 ALA A O 1 ATOM 3274 C CB . ALA A 1 409 ? 45.400 53.536 7.104 1.00 38.14 ? 462 ALA A CB 1 ATOM 3275 N N . GLU A 1 410 ? 43.066 51.483 7.043 1.00 31.42 ? 463 GLU A N 1 ATOM 3276 C CA . GLU A 1 410 ? 41.674 51.312 6.655 1.00 36.39 ? 463 GLU A CA 1 ATOM 3277 C C . GLU A 1 410 ? 40.891 50.752 7.840 1.00 36.33 ? 463 GLU A C 1 ATOM 3278 O O . GLU A 1 410 ? 39.773 51.181 8.108 1.00 35.75 ? 463 GLU A O 1 ATOM 3279 C CB . GLU A 1 410 ? 41.513 50.405 5.427 1.00 38.44 ? 463 GLU A CB 1 ATOM 3280 C CG . GLU A 1 410 ? 42.384 49.159 5.423 1.00 41.50 ? 463 GLU A CG 1 ATOM 3281 C CD . GLU A 1 410 ? 42.541 48.562 4.031 1.00 43.37 ? 463 GLU A CD 1 ATOM 3282 O OE1 . GLU A 1 410 ? 43.679 48.565 3.510 1.00 42.55 ? 463 GLU A OE1 1 ATOM 3283 O OE2 . GLU A 1 410 ? 41.530 48.093 3.456 1.00 42.60 ? 463 GLU A OE2 1 ATOM 3284 N N . THR A 1 411 ? 41.481 49.800 8.552 1.00 36.06 ? 464 THR A N 1 ATOM 3285 C CA . THR A 1 411 ? 40.757 49.116 9.622 1.00 32.33 ? 464 THR A CA 1 ATOM 3286 C C . THR A 1 411 ? 40.519 50.080 10.786 1.00 26.90 ? 464 THR A C 1 ATOM 3287 O O . THR A 1 411 ? 39.462 50.078 11.408 1.00 29.87 ? 464 THR A O 1 ATOM 3288 C CB . THR A 1 411 ? 41.526 47.857 10.077 1.00 32.21 ? 464 THR A CB 1 ATOM 3289 O OG1 . THR A 1 411 ? 41.553 46.892 9.010 1.00 27.57 ? 464 THR A OG1 1 ATOM 3290 C CG2 . THR A 1 411 ? 40.774 47.141 11.215 1.00 31.17 ? 464 THR A CG2 1 ATOM 3291 N N . LYS A 1 412 ? 41.502 50.918 11.062 1.00 23.92 ? 465 LYS A N 1 ATOM 3292 C CA . LYS A 1 412 ? 41.312 52.029 11.967 1.00 28.78 ? 465 LYS A CA 1 ATOM 3293 C C . LYS A 1 412 ? 40.119 52.899 11.578 1.00 32.78 ? 465 LYS A C 1 ATOM 3294 O O . LYS A 1 412 ? 39.321 53.278 12.437 1.00 33.24 ? 465 LYS A O 1 ATOM 3295 C CB . LYS A 1 412 ? 42.575 52.870 12.035 1.00 27.85 ? 465 LYS A CB 1 ATOM 3296 C CG . LYS A 1 412 ? 43.716 52.158 12.701 1.00 26.91 ? 465 LYS A CG 1 ATOM 3297 C CD . LYS A 1 412 ? 44.845 53.107 13.056 1.00 28.35 ? 465 LYS A CD 1 ATOM 3298 C CE . LYS A 1 412 ? 46.043 52.331 13.545 1.00 26.45 ? 465 LYS A CE 1 ATOM 3299 N NZ . LYS A 1 412 ? 47.102 53.193 14.092 1.00 25.22 ? 465 LYS A NZ 1 ATOM 3300 N N . LYS A 1 413 ? 39.992 53.213 10.294 1.00 34.66 ? 466 LYS A N 1 ATOM 3301 C CA . LYS A 1 413 ? 38.916 54.089 9.848 1.00 38.76 ? 466 LYS A CA 1 ATOM 3302 C C . LYS A 1 413 ? 37.585 53.479 10.246 1.00 35.57 ? 466 LYS A C 1 ATOM 3303 O O . LYS A 1 413 ? 36.738 54.144 10.834 1.00 35.74 ? 466 LYS A O 1 ATOM 3304 C CB . LYS A 1 413 ? 38.966 54.292 8.330 1.00 42.06 ? 466 LYS A CB 1 ATOM 3305 C CG . LYS A 1 413 ? 38.439 55.637 7.869 1.00 45.71 ? 466 LYS A CG 1 ATOM 3306 C CD . LYS A 1 413 ? 38.577 55.805 6.354 1.00 48.34 ? 466 LYS A CD 1 ATOM 3307 C CE . LYS A 1 413 ? 40.038 55.901 5.918 1.00 49.66 ? 466 LYS A CE 1 ATOM 3308 N NZ . LYS A 1 413 ? 40.187 56.435 4.529 1.00 50.20 ? 466 LYS A NZ 1 ATOM 3309 N N . ARG A 1 414 ? 37.410 52.203 9.931 1.00 34.32 ? 467 ARG A N 1 ATOM 3310 C CA . ARG A 1 414 ? 36.138 51.541 10.162 1.00 38.65 ? 467 ARG A CA 1 ATOM 3311 C C . ARG A 1 414 ? 35.884 51.372 11.658 1.00 35.74 ? 467 ARG A C 1 ATOM 3312 O O . ARG A 1 414 ? 34.740 51.365 12.101 1.00 33.42 ? 467 ARG A O 1 ATOM 3313 C CB . ARG A 1 414 ? 36.125 50.183 9.481 1.00 42.75 ? 467 ARG A CB 1 ATOM 3314 C CG . ARG A 1 414 ? 36.293 50.254 7.983 1.00 48.04 ? 467 ARG A CG 1 ATOM 3315 C CD . ARG A 1 414 ? 36.823 48.975 7.388 1.00 52.08 ? 467 ARG A CD 1 ATOM 3316 N NE . ARG A 1 414 ? 36.262 48.704 6.071 1.00 56.03 ? 467 ARG A NE 1 ATOM 3317 C CZ . ARG A 1 414 ? 36.942 48.134 5.091 1.00 59.62 ? 467 ARG A CZ 1 ATOM 3318 N NH1 . ARG A 1 414 ? 38.206 47.781 5.288 1.00 59.96 ? 467 ARG A NH1 1 ATOM 3319 N NH2 . ARG A 1 414 ? 36.366 47.913 3.916 1.00 60.80 ? 467 ARG A NH2 1 ATOM 3320 N N . ALA A 1 415 ? 36.963 51.229 12.421 1.00 32.51 ? 468 ALA A N 1 ATOM 3321 C CA . ALA A 1 415 ? 36.877 51.168 13.870 1.00 30.61 ? 468 ALA A CA 1 ATOM 3322 C C . ALA A 1 415 ? 36.315 52.477 14.413 1.00 29.58 ? 468 ALA A C 1 ATOM 3323 O O . ALA A 1 415 ? 35.471 52.488 15.319 1.00 25.83 ? 468 ALA A O 1 ATOM 3324 C CB . ALA A 1 415 ? 38.249 50.906 14.460 1.00 28.97 ? 468 ALA A CB 1 ATOM 3325 N N . GLU A 1 416 ? 36.797 53.584 13.860 1.00 28.62 ? 469 GLU A N 1 ATOM 3326 C CA . GLU A 1 416 ? 36.318 54.894 14.261 1.00 29.72 ? 469 GLU A CA 1 ATOM 3327 C C . GLU A 1 416 ? 34.870 55.044 13.824 1.00 26.72 ? 469 GLU A C 1 ATOM 3328 O O . GLU A 1 416 ? 34.017 55.491 14.591 1.00 27.05 ? 469 GLU A O 1 ATOM 3329 C CB . GLU A 1 416 ? 37.201 55.999 13.657 1.00 31.09 ? 469 GLU A CB 1 ATOM 3330 C CG . GLU A 1 416 ? 36.532 57.364 13.553 1.00 33.20 ? 469 GLU A CG 1 ATOM 3331 C CD . GLU A 1 416 ? 37.518 58.487 13.246 1.00 36.91 ? 469 GLU A CD 1 ATOM 3332 O OE1 . GLU A 1 416 ? 37.132 59.667 13.352 1.00 37.79 ? 469 GLU A OE1 1 ATOM 3333 O OE2 . GLU A 1 416 ? 38.685 58.198 12.914 1.00 37.03 ? 469 GLU A OE2 1 ATOM 3334 N N . GLU A 1 417 ? 34.587 54.663 12.585 1.00 32.43 ? 470 GLU A N 1 ATOM 3335 C CA . GLU A 1 417 ? 33.210 54.597 12.119 1.00 32.46 ? 470 GLU A CA 1 ATOM 3336 C C . GLU A 1 417 ? 32.339 53.979 13.197 1.00 32.97 ? 470 GLU A C 1 ATOM 3337 O O . GLU A 1 417 ? 31.266 54.500 13.530 1.00 27.04 ? 470 GLU A O 1 ATOM 3338 C CB . GLU A 1 417 ? 33.112 53.753 10.857 1.00 37.04 ? 470 GLU A CB 1 ATOM 3339 C CG . GLU A 1 417 ? 32.727 54.530 9.613 1.00 42.98 ? 470 GLU A CG 1 ATOM 3340 C CD . GLU A 1 417 ? 33.305 53.910 8.359 1.00 45.07 ? 470 GLU A CD 1 ATOM 3341 O OE1 . GLU A 1 417 ? 34.345 54.408 7.874 1.00 49.66 ? 470 GLU A OE1 1 ATOM 3342 O OE2 . GLU A 1 417 ? 32.727 52.916 7.869 1.00 46.51 ? 470 GLU A OE2 1 ATOM 3343 N N . LYS A 1 418 ? 32.790 52.850 13.732 1.00 29.55 ? 471 LYS A N 1 ATOM 3344 C CA . LYS A 1 418 ? 31.950 52.088 14.647 1.00 29.17 ? 471 LYS A CA 1 ATOM 3345 C C . LYS A 1 418 ? 31.841 52.796 15.999 1.00 26.53 ? 471 LYS A C 1 ATOM 3346 O O . LYS A 1 418 ? 30.808 52.716 16.667 1.00 32.82 ? 471 LYS A O 1 ATOM 3347 C CB . LYS A 1 418 ? 32.477 50.667 14.833 1.00 28.87 ? 471 LYS A CB 1 ATOM 3348 C CG . LYS A 1 418 ? 31.729 49.900 15.929 1.00 31.32 ? 471 LYS A CG 1 ATOM 3349 C CD . LYS A 1 418 ? 31.842 48.395 15.779 1.00 30.26 ? 471 LYS A CD 1 ATOM 3350 C CE . LYS A 1 418 ? 30.576 47.707 16.317 1.00 32.72 ? 471 LYS A CE 1 ATOM 3351 N NZ . LYS A 1 418 ? 30.780 46.219 16.404 1.00 31.33 ? 471 LYS A NZ 1 ATOM 3352 N N . ALA A 1 419 ? 32.907 53.488 16.396 1.00 29.92 ? 472 ALA A N 1 ATOM 3353 C CA . ALA A 1 419 ? 32.905 54.279 17.627 1.00 30.63 ? 472 ALA A CA 1 ATOM 3354 C C . ALA A 1 419 ? 31.850 55.385 17.583 1.00 29.36 ? 472 ALA A C 1 ATOM 3355 O O . ALA A 1 419 ? 31.098 55.598 18.543 1.00 26.94 ? 472 ALA A O 1 ATOM 3356 C CB . ALA A 1 419 ? 34.277 54.879 17.866 1.00 30.23 ? 472 ALA A CB 1 ATOM 3357 N N . LEU A 1 420 ? 31.786 56.085 16.459 1.00 27.17 ? 473 LEU A N 1 ATOM 3358 C CA . LEU A 1 420 ? 30.982 57.286 16.356 1.00 26.07 ? 473 LEU A CA 1 ATOM 3359 C C . LEU A 1 420 ? 29.538 56.868 16.329 1.00 26.79 ? 473 LEU A C 1 ATOM 3360 O O . LEU A 1 420 ? 28.641 57.654 16.636 1.00 31.97 ? 473 LEU A O 1 ATOM 3361 C CB . LEU A 1 420 ? 31.338 58.041 15.081 1.00 27.89 ? 473 LEU A CB 1 ATOM 3362 C CG . LEU A 1 420 ? 32.728 58.661 15.014 1.00 30.20 ? 473 LEU A CG 1 ATOM 3363 C CD1 . LEU A 1 420 ? 33.047 59.021 13.556 1.00 33.33 ? 473 LEU A CD1 1 ATOM 3364 C CD2 . LEU A 1 420 ? 32.831 59.892 15.902 1.00 30.43 ? 473 LEU A CD2 1 ATOM 3365 N N . ALA A 1 421 ? 29.313 55.612 15.962 1.00 22.88 ? 474 ALA A N 1 ATOM 3366 C CA . ALA A 1 421 ? 27.978 55.119 15.698 1.00 25.10 ? 474 ALA A CA 1 ATOM 3367 C C . ALA A 1 421 ? 27.383 54.398 16.898 1.00 24.17 ? 474 ALA A C 1 ATOM 3368 O O . ALA A 1 421 ? 26.226 54.004 16.866 1.00 22.53 ? 474 ALA A O 1 ATOM 3369 C CB . ALA A 1 421 ? 27.997 54.186 14.520 1.00 26.00 ? 474 ALA A CB 1 ATOM 3370 N N . ILE A 1 422 ? 28.172 54.198 17.948 1.00 24.82 ? 475 ILE A N 1 ATOM 3371 C CA . ILE A 1 422 ? 27.621 53.595 19.163 1.00 27.58 ? 475 ILE A CA 1 ATOM 3372 C C . ILE A 1 422 ? 26.559 54.496 19.771 1.00 21.46 ? 475 ILE A C 1 ATOM 3373 O O . ILE A 1 422 ? 26.784 55.679 19.955 1.00 27.29 ? 475 ILE A O 1 ATOM 3374 C CB . ILE A 1 422 ? 28.709 53.342 20.188 1.00 27.32 ? 475 ILE A CB 1 ATOM 3375 C CG1 . ILE A 1 422 ? 29.587 52.176 19.732 1.00 29.57 ? 475 ILE A CG1 1 ATOM 3376 C CG2 . ILE A 1 422 ? 28.080 53.067 21.555 1.00 29.31 ? 475 ILE A CG2 1 ATOM 3377 C CD1 . ILE A 1 422 ? 30.978 52.223 20.317 1.00 32.01 ? 475 ILE A CD1 1 ATOM 3378 N N . LYS A 1 423 ? 25.406 53.926 20.089 1.00 23.91 ? 476 LYS A N 1 ATOM 3379 C CA . LYS A 1 423 ? 24.300 54.712 20.615 1.00 29.78 ? 476 LYS A CA 1 ATOM 3380 C C . LYS A 1 423 ? 24.121 54.437 22.098 1.00 30.13 ? 476 LYS A C 1 ATOM 3381 O O . LYS A 1 423 ? 23.961 53.288 22.516 1.00 33.23 ? 476 LYS A O 1 ATOM 3382 C CB . LYS A 1 423 ? 23.014 54.401 19.860 1.00 33.87 ? 476 LYS A CB 1 ATOM 3383 C CG . LYS A 1 423 ? 22.860 55.226 18.577 1.00 40.29 ? 476 LYS A CG 1 ATOM 3384 C CD . LYS A 1 423 ? 21.465 55.862 18.454 1.00 43.70 ? 476 LYS A CD 1 ATOM 3385 C CE . LYS A 1 423 ? 20.688 55.804 19.766 1.00 45.40 ? 476 LYS A CE 1 ATOM 3386 N NZ . LYS A 1 423 ? 20.220 57.148 20.198 1.00 46.35 ? 476 LYS A NZ 1 ATOM 3387 N N . GLU A 1 424 ? 24.161 55.494 22.894 1.00 28.25 ? 477 GLU A N 1 ATOM 3388 C CA . GLU A 1 424 ? 24.280 55.346 24.338 1.00 30.00 ? 477 GLU A CA 1 ATOM 3389 C C . GLU A 1 424 ? 22.919 55.520 25.003 1.00 27.23 ? 477 GLU A C 1 ATOM 3390 O O . GLU A 1 424 ? 22.038 56.218 24.483 1.00 21.15 ? 477 GLU A O 1 ATOM 3391 C CB . GLU A 1 424 ? 25.298 56.344 24.892 1.00 34.76 ? 477 GLU A CB 1 ATOM 3392 C CG . GLU A 1 424 ? 24.733 57.718 25.192 1.00 41.59 ? 477 GLU A CG 1 ATOM 3393 C CD . GLU A 1 424 ? 25.407 58.813 24.396 1.00 45.43 ? 477 GLU A CD 1 ATOM 3394 O OE1 . GLU A 1 424 ? 26.162 59.613 24.997 1.00 49.85 ? 477 GLU A OE1 1 ATOM 3395 O OE2 . GLU A 1 424 ? 25.172 58.878 23.171 1.00 48.32 ? 477 GLU A OE2 1 ATOM 3396 N N . ARG A 1 425 ? 22.750 54.849 26.133 1.00 20.03 ? 478 ARG A N 1 ATOM 3397 C CA . ARG A 1 425 ? 21.498 54.853 26.875 1.00 23.10 ? 478 ARG A CA 1 ATOM 3398 C C . ARG A 1 425 ? 21.815 54.999 28.356 1.00 21.93 ? 478 ARG A C 1 ATOM 3399 O O . ARG A 1 425 ? 22.507 54.159 28.919 1.00 18.41 ? 478 ARG A O 1 ATOM 3400 C CB . ARG A 1 425 ? 20.747 53.540 26.666 1.00 26.89 ? 478 ARG A CB 1 ATOM 3401 C CG . ARG A 1 425 ? 20.530 53.158 25.208 1.00 33.02 ? 478 ARG A CG 1 ATOM 3402 C CD . ARG A 1 425 ? 19.474 53.995 24.507 1.00 37.58 ? 478 ARG A CD 1 ATOM 3403 N NE . ARG A 1 425 ? 18.727 53.228 23.516 1.00 43.00 ? 478 ARG A NE 1 ATOM 3404 C CZ . ARG A 1 425 ? 18.007 53.775 22.547 1.00 48.85 ? 478 ARG A CZ 1 ATOM 3405 N NH1 . ARG A 1 425 ? 17.938 55.095 22.439 1.00 51.39 ? 478 ARG A NH1 1 ATOM 3406 N NH2 . ARG A 1 425 ? 17.351 53.007 21.688 1.00 51.11 ? 478 ARG A NH2 1 ATOM 3407 N N . ILE A 1 426 ? 21.309 56.055 28.982 1.00 17.34 ? 479 ILE A N 1 ATOM 3408 C CA . ILE A 1 426 ? 21.778 56.463 30.296 1.00 20.60 ? 479 ILE A CA 1 ATOM 3409 C C . ILE A 1 426 ? 20.609 56.559 31.256 1.00 20.45 ? 479 ILE A C 1 ATOM 3410 O O . ILE A 1 426 ? 19.670 57.302 31.000 1.00 18.20 ? 479 ILE A O 1 ATOM 3411 C CB . ILE A 1 426 ? 22.473 57.820 30.214 1.00 21.68 ? 479 ILE A CB 1 ATOM 3412 C CG1 . ILE A 1 426 ? 23.724 57.725 29.346 1.00 24.48 ? 479 ILE A CG1 1 ATOM 3413 C CG2 . ILE A 1 426 ? 22.854 58.302 31.591 1.00 23.19 ? 479 ILE A CG2 1 ATOM 3414 C CD1 . ILE A 1 426 ? 23.957 58.930 28.496 1.00 23.58 ? 479 ILE A CD1 1 ATOM 3415 N N . GLY A 1 427 ? 20.667 55.808 32.355 1.00 18.73 ? 480 GLY A N 1 ATOM 3416 C CA . GLY A 1 427 ? 19.720 55.967 33.449 1.00 18.97 ? 480 GLY A CA 1 ATOM 3417 C C . GLY A 1 427 ? 18.414 55.220 33.236 1.00 21.33 ? 480 GLY A C 1 ATOM 3418 O O . GLY A 1 427 ? 18.194 54.146 33.802 1.00 17.67 ? 480 GLY A O 1 ATOM 3419 N N . TYR A 1 428 ? 17.542 55.783 32.408 1.00 17.39 ? 481 TYR A N 1 ATOM 3420 C CA . TYR A 1 428 ? 16.262 55.159 32.118 1.00 18.38 ? 481 TYR A CA 1 ATOM 3421 C C . TYR A 1 428 ? 15.619 55.823 30.903 1.00 17.39 ? 481 TYR A C 1 ATOM 3422 O O . TYR A 1 428 ? 15.939 56.951 30.594 1.00 19.84 ? 481 TYR A O 1 ATOM 3423 C CB . TYR A 1 428 ? 15.344 55.306 33.320 1.00 18.55 ? 481 TYR A CB 1 ATOM 3424 C CG . TYR A 1 428 ? 15.003 56.737 33.633 1.00 21.37 ? 481 TYR A CG 1 ATOM 3425 C CD1 . TYR A 1 428 ? 13.822 57.305 33.171 1.00 20.85 ? 481 TYR A CD1 1 ATOM 3426 C CD2 . TYR A 1 428 ? 15.858 57.525 34.379 1.00 22.48 ? 481 TYR A CD2 1 ATOM 3427 C CE1 . TYR A 1 428 ? 13.506 58.617 33.458 1.00 21.59 ? 481 TYR A CE1 1 ATOM 3428 C CE2 . TYR A 1 428 ? 15.554 58.832 34.670 1.00 21.63 ? 481 TYR A CE2 1 ATOM 3429 C CZ . TYR A 1 428 ? 14.368 59.376 34.212 1.00 24.66 ? 481 TYR A CZ 1 ATOM 3430 O OH . TYR A 1 428 ? 14.052 60.689 34.503 1.00 27.74 ? 481 TYR A OH 1 ATOM 3431 N N . PRO A 1 429 ? 14.704 55.138 30.228 1.00 19.69 ? 482 PRO A N 1 ATOM 3432 C CA . PRO A 1 429 ? 13.911 55.785 29.171 1.00 20.75 ? 482 PRO A CA 1 ATOM 3433 C C . PRO A 1 429 ? 12.874 56.748 29.758 1.00 19.59 ? 482 PRO A C 1 ATOM 3434 O O . PRO A 1 429 ? 11.997 56.327 30.496 1.00 19.93 ? 482 PRO A O 1 ATOM 3435 C CB . PRO A 1 429 ? 13.222 54.618 28.449 1.00 20.33 ? 482 PRO A CB 1 ATOM 3436 C CG . PRO A 1 429 ? 13.457 53.373 29.271 1.00 21.36 ? 482 PRO A CG 1 ATOM 3437 C CD . PRO A 1 429 ? 14.345 53.724 30.423 1.00 20.69 ? 482 PRO A CD 1 ATOM 3438 N N . ASP A 1 430 ? 13.001 58.026 29.443 1.00 22.94 ? 483 ASP A N 1 ATOM 3439 C CA . ASP A 1 430 ? 12.070 59.040 29.930 1.00 27.48 ? 483 ASP A CA 1 ATOM 3440 C C . ASP A 1 430 ? 10.613 58.615 29.783 1.00 27.22 ? 483 ASP A C 1 ATOM 3441 O O . ASP A 1 430 ? 9.772 59.006 30.584 1.00 28.50 ? 483 ASP A O 1 ATOM 3442 C CB . ASP A 1 430 ? 12.286 60.347 29.187 1.00 31.36 ? 483 ASP A CB 1 ATOM 3443 C CG . ASP A 1 430 ? 12.515 61.507 30.125 1.00 39.44 ? 483 ASP A CG 1 ATOM 3444 O OD1 . ASP A 1 430 ? 11.536 62.226 30.428 1.00 40.34 ? 483 ASP A OD1 1 ATOM 3445 O OD2 . ASP A 1 430 ? 13.638 61.764 30.620 1.00 44.99 ? 483 ASP A OD2 1 ATOM 3446 N N . ASP A 1 431 ? 10.334 57.824 28.750 1.00 26.83 ? 484 ASP A N 1 ATOM 3447 C CA . ASP A 1 431 ? 9.015 57.243 28.517 1.00 32.10 ? 484 ASP A CA 1 ATOM 3448 C C . ASP A 1 431 ? 8.363 56.698 29.774 1.00 31.33 ? 484 ASP A C 1 ATOM 3449 O O . ASP A 1 431 ? 7.164 56.871 29.980 1.00 28.00 ? 484 ASP A O 1 ATOM 3450 C CB . ASP A 1 431 ? 9.122 56.095 27.507 1.00 36.30 ? 484 ASP A CB 1 ATOM 3451 C CG . ASP A 1 431 ? 8.769 56.529 26.116 1.00 39.42 ? 484 ASP A CG 1 ATOM 3452 O OD1 . ASP A 1 431 ? 8.696 55.671 25.211 1.00 39.88 ? 484 ASP A OD1 1 ATOM 3453 O OD2 . ASP A 1 431 ? 8.542 57.722 25.842 1.00 42.26 ? 484 ASP A OD2 1 ATOM 3454 N N . ILE A 1 432 ? 9.132 55.981 30.588 1.00 26.04 ? 485 ILE A N 1 ATOM 3455 C CA . ILE A 1 432 ? 8.509 55.107 31.576 1.00 26.09 ? 485 ILE A CA 1 ATOM 3456 C C . ILE A 1 432 ? 7.943 55.977 32.686 1.00 22.82 ? 485 ILE A C 1 ATOM 3457 O O . ILE A 1 432 ? 7.101 55.540 33.465 1.00 26.89 ? 485 ILE A O 1 ATOM 3458 C CB . ILE A 1 432 ? 9.508 54.066 32.137 1.00 22.71 ? 485 ILE A CB 1 ATOM 3459 C CG1 . ILE A 1 432 ? 10.635 54.746 32.914 1.00 22.39 ? 485 ILE A CG1 1 ATOM 3460 C CG2 . ILE A 1 432 ? 10.077 53.210 31.009 1.00 25.39 ? 485 ILE A CG2 1 ATOM 3461 C CD1 . ILE A 1 432 ? 11.579 53.759 33.595 1.00 23.04 ? 485 ILE A CD1 1 ATOM 3462 N N . VAL A 1 433 ? 8.396 57.222 32.749 1.00 24.86 ? 486 VAL A N 1 ATOM 3463 C CA . VAL A 1 433 ? 7.821 58.170 33.696 1.00 26.99 ? 486 VAL A CA 1 ATOM 3464 C C . VAL A 1 433 ? 6.802 59.087 33.019 1.00 26.11 ? 486 VAL A C 1 ATOM 3465 O O . VAL A 1 433 ? 5.815 59.487 33.629 1.00 23.42 ? 486 VAL A O 1 ATOM 3466 C CB . VAL A 1 433 ? 8.917 59.038 34.344 1.00 29.84 ? 486 VAL A CB 1 ATOM 3467 C CG1 . VAL A 1 433 ? 8.291 60.103 35.242 1.00 30.19 ? 486 VAL A CG1 1 ATOM 3468 C CG2 . VAL A 1 433 ? 9.891 58.169 35.130 1.00 29.67 ? 486 VAL A CG2 1 ATOM 3469 N N . SER A 1 434 ? 7.066 59.437 31.765 1.00 28.18 ? 487 SER A N 1 ATOM 3470 C CA . SER A 1 434 ? 6.343 60.522 31.110 1.00 30.35 ? 487 SER A CA 1 ATOM 3471 C C . SER A 1 434 ? 5.119 60.022 30.346 1.00 32.84 ? 487 SER A C 1 ATOM 3472 O O . SER A 1 434 ? 4.228 60.812 30.047 1.00 35.00 ? 487 SER A O 1 ATOM 3473 C CB . SER A 1 434 ? 7.265 61.297 30.169 1.00 32.19 ? 487 SER A CB 1 ATOM 3474 O OG . SER A 1 434 ? 7.505 60.573 28.978 1.00 33.30 ? 487 SER A OG 1 ATOM 3475 N N . ASN A 1 435 ? 5.074 58.725 30.029 1.00 28.83 ? 488 ASN A N 1 ATOM 3476 C CA . ASN A 1 435 ? 4.025 58.182 29.165 1.00 27.30 ? 488 ASN A CA 1 ATOM 3477 C C . ASN A 1 435 ? 3.217 57.063 29.816 1.00 26.49 ? 488 ASN A C 1 ATOM 3478 O O . ASN A 1 435 ? 3.526 55.889 29.659 1.00 23.40 ? 488 ASN A O 1 ATOM 3479 C CB . ASN A 1 435 ? 4.617 57.677 27.853 1.00 27.55 ? 488 ASN A CB 1 ATOM 3480 C CG . ASN A 1 435 ? 3.557 57.408 26.784 1.00 29.62 ? 488 ASN A CG 1 ATOM 3481 O OD1 . ASN A 1 435 ? 2.407 57.058 27.086 1.00 30.69 ? 488 ASN A OD1 1 ATOM 3482 N ND2 . ASN A 1 435 ? 3.954 57.540 25.528 1.00 25.99 ? 488 ASN A ND2 1 ATOM 3483 N N . ASP A 1 436 ? 2.163 57.432 30.530 1.00 22.78 ? 489 ASP A N 1 ATOM 3484 C CA . ASP A 1 436 ? 1.403 56.469 31.301 1.00 26.33 ? 489 ASP A CA 1 ATOM 3485 C C . ASP A 1 436 ? 0.724 55.427 30.403 1.00 30.43 ? 489 ASP A C 1 ATOM 3486 O O . ASP A 1 436 ? 0.762 54.223 30.691 1.00 26.52 ? 489 ASP A O 1 ATOM 3487 C CB . ASP A 1 436 ? 0.374 57.203 32.155 1.00 27.66 ? 489 ASP A CB 1 ATOM 3488 C CG . ASP A 1 436 ? 1.009 57.950 33.309 1.00 29.10 ? 489 ASP A CG 1 ATOM 3489 O OD1 . ASP A 1 436 ? 2.246 57.830 33.497 1.00 29.00 ? 489 ASP A OD1 1 ATOM 3490 O OD2 . ASP A 1 436 ? 0.349 58.683 34.080 1.00 28.15 ? 489 ASP A OD2 1 ATOM 3491 N N . ASN A 1 437 ? 0.110 55.894 29.313 1.00 27.52 ? 490 ASN A N 1 ATOM 3492 C CA . ASN A 1 437 ? -0.510 55.020 28.323 1.00 28.06 ? 490 ASN A CA 1 ATOM 3493 C C . ASN A 1 437 ? 0.389 53.881 27.836 1.00 23.29 ? 490 ASN A C 1 ATOM 3494 O O . ASN A 1 437 ? -0.017 52.728 27.813 1.00 22.01 ? 490 ASN A O 1 ATOM 3495 C CB . ASN A 1 437 ? -0.901 55.836 27.087 1.00 29.77 ? 490 ASN A CB 1 ATOM 3496 C CG . ASN A 1 437 ? -2.316 56.338 27.133 1.00 30.21 ? 490 ASN A CG 1 ATOM 3497 O OD1 . ASN A 1 437 ? -2.686 57.207 26.344 1.00 34.48 ? 490 ASN A OD1 1 ATOM 3498 N ND2 . ASN A 1 437 ? -3.123 55.804 28.042 1.00 28.25 ? 490 ASN A ND2 1 ATOM 3499 N N . LYS A 1 438 ? 1.578 54.233 27.370 1.00 25.39 ? 491 LYS A N 1 ATOM 3500 C CA . LYS A 1 438 ? 2.519 53.256 26.854 1.00 27.23 ? 491 LYS A CA 1 ATOM 3501 C C . LYS A 1 438 ? 2.818 52.194 27.915 1.00 29.67 ? 491 LYS A C 1 ATOM 3502 O O . LYS A 1 438 ? 2.869 50.999 27.607 1.00 25.56 ? 491 LYS A O 1 ATOM 3503 C CB . LYS A 1 438 ? 3.814 53.956 26.431 1.00 30.16 ? 491 LYS A CB 1 ATOM 3504 C CG . LYS A 1 438 ? 4.805 53.085 25.655 1.00 28.00 ? 491 LYS A CG 1 ATOM 3505 C CD . LYS A 1 438 ? 6.045 53.892 25.279 1.00 30.12 ? 491 LYS A CD 1 ATOM 3506 C CE . LYS A 1 438 ? 7.263 52.999 25.095 1.00 32.63 ? 491 LYS A CE 1 ATOM 3507 N NZ . LYS A 1 438 ? 8.382 53.717 24.426 1.00 36.23 ? 491 LYS A NZ 1 ATOM 3508 N N . LEU A 1 439 ? 3.029 52.639 29.158 1.00 26.02 ? 492 LEU A N 1 ATOM 3509 C CA . LEU A 1 439 ? 3.483 51.748 30.232 1.00 24.11 ? 492 LEU A CA 1 ATOM 3510 C C . LEU A 1 439 ? 2.381 50.782 30.634 1.00 20.39 ? 492 LEU A C 1 ATOM 3511 O O . LEU A 1 439 ? 2.611 49.589 30.724 1.00 22.76 ? 492 LEU A O 1 ATOM 3512 C CB . LEU A 1 439 ? 3.921 52.549 31.458 1.00 25.19 ? 492 LEU A CB 1 ATOM 3513 C CG . LEU A 1 439 ? 4.641 51.755 32.560 1.00 26.30 ? 492 LEU A CG 1 ATOM 3514 C CD1 . LEU A 1 439 ? 3.676 50.805 33.262 1.00 30.79 ? 492 LEU A CD1 1 ATOM 3515 C CD2 . LEU A 1 439 ? 5.838 50.986 32.002 1.00 26.56 ? 492 LEU A CD2 1 ATOM 3516 N N . ASN A 1 440 ? 1.181 51.309 30.860 1.00 24.61 ? 493 ASN A N 1 ATOM 3517 C CA . ASN A 1 440 ? -0.003 50.481 31.024 1.00 25.80 ? 493 ASN A CA 1 ATOM 3518 C C . ASN A 1 440 ? -0.139 49.455 29.901 1.00 26.34 ? 493 ASN A C 1 ATOM 3519 O O . ASN A 1 440 ? -0.352 48.274 30.147 1.00 27.29 ? 493 ASN A O 1 ATOM 3520 C CB . ASN A 1 440 ? -1.255 51.351 31.087 1.00 28.91 ? 493 ASN A CB 1 ATOM 3521 C CG . ASN A 1 440 ? -1.307 52.212 32.333 1.00 32.34 ? 493 ASN A CG 1 ATOM 3522 O OD1 . ASN A 1 440 ? -0.693 51.893 33.358 1.00 31.63 ? 493 ASN A OD1 1 ATOM 3523 N ND2 . ASN A 1 440 ? -2.042 53.320 32.250 1.00 28.27 ? 493 ASN A ND2 1 ATOM 3524 N N . ASN A 1 441 ? -0.007 49.899 28.662 1.00 29.55 ? 494 ASN A N 1 ATOM 3525 C CA . ASN A 1 441 ? -0.282 49.018 27.534 1.00 29.52 ? 494 ASN A CA 1 ATOM 3526 C C . ASN A 1 441 ? 0.746 47.899 27.403 1.00 30.46 ? 494 ASN A C 1 ATOM 3527 O O . ASN A 1 441 ? 0.459 46.847 26.831 1.00 28.47 ? 494 ASN A O 1 ATOM 3528 C CB . ASN A 1 441 ? -0.371 49.825 26.241 1.00 27.24 ? 494 ASN A CB 1 ATOM 3529 C CG . ASN A 1 441 ? -1.691 50.528 26.106 1.00 23.63 ? 494 ASN A CG 1 ATOM 3530 O OD1 . ASN A 1 441 ? -2.678 50.122 26.720 1.00 25.16 ? 494 ASN A OD1 1 ATOM 3531 N ND2 . ASN A 1 441 ? -1.723 51.607 25.319 1.00 25.99 ? 494 ASN A ND2 1 ATOM 3532 N N . GLU A 1 442 ? 1.939 48.108 27.956 1.00 27.04 ? 495 GLU A N 1 ATOM 3533 C CA . GLU A 1 442 ? 2.934 47.043 27.980 1.00 25.86 ? 495 GLU A CA 1 ATOM 3534 C C . GLU A 1 442 ? 2.414 45.825 28.745 1.00 23.22 ? 495 GLU A C 1 ATOM 3535 O O . GLU A 1 442 ? 2.747 44.685 28.432 1.00 22.91 ? 495 GLU A O 1 ATOM 3536 C CB . GLU A 1 442 ? 4.248 47.539 28.601 1.00 27.99 ? 495 GLU A CB 1 ATOM 3537 C CG . GLU A 1 442 ? 5.346 46.485 28.600 1.00 27.78 ? 495 GLU A CG 1 ATOM 3538 C CD . GLU A 1 442 ? 6.684 47.015 29.076 1.00 23.41 ? 495 GLU A CD 1 ATOM 3539 O OE1 . GLU A 1 442 ? 6.808 48.233 29.335 1.00 26.12 ? 495 GLU A OE1 1 ATOM 3540 O OE2 . GLU A 1 442 ? 7.618 46.199 29.182 1.00 30.50 ? 495 GLU A OE2 1 ATOM 3541 N N . TYR A 1 443 ? 1.604 46.069 29.763 1.00 22.62 ? 496 TYR A N 1 ATOM 3542 C CA . TYR A 1 443 ? 1.173 45.007 30.656 1.00 21.63 ? 496 TYR A CA 1 ATOM 3543 C C . TYR A 1 443 ? -0.329 44.744 30.526 1.00 22.73 ? 496 TYR A C 1 ATOM 3544 O O . TYR A 1 443 ? -0.935 44.092 31.379 1.00 24.25 ? 496 TYR A O 1 ATOM 3545 C CB . TYR A 1 443 ? 1.525 45.373 32.105 1.00 22.04 ? 496 TYR A CB 1 ATOM 3546 C CG . TYR A 1 443 ? 2.973 45.780 32.296 1.00 19.53 ? 496 TYR A CG 1 ATOM 3547 C CD1 . TYR A 1 443 ? 3.996 44.870 32.110 1.00 19.67 ? 496 TYR A CD1 1 ATOM 3548 C CD2 . TYR A 1 443 ? 3.310 47.078 32.676 1.00 20.84 ? 496 TYR A CD2 1 ATOM 3549 C CE1 . TYR A 1 443 ? 5.323 45.238 32.278 1.00 22.99 ? 496 TYR A CE1 1 ATOM 3550 C CE2 . TYR A 1 443 ? 4.638 47.458 32.844 1.00 20.91 ? 496 TYR A CE2 1 ATOM 3551 C CZ . TYR A 1 443 ? 5.636 46.528 32.659 1.00 20.52 ? 496 TYR A CZ 1 ATOM 3552 O OH . TYR A 1 443 ? 6.961 46.879 32.828 1.00 21.35 ? 496 TYR A OH 1 ATOM 3553 N N . LEU A 1 444 ? -0.924 45.259 29.451 1.00 24.71 ? 497 LEU A N 1 ATOM 3554 C CA . LEU A 1 444 ? -2.371 45.191 29.249 1.00 24.24 ? 497 LEU A CA 1 ATOM 3555 C C . LEU A 1 444 ? -2.875 43.765 29.369 1.00 20.30 ? 497 LEU A C 1 ATOM 3556 O O . LEU A 1 444 ? -3.900 43.506 29.992 1.00 22.18 ? 497 LEU A O 1 ATOM 3557 C CB . LEU A 1 444 ? -2.727 45.716 27.853 1.00 27.22 ? 497 LEU A CB 1 ATOM 3558 C CG . LEU A 1 444 ? -3.889 46.695 27.716 1.00 27.49 ? 497 LEU A CG 1 ATOM 3559 C CD1 . LEU A 1 444 ? -4.588 46.525 26.352 1.00 26.66 ? 497 LEU A CD1 1 ATOM 3560 C CD2 . LEU A 1 444 ? -4.872 46.554 28.847 1.00 28.88 ? 497 LEU A CD2 1 ATOM 3561 N N . GLU A 1 445 ? -2.166 42.838 28.748 1.00 24.74 ? 498 GLU A N 1 ATOM 3562 C CA . GLU A 1 445 ? -2.673 41.481 28.618 1.00 31.28 ? 498 GLU A CA 1 ATOM 3563 C C . GLU A 1 445 ? -2.358 40.668 29.874 1.00 30.37 ? 498 GLU A C 1 ATOM 3564 O O . GLU A 1 445 ? -2.674 39.484 29.947 1.00 29.01 ? 498 GLU A O 1 ATOM 3565 C CB . GLU A 1 445 ? -2.089 40.807 27.376 1.00 35.17 ? 498 GLU A CB 1 ATOM 3566 C CG . GLU A 1 445 ? -2.924 39.648 26.846 1.00 41.37 ? 498 GLU A CG 1 ATOM 3567 C CD . GLU A 1 445 ? -3.620 39.963 25.526 1.00 46.53 ? 498 GLU A CD 1 ATOM 3568 O OE1 . GLU A 1 445 ? -2.940 40.434 24.582 1.00 48.58 ? 498 GLU A OE1 1 ATOM 3569 O OE2 . GLU A 1 445 ? -4.847 39.732 25.430 1.00 43.29 ? 498 GLU A OE2 1 ATOM 3570 N N . LEU A 1 446 ? -1.761 41.313 30.873 1.00 27.14 ? 499 LEU A N 1 ATOM 3571 C CA . LEU A 1 446 ? -1.535 40.650 32.154 1.00 26.20 ? 499 LEU A CA 1 ATOM 3572 C C . LEU A 1 446 ? -2.576 41.058 33.184 1.00 27.26 ? 499 LEU A C 1 ATOM 3573 O O . LEU A 1 446 ? -2.929 42.230 33.289 1.00 26.58 ? 499 LEU A O 1 ATOM 3574 C CB . LEU A 1 446 ? -0.130 40.954 32.675 1.00 26.28 ? 499 LEU A CB 1 ATOM 3575 C CG . LEU A 1 446 ? 1.005 40.427 31.795 1.00 26.02 ? 499 LEU A CG 1 ATOM 3576 C CD1 . LEU A 1 446 ? 2.321 41.066 32.205 1.00 28.20 ? 499 LEU A CD1 1 ATOM 3577 C CD2 . LEU A 1 446 ? 1.107 38.899 31.859 1.00 29.08 ? 499 LEU A CD2 1 ATOM 3578 N N . ASN A 1 447 ? -3.070 40.082 33.941 1.00 28.44 ? 500 ASN A N 1 ATOM 3579 C CA . ASN A 1 447 ? -3.855 40.370 35.131 1.00 30.93 ? 500 ASN A CA 1 ATOM 3580 C C . ASN A 1 447 ? -3.571 39.363 36.230 1.00 30.57 ? 500 ASN A C 1 ATOM 3581 O O . ASN A 1 447 ? -3.693 38.146 36.037 1.00 25.12 ? 500 ASN A O 1 ATOM 3582 C CB . ASN A 1 447 ? -5.357 40.383 34.814 1.00 38.40 ? 500 ASN A CB 1 ATOM 3583 C CG . ASN A 1 447 ? -6.134 41.403 35.658 1.00 44.92 ? 500 ASN A CG 1 ATOM 3584 O OD1 . ASN A 1 447 ? -7.222 41.109 36.155 1.00 51.49 ? 500 ASN A OD1 1 ATOM 3585 N ND2 . ASN A 1 447 ? -5.580 42.605 35.812 1.00 44.39 ? 500 ASN A ND2 1 ATOM 3586 N N . TYR A 1 448 ? -3.201 39.890 37.391 1.00 29.45 ? 501 TYR A N 1 ATOM 3587 C CA . TYR A 1 448 ? -2.644 39.087 38.463 1.00 29.10 ? 501 TYR A CA 1 ATOM 3588 C C . TYR A 1 448 ? -3.688 38.920 39.555 1.00 33.09 ? 501 TYR A C 1 ATOM 3589 O O . TYR A 1 448 ? -4.409 39.864 39.894 1.00 34.64 ? 501 TYR A O 1 ATOM 3590 C CB . TYR A 1 448 ? -1.390 39.756 39.031 1.00 25.42 ? 501 TYR A CB 1 ATOM 3591 C CG . TYR A 1 448 ? -0.253 39.870 38.041 1.00 19.18 ? 501 TYR A CG 1 ATOM 3592 C CD1 . TYR A 1 448 ? 0.159 38.763 37.319 1.00 19.37 ? 501 TYR A CD1 1 ATOM 3593 C CD2 . TYR A 1 448 ? 0.427 41.062 37.851 1.00 18.12 ? 501 TYR A CD2 1 ATOM 3594 C CE1 . TYR A 1 448 ? 1.192 38.837 36.439 1.00 17.14 ? 501 TYR A CE1 1 ATOM 3595 C CE2 . TYR A 1 448 ? 1.462 41.150 36.953 1.00 17.19 ? 501 TYR A CE2 1 ATOM 3596 C CZ . TYR A 1 448 ? 1.840 40.033 36.249 1.00 18.22 ? 501 TYR A CZ 1 ATOM 3597 O OH . TYR A 1 448 ? 2.872 40.091 35.359 1.00 20.90 ? 501 TYR A OH 1 ATOM 3598 N N . LYS A 1 449 ? -3.768 37.710 40.096 1.00 31.21 ? 502 LYS A N 1 ATOM 3599 C CA . LYS A 1 449 ? -4.532 37.464 41.306 1.00 31.80 ? 502 LYS A CA 1 ATOM 3600 C C . LYS A 1 449 ? -3.600 37.397 42.514 1.00 33.44 ? 502 LYS A C 1 ATOM 3601 O O . LYS A 1 449 ? -2.575 36.710 42.476 1.00 29.89 ? 502 LYS A O 1 ATOM 3602 C CB . LYS A 1 449 ? -5.302 36.149 41.184 1.00 34.43 ? 502 LYS A CB 1 ATOM 3603 C CG . LYS A 1 449 ? -6.512 36.200 40.263 1.00 37.02 ? 502 LYS A CG 1 ATOM 3604 C CD . LYS A 1 449 ? -7.063 34.797 40.025 1.00 39.83 ? 502 LYS A CD 1 ATOM 3605 C CE . LYS A 1 449 ? -7.721 34.671 38.660 1.00 40.75 ? 502 LYS A CE 1 ATOM 3606 N NZ . LYS A 1 449 ? -7.292 33.433 37.947 1.00 38.86 ? 502 LYS A NZ 1 ATOM 3607 N N . GLU A 1 450 ? -3.965 38.094 43.586 1.00 29.54 ? 503 GLU A N 1 ATOM 3608 C CA . GLU A 1 450 ? -3.073 38.262 44.725 1.00 31.53 ? 503 GLU A CA 1 ATOM 3609 C C . GLU A 1 450 ? -2.917 36.972 45.526 1.00 29.67 ? 503 GLU A C 1 ATOM 3610 O O . GLU A 1 450 ? -1.941 36.805 46.252 1.00 32.08 ? 503 GLU A O 1 ATOM 3611 C CB . GLU A 1 450 ? -3.567 39.403 45.613 1.00 35.72 ? 503 GLU A CB 1 ATOM 3612 C CG . GLU A 1 450 ? -3.439 40.754 44.928 1.00 37.34 ? 503 GLU A CG 1 ATOM 3613 C CD . GLU A 1 450 ? -3.612 41.924 45.865 1.00 37.16 ? 503 GLU A CD 1 ATOM 3614 O OE1 . GLU A 1 450 ? -4.097 42.966 45.394 1.00 39.16 ? 503 GLU A OE1 1 ATOM 3615 O OE2 . GLU A 1 450 ? -3.252 41.811 47.062 1.00 41.97 ? 503 GLU A OE2 1 ATOM 3616 N N . ASP A 1 451 ? -3.860 36.053 45.358 1.00 28.60 ? 504 ASP A N 1 ATOM 3617 C CA . ASP A 1 451 ? -3.817 34.763 46.042 1.00 31.16 ? 504 ASP A CA 1 ATOM 3618 C C . ASP A 1 451 ? -3.309 33.615 45.161 1.00 22.98 ? 504 ASP A C 1 ATOM 3619 O O . ASP A 1 451 ? -3.358 32.466 45.565 1.00 25.14 ? 504 ASP A O 1 ATOM 3620 C CB . ASP A 1 451 ? -5.209 34.412 46.601 1.00 34.39 ? 504 ASP A CB 1 ATOM 3621 C CG . ASP A 1 451 ? -6.285 34.314 45.516 1.00 38.83 ? 504 ASP A CG 1 ATOM 3622 O OD1 . ASP A 1 451 ? -7.228 33.507 45.679 1.00 43.77 ? 504 ASP A OD1 1 ATOM 3623 O OD2 . ASP A 1 451 ? -6.289 35.000 44.476 1.00 39.95 ? 504 ASP A OD2 1 ATOM 3624 N N . GLU A 1 452 ? -2.830 33.918 43.960 1.00 22.91 ? 505 GLU A N 1 ATOM 3625 C CA . GLU A 1 452 ? -2.396 32.877 43.032 1.00 26.68 ? 505 GLU A CA 1 ATOM 3626 C C . GLU A 1 452 ? -1.021 33.181 42.438 1.00 24.63 ? 505 GLU A C 1 ATOM 3627 O O . GLU A 1 452 ? -0.888 33.373 41.231 1.00 21.21 ? 505 GLU A O 1 ATOM 3628 C CB . GLU A 1 452 ? -3.412 32.702 41.893 1.00 29.96 ? 505 GLU A CB 1 ATOM 3629 C CG . GLU A 1 452 ? -4.844 32.446 42.350 1.00 33.98 ? 505 GLU A CG 1 ATOM 3630 C CD . GLU A 1 452 ? -4.975 31.328 43.371 1.00 37.64 ? 505 GLU A CD 1 ATOM 3631 O OE1 . GLU A 1 452 ? -4.124 30.415 43.398 1.00 39.04 ? 505 GLU A OE1 1 ATOM 3632 O OE2 . GLU A 1 452 ? -5.953 31.352 44.149 1.00 44.86 ? 505 GLU A OE2 1 ATOM 3633 N N . TYR A 1 453 ? 0.003 33.219 43.282 1.00 21.47 ? 506 TYR A N 1 ATOM 3634 C CA . TYR A 1 453 ? 1.368 33.400 42.794 1.00 17.34 ? 506 TYR A CA 1 ATOM 3635 C C . TYR A 1 453 ? 1.706 32.467 41.616 1.00 17.32 ? 506 TYR A C 1 ATOM 3636 O O . TYR A 1 453 ? 2.212 32.920 40.589 1.00 19.24 ? 506 TYR A O 1 ATOM 3637 C CB . TYR A 1 453 ? 2.377 33.190 43.926 1.00 19.85 ? 506 TYR A CB 1 ATOM 3638 C CG . TYR A 1 453 ? 3.792 33.437 43.487 1.00 20.77 ? 506 TYR A CG 1 ATOM 3639 C CD1 . TYR A 1 453 ? 4.744 32.432 43.538 1.00 21.25 ? 506 TYR A CD1 1 ATOM 3640 C CD2 . TYR A 1 453 ? 4.172 34.679 42.988 1.00 22.10 ? 506 TYR A CD2 1 ATOM 3641 C CE1 . TYR A 1 453 ? 6.037 32.664 43.119 1.00 22.74 ? 506 TYR A CE1 1 ATOM 3642 C CE2 . TYR A 1 453 ? 5.454 34.914 42.568 1.00 18.40 ? 506 TYR A CE2 1 ATOM 3643 C CZ . TYR A 1 453 ? 6.383 33.909 42.635 1.00 21.49 ? 506 TYR A CZ 1 ATOM 3644 O OH . TYR A 1 453 ? 7.667 34.157 42.215 1.00 20.85 ? 506 TYR A OH 1 ATOM 3645 N N . PHE A 1 454 ? 1.444 31.174 41.762 1.00 19.98 ? 507 PHE A N 1 ATOM 3646 C CA . PHE A 1 454 ? 1.836 30.195 40.730 1.00 23.13 ? 507 PHE A CA 1 ATOM 3647 C C . PHE A 1 454 ? 1.202 30.486 39.376 1.00 24.12 ? 507 PHE A C 1 ATOM 3648 O O . PHE A 1 454 ? 1.869 30.439 38.345 1.00 23.44 ? 507 PHE A O 1 ATOM 3649 C CB . PHE A 1 454 ? 1.487 28.768 41.156 1.00 23.73 ? 507 PHE A CB 1 ATOM 3650 C CG . PHE A 1 454 ? 2.154 27.699 40.317 1.00 25.08 ? 507 PHE A CG 1 ATOM 3651 C CD1 . PHE A 1 454 ? 1.546 27.211 39.174 1.00 26.43 ? 507 PHE A CD1 1 ATOM 3652 C CD2 . PHE A 1 454 ? 3.390 27.182 40.687 1.00 26.86 ? 507 PHE A CD2 1 ATOM 3653 C CE1 . PHE A 1 454 ? 2.165 26.221 38.413 1.00 28.94 ? 507 PHE A CE1 1 ATOM 3654 C CE2 . PHE A 1 454 ? 4.007 26.192 39.928 1.00 25.95 ? 507 PHE A CE2 1 ATOM 3655 C CZ . PHE A 1 454 ? 3.391 25.724 38.790 1.00 28.14 ? 507 PHE A CZ 1 ATOM 3656 N N . GLU A 1 455 ? -0.089 30.807 39.378 1.00 25.93 ? 508 GLU A N 1 ATOM 3657 C CA . GLU A 1 455 ? -0.768 31.162 38.142 1.00 27.35 ? 508 GLU A CA 1 ATOM 3658 C C . GLU A 1 455 ? -0.140 32.420 37.573 1.00 23.70 ? 508 GLU A C 1 ATOM 3659 O O . GLU A 1 455 ? -0.035 32.584 36.356 1.00 23.18 ? 508 GLU A O 1 ATOM 3660 C CB . GLU A 1 455 ? -2.260 31.388 38.393 1.00 31.27 ? 508 GLU A CB 1 ATOM 3661 C CG . GLU A 1 455 ? -3.045 30.117 38.675 1.00 36.97 ? 508 GLU A CG 1 ATOM 3662 C CD . GLU A 1 455 ? -2.947 29.676 40.123 1.00 39.56 ? 508 GLU A CD 1 ATOM 3663 O OE1 . GLU A 1 455 ? -2.339 30.404 40.939 1.00 45.32 ? 508 GLU A OE1 1 ATOM 3664 O OE2 . GLU A 1 455 ? -3.471 28.586 40.442 1.00 44.45 ? 508 GLU A OE2 1 ATOM 3665 N N . ASN A 1 456 ? 0.288 33.323 38.454 1.00 21.68 ? 509 ASN A N 1 ATOM 3666 C CA . ASN A 1 456 ? 0.872 34.587 38.002 1.00 22.00 ? 509 ASN A CA 1 ATOM 3667 C C . ASN A 1 456 ? 2.204 34.329 37.293 1.00 19.41 ? 509 ASN A C 1 ATOM 3668 O O . ASN A 1 456 ? 2.502 34.922 36.257 1.00 21.23 ? 509 ASN A O 1 ATOM 3669 C CB . ASN A 1 456 ? 1.082 35.565 39.174 1.00 20.60 ? 509 ASN A CB 1 ATOM 3670 C CG . ASN A 1 456 ? -0.223 36.071 39.772 1.00 21.67 ? 509 ASN A CG 1 ATOM 3671 O OD1 . ASN A 1 456 ? -0.249 36.550 40.910 1.00 21.77 ? 509 ASN A OD1 1 ATOM 3672 N ND2 . ASN A 1 456 ? -1.307 35.959 39.015 1.00 16.44 ? 509 ASN A ND2 1 ATOM 3673 N N . ILE A 1 457 ? 3.014 33.450 37.862 1.00 20.54 ? 510 ILE A N 1 ATOM 3674 C CA . ILE A 1 457 ? 