data_5JUV # _entry.id 5JUV # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.280 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 5JUV WWPDB D_1000221248 # loop_ _pdbx_database_related.db_name _pdbx_database_related.details _pdbx_database_related.db_id _pdbx_database_related.content_type PDB '5IFP contains the same protein, native form' 5IFP unspecified PDB '5IFT contains the same protein, in complex with 3-b-Galactopyranosyl glucose' 5IFT unspecified PDB '5IHR contains the same protein, in complex with allolactose' 5IHR unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 5JUV _pdbx_database_status.recvd_initial_deposition_date 2016-05-10 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBE _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Rico-Diaz, A.' 1 'Ramirez-Escudero, M.' 2 'Vizoso Vazquez, A.' 3 'Cerdan, M.E.' 4 'Becerra, M.' 5 'Sanz-Aparicio, J.' 6 # _citation.abstract ? _citation.abstract_id_CAS ? _citation.book_id_ISBN ? _citation.book_publisher ? _citation.book_publisher_city ? _citation.book_title ? _citation.coordinate_linkage ? _citation.country UK _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev 'FEBS J.' _citation.journal_id_ASTM ? _citation.journal_id_CSD ? _citation.journal_id_ISSN 1742-4658 _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 284 _citation.language ? _citation.page_first 1815 _citation.page_last 1829 _citation.title 'Structural features of Aspergillus niger beta-galactosidase define its activity against glycoside linkages.' _citation.year 2017 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI 10.1111/febs.14083 _citation.pdbx_database_id_PubMed 28391618 _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Rico-Diaz, A.' 1 primary 'Ramirez-Escudero, M.' 2 primary 'Vizoso-Vazquez, A.' 3 primary 'Cerdan, M.E.' 4 primary 'Becerra, M.' 5 primary 'Sanz-Aparicio, J.' 6 # _cell.angle_alpha 90.00 _cell.angle_alpha_esd ? _cell.angle_beta 99.18 _cell.angle_beta_esd ? _cell.angle_gamma 90.00 _cell.angle_gamma_esd ? _cell.entry_id 5JUV _cell.details ? _cell.formula_units_Z ? _cell.length_a 58.100 _cell.length_a_esd ? _cell.length_b 106.393 _cell.length_b_esd ? _cell.length_c 83.723 _cell.length_c_esd ? _cell.volume ? _cell.volume_esd ? _cell.Z_PDB 2 _cell.reciprocal_angle_alpha ? _cell.reciprocal_angle_beta ? _cell.reciprocal_angle_gamma ? _cell.reciprocal_angle_alpha_esd ? _cell.reciprocal_angle_beta_esd ? _cell.reciprocal_angle_gamma_esd ? _cell.reciprocal_length_a ? _cell.reciprocal_length_b ? _cell.reciprocal_length_c ? _cell.reciprocal_length_a_esd ? _cell.reciprocal_length_b_esd ? _cell.reciprocal_length_c_esd ? _cell.pdbx_unique_axis ? # _symmetry.entry_id 5JUV _symmetry.cell_setting ? _symmetry.Int_Tables_number 4 _symmetry.space_group_name_Hall ? _symmetry.space_group_name_H-M 'P 1 21 1' _symmetry.pdbx_full_space_group_name_H-M ? # 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 'Probable beta-galactosidase A' 110627.859 1 3.2.1.23 E298Q ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 11 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 3 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 15 ? ? ? ? 5 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 6 non-polymer syn 'PENTAETHYLENE GLYCOL' 238.278 1 ? ? ? ? 7 non-polymer man BETA-D-GALACTOSE 180.156 2 ? ? ? ? 8 water nat water 18.015 224 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Lactase A' # _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 ;MKLSSACAIALLAAQAAGASIKHRINGFTLTEHSDPAKRELLQKYVTWDDKSLFINGERIMIFSGEFHPFRLPVKELQLD IFQKVKALGFNCVSFYVDWALVEGKPGEYRADGIFDLEPFFDAASEAGIYLLARPGPYINAESSGGGFPGWLQRVNGTLR SSDKAYLDATDNYVSHVAATIAKYQITNGGPIILYQPENEYTSGCCGVEFPDPVYMQYVEDQARNAGVVIPLINNDASAS GNNAPGTGKGAVDIYGHDSYPLGFDCANPTVWPSGDLPTNFRTLHLEQSPTTPYAIVQFQGGSYDPWGGPGFAACSELLN NEFERVFYKNDFSFQIAIMNLYMIFGGTNWGNLGYPNGYTSYDYGSAVTESRNITREKYSELKLLGNFAKVSPGYLTASP GNLTTSGYADTTDLTVTPLLGNSTGSFFVVRHSDYSSEESTSYKLRLPTSAGSVTIPQLGGTLTLNGRDSKIHVTDYNVS GTNIIYSTAEVFTWKKFADGKVLVLYGGAGEHHELAISTKSNVTVIEGSESGISSKQTSSSVVVGWDVSTTRRIIQVGDL KILLLDRNSAYNYWVPQLATDGTSPGFSTPEKVASSIIVKAGYLVRTAYLKGSGLYLTADFNATTSVEVIGVPSTAKNLF INGDKTSHTVDKNGIWSATVDYNAPDISLPSLKDLDWKYVDTLPEIQSSYDDSLWPAADLKQTKNTLRSLTTPTSLYSSD YGFHTGYLLYRGHFTATGNESTFAIDTQGGSAFGSSVWLNGTYLGSWTGLYANSDYNATYNLPQLQAGKTYVITVVIDNM GLEENWTVGEDLMKTPRGILNFLLAGRPSSAISWKLTGNLGGEDYEDKVRGPLNEGGLYAERQGFHQPEPPSQNWKSSSP LEGLSEAGIGFYSASFDLDLPKGWDVPLFLNIGNSTTPSPYRVQVYVNGYQYAKYISNIGPQTSFPVPEGILNYRGTNWL AVTLWALDSAGGKLESLELSYTTPVLTALGEVESVDQPKYKKRKGAYHHHHHH ; _entity_poly.pdbx_seq_one_letter_code_can ;MKLSSACAIALLAAQAAGASIKHRINGFTLTEHSDPAKRELLQKYVTWDDKSLFINGERIMIFSGEFHPFRLPVKELQLD IFQKVKALGFNCVSFYVDWALVEGKPGEYRADGIFDLEPFFDAASEAGIYLLARPGPYINAESSGGGFPGWLQRVNGTLR SSDKAYLDATDNYVSHVAATIAKYQITNGGPIILYQPENEYTSGCCGVEFPDPVYMQYVEDQARNAGVVIPLINNDASAS GNNAPGTGKGAVDIYGHDSYPLGFDCANPTVWPSGDLPTNFRTLHLEQSPTTPYAIVQFQGGSYDPWGGPGFAACSELLN NEFERVFYKNDFSFQIAIMNLYMIFGGTNWGNLGYPNGYTSYDYGSAVTESRNITREKYSELKLLGNFAKVSPGYLTASP GNLTTSGYADTTDLTVTPLLGNSTGSFFVVRHSDYSSEESTSYKLRLPTSAGSVTIPQLGGTLTLNGRDSKIHVTDYNVS GTNIIYSTAEVFTWKKFADGKVLVLYGGAGEHHELAISTKSNVTVIEGSESGISSKQTSSSVVVGWDVSTTRRIIQVGDL KILLLDRNSAYNYWVPQLATDGTSPGFSTPEKVASSIIVKAGYLVRTAYLKGSGLYLTADFNATTSVEVIGVPSTAKNLF INGDKTSHTVDKNGIWSATVDYNAPDISLPSLKDLDWKYVDTLPEIQSSYDDSLWPAADLKQTKNTLRSLTTPTSLYSSD YGFHTGYLLYRGHFTATGNESTFAIDTQGGSAFGSSVWLNGTYLGSWTGLYANSDYNATYNLPQLQAGKTYVITVVIDNM GLEENWTVGEDLMKTPRGILNFLLAGRPSSAISWKLTGNLGGEDYEDKVRGPLNEGGLYAERQGFHQPEPPSQNWKSSSP LEGLSEAGIGFYSASFDLDLPKGWDVPLFLNIGNSTTPSPYRVQVYVNGYQYAKYISNIGPQTSFPVPEGILNYRGTNWL AVTLWALDSAGGKLESLELSYTTPVLTALGEVESVDQPKYKKRKGAYHHHHHH ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 MET n 1 2 LYS n 1 3 LEU n 1 4 SER n 1 5 SER n 1 6 ALA n 1 7 CYS n 1 8 ALA n 1 9 ILE n 1 10 ALA n 1 11 LEU n 1 12 LEU n 1 13 ALA n 1 14 ALA n 1 15 GLN n 1 16 ALA n 1 17 ALA n 1 18 GLY n 1 19 ALA n 1 20 SER n 1 21 ILE n 1 22 LYS n 1 23 HIS n 1 24 ARG n 1 25 ILE n 1 26 ASN n 1 27 GLY n 1 28 PHE n 1 29 THR n 1 30 LEU n 1 31 THR n 1 32 GLU n 1 33 HIS n 1 34 SER n 1 35 ASP n 1 36 PRO n 1 37 ALA n 1 38 LYS n 1 39 ARG n 1 40 GLU n 1 41 LEU n 1 42 LEU n 1 43 GLN n 1 44 LYS n 1 45 TYR n 1 46 VAL n 1 47 THR n 1 48 TRP n 1 49 ASP n 1 50 ASP n 1 51 LYS n 1 52 SER n 1 53 LEU n 1 54 PHE n 1 55 ILE n 1 56 ASN n 1 57 GLY n 1 58 GLU n 1 59 ARG n 1 60 ILE n 1 61 MET n 1 62 ILE n 1 63 PHE n 1 64 SER n 1 65 GLY n 1 66 GLU n 1 67 PHE n 1 68 HIS n 1 69 PRO n 1 70 PHE n 1 71 ARG n 1 72 LEU n 1 73 PRO n 1 74 VAL n 1 75 LYS n 1 76 GLU n 1 77 LEU n 1 78 GLN n 1 79 LEU n 1 80 ASP n 1 81 ILE n 1 82 PHE n 1 83 GLN n 1 84 LYS n 1 85 VAL n 1 86 LYS n 1 87 ALA n 1 88 LEU n 1 89 GLY n 1 90 PHE n 1 91 ASN n 1 92 CYS n 1 93 VAL n 1 94 SER n 1 95 PHE n 1 96 TYR n 1 97 VAL n 1 98 ASP n 1 99 TRP n 1 100 ALA n 1 101 LEU n 1 102 VAL n 1 103 GLU n 1 104 GLY n 1 105 LYS n 1 106 PRO n 1 107 GLY n 1 108 GLU n 1 109 TYR n 1 110 ARG n 1 111 ALA n 1 112 ASP n 1 113 GLY n 1 114 ILE n 1 115 PHE n 1 116 ASP n 1 117 LEU n 1 118 GLU n 1 119 PRO n 1 120 PHE n 1 121 PHE n 1 122 ASP n 1 123 ALA n 1 124 ALA n 1 125 SER n 1 126 GLU n 1 127 ALA n 1 128 GLY n 1 129 ILE n 1 130 TYR n 1 131 LEU n 1 132 LEU n 1 133 ALA n 1 134 ARG n 1 135 PRO n 1 136 GLY n 1 137 PRO n 1 138 TYR n 1 139 ILE n 1 140 ASN n 1 141 ALA n 1 142 GLU n 1 143 SER n 1 144 SER n 1 145 GLY n 1 146 GLY n 1 147 GLY n 1 148 PHE n 1 149 PRO n 1 150 GLY n 1 151 TRP n 1 152 LEU n 1 153 GLN n 1 154 ARG n 1 155 VAL n 1 156 ASN n 1 157 GLY n 1 158 THR n 1 159 LEU n 1 160 ARG n 1 161 SER n 1 162 SER n 1 163 ASP n 1 164 LYS n 1 165 ALA n 1 166 TYR n 1 167 LEU n 1 168 ASP n 1 169 ALA n 1 170 THR n 1 171 ASP n 1 172 ASN n 1 173 TYR n 1 174 VAL n 1 175 SER n 1 176 HIS n 1 177 VAL n 1 178 ALA n 1 179 ALA n 1 180 THR n 1 181 ILE n 1 182 ALA n 1 183 LYS n 1 184 TYR n 1 185 GLN n 1 186 ILE n 1 187 THR n 1 188 ASN n 1 189 GLY n 1 190 GLY n 1 191 PRO n 1 192 ILE n 1 193 ILE n 1 194 LEU n 1 195 TYR n 1 196 GLN n 1 197 PRO n 1 198 GLU n 1 199 ASN n 1 200 GLU n 1 201 TYR n 1 202 THR n 1 203 SER n 1 204 GLY n 1 205 CYS n 1 206 CYS n 1 207 GLY n 1 208 VAL n 1 209 GLU n 1 210 PHE n 1 211 PRO n 1 212 ASP n 1 213 PRO n 1 214 VAL n 1 215 TYR n 1 216 MET n 1 217 GLN n 1 218 TYR n 1 219 VAL n 1 220 GLU n 1 221 ASP n 1 222 GLN n 1 223 ALA n 1 224 ARG n 1 225 ASN n 1 226 ALA n 1 227 GLY n 1 228 VAL n 1 229 VAL n 1 230 ILE n 1 231 PRO n 1 232 LEU n 1 233 ILE n 1 234 ASN n 1 235 ASN n 1 236 ASP n 1 237 ALA n 1 238 SER n 1 239 ALA n 1 240 SER n 1 241 GLY n 1 242 ASN n 1 243 ASN n 1 244 ALA n 1 245 PRO n 1 246 GLY n 1 247 THR n 1 248 GLY n 1 249 LYS n 1 250 GLY n 1 251 ALA n 1 252 VAL n 1 253 ASP n 1 254 ILE n 1 255 TYR n 1 256 GLY n 1 257 HIS n 1 258 ASP n 1 259 SER n 1 260 TYR n 1 261 PRO n 1 262 LEU n 1 263 GLY n 1 264 PHE n 1 265 ASP n 1 266 CYS n 1 267 ALA n 1 268 ASN n 1 269 PRO n 1 270 THR n 1 271 VAL n 1 272 TRP n 1 273 PRO n 1 274 SER n 1 275 GLY n 1 276 ASP n 1 277 LEU n 1 278 PRO n 1 279 THR n 1 280 ASN n 1 281 PHE n 1 282 ARG n 1 283 THR n 1 284 LEU n 1 285 HIS n 1 286 LEU n 1 287 GLU n 1 288 GLN n 1 289 SER n 1 290 PRO n 1 291 THR n 1 292 THR n 1 293 PRO n 1 294 TYR n 1 295 ALA n 1 296 ILE n 1 297 VAL n 1 298 GLN n 1 299 PHE n 1 300 GLN n 1 301 GLY n 1 302 GLY n 1 303 SER n 1 304 TYR n 1 305 ASP n 1 306 PRO n 1 307 TRP n 1 308 GLY n 1 309 GLY n 1 310 PRO n 1 311 GLY n 1 312 PHE n 1 313 ALA n 1 314 ALA n 1 315 CYS n 1 316 SER n 1 317 GLU n 1 318 LEU n 1 319 LEU n 1 320 ASN n 1 321 ASN n 1 322 GLU n 1 323 PHE n 1 324 GLU n 1 325 ARG n 1 326 VAL n 1 327 PHE n 1 328 TYR n 1 329 LYS n 1 330 ASN n 1 331 ASP n 1 332 PHE n 1 333 SER n 1 334 PHE n 1 335 GLN n 1 336 ILE n 1 337 ALA n 1 338 ILE n 1 339 MET n 1 340 ASN n 1 341 LEU n 1 342 TYR n 1 343 MET n 1 344 ILE n 1 345 PHE n 1 346 GLY n 1 347 GLY n 1 348 THR n 1 349 ASN n 1 350 TRP n 1 351 GLY n 1 352 ASN n 1 353 LEU n 1 354 GLY n 1 355 TYR n 1 356 PRO n 1 357 ASN n 1 358 GLY n 1 359 TYR n 1 360 THR n 1 361 SER n 1 362 TYR n 1 363 ASP n 1 364 TYR n 1 365 GLY n 1 366 SER n 1 367 ALA n 1 368 VAL n 1 369 THR n 1 370 GLU n 1 371 SER n 1 372 ARG n 1 373 ASN n 1 374 ILE n 1 375 THR n 1 376 ARG n 1 377 GLU n 1 378 LYS n 1 379 TYR n 1 380 SER n 1 381 GLU n 1 382 LEU n 1 383 LYS n 1 384 LEU n 1 385 LEU n 1 386 GLY n 1 387 ASN n 1 388 PHE n 1 389 ALA n 1 390 LYS n 1 391 VAL n 1 392 SER n 1 393 PRO n 1 394 GLY n 1 395 TYR n 1 396 LEU n 1 397 THR n 1 398 ALA n 1 399 SER n 1 400 PRO n 1 401 GLY n 1 402 ASN n 1 403 LEU n 1 404 THR n 1 405 THR n 1 406 SER n 1 407 GLY n 1 408 TYR n 1 409 ALA n 1 410 ASP n 1 411 THR n 1 412 THR n 1 413 ASP n 1 414 LEU n 1 415 THR n 1 416 VAL n 1 417 THR n 1 418 PRO n 1 419 LEU n 1 420 LEU n 1 421 GLY n 1 422 ASN n 1 423 SER n 1 424 THR n 1 425 GLY n 1 426 SER n 1 427 PHE n 1 428 PHE n 1 429 VAL n 1 430 VAL n 1 431 ARG n 1 432 HIS n 1 433 SER n 1 434 ASP n 1 435 TYR n 1 436 SER n 1 437 SER n 1 438 GLU n 1 439 GLU n 1 440 SER n 1 441 THR n 1 442 SER n 1 443 TYR n 1 444 LYS n 1 445 LEU n 1 446 ARG n 1 447 LEU n 1 448 PRO n 1 449 THR n 1 450 SER n 1 451 ALA n 1 452 GLY n 1 453 SER n 1 454 VAL n 1 455 THR n 1 456 ILE n 1 457 PRO n 1 458 GLN n 1 459 LEU n 1 460 GLY n 1 461 GLY n 1 462 THR n 1 463 LEU n 1 464 THR n 1 465 LEU n 1 466 ASN n 1 467 GLY n 1 468 ARG n 1 469 ASP n 1 470 SER n 1 471 LYS n 1 472 ILE n 1 473 HIS n 1 474 VAL n 1 475 THR n 1 476 ASP n 1 477 TYR n 1 478 ASN n 1 479 VAL n 1 480 SER n 1 481 GLY n 1 482 THR n 1 483 ASN n 1 484 ILE n 1 485 ILE n 1 486 TYR n 1 487 SER n 1 488 THR n 1 489 ALA n 1 490 GLU n 1 491 VAL n 1 492 PHE n 1 493 THR n 1 494 TRP n 1 495 LYS n 1 496 LYS n 1 497 PHE n 1 498 ALA n 1 499 ASP n 1 500 GLY n 1 501 LYS n 1 502 VAL n 1 503 LEU n 1 504 VAL n 1 505 LEU n 1 506 TYR n 1 507 GLY n 1 508 GLY n 1 509 ALA n 1 510 GLY n 1 511 GLU n 1 512 HIS n 1 513 HIS n 1 514 GLU n 1 515 LEU n 1 516 ALA n 1 517 ILE n 1 518 SER n 1 519 THR n 1 520 LYS n 1 521 SER n 1 522 ASN n 1 523 VAL n 1 524 THR n 1 525 VAL n 1 526 ILE n 1 527 GLU n 1 528 GLY n 1 529 SER n 1 530 GLU n 1 531 SER n 1 532 GLY n 1 533 ILE n 1 534 SER n 1 535 SER n 1 536 LYS n 1 537 GLN n 1 538 THR n 1 539 SER n 1 540 SER n 1 541 SER n 1 542 VAL n 1 543 VAL n 1 544 VAL n 1 545 GLY n 1 546 TRP n 1 547 ASP n 1 548 VAL n 1 549 SER n 1 550 THR n 1 551 THR n 1 552 ARG n 1 553 ARG n 1 554 ILE n 1 555 ILE n 1 556 GLN n 1 557 VAL n 1 558 GLY n 1 559 ASP n 1 560 LEU n 1 561 LYS n 1 562 ILE n 1 563 LEU n 1 564 LEU n 1 565 LEU n 1 566 ASP n 1 567 ARG n 1 568 ASN n 1 569 SER n 1 570 ALA n 1 571 TYR n 1 572 ASN n 1 573 TYR n 1 574 TRP n 1 575 VAL n 1 576 PRO n 1 577 GLN n 1 578 LEU n 1 579 ALA n 1 580 THR n 1 581 ASP n 1 582 GLY n 1 583 THR n 1 584 SER n 1 585 PRO n 1 586 GLY n 1 587 PHE n 1 588 SER n 1 589 THR n 1 590 PRO n 1 591 GLU n 1 592 LYS n 1 593 VAL n 1 594 ALA n 1 595 SER n 1 596 SER n 1 597 ILE n 1 598 ILE n 1 599 VAL n 1 600 LYS n 1 601 ALA n 1 602 GLY n 1 603 TYR n 1 604 LEU n 1 605 VAL n 1 606 ARG n 1 607 THR n 1 608 ALA n 1 609 TYR n 1 610 LEU n 1 611 LYS n 1 612 GLY n 1 613 SER n 1 614 GLY n 1 615 LEU n 1 616 TYR n 1 617 LEU n 1 618 THR n 1 619 ALA n 1 620 ASP n 1 621 PHE n 1 622 ASN n 1 623 ALA n 1 624 THR n 1 625 THR n 1 626 SER n 1 627 VAL n 1 628 GLU n 1 629 VAL n 1 630 ILE n 1 631 GLY n 1 632 VAL n 1 633 PRO n 1 634 SER n 1 635 THR n 1 636 ALA n 1 637 LYS n 1 638 ASN n 1 639 LEU n 1 640 PHE n 1 641 ILE n 1 642 ASN n 1 643 GLY n 1 644 ASP n 1 645 LYS n 1 646 THR n 1 647 SER n 1 648 HIS n 1 649 THR n 1 650 VAL n 1 651 ASP n 1 652 LYS n 1 653 ASN n 1 654 GLY n 1 655 ILE n 1 656 TRP n 1 657 SER n 1 658 ALA n 1 659 THR n 1 660 VAL n 1 661 ASP n 1 662 TYR n 1 663 ASN n 1 664 ALA n 1 665 PRO n 1 666 ASP n 1 667 ILE n 1 668 SER n 1 669 LEU n 1 670 PRO n 1 671 SER n 1 672 LEU n 1 673 LYS n 1 674 ASP n 1 675 LEU n 1 676 ASP n 1 677 TRP n 1 678 LYS n 1 679 TYR n 1 680 VAL n 1 681 ASP n 1 682 THR n 1 683 LEU n 1 684 PRO n 1 685 GLU n 1 686 ILE n 1 687 GLN n 1 688 SER n 1 689 SER n 1 690 TYR n 1 691 ASP n 1 692 ASP n 1 693 SER n 1 694 LEU n 1 695 TRP n 1 696 PRO n 1 697 ALA n 1 698 ALA n 1 699 ASP n 1 700 LEU n 1 701 LYS n 1 702 GLN n 1 703 THR n 1 704 LYS n 1 705 ASN n 1 706 THR n 1 707 LEU n 1 708 ARG n 1 709 SER n 1 710 LEU n 1 711 THR n 1 712 THR n 1 713 PRO n 1 714 THR n 1 715 SER n 1 716 LEU n 1 717 TYR n 1 718 SER n 1 719 SER n 1 720 ASP n 1 721 TYR n 1 722 GLY n 1 723 PHE n 1 724 HIS n 1 725 THR n 1 726 GLY n 1 727 TYR n 1 728 LEU n 1 729 LEU n 1 730 TYR n 1 731 ARG n 1 732 GLY n 1 733 HIS n 1 734 PHE n 1 735 THR n 1 736 ALA n 1 737 THR n 1 738 GLY n 1 739 ASN n 1 740 GLU n 1 741 SER n 1 742 THR n 1 743 PHE n 1 744 ALA n 1 745 ILE n 1 746 ASP n 1 747 THR n 1 748 GLN n 1 749 GLY n 1 750 GLY n 1 751 SER n 1 752 ALA n 1 753 PHE n 1 754 GLY n 1 755 SER n 1 756 SER n 1 757 VAL n 1 758 TRP n 1 759 LEU n 1 760 ASN n 1 761 GLY n 1 762 THR n 1 763 TYR n 1 764 LEU n 1 765 GLY n 1 766 SER n 1 767 TRP n 1 768 THR n 1 769 GLY n 1 770 LEU n 1 771 TYR n 1 772 ALA n 1 773 ASN n 1 774 SER n 1 775 ASP n 1 776 TYR n 1 777 ASN n 1 778 ALA n 1 779 THR n 1 780 TYR n 1 781 ASN n 1 782 LEU n 1 783 PRO n 1 784 GLN n 1 785 LEU n 1 786 GLN n 1 787 ALA n 1 788 GLY n 1 789 LYS n 1 790 THR n 1 791 TYR n 1 792 VAL n 1 793 ILE n 1 794 THR n 1 795 VAL n 1 796 VAL n 1 797 ILE n 1 798 ASP n 1 799 ASN n 1 800 MET n 1 801 GLY n 1 802 LEU n 1 803 GLU n 1 804 GLU n 1 805 ASN n 1 806 TRP n 1 807 THR n 1 808 VAL n 1 809 GLY n 1 810 GLU n 1 811 ASP n 1 812 LEU n 1 813 MET n 1 814 LYS n 1 815 THR n 1 816 PRO n 1 817 ARG n 1 818 GLY n 1 819 ILE n 1 820 LEU n 1 821 ASN n 1 822 PHE n 1 823 LEU n 1 824 LEU n 1 825 ALA n 1 826 GLY n 1 827 ARG n 1 828 PRO n 1 829 SER n 1 830 SER n 1 831 ALA n 1 832 ILE n 1 833 SER n 1 834 TRP n 1 835 LYS n 1 836 LEU n 1 837 THR n 1 838 GLY n 1 839 ASN n 1 840 LEU n 1 841 GLY n 1 842 GLY n 1 843 GLU n 1 844 ASP n 1 845 TYR n 1 846 GLU n 1 847 ASP n 1 848 LYS n 1 849 VAL n 1 850 ARG n 1 851 GLY n 1 852 PRO n 1 853 LEU n 1 854 ASN n 1 855 GLU n 1 856 GLY n 1 857 GLY n 1 858 LEU n 1 859 TYR n 1 860 ALA n 1 861 GLU n 1 862 ARG n 1 863 GLN n 1 864 GLY n 1 865 PHE n 1 866 HIS n 1 867 GLN n 1 868 PRO n 1 869 GLU n 1 870 PRO n 1 871 PRO n 1 872 SER n 1 873 GLN n 1 874 ASN n 1 875 TRP n 1 876 LYS n 1 877 SER n 1 878 SER n 1 879 SER n 1 880 PRO n 1 881 LEU n 1 882 GLU n 1 883 GLY n 1 884 LEU n 1 885 SER n 1 886 GLU n 1 887 ALA n 1 888 GLY n 1 889 ILE n 1 890 GLY n 1 891 PHE n 1 892 TYR n 1 893 SER n 1 894 ALA n 1 895 SER n 1 896 PHE n 1 897 ASP n 1 898 LEU n 1 899 ASP n 1 900 LEU n 1 901 PRO n 1 902 LYS n 1 903 GLY n 1 904 TRP n 1 905 ASP n 1 906 VAL n 1 907 PRO n 1 908 LEU n 1 909 PHE n 1 910 LEU n 1 911 ASN n 1 912 ILE n 1 913 GLY n 1 914 ASN n 1 915 SER n 1 916 THR n 1 917 THR n 1 918 PRO n 1 919 SER n 1 920 PRO n 1 921 TYR n 1 922 ARG n 1 923 VAL n 1 924 GLN n 1 925 VAL n 1 926 TYR n 1 927 VAL n 1 928 ASN n 1 929 GLY n 1 930 TYR n 1 931 GLN n 1 932 TYR n 1 933 ALA n 1 934 LYS n 1 935 TYR n 1 936 ILE n 1 937 SER n 1 938 ASN n 1 939 ILE n 1 940 GLY n 1 941 PRO n 1 942 GLN n 1 943 THR n 1 944 SER n 1 945 PHE n 1 946 PRO n 1 947 VAL n 1 948 PRO n 1 949 GLU n 1 950 GLY n 1 951 ILE n 1 952 LEU n 1 953 ASN n 1 954 TYR n 1 955 ARG n 1 956 GLY n 1 957 THR n 1 958 ASN n 1 959 TRP n 1 960 LEU n 1 961 ALA n 1 962 VAL n 1 963 THR n 1 964 LEU n 1 965 TRP n 1 966 ALA n 1 967 LEU n 1 968 ASP n 1 969 SER n 1 970 ALA n 1 971 GLY n 1 972 GLY n 1 973 LYS n 1 974 LEU n 1 975 GLU n 1 976 SER n 1 977 LEU n 1 978 GLU n 1 979 LEU n 1 980 SER n 1 981 TYR n 1 982 THR n 1 983 THR n 1 984 PRO n 1 985 VAL n 1 986 LEU n 1 987 THR n 1 988 ALA n 1 989 LEU n 1 990 GLY n 1 991 GLU n 1 992 VAL n 1 993 GLU n 1 994 SER n 1 995 VAL n 1 996 ASP n 1 997 GLN n 1 998 PRO n 1 999 LYS n 1 1000 TYR n 1 1001 LYS n 1 1002 LYS n 1 1003 ARG n 1 1004 LYS n 1 1005 GLY n 1 1006 ALA n 1 1007 TYR n 1 1008 HIS n 1 1009 HIS n 1 1010 HIS n 1 1011 HIS n 1 1012 HIS n 1 1013 HIS 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 'Biological sequence' _entity_src_gen.pdbx_beg_seq_num 1 _entity_src_gen.pdbx_end_seq_num 1013 _entity_src_gen.gene_src_common_name ? _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'lacA, An01g12150' _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 'Aspergillus niger CBS 513.88' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 425011 _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 ? _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 BJ3505 _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code BGALA_ASPNC _struct_ref.pdbx_db_accession A2QAN3 _struct_ref.pdbx_db_isoform ? _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;MKLSSACAIALLAAQAAGASIKHRINGFTLTEHSDPAKRELLQKYVTWDDKSLFINGERIMIFSGEFHPFRLPVKELQLD IFQKVKALGFNCVSFYVDWALVEGKPGEYRADGIFDLEPFFDAASEAGIYLLARPGPYINAESSGGGFPGWLQRVNGTLR SSDKAYLDATDNYVSHVAATIAKYQITNGGPIILYQPENEYTSGCCGVEFPDPVYMQYVEDQARNAGVVIPLINNDASAS GNNAPGTGKGAVDIYGHDSYPLGFDCANPTVWPSGDLPTNFRTLHLEQSPTTPYAIVEFQGGSYDPWGGPGFAACSELLN NEFERVFYKNDFSFQIAIMNLYMIFGGTNWGNLGYPNGYTSYDYGSAVTESRNITREKYSELKLLGNFAKVSPGYLTASP GNLTTSGYADTTDLTVTPLLGNSTGSFFVVRHSDYSSEESTSYKLRLPTSAGSVTIPQLGGTLTLNGRDSKIHVTDYNVS GTNIIYSTAEVFTWKKFADGKVLVLYGGAGEHHELAISTKSNVTVIEGSESGISSKQTSSSVVVGWDVSTTRRIIQVGDL KILLLDRNSAYNYWVPQLATDGTSPGFSTPEKVASSIIVKAGYLVRTAYLKGSGLYLTADFNATTSVEVIGVPSTAKNLF INGDKTSHTVDKNGIWSATVDYNAPDISLPSLKDLDWKYVDTLPEIQSSYDDSLWPAADLKQTKNTLRSLTTPTSLYSSD YGFHTGYLLYRGHFTATGNESTFAIDTQGGSAFGSSVWLNGTYLGSWTGLYANSDYNATYNLPQLQAGKTYVITVVIDNM GLEENWTVGEDLMKTPRGILNFLLAGRPSSAISWKLTGNLGGEDYEDKVRGPLNEGGLYAERQGFHQPEPPSQNWKSSSP LEGLSEAGIGFYSASFDLDLPKGWDVPLFLNIGNSTTPSPYRVQVYVNGYQYAKYISNIGPQTSFPVPEGILNYRGTNWL AVTLWALDSAGGKLESLELSYTTPVLTALGEVESVDQPKYKKRKGAY ; _struct_ref.pdbx_align_begin 1 # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 5JUV _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 1007 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession A2QAN3 _struct_ref_seq.db_align_beg 1 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 1007 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 1007 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 5JUV GLN A 298 ? UNP A2QAN3 GLU 298 'engineered mutation' 298 1 1 5JUV HIS A 1008 ? UNP A2QAN3 ? ? 'expression tag' 1008 2 1 5JUV HIS A 1009 ? UNP A2QAN3 ? ? 'expression tag' 1009 3 1 5JUV HIS A 1010 ? UNP A2QAN3 ? ? 'expression tag' 1010 4 1 5JUV HIS A 1011 ? UNP A2QAN3 ? ? 'expression tag' 1011 5 1 5JUV HIS A 1012 ? UNP A2QAN3 ? ? 'expression tag' 1012 6 1 5JUV HIS A 1013 ? UNP A2QAN3 ? ? 'expression tag' 1013 7 # 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 1PE non-polymer . 'PENTAETHYLENE GLYCOL' PEG400 'C10 H22 O6' 238.278 ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GAL D-saccharide . BETA-D-GALACTOSE ? 'C6 H12 O6' 180.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 5JUV _exptl.crystals_number 1 _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 2.42 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 49.22 _exptl_crystal.description 'Rod-shaped crystals' _exptl_crystal.F_000 ? _exptl_crystal.id 1 _exptl_crystal.preparation ? _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.colour_lustre ? _exptl_crystal.colour_modifier ? _exptl_crystal.colour_primary ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_esd ? _exptl_crystal.density_meas_gt ? _exptl_crystal.density_meas_lt ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_meas_temp_esd ? _exptl_crystal.density_meas_temp_gt ? _exptl_crystal.density_meas_temp_lt ? _exptl_crystal.pdbx_crystal_image_url ? _exptl_crystal.pdbx_crystal_image_format ? _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? # _exptl_crystal_grow.apparatus ? _exptl_crystal_grow.atmosphere ? _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.details ? _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH 6.0 _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 291 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details ;24% (W/V) PEG 3350, 0.1M BIS-TRIS BUFFER PH 6.0 , 0.2M LITHIUM SULPHATE, then soacked in 30mM 6-O-beta-D-Galactopyranosyl-D-galactose, and cryoprotected with 20% (W/V) PEG 400 ; _exptl_crystal_grow.pdbx_pH_range 5.5-6.5 # _diffrn.ambient_environment ? _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.ambient_temp_esd ? _diffrn.crystal_id 1 _diffrn.crystal_support ? _diffrn.crystal_treatment ? _diffrn.details ? _diffrn.id 1 _diffrn.ambient_pressure ? _diffrn.ambient_pressure_esd ? _diffrn.ambient_pressure_gt ? _diffrn.ambient_pressure_lt ? _diffrn.ambient_temp_gt ? _diffrn.ambient_temp_lt ? # _diffrn_detector.details Kbmirrors _diffrn_detector.detector PIXEL _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'DECTRIS PILATUS 6M' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2014-12-04 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator 'SI(111)' _diffrn_radiation.polarisn_norm ? _diffrn_radiation.polarisn_ratio ? _diffrn_radiation.probe ? _diffrn_radiation.type ? _diffrn_radiation.xray_symbol ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_wavelength_list ? _diffrn_radiation.pdbx_wavelength ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_analyzer ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.97949 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.current ? _diffrn_source.details ? _diffrn_source.diffrn_id 1 _diffrn_source.power ? _diffrn_source.size ? _diffrn_source.source SYNCHROTRON _diffrn_source.target ? _diffrn_source.type 'ALBA BEAMLINE XALOC' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 0.97949 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline XALOC _diffrn_source.pdbx_synchrotron_site ALBA # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 5JUV _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 2.27 _reflns.d_resolution_low 82.65 _reflns.details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.number_all ? _reflns.number_obs 46487 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 99.9 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 6.8 _reflns.pdbx_Rmerge_I_obs 0.157 _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 8.4 _reflns.pdbx_res_netI_over_av_sigmaI_2 ? _reflns.pdbx_res_netI_over_sigmaI_2 ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_d_res_high_opt ? _reflns.pdbx_d_res_low_opt ? _reflns.pdbx_d_res_opt_method ? _reflns.phase_calculation_details ? _reflns.pdbx_Rrim_I_all ? _reflns.pdbx_Rpim_I_all ? _reflns.pdbx_d_opt ? _reflns.pdbx_number_measured_all ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.pdbx_CC_half 0.99 _reflns.pdbx_R_split ? # _reflns_shell.d_res_high 2.27 _reflns_shell.d_res_low 2.34 _reflns_shell.meanI_over_sigI_all ? _reflns_shell.meanI_over_sigI_obs 3.3 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_possible ? _reflns_shell.number_unique_all ? _reflns_shell.number_unique_obs ? _reflns_shell.percent_possible_all 99.9 _reflns_shell.percent_possible_obs ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.Rmerge_I_obs 0.584 _reflns_shell.meanI_over_sigI_gt ? _reflns_shell.meanI_over_uI_all ? _reflns_shell.meanI_over_uI_gt ? _reflns_shell.number_measured_gt ? _reflns_shell.number_unique_gt ? _reflns_shell.percent_possible_gt ? _reflns_shell.Rmerge_F_gt ? _reflns_shell.Rmerge_I_gt ? _reflns_shell.pdbx_redundancy 6.6 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_netI_over_sigmaI_all ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_CC_half ? _reflns_shell.pdbx_R_split ? # _refine.aniso_B[1][1] 2.48 _refine.aniso_B[1][2] -0.00 _refine.aniso_B[1][3] 1.51 _refine.aniso_B[2][2] -1.57 _refine.aniso_B[2][3] -0.00 _refine.aniso_B[3][3] -1.32 _refine.B_iso_max ? _refine.B_iso_mean 23.497 _refine.B_iso_min ? _refine.correlation_coeff_Fo_to_Fc 0.944 _refine.correlation_coeff_Fo_to_Fc_free 0.903 _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.diff_density_max ? _refine.diff_density_max_esd ? _refine.diff_density_min ? _refine.diff_density_min_esd ? _refine.diff_density_rms ? _refine.diff_density_rms_esd ? _refine.entry_id 5JUV _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.ls_abs_structure_details ? _refine.ls_abs_structure_Flack ? _refine.ls_abs_structure_Flack_esd ? _refine.ls_abs_structure_Rogers ? _refine.ls_abs_structure_Rogers_esd ? _refine.ls_d_res_high 2.27 _refine.ls_d_res_low 82.65 _refine.ls_extinction_coef ? _refine.ls_extinction_coef_esd ? _refine.ls_extinction_expression ? _refine.ls_extinction_method ? _refine.ls_goodness_of_fit_all ? _refine.ls_goodness_of_fit_all_esd ? _refine.ls_goodness_of_fit_obs ? _refine.ls_goodness_of_fit_obs_esd ? _refine.ls_hydrogen_treatment ? _refine.ls_matrix_type ? _refine.ls_number_constraints ? _refine.ls_number_parameters ? _refine.ls_number_reflns_all ? _refine.ls_number_reflns_obs 44046 _refine.ls_number_reflns_R_free 2413 _refine.ls_number_reflns_R_work ? _refine.ls_number_restraints ? _refine.ls_percent_reflns_obs 99.91 _refine.ls_percent_reflns_R_free 5.2 _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.18132 _refine.ls_R_factor_R_free 0.23204 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_R_factor_R_work 0.17857 _refine.ls_R_Fsqd_factor_obs ? _refine.ls_R_I_factor_obs ? _refine.ls_redundancy_reflns_all ? _refine.ls_redundancy_reflns_obs ? _refine.ls_restrained_S_all ? _refine.ls_restrained_S_obs ? _refine.ls_shift_over_esd_max ? _refine.ls_shift_over_esd_mean ? _refine.ls_structure_factor_coef ? _refine.ls_weighting_details ? _refine.ls_weighting_scheme ? _refine.ls_wR_factor_all ? _refine.ls_wR_factor_obs ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.occupancy_max ? _refine.occupancy_min ? _refine.solvent_model_details ? _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.ls_R_factor_gt ? _refine.ls_goodness_of_fit_gt ? _refine.ls_goodness_of_fit_ref ? _refine.ls_shift_over_su_max ? _refine.ls_shift_over_su_max_lt ? _refine.ls_shift_over_su_mean ? _refine.ls_shift_over_su_mean_lt ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_ls_sigma_Fsqd ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_starting_model 5IFP _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_overall_ESU_R 0.345 _refine.pdbx_overall_ESU_R_Free 0.230 _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_real_space_R ? _refine.pdbx_density_correlation ? _refine.pdbx_pd_number_of_powder_patterns ? _refine.pdbx_pd_number_of_points ? _refine.pdbx_pd_meas_number_of_points ? _refine.pdbx_pd_proc_ls_prof_R_factor ? _refine.pdbx_pd_proc_ls_prof_wR_factor ? _refine.pdbx_pd_Marquardt_correlation_coeff ? _refine.pdbx_pd_Fsqrd_R_factor ? _refine.pdbx_pd_ls_matrix_band_width ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_diffrn_id 1 _refine.overall_SU_B 7.225 _refine.overall_SU_ML 0.174 _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_average_fsc_overall ? _refine.pdbx_average_fsc_work ? _refine.pdbx_average_fsc_free ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id 1 _refine_hist.pdbx_number_atoms_protein 7483 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 406 _refine_hist.number_atoms_solvent 224 _refine_hist.number_atoms_total 8113 _refine_hist.d_res_high 2.27 _refine_hist.d_res_low 82.65 # loop_ _refine_ls_restr.pdbx_refine_id _refine_ls_restr.criterion _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.number _refine_ls_restr.rejects _refine_ls_restr.type _refine_ls_restr.weight _refine_ls_restr.pdbx_restraint_function 'X-RAY DIFFRACTION' ? 0.008 0.020 8123 ? r_bond_refined_d ? ? 'X-RAY DIFFRACTION' ? 0.001 0.020 7264 ? r_bond_other_d ? ? 'X-RAY DIFFRACTION' ? 1.310 2.011 11120 ? r_angle_refined_deg ? ? 'X-RAY DIFFRACTION' ? 0.746 3.000 16705 ? r_angle_other_deg ? ? 'X-RAY DIFFRACTION' ? 6.415 5.000 967 ? r_dihedral_angle_1_deg ? ? 'X-RAY DIFFRACTION' ? 38.382 24.527 338 ? r_dihedral_angle_2_deg ? ? 'X-RAY DIFFRACTION' ? 12.635 15.000 1159 ? r_dihedral_angle_3_deg ? ? 'X-RAY DIFFRACTION' ? 16.926 15.000 27 ? r_dihedral_angle_4_deg ? ? 'X-RAY DIFFRACTION' ? 0.070 0.200 1295 ? r_chiral_restr ? ? 'X-RAY DIFFRACTION' ? 0.005 0.021 8955 ? r_gen_planes_refined ? ? 'X-RAY DIFFRACTION' ? 0.001 0.020 1792 ? r_gen_planes_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbd_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbd_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbtor_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbtor_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_xyhbond_nbd_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_xyhbond_nbd_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_metal_ion_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_metal_ion_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_vdw_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_vdw_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_hbond_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_hbond_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_metal_ion_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_metal_ion_other ? ? 'X-RAY DIFFRACTION' ? 0.946 2.265 3871 ? r_mcbond_it ? ? 'X-RAY DIFFRACTION' ? 0.941 2.264 3870 ? r_mcbond_other ? ? 'X-RAY DIFFRACTION' ? 1.600 3.395 4837 ? r_mcangle_it ? ? 'X-RAY DIFFRACTION' ? 1.601 3.395 4838 ? r_mcangle_other ? ? 'X-RAY DIFFRACTION' ? 1.327 2.523 4252 ? r_scbond_it ? ? 'X-RAY DIFFRACTION' ? 1.327 2.523 4253 ? r_scbond_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_scangle_it ? ? 'X-RAY DIFFRACTION' ? 2.198 3.736 6284 ? r_scangle_other ? ? 'X-RAY DIFFRACTION' ? 3.162 18.451 8932 ? r_long_range_B_refined ? ? 'X-RAY DIFFRACTION' ? 3.136 18.456 8875 ? r_long_range_B_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_rigid_bond_restr ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_sphericity_free ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_sphericity_bonded ? ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.d_res_high 2.270 _refine_ls_shell.d_res_low 2.329 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.number_reflns_R_free 185 _refine_ls_shell.number_reflns_R_work 3281 _refine_ls_shell.percent_reflns_obs 99.80 _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.R_factor_obs ? _refine_ls_shell.R_factor_R_free 0.307 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.R_factor_R_work 0.235 _refine_ls_shell.redundancy_reflns_all ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.wR_factor_all ? _refine_ls_shell.wR_factor_obs ? _refine_ls_shell.wR_factor_R_free ? _refine_ls_shell.wR_factor_R_work ? _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.pdbx_phase_error ? _refine_ls_shell.pdbx_fsc_work ? _refine_ls_shell.pdbx_fsc_free ? # _struct.entry_id 5JUV _struct.title 'STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH 6-b-Galactopyranosyl galactose' _struct.pdbx_descriptor beta-galactosidase _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag N # _struct_keywords.entry_id 5JUV _struct_keywords.text ;TIM barrel, GH35, GLYCOSIDE HYDROLASE, KINETICS, PROTEIN CONFORMATION, carbohydrate metabolism, b-galactosidase, Aspergillus niger, fungal protein, SUBSTRATE SPECIFICITY, prebiotics, galactooligosaccharides, GOS, recombinant, 6-O-beta-D-Galactopyranosyl-D-galactose, 6-b-Galactopyranosyl galactose, 6-Gal-Gal, HYDROLASE ; _struct_keywords.pdbx_keywords 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 4 ? H N N 4 ? I N N 4 ? J N N 4 ? K N N 2 ? L N N 2 ? M N N 2 ? N N N 3 ? O N N 4 ? P N N 4 ? Q N N 4 ? R N N 4 ? S N N 4 ? T N N 4 ? U N N 4 ? V N N 2 ? W N N 2 ? X N N 2 ? Y N N 2 ? Z N N 2 ? AA N N 3 ? BA N N 4 ? CA N N 4 ? DA N N 4 ? EA N N 5 ? FA N N 6 ? GA N N 7 ? HA N N 7 ? IA N N 8 ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 AA1 HIS A 68 ? LEU A 72 ? HIS A 68 LEU A 72 5 ? 5 HELX_P HELX_P2 AA2 VAL A 74 ? ALA A 87 ? VAL A 74 ALA A 87 1 ? 14 HELX_P HELX_P3 AA3 ASP A 98 ? GLU A 103 ? ASP A 98 GLU A 103 1 ? 6 HELX_P HELX_P4 AA4 ASP A 112 ? PHE A 115 ? ASP A 112 PHE A 115 5 ? 4 HELX_P HELX_P5 AA5 ASP A 116 ? GLY A 128 ? ASP A 116 GLY A 128 1 ? 13 HELX_P HELX_P6 AA6 SER A 143 ? PHE A 148 ? SER A 143 PHE A 148 5 ? 6 HELX_P HELX_P7 AA7 PRO A 149 ? VAL A 155 ? PRO A 149 VAL A 155 5 ? 7 HELX_P HELX_P8 AA8 ASP A 163 ? TYR A 184 ? ASP A 163 TYR A 184 1 ? 22 HELX_P HELX_P9 AA9 GLN A 185 ? GLY A 189 ? GLN A 185 GLY A 189 5 ? 5 HELX_P HELX_P10 AB1 ASP A 212 ? ALA A 226 ? ASP A 212 ALA A 226 1 ? 15 HELX_P HELX_P11 AB2 ASN A 280 ? SER A 289 ? ASN A 280 SER A 289 1 ? 10 HELX_P HELX_P12 AB3 GLY A 311 ? LEU A 319 ? GLY A 311 LEU A 319 1 ? 9 HELX_P HELX_P13 AB4 ASN A 320 ? SER A 333 ? ASN A 320 SER A 333 1 ? 14 HELX_P HELX_P14 AB5 ARG A 376 ? VAL A 391 ? ARG A 376 VAL A 391 1 ? 16 HELX_P HELX_P15 AB6 PRO A 393 ? ALA A 398 ? PRO A 393 ALA A 398 1 ? 6 HELX_P HELX_P16 AB7 ARG A 567 ? TYR A 571 ? ARG A 567 TYR A 571 1 ? 5 HELX_P HELX_P17 AB8 THR A 589 ? SER A 595 ? THR A 589 SER A 595 1 ? 7 HELX_P HELX_P18 AB9 SER A 671 ? LEU A 675 ? SER A 671 LEU A 675 5 ? 5 HELX_P HELX_P19 AC1 LEU A 683 ? GLN A 687 ? LEU A 683 GLN A 687 5 ? 5 HELX_P HELX_P20 AC2 TYR A 717 ? GLY A 722 ? TYR A 717 GLY A 722 5 ? 6 HELX_P HELX_P21 AC3 ASP A 811 ? THR A 815 ? ASP A 811 THR A 815 5 ? 5 HELX_P HELX_P22 AC4 PRO A 828 ? ILE A 832 ? PRO A 828 ILE A 832 5 ? 5 HELX_P HELX_P23 AC5 LEU A 858 ? GLN A 863 ? LEU A 858 GLN A 863 1 ? 6 # _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 205 SG ? ? ? 1_555 A CYS 206 SG ? ? A CYS 205 A CYS 206 1_555 ? ? ? ? ? ? ? 2.951 ? disulf2 disulf ? ? A CYS 266 SG ? ? ? 1_555 A CYS 315 SG ? ? A CYS 266 A CYS 315 1_555 ? ? ? ? ? ? ? 2.096 ? covale1 covale one ? A ASN 156 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 156 A NAG 1156 1_555 ? ? ? ? ? ? ? 1.438 ? covale2 covale one ? A ASN 373 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 373 A NAG 1373 1_555 ? ? ? ? ? ? ? 1.441 ? covale3 covale one ? A ASN 478 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 478 A NAG 1478 1_555 ? ? ? ? ? ? ? 1.462 ? covale4 covale one ? A ASN 622 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 622 A NAG 1622 1_555 ? ? ? ? ? ? ? 1.453 ? covale5 covale one ? A ASN 739 ND2 ? ? ? 1_555 V NAG . C1 ? ? A ASN 739 A NAG 1739 1_555 ? ? ? ? ? ? ? 1.452 ? covale6 covale one ? A ASN 760 ND2 ? ? ? 1_555 W NAG . C1 ? ? A ASN 760 A NAG 1760 1_555 ? ? ? ? ? ? ? 1.459 ? covale7 covale one ? A ASN 777 ND2 ? ? ? 1_555 X NAG . C1 ? ? A ASN 777 A NAG 1777 1_555 ? ? ? ? ? ? ? 1.426 ? covale8 covale one ? A ASN 914 ND2 ? ? ? 1_555 Y NAG . C1 ? ? A ASN 914 A NAG 1914 1_555 ? ? ? ? ? ? ? 1.453 ? covale9 covale both ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 1373 A NAG 1374 1_555 ? ? ? ? ? ? ? 1.429 ? covale10 covale both ? D NAG . O4 ? ? ? 1_555 E BMA . C1 ? ? A NAG 1374 A BMA 1375 1_555 ? ? ? ? ? ? ? 1.424 ? covale11 covale one ? E BMA . O3 ? ? ? 1_555 F MAN . C1 ? ? A BMA 1375 A MAN 1376 1_555 ? ? ? ? ? ? ? 1.389 ? covale12 covale one ? E BMA . O6 ? ? ? 1_555 I MAN . C1 ? ? A BMA 1375 A MAN 1379 1_555 ? ? ? ? ? ? ? 1.427 ? covale13 covale one ? F MAN . O2 ? ? ? 1_555 G MAN . C1 ? ? A MAN 1376 A MAN 1377 1_555 ? ? ? ? ? ? ? 1.388 ? covale14 covale one ? G MAN . O2 ? ? ? 1_555 H MAN . C1 ? ? A MAN 1377 A MAN 1378 1_555 ? ? ? ? ? ? ? 1.430 ? covale15 covale one ? I MAN . O3 ? ? ? 1_555 J MAN . C1 ? ? A MAN 1379 A MAN 1380 1_555 ? ? ? ? ? ? ? 1.428 ? covale16 covale both ? L NAG . O4 ? ? ? 1_555 M NAG . C1 ? ? A NAG 1622 A NAG 1623 1_555 ? ? ? ? ? ? ? 1.441 ? covale17 covale both ? M NAG . O4 ? ? ? 1_555 N BMA . C1 ? ? A NAG 1623 A BMA 1624 1_555 ? ? ? ? ? ? ? 1.436 ? covale18 covale one ? N BMA . O3 ? ? ? 1_555 Q MAN . C1 ? ? A BMA 1624 A MAN 1627 1_555 ? ? ? ? ? ? ? 1.435 ? covale19 covale one ? N BMA . O6 ? ? ? 1_555 O MAN . C1 ? ? A BMA 1624 A MAN 1625 1_555 ? ? ? ? ? ? ? 1.429 ? covale20 covale one ? O MAN . O3 ? ? ? 1_555 P MAN . C1 ? ? A MAN 1625 A MAN 1626 1_555 ? ? ? ? ? ? ? 1.450 ? covale21 covale one ? O MAN . O6 ? ? ? 1_555 T MAN . C1 ? ? A MAN 1625 A MAN 1630 1_555 ? ? ? ? ? ? ? 1.427 ? covale22 covale one ? Q MAN . O2 ? ? ? 1_555 R MAN . C1 ? ? A MAN 1627 A MAN 1628 1_555 ? ? ? ? ? ? ? 1.446 ? covale23 covale one ? R MAN . O2 ? ? ? 1_555 S MAN . C1 ? ? A MAN 1628 A MAN 1629 1_555 ? ? ? ? ? ? ? 1.448 ? covale24 covale one ? T MAN . O2 ? ? ? 1_555 U MAN . C1 ? ? A MAN 1630 A MAN 1631 1_555 ? ? ? ? ? ? ? 1.437 ? covale25 covale both ? Y NAG . O4 ? ? ? 1_555 Z NAG . C1 ? ? A NAG 1914 A NAG 1915 1_555 ? ? ? ? ? ? ? 1.434 ? covale26 covale both ? Z NAG . O4 ? ? ? 1_555 AA BMA . C1 ? ? A NAG 1915 A BMA 1916 1_555 ? ? ? ? ? ? ? 1.443 ? covale27 covale one ? AA BMA . O3 ? ? ? 1_555 BA MAN . C1 ? ? A BMA 1916 A MAN 1917 1_555 ? ? ? ? ? ? ? 1.438 ? covale28 covale one ? BA MAN . O2 ? ? ? 1_555 CA MAN . C1 ? ? A MAN 1917 A MAN 1918 1_555 ? ? ? ? ? ? ? 1.400 ? covale29 covale one ? CA MAN . O2 ? ? ? 1_555 DA MAN . C1 ? ? A MAN 1918 A MAN 1919 1_555 ? ? ? ? ? ? ? 1.471 ? covale30 covale none ? GA GAL . O1 ? ? ? 1_555 HA GAL . C6 ? ? A GAL 4001 A GAL 4002 1_555 ? ? ? ? ? ? ? 1.347 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # 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 GLY 136 A . ? GLY 136 A PRO 137 A ? PRO 137 A 1 15.40 2 PHE 210 A . ? PHE 210 A PRO 211 A ? PRO 211 A 1 0.81 3 TYR 342 A . ? TYR 342 A MET 343 A ? MET 343 A 1 -0.69 4 ILE 456 A . ? ILE 456 A PRO 457 A ? PRO 457 A 1 10.34 5 GLY 940 A . ? GLY 940 A PRO 941 A ? PRO 941 A 1 3.32 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 3 ? AA2 ? 7 ? AA3 ? 8 ? AA4 ? 2 ? AA5 ? 2 ? AA6 ? 5 ? AA7 ? 5 ? AA8 ? 5 ? AA9 ? 6 ? AB1 ? 5 ? AB2 ? 3 ? AB3 ? 2 ? AB4 ? 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 AA1 1 2 ? anti-parallel AA1 2 3 ? anti-parallel AA2 1 2 ? parallel AA2 2 3 ? parallel AA2 3 4 ? parallel AA2 4 5 ? parallel AA2 5 6 ? parallel AA2 6 7 ? parallel AA3 1 2 ? anti-parallel AA3 2 3 ? anti-parallel AA3 3 4 ? anti-parallel AA3 4 5 ? anti-parallel AA3 5 6 ? anti-parallel AA3 6 7 ? anti-parallel AA3 7 8 ? anti-parallel AA4 1 2 ? anti-parallel AA5 1 2 ? anti-parallel AA6 1 2 ? anti-parallel AA6 2 3 ? parallel AA6 3 4 ? anti-parallel AA6 4 5 ? anti-parallel AA7 1 2 ? anti-parallel AA7 2 3 ? anti-parallel AA7 3 4 ? anti-parallel AA7 4 5 ? anti-parallel AA8 1 2 ? parallel AA8 2 3 ? anti-parallel AA8 3 4 ? parallel AA8 4 5 ? anti-parallel AA9 1 2 ? anti-parallel AA9 2 3 ? anti-parallel AA9 3 4 ? anti-parallel AA9 4 5 ? anti-parallel AA9 5 6 ? anti-parallel AB1 1 2 ? anti-parallel AB1 2 3 ? anti-parallel AB1 3 4 ? anti-parallel AB1 4 5 ? anti-parallel AB2 1 2 ? anti-parallel AB2 2 3 ? anti-parallel AB3 1 2 ? anti-parallel AB4 1 2 ? anti-parallel AB4 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 AA1 1 VAL A 46 ? TRP A 48 ? VAL A 46 TRP A 48 AA1 2 LEU A 53 ? ILE A 55 ? LEU A 53 ILE A 55 AA1 3 GLU A 58 ? ILE A 60 ? GLU A 58 ILE A 60 AA2 1 ILE A 192 ? TYR A 195 ? ILE A 192 TYR A 195 AA2 2 TYR A 130 ? ARG A 134 ? TYR A 130 ARG A 134 AA2 3 CYS A 92 ? TYR A 96 ? CYS A 92 TYR A 96 AA2 4 ILE A 62 ? GLU A 66 ? ILE A 62 GLU A 66 AA2 5 ILE A 338 ? TYR A 342 ? ILE A 338 TYR A 342 AA2 6 ALA A 295 ? GLN A 300 ? ALA A 295 GLN A 300 AA2 7 HIS A 257 ? SER A 259 ? HIS A 257 SER A 259 AA3 1 SER A 399 ? PRO A 400 ? SER A 399 PRO A 400 AA3 2 LEU A 414 ? LEU A 420 ? LEU A 414 LEU A 420 AA3 3 SER A 426 ? HIS A 432 ? SER A 426 HIS A 432 AA3 4 LYS A 471 ? VAL A 479 ? LYS A 471 VAL A 479 AA3 5 THR A 482 ? SER A 487 ? THR A 482 SER A 487 AA3 6 HIS A 512 ? SER A 518 ? HIS A 512 SER A 518 AA3 7 SER A 541 ? ASP A 547 ? SER A 541 ASP A 547 AA3 8 SER A 534 ? GLN A 537 ? SER A 534 GLN A 537 AA4 1 SER A 440 ? TYR A 443 ? SER A 440 TYR A 443 AA4 2 LEU A 463 ? ASN A 466 ? LEU A 463 ASN A 466 AA5 1 LEU A 445 ? LEU A 447 ? LEU A 445 LEU A 447 AA5 2 VAL A 454 ? ILE A 456 ? VAL A 454 ILE A 456 AA6 1 GLU A 490 ? PHE A 497 ? GLU A 490 PHE A 497 AA6 2 GLY A 500 ? GLY A 507 ? GLY A 500 GLY A 507 AA6 3 LEU A 560 ? ASP A 566 ? LEU A 560 ASP A 566 AA6 4 ARG A 553 ? VAL A 557 ? ARG A 553 VAL A 557 AA6 5 VAL A 523 ? GLU A 527 ? VAL A 523 GLU A 527 AA7 1 TYR A 573 ? TRP A 574 ? TYR A 573 TRP A 574 AA7 2 ILE A 598 ? LYS A 600 ? ILE A 598 LYS A 600 AA7 3 THR A 625 ? ILE A 630 ? THR A 625 ILE A 630 AA7 4 TRP A 656 ? VAL A 660 ? TRP A 656 VAL A 660 AA7 5 THR A 649 ? VAL A 650 ? THR A 649 VAL A 650 AA8 1 LEU A 578 ? ALA A 579 ? LEU A 578 ALA A 579 AA8 2 LEU A 604 ? LYS A 611 ? LEU A 604 LYS A 611 AA8 3 GLY A 614 ? ASP A 620 ? GLY A 614 ASP A 620 AA8 4 ASN A 638 ? ILE A 641 ? ASN A 638 ILE A 641 AA8 5 ASP A 644 ? THR A 646 ? ASP A 644 THR A 646 AA9 1 LYS A 876 ? SER A 877 ? LYS A 876 SER A 877 AA9 2 LYS A 678 ? ASP A 681 ? LYS A 678 ASP A 681 AA9 3 GLY A 888 ? ASP A 897 ? GLY A 888 ASP A 897 AA9 4 THR A 957 ? ALA A 966 ? THR A 957 ALA A 966 AA9 5 TYR A 921 ? VAL A 927 ? TYR A 921 VAL A 927 AA9 6 TYR A 930 ? ILE A 936 ? TYR A 930 ILE A 936 AB1 1 THR A 762 ? TRP A 767 ? THR A 762 TRP A 767 AB1 2 SER A 755 ? LEU A 759 ? SER A 755 LEU A 759 AB1 3 THR A 790 ? ASP A 798 ? THR A 790 ASP A 798 AB1 4 TYR A 727 ? THR A 735 ? TYR A 727 THR A 735 AB1 5 SER A 833 ? THR A 837 ? SER A 833 THR A 837 AB2 1 ASP A 775 ? ASN A 781 ? ASP A 775 ASN A 781 AB2 2 THR A 742 ? GLN A 748 ? THR A 742 GLN A 748 AB2 3 GLY A 818 ? LEU A 824 ? GLY A 818 LEU A 824 AB3 1 TRP A 904 ? ASP A 905 ? TRP A 904 ASP A 905 AB3 2 VAL A 985 ? LEU A 986 ? VAL A 985 LEU A 986 AB4 1 SER A 944 ? VAL A 947 ? SER A 944 VAL A 947 AB4 2 LEU A 908 ? ILE A 912 ? LEU A 908 ILE A 912 AB4 3 LEU A 977 ? TYR A 981 ? LEU A 977 TYR A 981 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA1 1 2 N THR A 47 ? N THR A 47 O PHE A 54 ? O PHE A 54 AA1 2 3 N ILE A 55 ? N ILE A 55 O GLU A 58 ? O GLU A 58 AA2 1 2 O ILE A 193 ? O ILE A 193 N LEU A 131 ? N LEU A 131 AA2 2 3 O LEU A 132 ? O LEU A 132 N VAL A 93 ? N VAL A 93 AA2 3 4 O SER A 94 ? O SER A 94 N GLY A 65 ? N GLY A 65 AA2 4 5 N SER A 64 ? N SER A 64 O MET A 339 ? O MET A 339 AA2 5 6 O ASN A 340 ? O ASN A 340 N PHE A 299 ? N PHE A 299 AA2 6 7 O GLN A 298 ? O GLN A 298 N SER A 259 ? N SER A 259 AA3 1 2 N SER A 399 ? N SER A 399 O LEU A 420 ? O LEU A 420 AA3 2 3 N THR A 415 ? N THR A 415 O ARG A 431 ? O ARG A 431 AA3 3 4 N PHE A 428 ? N PHE A 428 O HIS A 473 ? O HIS A 473 AA3 4 5 N VAL A 479 ? N VAL A 479 O THR A 482 ? O THR A 482 AA3 5 6 N ASN A 483 ? N ASN A 483 O SER A 518 ? O SER A 518 AA3 6 7 N HIS A 513 ? N HIS A 513 O TRP A 546 ? O TRP A 546 AA3 7 8 O VAL A 543 ? O VAL A 543 N LYS A 536 ? N LYS A 536 AA4 1 2 N TYR A 443 ? N TYR A 443 O LEU A 463 ? O LEU A 463 AA5 1 2 N LEU A 445 ? N LEU A 445 O ILE A 456 ? O ILE A 456 AA6 1 2 N PHE A 492 ? N PHE A 492 O VAL A 504 ? O VAL A 504 AA6 2 3 N LEU A 503 ? N LEU A 503 O LEU A 563 ? O LEU A 563 AA6 3 4 O ILE A 562 ? O ILE A 562 N ILE A 555 ? N ILE A 555 AA6 4 5 O GLN A 556 ? O GLN A 556 N THR A 524 ? N THR A 524 AA7 1 2 N TRP A 574 ? N TRP A 574 O VAL A 599 ? O VAL A 599 AA7 2 3 N ILE A 598 ? N ILE A 598 O ILE A 630 ? O ILE A 630 AA7 3 4 N VAL A 627 ? N VAL A 627 O ALA A 658 ? O ALA A 658 AA7 4 5 O SER A 657 ? O SER A 657 N THR A 649 ? N THR A 649 AA8 1 2 N ALA A 579 ? N ALA A 579 O LEU A 610 ? O LEU A 610 AA8 2 3 N TYR A 609 ? N TYR A 609 O TYR A 616 ? O TYR A 616 AA8 3 4 N LEU A 615 ? N LEU A 615 O PHE A 640 ? O PHE A 640 AA8 4 5 N LEU A 639 ? N LEU A 639 O THR A 646 ? O THR A 646 AA9 1 2 O LYS A 876 ? O LYS A 876 N TYR A 679 ? N TYR A 679 AA9 2 3 N LYS A 678 ? N LYS A 678 O SER A 893 ? O SER A 893 AA9 3 4 N ALA A 894 ? N ALA A 894 O LEU A 960 ? O LEU A 960 AA9 4 5 O TRP A 965 ? O TRP A 965 N ARG A 922 ? N ARG A 922 AA9 5 6 N VAL A 927 ? N VAL A 927 O TYR A 930 ? O TYR A 930 AB1 1 2 O THR A 762 ? O THR A 762 N LEU A 759 ? N LEU A 759 AB1 2 3 N SER A 756 ? N SER A 756 O VAL A 796 ? O VAL A 796 AB1 3 4 O TYR A 791 ? O TYR A 791 N PHE A 734 ? N PHE A 734 AB1 4 5 N ARG A 731 ? N ARG A 731 O LYS A 835 ? O LYS A 835 AB2 1 2 O ALA A 778 ? O ALA A 778 N ILE A 745 ? N ILE A 745 AB2 2 3 N ALA A 744 ? N ALA A 744 O LEU A 823 ? O LEU A 823 AB3 1 2 N ASP A 905 ? N ASP A 905 O VAL A 985 ? O VAL A 985 AB4 1 2 O PHE A 945 ? O PHE A 945 N LEU A 910 ? N LEU A 910 AB4 2 3 N ASN A 911 ? N ASN A 911 O GLU A 978 ? O GLU A 978 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software A CL 2001 ? 3 'binding site for residue CL A 2001' AC2 Software A 1PE 3001 ? 5 'binding site for residue 1PE A 3001' AC3 Software A NAG 1156 ? 1 'binding site for Mono-Saccharide NAG A 1156 bound to ASN A 156' AC4 Software A ASN 373 ? 19 'binding site for Poly-Saccharide residues NAG A 1373 through MAN A 1380 bound to ASN A 373' AC5 Software A NAG 1478 ? 3 'binding site for Mono-Saccharide NAG A 1478 bound to ASN A 478' AC6 Software A ASN 622 ? 20 'binding site for Poly-Saccharide residues NAG A 1622 through MAN A 1631 bound to ASN A 622' AC7 Software A NAG 1739 ? 1 'binding site for Mono-Saccharide NAG A 1739 bound to ASN A 739' AC8 Software A NAG 1760 ? 6 'binding site for Mono-Saccharide NAG A 1760 bound to ASN A 760' AC9 Software A NAG 1777 ? 3 'binding site for Mono-Saccharide NAG A 1777 bound to ASN A 777' AD1 Software A ASN 914 ? 13 'binding site for Poly-Saccharide residues NAG A 1914 through MAN A 1919 bound to ASN A 914' AD2 Software A GAL 4001 ? 16 'binding site for Poly-Saccharide residues GAL A 4001 through GAL A 4002' # 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 3 ARG A 862 ? ARG A 862 . ? 1_555 ? 2 AC1 3 GLN A 863 ? GLN A 863 . ? 1_555 ? 3 AC1 3 TYR A 1007 ? TYR A 1007 . ? 1_555 ? 4 AC2 5 ASN A 140 ? ASN A 140 . ? 1_555 ? 5 AC2 5 GLU A 142 ? GLU A 142 . ? 1_555 ? 6 AC2 5 GLU A 804 ? GLU A 804 . ? 1_555 ? 7 AC2 5 TRP A 806 ? TRP A 806 . ? 1_555 ? 8 AC2 5 GAL GA . ? GAL A 4001 . ? 1_555 ? 9 AC3 1 ASN A 156 ? ASN A 156 . ? 1_555 ? 10 AC4 19 ALA A 313 ? ALA A 313 . ? 1_555 ? 11 AC4 19 GLU A 317 ? GLU A 317 . ? 1_555 ? 12 AC4 19 THR A 369 ? THR A 369 . ? 1_555 ? 13 AC4 19 SER A 371 ? SER A 371 . ? 1_555 ? 14 AC4 19 ASN A 373 ? ASN A 373 . ? 1_555 ? 15 AC4 19 ASN A 911 ? ASN A 911 . ? 1_555 ? 16 AC4 19 SER A 915 ? SER A 915 . ? 1_555 ? 17 AC4 19 THR A 943 ? THR A 943 . ? 1_555 ? 18 AC4 19 SER A 944 ? SER A 944 . ? 1_555 ? 19 AC4 19 GLU A 978 ? GLU A 978 . ? 1_555 ? 20 AC4 19 THR A 982 ? THR A 982 . ? 1_555 ? 21 AC4 19 THR A 983 ? THR A 983 . ? 1_555 ? 22 AC4 19 NAG L . ? NAG A 1622 . ? 1_555 ? 23 AC4 19 MAN Q . ? MAN A 1627 . ? 1_555 ? 24 AC4 19 MAN R . ? MAN A 1628 . ? 1_555 ? 25 AC4 19 HOH IA . ? HOH A 5028 . ? 1_555 ? 26 AC4 19 HOH IA . ? HOH A 5053 . ? 1_555 ? 27 AC4 19 HOH IA . ? HOH A 5079 . ? 1_555 ? 28 AC4 19 HOH IA . ? HOH A 5093 . ? 1_555 ? 29 AC5 3 SER A 423 ? SER A 423 . ? 1_555 ? 30 AC5 3 ASN A 478 ? ASN A 478 . ? 1_555 ? 31 AC5 3 SER A 480 ? SER A 480 . ? 1_555 ? 32 AC6 20 LEU A 42 ? LEU A 42 . ? 1_455 ? 33 AC6 20 VAL A 229 ? VAL A 229 . ? 1_455 ? 34 AC6 20 GLU A 317 ? GLU A 317 . ? 1_555 ? 35 AC6 20 ASN A 320 ? ASN A 320 . ? 1_555 ? 36 AC6 20 ASN A 321 ? ASN A 321 . ? 1_555 ? 37 AC6 20 GLU A 322 ? GLU A 322 . ? 1_555 ? 38 AC6 20 ARG A 325 ? ARG A 325 . ? 1_555 ? 39 AC6 20 THR A 375 ? THR A 375 . ? 1_555 ? 40 AC6 20 GLU A 377 ? GLU A 377 . ? 1_555 ? 41 AC6 20 ASN A 568 ? ASN A 568 . ? 1_555 ? 42 AC6 20 TYR A 603 ? TYR A 603 . ? 1_555 ? 43 AC6 20 ASN A 622 ? ASN A 622 . ? 1_555 ? 44 AC6 20 THR A 983 ? THR A 983 . ? 1_555 ? 45 AC6 20 NAG C . ? NAG A 1373 . ? 1_555 ? 46 AC6 20 MAN J . ? MAN A 1380 . ? 1_555 ? 47 AC6 20 HOH IA . ? HOH A 5011 . ? 1_555 ? 48 AC6 20 HOH IA . ? HOH A 5069 . ? 1_555 ? 49 AC6 20 HOH IA . ? HOH A 5123 . ? 1_555 ? 50 AC6 20 HOH IA . ? HOH A 5148 . ? 1_555 ? 51 AC6 20 HOH IA . ? HOH A 5149 . ? 1_555 ? 52 AC7 1 ASN A 739 ? ASN A 739 . ? 1_555 ? 53 AC8 6 SER A 688 ? SER A 688 . ? 1_555 ? 54 AC8 6 ARG A 731 ? ARG A 731 . ? 1_555 ? 55 AC8 6 ASN A 760 ? ASN A 760 . ? 1_555 ? 56 AC8 6 THR A 790 ? THR A 790 . ? 1_555 ? 57 AC8 6 TYR A 791 ? TYR A 791 . ? 1_555 ? 58 AC8 6 VAL A 792 ? VAL A 792 . ? 1_555 ? 59 AC9 3 ASN A 773 ? ASN A 773 . ? 1_555 ? 60 AC9 3 ASP A 775 ? ASP A 775 . ? 1_555 ? 61 AC9 3 ASN A 777 ? ASN A 777 . ? 1_555 ? 62 AD1 13 TRP A 307 ? TRP A 307 . ? 1_555 ? 63 AD1 13 GLY A 308 ? GLY A 308 . ? 1_555 ? 64 AD1 13 TYR A 771 ? TYR A 771 . ? 1_555 ? 65 AD1 13 ALA A 772 ? ALA A 772 . ? 1_555 ? 66 AD1 13 ASN A 914 ? ASN A 914 . ? 1_555 ? 67 AD1 13 TYR A 935 ? TYR A 935 . ? 1_555 ? 68 AD1 13 ILE A 936 ? ILE A 936 . ? 1_555 ? 69 AD1 13 SER A 937 ? SER A 937 . ? 1_555 ? 70 AD1 13 ILE A 939 ? ILE A 939 . ? 1_555 ? 71 AD1 13 GLY A 940 ? GLY A 940 . ? 1_555 ? 72 AD1 13 PRO A 941 ? PRO A 941 . ? 1_555 ? 73 AD1 13 HOH IA . ? HOH A 5074 . ? 1_555 ? 74 AD1 13 HOH IA . ? HOH A 5092 . ? 1_555 ? 75 AD2 16 TYR A 96 ? TYR A 96 . ? 1_555 ? 76 AD2 16 ILE A 139 ? ILE A 139 . ? 1_555 ? 77 AD2 16 ASN A 140 ? ASN A 140 . ? 1_555 ? 78 AD2 16 ALA A 141 ? ALA A 141 . ? 1_555 ? 79 AD2 16 GLU A 142 ? GLU A 142 . ? 1_555 ? 80 AD2 16 ASN A 199 ? ASN A 199 . ? 1_555 ? 81 AD2 16 GLU A 200 ? GLU A 200 . ? 1_555 ? 82 AD2 16 ALA A 237 ? ALA A 237 . ? 1_555 ? 83 AD2 16 ASP A 258 ? ASP A 258 . ? 1_555 ? 84 AD2 16 SER A 259 ? SER A 259 . ? 1_555 ? 85 AD2 16 TYR A 260 ? TYR A 260 . ? 1_555 ? 86 AD2 16 GLN A 298 ? GLN A 298 . ? 1_555 ? 87 AD2 16 TYR A 304 ? TYR A 304 . ? 1_555 ? 88 AD2 16 TYR A 342 ? TYR A 342 . ? 1_555 ? 89 AD2 16 TYR A 364 ? TYR A 364 . ? 1_555 ? 90 AD2 16 1PE FA . ? 1PE A 3001 . ? 1_555 ? # _atom_sites.entry_id 5JUV _atom_sites.fract_transf_matrix[1][1] 0.017212 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.002782 _atom_sites.fract_transf_matrix[2][1] -0.000000 _atom_sites.fract_transf_matrix[2][2] 0.009399 _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] 0.012099 _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 CL N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . LEU A 1 41 ? 37.504 -0.515 8.258 1.00 34.36 ? 41 LEU A N 1 ATOM 2 C CA . LEU A 1 41 ? 38.334 0.684 8.610 1.00 34.62 ? 41 LEU A CA 1 ATOM 3 C C . LEU A 1 41 ? 39.278 0.430 9.803 1.00 32.78 ? 41 LEU A C 1 ATOM 4 O O . LEU A 1 41 ? 40.476 0.675 9.691 1.00 33.04 ? 41 LEU A O 1 ATOM 5 C CB . LEU A 1 41 ? 37.440 1.904 8.880 1.00 36.70 ? 41 LEU A CB 1 ATOM 6 C CG . LEU A 1 41 ? 38.047 3.302 8.705 1.00 39.03 ? 41 LEU A CG 1 ATOM 7 C CD1 . LEU A 1 41 ? 37.772 3.874 7.314 1.00 39.49 ? 41 LEU A CD1 1 ATOM 8 C CD2 . LEU A 1 41 ? 37.506 4.242 9.774 1.00 40.64 ? 41 LEU A CD2 1 ATOM 9 N N . LEU A 1 42 ? 38.748 -0.028 10.940 1.00 30.80 ? 42 LEU A N 1 ATOM 10 C CA . LEU A 1 42 ? 39.590 -0.396 12.099 1.00 29.96 ? 42 LEU A CA 1 ATOM 11 C C . LEU A 1 42 ? 39.618 -1.896 12.412 1.00 28.85 ? 42 LEU A C 1 ATOM 12 O O . LEU A 1 42 ? 40.449 -2.347 13.191 1.00 29.84 ? 42 LEU A O 1 ATOM 13 C CB . LEU A 1 42 ? 39.154 0.350 13.364 1.00 31.02 ? 42 LEU A CB 1 ATOM 14 C CG . LEU A 1 42 ? 39.375 1.855 13.482 1.00 31.51 ? 42 LEU A CG 1 ATOM 15 C CD1 . LEU A 1 42 ? 39.073 2.287 14.909 1.00 32.32 ? 42 LEU A CD1 1 ATOM 16 C CD2 . LEU A 1 42 ? 40.786 2.271 13.082 1.00 31.34 ? 42 LEU A CD2 1 ATOM 17 N N . GLN A 1 43 ? 38.702 -2.662 11.834 1.00 27.90 ? 43 GLN A N 1 ATOM 18 C CA . GLN A 1 43 ? 38.694 -4.118 11.972 1.00 26.52 ? 43 GLN A CA 1 ATOM 19 C C . GLN A 1 43 ? 38.070 -4.678 10.705 1.00 26.93 ? 43 GLN A C 1 ATOM 20 O O . GLN A 1 43 ? 37.584 -3.910 9.885 1.00 28.04 ? 43 GLN A O 1 ATOM 21 C CB . GLN A 1 43 ? 37.927 -4.547 13.232 1.00 25.25 ? 43 GLN A CB 1 ATOM 22 C CG . GLN A 1 43 ? 36.609 -3.820 13.456 1.00 24.15 ? 43 GLN A CG 1 ATOM 23 C CD . GLN A 1 43 ? 35.594 -4.115 12.377 1.00 23.16 ? 43 GLN A CD 1 ATOM 24 O OE1 . GLN A 1 43 ? 35.218 -5.263 12.179 1.00 22.61 ? 43 GLN A OE1 1 ATOM 25 N NE2 . GLN A 1 43 ? 35.143 -3.085 11.672 1.00 23.29 ? 43 GLN A NE2 1 ATOM 26 N N . LYS A 1 44 ? 38.081 -5.996 10.542 1.00 28.23 ? 44 LYS A N 1 ATOM 27 C CA . LYS A 1 44 ? 37.654 -6.619 9.286 1.00 30.65 ? 44 LYS A CA 1 ATOM 28 C C . LYS A 1 44 ? 36.385 -7.476 9.411 1.00 29.57 ? 44 LYS A C 1 ATOM 29 O O . LYS A 1 44 ? 35.902 -8.011 8.414 1.00 28.65 ? 44 LYS A O 1 ATOM 30 C CB . LYS A 1 44 ? 38.813 -7.446 8.715 1.00 34.34 ? 44 LYS A CB 1 ATOM 31 C CG . LYS A 1 44 ? 40.091 -6.622 8.512 1.00 38.70 ? 44 LYS A CG 1 ATOM 32 C CD . LYS A 1 44 ? 41.336 -7.484 8.283 1.00 41.89 ? 44 LYS A CD 1 ATOM 33 C CE . LYS A 1 44 ? 41.440 -7.985 6.844 1.00 43.01 ? 44 LYS A CE 1 ATOM 34 N NZ . LYS A 1 44 ? 42.075 -6.991 5.935 1.00 43.58 ? 44 LYS A NZ 1 ATOM 35 N N . TYR A 1 45 ? 35.840 -7.591 10.623 1.00 27.76 ? 45 TYR A N 1 ATOM 36 C CA . TYR A 1 45 ? 34.615 -8.367 10.852 1.00 26.85 ? 45 TYR A CA 1 ATOM 37 C C . TYR A 1 45 ? 33.357 -7.683 10.290 1.00 25.21 ? 45 TYR A C 1 ATOM 38 O O . TYR A 1 45 ? 32.453 -8.359 9.776 1.00 24.47 ? 45 TYR A O 1 ATOM 39 C CB . TYR A 1 45 ? 34.402 -8.624 12.349 1.00 26.77 ? 45 TYR A CB 1 ATOM 40 C CG . TYR A 1 45 ? 35.321 -9.652 12.993 1.00 26.70 ? 45 TYR A CG 1 ATOM 41 C CD1 . TYR A 1 45 ? 36.609 -9.306 13.402 1.00 26.74 ? 45 TYR A CD1 1 ATOM 42 C CD2 . TYR A 1 45 ? 34.881 -10.953 13.244 1.00 27.09 ? 45 TYR A CD2 1 ATOM 43 C CE1 . TYR A 1 45 ? 37.442 -10.226 14.020 1.00 26.80 ? 45 TYR A CE1 1 ATOM 44 C CE2 . TYR A 1 45 ? 35.708 -11.887 13.865 1.00 27.71 ? 45 TYR A CE2 1 ATOM 45 C CZ . TYR A 1 45 ? 36.991 -11.517 14.254 1.00 27.83 ? 45 TYR A CZ 1 ATOM 46 O OH . TYR A 1 45 ? 37.827 -12.424 14.872 1.00 26.94 ? 45 TYR A OH 1 ATOM 47 N N . VAL A 1 46 ? 33.295 -6.356 10.412 1.00 23.15 ? 46 VAL A N 1 ATOM 48 C CA . VAL A 1 46 ? 32.119 -5.600 10.005 1.00 23.23 ? 46 VAL A CA 1 ATOM 49 C C . VAL A 1 46 ? 32.491 -4.507 9.019 1.00 23.09 ? 46 VAL A C 1 ATOM 50 O O . VAL A 1 46 ? 33.065 -3.482 9.394 1.00 22.62 ? 46 VAL A O 1 ATOM 51 C CB . VAL A 1 46 ? 31.395 -4.941 11.202 1.00 23.18 ? 46 VAL A CB 1 ATOM 52 C CG1 . VAL A 1 46 ? 30.064 -4.334 10.746 1.00 23.02 ? 46 VAL A CG1 1 ATOM 53 C CG2 . VAL A 1 46 ? 31.164 -5.954 12.309 1.00 23.53 ? 46 VAL A CG2 1 ATOM 54 N N . THR A 1 47 ? 32.141 -4.728 7.761 1.00 23.12 ? 47 THR A N 1 ATOM 55 C CA . THR A 1 47 ? 32.435 -3.775 6.700 1.00 23.06 ? 47 THR A CA 1 ATOM 56 C C . THR A 1 47 ? 31.153 -3.374 5.991 1.00 22.76 ? 47 THR A C 1 ATOM 57 O O . THR A 1 47 ? 30.055 -3.755 6.406 1.00 21.38 ? 47 THR A O 1 ATOM 58 C CB . THR A 1 47 ? 33.434 -4.385 5.699 1.00 23.36 ? 47 THR A CB 1 ATOM 59 O OG1 . THR A 1 47 ? 32.916 -5.618 5.200 1.00 23.22 ? 47 THR A OG1 1 ATOM 60 C CG2 . THR A 1 47 ? 34.778 -4.645 6.388 1.00 23.33 ? 47 THR A CG2 1 ATOM 61 N N . TRP A 1 48 ? 31.285 -2.591 4.927 1.00 23.12 ? 48 TRP A N 1 ATOM 62 C CA . TRP A 1 48 ? 30.117 -2.150 4.183 1.00 23.81 ? 48 TRP A CA 1 ATOM 63 C C . TRP A 1 48 ? 30.497 -1.649 2.797 1.00 23.85 ? 48 TRP A C 1 ATOM 64 O O . TRP A 1 48 ? 31.674 -1.453 2.494 1.00 22.79 ? 48 TRP A O 1 ATOM 65 C CB . TRP A 1 48 ? 29.415 -1.018 4.949 1.00 23.80 ? 48 TRP A CB 1 ATOM 66 C CG . TRP A 1 48 ? 30.237 0.231 5.035 1.00 23.88 ? 48 TRP A CG 1 ATOM 67 C CD1 . TRP A 1 48 ? 30.278 1.258 4.127 1.00 24.08 ? 48 TRP A CD1 1 ATOM 68 C CD2 . TRP A 1 48 ? 31.148 0.581 6.073 1.00 24.33 ? 48 TRP A CD2 1 ATOM 69 N NE1 . TRP A 1 48 ? 31.159 2.226 4.543 1.00 23.78 ? 48 TRP A NE1 1 ATOM 70 C CE2 . TRP A 1 48 ? 31.712 1.836 5.731 1.00 24.38 ? 48 TRP A CE2 1 ATOM 71 C CE3 . TRP A 1 48 ? 31.544 -0.037 7.266 1.00 24.16 ? 48 TRP A CE3 1 ATOM 72 C CZ2 . TRP A 1 48 ? 32.636 2.486 6.548 1.00 24.66 ? 48 TRP A CZ2 1 ATOM 73 C CZ3 . TRP A 1 48 ? 32.471 0.603 8.073 1.00 23.88 ? 48 TRP A CZ3 1 ATOM 74 C CH2 . TRP A 1 48 ? 33.006 1.854 7.711 1.00 24.46 ? 48 TRP A CH2 1 ATOM 75 N N . ASP A 1 49 ? 29.481 -1.437 1.968 1.00 24.51 ? 49 ASP A N 1 ATOM 76 C CA . ASP A 1 49 ? 29.642 -0.659 0.735 1.00 25.15 ? 49 ASP A CA 1 ATOM 77 C C . ASP A 1 49 ? 28.386 0.188 0.562 1.00 25.26 ? 49 ASP A C 1 ATOM 78 O O . ASP A 1 49 ? 27.686 0.445 1.548 1.00 24.91 ? 49 ASP A O 1 ATOM 79 C CB . ASP A 1 49 ? 29.963 -1.560 -0.465 1.00 24.65 ? 49 ASP A CB 1 ATOM 80 C CG . ASP A 1 49 ? 28.856 -2.541 -0.799 1.00 25.30 ? 49 ASP A CG 1 ATOM 81 O OD1 . ASP A 1 49 ? 27.747 -2.474 -0.224 1.00 24.06 ? 49 ASP A OD1 1 ATOM 82 O OD2 . ASP A 1 49 ? 29.110 -3.396 -1.674 1.00 26.31 -1 49 ASP A OD2 1 ATOM 83 N N . ASP A 1 50 ? 28.095 0.632 -0.655 1.00 25.04 ? 50 ASP A N 1 ATOM 84 C CA . ASP A 1 50 ? 26.941 1.508 -0.877 1.00 26.26 ? 50 ASP A CA 1 ATOM 85 C C . ASP A 1 50 ? 25.593 0.810 -0.664 1.00 25.60 ? 50 ASP A C 1 ATOM 86 O O . ASP A 1 50 ? 24.589 1.481 -0.455 1.00 25.35 ? 50 ASP A O 1 ATOM 87 C CB . ASP A 1 50 ? 26.993 2.150 -2.278 1.00 27.36 ? 50 ASP A CB 1 ATOM 88 C CG . ASP A 1 50 ? 26.954 1.125 -3.397 1.00 29.11 ? 50 ASP A CG 1 ATOM 89 O OD1 . ASP A 1 50 ? 27.647 0.095 -3.285 1.00 30.19 ? 50 ASP A OD1 1 ATOM 90 O OD2 . ASP A 1 50 ? 26.233 1.345 -4.395 1.00 33.08 -1 50 ASP A OD2 1 ATOM 91 N N . LYS A 1 51 ? 25.567 -0.525 -0.709 1.00 25.68 ? 51 LYS A N 1 ATOM 92 C CA . LYS A 1 51 ? 24.315 -1.279 -0.582 1.00 25.25 ? 51 LYS A CA 1 ATOM 93 C C . LYS A 1 51 ? 24.020 -1.818 0.830 1.00 24.03 ? 51 LYS A C 1 ATOM 94 O O . LYS A 1 51 ? 22.879 -1.765 1.287 1.00 23.59 ? 51 LYS A O 1 ATOM 95 C CB . LYS A 1 51 ? 24.313 -2.453 -1.565 1.00 27.14 ? 51 LYS A CB 1 ATOM 96 C CG . LYS A 1 51 ? 24.377 -2.071 -3.040 1.00 28.60 ? 51 LYS A CG 1 ATOM 97 C CD . LYS A 1 51 ? 23.057 -1.472 -3.486 1.00 31.08 ? 51 LYS A CD 1 ATOM 98 C CE . LYS A 1 51 ? 23.085 -0.950 -4.914 1.00 32.94 ? 51 LYS A CE 1 ATOM 99 N NZ . LYS A 1 51 ? 21.817 -0.205 -5.168 1.00 33.25 ? 51 LYS A NZ 1 ATOM 100 N N . SER A 1 52 ? 25.019 -2.376 1.505 1.00 22.29 ? 52 SER A N 1 ATOM 101 C CA . SER A 1 52 ? 24.744 -3.127 2.725 1.00 21.96 ? 52 SER A CA 1 ATOM 102 C C . SER A 1 52 ? 25.976 -3.329 3.556 1.00 21.75 ? 52 SER A C 1 ATOM 103 O O . SER A 1 52 ? 27.091 -3.147 3.077 1.00 21.99 ? 52 SER A O 1 ATOM 104 C CB . SER A 1 52 ? 24.171 -4.508 2.382 1.00 22.06 ? 52 SER A CB 1 ATOM 105 O OG . SER A 1 52 ? 25.214 -5.448 2.191 1.00 21.06 ? 52 SER A OG 1 ATOM 106 N N . LEU A 1 53 ? 25.751 -3.720 4.807 1.00 21.58 ? 53 LEU A N 1 ATOM 107 C CA . LEU A 1 53 ? 26.803 -4.219 5.661 1.00 21.80 ? 53 LEU A CA 1 ATOM 108 C C . LEU A 1 53 ? 27.241 -5.592 5.185 1.00 22.73 ? 53 LEU A C 1 ATOM 109 O O . LEU A 1 53 ? 26.440 -6.354 4.620 1.00 23.03 ? 53 LEU A O 1 ATOM 110 C CB . LEU A 1 53 ? 