4.313 33.135 37.273 1.00 21.37 ? 510 ILE A CA 1 ATOM 3675 C C . ILE A 1 457 ? 4.124 32.401 35.959 1.00 19.22 ? 510 ILE A C 1 ATOM 3676 O O . ILE A 1 457 ? 4.848 32.637 34.988 1.00 17.68 ? 510 ILE A O 1 ATOM 3677 C CB . ILE A 1 457 ? 5.163 32.285 38.245 1.00 26.13 ? 510 ILE A CB 1 ATOM 3678 C CG1 . ILE A 1 457 ? 4.619 30.861 38.326 1.00 30.48 ? 510 ILE A CG1 1 ATOM 3679 C CG2 . ILE A 1 457 ? 5.168 32.943 39.621 1.00 26.85 ? 510 ILE A CG2 1 ATOM 3680 C CD1 . ILE A 1 457 ? 4.557 30.313 39.735 1.00 36.22 ? 510 ILE A CD1 1 ATOM 3681 N N . ILE A 1 458 ? 3.153 31.499 35.925 1.00 21.69 ? 511 ILE A N 1 ATOM 3682 C CA . ILE A 1 458 ? 2.877 30.787 34.691 1.00 26.17 ? 511 ILE A CA 1 ATOM 3683 C C . ILE A 1 458 ? 2.430 31.786 33.634 1.00 24.49 ? 511 ILE A C 1 ATOM 3684 O O . ILE A 1 458 ? 3.000 31.844 32.543 1.00 26.21 ? 511 ILE A O 1 ATOM 3685 C CB . ILE A 1 458 ? 1.838 29.685 34.918 1.00 26.65 ? 511 ILE A CB 1 ATOM 3686 C CG1 . ILE A 1 458 ? 2.433 28.578 35.794 1.00 25.89 ? 511 ILE A CG1 1 ATOM 3687 C CG2 . ILE A 1 458 ? 1.349 29.125 33.587 1.00 27.03 ? 511 ILE A CG2 1 ATOM 3688 C CD1 . ILE A 1 458 ? 3.811 28.085 35.361 1.00 26.44 ? 511 ILE A CD1 1 ATOM 3689 N N . GLN A 1 459 ? 1.450 32.617 33.974 1.00 21.77 ? 512 GLN A N 1 ATOM 3690 C CA . GLN A 1 459 ? 1.024 33.669 33.068 1.00 22.32 ? 512 GLN A CA 1 ATOM 3691 C C . GLN A 1 459 ? 2.223 34.414 32.514 1.00 26.14 ? 512 GLN A C 1 ATOM 3692 O O . GLN A 1 459 ? 2.291 34.684 31.312 1.00 24.39 ? 512 GLN A O 1 ATOM 3693 C CB . GLN A 1 459 ? 0.072 34.647 33.770 1.00 27.59 ? 512 GLN A CB 1 ATOM 3694 C CG . GLN A 1 459 ? -0.755 35.477 32.824 1.00 28.62 ? 512 GLN A CG 1 ATOM 3695 C CD . GLN A 1 459 ? -1.635 36.504 33.537 1.00 30.58 ? 512 GLN A CD 1 ATOM 3696 O OE1 . GLN A 1 459 ? -1.913 37.564 32.987 1.00 30.53 ? 512 GLN A OE1 1 ATOM 3697 N NE2 . GLN A 1 459 ? -2.073 36.185 34.752 1.00 27.76 ? 512 GLN A NE2 1 ATOM 3698 N N . ASN A 1 460 ? 3.180 34.764 33.373 1.00 20.42 ? 513 ASN A N 1 ATOM 3699 C CA . ASN A 1 460 ? 4.331 35.510 32.883 1.00 20.86 ? 513 ASN A CA 1 ATOM 3700 C C . ASN A 1 460 ? 5.151 34.706 31.870 1.00 19.35 ? 513 ASN A C 1 ATOM 3701 O O . ASN A 1 460 ? 5.569 35.240 30.850 1.00 20.46 ? 513 ASN A O 1 ATOM 3702 C CB . ASN A 1 460 ? 5.219 35.986 34.038 1.00 20.68 ? 513 ASN A CB 1 ATOM 3703 C CG . ASN A 1 460 ? 4.653 37.213 34.723 1.00 23.03 ? 513 ASN A CG 1 ATOM 3704 O OD1 . ASN A 1 460 ? 3.776 37.889 34.172 1.00 23.12 ? 513 ASN A OD1 1 ATOM 3705 N ND2 . ASN A 1 460 ? 5.121 37.493 35.934 1.00 21.91 ? 513 ASN A ND2 1 ATOM 3706 N N . LEU A 1 461 ? 5.387 33.429 32.150 1.00 22.25 ? 514 LEU A N 1 ATOM 3707 C CA . LEU A 1 461 ? 6.120 32.588 31.211 1.00 20.42 ? 514 LEU A CA 1 ATOM 3708 C C . LEU A 1 461 ? 5.392 32.574 29.865 1.00 23.18 ? 514 LEU A C 1 ATOM 3709 O O . LEU A 1 461 ? 6.010 32.771 28.830 1.00 19.93 ? 514 LEU A O 1 ATOM 3710 C CB . LEU A 1 461 ? 6.220 31.156 31.726 1.00 20.33 ? 514 LEU A CB 1 ATOM 3711 C CG . LEU A 1 461 ? 7.054 30.905 32.978 1.00 20.06 ? 514 LEU A CG 1 ATOM 3712 C CD1 . LEU A 1 461 ? 6.965 29.446 33.340 1.00 20.71 ? 514 LEU A CD1 1 ATOM 3713 C CD2 . LEU A 1 461 ? 8.496 31.327 32.765 1.00 20.76 ? 514 LEU A CD2 1 ATOM 3714 N N . LYS A 1 462 ? 4.084 32.316 29.884 1.00 24.35 ? 515 LYS A N 1 ATOM 3715 C CA . LYS A 1 462 ? 3.299 32.281 28.639 1.00 28.77 ? 515 LYS A CA 1 ATOM 3716 C C . LYS A 1 462 ? 3.399 33.612 27.898 1.00 29.83 ? 515 LYS A C 1 ATOM 3717 O O . LYS A 1 462 ? 3.577 33.656 26.678 1.00 29.59 ? 515 LYS A O 1 ATOM 3718 C CB . LYS A 1 462 ? 1.828 31.971 28.922 1.00 31.39 ? 515 LYS A CB 1 ATOM 3719 C CG . LYS A 1 462 ? 1.532 30.529 29.305 1.00 36.09 ? 515 LYS A CG 1 ATOM 3720 C CD . LYS A 1 462 ? 0.028 30.315 29.519 1.00 37.99 ? 515 LYS A CD 1 ATOM 3721 C CE . LYS A 1 462 ? -0.274 28.957 30.143 1.00 40.36 ? 515 LYS A CE 1 ATOM 3722 N NZ . LYS A 1 462 ? -1.039 28.047 29.228 1.00 41.63 ? 515 LYS A NZ 1 ATOM 3723 N N . PHE A 1 463 ? 3.281 34.704 28.640 1.00 32.17 ? 516 PHE A N 1 ATOM 3724 C CA . PHE A 1 463 ? 3.271 36.025 28.037 1.00 32.08 ? 516 PHE A CA 1 ATOM 3725 C C . PHE A 1 463 ? 4.596 36.302 27.339 1.00 33.62 ? 516 PHE A C 1 ATOM 3726 O O . PHE A 1 463 ? 4.619 36.696 26.175 1.00 34.35 ? 516 PHE A O 1 ATOM 3727 C CB . PHE A 1 463 ? 3.003 37.093 29.097 1.00 30.02 ? 516 PHE A CB 1 ATOM 3728 C CG . PHE A 1 463 ? 2.882 38.478 28.542 1.00 31.12 ? 516 PHE A CG 1 ATOM 3729 C CD1 . PHE A 1 463 ? 3.940 39.369 28.627 1.00 30.58 ? 516 PHE A CD1 1 ATOM 3730 C CD2 . PHE A 1 463 ? 1.710 38.893 27.931 1.00 35.57 ? 516 PHE A CD2 1 ATOM 3731 C CE1 . PHE A 1 463 ? 3.828 40.645 28.117 1.00 31.67 ? 516 PHE A CE1 1 ATOM 3732 C CE2 . PHE A 1 463 ? 1.595 40.172 27.420 1.00 36.26 ? 516 PHE A CE2 1 ATOM 3733 C CZ . PHE A 1 463 ? 2.654 41.050 27.522 1.00 31.91 ? 516 PHE A CZ 1 ATOM 3734 N N . SER A 1 464 ? 5.697 36.110 28.056 1.00 30.66 ? 517 SER A N 1 ATOM 3735 C CA . SER A 1 464 ? 6.998 36.540 27.567 1.00 32.73 ? 517 SER A CA 1 ATOM 3736 C C . SER A 1 464 ? 7.407 35.724 26.345 1.00 30.97 ? 517 SER A C 1 ATOM 3737 O O . SER A 1 464 ? 8.109 36.219 25.467 1.00 30.31 ? 517 SER A O 1 ATOM 3738 C CB . SER A 1 464 ? 8.061 36.399 28.659 1.00 34.62 ? 517 SER A CB 1 ATOM 3739 O OG . SER A 1 464 ? 7.602 36.954 29.881 1.00 36.29 ? 517 SER A OG 1 ATOM 3740 N N . GLN A 1 465 ? 6.960 34.475 26.293 1.00 29.36 ? 518 GLN A N 1 ATOM 3741 C CA . GLN A 1 465 ? 7.330 33.591 25.194 1.00 33.02 ? 518 GLN A CA 1 ATOM 3742 C C . GLN A 1 465 ? 6.454 33.825 23.959 1.00 33.11 ? 518 GLN A C 1 ATOM 3743 O O . GLN A 1 465 ? 6.949 33.836 22.832 1.00 30.41 ? 518 GLN A O 1 ATOM 3744 C CB . GLN A 1 465 ? 7.244 32.131 25.630 1.00 33.28 ? 518 GLN A CB 1 ATOM 3745 C CG . GLN A 1 465 ? 7.634 31.144 24.538 1.00 35.47 ? 518 GLN A CG 1 ATOM 3746 C CD . GLN A 1 465 ? 9.107 31.206 24.157 1.00 35.50 ? 518 GLN A CD 1 ATOM 3747 O OE1 . GLN A 1 465 ? 9.861 32.034 24.669 1.00 33.60 ? 518 GLN A OE1 1 ATOM 3748 N NE2 . GLN A 1 465 ? 9.514 30.327 23.255 1.00 38.28 ? 518 GLN A NE2 1 ATOM 3749 N N . SER A 1 466 ? 5.154 34.008 24.171 1.00 31.44 ? 519 SER A N 1 ATOM 3750 C CA . SER A 1 466 ? 4.275 34.447 23.088 1.00 35.92 ? 519 SER A CA 1 ATOM 3751 C C . SER A 1 466 ? 4.777 35.772 22.512 1.00 36.42 ? 519 SER A C 1 ATOM 3752 O O . SER A 1 466 ? 4.766 35.976 21.301 1.00 39.32 ? 519 SER A O 1 ATOM 3753 C CB . SER A 1 466 ? 2.831 34.587 23.580 1.00 34.45 ? 519 SER A CB 1 ATOM 3754 O OG . SER A 1 466 ? 2.002 35.130 22.568 1.00 39.75 ? 519 SER A OG 1 ATOM 3755 N N . LYS A 1 467 ? 5.237 36.654 23.392 1.00 35.93 ? 520 LYS A N 1 ATOM 3756 C CA . LYS A 1 467 ? 5.782 37.948 23.000 1.00 36.13 ? 520 LYS A CA 1 ATOM 3757 C C . LYS A 1 467 ? 7.018 37.828 22.111 1.00 35.14 ? 520 LYS A C 1 ATOM 3758 O O . LYS A 1 467 ? 7.183 38.597 21.158 1.00 35.12 ? 520 LYS A O 1 ATOM 3759 C CB . LYS A 1 467 ? 6.146 38.753 24.255 1.00 39.99 ? 520 LYS A CB 1 ATOM 3760 C CG . LYS A 1 467 ? 5.589 40.168 24.294 1.00 43.79 ? 520 LYS A CG 1 ATOM 3761 C CD . LYS A 1 467 ? 6.378 41.054 25.258 1.00 45.96 ? 520 LYS A CD 1 ATOM 3762 C CE . LYS A 1 467 ? 5.488 41.632 26.362 1.00 48.85 ? 520 LYS A CE 1 ATOM 3763 N NZ . LYS A 1 467 ? 5.346 43.129 26.296 1.00 49.50 ? 520 LYS A NZ 1 ATOM 3764 N N . GLN A 1 468 ? 7.907 36.896 22.448 1.00 31.98 ? 521 GLN A N 1 ATOM 3765 C CA . GLN A 1 468 ? 9.173 36.764 21.739 1.00 30.03 ? 521 GLN A CA 1 ATOM 3766 C C . GLN A 1 468 ? 8.896 36.152 20.374 1.00 28.29 ? 521 GLN A C 1 ATOM 3767 O O . GLN A 1 468 ? 9.456 36.575 19.369 1.00 31.69 ? 521 GLN A O 1 ATOM 3768 C CB . GLN A 1 468 ? 10.162 35.899 22.538 1.00 33.66 ? 521 GLN A CB 1 ATOM 3769 C CG . GLN A 1 468 ? 11.600 35.911 22.016 1.00 35.44 ? 521 GLN A CG 1 ATOM 3770 C CD . GLN A 1 468 ? 12.109 37.310 21.690 1.00 41.06 ? 521 GLN A CD 1 ATOM 3771 O OE1 . GLN A 1 468 ? 11.830 38.269 22.416 1.00 41.25 ? 521 GLN A OE1 1 ATOM 3772 N NE2 . GLN A 1 468 ? 12.868 37.429 20.599 1.00 43.11 ? 521 GLN A NE2 1 ATOM 3773 N N . LEU A 1 469 ? 8.003 35.174 20.340 1.00 28.39 ? 522 LEU A N 1 ATOM 3774 C CA . LEU A 1 469 ? 7.746 34.428 19.118 1.00 32.30 ? 522 LEU A CA 1 ATOM 3775 C C . LEU A 1 469 ? 7.146 35.329 18.041 1.00 35.25 ? 522 LEU A C 1 ATOM 3776 O O . LEU A 1 469 ? 7.551 35.278 16.879 1.00 36.45 ? 522 LEU A O 1 ATOM 3777 C CB . LEU A 1 469 ? 6.812 33.260 19.409 1.00 30.96 ? 522 LEU A CB 1 ATOM 3778 C CG . LEU A 1 469 ? 7.427 32.152 20.255 1.00 30.46 ? 522 LEU A CG 1 ATOM 3779 C CD1 . LEU A 1 469 ? 6.393 31.127 20.578 1.00 29.86 ? 522 LEU A CD1 1 ATOM 3780 C CD2 . LEU A 1 469 ? 8.604 31.518 19.524 1.00 31.79 ? 522 LEU A CD2 1 ATOM 3781 N N . LYS A 1 470 ? 6.186 36.158 18.437 1.00 34.54 ? 523 LYS A N 1 ATOM 3782 C CA . LYS A 1 470 ? 5.418 36.958 17.493 1.00 37.19 ? 523 LYS A CA 1 ATOM 3783 C C . LYS A 1 470 ? 6.321 37.965 16.805 1.00 37.01 ? 523 LYS A C 1 ATOM 3784 O O . LYS A 1 470 ? 5.922 38.642 15.864 1.00 37.67 ? 523 LYS A O 1 ATOM 3785 C CB . LYS A 1 470 ? 4.285 37.693 18.214 1.00 39.61 ? 523 LYS A CB 1 ATOM 3786 C CG . LYS A 1 470 ? 4.599 39.152 18.530 1.00 42.27 ? 523 LYS A CG 1 ATOM 3787 C CD . LYS A 1 470 ? 3.314 39.960 18.773 1.00 44.32 ? 523 LYS A CD 1 ATOM 3788 C CE . LYS A 1 470 ? 2.112 39.057 19.019 1.00 44.69 ? 523 LYS A CE 1 ATOM 3789 N NZ . LYS A 1 470 ? 2.533 37.652 19.255 1.00 43.54 ? 523 LYS A NZ 1 ATOM 3790 N N . LYS A 1 471 ? 7.549 38.065 17.286 1.00 38.01 ? 524 LYS A N 1 ATOM 3791 C CA . LYS A 1 471 ? 8.490 39.031 16.740 1.00 34.79 ? 524 LYS A CA 1 ATOM 3792 C C . LYS A 1 471 ? 9.072 38.566 15.399 1.00 31.89 ? 524 LYS A C 1 ATOM 3793 O O . LYS A 1 471 ? 9.764 39.324 14.728 1.00 26.84 ? 524 LYS A O 1 ATOM 3794 C CB . LYS A 1 471 ? 9.617 39.295 17.740 1.00 39.54 ? 524 LYS A CB 1 ATOM 3795 C CG . LYS A 1 471 ? 9.361 40.479 18.664 1.00 41.48 ? 524 LYS A CG 1 ATOM 3796 C CD . LYS A 1 471 ? 10.650 41.226 18.995 1.00 44.79 ? 524 LYS A CD 1 ATOM 3797 C CE . LYS A 1 471 ? 11.090 40.993 20.444 1.00 46.71 ? 524 LYS A CE 1 ATOM 3798 N NZ . LYS A 1 471 ? 12.110 41.986 20.923 1.00 45.34 ? 524 LYS A NZ 1 ATOM 3799 N N . LEU A 1 472 ? 8.788 37.331 15.002 1.00 31.40 ? 525 LEU A N 1 ATOM 3800 C CA . LEU A 1 472 ? 9.473 36.745 13.846 1.00 32.43 ? 525 LEU A CA 1 ATOM 3801 C C . LEU A 1 472 ? 9.420 37.672 12.634 1.00 36.99 ? 525 LEU A C 1 ATOM 3802 O O . LEU A 1 472 ? 10.457 38.049 12.071 1.00 35.43 ? 525 LEU A O 1 ATOM 3803 C CB . LEU A 1 472 ? 8.870 35.397 13.474 1.00 31.55 ? 525 LEU A CB 1 ATOM 3804 C CG . LEU A 1 472 ? 9.683 34.675 12.397 1.00 29.61 ? 525 LEU A CG 1 ATOM 3805 C CD1 . LEU A 1 472 ? 11.172 34.743 12.740 1.00 29.76 ? 525 LEU A CD1 1 ATOM 3806 C CD2 . LEU A 1 472 ? 9.236 33.253 12.235 1.00 27.92 ? 525 LEU A CD2 1 ATOM 3807 N N . ARG A 1 473 ? 8.205 38.045 12.242 1.00 37.41 ? 526 ARG A N 1 ATOM 3808 C CA . ARG A 1 473 ? 7.997 38.756 10.987 1.00 39.49 ? 526 ARG A CA 1 ATOM 3809 C C . ARG A 1 473 ? 8.074 40.259 11.182 1.00 40.59 ? 526 ARG A C 1 ATOM 3810 O O . ARG A 1 473 ? 7.836 41.024 10.245 1.00 43.51 ? 526 ARG A O 1 ATOM 3811 C CB . ARG A 1 473 ? 6.643 38.384 10.392 1.00 38.71 ? 526 ARG A CB 1 ATOM 3812 C CG . ARG A 1 473 ? 6.530 36.926 10.004 1.00 38.60 ? 526 ARG A CG 1 ATOM 3813 C CD . ARG A 1 473 ? 7.536 36.475 8.961 1.00 37.20 ? 526 ARG A CD 1 ATOM 3814 N NE . ARG A 1 473 ? 7.328 35.072 8.622 1.00 39.88 ? 526 ARG A NE 1 ATOM 3815 C CZ . ARG A 1 473 ? 8.271 34.145 8.659 1.00 40.15 ? 526 ARG A CZ 1 ATOM 3816 N NH1 . ARG A 1 473 ? 9.510 34.473 9.001 1.00 41.04 ? 526 ARG A NH1 1 ATOM 3817 N NH2 . ARG A 1 473 ? 7.981 32.890 8.339 1.00 41.26 ? 526 ARG A NH2 1 ATOM 3818 N N . GLU A 1 474 ? 8.405 40.681 12.401 1.00 41.04 ? 527 GLU A N 1 ATOM 3819 C CA . GLU A 1 474 ? 8.438 42.101 12.742 1.00 38.97 ? 527 GLU A CA 1 ATOM 3820 C C . GLU A 1 474 ? 9.867 42.621 12.807 1.00 37.83 ? 527 GLU A C 1 ATOM 3821 O O . GLU A 1 474 ? 10.801 41.863 13.051 1.00 39.06 ? 527 GLU A O 1 ATOM 3822 C CB . GLU A 1 474 ? 7.756 42.346 14.089 1.00 38.99 ? 527 GLU A CB 1 ATOM 3823 C CG . GLU A 1 474 ? 6.282 41.989 14.124 1.00 42.24 ? 527 GLU A CG 1 ATOM 3824 C CD . GLU A 1 474 ? 5.429 42.898 13.256 1.00 44.63 ? 527 GLU A CD 1 ATOM 3825 O OE1 . GLU A 1 474 ? 5.752 44.105 13.118 1.00 45.68 ? 527 GLU A OE1 1 ATOM 3826 O OE2 . GLU A 1 474 ? 4.425 42.396 12.711 1.00 47.56 ? 527 GLU A OE2 1 ATOM 3827 N N . LYS A 1 475 ? 10.032 43.921 12.606 1.00 36.91 ? 528 LYS A N 1 ATOM 3828 C CA . LYS A 1 475 ? 11.346 44.539 12.683 1.00 40.51 ? 528 LYS A CA 1 ATOM 3829 C C . LYS A 1 475 ? 11.794 44.676 14.136 1.00 41.07 ? 528 LYS A C 1 ATOM 3830 O O . LYS A 1 475 ? 10.971 44.711 15.052 1.00 37.91 ? 528 LYS A O 1 ATOM 3831 C CB . LYS A 1 475 ? 11.336 45.907 12.006 1.00 42.95 ? 528 LYS A CB 1 ATOM 3832 C CG . LYS A 1 475 ? 10.851 45.877 10.563 1.00 47.08 ? 528 LYS A CG 1 ATOM 3833 C CD . LYS A 1 475 ? 10.351 47.248 10.118 1.00 50.58 ? 528 LYS A CD 1 ATOM 3834 C CE . LYS A 1 475 ? 10.893 47.625 8.744 1.00 52.73 ? 528 LYS A CE 1 ATOM 3835 N NZ . LYS A 1 475 ? 10.884 49.102 8.516 1.00 53.97 ? 528 LYS A NZ 1 ATOM 3836 N N . VAL A 1 476 ? 13.102 44.753 14.340 1.00 40.55 ? 529 VAL A N 1 ATOM 3837 C CA . VAL A 1 476 ? 13.652 45.048 15.653 1.00 40.11 ? 529 VAL A CA 1 ATOM 3838 C C . VAL A 1 476 ? 13.389 46.505 16.030 1.00 40.88 ? 529 VAL A C 1 ATOM 3839 O O . VAL A 1 476 ? 13.583 47.415 15.225 1.00 38.66 ? 529 VAL A O 1 ATOM 3840 C CB . VAL A 1 476 ? 15.157 44.762 15.685 1.00 41.01 ? 529 VAL A CB 1 ATOM 3841 C CG1 . VAL A 1 476 ? 15.735 45.079 17.056 1.00 41.19 ? 529 VAL A CG1 1 ATOM 3842 C CG2 . VAL A 1 476 ? 15.414 43.311 15.309 1.00 40.83 ? 529 VAL A CG2 1 ATOM 3843 N N . ASP A 1 477 ? 12.934 46.723 17.258 1.00 42.48 ? 530 ASP A N 1 ATOM 3844 C CA . ASP A 1 477 ? 12.495 48.047 17.668 1.00 42.92 ? 530 ASP A CA 1 ATOM 3845 C C . ASP A 1 477 ? 13.644 48.893 18.209 1.00 46.51 ? 530 ASP A C 1 ATOM 3846 O O . ASP A 1 477 ? 14.225 48.582 19.251 1.00 44.43 ? 530 ASP A O 1 ATOM 3847 C CB . ASP A 1 477 ? 11.421 47.942 18.737 1.00 42.93 ? 530 ASP A CB 1 ATOM 3848 C CG . ASP A 1 477 ? 10.992 49.294 19.244 1.00 43.66 ? 530 ASP A CG 1 ATOM 3849 O OD1 . ASP A 1 477 ? 11.735 50.271 19.010 1.00 41.49 ? 530 ASP A OD1 1 ATOM 3850 O OD2 . ASP A 1 477 ? 9.935 49.476 19.874 1.00 46.46 ? 530 ASP A OD2 1 ATOM 3851 N N . LYS A 1 478 ? 13.959 49.977 17.509 1.00 49.22 ? 531 LYS A N 1 ATOM 3852 C CA . LYS A 1 478 ? 15.219 50.676 17.727 1.00 50.30 ? 531 LYS A CA 1 ATOM 3853 C C . LYS A 1 478 ? 15.159 51.525 18.995 1.00 46.43 ? 531 LYS A C 1 ATOM 3854 O O . LYS A 1 478 ? 16.177 52.026 19.464 1.00 43.83 ? 531 LYS A O 1 ATOM 3855 C CB . LYS A 1 478 ? 15.563 51.549 16.516 1.00 53.53 ? 531 LYS A CB 1 ATOM 3856 C CG . LYS A 1 478 ? 15.246 50.901 15.170 1.00 56.33 ? 531 LYS A CG 1 ATOM 3857 C CD . LYS A 1 478 ? 15.523 51.854 14.012 1.00 58.37 ? 531 LYS A CD 1 ATOM 3858 C CE . LYS A 1 478 ? 17.006 51.888 13.657 1.00 59.55 ? 531 LYS A CE 1 ATOM 3859 N NZ . LYS A 1 478 ? 17.359 50.902 12.598 1.00 60.33 ? 531 LYS A NZ 1 ATOM 3860 N N . ASP A 1 479 ? 13.961 51.674 19.549 1.00 44.49 ? 532 ASP A N 1 ATOM 3861 C CA . ASP A 1 479 ? 13.770 52.451 20.768 1.00 45.27 ? 532 ASP A CA 1 ATOM 3862 C C . ASP A 1 479 ? 14.112 51.643 22.016 1.00 40.41 ? 532 ASP A C 1 ATOM 3863 O O . ASP A 1 479 ? 14.337 52.204 23.086 1.00 39.62 ? 532 ASP A O 1 ATOM 3864 C CB . ASP A 1 479 ? 12.320 52.919 20.875 1.00 48.72 ? 532 ASP A CB 1 ATOM 3865 C CG . ASP A 1 479 ? 12.027 54.114 19.997 1.00 51.52 ? 532 ASP A CG 1 ATOM 3866 O OD1 . ASP A 1 479 ? 12.976 54.645 19.377 1.00 52.55 ? 532 ASP A OD1 1 ATOM 3867 O OD2 . ASP A 1 479 ? 10.875 54.584 19.868 1.00 51.90 ? 532 ASP A OD2 1 ATOM 3868 N N . GLU A 1 480 ? 14.114 50.325 21.881 1.00 34.42 ? 533 GLU A N 1 ATOM 3869 C CA . GLU A 1 480 ? 13.935 49.445 23.023 1.00 34.13 ? 533 GLU A CA 1 ATOM 3870 C C . GLU A 1 480 ? 15.242 49.349 23.797 1.00 27.77 ? 533 GLU A C 1 ATOM 3871 O O . GLU A 1 480 ? 16.295 49.162 23.205 1.00 26.26 ? 533 GLU A O 1 ATOM 3872 C CB . GLU A 1 480 ? 13.503 48.058 22.543 1.00 35.82 ? 533 GLU A CB 1 ATOM 3873 C CG . GLU A 1 480 ? 13.255 47.048 23.647 1.00 38.99 ? 533 GLU A CG 1 ATOM 3874 C CD . GLU A 1 480 ? 12.653 45.757 23.121 1.00 39.91 ? 533 GLU A CD 1 ATOM 3875 O OE1 . GLU A 1 480 ? 12.090 45.767 22.005 1.00 39.69 ? 533 GLU A OE1 1 ATOM 3876 O OE2 . GLU A 1 480 ? 12.748 44.729 23.820 1.00 41.50 ? 533 GLU A OE2 1 ATOM 3877 N N . TRP A 1 481 ? 15.169 49.465 25.120 1.00 27.23 ? 534 TRP A N 1 ATOM 3878 C CA . TRP A 1 481 ? 16.346 49.303 25.975 1.00 25.86 ? 534 TRP A CA 1 ATOM 3879 C C . TRP A 1 481 ? 16.591 47.827 26.270 1.00 25.94 ? 534 TRP A C 1 ATOM 3880 O O . TRP A 1 481 ? 15.643 47.046 26.350 1.00 25.68 ? 534 TRP A O 1 ATOM 3881 C CB . TRP A 1 481 ? 16.146 50.054 27.298 1.00 27.03 ? 534 TRP A CB 1 ATOM 3882 C CG . TRP A 1 481 ? 16.289 51.549 27.185 1.00 25.70 ? 534 TRP A CG 1 ATOM 3883 C CD1 . TRP A 1 481 ? 15.723 52.360 26.247 1.00 26.33 ? 534 TRP A CD1 1 ATOM 3884 C CD2 . TRP A 1 481 ? 17.025 52.411 28.062 1.00 25.24 ? 534 TRP A CD2 1 ATOM 3885 N NE1 . TRP A 1 481 ? 16.067 53.671 26.477 1.00 28.05 ? 534 TRP A NE1 1 ATOM 3886 C CE2 . TRP A 1 481 ? 16.870 53.729 27.586 1.00 25.01 ? 534 TRP A CE2 1 ATOM 3887 C CE3 . TRP A 1 481 ? 17.806 52.203 29.201 1.00 22.16 ? 534 TRP A CE3 1 ATOM 3888 C CZ2 . TRP A 1 481 ? 17.468 54.821 28.204 1.00 26.10 ? 534 TRP A CZ2 1 ATOM 3889 C CZ3 . TRP A 1 481 ? 18.399 53.290 29.809 1.00 22.75 ? 534 TRP A CZ3 1 ATOM 3890 C CH2 . TRP A 1 481 ? 18.229 54.581 29.309 1.00 25.43 ? 534 TRP A CH2 1 ATOM 3891 N N . ILE A 1 482 ? 17.856 47.450 26.451 1.00 26.58 ? 535 ILE A N 1 ATOM 3892 C CA . ILE A 1 482 ? 18.189 46.063 26.743 1.00 29.09 ? 535 ILE A CA 1 ATOM 3893 C C . ILE A 1 482 ? 18.287 45.784 28.240 1.00 26.79 ? 535 ILE A C 1 ATOM 3894 O O . ILE A 1 482 ? 18.532 44.649 28.628 1.00 26.22 ? 535 ILE A O 1 ATOM 3895 C CB . ILE A 1 482 ? 19.515 45.672 26.072 1.00 33.28 ? 535 ILE A CB 1 ATOM 3896 C CG1 . ILE A 1 482 ? 20.596 46.693 26.407 1.00 32.78 ? 535 ILE A CG1 1 ATOM 3897 C CG2 . ILE A 1 482 ? 19.330 45.556 24.570 1.00 37.63 ? 535 ILE A CG2 1 ATOM 3898 C CD1 . ILE A 1 482 ? 21.865 46.520 25.599 1.00 35.58 ? 535 ILE A CD1 1 ATOM 3899 N N . SER A 1 483 ? 18.092 46.812 29.067 1.00 23.22 ? 536 SER A N 1 ATOM 3900 C CA . SER A 1 483 ? 17.999 46.637 30.520 1.00 21.23 ? 536 SER A CA 1 ATOM 3901 C C . SER A 1 483 ? 16.980 47.582 31.137 1.00 21.51 ? 536 SER A C 1 ATOM 3902 O O . SER A 1 483 ? 16.845 48.728 30.713 1.00 21.70 ? 536 SER A O 1 ATOM 3903 C CB . SER A 1 483 ? 19.353 46.900 31.176 1.00 21.83 ? 536 SER A CB 1 ATOM 3904 O OG . SER A 1 483 ? 19.292 46.662 32.568 1.00 18.64 ? 536 SER A OG 1 ATOM 3905 N N . GLY A 1 484 ? 16.280 47.111 32.163 1.00 21.25 ? 537 GLY A N 1 ATOM 3906 C CA . GLY A 1 484 ? 15.586 48.005 33.068 1.00 23.53 ? 537 GLY A CA 1 ATOM 3907 C C . GLY A 1 484 ? 16.535 48.937 33.806 1.00 17.89 ? 537 GLY A C 1 ATOM 3908 O O . GLY A 1 484 ? 17.739 48.688 33.858 1.00 15.66 ? 537 GLY A O 1 ATOM 3909 N N . ALA A 1 485 ? 15.974 49.996 34.386 1.00 15.69 ? 538 ALA A N 1 ATOM 3910 C CA . ALA A 1 485 ? 16.745 51.023 35.077 1.00 15.83 ? 538 ALA A CA 1 ATOM 3911 C C . ALA A 1 485 ? 17.253 50.519 36.424 1.00 14.21 ? 538 ALA A C 1 ATOM 3912 O O . ALA A 1 485 ? 18.291 50.951 36.910 1.00 14.16 ? 538 ALA A O 1 ATOM 3913 C CB . ALA A 1 485 ? 15.905 52.271 35.259 1.00 17.40 ? 538 ALA A CB 1 ATOM 3914 N N . ALA A 1 486 ? 16.518 49.595 37.018 1.00 15.16 ? 539 ALA A N 1 ATOM 3915 C CA . ALA A 1 486 ? 16.746 49.217 38.403 1.00 14.43 ? 539 ALA A CA 1 ATOM 3916 C C . ALA A 1 486 ? 17.675 48.016 38.455 1.00 15.42 ? 539 ALA A C 1 ATOM 3917 O O . ALA A 1 486 ? 17.328 46.989 39.019 1.00 15.93 ? 539 ALA A O 1 ATOM 3918 C CB . ALA A 1 486 ? 15.425 48.903 39.089 1.00 15.65 ? 539 ALA A CB 1 ATOM 3919 N N . VAL A 1 487 ? 18.853 48.180 37.861 1.00 14.10 ? 540 VAL A N 1 ATOM 3920 C CA . VAL A 1 487 ? 19.799 47.094 37.655 1.00 16.40 ? 540 VAL A CA 1 ATOM 3921 C C . VAL A 1 487 ? 21.182 47.646 37.950 1.00 16.61 ? 540 VAL A C 1 ATOM 3922 O O . VAL A 1 487 ? 21.536 48.743 37.480 1.00 17.01 ? 540 VAL A O 1 ATOM 3923 C CB . VAL A 1 487 ? 19.732 46.569 36.210 1.00 19.32 ? 540 VAL A CB 1 ATOM 3924 C CG1 . VAL A 1 487 ? 20.847 45.550 35.922 1.00 22.08 ? 540 VAL A CG1 1 ATOM 3925 C CG2 . VAL A 1 487 ? 18.366 45.958 35.943 1.00 20.41 ? 540 VAL A CG2 1 ATOM 3926 N N . VAL A 1 488 ? 21.936 46.924 38.776 1.00 14.60 ? 541 VAL A N 1 ATOM 3927 C CA . VAL A 1 488 ? 23.320 47.283 39.060 1.00 13.28 ? 541 VAL A CA 1 ATOM 3928 C C . VAL A 1 488 ? 24.231 46.514 38.102 1.00 15.77 ? 541 VAL A C 1 ATOM 3929 O O . VAL A 1 488 ? 24.796 45.466 38.440 1.00 16.42 ? 541 VAL A O 1 ATOM 3930 C CB . VAL A 1 488 ? 23.712 47.004 40.535 1.00 12.90 ? 541 VAL A CB 1 ATOM 3931 C CG1 . VAL A 1 488 ? 25.096 47.503 40.803 1.00 16.57 ? 541 VAL A CG1 1 ATOM 3932 C CG2 . VAL A 1 488 ? 22.735 47.688 41.498 1.00 12.87 ? 541 VAL A CG2 1 ATOM 3933 N N . ASN A 1 489 ? 24.327 47.034 36.886 1.00 16.89 ? 542 ASN A N 1 ATOM 3934 C CA . ASN A 1 489 ? 25.127 46.443 35.833 1.00 16.13 ? 542 ASN A CA 1 ATOM 3935 C C . ASN A 1 489 ? 25.184 47.437 34.687 1.00 18.75 ? 542 ASN A C 1 ATOM 3936 O O . ASN A 1 489 ? 24.523 48.475 34.730 1.00 16.70 ? 542 ASN A O 1 ATOM 3937 C CB . ASN A 1 489 ? 24.515 45.110 35.373 1.00 17.28 ? 542 ASN A CB 1 ATOM 3938 C CG . ASN A 1 489 ? 25.573 44.080 35.020 1.00 16.44 ? 542 ASN A CG 1 ATOM 3939 O OD1 . ASN A 1 489 ? 26.716 44.437 34.736 1.00 14.97 ? 542 ASN A OD1 1 ATOM 3940 N ND2 . ASN A 1 489 ? 25.195 42.805 35.014 1.00 14.97 ? 542 ASN A ND2 1 ATOM 3941 N N . ALA A 1 490 ? 25.979 47.134 33.671 1.00 16.11 ? 543 ALA A N 1 ATOM 3942 C CA . ALA A 1 490 ? 25.908 47.873 32.418 1.00 15.29 ? 543 ALA A CA 1 ATOM 3943 C C . ALA A 1 490 ? 26.008 46.871 31.283 1.00 16.80 ? 543 ALA A C 1 ATOM 3944 O O . ALA A 1 490 ? 26.240 45.678 31.519 1.00 16.33 ? 543 ALA A O 1 ATOM 3945 C CB . ALA A 1 490 ? 27.021 48.895 32.328 1.00 12.92 ? 543 ALA A CB 1 ATOM 3946 N N . PHE A 1 491 ? 25.841 47.345 30.058 1.00 14.80 ? 544 PHE A N 1 ATOM 3947 C CA . PHE A 1 491 ? 25.625 46.436 28.932 1.00 16.03 ? 544 PHE A CA 1 ATOM 3948 C C . PHE A 1 491 ? 26.198 46.986 27.633 1.00 18.09 ? 544 PHE A C 1 ATOM 3949 O O . PHE A 1 491 ? 26.248 48.204 27.422 1.00 17.21 ? 544 PHE A O 1 ATOM 3950 C CB . PHE A 1 491 ? 24.139 46.143 28.745 1.00 18.55 ? 544 PHE A CB 1 ATOM 3951 C CG . PHE A 1 491 ? 23.465 45.605 29.975 1.00 20.55 ? 544 PHE A CG 1 ATOM 3952 C CD1 . PHE A 1 491 ? 23.350 44.240 30.179 1.00 23.38 ? 544 PHE A CD1 1 ATOM 3953 C CD2 . PHE A 1 491 ? 22.955 46.465 30.927 1.00 22.35 ? 544 PHE A CD2 1 ATOM 3954 C CE1 . PHE A 1 491 ? 22.724 43.748 31.319 1.00 25.38 ? 544 PHE A CE1 1 ATOM 3955 C CE2 . PHE A 1 491 ? 22.331 45.976 32.065 1.00 25.24 ? 544 PHE A CE2 1 ATOM 3956 C CZ . PHE A 1 491 ? 22.211 44.621 32.254 1.00 22.55 ? 544 PHE A CZ 1 ATOM 3957 N N . TYR A 1 492 ? 26.611 46.068 26.765 1.00 16.66 ? 545 TYR A N 1 ATOM 3958 C CA . TYR A 1 492 ? 26.811 46.350 25.350 1.00 21.16 ? 545 TYR A CA 1 ATOM 3959 C C . TYR A 1 492 ? 26.025 45.357 24.519 1.00 21.35 ? 545 TYR A C 1 ATOM 3960 O O . TYR A 1 492 ? 25.982 44.173 24.839 1.00 21.10 ? 545 TYR A O 1 ATOM 3961 C CB . TYR A 1 492 ? 28.288 46.240 24.977 1.00 18.16 ? 545 TYR A CB 1 ATOM 3962 C CG . TYR A 1 492 ? 28.532 46.410 23.502 1.00 18.23 ? 545 TYR A CG 1 ATOM 3963 C CD1 . TYR A 1 492 ? 28.500 47.671 22.930 1.00 20.91 ? 545 TYR A CD1 1 ATOM 3964 C CD2 . TYR A 1 492 ? 28.788 45.316 22.674 1.00 19.18 ? 545 TYR A CD2 1 ATOM 3965 C CE1 . TYR A 1 492 ? 28.715 47.850 21.601 1.00 23.22 ? 545 TYR A CE1 1 ATOM 3966 C CE2 . TYR A 1 492 ? 28.994 45.488 21.324 1.00 20.98 ? 545 TYR A CE2 1 ATOM 3967 C CZ . TYR A 1 492 ? 28.960 46.772 20.796 1.00 22.42 ? 545 TYR A CZ 1 ATOM 3968 O OH . TYR A 1 492 ? 29.169 47.017 19.462 1.00 25.47 ? 545 TYR A OH 1 ATOM 3969 N N . SER A 1 493 ? 25.393 45.852 23.461 1.00 22.61 ? 546 SER A N 1 ATOM 3970 C CA . SER A 1 493 ? 24.719 45.005 22.489 1.00 21.69 ? 546 SER A CA 1 ATOM 3971 C C . SER A 1 493 ? 25.371 45.122 21.120 1.00 22.93 ? 546 SER A C 1 ATOM 3972 O O . SER A 1 493 ? 25.493 46.226 20.567 1.00 18.85 ? 546 SER A O 1 ATOM 3973 C CB . SER A 1 493 ? 23.260 45.420 22.360 1.00 23.54 ? 546 SER A CB 1 ATOM 3974 O OG . SER A 1 493 ? 22.652 44.807 21.234 1.00 25.77 ? 546 SER A OG 1 ATOM 3975 N N . SER A 1 494 ? 25.761 43.984 20.559 1.00 23.06 ? 547 SER A N 1 ATOM 3976 C CA . SER A 1 494 ? 26.435 43.984 19.262 1.00 28.65 ? 547 SER A CA 1 ATOM 3977 C C . SER A 1 494 ? 25.430 44.139 18.115 1.00 25.59 ? 547 SER A C 1 ATOM 3978 O O . SER A 1 494 ? 25.682 44.853 17.146 1.00 26.90 ? 547 SER A O 1 ATOM 3979 C CB . SER A 1 494 ? 27.282 42.715 19.089 1.00 30.29 ? 547 SER A CB 1 ATOM 3980 O OG . SER A 1 494 ? 26.575 41.556 19.497 1.00 36.07 ? 547 SER A OG 1 ATOM 3981 N N . GLY A 1 495 ? 24.280 43.486 18.235 1.00 28.28 ? 548 GLY A N 1 ATOM 3982 C CA . GLY A 1 495 ? 23.215 43.645 17.258 1.00 27.56 ? 548 GLY A CA 1 ATOM 3983 C C . GLY A 1 495 ? 22.710 45.076 17.164 1.00 30.97 ? 548 GLY A C 1 ATOM 3984 O O . GLY A 1 495 ? 22.249 45.526 16.112 1.00 31.46 ? 548 GLY A O 1 ATOM 3985 N N . ARG A 1 496 ? 22.812 45.804 18.269 1.00 30.53 ? 549 ARG A N 1 ATOM 3986 C CA . ARG A 1 496 ? 22.249 47.144 18.338 1.00 28.06 ? 549 ARG A CA 1 ATOM 3987 C C . ARG A 1 496 ? 23.321 48.212 18.336 1.00 26.17 ? 549 ARG A C 1 ATOM 3988 O O . ARG A 1 496 ? 23.013 49.400 18.206 1.00 27.24 ? 549 ARG A O 1 ATOM 3989 C CB . ARG A 1 496 ? 21.385 47.298 19.590 1.00 30.20 ? 549 ARG A CB 1 ATOM 3990 C CG . ARG A 1 496 ? 20.082 46.565 19.520 1.00 32.67 ? 549 ARG A CG 1 ATOM 3991 C CD . ARG A 1 496 ? 19.103 47.002 20.588 1.00 36.21 ? 549 ARG A CD 1 ATOM 3992 N NE . ARG A 1 496 ? 18.128 45.961 20.879 1.00 38.15 ? 549 ARG A NE 1 ATOM 3993 C CZ . ARG A 1 496 ? 16.825 46.118 20.729 1.00 42.02 ? 549 ARG A CZ 1 ATOM 3994 N NH1 . ARG A 1 496 ? 16.352 47.277 20.286 1.00 42.50 ? 549 ARG A NH1 1 ATOM 3995 N NH2 . ARG A 1 496 ? 15.995 45.127 21.025 1.00 43.47 ? 549 ARG A NH2 1 ATOM 3996 N N . ASN A 1 497 ? 24.575 47.778 18.482 1.00 24.65 ? 550 ASN A N 1 ATOM 3997 C CA . ASN A 1 497 ? 25.712 48.670 18.716 1.00 24.78 ? 550 ASN A CA 1 ATOM 3998 C C . ASN A 1 497 ? 25.415 49.780 19.732 1.00 25.35 ? 550 ASN A C 1 ATOM 3999 O O . ASN A 1 497 ? 25.533 50.965 19.430 1.00 23.82 ? 550 ASN A O 1 ATOM 4000 C CB . ASN A 1 497 ? 26.240 49.249 17.390 1.00 27.54 ? 550 ASN A CB 1 ATOM 4001 C CG . ASN A 1 497 ? 27.550 49.986 17.547 1.00 26.69 ? 550 ASN A CG 1 ATOM 4002 O OD1 . ASN A 1 497 ? 27.781 51.010 16.905 1.00 31.72 ? 550 ASN A OD1 1 ATOM 4003 N ND2 . ASN A 1 497 ? 28.427 49.462 18.393 1.00 23.82 ? 550 ASN A ND2 1 ATOM 4004 N N . GLN A 1 498 ? 25.069 49.356 20.945 1.00 26.82 ? 551 GLN A N 1 ATOM 4005 C CA . GLN A 1 498 ? 24.452 50.206 21.960 1.00 26.89 ? 551 GLN A CA 1 ATOM 4006 C C . GLN A 1 498 ? 25.144 49.946 23.303 1.00 27.06 ? 551 GLN A C 1 ATOM 4007 O O . GLN A 1 498 ? 25.411 48.797 23.671 1.00 22.67 ? 551 GLN A O 1 ATOM 4008 C CB . GLN A 1 498 ? 22.953 49.909 22.029 1.00 28.97 ? 551 GLN A CB 1 ATOM 4009 C CG . GLN A 1 498 ? 22.224 50.352 23.291 1.00 32.66 ? 551 GLN A CG 1 ATOM 4010 C CD . GLN A 1 498 ? 20.714 50.150 23.186 1.00 34.26 ? 551 GLN A CD 1 ATOM 4011 O OE1 . GLN A 1 498 ? 20.120 50.441 22.149 1.00 38.88 ? 551 GLN A OE1 1 ATOM 4012 N NE2 . GLN A 1 498 ? 20.096 49.644 24.255 1.00 34.44 ? 551 GLN A NE2 1 ATOM 4013 N N . ILE A 1 499 ? 25.469 51.015 24.018 1.00 24.60 ? 552 ILE A N 1 ATOM 4014 C CA . ILE A 1 499 ? 25.932 50.884 25.393 1.00 22.63 ? 552 ILE A CA 1 ATOM 4015 C C . ILE A 1 499 ? 24.862 51.412 26.353 1.00 23.40 ? 552 ILE A C 1 ATOM 4016 O O . ILE A 1 499 ? 24.179 52.401 26.076 1.00 20.52 ? 552 ILE A O 1 ATOM 4017 C CB . ILE A 1 499 ? 27.271 51.613 25.606 1.00 18.58 ? 552 ILE A CB 1 ATOM 4018 C CG1 . ILE A 1 499 ? 27.213 53.050 25.088 1.00 21.30 ? 552 ILE A CG1 1 ATOM 4019 C CG2 . ILE A 1 499 ? 28.395 50.879 24.922 1.00 18.13 ? 552 ILE A CG2 1 ATOM 4020 C CD1 . ILE A 1 499 ? 28.409 53.875 25.505 1.00 18.69 ? 552 ILE A CD1 1 ATOM 4021 N N . VAL A 1 500 ? 24.682 50.708 27.459 1.00 20.10 ? 553 VAL A N 1 ATOM 4022 C CA . VAL A 1 500 ? 23.582 51.000 28.353 1.00 20.99 ? 553 VAL A CA 1 ATOM 4023 C C . VAL A 1 500 ? 24.077 51.059 29.783 1.00 20.13 ? 553 VAL A C 1 ATOM 4024 O O . VAL A 1 500 ? 24.769 50.154 30.244 1.00 14.75 ? 553 VAL A O 1 ATOM 4025 C CB . VAL A 1 500 ? 22.476 49.958 28.249 1.00 24.47 ? 553 VAL A CB 1 ATOM 4026 C CG1 . VAL A 1 500 ? 21.295 50.359 29.133 1.00 24.51 ? 553 VAL A CG1 1 ATOM 4027 C CG2 . VAL A 1 500 ? 22.037 49.797 26.798 1.00 29.85 ? 553 VAL A CG2 1 ATOM 4028 N N . PHE A 1 501 ? 23.720 52.142 30.465 1.00 16.09 ? 554 PHE A N 1 ATOM 4029 C CA . PHE A 1 501 ? 24.147 52.394 31.826 1.00 14.47 ? 554 PHE A CA 1 ATOM 4030 C C . PHE A 1 501 ? 22.919 52.709 32.671 1.00 15.08 ? 554 PHE A C 1 ATOM 4031 O O . PHE A 1 501 ? 22.572 53.866 32.883 1.00 16.72 ? 554 PHE A O 1 ATOM 4032 C CB . PHE A 1 501 ? 25.150 53.550 31.852 1.00 18.13 ? 554 PHE A CB 1 ATOM 4033 C CG . PHE A 1 501 ? 26.322 53.329 30.952 1.00 17.00 ? 554 PHE A CG 1 ATOM 4034 C CD1 . PHE A 1 501 ? 27.384 52.539 31.366 1.00 15.71 ? 554 PHE A CD1 1 ATOM 4035 C CD2 . PHE A 1 501 ? 26.348 53.868 29.675 1.00 20.51 ? 554 PHE A CD2 1 ATOM 4036 C CE1 . PHE A 1 501 ? 28.445 52.296 30.528 1.00 16.13 ? 554 PHE A CE1 1 ATOM 4037 C CE2 . PHE A 1 501 ? 27.421 53.646 28.840 1.00 19.93 ? 554 PHE A CE2 1 ATOM 4038 C CZ . PHE A 1 501 ? 28.467 52.853 29.264 1.00 17.08 ? 554 PHE A CZ 1 ATOM 4039 N N . PRO A 1 502 ? 22.247 51.665 33.129 1.00 16.05 ? 555 PRO A N 1 ATOM 4040 C CA . PRO A 1 502 ? 21.047 51.813 33.965 1.00 17.47 ? 555 PRO A CA 1 ATOM 4041 C C . PRO A 1 502 ? 21.320 52.667 35.197 1.00 16.80 ? 555 PRO A C 1 ATOM 4042 O O . PRO A 1 502 ? 22.423 52.655 35.737 1.00 15.07 ? 555 PRO A O 1 ATOM 4043 C CB . PRO A 1 502 ? 20.726 50.380 34.384 1.00 18.64 ? 555 PRO A CB 1 ATOM 4044 C CG . PRO A 1 502 ? 21.385 49.520 33.366 1.00 19.96 ? 555 PRO A CG 1 ATOM 4045 C CD . PRO A 1 502 ? 22.605 50.260 32.911 1.00 17.36 ? 555 PRO A CD 1 ATOM 4046 N N . ALA A 1 503 ? 20.304 53.400 35.633 1.00 15.67 ? 556 ALA A N 1 ATOM 4047 C CA . ALA A 1 503 ? 20.410 54.206 36.834 1.00 16.21 ? 556 ALA A CA 1 ATOM 4048 C C . ALA A 1 503 ? 21.046 53.408 37.966 1.00 16.50 ? 556 ALA A C 1 ATOM 4049 O O . ALA A 1 503 ? 21.830 53.934 38.758 1.00 16.00 ? 556 ALA A O 1 ATOM 4050 C CB . ALA A 1 503 ? 19.055 54.691 37.237 1.00 17.07 ? 556 ALA A CB 1 ATOM 4051 N N . GLY A 1 504 ? 20.694 52.134 38.040 1.00 14.96 ? 557 GLY A N 1 ATOM 4052 C CA . GLY A 1 504 ? 21.168 51.282 39.118 1.00 17.06 ? 557 GLY A CA 1 ATOM 4053 C C . GLY A 1 504 ? 22.674 51.303 39.367 1.00 18.05 ? 557 GLY A C 1 ATOM 4054 O O . GLY A 1 504 ? 23.130 51.133 40.502 1.00 18.09 ? 557 GLY A O 1 ATOM 4055 N N . ILE A 1 505 ? 23.470 51.470 38.316 1.00 17.09 ? 558 ILE A N 1 ATOM 4056 C CA . ILE A 1 505 ? 24.921 51.468 38.485 1.00 15.52 ? 558 ILE A CA 1 ATOM 4057 C C . ILE A 1 505 ? 25.503 52.886 38.591 1.00 18.42 ? 558 ILE A C 1 ATOM 4058 O O . ILE A 1 505 ? 26.704 53.049 38.791 1.00 18.24 ? 558 ILE A O 1 ATOM 4059 C CB . ILE A 1 505 ? 25.611 50.679 37.350 1.00 17.70 ? 558 ILE A CB 1 ATOM 4060 C CG1 . ILE A 1 505 ? 26.985 50.171 37.826 1.00 20.67 ? 558 ILE A CG1 1 ATOM 4061 C CG2 . ILE A 1 505 ? 25.743 51.539 36.117 1.00 18.73 ? 558 ILE A CG2 1 ATOM 4062 C CD1 . ILE A 1 505 ? 27.634 49.142 36.925 1.00 19.56 ? 558 ILE A CD1 1 ATOM 4063 N N . LEU A 1 506 ? 24.666 53.914 38.484 1.00 18.19 ? 559 LEU A N 1 ATOM 4064 C CA . LEU A 1 506 ? 25.177 55.276 38.522 1.00 19.64 ? 559 LEU A CA 1 ATOM 4065 C C . LEU A 1 506 ? 25.152 55.834 39.957 1.00 23.02 ? 559 LEU A C 1 ATOM 4066 O O . LEU A 1 506 ? 24.419 56.771 40.271 1.00 19.00 ? 559 LEU A O 1 ATOM 4067 C CB . LEU A 1 506 ? 24.393 56.159 37.539 1.00 20.54 ? 559 LEU A CB 1 ATOM 4068 C CG . LEU A 1 506 ? 24.355 55.600 36.112 1.00 19.14 ? 559 LEU A CG 1 ATOM 4069 C CD1 . LEU A 1 506 ? 23.495 56.442 35.188 1.00 21.48 ? 559 LEU A CD1 1 ATOM 4070 C CD2 . LEU A 1 506 ? 25.776 55.437 35.531 1.00 19.89 ? 559 LEU A CD2 1 ATOM 4071 N N . GLN A 1 507 ? 25.969 55.244 40.825 1.00 19.56 ? 560 GLN A N 1 ATOM 4072 C CA . GLN A 1 507 ? 25.998 55.607 42.236 1.00 18.17 ? 560 GLN A CA 1 ATOM 4073 C C . GLN A 1 507 ? 27.343 55.181 42.792 1.00 16.97 ? 560 GLN A C 1 ATOM 4074 O O . GLN A 1 507 ? 28.055 54.425 42.144 1.00 16.85 ? 560 GLN A O 1 ATOM 4075 C CB . GLN A 1 507 ? 24.859 54.927 43.007 1.00 20.23 ? 560 GLN A CB 1 ATOM 4076 C CG . GLN A 1 507 ? 24.889 53.432 42.972 1.00 21.43 ? 560 GLN A CG 1 ATOM 4077 C CD . GLN A 1 507 ? 23.802 52.808 43.832 1.00 25.69 ? 560 GLN A CD 1 ATOM 4078 O OE1 . GLN A 1 507 ? 23.546 53.267 44.939 1.00 29.33 ? 560 GLN A OE1 1 ATOM 4079 N NE2 . GLN A 1 507 ? 23.161 51.769 43.321 1.00 18.17 ? 560 GLN A NE2 1 ATOM 4080 N N . PRO A 1 508 ? 27.732 55.692 43.954 1.00 17.08 ? 561 PRO A N 1 ATOM 4081 C CA . PRO A 1 508 ? 29.017 55.305 44.538 1.00 20.12 ? 561 PRO A CA 1 ATOM 4082 C C . PRO A 1 508 ? 29.090 53.794 44.764 1.00 19.50 ? 561 PRO A C 1 ATOM 4083 O O . PRO A 1 508 ? 28.074 53.177 45.103 1.00 19.36 ? 561 PRO A O 1 ATOM 4084 C CB . PRO A 1 508 ? 29.061 56.105 45.846 1.00 21.43 ? 561 PRO A CB 1 ATOM 4085 C CG . PRO A 1 508 ? 28.179 57.275 45.578 1.00 21.82 ? 561 PRO A CG 1 ATOM 4086 C CD . PRO A 1 508 ? 27.047 56.715 44.763 1.00 21.73 ? 561 PRO A CD 1 ATOM 4087 N N . PRO A 1 509 ? 30.257 53.196 44.538 1.00 19.82 ? 562 PRO A N 1 ATOM 4088 C CA . PRO A 1 509 ? 31.510 53.920 44.351 1.00 19.07 ? 562 PRO A CA 1 ATOM 4089 C C . PRO A 1 509 ? 31.798 54.290 42.890 1.00 19.73 ? 562 PRO A C 1 ATOM 4090 O O . PRO A 1 509 ? 32.801 54.961 42.617 1.00 16.53 ? 562 PRO A O 1 ATOM 4091 C CB . PRO A 1 509 ? 32.545 52.916 44.849 1.00 19.11 ? 562 PRO A CB 1 ATOM 4092 C CG . PRO A 1 509 ? 31.946 51.567 44.498 1.00 20.56 ? 562 PRO A CG 1 ATOM 4093 C CD . PRO A 1 509 ? 30.459 51.737 44.465 1.00 19.12 ? 562 PRO A CD 1 ATOM 4094 N N . PHE A 1 510 ? 30.933 53.861 41.974 1.00 14.16 ? 563 PHE A N 1 ATOM 4095 C CA . PHE A 1 510 ? 31.140 54.117 40.544 1.00 17.54 ? 563 PHE A CA 1 ATOM 4096 C C . PHE A 1 510 ? 31.047 55.601 40.223 1.00 17.34 ? 563 PHE A C 1 ATOM 4097 O O . PHE A 1 510 ? 31.937 56.174 39.595 1.00 19.39 ? 563 PHE A O 1 ATOM 4098 C CB . PHE A 1 510 ? 30.106 53.362 39.707 1.00 15.75 ? 563 PHE A CB 1 ATOM 4099 C CG . PHE A 1 510 ? 30.288 51.850 39.715 1.00 17.03 ? 563 PHE A CG 1 ATOM 4100 C CD1 . PHE A 1 510 ? 31.218 51.226 38.889 1.00 11.10 ? 563 PHE A CD1 1 ATOM 4101 C CD2 . PHE A 1 510 ? 29.510 51.064 40.544 1.00 15.50 ? 563 PHE A CD2 1 ATOM 4102 C CE1 . PHE A 1 510 ? 31.353 49.874 38.893 1.00 16.18 ? 563 PHE A CE1 1 ATOM 4103 C CE2 . PHE A 1 510 ? 29.649 49.690 40.552 1.00 15.85 ? 563 PHE A CE2 1 ATOM 4104 C CZ . PHE A 1 510 ? 30.575 49.094 39.730 1.00 15.14 ? 563 PHE A CZ 1 ATOM 4105 N N . PHE A 1 511 ? 29.961 56.227 40.656 1.00 17.67 ? 564 PHE A N 1 ATOM 4106 C CA . PHE A 1 511 ? 29.667 57.586 40.220 1.00 20.20 ? 564 PHE A CA 1 ATOM 4107 C C . PHE A 1 511 ? 28.868 58.347 41.263 1.00 19.73 ? 564 PHE A C 1 ATOM 4108 O O . PHE A 1 511 ? 27.907 57.830 41.852 1.00 15.91 ? 564 PHE A O 1 ATOM 4109 C CB . PHE A 1 511 ? 28.920 57.595 38.886 1.00 20.85 ? 564 PHE A CB 1 ATOM 4110 C CG . PHE A 1 511 ? 28.474 58.947 38.473 1.00 22.13 ? 564 PHE A CG 1 ATOM 4111 C CD1 . PHE A 1 511 ? 29.359 59.850 37.903 1.00 22.24 ? 564 PHE A CD1 1 ATOM 4112 C CD2 . PHE A 1 511 ? 27.169 59.338 38.688 1.00 22.27 ? 564 PHE A CD2 1 ATOM 4113 C CE1 . PHE A 1 511 ? 28.945 61.118 37.543 1.00 24.25 ? 564 PHE A CE1 1 ATOM 4114 C CE2 . PHE A 1 511 ? 26.740 60.620 38.327 1.00 23.47 ? 564 PHE A CE2 1 ATOM 4115 C CZ . PHE A 1 511 ? 27.637 61.503 37.751 1.00 21.89 ? 564 PHE A CZ 1 ATOM 4116 N N . SER A 1 512 ? 29.286 59.586 41.472 1.00 20.32 ? 565 SER A N 1 ATOM 4117 C CA . SER A 1 512 ? 28.413 60.640 41.961 1.00 21.90 ? 565 SER A CA 1 ATOM 4118 C C . SER A 1 512 ? 28.931 61.990 41.471 1.00 22.24 ? 565 SER A C 1 ATOM 4119 O O . SER A 1 512 ? 30.140 62.239 41.473 1.00 22.23 ? 565 SER A O 1 ATOM 4120 C CB . SER A 1 512 ? 28.386 60.613 43.492 1.00 25.46 ? 565 SER A CB 1 ATOM 4121 O OG . SER A 1 512 ? 27.905 61.834 44.024 1.00 23.26 ? 565 SER A OG 1 ATOM 4122 N N . ALA A 1 513 ? 28.016 62.861 41.059 1.00 20.84 ? 566 ALA A N 1 ATOM 4123 C CA . ALA A 1 513 ? 28.368 64.235 40.704 1.00 24.72 ? 566 ALA A CA 1 ATOM 4124 C C . ALA A 1 513 ? 29.090 64.930 41.848 1.00 23.22 ? 566 ALA A C 1 ATOM 4125 O O . ALA A 1 513 ? 29.775 65.937 41.657 1.00 27.61 ? 566 ALA A O 1 ATOM 4126 C CB . ALA A 1 513 ? 27.122 65.019 40.326 1.00 24.31 ? 566 ALA A CB 1 ATOM 4127 N N . GLN A 1 514 ? 28.926 64.399 43.045 1.00 24.84 ? 567 GLN A N 1 ATOM 4128 C CA . GLN A 1 514 ? 29.472 65.032 44.237 1.00 29.03 ? 567 GLN A CA 1 ATOM 4129 C C . GLN A 1 514 ? 30.808 64.423 44.695 1.00 28.16 ? 567 GLN A C 1 ATOM 4130 O O . GLN A 1 514 ? 31.502 65.008 45.527 1.00 31.71 ? 567 GLN A O 1 ATOM 4131 C CB . GLN A 1 514 ? 28.439 64.961 45.364 1.00 34.26 ? 567 GLN A CB 1 ATOM 4132 C CG . GLN A 1 514 ? 27.376 66.065 45.299 1.00 35.63 ? 567 GLN A CG 1 ATOM 4133 C CD . GLN A 1 514 ? 26.315 65.817 44.235 1.00 38.18 ? 567 GLN A CD 1 ATOM 4134 O OE1 . GLN A 1 514 ? 25.734 64.728 44.165 1.00 37.23 ? 567 GLN A OE1 1 ATOM 4135 N NE2 . GLN A 1 514 ? 26.057 66.824 43.409 1.00 36.46 ? 567 GLN A NE2 1 ATOM 4136 N N . GLN A 1 515 ? 31.184 63.267 44.148 1.00 22.96 ? 568 GLN A N 1 ATOM 4137 C CA . GLN A 1 515 ? 32.442 62.633 44.545 1.00 24.02 ? 568 GLN A CA 1 ATOM 4138 C C . GLN A 1 515 ? 33.584 63.070 43.625 1.00 23.21 ? 568 GLN A C 1 ATOM 4139 O O . GLN A 1 515 ? 33.348 63.581 42.531 1.00 19.46 ? 568 GLN A O 1 ATOM 4140 C CB . GLN A 1 515 ? 32.291 61.104 44.606 1.00 26.08 ? 568 GLN A CB 1 ATOM 4141 C CG . GLN A 1 515 ? 32.586 60.342 43.327 1.00 21.90 ? 568 GLN A CG 1 ATOM 4142 C CD . GLN A 1 515 ? 32.486 58.825 43.522 1.00 25.67 ? 568 GLN A CD 1 ATOM 4143 O OE1 . GLN A 1 515 ? 32.391 58.356 44.649 1.00 22.16 ? 568 GLN A OE1 1 ATOM 4144 N NE2 . GLN A 1 515 ? 32.522 58.067 42.427 1.00 15.49 ? 568 GLN A NE2 1 ATOM 4145 N N . SER A 1 516 ? 34.818 62.900 44.078 1.00 21.96 ? 569 SER A N 1 ATOM 4146 C CA . SER A 1 516 ? 35.967 63.347 43.295 1.00 22.66 ? 569 SER A CA 1 ATOM 4147 C C . SER A 1 516 ? 36.003 62.733 41.889 1.00 22.49 ? 569 SER A C 1 ATOM 4148 O O . SER A 1 516 ? 35.632 61.575 41.687 1.00 19.41 ? 569 SER A O 1 ATOM 4149 C CB . SER A 1 516 ? 37.273 63.026 44.014 1.00 22.34 ? 569 SER A CB 1 ATOM 4150 O OG . SER A 1 516 ? 37.281 63.515 45.338 1.00 23.74 ? 569 SER A OG 1 ATOM 4151 N N . ASN A 1 517 ? 36.478 63.515 40.927 1.00 21.15 ? 570 ASN A N 1 ATOM 4152 C CA . ASN A 1 517 ? 36.637 63.056 39.552 1.00 20.32 ? 570 ASN A CA 1 ATOM 4153 C C . ASN A 1 517 ? 37.485 61.790 39.439 1.00 18.06 ? 570 ASN A C 1 ATOM 4154 O O . ASN A 1 517 ? 37.168 60.895 38.653 1.00 20.13 ? 570 ASN A O 1 ATOM 4155 C CB . ASN A 1 517 ? 37.238 64.177 38.691 1.00 25.68 ? 570 ASN A CB 1 ATOM 4156 C CG . ASN A 1 517 ? 36.405 65.458 38.720 1.00 34.04 ? 570 ASN A CG 1 ATOM 4157 O OD1 . ASN A 1 517 ? 35.382 65.567 38.039 1.00 34.75 ? 570 ASN A OD1 1 ATOM 4158 N ND2 . ASN A 1 517 ? 36.847 66.437 39.504 1.00 37.64 ? 570 ASN A ND2 1 ATOM 4159 N N . SER A 1 518 ? 38.558 61.704 40.219 1.00 19.62 ? 571 SER A N 1 ATOM 4160 C CA . SER A 1 518 ? 39.432 60.531 40.176 1.00 19.65 ? 571 SER A CA 1 ATOM 4161 C C . SER A 1 518 ? 38.638 59.256 40.450 1.00 21.72 ? 571 SER A C 1 ATOM 4162 O O . SER A 1 518 ? 38.817 58.229 39.769 1.00 17.63 ? 571 SER A O 1 ATOM 4163 C CB . SER A 1 518 ? 40.546 60.652 41.208 1.00 19.99 ? 571 SER A CB 1 ATOM 4164 O OG . SER A 1 518 ? 40.015 60.653 42.526 1.00 21.05 ? 571 SER A OG 1 ATOM 4165 N N . LEU A 1 519 ? 37.770 59.333 41.457 1.00 19.21 ? 572 LEU A N 1 ATOM 4166 C CA . LEU A 1 519 ? 36.860 58.245 41.777 1.00 19.36 ? 572 LEU A CA 1 ATOM 4167 C C . LEU A 1 519 ? 35.888 57.972 40.627 1.00 20.43 ? 572 LEU A C 1 ATOM 4168 O O . LEU A 1 519 ? 35.668 56.812 40.268 1.00 17.93 ? 572 LEU A O 1 ATOM 4169 C CB . LEU A 1 519 ? 36.091 58.562 43.060 1.00 18.62 ? 572 LEU A CB 1 ATOM 4170 C CG . LEU A 1 519 ? 36.926 58.964 44.277 1.00 21.78 ? 572 LEU A CG 1 ATOM 4171 C CD1 . LEU A 1 519 ? 36.047 59.130 45.518 1.00 24.07 ? 572 LEU A CD1 1 ATOM 4172 C CD2 . LEU A 1 519 ? 38.029 57.986 44.531 1.00 21.39 ? 572 LEU A CD2 1 ATOM 4173 N N . ASN A 1 520 ? 35.306 59.025 40.041 1.00 19.17 ? 573 ASN A N 1 ATOM 4174 C CA . ASN A 1 520 ? 34.324 58.825 38.964 1.00 20.50 ? 573 ASN A CA 1 ATOM 4175 C C . ASN A 1 520 ? 34.959 58.108 37.742 1.00 18.84 ? 573 ASN A C 1 ATOM 4176 O O . ASN A 1 520 ? 34.390 57.160 37.197 1.00 15.25 ? 573 ASN A O 1 ATOM 4177 C CB . ASN A 1 520 ? 33.638 60.139 38.572 1.00 18.85 ? 573 ASN A CB 1 ATOM 4178 C CG . ASN A 1 520 ? 32.603 60.595 39.612 1.00 22.69 ? 573 ASN A CG 1 ATOM 4179 O OD1 . ASN A 1 520 ? 31.949 59.776 40.280 1.00 19.40 ? 573 ASN A OD1 1 ATOM 4180 N ND2 . ASN A 1 520 ? 32.465 61.904 39.759 1.00 19.89 ? 573 ASN A ND2 1 ATOM 4181 N N . TYR A 1 521 ? 36.141 58.551 37.325 1.00 17.77 ? 574 TYR A N 1 ATOM 4182 C CA . TYR A 1 521 ? 36.799 57.977 36.154 1.00 16.91 ? 574 TYR A CA 1 ATOM 4183 C C . TYR A 1 521 ? 37.271 56.537 36.391 1.00 18.56 ? 574 TYR A C 1 ATOM 4184 O O . TYR A 1 521 ? 37.148 55.680 35.513 1.00 16.49 ? 574 TYR A O 1 ATOM 4185 C CB . TYR A 1 521 ? 37.972 58.858 35.733 1.00 19.36 ? 574 TYR A CB 1 ATOM 4186 C CG . TYR A 1 521 ? 37.550 60.128 35.024 1.00 19.65 ? 574 TYR A CG 1 ATOM 4187 C CD1 . TYR A 1 521 ? 37.342 60.144 33.653 1.00 23.54 ? 574 TYR A CD1 1 ATOM 4188 C CD2 . TYR A 1 521 ? 37.360 61.309 35.726 1.00 24.72 ? 574 TYR A CD2 1 ATOM 4189 C CE1 . TYR A 1 521 ? 36.965 61.306 32.994 1.00 21.46 ? 574 TYR A CE1 1 ATOM 4190 C CE2 . TYR A 1 521 ? 36.978 62.473 35.077 1.00 27.22 ? 574 TYR A CE2 1 ATOM 4191 C CZ . TYR A 1 521 ? 36.782 62.465 33.710 1.00 25.77 ? 574 TYR A CZ 1 ATOM 4192 O OH . TYR A 1 521 ? 36.398 63.615 33.053 1.00 23.43 ? 574 TYR A OH 1 ATOM 4193 N N . GLY A 1 522 ? 37.817 56.270 37.570 1.00 18.43 ? 575 GLY A N 1 ATOM 4194 C CA . GLY A 1 522 ? 38.321 54.941 37.887 1.00 19.34 ? 575 GLY A CA 1 ATOM 4195 C C . GLY A 1 522 ? 37.202 53.955 38.178 1.00 17.78 ? 575 GLY A C 1 ATOM 4196 O O . GLY A 1 522 ? 37.428 52.745 38.263 1.00 20.52 ? 575 GLY A O 1 ATOM 4197 N N . GLY A 1 523 ? 35.993 54.484 38.333 1.00 18.32 ? 576 GLY A N 1 ATOM 4198 C CA . GLY A 1 523 ? 34.800 53.681 38.539 1.00 15.48 ? 576 GLY A CA 1 ATOM 4199 C C . GLY A 1 523 ? 33.925 53.602 37.301 1.00 15.86 ? 576 GLY A C 1 ATOM 4200 O O . GLY A 1 523 ? 34.118 52.735 36.451 1.00 14.01 ? 576 GLY A O 1 ATOM 4201 N N . ILE A 1 524 ? 32.962 54.514 37.197 1.00 16.02 ? 577 ILE A N 1 ATOM 4202 C CA . ILE A 1 524 ? 32.041 54.523 36.063 1.00 14.05 ? 577 ILE A CA 1 ATOM 4203 C C . ILE A 1 524 ? 32.780 54.803 34.770 1.00 16.27 ? 577 ILE A C 1 ATOM 4204 O O . ILE A 1 524 ? 32.424 54.282 33.716 1.00 13.71 ? 577 ILE A O 1 ATOM 4205 C CB . ILE A 1 524 ? 30.890 55.522 36.262 1.00 14.90 ? 577 ILE A CB 1 ATOM 4206 C CG1 . ILE A 1 524 ? 29.695 55.153 35.375 1.00 12.83 ? 577 ILE A CG1 1 ATOM 4207 C CG2 . ILE A 1 524 ? 31.326 56.929 35.928 1.00 16.32 ? 577 ILE A CG2 1 ATOM 4208 C CD1 . ILE A 1 524 ? 29.140 53.809 35.618 1.00 13.83 ? 577 ILE A CD1 1 ATOM 4209 N N . GLY A 1 525 ? 33.833 55.600 34.839 1.00 14.92 ? 578 GLY A N 1 ATOM 4210 C CA . GLY A 1 525 ? 34.630 55.824 33.653 1.00 19.42 ? 578 GLY A CA 1 ATOM 4211 C C . GLY A 1 525 ? 35.158 54.506 33.112 1.00 19.80 ? 578 GLY A C 1 ATOM 4212 O O . GLY A 1 525 ? 35.046 54.223 31.922 1.00 17.47 ? 578 GLY A O 1 ATOM 4213 N N . MET A 1 526 ? 35.739 53.705 33.995 1.00 21.93 ? 579 MET A N 1 ATOM 4214 C CA . MET A 1 526 ? 36.219 52.379 33.629 1.00 21.27 ? 579 MET A CA 1 ATOM 4215 C C . MET A 1 526 ? 35.074 51.540 33.078 1.00 21.54 ? 579 MET A C 1 ATOM 4216 O O . MET A 1 526 ? 35.258 50.830 32.097 1.00 18.48 ? 579 MET A O 1 ATOM 4217 C CB . MET A 1 526 ? 36.871 51.680 34.834 1.00 26.06 ? 579 MET A CB 1 ATOM 4218 C CG . MET A 1 526 ? 36.946 50.142 34.711 1.00 28.79 ? 579 MET A CG 1 ATOM 4219 S SD . MET A 1 526 ? 38.134 49.663 33.444 1.00 33.23 ? 579 MET A SD 1 ATOM 4220 C CE . MET A 1 526 ? 38.234 47.854 33.730 1.00 32.15 ? 579 MET A CE 1 ATOM 4221 N N . VAL A 1 527 ? 33.882 51.628 33.679 1.00 17.39 ? 580 VAL A N 1 ATOM 4222 C CA . VAL A 1 527 ? 32.750 50.834 33.193 1.00 17.92 ? 580 VAL A CA 1 ATOM 4223 C C . VAL A 1 527 ? 32.337 51.266 31.774 1.00 15.39 ? 580 VAL A C 1 ATOM 4224 O O . VAL A 1 527 ? 32.105 50.425 30.911 1.00 17.78 ? 580 VAL A O 1 ATOM 4225 C CB . VAL A 1 527 ? 31.533 50.893 34.145 1.00 17.12 ? 580 VAL A CB 1 ATOM 4226 C CG1 . VAL A 1 527 ? 30.343 50.166 33.537 1.00 19.28 ? 580 VAL A CG1 1 ATOM 4227 C CG2 . VAL A 1 527 ? 31.884 50.285 35.494 1.00 20.10 ? 580 VAL A CG2 1 ATOM 4228 N N . ILE A 1 528 ? 32.287 52.572 31.521 1.00 15.59 ? 581 ILE A N 1 ATOM 4229 C CA . ILE A 1 528 ? 31.983 53.069 30.180 1.00 17.96 ? 581 ILE A CA 1 ATOM 4230 C C . ILE A 1 528 ? 32.942 52.537 29.102 1.00 15.90 ? 581 ILE A C 1 ATOM 4231 O O . ILE A 1 528 ? 32.508 52.095 28.034 1.00 19.02 ? 581 ILE A O 1 ATOM 4232 C CB . ILE A 1 528 ? 31.988 54.601 30.157 1.00 19.23 ? 581 ILE A CB 1 ATOM 4233 C CG1 . ILE A 1 528 ? 30.843 55.149 31.000 1.00 20.44 ? 581 ILE A CG1 1 ATOM 4234 C CG2 . ILE A 1 528 ? 31.879 55.095 28.723 1.00 20.83 ? 581 ILE A CG2 1 ATOM 4235 C CD1 . ILE A 1 528 ? 31.101 56.537 31.579 1.00 19.28 ? 581 ILE A CD1 1 ATOM 4236 N N . GLY A 1 529 ? 34.237 52.596 29.376 1.00 18.49 ? 582 GLY A N 1 ATOM 4237 C CA . GLY A 1 529 ? 35.242 52.113 28.436 1.00 16.87 ? 582 GLY A CA 1 ATOM 4238 C C . GLY A 1 529 ? 35.145 50.612 28.252 1.00 18.84 ? 582 GLY A C 1 ATOM 4239 O O . GLY A 1 529 ? 35.290 50.100 27.141 1.00 15.59 ? 582 GLY A O 1 ATOM 4240 N N . HIS A 1 530 ? 34.864 49.907 29.344 1.00 18.06 ? 583 HIS A N 1 ATOM 4241 C CA . HIS A 1 530 ? 34.580 48.471 29.283 1.00 16.74 ? 583 HIS A CA 1 ATOM 4242 C C . HIS A 1 530 ? 33.476 48.139 28.279 1.00 16.85 ? 583 HIS A C 1 ATOM 4243 O O . HIS A 1 530 ? 33.678 47.294 27.406 1.00 13.79 ? 583 HIS A O 1 ATOM 4244 C CB . HIS A 1 530 ? 34.241 47.933 30.673 1.00 15.67 ? 583 HIS A CB 1 ATOM 4245 C CG . HIS A 1 530 ? 33.880 46.478 30.698 1.00 15.37 ? 583 HIS A CG 1 ATOM 4246 N ND1 . HIS A 1 530 ? 34.707 45.516 31.236 1.00 17.43 ? 583 HIS A ND1 1 ATOM 4247 C CD2 . HIS A 1 530 ? 32.771 45.827 30.276 1.00 14.19 ? 583 HIS A CD2 1 ATOM 4248 C CE1 . HIS A 1 530 ? 34.128 44.335 31.133 1.00 17.08 ? 583 HIS A CE1 1 ATOM 4249 N NE2 . HIS A 1 530 ? 32.952 44.495 30.550 1.00 16.77 ? 583 HIS A NE2 1 ATOM 4250 N N . GLU A 1 531 ? 32.317 48.793 28.394 1.00 16.92 ? 584 GLU A N 1 ATOM 4251 C CA . GLU A 1 531 ? 31.209 48.532 27.474 1.00 17.83 ? 584 GLU A CA 1 ATOM 4252 C C . GLU A 1 531 ? 31.539 48.921 26.024 1.00 13.27 ? 584 GLU A C 1 ATOM 4253 O O . GLU A 1 531 ? 31.221 48.185 25.095 1.00 18.04 ? 584 GLU A O 1 ATOM 4254 C CB . GLU A 1 531 ? 29.928 49.262 27.905 1.00 16.67 ? 584 GLU A CB 1 ATOM 4255 C CG . GLU A 1 531 ? 29.389 48.939 29.296 1.00 16.00 ? 584 GLU A CG 1 ATOM 4256 C CD . GLU A 1 531 ? 29.466 47.473 29.692 1.00 17.30 ? 584 GLU A CD 1 ATOM 4257 O OE1 . GLU A 1 531 ? 29.021 46.581 28.924 1.00 17.88 ? 584 GLU A OE1 1 ATOM 4258 O OE2 . GLU A 1 531 ? 29.935 47.213 30.821 1.00 20.00 ? 584 GLU A OE2 1 ATOM 4259 N N . ILE A 1 532 ? 32.146 50.088 25.835 1.00 18.96 ? 585 ILE A N 1 ATOM 4260 C CA . ILE A 1 532 ? 32.597 50.489 24.508 1.00 18.21 ? 585 ILE A CA 1 ATOM 4261 C C . ILE A 1 532 ? 33.517 49.434 23.898 1.00 17.83 ? 585 ILE A C 1 ATOM 4262 O O . ILE A 1 532 ? 33.317 49.017 22.766 1.00 19.43 ? 585 ILE A O 1 ATOM 4263 C CB . ILE A 1 532 ? 33.263 51.848 24.546 1.00 19.59 ? 585 ILE A CB 1 ATOM 4264 C CG1 . ILE A 1 532 ? 32.198 52.927 24.752 1.00 20.60 ? 585 ILE A CG1 1 ATOM 4265 C CG2 . ILE A 1 532 ? 34.006 52.118 23.232 1.00 22.89 ? 585 ILE A CG2 1 ATOM 4266 C CD1 . ILE A 1 532 ? 32.770 54.218 25.220 1.00 19.29 ? 585 ILE A CD1 1 ATOM 4267 N N . THR A 1 533 ? 34.482 48.972 24.679 1.00 17.23 ? 586 THR A N 1 ATOM 4268 C CA . THR A 1 533 ? 35.502 48.068 24.190 1.00 17.33 ? 586 THR A CA 1 ATOM 4269 C C . THR A 1 533 ? 34.894 46.714 23.825 1.00 19.55 ? 586 THR A C 1 ATOM 4270 O O . THR A 1 533 ? 35.462 45.970 23.035 1.00 23.02 ? 586 THR A O 1 ATOM 4271 C CB . THR A 1 533 ? 36.619 47.940 25.242 1.00 22.27 ? 586 THR A CB 1 ATOM 4272 O OG1 . THR A 1 533 ? 37.181 49.232 25.506 1.00 18.78 ? 586 THR A OG1 1 ATOM 4273 C CG2 . THR A 1 533 ? 37.809 47.116 24.730 1.00 21.64 ? 586 THR A CG2 1 ATOM 4274 N N . HIS A 1 534 ? 33.714 46.409 24.361 1.00 19.11 ? 587 HIS A N 1 ATOM 4275 C CA . HIS A 1 534 ? 32.998 45.197 23.970 1.00 18.33 ? 587 HIS A CA 1 ATOM 4276 C C . HIS A 1 534 ? 32.630 45.209 22.488 1.00 21.11 ? 587 HIS A C 1 ATOM 4277 O O . HIS A 1 534 ? 32.441 44.157 21.880 1.00 20.96 ? 587 HIS A O 1 ATOM 4278 C CB . HIS A 1 534 ? 31.712 45.034 24.786 1.00 17.34 ? 587 HIS A CB 1 ATOM 4279 C CG . HIS A 1 534 ? 31.864 44.189 26.015 1.00 15.50 ? 587 HIS A CG 1 ATOM 4280 N ND1 . HIS A 1 534 ? 32.379 42.912 25.982 1.00 18.71 ? 587 HIS A ND1 1 ATOM 4281 C CD2 . HIS A 1 534 ? 31.554 44.438 27.312 1.00 19.25 ? 587 HIS A CD2 1 ATOM 4282 C CE1 . HIS A 1 534 ? 32.375 42.406 27.205 1.00 19.73 ? 587 HIS A CE1 1 ATOM 4283 N NE2 . HIS A 1 534 ? 31.888 43.318 28.033 1.00 19.54 ? 587 HIS A NE2 1 ATOM 4284 N N . GLY A 1 535 ? 32.481 46.403 21.920 1.00 23.02 ? 588 GLY A N 1 ATOM 4285 C CA . GLY A 1 535 ? 32.162 46.525 20.511 1.00 19.99 ? 588 GLY A CA 1 ATOM 4286 C C . GLY A 1 535 ? 33.345 46.095 19.673 1.00 23.36 ? 588 GLY A C 1 ATOM 4287 O O . GLY A 1 535 ? 33.250 46.020 18.447 1.00 24.71 ? 588 GLY A O 1 ATOM 4288 N N . PHE A 1 536 ? 34.453 45.796 20.348 1.00 21.85 ? 589 PHE A N 1 ATOM 4289 C CA . PHE A 1 536 ? 35.735 45.592 19.690 1.00 22.51 ? 589 PHE A CA 1 ATOM 4290 C C . PHE A 1 536 ? 36.501 44.417 20.295 1.00 21.78 ? 589 PHE A C 1 ATOM 4291 O O . PHE A 1 536 ? 37.713 44.282 20.072 1.00 23.89 ? 589 PHE A O 1 ATOM 4292 C CB . PHE A 1 536 ? 36.574 46.870 19.769 1.00 22.37 ? 589 PHE A CB 1 ATOM 4293 C CG . PHE A 1 536 ? 35.904 48.076 19.154 1.00 23.39 ? 589 PHE A CG 1 ATOM 4294 C CD1 . PHE A 1 536 ? 36.100 48.384 17.818 1.00 23.71 ? 589 PHE A CD1 1 ATOM 4295 C CD2 . PHE A 1 536 ? 35.095 48.901 19.914 1.00 19.46 ? 589 PHE A CD2 1 ATOM 4296 C CE1 . PHE A 1 536 ? 35.498 49.488 17.252 1.00 24.48 ? 589 PHE A CE1 1 ATOM 4297 C CE2 . PHE A 1 536 ? 34.480 49.997 19.355 1.00 24.66 ? 589 PHE A CE2 1 ATOM 4298 C CZ . PHE A 1 536 ? 34.677 50.295 18.021 1.00 25.87 ? 589 PHE A CZ 1 ATOM 4299 N N . ASP A 1 537 ? 35.811 43.562 21.055 1.00 20.65 ? 590 ASP A N 1 ATOM 4300 C CA . ASP A 1 537 ? 36.466 42.385 21.614 1.00 18.65 ? 590 ASP A CA 1 ATOM 4301 C C . ASP A 1 537 ? 36.315 41.223 20.653 1.00 18.52 ? 590 ASP A C 1 ATOM 4302 O O . ASP A 1 537 ? 35.864 41.402 19.520 1.00 20.90 ? 590 ASP A O 1 ATOM 4303 C CB . ASP A 1 537 ? 35.979 42.050 23.043 1.00 19.59 ? 590 ASP A CB 1 ATOM 4304 C CG . ASP A 1 537 ? 34.580 41.467 23.087 1.00 21.12 ? 590 ASP A CG 1 ATOM 4305 O OD1 . ASP A 1 537 ? 34.100 40.913 22.073 1.00 22.93 ? 590 ASP A OD1 1 ATOM 4306 O OD2 . ASP A 1 537 ? 33.881 41.513 24.127 1.00 19.07 ? 590 ASP A OD2 1 ATOM 4307 N N . ASP A 1 538 ? 36.701 40.031 21.075 1.00 19.34 ? 591 ASP A N 1 ATOM 4308 C CA . ASP A 1 538 ? 36.844 38.949 20.111 1.00 19.94 ? 591 ASP A CA 1 ATOM 4309 C C . ASP A 1 538 ? 35.486 38.542 19.532 1.00 23.14 ? 591 ASP A C 1 ATOM 4310 O O . ASP A 1 538 ? 35.416 37.888 18.488 1.00 18.81 ? 591 ASP A O 1 ATOM 4311 C CB . ASP A 1 538 ? 37.583 37.776 20.740 1.00 21.04 ? 591 ASP A CB 1 ATOM 4312 C CG . ASP A 1 538 ? 36.895 37.249 21.990 1.00 21.78 ? 591 ASP A CG 1 ATOM 4313 O OD1 . ASP A 1 538 ? 36.396 38.057 22.801 1.00 22.89 ? 591 ASP A OD1 1 ATOM 4314 O OD2 . ASP A 1 538 ? 36.815 36.034 22.235 1.00 21.18 ? 591 ASP A OD2 1 ATOM 4315 N N . ASN A 1 539 ? 34.398 38.946 20.192 1.00 24.08 ? 592 ASN A N 1 ATOM 4316 C CA . ASN A 1 539 ? 33.049 38.808 19.630 1.00 24.80 ? 592 ASN A CA 1 ATOM 4317 C C . ASN A 1 539 ? 32.619 40.044 18.837 1.00 24.17 ? 592 ASN A C 1 ATOM 4318 O O . ASN A 1 539 ? 32.378 39.964 17.633 1.00 21.92 ? 592 ASN A O 1 ATOM 4319 C CB . ASN A 1 539 ? 32.021 38.539 20.741 1.00 28.28 ? 592 ASN A CB 1 ATOM 4320 C CG . ASN A 1 539 ? 30.581 38.698 20.262 1.00 28.26 ? 592 ASN A CG 1 ATOM 4321 O OD1 . ASN A 1 539 ? 29.944 39.734 20.491 1.00 30.00 ? 592 ASN A OD1 1 ATOM 4322 N ND2 . ASN A 1 539 ? 30.062 37.672 19.603 1.00 27.76 ? 592 ASN A ND2 1 ATOM 4323 N N . GLY A 1 540 ? 32.545 41.187 19.513 1.00 25.27 ? 593 GLY A N 1 ATOM 4324 C CA . GLY A 1 540 ? 31.869 42.356 18.977 1.00 27.44 ? 593 GLY A CA 1 ATOM 4325 C C . GLY A 1 540 ? 32.704 43.155 17.988 1.00 25.07 ? 593 GLY A C 1 ATOM 4326 O O . GLY A 1 540 ? 32.316 44.247 17.577 1.00 37.87 ? 593 GLY A O 1 ATOM 4327 N N . ARG A 1 541 ? 33.863 42.627 17.607 1.00 25.05 ? 594 ARG A N 1 ATOM 4328 C CA . ARG A 1 541 ? 34.636 43.210 16.507 1.00 24.52 ? 594 ARG A CA 1 ATOM 4329 C C . ARG A 1 541 ? 34.152 42.648 15.182 1.00 22.28 ? 594 ARG A C 1 ATOM 4330 O O . ARG A 1 541 ? 34.358 43.245 14.128 1.00 27.33 ? 594 ARG A O 1 ATOM 4331 C CB . ARG A 1 541 ? 36.132 42.952 16.684 1.00 25.99 ? 594 ARG A CB 1 ATOM 4332 C CG . ARG A 1 541 ? 36.585 41.553 16.319 1.00 23.94 ? 594 ARG A CG 1 ATOM 4333 C CD . ARG A 1 541 ? 38.104 41.398 16.246 1.00 27.02 ? 594 ARG A CD 1 ATOM 4334 N NE . ARG A 1 541 ? 38.495 40.055 15.825 1.00 26.24 ? 594 ARG A NE 1 ATOM 4335 C CZ . ARG A 1 541 ? 38.634 39.668 14.558 1.00 29.37 ? 594 ARG A CZ 1 ATOM 4336 N NH1 . ARG A 1 541 ? 38.443 40.523 13.565 1.00 27.11 ? 594 ARG A NH1 1 ATOM 4337 N NH2 . ARG A 1 541 ? 38.973 38.421 14.282 1.00 25.74 ? 594 ARG A NH2 1 ATOM 4338 N N . ASN A 1 542 ? 33.479 41.506 15.249 1.00 24.70 ? 595 ASN A N 1 ATOM 4339 C CA . ASN A 1 542 ? 32.876 40.888 14.076 1.00 23.91 ? 595 ASN A CA 1 ATOM 4340 C C . ASN A 1 542 ? 31.588 41.575 13.612 1.00 24.00 ? 595 ASN A C 1 ATOM 4341 O O . ASN A 1 542 ? 31.031 41.256 12.552 1.00 23.57 ? 595 ASN A O 1 ATOM 4342 C CB . ASN A 1 542 ? 32.620 39.419 14.374 1.00 26.53 ? 595 ASN A CB 1 ATOM 4343 C CG . ASN A 1 542 ? 33.903 38.665 14.682 1.00 30.70 ? 595 ASN A CG 1 ATOM 4344 O OD1 . ASN A 1 542 ? 34.731 38.443 13.802 1.00 31.04 ? 595 ASN A OD1 1 ATOM 4345 N ND2 . ASN A 1 542 ? 34.088 38.299 15.938 1.00 28.69 ? 595 ASN A ND2 1 ATOM 4346 N N . PHE A 1 543 ? 31.096 42.517 14.403 1.00 20.70 ? 596 PHE A N 1 ATOM 4347 C CA . PHE A 1 543 ? 29.878 43.221 14.025 1.00 21.64 ? 596 PHE A CA 1 ATOM 4348 C C . PHE A 1 543 ? 30.191 44.658 13.655 1.00 18.58 ? 596 PHE A C 1 ATOM 4349 O O . PHE A 1 543 ? 31.090 45.267 14.224 1.00 23.83 ? 596 PHE A O 1 ATOM 4350 C CB . PHE A 1 543 ? 28.854 43.178 15.163 1.00 21.55 ? 596 PHE A CB 1 ATOM 4351 C CG . PHE A 1 543 ? 28.337 41.805 15.466 1.00 20.71 ? 596 PHE A CG 1 ATOM 4352 C CD1 . PHE A 1 543 ? 27.052 41.449 15.130 1.00 24.69 ? 596 PHE A CD1 1 ATOM 4353 C CD2 . PHE A 1 543 ? 29.137 40.880 16.110 1.00 23.14 ? 596 PHE A CD2 1 ATOM 4354 C CE1 . PHE A 1 543 ? 26.565 40.184 15.426 1.00 24.65 ? 596 PHE A CE1 1 ATOM 4355 C CE2 . PHE A 1 543 ? 28.670 39.626 16.405 1.00 25.11 ? 596 PHE A CE2 1 ATOM 4356 C CZ . PHE A 1 543 ? 27.372 39.272 16.069 1.00 26.72 ? 596 PHE A CZ 1 ATOM 4357 N N . ASN A 1 544 ? 29.454 45.200 12.695 1.00 25.12 ? 597 ASN A N 1 ATOM 4358 C CA . ASN A 1 544 ? 29.792 46.500 12.130 1.00 28.89 ? 597 ASN A CA 1 ATOM 4359 C C . ASN A 1 544 ? 28.982 47.607 12.782 1.00 30.98 ? 597 ASN A C 1 ATOM 4360 O O . ASN A 1 544 ? 28.336 47.385 13.802 1.00 26.88 ? 597 ASN A O 1 ATOM 4361 C CB . ASN A 1 544 ? 29.628 46.506 10.598 1.00 31.44 ? 597 ASN A CB 1 ATOM 4362 C CG . ASN A 1 544 ? 28.168 46.533 10.141 1.00 33.97 ? 597 ASN A CG 1 ATOM 4363 O OD1 . ASN A 1 544 ? 27.887 46.418 8.942 1.00 33.67 ? 597 ASN A OD1 1 ATOM 4364 N ND2 . ASN A 1 544 ? 27.240 46.671 11.081 1.00 28.60 ? 597 ASN A ND2 1 ATOM 4365 N N . LYS A 1 545 ? 29.044 48.802 12.205 1.00 33.22 ? 598 LYS A N 1 ATOM 4366 C CA . LYS A 1 545 ? 28.532 50.000 12.857 1.00 33.56 ? 598 LYS A CA 1 ATOM 4367 C C . LYS A 1 545 ? 27.037 49.878 13.072 1.00 32.19 ? 598 LYS A C 1 ATOM 4368 O O . LYS A 1 545 ? 26.461 50.542 13.933 1.00 30.45 ? 598 LYS A O 1 ATOM 4369 C CB . LYS A 1 545 ? 28.836 51.238 12.013 1.00 36.22 ? 598 LYS A CB 1 ATOM 4370 C CG . LYS A 1 545 ? 27.865 51.457 10.857 1.00 37.44 ? 598 LYS A CG 1 ATOM 4371 C CD . LYS A 1 545 ? 28.598 51.969 9.615 1.00 42.14 ? 598 LYS A CD 1 ATOM 4372 C CE . LYS A 1 545 ? 27.936 53.219 9.021 1.00 44.23 ? 598 LYS A CE 1 ATOM 4373 N NZ . LYS A 1 545 ? 26.499 52.995 8.689 1.00 45.55 ? 598 LYS A NZ 1 ATOM 4374 N N . ASP A 1 546 ? 26.400 49.023 12.289 1.00 31.20 ? 599 ASP A N 1 ATOM 4375 C CA . ASP A 1 546 ? 24.952 48.927 12.327 1.00 34.68 ? 599 ASP A CA 1 ATOM 4376 C C . ASP A 1 546 ? 24.499 47.650 13.019 1.00 30.71 ? 599 ASP A C 1 ATOM 4377 O O . ASP A 1 546 ? 23.314 47.351 13.046 1.00 31.48 ? 599 ASP A O 1 ATOM 4378 C CB . ASP A 1 546 ? 24.373 49.000 10.915 1.00 35.55 ? 599 ASP A CB 1 ATOM 4379 C CG . ASP A 1 546 ? 24.482 50.389 10.318 1.00 37.80 ? 599 ASP A CG 1 ATOM 4380 O OD1 . ASP A 1 546 ? 24.252 51.378 11.048 1.00 40.95 ? 599 ASP A OD1 1 ATOM 4381 O OD2 . ASP A 1 546 ? 24.802 50.591 9.135 1.00 40.68 ? 599 ASP A OD2 1 ATOM 4382 N N . GLY A 1 547 ? 25.445 46.903 13.579 1.00 32.23 ? 600 GLY A N 1 ATOM 4383 C CA . GLY A 1 547 ? 25.124 45.694 14.326 1.00 29.46 ? 600 GLY A CA 1 ATOM 4384 C C . GLY A 1 547 ? 25.013 44.445 13.463 1.00 29.39 ? 600 GLY A C 1 ATOM 4385 O O . GLY A 1 547 ? 24.529 43.412 13.915 1.00 28.76 ? 600 GLY A O 1 ATOM 4386 N N . ASP A 1 548 ? 25.465 44.530 12.216 1.00 29.29 ? 601 ASP A N 1 ATOM 4387 C CA . ASP A 1 548 ? 25.473 43.358 11.338 1.00 28.54 ? 601 ASP A CA 1 ATOM 4388 C C . ASP A 1 548 ? 26.796 42.608 11.419 1.00 25.75 ? 601 ASP A C 1 ATOM 4389 O O . ASP A 1 548 ? 27.867 43.201 11.518 1.00 27.13 ? 601 ASP A O 1 ATOM 4390 C CB . ASP A 1 548 ? 25.204 43.754 9.885 1.00 31.83 ? 601 ASP A CB 1 ATOM 4391 C CG . ASP A 1 548 ? 23.810 44.300 9.681 1.00 32.53 ? 601 ASP A CG 1 ATOM 4392 O OD1 . ASP A 1 548 ? 22.843 43.728 10.248 1.00 30.94 ? 601 ASP A OD1 1 ATOM 4393 O OD2 . ASP A 1 548 ? 23.594 45.301 8.967 1.00 33.63 ? 601 ASP A OD2 1 ATOM 4394 N N . LEU A 1 549 ? 26.700 41.290 11.374 1.00 27.53 ? 602 LEU A N 1 ATOM 4395 C CA . LEU A 1 549 ? 27.870 40.435 11.377 1.00 26.84 ? 602 LEU A CA 1 ATOM 4396 C C . LEU A 1 549 ? 28.511 40.452 9.997 1.00 28.27 ? 602 LEU A C 1 ATOM 4397 O O . LEU A 1 549 ? 28.094 39.735 9.088 1.00 31.07 ? 602 LEU A O 1 ATOM 4398 C CB . LEU A 1 549 ? 27.461 39.023 11.778 1.00 24.47 ? 602 LEU A CB 1 ATOM 4399 C CG . LEU A 1 549 ? 28.564 38.005 12.030 1.00 25.39 ? 602 LEU A CG 1 ATOM 4400 C CD1 . LEU A 1 549 ? 29.489 38.478 13.113 1.00 27.00 ? 602 LEU A CD1 1 ATOM 4401 C CD2 . LEU A 1 549 ? 27.926 36.689 12.402 1.00 23.74 ? 602 LEU A CD2 1 ATOM 4402 N N . VAL A 1 550 ? 29.530 41.281 9.849 1.00 30.15 ? 603 VAL A N 1 ATOM 4403 C CA . VAL A 1 550 ? 30.242 41.382 8.593 1.00 33.34 ? 603 VAL A CA 1 ATOM 4404 C C . VAL A 1 550 ? 31.680 41.819 8.836 1.00 31.74 ? 603 VAL A C 1 ATOM 4405 O O . VAL A 1 550 ? 31.952 42.701 9.652 1.00 28.75 ? 603 VAL A O 1 ATOM 4406 C CB . VAL A 1 550 ? 29.540 42.372 7.631 1.00 36.85 ? 603 VAL A CB 1 ATOM 4407 C CG1 . VAL A 1 550 ? 29.190 43.658 8.350 1.00 36.73 ? 603 VAL A CG1 1 ATOM 4408 C CG2 . VAL A 1 550 ? 30.418 42.661 6.424 1.00 39.69 ? 603 VAL A CG2 1 ATOM 4409 N N . ASP A 1 551 ? 32.598 41.187 8.110 1.00 31.46 ? 604 ASP A N 1 ATOM 4410 C CA . ASP A 1 551 ? 34.023 41.348 8.336 1.00 31.76 ? 604 ASP A CA 1 ATOM 4411 C C . ASP A 1 551 ? 34.492 42.711 7.842 1.00 31.23 ? 604 ASP A C 1 ATOM 4412 O O . ASP A 1 551 ? 34.558 42.948 6.638 1.00 30.78 ? 604 ASP A O 1 ATOM 4413 C CB . ASP A 1 551 ? 34.765 40.222 7.603 1.00 33.22 ? 604 ASP A CB 1 ATOM 4414 C CG . ASP A 1 551 ? 36.236 40.161 7.945 1.00 31.93 ? 604 ASP A CG 1 ATOM 4415 O OD1 . ASP A 1 551 ? 36.733 41.065 8.643 1.00 28.21 ? 604 ASP A OD1 1 ATOM 4416 O OD2 . ASP A 1 551 ? 36.979 39.234 7.547 1.00 33.63 ? 604 ASP A OD2 1 ATOM 4417 N N . TRP A 1 552 ? 34.828 43.619 8.755 1.00 28.44 ? 605 TRP A N 1 ATOM 4418 C CA . TRP A 1 552 ? 35.377 44.901 8.325 1.00 28.14 ? 605 TRP A CA 1 ATOM 4419 C C . TRP A 1 552 ? 36.857 45.000 8.635 1.00 25.32 ? 605 TRP A C 1 ATOM 4420 O O . TRP A 1 552 ? 37.419 46.092 8.700 1.00 22.45 ? 605 TRP A O 1 ATOM 4421 C CB . TRP A 1 552 ? 34.620 46.085 8.937 1.00 28.86 ? 605 TRP A CB 1 ATOM 4422 C CG . TRP A 1 552 ? 34.343 45.990 10.397 1.00 26.23 ? 605 TRP A CG 1 ATOM 4423 C CD1 . TRP A 1 552 ? 33.220 45.486 10.986 1.00 26.63 ? 605 TRP A CD1 1 ATOM 4424 C CD2 . TRP A 1 552 ? 35.176 46.451 11.460 1.00 24.38 ? 605 TRP A CD2 1 ATOM 4425 N NE1 . TRP A 1 552 ? 33.310 45.593 12.352 1.00 26.58 ? 605 TRP A NE1 1 ATOM 4426 C CE2 . TRP A 1 552 ? 34.504 46.179 12.672 1.00 23.80 ? 605 TRP A CE2 1 ATOM 4427 C CE3 . TRP A 1 552 ? 36.426 47.065 11.515 1.00 23.69 ? 605 TRP A CE3 1 ATOM 4428 C CZ2 . TRP A 1 552 ? 35.034 46.513 13.913 1.00 21.86 ? 605 TRP A CZ2 1 ATOM 4429 C CZ3 . TRP A 1 552 ? 36.960 47.388 12.753 1.00 25.17 ? 605 TRP A CZ3 1 ATOM 4430 C CH2 . TRP A 1 552 ? 36.262 47.110 13.935 1.00 22.88 ? 605 TRP A CH2 1 ATOM 4431 N N . TRP A 1 553 ? 37.481 43.843 8.821 1.00 27.33 ? 606 TRP A N 1 ATOM 4432 C CA . TRP A 1 553 ? 38.896 43.771 9.149 1.00 26.92 ? 606 TRP A CA 1 ATOM 4433 C C . TRP A 1 553 ? 39.690 43.293 7.935 1.00 27.93 ? 606 TRP A C 1 ATOM 4434 O O . TRP A 1 553 ? 39.225 42.438 7.181 1.00 29.65 ? 606 TRP A O 1 ATOM 4435 C CB . TRP A 1 553 ? 39.106 42.812 10.321 1.00 27.17 ? 606 TRP A CB 1 ATOM 4436 C CG . TRP A 1 553 ? 38.612 43.387 11.632 1.00 27.29 ? 606 TRP A CG 1 ATOM 4437 C CD1 . TRP A 1 553 ? 37.311 43.535 12.024 1.00 26.44 ? 606 TRP A CD1 1 ATOM 4438 C CD2 . TRP A 1 553 ? 39.410 43.913 12.696 1.00 25.29 ? 606 TRP A CD2 1 ATOM 4439 N NE1 . TRP A 1 553 ? 37.255 44.109 13.270 1.00 24.34 ? 606 TRP A NE1 1 ATOM 4440 C CE2 . TRP A 1 553 ? 38.529 44.349 13.707 1.00 25.09 ? 606 TRP A CE2 1 ATOM 4441 C CE3 . TRP A 1 553 ? 40.785 44.044 12.910 1.00 23.59 ? 606 TRP A CE3 1 ATOM 4442 C CZ2 . TRP A 1 553 ? 38.977 44.912 14.902 1.00 27.48 ? 606 TRP A CZ2 1 ATOM 4443 C CZ3 . TRP A 1 553 ? 41.227 44.607 14.092 1.00 26.54 ? 606 TRP A CZ3 1 ATOM 4444 C CH2 . TRP A 1 553 ? 40.322 45.028 15.079 1.00 27.58 ? 606 TRP A CH2 1 ATOM 4445 N N . THR A 1 554 ? 40.892 43.828 7.761 1.00 29.93 ? 607 THR A N 1 ATOM 4446 C CA . THR A 1 554 ? 41.864 43.205 6.871 1.00 30.20 ? 607 THR A CA 1 ATOM 4447 C C . THR A 1 554 ? 42.414 41.926 7.485 1.00 33.96 ? 607 THR A C 1 ATOM 4448 O O . THR A 1 554 ? 42.468 41.784 8.709 1.00 27.21 ? 607 THR A O 1 ATOM 4449 C CB . THR A 1 554 ? 43.006 44.169 6.556 1.00 30.32 ? 607 THR A CB 1 ATOM 4450 O OG1 . THR A 1 554 ? 43.815 44.374 7.718 1.00 27.53 ? 607 THR A OG1 1 ATOM 4451 C CG2 . THR A 1 554 ? 42.466 45.549 6.229 1.00 31.20 ? 607 THR A CG2 1 ATOM 4452 N N . GLN A 1 555 ? 42.813 40.997 6.620 1.00 33.03 ? 608 GLN A N 1 ATOM 4453 C CA . GLN A 1 555 ? 43.564 39.820 7.035 1.00 35.63 ? 608 GLN A CA 1 ATOM 4454 C C . GLN A 1 555 ? 44.614 40.143 8.087 1.00 30.96 ? 608 GLN A C 1 ATOM 4455 O O . GLN A 1 555 ? 44.638 39.529 9.153 1.00 33.72 ? 608 GLN A O 1 ATOM 4456 C CB . GLN A 1 555 ? 44.237 39.167 5.832 1.00 40.52 ? 608 GLN A CB 1 ATOM 4457 C CG . GLN A 1 555 ? 43.665 37.814 5.469 1.00 47.43 ? 608 GLN A CG 1 ATOM 4458 C CD . GLN A 1 555 ? 42.531 37.915 4.471 1.00 51.31 ? 608 GLN A CD 1 ATOM 4459 O OE1 . GLN A 1 555 ? 42.724 37.668 3.275 1.00 51.29 ? 608 GLN A OE1 1 ATOM 4460 N NE2 . GLN A 1 555 ? 41.344 38.283 4.955 1.00 53.44 ? 608 GLN A NE2 1 ATOM 4461 N N . GLN A 1 556 ? 45.497 41.090 7.795 1.00 26.80 ? 609 GLN A N 1 ATOM 4462 C CA . GLN A 1 556 ? 46.624 41.326 8.680 1.00 23.18 ? 609 GLN A CA 1 ATOM 4463 C C . GLN A 1 556 ? 46.157 41.823 10.047 1.00 25.44 ? 609 GLN A C 1 ATOM 4464 O O . GLN A 1 556 ? 46.642 41.361 11.076 1.00 22.08 ? 609 GLN A O 1 ATOM 4465 C CB . GLN A 1 556 ? 47.600 42.328 8.087 1.00 23.24 ? 609 GLN A CB 1 ATOM 4466 C CG . GLN A 1 556 ? 48.964 42.266 8.727 1.00 23.96 ? 609 GLN A CG 1 ATOM 4467 C CD . GLN A 1 556 ? 49.529 40.857 8.794 1.00 28.10 ? 609 GLN A CD 1 ATOM 4468 O OE1 . GLN A 1 556 ? 49.857 40.359 9.876 1.00 32.00 ? 609 GLN A OE1 1 ATOM 4469 N NE2 . GLN A 1 556 ? 49.662 40.220 7.644 1.00 26.36 ? 609 GLN A NE2 1 ATOM 4470 N N . SER A 1 557 ? 45.239 42.785 10.045 1.00 25.19 ? 610 SER A N 1 ATOM 4471 C CA . SER A 1 557 ? 44.815 43.430 11.280 1.00 26.85 ? 610 SER A CA 1 ATOM 4472 C C . SER A 1 557 ? 44.027 42.445 12.145 1.00 25.96 ? 610 SER A C 1 ATOM 4473 O O . SER A 1 557 ? 44.095 42.491 13.365 1.00 31.50 ? 610 SER A O 1 ATOM 4474 C CB . SER A 1 557 ? 