26.325 -4.382 7.102 1.00 21.79 ? 53 LEU A CB 1 ATOM 111 C CG . LEU A 1 53 ? 26.188 -3.190 8.051 1.00 21.91 ? 53 LEU A CG 1 ATOM 112 C CD1 . LEU A 1 53 ? 26.018 -3.727 9.466 1.00 21.72 ? 53 LEU A CD1 1 ATOM 113 C CD2 . LEU A 1 53 ? 27.366 -2.240 7.989 1.00 21.62 ? 53 LEU A CD2 1 ATOM 114 N N . PHE A 1 54 ? 28.509 -5.903 5.436 1.00 23.18 ? 54 PHE A N 1 ATOM 115 C CA . PHE A 1 54 ? 29.034 -7.256 5.299 1.00 23.91 ? 54 PHE A CA 1 ATOM 116 C C . PHE A 1 54 ? 29.433 -7.713 6.692 1.00 23.47 ? 54 PHE A C 1 ATOM 117 O O . PHE A 1 54 ? 30.097 -6.976 7.409 1.00 22.12 ? 54 PHE A O 1 ATOM 118 C CB . PHE A 1 54 ? 30.303 -7.277 4.435 1.00 25.05 ? 54 PHE A CB 1 ATOM 119 C CG . PHE A 1 54 ? 30.091 -6.970 2.972 1.00 24.82 ? 54 PHE A CG 1 ATOM 120 C CD1 . PHE A 1 54 ? 30.097 -5.658 2.514 1.00 25.30 ? 54 PHE A CD1 1 ATOM 121 C CD2 . PHE A 1 54 ? 29.976 -7.994 2.043 1.00 25.37 ? 54 PHE A CD2 1 ATOM 122 C CE1 . PHE A 1 54 ? 29.933 -5.369 1.162 1.00 25.24 ? 54 PHE A CE1 1 ATOM 123 C CE2 . PHE A 1 54 ? 29.808 -7.711 0.688 1.00 25.72 ? 54 PHE A CE2 1 ATOM 124 C CZ . PHE A 1 54 ? 29.784 -6.394 0.249 1.00 24.87 ? 54 PHE A CZ 1 ATOM 125 N N . ILE A 1 55 ? 29.052 -8.925 7.077 1.00 24.44 ? 55 ILE A N 1 ATOM 126 C CA . ILE A 1 55 ? 29.539 -9.513 8.324 1.00 25.12 ? 55 ILE A CA 1 ATOM 127 C C . ILE A 1 55 ? 30.314 -10.782 8.006 1.00 25.78 ? 55 ILE A C 1 ATOM 128 O O . ILE A 1 55 ? 29.736 -11.767 7.527 1.00 24.37 ? 55 ILE A O 1 ATOM 129 C CB . ILE A 1 55 ? 28.395 -9.798 9.315 1.00 25.79 ? 55 ILE A CB 1 ATOM 130 C CG1 . ILE A 1 55 ? 27.700 -8.472 9.655 1.00 26.81 ? 55 ILE A CG1 1 ATOM 131 C CG2 . ILE A 1 55 ? 28.928 -10.510 10.559 1.00 25.60 ? 55 ILE A CG2 1 ATOM 132 C CD1 . ILE A 1 55 ? 26.826 -8.479 10.893 1.00 27.45 ? 55 ILE A CD1 1 ATOM 133 N N . ASN A 1 56 ? 31.621 -10.739 8.279 1.00 26.89 ? 56 ASN A N 1 ATOM 134 C CA . ASN A 1 56 ? 32.549 -11.794 7.868 1.00 28.40 ? 56 ASN A CA 1 ATOM 135 C C . ASN A 1 56 ? 32.470 -12.057 6.358 1.00 28.27 ? 56 ASN A C 1 ATOM 136 O O . ASN A 1 56 ? 32.299 -13.194 5.926 1.00 28.21 ? 56 ASN A O 1 ATOM 137 C CB . ASN A 1 56 ? 32.295 -13.087 8.659 1.00 29.19 ? 56 ASN A CB 1 ATOM 138 C CG . ASN A 1 56 ? 32.673 -12.957 10.122 1.00 29.91 ? 56 ASN A CG 1 ATOM 139 O OD1 . ASN A 1 56 ? 33.815 -12.647 10.446 1.00 33.36 ? 56 ASN A OD1 1 ATOM 140 N ND2 . ASN A 1 56 ? 31.724 -13.202 11.009 1.00 29.36 ? 56 ASN A ND2 1 ATOM 141 N N . GLY A 1 57 ? 32.559 -10.982 5.573 1.00 28.66 ? 57 GLY A N 1 ATOM 142 C CA . GLY A 1 57 ? 32.557 -11.050 4.106 1.00 28.66 ? 57 GLY A CA 1 ATOM 143 C C . GLY A 1 57 ? 31.237 -11.333 3.396 1.00 29.23 ? 57 GLY A C 1 ATOM 144 O O . GLY A 1 57 ? 31.223 -11.506 2.180 1.00 30.30 ? 57 GLY A O 1 ATOM 145 N N . GLU A 1 58 ? 30.129 -11.377 4.126 1.00 29.49 ? 58 GLU A N 1 ATOM 146 C CA . GLU A 1 58 ? 28.847 -11.805 3.557 1.00 30.09 ? 58 GLU A CA 1 ATOM 147 C C . GLU A 1 58 ? 27.780 -10.743 3.817 1.00 27.23 ? 58 GLU A C 1 ATOM 148 O O . GLU A 1 58 ? 27.647 -10.277 4.935 1.00 27.03 ? 58 GLU A O 1 ATOM 149 C CB . GLU A 1 58 ? 28.427 -13.142 4.184 1.00 33.59 ? 58 GLU A CB 1 ATOM 150 C CG . GLU A 1 58 ? 29.358 -14.328 3.873 1.00 37.54 ? 58 GLU A CG 1 ATOM 151 C CD . GLU A 1 58 ? 28.950 -15.143 2.634 1.00 40.10 ? 58 GLU A CD 1 ATOM 152 O OE1 . GLU A 1 58 ? 28.104 -14.680 1.835 1.00 42.23 ? 58 GLU A OE1 1 ATOM 153 O OE2 . GLU A 1 58 ? 29.471 -16.269 2.464 1.00 42.06 -1 58 GLU A OE2 1 ATOM 154 N N . ARG A 1 59 ? 27.038 -10.346 2.789 1.00 25.60 ? 59 ARG A N 1 ATOM 155 C CA . ARG A 1 59 ? 26.008 -9.321 2.940 1.00 25.07 ? 59 ARG A CA 1 ATOM 156 C C . ARG A 1 59 ? 24.932 -9.767 3.910 1.00 25.06 ? 59 ARG A C 1 ATOM 157 O O . ARG A 1 59 ? 24.540 -10.919 3.919 1.00 25.08 ? 59 ARG A O 1 ATOM 158 C CB . ARG A 1 59 ? 25.313 -9.018 1.612 1.00 24.75 ? 59 ARG A CB 1 ATOM 159 C CG . ARG A 1 59 ? 26.188 -8.349 0.573 1.00 24.62 ? 59 ARG A CG 1 ATOM 160 C CD . ARG A 1 59 ? 25.349 -7.830 -0.570 1.00 24.12 ? 59 ARG A CD 1 ATOM 161 N NE . ARG A 1 59 ? 26.195 -7.216 -1.590 1.00 24.86 ? 59 ARG A NE 1 ATOM 162 C CZ . ARG A 1 59 ? 26.725 -5.998 -1.514 1.00 24.66 ? 59 ARG A CZ 1 ATOM 163 N NH1 . ARG A 1 59 ? 26.507 -5.206 -0.462 1.00 24.98 ? 59 ARG A NH1 1 ATOM 164 N NH2 . ARG A 1 59 ? 27.482 -5.566 -2.506 1.00 24.85 ? 59 ARG A NH2 1 ATOM 165 N N . ILE A 1 60 ? 24.446 -8.833 4.715 1.00 25.06 ? 60 ILE A N 1 ATOM 166 C CA . ILE A 1 60 ? 23.301 -9.082 5.552 1.00 23.62 ? 60 ILE A CA 1 ATOM 167 C C . ILE A 1 60 ? 22.445 -7.832 5.609 1.00 22.60 ? 60 ILE A C 1 ATOM 168 O O . ILE A 1 60 ? 22.970 -6.718 5.647 1.00 23.39 ? 60 ILE A O 1 ATOM 169 C CB . ILE A 1 60 ? 23.734 -9.509 6.966 1.00 24.39 ? 60 ILE A CB 1 ATOM 170 C CG1 . ILE A 1 60 ? 22.514 -9.855 7.825 1.00 24.61 ? 60 ILE A CG1 1 ATOM 171 C CG2 . ILE A 1 60 ? 24.567 -8.425 7.636 1.00 25.29 ? 60 ILE A CG2 1 ATOM 172 C CD1 . ILE A 1 60 ? 22.841 -10.702 9.032 1.00 24.83 ? 60 ILE A CD1 1 ATOM 173 N N . MET A 1 61 ? 21.133 -8.038 5.578 1.00 21.60 ? 61 MET A N 1 ATOM 174 C CA . MET A 1 61 ? 20.135 -7.012 5.877 1.00 22.15 ? 61 MET A CA 1 ATOM 175 C C . MET A 1 61 ? 19.898 -6.978 7.400 1.00 21.66 ? 61 MET A C 1 ATOM 176 O O . MET A 1 61 ? 19.369 -7.941 7.972 1.00 20.91 ? 61 MET A O 1 ATOM 177 C CB . MET A 1 61 ? 18.834 -7.375 5.154 1.00 23.29 ? 61 MET A CB 1 ATOM 178 C CG . MET A 1 61 ? 17.856 -6.234 4.920 1.00 25.22 ? 61 MET A CG 1 ATOM 179 S SD . MET A 1 61 ? 16.883 -5.660 6.331 1.00 26.71 ? 61 MET A SD 1 ATOM 180 C CE . MET A 1 61 ? 16.309 -7.183 7.005 1.00 27.95 ? 61 MET A CE 1 ATOM 181 N N . ILE A 1 62 ? 20.269 -5.896 8.054 1.00 20.26 ? 62 ILE A N 1 ATOM 182 C CA . ILE A 1 62 ? 20.043 -5.734 9.480 1.00 19.93 ? 62 ILE A CA 1 ATOM 183 C C . ILE A 1 62 ? 18.585 -5.305 9.772 1.00 19.43 ? 62 ILE A C 1 ATOM 184 O O . ILE A 1 62 ? 18.156 -4.260 9.426 1.00 18.84 ? 62 ILE A O 1 ATOM 185 C CB . ILE A 1 62 ? 21.050 -4.728 10.109 1.00 19.99 ? 62 ILE A CB 1 ATOM 186 C CG1 . ILE A 1 62 ? 22.506 -5.222 10.060 1.00 20.06 ? 62 ILE A CG1 1 ATOM 187 C CG2 . ILE A 1 62 ? 20.718 -4.398 11.524 1.00 20.14 ? 62 ILE A CG2 1 ATOM 188 C CD1 . ILE A 1 62 ? 22.790 -6.597 10.594 1.00 19.49 ? 62 ILE A CD1 1 ATOM 189 N N . PHE A 1 63 ? 17.827 -6.167 10.394 1.00 18.90 ? 63 PHE A N 1 ATOM 190 C CA . PHE A 1 63 ? 16.463 -5.877 10.777 1.00 18.78 ? 63 PHE A CA 1 ATOM 191 C C . PHE A 1 63 ? 16.522 -6.009 12.316 1.00 18.45 ? 63 PHE A C 1 ATOM 192 O O . PHE A 1 63 ? 16.775 -7.039 12.842 1.00 18.79 ? 63 PHE A O 1 ATOM 193 C CB . PHE A 1 63 ? 15.475 -6.809 10.096 1.00 19.25 ? 63 PHE A CB 1 ATOM 194 C CG . PHE A 1 63 ? 14.121 -6.204 9.820 1.00 19.42 ? 63 PHE A CG 1 ATOM 195 C CD1 . PHE A 1 63 ? 13.666 -5.121 10.511 1.00 19.96 ? 63 PHE A CD1 1 ATOM 196 C CD2 . PHE A 1 63 ? 13.312 -6.731 8.863 1.00 19.41 ? 63 PHE A CD2 1 ATOM 197 C CE1 . PHE A 1 63 ? 12.440 -4.569 10.251 1.00 20.38 ? 63 PHE A CE1 1 ATOM 198 C CE2 . PHE A 1 63 ? 12.084 -6.204 8.628 1.00 19.91 ? 63 PHE A CE2 1 ATOM 199 C CZ . PHE A 1 63 ? 11.644 -5.118 9.311 1.00 19.76 ? 63 PHE A CZ 1 ATOM 200 N N . SER A 1 64 ? 16.332 -4.903 12.981 1.00 18.02 ? 64 SER A N 1 ATOM 201 C CA . SER A 1 64 ? 16.496 -4.747 14.387 1.00 18.11 ? 64 SER A CA 1 ATOM 202 C C . SER A 1 64 ? 15.327 -4.202 15.170 1.00 18.85 ? 64 SER A C 1 ATOM 203 O O . SER A 1 64 ? 14.446 -3.617 14.644 1.00 19.32 ? 64 SER A O 1 ATOM 204 C CB . SER A 1 64 ? 17.750 -3.886 14.613 1.00 18.28 ? 64 SER A CB 1 ATOM 205 O OG . SER A 1 64 ? 17.994 -3.590 15.920 1.00 18.15 ? 64 SER A OG 1 ATOM 206 N N . GLY A 1 65 ? 15.375 -4.411 16.472 1.00 19.12 ? 65 GLY A N 1 ATOM 207 C CA . GLY A 1 65 ? 14.341 -3.947 17.398 1.00 19.32 ? 65 GLY A CA 1 ATOM 208 C C . GLY A 1 65 ? 14.953 -3.296 18.626 1.00 19.09 ? 65 GLY A C 1 ATOM 209 O O . GLY A 1 65 ? 15.948 -3.793 19.170 1.00 19.42 ? 65 GLY A O 1 ATOM 210 N N . GLU A 1 66 ? 14.369 -2.176 19.055 1.00 19.40 ? 66 GLU A N 1 ATOM 211 C CA . GLU A 1 66 ? 14.836 -1.449 20.246 1.00 19.08 ? 66 GLU A CA 1 ATOM 212 C C . GLU A 1 66 ? 14.336 -2.098 21.530 1.00 18.37 ? 66 GLU A C 1 ATOM 213 O O . GLU A 1 66 ? 13.131 -2.321 21.701 1.00 17.70 ? 66 GLU A O 1 ATOM 214 C CB . GLU A 1 66 ? 14.374 0.003 20.222 1.00 19.83 ? 66 GLU A CB 1 ATOM 215 C CG . GLU A 1 66 ? 15.083 0.900 21.239 1.00 20.80 ? 66 GLU A CG 1 ATOM 216 C CD . GLU A 1 66 ? 16.435 1.422 20.776 1.00 21.87 ? 66 GLU A CD 1 ATOM 217 O OE1 . GLU A 1 66 ? 16.804 1.204 19.601 1.00 22.66 ? 66 GLU A OE1 1 ATOM 218 O OE2 . GLU A 1 66 ? 17.131 2.076 21.596 1.00 23.36 -1 66 GLU A OE2 1 ATOM 219 N N . PHE A 1 67 ? 15.273 -2.352 22.440 1.00 17.64 ? 67 PHE A N 1 ATOM 220 C CA . PHE A 1 67 ? 15.004 -3.019 23.715 1.00 17.37 ? 67 PHE A CA 1 ATOM 221 C C . PHE A 1 67 ? 15.968 -2.408 24.718 1.00 16.94 ? 67 PHE A C 1 ATOM 222 O O . PHE A 1 67 ? 17.184 -2.413 24.485 1.00 17.17 ? 67 PHE A O 1 ATOM 223 C CB . PHE A 1 67 ? 15.207 -4.535 23.530 1.00 17.50 ? 67 PHE A CB 1 ATOM 224 C CG . PHE A 1 67 ? 15.252 -5.350 24.801 1.00 17.06 ? 67 PHE A CG 1 ATOM 225 C CD1 . PHE A 1 67 ? 14.691 -4.909 25.989 1.00 17.69 ? 67 PHE A CD1 1 ATOM 226 C CD2 . PHE A 1 67 ? 15.811 -6.607 24.768 1.00 16.63 ? 67 PHE A CD2 1 ATOM 227 C CE1 . PHE A 1 67 ? 14.733 -5.694 27.126 1.00 17.53 ? 67 PHE A CE1 1 ATOM 228 C CE2 . PHE A 1 67 ? 15.852 -7.397 25.888 1.00 17.10 ? 67 PHE A CE2 1 ATOM 229 C CZ . PHE A 1 67 ? 15.321 -6.939 27.076 1.00 17.39 ? 67 PHE A CZ 1 ATOM 230 N N . HIS A 1 68 ? 15.426 -1.833 25.792 1.00 16.53 ? 68 HIS A N 1 ATOM 231 C CA . HIS A 1 68 ? 16.243 -1.180 26.817 1.00 17.16 ? 68 HIS A CA 1 ATOM 232 C C . HIS A 1 68 ? 16.395 -2.031 28.077 1.00 17.14 ? 68 HIS A C 1 ATOM 233 O O . HIS A 1 68 ? 15.410 -2.285 28.767 1.00 18.16 ? 68 HIS A O 1 ATOM 234 C CB . HIS A 1 68 ? 15.675 0.180 27.190 1.00 17.14 ? 68 HIS A CB 1 ATOM 235 C CG . HIS A 1 68 ? 15.560 1.113 26.033 1.00 17.19 ? 68 HIS A CG 1 ATOM 236 N ND1 . HIS A 1 68 ? 14.718 2.198 26.043 1.00 17.27 ? 68 HIS A ND1 1 ATOM 237 C CD2 . HIS A 1 68 ? 16.163 1.117 24.823 1.00 17.56 ? 68 HIS A CD2 1 ATOM 238 C CE1 . HIS A 1 68 ? 14.812 2.843 24.896 1.00 17.49 ? 68 HIS A CE1 1 ATOM 239 N NE2 . HIS A 1 68 ? 15.682 2.206 24.136 1.00 17.90 ? 68 HIS A NE2 1 ATOM 240 N N . PRO A 1 69 ? 17.635 -2.443 28.394 1.00 16.72 ? 69 PRO A N 1 ATOM 241 C CA . PRO A 1 69 ? 17.894 -3.380 29.493 1.00 16.90 ? 69 PRO A CA 1 ATOM 242 C C . PRO A 1 69 ? 17.445 -2.861 30.860 1.00 16.63 ? 69 PRO A C 1 ATOM 243 O O . PRO A 1 69 ? 16.997 -3.637 31.698 1.00 16.75 ? 69 PRO A O 1 ATOM 244 C CB . PRO A 1 69 ? 19.423 -3.557 29.457 1.00 16.99 ? 69 PRO A CB 1 ATOM 245 C CG . PRO A 1 69 ? 19.942 -2.331 28.772 1.00 17.10 ? 69 PRO A CG 1 ATOM 246 C CD . PRO A 1 69 ? 18.882 -1.959 27.775 1.00 16.74 ? 69 PRO A CD 1 ATOM 247 N N . PHE A 1 70 ? 17.547 -1.549 31.060 1.00 16.90 ? 70 PHE A N 1 ATOM 248 C CA . PHE A 1 70 ? 17.110 -0.908 32.302 1.00 16.38 ? 70 PHE A CA 1 ATOM 249 C C . PHE A 1 70 ? 15.574 -0.859 32.484 1.00 16.66 ? 70 PHE A C 1 ATOM 250 O O . PHE A 1 70 ? 15.097 -0.544 33.579 1.00 17.08 ? 70 PHE A O 1 ATOM 251 C CB . PHE A 1 70 ? 17.727 0.493 32.420 1.00 16.51 ? 70 PHE A CB 1 ATOM 252 C CG . PHE A 1 70 ? 17.352 1.439 31.296 1.00 16.31 ? 70 PHE A CG 1 ATOM 253 C CD1 . PHE A 1 70 ? 16.161 2.166 31.340 1.00 16.14 ? 70 PHE A CD1 1 ATOM 254 C CD2 . PHE A 1 70 ? 18.196 1.613 30.202 1.00 15.80 ? 70 PHE A CD2 1 ATOM 255 C CE1 . PHE A 1 70 ? 15.827 3.042 30.313 1.00 15.87 ? 70 PHE A CE1 1 ATOM 256 C CE2 . PHE A 1 70 ? 17.859 2.473 29.176 1.00 15.59 ? 70 PHE A CE2 1 ATOM 257 C CZ . PHE A 1 70 ? 16.676 3.192 29.228 1.00 15.56 ? 70 PHE A CZ 1 ATOM 258 N N . ARG A 1 71 ? 14.802 -1.174 31.436 1.00 16.41 ? 71 ARG A N 1 ATOM 259 C CA . ARG A 1 71 ? 13.348 -1.223 31.554 1.00 16.41 ? 71 ARG A CA 1 ATOM 260 C C . ARG A 1 71 ? 12.798 -2.651 31.766 1.00 17.24 ? 71 ARG A C 1 ATOM 261 O O . ARG A 1 71 ? 11.576 -2.849 31.777 1.00 17.12 ? 71 ARG A O 1 ATOM 262 C CB . ARG A 1 71 ? 12.691 -0.522 30.362 1.00 15.92 ? 71 ARG A CB 1 ATOM 263 C CG . ARG A 1 71 ? 12.615 0.996 30.535 1.00 15.70 ? 71 ARG A CG 1 ATOM 264 C CD . ARG A 1 71 ? 12.384 1.752 29.232 1.00 15.43 ? 71 ARG A CD 1 ATOM 265 N NE . ARG A 1 71 ? 11.937 3.116 29.517 1.00 15.16 ? 71 ARG A NE 1 ATOM 266 C CZ . ARG A 1 71 ? 12.231 4.207 28.809 1.00 15.17 ? 71 ARG A CZ 1 ATOM 267 N NH1 . ARG A 1 71 ? 13.032 4.152 27.754 1.00 15.08 ? 71 ARG A NH1 1 ATOM 268 N NH2 . ARG A 1 71 ? 11.751 5.396 29.187 1.00 15.00 ? 71 ARG A NH2 1 ATOM 269 N N . LEU A 1 72 ? 13.701 -3.621 31.953 1.00 17.83 ? 72 LEU A N 1 ATOM 270 C CA . LEU A 1 72 ? 13.341 -5.019 32.234 1.00 18.80 ? 72 LEU A CA 1 ATOM 271 C C . LEU A 1 72 ? 14.520 -5.704 32.941 1.00 19.14 ? 72 LEU A C 1 ATOM 272 O O . LEU A 1 72 ? 15.282 -6.468 32.334 1.00 19.19 ? 72 LEU A O 1 ATOM 273 C CB . LEU A 1 72 ? 12.943 -5.769 30.948 1.00 19.14 ? 72 LEU A CB 1 ATOM 274 C CG . LEU A 1 72 ? 12.379 -7.184 31.150 1.00 19.79 ? 72 LEU A CG 1 ATOM 275 C CD1 . LEU A 1 72 ? 11.029 -7.119 31.858 1.00 19.86 ? 72 LEU A CD1 1 ATOM 276 C CD2 . LEU A 1 72 ? 12.251 -7.948 29.840 1.00 19.68 ? 72 LEU A CD2 1 ATOM 277 N N . PRO A 1 73 ? 14.680 -5.421 34.239 1.00 19.85 ? 73 PRO A N 1 ATOM 278 C CA . PRO A 1 73 ? 15.910 -5.786 34.933 1.00 20.41 ? 73 PRO A CA 1 ATOM 279 C C . PRO A 1 73 ? 15.845 -7.178 35.577 1.00 20.18 ? 73 PRO A C 1 ATOM 280 O O . PRO A 1 73 ? 16.144 -7.326 36.753 1.00 19.40 ? 73 PRO A O 1 ATOM 281 C CB . PRO A 1 73 ? 16.023 -4.677 35.983 1.00 20.32 ? 73 PRO A CB 1 ATOM 282 C CG . PRO A 1 73 ? 14.602 -4.430 36.357 1.00 20.35 ? 73 PRO A CG 1 ATOM 283 C CD . PRO A 1 73 ? 13.819 -4.569 35.080 1.00 20.08 ? 73 PRO A CD 1 ATOM 284 N N . VAL A 1 74 ? 15.450 -8.177 34.790 1.00 20.39 ? 74 VAL A N 1 ATOM 285 C CA . VAL A 1 74 ? 15.436 -9.573 35.210 1.00 21.09 ? 74 VAL A CA 1 ATOM 286 C C . VAL A 1 74 ? 16.064 -10.340 34.058 1.00 22.89 ? 74 VAL A C 1 ATOM 287 O O . VAL A 1 74 ? 15.524 -10.345 32.953 1.00 21.52 ? 74 VAL A O 1 ATOM 288 C CB . VAL A 1 74 ? 13.997 -10.100 35.424 1.00 20.76 ? 74 VAL A CB 1 ATOM 289 C CG1 . VAL A 1 74 ? 14.031 -11.518 35.977 1.00 20.87 ? 74 VAL A CG1 1 ATOM 290 C CG2 . VAL A 1 74 ? 13.186 -9.178 36.330 1.00 20.46 ? 74 VAL A CG2 1 ATOM 291 N N . LYS A 1 75 ? 17.200 -10.983 34.292 1.00 25.73 ? 75 LYS A N 1 ATOM 292 C CA . LYS A 1 75 ? 18.001 -11.474 33.162 1.00 28.38 ? 75 LYS A CA 1 ATOM 293 C C . LYS A 1 75 ? 17.331 -12.591 32.348 1.00 26.88 ? 75 LYS A C 1 ATOM 294 O O . LYS A 1 75 ? 17.494 -12.659 31.129 1.00 26.68 ? 75 LYS A O 1 ATOM 295 C CB . LYS A 1 75 ? 19.428 -11.840 33.597 1.00 31.29 ? 75 LYS A CB 1 ATOM 296 C CG . LYS A 1 75 ? 19.543 -12.978 34.588 1.00 34.05 ? 75 LYS A CG 1 ATOM 297 C CD . LYS A 1 75 ? 20.733 -12.770 35.503 1.00 36.41 ? 75 LYS A CD 1 ATOM 298 C CE . LYS A 1 75 ? 20.913 -13.971 36.415 1.00 39.45 ? 75 LYS A CE 1 ATOM 299 N NZ . LYS A 1 75 ? 22.081 -13.797 37.317 1.00 41.41 ? 75 LYS A NZ 1 ATOM 300 N N . GLU A 1 76 ? 16.528 -13.423 32.993 1.00 25.81 ? 76 GLU A N 1 ATOM 301 C CA . GLU A 1 76 ? 15.858 -14.507 32.279 1.00 25.92 ? 76 GLU A CA 1 ATOM 302 C C . GLU A 1 76 ? 14.758 -13.981 31.335 1.00 23.72 ? 76 GLU A C 1 ATOM 303 O O . GLU A 1 76 ? 14.486 -14.574 30.283 1.00 21.48 ? 76 GLU A O 1 ATOM 304 C CB . GLU A 1 76 ? 15.280 -15.537 33.256 1.00 28.29 ? 76 GLU A CB 1 ATOM 305 C CG . GLU A 1 76 ? 16.318 -16.180 34.177 1.00 30.72 ? 76 GLU A CG 1 ATOM 306 C CD . GLU A 1 76 ? 16.693 -15.337 35.406 1.00 32.11 ? 76 GLU A CD 1 ATOM 307 O OE1 . GLU A 1 76 ? 16.100 -14.254 35.646 1.00 31.61 ? 76 GLU A OE1 1 ATOM 308 O OE2 . GLU A 1 76 ? 17.604 -15.773 36.143 1.00 35.47 -1 76 GLU A OE2 1 ATOM 309 N N . LEU A 1 77 ? 14.127 -12.869 31.714 1.00 21.13 ? 77 LEU A N 1 ATOM 310 C CA . LEU A 1 77 ? 13.126 -12.255 30.858 1.00 20.04 ? 77 LEU A CA 1 ATOM 311 C C . LEU A 1 77 ? 13.770 -11.461 29.736 1.00 19.44 ? 77 LEU A C 1 ATOM 312 O O . LEU A 1 77 ? 13.152 -11.283 28.688 1.00 20.10 ? 77 LEU A O 1 ATOM 313 C CB . LEU A 1 77 ? 12.159 -11.387 31.666 1.00 19.56 ? 77 LEU A CB 1 ATOM 314 C CG . LEU A 1 77 ? 11.452 -12.135 32.812 1.00 18.81 ? 77 LEU A CG 1 ATOM 315 C CD1 . LEU A 1 77 ? 10.495 -11.191 33.513 1.00 18.51 ? 77 LEU A CD1 1 ATOM 316 C CD2 . LEU A 1 77 ? 10.749 -13.394 32.315 1.00 18.14 ? 77 LEU A CD2 1 ATOM 317 N N . GLN A 1 78 ? 14.999 -10.987 29.932 1.00 18.56 ? 78 GLN A N 1 ATOM 318 C CA . GLN A 1 78 ? 15.744 -10.355 28.832 1.00 18.80 ? 78 GLN A CA 1 ATOM 319 C C . GLN A 1 78 ? 15.971 -11.372 27.710 1.00 18.47 ? 78 GLN A C 1 ATOM 320 O O . GLN A 1 78 ? 15.741 -11.075 26.528 1.00 18.25 ? 78 GLN A O 1 ATOM 321 C CB . GLN A 1 78 ? 17.070 -9.739 29.317 1.00 18.53 ? 78 GLN A CB 1 ATOM 322 C CG . GLN A 1 78 ? 16.858 -8.525 30.207 1.00 18.98 ? 78 GLN A CG 1 ATOM 323 C CD . GLN A 1 78 ? 18.109 -8.025 30.914 1.00 18.91 ? 78 GLN A CD 1 ATOM 324 O OE1 . GLN A 1 78 ? 19.148 -8.669 30.899 1.00 19.21 ? 78 GLN A OE1 1 ATOM 325 N NE2 . GLN A 1 78 ? 18.000 -6.855 31.545 1.00 18.90 ? 78 GLN A NE2 1 ATOM 326 N N . LEU A 1 79 ? 16.399 -12.573 28.090 1.00 18.17 ? 79 LEU A N 1 ATOM 327 C CA . LEU A 1 79 ? 16.539 -13.666 27.139 1.00 18.27 ? 79 LEU A CA 1 ATOM 328 C C . LEU A 1 79 ? 15.233 -13.943 26.404 1.00 18.28 ? 79 LEU A C 1 ATOM 329 O O . LEU A 1 79 ? 15.241 -14.184 25.196 1.00 18.61 ? 79 LEU A O 1 ATOM 330 C CB . LEU A 1 79 ? 16.997 -14.939 27.838 1.00 18.37 ? 79 LEU A CB 1 ATOM 331 C CG . LEU A 1 79 ? 17.069 -16.185 26.957 1.00 18.70 ? 79 LEU A CG 1 ATOM 332 C CD1 . LEU A 1 79 ? 18.094 -15.997 25.849 1.00 19.00 ? 79 LEU A CD1 1 ATOM 333 C CD2 . LEU A 1 79 ? 17.412 -17.399 27.814 1.00 19.42 ? 79 LEU A CD2 1 ATOM 334 N N . ASP A 1 80 ? 14.118 -13.924 27.129 1.00 17.91 ? 80 ASP A N 1 ATOM 335 C CA . ASP A 1 80 ? 12.796 -14.121 26.518 1.00 18.06 ? 80 ASP A CA 1 ATOM 336 C C . ASP A 1 80 ? 12.544 -13.129 25.375 1.00 17.79 ? 80 ASP A C 1 ATOM 337 O O . ASP A 1 80 ? 12.074 -13.515 24.298 1.00 17.47 ? 80 ASP A O 1 ATOM 338 C CB . ASP A 1 80 ? 11.703 -13.959 27.563 1.00 18.59 ? 80 ASP A CB 1 ATOM 339 C CG . ASP A 1 80 ? 10.317 -14.111 26.985 1.00 19.70 ? 80 ASP A CG 1 ATOM 340 O OD1 . ASP A 1 80 ? 10.031 -15.136 26.322 1.00 20.49 ? 80 ASP A OD1 1 ATOM 341 O OD2 . ASP A 1 80 ? 9.498 -13.201 27.210 1.00 20.22 -1 80 ASP A OD2 1 ATOM 342 N N . ILE A 1 81 ? 12.856 -11.857 25.613 1.00 16.75 ? 81 ILE A N 1 ATOM 343 C CA . ILE A 1 81 ? 12.637 -10.838 24.595 1.00 16.31 ? 81 ILE A CA 1 ATOM 344 C C . ILE A 1 81 ? 13.508 -11.169 23.391 1.00 16.15 ? 81 ILE A C 1 ATOM 345 O O . ILE A 1 81 ? 13.015 -11.175 22.265 1.00 16.45 ? 81 ILE A O 1 ATOM 346 C CB . ILE A 1 81 ? 12.934 -9.393 25.096 1.00 15.91 ? 81 ILE A CB 1 ATOM 347 C CG1 . ILE A 1 81 ? 12.075 -9.044 26.310 1.00 15.76 ? 81 ILE A CG1 1 ATOM 348 C CG2 . ILE A 1 81 ? 12.701 -8.373 23.987 1.00 15.38 ? 81 ILE A CG2 1 ATOM 349 C CD1 . ILE A 1 81 ? 10.597 -9.265 26.097 1.00 16.11 ? 81 ILE A CD1 1 ATOM 350 N N . PHE A 1 82 ? 14.788 -11.461 23.625 1.00 16.39 ? 82 PHE A N 1 ATOM 351 C CA . PHE A 1 82 ? 15.705 -11.774 22.523 1.00 16.61 ? 82 PHE A CA 1 ATOM 352 C C . PHE A 1 82 ? 15.217 -12.947 21.691 1.00 16.35 ? 82 PHE A C 1 ATOM 353 O O . PHE A 1 82 ? 15.342 -12.937 20.472 1.00 16.09 ? 82 PHE A O 1 ATOM 354 C CB . PHE A 1 82 ? 17.136 -12.061 23.011 1.00 16.68 ? 82 PHE A CB 1 ATOM 355 C CG . PHE A 1 82 ? 17.899 -10.837 23.409 1.00 17.20 ? 82 PHE A CG 1 ATOM 356 C CD1 . PHE A 1 82 ? 18.083 -9.794 22.510 1.00 18.07 ? 82 PHE A CD1 1 ATOM 357 C CD2 . PHE A 1 82 ? 18.431 -10.719 24.669 1.00 17.75 ? 82 PHE A CD2 1 ATOM 358 C CE1 . PHE A 1 82 ? 18.782 -8.654 22.872 1.00 17.92 ? 82 PHE A CE1 1 ATOM 359 C CE2 . PHE A 1 82 ? 19.132 -9.581 25.042 1.00 18.41 ? 82 PHE A CE2 1 ATOM 360 C CZ . PHE A 1 82 ? 19.304 -8.544 24.142 1.00 18.22 ? 82 PHE A CZ 1 ATOM 361 N N . GLN A 1 83 ? 14.663 -13.956 22.344 1.00 16.27 ? 83 GLN A N 1 ATOM 362 C CA . GLN A 1 83 ? 14.146 -15.107 21.618 1.00 16.81 ? 83 GLN A CA 1 ATOM 363 C C . GLN A 1 83 ? 12.875 -14.767 20.820 1.00 16.85 ? 83 GLN A C 1 ATOM 364 O O . GLN A 1 83 ? 12.688 -15.259 19.706 1.00 16.48 ? 83 GLN A O 1 ATOM 365 C CB . GLN A 1 83 ? 13.899 -16.277 22.567 1.00 16.96 ? 83 GLN A CB 1 ATOM 366 C CG . GLN A 1 83 ? 15.178 -16.902 23.087 1.00 17.16 ? 83 GLN A CG 1 ATOM 367 C CD . GLN A 1 83 ? 14.905 -18.070 24.014 1.00 17.65 ? 83 GLN A CD 1 ATOM 368 O OE1 . GLN A 1 83 ? 13.927 -18.064 24.779 1.00 17.53 ? 83 GLN A OE1 1 ATOM 369 N NE2 . GLN A 1 83 ? 15.775 -19.076 23.964 1.00 17.41 ? 83 GLN A NE2 1 ATOM 370 N N . LYS A 1 84 ? 12.017 -13.924 21.375 1.00 16.74 ? 84 LYS A N 1 ATOM 371 C CA . LYS A 1 84 ? 10.843 -13.475 20.633 1.00 17.35 ? 84 LYS A CA 1 ATOM 372 C C . LYS A 1 84 ? 11.203 -12.615 19.403 1.00 17.59 ? 84 LYS A C 1 ATOM 373 O O . LYS A 1 84 ? 10.481 -12.632 18.391 1.00 16.50 ? 84 LYS A O 1 ATOM 374 C CB . LYS A 1 84 ? 9.866 -12.773 21.578 1.00 17.76 ? 84 LYS A CB 1 ATOM 375 C CG . LYS A 1 84 ? 9.180 -13.788 22.486 1.00 18.50 ? 84 LYS A CG 1 ATOM 376 C CD . LYS A 1 84 ? 8.502 -13.209 23.719 1.00 19.15 ? 84 LYS A CD 1 ATOM 377 C CE . LYS A 1 84 ? 7.513 -14.237 24.273 1.00 19.50 ? 84 LYS A CE 1 ATOM 378 N NZ . LYS A 1 84 ? 7.135 -14.006 25.695 1.00 20.05 ? 84 LYS A NZ 1 ATOM 379 N N . VAL A 1 85 ? 12.318 -11.879 19.487 1.00 17.75 ? 85 VAL A N 1 ATOM 380 C CA . VAL A 1 85 ? 12.772 -11.036 18.378 1.00 17.93 ? 85 VAL A CA 1 ATOM 381 C C . VAL A 1 85 ? 13.376 -11.878 17.258 1.00 17.76 ? 85 VAL A C 1 ATOM 382 O O . VAL A 1 85 ? 13.130 -11.618 16.083 1.00 18.00 ? 85 VAL A O 1 ATOM 383 C CB . VAL A 1 85 ? 13.789 -9.964 18.837 1.00 18.30 ? 85 VAL A CB 1 ATOM 384 C CG1 . VAL A 1 85 ? 14.423 -9.252 17.642 1.00 18.71 ? 85 VAL A CG1 1 ATOM 385 C CG2 . VAL A 1 85 ? 13.112 -8.942 19.729 1.00 18.68 ? 85 VAL A CG2 1 ATOM 386 N N . LYS A 1 86 ? 14.175 -12.870 17.628 1.00 18.11 ? 86 LYS A N 1 ATOM 387 C CA . LYS A 1 86 ? 14.738 -13.851 16.681 1.00 18.16 ? 86 LYS A CA 1 ATOM 388 C C . LYS A 1 86 ? 13.623 -14.596 15.916 1.00 17.46 ? 86 LYS A C 1 ATOM 389 O O . LYS A 1 86 ? 13.737 -14.875 14.702 1.00 17.35 ? 86 LYS A O 1 ATOM 390 C CB . LYS A 1 86 ? 15.602 -14.858 17.465 1.00 18.94 ? 86 LYS A CB 1 ATOM 391 C CG . LYS A 1 86 ? 16.333 -15.903 16.629 1.00 19.31 ? 86 LYS A CG 1 ATOM 392 C CD . LYS A 1 86 ? 17.544 -15.283 15.950 1.00 19.88 ? 86 LYS A CD 1 ATOM 393 C CE . LYS A 1 86 ? 18.451 -16.336 15.334 1.00 19.82 ? 86 LYS A CE 1 ATOM 394 N NZ . LYS A 1 86 ? 19.666 -15.686 14.785 1.00 19.65 ? 86 LYS A NZ 1 ATOM 395 N N . ALA A 1 87 ? 12.540 -14.922 16.615 1.00 16.57 ? 87 ALA A N 1 ATOM 396 C CA . ALA A 1 87 ? 11.388 -15.595 15.970 1.00 16.40 ? 87 ALA A CA 1 ATOM 397 C C . ALA A 1 87 ? 10.640 -14.711 14.948 1.00 15.90 ? 87 ALA A C 1 ATOM 398 O O . ALA A 1 87 ? 9.877 -15.219 14.118 1.00 15.82 ? 87 ALA A O 1 ATOM 399 C CB . ALA A 1 87 ? 10.424 -16.115 17.022 1.00 16.30 ? 87 ALA A CB 1 ATOM 400 N N . LEU A 1 88 ? 10.855 -13.396 15.005 1.00 15.48 ? 88 LEU A N 1 ATOM 401 C CA . LEU A 1 88 ? 10.366 -12.490 13.958 1.00 15.62 ? 88 LEU A CA 1 ATOM 402 C C . LEU A 1 88 ? 11.132 -12.603 12.646 1.00 15.38 ? 88 LEU A C 1 ATOM 403 O O . LEU A 1 88 ? 10.699 -12.043 11.648 1.00 16.21 ? 88 LEU A O 1 ATOM 404 C CB . LEU A 1 88 ? 10.437 -11.019 14.417 1.00 15.74 ? 88 LEU A CB 1 ATOM 405 C CG . LEU A 1 88 ? 9.466 -10.551 15.487 1.00 15.85 ? 88 LEU A CG 1 ATOM 406 C CD1 . LEU A 1 88 ? 9.930 -9.214 16.056 1.00 16.43 ? 88 LEU A CD1 1 ATOM 407 C CD2 . LEU A 1 88 ? 8.059 -10.438 14.928 1.00 15.64 ? 88 LEU A CD2 1 ATOM 408 N N . GLY A 1 89 ? 12.290 -13.267 12.658 1.00 15.52 ? 89 GLY A N 1 ATOM 409 C CA . GLY A 1 89 ? 13.215 -13.252 11.529 1.00 14.99 ? 89 GLY A CA 1 ATOM 410 C C . GLY A 1 89 ? 14.271 -12.178 11.667 1.00 15.29 ? 89 GLY A C 1 ATOM 411 O O . GLY A 1 89 ? 15.123 -12.024 10.783 1.00 14.45 ? 89 GLY A O 1 ATOM 412 N N . PHE A 1 90 ? 14.241 -11.444 12.786 1.00 15.51 ? 90 PHE A N 1 ATOM 413 C CA . PHE A 1 90 ? 15.231 -10.392 13.039 1.00 15.73 ? 90 PHE A CA 1 ATOM 414 C C . PHE A 1 90 ? 16.602 -10.979 13.380 1.00 16.08 ? 90 PHE A C 1 ATOM 415 O O . PHE A 1 90 ? 16.755 -12.181 13.671 1.00 16.39 ? 90 PHE A O 1 ATOM 416 C CB . PHE A 1 90 ? 14.784 -9.463 14.173 1.00 15.89 ? 90 PHE A CB 1 ATOM 417 C CG . PHE A 1 90 ? 13.759 -8.444 13.776 1.00 15.91 ? 90 PHE A CG 1 ATOM 418 C CD1 . PHE A 1 90 ? 12.859 -8.680 12.741 1.00 16.15 ? 90 PHE A CD1 1 ATOM 419 C CD2 . PHE A 1 90 ? 13.675 -7.245 14.469 1.00 16.28 ? 90 PHE A CD2 1 ATOM 420 C CE1 . PHE A 1 90 ? 11.921 -7.728 12.388 1.00 16.36 ? 90 PHE A CE1 1 ATOM 421 C CE2 . PHE A 1 90 ? 12.732 -6.292 14.127 1.00 16.49 ? 90 PHE A CE2 1 ATOM 422 C CZ . PHE A 1 90 ? 11.848 -6.539 13.091 1.00 16.51 ? 90 PHE A CZ 1 ATOM 423 N N . ASN A 1 91 ? 17.600 -10.114 13.333 1.00 15.60 ? 91 ASN A N 1 ATOM 424 C CA . ASN A 1 91 ? 18.960 -10.511 13.630 1.00 16.03 ? 91 ASN A CA 1 ATOM 425 C C . ASN A 1 91 ? 19.702 -9.514 14.509 1.00 16.05 ? 91 ASN A C 1 ATOM 426 O O . ASN A 1 91 ? 20.880 -9.698 14.771 1.00 17.13 ? 91 ASN A O 1 ATOM 427 C CB . ASN A 1 91 ? 19.721 -10.715 12.322 1.00 15.90 ? 91 ASN A CB 1 ATOM 428 C CG . ASN A 1 91 ? 19.665 -9.484 11.425 1.00 15.91 ? 91 ASN A CG 1 ATOM 429 O OD1 . ASN A 1 91 ? 19.609 -8.355 11.913 1.00 15.44 ? 91 ASN A OD1 1 ATOM 430 N ND2 . ASN A 1 91 ? 19.664 -9.700 10.111 1.00 15.87 ? 91 ASN A ND2 1 ATOM 431 N N . CYS A 1 92 ? 19.019 -8.477 14.980 1.00 16.60 ? 92 CYS A N 1 ATOM 432 C CA . CYS A 1 92 ? 19.661 -7.427 15.755 1.00 16.68 ? 92 CYS A CA 1 ATOM 433 C C . CYS A 1 92 ? 18.726 -6.793 16.809 1.00 16.25 ? 92 CYS A C 1 ATOM 434 O O . CYS A 1 92 ? 17.502 -6.831 16.681 1.00 15.80 ? 92 CYS A O 1 ATOM 435 C CB . CYS A 1 92 ? 20.188 -6.362 14.796 1.00 17.27 ? 92 CYS A CB 1 ATOM 436 S SG . CYS A 1 92 ? 21.310 -5.148 15.531 1.00 18.79 ? 92 CYS A SG 1 ATOM 437 N N . VAL A 1 93 ? 19.338 -6.236 17.852 1.00 15.94 ? 93 VAL A N 1 ATOM 438 C CA . VAL A 1 93 ? 18.670 -5.399 18.830 1.00 15.62 ? 93 VAL A CA 1 ATOM 439 C C . VAL A 1 93 ? 19.529 -4.141 19.092 1.00 15.79 ? 93 VAL A C 1 ATOM 440 O O . VAL A 1 93 ? 20.756 -4.204 19.162 1.00 15.48 ? 93 VAL A O 1 ATOM 441 C CB . VAL A 1 93 ? 18.390 -6.181 20.136 1.00 15.83 ? 93 VAL A CB 1 ATOM 442 C CG1 . VAL A 1 93 ? 18.223 -5.251 21.340 1.00 16.00 ? 93 VAL A CG1 1 ATOM 443 C CG2 . VAL A 1 93 ? 17.156 -7.072 19.979 1.00 15.80 ? 93 VAL A CG2 1 ATOM 444 N N . SER A 1 94 ? 18.860 -3.000 19.210 1.00 15.66 ? 94 SER A N 1 ATOM 445 C CA . SER A 1 94 ? 19.490 -1.738 19.546 1.00 15.78 ? 94 SER A CA 1 ATOM 446 C C . SER A 1 94 ? 19.124 -1.405 20.979 1.00 15.72 ? 94 SER A C 1 ATOM 447 O O . SER A 1 94 ? 18.001 -1.640 21.396 1.00 15.67 ? 94 SER A O 1 ATOM 448 C CB . SER A 1 94 ? 18.976 -0.641 18.612 1.00 16.05 ? 94 SER A CB 1 ATOM 449 O OG . SER A 1 94 ? 19.169 0.663 19.153 1.00 15.96 ? 94 SER A OG 1 ATOM 450 N N . PHE A 1 95 ? 20.054 -0.853 21.739 1.00 15.90 ? 95 PHE A N 1 ATOM 451 C CA . PHE A 1 95 ? 19.751 -0.538 23.131 1.00 16.85 ? 95 PHE A CA 1 ATOM 452 C C . PHE A 1 95 ? 20.427 0.730 23.612 1.00 16.77 ? 95 PHE A C 1 ATOM 453 O O . PHE A 1 95 ? 21.560 1.049 23.211 1.00 16.88 ? 95 PHE A O 1 ATOM 454 C CB . PHE A 1 95 ? 20.138 -1.707 24.060 1.00 16.42 ? 95 PHE A CB 1 ATOM 455 C CG . PHE A 1 95 ? 21.610 -1.916 24.169 1.00 16.41 ? 95 PHE A CG 1 ATOM 456 C CD1 . PHE A 1 95 ? 22.294 -2.653 23.196 1.00 16.35 ? 95 PHE A CD1 1 ATOM 457 C CD2 . PHE A 1 95 ? 22.328 -1.349 25.210 1.00 15.98 ? 95 PHE A CD2 1 ATOM 458 C CE1 . PHE A 1 95 ? 23.659 -2.835 23.286 1.00 16.10 ? 95 PHE A CE1 1 ATOM 459 C CE2 . PHE A 1 95 ? 23.696 -1.524 25.293 1.00 16.15 ? 95 PHE A CE2 1 ATOM 460 C CZ . PHE A 1 95 ? 24.362 -2.269 24.334 1.00 16.10 ? 95 PHE A CZ 1 ATOM 461 N N . TYR A 1 96 ? 19.721 1.434 24.490 1.00 16.58 ? 96 TYR A N 1 ATOM 462 C CA . TYR A 1 96 ? 20.291 2.570 25.193 1.00 16.75 ? 96 TYR A CA 1 ATOM 463 C C . TYR A 1 96 ? 20.877 2.058 26.516 1.00 17.06 ? 96 TYR A C 1 ATOM 464 O O . TYR A 1 96 ? 20.505 0.991 27.003 1.00 17.31 ? 96 TYR A O 1 ATOM 465 C CB . TYR A 1 96 ? 19.226 3.628 25.499 1.00 16.68 ? 96 TYR A CB 1 ATOM 466 C CG . TYR A 1 96 ? 18.773 4.549 24.374 1.00 16.64 ? 96 TYR A CG 1 ATOM 467 C CD1 . TYR A 1 96 ? 19.675 5.131 23.489 1.00 16.70 ? 96 TYR A CD1 1 ATOM 468 C CD2 . TYR A 1 96 ? 17.422 4.899 24.245 1.00 16.81 ? 96 TYR A CD2 1 ATOM 469 C CE1 . TYR A 1 96 ? 19.242 5.998 22.488 1.00 16.47 ? 96 TYR A CE1 1 ATOM 470 C CE2 . TYR A 1 96 ? 16.988 5.770 23.260 1.00 16.56 ? 96 TYR A CE2 1 ATOM 471 C CZ . TYR A 1 96 ? 17.899 6.319 22.382 1.00 16.49 ? 96 TYR A CZ 1 ATOM 472 O OH . TYR A 1 96 ? 17.458 7.190 21.394 1.00 16.28 ? 96 TYR A OH 1 ATOM 473 N N . VAL A 1 97 ? 21.796 2.830 27.088 1.00 17.19 ? 97 VAL A N 1 ATOM 474 C CA . VAL A 1 97 ? 22.217 2.672 28.478 1.00 16.88 ? 97 VAL A CA 1 ATOM 475 C C . VAL A 1 97 ? 21.836 3.990 29.165 1.00 17.27 ? 97 VAL A C 1 ATOM 476 O O . VAL A 1 97 ? 22.029 5.073 28.594 1.00 16.82 ? 97 VAL A O 1 ATOM 477 C CB . VAL A 1 97 ? 23.728 2.427 28.570 1.00 16.83 ? 97 VAL A CB 1 ATOM 478 C CG1 . VAL A 1 97 ? 24.172 2.223 30.014 1.00 17.16 ? 97 VAL A CG1 1 ATOM 479 C CG2 . VAL A 1 97 ? 24.109 1.214 27.724 1.00 17.07 ? 97 VAL A CG2 1 ATOM 480 N N . ASP A 1 98 ? 21.269 3.902 30.365 1.00 17.19 ? 98 ASP A N 1 ATOM 481 C CA . ASP A 1 98 ? 20.804 5.087 31.063 1.00 17.62 ? 98 ASP A CA 1 ATOM 482 C C . ASP A 1 98 ? 21.869 5.483 32.060 1.00 17.61 ? 98 ASP A C 1 ATOM 483 O O . ASP A 1 98 ? 22.000 4.873 33.113 1.00 17.48 ? 98 ASP A O 1 ATOM 484 C CB . ASP A 1 98 ? 19.451 4.839 31.735 1.00 18.09 ? 98 ASP A CB 1 ATOM 485 C CG . ASP A 1 98 ? 18.849 6.102 32.357 1.00 18.73 ? 98 ASP A CG 1 ATOM 486 O OD1 . ASP A 1 98 ? 19.562 7.119 32.512 1.00 19.25 ? 98 ASP A OD1 1 ATOM 487 O OD2 . ASP A 1 98 ? 17.652 6.070 32.713 1.00 18.99 -1 98 ASP A OD2 1 ATOM 488 N N . TRP A 1 99 ? 22.632 6.517 31.709 1.00 17.64 ? 99 TRP A N 1 ATOM 489 C CA . TRP A 1 99 ? 23.722 7.027 32.556 1.00 17.65 ? 99 TRP A CA 1 ATOM 490 C C . TRP A 1 99 ? 23.222 7.359 33.979 1.00 17.87 ? 99 TRP A C 1 ATOM 491 O O . TRP A 1 99 ? 23.854 6.985 34.972 1.00 17.81 ? 99 TRP A O 1 ATOM 492 C CB . TRP A 1 99 ? 24.358 8.231 31.838 1.00 17.72 ? 99 TRP A CB 1 ATOM 493 C CG . TRP A 1 99 ? 25.410 8.999 32.568 1.00 17.94 ? 99 TRP A CG 1 ATOM 494 C CD1 . TRP A 1 99 ? 26.147 8.584 33.638 1.00 17.73 ? 99 TRP A CD1 1 ATOM 495 C CD2 . TRP A 1 99 ? 25.896 10.307 32.229 1.00 17.86 ? 99 TRP A CD2 1 ATOM 496 N NE1 . TRP A 1 99 ? 27.029 9.560 34.004 1.00 18.25 ? 99 TRP A NE1 1 ATOM 497 C CE2 . TRP A 1 99 ? 26.892 10.634 33.163 1.00 17.86 ? 99 TRP A CE2 1 ATOM 498 C CE3 . TRP A 1 99 ? 25.569 11.240 31.236 1.00 17.87 ? 99 TRP A CE3 1 ATOM 499 C CZ2 . TRP A 1 99 ? 27.573 11.851 33.137 1.00 17.84 ? 99 TRP A CZ2 1 ATOM 500 C CZ3 . TRP A 1 99 ? 26.248 12.463 31.211 1.00 17.69 ? 99 TRP A CZ3 1 ATOM 501 C CH2 . TRP A 1 99 ? 27.244 12.748 32.148 1.00 17.87 ? 99 TRP A CH2 1 ATOM 502 N N . ALA A 1 100 ? 22.056 8.007 34.074 1.00 18.28 ? 100 ALA A N 1 ATOM 503 C CA . ALA A 1 100 ? 21.464 8.401 35.367 1.00 17.86 ? 100 ALA A CA 1 ATOM 504 C C . ALA A 1 100 ? 21.330 7.253 36.363 1.00 17.55 ? 100 ALA A C 1 ATOM 505 O O . ALA A 1 100 ? 21.323 7.484 37.570 1.00 17.30 ? 100 ALA A O 1 ATOM 506 C CB . ALA A 1 100 ? 20.097 9.039 35.148 1.00 17.87 ? 100 ALA A CB 1 ATOM 507 N N . LEU A 1 101 ? 21.196 6.025 35.865 1.00 17.40 ? 101 LEU A N 1 ATOM 508 C CA . LEU A 1 101 ? 20.994 4.874 36.735 1.00 17.53 ? 101 LEU A CA 1 ATOM 509 C C . LEU A 1 101 ? 22.290 4.236 37.229 1.00 18.15 ? 101 LEU A C 1 ATOM 510 O O . LEU A 1 101 ? 22.293 3.566 38.273 1.00 18.36 ? 101 LEU A O 1 ATOM 511 C CB . LEU A 1 101 ? 20.121 3.837 36.039 1.00 17.90 ? 101 LEU A CB 1 ATOM 512 C CG . LEU A 1 101 ? 18.630 4.193 36.048 1.00 18.07 ? 101 LEU A CG 1 ATOM 513 C CD1 . LEU A 1 101 ? 17.837 3.271 35.145 1.00 17.99 ? 101 LEU A CD1 1 ATOM 514 C CD2 . LEU A 1 101 ? 18.082 4.143 37.473 1.00 18.29 ? 101 LEU A CD2 1 ATOM 515 N N . VAL A 1 102 ? 23.388 4.458 36.505 1.00 18.25 ? 102 VAL A N 1 ATOM 516 C CA . VAL A 1 102 ? 24.654 3.789 36.799 1.00 18.34 ? 102 VAL A CA 1 ATOM 517 C C . VAL A 1 102 ? 25.775 4.733 37.278 1.00 18.18 ? 102 VAL A C 1 ATOM 518 O O . VAL A 1 102 ? 26.869 4.282 37.552 1.00 17.65 ? 102 VAL A O 1 ATOM 519 C CB . VAL A 1 102 ? 25.133 2.958 35.577 1.00 18.81 ? 102 VAL A CB 1 ATOM 520 C CG1 . VAL A 1 102 ? 24.173 1.809 35.305 1.00 18.71 ? 102 VAL A CG1 1 ATOM 521 C CG2 . VAL A 1 102 ? 25.281 3.823 34.333 1.00 18.73 ? 102 VAL A CG2 1 ATOM 522 N N . GLU A 1 103 ? 25.516 6.035 37.361 1.00 18.72 ? 103 GLU A N 1 ATOM 523 C CA . GLU A 1 103 ? 26.444 6.960 38.028 1.00 18.59 ? 103 GLU A CA 1 ATOM 524 C C . GLU A 1 103 ? 25.650 8.004 38.814 1.00 19.01 ? 103 GLU A C 1 ATOM 525 O O . GLU A 1 103 ? 25.825 9.217 38.643 1.00 18.38 ? 103 GLU A O 1 ATOM 526 C CB . GLU A 1 103 ? 27.412 7.619 37.039 1.00 18.66 ? 103 GLU A CB 1 ATOM 527 C CG . GLU A 1 103 ? 28.690 8.100 37.720 1.00 18.91 ? 103 GLU A CG 1 ATOM 528 C CD . GLU A 1 103 ? 29.625 8.927 36.843 1.00 18.97 ? 103 GLU A CD 1 ATOM 529 O OE1 . GLU A 1 103 ? 30.730 9.241 37.317 1.00 20.37 ? 103 GLU A OE1 1 ATOM 530 O OE2 . GLU A 1 103 ? 29.287 9.285 35.697 1.00 19.25 -1 103 GLU A OE2 1 ATOM 531 N N . GLY A 1 104 ? 24.782 7.504 39.693 1.00 19.82 ? 104 GLY A N 1 ATOM 532 C CA . GLY A 1 104 ? 23.967 8.340 40.566 1.00 20.50 ? 104 GLY A CA 1 ATOM 533 C C . GLY A 1 104 ? 24.845 9.182 41.465 1.00 21.04 ? 104 GLY A C 1 ATOM 534 O O . GLY A 1 104 ? 24.536 10.322 41.766 1.00 20.28 ? 104 GLY A O 1 ATOM 535 N N . LYS A 1 105 ? 25.958 8.599 41.880 1.00 22.63 ? 105 LYS A N 1 ATOM 536 C CA . LYS A 1 105 ? 26.931 9.293 42.697 1.00 24.38 ? 105 LYS A CA 1 ATOM 537 C C . LYS A 1 105 ? 28.072 9.684 41.781 1.00 24.02 ? 105 LYS A C 1 ATOM 538 O O . LYS A 1 105 ? 28.694 8.805 41.194 1.00 23.68 ? 105 LYS A O 1 ATOM 539 C CB . LYS A 1 105 ? 27.413 8.369 43.813 1.00 25.28 ? 105 LYS A CB 1 ATOM 540 C CG . LYS A 1 105 ? 28.725 8.764 44.448 1.00 27.53 ? 105 LYS A CG 1 ATOM 541 C CD . LYS A 1 105 ? 28.612 9.792 45.543 1.00 29.06 ? 105 LYS A CD 1 ATOM 542 C CE . LYS A 1 105 ? 29.940 9.848 46.305 1.00 30.72 ? 105 LYS A CE 1 ATOM 543 N NZ . LYS A 1 105 ? 30.187 11.207 46.861 1.00 32.35 ? 105 LYS A NZ 1 ATOM 544 N N . PRO A 1 106 ? 28.347 10.997 41.637 1.00 24.23 ? 106 PRO A N 1 ATOM 545 C CA . PRO A 1 106 ? 29.435 11.399 40.742 1.00 23.77 ? 106 PRO A CA 1 ATOM 546 C C . PRO A 1 106 ? 30.773 10.778 41.130 1.00 23.87 ? 106 PRO A C 1 ATOM 547 O O . PRO A 1 106 ? 31.190 10.870 42.288 1.00 23.62 ? 106 PRO A O 1 ATOM 548 C CB . PRO A 1 106 ? 29.481 12.929 40.874 1.00 23.66 ? 106 PRO A CB 1 ATOM 549 C CG . PRO A 1 106 ? 28.573 13.282 41.992 1.00 23.70 ? 106 PRO A CG 1 ATOM 550 C CD . PRO A 1 106 ? 27.604 12.156 42.156 1.00 24.10 ? 106 PRO A CD 1 ATOM 551 N N . GLY A 1 107 ? 31.425 10.142 40.156 1.00 24.01 ? 107 GLY A N 1 ATOM 552 C CA . GLY A 1 107 ? 32.701 9.470 40.380 1.00 23.83 ? 107 GLY A CA 1 ATOM 553 C C . GLY A 1 107 ? 32.584 7.991 40.685 1.00 23.94 ? 107 GLY A C 1 ATOM 554 O O . GLY A 1 107 ? 33.575 7.293 40.654 1.00 23.82 ? 107 GLY A O 1 ATOM 555 N N . GLU A 1 108 ? 31.378 7.510 40.980 1.00 24.64 ? 108 GLU A N 1 ATOM 556 C CA . GLU A 1 108 ? 31.153 6.097 41.294 1.00 25.77 ? 108 GLU A CA 1 ATOM 557 C C . GLU A 1 108 ? 30.286 5.406 40.244 1.00 24.21 ? 108 GLU A C 1 ATOM 558 O O . GLU A 1 108 ? 29.064 5.378 40.372 1.00 22.84 ? 108 GLU A O 1 ATOM 559 C CB . GLU A 1 108 ? 30.458 5.944 42.647 1.00 27.40 ? 108 GLU A CB 1 ATOM 560 C CG . GLU A 1 108 ? 31.318 6.204 43.860 1.00 30.11 ? 108 GLU A CG 1 ATOM 561 C CD . GLU A 1 108 ? 30.643 5.750 45.149 1.00 32.75 ? 108 GLU A CD 1 ATOM 562 O OE1 . GLU A 1 108 ? 29.944 4.707 45.122 1.00 34.76 ? 108 GLU A OE1 1 ATOM 563 O OE2 . GLU A 1 108 ? 30.804 6.444 46.183 1.00 33.80 -1 108 GLU A OE2 1 ATOM 564 N N . TYR A 1 109 ? 30.917 4.835 39.225 1.00 23.67 ? 109 TYR A N 1 ATOM 565 C CA . TYR A 1 109 ? 30.204 4.061 38.214 1.00 23.24 ? 109 TYR A CA 1 ATOM 566 C C . TYR A 1 109 ? 29.786 2.708 38.778 1.00 22.95 ? 109 TYR A C 1 ATOM 567 O O . TYR A 1 109 ? 30.633 1.936 39.208 1.00 23.32 ? 109 TYR A O 1 ATOM 568 C CB . TYR A 1 109 ? 31.103 3.836 37.000 1.00 23.11 ? 109 TYR A CB 1 ATOM 569 C CG . TYR A 1 109 ? 30.475 3.058 35.863 1.00 22.04 ? 109 TYR A CG 1 ATOM 570 C CD1 . TYR A 1 109 ? 30.528 1.662 35.822 1.00 22.11 ? 109 TYR A CD1 1 ATOM 571 C CD2 . TYR A 1 109 ? 29.849 3.722 34.816 1.00 21.67 ? 109 TYR A CD2 1 ATOM 572 C CE1 . TYR A 1 109 ? 29.972 0.949 34.758 1.00 21.65 ? 109 TYR A CE1 1 ATOM 573 C CE2 . TYR A 1 109 ? 29.289 3.032 33.763 1.00 21.80 ? 109 TYR A CE2 1 ATOM 574 C CZ . TYR A 1 109 ? 29.352 1.645 33.732 1.00 21.97 ? 109 TYR A CZ 1 ATOM 575 O OH . TYR A 1 109 ? 28.784 0.984 32.661 1.00 22.31 ? 109 TYR A OH 1 ATOM 576 N N . ARG A 1 110 ? 28.485 2.429 38.763 1.00 23.08 ? 110 ARG A N 1 ATOM 577 C CA . ARG A 1 110 ? 27.941 1.134 39.197 1.00 23.11 ? 110 ARG A CA 1 ATOM 578 C C . ARG A 1 110 ? 26.982 0.591 38.165 1.00 22.04 ? 110 ARG A C 1 ATOM 579 O O . ARG A 1 110 ? 25.895 1.133 37.981 1.00 21.32 ? 110 ARG A O 1 ATOM 580 C CB . ARG A 1 110 ? 27.145 1.288 40.485 1.00 24.65 ? 110 ARG A CB 1 ATOM 581 C CG . ARG A 1 110 ? 27.972 1.393 41.741 1.00 25.92 ? 110 ARG A CG 1 ATOM 582 C CD . ARG A 1 110 ? 27.058 1.579 42.937 1.00 26.76 ? 110 ARG A CD 1 ATOM 583 N NE . ARG A 1 110 ? 27.840 1.986 44.093 1.00 27.89 ? 110 ARG A NE 1 ATOM 584 C CZ . ARG A 1 110 ? 28.431 1.150 44.939 1.00 27.98 ? 110 ARG A CZ 1 ATOM 585 N NH1 . ARG A 1 110 ? 28.323 -0.163 44.786 1.00 27.17 ? 110 ARG A NH1 1 ATOM 586 N NH2 . ARG A 1 110 ? 29.134 1.644 45.947 1.00 28.89 ? 110 ARG A NH2 1 ATOM 587 N N . ALA A 1 111 ? 27.387 -0.481 37.504 1.00 21.46 ? 111 ALA A N 1 ATOM 588 C CA . ALA A 1 111 ? 26.542 -1.187 36.560 1.00 21.01 ? 111 ALA A CA 1 ATOM 589 C C . ALA A 1 111 ? 26.636 -2.660 36.891 1.00 21.05 ? 111 ALA A C 1 ATOM 590 O O . ALA A 1 111 ? 27.080 -3.469 36.088 1.00 20.58 ? 111 ALA A O 1 ATOM 591 C CB . ALA A 1 111 ? 26.976 -0.901 35.129 1.00 20.54 ? 111 ALA A CB 1 ATOM 592 N N . ASP A 1 112 ? 26.208 -2.979 38.107 1.00 22.79 ? 112 ASP A N 1 ATOM 593 C CA . ASP A 1 112 ? 26.261 -4.328 38.659 1.00 23.47 ? 112 ASP A CA 1 ATOM 594 C C . ASP A 1 112 ? 24.843 -4.829 38.967 1.00 23.26 ? 112 ASP A C 1 ATOM 595 O O . ASP A 1 112 ? 23.876 -4.048 38.975 1.00 22.09 ? 112 ASP A O 1 ATOM 596 C CB . ASP A 1 112 ? 27.085 -4.319 39.954 1.00 25.71 ? 112 ASP A CB 1 ATOM 597 C CG . ASP A 1 112 ? 28.377 -3.513 39.824 1.00 26.86 ? 112 ASP A CG 1 ATOM 598 O OD1 . ASP A 1 112 ? 29.052 -3.632 38.787 1.00 28.72 ? 112 ASP A OD1 1 ATOM 599 O OD2 . ASP A 1 112 ? 28.718 -2.745 40.747 1.00 28.73 -1 112 ASP A OD2 1 ATOM 600 N N . GLY A 1 113 ? 24.732 -6.130 39.231 1.00 22.41 ? 113 GLY A N 1 ATOM 601 C CA . GLY A 1 113 ? 23.458 -6.747 39.588 1.00 21.79 ? 113 GLY A CA 1 ATOM 602 C C . GLY A 1 113 ? 22.394 -6.556 38.518 1.00 21.68 ? 113 GLY A C 1 ATOM 603 O O . GLY A 1 113 ? 22.547 -7.020 37.384 1.00 21.02 ? 113 GLY A O 1 ATOM 604 N N . ILE A 1 114 ? 21.324 -5.846 38.867 1.00 20.86 ? 114 ILE A N 1 ATOM 605 C CA . ILE A 1 114 ? 20.212 -5.651 37.936 1.00 20.34 ? 114 ILE A CA 1 ATOM 606 C C . ILE A 1 114 ? 20.565 -4.674 36.808 1.00 20.58 ? 114 ILE A C 1 ATOM 607 O O . ILE A 1 114 ? 19.934 -4.683 35.756 1.00 19.69 ? 114 ILE A O 1 ATOM 608 C CB . ILE A 1 114 ? 18.910 -5.234 38.655 1.00 19.65 ? 114 ILE A CB 1 ATOM 609 C CG1 . ILE A 1 114 ? 18.999 -3.830 39.261 1.00 19.37 ? 114 ILE A CG1 1 ATOM 610 C CG2 . ILE A 1 114 ? 18.554 -6.254 39.730 1.00 19.96 ? 114 ILE A CG2 1 ATOM 611 C CD1 . ILE A 1 114 ? 17.635 -3.226 39.541 1.00 19.34 ? 114 ILE A CD1 1 ATOM 612 N N . PHE A 1 115 ? 21.590 -3.856 37.019 1.00 20.93 ? 115 PHE A N 1 ATOM 613 C CA . PHE A 1 115 ? 22.088 -2.968 35.975 1.00 21.29 ? 115 PHE A CA 1 ATOM 614 C C . PHE A 1 115 ? 23.276 -3.529 35.167 1.00 21.49 ? 115 PHE A C 1 ATOM 615 O O . PHE A 1 115 ? 23.838 -2.830 34.331 1.00 21.08 ? 115 PHE A O 1 ATOM 616 C CB . PHE A 1 115 ? 22.462 -1.643 36.607 1.00 21.75 ? 115 PHE A CB 1 ATOM 617 C CG . PHE A 1 115 ? 21.358 -1.049 37.426 1.00 22.69 ? 115 PHE A CG 1 ATOM 618 C CD1 . PHE A 1 115 ? 20.273 -0.445 36.808 1.00 22.99 ? 115 PHE A CD1 1 ATOM 619 C CD2 . PHE A 1 115 ? 21.386 -1.126 38.814 1.00 23.28 ? 115 PHE A CD2 1 ATOM 620 C CE1 . PHE A 1 115 ? 19.239 0.092 37.557 1.00 23.50 ? 115 PHE A CE1 1 ATOM 621 C CE2 . PHE A 1 115 ? 20.360 -0.583 39.569 1.00 24.18 ? 115 PHE A CE2 1 ATOM 622 C CZ . PHE A 1 115 ? 19.281 0.026 38.936 1.00 24.01 ? 115 PHE A CZ 1 ATOM 623 N N . ASP A 1 116 ? 23.642 -4.787 35.405 1.00 21.31 ? 116 ASP A N 1 ATOM 624 C CA . ASP A 1 116 ? 24.782 -5.409 34.748 1.00 21.57 ? 116 ASP A CA 1 ATOM 625 C C . ASP A 1 116 ? 24.447 -5.668 33.273 1.00 21.08 ? 116 ASP A C 1 ATOM 626 O O . ASP A 1 116 ? 23.481 -6.361 32.947 1.00 20.82 ? 116 ASP A O 1 ATOM 627 C CB . ASP A 1 116 ? 25.142 -6.719 35.479 1.00 22.75 ? 116 ASP A CB 1 ATOM 628 C CG . ASP A 1 116 ? 26.497 -7.311 35.051 1.00 23.37 ? 116 ASP A CG 1 ATOM 629 O OD1 . ASP A 1 116 ? 27.043 -6.910 33.999 1.00 23.63 ? 116 ASP A OD1 1 ATOM 630 O OD2 . ASP A 1 116 ? 27.012 -8.197 35.779 1.00 24.10 -1 116 ASP A OD2 1 ATOM 631 N N . LEU A 1 117 ? 25.240 -5.091 32.377 1.00 21.29 ? 117 LEU A N 1 ATOM 632 C CA . LEU A 1 117 ? 25.012 -5.256 30.938 1.00 21.11 ? 117 LEU A CA 1 ATOM 633 C C . LEU A 1 117 ? 25.485 -6.618 30.425 1.00 20.20 ? 117 LEU A C 1 ATOM 634 O O . LEU A 1 117 ? 25.057 -7.058 29.369 1.00 19.64 ? 117 LEU A O 1 ATOM 635 C CB . LEU A 1 117 ? 25.711 -4.142 30.160 1.00 21.22 ? 117 LEU A CB 1 ATOM 636 C CG . LEU A 1 117 ? 25.245 -2.720 30.488 1.00 21.95 ? 117 LEU A CG 1 ATOM 637 C CD1 . LEU A 1 117 ? 26.183 -1.712 29.841 1.00 21.74 ? 117 LEU A CD1 1 ATOM 638 C CD2 . LEU A 1 117 ? 23.796 -2.492 30.061 1.00 21.57 ? 117 LEU A CD2 1 ATOM 639 N N . GLU A 1 118 ? 26.357 -7.282 31.175 1.00 20.32 ? 118 GLU A N 1 ATOM 640 C CA . GLU A 1 118 ? 27.001 -8.501 30.689 1.00 21.38 ? 118 GLU A CA 1 ATOM 641 C C . GLU A 1 118 ? 26.050 -9.678 30.460 1.00 20.84 ? 118 GLU A C 1 ATOM 642 O O . GLU A 1 118 ? 26.101 -10.278 29.389 1.00 20.46 ? 118 GLU A O 1 ATOM 643 C CB . GLU A 1 118 ? 28.206 -8.860 31.559 1.00 22.59 ? 118 GLU A CB 1 ATOM 644 C CG . GLU A 1 118 ? 29.265 -7.757 31.524 1.00 24.39 ? 118 GLU A CG 1 ATOM 645 C CD . GLU A 1 118 ? 30.612 -8.185 32.067 1.00 26.14 ? 118 GLU A CD 1 ATOM 646 O OE1 . GLU A 1 118 ? 30.728 -9.315 32.587 1.00 29.13 ? 118 GLU A OE1 1 ATOM 647 O OE2 . GLU A 1 118 ? 31.564 -7.390 31.959 1.00 28.06 -1 118 GLU A OE2 1 ATOM 648 N N . PRO A 1 119 ? 25.158 -9.983 31.429 1.00 20.50 ? 119 PRO A N 1 ATOM 649 C CA . PRO A 1 119 ? 24.071 -10.948 31.189 1.00 20.35 ? 119 PRO A CA 1 ATOM 650 C C . PRO A 1 119 ? 23.127 -10.583 30.031 1.00 19.70 ? 119 PRO A C 1 ATOM 651 O O . PRO A 1 119 ? 22.636 -11.467 29.343 1.00 19.72 ? 119 PRO A O 1 ATOM 652 C CB . PRO A 1 119 ? 23.300 -10.942 32.520 1.00 20.69 ? 119 PRO A CB 1 ATOM 653 C CG . PRO A 1 119 ? 24.316 -10.572 33.538 1.00 20.46 ? 119 PRO A CG 1 ATOM 654 C CD . PRO A 1 119 ? 25.200 -9.567 32.845 1.00 20.54 ? 119 PRO A CD 1 ATOM 655 N N . PHE A 1 120 ? 22.877 -9.295 29.822 1.00 19.71 ? 120 PHE A N 1 ATOM 656 C CA . PHE A 1 120 ? 22.065 -8.822 28.682 1.00 19.08 ? 120 PHE A CA 1 ATOM 657 C C . PHE A 1 120 ? 22.760 -9.198 27.361 1.00 18.13 ? 120 PHE A C 1 ATOM 658 O O . PHE A 1 120 ? 22.126 -9.735 26.448 1.00 18.38 ? 120 PHE A O 1 ATOM 659 C CB . PHE A 1 120 ? 21.840 -7.309 28.839 1.00 18.87 ? 120 PHE A CB 1 ATOM 660 C CG . PHE A 1 120 ? 21.109 -6.636 27.699 1.00 19.03 ? 120 PHE A CG 1 ATOM 661 C CD1 . PHE A 1 120 ? 19.728 -6.726 27.580 1.00 19.53 ? 120 PHE A CD1 1 ATOM 662 C CD2 . PHE A 1 120 ? 21.796 -5.816 26.807 1.00 19.06 ? 120 PHE A CD2 1 ATOM 663 C CE1 . PHE A 1 120 ? 19.050 -6.050 26.565 1.00 19.38 ? 120 PHE A CE1 1 ATOM 664 C CE2 . PHE A 1 120 ? 21.134 -5.141 25.791 1.00 19.05 ? 120 PHE A CE2 1 ATOM 665 C CZ . PHE A 1 120 ? 19.755 -5.255 25.670 1.00 19.47 ? 120 PHE A CZ 1 ATOM 666 N N . PHE A 1 121 ? 24.069 -8.971 27.293 1.00 17.22 ? 121 PHE A N 1 ATOM 667 C CA . PHE A 1 121 ? 24.859 -9.298 26.107 1.00 16.93 ? 121 PHE A CA 1 ATOM 668 C C . PHE A 1 121 ? 24.937 -10.807 25.865 1.00 17.09 ? 121 PHE A C 1 ATOM 669 O O . PHE A 1 121 ? 24.714 -11.275 24.743 1.00 17.07 ? 121 PHE A O 1 ATOM 670 C CB . PHE A 1 121 ? 26.289 -8.757 26.227 1.00 16.74 ? 121 PHE A CB 1 ATOM 671 C CG . PHE A 1 121 ? 26.390 -7.264 26.345 1.00 16.69 ? 121 PHE A CG 1 ATOM 672 C CD1 . PHE A 1 121 ? 25.331 -6.423 26.022 1.00 17.01 ? 121 PHE A CD1 1 ATOM 673 C CD2 . PHE A 1 121 ? 27.578 -6.690 26.772 1.00 16.79 ? 121 PHE A CD2 1 ATOM 674 C CE1 . PHE A 1 121 ? 25.460 -5.043 26.133 1.00 16.80 ? 121 PHE A CE1 1 ATOM 675 C CE2 . PHE A 1 121 ? 27.706 -5.317 26.881 1.00 16.99 ? 121 PHE A CE2 1 ATOM 676 C CZ . PHE A 1 121 ? 26.646 -4.493 26.561 1.00 16.56 ? 121 PHE A CZ 1 ATOM 677 N N . ASP A 1 122 ? 25.251 -11.566 26.911 1.00 17.15 ? 122 ASP A N 1 ATOM 678 C CA . ASP A 1 122 ? 25.271 -13.024 26.815 1.00 17.81 ? 122 ASP A CA 1 ATOM 679 C C . ASP A 1 122 ? 23.922 -13.599 26.398 1.00 17.04 ? 122 ASP A C 1 ATOM 680 O O . ASP A 1 122 ? 23.865 -14.582 25.669 1.00 17.43 ? 122 ASP A O 1 ATOM 681 C CB . ASP A 1 122 ? 25.743 -13.651 28.133 1.00 18.87 ? 122 ASP A CB 1 ATOM 682 C CG . ASP A 1 122 ? 27.182 -13.307 28.447 1.00 19.67 ? 122 ASP A CG 1 ATOM 683 O OD1 . ASP A 1 122 ? 27.933 -13.001 27.502 1.00 20.57 ? 122 ASP A OD1 1 ATOM 684 O OD2 . ASP A 1 122 ? 27.570 -13.326 29.632 1.00 21.80 -1 122 ASP A OD2 1 ATOM 685 N N . ALA A 1 123 ? 22.837 -12.978 26.836 1.00 16.52 ? 123 ALA A N 1 ATOM 686 C CA . ALA A 1 123 ? 21.507 -13.391 26.395 1.00 16.23 ? 123 ALA A CA 1 ATOM 687 C C . ALA A 1 123 ? 21.291 -13.076 24.908 1.00 16.63 ? 123 ALA A C 1 ATOM 688 O O . ALA A 1 123 ? 20.658 -13.856 24.192 1.00 17.08 ? 123 ALA A O 1 ATOM 689 C CB . ALA A 1 123 ? 20.440 -12.731 27.236 1.00 16.03 ? 123 ALA A CB 1 ATOM 690 N N . ALA A 1 124 ? 21.812 -11.945 24.438 1.00 16.25 ? 124 ALA A N 1 ATOM 691 C CA . ALA A 1 124 ? 21.779 -11.669 23.006 1.00 16.56 ? 124 ALA A CA 1 ATOM 692 C C . ALA A 1 124 ? 22.528 -12.776 22.261 1.00 16.58 ? 124 ALA A C 1 ATOM 693 O O . ALA A 1 124 ? 21.972 -13.384 21.371 1.00 16.14 ? 124 ALA A O 1 ATOM 694 C CB . ALA A 1 124 ? 22.360 -10.287 22.678 1.00 16.25 ? 124 ALA A CB 1 ATOM 695 N N . SER A 1 125 ? 23.774 -13.042 22.655 1.00 17.35 ? 125 SER A N 1 ATOM 696 C CA . SER A 1 125 ? 24.564 -14.152 22.082 1.00 18.03 ? 125 SER A CA 1 ATOM 697 C C . SER A 1 125 ? 23.815 -15.478 22.091 1.00 18.81 ? 125 SER A C 1 ATOM 698 O O . SER A 1 125 ? 23.680 -16.117 21.049 1.00 18.70 ? 125 SER A O 1 ATOM 699 C CB . SER A 1 125 ? 25.900 -14.314 22.811 1.00 17.39 ? 125 SER A CB 1 ATOM 700 O OG . SER A 1 125 ? 26.724 -13.193 22.599 1.00 17.28 ? 125 SER A OG 1 ATOM 701 N N . GLU A 1 126 ? 23.303 -15.882 23.252 1.00 20.80 ? 126 GLU A N 1 ATOM 702 C CA . GLU A 1 126 ? 22.523 -17.130 23.348 1.00 22.56 ? 126 GLU A CA 1 ATOM 703 C C . GLU A 1 126 ? 21.329 -17.202 22.373 1.00 21.79 ? 126 GLU A C 1 ATOM 704 O O . GLU A 1 126 ? 21.016 -18.270 21.843 1.00 22.11 ? 126 GLU A O 1 ATOM 705 C CB . GLU A 1 126 ? 22.013 -17.349 24.773 1.00 25.22 ? 126 GLU A CB 1 ATOM 706 C CG . GLU A 1 126 ? 21.171 -18.617 24.911 1.00 27.70 ? 126 GLU A CG 1 ATOM 707 C CD . GLU A 1 126 ? 20.838 -18.959 26.344 1.00 30.79 ? 126 GLU A CD 1 ATOM 708 O OE1 . GLU A 1 126 ? 21.153 -18.133 27.234 1.00 33.69 ? 126 GLU A OE1 1 ATOM 709 O OE2 . GLU A 1 126 ? 20.257 -20.054 26.576 1.00 32.23 -1 126 GLU A OE2 1 ATOM 710 N N . ALA A 1 127 ? 20.659 -16.075 22.152 1.00 20.90 ? 127 ALA A N 1 ATOM 711 C CA . ALA A 1 127 ? 19.500 -16.026 21.251 1.00 20.04 ? 127 ALA A CA 1 ATOM 712 C C . ALA A 1 127 ? 19.884 -15.949 19.759 1.00 19.21 ? 127 ALA A C 1 ATOM 713 O O . ALA A 1 127 ? 19.036 -16.181 18.889 1.00 19.47 ? 127 ALA A O 1 ATOM 714 C CB . ALA A 1 127 ? 18.604 -14.859 21.628 1.00 19.95 ? 127 ALA A CB 1 ATOM 715 N N . GLY A 1 128 ? 21.152 -15.637 19.471 1.00 18.07 ? 128 GLY A N 1 ATOM 716 C CA . GLY A 1 128 ? 21.631 -15.455 18.105 1.00 17.27 ? 128 GLY A CA 1 ATOM 717 C C . GLY A 1 128 ? 21.351 -14.046 17.593 1.00 17.09 ? 128 GLY A C 1 ATOM 718 O O . GLY A 1 128 ? 21.068 -13.858 16.413 1.00 16.15 ? 128 GLY A O 1 ATOM 719 N N . ILE A 1 129 ? 21.423 -13.057 18.480 1.00 16.56 ? 129 ILE A N 1 ATOM 720 C CA . ILE A 1 129 ? 21.005 -11.699 18.150 1.00 16.75 ? 129 ILE A CA 1 ATOM 721 C C . ILE A 1 129 ? 22.186 -10.757 18.260 1.00 16.42 ? 129 ILE A C 1 ATOM 722 O O . ILE A 1 129 ? 22.839 -10.687 19.290 1.00 16.51 ? 129 ILE A O 1 ATOM 723 C CB . ILE A 1 129 ? 19.845 -11.228 19.064 1.00 17.09 ? 129 ILE A CB 1 ATOM 724 C CG1 . ILE A 1 129 ? 18.561 -11.990 18.716 1.00 17.36 ? 129 ILE A CG1 1 ATOM 725 C CG2 . ILE A 1 129 ? 19.623 -9.711 18.977 1.00 17.22 ? 129 ILE A CG2 1 ATOM 726 C CD1 . ILE A 1 129 ? 17.908 -11.607 17.399 1.00 17.59 ? 129 ILE A CD1 1 ATOM 727 N N . TYR A 1 130 ? 22.452 -10.045 17.176 1.00 16.68 ? 130 TYR A N 1 ATOM 728 C CA . TYR A 1 130 ? 23.512 -9.044 17.140 1.00 17.14 ? 130 TYR A CA 1 ATOM 729 C C . TYR A 1 130 ? 23.033 -7.791 17.863 1.00 16.46 ? 130 TYR A C 1 ATOM 730 O O . TYR A 1 130 ? 21.837 -7.601 18.053 1.00 16.36 ? 130 TYR A O 1 ATOM 731 C CB . TYR A 1 130 ? 23.845 -8.670 15.690 1.00 17.75 ? 130 TYR A CB 1 ATOM 732 C CG . TYR A 1 130 ? 24.516 -9.744 14.859 1.00 18.71 ? 130 TYR A CG 1 ATOM 733 C CD1 . TYR A 1 130 ? 25.745 -10.278 15.231 1.00 19.06 ? 130 TYR A CD1 1 ATOM 734 C CD2 . TYR A 1 130 ? 23.948 -10.187 13.672 1.00 19.10 ? 130 TYR A CD2 1 ATOM 735 C CE1 . TYR A 1 130 ? 26.371 -11.241 14.457 1.00 19.01 ? 130 TYR A CE1 1 ATOM 736 C CE2 . TYR A 1 130 ? 24.574 -11.137 12.891 1.00 18.90 ? 130 TYR A CE2 1 ATOM 737 C CZ . TYR A 1 130 ? 25.783 -11.654 13.287 1.00 19.20 ? 130 TYR A CZ 1 ATOM 738 O OH . TYR A 1 130 ? 26.385 -12.610 12.510 1.00 20.10 ? 130 TYR A OH 1 ATOM 739 N N . LEU A 1 131 ? 23.959 -6.918 18.225 1.00 16.29 ? 131 LEU A N 1 ATOM 740 C CA . LEU A 1 131 ? 23.594 -5.693 18.920 1.00 16.65 ? 131 LEU A CA 1 ATOM 741 C C . LEU A 1 131 ? 24.175 -4.411 18.307 1.00 16.89 ? 131 LEU A C 1 ATOM 742 O O . LEU A 1 131 ? 25.340 -4.363 17.868 1.00 16.90 ? 131 LEU A O 1 ATOM 743 C CB . LEU A 1 131 ? 23.993 -5.791 20.397 1.00 16.60 ? 131 LEU A CB 1 ATOM 744 C CG . LEU A 1 131 ? 23.273 -6.863 21.240 1.00 16.26 ? 131 LEU A CG 1 ATOM 745 C CD1 . LEU A 1 131 ? 23.856 -6.881 22.645 1.00 16.26 ? 131 LEU A CD1 1 ATOM 746 C CD2 . LEU A 1 131 ? 21.767 -6.639 21.299 1.00 15.94 ? 131 LEU A CD2 1 ATOM 747 N N . LEU A 1 132 ? 23.323 -3.389 18.272 1.00 17.11 ? 132 LEU A N 1 ATOM 748 C CA . LEU A 1 132 ? 23.729 -1.998 18.049 1.00 17.03 ? 132 LEU A CA 1 ATOM 749 C C . LEU A 1 132 ? 23.705 -1.339 19.413 1.00 16.76 ? 132 LEU A C 1 ATOM 750 O O . LEU A 1 132 ? 22.643 -1.197 20.003 1.00 16.77 ? 132 LEU A O 1 ATOM 751 C CB . LEU A 1 132 ? 22.761 -1.305 17.080 1.00 17.14 ? 132 LEU A CB 1 ATOM 752 C CG . LEU A 1 132 ? 22.625 0.229 17.073 1.00 17.56 ? 132 LEU A CG 1 ATOM 753 C CD1 . LEU A 1 132 ? 23.959 0.948 17.007 1.00 17.62 ? 132 LEU A CD1 1 ATOM 754 C CD2 . LEU A 1 132 ? 21.768 0.657 15.899 1.00 17.56 ? 132 LEU A CD2 1 ATOM 755 N N . ALA A 1 133 ? 24.875 -0.967 19.925 1.00 16.91 ? 133 ALA A N 1 ATOM 756 C CA . ALA A 1 133 ? 24.983 -0.289 21.222 1.00 17.27 ? 133 ALA A CA 1 ATOM 757 C C . ALA A 1 133 ? 24.892 1.236 21.113 1.00 17.61 ? 133 ALA A C 1 ATOM 758 O O . ALA A 1 133 ? 25.517 1.837 20.245 1.00 17.81 ? 133 ALA A O 1 ATOM 759 C CB . ALA A 1 133 ? 26.282 -0.681 21.900 1.00 17.35 ? 133 ALA A CB 1 ATOM 760 N N . ARG A 1 134 ? 24.130 1.856 22.022 1.00 17.83 ? 134 ARG A N 1 ATOM 761 C CA . ARG A 1 134 ? 23.867 3.295 21.990 1.00 17.99 ? 134 ARG A CA 1 ATOM 762 C C . ARG A 1 134 ? 23.922 3.880 23.406 1.00 17.66 ? 134 ARG A C 1 ATOM 763 O O . ARG A 1 134 ? 22.894 4.144 24.009 1.00 17.88 ? 134 ARG A O 1 ATOM 764 C CB . ARG A 1 134 ? 22.489 3.561 21.360 1.00 18.57 ? 134 ARG A CB 1 ATOM 765 C CG . ARG A 1 134 ? 22.059 2.551 20.298 1.00 18.18 ? 134 ARG A CG 1 ATOM 766 C CD . ARG A 1 134 ? 21.075 3.149 19.318 1.00 18.09 ? 134 ARG A CD 1 ATOM 767 N NE . ARG A 1 134 ? 19.737 3.366 19.870 1.00 18.43 ? 134 ARG A NE 1 ATOM 768 C CZ . ARG A 1 134 ? 18.935 4.369 19.513 1.00 18.70 ? 134 ARG A CZ 1 ATOM 769 N NH1 . ARG A 1 134 ? 19.340 5.265 18.618 1.00 19.71 ? 134 ARG A NH1 1 ATOM 770 N NH2 . ARG A 1 134 ? 17.727 4.482 20.042 1.00 18.42 ? 134 ARG A NH2 1 ATOM 771 N N . PRO A 1 135 ? 25.100 3.998 23.965 1.00 17.58 ? 135 PRO A N 1 ATOM 772 C CA . PRO A 1 135 ? 25.177 4.380 25.370 1.00 17.71 ? 135 PRO A CA 1 ATOM 773 C C . PRO A 1 135 ? 25.099 5.848 25.684 1.00 17.49 ? 135 PRO A C 1 ATOM 774 O O . PRO A 1 135 ? 25.282 6.235 26.759 1.00 17.84 ? 135 PRO A O 1 ATOM 775 C CB . PRO A 1 135 ? 26.513 3.777 25.794 1.00 17.85 ? 135 PRO A CB 1 ATOM 776 C CG . PRO A 1 135 ? 27.325 3.830 24.582 1.00 17.67 ? 135 PRO A CG 1 ATOM 777 C CD . PRO A 1 135 ? 26.432 3.707 23.418 1.00 17.73 ? 135 PRO A CD 1 ATOM 778 N N . GLY A 1 136 ? 24.850 6.633 24.685 1.00 17.40 ? 136 GLY A N 1 ATOM 779 C CA . GLY A 1 136 ? 24.725 8.033 24.825 1.00 17.72 ? 136 GLY A CA 1 ATOM 780 C C . GLY A 1 136 ? 26.000 8.857 24.823 1.00 17.54 ? 136 GLY A C 1 ATOM 781 O O . GLY A 1 136 ? 26.702 8.734 23.900 1.00 17.99 ? 136 GLY A O 1 ATOM 782 N N . PRO A 1 137 ? 26.307 9.714 25.795 1.00 16.82 ? 137 PRO A N 1 ATOM 783 C CA . PRO A 1 137 ? 25.722 9.823 27.130 1.00 16.55 ? 137 PRO A CA 1 ATOM 784 C C . PRO A 1 137 ? 24.278 10.328 27.205 1.00 16.65 ? 137 PRO A C 1 ATOM 785 O O . PRO A 1 137 ? 23.586 9.972 28.089 1.00 16.66 ? 137 PRO A O 1 ATOM 786 C CB . PRO A 1 137 ? 26.641 10.819 27.826 1.00 16.63 ? 137 PRO A CB 1 ATOM 787 C CG . PRO A 1 137 ? 27.843 10.917 27.032 1.00 16.45 ? 137 PRO A CG 1 ATOM 788 C CD . PRO A 1 137 ? 27.648 10.306 25.723 1.00 16.46 ? 137 PRO A CD 1 ATOM 789 N N . TYR A 1 138 ? 23.883 11.112 26.233 1.00 16.02 ? 138 TYR A N 1 ATOM 790 C CA . TYR A 1 138 ? 22.553 11.589 26.130 1.00 15.64 ? 138 TYR A CA 1 ATOM 791 C C . TYR A 1 138 ? 21.777 10.589 25.318 1.00 15.61 ? 138 TYR A C 1 ATOM 792 O O . TYR A 1 138 ? 22.198 10.184 24.283 1.00 15.37 ? 138 TYR A O 1 ATOM 793 C CB . TYR A 1 138 ? 22.468 12.999 25.558 1.00 15.70 ? 138 TYR A CB 1 ATOM 794 C CG . TYR A 1 138 ? 21.078 13.481 25.572 1.00 15.66 ? 138 TYR A CG 1 ATOM 795 C CD1 . TYR A 1 138 ? 20.497 13.869 26.735 1.00 15.72 ? 138 TYR A CD1 1 ATOM 796 C CD2 . TYR A 1 138 ? 20.327 13.504 24.440 1.00 15.91 ? 138 TYR A CD2 1 ATOM 797 C CE1 . TYR A 1 138 ? 19.211 14.273 26.774 1.00 15.94 ? 138 TYR A CE1 1 ATOM 798 C CE2 . TYR A 1 138 ? 19.043 13.942 24.468 1.00 16.30 ? 138 TYR A CE2 1 ATOM 799 C CZ . TYR A 1 138 ? 18.492 14.303 25.643 1.00 16.25 ? 138 TYR A CZ 1 ATOM 800 O OH . TYR A 1 138 ? 17.240 14.709 25.683 1.00 16.56 ? 138 TYR A OH 1 ATOM 801 N N . ILE A 1 139 ? 20.619 10.232 25.805 1.00 15.52 ? 139 ILE A N 1 ATOM 802 C CA . ILE A 1 139 ? 19.819 9.243 25.124 1.00 15.56 ? 139 ILE A CA 1 ATOM 803 C C . ILE A 1 139 ? 18.375 9.605 24.853 1.00 16.42 ? 139 ILE A C 1 ATOM 804 O O . ILE A 1 139 ? 17.763 8.904 24.123 1.00 17.67 ? 139 ILE A O 1 ATOM 805 C CB . ILE A 1 139 ? 19.825 7.874 25.878 1.00 15.22 ? 139 ILE A CB 1 ATOM 806 C CG1 . ILE A 1 139 ? 19.140 7.993 27.251 1.00 15.02 ? 139 ILE A CG1 1 ATOM 807 C CG2 . ILE A 1 139 ? 21.199 7.257 25.881 1.00 14.85 ? 139 ILE A CG2 1 ATOM 808 C CD1 . ILE A 1 139 ? 18.729 6.707 27.876 1.00 14.92 ? 139 ILE A CD1 1 ATOM 809 N N . ASN A 1 140 ? 17.873 10.686 25.458 1.00 16.18 ? 140 ASN A N 1 ATOM 810 C CA . ASN A 1 140 ? 16.495 11.176 25.388 1.00 15.78 ? 140 ASN A CA 1 ATOM 811 C C . ASN A 1 140 ? 15.631 10.067 25.949 1.00 15.60 ? 140 ASN A C 1 ATOM 812 O O . ASN A 1 140 ? 15.509 9.936 27.135 1.00 15.21 ? 140 ASN A O 1 ATOM 813 C CB . ASN A 1 140 ? 16.123 11.666 23.996 1.00 16.11 ? 140 ASN A CB 1 ATOM 814 C CG . ASN A 1 140 ? 14.967 12.657 23.987 1.00 16.17 ? 140 ASN A CG 1 ATOM 815 O OD1 . ASN A 1 140 ? 15.084 13.747 24.420 1.00 15.61 ? 140 ASN A OD1 1 ATOM 816 N ND2 . ASN A 1 140 ? 13.868 12.250 23.442 1.00 16.33 ? 140 ASN A ND2 1 ATOM 817 N N . ALA A 1 141 ? 15.031 9.309 25.072 1.00 15.04 ? 141 ALA A N 1 ATOM 818 C CA . ALA A 1 141 ? 14.370 8.077 25.419 1.00 15.28 ? 141 ALA A CA 1 ATOM 819 C C . ALA A 1 141 ? 13.296 8.081 26.466 1.00 15.31 ? 141 ALA A C 1 ATOM 820 O O . ALA A 1 141 ? 13.045 7.096 27.061 1.00 14.61 ? 141 ALA A O 1 ATOM 821 C CB . ALA A 1 141 ? 15.422 7.037 25.798 1.00 14.89 ? 141 ALA A CB 1 ATOM 822 N N . GLU A 1 142 ? 12.512 9.176 26.611 1.00 15.81 ? 142 GLU A N 1 ATOM 823 C CA . GLU A 1 142 ? 11.494 9.406 27.598 1.00 15.64 ? 142 GLU A CA 1 ATOM 824 C C . GLU A 1 142 ? 12.007 9.028 28.998 1.00 15.06 ? 142 GLU A C 1 ATOM 825 O O . GLU A 1 142 ? 11.279 8.547 29.741 1.00 14.82 ? 142 GLU A O 1 ATOM 826 C CB . GLU A 1 142 ? 10.216 8.632 27.267 1.00 16.17 ? 142 GLU A CB 1 ATOM 827 C CG . GLU A 1 142 ? 9.336 9.195 26.215 1.00 16.39 ? 142 GLU A CG 1 ATOM 828 C CD . GLU A 1 142 ? 9.827 8.990 24.815 1.00 16.92 ? 142 GLU A CD 1 ATOM 829 O OE1 . GLU A 1 142 ? 9.978 7.857 24.354 1.00 16.24 ? 142 GLU A OE1 1 ATOM 830 O OE2 . GLU A 1 142 ? 10.048 10.000 24.206 1.00 17.12 -1 142 GLU A OE2 1 ATOM 831 N N . SER A 1 143 ? 13.274 9.262 29.298 1.00 14.94 ? 143 SER A N 1 ATOM 832 C CA . SER A 1 143 ? 13.868 8.929 30.583 1.00 14.85 ? 143 SER A CA 1 ATOM 833 C C . SER A 1 143 ? 14.177 10.233 31.302 1.00 14.67 ? 143 SER A C 1 ATOM 834 O O . SER A 1 143 ? 14.406 11.253 30.663 1.00 14.29 ? 143 SER A O 1 ATOM 835 C CB . SER A 1 143 ? 15.126 8.092 30.391 1.00 14.94 ? 143 SER A CB 1 ATOM 836 O OG . SER A 1 143 ? 16.103 8.840 29.687 1.00 16.25 ? 143 SER A OG 1 ATOM 837 N N . SER A 1 144 ? 14.145 10.190 32.632 1.00 14.27 ? 144 SER A N 1 ATOM 838 C CA . SER A 1 144 ? 14.452 11.341 33.452 1.00 14.03 ? 144 SER A CA 1 ATOM 839 C C . SER A 1 144 ? 15.821 11.875 33.059 1.00 14.12 ? 144 SER A C 1 ATOM 840 O O . SER A 1 144 ? 16.812 11.128 33.043 1.00 14.35 ? 144 SER A O 1 ATOM 841 C CB . SER A 1 144 ? 14.472 10.943 34.927 1.00 14.22 ? 144 SER A CB 1 ATOM 842 O OG . SER A 1 144 ? 14.789 12.054 35.764 1.00 14.89 ? 144 SER A OG 1 ATOM 843 N N . GLY A 1 145 ? 15.859 13.158 32.719 1.00 13.79 ? 145 GLY A N 1 ATOM 844 C CA . GLY A 1 145 ? 17.092 13.842 32.366 1.00 13.82 ? 145 GLY A CA 1 ATOM 845 C C . GLY A 1 145 ? 17.531 13.505 30.960 1.00 13.72 ? 145 GLY A C 1 ATOM 846 O O . GLY A 1 145 ? 18.647 13.847 30.548 1.00 13.84 ? 145 GLY A O 1 ATOM 847 N N . GLY A 1 146 ? 16.664 12.814 30.224 1.00 13.57 ? 146 GLY A N 1 ATOM 848 C CA . GLY A 1 146 ? 17.063 12.205 28.972 1.00 13.85 ? 146 GLY A CA 1 ATOM 849 C C . GLY A 1 146 ? 18.297 11.336 29.138 1.00 14.24 ? 146 GLY A C 1 ATOM 850 O O . GLY A 1 146 ? 19.048 11.155 28.178 1.00 14.03 ? 146 GLY A O 1 ATOM 851 N N . GLY A 1 147 ? 18.497 10.795 30.347 1.00 14.45 ? 147 GLY A N 1 ATOM 852 C CA . GLY A 1 147 ? 19.652 9.957 30.657 1.00 14.85 ? 147 GLY A CA 1 ATOM 853 C C . GLY A 1 147 ? 20.728 10.609 31.507 1.00 15.25 ? 147 GLY A C 1 ATOM 854 O O . GLY A 1 147 ? 21.505 9.913 32.142 1.00 15.14 ? 147 GLY A O 1 ATOM 855 N N . PHE A 1 148 ? 20.781 11.940 31.515 1.00 15.93 ? 148 PHE A N 1 ATOM 856 C CA . PHE A 1 148 ? 21.721 12.683 32.347 1.00 16.61 ? 148 PHE A CA 1 ATOM 857 C C . PHE A 1 148 ? 21.330 12.583 33.828 1.00 17.44 ? 148 PHE A C 1 ATOM 858 O O . PHE A 1 148 ? 20.158 12.782 34.173 1.00 18.07 ? 148 PHE A O 1 ATOM 859 C CB . PHE A 1 148 ? 21.711 14.178 31.982 1.00 16.82 ? 148 PHE A CB 1 ATOM 860 C CG . PHE A 1 148 ? 22.290 14.511 30.630 1.00 16.89 ? 148 PHE A CG 1 ATOM 861 C CD1 . PHE A 1 148 ? 23.198 13.679 29.995 1.00 17.03 ? 148 PHE A CD1 1 ATOM 862 C CD2 . PHE A 1 148 ? 21.965 15.718 30.026 1.00 17.23 ? 148 PHE A CD2 1 ATOM 863 C CE1 . PHE A 1 148 ? 23.742 14.031 28.773 1.00 17.24 ? 148 PHE A CE1 1 ATOM 864 C CE2 . PHE A 1 148 ? 22.496 16.074 28.809 1.00 17.12 ? 148 PHE A CE2 1 ATOM 865 C CZ . PHE A 1 148 ? 23.391 15.231 28.179 1.00 17.30 ? 148 PHE A CZ 1 ATOM 866 N N . PRO A 1 149 ? 22.305 12.302 34.711 1.00 17.77 ? 149 PRO A N 1 ATOM 867 C CA . PRO A 1 149 ? 22.065 12.318 36.148 1.00 18.04 ? 149 PRO A CA 1 ATOM 868 C C . PRO A 1 149 ? 21.770 13.722 36.645 1.00 18.47 ? 149 PRO A C 1 ATOM 869 O O . PRO A 1 149 ? 22.284 14.702 36.089 1.00 18.34 ? 149 PRO A O 1 ATOM 870 C CB . PRO A 1 149 ? 23.391 11.857 36.747 1.00 17.93 ? 149 PRO A CB 1 ATOM 871 C CG . PRO A 1 149 ? 24.143 11.221 35.649 1.00 17.83 ? 149 PRO A CG 1 ATOM 872 C CD . PRO A 1 149 ? 23.658 11.828 34.379 1.00 17.93 ? 149 PRO A CD 1 ATOM 873 N N . GLY A 1 150 ? 