43.967 44.654 10.961 1.00 28.13 ? 610 SER A CB 1 ATOM 4475 O OG . SER A 1 557 ? 44.797 45.732 10.553 1.00 27.81 ? 610 SER A OG 1 ATOM 4476 N N . ALA A 1 558 ? 43.290 41.552 11.494 1.00 26.49 ? 611 ALA A N 1 ATOM 4477 C CA . ALA A 1 558 ? 42.552 40.509 12.186 1.00 27.20 ? 611 ALA A CA 1 ATOM 4478 C C . ALA A 1 558 ? 43.484 39.465 12.788 1.00 27.56 ? 611 ALA A C 1 ATOM 4479 O O . ALA A 1 558 ? 43.257 38.998 13.896 1.00 23.52 ? 611 ALA A O 1 ATOM 4480 C CB . ALA A 1 558 ? 41.569 39.851 11.242 1.00 28.32 ? 611 ALA A CB 1 ATOM 4481 N N . SER A 1 559 ? 44.531 39.093 12.058 1.00 26.15 ? 612 SER A N 1 ATOM 4482 C CA . SER A 1 559 ? 45.539 38.204 12.607 1.00 25.73 ? 612 SER A CA 1 ATOM 4483 C C . SER A 1 559 ? 46.286 38.881 13.735 1.00 25.23 ? 612 SER A C 1 ATOM 4484 O O . SER A 1 559 ? 46.662 38.239 14.715 1.00 28.95 ? 612 SER A O 1 ATOM 4485 C CB . SER A 1 559 ? 46.530 37.750 11.524 1.00 28.40 ? 612 SER A CB 1 ATOM 4486 O OG . SER A 1 559 ? 47.738 37.302 12.125 1.00 27.80 ? 612 SER A OG 1 ATOM 4487 N N . ASN A 1 560 ? 46.508 40.187 13.613 1.00 23.36 ? 613 ASN A N 1 ATOM 4488 C CA . ASN A 1 560 ? 47.219 40.911 14.649 1.00 23.08 ? 613 ASN A CA 1 ATOM 4489 C C . ASN A 1 560 ? 46.393 41.012 15.938 1.00 23.54 ? 613 ASN A C 1 ATOM 4490 O O . ASN A 1 560 ? 46.935 40.945 17.041 1.00 26.35 ? 613 ASN A O 1 ATOM 4491 C CB . ASN A 1 560 ? 47.595 42.305 14.162 1.00 26.82 ? 613 ASN A CB 1 ATOM 4492 C CG . ASN A 1 560 ? 48.612 42.269 13.031 1.00 29.07 ? 613 ASN A CG 1 ATOM 4493 O OD1 . ASN A 1 560 ? 49.222 41.236 12.769 1.00 24.99 ? 613 ASN A OD1 1 ATOM 4494 N ND2 . ASN A 1 560 ? 48.796 43.403 12.361 1.00 29.79 ? 613 ASN A ND2 1 ATOM 4495 N N . PHE A 1 561 ? 45.087 41.170 15.786 1.00 26.54 ? 614 PHE A N 1 ATOM 4496 C CA . PHE A 1 561 ? 44.177 41.213 16.938 1.00 26.12 ? 614 PHE A CA 1 ATOM 4497 C C . PHE A 1 561 ? 44.302 39.922 17.735 1.00 28.09 ? 614 PHE A C 1 ATOM 4498 O O . PHE A 1 561 ? 44.470 39.933 18.957 1.00 23.06 ? 614 PHE A O 1 ATOM 4499 C CB . PHE A 1 561 ? 42.746 41.385 16.453 1.00 26.09 ? 614 PHE A CB 1 ATOM 4500 C CG . PHE A 1 561 ? 41.717 41.339 17.548 1.00 25.93 ? 614 PHE A CG 1 ATOM 4501 C CD1 . PHE A 1 561 ? 41.204 40.130 17.984 1.00 26.38 ? 614 PHE A CD1 1 ATOM 4502 C CD2 . PHE A 1 561 ? 41.269 42.506 18.141 1.00 27.55 ? 614 PHE A CD2 1 ATOM 4503 C CE1 . PHE A 1 561 ? 40.238 40.083 18.990 1.00 29.62 ? 614 PHE A CE1 1 ATOM 4504 C CE2 . PHE A 1 561 ? 40.291 42.467 19.146 1.00 29.53 ? 614 PHE A CE2 1 ATOM 4505 C CZ . PHE A 1 561 ? 39.782 41.253 19.571 1.00 26.89 ? 614 PHE A CZ 1 ATOM 4506 N N . LYS A 1 562 ? 44.249 38.803 17.027 1.00 28.54 ? 615 LYS A N 1 ATOM 4507 C CA . LYS A 1 562 ? 44.409 37.509 17.665 1.00 29.82 ? 615 LYS A CA 1 ATOM 4508 C C . LYS A 1 562 ? 45.724 37.445 18.417 1.00 29.16 ? 615 LYS A C 1 ATOM 4509 O O . LYS A 1 562 ? 45.755 37.053 19.584 1.00 27.32 ? 615 LYS A O 1 ATOM 4510 C CB . LYS A 1 562 ? 44.266 36.386 16.633 1.00 32.71 ? 615 LYS A CB 1 ATOM 4511 C CG . LYS A 1 562 ? 42.913 36.438 15.921 1.00 31.54 ? 615 LYS A CG 1 ATOM 4512 C CD . LYS A 1 562 ? 42.583 35.148 15.209 1.00 34.05 ? 615 LYS A CD 1 ATOM 4513 C CE . LYS A 1 562 ? 41.479 35.351 14.180 1.00 36.42 ? 615 LYS A CE 1 ATOM 4514 N NZ . LYS A 1 562 ? 41.714 34.567 12.933 1.00 35.03 ? 615 LYS A NZ 1 ATOM 4515 N N . GLU A 1 563 ? 46.812 37.865 17.772 1.00 27.84 ? 616 GLU A N 1 ATOM 4516 C CA . GLU A 1 563 ? 48.097 37.881 18.432 1.00 25.75 ? 616 GLU A CA 1 ATOM 4517 C C . GLU A 1 563 ? 48.105 38.717 19.704 1.00 26.76 ? 616 GLU A C 1 ATOM 4518 O O . GLU A 1 563 ? 48.594 38.261 20.742 1.00 23.27 ? 616 GLU A O 1 ATOM 4519 C CB . GLU A 1 563 ? 49.206 38.397 17.496 1.00 31.22 ? 616 GLU A CB 1 ATOM 4520 C CG . GLU A 1 563 ? 49.917 37.309 16.716 1.00 34.74 ? 616 GLU A CG 1 ATOM 4521 C CD . GLU A 1 563 ? 51.134 37.831 15.975 1.00 42.04 ? 616 GLU A CD 1 ATOM 4522 O OE1 . GLU A 1 563 ? 51.826 38.730 16.513 1.00 46.47 ? 616 GLU A OE1 1 ATOM 4523 O OE2 . GLU A 1 563 ? 51.398 37.340 14.855 1.00 44.95 ? 616 GLU A OE2 1 ATOM 4524 N N . GLN A 1 564 ? 47.613 39.948 19.622 1.00 23.78 ? 617 GLN A N 1 ATOM 4525 C CA . GLN A 1 564 ? 47.644 40.829 20.779 1.00 24.47 ? 617 GLN A CA 1 ATOM 4526 C C . GLN A 1 564 ? 46.818 40.194 21.904 1.00 22.80 ? 617 GLN A C 1 ATOM 4527 O O . GLN A 1 564 ? 47.177 40.265 23.073 1.00 22.12 ? 617 GLN A O 1 ATOM 4528 C CB . GLN A 1 564 ? 47.080 42.205 20.433 1.00 27.65 ? 617 GLN A CB 1 ATOM 4529 C CG . GLN A 1 564 ? 47.892 43.012 19.418 1.00 28.12 ? 617 GLN A CG 1 ATOM 4530 C CD . GLN A 1 564 ? 49.372 43.109 19.763 1.00 31.19 ? 617 GLN A CD 1 ATOM 4531 O OE1 . GLN A 1 564 ? 50.219 42.880 18.904 1.00 31.22 ? 617 GLN A OE1 1 ATOM 4532 N NE2 . GLN A 1 564 ? 49.683 43.447 21.012 1.00 31.53 ? 617 GLN A NE2 1 ATOM 4533 N N . SER A 1 565 ? 45.709 39.574 21.540 1.00 22.74 ? 618 SER A N 1 ATOM 4534 C CA . SER A 1 565 ? 44.757 39.102 22.539 1.00 24.45 ? 618 SER A CA 1 ATOM 4535 C C . SER A 1 565 ? 45.225 37.789 23.144 1.00 26.23 ? 618 SER A C 1 ATOM 4536 O O . SER A 1 565 ? 44.930 37.472 24.301 1.00 23.33 ? 618 SER A O 1 ATOM 4537 C CB . SER A 1 565 ? 43.373 38.947 21.915 1.00 25.12 ? 618 SER A CB 1 ATOM 4538 O OG . SER A 1 565 ? 43.384 37.984 20.886 1.00 28.16 ? 618 SER A OG 1 ATOM 4539 N N . GLN A 1 566 ? 45.977 37.025 22.363 1.00 25.88 ? 619 GLN A N 1 ATOM 4540 C CA . GLN A 1 566 ? 46.568 35.794 22.864 1.00 26.00 ? 619 GLN A CA 1 ATOM 4541 C C . GLN A 1 566 ? 47.393 36.028 24.129 1.00 22.82 ? 619 GLN A C 1 ATOM 4542 O O . GLN A 1 566 ? 47.443 35.175 24.997 1.00 19.51 ? 619 GLN A O 1 ATOM 4543 C CB . GLN A 1 566 ? 47.427 35.120 21.780 1.00 27.88 ? 619 GLN A CB 1 ATOM 4544 C CG . GLN A 1 566 ? 47.934 33.732 22.167 1.00 27.58 ? 619 GLN A CG 1 ATOM 4545 C CD . GLN A 1 566 ? 46.811 32.721 22.363 1.00 30.68 ? 619 GLN A CD 1 ATOM 4546 O OE1 . GLN A 1 566 ? 46.969 31.753 23.107 1.00 33.79 ? 619 GLN A OE1 1 ATOM 4547 N NE2 . GLN A 1 566 ? 45.685 32.937 21.694 1.00 31.28 ? 619 GLN A NE2 1 ATOM 4548 N N . CYS A 1 567 ? 48.037 37.186 24.245 1.00 24.00 ? 620 CYS A N 1 ATOM 4549 C CA . CYS A 1 567 ? 48.772 37.500 25.460 1.00 20.89 ? 620 CYS A CA 1 ATOM 4550 C C . CYS A 1 567 ? 47.851 37.416 26.693 1.00 21.79 ? 620 CYS A C 1 ATOM 4551 O O . CYS A 1 567 ? 48.257 36.961 27.766 1.00 19.50 ? 620 CYS A O 1 ATOM 4552 C CB . CYS A 1 567 ? 49.391 38.898 25.348 1.00 22.79 ? 620 CYS A CB 1 ATOM 4553 S SG . CYS A 1 567 ? 50.392 39.383 26.756 1.00 27.28 ? 620 CYS A SG 1 ATOM 4554 N N . MET A 1 568 ? 46.606 37.852 26.544 1.00 22.16 ? 621 MET A N 1 ATOM 4555 C CA . MET A 1 568 ? 45.683 37.865 27.684 1.00 21.47 ? 621 MET A CA 1 ATOM 4556 C C . MET A 1 568 ? 45.120 36.475 27.964 1.00 20.92 ? 621 MET A C 1 ATOM 4557 O O . MET A 1 568 ? 44.857 36.122 29.107 1.00 20.10 ? 621 MET A O 1 ATOM 4558 C CB . MET A 1 568 ? 44.546 38.862 27.443 1.00 21.01 ? 621 MET A CB 1 ATOM 4559 C CG . MET A 1 568 ? 45.016 40.318 27.408 1.00 20.10 ? 621 MET A CG 1 ATOM 4560 S SD . MET A 1 568 ? 43.722 41.519 27.089 1.00 19.62 ? 621 MET A SD 1 ATOM 4561 C CE . MET A 1 568 ? 44.673 43.044 26.856 1.00 22.88 ? 621 MET A CE 1 ATOM 4562 N N . VAL A 1 569 ? 44.946 35.681 26.917 1.00 22.43 ? 622 VAL A N 1 ATOM 4563 C CA . VAL A 1 569 ? 44.546 34.290 27.079 1.00 22.50 ? 622 VAL A CA 1 ATOM 4564 C C . VAL A 1 569 ? 45.539 33.566 27.987 1.00 24.90 ? 622 VAL A C 1 ATOM 4565 O O . VAL A 1 569 ? 45.138 32.890 28.937 1.00 21.86 ? 622 VAL A O 1 ATOM 4566 C CB . VAL A 1 569 ? 44.441 33.582 25.720 1.00 23.02 ? 622 VAL A CB 1 ATOM 4567 C CG1 . VAL A 1 569 ? 44.279 32.074 25.903 1.00 23.16 ? 622 VAL A CG1 1 ATOM 4568 C CG2 . VAL A 1 569 ? 43.267 34.141 24.916 1.00 22.98 ? 622 VAL A CG2 1 ATOM 4569 N N . TYR A 1 570 ? 46.831 33.743 27.711 1.00 23.33 ? 623 TYR A N 1 ATOM 4570 C CA . TYR A 1 570 ? 47.897 33.155 28.523 1.00 25.13 ? 623 TYR A CA 1 ATOM 4571 C C . TYR A 1 570 ? 48.027 33.758 29.934 1.00 22.33 ? 623 TYR A C 1 ATOM 4572 O O . TYR A 1 570 ? 48.214 33.033 30.902 1.00 19.57 ? 623 TYR A O 1 ATOM 4573 C CB . TYR A 1 570 ? 49.247 33.300 27.815 1.00 27.07 ? 623 TYR A CB 1 ATOM 4574 C CG . TYR A 1 570 ? 49.421 32.413 26.608 1.00 29.41 ? 623 TYR A CG 1 ATOM 4575 C CD1 . TYR A 1 570 ? 48.733 31.211 26.493 1.00 32.91 ? 623 TYR A CD1 1 ATOM 4576 C CD2 . TYR A 1 570 ? 50.282 32.778 25.579 1.00 33.73 ? 623 TYR A CD2 1 ATOM 4577 C CE1 . TYR A 1 570 ? 48.897 30.398 25.383 1.00 36.19 ? 623 TYR A CE1 1 ATOM 4578 C CE2 . TYR A 1 570 ? 50.452 31.974 24.466 1.00 33.60 ? 623 TYR A CE2 1 ATOM 4579 C CZ . TYR A 1 570 ? 49.761 30.789 24.375 1.00 35.22 ? 623 TYR A CZ 1 ATOM 4580 O OH . TYR A 1 570 ? 49.930 29.996 23.271 1.00 38.33 ? 623 TYR A OH 1 ATOM 4581 N N . GLN A 1 571 ? 47.962 35.078 30.048 1.00 19.91 ? 624 GLN A N 1 ATOM 4582 C CA . GLN A 1 571 ? 48.094 35.737 31.352 1.00 18.62 ? 624 GLN A CA 1 ATOM 4583 C C . GLN A 1 571 ? 47.022 35.260 32.336 1.00 21.72 ? 624 GLN A C 1 ATOM 4584 O O . GLN A 1 571 ? 47.323 34.904 33.480 1.00 19.79 ? 624 GLN A O 1 ATOM 4585 C CB . GLN A 1 571 ? 48.021 37.258 31.193 1.00 20.10 ? 624 GLN A CB 1 ATOM 4586 C CG . GLN A 1 571 ? 47.895 38.027 32.495 1.00 22.08 ? 624 GLN A CG 1 ATOM 4587 C CD . GLN A 1 571 ? 47.542 39.496 32.271 1.00 22.82 ? 624 GLN A CD 1 ATOM 4588 O OE1 . GLN A 1 571 ? 47.053 39.862 31.208 1.00 20.62 ? 624 GLN A OE1 1 ATOM 4589 N NE2 . GLN A 1 571 ? 47.799 40.328 33.265 1.00 23.03 ? 624 GLN A NE2 1 ATOM 4590 N N . TYR A 1 572 ? 45.772 35.261 31.893 1.00 18.90 ? 625 TYR A N 1 ATOM 4591 C CA . TYR A 1 572 ? 44.662 34.969 32.792 1.00 20.19 ? 625 TYR A CA 1 ATOM 4592 C C . TYR A 1 572 ? 44.500 33.463 32.976 1.00 18.21 ? 625 TYR A C 1 ATOM 4593 O O . TYR A 1 572 ? 44.179 32.996 34.063 1.00 20.01 ? 625 TYR A O 1 ATOM 4594 C CB . TYR A 1 572 ? 43.368 35.599 32.252 1.00 16.94 ? 625 TYR A CB 1 ATOM 4595 C CG . TYR A 1 572 ? 43.263 37.093 32.499 1.00 16.02 ? 625 TYR A CG 1 ATOM 4596 C CD1 . TYR A 1 572 ? 43.931 38.001 31.695 1.00 17.10 ? 625 TYR A CD1 1 ATOM 4597 C CD2 . TYR A 1 572 ? 42.482 37.595 33.539 1.00 14.91 ? 625 TYR A CD2 1 ATOM 4598 C CE1 . TYR A 1 572 ? 43.826 39.369 31.911 1.00 17.45 ? 625 TYR A CE1 1 ATOM 4599 C CE2 . TYR A 1 572 ? 42.369 38.959 33.758 1.00 16.72 ? 625 TYR A CE2 1 ATOM 4600 C CZ . TYR A 1 572 ? 43.040 39.842 32.947 1.00 20.27 ? 625 TYR A CZ 1 ATOM 4601 O OH . TYR A 1 572 ? 42.935 41.200 33.172 1.00 19.13 ? 625 TYR A OH 1 ATOM 4602 N N . GLY A 1 573 ? 44.740 32.709 31.906 1.00 23.53 ? 626 GLY A N 1 ATOM 4603 C CA . GLY A 1 573 ? 44.806 31.257 31.970 1.00 21.11 ? 626 GLY A CA 1 ATOM 4604 C C . GLY A 1 573 ? 45.813 30.754 32.990 1.00 22.88 ? 626 GLY A C 1 ATOM 4605 O O . GLY A 1 573 ? 45.687 29.646 33.524 1.00 24.79 ? 626 GLY A O 1 ATOM 4606 N N . ASN A 1 574 ? 46.822 31.566 33.255 1.00 22.61 ? 627 ASN A N 1 ATOM 4607 C CA . ASN A 1 574 ? 47.853 31.214 34.217 1.00 23.91 ? 627 ASN A CA 1 ATOM 4608 C C . ASN A 1 574 ? 47.504 31.602 35.645 1.00 24.41 ? 627 ASN A C 1 ATOM 4609 O O . ASN A 1 574 ? 48.247 31.293 36.575 1.00 24.16 ? 627 ASN A O 1 ATOM 4610 C CB . ASN A 1 574 ? 49.162 31.891 33.836 1.00 27.22 ? 627 ASN A CB 1 ATOM 4611 C CG . ASN A 1 574 ? 50.054 30.992 33.036 1.00 30.82 ? 627 ASN A CG 1 ATOM 4612 O OD1 . ASN A 1 574 ? 51.002 30.428 33.565 1.00 35.55 ? 627 ASN A OD1 1 ATOM 4613 N ND2 . ASN A 1 574 ? 49.742 30.831 31.756 1.00 33.85 ? 627 ASN A ND2 1 ATOM 4614 N N . PHE A 1 575 ? 46.388 32.296 35.833 1.00 20.69 ? 628 PHE A N 1 ATOM 4615 C CA . PHE A 1 575 ? 45.921 32.546 37.191 1.00 20.42 ? 628 PHE A CA 1 ATOM 4616 C C . PHE A 1 575 ? 45.273 31.285 37.755 1.00 22.86 ? 628 PHE A C 1 ATOM 4617 O O . PHE A 1 575 ? 44.374 30.718 37.142 1.00 23.39 ? 628 PHE A O 1 ATOM 4618 C CB . PHE A 1 575 ? 44.913 33.698 37.224 1.00 19.87 ? 628 PHE A CB 1 ATOM 4619 C CG . PHE A 1 575 ? 45.513 35.051 36.995 1.00 20.55 ? 628 PHE A CG 1 ATOM 4620 C CD1 . PHE A 1 575 ? 46.643 35.460 37.684 1.00 21.01 ? 628 PHE A CD1 1 ATOM 4621 C CD2 . PHE A 1 575 ? 44.915 35.938 36.124 1.00 21.61 ? 628 PHE A CD2 1 ATOM 4622 C CE1 . PHE A 1 575 ? 47.185 36.714 37.476 1.00 22.33 ? 628 PHE A CE1 1 ATOM 4623 C CE2 . PHE A 1 575 ? 45.447 37.194 35.913 1.00 22.11 ? 628 PHE A CE2 1 ATOM 4624 C CZ . PHE A 1 575 ? 46.584 37.587 36.595 1.00 21.15 ? 628 PHE A CZ 1 ATOM 4625 N N . SER A 1 576 ? 45.710 30.850 38.930 1.00 24.01 ? 629 SER A N 1 ATOM 4626 C CA . SER A 1 576 ? 45.004 29.775 39.617 1.00 25.17 ? 629 SER A CA 1 ATOM 4627 C C . SER A 1 576 ? 44.267 30.291 40.840 1.00 21.75 ? 629 SER A C 1 ATOM 4628 O O . SER A 1 576 ? 44.727 31.206 41.537 1.00 21.68 ? 629 SER A O 1 ATOM 4629 C CB . SER A 1 576 ? 45.949 28.627 40.004 1.00 31.03 ? 629 SER A CB 1 ATOM 4630 O OG . SER A 1 576 ? 47.093 29.096 40.685 1.00 34.10 ? 629 SER A OG 1 ATOM 4631 N N . TRP A 1 577 ? 43.116 29.684 41.091 1.00 21.64 ? 630 TRP A N 1 ATOM 4632 C CA . TRP A 1 577 ? 42.109 30.246 41.971 1.00 18.19 ? 630 TRP A CA 1 ATOM 4633 C C . TRP A 1 577 ? 41.894 29.315 43.152 1.00 15.67 ? 630 TRP A C 1 ATOM 4634 O O . TRP A 1 577 ? 41.304 28.231 43.010 1.00 18.56 ? 630 TRP A O 1 ATOM 4635 C CB . TRP A 1 577 ? 40.801 30.443 41.208 1.00 18.53 ? 630 TRP A CB 1 ATOM 4636 C CG . TRP A 1 577 ? 39.816 31.336 41.926 1.00 21.04 ? 630 TRP A CG 1 ATOM 4637 C CD1 . TRP A 1 577 ? 40.046 32.092 43.033 1.00 20.41 ? 630 TRP A CD1 1 ATOM 4638 C CD2 . TRP A 1 577 ? 38.447 31.542 41.579 1.00 18.66 ? 630 TRP A CD2 1 ATOM 4639 N NE1 . TRP A 1 577 ? 38.899 32.759 43.403 1.00 20.79 ? 630 TRP A NE1 1 ATOM 4640 C CE2 . TRP A 1 577 ? 37.904 32.445 42.518 1.00 21.23 ? 630 TRP A CE2 1 ATOM 4641 C CE3 . TRP A 1 577 ? 37.625 31.068 40.560 1.00 19.66 ? 630 TRP A CE3 1 ATOM 4642 C CZ2 . TRP A 1 577 ? 36.579 32.872 42.467 1.00 22.10 ? 630 TRP A CZ2 1 ATOM 4643 C CZ3 . TRP A 1 577 ? 36.314 31.496 40.507 1.00 19.09 ? 630 TRP A CZ3 1 ATOM 4644 C CH2 . TRP A 1 577 ? 35.803 32.382 41.459 1.00 20.74 ? 630 TRP A CH2 1 ATOM 4645 N N . ASP A 1 578 ? 42.396 29.723 44.309 1.00 20.38 ? 631 ASP A N 1 ATOM 4646 C CA . ASP A 1 578 ? 42.356 28.872 45.482 1.00 24.95 ? 631 ASP A CA 1 ATOM 4647 C C . ASP A 1 578 ? 40.923 28.420 45.754 1.00 25.93 ? 631 ASP A C 1 ATOM 4648 O O . ASP A 1 578 ? 40.680 27.252 46.034 1.00 24.23 ? 631 ASP A O 1 ATOM 4649 C CB . ASP A 1 578 ? 42.963 29.572 46.704 1.00 29.16 ? 631 ASP A CB 1 ATOM 4650 C CG . ASP A 1 578 ? 42.472 31.001 46.886 1.00 32.81 ? 631 ASP A CG 1 ATOM 4651 O OD1 . ASP A 1 578 ? 42.950 31.651 47.838 1.00 37.49 ? 631 ASP A OD1 1 ATOM 4652 O OD2 . ASP A 1 578 ? 41.622 31.565 46.160 1.00 32.06 ? 631 ASP A OD2 1 ATOM 4653 N N . LEU A 1 579 ? 39.963 29.330 45.635 1.00 24.84 ? 632 LEU A N 1 ATOM 4654 C CA . LEU A 1 579 ? 38.602 29.023 46.084 1.00 24.40 ? 632 LEU A CA 1 ATOM 4655 C C . LEU A 1 579 ? 37.962 27.988 45.171 1.00 22.67 ? 632 LEU A C 1 ATOM 4656 O O . LEU A 1 579 ? 37.057 27.263 45.576 1.00 20.89 ? 632 LEU A O 1 ATOM 4657 C CB . LEU A 1 579 ? 37.746 30.287 46.147 1.00 25.98 ? 632 LEU A CB 1 ATOM 4658 C CG . LEU A 1 579 ? 38.225 31.356 47.129 1.00 27.05 ? 632 LEU A CG 1 ATOM 4659 C CD1 . LEU A 1 579 ? 37.319 32.569 47.050 1.00 28.81 ? 632 LEU A CD1 1 ATOM 4660 C CD2 . LEU A 1 579 ? 38.286 30.819 48.553 1.00 28.72 ? 632 LEU A CD2 1 ATOM 4661 N N . ALA A 1 580 ? 38.458 27.902 43.942 1.00 21.64 ? 633 ALA A N 1 ATOM 4662 C CA . ALA A 1 580 ? 38.005 26.894 43.003 1.00 21.29 ? 633 ALA A CA 1 ATOM 4663 C C . ALA A 1 580 ? 38.949 25.696 42.991 1.00 26.25 ? 633 ALA A C 1 ATOM 4664 O O . ALA A 1 580 ? 39.062 25.003 41.979 1.00 25.87 ? 633 ALA A O 1 ATOM 4665 C CB . ALA A 1 580 ? 37.902 27.492 41.598 1.00 21.50 ? 633 ALA A CB 1 ATOM 4666 N N . GLY A 1 581 ? 39.629 25.464 44.110 1.00 25.24 ? 634 GLY A N 1 ATOM 4667 C CA . GLY A 1 581 ? 40.410 24.248 44.289 1.00 26.09 ? 634 GLY A CA 1 ATOM 4668 C C . GLY A 1 581 ? 41.762 24.283 43.601 1.00 25.93 ? 634 GLY A C 1 ATOM 4669 O O . GLY A 1 581 ? 42.364 23.240 43.353 1.00 23.30 ? 634 GLY A O 1 ATOM 4670 N N . GLY A 1 582 ? 42.239 25.482 43.286 1.00 25.73 ? 635 GLY A N 1 ATOM 4671 C CA . GLY A 1 582 ? 43.495 25.649 42.576 1.00 24.24 ? 635 GLY A CA 1 ATOM 4672 C C . GLY A 1 582 ? 43.402 25.611 41.057 1.00 24.80 ? 635 GLY A C 1 ATOM 4673 O O . GLY A 1 582 ? 44.404 25.800 40.369 1.00 24.75 ? 635 GLY A O 1 ATOM 4674 N N . GLN A 1 583 ? 42.208 25.386 40.519 1.00 21.63 ? 636 GLN A N 1 ATOM 4675 C CA . GLN A 1 583 ? 42.022 25.431 39.073 1.00 23.39 ? 636 GLN A CA 1 ATOM 4676 C C . GLN A 1 583 ? 42.451 26.782 38.477 1.00 24.21 ? 636 GLN A C 1 ATOM 4677 O O . GLN A 1 583 ? 42.324 27.831 39.110 1.00 19.97 ? 636 GLN A O 1 ATOM 4678 C CB . GLN A 1 583 ? 40.557 25.201 38.725 1.00 24.46 ? 636 GLN A CB 1 ATOM 4679 C CG . GLN A 1 583 ? 40.043 23.804 38.983 1.00 26.68 ? 636 GLN A CG 1 ATOM 4680 C CD . GLN A 1 583 ? 38.581 23.698 38.621 1.00 26.74 ? 636 GLN A CD 1 ATOM 4681 O OE1 . GLN A 1 583 ? 38.246 23.374 37.480 1.00 29.53 ? 636 GLN A OE1 1 ATOM 4682 N NE2 . GLN A 1 583 ? 37.702 24.022 39.573 1.00 24.33 ? 636 GLN A NE2 1 ATOM 4683 N N . HIS A 1 584 ? 42.949 26.726 37.245 1.00 24.20 ? 637 HIS A N 1 ATOM 4684 C CA . HIS A 1 584 ? 43.277 27.903 36.451 1.00 26.72 ? 637 HIS A CA 1 ATOM 4685 C C . HIS A 1 584 ? 42.009 28.463 35.851 1.00 20.59 ? 637 HIS A C 1 ATOM 4686 O O . HIS A 1 584 ? 41.110 27.716 35.487 1.00 18.46 ? 637 HIS A O 1 ATOM 4687 C CB . HIS A 1 584 ? 44.213 27.527 35.309 1.00 31.28 ? 637 HIS A CB 1 ATOM 4688 C CG . HIS A 1 584 ? 45.643 27.386 35.720 1.00 39.11 ? 637 HIS A CG 1 ATOM 4689 N ND1 . HIS A 1 584 ? 46.105 26.309 36.446 1.00 45.65 ? 637 HIS A ND1 1 ATOM 4690 C CD2 . HIS A 1 584 ? 46.716 28.181 35.501 1.00 42.41 ? 637 HIS A CD2 1 ATOM 4691 C CE1 . HIS A 1 584 ? 47.401 26.451 36.662 1.00 45.83 ? 637 HIS A CE1 1 ATOM 4692 N NE2 . HIS A 1 584 ? 47.796 27.579 36.100 1.00 44.21 ? 637 HIS A NE2 1 ATOM 4693 N N . LEU A 1 585 ? 41.951 29.779 35.725 1.00 19.88 ? 638 LEU A N 1 ATOM 4694 C CA . LEU A 1 585 ? 40.881 30.411 34.963 1.00 20.99 ? 638 LEU A CA 1 ATOM 4695 C C . LEU A 1 585 ? 40.906 29.903 33.534 1.00 21.01 ? 638 LEU A C 1 ATOM 4696 O O . LEU A 1 585 ? 41.944 29.481 33.041 1.00 19.33 ? 638 LEU A O 1 ATOM 4697 C CB . LEU A 1 585 ? 41.040 31.929 34.962 1.00 17.37 ? 638 LEU A CB 1 ATOM 4698 C CG . LEU A 1 585 ? 41.179 32.648 36.299 1.00 18.88 ? 638 LEU A CG 1 ATOM 4699 C CD1 . LEU A 1 585 ? 41.298 34.127 36.044 1.00 21.35 ? 638 LEU A CD1 1 ATOM 4700 C CD2 . LEU A 1 585 ? 40.001 32.362 37.218 1.00 18.82 ? 638 LEU A CD2 1 ATOM 4701 N N . ASN A 1 586 ? 39.763 29.970 32.859 1.00 21.41 ? 639 ASN A N 1 ATOM 4702 C CA . ASN A 1 586 ? 39.722 29.766 31.424 1.00 18.63 ? 639 ASN A CA 1 ATOM 4703 C C . ASN A 1 586 ? 39.997 31.057 30.656 1.00 22.27 ? 639 ASN A C 1 ATOM 4704 O O . ASN A 1 586 ? 39.142 31.955 30.567 1.00 19.50 ? 639 ASN A O 1 ATOM 4705 C CB . ASN A 1 586 ? 38.380 29.180 31.014 1.00 19.76 ? 639 ASN A CB 1 ATOM 4706 C CG . ASN A 1 586 ? 38.394 28.605 29.608 1.00 22.60 ? 639 ASN A CG 1 ATOM 4707 O OD1 . ASN A 1 586 ? 38.799 29.273 28.651 1.00 23.31 ? 639 ASN A OD1 1 ATOM 4708 N ND2 . ASN A 1 586 ? 37.914 27.374 29.471 1.00 20.74 ? 639 ASN A ND2 1 ATOM 4709 N N . GLY A 1 587 ? 41.200 31.137 30.098 1.00 19.79 ? 640 GLY A N 1 ATOM 4710 C CA . GLY A 1 587 ? 41.682 32.359 29.491 1.00 20.21 ? 640 GLY A CA 1 ATOM 4711 C C . GLY A 1 587 ? 41.008 32.649 28.165 1.00 19.62 ? 640 GLY A C 1 ATOM 4712 O O . GLY A 1 587 ? 40.986 33.799 27.705 1.00 20.48 ? 640 GLY A O 1 ATOM 4713 N N . ILE A 1 588 ? 40.446 31.610 27.556 1.00 20.09 ? 641 ILE A N 1 ATOM 4714 C CA . ILE A 1 588 ? 39.649 31.765 26.352 1.00 20.15 ? 641 ILE A CA 1 ATOM 4715 C C . ILE A 1 588 ? 38.220 32.241 26.629 1.00 22.31 ? 641 ILE A C 1 ATOM 4716 O O . ILE A 1 588 ? 37.737 33.180 26.002 1.00 20.04 ? 641 ILE A O 1 ATOM 4717 C CB . ILE A 1 588 ? 39.619 30.455 25.554 1.00 24.85 ? 641 ILE A CB 1 ATOM 4718 C CG1 . ILE A 1 588 ? 40.999 30.181 24.941 1.00 27.34 ? 641 ILE A CG1 1 ATOM 4719 C CG2 . ILE A 1 588 ? 38.601 30.559 24.443 1.00 26.09 ? 641 ILE A CG2 1 ATOM 4720 C CD1 . ILE A 1 588 ? 41.103 28.830 24.258 1.00 30.62 ? 641 ILE A CD1 1 ATOM 4721 N N . ASN A 1 589 ? 37.551 31.590 27.572 1.00 17.50 ? 642 ASN A N 1 ATOM 4722 C CA . ASN A 1 589 ? 36.182 31.940 27.911 1.00 18.55 ? 642 ASN A CA 1 ATOM 4723 C C . ASN A 1 589 ? 36.073 33.323 28.572 1.00 18.87 ? 642 ASN A C 1 ATOM 4724 O O . ASN A 1 589 ? 35.030 33.962 28.508 1.00 19.35 ? 642 ASN A O 1 ATOM 4725 C CB . ASN A 1 589 ? 35.583 30.858 28.811 1.00 20.09 ? 642 ASN A CB 1 ATOM 4726 C CG . ASN A 1 589 ? 35.281 29.569 28.057 1.00 24.67 ? 642 ASN A CG 1 ATOM 4727 O OD1 . ASN A 1 589 ? 35.350 29.519 26.824 1.00 30.87 ? 642 ASN A OD1 1 ATOM 4728 N ND2 . ASN A 1 589 ? 34.927 28.525 28.793 1.00 25.44 ? 642 ASN A ND2 1 ATOM 4729 N N . THR A 1 590 ? 37.141 33.788 29.211 1.00 13.33 ? 643 THR A N 1 ATOM 4730 C CA . THR A 1 590 ? 37.102 35.102 29.845 1.00 18.35 ? 643 THR A CA 1 ATOM 4731 C C . THR A 1 590 ? 37.704 36.174 28.941 1.00 16.42 ? 643 THR A C 1 ATOM 4732 O O . THR A 1 590 ? 37.804 37.328 29.337 1.00 17.85 ? 643 THR A O 1 ATOM 4733 C CB . THR A 1 590 ? 37.843 35.112 31.191 1.00 15.04 ? 643 THR A CB 1 ATOM 4734 O OG1 . THR A 1 590 ? 39.213 34.750 30.994 1.00 17.95 ? 643 THR A OG1 1 ATOM 4735 C CG2 . THR A 1 590 ? 37.284 34.038 32.160 1.00 16.32 ? 643 THR A CG2 1 ATOM 4736 N N . LEU A 1 591 ? 38.088 35.800 27.729 1.00 14.14 ? 644 LEU A N 1 ATOM 4737 C CA . LEU A 1 591 ? 38.924 36.678 26.916 1.00 17.82 ? 644 LEU A CA 1 ATOM 4738 C C . LEU A 1 591 ? 38.228 38.007 26.660 1.00 16.35 ? 644 LEU A C 1 ATOM 4739 O O . LEU A 1 591 ? 38.818 39.062 26.849 1.00 14.65 ? 644 LEU A O 1 ATOM 4740 C CB . LEU A 1 591 ? 39.271 36.031 25.576 1.00 17.40 ? 644 LEU A CB 1 ATOM 4741 C CG . LEU A 1 591 ? 40.057 36.952 24.649 1.00 18.97 ? 644 LEU A CG 1 ATOM 4742 C CD1 . LEU A 1 591 ? 41.302 37.444 25.372 1.00 20.40 ? 644 LEU A CD1 1 ATOM 4743 C CD2 . LEU A 1 591 ? 40.434 36.249 23.340 1.00 23.02 ? 644 LEU A CD2 1 ATOM 4744 N N . GLY A 1 592 ? 36.978 37.939 26.216 1.00 17.72 ? 645 GLY A N 1 ATOM 4745 C CA . GLY A 1 592 ? 36.242 39.129 25.827 1.00 17.93 ? 645 GLY A CA 1 ATOM 4746 C C . GLY A 1 592 ? 36.143 40.108 26.975 1.00 16.43 ? 645 GLY A C 1 ATOM 4747 O O . GLY A 1 592 ? 36.370 41.312 26.805 1.00 17.85 ? 645 GLY A O 1 ATOM 4748 N N . GLU A 1 593 ? 35.802 39.594 28.153 1.00 12.96 ? 646 GLU A N 1 ATOM 4749 C CA . GLU A 1 593 ? 35.705 40.434 29.347 1.00 16.66 ? 646 GLU A CA 1 ATOM 4750 C C . GLU A 1 593 ? 37.045 41.022 29.744 1.00 18.52 ? 646 GLU A C 1 ATOM 4751 O O . GLU A 1 593 ? 37.123 42.174 30.193 1.00 16.93 ? 646 GLU A O 1 ATOM 4752 C CB . GLU A 1 593 ? 35.126 39.638 30.514 1.00 14.25 ? 646 GLU A CB 1 ATOM 4753 C CG . GLU A 1 593 ? 33.686 39.232 30.306 1.00 15.01 ? 646 GLU A CG 1 ATOM 4754 C CD . GLU A 1 593 ? 32.766 40.431 30.149 1.00 15.45 ? 646 GLU A CD 1 ATOM 4755 O OE1 . GLU A 1 593 ? 33.096 41.549 30.631 1.00 12.51 ? 646 GLU A OE1 1 ATOM 4756 O OE2 . GLU A 1 593 ? 31.712 40.239 29.542 1.00 13.03 ? 646 GLU A OE2 1 ATOM 4757 N N . ASN A 1 594 ? 38.106 40.232 29.586 1.00 20.23 ? 647 ASN A N 1 ATOM 4758 C CA . ASN A 1 594 ? 39.436 40.694 29.952 1.00 19.77 ? 647 ASN A CA 1 ATOM 4759 C C . ASN A 1 594 ? 39.940 41.777 29.000 1.00 20.16 ? 647 ASN A C 1 ATOM 4760 O O . ASN A 1 594 ? 40.599 42.734 29.427 1.00 16.88 ? 647 ASN A O 1 ATOM 4761 C CB . ASN A 1 594 ? 40.412 39.516 30.013 1.00 18.59 ? 647 ASN A CB 1 ATOM 4762 C CG . ASN A 1 594 ? 40.114 38.576 31.176 1.00 20.00 ? 647 ASN A CG 1 ATOM 4763 O OD1 . ASN A 1 594 ? 39.533 38.988 32.177 1.00 16.50 ? 647 ASN A OD1 1 ATOM 4764 N ND2 . ASN A 1 594 ? 40.507 37.309 31.042 1.00 18.39 ? 647 ASN A ND2 1 ATOM 4765 N N . ILE A 1 595 ? 39.608 41.638 27.719 1.00 18.52 ? 648 ILE A N 1 ATOM 4766 C CA . ILE A 1 595 ? 39.899 42.678 26.732 1.00 17.90 ? 648 ILE A CA 1 ATOM 4767 C C . ILE A 1 595 ? 39.178 43.981 27.071 1.00 18.16 ? 648 ILE A C 1 ATOM 4768 O O . ILE A 1 595 ? 39.779 45.053 27.063 1.00 19.75 ? 648 ILE A O 1 ATOM 4769 C CB . ILE A 1 595 ? 39.486 42.220 25.341 1.00 17.93 ? 648 ILE A CB 1 ATOM 4770 C CG1 . ILE A 1 595 ? 40.470 41.177 24.813 1.00 17.97 ? 648 ILE A CG1 1 ATOM 4771 C CG2 . ILE A 1 595 ? 39.404 43.414 24.382 1.00 20.07 ? 648 ILE A CG2 1 ATOM 4772 C CD1 . ILE A 1 595 ? 40.040 40.590 23.495 1.00 17.67 ? 648 ILE A CD1 1 ATOM 4773 N N . ALA A 1 596 ? 37.891 43.879 27.386 1.00 18.45 ? 649 ALA A N 1 ATOM 4774 C CA . ALA A 1 596 ? 37.113 45.040 27.787 1.00 19.32 ? 649 ALA A CA 1 ATOM 4775 C C . ALA A 1 596 ? 37.668 45.704 29.039 1.00 18.88 ? 649 ALA A C 1 ATOM 4776 O O . ALA A 1 596 ? 37.702 46.925 29.124 1.00 16.37 ? 649 ALA A O 1 ATOM 4777 C CB . ALA A 1 596 ? 35.651 44.656 27.997 1.00 19.72 ? 649 ALA A CB 1 ATOM 4778 N N . ASP A 1 597 ? 38.103 44.903 30.009 1.00 17.11 ? 650 ASP A N 1 ATOM 4779 C CA . ASP A 1 597 ? 38.625 45.443 31.259 1.00 18.05 ? 650 ASP A CA 1 ATOM 4780 C C . ASP A 1 597 ? 39.929 46.216 31.021 1.00 21.52 ? 650 ASP A C 1 ATOM 4781 O O . ASP A 1 597 ? 40.112 47.338 31.517 1.00 21.25 ? 650 ASP A O 1 ATOM 4782 C CB . ASP A 1 597 ? 38.904 44.315 32.261 1.00 17.93 ? 650 ASP A CB 1 ATOM 4783 C CG . ASP A 1 597 ? 37.660 43.844 32.999 1.00 19.61 ? 650 ASP A CG 1 ATOM 4784 O OD1 . ASP A 1 597 ? 37.757 42.792 33.674 1.00 17.97 ? 650 ASP A OD1 1 ATOM 4785 O OD2 . ASP A 1 597 ? 36.564 44.444 32.974 1.00 15.15 ? 650 ASP A OD2 1 ATOM 4786 N N . ASN A 1 598 ? 40.855 45.592 30.296 1.00 17.11 ? 651 ASN A N 1 ATOM 4787 C CA . ASN A 1 598 ? 42.166 46.195 30.072 1.00 17.94 ? 651 ASN A CA 1 ATOM 4788 C C . ASN A 1 598 ? 42.086 47.450 29.201 1.00 17.68 ? 651 ASN A C 1 ATOM 4789 O O . ASN A 1 598 ? 42.700 48.471 29.511 1.00 17.78 ? 651 ASN A O 1 ATOM 4790 C CB . ASN A 1 598 ? 43.121 45.170 29.456 1.00 17.69 ? 651 ASN A CB 1 ATOM 4791 C CG . ASN A 1 598 ? 43.771 44.297 30.507 1.00 17.87 ? 651 ASN A CG 1 ATOM 4792 O OD1 . ASN A 1 598 ? 44.726 44.708 31.154 1.00 19.52 ? 651 ASN A OD1 1 ATOM 4793 N ND2 . ASN A 1 598 ? 43.216 43.109 30.723 1.00 18.94 ? 651 ASN A ND2 1 ATOM 4794 N N . GLY A 1 599 ? 41.317 47.372 28.122 1.00 20.00 ? 652 GLY A N 1 ATOM 4795 C CA . GLY A 1 599 ? 40.998 48.548 27.319 1.00 21.68 ? 652 GLY A CA 1 ATOM 4796 C C . GLY A 1 599 ? 40.320 49.651 28.106 1.00 21.36 ? 652 GLY A C 1 ATOM 4797 O O . GLY A 1 599 ? 40.740 50.812 28.091 1.00 19.01 ? 652 GLY A O 1 ATOM 4798 N N . GLY A 1 600 ? 39.257 49.287 28.809 1.00 17.67 ? 653 GLY A N 1 ATOM 4799 C CA . GLY A 1 600 ? 38.468 50.259 29.530 1.00 21.42 ? 653 GLY A CA 1 ATOM 4800 C C . GLY A 1 600 ? 39.279 50.987 30.581 1.00 18.51 ? 653 GLY A C 1 ATOM 4801 O O . GLY A 1 600 ? 39.103 52.180 30.780 1.00 18.85 ? 653 GLY A O 1 ATOM 4802 N N . LEU A 1 601 ? 40.160 50.271 31.269 1.00 16.47 ? 654 LEU A N 1 ATOM 4803 C CA . LEU A 1 601 ? 40.994 50.893 32.285 1.00 18.68 ? 654 LEU A CA 1 ATOM 4804 C C . LEU A 1 601 ? 41.875 51.965 31.641 1.00 18.38 ? 654 LEU A C 1 ATOM 4805 O O . LEU A 1 601 ? 41.952 53.085 32.135 1.00 17.73 ? 654 LEU A O 1 ATOM 4806 C CB . LEU A 1 601 ? 41.861 49.857 33.016 1.00 21.99 ? 654 LEU A CB 1 ATOM 4807 C CG . LEU A 1 601 ? 42.997 50.440 33.855 1.00 24.55 ? 654 LEU A CG 1 ATOM 4808 C CD1 . LEU A 1 601 ? 42.440 51.230 35.021 1.00 26.40 ? 654 LEU A CD1 1 ATOM 4809 C CD2 . LEU A 1 601 ? 43.961 49.378 34.359 1.00 28.02 ? 654 LEU A CD2 1 ATOM 4810 N N . GLY A 1 602 ? 42.533 51.620 30.540 1.00 20.24 ? 655 GLY A N 1 ATOM 4811 C CA . GLY A 1 602 ? 43.422 52.562 29.874 1.00 21.05 ? 655 GLY A CA 1 ATOM 4812 C C . GLY A 1 602 ? 42.657 53.791 29.383 1.00 21.38 ? 655 GLY A C 1 ATOM 4813 O O . GLY A 1 602 ? 43.097 54.928 29.542 1.00 22.70 ? 655 GLY A O 1 ATOM 4814 N N . GLN A 1 603 ? 41.505 53.551 28.775 1.00 19.69 ? 656 GLN A N 1 ATOM 4815 C CA . GLN A 1 603 ? 40.662 54.628 28.286 1.00 20.68 ? 656 GLN A CA 1 ATOM 4816 C C . GLN A 1 603 ? 40.261 55.592 29.403 1.00 18.85 ? 656 GLN A C 1 ATOM 4817 O O . GLN A 1 603 ? 40.391 56.802 29.252 1.00 17.55 ? 656 GLN A O 1 ATOM 4818 C CB . GLN A 1 603 ? 39.420 54.061 27.609 1.00 20.90 ? 656 GLN A CB 1 ATOM 4819 C CG . GLN A 1 603 ? 39.679 53.488 26.223 1.00 22.01 ? 656 GLN A CG 1 ATOM 4820 C CD . GLN A 1 603 ? 38.951 52.184 25.986 1.00 20.55 ? 656 GLN A CD 1 ATOM 4821 O OE1 . GLN A 1 603 ? 39.320 51.417 25.103 1.00 23.23 ? 656 GLN A OE1 1 ATOM 4822 N NE2 . GLN A 1 603 ? 37.900 51.936 26.759 1.00 15.12 ? 656 GLN A NE2 1 ATOM 4823 N N . ALA A 1 604 ? 39.780 55.056 30.521 1.00 20.41 ? 657 ALA A N 1 ATOM 4824 C CA . ALA A 1 604 ? 39.324 55.892 31.634 1.00 21.24 ? 657 ALA A CA 1 ATOM 4825 C C . ALA A 1 604 ? 40.461 56.749 32.190 1.00 21.06 ? 657 ALA A C 1 ATOM 4826 O O . ALA A 1 604 ? 40.292 57.946 32.457 1.00 20.09 ? 657 ALA A O 1 ATOM 4827 C CB . ALA A 1 604 ? 38.722 55.024 32.750 1.00 17.59 ? 657 ALA A CB 1 ATOM 4828 N N . TYR A 1 605 ? 41.613 56.130 32.393 1.00 21.14 ? 658 TYR A N 1 ATOM 4829 C CA . TYR A 1 605 ? 42.745 56.836 32.977 1.00 24.30 ? 658 TYR A CA 1 ATOM 4830 C C . TYR A 1 605 ? 43.220 57.967 32.074 1.00 23.25 ? 658 TYR A C 1 ATOM 4831 O O . TYR A 1 605 ? 43.505 59.078 32.542 1.00 22.96 ? 658 TYR A O 1 ATOM 4832 C CB . TYR A 1 605 ? 43.909 55.889 33.244 1.00 25.11 ? 658 TYR A CB 1 ATOM 4833 C CG . TYR A 1 605 ? 45.010 56.550 34.037 1.00 27.24 ? 658 TYR A CG 1 ATOM 4834 C CD1 . TYR A 1 605 ? 44.843 56.833 35.387 1.00 30.98 ? 658 TYR A CD1 1 ATOM 4835 C CD2 . TYR A 1 605 ? 46.201 56.930 33.428 1.00 25.96 ? 658 TYR A CD2 1 ATOM 4836 C CE1 . TYR A 1 605 ? 45.839 57.455 36.114 1.00 31.66 ? 658 TYR A CE1 1 ATOM 4837 C CE2 . TYR A 1 605 ? 47.201 57.540 34.146 1.00 30.47 ? 658 TYR A CE2 1 ATOM 4838 C CZ . TYR A 1 605 ? 47.016 57.798 35.489 1.00 32.74 ? 658 TYR A CZ 1 ATOM 4839 O OH . TYR A 1 605 ? 48.010 58.415 36.210 1.00 38.27 ? 658 TYR A OH 1 ATOM 4840 N N . ARG A 1 606 ? 43.296 57.681 30.782 1.00 27.64 ? 659 ARG A N 1 ATOM 4841 C CA . ARG A 1 606 ? 43.604 58.705 29.793 1.00 30.23 ? 659 ARG A CA 1 ATOM 4842 C C . ARG A 1 606 ? 42.614 59.854 29.896 1.00 27.97 ? 659 ARG A C 1 ATOM 4843 O O . ARG A 1 606 ? 43.002 61.025 29.909 1.00 28.70 ? 659 ARG A O 1 ATOM 4844 C CB . ARG A 1 606 ? 43.541 58.114 28.390 1.00 33.30 ? 659 ARG A CB 1 ATOM 4845 C CG . ARG A 1 606 ? 44.888 57.904 27.748 1.00 37.92 ? 659 ARG A CG 1 ATOM 4846 C CD . ARG A 1 606 ? 44.861 56.935 26.567 1.00 40.08 ? 659 ARG A CD 1 ATOM 4847 N NE . ARG A 1 606 ? 45.693 55.772 26.830 1.00 40.14 ? 659 ARG A NE 1 ATOM 4848 C CZ . ARG A 1 606 ? 45.291 54.520 26.699 1.00 39.53 ? 659 ARG A CZ 1 ATOM 4849 N NH1 . ARG A 1 606 ? 44.062 54.248 26.274 1.00 39.34 ? 659 ARG A NH1 1 ATOM 4850 N NH2 . ARG A 1 606 ? 46.129 53.535 26.985 1.00 40.02 ? 659 ARG A NH2 1 ATOM 4851 N N . ALA A 1 607 ? 41.332 59.517 29.984 1.00 27.13 ? 660 ALA A N 1 ATOM 4852 C CA . ALA A 1 607 ? 40.286 60.536 30.071 1.00 23.36 ? 660 ALA A CA 1 ATOM 4853 C C . ALA A 1 607 ? 40.442 61.370 31.328 1.00 24.95 ? 660 ALA A C 1 ATOM 4854 O O . ALA A 1 607 ? 40.154 62.577 31.329 1.00 26.60 ? 660 ALA A O 1 ATOM 4855 C CB . ALA A 1 607 ? 38.911 59.899 30.018 1.00 23.80 ? 660 ALA A CB 1 ATOM 4856 N N . TYR A 1 608 ? 40.893 60.743 32.410 1.00 23.90 ? 661 TYR A N 1 ATOM 4857 C CA . TYR A 1 608 ? 41.132 61.488 33.640 1.00 25.27 ? 661 TYR A CA 1 ATOM 4858 C C . TYR A 1 608 ? 42.338 62.413 33.461 1.00 25.86 ? 661 TYR A C 1 ATOM 4859 O O . TYR A 1 608 ? 42.283 63.586 33.810 1.00 26.66 ? 661 TYR A O 1 ATOM 4860 C CB . TYR A 1 608 ? 41.343 60.559 34.836 1.00 26.38 ? 661 TYR A CB 1 ATOM 4861 C CG . TYR A 1 608 ? 41.513 61.294 36.146 1.00 24.97 ? 661 TYR A CG 1 ATOM 4862 C CD1 . TYR A 1 608 ? 40.605 62.269 36.539 1.00 26.11 ? 661 TYR A CD1 1 ATOM 4863 C CD2 . TYR A 1 608 ? 42.583 61.025 36.985 1.00 28.65 ? 661 TYR A CD2 1 ATOM 4864 C CE1 . TYR A 1 608 ? 40.748 62.945 37.730 1.00 24.93 ? 661 TYR A CE1 1 ATOM 4865 C CE2 . TYR A 1 608 ? 42.738 61.701 38.183 1.00 27.72 ? 661 TYR A CE2 1 ATOM 4866 C CZ . TYR A 1 608 ? 41.816 62.666 38.549 1.00 29.13 ? 661 TYR A CZ 1 ATOM 4867 O OH . TYR A 1 608 ? 41.971 63.331 39.743 1.00 31.55 ? 661 TYR A OH 1 ATOM 4868 N N . GLN A 1 609 ? 43.419 61.877 32.908 1.00 27.32 ? 662 GLN A N 1 ATOM 4869 C CA . GLN A 1 609 ? 44.604 62.677 32.623 1.00 29.49 ? 662 GLN A CA 1 ATOM 4870 C C . GLN A 1 609 ? 44.205 63.913 31.844 1.00 25.15 ? 662 GLN A C 1 ATOM 4871 O O . GLN A 1 609 ? 44.660 65.010 32.136 1.00 32.03 ? 662 GLN A O 1 ATOM 4872 C CB . GLN A 1 609 ? 45.616 61.875 31.813 1.00 28.84 ? 662 GLN A CB 1 ATOM 4873 C CG . GLN A 1 609 ? 46.289 60.757 32.575 1.00 32.76 ? 662 GLN A CG 1 ATOM 4874 C CD . GLN A 1 609 ? 47.358 60.076 31.745 1.00 37.16 ? 662 GLN A CD 1 ATOM 4875 O OE1 . GLN A 1 609 ? 47.048 59.359 30.790 1.00 38.28 ? 662 GLN A OE1 1 ATOM 4876 N NE2 . GLN A 1 609 ? 48.620 60.315 32.091 1.00 42.66 ? 662 GLN A NE2 1 ATOM 4877 N N . ASN A 1 610 ? 43.346 63.730 30.852 1.00 26.94 ? 663 ASN A N 1 ATOM 4878 C CA . ASN A 1 610 ? 42.866 64.847 30.060 1.00 28.76 ? 663 ASN A CA 1 ATOM 4879 C C . ASN A 1 610 ? 42.057 65.825 30.899 1.00 32.52 ? 663 ASN A C 1 ATOM 4880 O O . ASN A 1 610 ? 42.242 67.037 30.797 1.00 34.72 ? 663 ASN A O 1 ATOM 4881 C CB . ASN A 1 610 ? 42.065 64.349 28.856 1.00 29.09 ? 663 ASN A CB 1 ATOM 4882 C CG . ASN A 1 610 ? 42.938 63.621 27.841 1.00 31.46 ? 663 ASN A CG 1 ATOM 4883 O OD1 . ASN A 1 610 ? 44.156 63.585 27.982 1.00 33.03 ? 663 ASN A OD1 1 ATOM 4884 N ND2 . ASN A 1 610 ? 42.318 63.030 26.824 1.00 27.31 ? 663 ASN A ND2 1 ATOM 4885 N N . TYR A 1 611 ? 41.180 65.302 31.749 1.00 31.38 ? 664 TYR A N 1 ATOM 4886 C CA . TYR A 1 611 ? 40.455 66.138 32.699 1.00 31.12 ? 664 TYR A CA 1 ATOM 4887 C C . TYR A 1 611 ? 41.412 67.033 33.477 1.00 30.63 ? 664 TYR A C 1 ATOM 4888 O O . TYR A 1 611 ? 41.204 68.237 33.569 1.00 32.02 ? 664 TYR A O 1 ATOM 4889 C CB . TYR A 1 611 ? 39.640 65.282 33.680 1.00 31.69 ? 664 TYR A CB 1 ATOM 4890 C CG . TYR A 1 611 ? 38.967 66.105 34.753 1.00 34.07 ? 664 TYR A CG 1 ATOM 4891 C CD1 . TYR A 1 611 ? 39.557 66.275 35.994 1.00 35.04 ? 664 TYR A CD1 1 ATOM 4892 C CD2 . TYR A 1 611 ? 37.753 66.732 34.512 1.00 37.07 ? 664 TYR A CD2 1 ATOM 4893 C CE1 . TYR A 1 611 ? 38.954 67.038 36.968 1.00 39.44 ? 664 TYR A CE1 1 ATOM 4894 C CE2 . TYR A 1 611 ? 37.141 67.499 35.482 1.00 39.13 ? 664 TYR A CE2 1 ATOM 4895 C CZ . TYR A 1 611 ? 37.747 67.647 36.708 1.00 39.15 ? 664 TYR A CZ 1 ATOM 4896 O OH . TYR A 1 611 ? 37.148 68.404 37.687 1.00 43.49 ? 664 TYR A OH 1 ATOM 4897 N N . ILE A 1 612 ? 42.459 66.441 34.035 1.00 29.74 ? 665 ILE A N 1 ATOM 4898 C CA . ILE A 1 612 ? 43.399 67.194 34.853 1.00 35.49 ? 665 ILE A CA 1 ATOM 4899 C C . ILE A 1 612 ? 44.104 68.271 34.029 1.00 37.16 ? 665 ILE A C 1 ATOM 4900 O O . ILE A 1 612 ? 44.172 69.431 34.439 1.00 38.92 ? 665 ILE A O 1 ATOM 4901 C CB . ILE A 1 612 ? 44.437 66.249 35.483 1.00 38.50 ? 665 ILE A CB 1 ATOM 4902 C CG1 . ILE A 1 612 ? 43.755 65.296 36.463 1.00 37.81 ? 665 ILE A CG1 1 ATOM 4903 C CG2 . ILE A 1 612 ? 45.521 67.048 36.196 1.00 41.42 ? 665 ILE A CG2 1 ATOM 4904 C CD1 . ILE A 1 612 ? 44.378 65.296 37.838 1.00 39.86 ? 665 ILE A CD1 1 ATOM 4905 N N . LYS A 1 613 ? 44.629 67.881 32.873 1.00 38.86 ? 666 LYS A N 1 ATOM 4906 C CA . LYS A 1 613 ? 45.144 68.839 31.897 1.00 39.77 ? 666 LYS A CA 1 ATOM 4907 C C . LYS A 1 613 ? 44.250 70.068 31.813 1.00 38.57 ? 666 LYS A C 1 ATOM 4908 O O . LYS A 1 613 ? 44.701 71.189 32.027 1.00 37.57 ? 666 LYS A O 1 ATOM 4909 C CB . LYS A 1 613 ? 45.264 68.180 30.521 1.00 41.77 ? 666 LYS A CB 1 ATOM 4910 C CG . LYS A 1 613 ? 46.097 68.966 29.512 1.00 45.55 ? 666 LYS A CG 1 ATOM 4911 C CD . LYS A 1 613 ? 45.899 68.439 28.084 1.00 47.41 ? 666 LYS A CD 1 ATOM 4912 C CE . LYS A 1 613 ? 46.292 66.970 27.967 1.00 46.89 ? 666 LYS A CE 1 ATOM 4913 N NZ . LYS A 1 613 ? 46.926 66.642 26.655 1.00 48.87 ? 666 LYS A NZ 1 ATOM 4914 N N . LYS A 1 614 ? 42.980 69.854 31.500 1.00 38.94 ? 667 LYS A N 1 ATOM 4915 C CA . LYS A 1 614 ? 42.071 70.955 31.203 1.00 41.11 ? 667 LYS A CA 1 ATOM 4916 C C . LYS A 1 614 ? 41.673 71.734 32.456 1.00 42.11 ? 667 LYS A C 1 ATOM 4917 O O . LYS A 1 614 ? 41.516 72.954 32.402 1.00 40.03 ? 667 LYS A O 1 ATOM 4918 C CB . LYS A 1 614 ? 40.821 70.439 30.498 1.00 42.27 ? 667 LYS A CB 1 ATOM 4919 C CG . LYS A 1 614 ? 39.539 71.121 30.941 1.00 44.53 ? 667 LYS A CG 1 ATOM 4920 C CD . LYS A 1 614 ? 38.643 71.443 29.757 1.00 47.15 ? 667 LYS A CD 1 ATOM 4921 C CE . LYS A 1 614 ? 38.667 70.330 28.715 1.00 49.02 ? 667 LYS A CE 1 ATOM 4922 N NZ . LYS A 1 614 ? 38.292 70.823 27.355 1.00 49.35 ? 667 LYS A NZ 1 ATOM 4923 N N . ASN A 1 615 ? 41.502 71.040 33.579 1.00 39.64 ? 668 ASN A N 1 ATOM 4924 C CA . ASN A 1 615 ? 40.766 71.614 34.704 1.00 42.88 ? 668 ASN A CA 1 ATOM 4925 C C . ASN A 1 615 ? 41.639 71.872 35.928 1.00 43.41 ? 668 ASN A C 1 ATOM 4926 O O . ASN A 1 615 ? 41.220 72.555 36.869 1.00 46.52 ? 668 ASN A O 1 ATOM 4927 C CB . ASN A 1 615 ? 39.597 70.712 35.093 1.00 43.33 ? 668 ASN A CB 1 ATOM 4928 C CG . ASN A 1 615 ? 38.536 70.653 34.024 1.00 44.94 ? 668 ASN A CG 1 ATOM 4929 O OD1 . ASN A 1 615 ? 37.757 71.591 33.860 1.00 45.67 ? 668 ASN A OD1 1 ATOM 4930 N ND2 . ASN A 1 615 ? 38.501 69.550 33.278 1.00 43.98 ? 668 ASN A ND2 1 ATOM 4931 N N . GLY A 1 616 ? 42.851 71.329 35.920 1.00 40.81 ? 669 GLY A N 1 ATOM 4932 C CA . GLY A 1 616 ? 43.698 71.380 37.096 1.00 39.91 ? 669 GLY A CA 1 ATOM 4933 C C . GLY A 1 616 ? 43.447 70.213 38.034 1.00 40.10 ? 669 GLY A C 1 ATOM 4934 O O . GLY A 1 616 ? 42.460 69.488 37.896 1.00 32.45 ? 669 GLY A O 1 ATOM 4935 N N . GLU A 1 617 ? 44.349 70.026 38.992 1.00 40.81 ? 670 GLU A N 1 ATOM 4936 C CA . GLU A 1 617 ? 44.284 68.877 39.885 1.00 42.68 ? 670 GLU A CA 1 ATOM 4937 C C . GLU A 1 617 ? 43.234 69.087 40.969 1.00 40.37 ? 670 GLU A C 1 ATOM 4938 O O . GLU A 1 617 ? 42.868 70.223 41.277 1.00 33.86 ? 670 GLU A O 1 ATOM 4939 C CB . GLU A 1 617 ? 45.653 68.624 40.519 1.00 46.42 ? 670 GLU A CB 1 ATOM 4940 C CG . GLU A 1 617 ? 46.433 67.497 39.859 1.00 50.87 ? 670 GLU A CG 1 ATOM 4941 C CD . GLU A 1 617 ? 47.917 67.564 40.157 1.00 56.03 ? 670 GLU A CD 1 ATOM 4942 O OE1 . GLU A 1 617 ? 48.460 66.582 40.715 1.00 58.15 ? 670 GLU A OE1 1 ATOM 4943 O OE2 . GLU A 1 617 ? 48.539 68.599 39.835 1.00 57.62 ? 670 GLU A OE2 1 ATOM 4944 N N . GLU A 1 618 ? 42.741 67.987 41.537 1.00 34.92 ? 671 GLU A N 1 ATOM 4945 C CA . GLU A 1 618 ? 41.672 68.059 42.527 1.00 36.77 ? 671 GLU A CA 1 ATOM 4946 C C . GLU A 1 618 ? 42.241 68.177 43.932 1.00 30.31 ? 671 GLU A C 1 ATOM 4947 O O . GLU A 1 618 ? 43.334 67.694 44.216 1.00 29.31 ? 671 GLU A O 1 ATOM 4948 C CB . GLU A 1 618 ? 40.773 66.820 42.444 1.00 35.05 ? 671 GLU A CB 1 ATOM 4949 C CG . GLU A 1 618 ? 40.249 66.541 41.050 1.00 35.83 ? 671 GLU A CG 1 ATOM 4950 C CD . GLU A 1 618 ? 39.199 65.446 41.031 1.00 34.02 ? 671 GLU A CD 1 ATOM 4951 O OE1 . GLU A 1 618 ? 39.560 64.278 40.776 1.00 30.62 ? 671 GLU A OE1 1 ATOM 4952 O OE2 . GLU A 1 618 ? 38.016 65.761 41.268 1.00 36.48 ? 671 GLU A OE2 1 ATOM 4953 N N . LYS A 1 619 ? 41.487 68.814 44.819 1.00 31.15 ? 672 LYS A N 1 ATOM 4954 C CA . LYS A 1 619 ? 41.830 68.797 46.232 1.00 31.35 ? 672 LYS A CA 1 ATOM 4955 C C . LYS A 1 619 ? 41.890 67.365 46.732 1.00 30.37 ? 672 LYS A C 1 ATOM 4956 O O . LYS A 1 619 ? 41.079 66.521 46.345 1.00 24.41 ? 672 LYS A O 1 ATOM 4957 C CB . LYS A 1 619 ? 40.812 69.594 47.044 1.00 34.60 ? 672 LYS A CB 1 ATOM 4958 C CG . LYS A 1 619 ? 40.971 71.108 46.914 1.00 39.65 ? 672 LYS A CG 1 ATOM 4959 C CD . LYS A 1 619 ? 39.925 71.850 47.745 1.00 42.83 ? 672 LYS A CD 1 ATOM 4960 C CE . LYS A 1 619 ? 39.583 73.200 47.134 1.00 44.12 ? 672 LYS A CE 1 ATOM 4961 N NZ . LYS A 1 619 ? 38.524 73.085 46.079 1.00 46.44 ? 672 LYS A NZ 1 ATOM 4962 N N . LEU A 1 620 ? 42.867 67.096 47.586 1.00 31.19 ? 673 LEU A N 1 ATOM 4963 C CA . LEU A 1 620 ? 43.100 65.758 48.106 1.00 31.66 ? 673 LEU A CA 1 ATOM 4964 C C . LEU A 1 620 ? 42.013 65.343 49.097 1.00 29.32 ? 673 LEU A C 1 ATOM 4965 O O . LEU A 1 620 ? 41.307 66.186 49.643 1.00 25.90 ? 673 LEU A O 1 ATOM 4966 C CB . LEU A 1 620 ? 44.462 65.708 48.795 1.00 31.82 ? 673 LEU A CB 1 ATOM 4967 C CG . LEU A 1 620 ? 45.657 66.146 47.943 1.00 36.18 ? 673 LEU A CG 1 ATOM 4968 C CD1 . LEU A 1 620 ? 46.840 66.520 48.827 1.00 37.46 ? 673 LEU A CD1 1 ATOM 4969 C CD2 . LEU A 1 620 ? 46.049 65.049 46.968 1.00 37.78 ? 673 LEU A CD2 1 ATOM 4970 N N . LEU A 1 621 ? 41.897 64.040 49.336 1.00 29.45 ? 674 LEU A N 1 ATOM 4971 C CA . LEU A 1 621 ? 41.001 63.529 50.367 1.00 26.27 ? 674 LEU A CA 1 ATOM 4972 C C . LEU A 1 621 ? 41.719 63.433 51.700 1.00 26.15 ? 674 LEU A C 1 ATOM 4973 O O . LEU A 1 621 ? 42.878 63.019 51.771 1.00 25.39 ? 674 LEU A O 1 ATOM 4974 C CB . LEU A 1 621 ? 40.452 62.149 49.989 1.00 24.05 ? 674 LEU A CB 1 ATOM 4975 C CG . LEU A 1 621 ? 39.547 62.066 48.754 1.00 24.90 ? 674 LEU A CG 1 ATOM 4976 C CD1 . LEU A 1 621 ? 39.050 60.633 48.571 1.00 23.57 ? 674 LEU A CD1 1 ATOM 4977 C CD2 . LEU A 1 621 ? 38.364 63.049 48.852 1.00 22.31 ? 674 LEU A CD2 1 ATOM 4978 N N . PRO A 1 622 ? 41.012 63.802 52.760 1.00 25.35 ? 675 PRO A N 1 ATOM 4979 C CA . PRO A 1 622 ? 41.546 63.732 54.120 1.00 26.66 ? 675 PRO A CA 1 ATOM 4980 C C . PRO A 1 622 ? 41.677 62.296 54.599 1.00 27.34 ? 675 PRO A C 1 ATOM 4981 O O . PRO A 1 622 ? 40.847 61.448 54.255 1.00 23.85 ? 675 PRO A O 1 ATOM 4982 C CB . PRO A 1 622 ? 40.488 64.466 54.945 1.00 26.59 ? 675 PRO A CB 1 ATOM 4983 C CG . PRO A 1 622 ? 39.236 64.289 54.179 1.00 27.25 ? 675 PRO A CG 1 ATOM 4984 C CD . PRO A 1 622 ? 39.630 64.306 52.731 1.00 26.74 ? 675 PRO A CD 1 ATOM 4985 N N . GLY A 1 623 ? 42.714 62.034 55.389 1.00 24.15 ? 676 GLY A N 1 ATOM 4986 C CA . GLY A 1 623 ? 42.891 60.744 56.027 1.00 26.74 ? 676 GLY A CA 1 ATOM 4987 C C . GLY A 1 623 ? 43.645 59.774 55.141 1.00 24.79 ? 676 GLY A C 1 ATOM 4988 O O . GLY A 1 623 ? 43.991 58.669 55.557 1.00 28.94 ? 676 GLY A O 1 ATOM 4989 N N . LEU A 1 624 ? 43.909 60.204 53.912 1.00 26.00 ? 677 LEU A N 1 ATOM 4990 C CA . LEU A 1 624 ? 44.560 59.353 52.916 1.00 27.71 ? 677 LEU A CA 1 ATOM 4991 C C . LEU A 1 624 ? 45.805 60.031 52.342 1.00 31.36 ? 677 LEU A C 1 ATOM 4992 O O . LEU A 1 624 ? 45.720 61.062 51.653 1.00 26.65 ? 677 LEU A O 1 ATOM 4993 C CB . LEU A 1 624 ? 43.598 59.035 51.769 1.00 26.57 ? 677 LEU A CB 1 ATOM 4994 C CG . LEU A 1 624 ? 42.558 57.959 52.060 1.00 24.64 ? 677 LEU A CG 1 ATOM 4995 C CD1 . LEU A 1 624 ? 41.347 58.147 51.163 1.00 26.42 ? 677 LEU A CD1 1 ATOM 4996 C CD2 . LEU A 1 624 ? 43.154 56.568 51.899 1.00 27.77 ? 677 LEU A CD2 1 ATOM 4997 N N . ASP A 1 625 ? 46.956 59.438 52.630 1.00 29.63 ? 678 ASP A N 1 ATOM 4998 C CA . ASP A 1 625 ? 48.223 59.907 52.105 1.00 33.63 ? 678 ASP A CA 1 ATOM 4999 C C . ASP A 1 625 ? 48.413 59.361 50.695 1.00 33.37 ? 678 ASP A C 1 ATOM 5000 O O . ASP A 1 625 ? 49.388 58.659 50.394 1.00 31.00 ? 678 ASP A O 1 ATOM 5001 C CB . ASP A 1 625 ? 49.362 59.467 53.028 1.00 35.47 ? 678 ASP A CB 1 ATOM 5002 C CG . ASP A 1 625 ? 49.163 59.937 54.462 1.00 37.07 ? 678 ASP A CG 1 ATOM 5003 O OD1 . ASP A 1 625 ? 48.402 60.905 54.670 1.00 44.11 ? 678 ASP A OD1 1 ATOM 5004 O OD2 . ASP A 1 625 ? 49.720 59.397 55.442 1.00 45.67 ? 678 ASP A OD2 1 ATOM 5005 N N . LEU A 1 626 ? 47.446 59.675 49.842 1.00 32.35 ? 679 LEU A N 1 ATOM 5006 C CA . LEU A 1 626 ? 47.485 59.291 48.444 1.00 29.77 ? 679 LEU A CA 1 ATOM 5007 C C . LEU A 1 626 ? 47.138 60.497 47.601 1.00 26.14 ? 679 LEU A C 1 ATOM 5008 O O . LEU A 1 626 ? 46.350 61.342 48.016 1.00 27.40 ? 679 LEU A O 1 ATOM 5009 C CB . LEU A 1 626 ? 46.477 58.179 48.178 1.00 28.69 ? 679 LEU A CB 1 ATOM 5010 C CG . LEU A 1 626 ? 46.802 56.820 48.787 1.00 27.20 ? 679 LEU A CG 1 ATOM 5011 C CD1 . LEU A 1 626 ? 45.695 55.836 48.449 1.00 27.13 ? 679 LEU A CD1 1 ATOM 5012 C CD2 . LEU A 1 626 ? 48.139 56.330 48.282 1.00 25.59 ? 679 LEU A CD2 1 ATOM 5013 N N . ASN A 1 627 ? 47.719 60.579 46.414 1.00 27.07 ? 680 ASN A N 1 ATOM 5014 C CA . ASN A 1 627 ? 47.270 61.558 45.430 1.00 26.89 ? 680 ASN A CA 1 ATOM 5015 C C . ASN A 1 627 ? 46.167 60.989 44.549 1.00 27.80 ? 680 ASN A C 1 ATOM 5016 O O . ASN A 1 627 ? 45.720 59.854 44.749 1.00 22.72 ? 680 ASN A O 1 ATOM 5017 C CB . ASN A 1 627 ? 48.443 62.024 44.569 1.00 28.19 ? 680 ASN A CB 1 ATOM 5018 C CG . ASN A 1 627 ? 49.078 60.891 43.786 1.00 30.93 ? 680 ASN A CG 1 ATOM 5019 O OD1 . ASN A 1 627 ? 48.383 60.060 43.200 1.00 26.74 ? 680 ASN A OD1 1 ATOM 5020 N ND2 . ASN A 1 627 ? 50.408 60.854 43.773 1.00 27.60 ? 680 ASN A ND2 1 ATOM 5021 N N . HIS A 1 628 ? 45.711 61.773 43.579 1.00 25.58 ? 681 HIS A N 1 ATOM 5022 C CA . HIS A 1 628 ? 44.464 61.441 42.906 1.00 29.21 ? 681 HIS A CA 1 ATOM 5023 C C . HIS A 1 628 ? 44.648 60.384 41.824 1.00 29.56 ? 681 HIS A C 1 ATOM 5024 O O . HIS A 1 628 ? 43.729 59.614 41.551 1.00 25.73 ? 681 HIS A O 1 ATOM 5025 C CB . HIS A 1 628 ? 43.794 62.686 42.340 1.00 27.89 ? 681 HIS A CB 1 ATOM 5026 C CG . HIS A 1 628 ? 42.758 63.252 43.252 1.00 26.03 ? 681 HIS A CG 1 ATOM 5027 N ND1 . HIS A 1 628 ? 41.597 62.577 43.559 1.00 24.85 ? 681 HIS A ND1 1 ATOM 5028 C CD2 . HIS A 1 628 ? 42.723 64.404 43.961 1.00 27.04 ? 681 HIS A CD2 1 ATOM 5029 C CE1 . HIS A 1 628 ? 40.885 63.294 44.409 1.00 27.45 ? 681 HIS A CE1 1 ATOM 5030 N NE2 . HIS A 1 628 ? 41.544 64.410 44.667 1.00 29.38 ? 681 HIS A NE2 1 ATOM 5031 N N . LYS A 1 629 ? 45.829 60.340 41.214 1.00 28.57 ? 682 LYS A N 1 ATOM 5032 C CA . LYS A 1 629 ? 46.199 59.205 40.380 1.00 28.90 ? 682 LYS A CA 1 ATOM 5033 C C . LYS A 1 629 ? 46.139 57.903 41.178 1.00 24.50 ? 682 LYS A C 1 ATOM 5034 O O . LYS A 1 629 ? 45.603 56.902 40.704 1.00 22.13 ? 682 LYS A O 1 ATOM 5035 C CB . LYS A 1 629 ? 47.589 59.406 39.780 1.00 35.30 ? 682 LYS A CB 1 ATOM 5036 C CG . LYS A 1 629 ? 47.814 60.810 39.224 1.00 40.73 ? 682 LYS A CG 1 ATOM 5037 C CD . LYS A 1 629 ? 48.801 60.815 38.066 1.00 43.87 ? 682 LYS A CD 1 ATOM 5038 C CE . LYS A 1 629 ? 48.290 61.638 36.882 1.00 46.46 ? 682 LYS A CE 1 ATOM 5039 N NZ . LYS A 1 629 ? 48.695 61.025 35.574 1.00 46.76 ? 682 LYS A NZ 1 ATOM 5040 N N . GLN A 1 630 ? 46.685 57.922 42.388 1.00 21.94 ? 683 GLN A N 1 ATOM 5041 C CA . GLN A 1 630 ? 46.640 56.757 43.253 1.00 25.77 ? 683 GLN A CA 1 ATOM 5042 C C . GLN A 1 630 ? 45.180 56.418 43.612 1.00 25.35 ? 683 GLN A C 1 ATOM 5043 O O . GLN A 1 630 ? 44.789 55.253 43.603 1.00 23.72 ? 683 GLN A O 1 ATOM 5044 C CB . GLN A 1 630 ? 47.509 56.979 44.504 1.00 26.24 ? 683 GLN A CB 1 ATOM 5045 C CG . GLN A 1 630 ? 48.985 57.304 44.176 1.00 27.65 ? 683 GLN A CG 1 ATOM 5046 C CD . GLN A 1 630 ? 49.848 57.624 45.411 1.00 28.88 ? 683 GLN A CD 1 ATOM 5047 O OE1 . GLN A 1 630 ? 49.433 58.368 46.301 1.00 21.58 ? 683 GLN A OE1 1 ATOM 5048 N NE2 . GLN A 1 630 ? 51.053 57.059 45.451 1.00 29.40 ? 683 GLN A NE2 1 ATOM 5049 N N . LEU A 1 631 ? 44.377 57.441 43.888 1.00 25.35 ? 684 LEU A N 1 ATOM 5050 C CA . LEU A 1 631 ? 42.982 57.257 44.297 1.00 21.73 ? 684 LEU A CA 1 ATOM 5051 C C . LEU A 1 631 ? 42.135 56.664 43.176 1.00 20.71 ? 684 LEU A C 1 ATOM 5052 O O . LEU A 1 631 ? 41.227 55.849 43.420 1.00 17.84 ? 684 LEU A O 1 ATOM 5053 C CB . LEU A 1 631 ? 42.378 58.597 44.755 1.00 22.05 ? 684 LEU A CB 1 ATOM 5054 C CG . LEU A 1 631 ? 42.857 59.111 46.118 1.00 21.32 ? 684 LEU A CG 1 ATOM 5055 C CD1 . LEU A 1 631 ? 42.308 60.505 46.422 1.00 23.19 ? 684 LEU A CD1 1 ATOM 5056 C CD2 . LEU A 1 631 ? 42.500 58.150 47.242 1.00 21.67 ? 684 LEU A CD2 1 ATOM 5057 N N . PHE A 1 632 ? 42.427 57.083 41.946 1.00 19.56 ? 685 PHE A N 1 ATOM 5058 C CA . PHE A 1 632 ? 41.802 56.516 40.759 1.00 19.33 ? 685 PHE A CA 1 ATOM 5059 C C . PHE A 1 632 ? 41.934 54.998 40.811 1.00 21.50 ? 685 PHE A C 1 ATOM 5060 O O . PHE A 1 632 ? 40.953 54.275 40.632 1.00 20.04 ? 685 PHE A O 1 ATOM 5061 C CB . PHE A 1 632 ? 42.465 57.092 39.502 1.00 18.47 ? 685 PHE A CB 1 ATOM 5062 C CG . PHE A 1 632 ? 42.028 56.448 38.218 1.00 19.81 ? 685 PHE A CG 1 ATOM 5063 C CD1 . PHE A 1 632 ? 42.572 55.244 37.823 1.00 20.57 ? 685 PHE A CD1 1 ATOM 5064 C CD2 . PHE A 1 632 ? 41.101 57.067 37.388 1.00 15.56 ? 685 PHE A CD2 1 ATOM 5065 C CE1 . PHE A 1 632 ? 42.193 54.650 36.638 1.00 21.00 ? 685 PHE A CE1 1 ATOM 5066 C CE2 . PHE A 1 632 ? 40.722 56.477 36.207 1.00 18.13 ? 685 PHE A CE2 1 ATOM 5067 C CZ . PHE A 1 632 ? 41.276 55.261 35.828 1.00 18.52 ? 685 PHE A CZ 1 ATOM 5068 N N . PHE A 1 633 ? 43.141 54.506 41.087 1.00 19.60 ? 686 PHE A N 1 ATOM 5069 C CA . PHE A 1 633 ? 43.381 53.065 41.050 1.00 19.08 ? 686 PHE A CA 1 ATOM 5070 C C . PHE A 1 633 ? 42.797 52.373 42.276 1.00 19.28 ? 686 PHE A C 1 ATOM 5071 O O . PHE A 1 633 ? 42.282 51.265 42.176 1.00 18.85 ? 686 PHE A O 1 ATOM 5072 C CB . PHE A 1 633 ? 44.872 52.758 40.924 1.00 22.30 ? 686 PHE A CB 1 ATOM 5073 C CG . PHE A 1 633 ? 45.422 53.022 39.560 1.00 23.25 ? 686 PHE A CG 1 ATOM 5074 C CD1 . PHE A 1 633 ? 46.321 54.056 39.343 1.00 23.98 ? 686 PHE A CD1 1 ATOM 5075 C CD2 . PHE A 1 633 ? 45.023 52.250 38.481 1.00 21.93 ? 686 PHE A CD2 1 ATOM 5076 C CE1 . PHE A 1 633 ? 46.834 54.288 38.079 1.00 24.49 ? 686 PHE A CE1 1 ATOM 5077 C CE2 . PHE A 1 633 ? 45.510 52.504 37.216 1.00 24.38 ? 686 PHE A CE2 1 ATOM 5078 C CZ . PHE A 1 633 ? 46.421 53.520 37.015 1.00 24.99 ? 686 PHE A CZ 1 ATOM 5079 N N . LEU A 1 634 ? 42.898 53.027 43.429 1.00 19.92 ? 687 LEU A N 1 ATOM 5080 C CA . LEU A 1 634 ? 42.279 52.535 44.650 1.00 22.94 ? 687 LEU A CA 1 ATOM 5081 C C . LEU A 1 634 ? 40.789 52.294 44.431 1.00 19.93 ? 687 LEU A C 1 ATOM 5082 O O . LEU A 1 634 ? 40.288 51.242 44.768 1.00 18.36 ? 687 LEU A O 1 ATOM 5083 C CB . LEU A 1 634 ? 42.470 53.532 45.784 1.00 25.23 ? 687 LEU A CB 1 ATOM 5084 C CG . LEU A 1 634 ? 42.800 52.983 47.162 1.00 28.14 ? 687 LEU A CG 1 ATOM 5085 C CD1 . LEU A 1 634 ? 42.309 53.951 48.226 1.00 27.28 ? 687 LEU A CD1 1 ATOM 5086 C CD2 . LEU A 1 634 ? 42.244 51.605 47.387 1.00 30.70 ? 687 LEU A CD2 1 ATOM 5087 N N . ASN A 1 635 ? 40.087 53.269 43.866 1.00 20.34 ? 688 ASN A N 1 ATOM 5088 C CA . ASN A 1 635 ? 38.633 53.169 43.746 1.00 18.66 ? 688 ASN A CA 1 ATOM 5089 C C . ASN A 1 635 ? 38.271 52.079 42.745 1.00 15.78 ? 688 ASN A C 1 ATOM 5090 O O . ASN A 1 635 ? 37.379 51.250 42.976 1.00 15.67 ? 688 ASN A O 1 ATOM 5091 C CB . ASN A 1 635 ? 38.027 54.494 43.281 1.00 18.29 ? 688 ASN A CB 1 ATOM 5092 C CG . ASN A 1 635 ? 36.509 54.529 43.443 1.00 18.33 ? 688 ASN A CG 1 ATOM 5093 O OD1 . ASN A 1 635 ? 35.755 54.776 42.486 1.00 22.50 ? 688 ASN A OD1 1 ATOM 5094 N ND2 . ASN A 1 635 ? 36.057 54.273 44.647 1.00 12.79 ? 688 ASN A ND2 1 ATOM 5095 N N . PHE A 1 636 ? 38.981 52.101 41.630 1.00 17.41 ? 689 PHE A N 1 ATOM 5096 C CA . PHE A 1 636 ? 38.929 51.042 40.635 1.00 20.70 ? 689 PHE A CA 1 ATOM 5097 C C . PHE A 1 636 ? 38.956 49.668 41.318 1.00 19.12 ? 689 PHE A C 1 ATOM 5098 O O . PHE A 1 636 ? 38.044 48.852 41.145 1.00 14.16 ? 689 PHE A O 1 ATOM 5099 C CB . PHE A 1 636 ? 40.107 51.233 39.670 1.00 21.89 ? 689 PHE A CB 1 ATOM 5100 C CG . PHE A 1 636 ? 40.304 50.108 38.698 1.00 19.98 ? 689 PHE A CG 1 ATOM 5101 C CD1 . PHE A 1 636 ? 41.353 49.237 38.859 1.00 20.43 ? 689 PHE A CD1 1 ATOM 5102 C CD2 . PHE A 1 636 ? 39.468 49.956 37.603 1.00 23.60 ? 689 PHE A CD2 1 ATOM 5103 C CE1 . PHE A 1 636 ? 41.559 48.203 37.969 1.00 21.40 ? 689 PHE A CE1 1 ATOM 5104 C CE2 . PHE A 1 636 ? 39.670 48.922 36.701 1.00 24.00 ? 689 PHE A CE2 1 ATOM 5105 C CZ . PHE A 1 636 ? 40.720 48.041 36.890 1.00 20.14 ? 689 PHE A CZ 1 ATOM 5106 N N . ALA A 1 637 ? 39.976 49.435 42.136 1.00 20.23 ? 690 ALA A N 1 ATOM 5107 C CA . ALA A 1 637 ? 40.163 48.128 42.762 1.00 19.63 ? 690 ALA A CA 1 ATOM 5108 C C . ALA A 1 637 ? 39.027 47.762 43.723 1.00 17.95 ? 690 ALA A C 1 ATOM 5109 O O . ALA A 1 637 ? 38.617 46.608 43.803 1.00 19.32 ? 690 ALA A O 1 ATOM 5110 C CB . ALA A 1 637 ? 41.497 48.089 43.495 1.00 18.35 ? 690 ALA A CB 1 ATOM 5111 N N . GLN A 1 638 ? 38.543 48.743 44.471 1.00 18.54 ? 691 GLN A N 1 ATOM 5112 C CA . GLN A 1 638 ? 37.631 48.476 45.572 1.00 19.09 ? 691 GLN A CA 1 ATOM 5113 C C . GLN A 1 638 ? 36.245 48.140 45.051 1.00 19.46 ? 691 GLN A C 1 ATOM 5114 O O . GLN A 1 638 ? 35.432 47.566 45.772 1.00 18.36 ? 691 GLN A O 1 ATOM 5115 C CB . GLN A 1 638 ? 37.567 49.671 46.528 1.00 18.34 ? 691 GLN A CB 1 ATOM 5116 C CG . GLN A 1 638 ? 38.789 49.727 47.450 1.00 17.07 ? 691 GLN A CG 1 ATOM 5117 C CD . GLN A 1 638 ? 38.676 50.769 48.540 1.00 17.53 ? 691 GLN A CD 1 ATOM 5118 O OE1 . GLN A 1 638 ? 37.662 51.461 48.643 1.00 17.39 ? 691 GLN A OE1 1 ATOM 5119 N NE2 . GLN A 1 638 ? 39.713 50.868 49.385 1.00 19.37 ? 691 GLN A NE2 1 ATOM 5120 N N . VAL A 1 639 ? 35.974 48.473 43.793 1.00 16.03 ? 692 VAL A N 1 ATOM 5121 C CA . VAL A 1 639 ? 34.777 47.939 43.159 1.00 16.44 ? 692 VAL A CA 1 ATOM 5122 C C . VAL A 1 639 ? 34.678 46.438 43.418 1.00 16.69 ? 692 VAL A C 1 ATOM 5123 O O . VAL A 1 639 ? 33.575 45.901 43.533 1.00 16.17 ? 692 VAL A O 1 ATOM 5124 C CB . VAL A 1 639 ? 34.727 48.209 41.648 1.00 17.38 ? 692 VAL A CB 1 ATOM 5125 C CG1 . VAL A 1 639 ? 33.589 47.433 41.020 1.00 19.84 ? 692 VAL A CG1 1 ATOM 5126 C CG2 . VAL A 1 639 ? 34.550 49.684 41.378 1.00 17.00 ? 692 VAL A CG2 1 ATOM 5127 N N . TRP A 1 640 ? 35.822 45.750 43.485 1.00 14.91 ? 693 TRP A N 1 ATOM 5128 C CA . TRP A 1 640 ? 35.804 44.294 43.534 1.00 14.17 ? 693 TRP A CA 1 ATOM 5129 C C . TRP A 1 640 ? 36.309 43.712 44.852 1.00 16.04 ? 693 TRP A C 1 ATOM 5130 O O . TRP A 1 640 ? 36.622 42.521 44.920 1.00 15.92 ? 693 TRP A O 1 ATOM 5131 C CB . TRP A 1 640 ? 36.579 43.702 42.340 1.00 19.15 ? 693 TRP A CB 1 ATOM 5132 C CG . TRP A 1 640 ? 35.807 43.885 41.071 1.00 18.58 ? 693 TRP A CG 1 ATOM 5133 C CD1 . TRP A 1 640 ? 36.168 44.627 39.989 1.00 22.60 ? 693 TRP A CD1 1 ATOM 5134 C CD2 . TRP A 1 640 ? 34.510 43.361 40.784 1.00 18.83 ? 693 TRP A CD2 1 ATOM 5135 N NE1 . TRP A 1 640 ? 35.178 44.587 39.036 1.00 21.25 ? 693 TRP A NE1 1 ATOM 5136 C CE2 . TRP A 1 640 ? 34.147 43.814 39.501 1.00 18.96 ? 693 TRP A CE2 1 ATOM 5137 C CE3 . TRP A 1 640 ? 33.614 42.541 41.483 1.00 20.51 ? 693 TRP A CE3 1 ATOM 5138 C CZ2 . TRP A 1 640 ? 32.929 43.482 38.903 1.00 22.94 ? 693 TRP A CZ2 1 ATOM 5139 C CZ3 . TRP A 1 640 ? 32.397 42.211 40.887 1.00 25.03 ? 693 TRP A CZ3 1 ATOM 5140 C CH2 . TRP A 1 640 ? 32.074 42.678 39.609 1.00 22.50 ? 693 TRP A CH2 1 ATOM 5141 N N . CYS A 1 641 ? 36.371 44.519 45.909 1.00 16.78 ? 694 CYS A N 1 ATOM 5142 C CA . CYS A 1 641 ? 36.547 43.934 47.240 1.00 16.64 ? 694 CYS A CA 1 ATOM 5143 C C . CYS A 1 641 ? 35.417 42.932 47.429 1.00 18.48 ? 694 CYS A C 1 ATOM 5144 O O . CYS A 1 641 ? 34.249 43.287 47.287 1.00 15.14 ? 694 CYS A O 1 ATOM 5145 C CB . CYS A 1 641 ? 36.484 44.977 48.348 1.00 19.51 ? 694 CYS A CB 1 ATOM 5146 S SG . CYS A 1 641 ? 37.733 46.274 48.253 1.00 19.16 ? 694 CYS A SG 1 ATOM 5147 N N . GLY A 1 642 ? 35.766 41.686 47.722 1.00 17.18 ? 695 GLY A N 1 ATOM 5148 C CA . GLY A 1 642 ? 34.772 40.630 47.819 1.00 18.09 ? 695 GLY A CA 1 ATOM 5149 C C . GLY A 1 642 ? 35.367 39.243 47.817 1.00 17.55 ? 695 GLY A C 1 ATOM 5150 O O . GLY A 1 642 ? 36.579 39.076 47.689 1.00 20.17 ? 695 GLY A O 1 ATOM 5151 N N . THR A 1 643 ? 34.508 38.237 47.954 1.00 14.97 ? 696 THR A N 1 ATOM 5152 C CA . THR A 1 643 ? 34.966 36.861 47.998 1.00 16.95 ? 696 THR A CA 1 ATOM 5153 C C . THR A 1 643 ? 33.860 35.916 47.545 1.00 13.56 ? 696 THR A C 1 ATOM 5154 O O . THR A 1 643 ? 32.740 36.360 47.295 1.00 18.22 ? 696 THR A O 1 ATOM 5155 C CB . THR A 1 643 ? 35.490 36.524 49.424 1.00 22.91 ? 696 THR A CB 1 ATOM 5156 O OG1 . THR A 1 643 ? 35.973 35.180 49.467 1.00 19.89 ? 696 THR A OG1 1 ATOM 5157 C CG2 . THR A 1 643 ? 34.380 36.561 50.453 1.00 20.96 ? 696 THR A CG2 1 ATOM 5158 N N . TYR A 1 644 ? 34.201 34.639 47.367 1.00 14.52 ? 697 TYR A N 1 ATOM 5159 C CA . TYR A 1 644 ? 33.284 33.615 46.862 1.00 16.76 ? 697 TYR A CA 1 ATOM 5160 C C . TYR A 1 644 ? 33.249 32.410 47.807 1.00 18.43 ? 697 TYR A C 1 ATOM 5161 O O . TYR A 1 644 ? 34.278 32.030 48.365 1.00 17.05 ? 697 TYR A O 1 ATOM 5162 C CB . TYR A 1 644 ? 33.742 33.098 45.502 1.00 16.52 ? 697 TYR A CB 1 ATOM 5163 C CG . TYR A 1 644 ? 33.753 34.122 44.392 1.00 16.38 ? 697 TYR A CG 1 ATOM 5164 C CD1 . TYR A 1 644 ? 32.923 33.978 43.282 1.00 19.83 ? 697 TYR A CD1 1 ATOM 5165 C CD2 . TYR A 1 644 ? 34.607 35.210 44.434 1.00 20.35 ? 697 TYR A CD2 1 ATOM 5166 C CE1 . TYR A 1 644 ? 32.928 34.916 42.247 1.00 20.12 ? 697 TYR A CE1 1 ATOM 5167 C CE2 . TYR A 1 644 ? 34.627 36.148 43.405 1.00 22.87 ? 697 TYR A CE2 1 ATOM 5168 C CZ . TYR A 1 644 ? 33.787 35.992 42.318 1.00 23.59 ? 697 TYR A CZ 1 ATOM 5169 O OH . TYR A 1 644 ? 33.813 36.923 41.300 1.00 32.45 ? 697 TYR A OH 1 ATOM 5170 N N . ARG A 1 645 ? 32.090 31.777 47.940 1.00 15.79 ? 698 ARG A N 1 ATOM 5171 C CA . ARG A 1 645 ? 32.042 30.402 48.430 1.00 16.48 ? 698 ARG A CA 1 ATOM 5172 C C . ARG A 1 645 ? 32.736 29.457 47.454 1.00 16.74 ? 698 ARG A C 1 ATOM 5173 O O . ARG A 1 645 ? 32.590 29.585 46.241 1.00 16.91 ? 698 ARG A O 1 ATOM 5174 C CB . ARG A 1 645 ? 30.598 29.961 48.663 1.00 15.79 ? 698 ARG A CB 1 ATOM 5175 C CG . ARG A 1 645 ? 29.907 30.752 49.751 1.00 19.75 ? 698 ARG A CG 1 ATOM 5176 C CD . ARG A 1 645 ? 28.557 30.223 50.175 1.00 19.60 ? 698 ARG A CD 1 ATOM 5177 N NE . ARG A 1 645 ? 28.104 30.940 51.358 1.00 17.75 ? 698 ARG A NE 1 ATOM 5178 C CZ . ARG A 1 645 ? 28.367 30.590 52.614 1.00 20.23 ? 698 ARG A CZ 1 ATOM 5179 N NH1 . ARG A 1 645 ? 29.058 29.498 52.885 1.00 17.54 ? 698 ARG A NH1 1 ATOM 5180 N NH2 . ARG A 1 645 ? 27.930 31.345 53.615 1.00 22.51 ? 698 ARG A NH2 1 ATOM 5181 N N . PRO A 1 646 ? 33.491 28.506 47.997 1.00 17.66 ? 699 PRO A N 1 ATOM 5182 C CA . PRO A 1 646 ? 34.185 27.489 47.200 1.00 17.59 ? 699 PRO A CA 1 ATOM 5183 C C . PRO A 1 646 ? 33.290 26.800 46.192 1.00 16.32 ? 699 PRO A C 1 ATOM 5184 O O . PRO A 1 646 ? 33.688 26.578 45.045 1.00 17.38 ? 699 PRO A O 1 ATOM 5185 C CB . PRO A 1 646 ? 34.656 26.487 48.258 1.00 23.14 ? 699 PRO A CB 1 ATOM 5186 C CG . PRO A 1 646 ? 34.825 27.304 49.481 1.00 26.63 ? 699 PRO A CG 1 ATOM 5187 C CD . PRO A 1 646 ? 33.741 28.347 49.442 1.00 20.40 ? 699 PRO A CD 1 ATOM 5188 N N . GLU A 1 647 ? 32.079 26.461 46.610 1.00 13.68 ? 700 GLU A N 1 ATOM 5189 C CA . GLU A 1 647 ? 31.165 25.767 45.726 1.00 14.45 ? 700 GLU A CA 1 ATOM 5190 C C . GLU A 1 647 ? 30.839 26.657 44.536 1.00 17.66 ? 700 GLU A C 1 ATOM 5191 O O . GLU A 1 647 ? 30.764 26.187 43.404 1.00 14.64 ? 700 GLU A O 1 ATOM 5192 C CB . GLU A 1 647 ? 29.881 25.407 46.464 1.00 16.85 ? 700 GLU A CB 1 ATOM 5193 C CG . GLU A 1 647 ? 30.067 24.371 47.560 1.00 16.12 ? 700 GLU A CG 1 ATOM 5194 C CD . GLU A 1 647 ? 30.338 24.991 48.910 1.00 19.58 ? 700 GLU A CD 1 ATOM 5195 O OE1 . GLU A 1 647 ? 30.182 24.270 49.915 1.00 23.91 ? 700 GLU A OE1 1 ATOM 5196 O OE2 . GLU A 1 647 ? 30.709 26.188 48.965 1.00 17.31 ? 700 GLU A OE2 1 ATOM 5197 N N . TYR A 1 648 ? 30.634 27.943 44.794 1.00 18.37 ? 701 TYR A N 1 ATOM 5198 C CA . TYR A 1 648 ? 30.283 28.860 43.720 1.00 16.68 ? 701 TYR A CA 1 ATOM 5199 C C . TYR A 1 648 ? 31.499 29.175 42.849 1.00 14.89 ? 701 TYR A C 1 ATOM 5200 O O . TYR A 1 648 ? 31.359 29.421 41.657 1.00 18.24 ? 701 TYR A O 1 ATOM 5201 C CB . TYR A 1 648 ? 29.648 30.156 44.246 1.00 18.05 ? 701 TYR A CB 1 ATOM 5202 C CG . TYR A 1 648 ? 29.144 31.016 43.116 1.00 16.81 ? 701 TYR A CG 1 ATOM 5203 C CD1 . TYR A 1 648 ? 29.630 32.293 42.919 1.00 18.36 ? 701 TYR A CD1 1 ATOM 5204 C CD2 . TYR A 1 648 ? 28.219 30.515 42.203 1.00 21.09 ? 701 TYR A CD2 1 ATOM 5205 C CE1 . TYR A 1 648 ? 29.187 33.067 41.859 1.00 20.73 ? 701 TYR A CE1 1 ATOM 5206 C CE2 . TYR A 1 648 ? 27.776 31.272 41.147 1.00 21.46 ? 701 TYR A CE2 1 ATOM 5207 C CZ . TYR A 1 648 ? 28.255 32.551 40.984 1.00 21.72 ? 701 TYR A CZ 1 ATOM 5208 O OH . TYR A 1 648 ? 27.811 33.313 39.940 1.00 23.59 ? 701 TYR A OH 1 ATOM 5209 N N . ALA A 1 649 ? 32.692 29.165 43.434 1.00 12.91 ? 702 ALA A N 1 ATOM 5210 C CA . ALA A 1 649 ? 33.892 29.417 42.656 1.00 12.38 ? 702 ALA A CA 1 ATOM 5211 C C . ALA A 1 649 ? 34.029 28.320 41.589 1.00 13.87 ? 702 ALA A C 1 ATOM 5212 O O . ALA A 1 649 ? 34.364 28.609 40.448 1.00 18.08 ? 702 ALA A O 1 ATOM 5213 C CB . ALA A 1 649 ? 35.112 29.443 43.556 1.00 16.32 ? 702 ALA A CB 1 ATOM 5214 N N . VAL A 1 650 ? 33.765 27.072 41.986 1.00 15.71 ? 703 VAL A N 1 ATOM 5215 C CA . VAL A 1 650 ? 33.746 25.926 41.068 1.00 19.19 ? 703 VAL A CA 1 ATOM 5216 C C . VAL A 1 650 ? 32.725 26.120 39.937 1.00 15.99 ? 703 VAL A C 1 ATOM 5217 O O . VAL A 1 650 ? 32.976 25.765 38.787 1.00 17.23 ? 703 VAL A O 1 ATOM 5218 C CB . VAL A 1 650 ? 33.421 24.618 41.841 1.00 21.19 ? 703 VAL A CB 1 ATOM 5219 C CG1 . VAL A 1 650 ? 33.068 23.487 40.895 1.00 23.73 ? 703 VAL A CG1 1 ATOM 5220 C CG2 . VAL A 1 650 ? 34.587 24.221 42.723 1.00 22.93 ? 703 VAL A CG2 1 ATOM 5221 N N . ASN A 1 651 ? 31.586 26.714 40.276 1.00 16.87 ? 704 ASN A N 1 ATOM 5222 C CA . ASN A 1 651 ? 30.537 27.064 39.313 1.00 14.03 ? 704 ASN A CA 1 ATOM 5223 C C . ASN A 1 651 ? 31.023 28.162 38.341 1.00 13.38 ? 704 ASN A C 1 ATOM 5224 O O . ASN A 1 651 ? 31.065 27.975 37.119 1.00 13.40 ? 704 ASN A O 1 ATOM 5225 C CB . ASN A 1 651 ? 29.291 27.503 40.104 1.00 16.52 ? 704 ASN A CB 1 ATOM 5226 C CG . ASN A 1 651 ? 28.066 27.739 39.225 1.00 16.94 ? 704 ASN A CG 1 ATOM 5227 O OD1 . ASN A 1 651 ? 28.188 28.164 38.078 1.00 16.51 ? 704 ASN A OD1 1 ATOM 5228 N ND2 . ASN A 1 651 ? 26.869 27.479 39.778 1.00 12.33 ? 704 ASN A ND2 1 ATOM 5229 N N . SER A 1 652 ? 31.436 29.299 38.880 1.00 13.37 ? 705 SER A N 1 ATOM 5230 C CA . SER A 1 652 ? 31.646 30.467 38.040 1.00 16.73 ? 705 SER A CA 1 ATOM 5231 C C . SER A 1 652 ? 32.943 30.427 37.224 1.00 13.48 ? 705 SER A C 1 ATOM 5232 O O . SER A 1 652 ? 33.036 31.072 36.186 1.00 14.50 ? 705 SER A O 1 ATOM 5233 C CB . SER A 1 652 ? 31.595 31.726 38.885 1.00 21.22 ? 705 SER A CB 1 ATOM 5234 O OG . SER A 1 652 ? 32.718 31.834 39.725 1.00 23.54 ? 705 SER A OG 1 ATOM 5235 N N . ILE A 1 653 ? 33.927 29.648 37.669 1.00 14.53 ? 706 ILE A N 1 ATOM 5236 C CA . ILE A 1 653 ? 35.120 29.440 36.866 1.00 17.88 ? 706 ILE A CA 1 ATOM 5237 C C . ILE A 1 653 ? 34.744 28.819 35.526 1.00 16.49 ? 706 ILE A C 1 ATOM 5238 O O . ILE A 1 653 ? 35.411 29.032 34.499 1.00 18.49 ? 706 ILE A O 1 ATOM 5239 C CB . ILE A 1 653 ? 36.160 28.579 37.620 1.00 20.18 ? 706 ILE A CB 1 ATOM 5240 C CG1 . ILE A 1 653 ? 37.569 28.960 37.173 1.00 23.02 ? 706 ILE A CG1 1 ATOM 5241 C CG2 . ILE A 1 653 ? 35.908 27.083 37.419 1.00 20.94 ? 706 ILE A CG2 1 ATOM 5242 C CD1 . ILE A 1 653 ? 38.671 28.300 37.988 1.00 20.48 ? 706 ILE A CD1 1 ATOM 5243 N N . LYS A 1 654 ? 33.647 28.090 35.530 1.00 17.24 ? 707 LYS A N 1 ATOM 5244 C CA . LYS A 1 654 ? 33.091 27.529 34.305 1.00 19.37 ? 707 LYS A CA 1 ATOM 5245 C C . LYS A 1 654 ? 32.043 28.425 33.628 1.00 18.85 ? 707 LYS A C 1 ATOM 5246 O O . LYS A 1 654 ? 32.021 28.521 32.411 1.00 23.16 ? 707 LYS A O 1 ATOM 5247 C CB . LYS A 1 654 ? 32.504 26.145 34.590 1.00 18.38 ? 707 LYS A CB 1 ATOM 5248 C CG . LYS A 1 654 ? 33.528 25.128 35.072 1.00 18.62 ? 707 LYS A CG 1 ATOM 5249 C CD . LYS A 1 654 ? 34.718 24.999 34.143 1.00 21.00 ? 707 LYS A CD 1 ATOM 5250 C CE . LYS A 1 654 ? 35.554 23.729 34.424 1.00 21.61 ? 707 LYS A CE 1 ATOM 5251 N NZ . LYS A 1 654 ? 36.548 23.896 35.527 1.00 17.30 ? 707 LYS A NZ 1 ATOM 5252 N N . THR A 1 655 ? 31.175 29.071 34.400 1.00 21.16 ? 708 THR A N 1 ATOM 5253 C CA . THR A 1 655 ? 29.951 29.639 33.840 1.00 19.77 ? 708 THR A CA 1 ATOM 5254 C C . THR A 1 655 ? 30.000 31.155 33.685 1.00 19.98 ? 708 THR A C 1 ATOM 5255 O O . THR A 1 655 ? 29.167 31.732 32.989 1.00 16.49 ? 708 THR A O 1 ATOM 5256 C CB . THR A 1 655 ? 28.714 29.297 34.707 1.00 21.56 ? 708 THR A CB 1 ATOM 5257 O OG1 . THR A 1 655 ? 28.912 29.750 36.055 1.00 19.99 ? 708 THR A OG1 1 ATOM 5258 C CG2 . THR A 1 655 ? 28.509 27.795 34.829 1.00 20.58 ? 708 THR A CG2 1 ATOM 5259 N N . ASP A 1 656 ? 30.926 31.808 34.372 1.00 15.34 ? 709 ASP A N 1 ATOM 5260 C CA . ASP A 1 656 ? 31.028 33.249 34.277 1.00 18.74 ? 709 ASP A CA 1 ATOM 5261 C C . ASP A 1 656 ? 32.081 33.615 33.254 1.00 17.88 ? 709 ASP A C 1 ATOM 5262 O O . ASP A 1 656 ? 33.217 33.153 33.337 1.00 19.43 ? 709 ASP A O 1 ATOM 5263 C CB . ASP A 1 656 ? 31.375 33.851 35.637 1.00 18.41 ? 709 ASP A CB 1 ATOM 5264 C CG . ASP A 1 656 ? 31.087 35.340 35.704 1.00 19.71 ? 709 ASP A CG 1 ATOM 5265 O OD1 . ASP A 1 656 ? 30.978 35.979 34.638 1.00 19.02 ? 709 ASP A OD1 1 ATOM 5266 O OD2 . ASP A 1 656 ? 30.962 35.950 36.784 1.00 19.96 ? 709 ASP A OD2 1 ATOM 5267 N N . VAL A 1 657 ? 31.708 34.452 32.294 1.00 17.51 ? 710 VAL A N 1 ATOM 5268 C CA . VAL A 1 657 ? 32.631 34.853 31.239 1.00 18.37 ? 710 VAL A CA 1 ATOM 5269 C C . VAL A 1 657 ? 33.527 35.991 31.710 1.00 16.54 ? 710 VAL A C 1 ATOM 5270 O O . VAL A 1 657 ? 34.461 36.385 31.022 1.00 17.75 ? 710 VAL A O 1 ATOM 5271 C CB . VAL A 1 657 ? 31.884 35.277 29.939 1.00 19.00 ? 