20.974 13.811 37.704 1.00 17.84 ? 150 GLY A N 1 ATOM 874 C CA . GLY A 1 150 ? 20.566 15.099 38.240 1.00 18.02 ? 150 GLY A CA 1 ATOM 875 C C . GLY A 1 150 ? 21.705 16.037 38.571 1.00 17.64 ? 150 GLY A C 1 ATOM 876 O O . GLY A 1 150 ? 21.526 17.244 38.551 1.00 17.54 ? 150 GLY A O 1 ATOM 877 N N . TRP A 1 151 ? 22.882 15.488 38.847 1.00 18.43 ? 151 TRP A N 1 ATOM 878 C CA . TRP A 1 151 ? 24.056 16.312 39.157 1.00 18.85 ? 151 TRP A CA 1 ATOM 879 C C . TRP A 1 151 ? 24.565 17.196 38.024 1.00 19.30 ? 151 TRP A C 1 ATOM 880 O O . TRP A 1 151 ? 25.289 18.151 38.288 1.00 19.40 ? 151 TRP A O 1 ATOM 881 C CB . TRP A 1 151 ? 25.203 15.512 39.809 1.00 18.98 ? 151 TRP A CB 1 ATOM 882 C CG . TRP A 1 151 ? 25.657 14.223 39.198 1.00 19.02 ? 151 TRP A CG 1 ATOM 883 C CD1 . TRP A 1 151 ? 25.228 12.974 39.523 1.00 19.29 ? 151 TRP A CD1 1 ATOM 884 C CD2 . TRP A 1 151 ? 26.718 14.047 38.254 1.00 19.60 ? 151 TRP A CD2 1 ATOM 885 N NE1 . TRP A 1 151 ? 25.918 12.029 38.803 1.00 19.55 ? 151 TRP A NE1 1 ATOM 886 C CE2 . TRP A 1 151 ? 26.837 12.661 38.013 1.00 19.32 ? 151 TRP A CE2 1 ATOM 887 C CE3 . TRP A 1 151 ? 27.563 14.931 37.563 1.00 19.85 ? 151 TRP A CE3 1 ATOM 888 C CZ2 . TRP A 1 151 ? 27.775 12.130 37.123 1.00 19.40 ? 151 TRP A CZ2 1 ATOM 889 C CZ3 . TRP A 1 151 ? 28.501 14.401 36.677 1.00 19.81 ? 151 TRP A CZ3 1 ATOM 890 C CH2 . TRP A 1 151 ? 28.590 13.007 36.464 1.00 19.71 ? 151 TRP A CH2 1 ATOM 891 N N . LEU A 1 152 ? 24.154 16.922 36.785 1.00 20.52 ? 152 LEU A N 1 ATOM 892 C CA . LEU A 1 152 ? 24.411 17.844 35.666 1.00 21.37 ? 152 LEU A CA 1 ATOM 893 C C . LEU A 1 152 ? 23.691 19.208 35.796 1.00 22.04 ? 152 LEU A C 1 ATOM 894 O O . LEU A 1 152 ? 23.991 20.142 35.040 1.00 22.37 ? 152 LEU A O 1 ATOM 895 C CB . LEU A 1 152 ? 24.085 17.188 34.312 1.00 21.46 ? 152 LEU A CB 1 ATOM 896 C CG . LEU A 1 152 ? 25.314 16.582 33.632 1.00 22.32 ? 152 LEU A CG 1 ATOM 897 C CD1 . LEU A 1 152 ? 25.852 15.413 34.443 1.00 22.58 ? 152 LEU A CD1 1 ATOM 898 C CD2 . LEU A 1 152 ? 25.017 16.153 32.202 1.00 22.65 ? 152 LEU A CD2 1 ATOM 899 N N . GLN A 1 153 ? 22.759 19.330 36.743 1.00 21.48 ? 153 GLN A N 1 ATOM 900 C CA . GLN A 1 153 ? 22.197 20.643 37.077 1.00 21.40 ? 153 GLN A CA 1 ATOM 901 C C . GLN A 1 153 ? 23.217 21.547 37.791 1.00 21.69 ? 153 GLN A C 1 ATOM 902 O O . GLN A 1 153 ? 22.976 22.740 37.958 1.00 21.99 ? 153 GLN A O 1 ATOM 903 C CB . GLN A 1 153 ? 20.929 20.508 37.939 1.00 20.86 ? 153 GLN A CB 1 ATOM 904 C CG . GLN A 1 153 ? 19.767 19.787 37.263 1.00 20.91 ? 153 GLN A CG 1 ATOM 905 C CD . GLN A 1 153 ? 18.401 20.318 37.689 1.00 20.78 ? 153 GLN A CD 1 ATOM 906 O OE1 . GLN A 1 153 ? 18.270 20.962 38.732 1.00 20.38 ? 153 GLN A OE1 1 ATOM 907 N NE2 . GLN A 1 153 ? 17.377 20.040 36.886 1.00 19.92 ? 153 GLN A NE2 1 ATOM 908 N N . ARG A 1 154 ? 24.344 20.988 38.219 1.00 21.85 ? 154 ARG A N 1 ATOM 909 C CA . ARG A 1 154 ? 25.390 21.776 38.869 1.00 22.49 ? 154 ARG A CA 1 ATOM 910 C C . ARG A 1 154 ? 26.595 22.048 37.958 1.00 24.00 ? 154 ARG A C 1 ATOM 911 O O . ARG A 1 154 ? 27.588 22.630 38.389 1.00 23.82 ? 154 ARG A O 1 ATOM 912 C CB . ARG A 1 154 ? 25.825 21.083 40.165 1.00 21.70 ? 154 ARG A CB 1 ATOM 913 C CG . ARG A 1 154 ? 24.694 20.930 41.172 1.00 21.04 ? 154 ARG A CG 1 ATOM 914 C CD . ARG A 1 154 ? 25.188 20.683 42.593 1.00 20.80 ? 154 ARG A CD 1 ATOM 915 N NE . ARG A 1 154 ? 26.075 19.521 42.691 1.00 20.38 ? 154 ARG A NE 1 ATOM 916 C CZ . ARG A 1 154 ? 25.680 18.250 42.807 1.00 20.28 ? 154 ARG A CZ 1 ATOM 917 N NH1 . ARG A 1 154 ? 24.381 17.918 42.823 1.00 19.67 ? 154 ARG A NH1 1 ATOM 918 N NH2 . ARG A 1 154 ? 26.600 17.290 42.894 1.00 19.49 ? 154 ARG A NH2 1 ATOM 919 N N . VAL A 1 155 ? 26.487 21.651 36.691 1.00 26.36 ? 155 VAL A N 1 ATOM 920 C CA . VAL A 1 155 ? 27.582 21.781 35.731 1.00 26.68 ? 155 VAL A CA 1 ATOM 921 C C . VAL A 1 155 ? 27.604 23.167 35.092 1.00 27.51 ? 155 VAL A C 1 ATOM 922 O O . VAL A 1 155 ? 26.643 23.606 34.461 1.00 26.14 ? 155 VAL A O 1 ATOM 923 C CB . VAL A 1 155 ? 27.488 20.709 34.629 1.00 26.26 ? 155 VAL A CB 1 ATOM 924 C CG1 . VAL A 1 155 ? 28.461 20.997 33.495 1.00 26.84 ? 155 VAL A CG1 1 ATOM 925 C CG2 . VAL A 1 155 ? 27.786 19.346 35.216 1.00 27.13 ? 155 VAL A CG2 1 ATOM 926 N N . ASN A 1 156 ? 28.734 23.831 35.247 1.00 29.97 ? 156 ASN A N 1 ATOM 927 C CA . ASN A 1 156 ? 28.916 25.169 34.742 1.00 32.81 ? 156 ASN A CA 1 ATOM 928 C C . ASN A 1 156 ? 29.367 25.100 33.291 1.00 31.04 ? 156 ASN A C 1 ATOM 929 O O . ASN A 1 156 ? 30.564 25.152 32.989 1.00 31.48 ? 156 ASN A O 1 ATOM 930 C CB . ASN A 1 156 ? 29.960 25.872 35.601 1.00 37.13 ? 156 ASN A CB 1 ATOM 931 C CG . ASN A 1 156 ? 30.073 27.339 35.294 1.00 43.13 ? 156 ASN A CG 1 ATOM 932 O OD1 . ASN A 1 156 ? 29.232 27.910 34.598 1.00 43.03 ? 156 ASN A OD1 1 ATOM 933 N ND2 . ASN A 1 156 ? 31.124 27.962 35.820 1.00 52.72 ? 156 ASN A ND2 1 ATOM 934 N N . GLY A 1 157 ? 28.401 24.972 32.396 1.00 27.96 ? 157 GLY A N 1 ATOM 935 C CA . GLY A 1 157 ? 28.695 24.741 30.997 1.00 26.70 ? 157 GLY A CA 1 ATOM 936 C C . GLY A 1 157 ? 27.490 24.197 30.260 1.00 25.77 ? 157 GLY A C 1 ATOM 937 O O . GLY A 1 157 ? 26.608 23.572 30.852 1.00 27.11 ? 157 GLY A O 1 ATOM 938 N N . THR A 1 158 ? 27.457 24.440 28.960 1.00 23.47 ? 158 THR A N 1 ATOM 939 C CA . THR A 1 158 ? 26.379 23.976 28.113 1.00 22.92 ? 158 THR A CA 1 ATOM 940 C C . THR A 1 158 ? 26.407 22.463 27.963 1.00 21.89 ? 158 THR A C 1 ATOM 941 O O . THR A 1 158 ? 27.433 21.878 27.642 1.00 20.89 ? 158 THR A O 1 ATOM 942 C CB . THR A 1 158 ? 26.494 24.635 26.729 1.00 22.40 ? 158 THR A CB 1 ATOM 943 O OG1 . THR A 1 158 ? 26.532 26.054 26.907 1.00 22.62 ? 158 THR A OG1 1 ATOM 944 C CG2 . THR A 1 158 ? 25.328 24.273 25.839 1.00 21.77 ? 158 THR A CG2 1 ATOM 945 N N . LEU A 1 159 ? 25.269 21.829 28.204 1.00 22.62 ? 159 LEU A N 1 ATOM 946 C CA . LEU A 1 159 ? 25.154 20.383 28.012 1.00 22.72 ? 159 LEU A CA 1 ATOM 947 C C . LEU A 1 159 ? 25.163 20.058 26.506 1.00 22.04 ? 159 LEU A C 1 ATOM 948 O O . LEU A 1 159 ? 24.587 20.783 25.691 1.00 20.87 ? 159 LEU A O 1 ATOM 949 C CB . LEU A 1 159 ? 23.887 19.837 28.680 1.00 23.19 ? 159 LEU A CB 1 ATOM 950 C CG . LEU A 1 159 ? 23.687 20.152 30.170 1.00 23.73 ? 159 LEU A CG 1 ATOM 951 C CD1 . LEU A 1 159 ? 22.494 19.378 30.714 1.00 23.99 ? 159 LEU A CD1 1 ATOM 952 C CD2 . LEU A 1 159 ? 24.925 19.836 30.991 1.00 23.56 ? 159 LEU A CD2 1 ATOM 953 N N . ARG A 1 160 ? 25.840 18.963 26.171 1.00 21.58 ? 160 ARG A N 1 ATOM 954 C CA . ARG A 1 160 ? 26.018 18.469 24.797 1.00 20.78 ? 160 ARG A CA 1 ATOM 955 C C . ARG A 1 160 ? 26.845 19.439 23.934 1.00 20.90 ? 160 ARG A C 1 ATOM 956 O O . ARG A 1 160 ? 26.617 19.593 22.727 1.00 19.57 ? 160 ARG A O 1 ATOM 957 C CB . ARG A 1 160 ? 24.657 18.117 24.171 1.00 20.27 ? 160 ARG A CB 1 ATOM 958 C CG . ARG A 1 160 ? 23.833 17.126 25.005 1.00 19.58 ? 160 ARG A CG 1 ATOM 959 C CD . ARG A 1 160 ? 22.454 16.855 24.413 1.00 19.01 ? 160 ARG A CD 1 ATOM 960 N NE . ARG A 1 160 ? 22.543 16.231 23.096 1.00 18.63 ? 160 ARG A NE 1 ATOM 961 C CZ . ARG A 1 160 ? 21.542 16.110 22.232 1.00 18.22 ? 160 ARG A CZ 1 ATOM 962 N NH1 . ARG A 1 160 ? 20.330 16.558 22.524 1.00 18.65 ? 160 ARG A NH1 1 ATOM 963 N NH2 . ARG A 1 160 ? 21.754 15.530 21.061 1.00 18.04 ? 160 ARG A NH2 1 ATOM 964 N N . SER A 1 161 ? 27.807 20.099 24.575 1.00 21.81 ? 161 SER A N 1 ATOM 965 C CA . SER A 1 161 ? 28.693 21.051 23.884 1.00 22.75 ? 161 SER A CA 1 ATOM 966 C C . SER A 1 161 ? 30.133 20.680 24.159 1.00 23.75 ? 161 SER A C 1 ATOM 967 O O . SER A 1 161 ? 30.415 19.731 24.926 1.00 23.30 ? 161 SER A O 1 ATOM 968 C CB . SER A 1 161 ? 28.459 22.495 24.356 1.00 22.27 ? 161 SER A CB 1 ATOM 969 O OG . SER A 1 161 ? 29.107 22.738 25.609 1.00 22.49 ? 161 SER A OG 1 ATOM 970 N N . SER A 1 162 ? 31.041 21.451 23.566 1.00 24.07 ? 162 SER A N 1 ATOM 971 C CA . SER A 1 162 ? 32.467 21.270 23.810 1.00 26.01 ? 162 SER A CA 1 ATOM 972 C C . SER A 1 162 ? 32.986 22.038 25.035 1.00 26.44 ? 162 SER A C 1 ATOM 973 O O . SER A 1 162 ? 34.197 22.056 25.256 1.00 27.81 ? 162 SER A O 1 ATOM 974 C CB . SER A 1 162 ? 33.280 21.640 22.554 1.00 26.55 ? 162 SER A CB 1 ATOM 975 O OG . SER A 1 162 ? 33.111 23.006 22.220 1.00 27.03 ? 162 SER A OG 1 ATOM 976 N N . ASP A 1 163 ? 32.107 22.665 25.827 1.00 26.99 ? 163 ASP A N 1 ATOM 977 C CA . ASP A 1 163 ? 32.526 23.264 27.113 1.00 28.60 ? 163 ASP A CA 1 ATOM 978 C C . ASP A 1 163 ? 33.123 22.166 27.981 1.00 29.44 ? 163 ASP A C 1 ATOM 979 O O . ASP A 1 163 ? 32.536 21.084 28.149 1.00 27.74 ? 163 ASP A O 1 ATOM 980 C CB . ASP A 1 163 ? 31.365 23.912 27.877 1.00 29.39 ? 163 ASP A CB 1 ATOM 981 C CG . ASP A 1 163 ? 30.782 25.108 27.162 1.00 30.47 ? 163 ASP A CG 1 ATOM 982 O OD1 . ASP A 1 163 ? 31.372 25.544 26.156 1.00 30.62 ? 163 ASP A OD1 1 ATOM 983 O OD2 . ASP A 1 163 ? 29.717 25.609 27.599 1.00 32.56 -1 163 ASP A OD2 1 ATOM 984 N N . LYS A 1 164 ? 34.294 22.454 28.527 1.00 30.09 ? 164 LYS A N 1 ATOM 985 C CA . LYS A 1 164 ? 35.089 21.441 29.188 1.00 31.70 ? 164 LYS A CA 1 ATOM 986 C C . LYS A 1 164 ? 34.388 20.876 30.419 1.00 28.27 ? 164 LYS A C 1 ATOM 987 O O . LYS A 1 164 ? 34.504 19.692 30.705 1.00 27.92 ? 164 LYS A O 1 ATOM 988 C CB . LYS A 1 164 ? 36.465 21.995 29.550 1.00 34.67 ? 164 LYS A CB 1 ATOM 989 C CG . LYS A 1 164 ? 37.423 20.924 30.045 1.00 38.79 ? 164 LYS A CG 1 ATOM 990 C CD . LYS A 1 164 ? 38.835 21.139 29.507 1.00 41.41 ? 164 LYS A CD 1 ATOM 991 C CE . LYS A 1 164 ? 39.848 20.304 30.277 1.00 42.79 ? 164 LYS A CE 1 ATOM 992 N NZ . LYS A 1 164 ? 39.843 20.628 31.734 1.00 42.22 ? 164 LYS A NZ 1 ATOM 993 N N . ALA A 1 165 ? 33.656 21.725 31.127 1.00 26.42 ? 165 ALA A N 1 ATOM 994 C CA . ALA A 1 165 ? 32.896 21.307 32.304 1.00 25.58 ? 165 ALA A CA 1 ATOM 995 C C . ALA A 1 165 ? 31.862 20.212 31.986 1.00 24.69 ? 165 ALA A C 1 ATOM 996 O O . ALA A 1 165 ? 31.662 19.308 32.804 1.00 24.58 ? 165 ALA A O 1 ATOM 997 C CB . ALA A 1 165 ? 32.220 22.502 32.948 1.00 25.54 ? 165 ALA A CB 1 ATOM 998 N N . TYR A 1 166 ? 31.226 20.283 30.811 1.00 23.25 ? 166 TYR A N 1 ATOM 999 C CA . TYR A 1 166 ? 30.326 19.218 30.371 1.00 23.29 ? 166 TYR A CA 1 ATOM 1000 C C . TYR A 1 166 ? 31.093 17.956 29.956 1.00 24.02 ? 166 TYR A C 1 ATOM 1001 O O . TYR A 1 166 ? 30.730 16.856 30.356 1.00 22.67 ? 166 TYR A O 1 ATOM 1002 C CB . TYR A 1 166 ? 29.405 19.639 29.214 1.00 22.64 ? 166 TYR A CB 1 ATOM 1003 C CG . TYR A 1 166 ? 28.632 18.446 28.677 1.00 22.73 ? 166 TYR A CG 1 ATOM 1004 C CD1 . TYR A 1 166 ? 27.594 17.873 29.414 1.00 22.29 ? 166 TYR A CD1 1 ATOM 1005 C CD2 . TYR A 1 166 ? 28.984 17.844 27.468 1.00 22.31 ? 166 TYR A CD2 1 ATOM 1006 C CE1 . TYR A 1 166 ? 26.902 16.762 28.939 1.00 22.15 ? 166 TYR A CE1 1 ATOM 1007 C CE2 . TYR A 1 166 ? 28.310 16.729 26.996 1.00 21.84 ? 166 TYR A CE2 1 ATOM 1008 C CZ . TYR A 1 166 ? 27.268 16.192 27.729 1.00 22.03 ? 166 TYR A CZ 1 ATOM 1009 O OH . TYR A 1 166 ? 26.610 15.091 27.249 1.00 21.18 ? 166 TYR A OH 1 ATOM 1010 N N . LEU A 1 167 ? 32.124 18.111 29.128 1.00 24.70 ? 167 LEU A N 1 ATOM 1011 C CA . LEU A 1 167 ? 32.869 16.957 28.627 1.00 25.53 ? 167 LEU A CA 1 ATOM 1012 C C . LEU A 1 167 ? 33.566 16.176 29.746 1.00 25.68 ? 167 LEU A C 1 ATOM 1013 O O . LEU A 1 167 ? 33.571 14.941 29.732 1.00 25.59 ? 167 LEU A O 1 ATOM 1014 C CB . LEU A 1 167 ? 33.885 17.384 27.568 1.00 26.06 ? 167 LEU A CB 1 ATOM 1015 C CG . LEU A 1 167 ? 33.319 17.968 26.264 1.00 26.45 ? 167 LEU A CG 1 ATOM 1016 C CD1 . LEU A 1 167 ? 34.461 18.477 25.392 1.00 26.64 ? 167 LEU A CD1 1 ATOM 1017 C CD2 . LEU A 1 167 ? 32.462 16.954 25.518 1.00 26.72 ? 167 LEU A CD2 1 ATOM 1018 N N . ASP A 1 168 ? 34.148 16.885 30.710 1.00 25.47 ? 168 ASP A N 1 ATOM 1019 C CA . ASP A 1 168 ? 34.751 16.227 31.880 1.00 26.67 ? 168 ASP A CA 1 ATOM 1020 C C . ASP A 1 168 ? 33.728 15.447 32.708 1.00 24.59 ? 168 ASP A C 1 ATOM 1021 O O . ASP A 1 168 ? 34.039 14.380 33.236 1.00 23.10 ? 168 ASP A O 1 ATOM 1022 C CB . ASP A 1 168 ? 35.469 17.239 32.787 1.00 28.93 ? 168 ASP A CB 1 ATOM 1023 C CG . ASP A 1 168 ? 36.823 17.671 32.237 1.00 29.95 ? 168 ASP A CG 1 ATOM 1024 O OD1 . ASP A 1 168 ? 37.360 16.958 31.362 1.00 31.11 ? 168 ASP A OD1 1 ATOM 1025 O OD2 . ASP A 1 168 ? 37.346 18.723 32.695 1.00 31.99 -1 168 ASP A OD2 1 ATOM 1026 N N . ALA A 1 169 ? 32.515 15.984 32.825 1.00 23.15 ? 169 ALA A N 1 ATOM 1027 C CA . ALA A 1 169 ? 31.438 15.294 33.537 1.00 22.44 ? 169 ALA A CA 1 ATOM 1028 C C . ALA A 1 169 ? 31.044 13.970 32.872 1.00 21.69 ? 169 ALA A C 1 ATOM 1029 O O . ALA A 1 169 ? 30.571 13.064 33.561 1.00 21.54 ? 169 ALA A O 1 ATOM 1030 C CB . ALA A 1 169 ? 30.217 16.190 33.675 1.00 22.34 ? 169 ALA A CB 1 ATOM 1031 N N . THR A 1 170 ? 31.238 13.850 31.557 1.00 20.46 ? 170 THR A N 1 ATOM 1032 C CA . THR A 1 170 ? 30.959 12.590 30.854 1.00 20.86 ? 170 THR A CA 1 ATOM 1033 C C . THR A 1 170 ? 32.072 11.537 30.881 1.00 21.01 ? 170 THR A C 1 ATOM 1034 O O . THR A 1 170 ? 31.809 10.376 30.574 1.00 20.57 ? 170 THR A O 1 ATOM 1035 C CB . THR A 1 170 ? 30.624 12.808 29.363 1.00 20.37 ? 170 THR A CB 1 ATOM 1036 O OG1 . THR A 1 170 ? 31.800 13.216 28.652 1.00 19.58 ? 170 THR A OG1 1 ATOM 1037 C CG2 . THR A 1 170 ? 29.506 13.824 29.195 1.00 20.30 ? 170 THR A CG2 1 ATOM 1038 N N . ASP A 1 171 ? 33.299 11.931 31.229 1.00 22.10 ? 171 ASP A N 1 ATOM 1039 C CA . ASP A 1 171 ? 34.485 11.086 30.964 1.00 22.28 ? 171 ASP A CA 1 ATOM 1040 C C . ASP A 1 171 ? 34.467 9.751 31.692 1.00 21.39 ? 171 ASP A C 1 ATOM 1041 O O . ASP A 1 171 ? 34.668 8.707 31.078 1.00 21.17 ? 171 ASP A O 1 ATOM 1042 C CB . ASP A 1 171 ? 35.791 11.842 31.285 1.00 23.08 ? 171 ASP A CB 1 ATOM 1043 C CG . ASP A 1 171 ? 36.241 12.770 30.152 1.00 23.74 ? 171 ASP A CG 1 ATOM 1044 O OD1 . ASP A 1 171 ? 35.864 12.557 28.975 1.00 23.05 ? 171 ASP A OD1 1 ATOM 1045 O OD2 . ASP A 1 171 ? 37.001 13.722 30.443 1.00 26.98 -1 171 ASP A OD2 1 ATOM 1046 N N . ASN A 1 172 ? 34.213 9.787 32.995 1.00 21.12 ? 172 ASN A N 1 ATOM 1047 C CA . ASN A 1 172 ? 34.216 8.579 33.809 1.00 21.48 ? 172 ASN A CA 1 ATOM 1048 C C . ASN A 1 172 ? 33.162 7.570 33.366 1.00 21.20 ? 172 ASN A C 1 ATOM 1049 O O . ASN A 1 172 ? 33.427 6.359 33.340 1.00 21.34 ? 172 ASN A O 1 ATOM 1050 C CB . ASN A 1 172 ? 34.010 8.927 35.284 1.00 22.47 ? 172 ASN A CB 1 ATOM 1051 C CG . ASN A 1 172 ? 34.127 7.713 36.198 1.00 23.61 ? 172 ASN A CG 1 ATOM 1052 O OD1 . ASN A 1 172 ? 35.091 6.948 36.117 1.00 23.13 ? 172 ASN A OD1 1 ATOM 1053 N ND2 . ASN A 1 172 ? 33.150 7.543 37.089 1.00 24.46 ? 172 ASN A ND2 1 ATOM 1054 N N . TYR A 1 173 ? 31.974 8.065 33.022 1.00 20.74 ? 173 TYR A N 1 ATOM 1055 C CA . TYR A 1 173 ? 30.891 7.196 32.556 1.00 20.83 ? 173 TYR A CA 1 ATOM 1056 C C . TYR A 1 173 ? 31.270 6.518 31.235 1.00 20.85 ? 173 TYR A C 1 ATOM 1057 O O . TYR A 1 173 ? 31.177 5.294 31.118 1.00 20.52 ? 173 TYR A O 1 ATOM 1058 C CB . TYR A 1 173 ? 29.571 7.972 32.397 1.00 20.35 ? 173 TYR A CB 1 ATOM 1059 C CG . TYR A 1 173 ? 28.518 7.213 31.602 1.00 20.15 ? 173 TYR A CG 1 ATOM 1060 C CD1 . TYR A 1 173 ? 27.800 6.171 32.176 1.00 19.87 ? 173 TYR A CD1 1 ATOM 1061 C CD2 . TYR A 1 173 ? 28.248 7.545 30.279 1.00 19.70 ? 173 TYR A CD2 1 ATOM 1062 C CE1 . TYR A 1 173 ? 26.852 5.469 31.451 1.00 20.19 ? 173 TYR A CE1 1 ATOM 1063 C CE2 . TYR A 1 173 ? 27.300 6.858 29.546 1.00 20.15 ? 173 TYR A CE2 1 ATOM 1064 C CZ . TYR A 1 173 ? 26.604 5.810 30.134 1.00 19.95 ? 173 TYR A CZ 1 ATOM 1065 O OH . TYR A 1 173 ? 25.654 5.126 29.405 1.00 18.70 ? 173 TYR A OH 1 ATOM 1066 N N . VAL A 1 174 ? 31.708 7.310 30.258 1.00 20.51 ? 174 VAL A N 1 ATOM 1067 C CA . VAL A 1 174 ? 31.968 6.770 28.925 1.00 22.02 ? 174 VAL A CA 1 ATOM 1068 C C . VAL A 1 174 ? 33.131 5.781 28.935 1.00 22.96 ? 174 VAL A C 1 ATOM 1069 O O . VAL A 1 174 ? 33.060 4.750 28.258 1.00 23.84 ? 174 VAL A O 1 ATOM 1070 C CB . VAL A 1 174 ? 32.243 7.858 27.859 1.00 22.07 ? 174 VAL A CB 1 ATOM 1071 C CG1 . VAL A 1 174 ? 32.585 7.210 26.518 1.00 22.38 ? 174 VAL A CG1 1 ATOM 1072 C CG2 . VAL A 1 174 ? 31.040 8.766 27.696 1.00 21.50 ? 174 VAL A CG2 1 ATOM 1073 N N . SER A 1 175 ? 34.183 6.074 29.702 1.00 22.92 ? 175 SER A N 1 ATOM 1074 C CA . SER A 1 175 ? 35.345 5.178 29.738 1.00 22.96 ? 175 SER A CA 1 ATOM 1075 C C . SER A 1 175 ? 35.010 3.822 30.372 1.00 22.21 ? 175 SER A C 1 ATOM 1076 O O . SER A 1 175 ? 35.603 2.820 29.995 1.00 22.64 ? 175 SER A O 1 ATOM 1077 C CB . SER A 1 175 ? 36.558 5.833 30.415 1.00 23.19 ? 175 SER A CB 1 ATOM 1078 O OG . SER A 1 175 ? 36.430 5.844 31.821 1.00 25.09 ? 175 SER A OG 1 ATOM 1079 N N . HIS A 1 176 ? 34.052 3.786 31.301 1.00 21.37 ? 176 HIS A N 1 ATOM 1080 C CA . HIS A 1 176 ? 33.593 2.513 31.883 1.00 21.22 ? 176 HIS A CA 1 ATOM 1081 C C . HIS A 1 176 ? 32.630 1.743 30.970 1.00 20.56 ? 176 HIS A C 1 ATOM 1082 O O . HIS A 1 176 ? 32.849 0.576 30.684 1.00 20.16 ? 176 HIS A O 1 ATOM 1083 C CB . HIS A 1 176 ? 32.926 2.733 33.246 1.00 21.59 ? 176 HIS A CB 1 ATOM 1084 C CG . HIS A 1 176 ? 33.897 2.884 34.372 1.00 22.16 ? 176 HIS A CG 1 ATOM 1085 N ND1 . HIS A 1 176 ? 34.337 4.111 34.819 1.00 22.20 ? 176 HIS A ND1 1 ATOM 1086 C CD2 . HIS A 1 176 ? 34.528 1.956 35.130 1.00 22.75 ? 176 HIS A CD2 1 ATOM 1087 C CE1 . HIS A 1 176 ? 35.184 3.932 35.818 1.00 22.50 ? 176 HIS A CE1 1 ATOM 1088 N NE2 . HIS A 1 176 ? 35.316 2.635 36.026 1.00 22.75 ? 176 HIS A NE2 1 ATOM 1089 N N . VAL A 1 177 ? 31.566 2.400 30.516 1.00 19.94 ? 177 VAL A N 1 ATOM 1090 C CA . VAL A 1 177 ? 30.535 1.713 29.749 1.00 19.56 ? 177 VAL A CA 1 ATOM 1091 C C . VAL A 1 177 ? 31.035 1.271 28.372 1.00 18.98 ? 177 VAL A C 1 ATOM 1092 O O . VAL A 1 177 ? 30.685 0.195 27.890 1.00 17.84 ? 177 VAL A O 1 ATOM 1093 C CB . VAL A 1 177 ? 29.245 2.558 29.639 1.00 19.51 ? 177 VAL A CB 1 ATOM 1094 C CG1 . VAL A 1 177 ? 29.399 3.677 28.630 1.00 19.43 ? 177 VAL A CG1 1 ATOM 1095 C CG2 . VAL A 1 177 ? 28.052 1.669 29.292 1.00 19.83 ? 177 VAL A CG2 1 ATOM 1096 N N . ALA A 1 178 ? 31.871 2.099 27.758 1.00 19.43 ? 178 ALA A N 1 ATOM 1097 C CA . ALA A 1 178 ? 32.459 1.779 26.457 1.00 19.42 ? 178 ALA A CA 1 ATOM 1098 C C . ALA A 1 178 ? 33.485 0.641 26.570 1.00 19.54 ? 178 ALA A C 1 ATOM 1099 O O . ALA A 1 178 ? 33.637 -0.147 25.637 1.00 20.91 ? 178 ALA A O 1 ATOM 1100 C CB . ALA A 1 178 ? 33.082 3.023 25.841 1.00 19.02 ? 178 ALA A CB 1 ATOM 1101 N N . ALA A 1 179 ? 34.160 0.534 27.711 1.00 19.09 ? 179 ALA A N 1 ATOM 1102 C CA . ALA A 1 179 ? 35.080 -0.586 27.958 1.00 19.57 ? 179 ALA A CA 1 ATOM 1103 C C . ALA A 1 179 ? 34.319 -1.918 28.054 1.00 20.07 ? 179 ALA A C 1 ATOM 1104 O O . ALA A 1 179 ? 34.761 -2.924 27.521 1.00 20.14 ? 179 ALA A O 1 ATOM 1105 C CB . ALA A 1 179 ? 35.909 -0.340 29.217 1.00 19.03 ? 179 ALA A CB 1 ATOM 1106 N N . THR A 1 180 ? 33.163 -1.914 28.718 1.00 20.39 ? 180 THR A N 1 ATOM 1107 C CA . THR A 1 180 ? 32.303 -3.098 28.777 1.00 19.35 ? 180 THR A CA 1 ATOM 1108 C C . THR A 1 180 ? 31.770 -3.465 27.392 1.00 19.06 ? 180 THR A C 1 ATOM 1109 O O . THR A 1 180 ? 31.786 -4.635 26.999 1.00 18.37 ? 180 THR A O 1 ATOM 1110 C CB . THR A 1 180 ? 31.125 -2.872 29.732 1.00 19.43 ? 180 THR A CB 1 ATOM 1111 O OG1 . THR A 1 180 ? 31.622 -2.367 30.963 1.00 19.17 ? 180 THR A OG1 1 ATOM 1112 C CG2 . THR A 1 180 ? 30.378 -4.165 30.010 1.00 19.73 ? 180 THR A CG2 1 ATOM 1113 N N . ILE A 1 181 ? 31.316 -2.458 26.649 1.00 18.30 ? 181 ILE A N 1 ATOM 1114 C CA . ILE A 1 181 ? 30.884 -2.656 25.276 1.00 17.72 ? 181 ILE A CA 1 ATOM 1115 C C . ILE A 1 181 ? 32.024 -3.231 24.418 1.00 18.00 ? 181 ILE A C 1 ATOM 1116 O O . ILE A 1 181 ? 31.809 -4.144 23.606 1.00 17.41 ? 181 ILE A O 1 ATOM 1117 C CB . ILE A 1 181 ? 30.321 -1.341 24.683 1.00 17.87 ? 181 ILE A CB 1 ATOM 1118 C CG1 . ILE A 1 181 ? 28.952 -1.039 25.310 1.00 17.91 ? 181 ILE A CG1 1 ATOM 1119 C CG2 . ILE A 1 181 ? 30.171 -1.434 23.171 1.00 17.66 ? 181 ILE A CG2 1 ATOM 1120 C CD1 . ILE A 1 181 ? 28.424 0.366 25.073 1.00 17.60 ? 181 ILE A CD1 1 ATOM 1121 N N . ALA A 1 182 ? 33.235 -2.716 24.626 1.00 18.54 ? 182 ALA A N 1 ATOM 1122 C CA . ALA A 1 182 ? 34.423 -3.141 23.857 1.00 19.07 ? 182 ALA A CA 1 ATOM 1123 C C . ALA A 1 182 ? 34.710 -4.619 24.018 1.00 19.17 ? 182 ALA A C 1 ATOM 1124 O O . ALA A 1 182 ? 34.992 -5.328 23.034 1.00 19.47 ? 182 ALA A O 1 ATOM 1125 C CB . ALA A 1 182 ? 35.643 -2.335 24.271 1.00 18.97 ? 182 ALA A CB 1 ATOM 1126 N N . LYS A 1 183 ? 34.613 -5.072 25.262 1.00 19.34 ? 183 LYS A N 1 ATOM 1127 C CA . LYS A 1 183 ? 34.813 -6.470 25.614 1.00 20.02 ? 183 LYS A CA 1 ATOM 1128 C C . LYS A 1 183 ? 33.864 -7.431 24.899 1.00 18.84 ? 183 LYS A C 1 ATOM 1129 O O . LYS A 1 183 ? 34.184 -8.607 24.751 1.00 19.76 ? 183 LYS A O 1 ATOM 1130 C CB . LYS A 1 183 ? 34.657 -6.653 27.133 1.00 21.46 ? 183 LYS A CB 1 ATOM 1131 C CG . LYS A 1 183 ? 34.960 -8.076 27.587 1.00 23.27 ? 183 LYS A CG 1 ATOM 1132 C CD . LYS A 1 183 ? 35.248 -8.177 29.072 1.00 24.70 ? 183 LYS A CD 1 ATOM 1133 C CE . LYS A 1 183 ? 35.759 -9.572 29.395 1.00 25.27 ? 183 LYS A CE 1 ATOM 1134 N NZ . LYS A 1 183 ? 35.958 -9.770 30.855 1.00 26.11 ? 183 LYS A NZ 1 ATOM 1135 N N . TYR A 1 184 ? 32.693 -6.947 24.491 1.00 18.00 ? 184 TYR A N 1 ATOM 1136 C CA . TYR A 1 184 ? 31.673 -7.783 23.872 1.00 17.17 ? 184 TYR A CA 1 ATOM 1137 C C . TYR A 1 184 ? 31.454 -7.456 22.403 1.00 17.21 ? 184 TYR A C 1 ATOM 1138 O O . TYR A 1 184 ? 30.425 -7.809 21.837 1.00 17.11 ? 184 TYR A O 1 ATOM 1139 C CB . TYR A 1 184 ? 30.365 -7.658 24.645 1.00 17.33 ? 184 TYR A CB 1 ATOM 1140 C CG . TYR A 1 184 ? 30.413 -8.384 25.980 1.00 17.62 ? 184 TYR A CG 1 ATOM 1141 C CD1 . TYR A 1 184 ? 31.052 -7.814 27.079 1.00 17.12 ? 184 TYR A CD1 1 ATOM 1142 C CD2 . TYR A 1 184 ? 29.825 -9.633 26.138 1.00 16.96 ? 184 TYR A CD2 1 ATOM 1143 C CE1 . TYR A 1 184 ? 31.111 -8.471 28.287 1.00 17.18 ? 184 TYR A CE1 1 ATOM 1144 C CE2 . TYR A 1 184 ? 29.871 -10.291 27.348 1.00 17.05 ? 184 TYR A CE2 1 ATOM 1145 C CZ . TYR A 1 184 ? 30.515 -9.710 28.418 1.00 17.45 ? 184 TYR A CZ 1 ATOM 1146 O OH . TYR A 1 184 ? 30.582 -10.363 29.633 1.00 18.29 ? 184 TYR A OH 1 ATOM 1147 N N . GLN A 1 185 ? 32.421 -6.804 21.770 1.00 16.98 ? 185 GLN A N 1 ATOM 1148 C CA . GLN A 1 185 ? 32.339 -6.582 20.336 1.00 17.75 ? 185 GLN A CA 1 ATOM 1149 C C . GLN A 1 185 ? 32.444 -7.913 19.634 1.00 18.10 ? 185 GLN A C 1 ATOM 1150 O O . GLN A 1 185 ? 32.914 -8.897 20.218 1.00 18.35 ? 185 GLN A O 1 ATOM 1151 C CB . GLN A 1 185 ? 33.465 -5.678 19.841 1.00 17.91 ? 185 GLN A CB 1 ATOM 1152 C CG . GLN A 1 185 ? 33.323 -4.239 20.278 1.00 18.23 ? 185 GLN A CG 1 ATOM 1153 C CD . GLN A 1 185 ? 34.592 -3.455 20.051 1.00 18.15 ? 185 GLN A CD 1 ATOM 1154 O OE1 . GLN A 1 185 ? 34.619 -2.529 19.259 1.00 17.89 ? 185 GLN A OE1 1 ATOM 1155 N NE2 . GLN A 1 185 ? 35.652 -3.826 20.749 1.00 18.38 ? 185 GLN A NE2 1 ATOM 1156 N N . ILE A 1 186 ? 32.023 -7.924 18.375 1.00 18.34 ? 186 ILE A N 1 ATOM 1157 C CA . ILE A 1 186 ? 32.183 -9.089 17.506 1.00 19.27 ? 186 ILE A CA 1 ATOM 1158 C C . ILE A 1 186 ? 33.654 -9.446 17.249 1.00 19.82 ? 186 ILE A C 1 ATOM 1159 O O . ILE A 1 186 ? 33.979 -10.608 16.991 1.00 20.99 ? 186 ILE A O 1 ATOM 1160 C CB . ILE A 1 186 ? 31.438 -8.914 16.166 1.00 18.86 ? 186 ILE A CB 1 ATOM 1161 C CG1 . ILE A 1 186 ? 31.582 -10.181 15.329 1.00 19.14 ? 186 ILE A CG1 1 ATOM 1162 C CG2 . ILE A 1 186 ? 31.938 -7.695 15.398 1.00 19.05 ? 186 ILE A CG2 1 ATOM 1163 C CD1 . ILE A 1 186 ? 30.465 -10.353 14.334 1.00 19.77 ? 186 ILE A CD1 1 ATOM 1164 N N . THR A 1 187 ? 34.528 -8.449 17.335 1.00 20.24 ? 187 THR A N 1 ATOM 1165 C CA . THR A 1 187 ? 35.970 -8.654 17.201 1.00 21.00 ? 187 THR A CA 1 ATOM 1166 C C . THR A 1 187 ? 36.515 -9.503 18.343 1.00 21.46 ? 187 THR A C 1 ATOM 1167 O O . THR A 1 187 ? 37.592 -10.081 18.209 1.00 22.14 ? 187 THR A O 1 ATOM 1168 C CB . THR A 1 187 ? 36.730 -7.312 17.190 1.00 20.86 ? 187 THR A CB 1 ATOM 1169 O OG1 . THR A 1 187 ? 36.354 -6.542 18.336 1.00 20.85 ? 187 THR A OG1 1 ATOM 1170 C CG2 . THR A 1 187 ? 36.394 -6.521 15.947 1.00 21.12 ? 187 THR A CG2 1 ATOM 1171 N N . ASN A 1 188 ? 35.782 -9.542 19.464 1.00 21.26 ? 188 ASN A N 1 ATOM 1172 C CA . ASN A 1 188 ? 36.159 -10.332 20.624 1.00 20.88 ? 188 ASN A CA 1 ATOM 1173 C C . ASN A 1 188 ? 35.198 -11.487 20.897 1.00 20.88 ? 188 ASN A C 1 ATOM 1174 O O . ASN A 1 188 ? 35.066 -11.921 22.036 1.00 20.36 ? 188 ASN A O 1 ATOM 1175 C CB . ASN A 1 188 ? 36.235 -9.436 21.858 1.00 21.04 ? 188 ASN A CB 1 ATOM 1176 C CG . ASN A 1 188 ? 37.185 -9.974 22.906 1.00 21.46 ? 188 ASN A CG 1 ATOM 1177 O OD1 . ASN A 1 188 ? 38.238 -10.501 22.568 1.00 22.43 ? 188 ASN A OD1 1 ATOM 1178 N ND2 . ASN A 1 188 ? 36.831 -9.831 24.183 1.00 21.42 ? 188 ASN A ND2 1 ATOM 1179 N N . GLY A 1 189 ? 34.547 -11.995 19.853 1.00 21.13 ? 189 GLY A N 1 ATOM 1180 C CA . GLY A 1 189 ? 33.638 -13.137 19.985 1.00 20.94 ? 189 GLY A CA 1 ATOM 1181 C C . GLY A 1 189 ? 32.266 -12.772 20.528 1.00 21.28 ? 189 GLY A C 1 ATOM 1182 O O . GLY A 1 189 ? 31.449 -13.656 20.762 1.00 20.16 ? 189 GLY A O 1 ATOM 1183 N N . GLY A 1 190 ? 32.017 -11.472 20.738 1.00 21.38 ? 190 GLY A N 1 ATOM 1184 C CA . GLY A 1 190 ? 30.740 -10.998 21.278 1.00 21.49 ? 190 GLY A CA 1 ATOM 1185 C C . GLY A 1 190 ? 29.683 -10.757 20.208 1.00 20.84 ? 190 GLY A C 1 ATOM 1186 O O . GLY A 1 190 ? 29.921 -10.993 19.035 1.00 21.69 ? 190 GLY A O 1 ATOM 1187 N N . PRO A 1 191 ? 28.497 -10.281 20.610 1.00 20.18 ? 191 PRO A N 1 ATOM 1188 C CA . PRO A 1 191 ? 27.451 -9.991 19.638 1.00 19.46 ? 191 PRO A CA 1 ATOM 1189 C C . PRO A 1 191 ? 27.403 -8.540 19.132 1.00 18.64 ? 191 PRO A C 1 ATOM 1190 O O . PRO A 1 191 ? 26.615 -8.254 18.245 1.00 18.46 ? 191 PRO A O 1 ATOM 1191 C CB . PRO A 1 191 ? 26.181 -10.294 20.421 1.00 19.08 ? 191 PRO A CB 1 ATOM 1192 C CG . PRO A 1 191 ? 26.527 -9.902 21.817 1.00 19.73 ? 191 PRO A CG 1 ATOM 1193 C CD . PRO A 1 191 ? 28.012 -10.107 21.991 1.00 19.81 ? 191 PRO A CD 1 ATOM 1194 N N . ILE A 1 192 ? 28.210 -7.634 19.671 1.00 18.18 ? 192 ILE A N 1 ATOM 1195 C CA . ILE A 1 192 ? 28.027 -6.211 19.368 1.00 18.13 ? 192 ILE A CA 1 ATOM 1196 C C . ILE A 1 192 ? 28.705 -5.823 18.068 1.00 18.33 ? 192 ILE A C 1 ATOM 1197 O O . ILE A 1 192 ? 29.933 -5.944 17.944 1.00 18.40 ? 192 ILE A O 1 ATOM 1198 C CB . ILE A 1 192 ? 28.544 -5.298 20.488 1.00 18.41 ? 192 ILE A CB 1 ATOM 1199 C CG1 . ILE A 1 192 ? 27.875 -5.658 21.817 1.00 18.73 ? 192 ILE A CG1 1 ATOM 1200 C CG2 . ILE A 1 192 ? 28.258 -3.846 20.143 1.00 18.47 ? 192 ILE A CG2 1 ATOM 1201 C CD1 . ILE A 1 192 ? 28.286 -4.780 22.983 1.00 18.91 ? 192 ILE A CD1 1 ATOM 1202 N N . ILE A 1 193 ? 27.907 -5.309 17.122 1.00 18.11 ? 193 ILE A N 1 ATOM 1203 C CA . ILE A 1 193 ? 28.380 -5.049 15.751 1.00 17.74 ? 193 ILE A CA 1 ATOM 1204 C C . ILE A 1 193 ? 28.458 -3.583 15.342 1.00 17.89 ? 193 ILE A C 1 ATOM 1205 O O . ILE A 1 193 ? 29.219 -3.255 14.431 1.00 18.68 ? 193 ILE A O 1 ATOM 1206 C CB . ILE A 1 193 ? 27.525 -5.782 14.700 1.00 17.60 ? 193 ILE A CB 1 ATOM 1207 C CG1 . ILE A 1 193 ? 26.059 -5.343 14.798 1.00 17.43 ? 193 ILE A CG1 1 ATOM 1208 C CG2 . ILE A 1 193 ? 27.646 -7.291 14.885 1.00 17.82 ? 193 ILE A CG2 1 ATOM 1209 C CD1 . ILE A 1 193 ? 25.226 -5.724 13.604 1.00 17.30 ? 193 ILE A CD1 1 ATOM 1210 N N . LEU A 1 194 ? 27.665 -2.714 15.974 1.00 17.49 ? 194 LEU A N 1 ATOM 1211 C CA . LEU A 1 194 ? 27.679 -1.280 15.676 1.00 16.78 ? 194 LEU A CA 1 ATOM 1212 C C . LEU A 1 194 ? 27.595 -0.466 16.970 1.00 16.57 ? 194 LEU A C 1 ATOM 1213 O O . LEU A 1 194 ? 27.082 -0.951 17.984 1.00 15.95 ? 194 LEU A O 1 ATOM 1214 C CB . LEU A 1 194 ? 26.503 -0.912 14.770 1.00 16.82 ? 194 LEU A CB 1 ATOM 1215 C CG . LEU A 1 194 ? 26.402 -1.527 13.381 1.00 16.70 ? 194 LEU A CG 1 ATOM 1216 C CD1 . LEU A 1 194 ? 24.999 -1.340 12.854 1.00 16.87 ? 194 LEU A CD1 1 ATOM 1217 C CD2 . LEU A 1 194 ? 27.394 -0.880 12.435 1.00 16.99 ? 194 LEU A CD2 1 ATOM 1218 N N . TYR A 1 195 ? 28.088 0.771 16.923 1.00 16.15 ? 195 TYR A N 1 ATOM 1219 C CA . TYR A 1 195 ? 28.084 1.659 18.086 1.00 16.42 ? 195 TYR A CA 1 ATOM 1220 C C . TYR A 1 195 ? 27.601 3.040 17.666 1.00 17.32 ? 195 TYR A C 1 ATOM 1221 O O . TYR A 1 195 ? 28.099 3.600 16.681 1.00 17.23 ? 195 TYR A O 1 ATOM 1222 C CB . TYR A 1 195 ? 29.498 1.763 18.651 1.00 16.18 ? 195 TYR A CB 1 ATOM 1223 C CG . TYR A 1 195 ? 29.674 2.578 19.926 1.00 16.14 ? 195 TYR A CG 1 ATOM 1224 C CD1 . TYR A 1 195 ? 29.691 3.973 19.903 1.00 15.97 ? 195 TYR A CD1 1 ATOM 1225 C CD2 . TYR A 1 195 ? 29.884 1.948 21.151 1.00 15.98 ? 195 TYR A CD2 1 ATOM 1226 C CE1 . TYR A 1 195 ? 29.879 4.712 21.064 1.00 15.55 ? 195 TYR A CE1 1 ATOM 1227 C CE2 . TYR A 1 195 ? 30.071 2.684 22.312 1.00 16.14 ? 195 TYR A CE2 1 ATOM 1228 C CZ . TYR A 1 195 ? 30.057 4.065 22.260 1.00 15.85 ? 195 TYR A CZ 1 ATOM 1229 O OH . TYR A 1 195 ? 30.261 4.781 23.413 1.00 15.95 ? 195 TYR A OH 1 ATOM 1230 N N . GLN A 1 196 ? 26.692 3.586 18.439 1.00 17.90 ? 196 GLN A N 1 ATOM 1231 C CA . GLN A 1 196 ? 26.162 4.897 18.239 1.00 18.08 ? 196 GLN A CA 1 ATOM 1232 C C . GLN A 1 196 ? 26.690 5.912 19.226 1.00 19.05 ? 196 GLN A C 1 ATOM 1233 O O . GLN A 1 196 ? 26.476 5.808 20.380 1.00 21.06 ? 196 GLN A O 1 ATOM 1234 C CB . GLN A 1 196 ? 24.651 4.916 18.322 1.00 17.91 ? 196 GLN A CB 1 ATOM 1235 C CG . GLN A 1 196 ? 24.079 6.313 18.134 1.00 17.72 ? 196 GLN A CG 1 ATOM 1236 C CD . GLN A 1 196 ? 22.584 6.363 18.150 1.00 17.86 ? 196 GLN A CD 1 ATOM 1237 O OE1 . GLN A 1 196 ? 21.926 5.912 17.254 1.00 17.34 ? 196 GLN A OE1 1 ATOM 1238 N NE2 . GLN A 1 196 ? 22.056 6.896 19.194 1.00 18.51 ? 196 GLN A NE2 1 ATOM 1239 N N . PRO A 1 197 ? 27.447 6.877 18.787 1.00 19.30 ? 197 PRO A N 1 ATOM 1240 C CA . PRO A 1 197 ? 27.935 7.930 19.682 1.00 19.91 ? 197 PRO A CA 1 ATOM 1241 C C . PRO A 1 197 ? 26.906 9.066 19.755 1.00 19.41 ? 197 PRO A C 1 ATOM 1242 O O . PRO A 1 197 ? 26.467 9.376 18.736 1.00 19.32 ? 197 PRO A O 1 ATOM 1243 C CB . PRO A 1 197 ? 29.188 8.366 18.995 1.00 20.17 ? 197 PRO A CB 1 ATOM 1244 C CG . PRO A 1 197 ? 28.825 8.266 17.589 1.00 19.98 ? 197 PRO A CG 1 ATOM 1245 C CD . PRO A 1 197 ? 27.917 7.099 17.433 1.00 19.72 ? 197 PRO A CD 1 ATOM 1246 N N . GLU A 1 198 ? 26.549 9.628 20.904 1.00 18.65 ? 198 GLU A N 1 ATOM 1247 C CA . GLU A 1 198 ? 25.516 10.697 21.057 1.00 18.90 ? 198 GLU A CA 1 ATOM 1248 C C . GLU A 1 198 ? 24.096 10.267 20.684 1.00 18.60 ? 198 GLU A C 1 ATOM 1249 O O . GLU A 1 198 ? 23.815 9.137 20.546 1.00 19.62 ? 198 GLU A O 1 ATOM 1250 C CB . GLU A 1 198 ? 25.889 12.043 20.373 1.00 18.63 ? 198 GLU A CB 1 ATOM 1251 C CG . GLU A 1 198 ? 26.208 13.208 21.271 1.00 19.02 ? 198 GLU A CG 1 ATOM 1252 C CD . GLU A 1 198 ? 24.990 14.013 21.670 1.00 19.17 ? 198 GLU A CD 1 ATOM 1253 O OE1 . GLU A 1 198 ? 25.074 14.824 22.539 1.00 19.61 ? 198 GLU A OE1 1 ATOM 1254 O OE2 . GLU A 1 198 ? 23.945 13.826 21.158 1.00 20.06 -1 198 GLU A OE2 1 ATOM 1255 N N . ASN A 1 199 ? 23.193 11.191 20.527 1.00 18.01 ? 199 ASN A N 1 ATOM 1256 C CA . ASN A 1 199 ? 21.819 10.878 20.123 1.00 18.00 ? 199 ASN A CA 1 ATOM 1257 C C . ASN A 1 199 ? 21.139 12.027 19.520 1.00 17.55 ? 199 ASN A C 1 ATOM 1258 O O . ASN A 1 199 ? 20.828 12.985 20.163 1.00 17.37 ? 199 ASN A O 1 ATOM 1259 C CB . ASN A 1 199 ? 20.947 10.379 21.270 1.00 18.05 ? 199 ASN A CB 1 ATOM 1260 C CG . ASN A 1 199 ? 19.674 9.744 20.798 1.00 18.25 ? 199 ASN A CG 1 ATOM 1261 O OD1 . ASN A 1 199 ? 19.686 8.669 20.354 1.00 19.33 ? 199 ASN A OD1 1 ATOM 1262 N ND2 . ASN A 1 199 ? 18.589 10.426 20.922 1.00 18.67 ? 199 ASN A ND2 1 ATOM 1263 N N . GLU A 1 200 ? 20.717 11.863 18.283 1.00 17.52 ? 200 GLU A N 1 ATOM 1264 C CA . GLU A 1 200 ? 20.045 12.880 17.524 1.00 18.40 ? 200 GLU A CA 1 ATOM 1265 C C . GLU A 1 200 ? 20.630 14.294 17.634 1.00 18.35 ? 200 GLU A C 1 ATOM 1266 O O . GLU A 1 200 ? 19.926 15.197 17.855 1.00 17.67 ? 200 GLU A O 1 ATOM 1267 C CB . GLU A 1 200 ? 18.525 12.893 17.736 1.00 18.86 ? 200 GLU A CB 1 ATOM 1268 C CG . GLU A 1 200 ? 17.775 11.662 17.331 1.00 19.45 ? 200 GLU A CG 1 ATOM 1269 C CD . GLU A 1 200 ? 16.285 11.731 17.568 1.00 20.00 ? 200 GLU A CD 1 ATOM 1270 O OE1 . GLU A 1 200 ? 15.833 12.471 18.425 1.00 20.53 ? 200 GLU A OE1 1 ATOM 1271 O OE2 . GLU A 1 200 ? 15.586 11.030 16.882 1.00 20.27 -1 200 GLU A OE2 1 ATOM 1272 N N . TYR A 1 201 ? 21.933 14.429 17.418 1.00 18.61 ? 201 TYR A N 1 ATOM 1273 C CA . TYR A 1 201 ? 22.656 15.679 17.402 1.00 19.45 ? 201 TYR A CA 1 ATOM 1274 C C . TYR A 1 201 ? 22.242 16.289 16.090 1.00 19.83 ? 201 TYR A C 1 ATOM 1275 O O . TYR A 1 201 ? 22.828 16.052 15.101 1.00 20.34 ? 201 TYR A O 1 ATOM 1276 C CB . TYR A 1 201 ? 24.173 15.436 17.528 1.00 19.32 ? 201 TYR A CB 1 ATOM 1277 C CG . TYR A 1 201 ? 25.018 16.660 17.702 1.00 18.97 ? 201 TYR A CG 1 ATOM 1278 C CD1 . TYR A 1 201 ? 24.975 17.417 18.851 1.00 19.19 ? 201 TYR A CD1 1 ATOM 1279 C CD2 . TYR A 1 201 ? 25.857 17.062 16.712 1.00 19.12 ? 201 TYR A CD2 1 ATOM 1280 C CE1 . TYR A 1 201 ? 25.757 18.525 18.992 1.00 19.25 ? 201 TYR A CE1 1 ATOM 1281 C CE2 . TYR A 1 201 ? 26.645 18.161 16.843 1.00 18.72 ? 201 TYR A CE2 1 ATOM 1282 C CZ . TYR A 1 201 ? 26.602 18.886 17.976 1.00 19.20 ? 201 TYR A CZ 1 ATOM 1283 O OH . TYR A 1 201 ? 27.345 19.967 18.066 1.00 18.78 ? 201 TYR A OH 1 ATOM 1284 N N . THR A 1 202 ? 21.195 17.096 16.142 1.00 21.72 ? 202 THR A N 1 ATOM 1285 C CA . THR A 1 202 ? 20.475 17.606 14.988 1.00 22.72 ? 202 THR A CA 1 ATOM 1286 C C . THR A 1 202 ? 20.045 19.060 15.052 1.00 25.33 ? 202 THR A C 1 ATOM 1287 O O . THR A 1 202 ? 20.047 19.718 14.068 1.00 26.67 ? 202 THR A O 1 ATOM 1288 C CB . THR A 1 202 ? 19.193 16.751 14.782 1.00 22.24 ? 202 THR A CB 1 ATOM 1289 O OG1 . THR A 1 202 ? 19.499 15.384 14.720 1.00 21.38 ? 202 THR A OG1 1 ATOM 1290 C CG2 . THR A 1 202 ? 18.450 17.108 13.537 1.00 21.66 ? 202 THR A CG2 1 ATOM 1291 N N . SER A 1 203 ? 19.649 19.553 16.206 1.00 27.81 ? 203 SER A N 1 ATOM 1292 C CA . SER A 1 203 ? 19.259 20.960 16.331 1.00 30.38 ? 203 SER A CA 1 ATOM 1293 C C . SER A 1 203 ? 19.924 21.650 17.525 1.00 30.09 ? 203 SER A C 1 ATOM 1294 O O . SER A 1 203 ? 20.020 21.089 18.624 1.00 29.84 ? 203 SER A O 1 ATOM 1295 C CB . SER A 1 203 ? 17.740 21.074 16.460 1.00 32.12 ? 203 SER A CB 1 ATOM 1296 O OG . SER A 1 203 ? 17.281 20.190 17.465 1.00 35.06 ? 203 SER A OG 1 ATOM 1297 N N . GLY A 1 204 ? 20.367 22.878 17.285 1.00 29.50 ? 204 GLY A N 1 ATOM 1298 C CA . GLY A 1 204 ? 21.048 23.686 18.282 1.00 30.78 ? 204 GLY A CA 1 ATOM 1299 C C . GLY A 1 204 ? 20.350 25.020 18.413 1.00 31.69 ? 204 GLY A C 1 ATOM 1300 O O . GLY A 1 204 ? 19.524 25.373 17.580 1.00 30.87 ? 204 GLY A O 1 ATOM 1301 N N . CYS A 1 205 ? 20.705 25.758 19.435 1.00 33.66 ? 205 CYS A N 1 ATOM 1302 C CA . CYS A 1 205 ? 20.144 27.054 19.676 1.00 35.09 ? 205 CYS A CA 1 ATOM 1303 C C . CYS A 1 205 ? 20.990 27.806 20.665 1.00 35.05 ? 205 CYS A C 1 ATOM 1304 O O . CYS A 1 205 ? 21.990 27.335 21.098 1.00 33.73 ? 205 CYS A O 1 ATOM 1305 C CB . CYS A 1 205 ? 18.752 26.901 20.240 1.00 36.18 ? 205 CYS A CB 1 ATOM 1306 S SG . CYS A 1 205 ? 18.744 26.430 21.959 1.00 38.86 ? 205 CYS A SG 1 ATOM 1307 N N . CYS A 1 206 ? 20.535 28.998 20.997 1.00 36.67 ? 206 CYS A N 1 ATOM 1308 C CA . CYS A 1 206 ? 21.098 29.839 22.031 1.00 38.00 ? 206 CYS A CA 1 ATOM 1309 C C . CYS A 1 206 ? 22.555 30.188 22.037 1.00 37.41 ? 206 CYS A C 1 ATOM 1310 O O . CYS A 1 206 ? 23.145 30.331 23.058 1.00 39.02 ? 206 CYS A O 1 ATOM 1311 C CB . CYS A 1 206 ? 20.715 29.227 23.376 1.00 39.46 ? 206 CYS A CB 1 ATOM 1312 S SG . CYS A 1 206 ? 18.963 28.917 23.533 1.00 43.83 ? 206 CYS A SG 1 ATOM 1313 N N . GLY A 1 207 ? 23.148 30.315 20.890 1.00 37.55 ? 207 GLY A N 1 ATOM 1314 C CA . GLY A 1 207 ? 24.558 30.697 20.823 1.00 38.83 ? 207 GLY A CA 1 ATOM 1315 C C . GLY A 1 207 ? 25.539 29.554 20.622 1.00 40.84 ? 207 GLY A C 1 ATOM 1316 O O . GLY A 1 207 ? 26.753 29.770 20.596 1.00 40.44 ? 207 GLY A O 1 ATOM 1317 N N . VAL A 1 208 ? 25.020 28.358 20.443 1.00 41.96 ? 208 VAL A N 1 ATOM 1318 C CA . VAL A 1 208 ? 25.839 27.202 20.206 1.00 42.47 ? 208 VAL A CA 1 ATOM 1319 C C . VAL A 1 208 ? 26.155 27.178 18.728 1.00 44.27 ? 208 VAL A C 1 ATOM 1320 O O . VAL A 1 208 ? 25.305 27.404 17.930 1.00 44.39 ? 208 VAL A O 1 ATOM 1321 C CB . VAL A 1 208 ? 25.078 25.911 20.565 1.00 42.02 ? 208 VAL A CB 1 ATOM 1322 C CG1 . VAL A 1 208 ? 25.797 24.665 20.083 1.00 41.16 ? 208 VAL A CG1 1 ATOM 1323 C CG2 . VAL A 1 208 ? 24.846 25.844 22.042 1.00 41.33 ? 208 VAL A CG2 1 ATOM 1324 N N . GLU A 1 209 ? 27.390 26.904 18.368 1.00 47.83 ? 209 GLU A N 1 ATOM 1325 C CA . GLU A 1 209 ? 27.751 26.811 16.965 1.00 50.42 ? 209 GLU A CA 1 ATOM 1326 C C . GLU A 1 209 ? 27.397 25.421 16.439 1.00 45.92 ? 209 GLU A C 1 ATOM 1327 O O . GLU A 1 209 ? 28.196 24.566 16.376 1.00 44.41 ? 209 GLU A O 1 ATOM 1328 C CB . GLU A 1 209 ? 29.235 27.116 16.777 1.00 54.76 ? 209 GLU A CB 1 ATOM 1329 C CG . GLU A 1 209 ? 29.539 28.503 16.268 1.00 59.91 ? 209 GLU A CG 1 ATOM 1330 C CD . GLU A 1 209 ? 31.036 28.811 16.241 1.00 65.03 ? 209 GLU A CD 1 ATOM 1331 O OE1 . GLU A 1 209 ? 31.799 28.108 15.543 1.00 67.88 ? 209 GLU A OE1 1 ATOM 1332 O OE2 . GLU A 1 209 ? 31.455 29.757 16.916 1.00 67.27 -1 209 GLU A OE2 1 ATOM 1333 N N . PHE A 1 210 ? 26.157 25.245 16.048 1.00 42.68 ? 210 PHE A N 1 ATOM 1334 C CA . PHE A 1 210 ? 25.681 23.970 15.583 1.00 38.32 ? 210 PHE A CA 1 ATOM 1335 C C . PHE A 1 210 ? 25.805 23.798 14.088 1.00 34.44 ? 210 PHE A C 1 ATOM 1336 O O . PHE A 1 210 ? 25.424 24.625 13.352 1.00 34.42 ? 210 PHE A O 1 ATOM 1337 C CB . PHE A 1 210 ? 24.255 23.726 16.091 1.00 37.89 ? 210 PHE A CB 1 ATOM 1338 C CG . PHE A 1 210 ? 23.804 22.328 15.929 1.00 37.57 ? 210 PHE A CG 1 ATOM 1339 C CD1 . PHE A 1 210 ? 23.213 21.924 14.778 1.00 37.91 ? 210 PHE A CD1 1 ATOM 1340 C CD2 . PHE A 1 210 ? 24.021 21.410 16.908 1.00 37.64 ? 210 PHE A CD2 1 ATOM 1341 C CE1 . PHE A 1 210 ? 22.843 20.634 14.606 1.00 37.74 ? 210 PHE A CE1 1 ATOM 1342 C CE2 . PHE A 1 210 ? 23.624 20.110 16.745 1.00 37.27 ? 210 PHE A CE2 1 ATOM 1343 C CZ . PHE A 1 210 ? 23.048 19.724 15.592 1.00 37.31 ? 210 PHE A CZ 1 ATOM 1344 N N . PRO A 1 211 ? 26.343 22.694 13.645 1.00 32.37 ? 211 PRO A N 1 ATOM 1345 C CA . PRO A 1 211 ? 26.815 21.613 14.493 1.00 30.79 ? 211 PRO A CA 1 ATOM 1346 C C . PRO A 1 211 ? 28.279 21.744 14.829 1.00 29.91 ? 211 PRO A C 1 ATOM 1347 O O . PRO A 1 211 ? 29.014 22.189 13.978 1.00 29.81 ? 211 PRO A O 1 ATOM 1348 C CB . PRO A 1 211 ? 26.637 20.428 13.594 1.00 31.53 ? 211 PRO A CB 1 ATOM 1349 C CG . PRO A 1 211 ? 26.867 20.969 12.260 1.00 31.71 ? 211 PRO A CG 1 ATOM 1350 C CD . PRO A 1 211 ? 26.222 22.281 12.258 1.00 31.52 ? 211 PRO A CD 1 ATOM 1351 N N . ASP A 1 212 ? 28.683 21.379 16.030 1.00 27.84 ? 212 ASP A N 1 ATOM 1352 C CA . ASP A 1 212 ? 30.061 21.479 16.457 1.00 27.67 ? 212 ASP A CA 1 ATOM 1353 C C . ASP A 1 212 ? 30.871 20.206 16.198 1.00 27.82 ? 212 ASP A C 1 ATOM 1354 O O . ASP A 1 212 ? 30.665 19.208 16.825 1.00 28.42 ? 212 ASP A O 1 ATOM 1355 C CB . ASP A 1 212 ? 30.094 21.884 17.917 1.00 28.14 ? 212 ASP A CB 1 ATOM 1356 C CG . ASP A 1 212 ? 31.476 22.158 18.446 1.00 29.29 ? 212 ASP A CG 1 ATOM 1357 O OD1 . ASP A 1 212 ? 32.453 22.093 17.751 1.00 31.97 ? 212 ASP A OD1 1 ATOM 1358 O OD2 . ASP A 1 212 ? 31.591 22.456 19.600 1.00 31.03 -1 212 ASP A OD2 1 ATOM 1359 N N . PRO A 1 213 ? 31.785 20.269 15.246 1.00 27.57 ? 213 PRO A N 1 ATOM 1360 C CA . PRO A 1 213 ? 32.620 19.133 14.883 1.00 26.64 ? 213 PRO A CA 1 ATOM 1361 C C . PRO A 1 213 ? 33.600 18.754 15.951 1.00 25.72 ? 213 PRO A C 1 ATOM 1362 O O . PRO A 1 213 ? 33.884 17.615 16.067 1.00 24.31 ? 213 PRO A O 1 ATOM 1363 C CB . PRO A 1 213 ? 33.313 19.575 13.622 1.00 27.24 ? 213 PRO A CB 1 ATOM 1364 C CG . PRO A 1 213 ? 33.136 21.032 13.544 1.00 28.12 ? 213 PRO A CG 1 ATOM 1365 C CD . PRO A 1 213 ? 32.262 21.505 14.647 1.00 28.10 ? 213 PRO A CD 1 ATOM 1366 N N . VAL A 1 214 ? 34.025 19.707 16.749 1.00 25.51 ? 214 VAL A N 1 ATOM 1367 C CA . VAL A 1 214 ? 34.947 19.406 17.837 1.00 25.63 ? 214 VAL A CA 1 ATOM 1368 C C . VAL A 1 214 ? 34.250 18.533 18.867 1.00 24.46 ? 214 VAL A C 1 ATOM 1369 O O . VAL A 1 214 ? 34.848 17.604 19.406 1.00 23.93 ? 214 VAL A O 1 ATOM 1370 C CB . VAL A 1 214 ? 35.465 20.689 18.520 1.00 26.56 ? 214 VAL A CB 1 ATOM 1371 C CG1 . VAL A 1 214 ? 36.324 20.347 19.733 1.00 26.39 ? 214 VAL A CG1 1 ATOM 1372 C CG2 . VAL A 1 214 ? 36.250 21.531 17.527 1.00 26.95 ? 214 VAL A CG2 1 ATOM 1373 N N . TYR A 1 215 ? 32.985 18.849 19.135 1.00 23.78 ? 215 TYR A N 1 ATOM 1374 C CA . TYR A 1 215 ? 32.175 18.080 20.079 1.00 22.86 ? 215 TYR A CA 1 ATOM 1375 C C . TYR A 1 215 ? 31.987 16.641 19.594 1.00 22.82 ? 215 TYR A C 1 ATOM 1376 O O . TYR A 1 215 ? 32.368 15.686 20.287 1.00 21.99 ? 215 TYR A O 1 ATOM 1377 C CB . TYR A 1 215 ? 30.807 18.724 20.296 1.00 22.17 ? 215 TYR A CB 1 ATOM 1378 C CG . TYR A 1 215 ? 29.873 17.892 21.167 1.00 21.88 ? 215 TYR A CG 1 ATOM 1379 C CD1 . TYR A 1 215 ? 30.165 17.662 22.514 1.00 21.68 ? 215 TYR A CD1 1 ATOM 1380 C CD2 . TYR A 1 215 ? 28.698 17.339 20.643 1.00 21.37 ? 215 TYR A CD2 1 ATOM 1381 C CE1 . TYR A 1 215 ? 29.318 16.899 23.308 1.00 22.26 ? 215 TYR A CE1 1 ATOM 1382 C CE2 . TYR A 1 215 ? 27.841 16.580 21.429 1.00 21.37 ? 215 TYR A CE2 1 ATOM 1383 C CZ . TYR A 1 215 ? 28.146 16.362 22.759 1.00 21.99 ? 215 TYR A CZ 1 ATOM 1384 O OH . TYR A 1 215 ? 27.294 15.609 23.544 1.00 21.94 ? 215 TYR A OH 1 ATOM 1385 N N . MET A 1 216 ? 31.399 16.475 18.416 1.00 22.27 ? 216 MET A N 1 ATOM 1386 C CA . MET A 1 216 ? 31.121 15.122 17.952 1.00 22.71 ? 216 MET A CA 1 ATOM 1387 C C . MET A 1 216 ? 32.405 14.308 17.798 1.00 22.51 ? 216 MET A C 1 ATOM 1388 O O . MET A 1 216 ? 32.397 13.102 18.048 1.00 23.58 ? 216 MET A O 1 ATOM 1389 C CB . MET A 1 216 ? 30.271 15.115 16.680 1.00 22.84 ? 216 MET A CB 1 ATOM 1390 C CG . MET A 1 216 ? 28.780 15.343 16.943 1.00 22.90 ? 216 MET A CG 1 ATOM 1391 S SD . MET A 1 216 ? 27.971 14.005 17.863 1.00 23.13 ? 216 MET A SD 1 ATOM 1392 C CE . MET A 1 216 ? 27.971 12.704 16.635 1.00 21.54 ? 216 MET A CE 1 ATOM 1393 N N . GLN A 1 217 ? 33.514 14.958 17.452 1.00 22.80 ? 217 GLN A N 1 ATOM 1394 C CA . GLN A 1 217 ? 34.796 14.255 17.373 1.00 23.38 ? 217 GLN A CA 1 ATOM 1395 C C . GLN A 1 217 ? 35.266 13.783 18.748 1.00 22.25 ? 217 GLN A C 1 ATOM 1396 O O . GLN A 1 217 ? 35.758 12.673 18.870 1.00 22.21 ? 217 GLN A O 1 ATOM 1397 C CB . GLN A 1 217 ? 35.877 15.107 16.686 1.00 23.65 ? 217 GLN A CB 1 ATOM 1398 C CG . GLN A 1 217 ? 37.177 14.361 16.357 1.00 24.11 ? 217 GLN A CG 1 ATOM 1399 C CD . GLN A 1 217 ? 36.992 13.210 15.368 1.00 24.56 ? 217 GLN A CD 1 ATOM 1400 O OE1 . GLN A 1 217 ? 36.464 13.387 14.274 1.00 24.40 ? 217 GLN A OE1 1 ATOM 1401 N NE2 . GLN A 1 217 ? 37.434 12.016 15.761 1.00 25.98 ? 217 GLN A NE2 1 ATOM 1402 N N . TYR A 1 218 ? 35.102 14.613 19.776 1.00 22.33 ? 218 TYR A N 1 ATOM 1403 C CA . TYR A 1 218 ? 35.467 14.227 21.153 1.00 22.19 ? 218 TYR A CA 1 ATOM 1404 C C . TYR A 1 218 ? 34.630 13.050 21.672 1.00 22.19 ? 218 TYR A C 1 ATOM 1405 O O . TYR A 1 218 ? 35.153 12.159 22.338 1.00 22.21 ? 218 TYR A O 1 ATOM 1406 C CB . TYR A 1 218 ? 35.327 15.422 22.094 1.00 23.05 ? 218 TYR A CB 1 ATOM 1407 C CG . TYR A 1 218 ? 35.753 15.158 23.525 1.00 23.74 ? 218 TYR A CG 1 ATOM 1408 C CD1 . TYR A 1 218 ? 34.875 14.587 24.433 1.00 24.40 ? 218 TYR A CD1 1 ATOM 1409 C CD2 . TYR A 1 218 ? 37.030 15.502 23.975 1.00 24.48 ? 218 TYR A CD2 1 ATOM 1410 C CE1 . TYR A 1 218 ? 35.253 14.352 25.742 1.00 25.44 ? 218 TYR A CE1 1 ATOM 1411 C CE2 . TYR A 1 218 ? 37.423 15.261 25.283 1.00 24.82 ? 218 TYR A CE2 1 ATOM 1412 C CZ . TYR A 1 218 ? 36.528 14.692 26.164 1.00 25.82 ? 218 TYR A CZ 1 ATOM 1413 O OH . TYR A 1 218 ? 36.884 14.457 27.475 1.00 27.49 ? 218 TYR A OH 1 ATOM 1414 N N . VAL A 1 219 ? 33.336 13.057 21.360 1.00 21.77 ? 219 VAL A N 1 ATOM 1415 C CA . VAL A 1 219 ? 32.435 11.969 21.733 1.00 21.56 ? 219 VAL A CA 1 ATOM 1416 C C . VAL A 1 219 ? 32.870 10.684 21.033 1.00 21.66 ? 219 VAL A C 1 ATOM 1417 O O . VAL A 1 219 ? 32.961 9.623 21.652 1.00 21.02 ? 219 VAL A O 1 ATOM 1418 C CB . VAL A 1 219 ? 30.955 12.283 21.367 1.00 21.51 ? 219 VAL A CB 1 ATOM 1419 C CG1 . VAL A 1 219 ? 30.056 11.095 21.693 1.00 21.52 ? 219 VAL A CG1 1 ATOM 1420 C CG2 . VAL A 1 219 ? 30.452 13.523 22.110 1.00 21.29 ? 219 VAL A CG2 1 ATOM 1421 N N . GLU A 1 220 ? 33.128 10.792 19.733 1.00 22.57 ? 220 GLU A N 1 ATOM 1422 C CA . GLU A 1 220 ? 33.633 9.669 18.939 1.00 22.94 ? 220 GLU A CA 1 ATOM 1423 C C . GLU A 1 220 ? 34.962 9.120 19.489 1.00 23.98 ? 220 GLU A C 1 ATOM 1424 O O . GLU A 1 220 ? 35.103 7.906 19.660 1.00 23.98 ? 220 GLU A O 1 ATOM 1425 C CB . GLU A 1 220 ? 33.773 10.090 17.472 1.00 23.22 ? 220 GLU A CB 1 ATOM 1426 C CG . GLU A 1 220 ? 32.427 10.256 16.790 1.00 23.97 ? 220 GLU A CG 1 ATOM 1427 C CD . GLU A 1 220 ? 32.428 11.167 15.576 1.00 25.07 ? 220 GLU A CD 1 ATOM 1428 O OE1 . GLU A 1 220 ? 33.504 11.478 15.021 1.00 25.62 ? 220 GLU A OE1 1 ATOM 1429 O OE2 . GLU A 1 220 ? 31.315 11.561 15.156 1.00 25.33 -1 220 GLU A OE2 1 ATOM 1430 N N . ASP A 1 221 ? 35.912 10.011 19.791 1.00 24.69 ? 221 ASP A N 1 ATOM 1431 C CA . ASP A 1 221 ? 37.221 9.623 20.347 1.00 25.41 ? 221 ASP A CA 1 ATOM 1432 C C . ASP A 1 221 ? 37.126 8.917 21.721 1.00 25.57 ? 221 ASP A C 1 ATOM 1433 O O . ASP A 1 221 ? 37.928 8.012 22.009 1.00 24.69 ? 221 ASP A O 1 ATOM 1434 C CB . ASP A 1 221 ? 38.153 10.846 20.475 1.00 26.82 ? 221 ASP A CB 1 ATOM 1435 C CG . ASP A 1 221 ? 38.667 11.376 19.118 1.00 29.07 ? 221 ASP A CG 1 ATOM 1436 O OD1 . ASP A 1 221 ? 38.422 10.759 18.043 1.00 29.95 ? 221 ASP A OD1 1 ATOM 1437 O OD2 . ASP A 1 221 ? 39.340 12.437 19.137 1.00 31.68 -1 221 ASP A OD2 1 ATOM 1438 N N . GLN A 1 222 ? 36.174 9.334 22.566 1.00 25.39 ? 222 GLN A N 1 ATOM 1439 C CA . GLN A 1 222 ? 35.975 8.709 23.888 1.00 24.63 ? 222 GLN A CA 1 ATOM 1440 C C . GLN A 1 222 ? 35.743 7.215 23.755 1.00 24.03 ? 222 GLN A C 1 ATOM 1441 O O . GLN A 1 222 ? 36.254 6.418 24.539 1.00 24.21 ? 222 GLN A O 1 ATOM 1442 C CB . GLN A 1 222 ? 34.761 9.291 24.603 1.00 25.06 ? 222 GLN A CB 1 ATOM 1443 C CG . GLN A 1 222 ? 34.970 10.591 25.349 1.00 25.56 ? 222 GLN A CG 1 ATOM 1444 C CD . GLN A 1 222 ? 33.678 11.098 25.978 1.00 26.28 ? 222 GLN A CD 1 ATOM 1445 O OE1 . GLN A 1 222 ? 32.647 11.233 25.303 1.00 26.48 ? 222 GLN A OE1 1 ATOM 1446 N NE2 . GLN A 1 222 ? 33.724 11.379 27.273 1.00 25.77 ? 222 GLN A NE2 1 ATOM 1447 N N . ALA A 1 223 ? 34.948 6.853 22.759 1.00 23.70 ? 223 ALA A N 1 ATOM 1448 C CA . ALA A 1 223 ? 34.580 5.471 22.525 1.00 23.81 ? 223 ALA A CA 1 ATOM 1449 C C . ALA A 1 223 ? 35.774 4.695 22.001 1.00 23.40 ? 223 ALA A C 1 ATOM 1450 O O . ALA A 1 223 ? 36.068 3.595 22.461 1.00 22.54 ? 223 ALA A O 1 ATOM 1451 C CB . ALA A 1 223 ? 33.429 5.402 21.530 1.00 23.63 ? 223 ALA A CB 1 ATOM 1452 N N . ARG A 1 224 ? 36.443 5.279 21.020 1.00 24.49 ? 224 ARG A N 1 ATOM 1453 C CA . ARG A 1 224 ? 37.634 4.675 20.419 1.00 25.21 ? 224 ARG A CA 1 ATOM 1454 C C . ARG A 1 224 ? 38.724 4.462 21.468 1.00 24.24 ? 224 ARG A C 1 ATOM 1455 O O . ARG A 1 224 ? 39.319 3.390 21.516 1.00 23.60 ? 224 ARG A O 1 ATOM 1456 C CB . ARG A 1 224 ? 38.156 5.551 19.280 1.00 26.09 ? 224 ARG A CB 1 ATOM 1457 C CG . ARG A 1 224 ? 37.227 5.621 18.074 1.00 27.25 ? 224 ARG A CG 1 ATOM 1458 C CD . ARG A 1 224 ? 37.421 4.413 17.183 1.00 28.10 ? 224 ARG A CD 1 ATOM 1459 N NE . ARG A 1 224 ? 36.645 4.460 15.934 1.00 28.77 ? 224 ARG A NE 1 ATOM 1460 C CZ . ARG A 1 224 ? 35.743 3.557 15.552 1.00 27.54 ? 224 ARG A CZ 1 ATOM 1461 N NH1 . ARG A 1 224 ? 35.439 2.519 16.323 1.00 29.43 ? 224 ARG A NH1 1 ATOM 1462 N NH2 . ARG A 1 224 ? 35.132 3.693 14.386 1.00 27.14 ? 224 ARG A NH2 1 ATOM 1463 N N . ASN A 1 225 ? 38.944 5.467 22.322 1.00 24.27 ? 225 ASN A N 1 ATOM 1464 C CA . ASN A 1 225 ? 39.920 5.381 23.425 1.00 24.47 ? 225 ASN A CA 1 ATOM 1465 C C . ASN A 1 225 ? 39.614 4.265 24.426 1.00 23.79 ? 225 ASN A C 1 ATOM 1466 O O . ASN A 1 225 ? 40.528 3.674 24.978 1.00 23.50 ? 225 ASN A O 1 ATOM 1467 C CB . ASN A 1 225 ? 40.028 6.716 24.189 1.00 24.89 ? 225 ASN A CB 1 ATOM 1468 C CG . ASN A 1 225 ? 40.666 7.829 23.361 1.00 26.10 ? 225 ASN A CG 1 ATOM 1469 O OD1 . ASN A 1 225 ? 41.129 7.599 22.250 1.00 26.81 ? 225 ASN A OD1 1 ATOM 1470 N ND2 . ASN A 1 225 ? 40.663 9.052 23.894 1.00 26.18 ? 225 ASN A ND2 1 ATOM 1471 N N . ALA A 1 226 ? 38.335 4.003 24.678 1.00 24.40 ? 226 ALA A N 1 ATOM 1472 C CA . ALA A 1 226 ? 37.919 2.875 25.531 1.00 24.60 ? 226 ALA A CA 1 ATOM 1473 C C . ALA A 1 226 ? 38.030 1.523 24.823 1.00 24.48 ? 226 ALA A C 1 ATOM 1474 O O . ALA A 1 226 ? 37.723 0.489 25.412 1.00 25.88 ? 226 ALA A O 1 ATOM 1475 C CB . ALA A 1 226 ? 36.498 3.081 26.016 1.00 24.52 ? 226 ALA A CB 1 ATOM 1476 N N . GLY A 1 227 ? 38.449 1.526 23.560 1.00 24.26 ? 227 GLY A N 1 ATOM 1477 C CA . GLY A 1 227 ? 38.735 0.291 22.836 1.00 24.16 ? 227 GLY A CA 1 ATOM 1478 C C . GLY A 1 227 ? 37.674 -0.140 21.841 1.00 23.75 ? 227 GLY A C 1 ATOM 1479 O O . GLY A 1 227 ? 37.739 -1.245 21.327 1.00 24.97 ? 227 GLY A O 1 ATOM 1480 N N . VAL A 1 228 ? 36.707 0.726 21.546 1.00 23.74 ? 228 VAL A N 1 ATOM 1481 C CA . VAL A 1 228 ? 35.668 0.411 20.562 1.00 23.58 ? 228 VAL A CA 1 ATOM 1482 C C . VAL A 1 228 ? 36.258 0.507 19.150 1.00 23.65 ? 228 VAL A C 1 ATOM 1483 O O . VAL A 1 228 ? 36.737 1.562 18.748 1.00 23.02 ? 228 VAL A O 1 ATOM 1484 C CB . VAL A 1 228 ? 34.454 1.364 20.678 1.00 23.95 ? 228 VAL A CB 1 ATOM 1485 C CG1 . VAL A 1 228 ? 33.403 1.017 19.637 1.00 24.46 ? 228 VAL A CG1 1 ATOM 1486 C CG2 . VAL A 1 228 ? 33.840 1.314 22.071 1.00 23.67 ? 228 VAL A CG2 1 ATOM 1487 N N . VAL A 1 229 ? 36.238 -0.604 18.411 1.00 23.04 ? 229 VAL A N 1 ATOM 1488 C CA . VAL A 1 229 ? 36.790 -0.653 17.058 1.00 22.49 ? 229 VAL A CA 1 ATOM 1489 C C . VAL A 1 229 ? 35.737 -0.798 15.966 1.00 21.81 ? 229 VAL A C 1 ATOM 1490 O O . VAL A 1 229 ? 36.010 -0.519 14.797 1.00 20.90 ? 229 VAL A O 1 ATOM 1491 C CB . VAL A 1 229 ? 37.830 -1.785 16.894 1.00 23.05 ? 229 VAL A CB 1 ATOM 1492 C CG1 . VAL A 1 229 ? 39.103 -1.439 17.652 1.00 23.52 ? 229 VAL A CG1 1 ATOM 1493 C CG2 . VAL A 1 229 ? 37.282 -3.132 17.346 1.00 23.60 ? 229 VAL A CG2 1 ATOM 1494 N N . ILE A 1 230 ? 34.549 -1.258 16.346 1.00 20.77 ? 230 ILE A N 1 ATOM 1495 C CA . ILE A 1 230 ? 33.453 -1.454 15.397 1.00 20.12 ? 230 ILE A CA 1 ATOM 1496 C C . ILE A 1 230 ? 32.959 -0.123 14.812 1.00 19.70 ? 230 ILE A C 1 ATOM 1497 O O . ILE A 1 230 ? 33.221 0.946 15.392 1.00 18.98 ? 230 ILE A O 1 ATOM 1498 C CB . ILE A 1 230 ? 32.287 -2.217 16.052 1.00 20.19 ? 230 ILE A CB 1 ATOM 1499 C CG1 . ILE A 1 230 ? 31.803 -1.479 17.322 1.00 20.24 ? 230 ILE A CG1 1 ATOM 1500 C CG2 . ILE A 1 230 ? 32.714 -3.656 16.318 1.00 19.97 ? 230 ILE A CG2 1 ATOM 1501 C CD1 . ILE A 1 230 ? 30.637 -2.134 18.029 1.00 20.23 ? 230 ILE A CD1 1 ATOM 1502 N N . PRO A 1 231 ? 32.267 -0.178 13.657 1.00 18.88 ? 231 PRO A N 1 ATOM 1503 C CA . PRO A 1 231 ? 31.847 1.063 12.990 1.00 19.22 ? 231 PRO A CA 1 ATOM 1504 C C . PRO A 1 231 ? 30.926 1.945 13.838 1.00 18.85 ? 231 PRO A C 1 ATOM 1505 O O . PRO A 1 231 ? 30.145 1.434 14.636 1.00 18.62 ? 231 PRO A O 1 ATOM 1506 C CB . PRO A 1 231 ? 31.098 0.568 11.739 1.00 19.13 ? 231 PRO A CB 1 ATOM 1507 C CG . PRO A 1 231 ? 31.557 -0.822 11.521 1.00 19.16 ? 231 PRO A CG 1 ATOM 1508 C CD . PRO A 1 231 ? 31.902 -1.370 12.872 1.00 19.24 ? 231 PRO A CD 1 ATOM 1509 N N . LEU A 1 232 ? 31.041 3.257 13.655 1.00 19.14 ? 232 LEU A N 1 ATOM 1510 C CA . LEU A 1 232 ? 30.185 4.230 14.311 1.00 18.92 ? 232 LEU A CA 1 ATOM 1511 C C . LEU A 1 232 ? 29.051 4.626 13.391 1.00 19.22 ? 232 LEU A C 1 ATOM 1512 O O . LEU A 1 232 ? 29.273 4.874 12.206 1.00 21.17 ? 232 LEU A O 1 ATOM 1513 C CB . LEU A 1 232 ? 30.982 5.472 14.687 1.00 18.89 ? 232 LEU A CB 1 ATOM 1514 C CG . LEU A 1 232 ? 32.235 5.206 15.515 1.00 19.22 ? 232 LEU A CG 1 ATOM 1515 C CD1 . LEU A 1 232 ? 33.012 6.507 15.691 1.00 19.17 ? 232 LEU A CD1 1 ATOM 1516 C CD2 . LEU A 1 232 ? 31.893 4.571 16.861 1.00 19.12 ? 232 LEU A CD2 1 ATOM 1517 N N . ILE A 1 233 ? 27.841 4.697 13.936 1.00 18.87 ? 233 ILE A N 1 ATOM 1518 C CA . ILE A 1 233 ? 26.649 5.053 13.170 1.00 18.46 ? 233 ILE A CA 1 ATOM 1519 C C . ILE A 1 233 ? 25.865 6.100 13.949 1.00 18.36 ? 233 ILE A C 1 ATOM 1520 O O . ILE A 1 233 ? 25.685 5.974 15.162 1.00 18.31 ? 233 ILE A O 1 ATOM 1521 C CB . ILE A 1 233 ? 25.774 3.813 12.875 1.00 19.11 ? 233 ILE A CB 1 ATOM 1522 C CG1 . ILE A 1 233 ? 24.517 4.192 12.094 1.00 19.54 ? 233 ILE A CG1 1 ATOM 1523 C CG2 . ILE A 1 233 ? 25.360 3.091 14.152 1.00 19.44 ? 233 ILE A CG2 1 ATOM 1524 C CD1 . ILE A 1 233 ? 23.891 3.012 11.374 1.00 19.93 ? 233 ILE A CD1 1 ATOM 1525 N N . ASN A 1 234 ? 25.420 7.150 13.271 1.00 17.49 ? 234 ASN A N 1 ATOM 1526 C CA . ASN A 1 234 ? 24.662 8.192 13.948 1.00 17.14 ? 234 ASN A CA 1 ATOM 1527 C C . ASN A 1 234 ? 23.174 8.050 13.661 1.00 17.01 ? 234 ASN A C 1 ATOM 1528 O O . ASN A 1 234 ? 22.763 7.239 12.826 1.00 17.01 ? 234 ASN A O 1 ATOM 1529 C CB . ASN A 1 234 ? 25.187 9.594 13.595 1.00 16.91 ? 234 ASN A CB 1 ATOM 1530 C CG . ASN A 1 234 ? 24.786 10.037 12.206 1.00 17.02 ? 234 ASN A CG 1 ATOM 1531 O OD1 . ASN A 1 234 ? 24.900 9.275 11.257 1.00 17.00 ? 234 ASN A OD1 1 ATOM 1532 N ND2 . ASN A 1 234 ? 24.309 11.277 12.081 1.00 17.24 ? 234 ASN A ND2 1 ATOM 1533 N N . ASN A 1 235 ? 22.368 8.827 14.379 1.00 17.38 ? 235 ASN A N 1 ATOM 1534 C CA . ASN A 1 235 ? 20.916 8.832 14.184 1.00 17.58 ? 235 ASN A CA 1 ATOM 1535 C C . ASN A 1 235 ? 20.369 10.246 14.143 1.00 18.20 ? 235 ASN A C 1 ATOM 1536 O O . ASN A 1 235 ? 19.730 10.711 15.086 1.00 18.20 ? 235 ASN A O 1 ATOM 1537 C CB . ASN A 1 235 ? 20.219 8.027 15.284 1.00 17.20 ? 235 ASN A CB 1 ATOM 1538 C CG . ASN A 1 235 ? 20.411 8.625 16.665 1.00 17.11 ? 235 ASN A CG 1 ATOM 1539 O OD1 . ASN A 1 235 ? 21.467 9.164 16.986 1.00 16.83 ? 235 ASN A OD1 1 ATOM 1540 N ND2 . ASN A 1 235 ? 19.383 8.543 17.481 1.00 17.03 ? 235 ASN A ND2 1 ATOM 1541 N N . ASP A 1 236 ? 20.632 10.918 13.030 1.00 18.48 ? 236 ASP A N 1 ATOM 1542 C CA . ASP A 1 236 ? 20.141 12.266 12.777 1.00 18.07 ? 236 ASP A CA 1 ATOM 1543 C C . ASP A 1 236 ? 18.618 12.282 12.931 1.00 18.38 ? 236 ASP A C 1 ATOM 1544 O O . ASP A 1 236 ? 17.917 11.422 12.375 1.00 17.51 ? 236 ASP A O 1 ATOM 1545 C CB . ASP A 1 236 ? 20.545 12.656 11.351 1.00 18.70 ? 236 ASP A CB 1 ATOM 1546 C CG . ASP A 1 236 ? 20.817 14.152 11.167 1.00 19.43 ? 236 ASP A CG 1 ATOM 1547 O OD1 . ASP A 1 236 ? 20.740 14.972 12.128 1.00 19.54 ? 236 ASP A OD1 1 ATOM 1548 O OD2 . ASP A 1 236 ? 21.126 14.491 10.005 1.00 19.44 -1 236 ASP A OD2 1 ATOM 1549 N N . ALA A 1 237 ? 18.100 13.240 13.698 1.00 18.90 ? 237 ALA A N 1 ATOM 1550 C CA . ALA A 1 237 ? 16.658 13.266 14.016 1.00 20.41 ? 237 ALA A CA 1 ATOM 1551 C C . ALA A 1 237 ? 15.796 13.348 12.753 1.00 21.50 ? 237 ALA A C 1 ATOM 1552 O O . ALA A 1 237 ? 14.749 12.721 12.673 1.00 21.44 ? 237 ALA A O 1 ATOM 1553 C CB . ALA A 1 237 ? 16.318 14.407 14.976 1.00 20.70 ? 237 ALA A CB 1 ATOM 1554 N N . SER A 1 238 ? 16.244 14.137 11.780 1.00 22.25 ? 238 SER A N 1 ATOM 1555 C CA . SER A 1 238 ? 15.715 14.070 10.431 1.00 22.71 ? 238 SER A CA 1 ATOM 1556 C C . SER A 1 238 ? 16.861 13.800 9.468 1.00 22.85 ? 238 SER A C 1 ATOM 1557 O O . SER A 1 238 ? 18.030 13.871 9.838 1.00 22.85 ? 238 SER A O 1 ATOM 1558 C CB . SER A 1 238 ? 14.994 15.371 10.066 1.00 23.56 ? 238 SER A CB 1 ATOM 1559 O OG . SER A 1 238 ? 15.837 16.490 10.245 1.00 24.75 ? 238 SER A OG 1 ATOM 1560 N N . ALA A 1 239 ? 16.511 13.466 8.235 1.00 23.53 ? 239 ALA A N 1 ATOM 1561 C CA . ALA A 1 239 ? 17.479 13.283 7.166 1.00 23.13 ? 239 ALA A CA 1 ATOM 1562 C C . ALA A 1 239 ? 18.059 14.639 6.769 1.00 23.02 ? 239 ALA A C 1 ATOM 1563 O O . ALA A 1 239 ? 17.636 15.234 5.794 1.00 21.62 ? 239 ALA A O 1 ATOM 1564 C CB . ALA A 1 239 ? 16.794 12.630 5.971 1.00 23.57 ? 239 ALA A CB 1 ATOM 1565 N N . SER A 1 240 ? 19.019 15.124 7.547 1.00 24.18 ? 240 SER A N 1 ATOM 1566 C CA . SER A 1 240 ? 19.621 16.433 7.335 1.00 23.88 ? 240 SER A CA 1 ATOM 1567 C C . SER A 1 240 ? 21.108 16.391 7.001 1.00 23.78 ? 240 SER A C 1 ATOM 1568 O O . SER A 1 240 ? 21.696 17.420 6.736 1.00 23.54 ? 240 SER A O 1 ATOM 1569 C CB . SER A 1 240 ? 19.413 17.287 8.577 1.00 24.50 ? 240 SER A CB 1 ATOM 1570 O OG . SER A 1 240 ? 18.041 17.541 8.766 1.00 25.66 ? 240 SER A OG 1 ATOM 1571 N N . GLY A 1 241 ? 21.720 15.212 7.025 1.00 24.80 ? 241 GLY A N 1 ATOM 1572 C CA . GLY A 1 241 ? 23.113 15.049 6.594 1.00 24.09 ? 241 GLY A CA 1 ATOM 1573 C C . GLY A 1 241 ? 24.182 15.302 7.635 1.00 23.34 ? 241 GLY A C 1 ATOM 1574 O O . GLY A 1 241 ? 25.366 15.267 7.321 1.00 23.91 ? 241 GLY A O 1 ATOM 1575 N N . ASN A 1 242 ? 23.779 15.535 8.879 1.00 23.26 ? 242 ASN A N 1 ATOM 1576 C CA . ASN A 1 242 ? 24.721 15.898 9.929 1.00 22.12 ? 242 ASN A CA 1 ATOM 1577 C C . ASN A 1 242 ? 25.685 14.741 10.190 1.00 22.43 ? 242 ASN A C 1 ATOM 1578 O O . ASN A 1 242 ? 25.269 13.577 10.247 1.00 22.94 ? 242 ASN A O 1 ATOM 1579 C CB . ASN A 1 242 ? 23.978 16.266 11.216 1.00 22.47 ? 242 ASN A CB 1 ATOM 1580 C CG . ASN A 1 242 ? 23.121 17.524 11.077 1.00 22.81 ? 242 ASN A CG 1 ATOM 1581 O OD1 . ASN A 1 242 ? 21.889 17.481 11.215 1.00 22.44 ? 242 ASN A OD1 1 ATOM 1582 N ND2 . ASN A 1 242 ? 23.771 18.655 10.830 1.00 22.73 ? 242 ASN A ND2 1 ATOM 1583 N N . ASN A 1 243 ? 26.974 15.060 10.307 1.00 22.21 ? 243 ASN A N 1 ATOM 1584 C CA . ASN A 1 243 ? 28.018 14.084 10.624 1.00 22.14 ? 243 ASN A CA 1 ATOM 1585 C C . ASN A 1 243 ? 28.204 12.916 9.642 1.00 22.41 ? 243 ASN A C 1 ATOM 1586 O O . ASN A 1 243 ? 28.822 11.909 9.982 1.00 22.41 ? 243 ASN A O 1 ATOM 1587 C CB . ASN A 1 243 ? 27.796 13.550 12.038 1.00 22.90 ? 243 ASN A CB 1 ATOM 1588 C CG . ASN A 1 243 ? 27.747 14.663 13.061 1.00 22.46 ? 243 ASN A CG 1 ATOM 1589 O OD1 . ASN A 1 243 ? 28.734 15.365 13.267 1.00 22.76 ? 243 ASN A OD1 1 ATOM 1590 N ND2 . ASN A 1 243 ? 26.593 14.847 13.683 1.00 22.21 ? 243 ASN A ND2 1 ATOM 1591 N N . ALA A 1 244 ? 27.710 13.073 8.420 1.00 22.44 ? 244 ALA A N 1 ATOM 1592 C CA . ALA A 1 244 ? 27.897 12.079 7.374 1.00 23.16 ? 244 ALA A CA 1 ATOM 1593 C C . ALA A 1 244 ? 29.379 11.962 6.946 1.00 24.47 ? 244 ALA A C 1 ATOM 1594 O O . ALA A 1 244 ? 30.159 12.907 7.140 1.00 22.70 ? 244 ALA A O 1 ATOM 1595 C CB . ALA A 1 244 ? 27.040 12.448 6.171 1.00 22.52 ? 244 ALA A CB 1 ATOM 1596 N N . PRO A 1 245 ? 29.769 10.801 6.370 1.00 25.87 ? 245 PRO A N 1 ATOM 1597 C CA . PRO A 1 245 ? 31.067 10.677 5.689 1.00 27.72 ? 245 PRO A CA 1 ATOM 1598 C C . PRO A 1 245 ? 31.265 11.803 4.668 1.00 28.06 ? 245 PRO A C 1 ATOM 1599 O O . PRO A 1 245 ? 30.362 12.088 3.876 1.00 27.50 ? 245 PRO A O 1 ATOM 1600 C CB . PRO A 1 245 ? 30.967 9.334 4.959 1.00 27.07 ? 245 PRO A CB 1 ATOM 1601 C CG . PRO A 1 245 ? 29.984 8.550 5.752 1.00 27.68 ? 245 PRO A CG 1 ATOM 1602 C CD . PRO A 1 245 ? 29.031 9.529 6.385 1.00 26.94 ? 245 PRO A CD 1 ATOM 1603 N N . GLY A 1 246 ? 32.432 12.431 4.712 1.00 28.43 ? 246 GLY A N 1 ATOM 1604 C CA . GLY A 1 246 ? 32.749 13.556 3.850 1.00 29.73 ? 246 GLY A CA 1 ATOM 1605 C C . GLY A 1 246 ? 32.655 14.909 4.533 1.00 29.89 ? 246 GLY A C 1 ATOM 1606 O O . GLY A 1 246 ? 33.046 15.907 3.929 1.00 31.33 ? 246 GLY A O 1 ATOM 1607 N N . THR A 1 247 ? 32.143 14.959 5.771 1.00 28.76 ? 247 THR A N 1 ATOM 1608 C CA . THR A 1 247 ? 31.927 16.240 6.473 1.00 27.97 ? 247 THR A CA 1 ATOM 1609 C C . THR A 1 247 ? 33.141 16.706 7.277 1.00 28.08 ? 247 THR A C 1 ATOM 1610 O O . THR A 1 247 ? 33.114 17.781 7.886 1.00 27.88 ? 247 THR A O 1 ATOM 1611 C CB . THR A 1 247 ? 30.673 16.220 7.392 1.00 28.10 ? 247 THR A CB 1 ATOM 1612 O OG1 . THR A 1 247 ? 30.727 15.117 8.314 1.00 27.19 ? 247 THR A OG1 1 ATOM 1613 C CG2 . THR A 1 247 ? 29.405 16.135 6.562 1.00 27.27 ? 247 THR A CG2 1 ATOM 1614 N N . GLY A 1 248 ? 34.208 15.912 7.261 1.00 29.35 ? 248 GLY A N 1 ATOM 1615 C CA . GLY A 1 248 ? 35.458 16.276 7.922 1.00 29.10 ? 248 GLY A CA 1 ATOM 1616 C C . GLY A 1 248 ? 35.415 15.825 9.367 1.00 30.08 ? 248 GLY A C 1 ATOM 1617 O O . GLY A 1 248 ? 34.864 14.764 9.673 1.00 30.65 ? 248 GLY A O 1 ATOM 1618 N N . LYS A 1 249 ? 35.989 16.633 10.255 1.00 28.95 ? 249 LYS A N 1 ATOM 1619 C CA . LYS A 1 249 ? 36.031 16.320 11.674 1.00 28.53 ? 249 LYS A CA 1 ATOM 1620 C C . LYS A 1 249 ? 34.620 16.032 12.212 1.00 26.85 ? 