710 VAL A CB 1 ATOM 5272 C CG1 . VAL A 1 657 ? 31.139 34.087 29.348 1.00 23.64 ? 710 VAL A CG1 1 ATOM 5273 C CG2 . VAL A 1 657 ? 30.944 36.458 30.190 1.00 22.18 ? 710 VAL A CG2 1 ATOM 5274 N N . HIS A 1 658 ? 33.243 36.505 32.901 1.00 16.90 ? 711 HIS A N 1 ATOM 5275 C CA . HIS A 1 658 ? 34.136 37.437 33.570 1.00 15.19 ? 711 HIS A CA 1 ATOM 5276 C C . HIS A 1 658 ? 35.167 36.686 34.369 1.00 16.41 ? 711 HIS A C 1 ATOM 5277 O O . HIS A 1 658 ? 34.871 35.633 34.920 1.00 16.75 ? 711 HIS A O 1 ATOM 5278 C CB . HIS A 1 658 ? 33.345 38.330 34.532 1.00 17.20 ? 711 HIS A CB 1 ATOM 5279 C CG . HIS A 1 658 ? 32.210 39.050 33.882 1.00 14.38 ? 711 HIS A CG 1 ATOM 5280 N ND1 . HIS A 1 658 ? 30.936 38.533 33.834 1.00 16.11 ? 711 HIS A ND1 1 ATOM 5281 C CD2 . HIS A 1 658 ? 32.158 40.247 33.252 1.00 15.84 ? 711 HIS A CD2 1 ATOM 5282 C CE1 . HIS A 1 658 ? 30.147 39.381 33.196 1.00 15.95 ? 711 HIS A CE1 1 ATOM 5283 N NE2 . HIS A 1 658 ? 30.867 40.428 32.828 1.00 13.40 ? 711 HIS A NE2 1 ATOM 5284 N N . SER A 1 659 ? 36.364 37.247 34.480 1.00 13.63 ? 712 SER A N 1 ATOM 5285 C CA . SER A 1 659 ? 37.273 36.817 35.533 1.00 14.60 ? 712 SER A CA 1 ATOM 5286 C C . SER A 1 659 ? 36.663 37.181 36.878 1.00 18.02 ? 712 SER A C 1 ATOM 5287 O O . SER A 1 659 ? 35.928 38.152 36.979 1.00 16.48 ? 712 SER A O 1 ATOM 5288 C CB . SER A 1 659 ? 38.639 37.474 35.378 1.00 16.62 ? 712 SER A CB 1 ATOM 5289 O OG . SER A 1 659 ? 39.260 37.060 34.177 1.00 16.68 ? 712 SER A OG 1 ATOM 5290 N N . PRO A 1 660 ? 36.984 36.414 37.912 1.00 16.54 ? 713 PRO A N 1 ATOM 5291 C CA . PRO A 1 660 ? 36.675 36.800 39.289 1.00 17.04 ? 713 PRO A CA 1 ATOM 5292 C C . PRO A 1 660 ? 37.316 38.134 39.663 1.00 17.71 ? 713 PRO A C 1 ATOM 5293 O O . PRO A 1 660 ? 38.383 38.475 39.154 1.00 14.15 ? 713 PRO A O 1 ATOM 5294 C CB . PRO A 1 660 ? 37.274 35.650 40.122 1.00 17.04 ? 713 PRO A CB 1 ATOM 5295 C CG . PRO A 1 660 ? 37.405 34.509 39.178 1.00 20.65 ? 713 PRO A CG 1 ATOM 5296 C CD . PRO A 1 660 ? 37.676 35.118 37.842 1.00 16.91 ? 713 PRO A CD 1 ATOM 5297 N N . GLY A 1 661 ? 36.651 38.892 40.528 1.00 19.97 ? 714 GLY A N 1 ATOM 5298 C CA . GLY A 1 661 ? 37.000 40.282 40.742 1.00 18.17 ? 714 GLY A CA 1 ATOM 5299 C C . GLY A 1 661 ? 38.457 40.501 41.097 1.00 17.68 ? 714 GLY A C 1 ATOM 5300 O O . GLY A 1 661 ? 39.075 41.443 40.620 1.00 15.87 ? 714 GLY A O 1 ATOM 5301 N N . ASN A 1 662 ? 39.014 39.658 41.958 1.00 13.20 ? 715 ASN A N 1 ATOM 5302 C CA . ASN A 1 662 ? 40.400 39.849 42.349 1.00 14.15 ? 715 ASN A CA 1 ATOM 5303 C C . ASN A 1 662 ? 41.360 39.781 41.150 1.00 17.17 ? 715 ASN A C 1 ATOM 5304 O O . ASN A 1 662 ? 42.311 40.545 41.064 1.00 13.58 ? 715 ASN A O 1 ATOM 5305 C CB . ASN A 1 662 ? 40.796 38.862 43.455 1.00 16.39 ? 715 ASN A CB 1 ATOM 5306 C CG . ASN A 1 662 ? 40.673 37.412 43.029 1.00 19.65 ? 715 ASN A CG 1 ATOM 5307 O OD1 . ASN A 1 662 ? 39.602 36.945 42.614 1.00 17.05 ? 715 ASN A OD1 1 ATOM 5308 N ND2 . ASN A 1 662 ? 41.766 36.682 43.159 1.00 18.34 ? 715 ASN A ND2 1 ATOM 5309 N N . PHE A 1 663 ? 41.088 38.896 40.198 1.00 15.36 ? 716 PHE A N 1 ATOM 5310 C CA . PHE A 1 663 ? 41.922 38.804 38.998 1.00 15.50 ? 716 PHE A CA 1 ATOM 5311 C C . PHE A 1 663 ? 41.638 39.878 37.931 1.00 16.80 ? 716 PHE A C 1 ATOM 5312 O O . PHE A 1 663 ? 42.542 40.259 37.173 1.00 15.48 ? 716 PHE A O 1 ATOM 5313 C CB . PHE A 1 663 ? 41.797 37.411 38.392 1.00 17.53 ? 716 PHE A CB 1 ATOM 5314 C CG . PHE A 1 663 ? 42.417 36.324 39.249 1.00 16.55 ? 716 PHE A CG 1 ATOM 5315 C CD1 . PHE A 1 663 ? 41.647 35.297 39.749 1.00 20.13 ? 716 PHE A CD1 1 ATOM 5316 C CD2 . PHE A 1 663 ? 43.756 36.365 39.583 1.00 21.34 ? 716 PHE A CD2 1 ATOM 5317 C CE1 . PHE A 1 663 ? 42.207 34.314 40.547 1.00 21.74 ? 716 PHE A CE1 1 ATOM 5318 C CE2 . PHE A 1 663 ? 44.311 35.395 40.395 1.00 20.23 ? 716 PHE A CE2 1 ATOM 5319 C CZ . PHE A 1 663 ? 43.538 34.370 40.866 1.00 21.00 ? 716 PHE A CZ 1 ATOM 5320 N N . ARG A 1 664 ? 40.401 40.365 37.860 1.00 14.72 ? 717 ARG A N 1 ATOM 5321 C CA . ARG A 1 664 ? 40.131 41.547 37.058 1.00 17.79 ? 717 ARG A CA 1 ATOM 5322 C C . ARG A 1 664 ? 41.084 42.649 37.514 1.00 18.84 ? 717 ARG A C 1 ATOM 5323 O O . ARG A 1 664 ? 41.719 43.313 36.697 1.00 19.25 ? 717 ARG A O 1 ATOM 5324 C CB . ARG A 1 664 ? 38.677 41.994 37.194 1.00 18.15 ? 717 ARG A CB 1 ATOM 5325 C CG . ARG A 1 664 ? 37.687 40.935 36.782 1.00 17.18 ? 717 ARG A CG 1 ATOM 5326 C CD . ARG A 1 664 ? 36.237 41.391 36.790 1.00 15.89 ? 717 ARG A CD 1 ATOM 5327 N NE . ARG A 1 664 ? 35.934 42.278 35.677 1.00 16.22 ? 717 ARG A NE 1 ATOM 5328 C CZ . ARG A 1 664 ? 34.704 42.568 35.287 1.00 18.95 ? 717 ARG A CZ 1 ATOM 5329 N NH1 . ARG A 1 664 ? 33.669 42.036 35.928 1.00 19.77 ? 717 ARG A NH1 1 ATOM 5330 N NH2 . ARG A 1 664 ? 34.498 43.391 34.269 1.00 18.25 ? 717 ARG A NH2 1 ATOM 5331 N N . ILE A 1 665 ? 41.208 42.820 38.825 1.00 17.28 ? 718 ILE A N 1 ATOM 5332 C CA . ILE A 1 665 ? 42.093 43.843 39.366 1.00 18.06 ? 718 ILE A CA 1 ATOM 5333 C C . ILE A 1 665 ? 43.566 43.542 39.038 1.00 19.05 ? 718 ILE A C 1 ATOM 5334 O O . ILE A 1 665 ? 44.241 44.348 38.399 1.00 21.97 ? 718 ILE A O 1 ATOM 5335 C CB . ILE A 1 665 ? 41.896 43.993 40.879 1.00 21.01 ? 718 ILE A CB 1 ATOM 5336 C CG1 . ILE A 1 665 ? 40.416 44.232 41.201 1.00 25.83 ? 718 ILE A CG1 1 ATOM 5337 C CG2 . ILE A 1 665 ? 42.718 45.172 41.405 1.00 20.48 ? 718 ILE A CG2 1 ATOM 5338 C CD1 . ILE A 1 665 ? 39.616 42.957 41.296 1.00 28.95 ? 718 ILE A CD1 1 ATOM 5339 N N . ILE A 1 666 ? 44.060 42.383 39.465 1.00 20.06 ? 719 ILE A N 1 ATOM 5340 C CA . ILE A 1 666 ? 45.467 42.021 39.258 1.00 22.33 ? 719 ILE A CA 1 ATOM 5341 C C . ILE A 1 666 ? 45.821 41.977 37.773 1.00 20.87 ? 719 ILE A C 1 ATOM 5342 O O . ILE A 1 666 ? 46.819 42.552 37.340 1.00 23.67 ? 719 ILE A O 1 ATOM 5343 C CB . ILE A 1 666 ? 45.766 40.667 39.913 1.00 21.03 ? 719 ILE A CB 1 ATOM 5344 C CG1 . ILE A 1 666 ? 45.587 40.768 41.422 1.00 27.18 ? 719 ILE A CG1 1 ATOM 5345 C CG2 . ILE A 1 666 ? 47.169 40.189 39.565 1.00 25.33 ? 719 ILE A CG2 1 ATOM 5346 C CD1 . ILE A 1 666 ? 44.519 39.859 41.938 1.00 31.98 ? 719 ILE A CD1 1 ATOM 5347 N N . GLY A 1 667 ? 44.987 41.303 36.994 1.00 22.11 ? 720 GLY A N 1 ATOM 5348 C CA . GLY A 1 667 ? 45.157 41.264 35.555 1.00 23.46 ? 720 GLY A CA 1 ATOM 5349 C C . GLY A 1 667 ? 45.416 42.627 34.952 1.00 20.46 ? 720 GLY A C 1 ATOM 5350 O O . GLY A 1 667 ? 46.413 42.830 34.261 1.00 24.37 ? 720 GLY A O 1 ATOM 5351 N N . THR A 1 668 ? 44.503 43.560 35.174 1.00 21.16 ? 721 THR A N 1 ATOM 5352 C CA . THR A 1 668 ? 44.476 44.784 34.380 1.00 20.90 ? 721 THR A CA 1 ATOM 5353 C C . THR A 1 668 ? 45.610 45.685 34.807 1.00 23.49 ? 721 THR A C 1 ATOM 5354 O O . THR A 1 668 ? 46.255 46.319 33.985 1.00 23.22 ? 721 THR A O 1 ATOM 5355 C CB . THR A 1 668 ? 43.151 45.517 34.566 1.00 23.83 ? 721 THR A CB 1 ATOM 5356 O OG1 . THR A 1 668 ? 42.897 45.720 35.966 1.00 22.40 ? 721 THR A OG1 1 ATOM 5357 C CG2 . THR A 1 668 ? 42.010 44.649 34.096 1.00 19.23 ? 721 THR A CG2 1 ATOM 5358 N N . LEU A 1 669 ? 45.848 45.740 36.107 1.00 22.20 ? 722 LEU A N 1 ATOM 5359 C CA . LEU A 1 669 ? 46.890 46.600 36.626 1.00 22.36 ? 722 LEU A CA 1 ATOM 5360 C C . LEU A 1 669 ? 48.270 46.032 36.293 1.00 22.82 ? 722 LEU A C 1 ATOM 5361 O O . LEU A 1 669 ? 49.182 46.786 35.983 1.00 21.57 ? 722 LEU A O 1 ATOM 5362 C CB . LEU A 1 669 ? 46.723 46.793 38.135 1.00 19.43 ? 722 LEU A CB 1 ATOM 5363 C CG . LEU A 1 669 ? 45.438 47.536 38.528 1.00 21.74 ? 722 LEU A CG 1 ATOM 5364 C CD1 . LEU A 1 669 ? 45.206 47.456 40.027 1.00 22.82 ? 722 LEU A CD1 1 ATOM 5365 C CD2 . LEU A 1 669 ? 45.453 49.000 38.065 1.00 21.69 ? 722 LEU A CD2 1 ATOM 5366 N N . GLN A 1 670 ? 48.415 44.709 36.325 1.00 23.96 ? 723 GLN A N 1 ATOM 5367 C CA . GLN A 1 670 ? 49.648 44.079 35.853 1.00 23.27 ? 723 GLN A CA 1 ATOM 5368 C C . GLN A 1 670 ? 50.036 44.646 34.478 1.00 26.80 ? 723 GLN A C 1 ATOM 5369 O O . GLN A 1 670 ? 51.224 44.741 34.136 1.00 23.99 ? 723 GLN A O 1 ATOM 5370 C CB . GLN A 1 670 ? 49.499 42.558 35.760 1.00 23.65 ? 723 GLN A CB 1 ATOM 5371 C CG . GLN A 1 670 ? 49.837 41.795 37.047 1.00 22.17 ? 723 GLN A CG 1 ATOM 5372 C CD . GLN A 1 670 ? 49.643 40.284 36.911 1.00 21.43 ? 723 GLN A CD 1 ATOM 5373 O OE1 . GLN A 1 670 ? 49.235 39.805 35.860 1.00 24.34 ? 723 GLN A OE1 1 ATOM 5374 N NE2 . GLN A 1 670 ? 49.947 39.540 37.972 1.00 24.53 ? 723 GLN A NE2 1 ATOM 5375 N N . ASN A 1 671 ? 49.024 45.020 33.704 1.00 19.78 ? 724 ASN A N 1 ATOM 5376 C CA . ASN A 1 671 ? 49.192 45.409 32.309 1.00 21.40 ? 724 ASN A CA 1 ATOM 5377 C C . ASN A 1 671 ? 49.295 46.919 32.137 1.00 22.99 ? 724 ASN A C 1 ATOM 5378 O O . ASN A 1 671 ? 49.441 47.407 31.017 1.00 25.94 ? 724 ASN A O 1 ATOM 5379 C CB . ASN A 1 671 ? 48.016 44.892 31.465 1.00 22.63 ? 724 ASN A CB 1 ATOM 5380 C CG . ASN A 1 671 ? 48.129 43.414 31.150 1.00 22.44 ? 724 ASN A CG 1 ATOM 5381 O OD1 . ASN A 1 671 ? 49.237 42.860 31.089 1.00 23.37 ? 724 ASN A OD1 1 ATOM 5382 N ND2 . ASN A 1 671 ? 46.983 42.757 30.950 1.00 20.14 ? 724 ASN A ND2 1 ATOM 5383 N N . SER A 1 672 ? 49.208 47.659 33.240 1.00 20.54 ? 725 SER A N 1 ATOM 5384 C CA . SER A 1 672 ? 49.154 49.116 33.186 1.00 22.33 ? 725 SER A CA 1 ATOM 5385 C C . SER A 1 672 ? 50.474 49.759 33.643 1.00 24.63 ? 725 SER A C 1 ATOM 5386 O O . SER A 1 672 ? 50.792 49.774 34.824 1.00 25.43 ? 725 SER A O 1 ATOM 5387 C CB . SER A 1 672 ? 47.996 49.634 34.049 1.00 24.33 ? 725 SER A CB 1 ATOM 5388 O OG . SER A 1 672 ? 48.158 51.008 34.354 1.00 25.30 ? 725 SER A OG 1 ATOM 5389 N N . ALA A 1 673 ? 51.240 50.289 32.698 1.00 25.67 ? 726 ALA A N 1 ATOM 5390 C CA . ALA A 1 673 ? 52.409 51.094 33.036 1.00 28.21 ? 726 ALA A CA 1 ATOM 5391 C C . ALA A 1 673 ? 52.004 52.224 33.968 1.00 28.36 ? 726 ALA A C 1 ATOM 5392 O O . ALA A 1 673 ? 52.749 52.602 34.873 1.00 23.76 ? 726 ALA A O 1 ATOM 5393 C CB . ALA A 1 673 ? 53.044 51.660 31.773 1.00 29.43 ? 726 ALA A CB 1 ATOM 5394 N N . GLU A 1 674 ? 50.813 52.766 33.740 1.00 29.61 ? 727 GLU A N 1 ATOM 5395 C CA . GLU A 1 674 ? 50.339 53.905 34.516 1.00 29.92 ? 727 GLU A CA 1 ATOM 5396 C C . GLU A 1 674 ? 50.184 53.538 35.983 1.00 25.53 ? 727 GLU A C 1 ATOM 5397 O O . GLU A 1 674 ? 50.561 54.309 36.856 1.00 22.73 ? 727 GLU A O 1 ATOM 5398 C CB . GLU A 1 674 ? 49.023 54.424 33.952 1.00 33.46 ? 727 GLU A CB 1 ATOM 5399 C CG . GLU A 1 674 ? 49.174 55.096 32.599 1.00 36.20 ? 727 GLU A CG 1 ATOM 5400 C CD . GLU A 1 674 ? 49.518 54.113 31.498 1.00 38.66 ? 727 GLU A CD 1 ATOM 5401 O OE1 . GLU A 1 674 ? 49.160 52.921 31.624 1.00 37.01 ? 727 GLU A OE1 1 ATOM 5402 O OE2 . GLU A 1 674 ? 50.144 54.536 30.503 1.00 40.82 ? 727 GLU A OE2 1 ATOM 5403 N N . PHE A 1 675 ? 49.650 52.355 36.260 1.00 24.29 ? 728 PHE A N 1 ATOM 5404 C CA . PHE A 1 675 ? 49.514 51.923 37.647 1.00 23.71 ? 728 PHE A CA 1 ATOM 5405 C C . PHE A 1 675 ? 50.869 51.924 38.344 1.00 25.50 ? 728 PHE A C 1 ATOM 5406 O O . PHE A 1 675 ? 51.010 52.357 39.493 1.00 24.10 ? 728 PHE A O 1 ATOM 5407 C CB . PHE A 1 675 ? 48.934 50.517 37.741 1.00 24.43 ? 728 PHE A CB 1 ATOM 5408 C CG . PHE A 1 675 ? 49.029 49.943 39.111 1.00 22.97 ? 728 PHE A CG 1 ATOM 5409 C CD1 . PHE A 1 675 ? 50.021 49.036 39.428 1.00 21.20 ? 728 PHE A CD1 1 ATOM 5410 C CD2 . PHE A 1 675 ? 48.154 50.343 40.099 1.00 23.91 ? 728 PHE A CD2 1 ATOM 5411 C CE1 . PHE A 1 675 ? 50.118 48.520 40.695 1.00 23.52 ? 728 PHE A CE1 1 ATOM 5412 C CE2 . PHE A 1 675 ? 48.255 49.839 41.359 1.00 23.48 ? 728 PHE A CE2 1 ATOM 5413 C CZ . PHE A 1 675 ? 49.242 48.916 41.661 1.00 23.25 ? 728 PHE A CZ 1 ATOM 5414 N N . SER A 1 676 ? 51.865 51.399 37.643 1.00 25.88 ? 729 SER A N 1 ATOM 5415 C CA . SER A 1 676 ? 53.152 51.095 38.253 1.00 29.71 ? 729 SER A CA 1 ATOM 5416 C C . SER A 1 676 ? 53.909 52.403 38.422 1.00 31.94 ? 729 SER A C 1 ATOM 5417 O O . SER A 1 676 ? 54.683 52.572 39.363 1.00 29.74 ? 729 SER A O 1 ATOM 5418 C CB . SER A 1 676 ? 53.950 50.111 37.389 1.00 28.85 ? 729 SER A CB 1 ATOM 5419 O OG . SER A 1 676 ? 53.697 48.770 37.773 1.00 27.18 ? 729 SER A OG 1 ATOM 5420 N N . GLU A 1 677 ? 53.653 53.346 37.522 1.00 31.77 ? 730 GLU A N 1 ATOM 5421 C CA . GLU A 1 677 ? 54.124 54.708 37.711 1.00 35.64 ? 730 GLU A CA 1 ATOM 5422 C C . GLU A 1 677 ? 53.534 55.317 38.987 1.00 32.58 ? 730 GLU A C 1 ATOM 5423 O O . GLU A 1 677 ? 54.224 55.998 39.740 1.00 26.51 ? 730 GLU A O 1 ATOM 5424 C CB . GLU A 1 677 ? 53.760 55.562 36.499 1.00 40.47 ? 730 GLU A CB 1 ATOM 5425 C CG . GLU A 1 677 ? 54.407 56.934 36.502 1.00 46.17 ? 730 GLU A CG 1 ATOM 5426 C CD . GLU A 1 677 ? 53.935 57.799 37.655 1.00 49.42 ? 730 GLU A CD 1 ATOM 5427 O OE1 . GLU A 1 677 ? 53.050 58.659 37.435 1.00 50.19 ? 730 GLU A OE1 1 ATOM 5428 O OE2 . GLU A 1 677 ? 54.447 57.628 38.782 1.00 53.56 ? 730 GLU A OE2 1 ATOM 5429 N N . ALA A 1 678 ? 52.258 55.061 39.241 1.00 30.30 ? 731 ALA A N 1 ATOM 5430 C CA . ALA A 1 678 ? 51.561 55.760 40.313 1.00 27.17 ? 731 ALA A CA 1 ATOM 5431 C C . ALA A 1 678 ? 52.020 55.278 41.683 1.00 26.42 ? 731 ALA A C 1 ATOM 5432 O O . ALA A 1 678 ? 52.041 56.049 42.637 1.00 29.94 ? 731 ALA A O 1 ATOM 5433 C CB . ALA A 1 678 ? 50.054 55.587 40.161 1.00 30.10 ? 731 ALA A CB 1 ATOM 5434 N N . PHE A 1 679 ? 52.390 54.004 41.783 1.00 24.29 ? 732 PHE A N 1 ATOM 5435 C CA . PHE A 1 679 ? 52.795 53.429 43.058 1.00 29.35 ? 732 PHE A CA 1 ATOM 5436 C C . PHE A 1 679 ? 54.280 53.055 43.091 1.00 28.86 ? 732 PHE A C 1 ATOM 5437 O O . PHE A 1 679 ? 54.722 52.327 43.977 1.00 29.68 ? 732 PHE A O 1 ATOM 5438 C CB . PHE A 1 679 ? 51.911 52.221 43.378 1.00 26.30 ? 732 PHE A CB 1 ATOM 5439 C CG . PHE A 1 679 ? 50.508 52.606 43.741 1.00 26.45 ? 732 PHE A CG 1 ATOM 5440 C CD1 . PHE A 1 679 ? 50.192 52.960 45.040 1.00 27.20 ? 732 PHE A CD1 1 ATOM 5441 C CD2 . PHE A 1 679 ? 49.514 52.668 42.772 1.00 26.78 ? 732 PHE A CD2 1 ATOM 5442 C CE1 . PHE A 1 679 ? 48.903 53.349 45.374 1.00 25.70 ? 732 PHE A CE1 1 ATOM 5443 C CE2 . PHE A 1 679 ? 48.229 53.056 43.108 1.00 22.96 ? 732 PHE A CE2 1 ATOM 5444 C CZ . PHE A 1 679 ? 47.927 53.396 44.406 1.00 22.90 ? 732 PHE A CZ 1 ATOM 5445 N N . HIS A 1 680 ? 55.032 53.559 42.116 1.00 31.60 ? 733 HIS A N 1 ATOM 5446 C CA . HIS A 1 680 ? 56.490 53.446 42.117 1.00 33.89 ? 733 HIS A CA 1 ATOM 5447 C C . HIS A 1 680 ? 56.925 51.992 42.261 1.00 33.68 ? 733 HIS A C 1 ATOM 5448 O O . HIS A 1 680 ? 57.781 51.654 43.078 1.00 35.41 ? 733 HIS A O 1 ATOM 5449 C CB . HIS A 1 680 ? 57.087 54.305 43.233 1.00 35.74 ? 733 HIS A CB 1 ATOM 5450 C CG . HIS A 1 680 ? 56.488 55.673 43.316 1.00 39.37 ? 733 HIS A CG 1 ATOM 5451 N ND1 . HIS A 1 680 ? 55.520 56.006 44.239 1.00 40.39 ? 733 HIS A ND1 1 ATOM 5452 C CD2 . HIS A 1 680 ? 56.698 56.785 42.573 1.00 41.92 ? 733 HIS A CD2 1 ATOM 5453 C CE1 . HIS A 1 680 ? 55.170 57.269 44.069 1.00 41.77 ? 733 HIS A CE1 1 ATOM 5454 N NE2 . HIS A 1 680 ? 55.867 57.764 43.062 1.00 40.87 ? 733 HIS A NE2 1 ATOM 5455 N N . CYS A 1 681 ? 56.322 51.128 41.459 1.00 31.91 ? 734 CYS A N 1 ATOM 5456 C CA . CYS A 1 681 ? 56.582 49.703 41.555 1.00 29.92 ? 734 CYS A CA 1 ATOM 5457 C C . CYS A 1 681 ? 57.868 49.332 40.824 1.00 32.44 ? 734 CYS A C 1 ATOM 5458 O O . CYS A 1 681 ? 58.052 49.707 39.672 1.00 26.34 ? 734 CYS A O 1 ATOM 5459 C CB . CYS A 1 681 ? 55.416 48.937 40.950 1.00 31.55 ? 734 CYS A CB 1 ATOM 5460 S SG . CYS A 1 681 ? 53.883 49.209 41.864 1.00 26.07 ? 734 CYS A SG 1 ATOM 5461 N N . ARG A 1 682 ? 58.732 48.574 41.495 1.00 36.12 ? 735 ARG A N 1 ATOM 5462 C CA . ARG A 1 682 ? 59.930 48.009 40.870 1.00 40.87 ? 735 ARG A CA 1 ATOM 5463 C C . ARG A 1 682 ? 59.578 47.175 39.644 1.00 39.36 ? 735 ARG A C 1 ATOM 5464 O O . ARG A 1 682 ? 58.543 46.509 39.605 1.00 35.32 ? 735 ARG A O 1 ATOM 5465 C CB . ARG A 1 682 ? 60.692 47.135 41.876 1.00 45.60 ? 735 ARG A CB 1 ATOM 5466 C CG . ARG A 1 682 ? 62.070 47.666 42.262 1.00 51.55 ? 735 ARG A CG 1 ATOM 5467 C CD . ARG A 1 682 ? 62.515 47.303 43.683 1.00 56.86 ? 735 ARG A CD 1 ATOM 5468 N NE . ARG A 1 682 ? 63.882 46.779 43.720 1.00 61.96 ? 735 ARG A NE 1 ATOM 5469 C CZ . ARG A 1 682 ? 64.511 46.386 44.824 1.00 64.21 ? 735 ARG A CZ 1 ATOM 5470 N NH1 . ARG A 1 682 ? 63.902 46.450 46.003 1.00 64.50 ? 735 ARG A NH1 1 ATOM 5471 N NH2 . ARG A 1 682 ? 65.752 45.926 44.751 1.00 63.73 ? 735 ARG A NH2 1 ATOM 5472 N N . LYS A 1 683 ? 60.460 47.199 38.651 1.00 39.70 ? 736 LYS A N 1 ATOM 5473 C CA . LYS A 1 683 ? 60.409 46.245 37.549 1.00 40.82 ? 736 LYS A CA 1 ATOM 5474 C C . LYS A 1 683 ? 60.295 44.820 38.076 1.00 39.14 ? 736 LYS A C 1 ATOM 5475 O O . LYS A 1 683 ? 61.079 44.398 38.924 1.00 32.97 ? 736 LYS A O 1 ATOM 5476 C CB . LYS A 1 683 ? 61.661 46.379 36.685 1.00 45.12 ? 736 LYS A CB 1 ATOM 5477 C CG . LYS A 1 683 ? 61.451 46.045 35.215 1.00 47.69 ? 736 LYS A CG 1 ATOM 5478 C CD . LYS A 1 683 ? 62.676 46.427 34.392 1.00 51.66 ? 736 LYS A CD 1 ATOM 5479 C CE . LYS A 1 683 ? 63.890 45.575 34.763 1.00 53.45 ? 736 LYS A CE 1 ATOM 5480 N NZ . LYS A 1 683 ? 64.602 46.085 35.975 1.00 53.37 ? 736 LYS A NZ 1 ATOM 5481 N N . ASN A 1 684 ? 59.307 44.088 37.573 1.00 35.98 ? 737 ASN A N 1 ATOM 5482 C CA . ASN A 1 684 ? 59.154 42.675 37.899 1.00 35.07 ? 737 ASN A CA 1 ATOM 5483 C C . ASN A 1 684 ? 58.754 42.432 39.350 1.00 29.43 ? 737 ASN A C 1 ATOM 5484 O O . ASN A 1 684 ? 58.802 41.299 39.826 1.00 26.79 ? 737 ASN A O 1 ATOM 5485 C CB . ASN A 1 684 ? 60.450 41.919 37.604 1.00 38.21 ? 737 ASN A CB 1 ATOM 5486 C CG . ASN A 1 684 ? 60.515 41.414 36.181 1.00 40.97 ? 737 ASN A CG 1 ATOM 5487 O OD1 . ASN A 1 684 ? 59.503 40.994 35.607 1.00 42.16 ? 737 ASN A OD1 1 ATOM 5488 N ND2 . ASN A 1 684 ? 61.704 41.456 35.598 1.00 43.09 ? 737 ASN A ND2 1 ATOM 5489 N N . SER A 1 685 ? 58.346 43.485 40.050 1.00 26.48 ? 738 SER A N 1 ATOM 5490 C CA . SER A 1 685 ? 57.404 43.319 41.150 1.00 30.06 ? 738 SER A CA 1 ATOM 5491 C C . SER A 1 685 ? 56.200 42.536 40.651 1.00 24.98 ? 738 SER A C 1 ATOM 5492 O O . SER A 1 685 ? 55.943 42.485 39.448 1.00 26.90 ? 738 SER A O 1 ATOM 5493 C CB . SER A 1 685 ? 56.951 44.674 41.690 1.00 30.58 ? 738 SER A CB 1 ATOM 5494 O OG . SER A 1 685 ? 56.389 45.442 40.645 1.00 32.00 ? 738 SER A OG 1 ATOM 5495 N N . TYR A 1 686 ? 55.470 41.913 41.568 1.00 25.71 ? 739 TYR A N 1 ATOM 5496 C CA . TYR A 1 686 ? 54.325 41.112 41.166 1.00 24.13 ? 739 TYR A CA 1 ATOM 5497 C C . TYR A 1 686 ? 53.317 41.938 40.361 1.00 22.45 ? 739 TYR A C 1 ATOM 5498 O O . TYR A 1 686 ? 52.762 41.445 39.379 1.00 23.83 ? 739 TYR A O 1 ATOM 5499 C CB . TYR A 1 686 ? 53.644 40.465 42.363 1.00 24.33 ? 739 TYR A CB 1 ATOM 5500 C CG . TYR A 1 686 ? 52.461 39.619 41.966 1.00 22.95 ? 739 TYR A CG 1 ATOM 5501 C CD1 . TYR A 1 686 ? 51.164 40.038 42.240 1.00 24.42 ? 739 TYR A CD1 1 ATOM 5502 C CD2 . TYR A 1 686 ? 52.634 38.413 41.300 1.00 22.71 ? 739 TYR A CD2 1 ATOM 5503 C CE1 . TYR A 1 686 ? 50.072 39.278 41.872 1.00 23.19 ? 739 TYR A CE1 1 ATOM 5504 C CE2 . TYR A 1 686 ? 51.541 37.638 40.924 1.00 26.90 ? 739 TYR A CE2 1 ATOM 5505 C CZ . TYR A 1 686 ? 50.263 38.078 41.218 1.00 25.32 ? 739 TYR A CZ 1 ATOM 5506 O OH . TYR A 1 686 ? 49.171 37.331 40.862 1.00 24.81 ? 739 TYR A OH 1 ATOM 5507 N N . MET A 1 687 ? 53.080 43.181 40.763 1.00 19.43 ? 740 MET A N 1 ATOM 5508 C CA . MET A 1 687 ? 52.066 44.002 40.102 1.00 22.79 ? 740 MET A CA 1 ATOM 5509 C C . MET A 1 687 ? 52.583 44.616 38.797 1.00 23.40 ? 740 MET A C 1 ATOM 5510 O O . MET A 1 687 ? 51.823 45.221 38.040 1.00 21.66 ? 740 MET A O 1 ATOM 5511 C CB . MET A 1 687 ? 51.561 45.097 41.044 1.00 20.48 ? 740 MET A CB 1 ATOM 5512 C CG . MET A 1 687 ? 50.778 44.550 42.242 1.00 19.84 ? 740 MET A CG 1 ATOM 5513 S SD . MET A 1 687 ? 49.348 43.546 41.768 1.00 22.25 ? 740 MET A SD 1 ATOM 5514 C CE . MET A 1 687 ? 48.607 44.539 40.527 1.00 20.74 ? 740 MET A CE 1 ATOM 5515 N N . ASN A 1 688 ? 53.873 44.444 38.535 1.00 26.30 ? 741 ASN A N 1 ATOM 5516 C CA . ASN A 1 688 ? 54.559 45.149 37.458 1.00 28.01 ? 741 ASN A CA 1 ATOM 5517 C C . ASN A 1 688 ? 55.468 44.237 36.621 1.00 29.24 ? 741 ASN A C 1 ATOM 5518 O O . ASN A 1 688 ? 56.675 44.489 36.506 1.00 26.31 ? 741 ASN A O 1 ATOM 5519 C CB . ASN A 1 688 ? 55.399 46.271 38.056 1.00 26.86 ? 741 ASN A CB 1 ATOM 5520 C CG . ASN A 1 688 ? 55.927 47.224 37.015 1.00 26.44 ? 741 ASN A CG 1 ATOM 5521 O OD1 . ASN A 1 688 ? 55.557 47.157 35.850 1.00 28.65 ? 741 ASN A OD1 1 ATOM 5522 N ND2 . ASN A 1 688 ? 56.803 48.127 37.435 1.00 32.04 ? 741 ASN A ND2 1 ATOM 5523 N N . PRO A 1 689 ? 54.900 43.204 36.012 1.00 29.32 ? 742 PRO A N 1 ATOM 5524 C CA . PRO A 1 689 ? 55.683 42.328 35.135 1.00 27.78 ? 742 PRO A CA 1 ATOM 5525 C C . PRO A 1 689 ? 56.220 43.100 33.940 1.00 31.09 ? 742 PRO A C 1 ATOM 5526 O O . PRO A 1 689 ? 55.597 44.041 33.454 1.00 28.14 ? 742 PRO A O 1 ATOM 5527 C CB . PRO A 1 689 ? 54.667 41.270 34.687 1.00 29.35 ? 742 PRO A CB 1 ATOM 5528 C CG . PRO A 1 689 ? 53.336 41.933 34.850 1.00 27.77 ? 742 PRO A CG 1 ATOM 5529 C CD . PRO A 1 689 ? 53.484 42.805 36.072 1.00 29.47 ? 742 PRO A CD 1 ATOM 5530 N N . GLU A 1 690 ? 57.397 42.703 33.477 1.00 36.37 ? 743 GLU A N 1 ATOM 5531 C CA . GLU A 1 690 ? 58.009 43.333 32.326 1.00 35.58 ? 743 GLU A CA 1 ATOM 5532 C C . GLU A 1 690 ? 57.146 43.143 31.094 1.00 31.83 ? 743 GLU A C 1 ATOM 5533 O O . GLU A 1 690 ? 56.908 44.089 30.348 1.00 30.20 ? 743 GLU A O 1 ATOM 5534 C CB . GLU A 1 690 ? 59.391 42.734 32.086 1.00 41.66 ? 743 GLU A CB 1 ATOM 5535 C CG . GLU A 1 690 ? 60.501 43.757 32.147 1.00 48.00 ? 743 GLU A CG 1 ATOM 5536 C CD . GLU A 1 690 ? 60.802 44.347 30.789 1.00 53.58 ? 743 GLU A CD 1 ATOM 5537 O OE1 . GLU A 1 690 ? 60.700 43.597 29.790 1.00 58.09 ? 743 GLU A OE1 1 ATOM 5538 O OE2 . GLU A 1 690 ? 61.136 45.553 30.723 1.00 54.59 ? 743 GLU A OE2 1 ATOM 5539 N N . LYS A 1 691 ? 56.678 41.917 30.877 1.00 30.85 ? 744 LYS A N 1 ATOM 5540 C CA . LYS A 1 691 ? 55.795 41.646 29.757 1.00 31.24 ? 744 LYS A CA 1 ATOM 5541 C C . LYS A 1 691 ? 54.368 42.035 30.117 1.00 31.90 ? 744 LYS A C 1 ATOM 5542 O O . LYS A 1 691 ? 53.799 41.539 31.097 1.00 29.09 ? 744 LYS A O 1 ATOM 5543 C CB . LYS A 1 691 ? 55.830 40.177 29.352 1.00 32.63 ? 744 LYS A CB 1 ATOM 5544 C CG . LYS A 1 691 ? 54.785 39.835 28.283 1.00 37.00 ? 744 LYS A CG 1 ATOM 5545 C CD . LYS A 1 691 ? 55.009 38.458 27.656 1.00 40.02 ? 744 LYS A CD 1 ATOM 5546 C CE . LYS A 1 691 ? 54.892 38.499 26.131 1.00 41.43 ? 744 LYS A CE 1 ATOM 5547 N NZ . LYS A 1 691 ? 53.502 38.765 25.651 1.00 41.36 ? 744 LYS A NZ 1 ATOM 5548 N N . LYS A 1 692 ? 53.802 42.921 29.310 1.00 30.43 ? 745 LYS A N 1 ATOM 5549 C CA . LYS A 1 692 ? 52.463 43.415 29.536 1.00 33.07 ? 745 LYS A CA 1 ATOM 5550 C C . LYS A 1 692 ? 51.666 43.216 28.264 1.00 31.70 ? 745 LYS A C 1 ATOM 5551 O O . LYS A 1 692 ? 52.186 43.413 27.165 1.00 33.72 ? 745 LYS A O 1 ATOM 5552 C CB . LYS A 1 692 ? 52.507 44.890 29.937 1.00 32.61 ? 745 LYS A CB 1 ATOM 5553 C CG . LYS A 1 692 ? 53.187 45.126 31.278 1.00 31.25 ? 745 LYS A CG 1 ATOM 5554 C CD . LYS A 1 692 ? 52.907 46.526 31.815 1.00 32.02 ? 745 LYS A CD 1 ATOM 5555 C CE . LYS A 1 692 ? 53.851 46.888 32.944 1.00 32.88 ? 745 LYS A CE 1 ATOM 5556 N NZ . LYS A 1 692 ? 53.915 45.815 33.972 1.00 30.58 ? 745 LYS A NZ 1 ATOM 5557 N N . CYS A 1 693 ? 50.412 42.799 28.425 1.00 25.37 ? 746 CYS A N 1 ATOM 5558 C CA . CYS A 1 693 ? 49.497 42.610 27.308 1.00 22.90 ? 746 CYS A CA 1 ATOM 5559 C C . CYS A 1 693 ? 48.789 43.907 26.961 1.00 23.47 ? 746 CYS A C 1 ATOM 5560 O O . CYS A 1 693 ? 48.473 44.707 27.830 1.00 20.81 ? 746 CYS A O 1 ATOM 5561 C CB . CYS A 1 693 ? 48.447 41.551 27.659 1.00 23.85 ? 746 CYS A CB 1 ATOM 5562 S SG . CYS A 1 693 ? 49.116 39.975 28.236 1.00 25.60 ? 746 CYS A SG 1 ATOM 5563 N N . ARG A 1 694 ? 48.523 44.109 25.684 1.00 27.20 ? 747 ARG A N 1 ATOM 5564 C CA . ARG A 1 694 ? 47.767 45.266 25.251 1.00 26.08 ? 747 ARG A CA 1 ATOM 5565 C C . ARG A 1 694 ? 47.006 44.915 23.996 1.00 24.60 ? 747 ARG A C 1 ATOM 5566 O O . ARG A 1 694 ? 47.573 44.366 23.055 1.00 28.38 ? 747 ARG A O 1 ATOM 5567 C CB . ARG A 1 694 ? 48.713 46.433 24.979 1.00 31.06 ? 747 ARG A CB 1 ATOM 5568 C CG . ARG A 1 694 ? 48.027 47.640 24.365 1.00 33.40 ? 747 ARG A CG 1 ATOM 5569 C CD . ARG A 1 694 ? 47.943 48.824 25.297 1.00 33.65 ? 747 ARG A CD 1 ATOM 5570 N NE . ARG A 1 694 ? 46.929 49.797 24.888 1.00 33.70 ? 747 ARG A NE 1 ATOM 5571 C CZ . ARG A 1 694 ? 47.190 51.073 24.637 1.00 31.80 ? 747 ARG A CZ 1 ATOM 5572 N NH1 . ARG A 1 694 ? 48.434 51.523 24.735 1.00 32.46 ? 747 ARG A NH1 1 ATOM 5573 N NH2 . ARG A 1 694 ? 46.213 51.894 24.282 1.00 30.03 ? 747 ARG A NH2 1 ATOM 5574 N N . VAL A 1 695 ? 45.716 45.214 23.969 1.00 20.33 ? 748 VAL A N 1 ATOM 5575 C CA . VAL A 1 695 ? 45.001 45.209 22.704 1.00 22.05 ? 748 VAL A CA 1 ATOM 5576 C C . VAL A 1 695 ? 44.465 46.609 22.398 1.00 25.90 ? 748 VAL A C 1 ATOM 5577 O O . VAL A 1 695 ? 45.078 47.325 21.607 1.00 28.14 ? 748 VAL A O 1 ATOM 5578 C CB . VAL A 1 695 ? 43.939 44.082 22.668 1.00 24.44 ? 748 VAL A CB 1 ATOM 5579 C CG1 . VAL A 1 695 ? 43.407 43.820 24.068 1.00 30.69 ? 748 VAL A CG1 1 ATOM 5580 C CG2 . VAL A 1 695 ? 42.829 44.378 21.671 1.00 23.99 ? 748 VAL A CG2 1 ATOM 5581 N N . TRP A 1 696 ? 43.383 47.035 23.045 1.00 24.26 ? 749 TRP A N 1 ATOM 5582 C CA . TRP A 1 696 ? 42.961 48.435 22.956 1.00 24.65 ? 749 TRP A CA 1 ATOM 5583 C C . TRP A 1 696 ? 43.570 49.343 24.020 1.00 25.30 ? 749 TRP A C 1 ATOM 5584 O O . TRP A 1 696 ? 43.414 50.568 23.932 1.00 27.47 ? 749 TRP A O 1 ATOM 5585 C CB . TRP A 1 696 ? 41.430 48.544 22.982 1.00 21.64 ? 749 TRP A CB 1 ATOM 5586 C CG . TRP A 1 696 ? 40.813 47.725 21.944 1.00 21.95 ? 749 TRP A CG 1 ATOM 5587 C CD1 . TRP A 1 696 ? 40.217 46.515 22.109 1.00 20.35 ? 749 TRP A CD1 1 ATOM 5588 C CD2 . TRP A 1 696 ? 40.764 48.012 20.543 1.00 22.92 ? 749 TRP A CD2 1 ATOM 5589 N NE1 . TRP A 1 696 ? 39.783 46.036 20.898 1.00 20.94 ? 749 TRP A NE1 1 ATOM 5590 C CE2 . TRP A 1 696 ? 40.115 46.938 19.919 1.00 21.95 ? 749 TRP A CE2 1 ATOM 5591 C CE3 . TRP A 1 696 ? 41.215 49.078 19.749 1.00 26.08 ? 749 TRP A CE3 1 ATOM 5592 C CZ2 . TRP A 1 696 ? 39.885 46.898 18.541 1.00 24.34 ? 749 TRP A CZ2 1 ATOM 5593 C CZ3 . TRP A 1 696 ? 41.005 49.034 18.391 1.00 25.77 ? 749 TRP A CZ3 1 ATOM 5594 C CH2 . TRP A 1 696 ? 40.334 47.956 17.797 1.00 26.02 ? 749 TRP A CH2 1 ATOM 5595 O OXT . TRP A 1 696 ? 44.236 48.916 24.969 1.00 22.34 ? 749 TRP A OXT 1 HETATM 5596 C C1 . NAG B 2 . ? -2.529 35.845 52.029 1.00 37.72 ? 752 NAG A C1 1 HETATM 5597 C C2 . NAG B 2 . ? -3.150 37.053 52.719 1.00 39.97 ? 752 NAG A C2 1 HETATM 5598 C C3 . NAG B 2 . ? -4.368 36.626 53.537 1.00 42.11 ? 752 NAG A C3 1 HETATM 5599 C C4 . NAG B 2 . ? -5.338 35.870 52.646 1.00 43.56 ? 752 NAG A C4 1 HETATM 5600 C C5 . NAG B 2 . ? -4.595 34.770 51.894 1.00 43.15 ? 752 NAG A C5 1 HETATM 5601 C C6 . NAG B 2 . ? -5.522 34.054 50.926 1.00 42.75 ? 752 NAG A C6 1 HETATM 5602 C C7 . NAG B 2 . ? -1.803 38.943 53.452 1.00 41.26 ? 752 NAG A C7 1 HETATM 5603 C C8 . NAG B 2 . ? -1.205 39.561 54.679 1.00 40.65 ? 752 NAG A C8 1 HETATM 5604 N N2 . NAG B 2 . ? -2.169 37.671 53.575 1.00 38.74 ? 752 NAG A N2 1 HETATM 5605 O O3 . NAG B 2 . ? -5.027 37.743 54.086 1.00 41.15 ? 752 NAG A O3 1 HETATM 5606 O O4 . NAG B 2 . ? -6.376 35.322 53.433 1.00 45.21 ? 752 NAG A O4 1 HETATM 5607 O O5 . NAG B 2 . ? -3.521 35.330 51.174 1.00 40.22 ? 752 NAG A O5 1 HETATM 5608 O O6 . NAG B 2 . ? -6.545 33.439 51.674 1.00 45.50 ? 752 NAG A O6 1 HETATM 5609 O O7 . NAG B 2 . ? -1.924 39.596 52.413 1.00 41.71 ? 752 NAG A O7 1 HETATM 5610 C C1 . NAG C 2 . ? 2.458 18.046 13.543 1.00 43.03 ? 753 NAG A C1 1 HETATM 5611 C C2 . NAG C 2 . ? 1.053 18.585 13.274 1.00 44.79 ? 753 NAG A C2 1 HETATM 5612 C C3 . NAG C 2 . ? -0.038 17.770 13.958 1.00 46.53 ? 753 NAG A C3 1 HETATM 5613 C C4 . NAG C 2 . ? 0.200 16.290 13.723 1.00 47.53 ? 753 NAG A C4 1 HETATM 5614 C C5 . NAG C 2 . ? 1.631 15.957 14.119 1.00 46.25 ? 753 NAG A C5 1 HETATM 5615 C C6 . NAG C 2 . ? 1.913 14.468 14.006 1.00 45.99 ? 753 NAG A C6 1 HETATM 5616 C C7 . NAG C 2 . ? 1.154 20.955 12.877 1.00 43.19 ? 753 NAG A C7 1 HETATM 5617 C C8 . NAG C 2 . ? 1.274 22.321 13.487 1.00 42.07 ? 753 NAG A C8 1 HETATM 5618 N N2 . NAG C 2 . ? 0.979 19.953 13.724 1.00 42.11 ? 753 NAG A N2 1 HETATM 5619 O O3 . NAG C 2 . ? -1.310 18.127 13.456 1.00 46.57 ? 753 NAG A O3 1 HETATM 5620 O O4 . NAG C 2 . ? -0.721 15.539 14.481 1.00 49.83 ? 753 NAG A O4 1 HETATM 5621 O O5 . NAG C 2 . ? 2.497 16.672 13.268 1.00 45.68 ? 753 NAG A O5 1 HETATM 5622 O O6 . NAG C 2 . ? 0.861 13.780 14.640 1.00 47.58 ? 753 NAG A O6 1 HETATM 5623 O O7 . NAG C 2 . ? 1.215 20.792 11.657 1.00 46.11 ? 753 NAG A O7 1 HETATM 5624 C C1 . NAG D 2 . ? 50.855 30.227 31.080 1.00 41.63 ? 754 NAG A C1 1 HETATM 5625 C C2 . NAG D 2 . ? 50.045 29.474 30.038 1.00 42.65 ? 754 NAG A C2 1 HETATM 5626 C C3 . NAG D 2 . ? 50.983 28.761 29.077 1.00 44.62 ? 754 NAG A C3 1 HETATM 5627 C C4 . NAG D 2 . ? 51.924 29.792 28.475 1.00 44.25 ? 754 NAG A C4 1 HETATM 5628 C C5 . NAG D 2 . ? 52.612 30.595 29.573 1.00 45.77 ? 754 NAG A C5 1 HETATM 5629 C C6 . NAG D 2 . ? 53.481 31.694 28.974 1.00 45.99 ? 754 NAG A C6 1 HETATM 5630 C C7 . NAG D 2 . ? 47.822 28.712 30.533 1.00 42.01 ? 754 NAG A C7 1 HETATM 5631 C C8 . NAG D 2 . ? 46.952 27.585 30.992 1.00 40.39 ? 754 NAG A C8 1 HETATM 5632 N N2 . NAG D 2 . ? 49.131 28.540 30.659 1.00 42.77 ? 754 NAG A N2 1 HETATM 5633 O O3 . NAG D 2 . ? 50.253 28.120 28.056 1.00 42.33 ? 754 NAG A O3 1 HETATM 5634 O O4 . NAG D 2 . ? 52.889 29.128 27.700 1.00 48.39 ? 754 NAG A O4 1 HETATM 5635 O O5 . NAG D 2 . ? 51.647 31.186 30.416 1.00 43.52 ? 754 NAG A O5 1 HETATM 5636 O O6 . NAG D 2 . ? 52.798 32.258 27.880 1.00 46.42 ? 754 NAG A O6 1 HETATM 5637 O O7 . NAG D 2 . ? 47.327 29.736 30.065 1.00 42.49 ? 754 NAG A O7 1 HETATM 5638 ZN ZN . ZN E 3 . ? 31.799 42.960 30.117 1.00 20.38 ? 1001 ZN A ZN 1 HETATM 5639 C C3 . BIR F 4 . ? 27.859 41.356 29.945 1.00 25.00 ? 2001 BIR A C3 1 HETATM 5640 C C2 . BIR F 4 . ? 27.708 42.362 31.092 1.00 20.83 ? 2001 BIR A C2 1 HETATM 5641 N N1 . BIR F 4 . ? 26.400 42.999 31.015 1.00 20.66 ? 2001 BIR A N1 1 HETATM 5642 P P4 . BIR F 4 . ? 29.016 43.502 31.026 1.00 16.41 ? 2001 BIR A P4 1 HETATM 5643 O O6 . BIR F 4 . ? 30.230 42.650 31.223 1.00 15.58 ? 2001 BIR A O6 1 HETATM 5644 O O5 . BIR F 4 . ? 28.936 44.315 29.767 1.00 17.22 ? 2001 BIR A O5 1 HETATM 5645 C C7 . BIR F 4 . ? 28.861 44.556 32.394 1.00 14.85 ? 2001 BIR A C7 1 HETATM 5646 C C8 . BIR F 4 . ? 30.148 44.742 33.211 1.00 13.59 ? 2001 BIR A C8 1 HETATM 5647 C C10 . BIR F 4 . ? 30.375 43.578 34.141 1.00 16.00 ? 2001 BIR A C10 1 HETATM 5648 O O23 . BIR F 4 . ? 31.501 43.177 34.391 1.00 17.04 ? 2001 BIR A O23 1 HETATM 5649 N N24 . BIR F 4 . ? 29.310 42.986 34.665 1.00 17.47 ? 2001 BIR A N24 1 HETATM 5650 C C25 . BIR F 4 . ? 29.528 41.922 35.631 1.00 18.39 ? 2001 BIR A C25 1 HETATM 5651 C C26 . BIR F 4 . ? 29.447 42.472 37.053 1.00 19.69 ? 2001 BIR A C26 1 HETATM 5652 C C27 . BIR F 4 . ? 28.525 40.835 35.461 1.00 21.96 ? 2001 BIR A C27 1 HETATM 5653 O O28 . BIR F 4 . ? 27.600 40.977 34.658 1.00 18.40 ? 2001 BIR A O28 1 HETATM 5654 O O29 . BIR F 4 . ? 28.647 39.816 36.123 1.00 15.82 ? 2001 BIR A O29 1 HETATM 5655 C C9 . BIR F 4 . ? 30.052 46.051 34.009 1.00 12.30 ? 2001 BIR A C9 1 HETATM 5656 C C11 . BIR F 4 . ? 31.328 46.340 34.747 1.00 18.96 ? 2001 BIR A C11 1 HETATM 5657 C C12 . BIR F 4 . ? 31.318 46.489 36.132 1.00 16.68 ? 2001 BIR A C12 1 HETATM 5658 C C13 . BIR F 4 . ? 32.501 46.740 36.819 1.00 19.83 ? 2001 BIR A C13 1 HETATM 5659 C C14 . BIR F 4 . ? 33.717 46.841 36.131 1.00 20.16 ? 2001 BIR A C14 1 HETATM 5660 C C15 . BIR F 4 . ? 33.717 46.695 34.739 1.00 19.59 ? 2001 BIR A C15 1 HETATM 5661 C C16 . BIR F 4 . ? 32.533 46.448 34.054 1.00 15.55 ? 2001 BIR A C16 1 HETATM 5662 C C17 . BIR F 4 . ? 34.970 47.086 36.855 1.00 25.82 ? 2001 BIR A C17 1 HETATM 5663 C C18 . BIR F 4 . ? 36.121 46.348 36.552 1.00 25.78 ? 2001 BIR A C18 1 HETATM 5664 C C19 . BIR F 4 . ? 37.310 46.574 37.240 1.00 29.21 ? 2001 BIR A C19 1 HETATM 5665 C C20 . BIR F 4 . ? 37.365 47.544 38.238 1.00 28.44 ? 2001 BIR A C20 1 HETATM 5666 C C21 . BIR F 4 . ? 36.226 48.285 38.547 1.00 29.07 ? 2001 BIR A C21 1 HETATM 5667 C C22 . BIR F 4 . ? 35.037 48.056 37.862 1.00 29.62 ? 2001 BIR A C22 1 HETATM 5668 O O . HOH G 5 . ? 34.652 36.868 28.183 1.00 14.13 ? 2002 HOH A O 1 HETATM 5669 O O . HOH G 5 . ? 35.503 35.558 25.550 1.00 29.85 ? 