249 LYS A C 1 ATOM 1621 O O . LYS A 1 249 ? 33.645 16.697 11.837 1.00 25.24 ? 249 LYS A O 1 ATOM 1622 C CB . LYS A 1 249 ? 36.673 17.478 12.438 1.00 30.75 ? 249 LYS A CB 1 ATOM 1623 C CG . LYS A 1 249 ? 36.943 17.191 13.907 1.00 32.49 ? 249 LYS A CG 1 ATOM 1624 C CD . LYS A 1 249 ? 37.494 18.409 14.633 1.00 34.16 ? 249 LYS A CD 1 ATOM 1625 C CE . LYS A 1 249 ? 38.885 18.788 14.137 1.00 34.51 ? 249 LYS A CE 1 ATOM 1626 N NZ . LYS A 1 249 ? 39.489 19.841 15.001 1.00 35.16 ? 249 LYS A NZ 1 ATOM 1627 N N . GLY A 1 250 ? 34.523 15.019 13.069 1.00 24.78 ? 250 GLY A N 1 ATOM 1628 C CA . GLY A 1 250 ? 33.247 14.627 13.679 1.00 24.73 ? 250 GLY A CA 1 ATOM 1629 C C . GLY A 1 250 ? 32.321 13.754 12.841 1.00 24.23 ? 250 GLY A C 1 ATOM 1630 O O . GLY A 1 250 ? 31.187 13.489 13.252 1.00 24.36 ? 250 GLY A O 1 ATOM 1631 N N . ALA A 1 251 ? 32.785 13.322 11.667 1.00 22.98 ? 251 ALA A N 1 ATOM 1632 C CA . ALA A 1 251 ? 32.010 12.435 10.810 1.00 22.91 ? 251 ALA A CA 1 ATOM 1633 C C . ALA A 1 251 ? 32.037 11.016 11.369 1.00 22.86 ? 251 ALA A C 1 ATOM 1634 O O . ALA A 1 251 ? 33.065 10.544 11.831 1.00 21.43 ? 251 ALA A O 1 ATOM 1635 C CB . ALA A 1 251 ? 32.564 12.433 9.390 1.00 22.83 ? 251 ALA A CB 1 ATOM 1636 N N . VAL A 1 252 ? 30.896 10.345 11.308 1.00 23.27 ? 252 VAL A N 1 ATOM 1637 C CA . VAL A 1 252 ? 30.815 8.940 11.668 1.00 24.01 ? 252 VAL A CA 1 ATOM 1638 C C . VAL A 1 252 ? 31.144 8.084 10.441 1.00 24.35 ? 252 VAL A C 1 ATOM 1639 O O . VAL A 1 252 ? 31.431 8.618 9.352 1.00 24.95 ? 252 VAL A O 1 ATOM 1640 C CB . VAL A 1 252 ? 29.420 8.594 12.244 1.00 24.49 ? 252 VAL A CB 1 ATOM 1641 C CG1 . VAL A 1 252 ? 29.218 9.306 13.568 1.00 24.07 ? 252 VAL A CG1 1 ATOM 1642 C CG2 . VAL A 1 252 ? 28.297 8.935 11.258 1.00 24.59 ? 252 VAL A CG2 1 ATOM 1643 N N . ASP A 1 253 ? 31.106 6.763 10.610 1.00 23.41 ? 253 ASP A N 1 ATOM 1644 C CA . ASP A 1 253 ? 31.397 5.845 9.509 1.00 22.53 ? 253 ASP A CA 1 ATOM 1645 C C . ASP A 1 253 ? 30.175 5.564 8.644 1.00 21.23 ? 253 ASP A C 1 ATOM 1646 O O . ASP A 1 253 ? 30.280 5.482 7.419 1.00 21.70 ? 253 ASP A O 1 ATOM 1647 C CB . ASP A 1 253 ? 31.935 4.526 10.056 1.00 23.43 ? 253 ASP A CB 1 ATOM 1648 C CG . ASP A 1 253 ? 33.206 4.702 10.840 1.00 23.47 ? 253 ASP A CG 1 ATOM 1649 O OD1 . ASP A 1 253 ? 34.106 5.434 10.378 1.00 25.05 ? 253 ASP A OD1 1 ATOM 1650 O OD2 . ASP A 1 253 ? 33.315 4.092 11.916 1.00 24.42 -1 253 ASP A OD2 1 ATOM 1651 N N . ILE A 1 254 ? 29.024 5.388 9.280 1.00 19.93 ? 254 ILE A N 1 ATOM 1652 C CA . ILE A 1 254 ? 27.781 5.153 8.555 1.00 18.89 ? 254 ILE A CA 1 ATOM 1653 C C . ILE A 1 254 ? 26.744 6.174 8.980 1.00 18.57 ? 254 ILE A C 1 ATOM 1654 O O . ILE A 1 254 ? 26.423 6.277 10.158 1.00 18.56 ? 254 ILE A O 1 ATOM 1655 C CB . ILE A 1 254 ? 27.246 3.725 8.791 1.00 18.64 ? 254 ILE A CB 1 ATOM 1656 C CG1 . ILE A 1 254 ? 28.269 2.683 8.327 1.00 18.47 ? 254 ILE A CG1 1 ATOM 1657 C CG2 . ILE A 1 254 ? 25.923 3.519 8.067 1.00 18.27 ? 254 ILE A CG2 1 ATOM 1658 C CD1 . ILE A 1 254 ? 27.858 1.249 8.618 1.00 18.81 ? 254 ILE A CD1 1 ATOM 1659 N N . TYR A 1 255 ? 26.224 6.928 8.014 1.00 18.87 ? 255 TYR A N 1 ATOM 1660 C CA . TYR A 1 255 ? 25.182 7.933 8.276 1.00 18.70 ? 255 TYR A CA 1 ATOM 1661 C C . TYR A 1 255 ? 23.831 7.256 8.447 1.00 18.85 ? 255 TYR A C 1 ATOM 1662 O O . TYR A 1 255 ? 23.363 6.557 7.541 1.00 18.19 ? 255 TYR A O 1 ATOM 1663 C CB . TYR A 1 255 ? 25.084 8.968 7.136 1.00 18.37 ? 255 TYR A CB 1 ATOM 1664 C CG . TYR A 1 255 ? 23.998 9.970 7.390 1.00 17.84 ? 255 TYR A CG 1 ATOM 1665 C CD1 . TYR A 1 255 ? 24.220 11.080 8.207 1.00 17.95 ? 255 TYR A CD1 1 ATOM 1666 C CD2 . TYR A 1 255 ? 22.719 9.778 6.880 1.00 17.72 ? 255 TYR A CD2 1 ATOM 1667 C CE1 . TYR A 1 255 ? 23.197 11.988 8.477 1.00 17.64 ? 255 TYR A CE1 1 ATOM 1668 C CE2 . TYR A 1 255 ? 21.692 10.679 7.145 1.00 17.49 ? 255 TYR A CE2 1 ATOM 1669 C CZ . TYR A 1 255 ? 21.932 11.779 7.947 1.00 17.46 ? 255 TYR A CZ 1 ATOM 1670 O OH . TYR A 1 255 ? 20.910 12.672 8.215 1.00 16.77 ? 255 TYR A OH 1 ATOM 1671 N N . GLY A 1 256 ? 23.212 7.466 9.609 1.00 19.30 ? 256 GLY A N 1 ATOM 1672 C CA . GLY A 1 256 ? 21.834 7.023 9.851 1.00 19.38 ? 256 GLY A CA 1 ATOM 1673 C C . GLY A 1 256 ? 20.955 8.200 10.243 1.00 19.92 ? 256 GLY A C 1 ATOM 1674 O O . GLY A 1 256 ? 21.447 9.233 10.713 1.00 19.60 ? 256 GLY A O 1 ATOM 1675 N N . HIS A 1 257 ? 19.650 8.046 10.032 1.00 20.25 ? 257 HIS A N 1 ATOM 1676 C CA . HIS A 1 257 ? 18.664 9.017 10.501 1.00 20.49 ? 257 HIS A CA 1 ATOM 1677 C C . HIS A 1 257 ? 17.413 8.310 11.027 1.00 21.08 ? 257 HIS A C 1 ATOM 1678 O O . HIS A 1 257 ? 17.312 7.092 10.959 1.00 20.45 ? 257 HIS A O 1 ATOM 1679 C CB . HIS A 1 257 ? 18.331 10.047 9.408 1.00 20.17 ? 257 HIS A CB 1 ATOM 1680 C CG . HIS A 1 257 ? 17.449 9.530 8.318 1.00 20.20 ? 257 HIS A CG 1 ATOM 1681 N ND1 . HIS A 1 257 ? 16.072 9.508 8.420 1.00 20.29 ? 257 HIS A ND1 1 ATOM 1682 C CD2 . HIS A 1 257 ? 17.741 9.043 7.090 1.00 19.86 ? 257 HIS A CD2 1 ATOM 1683 C CE1 . HIS A 1 257 ? 15.558 9.020 7.305 1.00 19.67 ? 257 HIS A CE1 1 ATOM 1684 N NE2 . HIS A 1 257 ? 16.548 8.725 6.484 1.00 19.36 ? 257 HIS A NE2 1 ATOM 1685 N N . ASP A 1 258 ? 16.483 9.083 11.583 1.00 22.41 ? 258 ASP A N 1 ATOM 1686 C CA . ASP A 1 258 ? 15.298 8.531 12.251 1.00 22.72 ? 258 ASP A CA 1 ATOM 1687 C C . ASP A 1 258 ? 14.020 9.014 11.579 1.00 22.51 ? 258 ASP A C 1 ATOM 1688 O O . ASP A 1 258 ? 14.052 9.939 10.769 1.00 23.26 ? 258 ASP A O 1 ATOM 1689 C CB . ASP A 1 258 ? 15.290 8.940 13.730 1.00 22.77 ? 258 ASP A CB 1 ATOM 1690 C CG . ASP A 1 258 ? 16.490 8.403 14.500 1.00 22.83 ? 258 ASP A CG 1 ATOM 1691 O OD1 . ASP A 1 258 ? 17.161 7.477 14.000 1.00 21.90 ? 258 ASP A OD1 1 ATOM 1692 O OD2 . ASP A 1 258 ? 16.761 8.907 15.616 1.00 23.64 -1 258 ASP A OD2 1 ATOM 1693 N N . SER A 1 259 ? 12.896 8.395 11.931 1.00 21.97 ? 259 SER A N 1 ATOM 1694 C CA . SER A 1 259 ? 11.624 8.707 11.292 1.00 21.88 ? 259 SER A CA 1 ATOM 1695 C C . SER A 1 259 ? 10.426 8.166 12.082 1.00 21.49 ? 259 SER A C 1 ATOM 1696 O O . SER A 1 259 ? 10.314 6.959 12.311 1.00 20.21 ? 259 SER A O 1 ATOM 1697 C CB . SER A 1 259 ? 11.597 8.129 9.877 1.00 22.27 ? 259 SER A CB 1 ATOM 1698 O OG . SER A 1 259 ? 10.366 8.407 9.241 1.00 23.27 ? 259 SER A OG 1 ATOM 1699 N N . TYR A 1 260 ? 9.533 9.070 12.483 1.00 20.94 ? 260 TYR A N 1 ATOM 1700 C CA . TYR A 1 260 ? 8.269 8.696 13.107 1.00 21.18 ? 260 TYR A CA 1 ATOM 1701 C C . TYR A 1 260 ? 7.156 9.376 12.316 1.00 22.02 ? 260 TYR A C 1 ATOM 1702 O O . TYR A 1 260 ? 6.607 10.398 12.737 1.00 22.30 ? 260 TYR A O 1 ATOM 1703 C CB . TYR A 1 260 ? 8.242 9.115 14.576 1.00 20.86 ? 260 TYR A CB 1 ATOM 1704 C CG . TYR A 1 260 ? 9.253 8.417 15.469 1.00 20.58 ? 260 TYR A CG 1 ATOM 1705 C CD1 . TYR A 1 260 ? 10.597 8.781 15.450 1.00 21.14 ? 260 TYR A CD1 1 ATOM 1706 C CD2 . TYR A 1 260 ? 8.867 7.422 16.360 1.00 20.63 ? 260 TYR A CD2 1 ATOM 1707 C CE1 . TYR A 1 260 ? 11.531 8.167 16.268 1.00 20.85 ? 260 TYR A CE1 1 ATOM 1708 C CE2 . TYR A 1 260 ? 9.799 6.794 17.184 1.00 20.44 ? 260 TYR A CE2 1 ATOM 1709 C CZ . TYR A 1 260 ? 11.125 7.179 17.137 1.00 20.82 ? 260 TYR A CZ 1 ATOM 1710 O OH . TYR A 1 260 ? 12.064 6.580 17.948 1.00 21.59 ? 260 TYR A OH 1 ATOM 1711 N N . PRO A 1 261 ? 6.833 8.820 11.144 1.00 23.10 ? 261 PRO A N 1 ATOM 1712 C CA . PRO A 1 261 ? 6.017 9.543 10.169 1.00 24.27 ? 261 PRO A CA 1 ATOM 1713 C C . PRO A 1 261 ? 4.532 9.699 10.544 1.00 25.22 ? 261 PRO A C 1 ATOM 1714 O O . PRO A 1 261 ? 3.866 10.593 10.030 1.00 25.60 ? 261 PRO A O 1 ATOM 1715 C CB . PRO A 1 261 ? 6.171 8.697 8.899 1.00 24.02 ? 261 PRO A CB 1 ATOM 1716 C CG . PRO A 1 261 ? 6.407 7.319 9.406 1.00 23.84 ? 261 PRO A CG 1 ATOM 1717 C CD . PRO A 1 261 ? 7.213 7.480 10.662 1.00 23.56 ? 261 PRO A CD 1 ATOM 1718 N N . LEU A 1 262 ? 4.024 8.855 11.430 1.00 25.92 ? 262 LEU A N 1 ATOM 1719 C CA . LEU A 1 262 ? 2.609 8.902 11.795 1.00 27.38 ? 262 LEU A CA 1 ATOM 1720 C C . LEU A 1 262 ? 2.362 9.667 13.094 1.00 29.63 ? 262 LEU A C 1 ATOM 1721 O O . LEU A 1 262 ? 1.235 9.714 13.579 1.00 31.63 ? 262 LEU A O 1 ATOM 1722 C CB . LEU A 1 262 ? 2.054 7.479 11.889 1.00 27.43 ? 262 LEU A CB 1 ATOM 1723 C CG . LEU A 1 262 ? 0.689 7.181 11.272 1.00 27.40 ? 262 LEU A CG 1 ATOM 1724 C CD1 . LEU A 1 262 ? 0.513 7.856 9.919 1.00 26.85 ? 262 LEU A CD1 1 ATOM 1725 C CD2 . LEU A 1 262 ? 0.494 5.671 11.159 1.00 27.37 ? 262 LEU A CD2 1 ATOM 1726 N N . GLY A 1 263 ? 3.409 10.271 13.653 1.00 31.15 ? 263 GLY A N 1 ATOM 1727 C CA . GLY A 1 263 ? 3.259 11.143 14.809 1.00 32.07 ? 263 GLY A CA 1 ATOM 1728 C C . GLY A 1 263 ? 3.035 10.369 16.092 1.00 35.12 ? 263 GLY A C 1 ATOM 1729 O O . GLY A 1 263 ? 3.165 9.139 16.119 1.00 34.63 ? 263 GLY A O 1 ATOM 1730 N N . PHE A 1 264 ? 2.686 11.099 17.152 1.00 37.31 ? 264 PHE A N 1 ATOM 1731 C CA . PHE A 1 264 ? 2.520 10.530 18.487 1.00 38.22 ? 264 PHE A CA 1 ATOM 1732 C C . PHE A 1 264 ? 1.130 10.793 19.063 1.00 42.11 ? 264 PHE A C 1 ATOM 1733 O O . PHE A 1 264 ? 0.951 10.821 20.282 1.00 43.43 ? 264 PHE A O 1 ATOM 1734 C CB . PHE A 1 264 ? 3.594 11.097 19.399 1.00 37.17 ? 264 PHE A CB 1 ATOM 1735 C CG . PHE A 1 264 ? 4.980 10.884 18.878 1.00 35.94 ? 264 PHE A CG 1 ATOM 1736 C CD1 . PHE A 1 264 ? 5.520 9.605 18.826 1.00 34.79 ? 264 PHE A CD1 1 ATOM 1737 C CD2 . PHE A 1 264 ? 5.732 11.948 18.415 1.00 34.96 ? 264 PHE A CD2 1 ATOM 1738 C CE1 . PHE A 1 264 ? 6.791 9.392 18.331 1.00 34.73 ? 264 PHE A CE1 1 ATOM 1739 C CE2 . PHE A 1 264 ? 7.008 11.745 17.924 1.00 34.86 ? 264 PHE A CE2 1 ATOM 1740 C CZ . PHE A 1 264 ? 7.541 10.465 17.883 1.00 35.49 ? 264 PHE A CZ 1 ATOM 1741 N N . ASP A 1 265 ? 0.146 10.946 18.178 1.00 45.00 ? 265 ASP A N 1 ATOM 1742 C CA . ASP A 1 265 ? -1.216 11.251 18.575 1.00 45.06 ? 265 ASP A CA 1 ATOM 1743 C C . ASP A 1 265 ? -2.064 10.002 18.444 1.00 41.44 ? 265 ASP A C 1 ATOM 1744 O O . ASP A 1 265 ? -2.707 9.774 17.424 1.00 43.63 ? 265 ASP A O 1 ATOM 1745 C CB . ASP A 1 265 ? -1.790 12.376 17.711 1.00 48.64 ? 265 ASP A CB 1 ATOM 1746 C CG . ASP A 1 265 ? -3.187 12.789 18.148 1.00 52.00 ? 265 ASP A CG 1 ATOM 1747 O OD1 . ASP A 1 265 ? -3.340 13.171 19.337 1.00 50.82 ? 265 ASP A OD1 1 ATOM 1748 O OD2 . ASP A 1 265 ? -4.121 12.723 17.305 1.00 52.44 -1 265 ASP A OD2 1 ATOM 1749 N N . CYS A 1 266 ? -2.078 9.207 19.505 1.00 37.46 ? 266 CYS A N 1 ATOM 1750 C CA . CYS A 1 266 ? -2.792 7.945 19.519 1.00 35.36 ? 266 CYS A CA 1 ATOM 1751 C C . CYS A 1 266 ? -4.322 8.110 19.735 1.00 33.78 ? 266 CYS A C 1 ATOM 1752 O O . CYS A 1 266 ? -5.039 7.110 19.868 1.00 32.63 ? 266 CYS A O 1 ATOM 1753 C CB . CYS A 1 266 ? -2.187 7.032 20.608 1.00 35.88 ? 266 CYS A CB 1 ATOM 1754 S SG . CYS A 1 266 ? -0.399 6.663 20.470 1.00 38.90 ? 266 CYS A SG 1 ATOM 1755 N N . ALA A 1 267 ? -4.819 9.352 19.777 1.00 31.57 ? 267 ALA A N 1 ATOM 1756 C CA . ALA A 1 267 ? -6.245 9.622 20.052 1.00 30.90 ? 267 ALA A CA 1 ATOM 1757 C C . ALA A 1 267 ? -7.165 9.289 18.871 1.00 30.02 ? 267 ALA A C 1 ATOM 1758 O O . ALA A 1 267 ? -8.326 8.945 19.068 1.00 29.27 ? 267 ALA A O 1 ATOM 1759 C CB . ALA A 1 267 ? -6.449 11.079 20.464 1.00 30.82 ? 267 ALA A CB 1 ATOM 1760 N N . ASN A 1 268 ? -6.645 9.401 17.654 1.00 28.53 ? 268 ASN A N 1 ATOM 1761 C CA . ASN A 1 268 ? -7.400 9.098 16.449 1.00 27.67 ? 268 ASN A CA 1 ATOM 1762 C C . ASN A 1 268 ? -6.706 7.969 15.685 1.00 27.03 ? 268 ASN A C 1 ATOM 1763 O O . ASN A 1 268 ? -6.116 8.194 14.635 1.00 25.72 ? 268 ASN A O 1 ATOM 1764 C CB . ASN A 1 268 ? -7.491 10.361 15.589 1.00 28.76 ? 268 ASN A CB 1 ATOM 1765 C CG . ASN A 1 268 ? -8.122 11.533 16.335 1.00 29.60 ? 268 ASN A CG 1 ATOM 1766 O OD1 . ASN A 1 268 ? -7.440 12.484 16.730 1.00 29.48 ? 268 ASN A OD1 1 ATOM 1767 N ND2 . ASN A 1 268 ? -9.426 11.456 16.545 1.00 29.61 ? 268 ASN A ND2 1 ATOM 1768 N N . PRO A 1 269 ? -6.779 6.737 16.214 1.00 26.33 ? 269 PRO A N 1 ATOM 1769 C CA . PRO A 1 269 ? -5.941 5.662 15.690 1.00 26.05 ? 269 PRO A CA 1 ATOM 1770 C C . PRO A 1 269 ? -6.234 5.198 14.261 1.00 24.96 ? 269 PRO A C 1 ATOM 1771 O O . PRO A 1 269 ? -5.392 4.507 13.679 1.00 23.93 ? 269 PRO A O 1 ATOM 1772 C CB . PRO A 1 269 ? -6.153 4.515 16.688 1.00 26.23 ? 269 PRO A CB 1 ATOM 1773 C CG . PRO A 1 269 ? -7.405 4.846 17.408 1.00 26.53 ? 269 PRO A CG 1 ATOM 1774 C CD . PRO A 1 269 ? -7.528 6.329 17.411 1.00 26.24 ? 269 PRO A CD 1 ATOM 1775 N N . THR A 1 270 ? -7.387 5.560 13.701 1.00 23.56 ? 270 THR A N 1 ATOM 1776 C CA . THR A 1 270 ? -7.709 5.188 12.313 1.00 23.26 ? 270 THR A CA 1 ATOM 1777 C C . THR A 1 270 ? -7.330 6.269 11.305 1.00 22.63 ? 270 THR A C 1 ATOM 1778 O O . THR A 1 270 ? -7.474 6.072 10.097 1.00 22.36 ? 270 THR A O 1 ATOM 1779 C CB . THR A 1 270 ? -9.209 4.881 12.139 1.00 23.17 ? 270 THR A CB 1 ATOM 1780 O OG1 . THR A 1 270 ? -9.966 6.070 12.336 1.00 22.74 ? 270 THR A OG1 1 ATOM 1781 C CG2 . THR A 1 270 ? -9.660 3.825 13.150 1.00 23.93 ? 270 THR A CG2 1 ATOM 1782 N N . VAL A 1 271 ? -6.854 7.412 11.794 1.00 21.96 ? 271 VAL A N 1 ATOM 1783 C CA . VAL A 1 271 ? -6.564 8.545 10.927 1.00 21.65 ? 271 VAL A CA 1 ATOM 1784 C C . VAL A 1 271 ? -5.121 8.480 10.454 1.00 20.99 ? 271 VAL A C 1 ATOM 1785 O O . VAL A 1 271 ? -4.209 8.442 11.267 1.00 19.31 ? 271 VAL A O 1 ATOM 1786 C CB . VAL A 1 271 ? -6.832 9.893 11.632 1.00 21.85 ? 271 VAL A CB 1 ATOM 1787 C CG1 . VAL A 1 271 ? -6.388 11.059 10.755 1.00 21.93 ? 271 VAL A CG1 1 ATOM 1788 C CG2 . VAL A 1 271 ? -8.311 10.023 11.959 1.00 22.25 ? 271 VAL A CG2 1 ATOM 1789 N N . TRP A 1 272 ? -4.950 8.464 9.131 1.00 21.32 ? 272 TRP A N 1 ATOM 1790 C CA . TRP A 1 272 ? -3.651 8.479 8.474 1.00 21.91 ? 272 TRP A CA 1 ATOM 1791 C C . TRP A 1 272 ? -3.526 9.765 7.645 1.00 23.18 ? 272 TRP A C 1 ATOM 1792 O O . TRP A 1 272 ? -3.871 9.767 6.466 1.00 23.42 ? 272 TRP A O 1 ATOM 1793 C CB . TRP A 1 272 ? -3.527 7.248 7.562 1.00 21.25 ? 272 TRP A CB 1 ATOM 1794 C CG . TRP A 1 272 ? -3.158 5.969 8.258 1.00 20.46 ? 272 TRP A CG 1 ATOM 1795 C CD1 . TRP A 1 272 ? -3.255 5.689 9.591 1.00 20.36 ? 272 TRP A CD1 1 ATOM 1796 C CD2 . TRP A 1 272 ? -2.668 4.771 7.632 1.00 20.45 ? 272 TRP A CD2 1 ATOM 1797 N NE1 . TRP A 1 272 ? -2.838 4.397 9.837 1.00 20.76 ? 272 TRP A NE1 1 ATOM 1798 C CE2 . TRP A 1 272 ? -2.470 3.815 8.652 1.00 20.16 ? 272 TRP A CE2 1 ATOM 1799 C CE3 . TRP A 1 272 ? -2.361 4.422 6.311 1.00 20.29 ? 272 TRP A CE3 1 ATOM 1800 C CZ2 . TRP A 1 272 ? -1.985 2.537 8.392 1.00 20.21 ? 272 TRP A CZ2 1 ATOM 1801 C CZ3 . TRP A 1 272 ? -1.872 3.154 6.053 1.00 20.11 ? 272 TRP A CZ3 1 ATOM 1802 C CH2 . TRP A 1 272 ? -1.690 2.225 7.088 1.00 20.12 ? 272 TRP A CH2 1 ATOM 1803 N N . PRO A 1 273 ? -3.027 10.866 8.250 1.00 24.61 ? 273 PRO A N 1 ATOM 1804 C CA . PRO A 1 273 ? -3.092 12.172 7.568 1.00 24.73 ? 273 PRO A CA 1 ATOM 1805 C C . PRO A 1 273 ? -2.426 12.214 6.186 1.00 26.30 ? 273 PRO A C 1 ATOM 1806 O O . PRO A 1 273 ? -1.465 11.476 5.914 1.00 25.00 ? 273 PRO A O 1 ATOM 1807 C CB . PRO A 1 273 ? -2.381 13.124 8.542 1.00 24.39 ? 273 PRO A CB 1 ATOM 1808 C CG . PRO A 1 273 ? -2.520 12.476 9.872 1.00 25.01 ? 273 PRO A CG 1 ATOM 1809 C CD . PRO A 1 273 ? -2.458 10.990 9.604 1.00 24.96 ? 273 PRO A CD 1 ATOM 1810 N N . SER A 1 274 ? -2.951 13.090 5.332 1.00 26.56 ? 274 SER A N 1 ATOM 1811 C CA . SER A 1 274 ? -2.477 13.242 3.964 1.00 26.03 ? 274 SER A CA 1 ATOM 1812 C C . SER A 1 274 ? -0.971 13.534 3.941 1.00 24.78 ? 274 SER A C 1 ATOM 1813 O O . SER A 1 274 ? -0.472 14.309 4.738 1.00 24.84 ? 274 SER A O 1 ATOM 1814 C CB . SER A 1 274 ? -3.254 14.389 3.307 1.00 27.34 ? 274 SER A CB 1 ATOM 1815 O OG . SER A 1 274 ? -2.864 14.589 1.961 1.00 29.33 ? 274 SER A OG 1 ATOM 1816 N N . GLY A 1 275 ? -0.240 12.868 3.062 1.00 24.50 ? 275 GLY A N 1 ATOM 1817 C CA . GLY A 1 275 ? 1.180 13.173 2.861 1.00 24.43 ? 275 GLY A CA 1 ATOM 1818 C C . GLY A 1 275 ? 2.198 12.676 3.877 1.00 24.33 ? 275 GLY A C 1 ATOM 1819 O O . GLY A 1 275 ? 3.385 12.941 3.719 1.00 23.27 ? 275 GLY A O 1 ATOM 1820 N N . ASP A 1 276 ? 1.756 11.943 4.899 1.00 24.52 ? 276 ASP A N 1 ATOM 1821 C CA . ASP A 1 276 ? 2.652 11.528 5.967 1.00 26.09 ? 276 ASP A CA 1 ATOM 1822 C C . ASP A 1 276 ? 3.511 10.305 5.613 1.00 24.85 ? 276 ASP A C 1 ATOM 1823 O O . ASP A 1 276 ? 4.449 9.992 6.323 1.00 25.37 ? 276 ASP A O 1 ATOM 1824 C CB . ASP A 1 276 ? 1.880 11.291 7.276 1.00 27.47 ? 276 ASP A CB 1 ATOM 1825 C CG . ASP A 1 276 ? 1.601 12.595 8.051 1.00 29.84 ? 276 ASP A CG 1 ATOM 1826 O OD1 . ASP A 1 276 ? 1.984 13.686 7.565 1.00 31.60 ? 276 ASP A OD1 1 ATOM 1827 O OD2 . ASP A 1 276 ? 1.000 12.520 9.152 1.00 31.29 -1 276 ASP A OD2 1 ATOM 1828 N N . LEU A 1 277 ? 3.210 9.612 4.528 1.00 24.56 ? 277 LEU A N 1 ATOM 1829 C CA . LEU A 1 277 ? 4.072 8.510 4.100 1.00 24.32 ? 277 LEU A CA 1 ATOM 1830 C C . LEU A 1 277 ? 5.280 9.106 3.381 1.00 24.22 ? 277 LEU A C 1 ATOM 1831 O O . LEU A 1 277 ? 5.116 9.787 2.367 1.00 24.84 ? 277 LEU A O 1 ATOM 1832 C CB . LEU A 1 277 ? 3.339 7.553 3.176 1.00 23.76 ? 277 LEU A CB 1 ATOM 1833 C CG . LEU A 1 277 ? 4.153 6.306 2.816 1.00 24.88 ? 277 LEU A CG 1 ATOM 1834 C CD1 . LEU A 1 277 ? 3.841 5.128 3.728 1.00 24.65 ? 277 LEU A CD1 1 ATOM 1835 C CD2 . LEU A 1 277 ? 3.874 5.921 1.374 1.00 25.91 ? 277 LEU A CD2 1 ATOM 1836 N N . PRO A 1 278 ? 6.499 8.875 3.907 1.00 23.53 ? 278 PRO A N 1 ATOM 1837 C CA . PRO A 1 278 ? 7.660 9.423 3.210 1.00 23.14 ? 278 PRO A CA 1 ATOM 1838 C C . PRO A 1 278 ? 7.824 8.880 1.783 1.00 22.66 ? 278 PRO A C 1 ATOM 1839 O O . PRO A 1 278 ? 7.533 7.713 1.518 1.00 20.79 ? 278 PRO A O 1 ATOM 1840 C CB . PRO A 1 278 ? 8.842 8.992 4.088 1.00 23.61 ? 278 PRO A CB 1 ATOM 1841 C CG . PRO A 1 278 ? 8.324 7.926 4.977 1.00 23.47 ? 278 PRO A CG 1 ATOM 1842 C CD . PRO A 1 278 ? 6.876 8.220 5.171 1.00 23.29 ? 278 PRO A CD 1 ATOM 1843 N N . THR A 1 279 ? 8.260 9.751 0.880 1.00 22.39 ? 279 THR A N 1 ATOM 1844 C CA . THR A 1 279 ? 8.558 9.364 -0.494 1.00 22.55 ? 279 THR A CA 1 ATOM 1845 C C . THR A 1 279 ? 9.983 9.717 -0.959 1.00 23.02 ? 279 THR A C 1 ATOM 1846 O O . THR A 1 279 ? 10.460 9.123 -1.925 1.00 22.60 ? 279 THR A O 1 ATOM 1847 C CB . THR A 1 279 ? 7.531 9.972 -1.468 1.00 21.96 ? 279 THR A CB 1 ATOM 1848 O OG1 . THR A 1 279 ? 7.451 11.388 -1.268 1.00 21.00 ? 279 THR A OG1 1 ATOM 1849 C CG2 . THR A 1 279 ? 6.158 9.347 -1.244 1.00 21.95 ? 279 THR A CG2 1 ATOM 1850 N N . ASN A 1 280 ? 10.660 10.649 -0.276 1.00 23.90 ? 280 ASN A N 1 ATOM 1851 C CA . ASN A 1 280 ? 11.936 11.220 -0.768 1.00 24.15 ? 280 ASN A CA 1 ATOM 1852 C C . ASN A 1 280 ? 13.196 10.687 -0.085 1.00 22.82 ? 280 ASN A C 1 ATOM 1853 O O . ASN A 1 280 ? 14.275 11.241 -0.261 1.00 21.45 ? 280 ASN A O 1 ATOM 1854 C CB . ASN A 1 280 ? 11.911 12.749 -0.661 1.00 25.06 ? 280 ASN A CB 1 ATOM 1855 C CG . ASN A 1 280 ? 11.872 13.245 0.774 1.00 27.14 ? 280 ASN A CG 1 ATOM 1856 O OD1 . ASN A 1 280 ? 11.601 12.494 1.712 1.00 28.50 ? 280 ASN A OD1 1 ATOM 1857 N ND2 . ASN A 1 280 ? 12.133 14.525 0.949 1.00 28.84 ? 280 ASN A ND2 1 ATOM 1858 N N . PHE A 1 281 ? 13.052 9.605 0.676 1.00 22.92 ? 281 PHE A N 1 ATOM 1859 C CA . PHE A 1 281 ? 14.116 9.117 1.562 1.00 23.17 ? 281 PHE A CA 1 ATOM 1860 C C . PHE A 1 281 ? 15.341 8.594 0.802 1.00 22.34 ? 281 PHE A C 1 ATOM 1861 O O . PHE A 1 281 ? 16.473 8.795 1.241 1.00 21.33 ? 281 PHE A O 1 ATOM 1862 C CB . PHE A 1 281 ? 13.572 8.031 2.522 1.00 23.46 ? 281 PHE A CB 1 ATOM 1863 C CG . PHE A 1 281 ? 12.961 8.564 3.802 1.00 23.77 ? 281 PHE A CG 1 ATOM 1864 C CD1 . PHE A 1 281 ? 12.789 9.925 4.032 1.00 24.16 ? 281 PHE A CD1 1 ATOM 1865 C CD2 . PHE A 1 281 ? 12.527 7.674 4.779 1.00 24.09 ? 281 PHE A CD2 1 ATOM 1866 C CE1 . PHE A 1 281 ? 12.226 10.383 5.220 1.00 24.13 ? 281 PHE A CE1 1 ATOM 1867 C CE2 . PHE A 1 281 ? 11.970 8.125 5.962 1.00 23.73 ? 281 PHE A CE2 1 ATOM 1868 C CZ . PHE A 1 281 ? 11.818 9.479 6.185 1.00 24.10 ? 281 PHE A CZ 1 ATOM 1869 N N . ARG A 1 282 ? 15.119 7.920 -0.321 1.00 23.05 ? 282 ARG A N 1 ATOM 1870 C CA . ARG A 1 282 ? 16.235 7.463 -1.127 1.00 24.39 ? 282 ARG A CA 1 ATOM 1871 C C . ARG A 1 282 ? 16.933 8.651 -1.798 1.00 23.03 ? 282 ARG A C 1 ATOM 1872 O O . ARG A 1 282 ? 18.157 8.723 -1.803 1.00 21.77 ? 282 ARG A O 1 ATOM 1873 C CB . ARG A 1 282 ? 15.820 6.432 -2.179 1.00 26.14 ? 282 ARG A CB 1 ATOM 1874 C CG . ARG A 1 282 ? 17.004 6.072 -3.066 1.00 28.19 ? 282 ARG A CG 1 ATOM 1875 C CD . ARG A 1 282 ? 16.937 4.707 -3.726 1.00 30.44 ? 282 ARG A CD 1 ATOM 1876 N NE . ARG A 1 282 ? 18.258 4.389 -4.281 1.00 32.96 ? 282 ARG A NE 1 ATOM 1877 C CZ . ARG A 1 282 ? 19.293 3.914 -3.577 1.00 35.40 ? 282 ARG A CZ 1 ATOM 1878 N NH1 . ARG A 1 282 ? 19.181 3.658 -2.267 1.00 35.91 ? 282 ARG A NH1 1 ATOM 1879 N NH2 . ARG A 1 282 ? 20.452 3.669 -4.190 1.00 35.68 ? 282 ARG A NH2 1 ATOM 1880 N N . THR A 1 283 ? 16.151 9.570 -2.354 1.00 21.98 ? 283 THR A N 1 ATOM 1881 C CA . THR A 1 283 ? 16.705 10.790 -2.936 1.00 22.16 ? 283 THR A CA 1 ATOM 1882 C C . THR A 1 283 ? 17.622 11.494 -1.928 1.00 22.15 ? 283 THR A C 1 ATOM 1883 O O . THR A 1 283 ? 18.768 11.818 -2.251 1.00 21.88 ? 283 THR A O 1 ATOM 1884 C CB . THR A 1 283 ? 15.583 11.740 -3.418 1.00 22.50 ? 283 THR A CB 1 ATOM 1885 O OG1 . THR A 1 283 ? 14.823 11.092 -4.445 1.00 22.94 ? 283 THR A OG1 1 ATOM 1886 C CG2 . THR A 1 283 ? 16.154 13.033 -3.969 1.00 22.93 ? 283 THR A CG2 1 ATOM 1887 N N . LEU A 1 284 ? 17.142 11.701 -0.701 1.00 21.64 ? 284 LEU A N 1 ATOM 1888 C CA . LEU A 1 284 ? 17.968 12.377 0.308 1.00 21.81 ? 284 LEU A CA 1 ATOM 1889 C C . LEU A 1 284 ? 19.208 11.556 0.697 1.00 21.57 ? 284 LEU A C 1 ATOM 1890 O O . LEU A 1 284 ? 20.281 12.117 0.921 1.00 21.76 ? 284 LEU A O 1 ATOM 1891 C CB . LEU A 1 284 ? 17.139 12.752 1.544 1.00 22.19 ? 284 LEU A CB 1 ATOM 1892 C CG . LEU A 1 284 ? 16.045 13.813 1.343 1.00 22.66 ? 284 LEU A CG 1 ATOM 1893 C CD1 . LEU A 1 284 ? 15.257 14.029 2.629 1.00 22.79 ? 284 LEU A CD1 1 ATOM 1894 C CD2 . LEU A 1 284 ? 16.610 15.143 0.865 1.00 22.79 ? 284 LEU A CD2 1 ATOM 1895 N N . HIS A 1 285 ? 19.067 10.233 0.762 1.00 21.34 ? 285 HIS A N 1 ATOM 1896 C CA . HIS A 1 285 ? 20.203 9.343 1.040 1.00 21.68 ? 285 HIS A CA 1 ATOM 1897 C C . HIS A 1 285 ? 21.378 9.477 0.050 1.00 22.78 ? 285 HIS A C 1 ATOM 1898 O O . HIS A 1 285 ? 22.545 9.545 0.452 1.00 22.35 ? 285 HIS A O 1 ATOM 1899 C CB . HIS A 1 285 ? 19.741 7.882 1.069 1.00 21.34 ? 285 HIS A CB 1 ATOM 1900 C CG . HIS A 1 285 ? 20.874 6.918 1.100 1.00 21.15 ? 285 HIS A CG 1 ATOM 1901 N ND1 . HIS A 1 285 ? 21.719 6.814 2.179 1.00 21.08 ? 285 HIS A ND1 1 ATOM 1902 C CD2 . HIS A 1 285 ? 21.350 6.068 0.162 1.00 21.35 ? 285 HIS A CD2 1 ATOM 1903 C CE1 . HIS A 1 285 ? 22.646 5.914 1.918 1.00 21.27 ? 285 HIS A CE1 1 ATOM 1904 N NE2 . HIS A 1 285 ? 22.448 5.450 0.698 1.00 21.09 ? 285 HIS A NE2 1 ATOM 1905 N N . LEU A 1 286 ? 21.060 9.504 -1.238 1.00 24.37 ? 286 LEU A N 1 ATOM 1906 C CA . LEU A 1 286 ? 22.066 9.666 -2.287 1.00 26.48 ? 286 LEU A CA 1 ATOM 1907 C C . LEU A 1 286 ? 22.712 11.052 -2.285 1.00 27.18 ? 286 LEU A C 1 ATOM 1908 O O . LEU A 1 286 ? 23.892 11.181 -2.608 1.00 29.69 ? 286 LEU A O 1 ATOM 1909 C CB . LEU A 1 286 ? 21.449 9.372 -3.665 1.00 27.50 ? 286 LEU A CB 1 ATOM 1910 C CG . LEU A 1 286 ? 20.983 7.924 -3.895 1.00 28.41 ? 286 LEU A CG 1 ATOM 1911 C CD1 . LEU A 1 286 ? 20.442 7.718 -5.306 1.00 28.45 ? 286 LEU A CD1 1 ATOM 1912 C CD2 . LEU A 1 286 ? 22.127 6.957 -3.623 1.00 29.08 ? 286 LEU A CD2 1 ATOM 1913 N N . GLU A 1 287 ? 21.955 12.082 -1.925 1.00 26.91 ? 287 GLU A N 1 ATOM 1914 C CA . GLU A 1 287 ? 22.530 13.415 -1.730 1.00 27.71 ? 287 GLU A CA 1 ATOM 1915 C C . GLU A 1 287 ? 23.443 13.471 -0.493 1.00 26.90 ? 287 GLU A C 1 ATOM 1916 O O . GLU A 1 287 ? 24.486 14.124 -0.516 1.00 28.61 ? 287 GLU A O 1 ATOM 1917 C CB . GLU A 1 287 ? 21.419 14.479 -1.607 1.00 29.14 ? 287 GLU A CB 1 ATOM 1918 C CG . GLU A 1 287 ? 20.533 14.623 -2.844 1.00 30.12 ? 287 GLU A CG 1 ATOM 1919 C CD . GLU A 1 287 ? 19.369 15.610 -2.676 1.00 31.71 ? 287 GLU A CD 1 ATOM 1920 O OE1 . GLU A 1 287 ? 19.162 16.167 -1.580 1.00 32.53 ? 287 GLU A OE1 1 ATOM 1921 O OE2 . GLU A 1 287 ? 18.648 15.851 -3.666 1.00 33.94 -1 287 GLU A OE2 1 ATOM 1922 N N . GLN A 1 288 ? 23.070 12.776 0.578 1.00 25.05 ? 288 GLN A N 1 ATOM 1923 C CA . GLN A 1 288 ? 23.716 12.980 1.871 1.00 24.57 ? 288 GLN A CA 1 ATOM 1924 C C . GLN A 1 288 ? 24.817 11.976 2.247 1.00 23.91 ? 288 GLN A C 1 ATOM 1925 O O . GLN A 1 288 ? 25.738 12.315 2.996 1.00 23.24 ? 288 GLN A O 1 ATOM 1926 C CB . GLN A 1 288 ? 22.650 13.004 2.968 1.00 25.19 ? 288 GLN A CB 1 ATOM 1927 C CG . GLN A 1 288 ? 21.773 14.245 2.957 1.00 25.59 ? 288 GLN A CG 1 ATOM 1928 C CD . GLN A 1 288 ? 20.544 14.103 3.844 1.00 26.99 ? 288 GLN A CD 1 ATOM 1929 O OE1 . GLN A 1 288 ? 20.407 13.128 4.594 1.00 29.98 ? 288 GLN A OE1 1 ATOM 1930 N NE2 . GLN A 1 288 ? 19.639 15.076 3.765 1.00 26.03 ? 288 GLN A NE2 1 ATOM 1931 N N . SER A 1 289 ? 24.703 10.735 1.779 1.00 23.56 ? 289 SER A N 1 ATOM 1932 C CA . SER A 1 289 ? 25.680 9.708 2.126 1.00 23.27 ? 289 SER A CA 1 ATOM 1933 C C . SER A 1 289 ? 25.610 8.526 1.189 1.00 22.20 ? 289 SER A C 1 ATOM 1934 O O . SER A 1 289 ? 25.370 7.400 1.629 1.00 21.47 ? 289 SER A O 1 ATOM 1935 C CB . SER A 1 289 ? 25.485 9.228 3.569 1.00 23.63 ? 289 SER A CB 1 ATOM 1936 O OG . SER A 1 289 ? 26.569 8.398 3.957 1.00 24.40 ? 289 SER A OG 1 ATOM 1937 N N . PRO A 1 290 ? 25.866 8.769 -0.108 1.00 23.03 ? 290 PRO A N 1 ATOM 1938 C CA . PRO A 1 290 ? 25.711 7.726 -1.133 1.00 22.78 ? 290 PRO A CA 1 ATOM 1939 C C . PRO A 1 290 ? 26.669 6.532 -0.988 1.00 22.94 ? 290 PRO A C 1 ATOM 1940 O O . PRO A 1 290 ? 26.427 5.498 -1.595 1.00 22.51 ? 290 PRO A O 1 ATOM 1941 C CB . PRO A 1 290 ? 25.978 8.483 -2.446 1.00 22.98 ? 290 PRO A CB 1 ATOM 1942 C CG . PRO A 1 290 ? 26.855 9.622 -2.061 1.00 23.28 ? 290 PRO A CG 1 ATOM 1943 C CD . PRO A 1 290 ? 26.440 10.012 -0.667 1.00 22.98 ? 290 PRO A CD 1 ATOM 1944 N N . THR A 1 291 ? 27.733 6.667 -0.191 1.00 23.78 ? 291 THR A N 1 ATOM 1945 C CA . THR A 1 291 ? 28.750 5.616 -0.074 1.00 23.93 ? 291 THR A CA 1 ATOM 1946 C C . THR A 1 291 ? 28.486 4.570 1.030 1.00 24.17 ? 291 THR A C 1 ATOM 1947 O O . THR A 1 291 ? 29.181 3.555 1.085 1.00 23.77 ? 291 THR A O 1 ATOM 1948 C CB . THR A 1 291 ? 30.146 6.220 0.177 1.00 24.15 ? 291 THR A CB 1 ATOM 1949 O OG1 . THR A 1 291 ? 30.230 6.727 1.514 1.00 24.93 ? 291 THR A OG1 1 ATOM 1950 C CG2 . THR A 1 291 ? 30.440 7.339 -0.812 1.00 24.79 ? 291 THR A CG2 1 ATOM 1951 N N . THR A 1 292 ? 27.506 4.829 1.903 1.00 23.95 ? 292 THR A N 1 ATOM 1952 C CA . THR A 1 292 ? 27.169 3.926 3.014 1.00 22.60 ? 292 THR A CA 1 ATOM 1953 C C . THR A 1 292 ? 25.755 3.349 2.854 1.00 21.62 ? 292 THR A C 1 ATOM 1954 O O . THR A 1 292 ? 24.923 3.943 2.172 1.00 21.40 ? 292 THR A O 1 ATOM 1955 C CB . THR A 1 292 ? 27.277 4.661 4.360 1.00 22.48 ? 292 THR A CB 1 ATOM 1956 O OG1 . THR A 1 292 ? 26.476 5.852 4.336 1.00 21.32 ? 292 THR A OG1 1 ATOM 1957 C CG2 . THR A 1 292 ? 28.734 5.021 4.640 1.00 22.53 ? 292 THR A CG2 1 ATOM 1958 N N . PRO A 1 293 ? 25.474 2.190 3.481 1.00 20.20 ? 293 PRO A N 1 ATOM 1959 C CA . PRO A 1 293 ? 24.137 1.586 3.315 1.00 20.00 ? 293 PRO A CA 1 ATOM 1960 C C . PRO A 1 293 ? 23.000 2.462 3.858 1.00 18.78 ? 293 PRO A C 1 ATOM 1961 O O . PRO A 1 293 ? 23.202 3.196 4.828 1.00 17.71 ? 293 PRO A O 1 ATOM 1962 C CB . PRO A 1 293 ? 24.239 0.264 4.104 1.00 19.94 ? 293 PRO A CB 1 ATOM 1963 C CG . PRO A 1 293 ? 25.705 -0.016 4.189 1.00 20.05 ? 293 PRO A CG 1 ATOM 1964 C CD . PRO A 1 293 ? 26.350 1.342 4.309 1.00 20.30 ? 293 PRO A CD 1 ATOM 1965 N N . TYR A 1 294 ? 21.827 2.403 3.227 1.00 18.43 ? 294 TYR A N 1 ATOM 1966 C CA . TYR A 1 294 ? 20.708 3.217 3.687 1.00 18.66 ? 294 TYR A CA 1 ATOM 1967 C C . TYR A 1 294 ? 20.186 2.688 5.023 1.00 18.63 ? 294 TYR A C 1 ATOM 1968 O O . TYR A 1 294 ? 19.815 1.521 5.127 1.00 18.62 ? 294 TYR A O 1 ATOM 1969 C CB . TYR A 1 294 ? 19.559 3.325 2.671 1.00 18.82 ? 294 TYR A CB 1 ATOM 1970 C CG . TYR A 1 294 ? 18.444 4.213 3.202 1.00 18.76 ? 294 TYR A CG 1 ATOM 1971 C CD1 . TYR A 1 294 ? 18.736 5.459 3.755 1.00 19.06 ? 294 TYR A CD1 1 ATOM 1972 C CD2 . TYR A 1 294 ? 17.116 3.797 3.201 1.00 19.12 ? 294 TYR A CD2 1 ATOM 1973 C CE1 . TYR A 1 294 ? 17.745 6.269 4.272 1.00 19.29 ? 294 TYR A CE1 1 ATOM 1974 C CE2 . TYR A 1 294 ? 16.114 4.604 3.721 1.00 19.01 ? 294 TYR A CE2 1 ATOM 1975 C CZ . TYR A 1 294 ? 16.438 5.838 4.255 1.00 19.26 ? 294 TYR A CZ 1 ATOM 1976 O OH . TYR A 1 294 ? 15.474 6.656 4.791 1.00 19.49 ? 294 TYR A OH 1 ATOM 1977 N N . ALA A 1 295 ? 20.156 3.571 6.023 1.00 18.40 ? 295 ALA A N 1 ATOM 1978 C CA . ALA A 1 295 ? 19.945 3.197 7.421 1.00 18.60 ? 295 ALA A CA 1 ATOM 1979 C C . ALA A 1 295 ? 18.948 4.109 8.133 1.00 18.51 ? 295 ALA A C 1 ATOM 1980 O O . ALA A 1 295 ? 19.132 5.324 8.198 1.00 18.14 ? 295 ALA A O 1 ATOM 1981 C CB . ALA A 1 295 ? 21.273 3.230 8.168 1.00 18.53 ? 295 ALA A CB 1 ATOM 1982 N N . ILE A 1 296 ? 17.894 3.513 8.680 1.00 18.88 ? 296 ILE A N 1 ATOM 1983 C CA . ILE A 1 296 ? 17.038 4.225 9.615 1.00 18.44 ? 296 ILE A CA 1 ATOM 1984 C C . ILE A 1 296 ? 17.235 3.575 10.983 1.00 18.48 ? 296 ILE A C 1 ATOM 1985 O O . ILE A 1 296 ? 16.861 2.421 11.197 1.00 17.98 ? 296 ILE A O 1 ATOM 1986 C CB . ILE A 1 296 ? 15.570 4.228 9.171 1.00 18.57 ? 296 ILE A CB 1 ATOM 1987 C CG1 . ILE A 1 296 ? 15.421 5.016 7.857 1.00 18.63 ? 296 ILE A CG1 1 ATOM 1988 C CG2 . ILE A 1 296 ? 14.702 4.855 10.250 1.00 18.78 ? 296 ILE A CG2 1 ATOM 1989 C CD1 . ILE A 1 296 ? 14.055 4.867 7.205 1.00 18.59 ? 296 ILE A CD1 1 ATOM 1990 N N . VAL A 1 297 ? 17.839 4.337 11.895 1.00 18.16 ? 297 VAL A N 1 ATOM 1991 C CA . VAL A 1 297 ? 18.281 3.827 13.183 1.00 18.07 ? 297 VAL A CA 1 ATOM 1992 C C . VAL A 1 297 ? 17.141 3.831 14.223 1.00 17.32 ? 297 VAL A C 1 ATOM 1993 O O . VAL A 1 297 ? 17.142 3.025 15.162 1.00 16.17 ? 297 VAL A O 1 ATOM 1994 C CB . VAL A 1 297 ? 19.524 4.615 13.661 1.00 18.69 ? 297 VAL A CB 1 ATOM 1995 C CG1 . VAL A 1 297 ? 19.966 4.173 15.045 1.00 18.93 ? 297 VAL A CG1 1 ATOM 1996 C CG2 . VAL A 1 297 ? 20.670 4.454 12.662 1.00 19.05 ? 297 VAL A CG2 1 ATOM 1997 N N . GLN A 1 298 ? 16.177 4.732 14.056 1.00 16.63 ? 298 GLN A N 1 ATOM 1998 C CA . GLN A 1 298 ? 14.922 4.648 14.798 1.00 16.74 ? 298 GLN A CA 1 ATOM 1999 C C . GLN A 1 298 ? 13.766 4.890 13.855 1.00 16.70 ? 298 GLN A C 1 ATOM 2000 O O . GLN A 1 298 ? 13.487 6.033 13.495 1.00 15.98 ? 298 GLN A O 1 ATOM 2001 C CB . GLN A 1 298 ? 14.848 5.677 15.933 1.00 17.08 ? 298 GLN A CB 1 ATOM 2002 C CG . GLN A 1 298 ? 15.932 5.598 16.981 1.00 17.20 ? 298 GLN A CG 1 ATOM 2003 C CD . GLN A 1 298 ? 15.827 6.729 17.991 1.00 17.66 ? 298 GLN A CD 1 ATOM 2004 O OE1 . GLN A 1 298 ? 14.744 7.200 18.319 1.00 18.80 ? 298 GLN A OE1 1 ATOM 2005 N NE2 . GLN A 1 298 ? 16.957 7.180 18.468 1.00 17.89 ? 298 GLN A NE2 1 ATOM 2006 N N . PHE A 1 299 ? 13.111 3.810 13.433 1.00 17.33 ? 299 PHE A N 1 ATOM 2007 C CA . PHE A 1 299 ? 11.865 3.936 12.702 1.00 17.47 ? 299 PHE A CA 1 ATOM 2008 C C . PHE A 1 299 ? 10.727 3.594 13.627 1.00 16.95 ? 299 PHE A C 1 ATOM 2009 O O . PHE A 1 299 ? 10.834 2.683 14.446 1.00 16.70 ? 299 PHE A O 1 ATOM 2010 C CB . PHE A 1 299 ? 11.788 3.029 11.476 1.00 18.75 ? 299 PHE A CB 1 ATOM 2011 C CG . PHE A 1 299 ? 10.686 3.428 10.543 1.00 19.92 ? 299 PHE A CG 1 ATOM 2012 C CD1 . PHE A 1 299 ? 10.895 4.411 9.590 1.00 20.71 ? 299 PHE A CD1 1 ATOM 2013 C CD2 . PHE A 1 299 ? 9.420 2.901 10.679 1.00 20.25 ? 299 PHE A CD2 1 ATOM 2014 C CE1 . PHE A 1 299 ? 9.880 4.814 8.745 1.00 20.79 ? 299 PHE A CE1 1 ATOM 2015 C CE2 . PHE A 1 299 ? 8.399 3.299 9.838 1.00 20.63 ? 299 PHE A CE2 1 ATOM 2016 C CZ . PHE A 1 299 ? 8.628 4.255 8.870 1.00 20.71 ? 299 PHE A CZ 1 ATOM 2017 N N . GLN A 1 300 ? 9.627 4.319 13.466 1.00 16.80 ? 300 GLN A N 1 ATOM 2018 C CA . GLN A 1 300 ? 8.461 4.179 14.323 1.00 16.30 ? 300 GLN A CA 1 ATOM 2019 C C . GLN A 1 300 ? 7.963 2.737 14.457 1.00 16.36 ? 300 GLN A C 1 ATOM 2020 O O . GLN A 1 300 ? 7.640 2.084 13.464 1.00 16.48 ? 300 GLN A O 1 ATOM 2021 C CB . GLN A 1 300 ? 7.344 5.051 13.784 1.00 16.01 ? 300 GLN A CB 1 ATOM 2022 C CG . GLN A 1 300 ? 6.076 5.025 14.630 1.00 15.84 ? 300 GLN A CG 1 ATOM 2023 C CD . GLN A 1 300 ? 5.310 6.327 14.545 1.00 15.45 ? 300 GLN A CD 1 ATOM 2024 O OE1 . GLN A 1 300 ? 5.351 7.014 13.529 1.00 14.79 ? 300 GLN A OE1 1 ATOM 2025 N NE2 . GLN A 1 300 ? 4.635 6.685 15.626 1.00 15.24 ? 300 GLN A NE2 1 ATOM 2026 N N . GLY A 1 301 ? 7.917 2.262 15.699 1.00 16.76 ? 301 GLY A N 1 ATOM 2027 C CA . GLY A 1 301 ? 7.320 0.974 16.050 1.00 17.43 ? 301 GLY A CA 1 ATOM 2028 C C . GLY A 1 301 ? 6.239 1.090 17.117 1.00 17.53 ? 301 GLY A C 1 ATOM 2029 O O . GLY A 1 301 ? 5.790 0.078 17.680 1.00 18.43 ? 301 GLY A O 1 ATOM 2030 N N . GLY A 1 302 ? 5.791 2.316 17.364 1.00 17.45 ? 302 GLY A N 1 ATOM 2031 C CA . GLY A 1 302 ? 4.797 2.604 18.396 1.00 17.19 ? 302 GLY A CA 1 ATOM 2032 C C . GLY A 1 302 ? 4.785 4.087 18.736 1.00 17.13 ? 302 GLY A C 1 ATOM 2033 O O . GLY A 1 302 ? 5.129 4.935 17.906 1.00 16.72 ? 302 GLY A O 1 ATOM 2034 N N . SER A 1 303 ? 4.397 4.405 19.963 1.00 17.36 ? 303 SER A N 1 ATOM 2035 C CA . SER A 1 303 ? 4.373 5.787 20.397 1.00 17.87 ? 303 SER A CA 1 ATOM 2036 C C . SER A 1 303 ? 4.432 5.869 21.900 1.00 17.98 ? 303 SER A C 1 ATOM 2037 O O . SER A 1 303 ? 4.030 4.939 22.580 1.00 17.56 ? 303 SER A O 1 ATOM 2038 C CB . SER A 1 303 ? 3.098 6.469 19.913 1.00 18.26 ? 303 SER A CB 1 ATOM 2039 O OG . SER A 1 303 ? 3.066 7.818 20.357 1.00 19.26 ? 303 SER A OG 1 ATOM 2040 N N . TYR A 1 304 ? 4.955 6.981 22.406 1.00 18.35 ? 304 TYR A N 1 ATOM 2041 C CA . TYR A 1 304 ? 4.860 7.298 23.825 1.00 18.70 ? 304 TYR A CA 1 ATOM 2042 C C . TYR A 1 304 ? 3.458 7.824 24.138 1.00 17.93 ? 304 TYR A C 1 ATOM 2043 O O . TYR A 1 304 ? 2.701 8.131 23.225 1.00 17.19 ? 304 TYR A O 1 ATOM 2044 C CB . TYR A 1 304 ? 5.930 8.316 24.240 1.00 19.79 ? 304 TYR A CB 1 ATOM 2045 C CG . TYR A 1 304 ? 5.803 9.679 23.601 1.00 21.53 ? 304 TYR A CG 1 ATOM 2046 C CD1 . TYR A 1 304 ? 4.855 10.601 24.047 1.00 22.45 ? 304 TYR A CD1 1 ATOM 2047 C CD2 . TYR A 1 304 ? 6.645 10.056 22.563 1.00 23.20 ? 304 TYR A CD2 1 ATOM 2048 C CE1 . TYR A 1 304 ? 4.744 11.853 23.466 1.00 24.01 ? 304 TYR A CE1 1 ATOM 2049 C CE2 . TYR A 1 304 ? 6.549 11.311 21.978 1.00 24.94 ? 304 TYR A CE2 1 ATOM 2050 C CZ . TYR A 1 304 ? 5.597 12.199 22.432 1.00 25.55 ? 304 TYR A CZ 1 ATOM 2051 O OH . TYR A 1 304 ? 5.501 13.438 21.852 1.00 29.19 ? 304 TYR A OH 1 ATOM 2052 N N . ASP A 1 305 ? 3.122 7.916 25.423 1.00 17.57 ? 305 ASP A N 1 ATOM 2053 C CA . ASP A 1 305 ? 1.797 8.374 25.865 1.00 17.76 ? 305 ASP A CA 1 ATOM 2054 C C . ASP A 1 305 ? 1.942 9.177 27.152 1.00 17.33 ? 305 ASP A C 1 ATOM 2055 O O . ASP A 1 305 ? 2.509 8.693 28.114 1.00 18.21 ? 305 ASP A O 1 ATOM 2056 C CB . ASP A 1 305 ? 0.888 7.169 26.106 1.00 17.99 ? 305 ASP A CB 1 ATOM 2057 C CG . ASP A 1 305 ? -0.561 7.547 26.269 1.00 18.56 ? 305 ASP A CG 1 ATOM 2058 O OD1 . ASP A 1 305 ? -1.055 8.354 25.470 1.00 19.04 ? 305 ASP A OD1 1 ATOM 2059 O OD2 . ASP A 1 305 ? -1.230 7.017 27.187 1.00 19.53 -1 305 ASP A OD2 1 ATOM 2060 N N . PRO A 1 306 ? 1.441 10.411 27.179 1.00 17.00 ? 306 PRO A N 1 ATOM 2061 C CA . PRO A 1 306 ? 1.631 11.217 28.388 1.00 16.72 ? 306 PRO A CA 1 ATOM 2062 C C . PRO A 1 306 ? 0.602 10.955 29.492 1.00 16.35 ? 306 PRO A C 1 ATOM 2063 O O . PRO A 1 306 ? -0.379 10.242 29.271 1.00 16.46 ? 306 PRO A O 1 ATOM 2064 C CB . PRO A 1 306 ? 1.481 12.639 27.858 1.00 16.68 ? 306 PRO A CB 1 ATOM 2065 C CG . PRO A 1 306 ? 0.466 12.490 26.778 1.00 16.86 ? 306 PRO A CG 1 ATOM 2066 C CD . PRO A 1 306 ? 0.750 11.166 26.121 1.00 16.78 ? 306 PRO A CD 1 ATOM 2067 N N . TRP A 1 307 ? 0.850 11.505 30.679 1.00 16.10 ? 307 TRP A N 1 ATOM 2068 C CA . TRP A 1 307 ? -0.165 11.571 31.734 1.00 16.16 ? 307 TRP A CA 1 ATOM 2069 C C . TRP A 1 307 ? -1.463 12.109 31.144 1.00 16.50 ? 307 TRP A C 1 ATOM 2070 O O . TRP A 1 307 ? -1.438 13.043 30.343 1.00 16.50 ? 307 TRP A O 1 ATOM 2071 C CB . TRP A 1 307 ? 0.265 12.513 32.863 1.00 15.61 ? 307 TRP A CB 1 ATOM 2072 C CG . TRP A 1 307 ? 1.401 12.015 33.687 1.00 15.40 ? 307 TRP A CG 1 ATOM 2073 C CD1 . TRP A 1 307 ? 2.703 12.434 33.631 1.00 15.26 ? 307 TRP A CD1 1 ATOM 2074 C CD2 . TRP A 1 307 ? 1.345 11.021 34.708 1.00 14.79 ? 307 TRP A CD2 1 ATOM 2075 N NE1 . TRP A 1 307 ? 3.459 11.754 34.550 1.00 15.19 ? 307 TRP A NE1 1 ATOM 2076 C CE2 . TRP A 1 307 ? 2.655 10.865 35.212 1.00 14.97 ? 307 TRP A CE2 1 ATOM 2077 C CE3 . TRP A 1 307 ? 0.328 10.226 35.226 1.00 14.56 ? 307 TRP A CE3 1 ATOM 2078 C CZ2 . TRP A 1 307 ? 2.959 9.967 36.227 1.00 14.71 ? 307 TRP A CZ2 1 ATOM 2079 C CZ3 . TRP A 1 307 ? 0.636 9.318 36.225 1.00 14.43 ? 307 TRP A CZ3 1 ATOM 2080 C CH2 . TRP A 1 307 ? 1.929 9.202 36.721 1.00 14.53 ? 307 TRP A CH2 1 ATOM 2081 N N . GLY A 1 308 ? -2.588 11.521 31.536 1.00 17.24 ? 308 GLY A N 1 ATOM 2082 C CA . GLY A 1 308 ? -3.904 11.936 31.020 1.00 17.64 ? 308 GLY A CA 1 ATOM 2083 C C . GLY A 1 308 ? -4.223 11.530 29.586 1.00 18.05 ? 308 GLY A C 1 ATOM 2084 O O . GLY A 1 308 ? -5.320 11.789 29.103 1.00 18.48 ? 308 GLY A O 1 ATOM 2085 N N . GLY A 1 309 ? -3.294 10.857 28.915 1.00 17.97 ? 309 GLY A N 1 ATOM 2086 C CA . GLY A 1 309 ? -3.456 10.535 27.511 1.00 18.17 ? 309 GLY A CA 1 ATOM 2087 C C . GLY A 1 309 ? -4.407 9.379 27.260 1.00 18.71 ? 309 GLY A C 1 ATOM 2088 O O . GLY A 1 309 ? -5.015 8.835 28.189 1.00 18.63 ? 309 GLY A O 1 ATOM 2089 N N . PRO A 1 310 ? -4.545 8.995 25.988 1.00 19.23 ? 310 PRO A N 1 ATOM 2090 C CA . PRO A 1 310 ? -5.550 8.006 25.600 1.00 19.45 ? 310 PRO A CA 1 ATOM 2091 C C . PRO A 1 310 ? -5.221 6.559 25.967 1.00 19.82 ? 310 PRO A C 1 ATOM 2092 O O . PRO A 1 310 ? -6.134 5.734 25.991 1.00 20.08 ? 310 PRO A O 1 ATOM 2093 C CB . PRO A 1 310 ? -5.620 8.163 24.081 1.00 19.92 ? 310 PRO A CB 1 ATOM 2094 C CG . PRO A 1 310 ? -4.276 8.697 23.695 1.00 20.10 ? 310 PRO A CG 1 ATOM 2095 C CD . PRO A 1 310 ? -3.884 9.607 24.823 1.00 19.61 ? 310 PRO A CD 1 ATOM 2096 N N . GLY A 1 311 ? -3.946 6.255 26.236 1.00 19.14 ? 311 GLY A N 1 ATOM 2097 C CA . GLY A 1 311 ? -3.523 4.917 26.664 1.00 18.57 ? 311 GLY A CA 1 ATOM 2098 C C . GLY A 1 311 ? -2.738 4.201 25.582 1.00 18.40 ? 311 GLY A C 1 ATOM 2099 O O . GLY A 1 311 ? -2.824 4.532 24.401 1.00 17.77 ? 311 GLY A O 1 ATOM 2100 N N . PHE A 1 312 ? -1.956 3.212 25.983 1.00 18.42 ? 312 PHE A N 1 ATOM 2101 C CA . PHE A 1 312 ? -1.083 2.552 25.033 1.00 17.99 ? 312 PHE A CA 1 ATOM 2102 C C . PHE A 1 312 ? -1.832 1.585 24.129 1.00 18.33 ? 312 PHE A C 1 ATOM 2103 O O . PHE A 1 312 ? -1.354 1.284 23.040 1.00 19.38 ? 312 PHE A O 1 ATOM 2104 C CB . PHE A 1 312 ? 0.088 1.859 25.741 1.00 17.29 ? 312 PHE A CB 1 ATOM 2105 C CG . PHE A 1 312 ? 1.188 2.794 26.145 1.00 16.25 ? 312 PHE A CG 1 ATOM 2106 C CD1 . PHE A 1 312 ? 1.885 3.515 25.191 1.00 15.98 ? 312 PHE A CD1 1 ATOM 2107 C CD2 . PHE A 1 312 ? 1.542 2.942 27.482 1.00 15.92 ? 312 PHE A CD2 1 ATOM 2108 C CE1 . PHE A 1 312 ? 2.907 4.374 25.555 1.00 15.53 ? 312 PHE A CE1 1 ATOM 2109 C CE2 . PHE A 1 312 ? 2.560 3.793 27.849 1.00 15.49 ? 312 PHE A CE2 1 ATOM 2110 C CZ . PHE A 1 312 ? 3.241 4.508 26.883 1.00 15.71 ? 312 PHE A CZ 1 ATOM 2111 N N . ALA A 1 313 ? -3.001 1.105 24.542 1.00 18.97 ? 313 ALA A N 1 ATOM 2112 C CA . ALA A 1 313 ? -3.796 0.250 23.645 1.00 19.28 ? 313 ALA A CA 1 ATOM 2113 C C . ALA A 1 313 ? -4.139 1.041 22.387 1.00 20.18 ? 313 ALA A C 1 ATOM 2114 O O . ALA A 1 313 ? -4.073 0.506 21.287 1.00 20.22 ? 313 ALA A O 1 ATOM 2115 C CB . ALA A 1 313 ? -5.053 -0.259 24.322 1.00 19.09 ? 313 ALA A CB 1 ATOM 2116 N N . ALA A 1 314 ? -4.476 2.324 22.553 1.00 20.83 ? 314 ALA A N 1 ATOM 2117 C CA . ALA A 1 314 ? -4.711 3.218 21.413 1.00 20.69 ? 314 ALA A CA 1 ATOM 2118 C C . ALA A 1 314 ? -3.465 3.386 20.534 1.00 22.00 ? 314 ALA A C 1 ATOM 2119 O O . ALA A 1 314 ? -3.557 3.391 19.304 1.00 21.89 ? 314 ALA A O 1 ATOM 2120 C CB . ALA A 1 314 ? -5.201 4.566 21.891 1.00 20.45 ? 314 ALA A CB 1 ATOM 2121 N N . CYS A 1 315 ? -2.298 3.513 21.159 1.00 23.34 ? 315 CYS A N 1 ATOM 2122 C CA . CYS A 1 315 ? -1.038 3.562 20.410 1.00 24.09 ? 315 CYS A CA 1 ATOM 2123 C C . CYS A 1 315 ? -0.824 2.302 19.573 1.00 23.24 ? 315 CYS A C 1 ATOM 2124 O O . CYS A 1 315 ? -0.435 2.397 18.414 1.00 22.34 ? 315 CYS A O 1 ATOM 2125 C CB . CYS A 1 315 ? 0.145 3.812 21.348 1.00 25.63 ? 315 CYS A CB 1 ATOM 2126 S SG . CYS A 1 315 ? 0.023 5.436 22.116 1.00 28.04 ? 315 CYS A SG 1 ATOM 2127 N N . SER A 1 316 ? -1.110 1.136 20.141 1.00 22.24 ? 316 SER A N 1 ATOM 2128 C CA . SER A 1 316 ? -1.001 -0.123 19.386 1.00 22.55 ? 316 SER A CA 1 ATOM 2129 C C . SER A 1 316 ? -1.959 -0.186 18.193 1.00 22.49 ? 316 SER A C 1 ATOM 2130 O O . SER A 1 316 ? -1.649 -0.807 17.181 1.00 22.86 ? 316 SER A O 1 ATOM 2131 C CB . SER A 1 316 ? -1.249 -1.321 20.296 1.00 22.48 ? 316 SER A CB 1 ATOM 2132 O OG . SER A 1 316 ? -2.626 -1.428 20.623 1.00 22.80 ? 316 SER A OG 1 ATOM 2133 N N . GLU A 1 317 ? -3.118 0.455 18.325 1.00 23.92 ? 317 GLU A N 1 ATOM 2134 C CA . GLU A 1 317 ? -4.110 0.544 17.244 1.00 24.31 ? 317 GLU A CA 1 ATOM 2135 C C . GLU A 1 317 ? -3.657 1.458 16.093 1.00 23.06 ? 317 GLU A C 1 ATOM 2136 O O . GLU A 1 317 ? -3.933 1.175 14.920 1.00 22.24 ? 317 GLU A O 1 ATOM 2137 C CB . GLU A 1 317 ? -5.456 1.052 17.783 1.00 26.78 ? 317 GLU A CB 1 ATOM 2138 C CG . GLU A 1 317 ? -6.181 0.145 18.774 1.00 29.85 ? 317 GLU A CG 1 ATOM 2139 C CD . GLU A 1 317 ? -7.509 0.750 19.237 1.00 34.83 ? 317 GLU A CD 1 ATOM 2140 O OE1 . GLU A 1 317 ? -8.197 1.395 18.402 1.00 36.31 ? 317 GLU A OE1 1 ATOM 2141 O OE2 . GLU A 1 317 ? -7.872 0.582 20.432 1.00 38.21 -1 317 GLU A OE2 1 ATOM 2142 N N . LEU A 1 318 ? -2.998 2.567 16.426 1.00 21.69 ? 318 LEU A N 1 ATOM 2143 C CA . LEU A 1 318 ? -2.470 3.481 15.404 1.00 21.11 ? 318 LEU A CA 1 ATOM 2144 C C . LEU A 1 318 ? -1.293 2.814 14.682 1.00 20.30 ? 318 LEU A C 1 ATOM 2145 O O . LEU A 1 318 ? -1.251 2.785 13.457 1.00 22.09 ? 318 LEU A O 1 ATOM 2146 C CB . LEU A 1 318 ? -2.058 4.826 16.027 1.00 21.01 ? 318 LEU A CB 1 ATOM 2147 C CG . LEU A 1 318 ? -1.467 5.892 15.092 1.00 21.68 ? 318 LEU A CG 1 ATOM 2148 C CD1 . LEU A 1 318 ? -2.334 6.101 13.861 1.00 21.59 ? 318 LEU A CD1 1 ATOM 2149 C CD2 . LEU A 1 318 ? -1.268 7.226 15.802 1.00 21.59 ? 318 LEU A CD2 1 ATOM 2150 N N . LEU A 1 319 ? -0.358 2.242 15.433 1.00 18.96 ? 319 LEU A N 1 ATOM 2151 C CA . LEU A 1 319 ? 0.789 1.577 14.826 1.00 18.53 ? 319 LEU A CA 1 ATOM 2152 C C . LEU A 1 319 ? 0.565 0.062 14.730 1.00 18.75 ? 319 LEU A C 1 ATOM 2153 O O . LEU A 1 319 ? 1.375 -0.743 15.182 1.00 18.69 ? 319 LEU A O 1 ATOM 2154 C CB . LEU A 1 319 ? 2.062 1.908 15.594 1.00 17.84 ? 319 LEU A CB 1 ATOM 2155 C CG . LEU A 1 319 ? 2.499 3.381 15.684 1.00 17.97 ? 319 LEU A CG 1 ATOM 2156 C CD1 . LEU A 1 319 ? 2.308 4.156 14.371 1.00 17.79 ? 319 LEU A CD1 1 ATOM 2157 C CD2 . LEU A 1 319 ? 1.824 4.105 16.836 1.00 17.59 ? 319 LEU A CD2 1 ATOM 2158 N N . ASN A 1 320 ? -0.546 -0.310 14.107 1.00 19.04 ? 320 ASN A N 1 ATOM 2159 C CA . ASN A 1 320 ? -0.983 -1.692 14.052 1.00 18.99 ? 320 ASN A CA 1 ATOM 2160 C C . ASN A 1 320 ? -0.403 -2.440 12.833 1.00 19.24 ? 320 ASN A C 1 ATOM 2161 O O . ASN A 1 320 ? 0.552 -1.967 12.195 1.00 19.92 ? 320 ASN A O 1 ATOM 2162 C CB . ASN A 1 320 ? -2.513 -1.723 14.053 1.00 19.53 ? 320 ASN A CB 1 ATOM 2163 C CG . ASN A 1 320 ? -3.120 -1.138 12.785 1.00 19.62 ? 320 ASN A CG 1 ATOM 2164 O OD1 . ASN A 1 320 ? -2.410 -0.732 11.869 1.00 20.17 ? 320 ASN A OD1 1 ATOM 2165 N ND2 . ASN A 1 320 ? -4.435 -1.080 12.741 1.00 19.36 ? 320 ASN A ND2 1 ATOM 2166 N N . ASN A 1 321 ? -0.951 -3.611 12.519 1.00 18.78 ? 321 ASN A N 1 ATOM 2167 C CA . ASN A 1 321 ? -0.443 -4.395 11.391 1.00 19.16 ? 321 ASN A CA 1 ATOM 2168 C C . ASN A 1 321 ? -0.559 -3.675 10.045 1.00 18.83 ? 321 ASN A C 1 ATOM 2169 O O . ASN A 1 321 ? 0.292 -3.859 9.176 1.00 18.74 ? 321 ASN A O 1 ATOM 2170 C CB . ASN A 1 321 ? -1.145 -5.755 11.292 1.00 19.25 ? 321 ASN A CB 1 ATOM 2171 C CG . ASN A 1 321 ? -2.613 -5.623 10.966 1.00 19.69 ? 321 ASN A CG 1 ATOM 2172 O OD1 . ASN A 1 321 ? -3.360 -4.973 11.700 1.00 19.15 ? 321 ASN A OD1 1 ATOM 2173 N ND2 . ASN A 1 321 ? -3.037 -6.227 9.852 1.00 20.21 ? 321 ASN A ND2 1 ATOM 2174 N N . GLU A 1 322 ? -1.612 -2.877 9.876 1.00 17.83 ? 322 GLU A N 1 ATOM 2175 C CA . GLU A 1 322 ? -1.816 -2.157 8.634 1.00 17.98 ? 322 GLU A CA 1 ATOM 2176 C C . GLU A 1 322 ? -0.724 -1.118 8.409 1.00 17.54 ? 322 GLU A C 1 ATOM 2177 O O . GLU A 1 322 ? -0.201 -0.998 7.309 1.00 18.00 ? 322 GLU A O 1 ATOM 2178 C CB . GLU A 1 322 ? -3.206 -1.529 8.596 1.00 18.66 ? 322 GLU A CB 1 ATOM 2179 C CG . GLU A 1 322 ? -4.317 -2.573 8.569 1.00 19.80 ? 322 GLU A CG 1 ATOM 2180 C CD . GLU A 1 322 ? -5.702 -1.989 8.369 1.00 21.21 ? 322 GLU A CD 1 ATOM 2181 O OE1 . GLU A 1 322 ? -5.860 -0.748 8.511 1.00 23.18 ? 322 GLU A OE1 1 ATOM 2182 O OE2 . GLU A 1 322 ? -6.638 -2.774 8.071 1.00 22.04 -1 322 GLU A OE2 1 ATOM 2183 N N . PHE A 1 323 ? -0.400 -0.372 9.463 1.00 17.36 ? 323 PHE A N 1 ATOM 2184 C CA . PHE A 1 323 ? 0.717 0.562 9.485 1.00 16.37 ? 323 PHE A CA 1 ATOM 2185 C C . PHE A 1 323 ? 2.034 -0.111 9.116 1.00 16.68 ? 323 PHE A C 1 ATOM 2186 O O . PHE A 1 323 ? 2.790 0.423 8.313 1.00 17.07 ? 323 PHE A O 1 ATOM 2187 C CB . PHE A 1 323 ? 0.841 1.210 10.871 1.00 15.97 ? 323 PHE A CB 1 ATOM 2188 C CG . PHE A 1 323 ? 2.193 1.789 11.150 1.00 16.09 ? 323 PHE A CG 1 ATOM 2189 C CD1 . PHE A 1 323 ? 2.576 3.000 10.576 1.00 16.22 ? 323 PHE A CD1 1 ATOM 2190 C CD2 . PHE A 1 323 ? 3.100 1.119 11.961 1.00 16.28 ? 323 PHE A CD2 1 ATOM 2191 C CE1 . PHE A 1 323 ? 3.826 3.532 10.814 1.00 15.82 ? 323 PHE A CE1 1 ATOM 2192 C CE2 . PHE A 1 323 ? 4.348 1.652 12.210 1.00 16.04 ? 323 PHE A CE2 1 ATOM 2193 C CZ . PHE A 1 323 ? 4.709 2.859 11.637 1.00 16.27 ? 323 PHE A CZ 1 ATOM 2194 N N . GLU A 1 324 ? 2.313 -1.266 9.719 1.00 16.69 ? 324 GLU A N 1 ATOM 2195 C CA . GLU A 1 324 ? 3.557 -1.992 9.464 1.00 16.65 ? 324 GLU A CA 1 ATOM 2196 C C . GLU A 1 324 ? 3.721 -2.375 7.984 1.00 17.38 ? 324 GLU A C 1 ATOM 2197 O O . GLU A 1 324 ? 4.736 -2.069 7.363 1.00 17.30 ? 324 GLU A O 1 ATOM 2198 C CB . GLU A 1 324 ? 3.626 -3.260 10.314 1.00 16.30 ? 324 GLU A CB 1 ATOM 2199 C CG . GLU A 1 324 ? 3.810 -2.990 11.800 1.00 16.56 ? 324 GLU A CG 1 ATOM 2200 C CD . GLU A 1 324 ? 3.939 -4.263 12.616 1.00 16.76 ? 324 GLU A CD 1 ATOM 2201 O OE1 . GLU A 1 324 ? 4.697 -4.259 13.607 1.00 16.30 ? 324 GLU A OE1 1 ATOM 2202 O OE2 . GLU A 1 324 ? 3.287 -5.272 12.249 1.00 17.16 -1 324 GLU A OE2 1 ATOM 2203 N N . ARG A 1 325 ? 2.727 -3.044 7.425 1.00 17.41 ? 325 ARG A N 1 ATOM 2204 C CA . ARG A 1 325 ? 2.852 -3.549 6.058 1.00 18.05 ? 325 ARG A CA 1 ATOM 2205 C C . ARG A 1 325 ? 2.891 -2.419 5.003 1.00 18.52 ? 325 ARG A C 1 ATOM 2206 O O . ARG A 1 325 ? 3.562 -2.558 3.973 1.00 19.21 ? 325 ARG A O 1 ATOM 2207 C CB . ARG A 1 325 ? 1.772 -4.579 5.754 1.00 17.69 ? 325 ARG A CB 1 ATOM 2208 C CG . ARG A 1 325 ? 0.354 -4.059 5.824 1.00 18.39 ? 325 ARG A CG 1 ATOM 2209 C CD . ARG A 1 325 ? -0.647 -5.206 5.926 1.00 18.82 ? 325 ARG A CD 1 ATOM 2210 N NE . ARG A 1 325 ? -1.994 -4.744 5.605 1.00 19.35 ? 325 ARG A NE 1 ATOM 2211 C CZ . ARG A 1 325 ? -3.117 -5.410 5.872 1.00 19.80 ? 325 ARG A CZ 1 ATOM 2212 N NH1 . ARG A 1 325 ? -3.096 -6.592 6.493 1.00 19.86 ? 325 ARG A NH1 1 ATOM 2213 N NH2 . ARG A 1 325 ? -4.274 -4.877 5.526 1.00 19.48 ? 325 ARG A NH2 1 ATOM 2214 N N . VAL A 1 326 ? 2.211 -1.308 5.270 1.00 17.57 ? 326 VAL A N 1 ATOM 2215 C CA . VAL A 1 326 ? 2.297 -0.140 4.387 1.00 17.70 ? 326 VAL A CA 1 ATOM 2216 C C . VAL A 1 326 ? 3.605 0.637 4.544 1.00 17.27 ? 326 VAL A C 1 ATOM 2217 O O . VAL A 1 326 ? 4.295 0.875 3.550 1.00 17.43 ? 326 VAL A O 1 ATOM 2218 C CB . VAL A 1 326 ? 1.106 0.821 4.573 1.00 17.41 ? 326 VAL A CB 1 ATOM 2219 C CG1 . VAL A 1 326 ? 1.284 2.062 3.712 1.00 17.64 ? 326 VAL A CG1 1 ATOM 2220 C CG2 . VAL A 1 326 ? -0.189 0.110 4.192 1.00 17.51 ? 326 VAL A CG2 1 ATOM 2221 N N . PHE A 1 327 ? 3.946 1.032 5.770 1.00 16.72 ? 327 PHE A N 1 ATOM 2222 C CA . PHE A 1 327 ? 5.131 1.875 6.007 1.00 16.69 ? 327 PHE A CA 1 ATOM 2223 C C . PHE A 1 327 ? 6.464 1.119 6.001 1.00 16.55 ? 327 PHE A C 1 ATOM 2224 O O . PHE A 1 327 ? 7.483 1.694 5.648 1.00 16.24 ? 327 PHE A O 1 ATOM 2225 C CB . PHE A 1 327 ? 5.012 2.645 7.333 1.00 16.72 ? 327 PHE A CB 1 ATOM 2226 C CG . PHE A 1 327 ? 4.095 3.846 7.279 1.00 17.13 ? 327 PHE A CG 1 ATOM 2227 C CD1 . PHE A 1 327 ? 2.721 3.692 7.267 1.00 17.26 ? 327 PHE A CD1 1 ATOM 2228 C CD2 . PHE A 1 327 ? 4.613 5.130 7.282 1.00 17.09 ? 327 PHE A CD2 1 ATOM 2229 C CE1 . PHE A 1 327 ? 1.884 4.794 7.237 1.00 17.38 ? 327 PHE A CE1 1 ATOM 2230 C CE2 . PHE A 1 327 ? 3.784 6.230 7.237 1.00 17.35 ? 327 PHE A CE2 1 ATOM 2231 C CZ . PHE A 1 327 ? 2.415 6.064 7.229 1.00 17.30 ? 327 PHE A CZ 1 ATOM 2232 N N . TYR A 1 328 ? 6.492 -0.142 6.431 1.00 16.71 ? 328 TYR A N 1 ATOM 2233 C CA . TYR A 1 328 ? 7.769 -0.857 6.504 1.00 16.79 ? 328 TYR A CA 1 ATOM 2234 C C . TYR A 1 328 ? 8.159 -1.354 5.129 1.00 17.66 ? 328 TYR A C 1 ATOM 2235 O O . TYR A 1 328 ? 9.334 -1.339 4.772 1.00 17.92 ? 328 TYR A O 1 ATOM 2236 C CB . TYR A 1 328 ? 7.753 -2.022 7.507 1.00 16.87 ? 328 TYR A CB 1 ATOM 2237 C CG . TYR A 1 328 ? 7.569 -1.638 8.960 1.00 16.80 ? 328 TYR A CG 1 ATOM 2238 C CD1 . TYR A 1 328 ? 7.608 -0.301 9.377 1.00 16.67 ? 328 TYR A CD1 1 ATOM 2239 C CD2 . TYR A 1 328 ? 7.401 -2.619 9.941 1.00 16.74 ? 328 TYR A CD2 1 ATOM 2240 C CE1 . TYR A 1 328 ? 7.460 0.034 10.706 1.00 16.24 ? 328 TYR A CE1 1 ATOM 2241 C CE2 . TYR A 1 328 ? 7.249 -2.278 11.277 1.00 16.26 ? 328 TYR A CE2 1 ATOM 2242 C CZ . TYR A 1 328 ? 7.282 -0.949 11.649 1.00 16.40 ? 328 TYR A CZ 1 ATOM 2243 O OH . TYR A 1 328 ? 7.137 -0.568 12.967 1.00 16.29 ? 328 TYR A OH 1 ATOM 2244 N N . LYS A 1 329 ? 7.183 -1.787 4.339 1.00 18.34 ? 329 LYS A N 1 ATOM 2245 C CA . LYS A 1 329 ? 7.494 -2.135 2.960 1.00 18.79 ? 329 LYS A CA 1 ATOM 2246 C C . LYS A 1 329 ? 7.856 -0.891 2.154 1.00 18.87 ? 329 LYS A C 1 ATOM 2247 O O . LYS A 1 329 ? 8.621 -0.981 1.202 1.00 19.22 ? 329 LYS A O 1 ATOM 2248 C CB . LYS A 1 329 ? 6.359 -2.915 2.319 1.00 19.59 ? 329 LYS A CB 1 ATOM 2249 C CG . LYS A 1 329 ? 6.135 -4.258 2.999 1.00 19.91 ? 329 LYS A CG 1 ATOM 2250 C CD . LYS A 1 329 ? 4.928 -5.003 2.450 1.00 20.04 ? 329 LYS A CD 1 ATOM 2251 C CE . LYS A 1 329 ? 4.498 -6.085 3.428 1.00 19.65 ? 329 LYS A CE 1 ATOM 2252 N NZ . LYS A 1 329 ? 3.708 -7.154 2.786 1.00 19.67 ? 329 LYS A NZ 1 ATOM 2253 N N . ASN A 1 330 ? 7.336 0.271 2.554 1.00 18.75 ? 330 ASN A N 1 ATOM 2254 C CA . ASN A 1 330 ? 7.727 1.536 1.929 1.00 18.47 ? 330 ASN A CA 1 ATOM 2255 C C . ASN A 1 330 ? 9.201 1.841 2.171 1.00 19.84 ? 330 ASN A C 1 ATOM 2256 O O . ASN A 1 330 ? 9.845 2.458 1.331 1.00 20.53 ? 330 ASN A O 1 ATOM 2257 C CB . ASN A 1 330 ? 6.834 2.679 2.424 1.00 17.86 ? 330 ASN A CB 1 ATOM 2258 C CG . ASN A 1 330 ? 7.156 4.014 1.777 1.00 17.02 ? 330 ASN A CG 1 ATOM 2259 O OD1 . ASN A 1 330 ? 7.066 4.168 0.565 1.00 16.71 ? 330 ASN A OD1 1 ATOM 2260 N ND2 . ASN A 1 330 ? 7.519 4.993 2.593 1.00 16.84 ? 330 ASN A ND2 1 ATOM 2261 N N . ASP A 1 331 ? 9.749 1.396 3.301 1.00 21.47 ? 331 ASP A N 1 ATOM 2262 C CA . ASP A 1 331 ? 11.173 1.600 3.588 1.00 22.36 ? 331 ASP A CA 1 ATOM 2263 C C . ASP A 1 331 ? 12.024 0.650 2.753 1.00 21.36 ? 331 ASP A C 1 ATOM 2264 O O . ASP A 1 331 ? 13.150 0.979 2.366 1.00 20.16 ? 331 ASP A O 1 ATOM 2265 C CB . ASP A 1 331 ? 11.477 1.424 5.091 1.00 24.59 ? 331 ASP A CB 1 ATOM 2266 C CG . ASP A 1 331 ? 10.834 2.515 5.971 1.00 26.66 ? 331 ASP A CG 1 ATOM 2267 O OD1 . ASP A 1 331 ? 10.721 3.687 5.515 1.00 26.81 ? 331 ASP A OD1 1 ATOM 2268 O OD2 . ASP A 1 331 ? 10.444 2.191 7.127 1.00 28.34 -1 331 ASP A OD2 1 ATOM 2269 N N . PHE A 1 332 ? 11.476 -0.534 2.501 1.00 21.17 ? 332 PHE A N 1 ATOM 2270 C CA . PHE A 1 332 ? 12.076 -1.509 1.594 1.00 21.03 ? 332 PHE A CA 1 ATOM 2271 C C . PHE A 1 332 ? 12.081 -0.995 0.148 1.00 19.90 ? 332 PHE A C 1 ATOM 2272 O O . PHE A 1 332 ? 12.951 -1.365 -0.652 1.00 19.66 ? 332 PHE A O 1 ATOM 2273 C CB . PHE A 1 332 ? 11.352 -2.863 1.713 1.00 21.50 ? 332 PHE A CB 1 ATOM 2274 C CG . PHE A 1 332 ? 11.906 -3.747 2.811 1.00 22.35 ? 332 PHE A CG 1 ATOM 2275 C CD1 . PHE A 1 332 ? 11.708 -3.430 4.140 1.00 22.48 ? 332 PHE A CD1 1 ATOM 2276 C CD2 . PHE A 1 332 ? 12.639 -4.886 2.509 1.00 22.70 ? 332 PHE A CD2 1 ATOM 2277 C CE1 . PHE A 1 332 ? 12.229 -4.227 5.147 1.00 23.05 ? 332 PHE A CE1 1 ATOM 2278 C CE2 . PHE A 1 332 ? 13.154 -5.690 3.514 1.00 22.85 ? 332 PHE A CE2 1 ATOM 2279 C CZ . PHE A 1 332 ? 12.952 -5.362 4.835 1.00 22.70 ? 332 PHE A CZ 1 ATOM 2280 N N . SER A 1 333 ? 11.118 -0.135 -0.172 1.00 18.28 ? 333 SER A N 1 ATOM 2281 C CA . SER A 1 333 ? 11.084 0.550 -1.462 1.00 17.80 ? 333 SER A CA 1 ATOM 2282 C C . SER A 1 333 ? 12.314 1.437 -1.682 1.00 17.85 ? 333 SER A C 1 ATOM 2283 O O . SER A 1 333 ? 12.681 1.657 -2.820 1.00 17.77 ? 333 SER A O 1 ATOM 2284 C CB . SER A 1 333 ? 9.794 1.376 -1.627 1.00 17.36 ? 333 SER A CB 1 ATOM 2285 O OG . SER A 1 333 ? 9.947 2.693 -1.135 1.00 16.67 ? 333 SER A OG 1 ATOM 2286 N N . PHE A 1 334 ? 12.948 1.917 -0.603 1.00 17.70 ? 334 PHE A N 1 ATOM 2287 C CA . PHE A 1 334 ? 14.174 2.732 -0.689 1.00 18.01 ? 334 PHE A CA 1 ATOM 2288 C C . PHE A 1 334 ? 15.468 1.922 -0.548 1.00 18.49 ? 334 PHE A C 1 ATOM 2289 O O . PHE A 1 334 ? 16.544 2.506 -0.379 1.00 18.15 ? 334 PHE A O 1 ATOM 2290 C CB . PHE A 1 334 ? 14.209 3.812 0.405 1.00 18.37 ? 334 PHE A CB 1 ATOM 2291 C CG . PHE A 1 334 ? 12.924 4.589 0.572 1.00 18.52 ? 334 PHE A CG 1 ATOM 2292 C CD1 . PHE A 1 334 ? 12.400 5.345 -0.475 1.00 17.99 ? 334 PHE A CD1 1 ATOM 2293 C CD2 . PHE A 1 334 ? 12.265 4.593 1.791 1.00 18.30 ? 334 PHE A CD2 1 ATOM 2294 C CE1 . PHE A 1 334 ? 11.231 6.065 -0.315 1.00 17.95 ? 334 PHE A CE1 1 ATOM 2295 C CE2 . PHE A 1 334 ? 11.097 5.325 1.962 1.00 18.92 ? 334 PHE A CE2 1 ATOM 2296 C CZ . PHE A 1 334 ? 10.581 6.066 0.905 1.00 18.38 ? 334 PHE A CZ 1 ATOM 2297 N N . GLN A 1 335 ? 15.354 0.596 -0.599 1.00 18.93 ? 335 GLN A N 1 ATOM 2298 C CA . GLN A 1 335 ? 16.455 -0.331 -0.346 1.00 19.49 ? 335 GLN A CA 1 ATOM 2299 C C . GLN A 1 335 ? 17.154 -0.110 1.004 1.00 19.42 ? 335 GLN A C 1 ATOM 2300 O O . GLN A 1 335 ? 18.381 -0.061 1.093 1.00 20.27 ? 335 GLN A O 1 ATOM 2301 C CB . GLN A 1 335 ? 17.462 -0.323 -1.494 1.00 20.17 ? 335 GLN A CB 1 ATOM 2302 C CG . GLN A 1 335 ? 18.381 -1.548 -1.519 1.00 20.38 ? 335 GLN A CG 1 ATOM 2303 C CD . GLN A 1 335 ? 19.145 -1.661 -2.822 1.00 20.92 ? 335 GLN A CD 1 ATOM 2304 O OE1 . GLN A 1 335 ? 19.976 -0.815 -3.140 1.00 22.11 ? 335 GLN A OE1 1 ATOM 2305 N NE2 . GLN A 1 335 ? 18.872 -2.707 -3.582 1.00 21.35 ? 335 GLN A NE2 1 ATOM 2306 N N . ILE A 1 336 ? 16.357 0.021 2.054 1.00 18.64 ? 336 ILE A N 1 ATOM 2307 C CA . ILE A 1 336 ? 16.890 0.120 3.409 1.00 18.13 ? 336 ILE A CA 1 ATOM 2308 C C . ILE A 1 336 ? 17.666 -1.162 3.744 1.00 17.67 ? 336 ILE A C 1 ATOM 2309 O O . ILE A 1 336 ? 17.197 -2.268 3.466 1.00 16.43 ? 336 ILE A O 1 ATOM 2310 C CB . ILE A 1 336 ? 15.771 0.372 4.435 1.00 18.32 ? 336 ILE A CB 1 ATOM 2311 C CG1 . ILE A 1 336 ? 16.372 0.757 5.787 1.00 19.15 ? 336 ILE A CG1 1 ATOM 2312 C CG2 . ILE A 1 336 ? 14.854 -0.844 4.569 1.00 18.36 ? 336 ILE A CG2 1 ATOM 2313 C CD1 . ILE A 1 336 ? 15.373 1.342 6.766 1.00 19.23 ? 336 ILE A CD1 1 ATOM 2314 N N . ALA A 1 337 ? 18.867 -0.984 4.290 1.00 16.98 ? 337 ALA A N 1 ATOM 2315 C CA . ALA A 1 337 ? 19.777 -2.079 4.606 1.00 17.30 ? 337 ALA A CA 1 ATOM 2316 C C . ALA A 1 337 ? 20.002 -2.266 6.110 1.00 17.63 ? 337 ALA A C 1 ATOM 2317 O O . ALA A 1 337 ? 20.473 -3.325 6.535 1.00 16.98 ? 337 ALA A O 1 ATOM 2318 C CB . ALA A 1 337 ? 21.116 -1.844 3.916 1.00 17.33 ? 337 ALA A CB 1 ATOM 2319 N N . ILE A 1 338 ? 19.721 -1.225 6.894 1.00 18.08 ? 338 ILE A N 1 ATOM 2320 C CA . ILE A 1 338 ? 19.819 -1.272 8.355 1.00 19.20 ? 338 ILE A CA 1 ATOM 2321 C C . ILE A 1 338 ? 18.567 -0.598 8.890 1.00 19.69 ? 338 ILE A C 1 ATOM 2322 O O . ILE A 1 338 ? 18.360 0.594 8.688 1.00 20.56 ? 338 ILE A O 1 ATOM 2323 C CB . ILE A 1 338 ? 21.080 -0.539 8.889 1.00 19.44 ? 338 ILE A CB 1 ATOM 2324 C CG1 . ILE A 1 338 ? 22.349 -1.125 8.258 1.00 20.01 ? 338 ILE A CG1 1 ATOM 2325 C CG2 . ILE A 1 338 ? 21.143 -0.607 10.409 1.00 19.60 ? 338 ILE A CG2 1 ATOM 2326 C CD1 . ILE A 1 338 ? 23.645 -0.460 8.701 1.00 20.04 ? 338 ILE A CD1 1 ATOM 2327 N N . MET A 1 339 ? 17.716 -1.367 9.547 1.00 20.50 ? 339 MET A N 1 ATOM 2328 C CA . MET A 1 339 ? 16.418 -0.871 9.959 1.00 21.58 ? 339 MET A CA 1 ATOM 2329 C C . MET A 1 339 ? 16.156 -1.275 11.396 1.00 20.67 ? 339 MET A C 1 ATOM 2330 O O . MET A 1 339 ? 16.196 -2.458 11.719 1.00 20.70 ? 339 MET A O 1 ATOM 2331 C CB . MET A 1 339 ? 15.342 -1.443 9.045 1.00 22.56 ? 339 MET A CB 1 ATOM 2332 C CG . MET A 1 339 ? 13.938 -0.933 9.338 1.00 24.51 ? 339 MET A CG 1 ATOM 2333 S SD . MET A 1 339 ? 12.825 -1.360 7.996 1.00 27.10 ? 339 MET A SD 1 ATOM 2334 C CE . MET A 1 339 ? 11.271 -0.693 8.576 1.00 27.15 ? 339 MET A CE 1 ATOM 2335 N N . ASN A 1 340 ? 15.900 -0.291 12.254 1.00 20.09 ? 340 ASN A N 1 ATOM 2336 C CA . ASN A 1 340 ? 15.632 -0.542 13.681 1.00 19.56 ? 340 ASN A CA 1 ATOM 2337 C C . ASN A 1 340 ? 14.287 0.059 14.133 1.00 19.01 ? 340 ASN A C 1 ATOM 2338 O O . ASN A 1 340 ? 14.053 1.272 13.995 1.00 18.45 ? 340 ASN A O 1 ATOM 2339 C CB . ASN A 1 340 ? 16.787 -0.013 14.525 1.00 19.31 ? 340 ASN A CB 1 ATOM 2340 C CG . ASN A 1 340 ? 16.628 -0.313 16.005 1.00 20.06 ? 340 ASN A CG 1 ATOM 2341 O OD1 . ASN A 1 340 ? 16.559 -1.479 16.422 1.00 20.61 ? 340 ASN A OD1 1 ATOM 2342 N ND2 . ASN A 1 340 ? 16.601 0.738 16.818 1.00 19.94 ? 340 ASN A ND2 1 ATOM 2343 N N . LEU A 1 341 ? 13.420 -0.800 14.671 1.00 18.27 ? 341 LEU A N 1 ATOM 2344 C CA . LEU A 1 341 ? 12.103 -0.386 15.173 1.00 18.53 ? 341 LEU A CA 1 ATOM 2345 C C . LEU A 1 341 ? 12.160 0.055 16.632 1.00 18.01 ? 341 LEU A C 1 ATOM 2346 O O . LEU A 1 341 ? 12.472 -0.738 17.516 1.00 17.68 ? 341 LEU A O 1 ATOM 2347 C CB . LEU A 1 341 ? 11.073 -1.515 15.024 1.00 18.65 ? 341 LEU A CB 1 ATOM 2348 C CG . LEU A 1 341 ? 11.010 -2.157 13.639 1.00 19.58 ? 341 LEU A CG 1 ATOM 2349 C CD1 . LEU A 1 341 ? 9.975 -3.267 13.572 1.00 19.60 ? 341 LEU A CD1 1 ATOM 2350 C CD2 . LEU A 1 341 ? 10.751 -1.094 12.575 1.00 20.17 ? 341 LEU A CD2 1 ATOM 2351 N N . TYR A 1 342 ? 11.857 1.330 16.869 1.00 18.04 ? 342 TYR A N 1 ATOM 2352 C CA . TYR A 1 342 ? 11.779 1.890 18.218 1.00 17.51 ? 342 TYR A CA 1 ATOM 2353 C C . TYR A 1 342 ? 10.301 2.015 18.593 1.00 16.91 ? 342 TYR A C 1 ATOM 2354 O O . TYR A 1 342 ? 9.617 2.867 18.032 1.00 16.52 ? 342 TYR A O 1 ATOM 2355 C CB . TYR A 1 342 ? 12.435 3.283 18.239 1.00 17.87 ? 342 TYR A CB 1 ATOM 2356 C CG . TYR A 1 342 ? 12.539 3.886 19.628 1.00 18.30 ? 342 TYR A CG 1 ATOM 2357 C CD1 . TYR A 1 342 ? 11.398 4.335 20.320 1.00 18.40 ? 342 TYR A CD1 1 ATOM 2358 C CD2 . TYR A 1 342 ? 13.771 4.007 20.257 1.00 17.99 ? 342 TYR A CD2 1 ATOM 2359 C CE1 . TYR A 1 342 ? 11.501 4.877 21.592 1.00 18.39 ? 342 TYR A CE1 1 ATOM 2360 C CE2 . TYR A 1 342 ? 13.876 4.547 21.531 1.00 17.81 ? 342 TYR A CE2 1 ATOM 2361 C CZ . TYR A 1 342 ? 12.747 4.987 22.191 1.00 17.94 ? 342 TYR A CZ 1 ATOM 2362 O OH . TYR A 1 342 ? 12.863 5.507 23.461 1.00 17.13 ? 342 TYR A OH 1 ATOM 2363 N N . MET A 1 343 ? 9.763 1.220 19.515 1.00 16.44 ? 343 MET A N 1 ATOM 2364 C CA . MET A 1 343 ? 10.423 0.167 20.260 1.00 16.49 ? 343 MET A CA 1 ATOM 2365 C C . MET A 1 343 ? 9.916 -1.149 19.713 1.00 16.66 ? 343 MET A C 1 ATOM 2366 O O . MET A 1 343 ? 8.814 -1.200 19.162 1.00 17.68 ? 343 MET A O 1 ATOM 2367 C CB . MET A 1 343 ? 9.995 0.222 21.731 1.00 16.49 ? 343 MET A CB 1 ATOM 2368 C CG . MET A 1 343 ? 10.277 1.521 22.466 1.00 16.38 ? 343 MET A CG 1 ATOM 2369 S SD . MET A 1 343 ? 12.023 1.747 22.809 1.00 16.26 ? 343 MET A SD 1 ATOM 2370 C CE . MET A 1 343 ? 12.410 0.374 23.878 1.00 16.38 ? 343 MET A CE 1 ATOM 2371 N N . ILE A 1 344 ? 10.688 -2.216 19.885 1.00 16.51 ? 344 ILE A N 1 ATOM 2372 C CA . ILE A 1 344 ? 10.167 -3.568 19.661 1.00 16.44 ? 344 ILE A CA 1 ATOM 2373 C C . ILE A 1 344 ? 9.577 -4.135 20.950 1.00 15.76 ? 344 ILE A C 1 ATOM 2374 O O . ILE A 1 344 ? 8.598 -4.866 20.909 1.00 16.06 ? 344 ILE A O 1 ATOM 2375 C CB . ILE A 1 344 ? 11.230 -4.513 19.066 1.00 16.99 ? 344 ILE A CB 1 ATOM 2376 C CG1 . ILE A 1 344 ? 10.567 -5.654 18.298 1.00 17.43 ? 344 ILE A CG1 1 ATOM 2377 C CG2 . ILE A 1 344 ? 12.141 -5.093 20.138 1.00 17.53 ? 344 ILE A CG2 1 ATOM 2378 C CD1 . ILE A 1 344 ? 9.946 -5.222 16.991 1.00 17.44 ? 344 ILE A CD1 1 ATOM 2379 N N . PHE A 1 345 ? 10.187 -3.806 22.084 1.00 15.24 ? 345 PHE A N 1 ATOM 2380 C CA . PHE A 1 345 ? 9.643 -4.116 23.412 1.00 15.11 ? 345 PHE A CA 1 ATOM 2381 C C . PHE A 1 345 ? 9.970 -2.903 24.286 1.00 15.04 ? 345 PHE A C 1 ATOM 2382 O O . PHE A 1 345 ? 11.115 -2.467 24.331 1.00 15.98 ? 345 PHE A O 1 ATOM 2383 C CB . PHE A 1 345 ? 10.237 -5.403 24.011 1.00 14.82 ? 345 PHE A CB 1 ATOM 2384 C CG . PHE A 1 345 ? 9.998 -5.550 25.492 1.00 15.09 ? 345 PHE A CG 1 ATOM 2385 C CD1 . PHE A 1 345 ? 8.782 -5.999 25.975 1.00 15.29 ? 345 PHE A CD1 1 ATOM 2386 C CD2 . PHE A 1 345 ? 10.982 -5.213 26.408 1.00 15.27 ? 345 PHE A CD2 1 ATOM 2387 C CE1 . PHE A 1 345 ? 8.556 -6.123 27.336 1.00 15.15 ? 345 PHE A CE1 1 ATOM 2388 C CE2 . PHE A 1 345 ? 10.759 -5.325 27.770 1.00 15.37 ? 345 PHE A CE2 1 ATOM 2389 C CZ . PHE A 1 345 ? 9.539 -5.794 28.235 1.00 15.38 ? 345 PHE A CZ 1 ATOM 2390 N N . GLY A 1 346 ? 8.962 -2.371 24.966 1.00 14.72 ? 346 GLY A N 1 ATOM 2391 C CA . GLY A 1 346 ? 9.091 -1.137 25.711 1.00 14.97 ? 346 GLY A CA 1 ATOM 2392 C C . GLY A 1 346 ? 9.385 -1.313 27.180 1.00 14.94 ? 346 GLY A C 1 ATOM 2393 O O . GLY A 1 346 ? 10.262 -0.654 27.719 1.00 15.85 ? 346 GLY A O 1 ATOM 2394 N N . GLY A 1 347 ? 8.646 -2.190 27.839 1.00 14.73 ? 347 GLY A N 1 ATOM 2395 C CA . GLY A 1 347 ? 8.829 -2.408 29.265 1.00 14.61 ? 347 GLY A CA 1 ATOM 2396 C C . GLY A 1 347 ? 8.199 -1.354 30.157 1.00 14.46 ? 347 GLY A C 1 ATOM 2397 O O . GLY A 1 347 ? 7.144 -0.808 29.851 1.00 14.34 ? 347 GLY A O 1 ATOM 2398 N N . THR A 1 348 ? 8.869 -1.075 31.267 1.00 14.61 ? 348 THR A N 1 ATOM 2399 C CA . THR A 1 348 ? 8.288 -0.343 32.368 1.00 14.67 ? 348 THR A CA 1 ATOM 2400 C C . THR A 1 348 ? 9.247 0.700 32.901 1.00 14.47 ? 348 THR A C 1 ATOM 2401 O O . THR A 1 348 ? 10.435 0.415 33.090 1.00 14.55 ? 348 THR A O 1 ATOM 2402 C CB . THR A 1 348 ? 7.946 -1.322 33.501 1.00 14.73 ? 348 THR A CB 1 ATOM 2403 O OG1 . THR A 1 348 ? 7.085 -2.324 32.975 1.00 15.12 ? 348 THR A OG1 1 ATOM 2404 C CG2 . THR A 1 348 ? 7.234 -0.622 34.652 1.00 15.13 ? 348 THR A CG2 1 ATOM 2405 N N . ASN A 1 349 ? 8.711 1.895 33.155 1.00 14.24 ? 349 ASN A N 1 ATOM 2406 C CA . ASN A 1 349 ? 9.435 2.989 33.796 1.00 13.83 ? 349 ASN A CA 1 ATOM 2407 C C . ASN A 1 349 ? 9.363 2.813 35.299 1.00 13.80 ? 349 ASN A C 1 ATOM 2408 O O . ASN A 1 349 ? 8.791 3.632 35.997 1.00 13.86 ? 349 ASN A O 1 ATOM 2409 C CB . ASN A 1 349 ? 8.805 4.341 33.415 1.00 14.20 ? 349 ASN A CB 1 ATOM 2410 C CG . ASN A 1 349 ? 8.756 4.565 31.909 1.00 14.25 ? 349 ASN A CG 1 ATOM 2411 O OD1 . ASN A 1 349 ? 7.722 4.912 31.334 1.00 14.74 ? 349 ASN A OD1 1 ATOM 2412 N ND2 . ASN A 1 349 ? 9.871 4.340 31.267 1.00 13.86 ? 349 ASN A ND2 1 ATOM 2413 N N . TRP A 1 350 ? 9.946 1.733 35.804 1.00 13.89 ? 350 TRP A N 1 ATOM 2414 C CA . TRP A 1 350 ? 9.956 1.464 37.236 1.00 13.55 ? 350 TRP A CA 1 ATOM 2415 C C . TRP A 1 350 ? 10.920 2.402 37.978 1.00 13.81 ? 350 TRP A C 1 ATOM 2416 O O . TRP A 1 350 ? 11.832 2.993 37.376 1.00 14.29 ? 350 TRP A O 1 ATOM 2417 C CB . TRP A 1 350 ? 10.328 0.015 37.504 1.00 13.42 ? 350 TRP A CB 1 ATOM 2418 C CG . TRP A 1 350 ? 11.729 -0.290 37.172 1.00 13.49 ? 350 TRP A CG 1 ATOM 2419 C CD1 . TRP A 1 350 ? 12.224 -0.670 35.961 1.00 13.71 ? 350 TRP A CD1 1 ATOM 2420 C CD2 . TRP A 1 350 ? 12.833 -0.243 38.064 1.00 13.69 ? 350 TRP A CD2 1 ATOM 2421 N NE1 . TRP A 1 350 ? 13.587 -0.849 36.044 1.00 14.07 ? 350 TRP A NE1 1 ATOM 2422 C CE2 . TRP A 1 350 ? 13.978 -0.609 37.334 1.00 13.85 ? 350 TRP A CE2 1 ATOM 2423 C CE3 . TRP A 1 350 ? 12.968 0.066 39.421 1.00 14.03 ? 350 TRP A CE3 1 ATOM 2424 C CZ2 . TRP A 1 350 ? 15.238 -0.662 37.909 1.00 13.90 ? 350 TRP A CZ2 1 ATOM 2425 C CZ3 . TRP A 1 350 ? 14.221 0.002 39.991 1.00 14.00 ? 350 TRP A CZ3 1 ATOM 2426 C CH2 . TRP A 1 350 ? 15.342 -0.345 39.233 1.00 13.83 ? 350 TRP A CH2 1 ATOM 2427 N N . GLY A 1 351 ? 10.708 2.526 39.285 1.00 13.19 ? 351 GLY A N 1 ATOM 2428 C CA . GLY A 1 351 ? 11.621 3.243 40.148 1.00 13.44 ? 351 GLY A CA 1 ATOM 2429 C C . GLY A 1 351 ? 11.983 4.633 39.663 1.00 12.81 ? 351 GLY A C 1 ATOM 2430 O O . GLY A 1 351 ? 13.141 5.006 39.684 1.00 12.49 ? 351 GLY A O 1 ATOM 2431 N N . ASN A 1 352 ? 10.973 5.363 39.211 1.00 12.68 ? 352 ASN A N 1 ATOM 2432 C CA . ASN A 1 352 ? 11.077 6.747 38.785 1.00 12.91 ? 352 ASN A CA 1 ATOM 2433 C C . ASN A 1 352 ? 12.085 7.015 37.659 1.00 13.18 ? 352 ASN A C 1 ATOM 2434 O O . ASN A 1 352 ? 12.551 8.147 37.526 1.00 12.79 ? 352 ASN A O 1 ATOM 2435 C CB . ASN A 1 352 ? 11.416 7.635 39.989 1.00 12.95 ? 352 ASN A CB 1 ATOM 2436 C CG . ASN A 1 352 ? 10.489 7.406 41.159 1.00 13.14 ? 352 ASN A CG 1 ATOM 2437 O OD1 . ASN A 1 352 ? 9.285 7.527 41.029 1.00 13.10 ? 352 ASN A OD1 1 ATOM 2438 N ND2 . ASN A 1 352 ? 11.054 7.075 42.318 1.00 13.66 ? 352 ASN A ND2 1 ATOM 2439 N N . LEU A 1 353 ? 12.418 6.011 36.840 1.00 13.46 ? 353 LEU A N 1 ATOM 2440 C CA . LEU A 1 353 ? 13.456 6.218 35.806 1.00 13.72 ? 353 LEU A CA 1 ATOM 2441 C C . LEU A 1 353 ? 12.967 7.095 34.652 1.00 13.92 ? 353 LEU A C 1 ATOM 2442 O O . LEU A 1 353 ? 13.774 7.629 33.876 1.00 13.41 ? 353 LEU A O 1 ATOM 2443 C CB . LEU A 1 353 ? 14.033 4.895 35.295 1.00 13.46 ? 353 LEU A CB 1 ATOM 2444 C CG . LEU A 1 353 ? 13.179 3.986 34.410 1.00 13.47 ? 353 LEU A CG 1 ATOM 2445 C CD1 . LEU A 1 353 ? 13.237 4.401 32.950 1.00 13.41 ? 353 LEU A CD1 1 ATOM 2446 C CD2 . LEU A 1 353 ? 13.637 2.533 34.556 1.00 13.49 ? 353 LEU A CD2 1 ATOM 2447 N N . GLY A 1 354 ? 11.646 7.246 34.554 1.00 14.48 ? 354 GLY A N 1 ATOM 2448 C CA . GLY A 1 354 ? 11.018 7.929 33.418 1.00 14.89 ? 354 GLY A CA 1 ATOM 2449 C C . GLY A 1 354 ? 10.999 9.436 33.504 1.00 14.98 ? 354 GLY A C 1 ATOM 2450 O O . GLY A 1 354 ? 11.153 10.006 34.576 1.00 14.54 ? 354 GLY A O 1 ATOM 2451 N N . TYR A 1 355 ? 10.801 10.074 32.355 1.00 16.17 ? 355 TYR A N 1 ATOM 2452 C CA . TYR A 1 355 ? 10.738 11.533 32.268 1.00 17.42 ? 355 TYR A CA 1 ATOM 2453 C C . TYR A 1 355 ? 9.379 12.059 32.731 1.00 18.09 ? 355 TYR A C 1 ATOM 2454 O O . TYR A 1 355 ? 8.441 11.280 32.894 1.00 17.79 ? 355 TYR A O 1 ATOM 2455 C CB . TYR A 1 355 ? 11.089 11.988 30.840 1.00 18.45 ? 355 TYR A CB 1 ATOM 2456 C CG . TYR A 1 355 ? 9.988 12.033 29.800 1.00 18.97 ? 355 TYR A CG 1 ATOM 2457 C CD1 . TYR A 1 355 ? 9.005 11.042 29.718 1.00 19.79 ? 355 TYR A CD1 1 ATOM 2458 C CD2 . TYR A 1 355 ? 9.974 13.046 28.843 1.00 19.74 ? 355 TYR A CD2 1 ATOM 2459 C CE1 . TYR A 1 355 ? 8.027 11.083 28.731 1.00 19.86 ? 355 TYR A CE1 1 ATOM 2460 C CE2 . TYR A 1 355 ? 9.009 13.090 27.849 1.00 19.68 ? 355 TYR A CE2 1 ATOM 2461 C CZ . TYR A 1 355 ? 8.037 12.113 27.795 1.00 20.08 ? 355 TYR A CZ 1 ATOM 2462 O OH . TYR A 1 355 ? 7.082 12.170 26.804 1.00 20.12 ? 355 TYR A OH 1 ATOM 2463 N N . PRO A 1 356 ? 9.270 13.383 32.955 1.00 18.67 ? 356 PRO A N 1 ATOM 2464 C CA . PRO A 1 356 ? 8.080 13.903 33.638 1.00 18.85 ? 356 PRO A CA 1 ATOM 2465 C C . PRO A 1 356 ? 6.752 13.758 32.892 1.00 19.08 ? 356 PRO A C 1 ATOM 2466 O O . PRO A 1 356 ? 5.703 13.608 33.541 1.00 18.65 ? 356 PRO A O 1 ATOM 2467 C CB . PRO A 1 356 ? 8.418 15.384 33.886 1.00 18.43 ? 356 PRO A CB 1 ATOM 2468 C CG . PRO A 1 356 ? 9.567 15.691 32.999 1.00 18.53 ? 356 PRO A CG 1 ATOM 2469 C CD . PRO A 1 356 ? 10.305 14.417 32.788 1.00 18.34 ? 356 PRO A CD 1 ATOM 2470 N N . ASN A 1 357 ? 6.794 13.788 31.565 1.00 18.95 ? 357 ASN A N 1 ATOM 2471 C CA . ASN A 1 357 ? 5.578 13.752 30.764 1.00 19.27 ? 357 ASN A CA 1 ATOM 2472 C C . ASN A 1 357 ? 4.957 12.365 30.666 1.00 19.16 ? 357 ASN A C 1 ATOM 2473 O O . ASN A 1 357 ? 3.806 12.258 30.259 1.00 20.68 ? 357 ASN A O 1 ATOM 2474 C CB . ASN A 1 357 ? 5.827 14.248 29.337 1.00 20.08 ? 357 ASN A CB 1 ATOM 2475 C CG . ASN A 1 357 ? 6.434 15.638 29.280 1.00 20.72 ? 357 ASN A CG 1 ATOM 2476 O OD1 . ASN A 1 357 ? 6.357 16.413 30.227 1.00 21.78 ? 357 ASN A OD1 1 ATOM 2477 N ND2 . ASN A 1 357 ? 7.045 15.956 28.149 1.00 21.25 ? 357 ASN A ND2 1 ATOM 2478 N N . GLY A 1 358 ? 5.708 11.317 31.010 1.00 17.39 ? 358 GLY A N 1 ATOM 2479 C CA . GLY A 1 358 ? 5.237 9.945 30.897 1.00 16.28 ? 358 GLY A CA 1 ATOM 2480 C C . GLY A 1 358 ? 4.985 9.305 32.250 1.00 15.80 ? 358 GLY A C 1 ATOM 2481 O O . GLY A 1 358 ? 5.403 9.818 33.287 1.00 14.91 ? 358 GLY A O 1 ATOM 2482 N N . TYR A 1 359 ? 4.306 8.165 32.231 1.00 15.55 ? 359 TYR A N 1 ATOM 2483 C CA . TYR A 1 359 ? 3.852 7.521 33.457 1.00 15.70 ? 359 TYR A CA 1 ATOM 2484 C C . TYR A 1 359 ? 4.544 6.162 33.595 1.00 15.09 ? 359 TYR A C 1 ATOM 2485 O O . TYR A 1 359 ? 5.567 5.936 32.960 1.00 15.08 ? 359 TYR A O 1 ATOM 2486 C CB . TYR A 1 359 ? 2.312 7.495 33.516 1.00 16.05 ? 359 TYR A CB 1 ATOM 2487 C CG . TYR A 1 359 ? 1.580 6.938 32.304 1.00 16.35 ? 359 TYR A CG 1 ATOM 2488 C CD1 . TYR A 1 359 ? 1.197 7.770 31.243 1.00 16.52 ? 359 TYR A CD1 1 ATOM 2489 C CD2 . TYR A 1 359 ? 1.240 5.578 32.232 1.00 16.27 ? 359 TYR A CD2 1 ATOM 2490 C CE1 . TYR A 1 359 ? 0.518 7.254 30.143 1.00 16.47 ? 359 TYR A CE1 1 ATOM 2491 C CE2 . TYR A 1 359 ? 0.560 5.057 31.139 1.00 15.93 ? 359 TYR A CE2 1 ATOM 2492 C CZ . TYR A 1 359 ? 0.191 5.894 30.101 1.00 16.13 ? 359 TYR A CZ 1 ATOM 2493 O OH . TYR A 1 359 ? -0.478 5.372 29.018 1.00 14.70 ? 359 TYR A OH 1 ATOM 2494 N N . THR A 1 360 ? 4.052 5.280 34.448 1.00 14.84 ? 360 THR A N 1 ATOM 2495 C CA . THR A 1 360 ? 4.807 4.069 34.772 1.00 14.39 ? 360 THR A CA 1 ATOM 2496 C C . THR A 1 360 ? 4.983 3.137 33.562 1.00 14.21 ? 360 THR A C 1 ATOM 2497 O O . THR A 1 360 ? 6.064 2.612 33.328 1.00 14.30 ? 360 THR A O 1 ATOM 2498 C CB . THR A 1 360 ? 4.165 3.321 35.945 1.00 14.31 ? 360 THR A CB 1 ATOM 2499 O OG1 . THR A 1 360 ? 4.022 4.222 37.044 1.00 14.18 ? 360 THR A OG1 1 ATOM 2500 C CG2 . THR A 1 360 ? 5.013 2.117 36.391 1.00 14.16 ? 360 THR A CG2 1 ATOM 2501 N N . SER A 1 361 ? 3.933 2.943 32.790 1.00 14.03 ? 361 SER A N 1 ATOM 2502 C CA . SER A 1 361 ? 4.011 2.076 31.618 1.00 13.91 ? 361 SER A CA 1 ATOM 2503 C C . SER A 1 361 ? 4.871 2.701 30.508 1.00 13.53 ? 361 SER A C 1 ATOM 2504 O O . SER A 1 361 ? 4.821 3.905 30.278 1.00 13.35 ? 361 SER A O 1 ATOM 2505 C CB . SER A 1 361 ? 2.603 1.790 31.076 1.00 13.75 ? 361 SER A CB 1 ATOM 2506 O OG . SER A 1 361 ? 2.645 0.963 29.914 1.00 13.88 ? 361 SER A OG 1 ATOM 2507 N N . TYR A 1 362 ? 5.650 1.854 29.841 1.00 13.37 ? 362 TYR A N 1 ATOM 2508 C CA . TYR A 1 362 ? 6.286 2.174 28.569 1.00 13.71 ? 362 TYR A CA 1 ATOM 2509 C C . TYR A 1 362 ? 5.949 1.083 27.549 1.00 13.58 ? 362 TYR A C 1 ATOM 2510 O O . TYR A 1 362 ? 6.795 0.652 26.783 1.00 13.91 ? 362 TYR A O 1 ATOM 2511 C CB . TYR A 1 362 ? 7.807 2.305 28.748 1.00 13.78 ? 362 TYR A CB 1 ATOM 2512 C CG . TYR A 1 362 ? 8.489 3.119 27.676 1.00 14.01 ? 362 TYR A CG 1 ATOM 2513 C CD1 . TYR A 1 362 ? 8.117 4.432 27.425 1.00 14.27 ? 362 TYR A CD1 1 ATOM 2514 C CD2 . TYR A 1 362 ? 9.509 2.583 26.908 1.00 14.24 ? 362 TYR A CD2 1 ATOM 2515 C CE1 . TYR A 1 362 ? 8.750 5.189 26.447 1.00 14.05 ? 362 TYR A CE1 1 ATOM 2516 C CE2 . TYR A 1 362 ? 10.148 3.333 25.938 1.00 14.03 ? 362 TYR A CE2 1 ATOM 2517 C CZ . TYR A 1 362 ? 9.771 4.633 25.715 1.00 14.01 ? 362 TYR A CZ 1 ATOM 2518 O OH . TYR A 1 362 ? 10.402 5.362 24.732 1.00 14.11 ? 362 TYR A OH 1 ATOM 2519 N N . ASP A 1 363 ? 4.698 0.650 27.533 1.00 13.85 ? 363 ASP A N 1 ATOM 2520 C CA . ASP A 1 363 ? 4.267 -0.414 26.631 1.00 13.97 ? 363 ASP A CA 1 ATOM 2521 C C . ASP A 1 363 ? 4.560 0.005 25.190 1.00 14.49 ? 363 ASP A C 1 ATOM 2522 O O . ASP A 1 363 ? 5.022 -0.796 24.379 1.00 14.17 ? 363 ASP A O 1 ATOM 2523 C CB . ASP A 1 363 ? 2.774 -0.698 26.821 1.00 13.84 ? 363 ASP A CB 1 ATOM 2524 C CG . ASP A 1 363 ? 2.227 -1.663 25.796 1.00 13.64 ? 363 ASP A CG 1 ATOM 2525 O OD1 . ASP A 1 363 ? 1.817 -1.209 24.715 1.00 13.44 ? 363 ASP A OD1 1 ATOM 2526 O OD2 . ASP A 1 363 ? 2.201 -2.882 26.063 1.00 13.59 -1 363 ASP A OD2 1 ATOM 2527 N N . TYR A 1 364 ? 4.279 1.269 24.889 1.00 14.40 ? 364 TYR A N 1 ATOM 2528 C CA . TYR A 1 364 ? 4.649 1.884 23.609 1.00 14.61 ? 364 TYR A CA 1 ATOM 2529 C C . TYR A 1 364 ? 3.805 1.430 22.409 1.00 14.43 ? 364 TYR A C 1 ATOM 2530 O O . TYR A 1 364 ? 4.066 1.828 21.284 1.00 13.94 ? 364 TYR A O 1 ATOM 2531 C CB . TYR A 1 364 ? 6.152 1.672 23.307 1.00 14.46 ? 364 TYR A CB 1 ATOM 2532 C CG . TYR A 1 364 ? 6.752 2.794 22.508 1.00 14.53 ? 364 TYR A CG 1 ATOM 2533 C CD1 . TYR A 1 364 ? 7.101 3.983 23.112 1.00 14.58 ? 364 TYR A CD1 1 ATOM 2534 C CD2 . TYR A 1 364 ? 6.951 2.680 21.143 1.00 15.00 ? 364 TYR A CD2 1 ATOM 2535 C CE1 . TYR A 1 364 ? 7.624 5.038 22.383 1.00 14.58 ? 364 TYR A CE1 1 ATOM 2536 C CE2 . TYR A 1 364 ? 7.492 3.729 20.407 1.00 14.86 ? 364 TYR A CE2 1 ATOM 2537 C CZ . TYR A 1 364 ? 7.825 4.908 21.035 1.00 14.56 ? 364 TYR A CZ 1 ATOM 2538 O OH . TYR A 1 364 ? 8.350 5.970 20.308 1.00 14.73 ? 364 TYR A OH 1 ATOM 2539 N N . GLY A 1 365 ? 2.787 0.613 22.650 1.00 14.75 ? 365 GLY A N 1 ATOM 2540 C CA . GLY A 1 365 ? 2.065 -0.037 21.571 1.00 15.11 ? 365 GLY A CA 1 ATOM 2541 C C . GLY A 1 365 ? 2.955 -0.913 20.696 1.00 15.70 ? 365 GLY A C 1 ATOM 2542 O O . GLY A 1 365 ? 2.638 -1.155 19.529 1.00 16.59 ? 365 GLY A O 1 ATOM 2543 N N . SER A 1 366 ? 4.055 -1.418 21.246 1.00 15.95 ? 366 SER A N 1 ATOM 2544 C CA . SER A 1 366 ? 5.001 -2.173 20.445 1.00 16.11 ? 366 SER A CA 1 ATOM 2545 C C . SER A 1 366 ? 4.529 -3.605 20.151 1.00 15.64 ? 366 SER A C 1 ATOM 2546 O O . SER A 1 366 ? 3.537 -4.081 20.686 1.00 14.86 ? 366 SER A O 1 ATOM 2547 C CB . SER A 1 366 ? 6.393 -2.139 21.087 1.00 16.64 ? 366 SER A CB 1 ATOM 2548 O OG . SER A 1 366 ? 6.378 -2.642 22.405 1.00 17.29 ? 366 SER A OG 1 ATOM 2549 N N . ALA A 1 367 ? 5.233 -4.268 19.241 1.00 15.95 ? 367 ALA A N 1 ATOM 2550 C CA . ALA A 1 367 ? 4.912 -5.646 18.831 1.00 15.79 ? 367 ALA A CA 1 ATOM 2551 C C . ALA A 1 367 ? 4.950 -6.654 19.994 1.00 15.41 ? 367 ALA A C 1 ATOM 2552 O O . ALA A 1 367 ? 4.173 -7.603 20.021 1.00 14.91 ? 367 ALA A O 1 ATOM 2553 C CB . ALA A 1 367 ? 5.863 -6.085 17.729 1.00 15.87 ? 367 ALA A CB 1 ATOM 2554 N N . VAL A 1 368 ? 5.859 -6.445 20.937 1.00 15.30 ? 368 VAL A N 1 ATOM 2555 C CA . VAL A 1 368 ? 5.859 -7.203 22.195 1.00 15.93 ? 368 VAL A CA 1 ATOM 2556 C C . VAL A 1 368 ? 5.357 -6.250 23.286 1.00 16.08 ? 368 VAL A C 1 ATOM 2557 O O . VAL A 1 368 ? 5.918 -5.173 23.476 1.00 16.77 ? 368 VAL A O 1 ATOM 2558 C CB . VAL A 1 368 ? 7.270 -7.731 22.560 1.00 15.45 ? 368 VAL A CB 1 ATOM 2559 C CG1 . VAL A 1 368 ? 7.218 -8.630 23.790 1.00 15.77 ? 368 VAL A CG1 1 ATOM 2560 C CG2 . VAL A 1 368 ? 7.889 -8.483 21.392 1.00 15.48 ? 368 VAL A CG2 1 ATOM 2561 N N . THR A 1 369 ? 4.315 -6.654 24.001 1.00 16.16 ? 369 THR A N 1 ATOM 2562 C CA . THR A 1 369 ? 3.666 -5.784 24.978 1.00 16.40 ? 369 THR A CA 1 ATOM 2563 C C . THR A 1 369 ? 4.502 -5.646 26.250 1.00 17.16 ? 369 THR A C 1 ATOM 2564 O O . THR A 1 369 ? 5.481 -6.374 26.454 1.00 17.53 ? 369 THR A O 1 ATOM 2565 C CB . THR A 1 369 ? 2.251 -6.267 25.367 1.00 15.92 ? 369 THR A CB 1 ATOM 2566 O OG1 . THR A 1 369 ? 2.342 -7.374 26.258 1.00 15.65 ? 369 THR A OG1 1 ATOM 2567 C CG2 . THR A 1 369 ? 1.443 -6.663 24.152 1.00 15.65 ? 369 THR A CG2 1 ATOM 2568 N N . GLU A 1 370 ? 4.107 -4.701 27.103 1.00 17.61 ? 370 GLU A N 1 ATOM 2569 C CA . GLU A 1 370 ? 4.805 -4.442 28.357 1.00 17.24 ? 370 GLU A CA 1 ATOM 2570 C C . GLU A 1 370 ? 4.913 -5.704 29.193 1.00 17.70 ? 370 GLU A C 1 ATOM 2571 O O . GLU A 1 370 ? 5.944 -5.925 29.829 1.00 15.87 ? 370 GLU A O 1 ATOM 2572 C CB . GLU A 1 370 ? 4.092 -3.374 29.167 1.00 17.68 ? 370 GLU A CB 1 ATOM 2573 C CG . GLU A 1 370 ? 4.757 -3.095 30.503 1.00 18.35 ? 370 GLU A CG 1 ATOM 2574 C CD . GLU A 1 370 ? 4.235 -1.845 31.178 1.00 18.62 ? 370 GLU A CD 1 ATOM 2575 O OE1 . GLU A 1 370 ? 3.174 -1.348 30.762 1.00 19.16 ? 370 GLU A OE1 1 ATOM 2576 O OE2 . GLU A 1 370 ? 4.887 -1.371 32.140 1.00 19.26 -1 370 GLU A OE2 1 ATOM 2577 N N . SER A 1 371 ? 3.848 -6.517 29.185 1.00 18.01 ? 371 SER A N 1 ATOM 2578 C CA . SER A 1 371 ? 3.826 -7.790 29.910 1.00 18.82 ? 371 SER A CA 1 ATOM 2579 C C . SER A 1 371 ? 4.452 -8.941 29.107 1.00 19.01 ? 371 SER A C 1 ATOM 2580 O O . SER A 1 371 ? 4.352 -10.098 29.512 1.00 18.40 ? 371 SER A O 1 ATOM 2581 C CB . SER A 1 371 ? 2.391 -8.144 30.322 1.00 18.99 ? 371 SER A CB 1 ATOM 2582 O OG . SER A 1 371 ? 1.559 -8.233 29.190 1.00 20.02 ? 371 SER A OG 1 ATOM 2583 N N . ARG A 1 372 ? 5.086 -8.614 27.976 1.00 19.06 ? 372 ARG A N 1 ATOM 2584 C CA . ARG A 1 372 ? 5.884 -9.568 27.184 1.00 19.29 ? 372 ARG A CA 1 ATOM 2585 C C . ARG A 1 372 ? 5.071 -10.510 26.320 1.00 18.78 ? 372 ARG A C 1 ATOM 2586 O O . ARG A 1 372 ? 5.637 -11.457 25.756 1.00 19.31 ? 372 ARG A O 1 ATOM 2587 C CB . ARG A 1 372 ? 6.826 -10.411 28.071 1.00 19.81 ? 372 ARG A CB 1 ATOM 2588 C CG . ARG A 1 372 ? 7.857 -9.616 28.852 1.00 19.68 ? 372 ARG A CG 1 ATOM 2589 C CD . ARG A 1 372 ? 8.804 -10.552 29.600 1.00 19.05 ? 372 ARG A CD 1 ATOM 2590 N NE . ARG A 1 372 ? 8.110 -11.202 30.703 1.00 18.94 ? 372 ARG A NE 1 ATOM 2591 C CZ . ARG A 1 372 ? 7.675 -12.464 30.721 1.00 19.28 ? 372 ARG A CZ 1 ATOM 2592 N NH1 . ARG A 1 372 ? 7.889 -13.319 29.703 1.00 19.14 ? 372 ARG A NH1 1 ATOM 2593 N NH2 . ARG A 1 372 ? 7.046 -12.893 31.800 1.00 18.85 ? 372 ARG A NH2 1 ATOM 2594 N N . ASN A 1 373 ? 3.764 -10.288 26.189 1.00 17.61 ? 373 ASN A N 1 ATOM 2595 C CA . ASN A 1 373 ? 3.004 -11.172 25.325 1.00 17.11 ? 373 ASN A CA 1 ATOM 2596 C C . ASN A 1 373 ? 3.093 -10.751 23.868 1.00 16.92 ? 373 ASN A C 1 ATOM 2597 O O . ASN A 1 373 ? 3.341 -9.581 23.552 1.00 16.69 ? 373 ASN A O 1 ATOM 2598 C CB . ASN A 1 373 ? 1.559 -11.363 25.803 1.00 17.40 ? 373 ASN A CB 1 ATOM 2599 C CG . ASN A 1 373 ? 0.652 -10.177 25.518 1.00 17.19 ? 373 ASN A CG 1 ATOM 2600 O OD1 . ASN A 1 373 ? 0.399 -9.841 24.368 1.00 16.80 ? 373 ASN A OD1 1 ATOM 2601 N ND2 . ASN A 1 373 ? 0.130 -9.566 26.581 1.00 17.46 ? 373 ASN A ND2 1 ATOM 2602 N N . ILE A 1 374 ? 2.900 -11.718 22.984 1.00 16.41 ? 374 ILE A N 1 ATOM 2603 C CA . ILE A 1 374 ? 2.976 -11.470 21.552 1.00 16.31 ? 374 ILE A CA 1 ATOM 2604 C C . ILE A 1 374 ? 1.641 -11.809 20.892 1.00 16.14 ? 374 ILE A C 1 ATOM 2605 O O . ILE A 1 374 ? 1.603 -12.424 19.839 1.00 16.04 ? 374 ILE A O 1 ATOM 2606 C CB . ILE A 1 374 ? 4.156 -12.232 20.897 1.00 16.40 ? 374 ILE A CB 1 ATOM 2607 C CG1 . ILE A 1 374 ? 4.136 -13.715 21.263 1.00 16.50 ? 374 ILE A CG1 1 ATOM 2608 C CG2 . ILE A 1 374 ? 5.485 -11.621 21.324 1.00 16.05 ? 374 ILE A CG2 1 ATOM 2609 C CD1 . ILE A 1 374 ? 5.113 -14.551 20.464 1.00 16.52 ? 374 ILE A CD1 1 ATOM 2610 N N . THR A 1 375 ? 0.544 -11.386 21.516 1.00 16.29 ? 375 THR A N 1 ATOM 2611 C CA . THR A 1 375 ? -0.786 -11.584 20.949 1.00 16.34 ? 375 THR A CA 1 ATOM 2612 C C . THR A 1 375 ? -1.137 -10.573 19.847 1.00 16.82 ? 375 THR A C 1 ATOM 2613 O O . THR A 1 375 ? -1.971 -10.877 18.982 1.00 17.19 ? 375 THR A O 1 ATOM 2614 C CB . THR A 1 375 ? -1.890 -11.508 22.021 1.00 16.11 ? 375 THR A CB 1 ATOM 2615 O OG1 . THR A 1 375 ? -1.885 -10.209 22.621 1.00 16.50 ? 375 THR A OG1 1 ATOM 2616 C CG2 . THR A 1 375 ? -1.699 -12.586 23.112 1.00 15.87 ? 375 THR A CG2 1 ATOM 2617 N N . ARG A 1 376 ? -0.540 -9.381 19.863 1.00 16.50 ? 376 ARG A N 1 ATOM 2618 C CA . ARG A 1 376 ? -0.995 -8.329 18.934 1.00 16.52 ? 376 ARG A CA 1 ATOM 2619 C C . ARG A 1 376 ? -0.752 -8.779 17.492 1.00 16.67 ? 376 ARG A C 1 ATOM 2620 O O . ARG A 1 376 ? 0.276 -9.402 17.193 1.00 16.43 ? 376 ARG A O 1 ATOM 2621 C CB . ARG A 1 376 ? -0.300 -6.998 19.199 1.00 16.72 ? 376 ARG A CB 1 ATOM 2622 C CG . ARG A 1 376 ? -0.647 -6.362 20.532 1.00 17.37 ? 376 ARG A CG 1 ATOM 2623 C CD . ARG A 1 376 ? 0.126 -5.060 20.807 1.00 17.39 ? 376 ARG A CD 1 ATOM 2624 N NE . ARG A 1 376 ? -0.377 -4.420 22.031 1.00 17.16 ? 376 ARG A NE 1 ATOM 2625 C CZ . ARG A 1 376 ? 0.295 -3.579 22.820 1.00 17.67 ? 376 ARG A CZ 1 ATOM 2626 N NH1 . ARG A 1 376 ? 1.543 -3.215 22.570 1.00 17.91 ? 376 ARG A NH1 1 ATOM 2627 N NH2 . ARG A 1 376 ? -0.297 -3.094 23.898 1.00 18.24 ? 376 ARG A NH2 1 ATOM 2628 N N . GLU A 1 377 ? -1.694 -8.472 16.603 1.00 17.22 ? 377 GLU A N 1 ATOM 2629 C CA . GLU A 1 377 ? -1.579 -8.897 15.211 1.00 17.73 ? 377 GLU A CA 1 ATOM 2630 C C . GLU A 1 377 ? -0.324 -8.341 14.528 1.00 16.91 ? 377 GLU A C 1 ATOM 2631 O O . GLU A 1 377 ? 0.256 -8.999 13.659 1.00 15.65 ? 377 GLU A O 1 ATOM 2632 C CB . GLU A 1 377 ? -2.823 -8.538 14.407 1.00 19.20 ? 377 GLU A CB 1 ATOM 2633 C CG . GLU A 1 377 ? -2.925 -9.357 13.116 1.00 20.54 ? 377 GLU A CG 1 ATOM 2634 C CD . GLU A 1 377 ? -4.308 -9.318 12.490 1.00 21.26 ? 377 GLU A CD 1 ATOM 2635 O OE1 . GLU A 1 377 ? -5.308 -9.349 13.249 1.00 21.15 ? 377 GLU A OE1 1 ATOM 2636 O OE2 . GLU A 1 377 ? -4.379 -9.268 11.233 1.00 22.38 -1 377 GLU A OE2 1 ATOM 2637 N N . LYS A 1 378 ? 0.092 -7.146 14.954 1.00 15.74 ? 378 LYS A N 1 ATOM 2638 C CA . LYS A 1 378 ? 1.312 -6.519 14.453 1.00 15.42 ? 378 LYS A CA 1 ATOM 2639 C C . LYS A 1 378 ? 2.588 -7.369 14.658 1.00 14.48 ? 378 LYS A C 1 ATOM 2640 O O . LYS A 1 378 ? 3.494 -7.326 13.845 1.00 13.96 ? 378 LYS A O 1 ATOM 2641 C CB . LYS A 1 378 ? 1.481 -5.107 15.040 1.00 15.64 ? 378 LYS A CB 1 ATOM 2642 C CG . LYS A 1 378 ? 1.659 -5.018 16.555 1.00 15.95 ? 378 LYS A CG 1 ATOM 2643 C CD . LYS A 1 378 ? 1.815 -3.566 17.008 1.00 16.37 ? 378 LYS A CD 1 ATOM 2644 C CE . LYS A 1 378 ? 3.116 -2.948 16.495 1.00 16.42 ? 378 LYS A CE 1 ATOM 2645 N NZ . LYS A 1 378 ? 3.290 -1.544 16.944 1.00 16.82 ? 378 LYS A NZ 1 ATOM 2646 N N . TYR A 1 379 ? 2.650 -8.155 15.723 1.00 14.32 ? 379 TYR A N 1 ATOM 2647 C CA . TYR A 1 379 ? 3.745 -9.103 15.878 1.00 14.31 ? 379 TYR A CA 1 ATOM 2648 C C . TYR A 1 379 ? 3.765 -10.111 14.713 1.00 14.51 ? 379 TYR A C 1 ATOM 2649 O O . TYR A 1 379 ? 4.790 -10.304 14.087 1.00 14.47 ? 379 TYR A O 1 ATOM 2650 C CB . TYR A 1 379 ? 3.682 -9.838 17.223 1.00 14.16 ? 379 TYR A CB 1 ATOM 2651 C CG . TYR A 1 379 ? 4.851 -10.784 17.409 1.00 14.33 ? 379 TYR A CG 1 ATOM 2652 C CD1 . TYR A 1 379 ? 4.804 -12.077 16.904 1.00 14.07 ? 379 TYR A CD1 1 ATOM 2653 C CD2 . TYR A 1 379 ? 6.019 -10.374 18.063 1.00 14.62 ? 379 TYR A CD2 1 ATOM 2654 C CE1 . TYR A 1 379 ? 5.870 -12.938 17.038 1.00 14.42 ? 379 TYR A CE1 1 ATOM 2655 C CE2 . TYR A 1 379 ? 7.102 -11.238 18.205 1.00 14.31 ? 379 TYR A CE2 1 ATOM 2656 C CZ . TYR A 1 379 ? 7.024 -12.516 17.686 1.00 14.41 ? 379 TYR A CZ 1 ATOM 2657 O OH . TYR A 1 379 ? 8.068 -13.405 17.818 1.00 14.22 ? 379 TYR A OH 1 ATOM 2658 N N . SER A 1 380 ? 2.632 -10.736 14.428 1.00 15.23 ? 380 SER A N 1 ATOM 2659 C CA . SER A 1 380 ? 2.552 -11.772 13.384 1.00 16.22 ? 380 SER A CA 1 ATOM 2660 C C . SER A 1 380 ? 2.783 -11.228 11.973 1.00 17.02 ? 380 SER A C 1 ATOM 2661 O O . SER A 1 380 ? 3.450 -11.867 11.162 1.00 17.11 ? 380 SER A O 1 ATOM 2662 C CB . SER A 1 380 ? 1.196 -12.477 13.441 1.00 15.77 ? 380 SER A CB 1 ATOM 2663 O OG . SER A 1 380 ? 0.984 -13.050 14.710 1.00 15.77 ? 380 SER A OG 1 ATOM 2664 N N . GLU A 1 381 ? 2.225 -10.054 11.690 1.00 18.48 ? 381 GLU A N 1 ATOM 2665 C CA . GLU A 1 381 ? 2.453 -9.380 10.419 1.00 19.57 ? 381 GLU A CA 1 ATOM 2666 C C . GLU A 1 381 ? 3.947 -9.055 10.210 1.00 19.13 ? 381 GLU A C 1 ATOM 2667 O O . GLU A 1 381 ? 4.486 -9.236 9.109 1.00 19.31 ? 381 GLU A O 1 ATOM 2668 C CB . GLU A 1 381 ? 1.598 -8.107 10.343 1.00 21.81 ? 381 GLU A CB 1 ATOM 2669 C CG . GLU A 1 381 ? 1.933 -7.162 9.188 1.00 23.39 ? 381 GLU A CG 1 ATOM 2670 C CD . GLU A 1 381 ? 1.831 -7.832 7.821 1.00 26.01 ? 381 GLU A CD 1 ATOM 2671 O OE1 . GLU A 1 381 ? 0.816 -8.522 7.579 1.00 26.15 ? 381 GLU A OE1 1 ATOM 2672 O OE2 . GLU A 1 381 ? 2.767 -7.664 6.983 1.00 30.21 -1 381 GLU A OE2 1 ATOM 2673 N N . LEU A 1 382 ? 4.611 -8.574 11.260 1.00 18.22 ? 382 LEU A N 1 ATOM 2674 C CA . LEU A 1 382 ? 6.021 -8.167 11.169 1.00 17.35 ? 382 LEU A CA 1 ATOM 2675 C C . LEU A 1 382 ? 6.920 -9.377 10.974 1.00 17.04 ? 382 LEU A C 1 ATOM 2676 O O . LEU A 1 382 ? 7.972 -9.278 10.354 1.00 17.07 ? 382 LEU A O 1 ATOM 2677 C CB . LEU A 1 382 ? 6.442 -7.404 12.430 1.00 16.97 ? 382 LEU A CB 1 ATOM 2678 C CG . LEU A 1 382 ? 7.858 -6.818 12.527 1.00 16.66 ? 382 LEU A CG 1 ATOM 2679 C CD1 . LEU A 1 382 ? 8.210 -5.984 11.303 1.00 16.19 ? 382 LEU A CD1 1 ATOM 2680 C CD2 . LEU A 1 382 ? 7.986 -5.989 13.802 1.00 16.29 ? 382 LEU A CD2 1 ATOM 2681 N N . LYS A 1 383 ? 6.500 -10.515 11.518 1.00 16.77 ? 383 LYS A N 1 ATOM 2682 C CA . LYS A 1 383 ? 7.225 -11.774 11.357 1.00 16.18 ? 383 LYS A CA 1 ATOM 2683 C C . LYS A 1 383 ? 7.274 -12.177 9.894 1.00 15.62 ? 383 LYS A C 1 ATOM 2684 O O . LYS A 1 383 ? 8.249 -12.735 9.447 1.00 15.05 ? 383 LYS A O 1 ATOM 2685 C CB . LYS A 1 383 ? 6.556 -12.878 12.180 1.00 16.13 ? 383 LYS A CB 1 ATOM 2686 C CG . LYS A 1 383 ? 7.163 -14.264 12.024 1.00 15.93 ? 383 LYS A CG 1 ATOM 2687 C CD . LYS A 1 383 ? 6.533 -15.257 12.986 1.00 16.19 ? 383 LYS A CD 1 ATOM 2688 C CE . LYS A 1 383 ? 5.036 -15.429 12.730 1.00 16.22 ? 383 LYS A CE 1 ATOM 2689 N NZ . LYS A 1 383 ? 4.482 -16.642 13.396 1.00 16.47 ? 383 LYS A NZ 1 ATOM 2690 N N . LEU A 1 384 ? 6.214 -11.877 9.154 1.00 16.48 ? 384 LEU A N 1 ATOM 2691 C CA . LEU A 1 384 ? 6.147 -12.200 7.729 1.00 16.53 ? 384 LEU A CA 1 ATOM 2692 C C . LEU A 1 384 ? 7.176 -11.410 6.914 1.00 16.46 ? 384 LEU A C 1 ATOM 2693 O O . LEU A 1 384 ? 7.816 -11.961 6.032 1.00 16.91 ? 384 LEU A O 1 ATOM 2694 C CB . LEU A 1 384 ? 4.743 -11.958 7.182 1.00 16.48 ? 384 LEU A CB 1 ATOM 2695 C CG . LEU A 1 384 ? 3.543 -12.679 7.813 1.00 16.56 ? 384 LEU A CG 1 ATOM 2696 C CD1 . LEU A 1 384 ? 2.289 -12.282 7.062 1.00 16.58 ? 384 LEU A CD1 1 ATOM 2697 C CD2 . LEU A 1 384 ? 3.681 -14.197 7.800 1.00 16.80 ? 384 LEU A CD2 1 ATOM 2698 N N . LEU A 1 385 ? 7.359 -10.134 7.222 1.00 16.74 ? 385 LEU A N 1 ATOM 2699 C CA . LEU A 1 385 ? 8.360 -9.324 6.513 1.00 16.81 ? 385 LEU A CA 1 ATOM 2700 C C . LEU A 1 385 ? 9.810 -9.630 6.962 1.00 16.43 ? 385 LEU A C 1 ATOM 2701 O O . LEU A 1 385 ? 10.732 -9.630 6.154 1.00 15.89 ? 385 LEU A O 1 ATOM 2702 C CB . LEU A 1 385 ? 8.039 -7.841 6.691 1.00 17.11 ? 385 LEU A CB 1 ATOM 2703 C CG . LEU A 1 385 ? 8.980 -6.872 5.969 1.00 17.79 ? 385 LEU A CG 1 ATOM 2704 C CD1 . LEU A 1 385 ? 9.049 -7.177 4.474 1.00 18.13 ? 385 LEU A CD1 1 ATOM 2705 C CD2 . LEU A 1 385 ? 8.545 -5.442 6.229 1.00 18.09 ? 385 LEU A CD2 1 ATOM 2706 N N . GLY A 1 386 ? 10.018 -9.875 8.254 1.00 16.72 ? 386 GLY A N 1 ATOM 2707 C CA . GLY A 1 386 ? 11.362 -10.200 8.763 1.00 17.08 ? 386 GLY A CA 1 ATOM 2708 C C . GLY A 1 386 ? 11.896 -11.470 8.119 1.00 16.91 ? 386 GLY A C 1 ATOM 2709 O O . GLY A 1 386 ? 13.068 -11.557 7.749 1.00 16.28 ? 386 GLY A O 1 ATOM 2710 N N . ASN A 1 387 ? 11.006 -12.439 7.956 1.00 17.48 ? 387 ASN A N 1 ATOM 2711 C CA . ASN A 1 387 ? 11.353 -13.704 7.321 1.00 18.24 ? 387 ASN A CA 1 ATOM 2712 C C . ASN A 1 387 ? 11.568 -13.575 5.823 1.00 19.21 ? 387 ASN A C 1 ATOM 2713 O O . ASN A 1 387 ? 12.477 -14.198 5.279 1.00 20.28 ? 387 ASN A O 1 ATOM 2714 C CB . ASN A 1 387 ? 10.322 -14.775 7.663 1.00 17.73 ? 387 ASN A CB 1 ATOM 2715 C CG . ASN A 1 387 ? 10.624 -15.451 8.992 1.00 17.68 ? 387 ASN A CG 1 ATOM 2716 O OD1 . ASN A 1 387 ? 11.515 -16.291 9.076 1.00 17.42 ? 387 ASN A OD1 1 ATOM 2717 N ND2 . ASN A 1 387 ? 9.913 -15.053 10.045 1.00 17.55 ? 387 ASN A ND2 1 ATOM 2718 N N . PHE A 1 388 ? 10.763 -12.747 5.164 1.00 20.23 ? 388 PHE A N 1 ATOM 2719 C CA . PHE A 1 388 ? 11.025 -12.391 3.777 1.00 21.26 ? 388 PHE A CA 1 ATOM 2720 C C . PHE A 1 388 ? 12.470 -11.917 3.586 1.00 20.22 ? 388 PHE A C 1 ATOM 2721 O O . PHE A 1 388 ? 13.195 -12.439 2.747 1.00 20.21 ? 388 PHE A O 1 ATOM 2722 C CB . PHE A 1 388 ? 10.063 -11.306 3.284 1.00 22.78 ? 388 PHE A CB 1 ATOM 2723 C CG . PHE A 1 388 ? 10.504 -10.660 1.987 1.00 24.86 ? 388 PHE A CG 1 ATOM 2724 C CD1 . PHE A 1 388 ? 10.402 -11.350 0.787 1.00 25.68 ? 388 PHE A CD1 1 ATOM 2725 C CD2 . PHE A 1 388 ? 11.065 -9.387 1.978 1.00 25.97 ? 388 PHE A CD2 1 ATOM 2726 C CE1 . PHE A 1 388 ? 10.821 -10.780 -0.401 1.00 26.41 ? 388 PHE A CE1 1 ATOM 2727 C CE2 . PHE A 1 388 ? 11.493 -8.810 0.791 1.00 27.11 ? 388 PHE A CE2 1 ATOM 2728 C CZ . PHE A 1 388 ? 11.365 -9.510 -0.400 1.00 26.66 ? 388 PHE A CZ 1 ATOM 2729 N N . ALA A 1 389 ? 12.884 -10.929 4.369 1.00 19.68 ? 389 ALA A N 1 ATOM 2730 C CA . ALA A 1 389 ? 14.202 -10.317 4.203 1.00 19.07 ? 389 ALA A CA 1 ATOM 2731 C C . ALA A 1 389 ? 15.339 -11.235 4.631 1.00 19.13 ? 389 ALA A C 1 ATOM 2732 O O . ALA A 1 389 ? 16.439 -11.153 4.106 1.00 18.84 ? 389 ALA A O 1 ATOM 2733 C CB . ALA A 1 389 ? 14.270 -9.008 4.975 1.00 19.44 ? 389 ALA A CB 1 ATOM 2734 N N . LYS A 1 390 ? 15.076 -12.114 5.592 1.00 19.52 ? 390 LYS A N 1 ATOM 2735 C CA . LYS A 1 390 ? 16.102 -13.027 6.078 1.00 19.44 ? 390 LYS A CA 1 ATOM 2736 C C . LYS A 1 390 ? 16.598 -13.987 4.978 1.00 19.44 ? 390 LYS A C 1 ATOM 2737 O O . LYS A 1 390 ? 17.751 -14.408 5.009 1.00 19.04 ? 390 LYS A O 1 ATOM 2738 C CB . LYS A 1 390 ? 15.582 -13.811 7.298 1.00 19.31 ? 390 LYS A CB 1 ATOM 2739 C CG . LYS A 1 390 ? 16.638 -14.668 7.976 1.00 19.33 ? 390 LYS A CG 1 ATOM 2740 C CD . LYS A 1 390 ? 16.097 -15.376 9.222 1.00 19.29 ? 390 LYS A CD 1 ATOM 2741 C CE . LYS A 1 390 ? 17.203 -16.132 9.936 1.00 18.98 ? 390 LYS A CE 1 ATOM 2742 N NZ . LYS A 1 390 ? 16.794 -16.527 11.311 1.00 19.46 ? 390 LYS A NZ 1 ATOM 2743 N N . VAL A 1 391 ? 15.740 -14.312 4.011 1.00 19.86 ? 391 VAL A N 1 ATOM 2744 C CA . VAL A 1 391 ? 16.089 -15.279 2.947 1.00 20.87 ? 391 VAL A CA 1 ATOM 2745 C C . VAL A 1 391 ? 16.206 -14.702 1.515 1.00 21.35 ? 391 VAL A C 1 ATOM 2746 O O . VAL A 1 391 ? 16.320 -15.477 0.563 1.00 21.55 ? 391 VAL A O 1 ATOM 2747 C CB . VAL A 1 391 ? 15.089 -16.474 2.912 1.00 20.31 ? 391 VAL A CB 1 ATOM 2748 C CG1 . VAL A 1 391 ? 15.082 -17.208 4.250 1.00 20.55 ? 391 VAL A CG1 1 ATOM 2749 C CG2 . VAL A 1 391 ? 13.687 -16.017 2.533 1.00 19.80 ? 391 VAL A CG2 1 ATOM 2750 N N . SER A 1 392 ? 16.203 -13.371 1.368 1.00 21.71 ? 392 SER A N 1 ATOM 2751 C CA . SER A 1 392 ? 16.184 -12.715 0.042 1.00 21.38 ? 392 SER A CA 1 ATOM 2752 C C . SER A 1 392 ? 17.401 -11.798 -0.212 1.00 22.36 ? 392 SER A C 1 ATOM 2753 O O . SER A 1 392 ? 17.264 -10.570 -0.225 1.00 22.63 ? 392 SER A O 1 ATOM 2754 C CB . SER A 1 392 ? 14.895 -11.901 -0.108 1.00 20.45 ? 392 SER A CB 1 ATOM 2755 O OG . SER A 1 392 ? 13.760 -12.709 0.107 1.00 19.20 ? 392 SER A OG 1 ATOM 2756 N N . PRO A 1 393 ? 18.587 -12.390 -0.443 1.00 23.50 ? 393 PRO A N 1 ATOM 2757 C CA . PRO A 1 393 ? 19.806 -11.598 -0.672 1.00 24.13 ? 393 PRO A CA 1 ATOM 2758 C C . PRO A 1 393 ? 19.777 -10.734 -1.949 1.00 24.38 ? 393 PRO A C 1 ATOM 2759 O O . PRO A 1 393 ? 20.477 -9.724 -2.019 1.00 24.19 ? 393 PRO A O 1 ATOM 2760 C CB . PRO A 1 393 ? 20.909 -12.665 -0.784 1.00 24.43 ? 393 PRO A CB 1 ATOM 2761 C CG . PRO A 1 393 ? 20.204 -13.917 -1.214 1.00 24.66 ? 393 PRO A CG 1 ATOM 2762 C CD . PRO A 1 393 ? 18.823 -13.844 -0.619 1.00 24.45 ? 393 PRO A CD 1 ATOM 2763 N N . GLY A 1 394 ? 18.979 -11.136 -2.941 1.00 24.40 ? 394 GLY A N 1 ATOM 2764 C CA . GLY A 1 394 ? 18.786 -10.352 -4.169 1.00 24.24 ? 394 GLY A CA 1 ATOM 2765 C C . GLY A 1 394 ? 18.251 -8.951 -3.920 1.00 24.05 ? 394 GLY A C 1 ATOM 2766 O O . GLY A 1 394 ? 18.441 -8.054 -4.744 1.00 23.58 ? 394 GLY A O 1 ATOM 2767 N N . TYR A 1 395 ? 17.577 -8.764 -2.787 1.00 23.44 ? 395 TYR A N 1 ATOM 2768 C CA . TYR A 1 395 ? 17.034 -7.459 -2.408 1.00 23.76 ? 395 TYR A CA 1 ATOM 2769 C C . TYR A 1 395 ? 18.166 -6.442 -2.218 1.00 23.10 ? 395 TYR A C 1 ATOM 2770 O O . TYR A 1 395 ? 18.065 -5.284 -2.642 1.00 22.21 ? 395 TYR A O 1 ATOM 2771 C CB . TYR A 1 395 ? 16.155 -7.583 -1.135 1.00 24.27 ? 395 TYR A CB 1 ATOM 2772 C CG . TYR A 1 395 ? 15.923 -6.283 -0.406 1.00 23.85 ? 395 TYR A CG 1 ATOM 2773 C CD1 . TYR A 1 395 ? 15.016 -5.349 -0.893 1.00 24.26 ? 395 TYR A CD1 1 ATOM 2774 C CD2 . TYR A 1 395 ? 16.616 -5.983 0.762 1.00 23.87 ? 395 TYR A CD2 1 ATOM 2775 C CE1 . TYR A 1 395 ? 14.812 -4.150 -0.245 1.00 25.02 ? 395 TYR A CE1 1 ATOM 2776 C CE2 . TYR A 1 395 ? 16.417 -4.787 1.425 1.00 24.04 ? 395 TYR A CE2 1 ATOM 2777 C CZ . TYR A 1 395 ? 15.515 -3.869 0.918 1.00 24.82 ? 395 TYR A CZ 1 ATOM 2778 O OH . TYR A 1 395 ? 15.304 -2.667 1.558 1.00 24.54 ? 395 TYR A OH 1 ATOM 2779 N N . LEU A 1 396 ? 19.256 -6.883 -1.607 1.00 22.83 ? 396 LEU A N 1 ATOM 2780 C CA . LEU A 1 396 ? 20.365 -5.976 -1.296 1.00 23.47 ? 396 LEU A CA 1 ATOM 2781 C C . LEU A 1 396 ? 21.166 -5.544 -2.512 1.00 24.35 ? 396 LEU A C 1 ATOM 2782 O O . LEU A 1 396 ? 21.861 -4.536 -2.453 1.00 24.33 ? 396 LEU A O 1 ATOM 2783 C CB . LEU A 1 396 ? 21.307 -6.621 -0.278 1.00 23.20 ? 396 LEU A CB 1 ATOM 2784 C CG . LEU A 1 396 ? 20.697 -6.764 1.116 1.00 23.28 ? 396 LEU A CG 1 ATOM 2785 C CD1 . LEU A 1 396 ? 21.616 -7.582 2.009 1.00 23.14 ? 396 LEU A CD1 1 ATOM 2786 C CD2 . LEU A 1 396 ? 20.427 -5.389 1.711 1.00 23.05 ? 396 LEU A CD2 1 ATOM 2787 N N . THR A 1 397 ? 21.074 -6.312 -3.597 1.00 25.24 ? 397 THR A N 1 ATOM 2788 C CA . THR A 1 397 ? 21.903 -6.104 -4.773 1.00 26.55 ? 397 THR A CA 1 ATOM 2789 C C . THR A 1 397 ? 21.148 -5.469 -5.939 1.00 25.83 ? 397 THR A C 1 ATOM 2790 O O . THR A 1 397 ? 21.760 -5.121 -6.927 1.00 27.80 ? 397 THR A O 1 ATOM 2791 C CB . THR A 1 397 ? 22.523 -7.443 -5.241 1.00 27.91 ? 397 THR A CB 1 ATOM 2792 O OG1 . THR A 1 397 ? 21.488 -8.358 -5.623 1.00 28.42 ? 397 THR A OG1 1 ATOM 2793 C CG2 . THR A 1 397 ? 23.347 -8.079 -4.121 1.00 28.96 ? 397 THR A CG2 1 ATOM 2794 N N . ALA A 1 398 ? 19.830 -5.337 -5.836 1.00 25.47 ? 398 ALA A N 1 ATOM 2795 C CA . ALA A 1 398 ? 19.027 -4.688 -6.873 1.00 25.05 ? 398 ALA A CA 1 ATOM 2796 C C . ALA A 1 398 ? 19.312 -3.196 -6.977 1.00 25.60 ? 398 ALA A C 1 ATOM 2797 O O . ALA A 1 398 ? 19.905 -2.595 -6.080 1.00 25.66 ? 398 ALA A O 1 ATOM 2798 C CB . ALA A 1 398 ? 17.548 -4.904 -6.613 1.00 25.29 ? 398 ALA A CB 1 ATOM 2799 N N . SER A 1 399 ? 18.905 -2.618 -8.104 1.00 26.27 ? 399 SER A N 1 ATOM 2800 C CA . SER A 1 399 ? 19.034 -1.191 -8.358 1.00 26.37 ? 399 SER A CA 1 ATOM 2801 C C . SER A 1 399 ? 17.675 -0.572 -8.147 1.00 25.50 ? 399 SER A C 1 ATOM 2802 O O . SER A 1 399 ? 16.788 -0.785 -8.956 1.00 24.96 ? 399 SER A O 1 ATOM 2803 C CB . SER A 1 399 ? 19.462 -0.929 -9.805 1.00 26.97 ? 399 SER A CB 1 ATOM 2804 O OG . SER A 1 399 ? 20.734 -1.473 -10.073 1.00 28.80 ? 399 SER A OG 1 ATOM 2805 N N . PRO A 1 400 ? 17.498 0.201 -7.069 1.00 26.31 ? 400 PRO A N 1 ATOM 2806 C CA . PRO A 1 400 ? 16.184 0.825 -6.856 1.00 27.07 ? 400 PRO A CA 1 ATOM 2807 C C . PRO A 1 400 ? 15.929 1.980 -7.838 1.00 27.38 ? 400 PRO A C 1 ATOM 2808 O O . PRO A 1 400 ? 16.838 2.775 -8.098 1.00 26.73 ? 400 PRO A O 1 ATOM 2809 C CB . PRO A 1 400 ? 16.267 1.359 -5.413 1.00 26.66 ? 400 PRO A CB 1 ATOM 2810 C CG . PRO A 1 400 ? 17.654 1.049 -4.923 1.00 26.87 ? 400 PRO A CG 1 ATOM 2811 C CD . PRO A 1 400 ? 18.495 0.704 -6.114 1.00 26.46 ? 400 PRO A CD 1 ATOM 2812 N N . GLY A 1 401 ? 14.719 2.043 -8.390 1.00 27.33 ? 401 GLY A N 1 ATOM 2813 C CA . GLY A 1 401 ? 14.301 3.149 -9.245 1.00 26.40 ? 401 GLY A CA 1 ATOM 2814 C C . GLY A 1 401 ? 13.356 4.068 -8.492 1.00 26.89 ? 401 GLY A C 1 ATOM 2815 O O . GLY A 1 401 ? 13.147 3.908 -7.288 1.00 25.73 ? 401 GLY A O 1 ATOM 2816 N N . ASN A 1 402 ? 12.787 5.033 -9.203 1.00 27.17 ? 402 ASN A N 1 ATOM 2817 C CA . ASN A 1 402 ? 11.828 5.961 -8.615 1.00 28.58 ? 402 ASN A CA 1 ATOM 2818 C C . ASN A 1 402 ? 10.421 5.389 -8.665 1.00 27.52 ? 402 ASN A C 1 ATOM 2819 O O . ASN A 1 402 ? 10.095 4.601 -9.539 1.00 27.06 ? 402 ASN A O 1 ATOM 2820 C CB . ASN A 1 402 ? 11.876 7.322 -9.341 1.00 31.34 ? 402 ASN A CB 1 ATOM 2821 C CG . ASN A 1 402 ? 13.100 8.144 -8.961 1.00 33.68 ? 402 ASN A CG 1 ATOM 2822 O OD1 . ASN A 1 402 ? 13.535 8.121 -7.806 1.00 34.80 ? 402 ASN A OD1 1 ATOM 2823 N ND2 . ASN A 1 402 ? 13.669 8.869 -9.931 1.00 35.32 ? 402 ASN A ND2 1 ATOM 2824 N N . LEU A 1 403 ? 9.584 5.786 -7.716 1.00 27.39 ? 403 LEU A N 1 ATOM 2825 C CA . LEU A 1 403 ? 8.204 5.317 -7.683 1.00 26.95 ? 403 LEU A CA 1 ATOM 2826 C C . LEU A 1 403 ? 7.442 5.780 -8.928 1.00 26.72 ? 403 LEU A C 1 ATOM 2827 O O . LEU A 1 403 ? 7.711 6.869 -9.455 1.00 26.94 ? 403 LEU A O 1 ATOM 2828 C CB . LEU A 1 403 ? 7.514 5.790 -6.403 1.00 26.74 ? 403 LEU A CB 1 ATOM 2829 C CG . LEU A 1 403 ? 7.363 7.292 -6.160 1.00 26.97 ? 403 LEU A CG 1 ATOM 2830 C CD1 . LEU A 1 403 ? 6.046 7.849 -6.697 1.00 26.63 ? 403 LEU A CD1 1 ATOM 2831 C CD2 . LEU A 1 403 ? 7.468 7.538 -4.659 1.00 27.67 ? 403 LEU A CD2 1 ATOM 2832 N N . THR A 1 404 ? 6.506 4.951 -9.394 1.00 24.77 ? 404 THR A N 1 ATOM 2833 C CA . THR A 1 404 ? 5.750 5.236 -10.602 1.00 24.20 ? 404 THR A CA 1 ATOM 2834 C C . THR A 1 404 ? 4.255 5.031 -10.375 1.00 24.23 ? 404 THR A C 1 ATOM 2835 O O . THR A 1 404 ? 3.857 4.114 -9.657 1.00 24.07 ? 404 THR A O 1 ATOM 2836 C CB . THR A 1 404 ? 6.169 4.298 -11.767 1.00 25.52 ? 404 THR A CB 1 ATOM 2837 O OG1 . THR A 1 404 ? 5.576 2.995 -11.599 1.00 26.76 ? 404 THR A OG1 1 ATOM 2838 C CG2 . THR A 1 404 ? 7.687 4.153 -11.848 1.00 25.41 ? 404 THR A CG2 1 ATOM 2839 N N . THR A 1 405 ? 3.433 5.871 -11.004 1.00 22.94 ? 405 THR A N 1 ATOM 2840 C CA . THR A 1 405 ? 1.993 5.657 -11.065 1.00 22.89 ? 405 THR A CA 1 ATOM 2841 C C . THR A 1 405 ? 1.542 5.104 -12.428 1.00 22.61 ? 405 THR A C 1 ATOM 2842 O O . THR A 1 405 ? 0.348 4.894 -12.656 1.00 22.34 ? 405 THR A O 1 ATOM 2843 C CB . THR A 1 405 ? 1.247 6.962 -10.770 1.00 23.29 ? 405 THR A CB 1 ATOM 2844 O OG1 . THR A 1 405 ? 1.600 7.942 -11.748 1.00 23.18 ? 405 THR A OG1 1 ATOM 2845 C CG2 . THR A 1 405 ? 1.629 7.480 -9.395 1.00 23.34 ? 405 THR A CG2 1 ATOM 2846 N N . SER A 1 406 ? 2.498 4.873 -13.324 1.00 22.28 ? 406 SER A N 1 ATOM 2847 C CA . SER A 1 406 ? 2.247 4.199 -14.600 1.00 22.73 ? 406 SER A CA 1 ATOM 2848 C C . SER A 1 406 ? 3.514 3.467 -15.031 1.00 22.40 ? 406 SER A C 1 ATOM 2849 O O . SER A 1 406 ? 4.579 3.690 -14.479 1.00 23.03 ? 406 SER A O 1 ATOM 2850 C CB . SER A 1 406 ? 1.822 5.205 -15.675 1.00 22.73 ? 406 SER A CB 1 ATOM 2851 O OG . SER A 1 406 ? 2.835 6.184 -15.854 1.00 23.35 ? 406 SER A OG 1 ATOM 2852 N N . GLY A 1 407 ? 3.399 2.581 -16.005 1.00 23.37 ? 407 GLY A N 1 ATOM 2853 C CA . GLY A 1 407 ? 4.548 1.776 -16.441 1.00 24.34 ? 407 GLY A CA 1 ATOM 2854 C C . GLY A 1 407 ? 4.572 0.343 -15.930 1.00 24.91 ? 407 GLY A C 1 ATOM 2855 O O . GLY A 1 407 ? 4.913 -0.554 -16.687 1.00 26.15 ? 407 GLY A O 1 ATOM 2856 N N . TYR A 1 408 ? 4.229 0.114 -14.655 1.00 24.88 ? 408 TYR A N 1 ATOM 2857 C CA . TYR A 1 408 ? 4.179 -1.258 -14.107 1.00 25.12 ? 408 TYR A CA 1 ATOM 2858 C C . TYR A 1 408 ? 2.750 -1.761 -13.875 1.00 26.04 ? 408 TYR A C 1 ATOM 2859 O O . TYR A 1 408 ? 2.446 -2.901 -14.192 1.00 27.27 ? 408 TYR A O 1 ATOM 2860 C CB . TYR A 1 408 ? 5.023 -1.391 -12.836 1.00 24.01 ? 408 TYR A CB 1 ATOM 2861 C CG . TYR A 1 408 ? 6.501 -1.184 -13.094 1.00 23.92 ? 408 TYR A CG 1 ATOM 2862 C CD1 . TYR A 1 408 ? 7.297 -2.197 -13.642 1.00 23.19 ? 408 TYR A CD1 1 ATOM 2863 C CD2 . TYR A 1 408 ? 7.104 0.042 -12.820 1.00 23.62 ? 408 TYR A CD2 1 ATOM 2864 C CE1 . TYR A 1 408 ? 8.655 -1.994 -13.894 1.00 22.98 ? 408 TYR A CE1 1 ATOM 2865 C CE2 . TYR A 1 408 ? 8.449 0.254 -13.074 1.00 23.78 ? 408 TYR A CE2 1 ATOM 2866 C CZ . TYR A 1 408 ? 9.222 -0.759 -13.610 1.00 23.38 ? 408 TYR A CZ 1 ATOM 2867 O OH . TYR A 1 408 ? 10.554 -0.504 -13.827 1.00 22.46 ? 408 TYR A OH 1 ATOM 2868 N N . ALA A 1 409 ? 1.880 -0.922 -13.362 1.00 27.24 ? 409 ALA A N 1 ATOM 2869 C CA . ALA A 1 409 ? 0.527 -1.262 -13.105 1.00 28.02 ? 409 ALA A CA 1 ATOM 2870 C C . ALA A 1 409 ? -0.415 -0.409 -13.907 1.00 28.81 ? 409 ALA A C 1 ATOM 2871 O O . ALA A 1 409 ? -0.148 0.727 -14.154 1.00 29.80 ? 409 ALA A O 1 ATOM 2872 C CB . ALA A 1 409 ? 0.231 -1.147 -11.634 1.00 27.68 ? 409 ALA A CB 1 ATOM 2873 N N . ASP A 1 410 ? -1.534 -0.991 -14.282 1.00 29.91 ? 410 ASP A N 1 ATOM 2874 C CA . ASP A 1 410 ? -2.542 -0.330 -15.090 1.00 30.50 ? 410 ASP A CA 1 ATOM 2875 C C . ASP A 1 410 ? -3.481 0.709 -14.499 1.00 29.81 ? 410 ASP A C 1 ATOM 2876 O O . ASP A 1 410 ? -4.490 0.961 -15.080 1.00 29.17 ? 410 ASP A O 1 ATOM 2877 C CB . ASP A 1 410 ? -3.347 -1.363 -15.869 1.00 30.82 ? 410 ASP A CB 1 ATOM 2878 C CG . ASP A 1 410 ? -4.211 -2.229 -14.997 1.00 31.45 ? 410 ASP A CG 1 ATOM 2879 O OD1 . ASP A 1 410 ? -4.266 -2.059 -13.803 1.00 30.76 ? 410 ASP A OD1 1 ATOM 2880 O OD2 . ASP A 1 410 ? -4.873 -3.092 -15.533 1.00 32.56 -1 410 ASP A OD2 1 ATOM 2881 N N . THR A 1 411 ? -3.145 1.293 -13.362 1.00 29.33 ? 411 THR A N 1 ATOM 2882 C CA . THR A 1 411 ? -3.948 2.348 -12.755 1.00 28.39 ? 411 THR A CA 1 ATOM 2883 C C . THR A 1 411 ? -3.119 3.348 -11.966 1.00 28.52 ? 411 THR A C 1 ATOM 2884 O O . THR A 1 411 ? -2.216 2.990 -11.281 1.00 29.45 ? 411 THR A O 1 ATOM 2885 C CB . THR A 1 411 ? -5.135 1.832 -11.929 1.00 28.52 ? 411 THR A CB 1 ATOM 2886 O OG1 . THR A 1 411 ? -5.602 2.852 -11.067 1.00 28.06 ? 411 THR A OG1 1 ATOM 2887 C CG2 . THR A 1 411 ? -4.771 0.649 -11.103 1.00 29.58 ? 411 THR A CG2 1 ATOM 2888 N N . THR A 1 412 ? -3.450 4.616 -12.074 1.00 28.13 ? 412 THR A N 1 ATOM 2889 C CA . THR A 1 412 ? -2.758 5.624 -11.311 1.00 27.48 ? 412 THR A CA 1 ATOM 2890 C C . THR A 1 412 ? -3.182 5.530 -9.855 1.00 27.56 ? 412 THR A C 1 ATOM 2891 O O . THR A 1 412 ? -2.649 6.177 -9.050 1.00 28.75 ? 412 THR A O 1 ATOM 2892 C CB . THR A 1 412 ? -2.944 7.052 -11.819 1.00 26.49 ? 412 THR A CB 1 ATOM 2893 O OG1 . THR A 1 412 ? -4.315 7.385 -11.846 1.00 27.37 ? 412 THR A OG1 1 ATOM 2894 C CG2 . THR A 1 412 ? -2.355 7.206 -13.134 1.00 27.28 ? 412 THR A CG2 1 ATOM 2895 N N . ASP A 1 413 ? -4.148 4.692 -9.550 1.00 27.43 ? 413 ASP A N 1 ATOM 2896 C CA . ASP A 1 413 ? -4.576 4.490 -8.190 1.00 26.56 ? 413 ASP A CA 1 ATOM 2897 C C . ASP A 1 413 ? -3.537 3.710 -7.409 1.00 24.89 ? 413 ASP A C 1 ATOM 2898 O O . ASP A 1 413 ? -3.529 3.736 -6.220 1.00 24.88 ? 413 ASP A O 1 ATOM 2899 C CB . ASP A 1 413 ? -5.933 3.850 -8.121 1.00 28.14 ? 413 ASP A CB 1 ATOM 2900 C CG . ASP A 1 413 ? -7.024 4.787 -8.468 1.00 29.71 ? 413 ASP A CG 1 ATOM 2901 O OD1 . ASP A 1 413 ? -6.781 5.912 -8.856 1.00 31.55 ? 413 ASP A OD1 1 ATOM 2902 O OD2 . ASP A 1 413 ? -8.159 4.397 -8.382 1.00 32.78 -1 413 ASP A OD2 1 ATOM 2903 N N . LEU A 1 414 ? -2.655 3.027 -8.098 1.00 22.87 ? 414 LEU A N 1 ATOM 2904 C CA . LEU A 1 414 ? -1.587 2.327 -7.438 1.00 22.39 ? 414 LEU A CA 1 ATOM 2905 C C . LEU A 1 414 ? -0.253 2.981 -7.723 1.00 22.76 ? 414 LEU A C 1 ATOM 2906 O O . LEU A 1 414 ? -0.061 3.578 -8.755 1.00 23.90 ? 414 LEU A O 1 ATOM 2907 C CB . LEU A 1 414 ? -1.538 0.874 -7.858 1.00 21.58 ? 414 LEU A CB 1 ATOM 2908 C CG . LEU A 1 414 ? -2.738 0.037 -7.503 1.00 21.39 ? 414 LEU A CG 1 ATOM 2909 C CD1 . LEU A 1 414 ? -2.594 -1.357 -8.015 1.00 21.31 ? 414 LEU A CD1 1 ATOM 2910 C CD2 . LEU A 1 414 ? -3.086 0.058 -6.049 1.00 21.55 ? 414 LEU A CD2 1 ATOM 2911 N N . THR A 1 415 ? 0.652 2.878 -6.778 1.00 21.78 ? 415 THR A N 1 ATOM 2912 C CA . THR A 1 415 ? 2.032 3.300 -6.952 1.00 21.48 ? 415 THR A CA 1 ATOM 2913 C C . THR A 1 415 ? 2.906 2.052 -6.873 1.00 20.82 ? 415 THR A C 1 ATOM 2914 O O . THR A 1 415 ? 2.679 1.177 -6.041 1.00 21.11 ? 415 THR A O 1 ATOM 2915 C CB . THR A 1 415 ? 2.462 4.335 -5.884 1.00 21.74 ? 415 THR A CB 1 ATOM 2916 O OG1 . THR A 1 415 ? 1.775 5.576 -6.103 1.00 23.84 ? 415 THR A OG1 1 ATOM 2917 C CG2 . THR A 1 415 ? 3.931 4.620 -5.967 1.00 22.21 ? 415 THR A CG2 1 ATOM 2918 N N . VAL A 1 416 ? 3.899 1.973 -7.747 1.00 20.23 ? 416 VAL A N 1 ATOM 2919 C CA . VAL A 1 416 ? 4.803 0.837 -7.798 1.00 20.29 ? 416 VAL A CA 1 ATOM 2920 C C . VAL A 1 416 ? 6.221 1.341 -7.861 1.00 19.93 ? 416 VAL A C 1 ATOM 2921 O O . VAL A 1 416 ? 6.572 2.077 -8.781 1.00 20.47 ? 416 VAL A O 1 ATOM 2922 C CB . VAL A 1 416 ? 4.553 -0.049 -9.037 1.00 20.30 ? 416 VAL A CB 1 ATOM 2923 C CG1 . VAL A 1 416 ? 5.538 -1.224 -9.067 1.00 20.06 ? 416 VAL A CG1 1 ATOM 2924 C CG2 . VAL A 1 416 ? 3.110 -0.541 -9.057 1.00 20.09 ? 416 VAL A CG2 1 ATOM 2925 N N . THR A 1 417 ? 7.018 0.954 -6.874 1.00 19.83 ? 417 THR A N 1 ATOM 2926 C CA . THR A 1 417 ? 8.437 1.249 -6.862 1.00 20.02 ? 417 THR A CA 1 ATOM 2927 C C . THR A 1 417 ? 9.201 -0.024 -7.208 1.00 20.56 ? 417 THR A C 1 ATOM 2928 O O . THR A 1 417 ? 8.967 -1.074 -6.599 1.00 19.95 ? 417 THR A O 1 ATOM 2929 C CB . THR A 1 417 ? 8.885 1.762 -5.498 1.00 19.74 ? 417 THR A CB 1 ATOM 2930 O OG1 . THR A 1 417 ? 8.079 2.884 -5.134 1.00 20.28 ? 417 THR A OG1 1 ATOM 2931 C CG2 . THR A 1 417 ? 10.344 2.198 -5.544 1.00 20.02 ? 417 THR A CG2 1 ATOM 2932 N N . PRO A 1 418 ? 10.090 0.055 -8.212 1.00 21.35 ? 418 PRO A N 1 ATOM 2933 C CA . PRO A 1 418 ? 10.829 -1.115 -8.631 1.00 21.92 ? 418 PRO A CA 1 ATOM 2934 C C . PRO A 1 418 ? 12.260 -1.115 -8.115 1.00 22.06 ? 418 PRO A C 1 ATOM 2935 O O . PRO A 1 418 ? 12.884 -0.060 -8.016 1.00 22.63 ? 418 PRO A O 1 ATOM 2936 C CB . PRO A 1 418 ? 10.823 -0.974 -10.147 1.00 21.89 ? 418 PRO A CB 1 ATOM 2937 C CG . PRO A 1 418 ? 10.956 0.512 -10.344 1.00 22.10 ? 418 PRO A CG 1 ATOM 2938 C CD . PRO A 1 418 ? 10.266 1.162 -9.173 1.00 21.63 ? 418 PRO A CD 1 ATOM 2939 N N . LEU A 1 419 ? 12.784 -2.285 -7.854 1.00 22.71 ? 419 LEU A N 1 ATOM 2940 C CA . LEU A 1 419 ? 14.132 -2.517 -7.423 1.00 22.85 ? 419 LEU A CA 1 ATOM 2941 C C . LEU A 1 419 ? 14.531 -3.563 -8.430 1.00 23.20 ? 419 LEU A C 1 ATOM 2942 O O . LEU A 1 419 ? 14.167 -4.678 -8.345 1.00 22.29 ? 419 LEU A O 1 ATOM 2943 C CB . LEU A 1 419 ? 14.171 -3.054 -6.026 1.00 23.15 ? 419 LEU A CB 1 ATOM 2944 C CG . LEU A 1 419 ? 14.093 -2.102 -4.841 1.00 23.80 ? 419 LEU A CG 1 ATOM 2945 C CD1 . LEU A 1 419 ? 12.679 -1.749 -4.464 1.00 24.07 ? 419 LEU A CD1 1 ATOM 2946 C CD2 . LEU A 1 419 ? 14.832 -2.726 -3.693 1.00 24.06 ? 419 LEU A CD2 1 ATOM 2947 N N . LEU A 1 420 ? 15.290 -3.141 -9.411 1.00 23.60 ? 420 LEU A N 1 ATOM 2948 C CA . LEU A 1 420 ? 15.646 -3.983 -10.506 1.00 24.20 ? 420 LEU A CA 1 ATOM 2949 C C . LEU A 1 420 ? 16.986 -4.677 -10.413 1.00 25.34 ? 420 LEU A C 1 ATOM 2950 O O . LEU A 1 420 ? 17.991 -4.086 -10.323 1.00 24.82 ? 420 LEU A O 1 ATOM 2951 C CB . LEU A 1 420 ? 15.523 -3.210 -11.803 1.00 24.35 ? 420 LEU A CB 1 ATOM 2952 C CG . LEU A 1 420 ? 14.183 -2.677 -12.241 1.00 25.00 ? 420 LEU A CG 1 ATOM 2953 C CD1 . LEU A 1 420 ? 14.226 -1.648 -13.327 1.00 25.27 ? 420 LEU A CD1 1 ATOM 2954 C CD2 . LEU A 1 420 ? 13.178 -3.741 -12.545 1.00 25.58 ? 420 LEU A CD2 1 ATOM 2955 N N . GLY A 1 421 ? 16.945 -5.976 -10.380 1.00 28.14 ? 421 GLY A N 1 ATOM 2956 C CA . GLY A 1 421 ? 18.146 -6.779 -10.387 1.00 30.67 ? 421 GLY A CA 1 ATOM 2957 C C . GLY A 1 421 ? 18.329 -7.432 -11.739 1.00 33.62 ? 421 GLY A C 1 ATOM 2958 O O . GLY A 1 421 ? 17.436 -7.418 -12.562 1.00 35.81 ? 421 GLY A O 1 ATOM 2959 N N . ASN A 1 422 ? 19.480 -8.003 -12.011 1.00 37.72 ? 422 ASN A N 1 ATOM 2960 C CA . ASN A 1 422 ? 19.640 -8.630 -13.344 1.00 39.70 ? 422 ASN A CA 1 ATOM 2961 C C . ASN A 1 422 ? 19.148 -10.072 -13.235 1.00 38.97 ? 422 ASN A C 1 ATOM 2962 O O . ASN A 1 422 ? 17.971 -10.367 -13.054 1.00 35.90 ? 422 ASN A O 1 ATOM 2963 C CB . ASN A 1 422 ? 21.011 -8.428 -13.922 1.00 40.06 ? 422 ASN A CB 1 ATOM 2964 C CG . ASN A 1 422 ? 21.243 -7.000 -14.346 1.00 43.83 ? 422 ASN A CG 1 ATOM 2965 O OD1 . ASN A 1 422 ? 20.745 -6.562 -15.375 1.00 42.92 ? 422 ASN A OD1 1 ATOM 2966 N ND2 . ASN A 1 422 ? 22.010 -6.280 -13.596 1.00 47.49 ? 422 ASN A ND2 1 ATOM 2967 N N . SER A 1 423 ? 20.094 -10.951 -13.190 1.00 37.89 ? 423 SER A N 1 ATOM 2968 C CA . SER A 1 423 ? 19.827 -12.314 -12.843 1.00 37.29 ? 423 SER A CA 1 ATOM 2969 C C . SER A 1 423 ? 19.615 -12.541 -11.346 1.00 34.93 ? 423 SER A C 1 ATOM 2970 O O . SER A 1 423 ? 19.157 -13.572 -10.980 1.00 37.79 ? 423 SER A O 1 ATOM 2971 C CB . SER A 1 423 ? 20.947 -13.199 -13.376 1.00 37.76 ? 423 SER A CB 1 ATOM 2972 O OG . SER A 1 423 ? 22.205 -12.577 -13.321 1.00 37.55 ? 423 SER A OG 1 ATOM 2973 N N . THR A 1 424 ? 19.930 -11.580 -10.501 1.00 31.49 ? 424 THR A N 1 ATOM 2974 C CA . THR A 1 424 ? 19.747 -11.692 -9.085 1.00 29.79 ? 424 THR A CA 1 ATOM 2975 C C . THR A 1 424 ? 18.318 -11.517 -8.603 1.00 27.07 ? 424 THR A C 1 ATOM 2976 O O . THR A 1 424 ? 18.072 -11.748 -7.493 1.00 27.55 ? 424 THR A O 1 ATOM 2977 C CB . THR A 1 424 ? 20.709 -10.768 -8.295 1.00 30.82 ? 424 THR A CB 1 ATOM 2978 O OG1 . THR A 1 424 ? 20.831 -9.499 -8.916 1.00 31.92 ? 424 THR A OG1 1 ATOM 2979 C CG2 . THR A 1 424 ? 22.051 -11.377 -8.205 1.00 31.83 ? 424 THR A CG2 1 ATOM 2980 N N . GLY A 1 425 ? 17.404 -11.089 -9.445 1.00 25.18 ? 425 GLY A N 1 ATOM 2981 C CA . GLY A 1 425 ? 16.025 -10.915 -9.062 1.00 24.19 ? 425 GLY A CA 1 ATOM 2982 C C . GLY A 1 425 ? 15.541 -9.500 -8.888 1.00 23.90 ? 425 GLY A C 1 ATOM 2983 O O . GLY A 1 425 ? 16.285 -8.655 -8.550 1.00 25.39 ? 425 GLY A O 1 ATOM 2984 N N . SER A 1 426 ? 14.278 -9.256 -9.116 1.00 22.83 ? 426 SER A N 1 ATOM 2985 C CA . SER A 1 426 ? 13.696 -7.947 -8.988 1.00 21.90 ? 426 SER A CA 1 ATOM 2986 C C . SER A 1 426 ? 12.573 -7.922 -8.017 1.00 21.70 ? 426 SER A C 1 ATOM 2987 O O . SER A 1 426 ? 11.950 -8.880 -7.812 1.00 21.38 ? 426 SER A O 1 ATOM 2988 C CB . SER A 1 426 ? 13.180 -7.451 -10.311 1.00 21.23 ? 426 SER A CB 1 ATOM 2989 O OG . SER A 1 426 ? 14.223 -7.147 -11.124 1.00 21.81 ? 426 SER A OG 1 ATOM 2990 N N . PHE A 1 427 ? 12.303 -6.767 -7.450 1.00 22.07 ? 427 PHE A N 1 ATOM 2991 C CA . PHE A 1 427 ? 11.248 -6.613 -6.446 1.00 22.13 ? 427 PHE A CA 1 ATOM 2992 C C . PHE A 1 427 ? 10.421 -5.382 -6.777 1.00 21.76 ? 427 PHE A C 1 ATOM 2993 O O . PHE A 1 427 ? 10.977 -4.353 -7.147 1.00 21.81 ? 427 PHE A O 1 ATOM 2994 C CB . PHE A 1 427 ? 11.864 -6.492 -5.047 1.00 22.55 ? 427 PHE A CB 1 ATOM 2995 C CG . PHE A 1 427 ? 12.806 -7.616 -4.707 1.00 23.03 ? 427 PHE A CG 1 ATOM 2996 C CD1 . PHE A 1 427 ? 14.106 -7.620 -5.201 1.00 23.72 ? 427 PHE A CD1 1 ATOM 2997 C CD2 . PHE A 1 427 ? 12.395 -8.673 -3.913 1.00 22.93 ? 427 PHE A CD2 1 ATOM 2998 C CE1 . PHE A 1 427 ? 14.976 -8.662 -4.909 1.00 23.97 ? 427 PHE A CE1 1 ATOM 2999 C CE2 . PHE A 1 427 ? 13.258 -9.716 -3.618 1.00 23.82 ? 427 PHE A CE2 1 ATOM 3000 C CZ . PHE A 1 427 ? 14.552 -9.713 -4.114 1.00 23.87 ? 427 PHE A CZ 1 ATOM 3001 N N . PHE A 1 428 ? 9.102 -5.499 -6.637 1.00 20.99 ? 428 PHE A N 1 ATOM 3002 C CA . PHE A 1 428 ? 8.179 -4.428 -6.952 1.00 20.34 ? 428 PHE A CA 1 ATOM 3003 C C . PHE A 1 428 ? 7.252 -4.184 -5.774 1.00 20.32 ? 428 PHE A C 1 ATOM 3004 O O . PHE A 1 428 ? 6.446 -5.056 -5.405 1.00 19.77 ? 428 PHE A O 1 ATOM 3005 C CB . PHE A 1 428 ? 7.389 -4.774 -8.220 1.00 20.97 ? 428 PHE A CB 1 ATOM 3006 C CG . PHE A 1 428 ? 8.274 -5.047 -9.395 1.00 21.17 ? 428 PHE A CG 1 ATOM 3007 C CD1 . PHE A 1 428 ? 8.808 -6.311 -9.594 1.00 20.58 ? 428 PHE A CD1 1 ATOM 3008 C CD2 . PHE A 1 428 ? 8.636 -4.025 -10.256 1.00 21.07 ? 428 PHE A CD2 1 ATOM 3009 C CE1 . PHE A 1 428 ? 9.661 -6.558 -10.647 1.00 20.73 ? 428 PHE A CE1 1 ATOM 3010 C CE2 . PHE A 1 428 ? 9.497 -4.265 -11.312 1.00 21.36 ? 428 PHE A CE2 1 ATOM 3011 C CZ . PHE A 1 428 ? 10.010 -5.534 -11.508 1.00 21.17 ? 428 PHE A CZ 1 ATOM 3012 N N . VAL A 1 429 ? 7.380 -2.997 -5.181 1.00 19.61 ? 429 VAL A N 1 ATOM 3013 C CA . VAL A 1 429 ? 6.575 -2.618 -4.033 1.00 19.17 ? 429 VAL A CA 1 ATOM 3014 C C . VAL A 1 429 ? 5.352 -1.843 -4.500 1.00 19.18 ? 429 VAL A C 1 ATOM 3015 O O . VAL A 1 429 ? 5.481 -0.731 -5.035 1.00 18.60 ? 429 VAL A O 1 ATOM 3016 C CB . VAL A 1 429 ? 7.375 -1.763 -3.025 1.00 19.33 ? 429 VAL A CB 1 ATOM 3017 C CG1 . VAL A 1 429 ? 6.529 -1.453 -1.798 1.00 18.81 ? 429 VAL A CG1 1 ATOM 3018 C CG2 . VAL A 1 429 ? 8.668 -2.476 -2.634 1.00 19.02 ? 429 VAL A CG2 1 ATOM 3019 N N . VAL A 1 430 ? 4.179 -2.440 -4.274 1.00 19.11 ? 430 VAL A N 1 ATOM 3020 C CA . VAL A 1 430 ? 2.885 -1.899 -4.697 1.00 19.24 ? 430 VAL A CA 1 ATOM 3021 C C . VAL A 1 430 ? 2.086 -1.396 -3.488 1.00 19.48 ? 430 VAL A C 1 ATOM 3022 O O . VAL A 1 430 ? 1.998 -2.066 -2.451 1.00 20.45 ? 430 VAL A O 1 ATOM 3023 C CB . VAL A 1 430 ? 2.046 -2.969 -5.436 1.00 19.61 ? 430 VAL A CB 1 ATOM 3024 C CG1 . VAL A 1 430 ? 0.827 -2.349 -6.114 1.00 20.03 ? 430 VAL A CG1 1 ATOM 3025 C CG2 . VAL A 1 430 ? 2.900 -3.695 -6.463 1.00 19.59 ? 430 VAL A CG2 1 ATOM 3026 N N . ARG A 1 431 ? 1.519 -0.210 -3.628 1.00 18.88 ? 431 ARG A N 1 ATOM 3027 C CA . ARG A 1 431 ? 0.663 0.380 -2.605 1.00 19.02 ? 431 ARG A CA 1 ATOM 3028 C C . ARG A 1 431 ? -0.329 1.336 -3.272 1.00 18.61 ? 431 ARG A C 1 ATOM 3029 O O . ARG A 1 431 ? -0.193 1.641 -4.452 1.00 17.56 ? 431 ARG A O 1 ATOM 3030 C CB . ARG A 1 431 ? 1.493 1.146 -1.582 1.00 18.39 ? 431 ARG A CB 1 ATOM 3031 C CG . ARG A 1 431 ? 2.291 2.283 -2.178 1.00 18.40 ? 431 ARG A CG 1 ATOM 3032 C CD . ARG A 1 431 ? 2.528 3.353 -1.147 1.00 18.43 ? 431 ARG A CD 1 ATOM 3033 N NE . ARG A 1 431 ? 3.445 4.396 -1.606 1.00 18.49 ? 431 ARG A NE 1 ATOM 3034 C CZ . ARG A 1 431 ? 3.102 5.636 -1.971 1.00 17.71 ? 431 ARG A CZ 1 ATOM 3035 N NH1 . ARG A 1 431 ? 1.830 6.031 -1.980 1.00 17.26 ? 431 ARG A NH1 1 ATOM 3036 N NH2 . ARG A 1 431 ? 4.057 6.486 -2.341 1.00 17.24 ? 431 ARG A NH2 1 ATOM 3037 N N . HIS A 1 432 ? -1.279 1.826 -2.525 1.00 18.99 ? 432 HIS A N 1 ATOM 3038 C CA . HIS A 1 432 ? -2.211 2.802 -3.016 1.00 19.73 ? 432 HIS A CA 1 ATOM 3039 C C . HIS A 1 432 ? -1.447 4.118 -3.117 1.00 20.28 ? 432 HIS A C 1 ATOM 3040 O O . HIS A 1 432 ? -0.645 4.419 -2.297 1.00 19.92 ? 432 HIS A O 1 ATOM 3041 C CB . HIS A 1 432 ? -3.400 2.977 -2.094 1.00 19.97 ? 432 HIS A CB 1 ATOM 3042 C CG . HIS A 1 432 ? -4.471 1.957 -2.280 1.00 20.93 ? 432 HIS A CG 1 ATOM 3043 N ND1 . HIS A 1 432 ? -4.657 0.901 -1.432 1.00 21.12 ? 432 HIS A ND1 1 ATOM 3044 C CD2 . HIS A 1 432 ? -5.398 1.828 -3.237 1.00 21.17 ? 432 HIS A CD2 1 ATOM 3045 C CE1 . HIS A 1 432 ? -5.650 0.174 -1.861 1.00 21.72 ? 432 HIS A CE1 1 ATOM 3046 N NE2 . HIS A 1 432 ? -6.115 0.716 -2.956 1.00 21.90 ? 432 HIS A NE2 1 ATOM 3047 N N . SER A 1 433 ? -1.700 4.851 -4.173 1.00 21.12 ? 433 SER A N 1 ATOM 3048 C CA . SER A 1 433 ? -1.106 6.143 -4.408 1.00 22.66 ? 433 SER A CA 1 ATOM 3049 C C . SER A 1 433 ? -1.472 7.098 -3.294 1.00 22.92 ? 433 SER A C 1 ATOM 3050 O O . SER A 1 433 ? -0.670 7.801 -2.864 1.00 23.51 ? 433 SER A O 1 ATOM 3051 C CB . SER A 1 433 ? -1.426 6.677 -5.777 1.00 22.63 ? 433 SER A CB 1 ATOM 3052 O OG . SER A 1 433 ? -0.989 5.782 -6.711 1.00 22.34 ? 433 SER A OG 1 ATOM 3053 N N . ASP A 1 434 ? -2.696 7.068 -2.847 1.00 24.14 ? 434 ASP A N 1 ATOM 3054 C CA . ASP A 1 434 ? -3.102 7.783 -1.689 1.00 25.47 ? 434 ASP A CA 1 ATOM 3055 C C . ASP A 1 434 ? -2.923 6.645 -0.676 1.00 25.13 ? 434 ASP A C 1 ATOM 3056 O O . ASP A 1 434 ? -3.718 5.757 -0.629 1.00 23.15 ? 434 ASP A O 1 ATOM 3057 C CB . ASP A 1 434 ? -4.541 8.196 -1.734 1.00 26.97 ? 434 ASP A CB 1 ATOM 3058 C CG . ASP A 1 434 ? -5.056 8.648 -0.405 1.00 28.96 ? 434 ASP A CG 1 ATOM 3059 O OD1 . ASP A 1 434 ? -4.313 8.903 0.488 1.00 29.59 ? 434 ASP A OD1 1 ATOM 3060 O OD2 . ASP A 1 434 ? -6.248 8.744 -0.231 1.00 33.88 -1 434 ASP A OD2 1 ATOM 3061 N N . TYR A 1 435 ? -1.855 6.696 0.109 1.00 23.93 ? 435 TYR A N 1 ATOM 3062 C CA . TYR A 1 435 ? -1.475 5.659 1.080 1.00 23.12 ? 435 TYR A CA 1 ATOM 3063 C C . TYR A 1 435 ? -2.529 5.395 2.170 1.00 23.19 ? 435 TYR A C 1 ATOM 3064 O O . TYR A 1 435 ? -2.524 4.320 2.783 1.00 22.16 ? 435 TYR A O 1 ATOM 3065 C CB . TYR A 1 435 ? -0.133 6.014 1.738 1.00 22.54 ? 435 TYR A CB 1 ATOM 3066 C CG . TYR A 1 435 ? -0.281 6.886 2.961 1.00 22.18 ? 435 TYR A CG 1 ATOM 3067 C CD1 . TYR A 1 435 ? -0.385 8.272 2.859 1.00 21.69 ? 435 TYR A CD1 1 ATOM 3068 C CD2 . TYR A 1 435 ? -0.329 6.318 4.222 1.00 22.04 ? 435 TYR A CD2 1 ATOM 3069 C CE1 . TYR A 1 435 ? -0.538 9.057 3.990 1.00 21.38 ? 435 TYR A CE1 1 ATOM 3070 C CE2 . TYR A 1 435 ? -0.482 7.091 5.352 1.00 22.08 ? 435 TYR A CE2 1 ATOM 3071 C CZ . TYR A 1 435 ? -0.584 8.457 5.238 1.00 21.61 ? 435 TYR A CZ 1 ATOM 3072 O OH . TYR A 1 435 ? -0.745 9.186 6.400 1.00 20.88 ? 435 TYR A OH 1 ATOM 3073 N N . SER A 1 436 ? -3.394 6.377 2.443 1.00 23.60 ? 436 SER A N 1 ATOM 3074 C CA . SER A 1 436 ? -4.461 6.188 3.435 1.00 24.95 ? 436 SER A CA 1 ATOM 3075 C C . SER A 1 436 ? -5.672 5.434 2.903 1.00 24.30 ? 436 SER A C 1 ATOM 3076 O O . SER A 1 436 ? -6.472 4.939 3.685 1.00 24.30 ? 436 SER A O 1 ATOM 3077 C CB . SER A 1 436 ? -4.914 7.521 4.029 1.00 25.42 ? 436 SER A CB 1 ATOM 3078 O OG . SER A 1 436 ? -5.258 8.424 3.009 1.00 27.99 ? 436 SER A OG 1 ATOM 3079 N N . SER A 1 437 ? -5.792 5.325 1.587 1.00 24.44 ? 437 SER A N 1 ATOM 3080 C CA . SER A 1 437 ? -6.971 4.719 0.959 1.00 25.49 ? 437 SER A CA 1 ATOM 3081 C C . SER A 1 437 ? -7.362 3.372 1.559 1.00 26.10 ? 437 SER A C 1 ATOM 3082 O O . SER A 1 437 ? -6.511 2.494 1.750 1.00 25.25 ? 437 SER A O 1 ATOM 3083 C CB . SER A 1 437 ? -6.743 4.529 -0.545 1.00 24.89 ? 437 SER A CB 1 ATOM 3084 O OG . SER A 1 437 ? -7.817 3.807 -1.126 1.00 24.92 ? 437 SER A OG 1 ATOM 3085 N N . GLU A 1 438 ? -8.657 3.224 1.829 1.00 26.90 ? 438 GLU A N 1 ATOM 3086 C CA . GLU A 1 438 ? -9.226 1.952 2.260 1.00 29.06 ? 438 GLU A CA 1 ATOM 3087 C C . GLU A 1 438 ? -9.957 1.261 1.104 1.00 29.48 ? 438 GLU A C 1 ATOM 3088 O O . GLU A 1 438 ? -10.567 0.217 1.290 1.00 30.02 ? 438 GLU A O 1 ATOM 3089 C CB . GLU A 1 438 ? -10.114 2.148 3.508 1.00 30.05 ? 438 GLU A CB 1 ATOM 3090 C CG . GLU A 1 438 ? -9.324 1.951 4.806 1.00 32.61 ? 438 GLU A CG 1 ATOM 3091 C CD . GLU A 1 438 ? -9.891 2.654 6.040 1.00 35.48 ? 438 GLU A CD 1 ATOM 3092 O OE1 . GLU A 1 438 ? -10.442 3.769 5.914 1.00 35.39 ? 438 GLU A OE1 1 ATOM 3093 O OE2 . GLU A 1 438 ? -9.749 2.097 7.162 1.00 38.45 -1 438 GLU A OE2 1 ATOM 3094 N N . GLU A 1 439 ? -9.840 1.815 -0.103 1.00 31.15 ? 439 GLU A N 1 ATOM 3095 C CA . GLU A 1 439 ? -10.468 1.238 -1.296 1.00 31.36 ? 439 GLU A CA 1 ATOM 3096 C C . GLU A 1 439 ? -9.865 -0.104 -1.706 1.00 29.40 ? 439 GLU A C 1 ATOM 3097 O O . GLU A 1 439 ? -8.683 -0.368 -1.506 1.00 28.47 ? 439 GLU A O 1 ATOM 3098 C CB . GLU A 1 439 ? -10.383 2.211 -2.484 1.00 34.53 ? 439 GLU A CB 1 ATOM 3099 C CG . GLU A 1 439 ? -11.157 3.509 -2.279 1.00 38.02 ? 439 GLU A CG 1 ATOM 3100 C CD . GLU A 1 439 ? -12.638 3.258 -2.010 1.00 42.14 ? 439 GLU A CD 1 ATOM 3101 O OE1 . GLU A 1 439 ? -13.359 2.842 -2.953 1.00 44.58 ? 439 GLU A OE1 1 ATOM 3102 O OE2 . GLU A 1 439 ? -13.081 3.455 -0.850 1.00 46.63 -1 439 GLU A OE2 1 ATOM 3103 N N . SER A 1 440 ? -10.708 -0.949 -2.275 1.00 28.00 ? 440 SER A N 1 ATOM 3104 C CA . SER A 1 440 ? -10.279 -2.180 -2.886 1.00 29.19 ? 440 SER A CA 1 ATOM 3105 C C . SER A 1 440 ? -9.984 -1.885 -4.359 1.00 29.10 ? 440 SER A C 1 ATOM 3106 O O . SER A 1 440 ? -10.849 -1.375 -5.069 1.00 29.38 ? 440 SER A O 1 ATOM 3107 C CB . SER A 1 440 ? -11.386 -3.216 -2.763 1.00 29.09 ? 440 SER A CB 1 ATOM 3108 O OG . SER A 1 440 ? -10.981 -4.423 -3.369 1.00 31.63 ? 440 SER A OG 1 ATOM 3109 N N . THR A 1 441 ? -8.776 -2.196 -4.817 1.00 27.94 ? 441 THR A N 1 ATOM 3110 C CA . THR A 1 441 ? -8.362 -1.835 -6.171 1.00 27.30 ? 441 THR A CA 1 ATOM 3111 C C . THR A 1 441 ? -7.927 -3.049 -6.979 1.00 27.11 ? 441 THR A C 1 ATOM 3112 O O . THR A 1 441 ? -7.054 -3.798 -6.550 1.00 26.82 ? 441 THR A O 1 ATOM 3113 C CB . THR A 1 441 ? -7.195 -0.811 -6.136 1.00 28.13 ? 441 THR A CB 1 ATOM 3114 O OG1 . THR A 1 441 ? -7.539 0.296 -5.291 1.00 27.30 ? 441 THR A OG1 1 ATOM 3115 C CG2 . THR A 1 441 ? -6.869 -0.290 -7.544 1.00 27.94 ? 441 THR A CG2 1 ATOM 3116 N N . SER A 1 442 ? -8.528 -3.226 -8.157 1.00 27.65 ? 442 SER A N 1 ATOM 3117 C CA . SER A 1 442 ? -8.143 -4.293 -9.087 1.00 27.40 ? 442 SER A CA 1 ATOM 3118 C C . SER A 1 442 ? -7.039 -3.807 -10.010 1.00 26.75 ? 442 SER A C 1 ATOM 3119 O O . SER A 1 442 ? -7.023 -2.641 -10.398 1.00 25.95 ? 442 SER A O 1 ATOM 3120 C CB . SER A 1 442 ? -9.330 -4.727 -9.941 1.00 27.62 ? 442 SER A CB 1 ATOM 3121 O OG . SER A 1 442 ? -10.389 -5.204 -9.133 1.00 28.99 ? 442 SER A OG 1 ATOM 3122 N N . TYR A 1 443 ? -6.124 -4.698 -10.373 1.00 25.40 ? 443 TYR A N 1 ATOM 3123 C CA . TYR A 1 443 ? -5.065 -4.329 -11.295 1.00 24.20 ? 443 TYR A CA 1 ATOM 3124 C C . TYR A 1 443 ? -4.444 -5.500 -12.046 1.00 24.22 ? 443 TYR A C 1 ATOM 3125 O O . TYR A 1 443 ? -4.672 -6.663 -11.711 1.00 22.09 ? 