2003 HOH A O 1 HETATM 5670 O O . HOH G 5 . ? 36.969 33.629 23.207 1.00 31.53 ? 2004 HOH A O 1 HETATM 5671 O O . HOH G 5 . ? 34.101 36.990 23.767 1.00 26.35 ? 2005 HOH A O 1 HETATM 5672 O O . HOH G 5 . ? 32.276 37.696 26.748 1.00 25.08 ? 2006 HOH A O 1 HETATM 5673 O O . HOH G 5 . ? 31.151 35.555 25.754 1.00 35.57 ? 2007 HOH A O 1 HETATM 5674 O O . HOH G 5 . ? 28.771 35.081 32.363 1.00 25.04 ? 2008 HOH A O 1 HETATM 5675 O O . HOH G 5 . ? 27.759 37.541 31.759 1.00 23.92 ? 2009 HOH A O 1 HETATM 5676 O O . HOH G 5 . ? 26.053 39.014 33.228 1.00 28.74 ? 2010 HOH A O 1 HETATM 5677 O O . HOH G 5 . ? 24.526 40.805 31.649 1.00 28.76 ? 2011 HOH A O 1 HETATM 5678 O O . HOH G 5 . ? 31.033 38.760 37.346 1.00 16.11 ? 2012 HOH A O 1 HETATM 5679 O O . HOH G 5 . ? 33.190 39.631 37.803 1.00 17.66 ? 2013 HOH A O 1 HETATM 5680 O O . HOH G 5 . ? 36.982 39.834 33.306 1.00 16.48 ? 2014 HOH A O 1 HETATM 5681 O O . HOH G 5 . ? 34.876 33.751 37.859 1.00 23.48 ? 2015 HOH A O 1 HETATM 5682 O O . HOH G 5 . ? 35.430 32.902 35.329 1.00 16.50 ? 2016 HOH A O 1 HETATM 5683 O O . HOH G 5 . ? 37.420 30.958 34.078 1.00 19.09 ? 2017 HOH A O 1 HETATM 5684 O O . HOH G 5 . ? 37.947 26.158 34.195 1.00 33.74 ? 2018 HOH A O 1 HETATM 5685 O O . HOH G 5 . ? 36.417 26.165 31.471 1.00 34.72 ? 2019 HOH A O 1 HETATM 5686 O O . HOH G 5 . ? 33.727 26.797 30.805 1.00 27.15 ? 2020 HOH A O 1 HETATM 5687 O O . HOH G 5 . ? 36.153 23.548 30.734 1.00 27.99 ? 2021 HOH A O 1 HETATM 5688 O O . HOH G 5 . ? 38.589 22.434 31.434 1.00 36.81 ? 2022 HOH A O 1 HETATM 5689 O O . HOH G 5 . ? 35.180 24.190 37.997 1.00 15.96 ? 2023 HOH A O 1 HETATM 5690 O O . HOH G 5 . ? 36.723 21.014 35.716 1.00 22.15 ? 2024 HOH A O 1 HETATM 5691 O O . HOH G 5 . ? 29.657 23.576 42.525 1.00 15.39 ? 2025 HOH A O 1 HETATM 5692 O O . HOH G 5 . ? 29.731 21.254 45.313 1.00 19.20 ? 2026 HOH A O 1 HETATM 5693 O O . HOH G 5 . ? 29.360 20.361 47.984 1.00 33.50 ? 2027 HOH A O 1 HETATM 5694 O O . HOH G 5 . ? 32.825 19.199 46.422 1.00 36.21 ? 2028 HOH A O 1 HETATM 5695 O O . HOH G 5 . ? 29.942 19.126 43.743 1.00 22.14 ? 2029 HOH A O 1 HETATM 5696 O O . HOH G 5 . ? 32.132 16.731 45.353 1.00 21.70 ? 2030 HOH A O 1 HETATM 5697 O O . HOH G 5 . ? 30.388 8.790 36.087 1.00 58.14 ? 2031 HOH A O 1 HETATM 5698 O O . HOH G 5 . ? 21.002 15.038 48.237 1.00 22.97 ? 2032 HOH A O 1 HETATM 5699 O O . HOH G 5 . ? 19.250 16.628 46.765 1.00 21.64 ? 2033 HOH A O 1 HETATM 5700 O O . HOH G 5 . ? 18.329 19.191 46.836 1.00 21.05 ? 2034 HOH A O 1 HETATM 5701 O O . HOH G 5 . ? 16.374 16.384 47.578 1.00 27.38 ? 2035 HOH A O 1 HETATM 5702 O O . HOH G 5 . ? 14.532 16.604 50.522 1.00 40.99 ? 2036 HOH A O 1 HETATM 5703 O O . HOH G 5 . ? 10.862 13.542 48.947 1.00 25.17 ? 2037 HOH A O 1 HETATM 5704 O O . HOH G 5 . ? 8.564 13.142 51.112 1.00 31.00 ? 2038 HOH A O 1 HETATM 5705 O O . HOH G 5 . ? 4.883 14.339 51.052 1.00 32.14 ? 2039 HOH A O 1 HETATM 5706 O O . HOH G 5 . ? 3.616 15.610 48.795 1.00 30.55 ? 2040 HOH A O 1 HETATM 5707 O O . HOH G 5 . ? 4.110 17.244 50.487 1.00 43.52 ? 2041 HOH A O 1 HETATM 5708 O O . HOH G 5 . ? 4.315 22.360 52.828 1.00 44.20 ? 2042 HOH A O 1 HETATM 5709 O O . HOH G 5 . ? -4.190 29.988 47.536 1.00 34.10 ? 2043 HOH A O 1 HETATM 5710 O O . HOH G 5 . ? 0.146 34.112 47.296 1.00 31.25 ? 2044 HOH A O 1 HETATM 5711 O O . HOH G 5 . ? -0.702 31.826 45.979 1.00 20.64 ? 2045 HOH A O 1 HETATM 5712 O O . HOH G 5 . ? 0.275 29.978 44.294 1.00 18.82 ? 2046 HOH A O 1 HETATM 5713 O O . HOH G 5 . ? 2.158 28.152 44.520 1.00 23.57 ? 2047 HOH A O 1 HETATM 5714 O O . HOH G 5 . ? 1.770 25.985 46.367 1.00 20.55 ? 2048 HOH A O 1 HETATM 5715 O O . HOH G 5 . ? 0.873 39.706 50.533 1.00 20.08 ? 2049 HOH A O 1 HETATM 5716 O O . HOH G 5 . ? 7.509 33.537 35.433 1.00 20.69 ? 2050 HOH A O 1 HETATM 5717 O O . HOH G 5 . ? 8.537 35.029 33.487 1.00 19.87 ? 2051 HOH A O 1 HETATM 5718 O O . HOH G 5 . ? 11.490 35.573 35.812 1.00 22.52 ? 2052 HOH A O 1 HETATM 5719 O O . HOH G 5 . ? 9.386 32.023 36.565 1.00 29.59 ? 2053 HOH A O 1 HETATM 5720 O O . HOH G 5 . ? 8.813 46.162 31.226 1.00 20.57 ? 2054 HOH A O 1 HETATM 5721 O O . HOH G 5 . ? 16.112 44.403 33.135 1.00 22.15 ? 2055 HOH A O 1 HETATM 5722 O O . HOH G 5 . ? 14.780 42.760 31.403 1.00 39.51 ? 2056 HOH A O 1 HETATM 5723 O O . HOH G 5 . ? 19.032 43.863 32.908 1.00 23.46 ? 2057 HOH A O 1 HETATM 5724 O O . HOH G 5 . ? 16.097 42.472 36.772 1.00 32.77 ? 2058 HOH A O 1 HETATM 5725 O O . HOH G 5 . ? 19.882 57.950 27.346 1.00 20.40 ? 2059 HOH A O 1 HETATM 5726 O O . HOH G 5 . ? 17.295 58.360 28.847 1.00 26.71 ? 2060 HOH A O 1 HETATM 5727 O O . HOH G 5 . ? 14.962 59.097 27.199 1.00 30.43 ? 2061 HOH A O 1 HETATM 5728 O O . HOH G 5 . ? 11.683 57.213 26.218 1.00 31.37 ? 2062 HOH A O 1 HETATM 5729 O O . HOH G 5 . ? 20.961 60.421 26.492 1.00 31.96 ? 2063 HOH A O 1 HETATM 5730 O O . HOH G 5 . ? 22.768 60.950 25.186 1.00 38.20 ? 2064 HOH A O 1 HETATM 5731 O O . HOH G 5 . ? 24.904 65.916 28.420 1.00 33.89 ? 2065 HOH A O 1 HETATM 5732 O O . HOH G 5 . ? 19.508 64.851 25.802 1.00 40.02 ? 2066 HOH A O 1 HETATM 5733 O O . HOH G 5 . ? 25.186 62.301 41.513 1.00 31.24 ? 2067 HOH A O 1 HETATM 5734 O O . HOH G 5 . ? 13.983 61.118 37.681 1.00 46.18 ? 2068 HOH A O 1 HETATM 5735 O O . HOH G 5 . ? 34.170 65.385 33.990 1.00 31.73 ? 2069 HOH A O 1 HETATM 5736 O O . HOH G 5 . ? 30.416 67.101 37.398 1.00 33.40 ? 2070 HOH A O 1 HETATM 5737 O O . HOH G 5 . ? 30.958 64.773 38.079 1.00 34.45 ? 2071 HOH A O 1 HETATM 5738 O O . HOH G 5 . ? 38.924 69.938 44.019 1.00 35.90 ? 2072 HOH A O 1 HETATM 5739 O O . HOH G 5 . ? 35.133 62.578 46.927 1.00 29.54 ? 2073 HOH A O 1 HETATM 5740 O O . HOH G 5 . ? 49.455 35.231 34.974 1.00 22.74 ? 2074 HOH A O 1 HETATM 5741 O O . HOH G 5 . ? 47.935 32.670 40.629 1.00 31.63 ? 2075 HOH A O 1 HETATM 5742 O O . HOH G 5 . ? 39.280 36.207 48.029 1.00 50.48 ? 2076 HOH A O 1 HETATM 5743 O O . HOH G 5 . ? 44.195 32.154 44.326 1.00 27.17 ? 2077 HOH A O 1 HETATM 5744 O O . HOH G 5 . ? 33.910 38.843 40.878 1.00 29.19 ? 2078 HOH A O 1 HETATM 5745 O O . HOH G 5 . ? 36.045 39.917 43.897 1.00 27.12 ? 2079 HOH A O 1 HETATM 5746 O O . HOH G 5 . ? 32.619 43.648 44.882 1.00 17.82 ? 2080 HOH A O 1 HETATM 5747 O O . HOH G 5 . ? 30.480 35.047 39.163 1.00 23.83 ? 2081 HOH A O 1 HETATM 5748 O O . HOH G 5 . ? 28.070 32.356 36.566 1.00 24.17 ? 2082 HOH A O 1 HETATM 5749 O O . HOH G 5 . ? 24.204 45.535 20.241 1.00 45.50 ? 2083 HOH A O 1 HETATM 5750 O O . HOH G 5 . ? 32.582 61.963 21.764 1.00 35.92 ? 2084 HOH A O 1 HETATM 5751 O O . HOH G 5 . ? 21.749 59.797 40.993 1.00 39.57 ? 2085 HOH A O 1 HETATM 5752 O O . HOH G 5 . ? 20.848 54.877 41.309 1.00 26.37 ? 2086 HOH A O 1 HETATM 5753 O O . HOH G 5 . ? 19.744 54.018 46.337 1.00 23.78 ? 2087 HOH A O 1 HETATM 5754 O O . HOH G 5 . ? 19.619 51.760 44.837 1.00 15.86 ? 2088 HOH A O 1 HETATM 5755 O O . HOH G 5 . ? 21.934 50.293 45.366 1.00 11.72 ? 2089 HOH A O 1 HETATM 5756 O O . HOH G 5 . ? 23.320 51.752 47.599 1.00 18.78 ? 2090 HOH A O 1 HETATM 5757 O O . HOH G 5 . ? 25.905 53.933 46.561 1.00 20.41 ? 2091 HOH A O 1 HETATM 5758 O O . HOH G 5 . ? 25.632 55.710 47.961 1.00 33.96 ? 2092 HOH A O 1 HETATM 5759 O O . HOH G 5 . ? 21.087 53.078 48.548 1.00 26.57 ? 2093 HOH A O 1 HETATM 5760 O O . HOH G 5 . ? 19.227 51.126 49.911 1.00 17.25 ? 2094 HOH A O 1 HETATM 5761 O O . HOH G 5 . ? 14.580 52.911 50.484 1.00 31.79 ? 2095 HOH A O 1 HETATM 5762 O O . HOH G 5 . ? 17.235 52.705 51.051 1.00 22.12 ? 2096 HOH A O 1 HETATM 5763 O O . HOH G 5 . ? 20.587 50.426 51.995 1.00 24.33 ? 2097 HOH A O 1 HETATM 5764 O O . HOH G 5 . ? 20.605 45.276 52.065 1.00 17.03 ? 2098 HOH A O 1 HETATM 5765 O O . HOH G 5 . ? 20.880 47.628 53.551 1.00 21.19 ? 2099 HOH A O 1 HETATM 5766 O O . HOH G 5 . ? 23.966 47.973 53.295 1.00 24.54 ? 2100 HOH A O 1 HETATM 5767 O O . HOH G 5 . ? 24.070 42.929 52.137 1.00 26.12 ? 2101 HOH A O 1 HETATM 5768 O O . HOH G 5 . ? 26.509 47.391 54.117 1.00 38.98 ? 2102 HOH A O 1 HETATM 5769 O O . HOH G 5 . ? 31.122 47.089 52.781 1.00 23.64 ? 2103 HOH A O 1 HETATM 5770 O O . HOH G 5 . ? 29.202 48.938 48.392 1.00 21.17 ? 2104 HOH A O 1 HETATM 5771 O O . HOH G 5 . ? 31.461 50.433 48.157 1.00 21.27 ? 2105 HOH A O 1 HETATM 5772 O O . HOH G 5 . ? 32.806 49.790 50.667 1.00 19.39 ? 2106 HOH A O 1 HETATM 5773 O O . HOH G 5 . ? 33.116 48.408 53.791 1.00 29.77 ? 2107 HOH A O 1 HETATM 5774 O O . HOH G 5 . ? 27.427 39.041 56.774 1.00 48.61 ? 2108 HOH A O 1 HETATM 5775 O O . HOH G 5 . ? 18.440 37.750 52.666 1.00 23.84 ? 2109 HOH A O 1 HETATM 5776 O O . HOH G 5 . ? 20.093 39.098 51.562 1.00 27.46 ? 2110 HOH A O 1 HETATM 5777 O O . HOH G 5 . ? 20.456 36.807 53.871 1.00 51.05 ? 2111 HOH A O 1 HETATM 5778 O O . HOH G 5 . ? 29.108 35.700 51.996 1.00 72.55 ? 2112 HOH A O 1 HETATM 5779 O O . HOH G 5 . ? 20.281 40.088 48.563 1.00 29.51 ? 2113 HOH A O 1 HETATM 5780 O O . HOH G 5 . ? 22.553 37.176 50.598 1.00 22.06 ? 2114 HOH A O 1 HETATM 5781 O O . HOH G 5 . ? 25.235 35.691 46.281 1.00 21.75 ? 2115 HOH A O 1 HETATM 5782 O O . HOH G 5 . ? 22.306 34.395 46.614 1.00 30.91 ? 2116 HOH A O 1 HETATM 5783 O O . HOH G 5 . ? 23.177 32.195 45.337 1.00 21.94 ? 2117 HOH A O 1 HETATM 5784 O O . HOH G 5 . ? 21.816 30.469 46.602 1.00 24.90 ? 2118 HOH A O 1 HETATM 5785 O O . HOH G 5 . ? 20.468 31.931 48.799 1.00 22.69 ? 2119 HOH A O 1 HETATM 5786 O O . HOH G 5 . ? 24.769 39.801 42.738 1.00 30.03 ? 2120 HOH A O 1 HETATM 5787 O O . HOH G 5 . ? 20.181 39.744 40.743 1.00 37.14 ? 2121 HOH A O 1 HETATM 5788 O O . HOH G 5 . ? 19.396 41.987 43.020 1.00 35.10 ? 2122 HOH A O 1 HETATM 5789 O O . HOH G 5 . ? 16.349 43.016 40.659 1.00 19.35 ? 2123 HOH A O 1 HETATM 5790 O O . HOH G 5 . ? 21.323 44.586 39.871 1.00 27.78 ? 2124 HOH A O 1 HETATM 5791 O O . HOH G 5 . ? 21.058 41.592 38.486 1.00 51.07 ? 2125 HOH A O 1 HETATM 5792 O O . HOH G 5 . ? 24.690 39.829 37.020 1.00 27.29 ? 2126 HOH A O 1 HETATM 5793 O O . HOH G 5 . ? 22.733 38.999 35.876 1.00 40.82 ? 2127 HOH A O 1 HETATM 5794 O O . HOH G 5 . ? 18.263 32.518 47.331 1.00 49.15 ? 2128 HOH A O 1 HETATM 5795 O O . HOH G 5 . ? 28.235 25.831 52.349 1.00 23.97 ? 2129 HOH A O 1 HETATM 5796 O O . HOH G 5 . ? 30.596 27.449 51.300 1.00 21.95 ? 2130 HOH A O 1 HETATM 5797 O O . HOH G 5 . ? 34.945 31.454 50.959 1.00 22.05 ? 2131 HOH A O 1 HETATM 5798 O O . HOH G 5 . ? 33.599 34.438 54.496 1.00 35.39 ? 2132 HOH A O 1 HETATM 5799 O O . HOH G 5 . ? 35.983 37.893 53.527 1.00 26.15 ? 2133 HOH A O 1 HETATM 5800 O O . HOH G 5 . ? 28.005 33.307 57.221 1.00 15.83 ? 2134 HOH A O 1 HETATM 5801 O O . HOH G 5 . ? 26.841 35.389 58.670 1.00 18.76 ? 2135 HOH A O 1 HETATM 5802 O O . HOH G 5 . ? 24.346 34.888 57.126 1.00 22.97 ? 2136 HOH A O 1 HETATM 5803 O O . HOH G 5 . ? 23.285 34.290 59.562 1.00 44.02 ? 2137 HOH A O 1 HETATM 5804 O O . HOH G 5 . ? 45.557 47.098 31.839 1.00 20.38 ? 2138 HOH A O 1 HETATM 5805 O O . HOH G 5 . ? 44.379 46.586 26.124 1.00 19.92 ? 2139 HOH A O 1 HETATM 5806 O O . HOH G 5 . ? 41.932 45.799 25.442 1.00 21.67 ? 2140 HOH A O 1 HETATM 5807 O O . HOH G 5 . ? 41.515 52.194 23.309 1.00 25.45 ? 2141 HOH A O 1 HETATM 5808 O O . HOH G 5 . ? 41.087 52.657 20.717 1.00 21.75 ? 2142 HOH A O 1 HETATM 5809 O O . HOH G 5 . ? 49.208 41.808 23.899 1.00 25.24 ? 2143 HOH A O 1 HETATM 5810 O O . HOH G 5 . ? 47.153 45.318 5.817 1.00 23.49 ? 2144 HOH A O 1 HETATM 5811 O O . HOH G 5 . ? 44.672 43.936 2.837 1.00 38.35 ? 2145 HOH A O 1 HETATM 5812 O O . HOH G 5 . ? 49.577 38.419 12.567 1.00 27.39 ? 2146 HOH A O 1 HETATM 5813 O O . HOH G 5 . ? 43.128 28.928 29.592 1.00 26.68 ? 2147 HOH A O 1 HETATM 5814 O O . HOH G 5 . ? 32.481 24.344 29.929 1.00 23.86 ? 2148 HOH A O 1 HETATM 5815 O O . HOH G 5 . ? 30.040 33.166 18.709 1.00 26.04 ? 2149 HOH A O 1 HETATM 5816 O O . HOH G 5 . ? 27.349 50.371 49.207 1.00 22.07 ? 2150 HOH A O 1 HETATM 5817 O O . HOH G 5 . ? 30.177 40.261 57.825 1.00 46.66 ? 2151 HOH A O 1 HETATM 5818 O O . HOH G 5 . ? 44.760 38.316 44.855 1.00 31.74 ? 2152 HOH A O 1 HETATM 5819 O O . HOH G 5 . ? 30.805 41.721 22.700 1.00 33.01 ? 2153 HOH A O 1 HETATM 5820 O O . HOH G 5 . ? 26.473 41.791 22.334 1.00 33.49 ? 2154 HOH A O 1 HETATM 5821 O O . HOH G 5 . ? 27.671 12.383 24.064 1.00 26.40 ? 2155 HOH A O 1 HETATM 5822 O O . HOH G 5 . ? 27.019 9.682 23.465 1.00 25.37 ? 2156 HOH A O 1 HETATM 5823 O O . HOH G 5 . ? 27.573 24.575 18.713 1.00 29.91 ? 2157 HOH A O 1 HETATM 5824 O O . HOH G 5 . ? 28.878 22.984 15.607 1.00 29.47 ? 2158 HOH A O 1 HETATM 5825 O O . HOH G 5 . ? 21.874 35.061 14.039 1.00 28.30 ? 2159 HOH A O 1 HETATM 5826 O O . HOH G 5 . ? 21.342 35.660 19.636 1.00 38.48 ? 2160 HOH A O 1 HETATM 5827 O O . HOH G 5 . ? 22.728 41.827 14.459 1.00 33.91 ? 2161 HOH A O 1 HETATM 5828 O O . HOH G 5 . ? 52.130 47.460 36.232 1.00 25.57 ? 2162 HOH A O 1 HETATM 5829 O O . HOH G 5 . ? 40.276 41.155 33.690 1.00 16.12 ? 2163 HOH A O 1 HETATM 5830 O O . HOH G 5 . ? 27.702 36.637 35.731 1.00 40.18 ? 2164 HOH A O 1 HETATM 5831 O O . HOH G 5 . ? 28.914 24.578 26.358 1.00 21.08 ? 2165 HOH A O 1 HETATM 5832 O O . HOH G 5 . ? 25.358 26.082 25.307 1.00 24.46 ? 2166 HOH A O 1 HETATM 5833 O O . HOH G 5 . ? 27.035 22.754 27.283 1.00 21.91 ? 2167 HOH A O 1 HETATM 5834 O O . HOH G 5 . ? 24.433 24.154 26.884 1.00 26.59 ? 2168 HOH A O 1 HETATM 5835 O O . HOH G 5 . ? 15.229 26.999 28.944 1.00 22.89 ? 2169 HOH A O 1 HETATM 5836 O O . HOH G 5 . ? 10.858 28.429 31.015 1.00 22.01 ? 2170 HOH A O 1 HETATM 5837 O O . HOH G 5 . ? 11.009 27.834 33.851 1.00 30.85 ? 2171 HOH A O 1 HETATM 5838 O O . HOH G 5 . ? 16.797 25.543 34.378 1.00 25.08 ? 2172 HOH A O 1 HETATM 5839 O O . HOH G 5 . ? 20.936 24.894 37.422 1.00 39.76 ? 2173 HOH A O 1 HETATM 5840 O O . HOH G 5 . ? 16.276 24.011 40.440 1.00 19.53 ? 2174 HOH A O 1 HETATM 5841 O O . HOH G 5 . ? 12.752 25.933 41.959 1.00 23.46 ? 2175 HOH A O 1 HETATM 5842 O O . HOH G 5 . ? 10.352 28.563 41.448 1.00 24.28 ? 2176 HOH A O 1 HETATM 5843 O O . HOH G 5 . ? 10.364 32.006 38.744 1.00 26.84 ? 2177 HOH A O 1 HETATM 5844 O O . HOH G 5 . ? 27.732 34.474 34.717 1.00 27.99 ? 2178 HOH A O 1 HETATM 5845 O O . HOH G 5 . ? 16.284 27.038 46.607 1.00 25.44 ? 2179 HOH A O 1 HETATM 5846 O O . HOH G 5 . ? 10.218 38.387 53.583 1.00 22.52 ? 2180 HOH A O 1 HETATM 5847 O O . HOH G 5 . ? 33.608 39.607 43.590 1.00 35.89 ? 2181 HOH A O 1 HETATM 5848 O O . HOH G 5 . ? 31.740 41.116 44.799 1.00 32.51 ? 2182 HOH A O 1 HETATM 5849 O O . HOH G 5 . ? 40.857 34.565 46.190 1.00 38.78 ? 2183 HOH A O 1 HETATM 5850 O O . HOH G 5 . ? 43.053 33.209 49.224 1.00 54.18 ? 2184 HOH A O 1 HETATM 5851 O O . HOH G 5 . ? 38.006 33.847 51.490 1.00 42.88 ? 2185 HOH A O 1 HETATM 5852 O O . HOH G 5 . ? 46.866 30.589 44.349 1.00 48.36 ? 2186 HOH A O 1 HETATM 5853 O O . HOH G 5 . ? 38.663 37.274 17.135 1.00 33.23 ? 2187 HOH A O 1 HETATM 5854 O O . HOH G 5 . ? 38.992 36.519 11.722 1.00 38.36 ? 2188 HOH A O 1 HETATM 5855 O O . HOH G 5 . ? 42.214 31.247 13.505 1.00 52.27 ? 2189 HOH A O 1 HETATM 5856 O O . HOH G 5 . ? 42.483 41.364 3.787 1.00 25.25 ? 2190 HOH A O 1 HETATM 5857 O O . HOH G 5 . ? 51.663 45.921 5.583 1.00 23.26 ? 2191 HOH A O 1 HETATM 5858 O O . HOH G 5 . ? 49.495 44.202 5.706 1.00 26.97 ? 2192 HOH A O 1 HETATM 5859 O O . HOH G 5 . ? 49.206 41.277 5.125 1.00 30.70 ? 2193 HOH A O 1 HETATM 5860 O O . HOH G 5 . ? 49.920 39.780 2.858 1.00 22.01 ? 2194 HOH A O 1 HETATM 5861 O O . HOH G 5 . ? 45.999 41.798 4.751 1.00 38.59 ? 2195 HOH A O 1 HETATM 5862 O O . HOH G 5 . ? 44.963 50.148 4.951 1.00 33.53 ? 2196 HOH A O 1 HETATM 5863 O O . HOH G 5 . ? 26.735 38.067 36.448 1.00 43.29 ? 2197 HOH A O 1 HETATM 5864 O O . HOH G 5 . ? 23.220 32.820 41.963 1.00 3.03 ? 2198 HOH A O 1 HETATM 5865 O O . HOH G 5 . ? 14.053 47.781 36.246 1.00 20.99 ? 2199 HOH A O 1 HETATM 5866 O O . HOH G 5 . ? 5.339 59.088 36.232 1.00 46.95 ? 2200 HOH A O 1 HETATM 5867 O O . HOH G 5 . ? 19.237 29.886 43.125 1.00 31.50 ? 2201 HOH A O 1 HETATM 5868 O O . HOH G 5 . ? 7.296 33.240 47.254 1.00 28.17 ? 2202 HOH A O 1 HETATM 5869 O O . HOH G 5 . ? 10.603 33.206 45.216 1.00 30.19 ? 2203 HOH A O 1 HETATM 5870 O O . HOH G 5 . ? 24.866 19.441 48.825 1.00 18.03 ? 2204 HOH A O 1 HETATM 5871 O O . HOH G 5 . ? 32.394 39.035 24.547 1.00 29.96 ? 2205 HOH A O 1 HETATM 5872 O O . HOH G 5 . ? 29.139 41.465 25.568 1.00 45.25 ? 2206 HOH A O 1 HETATM 5873 O O . HOH G 5 . ? 28.302 43.180 27.196 1.00 32.20 ? 2207 HOH A O 1 HETATM 5874 O O . HOH G 5 . ? 26.013 43.308 28.115 1.00 27.01 ? 2208 HOH A O 1 HETATM 5875 O O . HOH G 5 . ? 27.660 37.826 28.930 1.00 31.22 ? 2209 HOH A O 1 HETATM 5876 O O . HOH G 5 . ? 27.238 36.640 19.096 1.00 32.59 ? 2210 HOH A O 1 HETATM 5877 O O . HOH G 5 . ? 26.843 34.214 15.339 1.00 27.48 ? 2211 HOH A O 1 HETATM 5878 O O . HOH G 5 . ? 23.209 41.551 20.488 1.00 31.91 ? 2212 HOH A O 1 HETATM 5879 O O . HOH G 5 . ? 21.158 36.008 17.441 1.00 30.19 ? 2213 HOH A O 1 HETATM 5880 O O . HOH G 5 . ? 13.211 45.114 19.364 1.00 36.41 ? 2214 HOH A O 1 HETATM 5881 O O . HOH G 5 . ? 7.696 40.668 7.599 1.00 39.20 ? 2215 HOH A O 1 HETATM 5882 O O . HOH G 5 . ? 12.996 31.856 10.456 1.00 28.58 ? 2216 HOH A O 1 HETATM 5883 O O . HOH G 5 . ? 25.644 31.521 6.795 1.00 35.81 ? 2217 HOH A O 1 HETATM 5884 O O . HOH G 5 . ? 34.204 42.373 11.491 1.00 22.87 ? 2218 HOH A O 1 HETATM 5885 O O . HOH G 5 . ? 43.091 51.410 26.564 1.00 30.77 ? 2219 HOH A O 1 HETATM 5886 O O . HOH G 5 . ? 55.396 45.184 27.733 1.00 32.36 ? 2220 HOH A O 1 HETATM 5887 O O . HOH G 5 . ? 34.900 24.368 28.222 1.00 33.28 ? 2221 HOH A O 1 HETATM 5888 O O . HOH G 5 . ? 38.164 23.364 28.157 1.00 36.10 ? 2222 HOH A O 1 HETATM 5889 O O . HOH G 5 . ? 36.372 19.882 33.170 1.00 24.52 ? 2223 HOH A O 1 HETATM 5890 O O . HOH G 5 . ? 39.107 24.004 33.087 1.00 38.23 ? 2224 HOH A O 1 HETATM 5891 O O . HOH G 5 . ? 40.469 22.664 35.872 1.00 36.11 ? 2225 HOH A O 1 HETATM 5892 O O . HOH G 5 . ? 42.953 24.015 36.041 1.00 25.62 ? 2226 HOH A O 1 HETATM 5893 O O . HOH G 5 . ? 50.254 37.513 35.465 1.00 30.57 ? 2227 HOH A O 1 HETATM 5894 O O . HOH G 5 . ? 54.008 39.433 37.730 1.00 31.65 ? 2228 HOH A O 1 HETATM 5895 O O . HOH G 5 . ? 51.256 40.669 31.991 1.00 26.98 ? 2229 HOH A O 1 HETATM 5896 O O . HOH G 5 . ? 58.209 47.569 44.521 1.00 27.51 ? 2230 HOH A O 1 HETATM 5897 O O . HOH G 5 . ? 38.520 63.903 29.867 1.00 23.63 ? 2231 HOH A O 1 HETATM 5898 O O . HOH G 5 . ? 15.446 56.607 25.241 1.00 31.89 ? 2232 HOH A O 1 HETATM 5899 O O . HOH G 5 . ? 12.858 49.930 26.152 1.00 35.14 ? 2233 HOH A O 1 HETATM 5900 O O . HOH G 5 . ? 13.541 35.123 8.450 1.00 35.53 ? 2234 HOH A O 1 HETATM 5901 O O . HOH G 5 . ? 3.494 23.929 21.010 1.00 31.22 ? 2235 HOH A O 1 HETATM 5902 O O . HOH G 5 . ? 2.821 21.088 20.974 1.00 29.06 ? 2236 HOH A O 1 HETATM 5903 O O . HOH G 5 . ? -8.195 32.145 43.882 1.00 43.81 ? 2237 HOH A O 1 HETATM 5904 O O . HOH G 5 . ? 10.307 29.849 35.919 1.00 41.90 ? 2238 HOH A O 1 HETATM 5905 O O . HOH G 5 . ? 18.884 42.302 36.942 1.00 41.96 ? 2239 HOH A O 1 HETATM 5906 O O . HOH G 5 . ? 20.099 42.185 34.321 1.00 27.45 ? 2240 HOH A O 1 HETATM 5907 O O . HOH G 5 . ? 14.956 44.279 35.622 1.00 31.13 ? 2241 HOH A O 1 HETATM 5908 O O . HOH G 5 . ? 25.178 28.026 33.554 1.00 31.32 ? 2242 HOH A O 1 HETATM 5909 O O . HOH G 5 . ? 17.644 19.831 27.395 1.00 31.36 ? 2243 HOH A O 1 HETATM 5910 O O . HOH G 5 . ? 17.334 22.383 28.564 1.00 25.18 ? 2244 HOH A O 1 HETATM 5911 O O . HOH G 5 . ? 18.882 19.648 29.456 1.00 26.73 ? 2245 HOH A O 1 HETATM 5912 O O . HOH G 5 . ? 13.914 8.135 20.824 1.00 34.08 ? 2246 HOH A O 1 HETATM 5913 O O . HOH G 5 . ? 30.744 49.566 9.810 1.00 34.86 ? 2247 HOH A O 1 HETATM 5914 O O . HOH G 5 . ? 36.494 24.598 45.772 1.00 23.62 ? 2248 HOH A O 1 HETATM 5915 O O . HOH G 5 . ? 32.315 21.619 44.684 1.00 26.38 ? 2249 HOH A O 1 HETATM 5916 O O . HOH G 5 . ? 15.989 11.826 47.853 1.00 38.24 ? 2250 HOH A O 1 HETATM 5917 O O . HOH G 5 . ? 27.548 39.518 38.387 1.00 24.19 ? 2251 HOH A O 1 HETATM 5918 O O . HOH G 5 . ? 13.436 50.548 33.290 1.00 25.41 ? 2252 HOH A O 1 HETATM 5919 O O . HOH G 5 . ? 15.000 50.588 30.847 1.00 24.39 ? 2253 HOH A O 1 HETATM 5920 O O . HOH G 5 . ? 11.568 51.557 26.396 1.00 38.17 ? 2254 HOH A O 1 HETATM 5921 O O . HOH G 5 . ? 25.380 59.342 19.626 1.00 44.31 ? 2255 HOH A O 1 HETATM 5922 O O . HOH G 5 . ? 28.281 60.163 22.990 1.00 35.36 ? 2256 HOH A O 1 HETATM 5923 O O . HOH G 5 . ? 32.320 65.164 40.286 1.00 29.36 ? 2257 HOH A O 1 HETATM 5924 O O . HOH G 5 . ? 38.799 72.427 40.400 1.00 34.97 ? 2258 HOH A O 1 HETATM 5925 O O . HOH G 5 . ? 33.090 67.714 37.082 1.00 36.08 ? 2259 HOH A O 1 HETATM 5926 O O . HOH G 5 . ? 45.450 73.983 34.517 1.00 43.98 ? 2260 HOH A O 1 HETATM 5927 O O . HOH G 5 . ? 53.073 57.548 47.115 1.00 37.79 ? 2261 HOH A O 1 HETATM 5928 O O . HOH G 5 . ? 52.281 54.344 48.356 1.00 36.77 ? 2262 HOH A O 1 HETATM 5929 O O . HOH G 5 . ? 43.984 62.088 49.248 1.00 30.74 ? 2263 HOH A O 1 HETATM 5930 O O . HOH G 5 . ? 58.248 50.625 47.273 1.00 44.14 ? 2264 HOH A O 1 HETATM 5931 O O . HOH G 5 . ? 14.883 43.821 5.846 1.00 41.55 ? 2265 HOH A O 1 HETATM 5932 O O . HOH G 5 . ? 16.632 24.867 0.136 1.00 31.71 ? 2266 HOH A O 1 HETATM 5933 O O . HOH G 5 . ? 23.150 14.384 10.977 1.00 34.98 ? 2267 HOH A O 1 HETATM 5934 O O . HOH G 5 . ? 26.694 11.235 19.335 1.00 27.72 ? 2268 HOH A O 1 HETATM 5935 O O . HOH G 5 . ? 28.837 14.026 29.914 1.00 21.35 ? 2269 HOH A O 1 HETATM 5936 O O . HOH G 5 . ? 31.341 12.206 23.517 1.00 42.36 ? 2270 HOH A O 1 HETATM 5937 O O . HOH G 5 . ? 32.575 9.720 22.606 1.00 45.44 ? 2271 HOH A O 1 HETATM 5938 O O . HOH G 5 . ? 33.668 35.952 38.371 1.00 29.31 ? 2272 HOH A O 1 HETATM 5939 O O . HOH G 5 . ? 26.163 36.783 42.465 1.00 36.04 ? 2273 HOH A O 1 HETATM 5940 O O . HOH G 5 . ? 24.372 28.066 38.434 1.00 24.05 ? 2274 HOH A O 1 HETATM 5941 O O . HOH G 5 . ? 35.488 11.104 42.437 1.00 26.06 ? 2275 HOH A O 1 HETATM 5942 O O . HOH G 5 . ? 23.885 19.113 51.671 1.00 28.02 ? 2276 HOH A O 1 HETATM 5943 O O . HOH G 5 . ? 2.262 35.053 55.084 1.00 50.02 ? 2277 HOH A O 1 HETATM 5944 O O . HOH G 5 . ? -3.960 51.608 43.982 1.00 25.52 ? 2278 HOH A O 1 HETATM 5945 O O . HOH G 5 . ? 5.068 56.582 39.677 1.00 45.91 ? 2279 HOH A O 1 HETATM 5946 O O . HOH G 5 . ? -2.507 58.622 34.197 1.00 36.46 ? 2280 HOH A O 1 HETATM 5947 O O . HOH G 5 . ? 7.961 5.089 26.507 1.00 30.22 ? 2281 HOH A O 1 HETATM 5948 O O . HOH G 5 . ? 13.080 29.449 51.143 1.00 46.56 ? 2282 HOH A O 1 HETATM 5949 O O . HOH G 5 . ? 19.422 32.205 56.882 1.00 34.01 ? 2283 HOH A O 1 HETATM 5950 O O . HOH G 5 . ? 18.763 25.769 38.462 1.00 40.36 ? 2284 HOH A O 1 HETATM 5951 O O . HOH G 5 . ? 22.910 39.839 44.417 1.00 35.49 ? 2285 HOH A O 1 HETATM 5952 O O . HOH G 5 . ? 18.653 44.210 40.365 1.00 42.52 ? 2286 HOH A O 1 HETATM 5953 O O . HOH G 5 . ? 5.356 51.316 48.236 1.00 28.21 ? 2287 HOH A O 1 HETATM 5954 O O . HOH G 5 . ? 4.987 52.916 45.624 1.00 25.50 ? 2288 HOH A O 1 HETATM 5955 O O . HOH G 5 . ? 7.345 51.908 51.926 1.00 25.80 ? 2289 HOH A O 1 HETATM 5956 O O . HOH G 5 . ? 20.382 64.440 35.988 1.00 66.34 ? 2290 HOH A O 1 HETATM 5957 O O . HOH G 5 . ? 44.759 50.153 57.229 1.00 33.42 ? 2291 HOH A O 1 HETATM 5958 O O . HOH G 5 . ? 40.988 38.292 55.908 1.00 35.60 ? 2292 HOH A O 1 HETATM 5959 O O . HOH G 5 . ? 37.562 37.842 45.311 1.00 30.46 ? 2293 HOH A O 1 HETATM 5960 O O . HOH G 5 . ? 41.814 36.129 28.817 1.00 27.30 ? 2294 HOH A O 1 HETATM 5961 O O . HOH G 5 . ? 34.807 30.865 32.083 1.00 25.80 ? 2295 HOH A O 1 HETATM 5962 O O . HOH G 5 . ? 30.781 29.794 55.105 1.00 78.47 ? 2296 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 GLY 1 54 54 GLY GLY A . n A 1 2 ILE 2 55 55 ILE ILE A . n A 1 3 CYS 3 56 56 CYS CYS A . n A 1 4 LYS 4 57 57 LYS LYS A . n A 1 5 SER 5 58 58 SER SER A . n A 1 6 SER 6 59 59 SER SER A . n A 1 7 ASP 7 60 60 ASP ASP A . n A 1 8 CYS 8 61 61 CYS CYS A . n A 1 9 ILE 9 62 62 ILE ILE A . n A 1 10 LYS 10 63 63 LYS LYS A . n A 1 11 SER 11 64 64 SER SER A . n A 1 12 ALA 12 65 65 ALA ALA A . n A 1 13 ALA 13 66 66 ALA ALA A . n A 1 14 ARG 14 67 67 ARG ARG A . n A 1 15 LEU 15 68 68 LEU LEU A . n A 1 16 ILE 16 69 69 ILE ILE A . n A 1 17 GLN 17 70 70 GLN GLN A . n A 1 18 ASN 18 71 71 ASN ASN A . n A 1 19 MET 19 72 72 MET MET A . n A 1 20 ASP 20 73 73 ASP ASP A . n A 1 21 ALA 21 74 74 ALA ALA A . n A 1 22 THR 22 75 75 THR THR A . n A 1 23 THR 23 76 76 THR THR A . n A 1 24 GLU 24 77 77 GLU GLU A . n A 1 25 PRO 25 78 78 PRO PRO A . n A 1 26 CYS 26 79 79 CYS CYS A . n A 1 27 THR 27 80 80 THR THR A . n A 1 28 ASP 28 81 81 ASP ASP A . n A 1 29 PHE 29 82 82 PHE PHE A . n A 1 30 PHE 30 83 83 PHE PHE A . n A 1 31 LYS 31 84 84 LYS LYS A . n A 1 32 TYR 32 85 85 TYR TYR A . n A 1 33 ALA 33 86 86 ALA ALA A . n A 1 34 CYS 34 87 87 CYS CYS A . n A 1 35 GLY 35 88 88 GLY GLY A . n A 1 36 GLY 36 89 89 GLY GLY A . n A 1 37 TRP 37 90 90 TRP TRP A . n A 1 38 LEU 38 91 91 LEU LEU A . n A 1 39 LYS 39 92 92 LYS LYS A . n A 1 40 ARG 40 93 93 ARG ARG A . n A 1 41 ASN 41 94 94 ASN ASN A . n A 1 42 VAL 42 95 95 VAL VAL A . n A 1 43 ILE 43 96 96 ILE ILE A . n A 1 44 PRO 44 97 97 PRO PRO A . n A 1 45 GLU 45 98 98 GLU GLU A . n A 1 46 THR 46 99 99 THR THR A . n A 1 47 SER 47 100 100 SER SER A . n A 1 48 SER 48 101 101 SER SER A . n A 1 49 ARG 49 102 102 ARG ARG A . n A 1 50 TYR 50 103 103 TYR TYR A . n A 1 51 GLY 51 104 104 GLY GLY A . n A 1 52 ASN 52 105 105 ASN ASN A . n A 1 53 PHE 53 106 106 PHE PHE A . n A 1 54 ASP 54 107 107 ASP ASP A . n A 1 55 ILE 55 108 108 ILE ILE A . n A 1 56 LEU 56 109 109 LEU LEU A . n A 1 57 ARG 57 110 110 ARG ARG A . n A 1 58 ASP 58 111 111 ASP ASP A . n A 1 59 GLU 59 112 112 GLU GLU A . n A 1 60 LEU 60 113 113 LEU LEU A . n A 1 61 GLU 61 114 114 GLU GLU A . n A 1 62 VAL 62 115 115 VAL VAL A . n A 1 63 VAL 63 116 116 VAL VAL A . n A 1 64 LEU 64 117 117 LEU LEU A . n A 1 65 LYS 65 118 118 LYS LYS A . n A 1 66 ASP 66 119 119 ASP ASP A . n A 1 67 VAL 67 120 120 VAL VAL A . n A 1 68 LEU 68 121 121 LEU LEU A . n A 1 69 GLN 69 122 122 GLN GLN A . n A 1 70 GLU 70 123 123 GLU GLU A . n A 1 71 PRO 71 124 124 PRO PRO A . n A 1 72 LYS 72 125 125 LYS LYS A . n A 1 73 THR 73 126 126 THR THR A . n A 1 74 GLU 74 127 127 GLU GLU A . n A 1 75 ASP 75 128 128 ASP ASP A . n A 1 76 ILE 76 129 129 ILE ILE A . n A 1 77 VAL 77 130 130 VAL VAL A . n A 1 78 ALA 78 131 131 ALA ALA A . n A 1 79 VAL 79 132 132 VAL VAL A . n A 1 80 GLN 80 133 133 GLN GLN A . n A 1 81 LYS 81 134 134 LYS LYS A . n A 1 82 ALA 82 135 135 ALA ALA A . n A 1 83 LYS 83 136 136 LYS LYS A . n A 1 84 ALA 84 137 137 ALA ALA A . n A 1 85 LEU 85 138 138 LEU LEU A . n A 1 86 TYR 86 139 139 TYR TYR A . n A 1 87 ARG 87 140 140 ARG ARG A . n A 1 88 SER 88 141 141 SER SER A . n A 1 89 CYS 89 142 142 CYS CYS A . n A 1 90 ILE 90 143 143 ILE ILE A . n A 1 91 ASN 91 144 144 ASN ASN A . n A 1 92 GLU 92 145 145 GLU GLU A . n A 1 93 SER 93 146 146 SER SER A . n A 1 94 ALA 94 147 147 ALA ALA A . n A 1 95 ILE 95 148 148 ILE ILE A . n A 1 96 ASP 96 149 149 ASP ASP A . n A 1 97 SER 97 150 150 SER SER A . n A 1 98 ARG 98 151 151 ARG ARG A . n A 1 99 GLY 99 152 152 GLY GLY A . n A 1 100 GLY 100 153 153 GLY GLY A . n A 1 101 GLU 101 154 154 GLU GLU A . n A 1 102 PRO 102 155 155 PRO PRO A . n A 1 103 LEU 103 156 156 LEU LEU A . n A 1 104 LEU 104 157 157 LEU LEU A . n A 1 105 LYS 105 158 158 LYS LYS A . n A 1 106 LEU 106 159 159 LEU LEU A . n A 1 107 LEU 107 160 160 LEU LEU A . n A 1 108 PRO 108 161 161 PRO PRO A . n A 1 109 ASP 109 162 162 ASP ASP A . n A 1 110 ILE 110 163 163 ILE ILE A . n A 1 111 TYR 111 164 164 TYR TYR A . n A 1 112 GLY 112 165 165 GLY GLY A . n A 1 113 TRP 113 166 166 TRP TRP A . n A 1 114 PRO 114 167 167 PRO PRO A . n A 1 115 VAL 115 168 168 VAL VAL A . n A 1 116 ALA 116 169 169 ALA ALA A . n A 1 117 THR 117 170 170 THR THR A . n A 1 118 GLU 118 171 171 GLU GLU A . n A 1 119 ASN 119 172 172 ASN ASN A . n A 1 120 TRP 120 173 173 TRP TRP A . n A 1 121 GLU 121 174 174 GLU GLU A . n A 1 122 GLN 122 175 175 GLN GLN A . n A 1 123 LYS 123 176 176 LYS LYS A . n A 1 124 TYR 124 177 177 TYR TYR A . n A 1 125 GLY 125 178 178 GLY GLY A . n A 1 126 ALA 126 179 179 ALA ALA A . n A 1 127 SER 127 180 180 SER SER A . n A 1 128 TRP 128 181 181 TRP TRP A . n A 1 129 THR 129 182 182 THR THR A . n A 1 130 ALA 130 183 183 ALA ALA A . n A 1 131 GLU 131 184 184 GLU GLU A . n A 1 132 LYS 132 185 185 LYS LYS A . n A 1 133 ALA 133 186 186 ALA ALA A . n A 1 134 ILE 134 187 187 ILE ILE A . n A 1 135 ALA 135 188 188 ALA ALA A . n A 1 136 GLN 136 189 189 GLN GLN A . n A 1 137 LEU 137 190 190 LEU LEU A . n A 1 138 ASN 138 191 191 ASN ASN A . n A 1 139 SER 139 192 192 SER SER A . n A 1 140 LYS 140 193 193 LYS LYS A . n A 1 141 TYR 141 194 194 TYR TYR A . n A 1 142 GLY 142 195 195 GLY GLY A . n A 1 143 LYS 143 196 196 LYS LYS A . n A 1 144 LYS 144 197 197 LYS LYS A . n A 1 145 VAL 145 198 198 VAL VAL A . n A 1 146 LEU 146 199 199 LEU LEU A . n A 1 147 ILE 147 200 200 ILE ILE A . n A 1 148 ASN 148 201 201 ASN ASN A . n A 1 149 LEU 149 202 202 LEU LEU A . n A 1 150 PHE 150 203 203 PHE PHE A . n A 1 151 VAL 151 204 204 VAL VAL A . n A 1 152 GLY 152 205 205 GLY GLY A . n A 1 153 THR 153 206 206 THR THR A . n A 1 154 ASP 154 207 207 ASP ASP A . n A 1 155 ASP 155 208 208 ASP ASP A . n A 1 156 LYS 156 209 209 LYS LYS A . n A 1 157 ASN 157 210 210 ASN ASN A . n A 1 158 SER 158 211 211 SER SER A . n A 1 159 VAL 159 212 212 VAL VAL A . n A 1 160 ASN 160 213 213 ASN ASN A . n A 1 161 HIS 161 214 214 HIS HIS A . n A 1 162 VAL 162 215 215 VAL VAL A . n A 1 163 ILE 163 216 216 ILE ILE A . n A 1 164 HIS 164 217 217 HIS HIS A . n A 1 165 ILE 165 218 218 ILE ILE A . n A 1 166 ASP 166 219 219 ASP ASP A . n A 1 167 GLN 167 220 220 GLN GLN A . n A 1 168 PRO 168 221 221 PRO PRO A . n A 1 169 ARG 169 222 222 ARG ARG A . n A 1 170 LEU 170 223 223 LEU LEU A . n A 1 171 GLY 171 224 224 GLY GLY A . n A 1 172 LEU 172 225 225 LEU LEU A . n A 1 173 PRO 173 226 226 PRO PRO A . n A 1 174 SER 174 227 227 SER SER A . n A 1 175 ARG 175 228 228 ARG ARG A . n A 1 176 ASP 176 229 229 ASP ASP A . n A 1 177 TYR 177 230 230 TYR TYR A . n A 1 178 TYR 178 231 231 TYR TYR A . n A 1 179 GLU 179 232 232 GLU GLU A . n A 1 180 CYS 180 233 233 CYS CYS A . n A 1 181 THR 181 234 234 THR THR A . n A 1 182 GLY 182 235 235 GLY GLY A . n A 1 183 ILE 183 236 236 ILE ILE A . n A 1 184 TYR 184 237 237 TYR TYR A . n A 1 185 LYS 185 238 238 LYS LYS A . n A 1 186 GLU 186 239 239 GLU GLU A . n A 1 187 ALA 187 240 240 ALA ALA A . n A 1 188 CYS 188 241 241 CYS CYS A . n A 1 189 THR 189 242 242 THR THR A . n A 1 190 ALA 190 243 243 ALA ALA A . n A 1 191 TYR 191 244 244 TYR TYR A . n A 1 192 VAL 192 245 245 VAL VAL A . n A 1 193 ASP 193 246 246 ASP ASP A . n A 1 194 PHE 194 247 247 PHE PHE A . n A 1 195 MET 195 248 248 MET MET A . n A 1 196 ILE 196 249 249 ILE ILE A . n A 1 197 SER 197 250 250 SER SER A . n A 1 198 VAL 198 251 251 VAL VAL A . n A 1 199 ALA 199 252 252 ALA ALA A . n A 1 200 ARG 200 253 253 ARG ARG A . n A 1 201 LEU 201 254 254 LEU LEU A . n A 1 202 ILE 202 255 255 ILE ILE A . n A 1 203 ARG 203 256 256 ARG ARG A . n A 1 204 GLN 204 257 257 GLN GLN A . n A 1 205 GLU 205 258 258 GLU GLU A . n A 1 206 GLU 206 259 259 GLU GLU A . n A 1 207 ARG 207 260 260 ARG ARG A . n A 1 208 LEU 208 261 261 LEU LEU A . n A 1 209 PRO 209 262 262 PRO PRO A . n A 1 210 ILE 210 263 263 ILE ILE A . n A 1 211 ASP 211 264 264 ASP ASP A . n A 1 212 GLU 212 265 265 GLU GLU A . n A 1 213 ASN 213 266 266 ASN ASN A . n A 1 214 GLN 214 267 267 GLN GLN A . n A 1 215 LEU 215 268 268 LEU LEU A . n A 1 216 ALA 216 269 269 ALA ALA A . n A 1 217 LEU 217 270 270 LEU LEU A . n A 1 218 GLU 218 271 271 GLU GLU A . n A 1 219 MET 219 272 272 MET MET A . n A 1 220 ASN 220 273 273 ASN ASN A . n A 1 221 LYS 221 274 274 LYS LYS A . n A 1 222 VAL 222 275 275 VAL VAL A . n A 1 223 MET 223 276 276 MET MET A . n A 1 224 GLU 224 277 277 GLU GLU A . n A 1 225 LEU 225 278 278 LEU LEU A . n A 1 226 GLU 226 279 279 GLU GLU A . n A 1 227 LYS 227 280 280 LYS LYS A . n A 1 228 GLU 228 281 281 GLU GLU A . n A 1 229 ILE 229 282 282 ILE ILE A . n A 1 230 ALA 230 283 283 ALA ALA A . n A 1 231 ASN 231 284 284 ASN ASN A . n A 1 232 ALA 232 285 285 ALA ALA A . n A 1 233 THR 233 286 286 THR THR A . n A 1 234 ALA 234 287 287 ALA ALA A . n A 1 235 LYS 235 288 288 LYS LYS A . n A 1 