443 TYR A O 1 ATOM 3126 C CB . TYR A 1 443 ? -3.972 -3.542 -10.565 1.00 23.07 ? 443 TYR A CB 1 ATOM 3127 C CG . TYR A 1 443 ? -3.186 -4.278 -9.483 1.00 22.59 ? 443 TYR A CG 1 ATOM 3128 C CD1 . TYR A 1 443 ? -3.750 -4.564 -8.231 1.00 22.41 ? 443 TYR A CD1 1 ATOM 3129 C CD2 . TYR A 1 443 ? -1.847 -4.617 -9.685 1.00 22.68 ? 443 TYR A CD2 1 ATOM 3130 C CE1 . TYR A 1 443 ? -3.013 -5.200 -7.238 1.00 21.97 ? 443 TYR A CE1 1 ATOM 3131 C CE2 . TYR A 1 443 ? -1.102 -5.248 -8.700 1.00 22.39 ? 443 TYR A CE2 1 ATOM 3132 C CZ . TYR A 1 443 ? -1.684 -5.538 -7.479 1.00 22.45 ? 443 TYR A CZ 1 ATOM 3133 O OH . TYR A 1 443 ? -0.921 -6.169 -6.521 1.00 21.68 ? 443 TYR A OH 1 ATOM 3134 N N . LYS A 1 444 ? -3.627 -5.145 -13.026 1.00 24.65 ? 444 LYS A N 1 ATOM 3135 C CA . LYS A 1 444 ? -2.825 -6.056 -13.812 1.00 26.31 ? 444 LYS A CA 1 ATOM 3136 C C . LYS A 1 444 ? -1.434 -5.470 -13.845 1.00 25.81 ? 444 LYS A C 1 ATOM 3137 O O . LYS A 1 444 ? -1.263 -4.322 -13.671 1.00 26.06 ? 444 LYS A O 1 ATOM 3138 C CB . LYS A 1 444 ? -3.349 -6.293 -15.216 1.00 27.23 ? 444 LYS A CB 1 ATOM 3139 C CG . LYS A 1 444 ? -4.784 -6.705 -15.316 1.00 29.19 ? 444 LYS A CG 1 ATOM 3140 C CD . LYS A 1 444 ? -5.156 -7.000 -16.730 1.00 30.99 ? 444 LYS A CD 1 ATOM 3141 C CE . LYS A 1 444 ? -5.380 -8.463 -16.927 1.00 33.83 ? 444 LYS A CE 1 ATOM 3142 N NZ . LYS A 1 444 ? -4.892 -9.028 -18.224 1.00 36.29 ? 444 LYS A NZ 1 ATOM 3143 N N . LEU A 1 445 ? -0.444 -6.295 -14.065 1.00 25.69 ? 445 LEU A N 1 ATOM 3144 C CA . LEU A 1 445 ? 0.913 -5.854 -14.108 1.00 25.62 ? 445 LEU A CA 1 ATOM 3145 C C . LEU A 1 445 ? 1.695 -6.209 -15.341 1.00 25.43 ? 445 LEU A C 1 ATOM 3146 O O . LEU A 1 445 ? 1.400 -7.154 -16.032 1.00 25.21 ? 445 LEU A O 1 ATOM 3147 C CB . LEU A 1 445 ? 1.675 -6.475 -12.967 1.00 26.28 ? 445 LEU A CB 1 ATOM 3148 C CG . LEU A 1 445 ? 1.515 -6.061 -11.522 1.00 26.24 ? 445 LEU A CG 1 ATOM 3149 C CD1 . LEU A 1 445 ? 2.164 -7.085 -10.624 1.00 25.86 ? 445 LEU A CD1 1 ATOM 3150 C CD2 . LEU A 1 445 ? 1.901 -4.623 -11.207 1.00 25.84 ? 445 LEU A CD2 1 ATOM 3151 N N . ARG A 1 446 ? 2.712 -5.405 -15.569 1.00 24.98 ? 446 ARG A N 1 ATOM 3152 C CA . ARG A 1 446 ? 3.689 -5.625 -16.600 1.00 25.43 ? 446 ARG A CA 1 ATOM 3153 C C . ARG A 1 446 ? 5.003 -5.607 -15.933 1.00 23.95 ? 446 ARG A C 1 ATOM 3154 O O . ARG A 1 446 ? 5.430 -4.618 -15.467 1.00 22.92 ? 446 ARG A O 1 ATOM 3155 C CB . ARG A 1 446 ? 3.642 -4.680 -17.786 1.00 26.64 ? 446 ARG A CB 1 ATOM 3156 C CG . ARG A 1 446 ? 4.473 -5.223 -18.924 1.00 27.87 ? 446 ARG A CG 1 ATOM 3157 C CD . ARG A 1 446 ? 4.844 -4.236 -19.994 1.00 28.83 ? 446 ARG A CD 1 ATOM 3158 N NE . ARG A 1 446 ? 3.687 -3.653 -20.624 1.00 30.17 ? 446 ARG A NE 1 ATOM 3159 C CZ . ARG A 1 446 ? 3.709 -2.832 -21.652 1.00 30.91 ? 446 ARG A CZ 1 ATOM 3160 N NH1 . ARG A 1 446 ? 4.830 -2.487 -22.201 1.00 31.21 ? 446 ARG A NH1 1 ATOM 3161 N NH2 . ARG A 1 446 ? 2.593 -2.363 -22.125 1.00 30.28 ? 446 ARG A NH2 1 ATOM 3162 N N . LEU A 1 447 ? 5.638 -6.749 -15.883 1.00 24.68 ? 447 LEU A N 1 ATOM 3163 C CA . LEU A 1 447 ? 6.891 -6.872 -15.154 1.00 25.05 ? 447 LEU A CA 1 ATOM 3164 C C . LEU A 1 447 ? 7.933 -7.472 -16.069 1.00 26.00 ? 447 LEU A C 1 ATOM 3165 O O . LEU A 1 447 ? 7.641 -8.414 -16.797 1.00 27.24 ? 447 LEU A O 1 ATOM 3166 C CB . LEU A 1 447 ? 6.710 -7.774 -13.933 1.00 25.01 ? 447 LEU A CB 1 ATOM 3167 C CG . LEU A 1 447 ? 5.690 -7.358 -12.871 1.00 24.45 ? 447 LEU A CG 1 ATOM 3168 C CD1 . LEU A 1 447 ? 5.721 -8.360 -11.728 1.00 24.54 ? 447 LEU A CD1 1 ATOM 3169 C CD2 . LEU A 1 447 ? 5.977 -5.955 -12.360 1.00 24.22 ? 447 LEU A CD2 1 ATOM 3170 N N . PRO A 1 448 ? 9.149 -6.923 -16.053 1.00 26.56 ? 448 PRO A N 1 ATOM 3171 C CA . PRO A 1 448 ? 10.205 -7.506 -16.860 1.00 27.51 ? 448 PRO A CA 1 ATOM 3172 C C . PRO A 1 448 ? 10.718 -8.772 -16.197 1.00 29.22 ? 448 PRO A C 1 ATOM 3173 O O . PRO A 1 448 ? 10.860 -8.791 -14.981 1.00 29.68 ? 448 PRO A O 1 ATOM 3174 C CB . PRO A 1 448 ? 11.278 -6.418 -16.853 1.00 27.33 ? 448 PRO A CB 1 ATOM 3175 C CG . PRO A 1 448 ? 11.091 -5.712 -15.545 1.00 26.98 ? 448 PRO A CG 1 ATOM 3176 C CD . PRO A 1 448 ? 9.614 -5.764 -15.269 1.00 26.57 ? 448 PRO A CD 1 ATOM 3177 N N . THR A 1 449 ? 10.962 -9.824 -16.974 1.00 30.79 ? 449 THR A N 1 ATOM 3178 C CA . THR A 1 449 ? 11.591 -11.038 -16.445 1.00 32.22 ? 449 THR A CA 1 ATOM 3179 C C . THR A 1 449 ? 12.621 -11.592 -17.426 1.00 34.45 ? 449 THR A C 1 ATOM 3180 O O . THR A 1 449 ? 12.807 -11.069 -18.523 1.00 34.73 ? 449 THR A O 1 ATOM 3181 C CB . THR A 1 449 ? 10.571 -12.169 -16.131 1.00 31.40 ? 449 THR A CB 1 ATOM 3182 O OG1 . THR A 1 449 ? 10.191 -12.829 -17.338 1.00 30.00 ? 449 THR A OG1 1 ATOM 3183 C CG2 . THR A 1 449 ? 9.324 -11.643 -15.433 1.00 31.32 ? 449 THR A CG2 1 ATOM 3184 N N . SER A 1 450 ? 13.280 -12.663 -17.004 1.00 36.96 ? 450 SER A N 1 ATOM 3185 C CA . SER A 1 450 ? 14.181 -13.431 -17.858 1.00 39.26 ? 450 SER A CA 1 ATOM 3186 C C . SER A 1 450 ? 13.448 -14.057 -19.043 1.00 38.82 ? 450 SER A C 1 ATOM 3187 O O . SER A 1 450 ? 14.031 -14.223 -20.101 1.00 40.63 ? 450 SER A O 1 ATOM 3188 C CB . SER A 1 450 ? 14.835 -14.545 -17.037 1.00 39.62 ? 450 SER A CB 1 ATOM 3189 O OG . SER A 1 450 ? 13.840 -15.402 -16.483 1.00 38.89 ? 450 SER A OG 1 ATOM 3190 N N . ALA A 1 451 ? 12.174 -14.395 -18.853 1.00 39.29 ? 451 ALA A N 1 ATOM 3191 C CA . ALA A 1 451 ? 11.345 -15.015 -19.895 1.00 40.13 ? 451 ALA A CA 1 ATOM 3192 C C . ALA A 1 451 ? 10.488 -14.009 -20.680 1.00 40.05 ? 451 ALA A C 1 ATOM 3193 O O . ALA A 1 451 ? 9.396 -14.345 -21.153 1.00 40.00 ? 451 ALA A O 1 ATOM 3194 C CB . ALA A 1 451 ? 10.443 -16.068 -19.262 1.00 40.75 ? 451 ALA A CB 1 ATOM 3195 N N . GLY A 1 452 ? 10.985 -12.786 -20.827 1.00 38.74 ? 452 GLY A N 1 ATOM 3196 C CA . GLY A 1 452 ? 10.223 -11.722 -21.454 1.00 37.39 ? 452 GLY A CA 1 ATOM 3197 C C . GLY A 1 452 ? 9.459 -10.910 -20.433 1.00 35.96 ? 452 GLY A C 1 ATOM 3198 O O . GLY A 1 452 ? 9.306 -11.322 -19.289 1.00 36.92 ? 452 GLY A O 1 ATOM 3199 N N . SER A 1 453 ? 8.990 -9.742 -20.850 1.00 34.16 ? 453 SER A N 1 ATOM 3200 C CA . SER A 1 453 ? 8.148 -8.914 -20.019 1.00 33.51 ? 453 SER A CA 1 ATOM 3201 C C . SER A 1 453 ? 6.728 -9.465 -20.132 1.00 34.66 ? 453 SER A C 1 ATOM 3202 O O . SER A 1 453 ? 6.210 -9.620 -21.236 1.00 34.37 ? 453 SER A O 1 ATOM 3203 C CB . SER A 1 453 ? 8.206 -7.449 -20.464 1.00 32.76 ? 453 SER A CB 1 ATOM 3204 O OG . SER A 1 453 ? 9.512 -6.919 -20.308 1.00 31.25 ? 453 SER A OG 1 ATOM 3205 N N . VAL A 1 454 ? 6.114 -9.756 -18.985 1.00 34.57 ? 454 VAL A N 1 ATOM 3206 C CA . VAL A 1 454 ? 4.833 -10.453 -18.917 1.00 33.97 ? 454 VAL A CA 1 ATOM 3207 C C . VAL A 1 454 ? 3.709 -9.537 -18.438 1.00 32.46 ? 454 VAL A C 1 ATOM 3208 O O . VAL A 1 454 ? 3.890 -8.772 -17.489 1.00 31.53 ? 454 VAL A O 1 ATOM 3209 C CB . VAL A 1 454 ? 4.911 -11.631 -17.922 1.00 35.06 ? 454 VAL A CB 1 ATOM 3210 C CG1 . VAL A 1 454 ? 3.588 -12.385 -17.894 1.00 35.12 ? 454 VAL A CG1 1 ATOM 3211 C CG2 . VAL A 1 454 ? 6.070 -12.561 -18.269 1.00 35.46 ? 454 VAL A CG2 1 ATOM 3212 N N . THR A 1 455 ? 2.548 -9.639 -19.084 1.00 31.34 ? 455 THR A N 1 ATOM 3213 C CA . THR A 1 455 ? 1.324 -9.040 -18.571 1.00 31.46 ? 455 THR A CA 1 ATOM 3214 C C . THR A 1 455 ? 0.631 -10.032 -17.643 1.00 30.60 ? 455 THR A C 1 ATOM 3215 O O . THR A 1 455 ? 0.151 -11.073 -18.085 1.00 29.77 ? 455 THR A O 1 ATOM 3216 C CB . THR A 1 455 ? 0.367 -8.629 -19.696 1.00 31.62 ? 455 THR A CB 1 ATOM 3217 O OG1 . THR A 1 455 ? 1.033 -7.711 -20.569 1.00 33.97 ? 455 THR A OG1 1 ATOM 3218 C CG2 . THR A 1 455 ? -0.881 -7.958 -19.120 1.00 31.48 ? 455 THR A CG2 1 ATOM 3219 N N . ILE A 1 456 ? 0.588 -9.691 -16.357 1.00 30.72 ? 456 ILE A N 1 ATOM 3220 C CA . ILE A 1 456 ? 0.137 -10.600 -15.300 1.00 30.91 ? 456 ILE A CA 1 ATOM 3221 C C . ILE A 1 456 ? -1.162 -10.055 -14.723 1.00 31.42 ? 456 ILE A C 1 ATOM 3222 O O . ILE A 1 456 ? -1.210 -8.883 -14.346 1.00 31.24 ? 456 ILE A O 1 ATOM 3223 C CB . ILE A 1 456 ? 1.191 -10.698 -14.173 1.00 30.80 ? 456 ILE A CB 1 ATOM 3224 C CG1 . ILE A 1 456 ? 2.573 -11.043 -14.749 1.00 30.90 ? 456 ILE A CG1 1 ATOM 3225 C CG2 . ILE A 1 456 ? 0.788 -11.739 -13.144 1.00 30.00 ? 456 ILE A CG2 1 ATOM 3226 C CD1 . ILE A 1 456 ? 3.700 -10.949 -13.742 1.00 31.32 ? 456 ILE A CD1 1 ATOM 3227 N N . PRO A 1 457 ? -2.198 -10.909 -14.582 1.00 32.74 ? 457 PRO A N 1 ATOM 3228 C CA . PRO A 1 457 ? -2.224 -12.380 -14.715 1.00 34.45 ? 457 PRO A CA 1 ATOM 3229 C C . PRO A 1 457 ? -2.364 -12.912 -16.147 1.00 34.58 ? 457 PRO A C 1 ATOM 3230 O O . PRO A 1 457 ? -3.257 -12.488 -16.877 1.00 36.38 ? 457 PRO A O 1 ATOM 3231 C CB . PRO A 1 457 ? -3.463 -12.787 -13.884 1.00 33.94 ? 457 PRO A CB 1 ATOM 3232 C CG . PRO A 1 457 ? -3.896 -11.542 -13.168 1.00 33.53 ? 457 PRO A CG 1 ATOM 3233 C CD . PRO A 1 457 ? -3.488 -10.422 -14.071 1.00 33.17 ? 457 PRO A CD 1 ATOM 3234 N N . GLN A 1 458 ? -1.494 -13.846 -16.528 1.00 34.22 ? 458 GLN A N 1 ATOM 3235 C CA . GLN A 1 458 ? -1.546 -14.462 -17.864 1.00 33.98 ? 458 GLN A CA 1 ATOM 3236 C C . GLN A 1 458 ? -2.781 -15.340 -18.113 1.00 33.01 ? 458 GLN A C 1 ATOM 3237 O O . GLN A 1 458 ? -3.288 -15.379 -19.230 1.00 32.96 ? 458 GLN A O 1 ATOM 3238 C CB . GLN A 1 458 ? -0.308 -15.317 -18.114 1.00 33.86 ? 458 GLN A CB 1 ATOM 3239 C CG . GLN A 1 458 ? 1.005 -14.561 -18.092 1.00 34.26 ? 458 GLN A CG 1 ATOM 3240 C CD . GLN A 1 458 ? 2.165 -15.459 -18.471 1.00 33.98 ? 458 GLN A CD 1 ATOM 3241 O OE1 . GLN A 1 458 ? 3.129 -15.595 -17.730 1.00 33.21 ? 458 GLN A OE1 1 ATOM 3242 N NE2 . GLN A 1 458 ? 2.062 -16.096 -19.624 1.00 35.32 ? 458 GLN A NE2 1 ATOM 3243 N N . LEU A 1 459 ? -3.256 -16.050 -17.093 1.00 32.47 ? 459 LEU A N 1 ATOM 3244 C CA . LEU A 1 459 ? -4.316 -17.049 -17.284 1.00 34.15 ? 459 LEU A CA 1 ATOM 3245 C C . LEU A 1 459 ? -5.722 -16.531 -16.977 1.00 34.72 ? 459 LEU A C 1 ATOM 3246 O O . LEU A 1 459 ? -6.633 -17.323 -16.732 1.00 36.42 ? 459 LEU A O 1 ATOM 3247 C CB . LEU A 1 459 ? -4.023 -18.306 -16.445 1.00 34.46 ? 459 LEU A CB 1 ATOM 3248 C CG . LEU A 1 459 ? -2.606 -18.887 -16.565 1.00 34.80 ? 459 LEU A CG 1 ATOM 3249 C CD1 . LEU A 1 459 ? -2.509 -20.222 -15.835 1.00 35.37 ? 459 LEU A CD1 1 ATOM 3250 C CD2 . LEU A 1 459 ? -2.199 -19.054 -18.022 1.00 34.87 ? 459 LEU A CD2 1 ATOM 3251 N N . GLY A 1 460 ? -5.901 -15.211 -16.999 1.00 35.59 ? 460 GLY A N 1 ATOM 3252 C CA . GLY A 1 460 ? -7.208 -14.597 -16.749 1.00 34.87 ? 460 GLY A CA 1 ATOM 3253 C C . GLY A 1 460 ? -7.350 -14.044 -15.343 1.00 34.01 ? 460 GLY A C 1 ATOM 3254 O O . GLY A 1 460 ? -6.602 -14.415 -14.435 1.00 32.89 ? 460 GLY A O 1 ATOM 3255 N N . GLY A 1 461 ? -8.323 -13.153 -15.175 1.00 32.98 ? 461 GLY A N 1 ATOM 3256 C CA . GLY A 1 461 ? -8.556 -12.486 -13.905 1.00 32.54 ? 461 GLY A CA 1 ATOM 3257 C C . GLY A 1 461 ? -7.600 -11.337 -13.631 1.00 31.41 ? 461 GLY A C 1 ATOM 3258 O O . GLY A 1 461 ? -6.792 -10.952 -14.492 1.00 30.79 ? 461 GLY A O 1 ATOM 3259 N N . THR A 1 462 ? -7.698 -10.808 -12.411 1.00 29.81 ? 462 THR A N 1 ATOM 3260 C CA . THR A 1 462 ? -6.968 -9.606 -11.985 1.00 28.82 ? 462 THR A CA 1 ATOM 3261 C C . THR A 1 462 ? -6.426 -9.763 -10.565 1.00 27.75 ? 462 THR A C 1 ATOM 3262 O O . THR A 1 462 ? -6.889 -10.601 -9.790 1.00 25.70 ? 462 THR A O 1 ATOM 3263 C CB . THR A 1 462 ? -7.858 -8.335 -12.021 1.00 28.28 ? 462 THR A CB 1 ATOM 3264 O OG1 . THR A 1 462 ? -9.007 -8.524 -11.192 1.00 27.77 ? 462 THR A OG1 1 ATOM 3265 C CG2 . THR A 1 462 ? -8.322 -8.014 -13.452 1.00 28.93 ? 462 THR A CG2 1 ATOM 3266 N N . LEU A 1 463 ? -5.433 -8.943 -10.249 1.00 26.84 ? 463 LEU A N 1 ATOM 3267 C CA . LEU A 1 463 ? -4.873 -8.884 -8.910 1.00 26.73 ? 463 LEU A CA 1 ATOM 3268 C C . LEU A 1 463 ? -5.696 -7.873 -8.144 1.00 25.67 ? 463 LEU A C 1 ATOM 3269 O O . LEU A 1 463 ? -6.378 -7.055 -8.749 1.00 25.76 ? 463 LEU A O 1 ATOM 3270 C CB . LEU A 1 463 ? -3.401 -8.451 -8.948 1.00 26.69 ? 463 LEU A CB 1 ATOM 3271 C CG . LEU A 1 463 ? -2.447 -9.277 -9.822 1.00 26.80 ? 463 LEU A CG 1 ATOM 3272 C CD1 . LEU A 1 463 ? -1.091 -8.597 -9.941 1.00 26.99 ? 463 LEU A CD1 1 ATOM 3273 C CD2 . LEU A 1 463 ? -2.281 -10.683 -9.264 1.00 26.92 ? 463 LEU A CD2 1 ATOM 3274 N N . THR A 1 464 ? -5.634 -7.941 -6.820 1.00 24.88 ? 464 THR A N 1 ATOM 3275 C CA . THR A 1 464 ? -6.364 -7.020 -5.956 1.00 24.66 ? 464 THR A CA 1 ATOM 3276 C C . THR A 1 464 ? -5.480 -6.498 -4.822 1.00 23.93 ? 464 THR A C 1 ATOM 3277 O O . THR A 1 464 ? -4.671 -7.236 -4.275 1.00 23.82 ? 464 THR A O 1 ATOM 3278 C CB . THR A 1 464 ? -7.611 -7.688 -5.334 1.00 24.62 ? 464 THR A CB 1 ATOM 3279 O OG1 . THR A 1 464 ? -8.410 -8.281 -6.363 1.00 24.17 ? 464 THR A OG1 1 ATOM 3280 C CG2 . THR A 1 464 ? -8.462 -6.659 -4.602 1.00 25.25 ? 464 THR A CG2 1 ATOM 3281 N N . LEU A 1 465 ? -5.631 -5.220 -4.492 1.00 23.81 ? 465 LEU A N 1 ATOM 3282 C CA . LEU A 1 465 ? -5.007 -4.644 -3.307 1.00 24.43 ? 465 LEU A CA 1 ATOM 3283 C C . LEU A 1 465 ? -6.142 -4.108 -2.446 1.00 24.65 ? 465 LEU A C 1 ATOM 3284 O O . LEU A 1 465 ? -6.839 -3.185 -2.871 1.00 24.82 ? 465 LEU A O 1 ATOM 3285 C CB . LEU A 1 465 ? -4.035 -3.517 -3.685 1.00 25.27 ? 465 LEU A CB 1 ATOM 3286 C CG . LEU A 1 465 ? -3.163 -2.945 -2.551 1.00 25.97 ? 465 LEU A CG 1 ATOM 3287 C CD1 . LEU A 1 465 ? -2.061 -3.925 -2.155 1.00 26.06 ? 465 LEU A CD1 1 ATOM 3288 C CD2 . LEU A 1 465 ? -2.544 -1.611 -2.941 1.00 25.92 ? 465 LEU A CD2 1 ATOM 3289 N N . ASN A 1 466 ? -6.337 -4.698 -1.261 1.00 24.53 ? 466 ASN A N 1 ATOM 3290 C CA . ASN A 1 466 ? -7.436 -4.323 -0.370 1.00 25.51 ? 466 ASN A CA 1 ATOM 3291 C C . ASN A 1 466 ? -7.013 -3.349 0.725 1.00 26.11 ? 466 ASN A C 1 ATOM 3292 O O . ASN A 1 466 ? -6.367 -3.729 1.701 1.00 27.13 ? 466 ASN A O 1 ATOM 3293 C CB . ASN A 1 466 ? -8.090 -5.567 0.265 1.00 26.22 ? 466 ASN A CB 1 ATOM 3294 C CG . ASN A 1 466 ? -8.940 -6.356 -0.725 1.00 26.19 ? 466 ASN A CG 1 ATOM 3295 O OD1 . ASN A 1 466 ? -8.768 -7.561 -0.879 1.00 29.23 ? 466 ASN A OD1 1 ATOM 3296 N ND2 . ASN A 1 466 ? -9.850 -5.680 -1.398 1.00 24.78 ? 466 ASN A ND2 1 ATOM 3297 N N . GLY A 1 467 ? -7.396 -2.090 0.546 1.00 25.53 ? 467 GLY A N 1 ATOM 3298 C CA . GLY A 1 467 ? -7.242 -1.071 1.562 1.00 24.63 ? 467 GLY A CA 1 ATOM 3299 C C . GLY A 1 467 ? -5.803 -0.740 1.907 1.00 24.45 ? 467 GLY A C 1 ATOM 3300 O O . GLY A 1 467 ? -4.941 -0.594 1.022 1.00 24.14 ? 467 GLY A O 1 ATOM 3301 N N . ARG A 1 468 ? -5.551 -0.629 3.207 1.00 22.69 ? 468 ARG A N 1 ATOM 3302 C CA . ARG A 1 468 ? -4.253 -0.248 3.718 1.00 21.76 ? 468 ARG A CA 1 ATOM 3303 C C . ARG A 1 468 ? -3.379 -1.490 3.802 1.00 20.92 ? 468 ARG A C 1 ATOM 3304 O O . ARG A 1 468 ? -3.160 -2.064 4.871 1.00 19.51 ? 468 ARG A O 1 ATOM 3305 C CB . ARG A 1 468 ? -4.409 0.456 5.068 1.00 21.86 ? 468 ARG A CB 1 ATOM 3306 C CG . ARG A 1 468 ? -5.305 1.681 4.983 1.00 21.72 ? 468 ARG A CG 1 ATOM 3307 C CD . ARG A 1 468 ? -5.553 2.321 6.336 1.00 21.57 ? 468 ARG A CD 1 ATOM 3308 N NE . ARG A 1 468 ? -6.082 3.677 6.212 1.00 21.25 ? 468 ARG A NE 1 ATOM 3309 C CZ . ARG A 1 468 ? -6.434 4.432 7.246 1.00 21.34 ? 468 ARG A CZ 1 ATOM 3310 N NH1 . ARG A 1 468 ? -6.324 3.960 8.493 1.00 21.56 ? 468 ARG A NH1 1 ATOM 3311 N NH2 . ARG A 1 468 ? -6.899 5.654 7.040 1.00 20.61 ? 468 ARG A NH2 1 ATOM 3312 N N . ASP A 1 469 ? -2.905 -1.890 2.627 1.00 20.39 ? 469 ASP A N 1 ATOM 3313 C CA . ASP A 1 469 ? -2.041 -3.043 2.456 1.00 20.54 ? 469 ASP A CA 1 ATOM 3314 C C . ASP A 1 469 ? -1.010 -2.678 1.402 1.00 20.14 ? 469 ASP A C 1 ATOM 3315 O O . ASP A 1 469 ? -1.229 -1.768 0.606 1.00 18.82 ? 469 ASP A O 1 ATOM 3316 C CB . ASP A 1 469 ? -2.840 -4.285 2.017 1.00 20.54 ? 469 ASP A CB 1 ATOM 3317 C CG . ASP A 1 469 ? -1.989 -5.565 1.999 1.00 21.14 ? 469 ASP A CG 1 ATOM 3318 O OD1 . ASP A 1 469 ? -0.861 -5.535 2.532 1.00 21.09 ? 469 ASP A OD1 1 ATOM 3319 O OD2 . ASP A 1 469 ? -2.429 -6.598 1.439 1.00 21.57 -1 469 ASP A OD2 1 ATOM 3320 N N . SER A 1 470 ? 0.122 -3.374 1.445 1.00 20.30 ? 470 SER A N 1 ATOM 3321 C CA . SER A 1 470 ? 1.182 -3.246 0.464 1.00 20.77 ? 470 SER A CA 1 ATOM 3322 C C . SER A 1 470 ? 1.765 -4.647 0.199 1.00 21.63 ? 470 SER A C 1 ATOM 3323 O O . SER A 1 470 ? 1.835 -5.493 1.104 1.00 20.01 ? 470 SER A O 1 ATOM 3324 C CB . SER A 1 470 ? 2.249 -2.277 0.976 1.00 21.17 ? 470 SER A CB 1 ATOM 3325 O OG . SER A 1 470 ? 3.212 -1.957 -0.015 1.00 22.19 ? 470 SER A OG 1 ATOM 3326 N N . LYS A 1 471 ? 2.128 -4.896 -1.057 1.00 22.50 ? 471 LYS A N 1 ATOM 3327 C CA . LYS A 1 471 ? 2.743 -6.151 -1.462 1.00 23.33 ? 471 LYS A CA 1 ATOM 3328 C C . LYS A 1 471 ? 4.160 -5.925 -1.976 1.00 23.32 ? 471 LYS A C 1 ATOM 3329 O O . LYS A 1 471 ? 4.462 -4.869 -2.550 1.00 22.62 ? 471 LYS A O 1 ATOM 3330 C CB . LYS A 1 471 ? 1.943 -6.804 -2.588 1.00 24.68 ? 471 LYS A CB 1 ATOM 3331 C CG . LYS A 1 471 ? 0.441 -6.902 -2.365 1.00 25.19 ? 471 LYS A CG 1 ATOM 3332 C CD . LYS A 1 471 ? 0.091 -7.946 -1.330 1.00 25.36 ? 471 LYS A CD 1 ATOM 3333 C CE . LYS A 1 471 ? -1.415 -8.142 -1.272 1.00 26.31 ? 471 LYS A CE 1 ATOM 3334 N NZ . LYS A 1 471 ? -1.849 -9.105 -0.219 1.00 26.73 ? 471 LYS A NZ 1 ATOM 3335 N N . ILE A 1 472 ? 5.013 -6.930 -1.790 1.00 22.53 ? 472 ILE A N 1 ATOM 3336 C CA . ILE A 1 472 ? 6.274 -7.015 -2.516 1.00 22.35 ? 472 ILE A CA 1 ATOM 3337 C C . ILE A 1 472 ? 6.223 -8.182 -3.515 1.00 21.98 ? 472 ILE A C 1 ATOM 3338 O O . ILE A 1 472 ? 6.460 -9.336 -3.144 1.00 23.36 ? 472 ILE A O 1 ATOM 3339 C CB . ILE A 1 472 ? 7.468 -7.172 -1.561 1.00 22.23 ? 472 ILE A CB 1 ATOM 3340 C CG1 . ILE A 1 472 ? 7.520 -5.971 -0.613 1.00 22.67 ? 472 ILE A CG1 1 ATOM 3341 C CG2 . ILE A 1 472 ? 8.781 -7.264 -2.343 1.00 22.37 ? 472 ILE A CG2 1 ATOM 3342 C CD1 . ILE A 1 472 ? 8.689 -5.984 0.353 1.00 22.82 ? 472 ILE A CD1 1 ATOM 3343 N N . HIS A 1 473 ? 5.900 -7.881 -4.774 1.00 21.10 ? 473 HIS A N 1 ATOM 3344 C CA . HIS A 1 473 ? 5.962 -8.883 -5.838 1.00 20.33 ? 473 HIS A CA 1 ATOM 3345 C C . HIS A 1 473 ? 7.426 -9.075 -6.213 1.00 20.87 ? 473 HIS A C 1 ATOM 3346 O O . HIS A 1 473 ? 8.217 -8.124 -6.149 1.00 21.61 ? 473 HIS A O 1 ATOM 3347 C CB . HIS A 1 473 ? 5.176 -8.466 -7.080 1.00 19.83 ? 473 HIS A CB 1 ATOM 3348 C CG . HIS A 1 473 ? 3.763 -8.053 -6.810 1.00 19.55 ? 473 HIS A CG 1 ATOM 3349 N ND1 . HIS A 1 473 ? 2.880 -8.831 -6.099 1.00 19.49 ? 473 HIS A ND1 1 ATOM 3350 C CD2 . HIS A 1 473 ? 3.078 -6.945 -7.170 1.00 19.58 ? 473 HIS A CD2 1 ATOM 3351 C CE1 . HIS A 1 473 ? 1.708 -8.227 -6.039 1.00 19.60 ? 473 HIS A CE1 1 ATOM 3352 N NE2 . HIS A 1 473 ? 1.801 -7.078 -6.680 1.00 19.46 ? 473 HIS A NE2 1 ATOM 3353 N N . VAL A 1 474 ? 7.768 -10.301 -6.611 1.00 20.42 ? 474 VAL A N 1 ATOM 3354 C CA . VAL A 1 474 ? 9.134 -10.681 -6.967 1.00 20.33 ? 474 VAL A CA 1 ATOM 3355 C C . VAL A 1 474 ? 9.181 -11.232 -8.406 1.00 21.03 ? 474 VAL A C 1 ATOM 3356 O O . VAL A 1 474 ? 8.171 -11.736 -8.919 1.00 20.63 ? 474 VAL A O 1 ATOM 3357 C CB . VAL A 1 474 ? 9.692 -11.738 -5.982 1.00 20.66 ? 474 VAL A CB 1 ATOM 3358 C CG1 . VAL A 1 474 ? 9.546 -11.258 -4.542 1.00 20.95 ? 474 VAL A CG1 1 ATOM 3359 C CG2 . VAL A 1 474 ? 9.003 -13.091 -6.150 1.00 20.05 ? 474 VAL A CG2 1 ATOM 3360 N N . THR A 1 475 ? 10.339 -11.086 -9.056 1.00 20.96 ? 475 THR A N 1 ATOM 3361 C CA . THR A 1 475 ? 10.623 -11.741 -10.331 1.00 21.55 ? 475 THR A CA 1 ATOM 3362 C C . THR A 1 475 ? 12.041 -12.302 -10.330 1.00 22.11 ? 475 THR A C 1 ATOM 3363 O O . THR A 1 475 ? 12.937 -11.754 -9.670 1.00 21.77 ? 475 THR A O 1 ATOM 3364 C CB . THR A 1 475 ? 10.502 -10.794 -11.540 1.00 21.58 ? 475 THR A CB 1 ATOM 3365 O OG1 . THR A 1 475 ? 11.549 -9.830 -11.482 1.00 21.32 ? 475 THR A OG1 1 ATOM 3366 C CG2 . THR A 1 475 ? 9.141 -10.079 -11.572 1.00 21.73 ? 475 THR A CG2 1 ATOM 3367 N N . ASP A 1 476 ? 12.234 -13.380 -11.093 1.00 22.51 ? 476 ASP A N 1 ATOM 3368 C CA . ASP A 1 476 ? 13.497 -14.112 -11.123 1.00 23.61 ? 476 ASP A CA 1 ATOM 3369 C C . ASP A 1 476 ? 14.051 -14.352 -9.710 1.00 23.16 ? 476 ASP A C 1 ATOM 3370 O O . ASP A 1 476 ? 15.223 -14.134 -9.432 1.00 23.85 ? 476 ASP A O 1 ATOM 3371 C CB . ASP A 1 476 ? 14.496 -13.388 -12.028 1.00 24.66 ? 476 ASP A CB 1 ATOM 3372 C CG . ASP A 1 476 ? 14.049 -13.383 -13.499 1.00 26.37 ? 476 ASP A CG 1 ATOM 3373 O OD1 . ASP A 1 476 ? 13.543 -14.423 -13.985 1.00 26.89 ? 476 ASP A OD1 1 ATOM 3374 O OD2 . ASP A 1 476 ? 14.182 -12.335 -14.170 1.00 29.05 -1 476 ASP A OD2 1 ATOM 3375 N N . TYR A 1 477 ? 13.175 -14.811 -8.827 1.00 22.67 ? 477 TYR A N 1 ATOM 3376 C CA . TYR A 1 477 ? 13.514 -15.051 -7.439 1.00 22.31 ? 477 TYR A CA 1 ATOM 3377 C C . TYR A 1 477 ? 14.122 -16.452 -7.297 1.00 22.65 ? 477 TYR A C 1 ATOM 3378 O O . TYR A 1 477 ? 13.493 -17.449 -7.641 1.00 20.77 ? 477 TYR A O 1 ATOM 3379 C CB . TYR A 1 477 ? 12.257 -14.907 -6.580 1.00 21.71 ? 477 TYR A CB 1 ATOM 3380 C CG . TYR A 1 477 ? 12.513 -14.973 -5.094 1.00 21.26 ? 477 TYR A CG 1 ATOM 3381 C CD1 . TYR A 1 477 ? 12.881 -13.837 -4.382 1.00 20.81 ? 477 TYR A CD1 1 ATOM 3382 C CD2 . TYR A 1 477 ? 12.378 -16.169 -4.397 1.00 20.83 ? 477 TYR A CD2 1 ATOM 3383 C CE1 . TYR A 1 477 ? 13.116 -13.887 -3.017 1.00 20.53 ? 477 TYR A CE1 1 ATOM 3384 C CE2 . TYR A 1 477 ? 12.624 -16.231 -3.031 1.00 21.31 ? 477 TYR A CE2 1 ATOM 3385 C CZ . TYR A 1 477 ? 12.980 -15.081 -2.341 1.00 20.71 ? 477 TYR A CZ 1 ATOM 3386 O OH . TYR A 1 477 ? 13.216 -15.131 -0.981 1.00 21.17 ? 477 TYR A OH 1 ATOM 3387 N N . ASN A 1 478 ? 15.347 -16.494 -6.783 1.00 24.43 ? 478 ASN A N 1 ATOM 3388 C CA . ASN A 1 478 ? 16.146 -17.706 -6.676 1.00 26.91 ? 478 ASN A CA 1 ATOM 3389 C C . ASN A 1 478 ? 15.808 -18.520 -5.423 1.00 27.43 ? 478 ASN A C 1 ATOM 3390 O O . ASN A 1 478 ? 16.067 -18.080 -4.302 1.00 26.74 ? 478 ASN A O 1 ATOM 3391 C CB . ASN A 1 478 ? 17.629 -17.298 -6.634 1.00 29.79 ? 478 ASN A CB 1 ATOM 3392 C CG . ASN A 1 478 ? 18.595 -18.476 -6.744 1.00 32.97 ? 478 ASN A CG 1 ATOM 3393 O OD1 . ASN A 1 478 ? 18.211 -19.609 -7.045 1.00 33.58 ? 478 ASN A OD1 1 ATOM 3394 N ND2 . ASN A 1 478 ? 19.883 -18.192 -6.495 1.00 38.50 ? 478 ASN A ND2 1 ATOM 3395 N N . VAL A 1 479 ? 15.239 -19.708 -5.613 1.00 27.08 ? 479 VAL A N 1 ATOM 3396 C CA . VAL A 1 479 ? 15.107 -20.675 -4.532 1.00 26.66 ? 479 VAL A CA 1 ATOM 3397 C C . VAL A 1 479 ? 16.175 -21.752 -4.733 1.00 27.81 ? 479 VAL A C 1 ATOM 3398 O O . VAL A 1 479 ? 15.921 -22.809 -5.317 1.00 26.96 ? 479 VAL A O 1 ATOM 3399 C CB . VAL A 1 479 ? 13.703 -21.287 -4.509 1.00 27.19 ? 479 VAL A CB 1 ATOM 3400 C CG1 . VAL A 1 479 ? 13.544 -22.250 -3.333 1.00 27.31 ? 479 VAL A CG1 1 ATOM 3401 C CG2 . VAL A 1 479 ? 12.665 -20.179 -4.453 1.00 27.58 ? 479 VAL A CG2 1 ATOM 3402 N N . SER A 1 480 ? 17.387 -21.441 -4.283 1.00 29.92 ? 480 SER A N 1 ATOM 3403 C CA . SER A 1 480 ? 18.532 -22.344 -4.373 1.00 31.42 ? 480 SER A CA 1 ATOM 3404 C C . SER A 1 480 ? 18.566 -23.099 -5.694 1.00 31.85 ? 480 SER A C 1 ATOM 3405 O O . SER A 1 480 ? 18.431 -24.313 -5.715 1.00 31.14 ? 480 SER A O 1 ATOM 3406 C CB . SER A 1 480 ? 18.520 -23.334 -3.203 1.00 32.08 ? 480 SER A CB 1 ATOM 3407 O OG . SER A 1 480 ? 19.766 -23.996 -3.070 1.00 33.72 ? 480 SER A OG 1 ATOM 3408 N N . GLY A 1 481 ? 18.728 -22.362 -6.792 1.00 32.76 ? 481 GLY A N 1 ATOM 3409 C CA . GLY A 1 481 ? 18.862 -22.963 -8.122 1.00 32.31 ? 481 GLY A CA 1 ATOM 3410 C C . GLY A 1 481 ? 17.585 -22.980 -8.948 1.00 31.43 ? 481 GLY A C 1 ATOM 3411 O O . GLY A 1 481 ? 17.640 -22.851 -10.164 1.00 33.62 ? 481 GLY A O 1 ATOM 3412 N N . THR A 1 482 ? 16.436 -23.167 -8.306 1.00 29.14 ? 482 THR A N 1 ATOM 3413 C CA . THR A 1 482 ? 15.163 -23.090 -8.999 1.00 27.48 ? 482 THR A CA 1 ATOM 3414 C C . THR A 1 482 ? 14.738 -21.626 -9.070 1.00 26.38 ? 482 THR A C 1 ATOM 3415 O O . THR A 1 482 ? 14.715 -20.912 -8.051 1.00 25.55 ? 482 THR A O 1 ATOM 3416 C CB . THR A 1 482 ? 14.085 -23.924 -8.296 1.00 28.35 ? 482 THR A CB 1 ATOM 3417 O OG1 . THR A 1 482 ? 14.556 -25.269 -8.134 1.00 29.06 ? 482 THR A OG1 1 ATOM 3418 C CG2 . THR A 1 482 ? 12.793 -23.939 -9.107 1.00 28.64 ? 482 THR A CG2 1 ATOM 3419 N N . ASN A 1 483 ? 14.433 -21.184 -10.287 1.00 24.64 ? 483 ASN A N 1 ATOM 3420 C CA . ASN A 1 483 ? 14.091 -19.803 -10.556 1.00 23.74 ? 483 ASN A CA 1 ATOM 3421 C C . ASN A 1 483 ? 12.589 -19.604 -10.644 1.00 23.16 ? 483 ASN A C 1 ATOM 3422 O O . ASN A 1 483 ? 11.926 -20.177 -11.508 1.00 23.62 ? 483 ASN A O 1 ATOM 3423 C CB . ASN A 1 483 ? 14.717 -19.353 -11.863 1.00 24.11 ? 483 ASN A CB 1 ATOM 3424 C CG . ASN A 1 483 ? 14.490 -17.884 -12.128 1.00 24.58 ? 483 ASN A CG 1 ATOM 3425 O OD1 . ASN A 1 483 ? 14.839 -17.030 -11.302 1.00 25.31 ? 483 ASN A OD1 1 ATOM 3426 N ND2 . ASN A 1 483 ? 13.895 -17.575 -13.269 1.00 24.48 ? 483 ASN A ND2 1 ATOM 3427 N N . ILE A 1 484 ? 12.054 -18.794 -9.742 1.00 22.25 ? 484 ILE A N 1 ATOM 3428 C CA . ILE A 1 484 ? 10.669 -18.382 -9.829 1.00 21.91 ? 484 ILE A CA 1 ATOM 3429 C C . ILE A 1 484 ? 10.654 -17.156 -10.721 1.00 21.76 ? 484 ILE A C 1 ATOM 3430 O O . ILE A 1 484 ? 11.164 -16.091 -10.349 1.00 22.64 ? 484 ILE A O 1 ATOM 3431 C CB . ILE A 1 484 ? 10.064 -18.073 -8.448 1.00 22.12 ? 484 ILE A CB 1 ATOM 3432 C CG1 . ILE A 1 484 ? 10.309 -19.243 -7.486 1.00 22.65 ? 484 ILE A CG1 1 ATOM 3433 C CG2 . ILE A 1 484 ? 8.566 -17.796 -8.563 1.00 22.56 ? 484 ILE A CG2 1 ATOM 3434 C CD1 . ILE A 1 484 ? 9.893 -20.598 -8.017 1.00 22.63 ? 484 ILE A CD1 1 ATOM 3435 N N . ILE A 1 485 ? 10.096 -17.297 -11.909 1.00 21.20 ? 485 ILE A N 1 ATOM 3436 C CA . ILE A 1 485 ? 10.010 -16.235 -12.892 1.00 20.76 ? 485 ILE A CA 1 ATOM 3437 C C . ILE A 1 485 ? 9.277 -15.063 -12.311 1.00 20.20 ? 485 ILE A C 1 ATOM 3438 O O . ILE A 1 485 ? 9.698 -13.977 -12.417 1.00 19.99 ? 485 ILE A O 1 ATOM 3439 C CB . ILE A 1 485 ? 9.401 -16.749 -14.202 1.00 20.50 ? 485 ILE A CB 1 ATOM 3440 C CG1 . ILE A 1 485 ? 10.255 -17.896 -14.727 1.00 20.79 ? 485 ILE A CG1 1 ATOM 3441 C CG2 . ILE A 1 485 ? 9.159 -15.628 -15.200 1.00 20.23 ? 485 ILE A CG2 1 ATOM 3442 C CD1 . ILE A 1 485 ? 9.620 -18.734 -15.778 1.00 20.62 ? 485 ILE A CD1 1 ATOM 3443 N N . TYR A 1 486 ? 8.186 -15.349 -11.646 1.00 20.53 ? 486 TYR A N 1 ATOM 3444 C CA . TYR A 1 486 ? 7.435 -14.353 -10.931 1.00 20.17 ? 486 TYR A CA 1 ATOM 3445 C C . TYR A 1 486 ? 6.457 -14.956 -9.977 1.00 19.80 ? 486 TYR A C 1 ATOM 3446 O O . TYR A 1 486 ? 6.009 -16.036 -10.180 1.00 19.71 ? 486 TYR A O 1 ATOM 3447 C CB . TYR A 1 486 ? 6.708 -13.377 -11.851 1.00 19.43 ? 486 TYR A CB 1 ATOM 3448 C CG . TYR A 1 486 ? 5.571 -13.953 -12.616 1.00 19.10 ? 486 TYR A CG 1 ATOM 3449 C CD1 . TYR A 1 486 ? 4.342 -14.176 -12.016 1.00 19.05 ? 486 TYR A CD1 1 ATOM 3450 C CD2 . TYR A 1 486 ? 5.708 -14.237 -13.930 1.00 18.92 ? 486 TYR A CD2 1 ATOM 3451 C CE1 . TYR A 1 486 ? 3.303 -14.707 -12.709 1.00 18.81 ? 486 TYR A CE1 1 ATOM 3452 C CE2 . TYR A 1 486 ? 4.675 -14.754 -14.646 1.00 19.18 ? 486 TYR A CE2 1 ATOM 3453 C CZ . TYR A 1 486 ? 3.476 -14.993 -14.034 1.00 19.51 ? 486 TYR A CZ 1 ATOM 3454 O OH . TYR A 1 486 ? 2.494 -15.505 -14.780 1.00 18.38 ? 486 TYR A OH 1 ATOM 3455 N N . SER A 1 487 ? 6.137 -14.200 -8.947 1.00 18.88 ? 487 SER A N 1 ATOM 3456 C CA . SER A 1 487 ? 5.108 -14.517 -8.004 1.00 18.56 ? 487 SER A CA 1 ATOM 3457 C C . SER A 1 487 ? 4.452 -13.225 -7.531 1.00 18.84 ? 487 SER A C 1 ATOM 3458 O O . SER A 1 487 ? 5.109 -12.324 -7.118 1.00 18.44 ? 487 SER A O 1 ATOM 3459 C CB . SER A 1 487 ? 5.570 -15.378 -6.858 1.00 18.71 ? 487 SER A CB 1 ATOM 3460 O OG . SER A 1 487 ? 4.544 -15.604 -5.978 1.00 18.99 ? 487 SER A OG 1 ATOM 3461 N N . THR A 1 488 ? 3.142 -13.163 -7.622 1.00 18.94 ? 488 THR A N 1 ATOM 3462 C CA . THR A 1 488 ? 2.410 -12.014 -7.167 1.00 19.44 ? 488 THR A CA 1 ATOM 3463 C C . THR A 1 488 ? 2.178 -12.170 -5.659 1.00 20.53 ? 488 THR A C 1 ATOM 3464 O O . THR A 1 488 ? 2.268 -11.237 -4.937 1.00 20.61 ? 488 THR A O 1 ATOM 3465 C CB . THR A 1 488 ? 1.133 -11.691 -7.969 1.00 19.19 ? 488 THR A CB 1 ATOM 3466 O OG1 . THR A 1 488 ? 0.202 -12.728 -7.854 1.00 19.27 ? 488 THR A OG1 1 ATOM 3467 C CG2 . THR A 1 488 ? 1.451 -11.477 -9.378 1.00 19.31 ? 488 THR A CG2 1 ATOM 3468 N N . ALA A 1 489 ? 1.887 -13.385 -5.235 1.00 21.50 ? 489 ALA A N 1 ATOM 3469 C CA . ALA A 1 489 ? 1.808 -13.713 -3.808 1.00 21.52 ? 489 ALA A CA 1 ATOM 3470 C C . ALA A 1 489 ? 3.166 -13.516 -3.172 1.00 21.67 ? 489 ALA A C 1 ATOM 3471 O O . ALA A 1 489 ? 4.186 -13.829 -3.788 1.00 21.78 ? 489 ALA A O 1 ATOM 3472 C CB . ALA A 1 489 ? 1.352 -15.146 -3.610 1.00 21.34 ? 489 ALA A CB 1 ATOM 3473 N N . GLU A 1 490 ? 3.168 -13.014 -1.938 1.00 21.31 ? 490 GLU A N 1 ATOM 3474 C CA . GLU A 1 490 ? 4.396 -12.679 -1.234 1.00 21.04 ? 490 GLU A CA 1 ATOM 3475 C C . GLU A 1 490 ? 5.055 -13.895 -0.614 1.00 20.36 ? 490 GLU A C 1 ATOM 3476 O O . GLU A 1 490 ? 4.385 -14.809 -0.151 1.00 21.19 ? 490 GLU A O 1 ATOM 3477 C CB . GLU A 1 490 ? 4.122 -11.655 -0.137 1.00 21.80 ? 490 GLU A CB 1 ATOM 3478 C CG . GLU A 1 490 ? 3.469 -10.380 -0.653 1.00 23.19 ? 490 GLU A CG 1 ATOM 3479 C CD . GLU A 1 490 ? 3.351 -9.323 0.416 1.00 23.70 ? 490 GLU A CD 1 ATOM 3480 O OE1 . GLU A 1 490 ? 2.288 -9.279 1.080 1.00 24.93 ? 490 GLU A OE1 1 ATOM 3481 O OE2 . GLU A 1 490 ? 4.330 -8.555 0.595 1.00 22.92 -1 490 GLU A OE2 1 ATOM 3482 N N . VAL A 1 491 ? 6.381 -13.856 -0.579 1.00 19.36 ? 491 VAL A N 1 ATOM 3483 C CA . VAL A 1 491 ? 7.212 -14.919 -0.040 1.00 19.13 ? 491 VAL A CA 1 ATOM 3484 C C . VAL A 1 491 ? 7.315 -14.782 1.477 1.00 19.47 ? 491 VAL A C 1 ATOM 3485 O O . VAL A 1 491 ? 7.658 -13.704 1.985 1.00 19.49 ? 491 VAL A O 1 ATOM 3486 C CB . VAL A 1 491 ? 8.628 -14.811 -0.634 1.00 18.80 ? 491 VAL A CB 1 ATOM 3487 C CG1 . VAL A 1 491 ? 9.590 -15.792 0.015 1.00 19.01 ? 491 VAL A CG1 1 ATOM 3488 C CG2 . VAL A 1 491 ? 8.577 -15.002 -2.139 1.00 19.10 ? 491 VAL A CG2 1 ATOM 3489 N N . PHE A 1 492 ? 7.011 -15.864 2.192 1.00 19.18 ? 492 PHE A N 1 ATOM 3490 C CA . PHE A 1 492 ? 7.238 -15.922 3.639 1.00 19.40 ? 492 PHE A CA 1 ATOM 3491 C C . PHE A 1 492 ? 8.649 -16.430 3.897 1.00 19.11 ? 492 PHE A C 1 ATOM 3492 O O . PHE A 1 492 ? 9.429 -15.786 4.594 1.00 19.07 ? 492 PHE A O 1 ATOM 3493 C CB . PHE A 1 492 ? 6.208 -16.831 4.348 1.00 19.67 ? 492 PHE A CB 1 ATOM 3494 C CG . PHE A 1 492 ? 6.505 -17.051 5.818 1.00 20.33 ? 492 PHE A CG 1 ATOM 3495 C CD1 . PHE A 1 492 ? 6.645 -15.972 6.681 1.00 20.51 ? 492 PHE A CD1 1 ATOM 3496 C CD2 . PHE A 1 492 ? 6.666 -18.330 6.331 1.00 21.49 ? 492 PHE A CD2 1 ATOM 3497 C CE1 . PHE A 1 492 ? 6.931 -16.163 8.021 1.00 21.25 ? 492 PHE A CE1 1 ATOM 3498 C CE2 . PHE A 1 492 ? 6.961 -18.535 7.680 1.00 21.64 ? 492 PHE A CE2 1 ATOM 3499 C CZ . PHE A 1 492 ? 7.081 -17.450 8.527 1.00 21.57 ? 492 PHE A CZ 1 ATOM 3500 N N . THR A 1 493 ? 8.950 -17.604 3.345 1.00 19.23 ? 493 THR A N 1 ATOM 3501 C CA . THR A 1 493 ? 10.277 -18.198 3.426 1.00 19.69 ? 493 THR A CA 1 ATOM 3502 C C . THR A 1 493 ? 10.453 -19.307 2.363 1.00 19.49 ? 493 THR A C 1 ATOM 3503 O O . THR A 1 493 ? 9.498 -19.703 1.682 1.00 18.29 ? 493 THR A O 1 ATOM 3504 C CB . THR A 1 493 ? 10.545 -18.754 4.842 1.00 20.16 ? 493 THR A CB 1 ATOM 3505 O OG1 . THR A 1 493 ? 11.939 -19.026 4.997 1.00 20.79 ? 493 THR A OG1 1 ATOM 3506 C CG2 . THR A 1 493 ? 9.756 -20.022 5.094 1.00 20.66 ? 493 THR A CG2 1 ATOM 3507 N N . TRP A 1 494 ? 11.686 -19.769 2.205 1.00 19.34 ? 494 TRP A N 1 ATOM 3508 C CA . TRP A 1 494 ? 11.975 -20.944 1.388 1.00 20.02 ? 494 TRP A CA 1 ATOM 3509 C C . TRP A 1 494 ? 13.183 -21.633 1.983 1.00 20.93 ? 494 TRP A C 1 ATOM 3510 O O . TRP A 1 494 ? 14.041 -20.967 2.579 1.00 19.79 ? 494 TRP A O 1 ATOM 3511 C CB . TRP A 1 494 ? 12.255 -20.569 -0.082 1.00 19.79 ? 494 TRP A CB 1 ATOM 3512 C CG . TRP A 1 494 ? 13.446 -19.672 -0.264 1.00 19.21 ? 494 TRP A CG 1 ATOM 3513 C CD1 . TRP A 1 494 ? 13.434 -18.305 -0.326 1.00 19.24 ? 494 TRP A CD1 1 ATOM 3514 C CD2 . TRP A 1 494 ? 14.822 -20.064 -0.384 1.00 19.04 ? 494 TRP A CD2 1 ATOM 3515 N NE1 . TRP A 1 494 ? 14.707 -17.825 -0.484 1.00 19.16 ? 494 TRP A NE1 1 ATOM 3516 C CE2 . TRP A 1 494 ? 15.583 -18.877 -0.515 1.00 19.06 ? 494 TRP A CE2 1 ATOM 3517 C CE3 . TRP A 1 494 ? 15.487 -21.296 -0.380 1.00 18.67 ? 494 TRP A CE3 1 ATOM 3518 C CZ2 . TRP A 1 494 ? 16.979 -18.886 -0.649 1.00 18.81 ? 494 TRP A CZ2 1 ATOM 3519 C CZ3 . TRP A 1 494 ? 16.866 -21.307 -0.508 1.00 18.61 ? 494 TRP A CZ3 1 ATOM 3520 C CH2 . TRP A 1 494 ? 17.601 -20.106 -0.640 1.00 18.97 ? 494 TRP A CH2 1 ATOM 3521 N N . LYS A 1 495 ? 13.251 -22.957 1.830 1.00 22.21 ? 495 LYS A N 1 ATOM 3522 C CA . LYS A 1 495 ? 14.430 -23.712 2.261 1.00 23.07 ? 495 LYS A CA 1 ATOM 3523 C C . LYS A 1 495 ? 14.770 -24.808 1.273 1.00 25.05 ? 495 LYS A C 1 ATOM 3524 O O . LYS A 1 495 ? 13.901 -25.269 0.542 1.00 24.79 ? 495 LYS A O 1 ATOM 3525 C CB . LYS A 1 495 ? 14.206 -24.345 3.639 1.00 22.60 ? 495 LYS A CB 1 ATOM 3526 C CG . LYS A 1 495 ? 13.957 -23.361 4.780 1.00 21.57 ? 495 LYS A CG 1 ATOM 3527 C CD . LYS A 1 495 ? 15.167 -22.491 5.090 1.00 21.13 ? 495 LYS A CD 1 ATOM 3528 C CE . LYS A 1 495 ? 14.751 -21.167 5.730 1.00 21.08 ? 495 LYS A CE 1 ATOM 3529 N NZ . LYS A 1 495 ? 15.871 -20.196 5.839 1.00 21.29 ? 495 LYS A NZ 1 ATOM 3530 N N . LYS A 1 496 ? 16.045 -25.205 1.274 1.00 27.43 ? 496 LYS A N 1 ATOM 3531 C CA . LYS A 1 496 ? 16.535 -26.366 0.538 1.00 30.42 ? 496 LYS A CA 1 ATOM 3532 C C . LYS A 1 496 ? 16.803 -27.496 1.528 1.00 30.96 ? 496 LYS A C 1 ATOM 3533 O O . LYS A 1 496 ? 17.688 -27.382 2.380 1.00 28.90 ? 496 LYS A O 1 ATOM 3534 C CB . LYS A 1 496 ? 17.831 -26.012 -0.188 1.00 33.38 ? 496 LYS A CB 1 ATOM 3535 C CG . LYS A 1 496 ? 18.439 -27.107 -1.065 1.00 35.83 ? 496 LYS A CG 1 ATOM 3536 C CD . LYS A 1 496 ? 19.881 -26.759 -1.433 1.00 38.47 ? 496 LYS A CD 1 ATOM 3537 C CE . LYS A 1 496 ? 20.212 -26.990 -2.907 1.00 41.35 ? 496 LYS A CE 1 ATOM 3538 N NZ . LYS A 1 496 ? 20.330 -28.435 -3.248 1.00 42.96 ? 496 LYS A NZ 1 ATOM 3539 N N . PHE A 1 497 ? 16.038 -28.580 1.421 1.00 32.06 ? 497 PHE A N 1 ATOM 3540 C CA . PHE A 1 497 ? 16.248 -29.751 2.278 1.00 33.57 ? 497 PHE A CA 1 ATOM 3541 C C . PHE A 1 497 ? 16.971 -30.851 1.509 1.00 36.02 ? 497 PHE A C 1 ATOM 3542 O O . PHE A 1 497 ? 17.139 -30.770 0.293 1.00 36.08 ? 497 PHE A O 1 ATOM 3543 C CB . PHE A 1 497 ? 14.916 -30.261 2.843 1.00 31.86 ? 497 PHE A CB 1 ATOM 3544 C CG . PHE A 1 497 ? 14.133 -29.209 3.576 1.00 31.22 ? 497 PHE A CG 1 ATOM 3545 C CD1 . PHE A 1 497 ? 14.689 -28.549 4.666 1.00 30.45 ? 497 PHE A CD1 1 ATOM 3546 C CD2 . PHE A 1 497 ? 12.843 -28.875 3.181 1.00 31.13 ? 497 PHE A CD2 1 ATOM 3547 C CE1 . PHE A 1 497 ? 13.984 -27.568 5.343 1.00 30.47 ? 497 PHE A CE1 1 ATOM 3548 C CE2 . PHE A 1 497 ? 12.128 -27.897 3.855 1.00 31.34 ? 497 PHE A CE2 1 ATOM 3549 C CZ . PHE A 1 497 ? 12.696 -27.241 4.939 1.00 30.85 ? 497 PHE A CZ 1 ATOM 3550 N N . ALA A 1 498 ? 17.414 -31.870 2.236 1.00 40.51 ? 498 ALA A N 1 ATOM 3551 C CA . ALA A 1 498 ? 18.088 -33.028 1.639 1.00 41.93 ? 498 ALA A CA 1 ATOM 3552 C C . ALA A 1 498 ? 17.246 -33.625 0.517 1.00 43.07 ? 498 ALA A C 1 ATOM 3553 O O . ALA A 1 498 ? 17.771 -33.963 -0.540 1.00 41.71 ? 498 ALA A O 1 ATOM 3554 C CB . ALA A 1 498 ? 18.370 -34.079 2.703 1.00 41.63 ? 498 ALA A CB 1 ATOM 3555 N N . ASP A 1 499 ? 15.938 -33.727 0.755 1.00 45.02 ? 499 ASP A N 1 ATOM 3556 C CA . ASP A 1 499 ? 14.993 -34.258 -0.228 1.00 47.24 ? 499 ASP A CA 1 ATOM 3557 C C . ASP A 1 499 ? 14.075 -33.169 -0.831 1.00 47.12 ? 499 ASP A C 1 ATOM 3558 O O . ASP A 1 499 ? 12.847 -33.238 -0.701 1.00 48.48 ? 499 ASP A O 1 ATOM 3559 C CB . ASP A 1 499 ? 14.138 -35.350 0.427 1.00 49.72 ? 499 ASP A CB 1 ATOM 3560 C CG . ASP A 1 499 ? 13.206 -34.800 1.502 1.00 51.82 ? 499 ASP A CG 1 ATOM 3561 O OD1 . ASP A 1 499 ? 13.561 -33.767 2.120 1.00 51.93 ? 499 ASP A OD1 1 ATOM 3562 O OD2 . ASP A 1 499 ? 12.120 -35.393 1.715 1.00 53.65 -1 499 ASP A OD2 1 ATOM 3563 N N . GLY A 1 500 ? 14.667 -32.170 -1.485 1.00 43.20 ? 500 GLY A N 1 ATOM 3564 C CA . GLY A 1 500 ? 13.893 -31.156 -2.207 1.00 40.26 ? 500 GLY A CA 1 ATOM 3565 C C . GLY A 1 500 ? 13.700 -29.826 -1.487 1.00 38.64 ? 500 GLY A C 1 ATOM 3566 O O . GLY A 1 500 ? 14.012 -29.671 -0.301 1.00 38.38 ? 500 GLY A O 1 ATOM 3567 N N . LYS A 1 501 ? 13.159 -28.865 -2.226 1.00 35.00 ? 501 LYS A N 1 ATOM 3568 C CA . LYS A 1 501 ? 12.998 -27.498 -1.755 1.00 34.29 ? 501 LYS A CA 1 ATOM 3569 C C . LYS A 1 501 ? 11.560 -27.225 -1.328 1.00 31.84 ? 501 LYS A C 1 ATOM 3570 O O . LYS A 1 501 ? 10.637 -27.877 -1.806 1.00 31.69 ? 501 LYS A O 1 ATOM 3571 C CB . LYS A 1 501 ? 13.388 -26.528 -2.875 1.00 34.85 ? 501 LYS A CB 1 ATOM 3572 C CG . LYS A 1 501 ? 14.819 -26.709 -3.360 1.00 35.72 ? 501 LYS A CG 1 ATOM 3573 C CD . LYS A 1 501 ? 14.967 -26.479 -4.855 1.00 35.81 ? 501 LYS A CD 1 ATOM 3574 C CE . LYS A 1 501 ? 16.350 -26.914 -5.319 1.00 36.71 ? 501 LYS A CE 1 ATOM 3575 N NZ . LYS A 1 501 ? 16.561 -26.709 -6.779 1.00 37.20 ? 501 LYS A NZ 1 ATOM 3576 N N . VAL A 1 502 ? 11.380 -26.257 -0.431 1.00 29.38 ? 502 VAL A N 1 ATOM 3577 C CA . VAL A 1 502 ? 10.050 -25.767 -0.090 1.00 28.21 ? 502 VAL A CA 1 ATOM 3578 C C . VAL A 1 502 ? 10.025 -24.244 -0.123 1.00 26.19 ? 502 VAL A C 1 ATOM 3579 O O . VAL A 1 502 ? 10.984 -23.584 0.255 1.00 26.57 ? 502 VAL A O 1 ATOM 3580 C CB . VAL A 1 502 ? 9.575 -26.268 1.288 1.00 28.66 ? 502 VAL A CB 1 ATOM 3581 C CG1 . VAL A 1 502 ? 8.164 -25.772 1.580 1.00 29.23 ? 502 VAL A CG1 1 ATOM 3582 C CG2 . VAL A 1 502 ? 9.615 -27.786 1.338 1.00 28.83 ? 502 VAL A CG2 1 ATOM 3583 N N . LEU A 1 503 ? 8.914 -23.715 -0.611 1.00 24.82 ? 503 LEU A N 1 ATOM 3584 C CA . LEU A 1 503 ? 8.668 -22.295 -0.713 1.00 23.79 ? 503 LEU A CA 1 ATOM 3585 C C . LEU A 1 503 ? 7.299 -22.046 -0.113 1.00 23.40 ? 503 LEU A C 1 ATOM 3586 O O . LEU A 1 503 ? 6.355 -22.817 -0.353 1.00 23.08 ? 503 LEU A O 1 ATOM 3587 C CB . LEU A 1 503 ? 8.670 -21.880 -2.181 1.00 23.72 ? 503 LEU A CB 1 ATOM 3588 C CG . LEU A 1 503 ? 8.211 -20.467 -2.561 1.00 23.35 ? 503 LEU A CG 1 ATOM 3589 C CD1 . LEU A 1 503 ? 9.069 -19.366 -1.943 1.00 23.26 ? 503 LEU A CD1 1 ATOM 3590 C CD2 . LEU A 1 503 ? 8.208 -20.347 -4.079 1.00 23.22 ? 503 LEU A CD2 1 ATOM 3591 N N . VAL A 1 504 ? 7.196 -20.984 0.675 1.00 22.44 ? 504 VAL A N 1 ATOM 3592 C CA . VAL A 1 504 ? 5.941 -20.604 1.302 1.00 22.10 ? 504 VAL A CA 1 ATOM 3593 C C . VAL A 1 504 ? 5.488 -19.227 0.832 1.00 21.26 ? 504 VAL A C 1 ATOM 3594 O O . VAL A 1 504 ? 6.210 -18.255 0.986 1.00 21.92 ? 504 VAL A O 1 ATOM 3595 C CB . VAL A 1 504 ? 6.082 -20.585 2.830 1.00 22.54 ? 504 VAL A CB 1 ATOM 3596 C CG1 . VAL A 1 504 ? 4.725 -20.304 3.490 1.00 22.51 ? 504 VAL A CG1 1 ATOM 3597 C CG2 . VAL A 1 504 ? 6.686 -21.908 3.305 1.00 23.05 ? 504 VAL A CG2 1 ATOM 3598 N N . LEU A 1 505 ? 4.281 -19.170 0.279 1.00 20.78 ? 505 LEU A N 1 ATOM 3599 C CA . LEU A 1 505 ? 3.704 -17.960 -0.302 1.00 19.93 ? 505 LEU A CA 1 ATOM 3600 C C . LEU A 1 505 ? 2.355 -17.702 0.329 1.00 19.45 ? 505 LEU A C 1 ATOM 3601 O O . LEU A 1 505 ? 1.630 -18.648 0.645 1.00 18.16 ? 505 LEU A O 1 ATOM 3602 C CB . LEU A 1 505 ? 3.466 -18.141 -1.798 1.00 20.21 ? 505 LEU A CB 1 ATOM 3603 C CG . LEU A 1 505 ? 4.649 -18.507 -2.681 1.00 20.22 ? 505 LEU A CG 1 ATOM 3604 C CD1 . LEU A 1 505 ? 4.166 -18.712 -4.107 1.00 21.06 ? 505 LEU A CD1 1 ATOM 3605 C CD2 . LEU A 1 505 ? 5.714 -17.440 -2.625 1.00 20.30 ? 505 LEU A CD2 1 ATOM 3606 N N . TYR A 1 506 ? 2.007 -16.422 0.481 1.00 19.02 ? 506 TYR A N 1 ATOM 3607 C CA . TYR A 1 506 ? 0.716 -16.052 1.021 1.00 18.59 ? 506 TYR A CA 1 ATOM 3608 C C . TYR A 1 506 ? 0.097 -14.863 0.308 1.00 18.62 ? 506 TYR A C 1 ATOM 3609 O O . TYR A 1 506 ? 0.784 -14.023 -0.269 1.00 18.07 ? 506 TYR A O 1 ATOM 3610 C CB . TYR A 1 506 ? 0.842 -15.753 2.527 1.00 18.93 ? 506 TYR A CB 1 ATOM 3611 C CG . TYR A 1 506 ? 1.665 -14.523 2.838 1.00 18.58 ? 506 TYR A CG 1 ATOM 3612 C CD1 . TYR A 1 506 ? 3.046 -14.595 2.914 1.00 18.25 ? 506 TYR A CD1 1 ATOM 3613 C CD2 . TYR A 1 506 ? 1.060 -13.282 3.020 1.00 19.14 ? 506 TYR A CD2 1 ATOM 3614 C CE1 . TYR A 1 506 ? 3.799 -13.475 3.179 1.00 18.61 ? 506 TYR A CE1 1 ATOM 3615 C CE2 . TYR A 1 506 ? 1.814 -12.143 3.280 1.00 19.04 ? 506 TYR A CE2 1 ATOM 3616 C CZ . TYR A 1 506 ? 3.179 -12.255 3.364 1.00 18.78 ? 506 TYR A CZ 1 ATOM 3617 O OH . TYR A 1 506 ? 3.940 -11.148 3.618 1.00 19.95 ? 506 TYR A OH 1 ATOM 3618 N N . GLY A 1 507 ? -1.223 -14.801 0.390 1.00 18.89 ? 507 GLY A N 1 ATOM 3619 C CA . GLY A 1 507 ? -1.983 -13.642 -0.012 1.00 19.96 ? 507 GLY A CA 1 ATOM 3620 C C . GLY A 1 507 ? -3.071 -13.382 1.004 1.00 20.58 ? 507 GLY A C 1 ATOM 3621 O O . GLY A 1 507 ? -3.341 -14.222 1.860 1.00 20.27 ? 507 GLY A O 1 ATOM 3622 N N . GLY A 1 508 ? -3.664 -12.199 0.930 1.00 21.40 ? 508 GLY A N 1 ATOM 3623 C CA . GLY A 1 508 ? -4.792 -11.839 1.782 1.00 22.74 ? 508 GLY A CA 1 ATOM 3624 C C . GLY A 1 508 ? -6.102 -12.347 1.204 1.00 23.94 ? 508 GLY A C 1 ATOM 3625 O O . GLY A 1 508 ? -6.188 -12.675 0.002 1.00 23.50 ? 508 GLY A O 1 ATOM 3626 N N . ALA A 1 509 ? -7.131 -12.394 2.048 1.00 24.03 ? 509 ALA A N 1 ATOM 3627 C CA . ALA A 1 509 ? -8.431 -12.955 1.654 1.00 24.76 ? 509 ALA A CA 1 ATOM 3628 C C . ALA A 1 509 ? -9.044 -12.264 0.429 1.00 24.66 ? 509 ALA A C 1 ATOM 3629 O O . ALA A 1 509 ? -8.964 -11.046 0.280 1.00 24.35 ? 509 ALA A O 1 ATOM 3630 C CB . ALA A 1 509 ? -9.407 -12.894 2.821 1.00 24.87 ? 509 ALA A CB 1 ATOM 3631 N N . GLY A 1 510 ? -9.651 -13.062 -0.442 1.00 25.19 ? 510 GLY A N 1 ATOM 3632 C CA . GLY A 1 510 ? -10.369 -12.548 -1.605 1.00 25.71 ? 510 GLY A CA 1 ATOM 3633 C C . GLY A 1 510 ? -9.505 -12.334 -2.834 1.00 26.03 ? 510 GLY A C 1 ATOM 3634 O O . GLY A 1 510 ? -10.022 -11.960 -3.890 1.00 27.90 ? 510 GLY A O 1 ATOM 3635 N N . GLU A 1 511 ? -8.203 -12.595 -2.707 1.00 24.68 ? 511 GLU A N 1 ATOM 3636 C CA . GLU A 1 511 ? -7.234 -12.306 -3.748 1.00 24.18 ? 511 GLU A CA 1 ATOM 3637 C C . GLU A 1 511 ? -6.994 -13.515 -4.663 1.00 24.86 ? 511 GLU A C 1 ATOM 3638 O O . GLU A 1 511 ? -6.888 -14.672 -4.198 1.00 23.27 ? 511 GLU A O 1 ATOM 3639 C CB . GLU A 1 511 ? -5.895 -11.868 -3.119 1.00 24.29 ? 511 GLU A CB 1 ATOM 3640 C CG . GLU A 1 511 ? -5.959 -10.585 -2.283 1.00 24.35 ? 511 GLU A CG 1 ATOM 3641 C CD . GLU A 1 511 ? -4.645 -10.261 -1.565 1.00 25.01 ? 511 GLU A CD 1 ATOM 3642 O OE1 . GLU A 1 511 ? -3.625 -10.958 -1.817 1.00 24.03 ? 511 GLU A OE1 1 ATOM 3643 O OE2 . GLU A 1 511 ? -4.624 -9.320 -0.726 1.00 24.29 -1 511 GLU A OE2 1 ATOM 3644 N N . HIS A 1 512 ? -6.897 -13.225 -5.963 1.00 24.64 ? 512 HIS A N 1 ATOM 3645 C CA . HIS A 1 512 ? -6.383 -14.171 -6.958 1.00 24.47 ? 512 HIS A CA 1 ATOM 3646 C C . HIS A 1 512 ? -4.901 -13.874 -7.227 1.00 23.56 ? 512 HIS A C 1 ATOM 3647 O O . HIS A 1 512 ? -4.528 -12.712 -7.427 1.00 22.20 ? 512 HIS A O 1 ATOM 3648 C CB . HIS A 1 512 ? -7.173 -14.053 -8.268 1.00 24.73 ? 512 HIS A CB 1 ATOM 3649 C CG . HIS A 1 512 ? -6.612 -14.884 -9.378 1.00 25.07 ? 512 HIS A CG 1 ATOM 3650 N ND1 . HIS A 1 512 ? -6.892 -16.225 -9.515 1.00 25.50 ? 512 HIS A ND1 1 ATOM 3651 C CD2 . HIS A 1 512 ? -5.772 -14.569 -10.393 1.00 25.69 ? 512 HIS A CD2 1 ATOM 3652 C CE1 . HIS A 1 512 ? -6.257 -16.700 -10.572 1.00 25.62 ? 512 HIS A CE1 1 ATOM 3653 N NE2 . HIS A 1 512 ? -5.571 -15.715 -11.122 1.00 26.18 ? 512 HIS A NE2 1 ATOM 3654 N N . HIS A 1 513 ? -4.072 -14.920 -7.258 1.00 23.08 ? 513 HIS A N 1 ATOM 3655 C CA . HIS A 1 513 ? -2.622 -14.766 -7.464 1.00 23.36 ? 513 HIS A CA 1 ATOM 3656 C C . HIS A 1 513 ? -2.061 -15.672 -8.542 1.00 23.11 ? 513 HIS A C 1 ATOM 3657 O O . HIS A 1 513 ? -2.702 -16.640 -8.956 1.00 23.53 ? 513 HIS A O 1 ATOM 3658 C CB . HIS A 1 513 ? -1.866 -15.011 -6.156 1.00 23.34 ? 513 HIS A CB 1 ATOM 3659 C CG . HIS A 1 513 ? -1.859 -13.826 -5.253 1.00 23.08 ? 513 HIS A CG 1 ATOM 3660 N ND1 . HIS A 1 513 ? -1.206 -12.658 -5.577 1.00 23.63 ? 513 HIS A ND1 1 ATOM 3661 C CD2 . HIS A 1 513 ? -2.452 -13.608 -4.057 1.00 22.87 ? 513 HIS A CD2 1 ATOM 3662 C CE1 . HIS A 1 513 ? -1.392 -11.770 -4.618 1.00 23.23 ? 513 HIS A CE1 1 ATOM 3663 N NE2 . HIS A 1 513 ? -2.144 -12.322 -3.683 1.00 23.43 ? 513 HIS A NE2 1 ATOM 3664 N N . GLU A 1 514 ? -0.850 -15.358 -8.985 1.00 22.60 ? 514 GLU A N 1 ATOM 3665 C CA . GLU A 1 514 ? -0.208 -16.134 -10.041 1.00 22.04 ? 514 GLU A CA 1 ATOM 3666 C C . GLU A 1 514 ? 1.297 -16.217 -9.873 1.00 21.70 ? 514 GLU A C 1 ATOM 3667 O O . GLU A 1 514 ? 1.944 -15.272 -9.416 1.00 20.62 ? 514 GLU A O 1 ATOM 3668 C CB . GLU A 1 514 ? -0.547 -15.540 -11.405 1.00 23.22 ? 514 GLU A CB 1 ATOM 3669 C CG . GLU A 1 514 ? -0.411 -16.519 -12.565 1.00 23.72 ? 514 GLU A CG 1 ATOM 3670 C CD . GLU A 1 514 ? -0.835 -15.909 -13.888 1.00 24.29 ? 514 GLU A CD 1 ATOM 3671 O OE1 . GLU A 1 514 ? -0.013 -15.194 -14.512 1.00 24.03 ? 514 GLU A OE1 1 ATOM 3672 O OE2 . GLU A 1 514 ? -1.992 -16.150 -14.299 1.00 24.54 -1 514 GLU A OE2 1 ATOM 3673 N N . LEU A 1 515 ? 1.846 -17.371 -10.228 1.00 22.84 ? 515 LEU A N 1 ATOM 3674 C CA . LEU A 1 515 ? 3.292 -17.554 -10.278 1.00 23.57 ? 515 LEU A CA 1 ATOM 3675 C C . LEU A 1 515 ? 3.694 -18.289 -11.563 1.00 23.68 ? 515 LEU A C 1 ATOM 3676 O O . LEU A 1 515 ? 2.847 -18.800 -12.297 1.00 23.00 ? 515 LEU A O 1 ATOM 3677 C CB . LEU A 1 515 ? 3.788 -18.314 -9.044 1.00 24.14 ? 515 LEU A CB 1 ATOM 3678 C CG . LEU A 1 515 ? 3.334 -19.769 -8.854 1.00 25.31 ? 515 LEU A CG 1 ATOM 3679 C CD1 . LEU A 1 515 ? 4.125 -20.748 -9.721 1.00 25.90 ? 515 LEU A CD1 1 ATOM 3680 C CD2 . LEU A 1 515 ? 3.450 -20.190 -7.395 1.00 26.09 ? 515 LEU A CD2 1 ATOM 3681 N N . ALA A 1 516 ? 4.995 -18.321 -11.814 1.00 23.55 ? 516 ALA A N 1 ATOM 3682 C CA . ALA A 1 516 ? 5.562 -19.033 -12.941 1.00 24.13 ? 516 ALA A CA 1 ATOM 3683 C C . ALA A 1 516 ? 6.978 -19.448 -12.581 1.00 24.93 ? 516 ALA A C 1 ATOM 3684 O O . ALA A 1 516 ? 7.703 -18.705 -11.914 1.00 25.57 ? 516 ALA A O 1 ATOM 3685 C CB . ALA A 1 516 ? 5.565 -18.159 -14.193 1.00 23.78 ? 516 ALA A CB 1 ATOM 3686 N N . ILE A 1 517 ? 7.363 -20.632 -13.050 1.00 25.63 ? 517 ILE A N 1 ATOM 3687 C CA . ILE A 1 517 ? 8.580 -21.301 -12.622 1.00 25.78 ? 517 ILE A CA 1 ATOM 3688 C C . ILE A 1 517 ? 9.362 -21.766 -13.841 1.00 26.29 ? 517 ILE A C 1 ATOM 3689 O O . ILE A 1 517 ? 8.769 -22.272 -14.774 1.00 25.16 ? 517 ILE A O 1 ATOM 3690 C CB . ILE A 1 517 ? 8.200 -22.528 -11.773 1.00 25.13 ? 517 ILE A CB 1 ATOM 3691 C CG1 . ILE A 1 517 ? 7.424 -22.071 -10.542 1.00 25.28 ? 517 ILE A CG1 1 ATOM 3692 C CG2 . ILE A 1 517 ? 9.427 -23.343 -11.391 1.00 25.02 ? 517 ILE A CG2 1 ATOM 3693 C CD1 . ILE A 1 517 ? 6.959 -23.202 -9.656 1.00 26.05 ? 517 ILE A CD1 1 ATOM 3694 N N . SER A 1 518 ? 10.685 -21.606 -13.824 1.00 27.54 ? 518 SER A N 1 ATOM 3695 C CA . SER A 1 518 ? 11.533 -22.153 -14.885 1.00 29.92 ? 518 SER A CA 1 ATOM 3696 C C . SER A 1 518 ? 11.724 -23.659 -14.670 1.00 31.09 ? 518 SER A C 1 ATOM 3697 O O . SER A 1 518 ? 12.422 -24.078 -13.745 1.00 30.04 ? 518 SER A O 1 ATOM 3698 C CB . SER A 1 518 ? 12.895 -21.463 -14.912 1.00 29.51 ? 518 SER A CB 1 ATOM 3699 O OG . SER A 1 518 ? 12.736 -20.068 -14.943 1.00 31.46 ? 518 SER A OG 1 ATOM 3700 N N . THR A 1 519 ? 11.112 -24.463 -15.532 1.00 33.91 ? 519 THR A N 1 ATOM 3701 C CA . THR A 1 519 ? 11.080 -25.915 -15.344 1.00 36.44 ? 519 THR A CA 1 ATOM 3702 C C . THR A 1 519 ? 10.582 -26.628 -16.600 1.00 38.46 ? 519 THR A C 1 ATOM 3703 O O . THR A 1 519 ? 9.878 -26.037 -17.424 1.00 37.78 ? 519 THR A O 1 ATOM 3704 C CB . THR A 1 519 ? 10.151 -26.291 -14.163 1.00 36.40 ? 519 THR A CB 1 ATOM 3705 O OG1 . THR A 1 519 ? 10.148 -27.708 -13.969 1.00 37.11 ? 519 THR A OG1 1 ATOM 3706 C CG2 . THR A 1 519 ? 8.713 -25.827 -14.426 1.00 35.97 ? 519 THR A CG2 1 ATOM 3707 N N . LYS A 1 520 ? 10.964 -27.897 -16.730 1.00 42.81 ? 520 LYS A N 1 ATOM 3708 C CA . LYS A 1 520 ? 10.371 -28.815 -17.708 1.00 45.03 ? 520 LYS A CA 1 ATOM 3709 C C . LYS A 1 520 ? 9.256 -29.645 -17.064 1.00 45.94 ? 520 LYS A C 1 ATOM 3710 O O . LYS A 1 520 ? 8.474 -30.299 -17.764 1.00 45.72 ? 520 LYS A O 1 ATOM 3711 C CB . LYS A 1 520 ? 11.429 -29.771 -18.267 1.00 46.33 ? 520 LYS A CB 1 ATOM 3712 C CG . LYS A 1 520 ? 12.660 -29.099 -18.857 1.00 48.47 ? 520 LYS A CG 1 ATOM 3713 C CD . LYS A 1 520 ? 12.312 -28.222 -20.054 1.00 50.26 ? 520 LYS A CD 1 ATOM 3714 C CE . LYS A 1 520 ? 13.569 -27.664 -20.714 1.00 51.09 ? 520 LYS A CE 1 ATOM 3715 N NZ . LYS A 1 520 ? 13.274 -26.541 -21.648 1.00 50.55 ? 520 LYS A NZ 1 ATOM 3716 N N . SER A 1 521 ? 9.178 -29.620 -15.733 1.00 45.34 ? 521 SER A N 1 ATOM 3717 C CA . SER A 1 521 ? 8.239 -30.472 -15.019 1.00 45.13 ? 521 SER A CA 1 ATOM 3718 C C . SER A 1 521 ? 6.852 -29.874 -14.953 1.00 45.14 ? 521 SER A C 1 ATOM 3719 O O . SER A 1 521 ? 6.652 -28.665 -15.094 1.00 42.89 ? 521 SER A O 1 ATOM 3720 C CB . SER A 1 521 ? 8.735 -30.765 -13.610 1.00 45.82 ? 521 SER A CB 1 ATOM 3721 O OG . SER A 1 521 ? 9.969 -31.452 -13.670 1.00 47.97 ? 521 SER A OG 1 ATOM 3722 N N . ASN A 1 522 ? 5.893 -30.755 -14.725 1.00 46.80 ? 522 ASN A N 1 ATOM 3723 C CA . ASN A 1 522 ? 4.498 -30.382 -14.648 1.00 48.50 ? 522 ASN A CA 1 ATOM 3724 C C . ASN A 1 522 ? 4.113 -29.986 -13.225 1.00 43.59 ? 522 ASN A C 1 ATOM 3725 O O . ASN A 1 522 ? 4.856 -30.259 -12.285 1.00 40.82 ? 522 ASN A O 1 ATOM 3726 C CB . ASN A 1 522 ? 3.662 -31.568 -15.096 1.00 53.25 ? 522 ASN A CB 1 ATOM 3727 C CG . ASN A 1 522 ? 2.223 -31.202 -15.374 1.00 60.50 ? 522 ASN A CG 1 ATOM 3728 O OD1 . ASN A 1 522 ? 1.899 -30.048 -15.691 1.00 57.04 ? 522 ASN A OD1 1 ATOM 3729 N ND2 . ASN A 1 522 ? 1.346 -32.196 -15.251 1.00 69.84 ? 522 ASN A ND2 1 ATOM 3730 N N . VAL A 1 523 ? 2.956 -29.343 -13.078 1.00 40.58 ? 523 VAL A N 1 ATOM 3731 C CA . VAL A 1 523 ? 2.404 -29.028 -11.760 1.00 39.57 ? 523 VAL A CA 1 ATOM 3732 C C . VAL A 1 523 ? 1.350 -30.050 -11.316 1.00 37.67 ? 523 VAL A C 1 ATOM 3733 O O . VAL A 1 523 ? 0.432 -30.390 -12.062 1.00 37.01 ? 523 VAL A O 1 ATOM 3734 C CB . VAL A 1 523 ? 1.818 -27.588 -11.698 1.00 39.05 ? 523 VAL A CB 1 ATOM 3735 C CG1 . VAL A 1 523 ? 0.549 -27.446 -12.531 1.00 39.12 ? 523 VAL A CG1 1 ATOM 3736 C CG2 . VAL A 1 523 ? 1.544 -27.189 -10.256 1.00 39.02 ? 523 VAL A CG2 1 ATOM 3737 N N . THR A 1 524 ? 1.494 -30.533 -10.088 1.00 36.64 ? 524 THR A N 1 ATOM 3738 C CA . THR A 1 524 ? 0.502 -31.418 -9.490 1.00 36.75 ? 524 THR A CA 1 ATOM 3739 C C . THR A 1 524 ? 0.158 -30.929 -8.080 1.00 34.92 ? 524 THR A C 1 ATOM 3740 O O . THR A 1 524 ? 1.037 -30.575 -7.300 1.00 35.03 ? 524 THR A O 1 ATOM 3741 C CB . THR A 1 524 ? 0.975 -32.896 -9.467 1.00 38.00 ? 524 THR A CB 1 ATOM 3742 O OG1 . THR A 1 524 ? 2.114 -33.046 -8.611 1.00 37.39 ? 524 THR A OG1 1 ATOM 3743 C CG2 . THR A 1 524 ? 1.347 -33.377 -10.887 1.00 39.48 ? 524 THR A CG2 1 ATOM 3744 N N . VAL A 1 525 ? -1.135 -30.893 -7.783 1.00 33.41 ? 525 VAL A N 1 ATOM 3745 C CA . VAL A 1 525 ? -1.640 -30.518 -6.474 1.00 33.64 ? 525 VAL A CA 1 ATOM 3746 C C . VAL A 1 525 ? -1.511 -31.711 -5.527 1.00 33.57 ? 525 VAL A C 1 ATOM 3747 O O . VAL A 1 525 ? -2.220 -32.699 -5.688 1.00 34.33 ? 525 VAL A O 1 ATOM 3748 C CB . VAL A 1 525 ? -3.117 -30.089 -6.582 1.00 33.89 ? 525 VAL A CB 1 ATOM 3749 C CG1 . VAL A 1 525 ? -3.718 -29.795 -5.208 1.00 33.94 ? 525 VAL A CG1 1 ATOM 3750 C CG2 . VAL A 1 525 ? -3.229 -28.884 -7.500 1.00 34.64 ? 525 VAL A CG2 1 ATOM 3751 N N . ILE A 1 526 ? -0.615 -31.610 -4.546 1.00 33.31 ? 526 ILE A N 1 ATOM 3752 C CA . ILE A 1 526 ? -0.384 -32.701 -3.571 1.00 32.94 ? 526 ILE A CA 1 ATOM 3753 C C . ILE A 1 526 ? -1.127 -32.544 -2.225 1.00 32.31 ? 526 ILE A C 1 ATOM 3754 O O . ILE A 1 526 ? -1.214 -33.498 -1.454 1.00 31.87 ? 526 ILE A O 1 ATOM 3755 C CB . ILE A 1 526 ? 1.129 -32.949 -3.311 1.00 32.20 ? 526 ILE A CB 1 ATOM 3756 C CG1 . ILE A 1 526 ? 1.816 -31.711 -2.708 1.00 32.26 ? 526 ILE A CG1 1 ATOM 3757 C CG2 . ILE A 1 526 ? 1.824 -33.382 -4.598 1.00 31.47 ? 526 ILE A CG2 1 ATOM 3758 C CD1 . ILE A 1 526 ? 3.259 -31.952 -2.302 1.00 31.99 ? 526 ILE A CD1 1 ATOM 3759 N N . GLU A 1 527 ? -1.644 -31.356 -1.932 1.00 31.52 ? 527 GLU A N 1 ATOM 3760 C CA . GLU A 1 527 ? -2.534 -31.193 -0.789 1.00 33.00 ? 527 GLU A CA 1 ATOM 3761 C C . GLU A 1 527 ? -3.624 -30.199 -1.125 1.00 33.21 ? 527 GLU A C 1 ATOM 3762 O O . GLU A 1 527 ? -3.340 -29.122 -1.644 1.00 33.74 ? 527 GLU A O 1 ATOM 3763 C CB . GLU A 1 527 ? -1.770 -30.734 0.460 1.00 34.47 ? 527 GLU A CB 1 ATOM 3764 C CG . GLU A 1 527 ? -2.513 -31.036 1.760 1.00 36.03 ? 527 GLU A CG 1 ATOM 3765 C CD . GLU A 1 527 ? -1.946 -30.302 2.971 1.00 38.18 ? 527 GLU A CD 1 ATOM 3766 O OE1 . GLU A 1 527 ? -1.135 -30.910 3.710 1.00 40.82 ? 527 GLU A OE1 1 ATOM 3767 O OE2 . GLU A 1 527 ? -2.316 -29.123 3.185 1.00 36.24 -1 527 GLU A OE2 1 ATOM 3768 N N . GLY A 1 528 ? -4.867 -30.567 -0.827 1.00 35.27 ? 528 GLY A N 1 ATOM 3769 C CA . GLY A 1 528 ? -6.029 -29.724 -1.106 1.00 36.90 ? 528 GLY A CA 1 ATOM 3770 C C . GLY A 1 528 ? -6.754 -30.119 -2.381 1.00 39.18 ? 528 GLY A C 1 ATOM 3771 O O . GLY A 1 528 ? -6.502 -31.183 -2.947 1.00 38.20 ? 528 GLY A O 1 ATOM 3772 N N . SER A 1 529 ? -7.657 -29.248 -2.827 1.00 41.63 ? 529 SER A N 1 ATOM 3773 C CA . SER A 1 529 ? -8.465 -29.479 -4.023 1.00 44.49 ? 529 SER A CA 1 ATOM 3774 C C . SER A 1 529 ? -7.858 -28.764 -5.239 1.00 47.01 ? 529 SER A C 1 ATOM 3775 O O . SER A 1 529 ? -7.198 -27.734 -5.088 1.00 47.91 ? 529 SER A O 1 ATOM 3776 C CB . SER A 1 529 ? -9.896 -28.978 -3.771 1.00 45.36 ? 529 SER A CB 1 ATOM 3777 O OG . SER A 1 529 ? -10.794 -29.389 -4.789 1.00 45.81 ? 529 SER A OG 1 ATOM 3778 N N . GLU A 1 530 ? -8.085 -29.315 -6.435 1.00 50.21 ? 530 GLU A N 1 ATOM 3779 C CA . GLU A 1 530 ? -7.661 -28.670 -7.691 1.00 52.83 ? 530 GLU A CA 1 ATOM 3780 C C . GLU A 1 530 ? -8.576 -27.505 -8.078 1.00 51.42 ? 530 GLU A C 1 ATOM 3781 O O . GLU A 1 530 ? -8.152 -26.583 -8.767 1.00 51.10 ? 530 GLU A O 1 ATOM 3782 C CB . GLU A 1 530 ? -7.610 -29.662 -8.857 1.00 54.91 ? 530 GLU A CB 1 ATOM 3783 C CG . GLU A 1 530 ? -6.775 -30.913 -8.620 1.00 57.99 ? 530 GLU A CG 1 ATOM 3784 C CD . GLU A 1 530 ? -7.618 -32.175 -8.478 1.00 61.79 ? 530 GLU A CD 1 ATOM 3785 O OE1 . GLU A 1 530 ? -7.229 -33.206 -9.070 1.00 61.80 ? 530 GLU A OE1 1 ATOM 3786 O OE2 . GLU A 1 530 ? -8.669 -32.141 -7.786 1.00 62.67 -1 530 GLU A OE2 1 ATOM 3787 N N . SER A 1 531 ? -9.834 -27.564 -7.658 1.00 51.58 ? 531 SER A N 1 ATOM 3788 C CA . SER A 1 531 ? -10.772 -26.457 -7.842 1.00 51.40 ? 531 SER A CA 1 ATOM 3789 C C . SER A 1 531 ? -10.111 -25.110 -7.533 1.00 50.61 ? 531 SER A C 1 ATOM 3790 O O . SER A 1 531 ? -9.629 -24.898 -6.424 1.00 50.94 ? 531 SER A O 1 ATOM 3791 C CB . SER A 1 531 ? -11.993 -26.666 -6.939 1.00 52.60 ? 531 SER A CB 1 ATOM 3792 O OG . SER A 1 531 ? -12.744 -25.475 -6.789 1.00 54.48 ? 531 SER A OG 1 ATOM 3793 N N . GLY A 1 532 ? -10.073 -24.212 -8.520 1.00 50.44 ? 532 GLY A N 1 ATOM 3794 C CA . GLY A 1 532 ? -9.424 -22.894 -8.370 1.00 46.91 ? 532 GLY A CA 1 ATOM 3795 C C . GLY A 1 532 ? -7.931 -22.866 -8.691 1.00 43.94 ? 532 GLY A C 1 ATOM 3796 O O . GLY A 1 532 ? -7.321 -21.796 -8.727 1.00 44.25 ? 532 GLY A O 1 ATOM 3797 N N . ILE A 1 533 ? -7.335 -24.036 -8.905 1.00 41.89 ? 533 ILE A N 1 ATOM 3798 C CA . ILE A 1 533 ? -5.951 -24.134 -9.361 1.00 41.85 ? 533 ILE A CA 1 ATOM 3799 C C . ILE A 1 533 ? -5.923 -24.254 -10.890 1.00 41.00 ? 533 ILE A C 1 ATOM 3800 O O . ILE A 1 533 ? -6.142 -25.333 -11.441 1.00 42.13 ? 533 ILE A O 1 ATOM 3801 C CB . ILE A 1 533 ? -5.222 -25.357 -8.749 1.00 41.24 ? 533 ILE A CB 1 ATOM 3802 C CG1 . ILE A 1 533 ? -5.299 -25.349 -7.215 1.00 40.41 ? 533 ILE A CG1 1 ATOM 3803 C CG2 . ILE A 1 533 ? -3.770 -25.406 -9.216 1.00 41.55 ? 533 ILE A CG2 1 ATOM 3804 C CD1 . ILE A 1 533 ? -4.647 -24.155 -6.563 1.00 40.38 ? 533 ILE A CD1 1 ATOM 3805 N N . SER A 1 534 ? -5.672 -23.144 -11.574 1.00 39.33 ? 534 SER A N 1 ATOM 3806 C CA . SER A 1 534 ? -5.507 -23.176 -13.023 1.00 38.81 ? 534 SER A CA 1 ATOM 3807 C C . SER A 1 534 ? -4.023 -23.206 -13.342 1.00 37.27 ? 534 SER A C 1 ATOM 3808 O O . SER A 1 534 ? -3.216 -22.654 -12.589 1.00 36.32 ? 534 SER A O 1 ATOM 3809 C CB . SER A 1 534 ? -6.182 -21.965 -13.676 1.00 38.96 ? 534 SER A CB 1 ATOM 3810 O OG . SER A 1 534 ? -5.754 -20.751 -13.084 1.00 41.08 ? 534 SER A OG 1 ATOM 3811 N N . SER A 1 535 ? -3.666 -23.862 -14.444 1.00 36.79 ? 535 SER A N 1 ATOM 3812 C CA . SER A 1 535 ? -2.279 -23.900 -14.898 1.00 37.58 ? 535 SER A CA 1 ATOM 3813 C C . SER A 1 535 ? -2.122 -24.066 -16.402 1.00 37.52 ? 535 SER A C 1 ATOM 3814 O O . SER A 1 535 ? -3.058 -24.427 -17.108 1.00 36.88 ? 535 SER A O 1 ATOM 3815 C CB . SER A 1 535 ? -1.532 -25.031 -14.210 1.00 38.23 ? 535 SER A CB 1 ATOM 3816 O OG . SER A 1 535 ? -2.035 -26.276 -14.636 1.00 40.26 ? 535 SER A OG 1 ATOM 3817 N N . LYS A 1 536 ? -0.903 -23.803 -16.863 1.00 38.61 ? 536 LYS A N 1 ATOM 3818 C CA . LYS A 1 536 ? -0.525 -23.929 -18.267 1.00 40.67 ? 536 LYS A CA 1 ATOM 3819 C C . LYS A 1 536 ? 0.962 -24.246 -18.326 1.00 39.96 ? 536 LYS A C 1 ATOM 3820 O O . LYS A 1 536 ? 1.755 -23.660 -17.590 1.00 40.39 ? 536 LYS A O 1 ATOM 3821 C CB . LYS A 1 536 ? -0.813 -22.627 -19.041 1.00 42.88 ? 536 LYS A CB 1 ATOM 3822 C CG . LYS A 1 536 ? -0.593 -22.723 -20.553 1.00 45.36 ? 536 LYS A CG 1 ATOM 3823 C CD . LYS A 1 536 ? -0.937 -21.432 -21.294 1.00 48.17 ? 536 LYS A CD 1 ATOM 3824 C CE . LYS A 1 536 ? 0.123 -20.351 -21.094 1.00 50.51 ? 536 LYS A CE 1 ATOM 3825 N NZ . LYS A 1 536 ? -0.211 -19.048 -21.746 1.00 51.41 ? 536 LYS A NZ 1 ATOM 3826 N N . GLN A 1 537 ? 1.333 -25.182 -19.193 1.00 40.03 ? 537 GLN A N 1 ATOM 3827 C CA . GLN A 1 537 ? 2.728 -25.565 -19.382 1.00 40.27 ? 537 GLN A CA 1 ATOM 3828 C C . GLN A 1 537 ? 3.263 -24.982 -20.683 1.00 41.03 ? 537 GLN A C 1 ATOM 3829 O O . GLN A 1 537 ? 2.532 -24.859 -21.660 1.00 41.58 ? 537 GLN A O 1 ATOM 3830 C CB . GLN A 1 537 ? 2.864 -27.090 -19.415 1.00 41.57 ? 537 GLN A CB 1 ATOM 3831 C CG . GLN A 1 537 ? 3.358 -27.722 -18.126 1.00 42.73 ? 537 GLN A CG 1 ATOM 3832 C CD . GLN A 1 537 ? 4.318 -28.866 -18.388 1.00 43.16 ? 537 GLN A CD 1 ATOM 3833 O OE1 . GLN A 1 537 ? 3.903 -30.001 -18.606 1.00 44.40 ? 537 GLN A OE1 1 ATOM 3834 N NE2 . GLN A 1 537 ? 5.611 -28.567 -18.378 1.00 44.45 ? 537 GLN A NE2 1 ATOM 3835 N N . THR A 1 538 ? 4.537 -24.605 -20.686 1.00 42.84 ? 538 THR A N 1 ATOM 3836 C CA . THR A 1 538 ? 5.231 -24.225 -21.914 1.00 43.48 ? 538 THR A CA 1 ATOM 3837 C C . THR A 1 538 ? 6.482 -25.100 -21.996 1.00 43.18 ? 538 THR A C 1 ATOM 3838 O O . THR A 1 538 ? 6.648 -26.011 -21.183 1.00 41.79 ? 538 THR A O 1 ATOM 3839 C CB . THR A 1 538 ? 5.580 -22.711 -21.966 1.00 44.46 ? 538 THR A CB 1 ATOM 3840 O OG1 . THR A 1 538 ? 6.788 -22.445 -21.245 1.00 44.15 ? 538 THR A OG1 1 ATOM 3841 C CG2 . THR A 1 538 ? 4.451 -21.859 -21.393 1.00 45.36 ? 538 THR A CG2 1 ATOM 3842 N N . SER A 1 539 ? 7.347 -24.834 -22.974 1.00 43.03 ? 539 SER A N 1 ATOM 3843 C CA . SER A 1 539 ? 8.534 -25.661 -23.198 1.00 42.24 ? 539 SER A CA 1 ATOM 3844 C C . SER A 1 539 ? 9.581 -25.461 -22.105 1.00 40.00 ? 539 SER A C 1 ATOM 3845 O O . SER A 1 539 ? 10.347 -26.384 -21.808 1.00 39.81 ? 539 SER A O 1 ATOM 3846 C CB . SER A 1 539 ? 9.143 -25.393 -24.588 1.00 43.96 ? 539 SER A CB 1 ATOM 3847 O OG . SER A 1 539 ? 9.467 -24.022 -24.774 1.00 44.25 ? 539 SER A OG 1 ATOM 3848 N N . SER A 1 540 ? 9.601 -24.273 -21.497 1.00 37.45 ? 540 SER A N 1 ATOM 3849 C CA . SER A 1 540 ? 10.589 -23.961 -20.459 1.00 36.36 ? 540 SER A CA 1 ATOM 3850 C C . SER A 1 540 ? 9.988 -23.441 -19.142 1.00 33.83 ? 540 SER A C 1 ATOM 3851 O O . SER A 1 540 ? 10.710 -22.913 -18.295 1.00 33.23 ? 540 SER A O 1 ATOM 3852 C CB . SER A 1 540 ? 11.582 -22.935 -21.000 1.00 35.67 ? 540 SER A CB 1 ATOM 3853 O OG . SER A 1 540 ? 10.897 -21.735 -21.291 1.00 37.66 ? 540 SER A OG 1 ATOM 3854 N N . SER A 1 541 ? 8.683 -23.593 -18.957 1.00 31.19 ? 541 SER A N 1 ATOM 3855 C CA . SER A 1 541 ? 8.046 -23.085 -17.751 1.00 31.07 ? 541 SER A CA 1 ATOM 3856 C C . SER A 1 541 ? 6.644 -23.639 -17.501 1.00 30.40 ? 541 SER A C 1 ATOM 3857 O O . SER A 1 541 ? 6.012 -24.229 -18.380 1.00 28.70 ? 541 SER A O 1 ATOM 3858 C CB . SER A 1 541 ? 7.985 -21.539 -17.774 1.00 30.58 ? 541 SER A CB 1 ATOM 3859 O OG . SER A 1 541 ? 7.086 -21.053 -18.757 1.00 29.70 ? 541 SER A OG 1 ATOM 3860 N N . VAL A 1 542 ? 6.175 -23.424 -16.278 1.00 29.56 ? 542 VAL A N 1 ATOM 3861 C CA . VAL A 1 542 ? 4.795 -23.670 -15.928 1.00 29.70 ? 542 VAL A CA 1 ATOM 3862 C C . VAL A 1 542 ? 4.224 -22.416 -15.243 1.00 28.77 ? 542 VAL A C 1 ATOM 3863 O O . VAL A 1 542 ? 4.899 -21.758 -14.454 1.00 29.32 ? 542 VAL A O 1 ATOM 3864 C CB . VAL A 1 542 ? 4.671 -24.949 -15.068 1.00 31.36 ? 542 VAL A CB 1 ATOM 3865 C CG1 . VAL A 1 542 ? 5.256 -24.749 -13.676 1.00 31.87 ? 542 VAL A CG1 1 ATOM 3866 C CG2 . VAL A 1 542 ? 3.224 -25.412 -15.005 1.00 32.10 ? 542 VAL A CG2 1 ATOM 3867 N N . VAL A 1 543 ? 2.998 -22.063 -15.594 1.00 27.63 ? 543 VAL A N 1 ATOM 3868 C CA . VAL A 1 543 ? 2.342 -20.903 -15.038 1.00 27.39 ? 543 VAL A CA 1 ATOM 3869 C C . VAL A 1 543 ? 1.189 -21.432 -14.195 1.00 27.09 ? 543 VAL A C 1 ATOM 3870 O O . VAL A 1 543 ? 0.414 -22.278 -14.661 1.00 26.71 ? 543 VAL A O 1 ATOM 3871 C CB . VAL A 1 543 ? 1.832 -19.947 -16.156 1.00 28.13 ? 543 VAL A CB 1 ATOM 3872 C CG1 . VAL A 1 543 ? 1.039 -18.774 -15.577 1.00 27.96 ? 543 VAL A CG1 1 ATOM 3873 C CG2 . VAL A 1 543 ? 2.996 -19.414 -16.990 1.00 27.89 ? 543 VAL A CG2 1 ATOM 3874 N N . VAL A 1 544 ? 1.081 -20.944 -12.956 1.00 25.56 ? 544 VAL A N 1 ATOM 3875 C CA . VAL A 1 544 ? 0.037 -21.401 -12.037 1.00 25.30 ? 544 VAL A CA 1 ATOM 3876 C C . VAL A 1 544 ? -0.715 -20.238 -11.409 1.00 24.76 ? 544 VAL A C 1 ATOM 3877 O O . VAL A 1 544 ? -0.108 -19.304 -10.893 1.00 23.87 ? 544 VAL A O 1 ATOM 3878 C CB . VAL A 1 544 ? 0.612 -22.252 -10.893 1.00 25.12 ? 544 VAL A CB 1 ATOM 3879 C CG1 . VAL A 1 544 ? -0.515 -22.807 -10.026 1.00 25.05 ? 544 VAL A CG1 1 ATOM 3880 C CG2 . VAL A 1 544 ? 1.476 -23.374 -11.442 1.00 25.51 ? 544 VAL A CG2 1 ATOM 3881 N N . GLY A 1 545 ? -2.038 -20.318 -11.451 1.00 24.93 ? 545 GLY A N 1 ATOM 3882 C CA . GLY A 1 545 ? -2.901 -19.302 -10.864 1.00 25.73 ? 545 GLY A CA 1 ATOM 3883 C C . GLY A 1 545 ? -3.710 -19.934 -9.750 1.00 25.96 ? 545 GLY A C 1 ATOM 3884 O O . GLY A 1 545 ? -4.073 -21.098 -9.844 1.00 27.06 ? 545 GLY A O 1 ATOM 3885 N N . TRP A 1 546 ? -3.987 -19.171 -8.697 1.00 26.08 ? 546 TRP A N 1 ATOM 3886 C CA . TRP A 1 546 ? -4.686 -19.698 -7.524 1.00 26.01 ? 546 TRP A CA 1 ATOM 3887 C C . TRP A 1 546 ? -5.396 -18.601 -6.767 1.00 26.51 ? 546 TRP A C 1 ATOM 3888 O O . TRP A 1 546 ? -4.964 -17.453 -6.769 1.00 27.02 ? 546 TRP A O 1 ATOM 3889 C CB . TRP A 1 546 ? -3.710 -20.428 -6.585 1.00 25.66 ? 546 TRP A CB 1 ATOM 3890 C CG . TRP A 1 546 ? -2.577 -19.584 -6.012 1.00 24.77 ? 546 TRP A CG 1 ATOM 3891 C CD1 . TRP A 1 546 ? -1.474 -19.123 -6.675 1.00 24.79 ? 546 TRP A CD1 1 ATOM 3892 C CD2 . TRP A 1 546 ? -2.435 -19.145 -4.654 1.00 24.03 ? 546 TRP A CD2 1 ATOM 3893 N NE1 . TRP A 1 546 ? -0.667 -18.406 -5.815 1.00 24.58 ? 546 TRP A NE1 1 ATOM 3894 C CE2 . TRP A 1 546 ? -1.239 -18.403 -4.573 1.00 23.86 ? 546 TRP A CE2 1 ATOM 3895 C CE3 . TRP A 1 546 ? -3.219 -19.283 -3.499 1.00 24.00 ? 546 TRP A CE3 1 ATOM 3896 C CZ2 . TRP A 1 546 ? -0.803 -17.826 -3.387 1.00 23.26 ? 546 TRP A CZ2 1 ATOM 3897 C CZ3 . TRP A 1 546 ? -2.779 -18.706 -2.322 1.00 22.85 ? 546 TRP A CZ3 1 ATOM 3898 C CH2 . TRP A 1 546 ? -1.585 -17.988 -2.276 1.00 23.05 ? 546 TRP A CH2 1 ATOM 3899 N N . ASP A 1 547 ? -6.490 -18.968 -6.117 1.00 27.42 ? 547 ASP A N 1 ATOM 3900 C CA . ASP A 1 547 ? -7.224 -18.051 -5.257 1.00 27.55 ? 547 ASP A CA 1 ATOM 3901 C C . ASP A 1 547 ? -6.905 -18.351 -3.805 1.00 26.20 ? 547 ASP A C 1 ATOM 3902 O O . ASP A 1 547 ? -6.775 -19.524 -3.409 1.00 25.62 ? 547 ASP A O 1 ATOM 3903 C CB . ASP A 1 547 ? -8.718 -18.189 -5.518 1.00 29.00 ? 547 ASP A CB 1 ATOM 3904 C CG . ASP A 1 547 ? -9.076 -17.886 -6.963 1.00 30.35 ? 547 ASP A CG 1 ATOM 3905 O OD1 . ASP A 1 547 ? -8.762 -16.768 -7.419 1.00 30.50 ? 547 ASP A OD1 1 ATOM 3906 O OD2 . ASP A 1 547 ? -9.640 -18.775 -7.646 1.00 32.85 -1 547 ASP A OD2 1 ATOM 3907 N N . VAL A 1 548 ? -6.773 -17.289 -3.016 1.00 25.20 ? 548 VAL A N 1 ATOM 3908 C CA . VAL A 1 548 ? -6.439 -17.413 -1.599 1.00 24.29 ? 548 VAL A CA 1 ATOM 3909 C C . VAL A 1 548 ? -7.601 -18.061 -0.870 1.00 24.75 ? 548 VAL A C 1 ATOM 3910 O O . VAL A 1 548 ? -8.767 -17.680 -1.046 1.00 25.61 ? 548 VAL A O 1 ATOM 3911 C CB . VAL A 1 548 ? -6.137 -16.048 -0.953 1.00 24.08 ? 548 VAL A CB 1 ATOM 3912 C CG1 . VAL A 1 548 ? -6.012 -16.172 0.566 1.00 23.42 ? 548 VAL A CG1 1 ATOM 3913 C CG2 . VAL A 1 548 ? -4.864 -15.462 -1.541 1.00 23.97 ? 548 VAL A CG2 1 ATOM 3914 N N . SER A 1 549 ? -7.277 -19.045 -0.051 1.00 23.71 ? 549 SER A N 1 ATOM 3915 C CA . SER A 1 549 ? -8.284 -19.770 0.695 1.00 23.86 ? 549 SER A CA 1 ATOM 3916 C C . SER A 1 549 ? -7.814 -19.962 2.133 1.00 23.16 ? 549 SER A C 1 ATOM 3917 O O . SER A 1 549 ? -6.616 -20.001 2.408 1.00 22.29 ? 549 SER A O 1 ATOM 3918 C CB . SER A 1 549 ? -8.537 -21.128 0.016 1.00 24.16 ? 549 SER A CB 1 ATOM 3919 O OG . SER A 1 549 ? -9.000 -22.102 0.935 1.00 25.53 ? 549 SER A OG 1 ATOM 3920 N N . THR A 1 550 ? -8.764 -20.113 3.043 1.00 23.94 ? 550 THR A N 1 ATOM 3921 C CA . THR A 1 550 ? -8.440 -20.524 4.408 1.00 25.19 ? 550 THR A CA 1 ATOM 3922 C C . THR A 1 550 ? -7.877 -21.959 4.426 1.00 25.76 ? 550 THR A C 1 ATOM 3923 O O . THR A 1 550 ? -7.163 -22.336 5.350 1.00 26.42 ? 550 THR A O 1 ATOM 3924 C CB . THR A 1 550 ? -9.651 -20.363 5.358 1.00 25.75 ? 550 THR A CB 1 ATOM 3925 O OG1 . THR A 1 550 ? -10.781 -21.090 4.861 1.00 25.56 ? 550 THR A OG1 1 ATOM 3926 C CG2 . THR A 1 550 ? -10.036 -18.878 5.479 1.00 25.86 ? 550 THR A CG2 1 ATOM 3927 N N . THR A 1 551 ? -8.160 -22.745 3.388 1.00 25.73 ? 551 THR A N 1 ATOM 3928 C CA . THR A 1 551 ? -7.575 -24.081 3.277 1.00 26.09 ? 551 THR A CA 1 ATOM 3929 C C . THR A 1 551 ? -6.256 -24.004 2.536 1.00 25.28 ? 551 THR A C 1 ATOM 3930 O O . THR A 1 551 ? -6.183 -23.444 1.430 1.00 27.13 ? 551 THR A O 1 ATOM 3931 C CB . THR A 1 551 ? -8.516 -25.054 2.538 1.00 25.81 ? 551 THR A CB 1 ATOM 3932 O OG1 . THR A 1 551 ? -9.805 -25.010 3.149 1.00 26.31 ? 551 THR A OG1 1 ATOM 3933 C CG2 . THR A 1 551 ? -7.993 -26.479 2.607 1.00 26.11 ? 551 THR A CG2 1 ATOM 3934 N N . ARG A 1 552 ? -5.223 -24.585 3.132 1.00 24.10 ? 552 ARG A N 1 ATOM 3935 C CA . ARG A 1 552 ? -3.907 -24.619 2.513 1.00 24.72 ? 552 ARG A CA 1 ATOM 3936 C C . ARG A 1 552 ? -3.882 -25.496 1.258 1.00 26.23 ? 552 ARG A C 1 ATOM 3937 O O . ARG A 1 552 ? -4.580 -26.507 1.170 1.00 26.37 ? 552 ARG A O 1 ATOM 3938 C CB . ARG A 1 552 ? -2.875 -25.141 3.506 1.00 24.94 ? 552 ARG A CB 1 ATOM 3939 C CG . ARG A 1 552 ? -1.507 -25.402 2.897 1.00 25.42 ? 552 ARG A CG 1 ATOM 3940 C CD . ARG A 1 552 ? -0.495 -25.736 3.964 1.00 25.84 ? 552 ARG A CD 1 ATOM 3941 N NE . ARG A 1 552 ? -0.732 -27.060 4.519 1.00 27.10 ? 552 ARG A NE 1 ATOM 3942 C CZ . ARG A 1 552 ? -0.062 -27.590 5.546 1.00 28.25 ? 552 ARG A CZ 1 ATOM 3943 N NH1 . ARG A 1 552 ? 0.915 -26.916 6.159 1.00 28.55 ? 552 ARG A NH1 1 ATOM 3944 N NH2 . ARG A 1 552 ? -0.371 -28.813 5.959 1.00 28.19 ? 552 ARG A NH2 1 ATOM 3945 N N . ARG A 1 553 ? -3.066 -25.106 0.282 1.00 27.38 ? 553 ARG A N 1 ATOM 3946 C CA . ARG A 1 553 ? -2.736 -26.003 -0.816 1.00 26.61 ? 553 ARG A CA 1 ATOM 3947 C C . ARG A 1 553 ? -1.240 -26.177 -0.933 1.00 25.70 ? 553 ARG A C 1 ATOM 3948 O O . ARG A 1 553 ? -0.473 -25.269 -0.632 1.00 25.29 ? 553 ARG A O 1 ATOM 3949 C CB . ARG A 1 553 ? -3.341 -25.510 -2.122 1.00 27.59 ? 553 ARG A CB 1 ATOM 3950 C CG . ARG A 1 553 ? -4.797 -25.917 -2.260 1.00 28.49 ? 553 ARG A CG 1 ATOM 3951 C CD . ARG A 1 553 ? -5.742 -24.946 -1.579 1.00 29.28 ? 553 ARG A CD 1 ATOM 3952 N NE . ARG A 1 553 ? -6.391 -24.171 -2.622 1.00 31.44 ? 553 ARG A NE 1 ATOM 3953 C CZ . ARG A 1 553 ? -6.299 -22.865 -2.808 1.00 31.72 ? 553 ARG A CZ 1 ATOM 3954 N NH1 . ARG A 1 553 ? -6.945 -22.336 -3.835 1.00 34.33 ? 553 ARG A NH1 1 ATOM 3955 N NH2 . ARG A 1 553 ? -5.615 -22.079 -1.981 1.00 31.90 ? 553 ARG A NH2 1 ATOM 3956 N N . ILE A 1 554 ? -0.828 -27.377 -1.320 1.00 25.01 ? 554 ILE A N 1 ATOM 3957 C CA . ILE A 1 554 ? 0.563 -27.628 -1.640 1.00 24.98 ? 554 ILE A CA 1 ATOM 3958 C C . ILE A 1 554 ? 0.620 -28.140 -3.076 1.00 25.69 ? 554 ILE A C 1 ATOM 3959 O O . ILE A 1 554 ? -0.044 -29.119 -3.433 1.00 26.36 ? 554 ILE A O 1 ATOM 3960 C CB . ILE A 1 554 ? 1.225 -28.632 -0.682 1.00 23.99 ? 554 ILE A CB 1 ATOM 3961 C CG1 . ILE A 1 554 ? 0.990 -28.214 0.766 1.00 24.54 ? 554 ILE A CG1 1 ATOM 3962 C CG2 . ILE A 1 554 ? 2.722 -28.707 -0.961 1.00 23.94 ? 554 ILE A CG2 1 ATOM 3963 C CD1 . ILE A 1 554 ? 1.717 -29.060 1.790 1.00 25.01 ? 554 ILE A CD1 1 ATOM 3964 N N . ILE A 1 555 ? 1.396 -27.453 -3.900 1.00 25.31 ? 555 ILE A N 1 ATOM 3965 C CA . ILE A 1 555 ? 1.599 -27.872 -5.274 1.00 26.24 ? 555 ILE A CA 1 ATOM 3966 C C . ILE A 1 555 ? 3.056 -28.297 -5.386 1.00 27.44 ? 555 ILE A C 1 ATOM 3967 O O . ILE A 1 555 ? 3.889 -27.897 -4.568 1.00 26.54 ? 555 ILE A O 1 ATOM 3968 C CB . ILE A 1 555 ? 1.199 -26.771 -6.289 1.00 26.07 ? 555 ILE A CB 1 ATOM 3969 C CG1 . ILE A 1 555 ? 2.072 -25.519 -6.158 1.00 26.24 ? 555 ILE A CG1 1 ATOM 3970 C CG2 . ILE A 1 555 ? -0.258 -26.376 -6.092 1.00 25.80 ? 555 ILE A CG2 1 ATOM 3971 C CD1 . ILE A 1 555 ? 1.897 -24.543 -7.303 1.00 26.81 ? 555 ILE A CD1 1 ATOM 3972 N N . GLN A 1 556 ? 3.342 -29.159 -6.357 1.00 29.68 ? 556 GLN A N 1 ATOM 3973 C CA . GLN A 1 556 ? 4.689 -29.669 -6.558 1.00 31.56 ? 556 GLN A CA 1 ATOM 3974 C C . GLN A 1 556 ? 5.110 -29.529 -8.016 1.00 30.94 ? 556 GLN A C 1 ATOM 3975 O O . GLN A 1 556 ? 4.364 -29.879 -8.935 1.00 28.53 ? 556 GLN A O 1 ATOM 3976 C CB . GLN A 1 556 ? 4.792 -31.129 -6.112 1.00 33.76 ? 556 GLN A CB 1 ATOM 3977 C CG . GLN A 1 556 ? 6.137 -31.761 -6.439 1.00 36.23 ? 556 GLN A CG 1 ATOM 3978 C CD . GLN A 1 556 ? 6.606 -32.749 -5.384 1.00 39.28 ? 556 GLN A CD 1 ATOM 3979 O OE1 . GLN A 1 556 ? 5.828 -33.576 -4.893 1.00 42.35 ? 556 GLN A OE1 1 ATOM 3980 N NE2 . GLN A 1 556 ? 7.889 -32.671 -5.033 1.00 39.74 ? 556 GLN A NE2 1 ATOM 3981 N N . VAL A 1 557 ? 6.327 -29.025 -8.201 1.00 31.16 ? 557 VAL A N 1 ATOM 3982 C CA . VAL A 1 557 ? 6.883 -28.744 -9.514 1.00 31.89 ? 557 VAL A CA 1 ATOM 3983 C C . VAL A 1 557 ? 8.326 -29.206 -9.505 1.00 31.87 ? 557 VAL A C 1 ATOM 3984 O O . VAL A 1 557 ? 9.215 -28.485 -9.048 1.00 31.14 ? 557 VAL A O 1 ATOM 3985 C CB . VAL A 1 557 ? 6.846 -27.230 -9.823 1.00 32.59 ? 557 VAL A CB 1 ATOM 3986 C CG1 . VAL A 1 557 ? 7.487 -26.941 -11.176 1.00 33.37 ? 557 VAL A CG1 1 ATOM 3987 C CG2 . VAL A 1 557 ? 5.418 -26.710 -9.767 1.00 32.68 ? 557 VAL A CG2 1 ATOM 3988 N N . GLY A 1 558 ? 8.559 -30.411 -10.013 1.00 33.18 ? 558 GLY A N 1 ATOM 3989 C CA . GLY A 1 558 ? 9.875 -31.037 -9.907 1.00 33.05 ? 558 GLY A CA 1 ATOM 3990 C C . GLY A 1 558 ? 10.169 -31.307 -8.441 1.00 33.89 ? 558 GLY A C 1 ATOM 3991 O O . GLY A 1 558 ? 9.321 -31.851 -7.726 1.00 33.96 ? 558 GLY A O 1 ATOM 3992 N N . ASP A 1 559 ? 11.353 -30.895 -7.989 1.00 34.71 ? 559 ASP A N 1 ATOM 3993 C CA . ASP A 1 559 ? 11.758 -31.059 -6.588 1.00 35.87 ? 559 ASP A CA 1 ATOM 3994 C C . ASP A 1 559 ? 11.408 -29.845 -5.685 1.00 33.41 ? 559 ASP A C 1 ATOM 3995 O O . ASP A 1 559 ? 12.009 -29.662 -4.631 1.00 32.63 ? 559 ASP A O 1 ATOM 3996 C CB . ASP A 1 559 ? 13.262 -31.415 -6.497 1.00 39.58 ? 559 ASP A CB 1 ATOM 3997 C CG . ASP A 1 559 ? 14.188 -30.305 -7.017 1.00 43.62 ? 559 ASP A CG 1 ATOM 3998 O OD1 . ASP A 1 559 ? 13.767 -29.495 -7.873 1.00 47.62 ? 559 ASP A OD1 1 ATOM 3999 O OD2 . ASP A 1 559 ? 15.364 -30.258 -6.575 1.00 48.88 -1 559 ASP A OD2 1 ATOM 4000 N N . LEU A 1 560 ? 10.425 -29.044 -6.094 1.00 30.12 ? 560 LEU A N 1 ATOM 4001 C CA . LEU A 1 560 ? 9.998 -27.874 -5.335 1.00 28.87 ? 560 LEU A CA 1 ATOM 4002 C C . LEU A 1 560 ? 8.554 -28.030 -4.882 1.00 27.69 ? 560 LEU A C 1 ATOM 4003 O O . LEU A 1 560 ? 7.665 -28.150 -5.711 1.00 27.71 ? 560 LEU A O 1 ATOM 4004 C CB . LEU A 1 560 ? 10.101 -26.604 -6.191 1.00 27.82 ? 560 LEU A CB 1 ATOM 4005 C CG . LEU A 1 560 ? 9.589 -25.324 -5.516 1.00 28.22 ? 560 LEU A CG 1 ATOM 4006 C CD1 . LEU A 1 560 ? 10.504 -24.911 -4.374 1.00 28.06 ? 560 LEU A CD1 1 ATOM 4007 C CD2 . LEU A 1 560 ? 9.430 -24.174 -6.503 1.00 28.56 ? 560 LEU A CD2 1 ATOM 4008 N N . LYS A 1 561 ? 8.319 -28.009 -3.574 1.00 26.58 ? 561 LYS A N 1 ATOM 4009 C CA . LYS A 1 561 ? 6.961 -27.899 -3.066 1.00 26.37 ? 561 LYS A CA 1 ATOM 4010 C C . LYS A 1 561 ? 6.671 -26.432 -2.773 1.00 24.95 ? 561 LYS A C 1 ATOM 4011 O O . LYS A 1 561 ? 7.566 -25.687 -2.350 1.00 24.05 ? 561 LYS A O 1 ATOM 4012 C CB . LYS A 1 561 ? 6.774 -28.751 -1.816 1.00 28.25 ? 561 LYS A CB 1 ATOM 4013 C CG . LYS A 1 561 ? 6.798 -30.249 -2.080 1.00 29.63 ? 561 LYS A CG 1 ATOM 4014 C CD . LYS A 1 561 ? 6.595 -31.022 -0.783 1.00 31.76 ? 561 LYS A CD 1 ATOM 4015 C CE . LYS A 1 561 ? 6.862 -32.507 -0.962 1.00 33.07 ? 561 LYS A CE 1 ATOM 4016 N NZ . LYS A 1 561 ? 8.297 -32.785 -1.216 1.00 33.88 ? 561 LYS A NZ 1 ATOM 4017 N N . ILE A 1 562 ? 5.432 -26.009 -3.025 1.00 23.44 ? 562 ILE A N 1 ATOM 4018 C CA . ILE A 1 562 ? 5.027 -24.644 -2.727 1.00 22.80 ? 562 ILE A CA 1 ATOM 4019 C C . ILE A 1 562 ? 3.751 -24.654 -1.922 1.00 21.64 ? 562 ILE A C 1 ATOM 4020 O O . ILE A 1 562 ? 2.739 -25.168 -2.379 1.00 21.37 ? 562 ILE A O 1 ATOM 4021 C CB . ILE A 1 562 ? 4.787 -23.800 -3.993 1.00 23.47 ? 562 ILE A CB 1 ATOM 4022 C CG1 . ILE A 1 562 ? 6.005 -23.841 -4.913 1.00 24.03 ? 562 ILE A CG1 1 ATOM 4023 C CG2 . ILE A 1 562 ? 4.473 -22.357 -3.615 1.00 22.93 ? 562 ILE A CG2 1 ATOM 4024 C CD1 . ILE A 1 562 ? 5.625 -23.745 -6.367 1.00 24.77 ? 562 ILE A CD1 1 ATOM 4025 N N . LEU A 1 563 ? 3.804 -24.027 -0.774 1.00 20.99 ? 563 LEU A N 1 ATOM 4026 C CA . LEU A 1 563 ? 2.684 -23.823 0.075 1.00 20.55 ? 563 LEU A CA 1 ATOM 4027 C C . LEU A 1 563 ? 1.987 -22.512 -0.340 1.00 21.19 ? 563 LEU A C 1 ATOM 4028 O O . LEU A 1 563 ? 2.621 -21.507 -0.496 1.00 21.96 ? 563 LEU A O 1 ATOM 4029 C CB . LEU A 1 563 ? 3.124 -23.783 1.509 1.00 20.56 ? 563 LEU A CB 1 ATOM 4030 C CG . LEU A 1 563 ? 3.297 -25.082 2.284 1.00 20.76 ? 563 LEU A CG 1 ATOM 4031 C CD1 . LEU A 1 563 ? 4.546 -25.816 1.894 1.00 20.82 ? 563 LEU A CD1 1 ATOM 4032 C CD2 . LEU A 1 563 ? 3.261 -24.866 3.779 1.00 20.36 ? 563 LEU A CD2 1 ATOM 4033 N N . LEU A 1 564 ? 0.687 -22.584 -0.562 1.00 21.17 ? 564 LEU A N 1 ATOM 4034 C CA . LEU A 1 564 ? -0.156 -21.485 -0.954 1.00 20.78 ? 564 LEU A CA 1 ATOM 4035 C C . LEU A 1 564 ? -1.145 -21.254 0.152 1.00 20.65 ? 564 LEU A C 1 ATOM 4036 O O . LEU A 1 564 ? -2.095 -21.941 0.284 1.00 20.62 ? 564 LEU A O 1 ATOM 4037 C CB . LEU A 1 564 ? -0.876 -21.766 -2.271 1.00 20.92 ? 564 LEU A CB 1 ATOM 4038 C CG . LEU A 1 564 ? -0.114 -22.285 -3.481 1.00 20.96 ? 564 LEU A CG 1 ATOM 4039 C CD1 . LEU A 1 564 ? -1.006 -22.688 -4.615 1.00 20.98 ? 564 LEU A CD1 1 ATOM 4040 C CD2 . LEU A 1 564 ? 0.959 -21.348 -3.954 1.00 21.41 ? 564 LEU A CD2 1 ATOM 4041 N N . LEU A 1 565 ? -0.868 -20.239 0.939 1.00 20.27 ? 565 LEU A N 1 ATOM 4042 C CA . LEU A 1 565 ? -1.635 -19.866 2.099 1.00 19.76 ? 565 LEU A CA 1 ATOM 4043 C C . LEU A 1 565 ? -2.312 -18.541 2.121 1.00 20.51 ? 565 LEU A C 1 ATOM 4044 O O . LEU A 1 565 ? -2.047 -17.696 1.348 1.00 21.29 ? 565 LEU A O 1 ATOM 4045 C CB . LEU A 1 565 ? -0.682 -19.805 3.260 1.00 19.01 ? 565 LEU A CB 1 ATOM 4046 C CG . LEU A 1 565 ? 0.247 -20.950 3.522 1.00 19.20 ? 565 LEU A CG 1 ATOM 4047 C CD1 . LEU A 1 565 ? 1.312 -20.627 4.538 1.00 19.05 ? 565 LEU A CD1 1 ATOM 4048 C CD2 . LEU A 1 565 ? -0.583 -22.159 3.866 1.00 19.38 ? 565 LEU A CD2 1 ATOM 4049 N N . ASP A 1 566 ? -3.185 -18.378 3.078 1.00 21.52 ? 566 ASP A N 1 ATOM 4050 C CA . ASP A 1 566 ? -3.788 -17.102 3.335 1.00 22.61 ? 566 ASP A CA 1 ATOM 4051 C C . ASP A 1 566 ? -2.938 -16.465 4.422 1.00 21.14 ? 566 ASP A C 1 ATOM 4052 O O . ASP A 1 566 ? -2.269 -17.133 5.149 1.00 19.71 ? 566 ASP A O 1 ATOM 4053 C CB . ASP A 1 566 ? -5.244 -17.196 3.739 1.00 24.45 ? 566 ASP A CB 1 ATOM 4054 C CG . ASP A 1 566 ? -5.452 -17.945 5.014 1.00 26.99 ? 566 ASP A CG 1 ATOM 4055 O OD1 . ASP A 1 566 ? -4.849 -18.965 5.217 1.00 27.99 ? 566 ASP A OD1 1 ATOM 4056 O OD2 . ASP A 1 566 ? -6.261 -17.538 5.802 1.00 31.37 -1 566 ASP A OD2 1 ATOM 4057 N N . ARG A 1 567 ? -2.974 -15.158 4.507 1.00 20.32 ? 567 ARG A N 1 ATOM 4058 C CA . ARG A 1 567 ? -2.211 -14.447 5.496 1.00 20.15 ? 567 ARG A CA 1 ATOM 4059 C C . ARG A 1 567 ? -2.417 -14.902 6.943 1.00 19.58 ? 567 ARG A C 1 ATOM 4060 O O . ARG A 1 567 ? -1.505 -14.989 7.659 1.00 18.62 ? 567 ARG A O 1 ATOM 4061 C CB . ARG A 1 567 ? -2.434 -12.954 5.390 1.00 20.94 ? 567 ARG A CB 1 ATOM 4062 C CG . ARG A 1 567 ? -1.482 -12.147 6.226 1.00 21.42 ? 567 ARG A CG 1 ATOM 4063 C CD . ARG A 1 567 ? -2.076 -10.841 6.636 1.00 22.52 ? 567 ARG A CD 1 ATOM 4064 N NE . ARG A 1 567 ? -2.730 -10.168 5.550 1.00 23.03 ? 567 ARG A NE 1 ATOM 4065 C CZ . ARG A 1 567 ? -2.106 -9.462 4.635 1.00 24.47 ? 567 ARG A CZ 1 ATOM 4066 N NH1 . ARG A 1 567 ? -2.782 -8.886 3.689 1.00 24.76 ? 567 ARG A NH1 1 ATOM 4067 N NH2 . ARG A 1 567 ? -0.795 -9.307 4.700 1.00 25.32 ? 567 ARG A NH2 1 ATOM 4068 N N . ASN A 1 568 ? -3.635 -15.202 7.319 1.00 19.76 ? 568 ASN A N 1 ATOM 4069 C CA . ASN A 1 568 ? -3.914 -15.629 8.691 1.00 21.42 ? 568 ASN A CA 1 ATOM 4070 C C . ASN A 1 568 ? -3.382 -17.006 9.062 1.00 21.16 ? 568 ASN A C 1 ATOM 4071 O O . ASN A 1 568 ? -3.061 -17.223 10.232 1.00 22.43 ? 568 ASN A O 1 ATOM 4072 C CB . ASN A 1 568 ? -5.402 -15.493 9.028 1.00 21.54 ? 568 ASN A CB 1 ATOM 4073 C CG . ASN A 1 568 ? -5.827 -14.040 9.125 1.00 21.29 ? 568 ASN A CG 1 ATOM 4074 O OD1 . ASN A 1 568 ? -5.951 -13.360 8.123 1.00 22.77 ? 568 ASN A OD1 1 ATOM 4075 N ND2 . ASN A 1 568 ? -6.040 -13.565 10.326 1.00 21.66 ? 568 ASN A ND2 1 ATOM 4076 N N . SER A 1 569 ? -3.263 -17.917 8.091 1.00 20.58 ? 569 SER A N 1 ATOM 4077 C CA . SER A 1 569 ? -2.598 -19.205 8.328 1.00 20.38 ? 569 SER A CA 1 ATOM 4078 C C . SER A 1 569 ? -1.100 -19.003 8.431 1.00 19.55 ? 569 SER A C 1 ATOM 4079 O O . SER A 1 569 ? -0.465 -19.571 9.303 1.00 19.95 ? 569 SER A O 1 ATOM 4080 C CB . SER A 1 569 ? -2.881 -20.232 7.222 1.00 20.66 ? 569 SER A CB 1 ATOM 4081 O OG . SER A 1 569 ? -4.249 -20.594 7.206 1.00 21.73 ? 569 SER A OG 1 ATOM 4082 N N . ALA A 1 570 ? -0.544 -18.200 7.531 1.00 19.22 ? 570 ALA A N 1 ATOM 4083 C CA . ALA A 1 570 ? 0.883 -17.833 7.555 1.00 19.66 ? 570 ALA A CA 1 ATOM 4084 C C . ALA A 1 570 ? 1.337 -17.187 8.877 1.00 19.72 ? 570 ALA A C 1 ATOM 4085 O O . ALA A 1 570 ? 2.503 -17.315 9.265 1.00 20.40 ? 570 ALA A O 1 ATOM 4086 C CB . ALA A 1 570 ? 1.195 -16.889 6.392 1.00 20.16 ? 570 ALA A CB 1 ATOM 4087 N N . TYR A 1 571 ? 0.427 -16.489 9.555 1.00 19.39 ? 571 TYR A N 1 ATOM 4088 C CA . TYR A 1 571 ? 0.709 -15.913 10.877 1.00 19.68 ? 571 TYR A CA 1 ATOM 4089 C C . TYR A 1 571 ? 1.168 -16.974 11.873 1.00 19.15 ? 571 TYR A C 1 ATOM 4090 O O . TYR A 1 571 ? 1.874 -16.659 12.818 1.00 19.76 ? 571 TYR A O 1 ATOM 4091 C CB . TYR A 1 571 ? -0.537 -15.231 11.477 1.00 19.27 ? 571 TYR A CB 1 ATOM 4092 C CG . TYR A 1 571 ? -0.936 -13.850 10.973 1.00 19.00 ? 571 TYR A CG 1 ATOM 4093 C CD1 . TYR A 1 571 ? -0.057 -13.023 10.269 1.00 18.40 ? 571 TYR A CD1 1 ATOM 4094 C CD2 . TYR A 1 571 ? -2.202 -13.342 11.280 1.00 18.69 ? 571 TYR A CD2 1 ATOM 4095 C CE1 . TYR A 1 571 ? -0.450 -11.754 9.863 1.00 18.44 ? 571 TYR A CE1 1 ATOM 4096 C CE2 . TYR A 1 571 ? -2.596 -12.081 10.878 1.00 18.34 ? 571 TYR A CE2 1 ATOM 4097 C CZ . TYR A 1 571 ? -1.727 -11.291 10.165 1.00 18.64 ? 571 TYR A CZ 1 ATOM 4098 O OH . TYR A 1 571 ? -2.142 -10.034 9.771 1.00 17.95 ? 571 TYR A OH 1 ATOM 4099 N N . ASN A 1 572 ? 0.743 -18.217 11.670 1.00 19.71 ? 572 ASN A N 1 ATOM 4100 C CA . ASN A 1 572 ? 1.069 -19.329 12.571 1.00 19.46 ? 572 ASN A CA 1 ATOM 4101 C C . ASN A 1 572 ? 2.338 -20.103 12.203 1.00 19.56 ? 572 ASN A C 1 ATOM 4102 O O . ASN A 1 572 ? 2.626 -21.128 12.828 1.00 19.83 ? 572 ASN A O 1 ATOM 4103 C CB . ASN A 1 572 ? -0.109 -20.306 12.644 1.00 19.81 ? 572 ASN A CB 1 ATOM 4104 C CG . ASN A 1 572 ? -1.327 -19.719 13.336 1.00 20.48 ? 572 ASN A CG 1 ATOM 4105 O OD1 . ASN A 1 572 ? -1.222 -18.959 14.299 1.00 20.69 ? 572 ASN A OD1 1 ATOM 4106 N ND2 . ASN A 1 572 ? -2.499 -20.092 12.853 1.00 21.35 ? 572 ASN A ND2 1 ATOM 4107 N N . TYR A 1 573 ? 3.104 -19.618 11.219 1.00 19.49 ? 573 TYR A N 1 ATOM 4108 C CA . TYR A 1 573 ? 4.325 -20.306 10.776 1.00 18.91 ? 573 TYR A CA 1 ATOM 4109 C C . TYR A 1 573 ? 5.575 -19.673 11.388 1.00 18.78 ? 573 TYR A C 1 ATOM 4110 O O . TYR A 1 573 ? 5.603 -18.489 11.711 1.00 18.72 ? 573 TYR A O 1 ATOM 4111 C CB . TYR A 1 573 ? 4.426 -20.364 9.233 1.00 18.71 ? 573 TYR A CB 1 ATOM 4112 C CG . TYR A 1 573 ? 3.500 -21.385 8.579 1.00 17.93 ? 573 TYR A CG 1 ATOM 4113 C CD1 . TYR A 1 573 ? 2.126 -21.217 8.625 1.00 17.83 ? 573 TYR A CD1 1 ATOM 4114 C CD2 . TYR A 1 573 ? 3.999 -22.498 7.907 1.00 18.31 ? 573 TYR A CD2 1 ATOM 4115 C CE1 . TYR A 1 573 ? 1.262 -22.125 8.045 1.00 17.90 ? 573 TYR A CE1 1 ATOM 4116 C CE2 . TYR A 1 573 ? 3.137 -23.428 7.313 1.00 18.39 ? 573 TYR A CE2 1 ATOM 4117 C CZ . TYR A 1 573 ? 1.765 -23.226 7.395 1.00 18.27 ? 573 TYR A CZ 1 ATOM 4118 O OH . TYR A 1 573 ? 0.879 -24.095 6.831 1.00 18.37 ? 573 TYR A OH 1 ATOM 4119 N N . TRP A 1 574 ? 6.601 -20.497 11.562 1.00 18.84 ? 574 TRP A N 1 ATOM 4120 C CA . TRP A 1 574 ? 7.837 -20.092 12.204 1.00 18.43 ? 574 TRP A CA 1 ATOM 4121 C C . TRP A 1 574 ? 8.976 -20.769 11.473 1.00 18.28 ? 574 TRP A C 1 ATOM 4122 O O . TRP A 1 574 ? 8.781 -21.844 10.873 1.00 18.47 ? 574 TRP A O 1 ATOM 4123 C CB . TRP A 1 574 ? 7.847 -20.534 13.676 1.00 18.95 ? 574 TRP A CB 1 ATOM 4124 C CG . TRP A 1 574 ? 6.648 -20.073 14.438 1.00 18.88 ? 574 TRP A CG 1 ATOM 4125 C CD1 . TRP A 1 574 ? 5.429 -20.678 14.490 1.00 18.44 ? 574 TRP A CD1 1 ATOM 4126 C CD2 . TRP A 1 574 ? 6.544 -18.888 15.228 1.00 18.58 ? 574 TRP A CD2 1 ATOM 4127 N NE1 . TRP A 1 574 ? 4.574 -19.944 15.269 1.00 18.53 ? 574 TRP A NE1 1 ATOM 4128 C CE2 . TRP A 1 574 ? 5.234 -18.839 15.734 1.00 18.61 ? 574 TRP A CE2 1 ATOM 4129 C CE3 . TRP A 1 574 ? 7.431 -17.863 15.555 1.00 18.82 ? 574 TRP A CE3 1 ATOM 4130 C CZ2 . TRP A 1 574 ? 4.793 -17.813 16.558 1.00 18.96 ? 574 TRP A CZ2 1 ATOM 4131 C CZ3 . TRP A 1 574 ? 6.990 -16.836 16.375 1.00 18.64 ? 574 TRP A CZ3 1 ATOM 4132 C CH2 . TRP A 1 574 ? 5.679 -16.812 16.852 1.00 18.87 ? 574 TRP A CH2 1 ATOM 4133 N N . VAL A 1 575 ? 10.159 -20.162 11.546 1.00 17.12 ? 575 VAL A N 1 ATOM 4134 C CA . VAL A 1 575 ? 11.324 -20.667 10.853 1.00 17.27 ? 575 VAL A CA 1 ATOM 4135 C C . VAL A 1 575 ? 12.526 -20.694 11.781 1.00 17.74 ? 575 VAL A C 1 ATOM 4136 O O . VAL A 1 575 ? 13.448 -19.909 11.618 1.00 17.50 ? 575 VAL A O 1 ATOM 4137 C CB . VAL A 1 575 ? 11.641 -19.821 9.587 1.00 17.19 ? 575 VAL A CB 1 ATOM 4138 C CG1 . VAL A 1 575 ? 12.590 -20.565 8.670 1.00 16.63 ? 575 VAL A CG1 1 ATOM 4139 C CG2 . VAL A 1 575 ? 10.370 -19.489 8.832 1.00 17.05 ? 575 VAL A CG2 1 ATOM 4140 N N . PRO A 1 576 ? 12.523 -21.606 12.775 1.00 18.70 ? 576 PRO A N 1 ATOM 4141 C CA . PRO A 1 576 ? 13.661 -21.654 13.695 1.00 18.76 ? 576 PRO A CA 1 ATOM 4142 C C . PRO A 1 576 ? 14.909 -22.175 12.996 1.00 19.11 ? 576 PRO A C 1 ATOM 4143 O O . PRO A 1 576 ? 14.794 -23.009 12.102 1.00 19.00 ? 576 PRO A O 1 ATOM 4144 C CB . PRO A 1 576 ? 13.201 -22.630 14.783 1.00 19.00 ? 576 PRO A CB 1 ATOM 4145 C CG . PRO A 1 576 ? 12.129 -23.445 14.142 1.00 18.94 ? 576 PRO A CG 1 ATOM 4146 C CD . PRO A 1 576 ? 11.461 -22.552 13.150 1.00 18.45 ? 576 PRO A CD 1 ATOM 4147 N N . GLN A 1 577 ? 16.077 -21.667 13.386 1.00 18.79 ? 577 GLN A N 1 ATOM 4148 C CA . GLN A 1 577 ? 17.346 -22.210 12.919 1.00 18.95 ? 577 GLN A CA 1 ATOM 4149 C C . GLN A 1 577 ? 17.553 -23.579 13.553 1.00 19.75 ? 577 GLN A C 1 ATOM 4150 O O . GLN A 1 577 ? 17.169 -23.793 14.699 1.00 19.95 ? 577 GLN A O 1 ATOM 4151 C CB . GLN A 1 577 ? 18.499 -21.266 13.253 1.00 18.38 ? 577 GLN A CB 1 ATOM 4152 C CG . GLN A 1 577 ? 18.346 -19.896 12.600 1.00 18.25 ? 577 GLN A CG 1 ATOM 4153 C CD . GLN A 1 577 ? 19.547 -18.987 12.766 1.00 18.27 ? 577 GLN A CD 1 ATOM 4154 O OE1 . GLN A 1 577 ? 20.569 -19.348 13.359 1.00 18.65 ? 577 GLN A OE1 1 ATOM 4155 N NE2 . GLN A 1 577 ? 19.429 -17.795 12.232 1.00 18.57 ? 577 GLN A NE2 1 ATOM 4156 N N . LEU A 1 578 ? 18.113 -24.514 12.791 1.00 21.17 ? 578 LEU A N 1 ATOM 4157 C CA . LEU A 1 578 ? 18.309 -25.882 13.274 1.00 22.52 ? 578 LEU A CA 1 ATOM 4158 C C . LEU A 1 578 ? 19.745 -26.047 13.690 1.00 23.34 ? 578 LEU A C 1 ATOM 4159 O O . LEU A 1 578 ? 20.627 -26.067 12.843 1.00 23.46 ? 578 LEU A O 1 ATOM 4160 C CB . LEU A 1 578 ? 17.974 -26.903 12.191 1.00 23.53 ? 578 LEU A CB 1 ATOM 4161 C CG . LEU A 1 578 ? 18.151 -28.374 12.589 1.00 23.44 ? 578 LEU A CG 1 ATOM 4162 C CD1 . LEU A 1 578 ? 17.120 -28.758 13.633 1.00 23.68 ? 578 LEU A CD1 1 ATOM 4163 C CD2 . LEU A 1 578 ? 18.033 -29.263 11.363 1.00 23.91 ? 578 LEU A CD2 1 ATOM 4164 N N . ALA A 1 579 ? 19.975 -26.157 14.995 1.00 24.53 ? 579 ALA A N 1 ATOM 4165 C CA . ALA A 1 579 ? 21.316 -26.320 15.531 1.00 25.94 ? 579 ALA A CA 1 ATOM 4166 C C . ALA A 1 579 ? 21.744 -27.801 15.496 1.00 27.94 ? 579 ALA A C 1 ATOM 4167 O O . ALA A 1 579 ? 20.947 -28.686 15.815 1.00 27.10 ? 579 ALA A O 1 ATOM 4168 C CB . ALA A 1 579 ? 21.371 -25.773 16.951 1.00 25.55 ? 579 ALA A CB 1 ATOM 4169 N N . THR A 1 580 ? 22.995 -28.053 15.096 1.00 30.82 ? 580 THR A N 1 ATOM 4170 C CA . THR A 1 580 ? 23.578 -29.412 15.072 1.00 34.35 ? 580 THR A CA 1 ATOM 4171 C C . THR A 1 580 ? 24.757 -29.614 16.050 1.00 38.26 ? 580 THR A C 1 ATOM 4172 O O . THR A 1 580 ? 25.076 -30.753 16.398 1.00 41.19 ? 580 THR A O 1 ATOM 4173 C CB . THR A 1 580 ? 24.048 -29.809 13.647 1.00 33.16 ? 580 THR A CB 1 ATOM 4174 O OG1 . THR A 1 580 ? 24.798 -28.735 13.073 1.00 34.64 ? 580 THR A OG1 1 ATOM 4175 C CG2 . THR A 1 580 ? 22.865 -30.126 12.739 1.00 32.31 ? 580 THR A CG2 1 ATOM 4176 N N . ASP A 1 581 ? 25.389 -28.519 16.480 1.00 41.60 ? 581 ASP A N 1 ATOM 4177 C CA . ASP A 1 581 ? 26.574 -28.547 17.360 1.00 43.98 ? 581 ASP A CA 1 ATOM 4178 C C . ASP A 1 581 ? 26.234 -28.341 18.844 1.00 43.09 ? 581 ASP A C 1 ATOM 4179 O O . ASP A 1 581 ? 27.073 -28.577 19.724 1.00 43.72 ? 581 ASP A O 1 ATOM 4180 C CB . ASP A 1 581 ? 27.569 -27.453 16.935 1.00 46.56 ? 581 ASP A CB 1 ATOM 4181 C CG . ASP A 1 581 ? 26.950 -26.042 16.960 1.00 49.03 ? 581 ASP A CG 1 ATOM 4182 O OD1 . ASP A 1 581 ? 25.969 -25.804 16.211 1.00 48.71 ? 581 ASP A OD1 1 ATOM 4183 O OD2 . ASP A 1 581 ? 27.439 -25.177 17.729 1.00 51.31 -1 581 ASP A OD2 1 ATOM 4184 N N . GLY A 1 582 ? 25.020 -27.867 19.108 1.00 39.60 ? 582 GLY A N 1 ATOM 4185 C CA . GLY A 1 582 ? 24.557 -27.598 20.468 1.00 36.90 ? 582 GLY A CA 1 ATOM 4186 C C . GLY A 1 582 ? 23.057 -27.371 20.469 1.00 33.38 ? 582 GLY A C 1 ATOM 4187 O O . GLY A 1 582 ? 22.343 -27.942 19.645 1.00 31.69 ? 582 GLY A O 1 ATOM 4188 N N . THR A 1 583 ? 22.581 -26.537 21.385 1.00 31.17 ? 583 THR A N 1 ATOM 4189 C CA . THR A 1 583 ? 21.156 -26.217 21.468 1.00 30.71 ? 583 THR A CA 1 ATOM 4190 C C . THR A 1 583 ? 20.806 -24.756 21.081 1.00 29.48 ? 583 THR A C 1 ATOM 4191 O O . THR A 1 583 ? 19.633 -24.442 20.878 1.00 28.05 ? 583 THR A O 1 ATOM 4192 C CB . THR A 1 583 ? 20.611 -26.529 22.877 1.00 31.72 ? 583 THR A CB 1 ATOM 4193 O OG1 . THR A 1 583 ? 21.255 -25.690 23.839 1.00 32.86 ? 583 THR A OG1 1 ATOM 4194 C CG2 . THR A 1 583 ? 20.859 -28.001 23.251 1.00 32.27 ? 583 THR A CG2 1 ATOM 4195 N N . SER A 1 584 ? 21.809 -23.882 20.973 1.00 27.78 ? 584 SER A N 1 ATOM 4196 C CA . SER A 1 584 ? 21.589 -22.474 20.620 1.00 27.10 ? 584 SER A CA 1 ATOM 4197 C C . SER A 1 584 ? 21.507 -22.299 19.103 1.00 25.53 ? 584 SER A C 1 ATOM 4198 O O . SER A 1 584 ? 22.153 -23.026 18.353 1.00 25.61 ? 584 SER A O 1 ATOM 4199 C CB . SER A 1 584 ? 22.721 -21.589 21.153 1.00 28.06 ? 584 SER A CB 1 ATOM 4200 O OG . SER A 1 584 ? 23.122 -21.981 22.447 1.00 29.74 ? 584 SER A OG 1 ATOM 4201 N N . PRO A 1 585 ? 20.713 -21.328 18.637 1.00 24.38 ? 585 PRO A N 1 ATOM 4202 C CA . PRO A 1 585 ? 20.544 -21.230 17.184 1.00 23.64 ? 585 PRO A CA 1 ATOM 4203 C C . PRO A 1 585 ? 21.729 -20.589 16.488 1.00 21.94 ? 585 PRO A C 1 ATOM 4204 O O . PRO A 1 585 ? 21.951 -20.838 15.309 1.00 21.43 ? 585 PRO A O 1 ATOM 4205 C CB . PRO A 1 585 ? 19.279 -20.380 17.025 1.00 23.42 ? 585 PRO A CB 1 ATOM 4206 C CG . PRO A 1 585 ? 19.152 -19.621 18.301 1.00 23.91 ? 585 PRO A CG 1 ATOM 4207 C CD . PRO A 1 585 ? 19.875 -20.367 19.375 1.00 24.03 ? 585 PRO A CD 1 ATOM 4208 N N . GLY A 1 586 ? 22.477 -19.769 17.218 1.00 21.59 ? 586 GLY A N 1 ATOM 4209 C CA . GLY A 1 586 ? 23.606 -19.038 16.653 1.00 20.81 ? 586 GLY A CA 1 ATOM 4210 C C . GLY A 1 586 ? 23.083 -17.822 15.924 1.00 19.58 ? 586 GLY A C 1 ATOM 4211 O O . GLY A 1 586 ? 21.872 -17.652 15.795 1.00 18.26 ? 586 GLY A O 1 ATOM 4212 N N . PHE A 1 587 ? 24.001 -16.978 15.460 1.00 19.47 ? 587 PHE A N 1 ATOM 4213 C CA . PHE A 1 587 ? 23.650 -15.774 14.698 1.00 19.75 ? 587 PHE A CA 1 ATOM 4214 C C . PHE A 1 587 ? 23.087 -16.138 13.326 1.00 20.30 ? 587 PHE A C 1 ATOM 4215 O O . PHE A 1 587 ? 23.174 -17.292 12.891 1.00 19.78 ? 587 PHE A O 1 ATOM 4216 C CB . PHE A 1 587 ? 24.863 -14.847 14.550 1.00 19.42 ? 587 PHE A CB 1 ATOM 4217 C CG . PHE A 1 587 ? 25.421 -14.372 15.866 1.00 19.39 ? 587 PHE A CG 1 ATOM 4218 C CD1 . PHE A 1 587 ? 24.667 -13.556 16.697 1.00 18.90 ? 587 PHE A CD1 1 ATOM 4219 C CD2 . PHE A 1 587 ? 26.691 -14.749 16.278 1.00 18.90 ? 587 PHE A CD2 1 ATOM 4220 C CE1 . PHE A 1 587 ? 25.167 -13.124 17.909 1.00 18.76 ? 587 PHE A CE1 1 ATOM 4221 C CE2 . PHE A 1 587 ? 27.196 -14.324 17.493 1.00 18.90 ? 587 PHE A CE2 1 ATOM 4222 C CZ . PHE A 1 587 ? 26.436 -13.508 18.310 1.00 18.77 ? 587 PHE A CZ 1 ATOM 4223 N N . SER A 1 588 ? 22.485 -15.156 12.664 1.00 21.47 ? 588 SER A N 1 ATOM 4224 C CA . SER A 1 588 ? 21.868 -15.365 11.361 1.00 22.42 ? 588 SER A CA 1 ATOM 4225 C C . SER A 1 588 ? 22.908 -15.241 10.237 1.00 23.38 ? 588 SER A C 1 ATOM 4226 O O . SER A 1 588 ? 22.930 -14.267 9.482 1.00 23.01 ? 588 SER A O 1 ATOM 4227 C CB . SER A 1 588 ? 20.684 -14.404 11.161 1.00 22.70 ? 588 SER A CB 1 ATOM 4228 O OG . SER A 1 588 ? 19.620 -14.673 12.082 1.00 22.47 ? 588 SER A OG 1 ATOM 4229 N N . THR A 1 589 ? 23.775 -16.246 10.149 1.00 25.01 ? 589 THR A N 1 ATOM 4230 C CA . THR A 1 589 ? 24.791 -16.330 9.102 1.00 26.42 ? 589 THR A CA 1 ATOM 4231 C C . THR A 1 589 ? 24.201 -17.143 7.957 1.00 27.31 ? 589 THR A C 1 ATOM 4232 O O . THR A 1 589 ? 23.258 -17.896 8.172 1.00 28.73 ? 589 THR A O 1 ATOM 4233 C CB . THR A 1 589 ? 26.070 -17.018 9.611 1.00 26.68 ? 589 THR A CB 1 ATOM 4234 O OG1 . THR A 1 589 ? 25.823 -18.418 9.802 1.00 27.69 ? 589 THR A OG1 1 ATOM 4235 C CG2 . THR A 1 589 ? 26.528 -16.397 10.922 1.00 26.42 ? 589 THR A CG2 1 ATOM 4236 N N . PRO A 1 590 ? 24.738 -16.991 6.737 1.00 28.08 ? 590 PRO A N 1 ATOM 4237 C CA . PRO A 1 590 ? 24.155 -17.698 5.587 1.00 28.68 ? 590 PRO A CA 1 ATOM 4238 C C . PRO A 1 590 ? 23.981 -19.194 5.818 1.00 29.02 ? 590 PRO A C 1 ATOM 4239 O O . PRO A 1 590 ? 22.924 -19.737 5.555 1.00 28.66 ? 590 PRO A O 1 ATOM 4240 C CB . PRO A 1 590 ? 25.169 -17.441 4.463 1.00 29.17 ? 590 PRO A CB 1 ATOM 4241 C CG . PRO A 1 590 ? 25.853 -16.167 4.851 1.00 29.07 ? 590 PRO A CG 1 ATOM 4242 C CD . PRO A 1 590 ? 25.907 -16.174 6.353 1.00 28.80 ? 590 PRO A CD 1 ATOM 4243 N N . GLU A 1 591 ? 25.016 -19.836 6.333 1.00 31.30 ? 591 GLU A N 1 ATOM 4244 C CA . GLU A 1 591 ? 24.997 -21.266 6.595 1.00 33.89 ? 591 GLU A CA 1 ATOM 4245 C C . GLU A 1 591 ? 23.885 -21.673 7.579 1.00 31.36 ? 591 GLU A C 1 ATOM 4246 O O . GLU A 1 591 ? 23.166 -22.642 7.336 1.00 31.33 ? 591 GLU A O 1 ATOM 4247 C CB . GLU A 1 591 ? 26.374 -21.699 7.109 1.00 38.00 ? 591 GLU A CB 1 ATOM 4248 C CG . GLU A 1 591 ? 26.491 -23.172 7.474 1.00 45.27 ? 591 GLU A CG 1 ATOM 4249 C CD . GLU A 1 591 ? 27.894 -23.561 7.928 1.00 51.68 ? 591 GLU A CD 1 ATOM 4250 O OE1 . GLU A 1 591 ? 28.577 -22.721 8.566 1.00 54.94 ? 591 GLU A OE1 1 ATOM 4251 O OE2 . GLU A 1 591 ? 28.315 -24.713 7.652 1.00 56.95 -1 591 GLU A OE2 1 ATOM 4252 N N . LYS A 1 592 ? 23.744 -20.936 8.678 1.00 29.38 ? 592 LYS A N 1 ATOM 4253 C CA . LYS A 1 592 ? 22.745 -21.259 9.701 1.00 28.20 ? 592 LYS A CA 1 ATOM 4254 C C . LYS A 1 592 ? 21.339 -20.856 9.283 1.00 26.86 ? 592 LYS A C 1 ATOM 4255 O O . LYS A 1 592 ? 20.372 -21.502 9.695 1.00 25.17 ? 592 LYS A O 1 ATOM 4256 C CB . LYS A 1 592 ? 23.089 -20.590 11.029 1.00 29.70 ? 592 LYS A CB 1 ATOM 4257 C CG . LYS A 1 592 ? 24.380 -21.085 11.649 1.00 31.45 ? 592 LYS A CG 1 ATOM 4258 C CD . LYS A 1 592 ? 24.796 -20.208 12.820 1.00 33.42 ? 592 LYS A CD 1 ATOM 4259 C CE . LYS A 1 592 ? 26.043 -20.744 13.505 1.00 34.21 ? 592 LYS A CE 1 ATOM 4260 N NZ . LYS A 1 592 ? 25.832 -22.140 13.979 1.00 34.68 ? 592 LYS A NZ 1 ATOM 4261 N N . VAL A 1 593 ? 21.231 -19.783 8.488 1.00 24.91 ? 593 VAL A N 1 ATOM 4262 C CA . VAL A 1 593 ? 19.972 -19.404 7.832 1.00 24.66 ? 593 VAL A CA 1 ATOM 4263 C C . VAL A 1 593 ? 19.476 -20.535 6.929 1.00 24.30 ? 593 VAL A C 1 ATOM 4264 O O . VAL A 1 593 ? 18.291 -20.884 6.970 1.00 24.03 ? 593 VAL A O 1 ATOM 4265 C CB . VAL A 1 593 ? 20.123 -18.099 6.981 1.00 24.99 ? 593 VAL A CB 1 ATOM 4266 C CG1 . VAL A 1 593 ? 18.966 -17.920 6.002 1.00 24.89 ? 593 VAL A CG1 1 ATOM 4267 C CG2 . VAL A 1 593 ? 20.239 -16.861 7.871 1.00 25.05 ? 593 VAL A CG2 1 ATOM 4268 N N . ALA A 1 594 ? 20.375 -21.073 6.101 1.00 24.17 ? 594 ALA A N 1 ATOM 4269 C CA . ALA A 1 594 ? 20.039 -22.150 5.159 1.00 26.75 ? 594 ALA A CA 1 ATOM 4270 C C . ALA A 1 594 ? 19.609 -23.412 5.907 1.00 28.24 ? 594 ALA A C 1 ATOM 4271 O O . ALA A 1 594 ? 18.638 -24.047 5.541 1.00 29.84 ? 594 ALA A O 1 ATOM 4272 C CB . ALA A 1 594 ? 21.219 -22.468 4.244 1.00 26.21 ? 594 ALA A CB 1 ATOM 4273 N N . SER A 1 595 ? 20.340 -23.759 6.956 1.00 29.46 ? 595 SER A N 1 ATOM 4274 C CA . SER A 1 595 ? 19.970 -24.869 7.836 1.00 32.04 ? 595 SER A CA 1 ATOM 4275 C C . SER A 1 595 ? 18.906 -24.466 8.882 1.00 31.09 ? 595 SER A C 1 ATOM 4276 O O . SER A 1 595 ? 19.183 -24.413 10.092 1.00 34.10 ? 595 SER A O 1 ATOM 4277 C CB . SER A 1 595 ? 21.219 -25.402 8.542 1.00 33.40 ? 595 SER A CB 1 ATOM 4278 O OG . SER A 1 595 ? 20.862 -26.237 9.627 1.00 38.51 ? 595 SER A OG 1 ATOM 4279 N N . SER A 1 596 ? 17.700 -24.179 8.409 1.00 27.84 ? 596 SER A N 1 ATOM 4280 C CA . SER A 1 596 ? 16.569 -23.856 9.266 1.00 26.12 ? 596 SER A CA 1 ATOM 4281 C C . SER A 1 596 ? 15.441 -24.790 8.863 1.00 26.61 ? 596 SER A C 1 ATOM 4282 O O . SER A 1 596 ? 15.485 -25.345 7.773 1.00 29.40 ? 596 SER A O 1 ATOM 4283 C CB . SER A 1 596 ? 16.141 -22.389 9.079 1.00 24.29 ? 596 SER A CB 1 ATOM 4284 O OG . SER A 1 596 ? 17.062 -21.488 9.659 1.00 21.54 ? 596 SER A OG 1 ATOM 4285 N N . ILE A 1 597 ? 14.439 -24.969 9.725 1.00 25.84 ? 597 ILE A N 1 ATOM 4286 C CA . ILE A 1 597 ? 13.270 -25.792 9.390 1.00 25.78 ? 597 ILE A CA 1 ATOM 4287 C C . ILE A 1 597 ? 12.019 -24.939 9.463 1.00 25.49 ? 597 ILE A C 1 ATOM 4288 O O . ILE A 1 597 ? 12.054 -23.844 10.020 1.00 24.57 ? 597 ILE A O 1 ATOM 4289 C CB . ILE A 1 597 ? 13.105 -27.017 10.324 1.00 26.58 ? 597 ILE A CB 1 ATOM 4290 C CG1 . ILE A 1 597 ? 13.037 -26.592 11.796 1.00 27.04 ? 597 ILE A CG1 1 ATOM 4291 C CG2 . ILE A 1 597 ? 14.248 -27.996 10.108 1.00 27.32 ? 597 ILE A CG2 1 ATOM 4292 C CD1 . ILE A 1 597 ? 12.412 -27.637 12.695 1.00 27.66 ? 597 ILE A CD1 1 ATOM 4293 N N . ILE A 1 598 ? 10.917 -25.450 8.911 1.00 24.63 ? 598 ILE A N 1 ATOM 4294 C CA . ILE A 1 598 ? 9.641 -24.720 8.884 1.00 24.40 ? 598 ILE A CA 1 ATOM 4295 C C . ILE A 1 598 ? 8.618 -25.393 9.797 1.00 24.50 ? 598 ILE A C 1 ATOM 4296 O O . ILE A 1 598 ? 8.324 -26.581 9.641 1.00 25.69 ? 598 ILE A O 1 ATOM 4297 C CB . ILE A 1 598 ? 9.074 -24.641 7.456 1.00 23.75 ? 598 ILE A CB 1 ATOM 4298 C CG1 . ILE A 1 598 ? 10.059 -23.900 6.546 1.00 23.27 ? 598 ILE A CG1 1 ATOM 4299 C CG2 . ILE A 1 598 ? 7.702 -23.977 7.457 1.00 23.80 ? 598 ILE A CG2 1 ATOM 4300 C CD1 . ILE A 1 598 ? 9.781 -24.064 5.070 1.00 22.83 ? 598 ILE A CD1 1 ATOM 4301 N N . VAL A 1 599 ? 8.113 -24.659 10.756 1.00 24.32 ? 599 VAL A N 1 ATOM 4302 C CA . VAL A 1 599 ? 7.196 -25.175 11.718 1.00 23.97 ? 599 VAL A CA 1 ATOM 4303 C C . VAL A 1 599 ? 5.902 -24.417 11.803 1.00 24.14 ? 599 VAL A C 1 ATOM 4304 O O . VAL A 1 599 ? 5.907 -23.248 11.939 1.00 25.62 ? 599 VAL A O 1 ATOM 4305 C CB . VAL A 1 599 ? 7.798 -25.164 13.138 1.00 23.64 ? 599 VAL A CB 1 ATOM 4306 C CG1 . VAL A 1 599 ? 6.853 -25.793 14.133 1.00 23.82 ? 599 VAL A CG1 1 ATOM 4307 C CG2 . VAL A 1 599 ? 9.117 -25.846 13.179 1.00 23.83 ? 599 VAL A CG2 1 ATOM 4308 N N . LYS A 1 600 ? 4.793 -25.124 11.704 1.00 24.07 ? 600 LYS A N 1 ATOM 4309 C CA . LYS A 1 600 ? 3.498 -24.539 11.890 1.00 25.31 ? 600 LYS A CA 1 ATOM 4310 C C . LYS A 1 600 ? 3.086 -24.876 13.299 1.00 24.87 ? 600 LYS A C 1 ATOM 4311 O O . LYS A 1 600 ? 3.133 -25.997 13.705 1.00 25.12 ? 600 LYS A O 1 ATOM 4312 C CB . LYS A 1 600 ? 2.462 -25.066 10.933 1.00 26.97 ? 600 LYS A CB 1 ATOM 4313 C CG . LYS A 1 600 ? 1.194 -24.253 10.953 1.00 29.61 ? 600 LYS A CG 1 ATOM 4314 C CD . LYS A 1 600 ? -0.034 -25.080 10.647 1.00 31.83 ? 600 LYS A CD 1 ATOM 4315 C CE . LYS A 1 600 ? -1.300 -24.495 11.250 1.00 33.59 ? 600 LYS A CE 1 ATOM 4316 N NZ . LYS A 1 600 ? -1.670 -24.846 12.660 1.00 33.96 ? 600 LYS A NZ 1 ATOM 4317 N N . ALA A 1 601 ? 2.731 -23.875 14.061 1.00 24.15 ? 601 ALA A N 1 ATOM 4318 C CA . ALA A 1 601 ? 2.334 -24.097 15.423 1.00 23.51 ? 601 ALA A CA 1 ATOM 4319 C C . ALA A 1 601 ? 1.333 -23.070 15.918 1.00 23.04 ? 601 ALA A C 1 ATOM 4320 O O . ALA A 1 601 ? 0.390 -22.791 15.273 1.00 22.05 ? 601 ALA A O 1 ATOM 4321 C CB . ALA A 1 601 ? 3.557 -24.172 16.310 1.00 23.46 ? 601 ALA A CB 1 ATOM 4322 N N . GLY A 1 602 ? 1.578 -22.528 17.087 1.00 23.18 ? 602 GLY A N 1 ATOM 4323 C CA . GLY A 1 602 ? 0.696 -21.558 17.661 1.00 22.75 ? 602 GLY A CA 1 ATOM 4324 C C . GLY A 1 602 ? 1.356 -20.279 18.050 1.00 22.37 ? 602 GLY A C 1 ATOM 4325 O O . GLY A 1 602 ? 1.952 -19.626 17.277 1.00 22.63 ? 602 GLY A O 1 ATOM 4326 N N . TYR A 1 603 ? 1.245 -19.989 19.316 1.00 21.23 ? 603 TYR A N 1 ATOM 4327 C CA . TYR A 1 603 ? 1.727 -18.792 19.937 1.00 19.92 ? 603 TYR A CA 1 ATOM 4328 C C . TYR A 1 603 ? 3.180 -18.384 19.714 1.00 19.07 ? 603 TYR A C 1 ATOM 4329 O O . TYR A 1 603 ? 3.448 -17.252 19.394 1.00 17.50 ? 603 TYR A O 1 ATOM 4330 C CB . TYR A 1 603 ? 1.400 -18.903 21.394 1.00 19.57 ? 603 TYR A CB 1 ATOM 4331 C CG . TYR A 1 603 ? 1.730 -17.711 22.182 1.00 19.22 ? 603 TYR A CG 1 ATOM 4332 C CD1 . TYR A 1 603 ? 0.948 -16.605 22.137 1.00 18.96 ? 603 TYR A CD1 1 ATOM 4333 C CD2 . TYR A 1 603 ? 2.806 -17.712 23.007 1.00 18.94 ? 603 TYR A CD2 1 ATOM 4334 C CE1 . TYR A 1 603 ? 1.262 -15.509 22.863 1.00 18.63 ? 603 TYR A CE1 1 ATOM 4335 C CE2 . TYR A 1 603 ? 3.100 -16.624 23.755 1.00 18.66 ? 603 TYR A CE2 1 ATOM 4336 C CZ . TYR A 1 603 ? 2.320 -15.533 23.666 1.00 18.14 ? 603 TYR A CZ 1 ATOM 4337 O OH . TYR A 1 603 ? 2.606 -14.474 24.391 1.00 17.99 ? 603 TYR A OH 1 ATOM 4338 N N . LEU A 1 604 ? 4.086 -19.334 19.866 1.00 17.90 ? 604 LEU A N 1 ATOM 4339 C CA . LEU A 1 604 ? 5.508 -19.070 19.683 1.00 17.70 ? 604 LEU A CA 1 ATOM 4340 C C . LEU A 1 604 ? 6.326 -20.355 19.458 1.00 17.81 ? 604 LEU A C 1 ATOM 4341 O O . LEU A 1 604 ? 6.125 -21.363 20.155 1.00 17.05 ? 604 LEU A O 1 ATOM 4342 C CB . LEU A 1 604 ? 6.055 -18.324 20.906 1.00 17.94 ? 604 LEU A CB 1 ATOM 4343 C CG . LEU A 1 604 ? 7.564 -18.034 20.990 1.00 18.32 ? 604 LEU A CG 1 ATOM 4344 C CD1 . LEU A 1 604 ? 8.018 -17.097 19.887 1.00 18.42 ? 604 LEU A CD1 1 ATOM 4345 C CD2 . LEU A 1 604 ? 7.923 -17.437 22.338 1.00 19.17 ? 604 LEU A CD2 1 ATOM 4346 N N . VAL A 1 605 ? 7.256 -20.292 18.505 1.00 17.18 ? 605 VAL A N 1 ATOM 4347 C CA . VAL A 1 605 ? 8.337 -21.277 18.404 1.00 18.03 ? 605 VAL A CA 1 ATOM 4348 C C . VAL A 1 605 ? 9.666 -20.545 18.604 1.00 18.39 ? 605 VAL A C 1 ATOM 4349 O O . VAL A 1 605 ? 9.947 -19.564 17.913 1.00 18.74 ? 605 VAL A O 1 ATOM 4350 C CB . VAL A 1 605 ? 8.339 -22.026 17.055 1.00 17.68 ? 605 VAL A CB 1 ATOM 4351 C CG1 . VAL A 1 605 ? 9.517 -22.982 16.973 1.00 17.81 ? 605 VAL A CG1 1 ATOM 4352 C CG2 . VAL A 1 605 ? 7.037 -22.782 16.856 1.00 17.92 ? 605 VAL A CG2 1 ATOM 4353 N N . ARG A 1 606 ? 10.460 -21.029 19.559 1.00 18.59 ? 606 ARG A N 1 ATOM 4354 C CA . ARG A 1 606 ? 11.675 -20.367 20.009 1.00 18.85 ? 606 ARG A CA 1 ATOM 4355 C C . ARG A 1 606 ? 12.908 -20.921 19.304 1.00 19.79 ? 606 ARG A C 1 ATOM 4356 O O . ARG A 1 606 ? 13.636 -20.179 18.642 1.00 19.61 ? 606 ARG A O 1 ATOM 4357 C CB . ARG A 1 606 ? 11.850 -20.537 21.530 1.00 18.79 ? 606 ARG A CB 1 ATOM 4358 C CG . ARG A 1 606 ? 10.920 -19.692 22.390 1.00 18.31 ? 606 ARG A CG 1 ATOM 4359 C CD . ARG A 1 606 ? 11.081 -20.013 23.871 1.00 18.20 ? 606 ARG A CD 1 ATOM 4360 N NE . ARG A 1 606 ? 10.050 -19.348 24.662 1.00 18.60 ? 606 ARG A NE 1 ATOM 4361 C CZ . ARG A 1 606 ? 10.114 -18.082 25.101 1.00 19.50 ? 606 ARG A CZ 1 ATOM 4362 N NH1 . ARG A 1 606 ? 11.185 -17.315 24.870 1.00 19.54 ? 606 ARG A NH1 1 ATOM 4363 N NH2 . ARG A 1 606 ? 9.095 -17.567 25.785 1.00 19.18 ? 606 ARG A NH2 1 ATOM 4364 N N . THR A 1 607 ? 13.154 -22.220 19.457 1.00 20.16 ? 607 THR A N 1 ATOM 4365 C CA . THR A 1 607 ? 14.352 -22.840 18.885 1.00 21.18 ? 607 THR A CA 1 ATOM 4366 C C . THR A 1 607 ? 14.072 -24.247 18.362 1.00 21.48 ? 607 THR A C 1 ATOM 4367 O O . THR A 1 607 ? 13.019 -24.836 18.614 1.00 21.90 ? 607 THR A O 1 ATOM 4368 C CB . THR A 1 607 ? 15.522 -22.929 19.906 1.00 21.53 ? 607 THR A CB 1 ATOM 4369 O OG1 . THR A 1 607 ? 15.151 -23.768 21.005 1.00 22.09 ? 607 THR A OG1 1 ATOM 4370 C CG2 . THR A 1 607 ? 15.907 -21.563 20.444 1.00 21.61 ? 607 THR A CG2 1 ATOM 4371 N N . ALA A 1 608 ? 15.036 -24.759 17.617 1.00 21.47 ? 608 ALA A N 1 ATOM 4372 C CA . ALA A 1 608 ? 15.037 -26.132 17.165 1.00 22.14 ? 608 ALA A CA 1 ATOM 4373 C C . ALA A 1 608 ? 16.466 -26.635 17.214 1.00 23.27 ? 608 ALA A C 1 ATOM 4374 O O . ALA A 1 608 ? 17.402 -25.883 16.941 1.00 24.56 ? 608 ALA A O 1 ATOM 4375 C CB . ALA A 1 608 ? 14.491 -26.231 15.757 1.00 21.96 ? 608 ALA A CB 1 ATOM 4376 N N . TYR A 1 609 ? 16.648 -27.886 17.614 1.00 24.26 ? 609 TYR A N 1 ATOM 4377 C CA . TYR A 1 609 ? 17.941 -28.538 17.450 1.00 25.35 ? 609 TYR A CA 1 ATOM 4378 C C . TYR A 1 609 ? 17.812 -30.033 17.188 1.00 25.55 ? 609 TYR A C 1 ATOM 4379 O O . TYR A 1 609 ? 16.791 -30.658 17.485 1.00 25.10 ? 609 TYR A O 1 ATOM 4380 C CB . TYR A 1 609 ? 18.893 -28.261 18.625 1.00 25.58 ? 609 TYR A CB 1 ATOM 4381 C CG . TYR A 1 609 ? 18.407 -28.683 20.000 1.00 25.60 ? 609 TYR A CG 1 ATOM 4382 C CD1 . TYR A 1 609 ? 17.665 -27.803 20.799 1.00 25.47 ? 609 TYR A CD1 1 ATOM 4383 C CD2 . TYR A 1 609 ? 18.716 -29.941 20.516 1.00 25.40 ? 609 TYR A CD2 1 ATOM 4384 C CE1 . TYR A 1 609 ? 17.235 -28.164 22.065 1.00 25.03 ? 609 TYR A CE1 1 ATOM 4385 C CE2 . TYR A 1 609 ? 18.286 -30.317 21.783 1.00 25.65 ? 609 TYR A CE2 1 ATOM 4386 C CZ . TYR A 1 609 ? 17.547 -29.420 22.553 1.00 25.99 ? 609 TYR A CZ 1 ATOM 4387 O OH . TYR A 1 609 ? 17.123 -29.776 23.808 1.00 26.83 ? 609 TYR A OH 1 ATOM 4388 N N . LEU A 1 610 ? 18.867 -30.572 16.595 1.00 26.75 ? 610 LEU A N 1 ATOM 4389 C CA . LEU A 1 610 ? 18.933 -31.963 16.202 1.00 27.79 ? 610 LEU A CA 1 ATOM 4390 C C . LEU A 1 610 ? 20.056 -32.586 16.992 1.00 27.89 ? 610 LEU A C 1 ATOM 4391 O O . LEU A 1 610 ? 21.126 -32.007 17.112 1.00 27.37 ? 610 LEU A O 1 ATOM 4392 C CB . LEU A 1 610 ? 19.235 -32.072 14.715 1.00 28.86 ? 610 LEU A CB 1 ATOM 4393 C CG . LEU A 1 610 ? 19.407 -33.471 14.122 1.00 29.17 ? 610 LEU A CG 1 ATOM 4394 C CD1 . LEU A 1 610 ? 18.106 -34.244 14.202 1.00 29.59 ? 610 LEU A CD1 1 ATOM 4395 C CD2 . LEU A 1 610 ? 19.887 -33.365 12.682 1.00 30.16 ? 610 LEU A CD2 1 ATOM 4396 N N . LYS A 1 611 ? 19.792 -33.771 17.522 1.00 29.01 ? 611 LYS A N 1 ATOM 4397 C CA . LYS A 1 611 ? 20.752 -34.504 18.327 1.00 30.85 ? 611 LYS A CA 1 ATOM 4398 C C . LYS A 1 611 ? 20.431 -35.996 18.209 1.00 30.31 ? 611 LYS A C 1 ATOM 4399 O O . LYS A 1 611 ? 19.380 -36.461 18.672 1.00 29.16 ? 611 LYS A O 1 ATOM 4400 C CB . LYS A 1 611 ? 20.650 -34.034 19.775 1.00 33.03 ? 611 LYS A CB 1 ATOM 4401 C CG . LYS A 1 611 ? 21.618 -34.688 20.733 1.00 34.27 ? 611 LYS A CG 1 ATOM 4402 C CD . LYS A 1 611 ? 21.587 -33.970 22.072 1.00 35.63 ? 611 LYS A CD 1 ATOM 4403 C CE . LYS A 1 611 ? 21.995 -34.887 23.212 1.00 35.66 ? 611 LYS A CE 1 ATOM 4404 N NZ . LYS A 1 611 ? 21.660 -34.247 24.508 1.00 35.24 ? 611 LYS A NZ 1 ATOM 4405 N N . GLY A 1 612 ? 21.333 -36.729 17.560 1.00 30.46 ? 612 GLY A N 1 ATOM 4406 C CA . GLY A 1 612 ? 21.097 -38.124 17.207 1.00 29.92 ? 612 GLY A CA 1 ATOM 4407 C C . GLY A 1 612 ? 19.804 -38.286 16.442 1.00 28.90 ? 612 GLY A C 1 ATOM 4408 O O . GLY A 1 612 ? 19.563 -37.574 15.463 1.00 29.39 ? 612 GLY A O 1 ATOM 4409 N N . SER A 1 613 ? 18.960 -39.197 16.925 1.00 27.91 ? 613 SER A N 1 ATOM 4410 C CA . SER A 1 613 ? 17.667 -39.486 16.308 1.00 27.72 ? 613 SER A CA 1 ATOM 4411 C C . SER A 1 613 ? 16.562 -38.529 16.781 1.00 27.15 ? 613 SER A C 1 ATOM 4412 O O . SER A 1 613 ? 15.388 -38.708 16.438 1.00 25.69 ? 613 SER A O 1 ATOM 4413 C CB . SER A 1 613 ? 17.255 -40.929 16.619 1.00 27.46 ? 613 SER A CB 1 ATOM 4414 O OG . SER A 1 613 ? 16.744 -41.036 17.937 1.00 27.88 ? 613 SER A OG 1 ATOM 4415 N N . GLY A 1 614 ? 16.940 -37.526 17.573 1.00 26.44 ? 614 GLY A N 1 ATOM 4416 C CA . GLY A 1 614 ? 15.983 -36.634 18.190 1.00 25.65 ? 614 GLY A CA 1 ATOM 4417 C C . GLY A 1 614 ? 15.955 -35.248 17.578 1.00 24.21 ? 614 GLY A C 1 ATOM 4418 O O . GLY A 1 614 ? 16.974 -34.543 17.542 1.00 22.59 ? 614 GLY A O 1 ATOM 4419 N N . LEU A 1 615 ? 14.771 -34.868 17.108 1.00 23.27 ? 615 LEU A N 1 ATOM 4420 C CA . LEU A 1 615 ? 14.480 -33.483 16.730 1.00 23.69 ? 615 LEU A CA 1 ATOM 4421 C C . LEU A 1 615 ? 13.776 -32.769 17.884 1.00 22.77 ? 615 LEU A C 1 ATOM 4422 O O . LEU A 1 615 ? 12.675 -33.161 18.269 1.00 21.73 ? 615 LEU A O 1 ATOM 4423 C CB . LEU A 1 615 ? 13.570 -33.452 15.501 1.00 24.43 ? 615 LEU A CB 1 ATOM 4424 C CG . LEU A 1 615 ? 13.067 -32.079 15.049 1.00 24.79 ? 615 LEU A CG 1 ATOM 4425 C CD1 . LEU A 1 615 ? 14.244 -31.193 14.674 1.00 24.93 ? 615 LEU A CD1 1 ATOM 4426 C CD2 . LEU A 1 615 ? 12.093 -32.242 13.889 1.00 25.12 ? 615 LEU A CD2 1 ATOM 4427 N N . TYR A 1 616 ? 14.393 -31.705 18.394 1.00 21.95 ? 616 TYR A N 1 ATOM 4428 C CA . TYR A 1 616 ? 13.892 -30.986 19.570 1.00 22.35 ? 616 TYR A CA 1 ATOM 4429 C C . TYR A 1 616 ? 13.392 -29.591 19.192 1.00 22.08 ? 616 TYR A C 1 ATOM 4430 O O . TYR A 1 616 ? 14.075 -28.849 18.483 1.00 22.45 ? 616 TYR A O 1 ATOM 4431 C CB . TYR A 1 616 ? 15.002 -30.851 20.627 1.00 22.52 ? 616 TYR A CB 1 ATOM 4432 C CG . TYR A 1 616 ? 15.463 -32.173 21.240 1.00 23.11 ? 616 TYR A CG 1 ATOM 4433 C CD1 . TYR A 1 616 ? 16.195 -33.105 20.482 1.00 23.95 ? 616 TYR A CD1 1 ATOM 4434 C CD2 . TYR A 1 616 ? 15.200 -32.481 22.579 1.00 22.85 ? 616 TYR A CD2 1 ATOM 4435 C CE1 . TYR A 1 616 ? 16.623 -34.306 21.028 1.00 23.52 ? 616 TYR A CE1 1 ATOM 4436 C CE2 . TYR A 1 616 ? 15.632 -33.682 23.138 1.00 23.24 ? 616 TYR A CE2 1 ATOM 4437 C CZ . TYR A 1 616 ? 16.345 -34.587 22.360 1.00 24.07 ? 616 TYR A CZ 1 ATOM 4438 O OH . TYR A 1 616 ? 16.766 -35.781 22.893 1.00 24.66 ? 616 TYR A OH 1 ATOM 4439 N N . LEU A 1 617 ? 12.196 -29.246 19.654 1.00 21.42 ? 617 LEU A N 1 ATOM 4440 C CA . LEU A 1 617 ? 11.677 -27.896 19.524 1.00 20.61 ? 617 LEU A CA 1 ATOM 4441 C C . LEU A 1 617 ? 11.476 -27.308 20.913 1.00 21.02 ? 617 LEU A C 1 ATOM 4442 O O . LEU A 1 617 ? 11.103 -28.026 21.848 1.00 20.04 ? 617 LEU A O 1 ATOM 4443 C CB . LEU A 1 617 ? 10.347 -27.908 18.794 1.00 20.39 ? 617 LEU A CB 1 ATOM 4444 C CG . LEU A 1 617 ? 10.335 -28.549 17.412 1.00 20.69 ? 617 LEU A CG 1 ATOM 4445 C CD1 . LEU A 1 617 ? 8.914 -28.640 16.877 1.00 20.61 ? 617 LEU A CD1 1 ATOM 4446 C CD2 . LEU A 1 617 ? 11.228 -27.780 16.463 1.00 20.87 ? 617 LEU A CD2 1 ATOM 4447 N N . THR A 1 618 ? 11.743 -26.007 21.052 1.00 21.21 ? 618 THR A N 1 ATOM 4448 C CA . THR A 1 618 ? 11.320 -25.274 22.234 1.00 20.35 ? 618 THR A CA 1 ATOM 4449 C C . THR A 1 618 ? 10.295 -24.276 21.744 1.00 19.96 ? 618 THR A C 1 ATOM 4450 O O . THR A 1 618 ? 10.476 -23.640 20.701 1.00 19.80 ? 618 THR A O 1 ATOM 4451 C CB . THR A 1 618 ? 12.492 -24.616 22.988 1.00 21.06 ? 618 THR A CB 1 ATOM 4452 O OG1 . THR A 1 618 ? 13.136 -23.646 22.160 1.00 22.35 ? 618 THR A OG1 1 ATOM 4453 C CG2 . THR A 1 618 ? 13.520 -25.665 23.402 1.00 21.31 ? 618 THR A CG2 1 ATOM 4454 N N . ALA A 1 619 ? 9.188 -24.184 22.470 1.00 19.49 ? 619 ALA A N 1 ATOM 4455 C CA . ALA A 1 619 ? 8.057 -23.382 22.047 1.00 18.59 ? 619 ALA A CA 1 ATOM 4456 C C . ALA A 1 619 ? 7.172 -23.051 23.240 1.00 18.86 ? 619 ALA A C 1 ATOM 4457 O O . ALA A 1 619 ? 7.285 -23.689 24.291 1.00 18.71 ? 619 ALA A O 1 ATOM 4458 C CB . ALA A 1 619 ? 7.260 -24.145 21.005 1.00 18.34 ? 619 ALA A CB 1 ATOM 4459 N N . ASP A 1 620 ? 6.291 -22.064 23.050 1.00 18.39 ? 620 ASP A N 1 ATOM 4460 C CA . ASP A 1 620 ? 5.290 -21.668 24.039 1.00 18.43 ? 620 ASP A CA 1 ATOM 4461 C C . ASP A 1 620 ? 3.893 -21.785 23.438 1.00 18.45 ? 620 ASP A C 1 ATOM 4462 O O . ASP A 1 620 ? 3.715 -21.673 22.224 1.00 18.37 ? 620 ASP A O 1 ATOM 4463 C CB . ASP A 1 620 ? 5.496 -20.218 24.503 1.00 18.28 ? 620 ASP A CB 1 ATOM 4464 C CG . ASP A 1 620 ? 6.735 -20.027 25.344 1.00 18.43 ? 620 ASP A CG 1 ATOM 4465 O OD1 . ASP A 1 620 ? 7.689 -20.817 25.210 1.00 17.64 ? 620 ASP A OD1 1 ATOM 4466 O OD2 . ASP A 1 620 ? 6.761 -19.048 26.138 1.00 20.05 -1 620 ASP A OD2 1 ATOM 4467 N N . PHE A 1 621 ? 2.901 -21.971 24.298 1.00 18.48 ? 621 PHE A N 1 ATOM 4468 C CA . PHE A 1 621 ? 1.554 -22.263 23.853 1.00 18.61 ? 621 PHE A CA 1 ATOM 4469 C C . PHE A 1 621 ? 0.539 -21.569 24.750 1.00 19.02 ? 621 PHE A C 1 ATOM 4470 O O . PHE A 1 621 ? 0.587 -21.717 25.974 1.00 18.49 ? 621 PHE A O 1 ATOM 4471 C CB . PHE A 1 621 ? 1.310 -23.777 23.894 1.00 18.52 ? 621 PHE A CB 1 ATOM 4472 C CG . PHE A 1 621 ? 2.303 -24.582 23.110 1.00 18.65 ? 621 PHE A CG 1 ATOM 4473 C CD1 . PHE A 1 621 ? 3.486 -25.007 23.693 1.00 19.10 ? 621 PHE A CD1 1 ATOM 4474 C CD2 . PHE A 1 621 ? 2.047 -24.941 21.786 1.00 19.27 ? 621 PHE A CD2 1 ATOM 4475 C CE1 . PHE A 1 621 ? 4.410 -25.749 22.976 1.00 18.64 ? 621 PHE A CE1 1 ATOM 4476 C CE2 . PHE A 1 621 ? 2.966 -25.688 21.061 1.00 19.03 ? 621 PHE A CE2 1 ATOM 4477 C CZ . PHE A 1 621 ? 4.150 -26.091 21.660 1.00 19.03 ? 621 PHE A CZ 1 ATOM 4478 N N . ASN A 1 622 ? -0.386 -20.825 24.138 1.00 19.84 ? 622 ASN A N 1 ATOM 4479 C CA . ASN A 1 622 ? -1.539 -20.285 24.859 1.00 20.31 ? 622 ASN A CA 1 ATOM 4480 C C . ASN A 1 622 ? -2.856 -21.017 24.582 1.00 20.18 ? 622 ASN A C 1 ATOM 4481 O O . ASN A 1 622 ? -3.919 -20.495 24.886 1.00 19.65 ? 622 ASN A O 1 ATOM 4482 C CB . ASN A 1 622 ? -1.714 -18.797 24.573 1.00 20.62 ? 622 ASN A CB 1 ATOM 4483 C CG . ASN A 1 622 ? -2.188 -18.515 23.167 1.00 20.69 ? 622 ASN A CG 1 ATOM 4484 O OD1 . ASN A 1 622 ? -2.097 -19.361 22.277 1.00 19.81 ? 622 ASN A OD1 1 ATOM 4485 N ND2 . ASN A 1 622 ? -2.694 -17.290 22.960 1.00 21.84 ? 622 ASN A ND2 1 ATOM 4486 N N . ALA A 1 623 ? -2.770 -22.219 24.017 1.00 20.38 ? 623 ALA A N 1 ATOM 4487 C CA . ALA A 1 623 ? -3.936 -23.090 23.806 1.00 21.33 ? 623 ALA A CA 1 ATOM 4488 C C . ALA A 1 623 ? -3.448 -24.410 23.239 1.00 21.71 ? 623 ALA A C 1 ATOM 4489 O O . ALA A 1 623 ? -2.272 -24.540 22.856 1.00 21.04 ? 623 ALA A O 1 ATOM 4490 C CB . ALA A 1 623 ? -4.948 -22.459 22.854 1.00 21.68 ? 623 ALA A CB 1 ATOM 4491 N N . THR A 1 624 ? -4.342 -25.393 23.182 1.00 22.31 ? 624 THR A N 1 ATOM 4492 C CA . THR A 1 624 ? -3.968 -26.685 22.629 1.00 22.49 ? 624 THR A CA 1 ATOM 4493 C C . THR A 1 624 ? -3.705 -26.482 21.152 1.00 23.01 ? 624 THR A C 1 ATOM 4494 O O . THR A 1 624 ? -4.513 -25.909 20.451 1.00 23.90 ? 624 THR A O 1 ATOM 4495 C CB . THR A 1 624 ? -5.018 -27.768 22.911 1.00 22.31 ? 624 THR A CB 1 ATOM 4496 O OG1 . THR A 1 624 ? -5.015 -28.047 24.314 1.00 21.46 ? 624 THR A OG1 1 ATOM 4497 C CG2 . THR A 1 624 ? -4.696 -29.066 22.157 1.00 22.15 ? 624 THR A CG2 1 ATOM 4498 N N . THR A 1 625 ? -2.543 -26.926 20.703 1.00 24.00 ? 625 THR A N 1 ATOM 4499 C CA . THR A 1 625 ? -2.025 -26.523 19.417 1.00 24.57 ? 625 THR A CA 1 ATOM 4500 C C . THR A 1 625 ? -1.587 -27.753 18.634 1.00 26.31 ? 625 THR A C 1 ATOM 4501 O O . THR A 1 625 ? -1.016 -28.683 19.193 1.00 27.09 ? 625 THR A O 1 ATOM 4502 C CB . THR A 1 625 ? -0.819 -25.577 19.596 1.00 24.34 ? 625 THR A CB 1 ATOM 4503 O OG1 . THR A 1 625 ? -1.197 -24.442 20.387 1.00 23.76 ? 625 THR A OG1 1 ATOM 4504 C CG2 . THR A 1 625 ? -0.306 -25.093 18.266 1.00 24.45 ? 625 THR A CG2 1 ATOM 4505 N N . SER A 1 626 ? -1.880 -27.755 17.337 1.00 27.16 ? 626 SER A N 1 ATOM 4506 C CA . SER A 1 626 ? -1.367 -28.768 16.449 1.00 28.40 ? 626 SER A CA 1 ATOM 4507 C C . SER A 1 626 ? -0.113 -28.192 15.822 1.00 28.67 ? 626 SER A C 1 ATOM 4508 O O . SER A 1 626 ? -0.072 -27.014 15.455 1.00 30.48 ? 626 SER A O 1 ATOM 4509 C CB . SER A 1 626 ? -2.396 -29.140 15.392 1.00 29.19 ? 626 SER A CB 1 ATOM 4510 O OG . SER A 1 626 ? -2.313 -28.262 14.297 1.00 30.28 ? 626 SER A OG 1 ATOM 4511 N N . VAL A 1 627 ? 0.915 -29.029 15.739 1.00 28.19 ? 627 VAL A N 1 ATOM 4512 C CA . VAL A 1 627 ? 2.227 -28.627 15.296 1.00 26.90 ? 627 VAL A CA 1 ATOM 4513 C C . VAL A 1 627 ? 2.528 -29.428 14.045 1.00 26.67 ? 627 VAL A C 1 ATOM 4514 O O . VAL A 1 627 ? 2.286 -30.629 14.025 1.00 26.05 ? 627 VAL A O 1 ATOM 4515 C CB . VAL A 1 627 ? 3.259 -28.926 16.393 1.00 27.13 ? 627 VAL A CB 1 ATOM 4516 C CG1 . VAL A 1 627 ? 4.667 -28.611 15.935 1.00 27.18 ? 627 VAL A CG1 1 ATOM 4517 C CG2 . VAL A 1 627 ? 2.931 -28.136 17.656 1.00 27.81 ? 627 VAL A CG2 1 ATOM 4518 N N . GLU A 1 628 ? 2.993 -28.761 12.989 1.00 26.32 ? 628 GLU A N 1 ATOM 4519 C CA . GLU A 1 628 ? 3.515 -29.455 11.817 1.00 27.41 ? 628 GLU A CA 1 ATOM 4520 C C . GLU A 1 628 ? 4.959 -29.031 11.591 1.00 26.58 ? 628 GLU A C 1 ATOM 4521 O O . GLU A 1 628 ? 5.314 -27.866 11.783 1.00 25.92 ? 628 GLU A O 1 ATOM 4522 C CB . GLU A 1 628 ? 2.690 -29.165 10.568 1.00 29.36 ? 628 GLU A CB 1 ATOM 4523 C CG . GLU A 1 628 ? 1.213 -29.529 10.675 1.00 31.00 ? 628 GLU A CG 1 ATOM 4524 C CD . GLU A 1 628 ? 0.389 -28.949 9.534 1.00 33.19 ? 628 GLU A CD 1 ATOM 4525 O OE1 . GLU A 1 628 ? 0.955 -28.763 8.424 1.00 32.90 ? 628 GLU A OE1 1 ATOM 4526 O OE2 . GLU A 1 628 ? -0.817 -28.670 9.754 1.00 35.12 -1 628 GLU A OE2 1 ATOM 4527 N N . VAL A 1 629 ? 5.793 -29.990 11.214 1.00 25.75 ? 629 VAL A N 1 ATOM 4528 C CA . VAL A 1 629 ? 7.190 -29.727 10.921 1.00 25.44 ? 629 VAL A CA 1 ATOM 4529 C C . VAL A 1 629 ? 7.461 -30.144 9.475 1.00 26.60 ? 629 VAL A C 1 ATOM 4530 O O . VAL A 1 629 ? 7.197 -31.279 9.086 1.00 25.98 ? 629 VAL A O 1 ATOM 4531 C CB . VAL A 1 629 ? 8.117 -30.500 11.862 1.00 24.61 ? 629 VAL A CB 1 ATOM 4532 C CG1 . VAL A 1 629 ? 9.571 -30.146 11.594 1.00 24.89 ? 629 VAL A CG1 1 ATOM 4533 C CG2 . VAL A 1 629 ? 7.757 -30.223 13.312 1.00 25.01 ? 629 VAL A CG2 1 ATOM 4534 N N . ILE A 1 630 ? 7.979 -29.204 8.694 1.00 27.29 ? 630 ILE A N 1 ATOM 4535 C CA . ILE A 1 630 ? 8.351 -29.433 7.303 1.00 27.87 ? 630 ILE A CA 1 ATOM 4536 C C . ILE A 1 630 ? 9.862 -29.226 7.195 1.00 27.69 ? 630 ILE A C 1 ATOM 4537 O O . ILE A 1 630 ? 10.400 -28.193 7.633 1.00 27.21 ? 630 ILE A O 1 ATOM 4538 C CB . ILE A 1 630 ? 7.604 -28.445 6.384 1.00 28.93 ? 630 ILE A CB 1 ATOM 4539 C CG1 . ILE A 1 630 ? 6.087 -28.599 6.569 1.00 29.68 ? 630 ILE A CG1 1 ATOM 4540 C CG2 . ILE A 1 630 ? 8.000 -28.653 4.927 1.00 29.34 ? 630 ILE A CG2 1 ATOM 4541 C CD1 . ILE A 1 630 ? 5.308 -27.314 6.426 1.00 30.59 ? 630 ILE A CD1 1 ATOM 4542 N N . GLY A 1 631 ? 10.542 -30.223 6.637 1.00 27.59 ? 631 GLY A N 1 ATOM 4543 C CA . GLY A 1 631 ? 12.004 -30.242 6.584 1.00 28.88 ? 631 GLY A CA 1 ATOM 4544 C C . GLY A 1 631 ? 12.667 -31.103 7.652 1.00 30.16 ? 631 GLY A C 1 ATOM 4545 O O . GLY A 1 631 ? 13.819 -30.855 8.032 1.00 29.55 ? 631 GLY A O 1 ATOM 4546 N N . VAL A 1 632 ? 11.958 -32.129 8.125 1.00 31.65 ? 632 VAL A N 1 ATOM 4547 C CA . VAL A 1 632 ? 12.498 -33.007 9.160 1.00 32.64 ? 632 VAL A CA 1 ATOM 4548 C C . VAL A 1 632 ? 13.668 -33.783 8.565 1.00 32.97 ? 632 VAL A C 1 ATOM 4549 O O . VAL A 1 632 ? 13.495 -34.461 7.559 1.00 33.17 ? 632 VAL A O 1 ATOM 4550 C CB . VAL A 1 632 ? 11.457 -34.006 9.682 1.00 32.94 ? 632 VAL A CB 1 ATOM 4551 C CG1 . VAL A 1 632 ? 12.078 -34.924 10.731 1.00 32.84 ? 632 VAL A CG1 1 ATOM 4552 C CG2 . VAL A 1 632 ? 10.257 -33.275 10.267 1.00 34.19 ? 632 VAL A CG2 1 ATOM 4553 N N . PRO A 1 633 ? 14.866 -33.667 9.166 1.00 33.17 ? 633 PRO A N 1 ATOM 4554 C CA . PRO A 1 633 ? 16.016 -34.364 8.590 1.00 33.63 ? 633 PRO A CA 1 ATOM 4555 C C . PRO A 1 633 ? 15.825 -35.875 8.611 1.00 33.51 ? 633 PRO A C 1 ATOM 4556 O O . PRO A 1 633 ? 15.226 -36.400 9.536 1.00 32.99 ? 633 PRO A O 1 ATOM 4557 C CB . PRO A 1 633 ? 17.186 -33.951 9.494 1.00 34.78 ? 633 PRO A CB 1 ATOM 4558 C CG . PRO A 1 633 ? 16.720 -32.757 10.253 1.00 34.76 ? 633 PRO A CG 1 ATOM 4559 C CD . PRO A 1 633 ? 15.228 -32.846 10.336 1.00 34.05 ? 633 PRO A CD 1 ATOM 4560 N N . SER A 1 634 ? 16.333 -36.554 7.591 1.00 35.30 ? 634 SER A N 1 ATOM 4561 C CA . SER A 1 634 ? 16.128 -38.000 7.413 1.00 36.67 ? 634 SER A CA 1 ATOM 4562 C C . SER A 1 634 ? 16.631 -38.862 8.577 1.00 38.13 ? 634 SER A C 1 ATOM 4563 O O . SER A 1 634 ? 16.130 -39.967 8.787 1.00 40.18 ? 634 SER A O 1 ATOM 4564 C CB . SER A 1 634 ? 16.804 -38.466 6.124 1.00 36.43 ? 634 SER A CB 1 ATOM 4565 O OG . SER A 1 634 ? 18.181 -38.112 6.115 1.00 35.47 ? 634 SER A OG 1 ATOM 4566 N N . THR A 1 635 ? 17.621 -38.361 9.319 1.00 39.12 ? 635 THR A N 1 ATOM 4567 C CA . THR A 1 635 ? 18.145 -39.047 10.508 1.00 39.06 ? 635 THR A CA 1 ATOM 4568 C C . THR A 1 635 ? 17.241 -38.926 11.762 1.00 38.78 ? 635 THR A C 1 ATOM 4569 O O . THR A 1 635 ? 17.530 -39.543 12.792 1.00 39.13 ? 635 THR A O 1 ATOM 4570 C CB . THR A 1 635 ? 19.555 -38.523 10.857 1.00 39.63 ? 635 THR A CB 1 ATOM 4571 O OG1 . THR A 1 635 ? 19.511 -37.099 11.052 1.00 41.14 ? 635 THR A OG1 1 ATOM 4572 C CG2 . THR A 1 635 ? 20.539 -38.843 9.737 1.00 39.62 ? 635 THR A CG2 1 ATOM 4573 N N . ALA A 1 636 ? 16.156 -38.154 11.676 1.00 37.03 ? 636 ALA A N 1 ATOM 4574 C CA . ALA A 1 636 ? 15.272 -37.910 12.821 1.00 36.56 ? 636 ALA A CA 1 ATOM 4575 C C . ALA A 1 636 ? 14.173 -38.962 12.922 1.00 36.43 ? 636 ALA A C 1 ATOM 4576 O O . ALA A 1 636 ? 13.485 -39.242 11.945 1.00 34.78 ? 636 ALA A O 1 ATOM 4577 C CB . ALA A 1 636 ? 14.652 -36.523 12.719 1.00 36.29 ? 636 ALA A CB 1 ATOM 4578 N N . LYS A 1 637 ? 14.013 -39.535 14.113 1.00 37.23 ? 637 LYS A N 1 ATOM 4579 C CA . LYS A 1 637 ? 12.999 -40.562 14.361 1.00 37.37 ? 637 LYS A CA 1 ATOM 4580 C C . LYS A 1 637 ? 11.951 -40.162 15.393 1.00 34.82 ? 637 LYS A C 1 ATOM 4581 O O . LYS A 1 637 ? 10.823 -40.650 15.344 1.00 35.87 ? 637 LYS A O 1 ATOM 4582 C CB . LYS A 1 637 ? 13.669 -41.876 14.784 1.00 40.36 ? 637 LYS A CB 1 ATOM 4583 C CG . LYS A 1 637 ? 13.759 -42.919 13.679 1.00 42.70 ? 637 LYS A CG 1 ATOM 4584 C CD . LYS A 1 637 ? 14.757 -42.555 12.586 1.00 44.08 ? 637 LYS A CD 1 ATOM 4585 C CE . LYS A 1 637 ? 14.521 -43.391 11.333 1.00 46.48 ? 637 LYS A CE 1 ATOM 4586 N NZ . LYS A 1 637 ? 15.519 -43.148 10.251 1.00 47.89 ? 637 LYS A NZ 1 ATOM 4587 N N . ASN A 1 638 ? 12.308 -39.288 16.329 1.00 32.54 ? 638 ASN A N 1 ATOM 4588 C CA . ASN A 1 638 ? 11.374 -38.864 17.375 1.00 30.54 ? 638 ASN A CA 1 ATOM 4589 C C . ASN A 1 638 ? 11.300 -37.355 17.480 1.00 28.97 ? 638 ASN A C 1 ATOM 4590 O O . ASN A 1 638 ? 12.240 -36.653 17.118 1.00 29.63 ? 638 ASN A O 1 ATOM 4591 C CB . ASN A 1 638 ? 11.809 -39.437 18.717 1.00 31.23 ? 638 ASN A CB 1 ATOM 4592 C CG . ASN A 1 638 ? 12.013 -40.941 18.665 1.00 31.91 ? 638 ASN A CG 1 ATOM 4593 O OD1 . ASN A 1 638 ? 11.055 -41.707 18.604 1.00 31.81 ? 638 ASN A OD1 1 ATOM 4594 N ND2 . ASN A 1 638 ? 13.263 -41.364 18.678 1.00 30.69 ? 638 ASN A ND2 1 ATOM 4595 N N . LEU A 1 639 ? 10.182 -36.859 17.993 1.00 27.30 ? 639 LEU A N 1 ATOM 4596 C CA . LEU A 1 639 ? 10.014 -35.437 18.222 1.00 25.86 ? 639 LEU A CA 1 ATOM 4597 C C . LEU A 1 639 ? 9.950 -35.189 19.720 1.00 25.58 ? 639 LEU A C 1 ATOM 4598 O O . LEU A 1 639 ? 9.207 -35.859 20.436 1.00 24.37 ? 639 LEU A O 1 ATOM 4599 C CB . LEU A 1 639 ? 8.743 -34.931 17.537 1.00 25.11 ? 639 LEU A CB 1 ATOM 4600 C CG . LEU A 1 639 ? 8.457 -33.425 17.611 1.00 24.63 ? 639 LEU A CG 1 ATOM 4601 C CD1 . LEU A 1 639 ? 9.446 -32.619 16.793 1.00 24.39 ? 639 LEU A CD1 1 ATOM 4602 C CD2 . LEU A 1 639 ? 7.042 -33.130 17.151 1.00 25.18 ? 639 LEU A CD2 1 ATOM 4603 N N . PHE A 1 640 ? 