236 PRO 236 289 289 PRO PRO A . n A 1 237 GLU 237 290 290 GLU GLU A . n A 1 238 ASP 238 291 291 ASP ASP A . n A 1 239 ARG 239 292 292 ARG ARG A . n A 1 240 ASN 240 293 293 ASN ASN A . n A 1 241 ASP 241 294 294 ASP ASP A . n A 1 242 PRO 242 295 295 PRO PRO A . n A 1 243 MET 243 296 296 MET MET A . n A 1 244 LEU 244 297 297 LEU LEU A . n A 1 245 LEU 245 298 298 LEU LEU A . n A 1 246 TYR 246 299 299 TYR TYR A . n A 1 247 ASN 247 300 300 ASN ASN A . n A 1 248 LYS 248 301 301 LYS LYS A . n A 1 249 MET 249 302 302 MET MET A . n A 1 250 THR 250 303 303 THR THR A . n A 1 251 LEU 251 304 304 LEU LEU A . n A 1 252 ALA 252 305 305 ALA ALA A . n A 1 253 GLN 253 306 306 GLN GLN A . n A 1 254 ILE 254 307 307 ILE ILE A . n A 1 255 GLN 255 308 308 GLN GLN A . n A 1 256 ASN 256 309 309 ASN ASN A . n A 1 257 ASN 257 310 310 ASN ASN A . n A 1 258 PHE 258 311 311 PHE PHE A . n A 1 259 SER 259 312 312 SER SER A . n A 1 260 LEU 260 313 313 LEU LEU A . n A 1 261 GLU 261 314 314 GLU GLU A . n A 1 262 ILE 262 315 315 ILE ILE A . n A 1 263 ASN 263 316 316 ASN ASN A . n A 1 264 GLY 264 317 317 GLY GLY A . n A 1 265 LYS 265 318 318 LYS LYS A . n A 1 266 PRO 266 319 319 PRO PRO A . n A 1 267 PHE 267 320 320 PHE PHE A . n A 1 268 SER 268 321 321 SER SER A . n A 1 269 TRP 269 322 322 TRP TRP A . n A 1 270 LEU 270 323 323 LEU LEU A . n A 1 271 ASN 271 324 324 ASN ASN A . n A 1 272 PHE 272 325 325 PHE PHE A . n A 1 273 THR 273 326 326 THR THR A . n A 1 274 ASN 274 327 327 ASN ASN A . n A 1 275 GLU 275 328 328 GLU GLU A . n A 1 276 ILE 276 329 329 ILE ILE A . n A 1 277 MET 277 330 330 MET MET A . n A 1 278 SER 278 331 331 SER SER A . n A 1 279 THR 279 332 332 THR THR A . n A 1 280 VAL 280 333 333 VAL VAL A . n A 1 281 ASN 281 334 334 ASN ASN A . n A 1 282 ILE 282 335 335 ILE ILE A . n A 1 283 SER 283 336 336 SER SER A . n A 1 284 ILE 284 337 337 ILE ILE A . n A 1 285 THR 285 338 338 THR THR A . n A 1 286 ASN 286 339 339 ASN ASN A . n A 1 287 GLU 287 340 340 GLU GLU A . n A 1 288 GLU 288 341 341 GLU GLU A . n A 1 289 ASP 289 342 342 ASP ASP A . n A 1 290 VAL 290 343 343 VAL VAL A . n A 1 291 VAL 291 344 344 VAL VAL A . n A 1 292 VAL 292 345 345 VAL VAL A . n A 1 293 TYR 293 346 346 TYR TYR A . n A 1 294 ALA 294 347 347 ALA ALA A . n A 1 295 PRO 295 348 348 PRO PRO A . n A 1 296 GLU 296 349 349 GLU GLU A . n A 1 297 TYR 297 350 350 TYR TYR A . n A 1 298 LEU 298 351 351 LEU LEU A . n A 1 299 THR 299 352 352 THR THR A . n A 1 300 LYS 300 353 353 LYS LYS A . n A 1 301 LEU 301 354 354 LEU LEU A . n A 1 302 LYS 302 355 355 LYS LYS A . n A 1 303 PRO 303 356 356 PRO PRO A . n A 1 304 ILE 304 357 357 ILE ILE A . n A 1 305 LEU 305 358 358 LEU LEU A . n A 1 306 THR 306 359 359 THR THR A . n A 1 307 LYS 307 360 360 LYS LYS A . n A 1 308 TYR 308 361 361 TYR TYR A . n A 1 309 SER 309 362 362 SER SER A . n A 1 310 ALA 310 363 363 ALA ALA A . n A 1 311 ARG 311 364 364 ARG ARG A . n A 1 312 ASP 312 365 365 ASP ASP A . n A 1 313 LEU 313 366 366 LEU LEU A . n A 1 314 GLN 314 367 367 GLN GLN A . n A 1 315 ASN 315 368 368 ASN ASN A . n A 1 316 LEU 316 369 369 LEU LEU A . n A 1 317 MET 317 370 370 MET MET A . n A 1 318 SER 318 371 371 SER SER A . n A 1 319 TRP 319 372 372 TRP TRP A . n A 1 320 ARG 320 373 373 ARG ARG A . n A 1 321 PHE 321 374 374 PHE PHE A . n A 1 322 ILE 322 375 375 ILE ILE A . n A 1 323 MET 323 376 376 MET MET A . n A 1 324 ASP 324 377 377 ASP ASP A . n A 1 325 LEU 325 378 378 LEU LEU A . n A 1 326 VAL 326 379 379 VAL VAL A . n A 1 327 SER 327 380 380 SER SER A . n A 1 328 SER 328 381 381 SER SER A . n A 1 329 LEU 329 382 382 LEU LEU A . n A 1 330 SER 330 383 383 SER SER A . n A 1 331 ARG 331 384 384 ARG ARG A . n A 1 332 THR 332 385 385 THR THR A . n A 1 333 TYR 333 386 386 TYR TYR A . n A 1 334 LYS 334 387 387 LYS LYS A . n A 1 335 GLU 335 388 388 GLU GLU A . n A 1 336 SER 336 389 389 SER SER A . n A 1 337 ARG 337 390 390 ARG ARG A . n A 1 338 ASN 338 391 391 ASN ASN A . n A 1 339 ALA 339 392 392 ALA ALA A . n A 1 340 PHE 340 393 393 PHE PHE A . n A 1 341 ARG 341 394 394 ARG ARG A . n A 1 342 LYS 342 395 395 LYS LYS A . n A 1 343 ALA 343 396 396 ALA ALA A . n A 1 344 LEU 344 397 397 LEU LEU A . n A 1 345 TYR 345 398 398 TYR TYR A . n A 1 346 GLY 346 399 399 GLY GLY A . n A 1 347 THR 347 400 400 THR THR A . n A 1 348 THR 348 401 401 THR THR A . n A 1 349 SER 349 402 402 SER SER A . n A 1 350 GLU 350 403 403 GLU GLU A . n A 1 351 THR 351 404 404 THR THR A . n A 1 352 ALA 352 405 405 ALA ALA A . n A 1 353 THR 353 406 406 THR THR A . n A 1 354 TRP 354 407 407 TRP TRP A . n A 1 355 ARG 355 408 408 ARG ARG A . n A 1 356 ARG 356 409 409 ARG ARG A . n A 1 357 CYS 357 410 410 CYS CYS A . n A 1 358 ALA 358 411 411 ALA ALA A . n A 1 359 ASN 359 412 412 ASN ASN A . n A 1 360 TYR 360 413 413 TYR TYR A . n A 1 361 VAL 361 414 414 VAL VAL A . n A 1 362 ASN 362 415 415 ASN ASN A . n A 1 363 GLY 363 416 416 GLY GLY A . n A 1 364 ASN 364 417 417 ASN ASN A . n A 1 365 MET 365 418 418 MET MET A . n A 1 366 GLU 366 419 419 GLU GLU A . n A 1 367 ASN 367 420 420 ASN ASN A . n A 1 368 ALA 368 421 421 ALA ALA A . n A 1 369 VAL 369 422 422 VAL VAL A . n A 1 370 GLY 370 423 423 GLY GLY A . n A 1 371 ARG 371 424 424 ARG ARG A . n A 1 372 LEU 372 425 425 LEU LEU A . n A 1 373 TYR 373 426 426 TYR TYR A . n A 1 374 VAL 374 427 427 VAL VAL A . n A 1 375 GLU 375 428 428 GLU GLU A . n A 1 376 ALA 376 429 429 ALA ALA A . n A 1 377 ALA 377 430 430 ALA ALA A . n A 1 378 PHE 378 431 431 PHE PHE A . n A 1 379 ALA 379 432 432 ALA ALA A . n A 1 380 GLY 380 433 433 GLY GLY A . n A 1 381 GLU 381 434 434 GLU GLU A . n A 1 382 SER 382 435 435 SER SER A . n A 1 383 LYS 383 436 436 LYS LYS A . n A 1 384 HIS 384 437 437 HIS HIS A . n A 1 385 VAL 385 438 438 VAL VAL A . n A 1 386 VAL 386 439 439 VAL VAL A . n A 1 387 GLU 387 440 440 GLU GLU A . n A 1 388 ASP 388 441 441 ASP ASP A . n A 1 389 LEU 389 442 442 LEU LEU A . n A 1 390 ILE 390 443 443 ILE ILE A . n A 1 391 ALA 391 444 444 ALA ALA A . n A 1 392 GLN 392 445 445 GLN GLN A . n A 1 393 ILE 393 446 446 ILE ILE A . n A 1 394 ARG 394 447 447 ARG ARG A . n A 1 395 GLU 395 448 448 GLU GLU A . n A 1 396 VAL 396 449 449 VAL VAL A . n A 1 397 PHE 397 450 450 PHE PHE A . n A 1 398 ILE 398 451 451 ILE ILE A . n A 1 399 GLN 399 452 452 GLN GLN A . n A 1 400 THR 400 453 453 THR THR A . n A 1 401 LEU 401 454 454 LEU LEU A . n A 1 402 ASP 402 455 455 ASP ASP A . n A 1 403 ASP 403 456 456 ASP ASP A . n A 1 404 LEU 404 457 457 LEU LEU A . n A 1 405 THR 405 458 458 THR THR A . n A 1 406 TRP 406 459 459 TRP TRP A . n A 1 407 MET 407 460 460 MET MET A . n A 1 408 ASP 408 461 461 ASP ASP A . n A 1 409 ALA 409 462 462 ALA ALA A . n A 1 410 GLU 410 463 463 GLU GLU A . n A 1 411 THR 411 464 464 THR THR A . n A 1 412 LYS 412 465 465 LYS LYS A . n A 1 413 LYS 413 466 466 LYS LYS A . n A 1 414 ARG 414 467 467 ARG ARG A . n A 1 415 ALA 415 468 468 ALA ALA A . n A 1 416 GLU 416 469 469 GLU GLU A . n A 1 417 GLU 417 470 470 GLU GLU A . n A 1 418 LYS 418 471 471 LYS LYS A . n A 1 419 ALA 419 472 472 ALA ALA A . n A 1 420 LEU 420 473 473 LEU LEU A . n A 1 421 ALA 421 474 474 ALA ALA A . n A 1 422 ILE 422 475 475 ILE ILE A . n A 1 423 LYS 423 476 476 LYS LYS A . n A 1 424 GLU 424 477 477 GLU GLU A . n A 1 425 ARG 425 478 478 ARG ARG A . n A 1 426 ILE 426 479 479 ILE ILE A . n A 1 427 GLY 427 480 480 GLY GLY A . n A 1 428 TYR 428 481 481 TYR TYR A . n A 1 429 PRO 429 482 482 PRO PRO A . n A 1 430 ASP 430 483 483 ASP ASP A . n A 1 431 ASP 431 484 484 ASP ASP A . n A 1 432 ILE 432 485 485 ILE ILE A . n A 1 433 VAL 433 486 486 VAL VAL A . n A 1 434 SER 434 487 487 SER SER A . n A 1 435 ASN 435 488 488 ASN ASN A . n A 1 436 ASP 436 489 489 ASP ASP A . n A 1 437 ASN 437 490 490 ASN ASN A . n A 1 438 LYS 438 491 491 LYS LYS A . n A 1 439 LEU 439 492 492 LEU LEU A . n A 1 440 ASN 440 493 493 ASN ASN A . n A 1 441 ASN 441 494 494 ASN ASN A . n A 1 442 GLU 442 495 495 GLU GLU A . n A 1 443 TYR 443 496 496 TYR TYR A . n A 1 444 LEU 444 497 497 LEU LEU A . n A 1 445 GLU 445 498 498 GLU GLU A . n A 1 446 LEU 446 499 499 LEU LEU A . n A 1 447 ASN 447 500 500 ASN ASN A . n A 1 448 TYR 448 501 501 TYR TYR A . n A 1 449 LYS 449 502 502 LYS LYS A . n A 1 450 GLU 450 503 503 GLU GLU A . n A 1 451 ASP 451 504 504 ASP ASP A . n A 1 452 GLU 452 505 505 GLU GLU A . n A 1 453 TYR 453 506 506 TYR TYR A . n A 1 454 PHE 454 507 507 PHE PHE A . n A 1 455 GLU 455 508 508 GLU GLU A . n A 1 456 ASN 456 509 509 ASN ASN A . n A 1 457 ILE 457 510 510 ILE ILE A . n A 1 458 ILE 458 511 511 ILE ILE A . n A 1 459 GLN 459 512 512 GLN GLN A . n A 1 460 ASN 460 513 513 ASN ASN A . n A 1 461 LEU 461 514 514 LEU LEU A . n A 1 462 LYS 462 515 515 LYS LYS A . n A 1 463 PHE 463 516 516 PHE PHE A . n A 1 464 SER 464 517 517 SER SER A . n A 1 465 GLN 465 518 518 GLN GLN A . n A 1 466 SER 466 519 519 SER SER A . n A 1 467 LYS 467 520 520 LYS LYS A . n A 1 468 GLN 468 521 521 GLN GLN A . n A 1 469 LEU 469 522 522 LEU LEU A . n A 1 470 LYS 470 523 523 LYS LYS A . n A 1 471 LYS 471 524 524 LYS LYS A . n A 1 472 LEU 472 525 525 LEU LEU A . n A 1 473 ARG 473 526 526 ARG ARG A . n A 1 474 GLU 474 527 527 GLU GLU A . n A 1 475 LYS 475 528 528 LYS LYS A . n A 1 476 VAL 476 529 529 VAL VAL A . n A 1 477 ASP 477 530 530 ASP ASP A . n A 1 478 LYS 478 531 531 LYS LYS A . n A 1 479 ASP 479 532 532 ASP ASP A . n A 1 480 GLU 480 533 533 GLU GLU A . n A 1 481 TRP 481 534 534 TRP TRP A . n A 1 482 ILE 482 535 535 ILE ILE A . n A 1 483 SER 483 536 536 SER SER A . n A 1 484 GLY 484 537 537 GLY GLY A . n A 1 485 ALA 485 538 538 ALA ALA A . n A 1 486 ALA 486 539 539 ALA ALA A . n A 1 487 VAL 487 540 540 VAL VAL A . n A 1 488 VAL 488 541 541 VAL VAL A . n A 1 489 ASN 489 542 542 ASN ASN A . n A 1 490 ALA 490 543 543 ALA ALA A . n A 1 491 PHE 491 544 544 PHE PHE A . n A 1 492 TYR 492 545 545 TYR TYR A . n A 1 493 SER 493 546 546 SER SER A . n A 1 494 SER 494 547 547 SER SER A . n A 1 495 GLY 495 548 548 GLY GLY A . n A 1 496 ARG 496 549 549 ARG ARG A . n A 1 497 ASN 497 550 550 ASN ASN A . n A 1 498 GLN 498 551 551 GLN GLN A . n A 1 499 ILE 499 552 552 ILE ILE A . n A 1 500 VAL 500 553 553 VAL VAL A . n A 1 501 PHE 501 554 554 PHE PHE A . n A 1 502 PRO 502 555 555 PRO PRO A . n A 1 503 ALA 503 556 556 ALA ALA A . n A 1 504 GLY 504 557 557 GLY GLY A . n A 1 505 ILE 505 558 558 ILE ILE A . n A 1 506 LEU 506 559 559 LEU LEU A . n A 1 507 GLN 507 560 560 GLN GLN A . n A 1 508 PRO 508 561 561 PRO PRO A . n A 1 509 PRO 509 562 562 PRO PRO A . n A 1 510 PHE 510 563 563 PHE PHE A . n A 1 511 PHE 511 564 564 PHE PHE A . n A 1 512 SER 512 565 565 SER SER A . n A 1 513 ALA 513 566 566 ALA ALA A . n A 1 514 GLN 514 567 567 GLN GLN A . n A 1 515 GLN 515 568 568 GLN GLN A . n A 1 516 SER 516 569 569 SER SER A . n A 1 517 ASN 517 570 570 ASN ASN A . n A 1 518 SER 518 571 571 SER SER A . n A 1 519 LEU 519 572 572 LEU LEU A . n A 1 520 ASN 520 573 573 ASN ASN A . n A 1 521 TYR 521 574 574 TYR TYR A . n A 1 522 GLY 522 575 575 GLY GLY A . n A 1 523 GLY 523 576 576 GLY GLY A . n A 1 524 ILE 524 577 577 ILE ILE A . n A 1 525 GLY 525 578 578 GLY GLY A . n A 1 526 MET 526 579 579 MET MET A . n A 1 527 VAL 527 580 580 VAL VAL A . n A 1 528 ILE 528 581 581 ILE ILE A . n A 1 529 GLY 529 582 582 GLY GLY A . n A 1 530 HIS 530 583 583 HIS HIS A . n A 1 531 GLU 531 584 584 GLU GLU A . n A 1 532 ILE 532 585 585 ILE ILE A . n A 1 533 THR 533 586 586 THR THR A . n A 1 534 HIS 534 587 587 HIS HIS A . n A 1 535 GLY 535 588 588 GLY GLY A . n A 1 536 PHE 536 589 589 PHE PHE A . n A 1 537 ASP 537 590 590 ASP ASP A . n A 1 538 ASP 538 591 591 ASP ASP A . n A 1 539 ASN 539 592 592 ASN ASN A . n A 1 540 GLY 540 593 593 GLY GLY A . n A 1 541 ARG 541 594 594 ARG ARG A . n A 1 542 ASN 542 595 595 ASN ASN A . n A 1 543 PHE 543 596 596 PHE PHE A . n A 1 544 ASN 544 597 597 ASN ASN A . n A 1 545 LYS 545 598 598 LYS LYS A . n A 1 546 ASP 546 599 599 ASP ASP A . n A 1 547 GLY 547 600 600 GLY GLY A . n A 1 548 ASP 548 601 601 ASP ASP A . n A 1 549 LEU 549 602 602 LEU LEU A . n A 1 550 VAL 550 603 603 VAL VAL A . n A 1 551 ASP 551 604 604 ASP ASP A . n A 1 552 TRP 552 605 605 TRP TRP A . n A 1 553 TRP 553 606 606 TRP TRP A . n A 1 554 THR 554 607 607 THR THR A . n A 1 555 GLN 555 608 608 GLN GLN A . n A 1 556 GLN 556 609 609 GLN GLN A . n A 1 557 SER 557 610 610 SER SER A . n A 1 558 ALA 558 611 611 ALA ALA A . n A 1 559 SER 559 612 612 SER SER A . n A 1 560 ASN 560 613 613 ASN ASN A . n A 1 561 PHE 561 614 614 PHE PHE A . n A 1 562 LYS 562 615 615 LYS LYS A . n A 1 563 GLU 563 616 616 GLU GLU A . n A 1 564 GLN 564 617 617 GLN GLN A . n A 1 565 SER 565 618 618 SER SER A . n A 1 566 GLN 566 619 619 GLN GLN A . n A 1 567 CYS 567 620 620 CYS CYS A . n A 1 568 MET 568 621 621 MET MET A . n A 1 569 VAL 569 622 622 VAL VAL A . n A 1 570 TYR 570 623 623 TYR TYR A . n A 1 571 GLN 571 624 624 GLN GLN A . n A 1 572 TYR 572 625 625 TYR TYR A . n A 1 573 GLY 573 626 626 GLY GLY A . n A 1 574 ASN 574 627 627 ASN ASN A . n A 1 575 PHE 575 628 628 PHE PHE A . n A 1 576 SER 576 629 629 SER SER A . n A 1 577 TRP 577 630 630 TRP TRP A . n A 1 578 ASP 578 631 631 ASP ASP A . n A 1 579 LEU 579 632 632 LEU LEU A . n A 1 580 ALA 580 633 633 ALA ALA A . n A 1 581 GLY 581 634 634 GLY GLY A . n A 1 582 GLY 582 635 635 GLY GLY A . n A 1 583 GLN 583 636 636 GLN GLN A . n A 1 584 HIS 584 637 637 HIS HIS A . n A 1 585 LEU 585 638 638 LEU LEU A . n A 1 586 ASN 586 639 639 ASN ASN A . n A 1 587 GLY 587 640 640 GLY GLY A . n A 1 588 ILE 588 641 641 ILE ILE A . n A 1 589 ASN 589 642 642 ASN ASN A . n A 1 590 THR 590 643 643 THR THR A . n A 1 591 LEU 591 644 644 LEU LEU A . n A 1 592 GLY 592 645 645 GLY GLY A . n A 1 593 GLU 593 646 646 GLU GLU A . n A 1 594 ASN 594 647 647 ASN ASN A . n A 1 595 ILE 595 648 648 ILE ILE A . n A 1 596 ALA 596 649 649 ALA ALA A . n A 1 597 ASP 597 650 650 ASP ASP A . n A 1 598 ASN 598 651 651 ASN ASN A . n A 1 599 GLY 599 652 652 GLY GLY A . n A 1 600 GLY 600 653 653 GLY GLY A . n A 1 601 LEU 601 654 654 LEU LEU A . n A 1 602 GLY 602 655 655 GLY GLY A . n A 1 603 GLN 603 656 656 GLN GLN A . n A 1 604 ALA 604 657 657 ALA ALA A . n A 1 605 TYR 605 658 658 TYR TYR A . n A 1 606 ARG 606 659 659 ARG ARG A . n A 1 607 ALA 607 660 660 ALA ALA A . n A 1 608 TYR 608 661 661 TYR TYR A . n A 1 609 GLN 609 662 662 GLN GLN A . n A 1 610 ASN 610 663 663 ASN ASN A . n A 1 611 TYR 611 664 664 TYR TYR A . n A 1 612 ILE 612 665 665 ILE ILE A . n A 1 613 LYS 613 666 666 LYS LYS A . n A 1 614 LYS 614 667 667 LYS LYS A . n A 1 615 ASN 615 668 668 ASN ASN A . n A 1 616 GLY 616 669 669 GLY GLY A . n A 1 617 GLU 617 670 670 GLU GLU A . n A 1 618 GLU 618 671 671 GLU GLU A . n A 1 619 LYS 619 672 672 LYS LYS A . n A 1 620 LEU 620 673 673 LEU LEU A . n A 1 621 LEU 621 674 674 LEU LEU A . n A 1 622 PRO 622 675 675 PRO PRO A . n A 1 623 GLY 623 676 676 GLY GLY A . n A 1 624 LEU 624 677 677 LEU LEU A . n A 1 625 ASP 625 678 678 ASP ASP A . n A 1 626 LEU 626 679 679 LEU LEU A . n A 1 627 ASN 627 680 680 ASN ASN A . n A 1 628 HIS 628 681 681 HIS HIS A . n A 1 629 LYS 629 682 682 LYS LYS A . n A 1 630 GLN 630 683 683 GLN GLN A . n A 1 631 LEU 631 684 684 LEU LEU A . n A 1 632 PHE 632 685 685 PHE PHE A . n A 1 633 PHE 633 686 686 PHE PHE A . n A 1 634 LEU 634 687 687 LEU LEU A . n A 1 635 ASN 635 688 688 ASN ASN A . n A 1 636 PHE 636 689 689 PHE PHE A . n A 1 637 ALA 637 690 690 ALA ALA A . n A 1 638 GLN 638 691 691 GLN GLN A . n A 1 639 VAL 639 692 692 VAL VAL A . n A 1 640 TRP 640 693 693 TRP TRP A . n A 1 641 CYS 641 694 694 CYS CYS A . n A 1 642 GLY 642 695 695 GLY GLY A . n A 1 643 THR 643 696 696 THR THR A . n A 1 644 TYR 644 697 697 TYR TYR A . n A 1 645 ARG 645 698 698 ARG ARG A . n A 1 646 PRO 646 699 699 PRO PRO A . n A 1 647 GLU 647 700 700 GLU GLU A . n A 1 648 TYR 648 701 701 TYR TYR A . n A 1 649 ALA 649 702 702 ALA ALA A . n A 1 650 VAL 650 703 703 VAL VAL A . n A 1 651 ASN 651 704 704 ASN ASN A . n A 1 652 SER 652 705 705 SER SER A . n A 1 653 ILE 653 706 706 ILE ILE A . n A 1 654 LYS 654 707 707 LYS LYS A . n A 1 655 THR 655 708 708 THR THR A . n A 1 656 ASP 656 709 709 ASP ASP A . n A 1 657 VAL 657 710 710 VAL VAL A . n A 1 658 HIS 658 711 711 HIS HIS A . n A 1 659 SER 659 712 712 SER SER A . n A 1 660 PRO 660 713 713 PRO PRO A . n A 1 661 GLY 661 714 714 GLY GLY A . n A 1 662 ASN 662 715 715 ASN ASN A . n A 1 663 PHE 663 716 716 PHE PHE A . n A 1 664 ARG 664 717 717 ARG ARG A . n A 1 665 ILE 665 718 718 ILE ILE A . n A 1 666 ILE 666 719 719 ILE ILE A . n A 1 667 GLY 667 720 720 GLY GLY A . n A 1 668 THR 668 721 721 THR THR A . n A 1 669 LEU 669 722 722 LEU LEU A . n A 1 670 GLN 670 723 723 GLN GLN A . n A 1 671 ASN 671 724 724 ASN ASN A . n A 1 672 SER 672 725 725 SER SER A . n A 1 673 ALA 673 726 726 ALA ALA A . n A 1 674 GLU 674 727 727 GLU GLU A . n A 1 675 PHE 675 728 728 PHE PHE A . n A 1 676 SER 676 729 729 SER SER A . n A 1 677 GLU 677 730 730 GLU GLU A . n A 1 678 ALA 678 731 731 ALA ALA A . n A 1 679 PHE 679 732 732 PHE PHE A . n A 1 680 HIS 680 733 733 HIS HIS A . n A 1 681 CYS 681 734 734 CYS CYS A . n A 1 682 ARG 682 735 735 ARG ARG A . n A 1 683 LYS 683 736 736 LYS LYS A . n A 1 684 ASN 684 737 737 ASN ASN A . n A 1 685 SER 685 738 738 SER SER A . n A 1 686 TYR 686 739 739 TYR TYR A . n A 1 687 MET 687 740 740 MET MET A . n A 1 688 ASN 688 741 741 ASN ASN A . n A 1 689 PRO 689 742 742 PRO PRO A . n A 1 690 GLU 690 743 743 GLU GLU A . n A 1 691 LYS 691 744 744 LYS LYS A . n A 1 692 LYS 692 745 745 LYS LYS A . n A 1 693 CYS 693 746 746 CYS CYS A . n A 1 694 ARG 694 747 747 ARG ARG A . n A 1 695 VAL 695 748 748 VAL VAL A . n A 1 696 TRP 696 749 749 TRP TRP 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 NAG 1 752 752 NAG NAG A . C 2 NAG 1 753 753 NAG NAG A . D 2 NAG 1 754 754 NAG NAG A . E 3 ZN 1 1001 1 ZN ZN A . F 4 BIR 1 2001 1 BIR BIR A . G 5 HOH 1 2002 1 HOH HOH A . G 5 HOH 2 2003 2 HOH HOH A . G 5 HOH 3 2004 3 HOH HOH A . G 5 HOH 4 2005 4 HOH HOH A . G 5 HOH 5 2006 5 HOH HOH A . G 5 HOH 6 2007 6 HOH HOH A . G 5 HOH 7 2008 7 HOH HOH A . G 5 HOH 8 2009 8 HOH HOH A . G 5 HOH 9 2010 9 HOH HOH A . G 5 HOH 10 2011 10 HOH HOH A . G 5 HOH 11 2012 11 HOH HOH A . G 5 HOH 12 2013 12 HOH HOH A . G 5 HOH 13 2014 13 HOH HOH A . G 5 HOH 14 2015 15 HOH HOH A . G 5 HOH 15 2016 16 HOH HOH A . G 5 HOH 16 2017 17 HOH HOH A . G 5 HOH 17 2018 18 HOH HOH A . G 5 HOH 18 2019 19 HOH HOH A . G 5 HOH 19 2020 20 HOH HOH A . G 5 HOH 20 2021 21 HOH HOH A . G 5 HOH 21 2022 22 HOH HOH A . G 5 HOH 22 2023 23 HOH HOH A . G 5 HOH 23 2024 24 HOH HOH A . G 5 HOH 24 2025 25 HOH HOH A . G 5 HOH 25 2026 26 HOH HOH A . G 5 HOH 26 2027 27 HOH HOH A . G 5 HOH 27 2028 28 HOH HOH A . G 5 HOH 28 2029 29 HOH HOH A . G 5 HOH 29 2030 30 HOH HOH A . G 5 HOH 30 2031 31 HOH HOH A . G 5 HOH 31 2032 32 HOH HOH A . G 5 HOH 32 2033 33 HOH HOH A . G 5 HOH 33 2034 34 HOH HOH A . G 5 HOH 34 2035 35 HOH HOH A . G 5 HOH 35 2036 36 HOH HOH A . G 5 HOH 36 2037 37 HOH HOH A . G 5 HOH 37 2038 38 HOH HOH A . G 5 HOH 38 2039 39 HOH HOH A . G 5 HOH 39 2040 40 HOH HOH A . G 5 HOH 40 2041 41 HOH HOH A . G 5 HOH 41 2042 42 HOH HOH A . G 5 HOH 42 2043 43 HOH HOH A . G 5 HOH 43 2044 44 HOH HOH A . G 5 HOH 44 2045 45 HOH HOH A . G 5 HOH 45 2046 46 HOH HOH A . G 5 HOH 46 2047 47 HOH HOH A . G 5 HOH 47 2048 48 HOH HOH A . G 5 HOH 48 2049 49 HOH HOH A . G 5 HOH 49 2050 50 HOH HOH A . G 5 HOH 50 2051 51 HOH HOH A . G 5 HOH 51 2052 52 HOH HOH A . G 5 HOH 52 2053 53 HOH HOH A . G 5 HOH 53 2054 54 HOH HOH A . G 5 HOH 54 2055 55 HOH HOH A . G 5 HOH 55 2056 56 HOH HOH A . G 5 HOH 56 2057 57 HOH HOH A . G 5 HOH 57 2058 58 HOH HOH A . G 5 HOH 58 2059 59 HOH HOH A . G 5 HOH 59 2060 60 HOH HOH A . G 5 HOH 60 2061 61 HOH HOH A . G 5 HOH 61 2062 62 HOH HOH A . G 5 HOH 62 2063 63 HOH HOH A . G 5 HOH 63 2064 64 HOH HOH A . G 5 HOH 64 2065 65 HOH HOH A . G 5 HOH 65 2066 66 HOH HOH A . G 5 HOH 66 2067 68 HOH HOH A . G 5 HOH 67 2068 69 HOH HOH A . G 5 HOH 68 2069 70 HOH HOH A . G 5 HOH 69 2070 71 HOH HOH A . G 5 HOH 70 2071 72 HOH HOH A . G 5 HOH 71 2072 73 HOH HOH A . G 5 HOH 72 2073 74 HOH HOH A . G 5 HOH 73 2074 75 HOH HOH A . G 5 HOH 74 2075 76 HOH HOH A . G 5 HOH 75 2076 77 HOH HOH A . G 5 HOH 76 2077 78 HOH HOH A . G 5 HOH 77 2078 79 HOH HOH A . G 5 HOH 78 2079 80 HOH HOH A . G 5 HOH 79 2080 81 HOH HOH A . G 5 HOH 80 2081 83 HOH HOH A . G 5 HOH 81 2082 84 HOH HOH A . G 5 HOH 82 2083 85 HOH HOH A . G 5 HOH 83 2084 86 HOH HOH A . G 5 HOH 84 2085 87 HOH HOH A . G 5 HOH 85 2086 88 HOH HOH A . G 5 HOH 86 2087 89 HOH HOH A . G 5 HOH 87 2088 90 HOH HOH A . G 5 HOH 88 2089 91 HOH HOH A . G 5 HOH 89 2090 92 HOH HOH A . G 5 HOH 90 2091 93 HOH HOH A . G 5 HOH 91 2092 94 HOH HOH A . G 5 HOH 92 2093 95 HOH HOH A . G 5 HOH 93 2094 96 HOH HOH A . G 5 HOH 94 2095 97 HOH HOH A . G 5 HOH 95 2096 98 HOH HOH A . G 5 HOH 96 2097 99 HOH HOH A . G 5 HOH 97 2098 100 HOH HOH A . G 5 HOH 98 2099 101 HOH HOH A . G 5 HOH 99 2100 102 HOH HOH A . G 5 HOH 100 2101 103 HOH HOH A . G 5 HOH 101 2102 104 HOH HOH A . G 5 HOH 102 2103 105 HOH HOH A . G 5 HOH 103 2104 106 HOH HOH A . G 5 HOH 104 2105 107 HOH HOH A . G 5 HOH 105 2106 108 HOH HOH A . G 5 HOH 106 2107 109 HOH HOH A . G 5 HOH 107 2108 110 HOH HOH A . G 5 HOH 108 2109 111 HOH HOH A . G 5 HOH 109 2110 112 HOH HOH A . G 5 HOH 110 2111 113 HOH HOH A . G 5 HOH 111 2112 114 HOH HOH A . G 5 HOH 112 2113 115 HOH HOH A . G 5 HOH 113 2114 116 HOH HOH A . G 5 HOH 114 2115 117 HOH HOH A . G 5 HOH 115 2116 118 HOH HOH A . G 5 HOH 116 2117 119 HOH HOH A . G 5 HOH 117 2118 120 HOH HOH A . G 5 HOH 118 2119 121 HOH HOH A . G 5 HOH 119 2120 122 HOH HOH A . G 5 HOH 120 2121 123 HOH HOH A . G 5 HOH 121 2122 124 HOH HOH A . G 5 HOH 122 2123 125 HOH HOH A . G 5 HOH 123 2124 126 HOH HOH A . G 5 HOH 124 2125 127 HOH HOH A . G 5 HOH 125 2126 128 HOH HOH A . G 5 HOH 126 2127 129 HOH HOH A . G 5 HOH 127 2128 130 HOH HOH A . G 5 HOH 128 2129 131 HOH HOH A . G 5 HOH 129 2130 132 HOH HOH A . G 5 HOH 130 2131 133 HOH HOH A . G 5 HOH 131 2132 134 HOH HOH A . G 5 HOH 132 2133 135 HOH HOH A . G 5 HOH 133 2134 136 HOH HOH A . G 5 HOH 134 2135 137 HOH HOH A . G 5 HOH 135 2136 138 HOH HOH A . G 5 HOH 136 2137 139 HOH HOH A . G 5 HOH 137 2138 140 HOH HOH A . G 5 HOH 138 2139 141 HOH HOH A . G 5 HOH 139 2140 142 HOH HOH A . G 5 HOH 140 2141 143 HOH HOH A . G 5 HOH 141 2142 144 HOH HOH A . G 5 HOH 142 2143 145 HOH HOH A . G 5 HOH 143 2144 146 HOH HOH A . G 5 HOH 144 2145 147 HOH HOH A . G 5 HOH 145 2146 148 HOH HOH A . G 5 HOH 146 2147 149 HOH HOH A . G 5 HOH 147 2148 150 HOH HOH A . G 5 HOH 148 2149 151 HOH HOH A . G 5 HOH 149 2150 152 HOH HOH A . G 5 HOH 150 2151 153 HOH HOH A . G 5 HOH 151 2152 154 HOH HOH A . G 5 HOH 152 2153 155 HOH HOH A . G 5 HOH 153 2154 156 HOH HOH A . G 5 HOH 154 2155 157 HOH HOH A . G 5 HOH 155 2156 158 HOH HOH A . G 5 HOH 156 2157 159 HOH HOH A . G 5 HOH 157 2158 160 HOH HOH A . G 5 HOH 158 2159 161 HOH HOH A . G 5 HOH 159 2160 162 HOH HOH A . G 5 HOH 160 2161 163 HOH HOH A . G 5 HOH 161 2162 164 HOH HOH A . G 5 HOH 162 2163 165 HOH HOH A . G 5 HOH 163 2164 166 HOH HOH A . G 5 HOH 164 2165 167 HOH HOH A . G 5 HOH 165 2166 168 HOH HOH A . G 5 HOH 166 2167 169 HOH HOH A . G 5 HOH 167 2168 170 HOH HOH A . G 5 HOH 168 2169 171 HOH HOH A . G 5 HOH 169 2170 172 HOH HOH A . G 5 HOH 170 2171 173 HOH HOH A . G 5 HOH 171 2172 174 HOH HOH A . G 5 HOH 172 2173 175 HOH HOH A . G 5 HOH 173 2174 176 HOH HOH A . G 5 HOH 174 2175 177 HOH HOH A . G 5 HOH 175 2176 178 HOH HOH A . G 5 HOH 176 2177 179 HOH HOH A . G 5 HOH 177 2178 180 HOH HOH A . G 5 HOH 178 2179 181 HOH HOH A . G 5 HOH 179 2180 182 HOH HOH A . G 5 HOH 180 2181 183 HOH HOH A . G 5 HOH 181 2182 184 HOH HOH A . G 5 HOH 182 2183 185 HOH HOH A . G 5 HOH 183 2184 186 HOH HOH A . G 5 HOH 184 2185 187 HOH HOH A . G 5 HOH 185 2186 188 HOH HOH A . G 5 HOH 186 2187 189 HOH HOH A . G 5 HOH 187 2188 190 HOH HOH A . G 5 HOH 188 2189 191 HOH HOH A . G 5 HOH 189 2190 192 HOH HOH A . G 5 HOH 190 2191 193 HOH HOH A . G 5 HOH 191 2192 194 HOH HOH A . G 5 HOH 192 2193 195 HOH HOH A . G 5 HOH 193 2194 196 HOH HOH A . G 5 HOH 194 2195 197 HOH HOH A . G 5 HOH 195 2196 198 HOH HOH A . G 5 HOH 196 2197 199 HOH HOH A . G 5 HOH 197 2198 200 HOH HOH A . G 5 HOH 198 2199 201 HOH HOH A . G 5 HOH 199 2200 202 HOH HOH A . G 5 HOH 200 2201 203 HOH HOH A . G 5 HOH 201 2202 204 HOH HOH A . G 5 HOH 202 2203 205 HOH HOH A . G 5 HOH 203 2204 206 HOH HOH A . G 5 HOH 204 2205 207 HOH HOH A . G 5 HOH 205 2206 208 HOH HOH A . G 5 HOH 206 2207 209 HOH HOH A . G 5 HOH 207 2208 210 HOH HOH A . G 5 HOH 208 2209 211 HOH HOH A . G 5 HOH 209 2210 212 HOH HOH A . G 5 HOH 210 2211 213 HOH HOH A . G 5 HOH 211 2212 214 HOH HOH A . G 5 HOH 212 2213 215 HOH HOH A . G 5 HOH 213 2214 216 HOH HOH A . G 5 HOH 214 2215 217 HOH HOH A . G 5 HOH 215 2216 218 HOH HOH A . G 5 HOH 216 2217 219 HOH HOH A . G 5 HOH 217 2218 220 HOH HOH A . G 5 HOH 218 2219 221 HOH HOH A . G 5 HOH 219 2220 222 HOH HOH A . G 5 HOH 220 2221 223 HOH HOH A . G 5 HOH 221 2222 224 HOH HOH A . G 5 HOH 222 2223 225 HOH HOH A . G 5 HOH 223 2224 226 HOH HOH A . G 5 HOH 224 2225 227 HOH HOH A . G 5 HOH 225 2226 228 HOH HOH A . G 5 HOH 226 2227 229 HOH HOH A . G 5 HOH 227 2228 230 HOH HOH A . G 5 HOH 228 2229 231 HOH HOH A . G 5 HOH 229 2230 232 HOH HOH A . G 5 HOH 230 2231 233 HOH HOH A . G 5 HOH 231 2232 234 HOH HOH A . G 5 HOH 232 2233 235 HOH HOH A . G 5 HOH 233 2234 236 HOH HOH A . G 5 HOH 234 2235 237 HOH HOH A . G 5 HOH 235 2236 238 HOH HOH A . G 5 HOH 236 2237 239 HOH HOH A . G 5 HOH 237 2238 240 HOH HOH A . G 5 HOH 238 2239 241 HOH HOH A . G 5 HOH 239 2240 242 HOH HOH A . G 5 HOH 240 2241 243 HOH HOH A . G 5 HOH 241 2242 245 HOH HOH A . G 5 HOH 242 2243 246 HOH HOH A . G 5 HOH 243 2244 247 HOH HOH A . G 5 HOH 244 2245 248 HOH HOH A . G 5 HOH 245 2246 249 HOH HOH A . G 5 HOH 246 2247 250 HOH HOH A . G 5 HOH 247 2248 251 HOH HOH A . G 5 HOH 248 2249 252 HOH HOH A . G 5 HOH 249 2250 253 HOH HOH A . G 5 HOH 250 2251 254 HOH HOH A . G 5 HOH 251 2252 255 HOH HOH A . G 5 HOH 252 2253 256 HOH HOH A . G 5 HOH 253 2254 257 HOH HOH A . G 5 HOH 254 2255 258 HOH HOH A . G 5 HOH 255 2256 259 HOH HOH A . G 5 HOH 256 2257 260 HOH HOH A . G 5 HOH 257 2258 261 HOH HOH A . G 5 HOH 258 2259 262 HOH HOH A . G 5 HOH 259 2260 263 HOH HOH A . G 5 HOH 260 2261 264 HOH HOH A . G 5 HOH 261 2262 265 HOH HOH A . G 5 HOH 262 2263 266 HOH HOH A . G 5 HOH 263 2264 267 HOH HOH A . G 5 HOH 264 2265 268 HOH HOH A . G 5 HOH 265 2266 269 HOH HOH A . G 5 HOH 266 2267 270 HOH HOH A . G 5 HOH 267 2268 271 HOH HOH A . G 5 HOH 268 2269 272 HOH HOH A . G 5 HOH 269 2270 273 HOH HOH A . G 5 HOH 270 2271 274 HOH HOH A . G 5 HOH 271 2272 275 HOH HOH A . G 5 HOH 272 2273 276 HOH HOH A . G 5 HOH 273 2274 277 HOH HOH A . G 5 HOH 274 2275 278 HOH HOH A . G 5 HOH 275 2276 279 HOH HOH A . G 5 HOH 276 2277 280 HOH HOH A . G 5 HOH 277 2278 281 HOH HOH A . G 5 HOH 278 2279 282 HOH HOH A . G 5 HOH 279 2280 283 HOH HOH A . G 5 HOH 280 2281 284 HOH HOH A . G 5 HOH 281 2282 285 HOH HOH A . G 5 HOH 282 2283 286 HOH HOH A . G 5 HOH 283 2284 287 HOH HOH A . G 5 HOH 284 2285 288 HOH HOH A . G 5 HOH 285 2286 289 HOH HOH A . G 5 HOH 286 2287 290 HOH HOH A . G 5 HOH 287 2288 291 HOH HOH A . G 5 HOH 288 2289 292 HOH HOH A . G 5 HOH 289 2290 293 HOH HOH A . G 5 HOH 290 2291 294 HOH HOH A . G 5 HOH 291 2292 295 HOH HOH A . G 5 HOH 292 2293 296 HOH HOH A . G 5 HOH 293 2294 297 HOH HOH A . G 5 HOH 294 2295 298 HOH HOH A . G 5 HOH 295 2296 299 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 91 A ASN 144 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 271 A ASN 324 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 574 A ASN 627 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_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 NE2 ? A HIS 530 ? A HIS 583 ? 1_555 ZN ? E ZN . ? A ZN 1001 ? 1_555 NE2 ? A HIS 534 ? A HIS 587 ? 1_555 93.4 ? 2 NE2 ? A HIS 530 ? A HIS 583 ? 1_555 ZN ? E ZN . ? A ZN 1001 ? 1_555 OE1 ? A GLU 593 ? A GLU 646 ? 1_555 96.6 ? 3 NE2 ? A HIS 534 ? A HIS 587 ? 1_555 ZN ? E ZN . ? A ZN 1001 ? 1_555 OE1 ? A GLU 593 ? A GLU 646 ? 1_555 110.4 ? 4 NE2 ? A HIS 530 ? A HIS 583 ? 1_555 ZN ? E ZN . ? A ZN 1001 ? 1_555 O6 ? F BIR . ? A BIR 2001 ? 1_555 118.2 ? 5 NE2 ? A HIS 534 ? A HIS 587 ? 1_555 ZN ? E ZN . ? A ZN 1001 ? 1_555 O6 ? F BIR . ? A BIR 2001 ? 1_555 128.4 ? 6 OE1 ? A GLU 593 ? A GLU 646 ? 1_555 ZN ? E ZN . ? A ZN 1001 ? 1_555 O6 ? F BIR . ? A BIR 2001 ? 1_555 105.5 ? # 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 2004-09-28 2 'Structure model' 1 1 2008-04-29 3 'Structure model' 1 2 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' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.0 ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 AMoRE phasing . ? 4 # 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 CA A GLU 434 ? ? O A HOH 2290 ? ? 1.25 2 1 N A GLU 434 ? ? O A HOH 2290 ? ? 1.34 3 1 CG2 A ILE 96 ? ? O A HOH 2112 ? ? 1.35 4 1 O A SER 546 ? ? O A HOH 2083 ? ? 1.50 5 1 C A SER 546 ? ? O A HOH 2083 ? ? 1.52 6 1 C A GLY 433 ? ? O A HOH 2290 ? ? 1.59 7 1 CA A ILE 96 ? ? O A HOH 2112 ? ? 1.65 8 1 CB A ILE 96 ? ? O A HOH 2112 ? ? 1.67 9 1 O A GLY 433 ? ? O A HOH 2290 ? ? 1.68 10 1 OD1 A ASN 284 ? ? O A HOH 2270 ? ? 1.73 11 1 O A GLY 714 ? ? CD1 A ILE 718 ? ? 1.74 12 1 O A HOH 2164 ? ? O A HOH 2197 ? ? 1.87 13 1 OH A TYR 697 ? ? O A HOH 2078 ? ? 1.97 14 1 OG A SER 546 ? ? O A HOH 2083 ? ? 1.98 15 1 C A GLU 434 ? ? O A HOH 2290 ? ? 2.06 16 1 OE1 A GLU 419 ? ? O A HOH 2056 ? ? 2.07 17 1 C A ILE 96 ? ? O A HOH 2112 ? ? 2.08 18 1 OD2 A ASP 119 ? ? O A HOH 2095 ? ? 2.08 19 1 OD1 A ASP 631 ? ? O A HOH 2184 ? ? 2.09 20 1 O A HOH 2233 ? ? O A HOH 2254 ? ? 2.09 21 1 O A SER 380 ? ? NZ A LYS 387 ? ? 2.11 22 1 OE1 A GLU 154 ? ? CE A LYS 158 ? ? 2.11 23 1 OD1 A ASP 484 ? ? NZ A LYS 491 ? ? 2.13 24 1 O A THR 338 ? ? N A GLU 341 ? ? 2.17 25 1 O A GLY 588 ? ? O A GLY 593 ? ? 2.18 # 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 2109 ? ? 1_555 O A HOH 2137 ? ? 4_556 1.04 2 1 OE1 A GLN 175 ? ? 1_555 O A ARG 260 ? ? 6_555 1.05 3 1 OE1 A GLN 175 ? ? 1_555 C A ARG 260 ? ? 6_555 1.55 4 1 O A HOH 2283 ? ? 1_555 O A HOH 2283 ? ? 4_556 1.59 5 1 CD A GLN 175 ? ? 1_555 O A ARG 260 ? ? 6_555 1.92 6 1 OE1 A GLN 175 ? ? 1_555 N A LEU 261 ? ? 6_555 2.00 7 1 OE1 A GLN 175 ? ? 1_555 CA A LEU 261 ? ? 6_555 2.09 8 1 CD A GLU 171 ? ? 1_555 CD A GLU 171 ? ? 6_555 2.11 9 1 CD A GLN 175 ? ? 1_555 C A ARG 260 ? ? 6_555 2.13 10 1 OE1 A GLU 171 ? ? 1_555 OE1 A GLU 171 ? ? 6_555 2.19 # 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 CB A ASP 73 ? ? CG A ASP 73 ? ? OD2 A ASP 73 ? ? 123.76 118.30 5.46 0.90 N 2 1 CB A ASP 504 ? ? CG A ASP 504 ? ? OD2 A ASP 504 ? ? 123.95 118.30 5.65 0.90 N 3 1 CB A ASP 631 ? ? CG A ASP 631 ? ? OD2 A ASP 631 ? ? 124.93 118.30 6.63 0.90 N 4 1 CB A ASP 650 ? ? CG A ASP 650 ? ? OD2 A ASP 650 ? ? 123.97 118.30 5.67 0.90 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 ASP A 81 ? ? -165.15 95.66 2 1 LEU A 199 ? ? 66.57 -52.52 3 1 ASN A 316 ? ? 49.34 18.85 4 1 LYS A 318 ? ? -83.94 -89.71 5 1 PRO A 319 ? ? -93.67 -159.33 6 1 ASN A 339 ? ? -35.91 -6.34 7 1 ALA A 347 ? ? -146.82 59.23 8 1 LEU A 382 ? ? -106.29 -161.41 9 1 ALA A 539 ? ? -93.81 57.13 10 1 ASN A 592 ? ? -91.10 -61.55 11 1 VAL A 748 ? ? -117.89 -76.72 # _pdbx_validate_peptide_omega.id 1 _pdbx_validate_peptide_omega.PDB_model_num 1 _pdbx_validate_peptide_omega.auth_comp_id_1 TRP _pdbx_validate_peptide_omega.auth_asym_id_1 A _pdbx_validate_peptide_omega.auth_seq_id_1 181 _pdbx_validate_peptide_omega.PDB_ins_code_1 ? _pdbx_validate_peptide_omega.label_alt_id_1 ? _pdbx_validate_peptide_omega.auth_comp_id_2 THR _pdbx_validate_peptide_omega.auth_asym_id_2 A _pdbx_validate_peptide_omega.auth_seq_id_2 182 _pdbx_validate_peptide_omega.PDB_ins_code_2 ? _pdbx_validate_peptide_omega.label_alt_id_2 ? _pdbx_validate_peptide_omega.omega 142.37 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 'ZINC ION' ZN 4 "N-[3-[(1-AMINOETHYL)(HYDROXY)PHOSPHORYL]-2-(1,1'-BIPHENYL-4-YLMETHYL)PROPANOYL]ALANINE" BIR 5 water HOH #