10.762 -34.242 20.184 1.00 25.76 ? 640 PHE A N 1 ATOM 4604 C CA . PHE A 1 640 ? 10.647 -33.693 21.536 1.00 26.33 ? 640 PHE A CA 1 ATOM 4605 C C . PHE A 1 640 ? 10.159 -32.250 21.464 1.00 26.15 ? 640 PHE A C 1 ATOM 4606 O O . PHE A 1 640 ? 10.609 -31.469 20.613 1.00 25.65 ? 640 PHE A O 1 ATOM 4607 C CB . PHE A 1 640 ? 11.994 -33.739 22.255 1.00 26.90 ? 640 PHE A CB 1 ATOM 4608 C CG . PHE A 1 640 ? 12.529 -35.127 22.440 1.00 27.16 ? 640 PHE A CG 1 ATOM 4609 C CD1 . PHE A 1 640 ? 12.211 -35.862 23.576 1.00 26.54 ? 640 PHE A CD1 1 ATOM 4610 C CD2 . PHE A 1 640 ? 13.342 -35.706 21.469 1.00 27.04 ? 640 PHE A CD2 1 ATOM 4611 C CE1 . PHE A 1 640 ? 12.697 -37.143 23.742 1.00 27.03 ? 640 PHE A CE1 1 ATOM 4612 C CE2 . PHE A 1 640 ? 13.829 -36.992 21.630 1.00 27.40 ? 640 PHE A CE2 1 ATOM 4613 C CZ . PHE A 1 640 ? 13.506 -37.712 22.768 1.00 27.33 ? 640 PHE A CZ 1 ATOM 4614 N N . ILE A 1 641 ? 9.220 -31.910 22.342 1.00 26.83 ? 641 ILE A N 1 ATOM 4615 C CA . ILE A 1 641 ? 8.757 -30.532 22.498 1.00 27.79 ? 641 ILE A CA 1 ATOM 4616 C C . ILE A 1 641 ? 8.954 -30.115 23.951 1.00 28.02 ? 641 ILE A C 1 ATOM 4617 O O . ILE A 1 641 ? 8.380 -30.729 24.853 1.00 27.99 ? 641 ILE A O 1 ATOM 4618 C CB . ILE A 1 641 ? 7.288 -30.387 22.069 1.00 28.10 ? 641 ILE A CB 1 ATOM 4619 C CG1 . ILE A 1 641 ? 7.197 -30.476 20.537 1.00 29.23 ? 641 ILE A CG1 1 ATOM 4620 C CG2 . ILE A 1 641 ? 6.725 -29.054 22.538 1.00 28.71 ? 641 ILE A CG2 1 ATOM 4621 C CD1 . ILE A 1 641 ? 5.830 -30.811 19.987 1.00 29.55 ? 641 ILE A CD1 1 ATOM 4622 N N . ASN A 1 642 ? 9.769 -29.078 24.162 1.00 27.72 ? 642 ASN A N 1 ATOM 4623 C CA . ASN A 1 642 ? 10.179 -28.631 25.500 1.00 28.43 ? 642 ASN A CA 1 ATOM 4624 C C . ASN A 1 642 ? 10.709 -29.782 26.352 1.00 29.35 ? 642 ASN A C 1 ATOM 4625 O O . ASN A 1 642 ? 10.362 -29.922 27.527 1.00 29.37 ? 642 ASN A O 1 ATOM 4626 C CB . ASN A 1 642 ? 9.027 -27.908 26.217 1.00 28.69 ? 642 ASN A CB 1 ATOM 4627 C CG . ASN A 1 642 ? 8.632 -26.602 25.536 1.00 28.92 ? 642 ASN A CG 1 ATOM 4628 O OD1 . ASN A 1 642 ? 9.384 -26.044 24.744 1.00 30.65 ? 642 ASN A OD1 1 ATOM 4629 N ND2 . ASN A 1 642 ? 7.453 -26.108 25.857 1.00 29.07 ? 642 ASN A ND2 1 ATOM 4630 N N . GLY A 1 643 ? 11.540 -30.614 25.735 1.00 31.06 ? 643 GLY A N 1 ATOM 4631 C CA . GLY A 1 643 ? 12.111 -31.789 26.392 1.00 31.86 ? 643 GLY A CA 1 ATOM 4632 C C . GLY A 1 643 ? 11.226 -33.029 26.466 1.00 32.26 ? 643 GLY A C 1 ATOM 4633 O O . GLY A 1 643 ? 11.721 -34.100 26.767 1.00 33.81 ? 643 GLY A O 1 ATOM 4634 N N . ASP A 1 644 ? 9.927 -32.908 26.205 1.00 33.26 ? 644 ASP A N 1 ATOM 4635 C CA . ASP A 1 644 ? 8.999 -34.041 26.390 1.00 34.98 ? 644 ASP A CA 1 ATOM 4636 C C . ASP A 1 644 ? 8.755 -34.781 25.087 1.00 34.54 ? 644 ASP A C 1 ATOM 4637 O O . ASP A 1 644 ? 8.358 -34.164 24.097 1.00 33.02 ? 644 ASP A O 1 ATOM 4638 C CB . ASP A 1 644 ? 7.664 -33.564 26.960 1.00 35.21 ? 644 ASP A CB 1 ATOM 4639 C CG . ASP A 1 644 ? 7.806 -32.964 28.354 1.00 37.30 ? 644 ASP A CG 1 ATOM 4640 O OD1 . ASP A 1 644 ? 8.814 -33.260 29.036 1.00 36.87 ? 644 ASP A OD1 1 ATOM 4641 O OD2 . ASP A 1 644 ? 6.908 -32.191 28.763 1.00 38.22 -1 644 ASP A OD2 1 ATOM 4642 N N . LYS A 1 645 ? 9.003 -36.094 25.089 1.00 35.38 ? 645 LYS A N 1 ATOM 4643 C CA . LYS A 1 645 ? 8.786 -36.918 23.902 1.00 36.89 ? 645 LYS A CA 1 ATOM 4644 C C . LYS A 1 645 ? 7.316 -36.834 23.543 1.00 36.22 ? 645 LYS A C 1 ATOM 4645 O O . LYS A 1 645 ? 6.449 -37.005 24.399 1.00 36.21 ? 645 LYS A O 1 ATOM 4646 C CB . LYS A 1 645 ? 9.201 -38.380 24.121 1.00 39.71 ? 645 LYS A CB 1 ATOM 4647 C CG . LYS A 1 645 ? 8.983 -39.270 22.895 1.00 42.31 ? 645 LYS A CG 1 ATOM 4648 C CD . LYS A 1 645 ? 9.569 -40.668 23.064 1.00 45.01 ? 645 LYS A CD 1 ATOM 4649 C CE . LYS A 1 645 ? 11.051 -40.714 22.716 1.00 47.13 ? 645 LYS A CE 1 ATOM 4650 N NZ . LYS A 1 645 ? 11.713 -41.973 23.182 1.00 47.71 ? 645 LYS A NZ 1 ATOM 4651 N N . THR A 1 646 ? 7.046 -36.530 22.280 1.00 35.84 ? 646 THR A N 1 ATOM 4652 C CA . THR A 1 646 ? 5.686 -36.295 21.827 1.00 35.93 ? 646 THR A CA 1 ATOM 4653 C C . THR A 1 646 ? 5.442 -37.144 20.594 1.00 35.83 ? 646 THR A C 1 ATOM 4654 O O . THR A 1 646 ? 6.281 -37.187 19.681 1.00 36.15 ? 646 THR A O 1 ATOM 4655 C CB . THR A 1 646 ? 5.455 -34.803 21.515 1.00 35.58 ? 646 THR A CB 1 ATOM 4656 O OG1 . THR A 1 646 ? 5.878 -34.012 22.635 1.00 34.54 ? 646 THR A OG1 1 ATOM 4657 C CG2 . THR A 1 646 ? 3.991 -34.520 21.234 1.00 35.53 ? 646 THR A CG2 1 ATOM 4658 N N . SER A 1 647 ? 4.293 -37.821 20.590 1.00 34.73 ? 647 SER A N 1 ATOM 4659 C CA . SER A 1 647 ? 3.887 -38.703 19.499 1.00 34.23 ? 647 SER A CA 1 ATOM 4660 C C . SER A 1 647 ? 3.674 -37.899 18.236 1.00 33.54 ? 647 SER A C 1 ATOM 4661 O O . SER A 1 647 ? 3.170 -36.780 18.289 1.00 35.17 ? 647 SER A O 1 ATOM 4662 C CB . SER A 1 647 ? 2.578 -39.417 19.851 1.00 34.39 ? 647 SER A CB 1 ATOM 4663 O OG . SER A 1 647 ? 2.684 -40.097 21.088 1.00 35.39 ? 647 SER A OG 1 ATOM 4664 N N . HIS A 1 648 ? 4.054 -38.468 17.100 1.00 33.21 ? 648 HIS A N 1 ATOM 4665 C CA . HIS A 1 648 ? 3.848 -37.807 15.828 1.00 33.17 ? 648 HIS A CA 1 ATOM 4666 C C . HIS A 1 648 ? 3.415 -38.791 14.759 1.00 34.36 ? 648 HIS A C 1 ATOM 4667 O O . HIS A 1 648 ? 3.749 -39.969 14.830 1.00 34.98 ? 648 HIS A O 1 ATOM 4668 C CB . HIS A 1 648 ? 5.118 -37.083 15.391 1.00 32.39 ? 648 HIS A CB 1 ATOM 4669 C CG . HIS A 1 648 ? 6.220 -37.994 14.954 1.00 32.55 ? 648 HIS A CG 1 ATOM 4670 N ND1 . HIS A 1 648 ? 7.073 -38.608 15.842 1.00 32.48 ? 648 HIS A ND1 1 ATOM 4671 C CD2 . HIS A 1 648 ? 6.620 -38.385 13.720 1.00 33.07 ? 648 HIS A CD2 1 ATOM 4672 C CE1 . HIS A 1 648 ? 7.944 -39.345 15.178 1.00 32.18 ? 648 HIS A CE1 1 ATOM 4673 N NE2 . HIS A 1 648 ? 7.694 -39.223 13.888 1.00 32.78 ? 648 HIS A NE2 1 ATOM 4674 N N . THR A 1 649 ? 2.660 -38.291 13.781 1.00 35.53 ? 649 THR A N 1 ATOM 4675 C CA . THR A 1 649 ? 2.346 -39.031 12.566 1.00 36.03 ? 649 THR A CA 1 ATOM 4676 C C . THR A 1 649 ? 2.970 -38.306 11.390 1.00 36.54 ? 649 THR A C 1 ATOM 4677 O O . THR A 1 649 ? 3.162 -37.095 11.426 1.00 35.07 ? 649 THR A O 1 ATOM 4678 C CB . THR A 1 649 ? 0.828 -39.171 12.341 1.00 37.13 ? 649 THR A CB 1 ATOM 4679 O OG1 . THR A 1 649 ? 0.210 -37.883 12.394 1.00 38.36 ? 649 THR A OG1 1 ATOM 4680 C CG2 . THR A 1 649 ? 0.199 -40.061 13.422 1.00 38.47 ? 649 THR A CG2 1 ATOM 4681 N N . VAL A 1 650 ? 3.299 -39.074 10.358 1.00 37.47 ? 650 VAL A N 1 ATOM 4682 C CA . VAL A 1 650 ? 3.902 -38.560 9.134 1.00 37.04 ? 650 VAL A CA 1 ATOM 4683 C C . VAL A 1 650 ? 2.872 -38.744 8.026 1.00 36.60 ? 650 VAL A C 1 ATOM 4684 O O . VAL A 1 650 ? 2.340 -39.840 7.860 1.00 38.70 ? 650 VAL A O 1 ATOM 4685 C CB . VAL A 1 650 ? 5.206 -39.329 8.817 1.00 36.59 ? 650 VAL A CB 1 ATOM 4686 C CG1 . VAL A 1 650 ? 5.920 -38.747 7.601 1.00 36.18 ? 650 VAL A CG1 1 ATOM 4687 C CG2 . VAL A 1 650 ? 6.121 -39.317 10.037 1.00 36.44 ? 650 VAL A CG2 1 ATOM 4688 N N . ASP A 1 651 ? 2.560 -37.679 7.291 1.00 33.72 ? 651 ASP A N 1 ATOM 4689 C CA . ASP A 1 651 ? 1.547 -37.773 6.240 1.00 32.70 ? 651 ASP A CA 1 ATOM 4690 C C . ASP A 1 651 ? 2.202 -38.115 4.893 1.00 33.24 ? 651 ASP A C 1 ATOM 4691 O O . ASP A 1 651 ? 3.426 -38.269 4.812 1.00 32.93 ? 651 ASP A O 1 ATOM 4692 C CB . ASP A 1 651 ? 0.643 -36.515 6.199 1.00 31.62 ? 651 ASP A CB 1 ATOM 4693 C CG . ASP A 1 651 ? 1.325 -35.262 5.610 1.00 31.38 ? 651 ASP A CG 1 ATOM 4694 O OD1 . ASP A 1 651 ? 2.516 -35.285 5.185 1.00 28.34 ? 651 ASP A OD1 1 ATOM 4695 O OD2 . ASP A 1 651 ? 0.614 -34.229 5.577 1.00 31.06 -1 651 ASP A OD2 1 ATOM 4696 N N . LYS A 1 652 ? 1.389 -38.247 3.849 1.00 34.00 ? 652 LYS A N 1 ATOM 4697 C CA . LYS A 1 652 ? 1.890 -38.648 2.520 1.00 36.22 ? 652 LYS A CA 1 ATOM 4698 C C . LYS A 1 652 ? 2.963 -37.715 1.926 1.00 36.64 ? 652 LYS A C 1 ATOM 4699 O O . LYS A 1 652 ? 3.678 -38.102 1.001 1.00 35.73 ? 652 LYS A O 1 ATOM 4700 C CB . LYS A 1 652 ? 0.724 -38.799 1.534 1.00 37.06 ? 652 LYS A CB 1 ATOM 4701 C CG . LYS A 1 652 ? 0.049 -37.493 1.123 1.00 38.06 ? 652 LYS A CG 1 ATOM 4702 C CD . LYS A 1 652 ? -1.308 -37.767 0.492 1.00 38.72 ? 652 LYS A CD 1 ATOM 4703 C CE . LYS A 1 652 ? -1.857 -36.549 -0.241 1.00 39.39 ? 652 LYS A CE 1 ATOM 4704 N NZ . LYS A 1 652 ? -1.354 -36.459 -1.643 1.00 39.80 ? 652 LYS A NZ 1 ATOM 4705 N N . ASN A 1 653 ? 3.070 -36.493 2.452 1.00 36.14 ? 653 ASN A N 1 ATOM 4706 C CA . ASN A 1 653 ? 4.064 -35.538 1.979 1.00 34.82 ? 653 ASN A CA 1 ATOM 4707 C C . ASN A 1 653 ? 5.283 -35.371 2.896 1.00 34.75 ? 653 ASN A C 1 ATOM 4708 O O . ASN A 1 653 ? 6.069 -34.442 2.715 1.00 33.13 ? 653 ASN A O 1 ATOM 4709 C CB . ASN A 1 653 ? 3.378 -34.200 1.719 1.00 34.45 ? 653 ASN A CB 1 ATOM 4710 C CG . ASN A 1 653 ? 2.506 -34.241 0.485 1.00 34.88 ? 653 ASN A CG 1 ATOM 4711 O OD1 . ASN A 1 653 ? 2.937 -34.728 -0.569 1.00 36.54 ? 653 ASN A OD1 1 ATOM 4712 N ND2 . ASN A 1 653 ? 1.276 -33.744 0.600 1.00 34.18 ? 653 ASN A ND2 1 ATOM 4713 N N . GLY A 1 654 ? 5.446 -36.272 3.865 1.00 35.04 ? 654 GLY A N 1 ATOM 4714 C CA . GLY A 1 654 ? 6.615 -36.245 4.752 1.00 34.93 ? 654 GLY A CA 1 ATOM 4715 C C . GLY A 1 654 ? 6.550 -35.229 5.886 1.00 33.89 ? 654 GLY A C 1 ATOM 4716 O O . GLY A 1 654 ? 7.541 -35.009 6.582 1.00 35.06 ? 654 GLY A O 1 ATOM 4717 N N . ILE A 1 655 ? 5.384 -34.624 6.081 1.00 33.15 ? 655 ILE A N 1 ATOM 4718 C CA . ILE A 1 655 ? 5.178 -33.625 7.121 1.00 32.78 ? 655 ILE A CA 1 ATOM 4719 C C . ILE A 1 655 ? 4.827 -34.324 8.437 1.00 32.97 ? 655 ILE A C 1 ATOM 4720 O O . ILE A 1 655 ? 3.851 -35.071 8.516 1.00 33.05 ? 655 ILE A O 1 ATOM 4721 C CB . ILE A 1 655 ? 4.033 -32.659 6.740 1.00 32.82 ? 655 ILE A CB 1 ATOM 4722 C CG1 . ILE A 1 655 ? 4.381 -31.921 5.437 1.00 33.16 ? 655 ILE A CG1 1 ATOM 4723 C CG2 . ILE A 1 655 ? 3.741 -31.683 7.879 1.00 32.26 ? 655 ILE A CG2 1 ATOM 4724 C CD1 . ILE A 1 655 ? 3.296 -30.981 4.948 1.00 33.39 ? 655 ILE A CD1 1 ATOM 4725 N N . TRP A 1 656 ? 5.623 -34.068 9.466 1.00 32.65 ? 656 TRP A N 1 ATOM 4726 C CA . TRP A 1 656 ? 5.345 -34.591 10.795 1.00 32.58 ? 656 TRP A CA 1 ATOM 4727 C C . TRP A 1 656 ? 4.258 -33.755 11.425 1.00 32.06 ? 656 TRP A C 1 ATOM 4728 O O . TRP A 1 656 ? 4.324 -32.535 11.377 1.00 33.43 ? 656 TRP A O 1 ATOM 4729 C CB . TRP A 1 656 ? 6.593 -34.526 11.669 1.00 33.09 ? 656 TRP A CB 1 ATOM 4730 C CG . TRP A 1 656 ? 7.593 -35.596 11.396 1.00 33.96 ? 656 TRP A CG 1 ATOM 4731 C CD1 . TRP A 1 656 ? 7.719 -36.329 10.260 1.00 35.00 ? 656 TRP A CD1 1 ATOM 4732 C CD2 . TRP A 1 656 ? 8.634 -36.030 12.272 1.00 34.15 ? 656 TRP A CD2 1 ATOM 4733 N NE1 . TRP A 1 656 ? 8.765 -37.205 10.376 1.00 36.30 ? 656 TRP A NE1 1 ATOM 4734 C CE2 . TRP A 1 656 ? 9.341 -37.047 11.607 1.00 35.75 ? 656 TRP A CE2 1 ATOM 4735 C CE3 . TRP A 1 656 ? 9.031 -35.661 13.561 1.00 35.23 ? 656 TRP A CE3 1 ATOM 4736 C CZ2 . TRP A 1 656 ? 10.431 -37.704 12.181 1.00 36.09 ? 656 TRP A CZ2 1 ATOM 4737 C CZ3 . TRP A 1 656 ? 10.113 -36.316 14.138 1.00 36.64 ? 656 TRP A CZ3 1 ATOM 4738 C CH2 . TRP A 1 656 ? 10.802 -37.324 13.445 1.00 36.64 ? 656 TRP A CH2 1 ATOM 4739 N N . SER A 1 657 ? 3.266 -34.424 12.005 1.00 32.34 ? 657 SER A N 1 ATOM 4740 C CA . SER A 1 657 ? 2.166 -33.789 12.729 1.00 32.16 ? 657 SER A CA 1 ATOM 4741 C C . SER A 1 657 ? 2.126 -34.282 14.176 1.00 31.39 ? 657 SER A C 1 ATOM 4742 O O . SER A 1 657 ? 2.337 -35.465 14.442 1.00 29.13 ? 657 SER A O 1 ATOM 4743 C CB . SER A 1 657 ? 0.830 -34.114 12.062 1.00 32.29 ? 657 SER A CB 1 ATOM 4744 O OG . SER A 1 657 ? 0.507 -33.140 11.095 1.00 33.97 ? 657 SER A OG 1 ATOM 4745 N N . ALA A 1 658 ? 1.838 -33.367 15.098 1.00 30.01 ? 658 ALA A N 1 ATOM 4746 C CA . ALA A 1 658 ? 1.754 -33.691 16.515 1.00 28.30 ? 658 ALA A CA 1 ATOM 4747 C C . ALA A 1 658 ? 0.856 -32.704 17.218 1.00 28.79 ? 658 ALA A C 1 ATOM 4748 O O . ALA A 1 658 ? 0.505 -31.659 16.665 1.00 27.81 ? 658 ALA A O 1 ATOM 4749 C CB . ALA A 1 658 ? 3.131 -33.677 17.141 1.00 28.53 ? 658 ALA A CB 1 ATOM 4750 N N . THR A 1 659 ? 0.484 -33.050 18.445 1.00 29.61 ? 659 THR A N 1 ATOM 4751 C CA . THR A 1 659 ? -0.434 -32.245 19.243 1.00 31.00 ? 659 THR A CA 1 ATOM 4752 C C . THR A 1 659 ? 0.172 -31.949 20.609 1.00 29.49 ? 659 THR A C 1 ATOM 4753 O O . THR A 1 659 ? 0.746 -32.833 21.267 1.00 27.98 ? 659 THR A O 1 ATOM 4754 C CB . THR A 1 659 ? -1.774 -32.970 19.438 1.00 33.02 ? 659 THR A CB 1 ATOM 4755 O OG1 . THR A 1 659 ? -2.199 -33.501 18.181 1.00 36.10 ? 659 THR A OG1 1 ATOM 4756 C CG2 . THR A 1 659 ? -2.852 -32.026 19.979 1.00 33.31 ? 659 THR A CG2 1 ATOM 4757 N N . VAL A 1 660 ? 0.037 -30.695 21.019 1.00 27.25 ? 660 VAL A N 1 ATOM 4758 C CA . VAL A 1 660 ? 0.548 -30.238 22.295 1.00 26.77 ? 660 VAL A CA 1 ATOM 4759 C C . VAL A 1 660 ? -0.646 -29.774 23.105 1.00 25.69 ? 660 VAL A C 1 ATOM 4760 O O . VAL A 1 660 ? -1.325 -28.827 22.727 1.00 25.60 ? 660 VAL A O 1 ATOM 4761 C CB . VAL A 1 660 ? 1.568 -29.099 22.130 1.00 26.30 ? 660 VAL A CB 1 ATOM 4762 C CG1 . VAL A 1 660 ? 2.073 -28.635 23.491 1.00 26.52 ? 660 VAL A CG1 1 ATOM 4763 C CG2 . VAL A 1 660 ? 2.728 -29.555 21.250 1.00 26.31 ? 660 VAL A CG2 1 ATOM 4764 N N . ASP A 1 661 ? -0.901 -30.469 24.207 1.00 26.19 ? 661 ASP A N 1 ATOM 4765 C CA . ASP A 1 661 ? -2.071 -30.220 25.043 1.00 27.48 ? 661 ASP A CA 1 ATOM 4766 C C . ASP A 1 661 ? -1.802 -29.068 25.999 1.00 26.15 ? 661 ASP A C 1 ATOM 4767 O O . ASP A 1 661 ? -0.696 -28.912 26.500 1.00 25.58 ? 661 ASP A O 1 ATOM 4768 C CB . ASP A 1 661 ? -2.448 -31.486 25.821 1.00 29.26 ? 661 ASP A CB 1 ATOM 4769 C CG . ASP A 1 661 ? -2.935 -32.615 24.910 1.00 31.51 ? 661 ASP A CG 1 ATOM 4770 O OD1 . ASP A 1 661 ? -3.923 -32.405 24.176 1.00 32.81 ? 661 ASP A OD1 1 ATOM 4771 O OD2 . ASP A 1 661 ? -2.341 -33.717 24.939 1.00 33.57 -1 661 ASP A OD2 1 ATOM 4772 N N . TYR A 1 662 ? -2.831 -28.268 26.236 1.00 26.52 ? 662 TYR A N 1 ATOM 4773 C CA . TYR A 1 662 ? -2.742 -27.086 27.072 1.00 26.40 ? 662 TYR A CA 1 ATOM 4774 C C . TYR A 1 662 ? -3.726 -27.286 28.196 1.00 28.41 ? 662 TYR A C 1 ATOM 4775 O O . TYR A 1 662 ? -4.920 -27.379 27.951 1.00 29.88 ? 662 TYR A O 1 ATOM 4776 C CB . TYR A 1 662 ? -3.106 -25.849 26.246 1.00 25.10 ? 662 TYR A CB 1 ATOM 4777 C CG . TYR A 1 662 ? -3.201 -24.569 27.031 1.00 23.74 ? 662 TYR A CG 1 ATOM 4778 C CD1 . TYR A 1 662 ? -4.332 -24.275 27.772 1.00 23.66 ? 662 TYR A CD1 1 ATOM 4779 C CD2 . TYR A 1 662 ? -2.167 -23.644 27.020 1.00 22.68 ? 662 TYR A CD2 1 ATOM 4780 C CE1 . TYR A 1 662 ? -4.424 -23.110 28.503 1.00 23.88 ? 662 TYR A CE1 1 ATOM 4781 C CE2 . TYR A 1 662 ? -2.251 -22.471 27.738 1.00 22.28 ? 662 TYR A CE2 1 ATOM 4782 C CZ . TYR A 1 662 ? -3.384 -22.204 28.472 1.00 23.02 ? 662 TYR A CZ 1 ATOM 4783 O OH . TYR A 1 662 ? -3.500 -21.046 29.198 1.00 22.60 ? 662 TYR A OH 1 ATOM 4784 N N . ASN A 1 663 ? -3.227 -27.375 29.422 1.00 31.82 ? 663 ASN A N 1 ATOM 4785 C CA . ASN A 1 663 ? -4.079 -27.520 30.602 1.00 34.38 ? 663 ASN A CA 1 ATOM 4786 C C . ASN A 1 663 ? -3.507 -26.730 31.759 1.00 32.62 ? 663 ASN A C 1 ATOM 4787 O O . ASN A 1 663 ? -2.711 -27.245 32.539 1.00 32.23 ? 663 ASN A O 1 ATOM 4788 C CB . ASN A 1 663 ? -4.231 -28.992 30.977 1.00 37.05 ? 663 ASN A CB 1 ATOM 4789 C CG . ASN A 1 663 ? -4.832 -29.800 29.851 1.00 41.87 ? 663 ASN A CG 1 ATOM 4790 O OD1 . ASN A 1 663 ? -6.024 -29.660 29.541 1.00 47.00 ? 663 ASN A OD1 1 ATOM 4791 N ND2 . ASN A 1 663 ? -4.008 -30.619 29.197 1.00 43.22 ? 663 ASN A ND2 1 ATOM 4792 N N . ALA A 1 664 ? -3.905 -25.466 31.847 1.00 32.56 ? 664 ALA A N 1 ATOM 4793 C CA . ALA A 1 664 ? -3.459 -24.608 32.919 1.00 33.44 ? 664 ALA A CA 1 ATOM 4794 C C . ALA A 1 664 ? -3.919 -25.197 34.235 1.00 33.92 ? 664 ALA A C 1 ATOM 4795 O O . ALA A 1 664 ? -5.048 -25.669 34.339 1.00 30.99 ? 664 ALA A O 1 ATOM 4796 C CB . ALA A 1 664 ? -4.012 -23.207 32.755 1.00 33.34 ? 664 ALA A CB 1 ATOM 4797 N N . PRO A 1 665 ? -3.030 -25.202 35.243 1.00 36.41 ? 665 PRO A N 1 ATOM 4798 C CA . PRO A 1 665 ? -3.530 -25.533 36.565 1.00 37.49 ? 665 PRO A CA 1 ATOM 4799 C C . PRO A 1 665 ? -4.218 -24.333 37.184 1.00 37.09 ? 665 PRO A C 1 ATOM 4800 O O . PRO A 1 665 ? -4.236 -23.244 36.600 1.00 34.34 ? 665 PRO A O 1 ATOM 4801 C CB . PRO A 1 665 ? -2.267 -25.911 37.364 1.00 37.10 ? 665 PRO A CB 1 ATOM 4802 C CG . PRO A 1 665 ? -1.148 -25.962 36.379 1.00 37.60 ? 665 PRO A CG 1 ATOM 4803 C CD . PRO A 1 665 ? -1.561 -25.101 35.223 1.00 37.34 ? 665 PRO A CD 1 ATOM 4804 N N . ASP A 1 666 ? -4.789 -24.569 38.359 1.00 39.28 ? 666 ASP A N 1 ATOM 4805 C CA . ASP A 1 666 ? -5.395 -23.536 39.180 1.00 38.93 ? 666 ASP A CA 1 ATOM 4806 C C . ASP A 1 666 ? -4.355 -22.429 39.349 1.00 35.56 ? 666 ASP A C 1 ATOM 4807 O O . ASP A 1 666 ? -3.221 -22.696 39.746 1.00 32.53 ? 666 ASP A O 1 ATOM 4808 C CB . ASP A 1 666 ? -5.775 -24.159 40.534 1.00 43.31 ? 666 ASP A CB 1 ATOM 4809 C CG . ASP A 1 666 ? -6.715 -23.294 41.368 1.00 46.80 ? 666 ASP A CG 1 ATOM 4810 O OD1 . ASP A 1 666 ? -7.194 -22.242 40.890 1.00 47.01 ? 666 ASP A OD1 1 ATOM 4811 O OD2 . ASP A 1 666 ? -6.978 -23.700 42.530 1.00 51.72 -1 666 ASP A OD2 1 ATOM 4812 N N . ILE A 1 667 ? -4.720 -21.210 38.959 1.00 33.68 ? 667 ILE A N 1 ATOM 4813 C CA . ILE A 1 667 ? -3.923 -20.032 39.253 1.00 31.84 ? 667 ILE A CA 1 ATOM 4814 C C . ILE A 1 667 ? -4.632 -19.381 40.429 1.00 32.00 ? 667 ILE A C 1 ATOM 4815 O O . ILE A 1 667 ? -5.700 -18.782 40.272 1.00 32.52 ? 667 ILE A O 1 ATOM 4816 C CB . ILE A 1 667 ? -3.867 -19.056 38.067 1.00 32.37 ? 667 ILE A CB 1 ATOM 4817 C CG1 . ILE A 1 667 ? -3.262 -19.735 36.828 1.00 32.46 ? 667 ILE A CG1 1 ATOM 4818 C CG2 . ILE A 1 667 ? -3.094 -17.793 38.435 1.00 31.58 ? 667 ILE A CG2 1 ATOM 4819 C CD1 . ILE A 1 667 ? -1.853 -20.250 37.013 1.00 33.48 ? 667 ILE A CD1 1 ATOM 4820 N N . SER A 1 668 ? -4.049 -19.532 41.609 1.00 29.93 ? 668 SER A N 1 ATOM 4821 C CA . SER A 1 668 ? -4.635 -19.023 42.828 1.00 30.81 ? 668 SER A CA 1 ATOM 4822 C C . SER A 1 668 ? -3.892 -17.748 43.226 1.00 30.24 ? 668 SER A C 1 ATOM 4823 O O . SER A 1 668 ? -2.664 -17.751 43.389 1.00 31.89 ? 668 SER A O 1 ATOM 4824 C CB . SER A 1 668 ? -4.546 -20.083 43.927 1.00 31.01 ? 668 SER A CB 1 ATOM 4825 O OG . SER A 1 668 ? -4.859 -19.527 45.183 1.00 33.83 ? 668 SER A OG 1 ATOM 4826 N N . LEU A 1 669 ? -4.641 -16.659 43.355 1.00 27.85 ? 669 LEU A N 1 ATOM 4827 C CA . LEU A 1 669 ? -4.085 -15.361 43.688 1.00 26.32 ? 669 LEU A CA 1 ATOM 4828 C C . LEU A 1 669 ? -4.783 -14.839 44.930 1.00 26.61 ? 669 LEU A C 1 ATOM 4829 O O . LEU A 1 669 ? -6.009 -14.847 45.000 1.00 25.56 ? 669 LEU A O 1 ATOM 4830 C CB . LEU A 1 669 ? -4.285 -14.385 42.531 1.00 25.14 ? 669 LEU A CB 1 ATOM 4831 C CG . LEU A 1 669 ? -3.543 -14.679 41.226 1.00 24.29 ? 669 LEU A CG 1 ATOM 4832 C CD1 . LEU A 1 669 ? -3.865 -13.608 40.203 1.00 24.13 ? 669 LEU A CD1 1 ATOM 4833 C CD2 . LEU A 1 669 ? -2.041 -14.740 41.452 1.00 24.43 ? 669 LEU A CD2 1 ATOM 4834 N N . PRO A 1 670 ? -4.008 -14.394 45.929 1.00 28.02 ? 670 PRO A N 1 ATOM 4835 C CA . PRO A 1 670 ? -4.666 -13.901 47.143 1.00 28.09 ? 670 PRO A CA 1 ATOM 4836 C C . PRO A 1 670 ? -5.410 -12.594 46.914 1.00 27.14 ? 670 PRO A C 1 ATOM 4837 O O . PRO A 1 670 ? -5.063 -11.824 46.024 1.00 26.53 ? 670 PRO A O 1 ATOM 4838 C CB . PRO A 1 670 ? -3.511 -13.701 48.128 1.00 28.26 ? 670 PRO A CB 1 ATOM 4839 C CG . PRO A 1 670 ? -2.290 -13.611 47.287 1.00 28.63 ? 670 PRO A CG 1 ATOM 4840 C CD . PRO A 1 670 ? -2.543 -14.443 46.067 1.00 28.14 ? 670 PRO A CD 1 ATOM 4841 N N . SER A 1 671 ? -6.448 -12.384 47.710 1.00 26.61 ? 671 SER A N 1 ATOM 4842 C CA . SER A 1 671 ? -7.205 -11.149 47.702 1.00 26.59 ? 671 SER A CA 1 ATOM 4843 C C . SER A 1 671 ? -6.390 -10.083 48.445 1.00 24.89 ? 671 SER A C 1 ATOM 4844 O O . SER A 1 671 ? -6.144 -10.211 49.639 1.00 24.36 ? 671 SER A O 1 ATOM 4845 C CB . SER A 1 671 ? -8.561 -11.375 48.382 1.00 27.56 ? 671 SER A CB 1 ATOM 4846 O OG . SER A 1 671 ? -9.173 -10.147 48.724 1.00 29.19 ? 671 SER A OG 1 ATOM 4847 N N . LEU A 1 672 ? -5.961 -9.039 47.738 1.00 23.48 ? 672 LEU A N 1 ATOM 4848 C CA . LEU A 1 672 ? -5.123 -7.995 48.353 1.00 21.26 ? 672 LEU A CA 1 ATOM 4849 C C . LEU A 1 672 ? -5.826 -7.260 49.486 1.00 21.30 ? 672 LEU A C 1 ATOM 4850 O O . LEU A 1 672 ? -5.197 -6.905 50.476 1.00 21.46 ? 672 LEU A O 1 ATOM 4851 C CB . LEU A 1 672 ? -4.624 -7.005 47.300 1.00 20.31 ? 672 LEU A CB 1 ATOM 4852 C CG . LEU A 1 672 ? -3.677 -7.612 46.256 1.00 19.54 ? 672 LEU A CG 1 ATOM 4853 C CD1 . LEU A 1 672 ? -3.044 -6.509 45.439 1.00 19.06 ? 672 LEU A CD1 1 ATOM 4854 C CD2 . LEU A 1 672 ? -2.598 -8.478 46.889 1.00 19.43 ? 672 LEU A CD2 1 ATOM 4855 N N . LYS A 1 673 ? -7.130 -7.049 49.364 1.00 22.09 ? 673 LYS A N 1 ATOM 4856 C CA . LYS A 1 673 ? -7.868 -6.362 50.410 1.00 23.31 ? 673 LYS A CA 1 ATOM 4857 C C . LYS A 1 673 ? -7.980 -7.145 51.735 1.00 23.34 ? 673 LYS A C 1 ATOM 4858 O O . LYS A 1 673 ? -8.245 -6.547 52.756 1.00 23.61 ? 673 LYS A O 1 ATOM 4859 C CB . LYS A 1 673 ? -9.249 -5.941 49.915 1.00 24.55 ? 673 LYS A CB 1 ATOM 4860 C CG . LYS A 1 673 ? -10.204 -7.081 49.568 1.00 26.41 ? 673 LYS A CG 1 ATOM 4861 C CD . LYS A 1 673 ? -11.646 -6.574 49.530 1.00 28.06 ? 673 LYS A CD 1 ATOM 4862 C CE . LYS A 1 673 ? -12.596 -7.615 48.969 1.00 29.26 ? 673 LYS A CE 1 ATOM 4863 N NZ . LYS A 1 673 ? -12.778 -8.751 49.916 1.00 29.97 ? 673 LYS A NZ 1 ATOM 4864 N N . ASP A 1 674 ? -7.765 -8.462 51.719 1.00 23.77 ? 674 ASP A N 1 ATOM 4865 C CA . ASP A 1 674 ? -7.876 -9.286 52.929 1.00 24.10 ? 674 ASP A CA 1 ATOM 4866 C C . ASP A 1 674 ? -6.555 -9.525 53.632 1.00 23.62 ? 674 ASP A C 1 ATOM 4867 O O . ASP A 1 674 ? -6.525 -10.230 54.641 1.00 24.14 ? 674 ASP A O 1 ATOM 4868 C CB . ASP A 1 674 ? -8.469 -10.654 52.599 1.00 25.40 ? 674 ASP A CB 1 ATOM 4869 C CG . ASP A 1 674 ? -9.893 -10.573 52.110 1.00 27.00 ? 674 ASP A CG 1 ATOM 4870 O OD1 . ASP A 1 674 ? -10.615 -9.615 52.475 1.00 27.96 ? 674 ASP A OD1 1 ATOM 4871 O OD2 . ASP A 1 674 ? -10.291 -11.486 51.356 1.00 30.05 -1 674 ASP A OD2 1 ATOM 4872 N N . LEU A 1 675 ? -5.465 -8.964 53.111 1.00 22.38 ? 675 LEU A N 1 ATOM 4873 C CA . LEU A 1 675 ? -4.148 -9.147 53.726 1.00 21.65 ? 675 LEU A CA 1 ATOM 4874 C C . LEU A 1 675 ? -4.082 -8.403 55.067 1.00 21.55 ? 675 LEU A C 1 ATOM 4875 O O . LEU A 1 675 ? -4.872 -7.501 55.309 1.00 20.45 ? 675 LEU A O 1 ATOM 4876 C CB . LEU A 1 675 ? -3.031 -8.680 52.783 1.00 20.69 ? 675 LEU A CB 1 ATOM 4877 C CG . LEU A 1 675 ? -2.955 -9.453 51.459 1.00 20.69 ? 675 LEU A CG 1 ATOM 4878 C CD1 . LEU A 1 675 ? -1.899 -8.848 50.550 1.00 21.18 ? 675 LEU A CD1 1 ATOM 4879 C CD2 . LEU A 1 675 ? -2.674 -10.930 51.702 1.00 20.36 ? 675 LEU A CD2 1 ATOM 4880 N N . ASP A 1 676 ? -3.153 -8.817 55.925 1.00 21.72 ? 676 ASP A N 1 ATOM 4881 C CA . ASP A 1 676 ? -2.924 -8.183 57.220 1.00 22.76 ? 676 ASP A CA 1 ATOM 4882 C C . ASP A 1 676 ? -2.186 -6.831 57.047 1.00 21.91 ? 676 ASP A C 1 ATOM 4883 O O . ASP A 1 676 ? -1.004 -6.709 57.374 1.00 23.16 ? 676 ASP A O 1 ATOM 4884 C CB . ASP A 1 676 ? -2.128 -9.153 58.127 1.00 23.49 ? 676 ASP A CB 1 ATOM 4885 C CG . ASP A 1 676 ? -2.011 -8.667 59.593 1.00 25.37 ? 676 ASP A CG 1 ATOM 4886 O OD1 . ASP A 1 676 ? -2.868 -7.868 60.045 1.00 26.00 ? 676 ASP A OD1 1 ATOM 4887 O OD2 . ASP A 1 676 ? -1.072 -9.117 60.302 1.00 27.11 -1 676 ASP A OD2 1 ATOM 4888 N N . TRP A 1 677 ? -2.890 -5.819 56.558 1.00 20.19 ? 677 TRP A N 1 ATOM 4889 C CA . TRP A 1 677 ? -2.275 -4.505 56.308 1.00 20.14 ? 677 TRP A CA 1 ATOM 4890 C C . TRP A 1 677 ? -1.875 -3.779 57.585 1.00 19.22 ? 677 TRP A C 1 ATOM 4891 O O . TRP A 1 677 ? -2.675 -3.662 58.509 1.00 18.19 ? 677 TRP A O 1 ATOM 4892 C CB . TRP A 1 677 ? -3.225 -3.594 55.516 1.00 20.03 ? 677 TRP A CB 1 ATOM 4893 C CG . TRP A 1 677 ? -3.397 -4.013 54.103 1.00 19.58 ? 677 TRP A CG 1 ATOM 4894 C CD1 . TRP A 1 677 ? -4.429 -4.725 53.575 1.00 19.36 ? 677 TRP A CD1 1 ATOM 4895 C CD2 . TRP A 1 677 ? -2.500 -3.744 53.027 1.00 19.16 ? 677 TRP A CD2 1 ATOM 4896 N NE1 . TRP A 1 677 ? -4.235 -4.912 52.219 1.00 19.31 ? 677 TRP A NE1 1 ATOM 4897 C CE2 . TRP A 1 677 ? -3.059 -4.314 51.860 1.00 19.28 ? 677 TRP A CE2 1 ATOM 4898 C CE3 . TRP A 1 677 ? -1.284 -3.067 52.931 1.00 18.51 ? 677 TRP A CE3 1 ATOM 4899 C CZ2 . TRP A 1 677 ? -2.430 -4.239 50.624 1.00 19.20 ? 677 TRP A CZ2 1 ATOM 4900 C CZ3 . TRP A 1 677 ? -0.665 -2.985 51.707 1.00 18.32 ? 677 TRP A CZ3 1 ATOM 4901 C CH2 . TRP A 1 677 ? -1.231 -3.570 50.567 1.00 18.69 ? 677 TRP A CH2 1 ATOM 4902 N N . LYS A 1 678 ? -0.641 -3.272 57.604 1.00 18.83 ? 678 LYS A N 1 ATOM 4903 C CA . LYS A 1 678 ? -0.120 -2.502 58.721 1.00 19.15 ? 678 LYS A CA 1 ATOM 4904 C C . LYS A 1 678 ? 0.212 -1.049 58.283 1.00 18.77 ? 678 LYS A C 1 ATOM 4905 O O . LYS A 1 678 ? 0.846 -0.832 57.245 1.00 18.09 ? 678 LYS A O 1 ATOM 4906 C CB . LYS A 1 678 ? 1.116 -3.210 59.298 1.00 19.92 ? 678 LYS A CB 1 ATOM 4907 C CG . LYS A 1 678 ? 0.831 -4.561 59.967 1.00 20.23 ? 678 LYS A CG 1 ATOM 4908 C CD . LYS A 1 678 ? 0.061 -4.382 61.267 1.00 20.71 ? 678 LYS A CD 1 ATOM 4909 C CE . LYS A 1 678 ? -0.410 -5.708 61.850 1.00 21.55 ? 678 LYS A CE 1 ATOM 4910 N NZ . LYS A 1 678 ? 0.640 -6.389 62.654 1.00 22.06 ? 678 LYS A NZ 1 ATOM 4911 N N . TYR A 1 679 ? -0.216 -0.072 59.089 1.00 17.62 ? 679 TYR A N 1 ATOM 4912 C CA . TYR A 1 679 ? -0.125 1.350 58.747 1.00 17.10 ? 679 TYR A CA 1 ATOM 4913 C C . TYR A 1 679 ? 0.846 2.102 59.650 1.00 16.76 ? 679 TYR A C 1 ATOM 4914 O O . TYR A 1 679 ? 0.921 1.851 60.850 1.00 16.15 ? 679 TYR A O 1 ATOM 4915 C CB . TYR A 1 679 ? -1.520 1.995 58.836 1.00 17.35 ? 679 TYR A CB 1 ATOM 4916 C CG . TYR A 1 679 ? -1.537 3.497 58.975 1.00 17.22 ? 679 TYR A CG 1 ATOM 4917 C CD1 . TYR A 1 679 ? -1.545 4.319 57.858 1.00 17.73 ? 679 TYR A CD1 1 ATOM 4918 C CD2 . TYR A 1 679 ? -1.564 4.095 60.222 1.00 18.14 ? 679 TYR A CD2 1 ATOM 4919 C CE1 . TYR A 1 679 ? -1.568 5.699 57.977 1.00 17.59 ? 679 TYR A CE1 1 ATOM 4920 C CE2 . TYR A 1 679 ? -1.575 5.482 60.361 1.00 17.85 ? 679 TYR A CE2 1 ATOM 4921 C CZ . TYR A 1 679 ? -1.576 6.275 59.233 1.00 17.49 ? 679 TYR A CZ 1 ATOM 4922 O OH . TYR A 1 679 ? -1.592 7.639 59.360 1.00 17.16 ? 679 TYR A OH 1 ATOM 4923 N N . VAL A 1 680 ? 1.580 3.034 59.059 1.00 16.69 ? 680 VAL A N 1 ATOM 4924 C CA . VAL A 1 680 ? 2.311 4.028 59.819 1.00 16.68 ? 680 VAL A CA 1 ATOM 4925 C C . VAL A 1 680 ? 2.185 5.369 59.088 1.00 17.08 ? 680 VAL A C 1 ATOM 4926 O O . VAL A 1 680 ? 2.150 5.410 57.871 1.00 16.49 ? 680 VAL A O 1 ATOM 4927 C CB . VAL A 1 680 ? 3.770 3.594 60.073 1.00 16.82 ? 680 VAL A CB 1 ATOM 4928 C CG1 . VAL A 1 680 ? 4.525 3.376 58.784 1.00 17.13 ? 680 VAL A CG1 1 ATOM 4929 C CG2 . VAL A 1 680 ? 4.500 4.601 60.956 1.00 17.25 ? 680 VAL A CG2 1 ATOM 4930 N N . ASP A 1 681 ? 2.054 6.451 59.851 1.00 17.67 ? 681 ASP A N 1 ATOM 4931 C CA . ASP A 1 681 ? 1.969 7.807 59.315 1.00 18.25 ? 681 ASP A CA 1 ATOM 4932 C C . ASP A 1 681 ? 3.322 8.194 58.716 1.00 18.22 ? 681 ASP A C 1 ATOM 4933 O O . ASP A 1 681 ? 4.312 8.274 59.424 1.00 17.93 ? 681 ASP A O 1 ATOM 4934 C CB . ASP A 1 681 ? 1.591 8.768 60.462 1.00 19.21 ? 681 ASP A CB 1 ATOM 4935 C CG . ASP A 1 681 ? 1.303 10.199 59.997 1.00 19.94 ? 681 ASP A CG 1 ATOM 4936 O OD1 . ASP A 1 681 ? 1.650 10.586 58.859 1.00 20.14 ? 681 ASP A OD1 1 ATOM 4937 O OD2 . ASP A 1 681 ? 0.727 10.959 60.812 1.00 21.08 -1 681 ASP A OD2 1 ATOM 4938 N N . THR A 1 682 ? 3.370 8.431 57.410 1.00 18.09 ? 682 THR A N 1 ATOM 4939 C CA . THR A 1 682 ? 4.633 8.778 56.766 1.00 17.89 ? 682 THR A CA 1 ATOM 4940 C C . THR A 1 682 ? 4.732 10.267 56.434 1.00 18.26 ? 682 THR A C 1 ATOM 4941 O O . THR A 1 682 ? 5.503 10.664 55.559 1.00 18.50 ? 682 THR A O 1 ATOM 4942 C CB . THR A 1 682 ? 4.930 7.902 55.528 1.00 17.57 ? 682 THR A CB 1 ATOM 4943 O OG1 . THR A 1 682 ? 6.270 8.153 55.089 1.00 17.14 ? 682 THR A OG1 1 ATOM 4944 C CG2 . THR A 1 682 ? 3.940 8.156 54.384 1.00 17.56 ? 682 THR A CG2 1 ATOM 4945 N N . LEU A 1 683 ? 3.958 11.083 57.152 1.00 18.90 ? 683 LEU A N 1 ATOM 4946 C CA . LEU A 1 683 ? 4.209 12.519 57.239 1.00 18.55 ? 683 LEU A CA 1 ATOM 4947 C C . LEU A 1 683 ? 4.259 12.965 58.713 1.00 19.07 ? 683 LEU A C 1 ATOM 4948 O O . LEU A 1 683 ? 3.506 13.854 59.135 1.00 19.46 ? 683 LEU A O 1 ATOM 4949 C CB . LEU A 1 683 ? 3.156 13.295 56.441 1.00 18.27 ? 683 LEU A CB 1 ATOM 4950 C CG . LEU A 1 683 ? 3.519 14.751 56.120 1.00 18.50 ? 683 LEU A CG 1 ATOM 4951 C CD1 . LEU A 1 683 ? 4.761 14.830 55.251 1.00 18.24 ? 683 LEU A CD1 1 ATOM 4952 C CD2 . LEU A 1 683 ? 2.345 15.483 55.475 1.00 18.53 ? 683 LEU A CD2 1 ATOM 4953 N N . PRO A 1 684 ? 5.172 12.373 59.508 1.00 19.18 ? 684 PRO A N 1 ATOM 4954 C CA . PRO A 1 684 ? 5.291 12.804 60.903 1.00 19.43 ? 684 PRO A CA 1 ATOM 4955 C C . PRO A 1 684 ? 5.844 14.227 61.049 1.00 19.47 ? 684 PRO A C 1 ATOM 4956 O O . PRO A 1 684 ? 5.889 14.751 62.157 1.00 18.67 ? 684 PRO A O 1 ATOM 4957 C CB . PRO A 1 684 ? 6.275 11.786 61.494 1.00 19.27 ? 684 PRO A CB 1 ATOM 4958 C CG . PRO A 1 684 ? 7.152 11.438 60.333 1.00 19.53 ? 684 PRO A CG 1 ATOM 4959 C CD . PRO A 1 684 ? 6.218 11.391 59.156 1.00 19.52 ? 684 PRO A CD 1 ATOM 4960 N N . GLU A 1 685 ? 6.263 14.829 59.936 1.00 19.36 ? 685 GLU A N 1 ATOM 4961 C CA . GLU A 1 685 ? 6.752 16.203 59.906 1.00 19.43 ? 685 GLU A CA 1 ATOM 4962 C C . GLU A 1 685 ? 5.708 17.232 60.358 1.00 21.13 ? 685 GLU A C 1 ATOM 4963 O O . GLU A 1 685 ? 6.073 18.291 60.868 1.00 20.72 ? 685 GLU A O 1 ATOM 4964 C CB . GLU A 1 685 ? 7.246 16.572 58.498 1.00 19.10 ? 685 GLU A CB 1 ATOM 4965 C CG . GLU A 1 685 ? 8.522 15.866 58.030 1.00 18.63 ? 685 GLU A CG 1 ATOM 4966 C CD . GLU A 1 685 ? 8.308 14.443 57.512 1.00 18.12 ? 685 GLU A CD 1 ATOM 4967 O OE1 . GLU A 1 685 ? 7.173 13.931 57.537 1.00 18.57 ? 685 GLU A OE1 1 ATOM 4968 O OE2 . GLU A 1 685 ? 9.280 13.817 57.077 1.00 17.03 -1 685 GLU A OE2 1 ATOM 4969 N N . ILE A 1 686 ? 4.421 16.940 60.183 1.00 22.46 ? 686 ILE A N 1 ATOM 4970 C CA . ILE A 1 686 ? 3.376 17.923 60.520 1.00 24.43 ? 686 ILE A CA 1 ATOM 4971 C C . ILE A 1 686 ? 2.872 17.863 61.968 1.00 26.63 ? 686 ILE A C 1 ATOM 4972 O O . ILE A 1 686 ? 1.926 18.574 62.325 1.00 26.55 ? 686 ILE A O 1 ATOM 4973 C CB . ILE A 1 686 ? 2.178 17.877 59.550 1.00 24.35 ? 686 ILE A CB 1 ATOM 4974 C CG1 . ILE A 1 686 ? 1.479 16.512 59.589 1.00 24.70 ? 686 ILE A CG1 1 ATOM 4975 C CG2 . ILE A 1 686 ? 2.643 18.235 58.143 1.00 24.44 ? 686 ILE A CG2 1 ATOM 4976 C CD1 . ILE A 1 686 ? 0.055 16.543 59.067 1.00 24.88 ? 686 ILE A CD1 1 ATOM 4977 N N . GLN A 1 687 ? 3.507 17.040 62.798 1.00 28.67 ? 687 GLN A N 1 ATOM 4978 C CA . GLN A 1 687 ? 3.259 17.065 64.234 1.00 31.43 ? 687 GLN A CA 1 ATOM 4979 C C . GLN A 1 687 ? 4.258 17.997 64.893 1.00 33.55 ? 687 GLN A C 1 ATOM 4980 O O . GLN A 1 687 ? 5.417 18.090 64.461 1.00 33.61 ? 687 GLN A O 1 ATOM 4981 C CB . GLN A 1 687 ? 3.407 15.677 64.830 1.00 33.63 ? 687 GLN A CB 1 ATOM 4982 C CG . GLN A 1 687 ? 2.440 14.654 64.265 1.00 35.93 ? 687 GLN A CG 1 ATOM 4983 C CD . GLN A 1 687 ? 2.818 13.244 64.658 1.00 38.84 ? 687 GLN A CD 1 ATOM 4984 O OE1 . GLN A 1 687 ? 3.485 13.029 65.668 1.00 41.40 ? 687 GLN A OE1 1 ATOM 4985 N NE2 . GLN A 1 687 ? 2.396 12.273 63.862 1.00 41.19 ? 687 GLN A NE2 1 ATOM 4986 N N . SER A 1 688 ? 3.813 18.662 65.959 1.00 34.82 ? 688 SER A N 1 ATOM 4987 C CA . SER A 1 688 ? 4.641 19.618 66.694 1.00 34.33 ? 688 SER A CA 1 ATOM 4988 C C . SER A 1 688 ? 5.833 18.991 67.433 1.00 32.81 ? 688 SER A C 1 ATOM 4989 O O . SER A 1 688 ? 6.749 19.697 67.836 1.00 32.28 ? 688 SER A O 1 ATOM 4990 C CB . SER A 1 688 ? 3.776 20.387 67.696 1.00 36.43 ? 688 SER A CB 1 ATOM 4991 O OG . SER A 1 688 ? 3.144 19.496 68.613 1.00 38.11 ? 688 SER A OG 1 ATOM 4992 N N . SER A 1 689 ? 5.824 17.681 67.633 1.00 32.13 ? 689 SER A N 1 ATOM 4993 C CA . SER A 1 689 ? 6.968 17.020 68.258 1.00 32.64 ? 689 SER A CA 1 ATOM 4994 C C . SER A 1 689 ? 8.154 16.812 67.298 1.00 31.88 ? 689 SER A C 1 ATOM 4995 O O . SER A 1 689 ? 9.262 16.541 67.761 1.00 30.75 ? 689 SER A O 1 ATOM 4996 C CB . SER A 1 689 ? 6.556 15.676 68.867 1.00 32.85 ? 689 SER A CB 1 ATOM 4997 O OG . SER A 1 689 ? 6.180 14.750 67.863 1.00 32.84 ? 689 SER A OG 1 ATOM 4998 N N . TYR A 1 690 ? 7.937 16.950 65.985 1.00 30.41 ? 690 TYR A N 1 ATOM 4999 C CA . TYR A 1 690 ? 8.967 16.596 65.008 1.00 28.89 ? 690 TYR A CA 1 ATOM 5000 C C . TYR A 1 690 ? 10.214 17.468 65.113 1.00 28.83 ? 690 TYR A C 1 ATOM 5001 O O . TYR A 1 690 ? 10.128 18.680 65.241 1.00 30.03 ? 690 TYR A O 1 ATOM 5002 C CB . TYR A 1 690 ? 8.447 16.635 63.563 1.00 28.00 ? 690 TYR A CB 1 ATOM 5003 C CG . TYR A 1 690 ? 9.427 15.979 62.609 1.00 26.69 ? 690 TYR A CG 1 ATOM 5004 C CD1 . TYR A 1 690 ? 9.506 14.593 62.500 1.00 26.39 ? 690 TYR A CD1 1 ATOM 5005 C CD2 . TYR A 1 690 ? 10.309 16.739 61.864 1.00 25.92 ? 690 TYR A CD2 1 ATOM 5006 C CE1 . TYR A 1 690 ? 10.425 13.986 61.654 1.00 25.81 ? 690 TYR A CE1 1 ATOM 5007 C CE2 . TYR A 1 690 ? 11.222 16.147 61.013 1.00 26.09 ? 690 TYR A CE2 1 ATOM 5008 C CZ . TYR A 1 690 ? 11.280 14.772 60.909 1.00 25.79 ? 690 TYR A CZ 1 ATOM 5009 O OH . TYR A 1 690 ? 12.199 14.208 60.057 1.00 23.62 ? 690 TYR A OH 1 ATOM 5010 N N . ASP A 1 691 ? 11.369 16.813 65.027 1.00 29.19 ? 691 ASP A N 1 ATOM 5011 C CA . ASP A 1 691 ? 12.671 17.428 65.205 1.00 27.95 ? 691 ASP A CA 1 ATOM 5012 C C . ASP A 1 691 ? 13.435 17.252 63.899 1.00 26.17 ? 691 ASP A C 1 ATOM 5013 O O . ASP A 1 691 ? 13.956 16.166 63.622 1.00 25.02 ? 691 ASP A O 1 ATOM 5014 C CB . ASP A 1 691 ? 13.380 16.718 66.361 1.00 30.11 ? 691 ASP A CB 1 ATOM 5015 C CG . ASP A 1 691 ? 14.757 17.292 66.679 1.00 32.51 ? 691 ASP A CG 1 ATOM 5016 O OD1 . ASP A 1 691 ? 15.236 18.217 65.981 1.00 31.51 ? 691 ASP A OD1 1 ATOM 5017 O OD2 . ASP A 1 691 ? 15.357 16.796 67.663 1.00 36.16 -1 691 ASP A OD2 1 ATOM 5018 N N . ASP A 1 692 ? 13.493 18.306 63.083 1.00 23.93 ? 692 ASP A N 1 ATOM 5019 C CA . ASP A 1 692 ? 14.191 18.222 61.795 1.00 23.57 ? 692 ASP A CA 1 ATOM 5020 C C . ASP A 1 692 ? 15.670 18.631 61.847 1.00 23.66 ? 692 ASP A C 1 ATOM 5021 O O . ASP A 1 692 ? 16.262 18.947 60.805 1.00 23.48 ? 692 ASP A O 1 ATOM 5022 C CB . ASP A 1 692 ? 13.460 19.048 60.733 1.00 23.11 ? 692 ASP A CB 1 ATOM 5023 C CG . ASP A 1 692 ? 13.470 20.558 61.020 1.00 22.90 ? 692 ASP A CG 1 ATOM 5024 O OD1 . ASP A 1 692 ? 14.293 21.062 61.825 1.00 20.99 ? 692 ASP A OD1 1 ATOM 5025 O OD2 . ASP A 1 692 ? 12.621 21.241 60.408 1.00 23.13 -1 692 ASP A OD2 1 ATOM 5026 N N . SER A 1 693 ? 16.272 18.613 63.036 1.00 23.80 ? 693 SER A N 1 ATOM 5027 C CA . SER A 1 693 ? 17.614 19.178 63.221 1.00 24.19 ? 693 SER A CA 1 ATOM 5028 C C . SER A 1 693 ? 18.685 18.458 62.407 1.00 23.99 ? 693 SER A C 1 ATOM 5029 O O . SER A 1 693 ? 19.696 19.065 62.075 1.00 23.72 ? 693 SER A O 1 ATOM 5030 C CB . SER A 1 693 ? 18.012 19.218 64.703 1.00 24.22 ? 693 SER A CB 1 ATOM 5031 O OG . SER A 1 693 ? 18.249 17.912 65.197 1.00 25.00 ? 693 SER A OG 1 ATOM 5032 N N . LEU A 1 694 ? 18.462 17.189 62.069 1.00 23.82 ? 694 LEU A N 1 ATOM 5033 C CA . LEU A 1 694 ? 19.373 16.475 61.166 1.00 24.41 ? 694 LEU A CA 1 ATOM 5034 C C . LEU A 1 694 ? 19.150 16.736 59.653 1.00 23.33 ? 694 LEU A C 1 ATOM 5035 O O . LEU A 1 694 ? 19.918 16.241 58.832 1.00 23.32 ? 694 LEU A O 1 ATOM 5036 C CB . LEU A 1 694 ? 19.331 14.968 61.442 1.00 25.20 ? 694 LEU A CB 1 ATOM 5037 C CG . LEU A 1 694 ? 19.656 14.536 62.869 1.00 26.59 ? 694 LEU A CG 1 ATOM 5038 C CD1 . LEU A 1 694 ? 19.763 13.018 62.935 1.00 26.63 ? 694 LEU A CD1 1 ATOM 5039 C CD2 . LEU A 1 694 ? 20.936 15.183 63.392 1.00 27.59 ? 694 LEU A CD2 1 ATOM 5040 N N . TRP A 1 695 ? 18.131 17.512 59.276 1.00 21.91 ? 695 TRP A N 1 ATOM 5041 C CA . TRP A 1 695 ? 17.867 17.767 57.853 1.00 21.12 ? 695 TRP A CA 1 ATOM 5042 C C . TRP A 1 695 ? 18.933 18.673 57.228 1.00 21.29 ? 695 TRP A C 1 ATOM 5043 O O . TRP A 1 695 ? 19.460 19.555 57.900 1.00 20.64 ? 695 TRP A O 1 ATOM 5044 C CB . TRP A 1 695 ? 16.483 18.409 57.640 1.00 20.36 ? 695 TRP A CB 1 ATOM 5045 C CG . TRP A 1 695 ? 15.317 17.465 57.840 1.00 19.41 ? 695 TRP A CG 1 ATOM 5046 C CD1 . TRP A 1 695 ? 15.197 16.526 58.808 1.00 19.07 ? 695 TRP A CD1 1 ATOM 5047 C CD2 . TRP A 1 695 ? 14.111 17.392 57.063 1.00 18.69 ? 695 TRP A CD2 1 ATOM 5048 N NE1 . TRP A 1 695 ? 14.008 15.876 58.691 1.00 18.91 ? 695 TRP A NE1 1 ATOM 5049 C CE2 . TRP A 1 695 ? 13.314 16.382 57.634 1.00 18.43 ? 695 TRP A CE2 1 ATOM 5050 C CE3 . TRP A 1 695 ? 13.624 18.088 55.949 1.00 18.50 ? 695 TRP A CE3 1 ATOM 5051 C CZ2 . TRP A 1 695 ? 12.048 16.036 57.133 1.00 18.36 ? 695 TRP A CZ2 1 ATOM 5052 C CZ3 . TRP A 1 695 ? 12.364 17.754 55.449 1.00 18.46 ? 695 TRP A CZ3 1 ATOM 5053 C CH2 . TRP A 1 695 ? 11.592 16.728 56.042 1.00 18.36 ? 695 TRP A CH2 1 ATOM 5054 N N . PRO A 1 696 ? 19.260 18.450 55.940 1.00 21.33 ? 696 PRO A N 1 ATOM 5055 C CA . PRO A 1 696 ? 20.086 19.415 55.224 1.00 21.91 ? 696 PRO A CA 1 ATOM 5056 C C . PRO A 1 696 ? 19.431 20.803 55.220 1.00 22.39 ? 696 PRO A C 1 ATOM 5057 O O . PRO A 1 696 ? 18.219 20.899 55.086 1.00 22.36 ? 696 PRO A O 1 ATOM 5058 C CB . PRO A 1 696 ? 20.147 18.842 53.801 1.00 21.86 ? 696 PRO A CB 1 ATOM 5059 C CG . PRO A 1 696 ? 19.886 17.386 53.956 1.00 21.48 ? 696 PRO A CG 1 ATOM 5060 C CD . PRO A 1 696 ? 18.986 17.245 55.138 1.00 21.44 ? 696 PRO A CD 1 ATOM 5061 N N . ALA A 1 697 ? 20.221 21.857 55.399 1.00 22.76 ? 697 ALA A N 1 ATOM 5062 C CA . ALA A 1 697 ? 19.698 23.213 55.350 1.00 23.34 ? 697 ALA A CA 1 ATOM 5063 C C . ALA A 1 697 ? 19.755 23.687 53.916 1.00 24.37 ? 697 ALA A C 1 ATOM 5064 O O . ALA A 1 697 ? 20.732 23.443 53.210 1.00 24.40 ? 697 ALA A O 1 ATOM 5065 C CB . ALA A 1 697 ? 20.501 24.144 56.245 1.00 23.31 ? 697 ALA A CB 1 ATOM 5066 N N . ALA A 1 698 ? 18.703 24.366 53.483 1.00 25.95 ? 698 ALA A N 1 ATOM 5067 C CA . ALA A 1 698 ? 18.686 24.966 52.166 1.00 26.88 ? 698 ALA A CA 1 ATOM 5068 C C . ALA A 1 698 ? 19.246 26.380 52.264 1.00 28.61 ? 698 ALA A C 1 ATOM 5069 O O . ALA A 1 698 ? 18.512 27.356 52.103 1.00 30.12 ? 698 ALA A O 1 ATOM 5070 C CB . ALA A 1 698 ? 17.277 24.974 51.619 1.00 27.04 ? 698 ALA A CB 1 ATOM 5071 N N . ASP A 1 699 ? 20.551 26.483 52.517 1.00 29.86 ? 699 ASP A N 1 ATOM 5072 C CA . ASP A 1 699 ? 21.184 27.775 52.823 1.00 31.12 ? 699 ASP A CA 1 ATOM 5073 C C . ASP A 1 699 ? 22.197 28.282 51.784 1.00 30.02 ? 699 ASP A C 1 ATOM 5074 O O . ASP A 1 699 ? 22.997 29.161 52.092 1.00 30.06 ? 699 ASP A O 1 ATOM 5075 C CB . ASP A 1 699 ? 21.828 27.742 54.222 1.00 32.15 ? 699 ASP A CB 1 ATOM 5076 C CG . ASP A 1 699 ? 22.887 26.657 54.374 1.00 33.56 ? 699 ASP A CG 1 ATOM 5077 O OD1 . ASP A 1 699 ? 23.309 26.054 53.358 1.00 33.67 ? 699 ASP A OD1 1 ATOM 5078 O OD2 . ASP A 1 699 ? 23.291 26.403 55.536 1.00 36.14 -1 699 ASP A OD2 1 ATOM 5079 N N . LEU A 1 700 ? 22.146 27.754 50.564 1.00 30.01 ? 700 LEU A N 1 ATOM 5080 C CA . LEU A 1 700 ? 23.041 28.194 49.496 1.00 30.51 ? 700 LEU A CA 1 ATOM 5081 C C . LEU A 1 700 ? 22.582 29.519 48.925 1.00 29.85 ? 700 LEU A C 1 ATOM 5082 O O . LEU A 1 700 ? 21.464 29.634 48.451 1.00 28.86 ? 700 LEU A O 1 ATOM 5083 C CB . LEU A 1 700 ? 23.108 27.162 48.372 1.00 32.32 ? 700 LEU A CB 1 ATOM 5084 C CG . LEU A 1 700 ? 23.898 25.894 48.711 1.00 34.48 ? 700 LEU A CG 1 ATOM 5085 C CD1 . LEU A 1 700 ? 23.730 24.857 47.602 1.00 34.65 ? 700 LEU A CD1 1 ATOM 5086 C CD2 . LEU A 1 700 ? 25.371 26.223 48.946 1.00 34.34 ? 700 LEU A CD2 1 ATOM 5087 N N . LYS A 1 701 ? 23.457 30.512 48.967 1.00 30.98 ? 701 LYS A N 1 ATOM 5088 C CA . LYS A 1 701 ? 23.128 31.851 48.505 1.00 33.69 ? 701 LYS A CA 1 ATOM 5089 C C . LYS A 1 701 ? 23.267 31.987 46.996 1.00 33.55 ? 701 LYS A C 1 ATOM 5090 O O . LYS A 1 701 ? 22.666 32.883 46.393 1.00 35.67 ? 701 LYS A O 1 ATOM 5091 C CB . LYS A 1 701 ? 24.017 32.875 49.202 1.00 36.60 ? 701 LYS A CB 1 ATOM 5092 C CG . LYS A 1 701 ? 23.917 32.825 50.717 1.00 40.91 ? 701 LYS A CG 1 ATOM 5093 C CD . LYS A 1 701 ? 24.761 33.918 51.351 1.00 45.50 ? 701 LYS A CD 1 ATOM 5094 C CE . LYS A 1 701 ? 24.637 33.920 52.867 1.00 47.16 ? 701 LYS A CE 1 ATOM 5095 N NZ . LYS A 1 701 ? 25.479 32.867 53.504 1.00 48.86 ? 701 LYS A NZ 1 ATOM 5096 N N . GLN A 1 702 ? 24.075 31.115 46.397 1.00 33.58 ? 702 GLN A N 1 ATOM 5097 C CA . GLN A 1 702 ? 24.328 31.122 44.957 1.00 34.40 ? 702 GLN A CA 1 ATOM 5098 C C . GLN A 1 702 ? 24.048 29.732 44.422 1.00 31.04 ? 702 GLN A C 1 ATOM 5099 O O . GLN A 1 702 ? 24.593 28.751 44.910 1.00 31.68 ? 702 GLN A O 1 ATOM 5100 C CB . GLN A 1 702 ? 25.791 31.479 44.646 1.00 37.22 ? 702 GLN A CB 1 ATOM 5101 C CG . GLN A 1 702 ? 26.286 32.804 45.220 1.00 40.38 ? 702 GLN A CG 1 ATOM 5102 C CD . GLN A 1 702 ? 25.600 34.022 44.612 1.00 43.53 ? 702 GLN A CD 1 ATOM 5103 O OE1 . GLN A 1 702 ? 25.399 34.104 43.396 1.00 44.67 ? 702 GLN A OE1 1 ATOM 5104 N NE2 . GLN A 1 702 ? 25.248 34.987 45.463 1.00 45.00 ? 702 GLN A NE2 1 ATOM 5105 N N . THR A 1 703 ? 23.196 29.648 43.417 1.00 28.61 ? 703 THR A N 1 ATOM 5106 C CA . THR A 1 703 ? 22.895 28.368 42.787 1.00 26.88 ? 703 THR A CA 1 ATOM 5107 C C . THR A 1 703 ? 24.005 27.970 41.822 1.00 26.36 ? 703 THR A C 1 ATOM 5108 O O . THR A 1 703 ? 24.700 28.835 41.315 1.00 25.83 ? 703 THR A O 1 ATOM 5109 C CB . THR A 1 703 ? 21.556 28.427 42.025 1.00 25.43 ? 703 THR A CB 1 ATOM 5110 O OG1 . THR A 1 703 ? 21.209 27.114 41.591 1.00 24.28 ? 703 THR A OG1 1 ATOM 5111 C CG2 . THR A 1 703 ? 21.634 29.374 40.810 1.00 24.75 ? 703 THR A CG2 1 ATOM 5112 N N . LYS A 1 704 ? 24.159 26.667 41.569 1.00 26.40 ? 704 LYS A N 1 ATOM 5113 C CA . LYS A 1 704 ? 25.041 26.178 40.494 1.00 27.47 ? 704 LYS A CA 1 ATOM 5114 C C . LYS A 1 704 ? 24.279 25.819 39.210 1.00 26.06 ? 704 LYS A C 1 ATOM 5115 O O . LYS A 1 704 ? 24.847 25.268 38.276 1.00 25.68 ? 704 LYS A O 1 ATOM 5116 C CB . LYS A 1 704 ? 25.849 24.978 40.974 1.00 29.56 ? 704 LYS A CB 1 ATOM 5117 C CG . LYS A 1 704 ? 26.929 25.345 41.978 1.00 32.08 ? 704 LYS A CG 1 ATOM 5118 C CD . LYS A 1 704 ? 27.511 24.104 42.634 1.00 33.92 ? 704 LYS A CD 1 ATOM 5119 C CE . LYS A 1 704 ? 28.400 24.449 43.818 1.00 35.18 ? 704 LYS A CE 1 ATOM 5120 N NZ . LYS A 1 704 ? 29.791 24.712 43.363 1.00 35.95 ? 704 LYS A NZ 1 ATOM 5121 N N . ASN A 1 705 ? 22.990 26.127 39.178 1.00 24.78 ? 705 ASN A N 1 ATOM 5122 C CA . ASN A 1 705 ? 22.166 25.918 38.004 1.00 24.08 ? 705 ASN A CA 1 ATOM 5123 C C . ASN A 1 705 ? 22.360 27.138 37.111 1.00 23.79 ? 705 ASN A C 1 ATOM 5124 O O . ASN A 1 705 ? 22.023 28.253 37.511 1.00 23.08 ? 705 ASN A O 1 ATOM 5125 C CB . ASN A 1 705 ? 20.701 25.767 38.453 1.00 23.89 ? 705 ASN A CB 1 ATOM 5126 C CG . ASN A 1 705 ? 19.771 25.322 37.339 1.00 23.57 ? 705 ASN A CG 1 ATOM 5127 O OD1 . ASN A 1 705 ? 19.843 25.819 36.215 1.00 25.19 ? 705 ASN A OD1 1 ATOM 5128 N ND2 . ASN A 1 705 ? 18.870 24.395 37.654 1.00 22.56 ? 705 ASN A ND2 1 ATOM 5129 N N . THR A 1 706 ? 22.900 26.932 35.910 1.00 23.47 ? 706 THR A N 1 ATOM 5130 C CA . THR A 1 706 ? 23.142 28.042 34.977 1.00 23.72 ? 706 THR A CA 1 ATOM 5131 C C . THR A 1 706 ? 21.907 28.470 34.184 1.00 24.84 ? 706 THR A C 1 ATOM 5132 O O . THR A 1 706 ? 21.929 29.517 33.520 1.00 25.63 ? 706 THR A O 1 ATOM 5133 C CB . THR A 1 706 ? 24.229 27.688 33.956 1.00 23.85 ? 706 THR A CB 1 ATOM 5134 O OG1 . THR A 1 706 ? 23.876 26.465 33.299 1.00 23.69 ? 706 THR A OG1 1 ATOM 5135 C CG2 . THR A 1 706 ? 25.587 27.538 34.637 1.00 23.66 ? 706 THR A CG2 1 ATOM 5136 N N . LEU A 1 707 ? 20.846 27.662 34.226 1.00 24.98 ? 707 LEU A N 1 ATOM 5137 C CA . LEU A 1 707 ? 19.648 27.924 33.426 1.00 25.47 ? 707 LEU A CA 1 ATOM 5138 C C . LEU A 1 707 ? 18.730 28.992 34.037 1.00 25.00 ? 707 LEU A C 1 ATOM 5139 O O . LEU A 1 707 ? 18.187 29.809 33.314 1.00 24.87 ? 707 LEU A O 1 ATOM 5140 C CB . LEU A 1 707 ? 18.864 26.623 33.184 1.00 26.12 ? 707 LEU A CB 1 ATOM 5141 C CG . LEU A 1 707 ? 17.463 26.722 32.545 1.00 26.58 ? 707 LEU A CG 1 ATOM 5142 C CD1 . LEU A 1 707 ? 17.530 27.269 31.124 1.00 26.66 ? 707 LEU A CD1 1 ATOM 5143 C CD2 . LEU A 1 707 ? 16.762 25.368 32.559 1.00 26.10 ? 707 LEU A CD2 1 ATOM 5144 N N . ARG A 1 708 ? 18.545 28.973 35.357 1.00 25.12 ? 708 ARG A N 1 ATOM 5145 C CA . ARG A 1 708 ? 17.572 29.842 36.002 1.00 25.09 ? 708 ARG A CA 1 ATOM 5146 C C . ARG A 1 708 ? 18.168 30.417 37.276 1.00 25.73 ? 708 ARG A C 1 ATOM 5147 O O . ARG A 1 708 ? 18.466 29.675 38.220 1.00 25.92 ? 708 ARG A O 1 ATOM 5148 C CB . ARG A 1 708 ? 16.281 29.067 36.313 1.00 25.72 ? 708 ARG A CB 1 ATOM 5149 C CG . ARG A 1 708 ? 15.096 29.947 36.714 1.00 25.78 ? 708 ARG A CG 1 ATOM 5150 C CD . ARG A 1 708 ? 14.026 29.165 37.475 1.00 25.57 ? 708 ARG A CD 1 ATOM 5151 N NE . ARG A 1 708 ? 13.002 30.036 38.058 1.00 25.52 ? 708 ARG A NE 1 ATOM 5152 C CZ . ARG A 1 708 ? 13.115 30.695 39.214 1.00 25.70 ? 708 ARG A CZ 1 ATOM 5153 N NH1 . ARG A 1 708 ? 14.216 30.604 39.955 1.00 25.85 ? 708 ARG A NH1 1 ATOM 5154 N NH2 . ARG A 1 708 ? 12.117 31.460 39.636 1.00 25.45 ? 708 ARG A NH2 1 ATOM 5155 N N . SER A 1 709 ? 18.346 31.738 37.292 1.00 25.66 ? 709 SER A N 1 ATOM 5156 C CA . SER A 1 709 ? 18.914 32.424 38.442 1.00 26.76 ? 709 SER A CA 1 ATOM 5157 C C . SER A 1 709 ? 17.896 32.520 39.572 1.00 26.33 ? 709 SER A C 1 ATOM 5158 O O . SER A 1 709 ? 16.694 32.495 39.352 1.00 27.37 ? 709 SER A O 1 ATOM 5159 C CB . SER A 1 709 ? 19.466 33.814 38.063 1.00 27.73 ? 709 SER A CB 1 ATOM 5160 O OG . SER A 1 709 ? 18.683 34.483 37.089 1.00 27.37 ? 709 SER A OG 1 ATOM 5161 N N . LEU A 1 710 ? 18.400 32.606 40.790 1.00 26.70 ? 710 LEU A N 1 ATOM 5162 C CA . LEU A 1 710 ? 17.556 32.621 41.977 1.00 26.86 ? 710 LEU A CA 1 ATOM 5163 C C . LEU A 1 710 ? 16.628 33.827 42.051 1.00 26.76 ? 710 LEU A C 1 ATOM 5164 O O . LEU A 1 710 ? 17.040 34.949 41.774 1.00 26.45 ? 710 LEU A O 1 ATOM 5165 C CB . LEU A 1 710 ? 18.423 32.564 43.236 1.00 26.67 ? 710 LEU A CB 1 ATOM 5166 C CG . LEU A 1 710 ? 19.203 31.265 43.413 1.00 25.93 ? 710 LEU A CG 1 ATOM 5167 C CD1 . LEU A 1 710 ? 19.935 31.265 44.740 1.00 25.87 ? 710 LEU A CD1 1 ATOM 5168 C CD2 . LEU A 1 710 ? 18.259 30.073 43.333 1.00 26.82 ? 710 LEU A CD2 1 ATOM 5169 N N . THR A 1 711 ? 15.367 33.553 42.397 1.00 26.98 ? 711 THR A N 1 ATOM 5170 C CA . THR A 1 711 ? 14.375 34.574 42.732 1.00 27.49 ? 711 THR A CA 1 ATOM 5171 C C . THR A 1 711 ? 13.950 34.437 44.210 1.00 27.71 ? 711 THR A C 1 ATOM 5172 O O . THR A 1 711 ? 12.929 34.989 44.618 1.00 28.93 ? 711 THR A O 1 ATOM 5173 C CB . THR A 1 711 ? 13.127 34.480 41.824 1.00 27.33 ? 711 THR A CB 1 ATOM 5174 O OG1 . THR A 1 711 ? 12.617 33.138 41.835 1.00 28.20 ? 711 THR A OG1 1 ATOM 5175 C CG2 . THR A 1 711 ? 13.455 34.860 40.389 1.00 27.04 ? 711 THR A CG2 1 ATOM 5176 N N . THR A 1 712 ? 14.737 33.695 44.993 1.00 26.94 ? 712 THR A N 1 ATOM 5177 C CA . THR A 1 712 ? 14.558 33.553 46.443 1.00 26.30 ? 712 THR A CA 1 ATOM 5178 C C . THR A 1 712 ? 15.901 33.829 47.128 1.00 25.87 ? 712 THR A C 1 ATOM 5179 O O . THR A 1 712 ? 16.945 33.853 46.459 1.00 26.15 ? 712 THR A O 1 ATOM 5180 C CB . THR A 1 712 ? 14.085 32.130 46.839 1.00 26.38 ? 712 THR A CB 1 ATOM 5181 O OG1 . THR A 1 712 ? 14.873 31.142 46.163 1.00 26.35 ? 712 THR A OG1 1 ATOM 5182 C CG2 . THR A 1 712 ? 12.635 31.932 46.488 1.00 26.10 ? 712 THR A CG2 1 ATOM 5183 N N . PRO A 1 713 ? 15.884 34.039 48.454 1.00 24.91 ? 713 PRO A N 1 ATOM 5184 C CA . PRO A 1 713 ? 17.122 34.354 49.189 1.00 24.87 ? 713 PRO A CA 1 ATOM 5185 C C . PRO A 1 713 ? 18.195 33.258 49.133 1.00 24.72 ? 713 PRO A C 1 ATOM 5186 O O . PRO A 1 713 ? 19.389 33.568 49.049 1.00 23.71 ? 713 PRO A O 1 ATOM 5187 C CB . PRO A 1 713 ? 16.641 34.551 50.630 1.00 24.43 ? 713 PRO A CB 1 ATOM 5188 C CG . PRO A 1 713 ? 15.207 34.917 50.515 1.00 24.69 ? 713 PRO A CG 1 ATOM 5189 C CD . PRO A 1 713 ? 14.679 34.264 49.275 1.00 24.72 ? 713 PRO A CD 1 ATOM 5190 N N . THR A 1 714 ? 17.764 32.002 49.212 1.00 23.80 ? 714 THR A N 1 ATOM 5191 C CA . THR A 1 714 ? 18.651 30.860 49.018 1.00 23.91 ? 714 THR A CA 1 ATOM 5192 C C . THR A 1 714 ? 18.087 29.964 47.931 1.00 22.77 ? 714 THR A C 1 ATOM 5193 O O . THR A 1 714 ? 16.898 30.059 47.590 1.00 22.06 ? 714 THR A O 1 ATOM 5194 C CB . THR A 1 714 ? 18.783 30.015 50.294 1.00 24.65 ? 714 THR A CB 1 ATOM 5195 O OG1 . THR A 1 714 ? 17.510 29.444 50.624 1.00 26.44 ? 714 THR A OG1 1 ATOM 5196 C CG2 . THR A 1 714 ? 19.289 30.867 51.472 1.00 24.85 ? 714 THR A CG2 1 ATOM 5197 N N . SER A 1 715 ? 18.935 29.097 47.386 1.00 21.51 ? 715 SER A N 1 ATOM 5198 C CA . SER A 1 715 ? 18.463 28.105 46.443 1.00 21.51 ? 715 SER A CA 1 ATOM 5199 C C . SER A 1 715 ? 17.527 27.131 47.132 1.00 20.48 ? 715 SER A C 1 ATOM 5200 O O . SER A 1 715 ? 17.863 26.548 48.164 1.00 20.30 ? 715 SER A O 1 ATOM 5201 C CB . SER A 1 715 ? 19.600 27.309 45.820 1.00 21.83 ? 715 SER A CB 1 ATOM 5202 O OG . SER A 1 715 ? 19.054 26.225 45.069 1.00 21.87 ? 715 SER A OG 1 ATOM 5203 N N . LEU A 1 716 ? 16.358 26.943 46.541 1.00 19.90 ? 716 LEU A N 1 ATOM 5204 C CA . LEU A 1 716 ? 15.454 25.893 46.986 1.00 19.27 ? 716 LEU A CA 1 ATOM 5205 C C . LEU A 1 716 ? 15.296 24.862 45.855 1.00 19.04 ? 716 LEU A C 1 ATOM 5206 O O . LEU A 1 716 ? 14.287 24.151 45.778 1.00 18.80 ? 716 LEU A O 1 ATOM 5207 C CB . LEU A 1 716 ? 14.127 26.509 47.440 1.00 19.19 ? 716 LEU A CB 1 ATOM 5208 C CG . LEU A 1 716 ? 14.240 27.590 48.534 1.00 19.51 ? 716 LEU A CG 1 ATOM 5209 C CD1 . LEU A 1 716 ? 12.903 28.290 48.758 1.00 19.87 ? 716 LEU A CD1 1 ATOM 5210 C CD2 . LEU A 1 716 ? 14.748 27.004 49.850 1.00 19.45 ? 716 LEU A CD2 1 ATOM 5211 N N . TYR A 1 717 ? 16.320 24.785 44.994 1.00 18.75 ? 717 TYR A N 1 ATOM 5212 C CA . TYR A 1 717 ? 16.392 23.806 43.911 1.00 17.93 ? 717 TYR A CA 1 ATOM 5213 C C . TYR A 1 717 ? 16.930 22.499 44.475 1.00 17.66 ? 717 TYR A C 1 ATOM 5214 O O . TYR A 1 717 ? 18.078 22.448 44.934 1.00 18.02 ? 717 TYR A O 1 ATOM 5215 C CB . TYR A 1 717 ? 17.353 24.253 42.800 1.00 17.79 ? 717 TYR A CB 1 ATOM 5216 C CG . TYR A 1 717 ? 17.076 25.581 42.085 1.00 18.22 ? 717 TYR A CG 1 ATOM 5217 C CD1 . TYR A 1 717 ? 15.857 26.253 42.205 1.00 17.90 ? 717 TYR A CD1 1 ATOM 5218 C CD2 . TYR A 1 717 ? 18.050 26.141 41.248 1.00 17.90 ? 717 TYR A CD2 1 ATOM 5219 C CE1 . TYR A 1 717 ? 15.633 27.454 41.545 1.00 17.73 ? 717 TYR A CE1 1 ATOM 5220 C CE2 . TYR A 1 717 ? 17.832 27.341 40.589 1.00 17.87 ? 717 TYR A CE2 1 ATOM 5221 C CZ . TYR A 1 717 ? 16.622 27.991 40.736 1.00 17.98 ? 717 TYR A CZ 1 ATOM 5222 O OH . TYR A 1 717 ? 16.409 29.174 40.065 1.00 17.56 ? 717 TYR A OH 1 ATOM 5223 N N . SER A 1 718 ? 16.134 21.434 44.400 1.00 17.13 ? 718 SER A N 1 ATOM 5224 C CA . SER A 1 718 ? 16.484 20.156 45.013 1.00 16.57 ? 718 SER A CA 1 ATOM 5225 C C . SER A 1 718 ? 17.833 19.612 44.564 1.00 17.09 ? 718 SER A C 1 ATOM 5226 O O . SER A 1 718 ? 18.588 19.059 45.375 1.00 17.47 ? 718 SER A O 1 ATOM 5227 C CB . SER A 1 718 ? 15.401 19.123 44.725 1.00 16.92 ? 718 SER A CB 1 ATOM 5228 O OG . SER A 1 718 ? 15.299 18.846 43.340 1.00 16.69 ? 718 SER A OG 1 ATOM 5229 N N . SER A 1 719 ? 18.146 19.762 43.281 1.00 17.45 ? 719 SER A N 1 ATOM 5230 C CA . SER A 1 719 ? 19.381 19.201 42.740 1.00 17.28 ? 719 SER A CA 1 ATOM 5231 C C . SER A 1 719 ? 20.641 19.967 43.179 1.00 17.82 ? 719 SER A C 1 ATOM 5232 O O . SER A 1 719 ? 21.722 19.375 43.195 1.00 18.38 ? 719 SER A O 1 ATOM 5233 C CB . SER A 1 719 ? 19.315 19.083 41.214 1.00 17.06 ? 719 SER A CB 1 ATOM 5234 O OG . SER A 1 719 ? 18.358 18.125 40.813 1.00 16.49 ? 719 SER A OG 1 ATOM 5235 N N . ASP A 1 720 ? 20.521 21.239 43.584 1.00 17.88 ? 720 ASP A N 1 ATOM 5236 C CA . ASP A 1 720 ? 21.664 21.933 44.230 1.00 17.60 ? 720 ASP A CA 1 ATOM 5237 C C . ASP A 1 720 ? 22.164 21.195 45.478 1.00 17.60 ? 720 ASP A C 1 ATOM 5238 O O . ASP A 1 720 ? 23.312 21.371 45.884 1.00 17.24 ? 720 ASP A O 1 ATOM 5239 C CB . ASP A 1 720 ? 21.317 23.374 44.648 1.00 18.11 ? 720 ASP A CB 1 ATOM 5240 C CG . ASP A 1 720 ? 21.542 24.401 43.535 1.00 18.75 ? 720 ASP A CG 1 ATOM 5241 O OD1 . ASP A 1 720 ? 22.547 24.321 42.789 1.00 18.75 ? 720 ASP A OD1 1 ATOM 5242 O OD2 . ASP A 1 720 ? 20.711 25.327 43.431 1.00 18.94 -1 720 ASP A OD2 1 ATOM 5243 N N . TYR A 1 721 ? 21.289 20.405 46.100 1.00 17.16 ? 721 TYR A N 1 ATOM 5244 C CA . TYR A 1 721 ? 21.612 19.679 47.328 1.00 17.27 ? 721 TYR A CA 1 ATOM 5245 C C . TYR A 1 721 ? 21.729 18.157 47.117 1.00 17.20 ? 721 TYR A C 1 ATOM 5246 O O . TYR A 1 721 ? 21.817 17.411 48.078 1.00 17.24 ? 721 TYR A O 1 ATOM 5247 C CB . TYR A 1 721 ? 20.551 20.004 48.398 1.00 17.01 ? 721 TYR A CB 1 ATOM 5248 C CG . TYR A 1 721 ? 20.441 21.489 48.653 1.00 17.11 ? 721 TYR A CG 1 ATOM 5249 C CD1 . TYR A 1 721 ? 19.664 22.289 47.842 1.00 17.28 ? 721 TYR A CD1 1 ATOM 5250 C CD2 . TYR A 1 721 ? 21.172 22.103 49.666 1.00 17.28 ? 721 TYR A CD2 1 ATOM 5251 C CE1 . TYR A 1 721 ? 19.580 23.656 48.046 1.00 17.67 ? 721 TYR A CE1 1 ATOM 5252 C CE2 . TYR A 1 721 ? 21.096 23.471 49.878 1.00 17.63 ? 721 TYR A CE2 1 ATOM 5253 C CZ . TYR A 1 721 ? 20.291 24.244 49.069 1.00 17.48 ? 721 TYR A CZ 1 ATOM 5254 O OH . TYR A 1 721 ? 20.190 25.602 49.273 1.00 17.25 ? 721 TYR A OH 1 ATOM 5255 N N . GLY A 1 722 ? 21.723 17.707 45.865 1.00 17.18 ? 722 GLY A N 1 ATOM 5256 C CA . GLY A 1 722 ? 21.889 16.293 45.551 1.00 16.96 ? 722 GLY A CA 1 ATOM 5257 C C . GLY A 1 722 ? 20.624 15.445 45.579 1.00 17.49 ? 722 GLY A C 1 ATOM 5258 O O . GLY A 1 722 ? 20.723 14.219 45.669 1.00 18.29 ? 722 GLY A O 1 ATOM 5259 N N . PHE A 1 723 ? 19.448 16.073 45.466 1.00 17.19 ? 723 PHE A N 1 ATOM 5260 C CA . PHE A 1 723 ? 18.157 15.365 45.517 1.00 17.16 ? 723 PHE A CA 1 ATOM 5261 C C . PHE A 1 723 ? 17.434 15.445 44.164 1.00 17.85 ? 723 PHE A C 1 ATOM 5262 O O . PHE A 1 723 ? 16.931 16.518 43.790 1.00 18.44 ? 723 PHE A O 1 ATOM 5263 C CB . PHE A 1 723 ? 17.263 15.975 46.602 1.00 16.55 ? 723 PHE A CB 1 ATOM 5264 C CG . PHE A 1 723 ? 17.824 15.869 48.013 1.00 15.68 ? 723 PHE A CG 1 ATOM 5265 C CD1 . PHE A 1 723 ? 18.075 14.628 48.595 1.00 14.96 ? 723 PHE A CD1 1 ATOM 5266 C CD2 . PHE A 1 723 ? 18.057 17.022 48.771 1.00 15.27 ? 723 PHE A CD2 1 ATOM 5267 C CE1 . PHE A 1 723 ? 18.575 14.534 49.887 1.00 14.79 ? 723 PHE A CE1 1 ATOM 5268 C CE2 . PHE A 1 723 ? 18.554 16.934 50.066 1.00 14.94 ? 723 PHE A CE2 1 ATOM 5269 C CZ . PHE A 1 723 ? 18.822 15.686 50.622 1.00 14.96 ? 723 PHE A CZ 1 ATOM 5270 N N . HIS A 1 724 ? 17.353 14.322 43.441 1.00 17.57 ? 724 HIS A N 1 ATOM 5271 C CA . HIS A 1 724 ? 16.888 14.345 42.035 1.00 17.40 ? 724 HIS A CA 1 ATOM 5272 C C . HIS A 1 724 ? 15.629 13.538 41.722 1.00 17.00 ? 724 HIS A C 1 ATOM 5273 O O . HIS A 1 724 ? 15.174 13.547 40.596 1.00 17.16 ? 724 HIS A O 1 ATOM 5274 C CB . HIS A 1 724 ? 18.001 13.851 41.121 1.00 17.26 ? 724 HIS A CB 1 ATOM 5275 C CG . HIS A 1 724 ? 19.349 14.393 41.472 1.00 17.62 ? 724 HIS A CG 1 ATOM 5276 N ND1 . HIS A 1 724 ? 19.637 15.740 41.437 1.00 17.23 ? 724 HIS A ND1 1 ATOM 5277 C CD2 . HIS A 1 724 ? 20.485 13.773 41.866 1.00 17.45 ? 724 HIS A CD2 1 ATOM 5278 C CE1 . HIS A 1 724 ? 20.892 15.927 41.803 1.00 17.34 ? 724 HIS A CE1 1 ATOM 5279 N NE2 . HIS A 1 724 ? 21.429 14.749 42.063 1.00 17.64 ? 724 HIS A NE2 1 ATOM 5280 N N . THR A 1 725 ? 15.066 12.842 42.696 1.00 17.04 ? 725 THR A N 1 ATOM 5281 C CA . THR A 1 725 ? 14.067 11.821 42.390 1.00 17.40 ? 725 THR A CA 1 ATOM 5282 C C . THR A 1 725 ? 13.037 11.662 43.507 1.00 17.23 ? 725 THR A C 1 ATOM 5283 O O . THR A 1 725 ? 13.338 11.889 44.679 1.00 17.86 ? 725 THR A O 1 ATOM 5284 C CB . THR A 1 725 ? 14.764 10.464 42.100 1.00 17.32 ? 725 THR A CB 1 ATOM 5285 O OG1 . THR A 1 725 ? 13.799 9.488 41.708 1.00 17.30 ? 725 THR A OG1 1 ATOM 5286 C CG2 . THR A 1 725 ? 15.522 9.956 43.326 1.00 17.36 ? 725 THR A CG2 1 ATOM 5287 N N . GLY A 1 726 ? 11.814 11.299 43.126 1.00 17.45 ? 726 GLY A N 1 ATOM 5288 C CA . GLY A 1 726 ? 10.750 10.978 44.085 1.00 17.23 ? 726 GLY A CA 1 ATOM 5289 C C . GLY A 1 726 ? 10.196 12.197 44.786 1.00 17.19 ? 726 GLY A C 1 ATOM 5290 O O . GLY A 1 726 ? 10.416 13.321 44.332 1.00 18.12 ? 726 GLY A O 1 ATOM 5291 N N . TYR A 1 727 ? 9.482 11.982 45.892 1.00 16.53 ? 727 TYR A N 1 ATOM 5292 C CA . TYR A 1 727 ? 8.828 13.076 46.613 1.00 16.54 ? 727 TYR A CA 1 ATOM 5293 C C . TYR A 1 727 ? 9.858 13.922 47.351 1.00 16.54 ? 727 TYR A C 1 ATOM 5294 O O . TYR A 1 727 ? 10.750 13.383 47.970 1.00 16.83 ? 727 TYR A O 1 ATOM 5295 C CB . TYR A 1 727 ? 7.790 12.547 47.619 1.00 16.15 ? 727 TYR A CB 1 ATOM 5296 C CG . TYR A 1 727 ? 6.554 11.863 47.034 1.00 15.95 ? 727 TYR A CG 1 ATOM 5297 C CD1 . TYR A 1 727 ? 6.394 11.659 45.663 1.00 16.00 ? 727 TYR A CD1 1 ATOM 5298 C CD2 . TYR A 1 727 ? 5.548 11.396 47.878 1.00 15.64 ? 727 TYR A CD2 1 ATOM 5299 C CE1 . TYR A 1 727 ? 5.257 11.036 45.163 1.00 15.95 ? 727 TYR A CE1 1 ATOM 5300 C CE2 . TYR A 1 727 ? 4.414 10.769 47.390 1.00 15.29 ? 727 TYR A CE2 1 ATOM 5301 C CZ . TYR A 1 727 ? 4.271 10.584 46.039 1.00 15.65 ? 727 TYR A CZ 1 ATOM 5302 O OH . TYR A 1 727 ? 3.151 9.950 45.563 1.00 15.77 ? 727 TYR A OH 1 ATOM 5303 N N . LEU A 1 728 ? 9.721 15.246 47.275 1.00 16.99 ? 728 LEU A N 1 ATOM 5304 C CA . LEU A 1 728 ? 10.612 16.169 47.991 1.00 18.12 ? 728 LEU A CA 1 ATOM 5305 C C . LEU A 1 728 ? 9.851 16.856 49.105 1.00 18.13 ? 728 LEU A C 1 ATOM 5306 O O . LEU A 1 728 ? 8.697 17.198 48.935 1.00 18.92 ? 728 LEU A O 1 ATOM 5307 C CB . LEU A 1 728 ? 11.188 17.240 47.053 1.00 18.18 ? 728 LEU A CB 1 ATOM 5308 C CG . LEU A 1 728 ? 11.751 16.803 45.694 1.00 18.14 ? 728 LEU A CG 1 ATOM 5309 C CD1 . LEU A 1 728 ? 11.916 18.004 44.768 1.00 18.32 ? 728 LEU A CD1 1 ATOM 5310 C CD2 . LEU A 1 728 ? 13.074 16.089 45.870 1.00 18.24 ? 728 LEU A CD2 1 ATOM 5311 N N . LEU A 1 729 ? 10.493 17.046 50.251 1.00 18.63 ? 729 LEU A N 1 ATOM 5312 C CA . LEU A 1 729 ? 9.876 17.766 51.360 1.00 18.38 ? 729 LEU A CA 1 ATOM 5313 C C . LEU A 1 729 ? 10.737 18.948 51.729 1.00 18.50 ? 729 LEU A C 1 ATOM 5314 O O . LEU A 1 729 ? 11.965 18.816 51.812 1.00 17.57 ? 729 LEU A O 1 ATOM 5315 C CB . LEU A 1 729 ? 9.726 16.872 52.577 1.00 18.87 ? 729 LEU A CB 1 ATOM 5316 C CG . LEU A 1 729 ? 8.740 15.714 52.436 1.00 19.02 ? 729 LEU A CG 1 ATOM 5317 C CD1 . LEU A 1 729 ? 9.419 14.491 51.860 1.00 19.22 ? 729 LEU A CD1 1 ATOM 5318 C CD2 . LEU A 1 729 ? 8.167 15.392 53.806 1.00 20.04 ? 729 LEU A CD2 1 ATOM 5319 N N . TYR A 1 730 ? 10.085 20.096 51.935 1.00 17.76 ? 730 TYR A N 1 ATOM 5320 C CA . TYR A 1 730 ? 10.749 21.313 52.385 1.00 17.61 ? 730 TYR A CA 1 ATOM 5321 C C . TYR A 1 730 ? 10.126 21.736 53.714 1.00 17.64 ? 730 TYR A C 1 ATOM 5322 O O . TYR A 1 730 ? 8.918 21.542 53.925 1.00 17.31 ? 730 TYR A O 1 ATOM 5323 C CB . TYR A 1 730 ? 10.585 22.435 51.357 1.00 17.64 ? 730 TYR A CB 1 ATOM 5324 C CG . TYR A 1 730 ? 11.355 22.211 50.074 1.00 17.58 ? 730 TYR A CG 1 ATOM 5325 C CD1 . TYR A 1 730 ? 10.893 21.321 49.105 1.00 17.37 ? 730 TYR A CD1 1 ATOM 5326 C CD2 . TYR A 1 730 ? 12.535 22.903 49.820 1.00 17.43 ? 730 TYR A CD2 1 ATOM 5327 C CE1 . TYR A 1 730 ? 11.593 21.121 47.927 1.00 17.46 ? 730 TYR A CE1 1 ATOM 5328 C CE2 . TYR A 1 730 ? 13.247 22.715 48.642 1.00 17.35 ? 730 TYR A CE2 1 ATOM 5329 C CZ . TYR A 1 730 ? 12.778 21.822 47.696 1.00 17.34 ? 730 TYR A CZ 1 ATOM 5330 O OH . TYR A 1 730 ? 13.489 21.621 46.533 1.00 16.42 ? 730 TYR A OH 1 ATOM 5331 N N . ARG A 1 731 ? 10.945 22.303 54.600 1.00 17.25 ? 731 ARG A N 1 ATOM 5332 C CA . ARG A 1 731 ? 10.478 22.799 55.899 1.00 17.80 ? 731 ARG A CA 1 ATOM 5333 C C . ARG A 1 731 ? 10.998 24.211 56.141 1.00 17.82 ? 731 ARG A C 1 ATOM 5334 O O . ARG A 1 731 ? 12.199 24.434 56.147 1.00 18.59 ? 731 ARG A O 1 ATOM 5335 C CB . ARG A 1 731 ? 10.883 21.840 57.020 1.00 17.75 ? 731 ARG A CB 1 ATOM 5336 C CG . ARG A 1 731 ? 10.015 20.596 57.039 1.00 17.87 ? 731 ARG A CG 1 ATOM 5337 C CD . ARG A 1 731 ? 10.500 19.534 58.009 1.00 18.52 ? 731 ARG A CD 1 ATOM 5338 N NE . ARG A 1 731 ? 10.473 19.958 59.414 1.00 19.21 ? 731 ARG A NE 1 ATOM 5339 C CZ . ARG A 1 731 ? 9.371 20.103 60.157 1.00 19.66 ? 731 ARG A CZ 1 ATOM 5340 N NH1 . ARG A 1 731 ? 8.150 19.904 59.648 1.00 19.00 ? 731 ARG A NH1 1 ATOM 5341 N NH2 . ARG A 1 731 ? 9.493 20.478 61.426 1.00 19.87 ? 731 ARG A NH2 1 ATOM 5342 N N . GLY A 1 732 ? 10.086 25.167 56.308 1.00 17.76 ? 732 GLY A N 1 ATOM 5343 C CA . GLY A 1 732 ? 10.457 26.572 56.418 1.00 18.09 ? 732 GLY A CA 1 ATOM 5344 C C . GLY A 1 732 ? 10.144 27.140 57.787 1.00 17.80 ? 732 GLY A C 1 ATOM 5345 O O . GLY A 1 732 ? 8.984 27.374 58.102 1.00 18.01 ? 732 GLY A O 1 ATOM 5346 N N . HIS A 1 733 ? 11.182 27.390 58.580 1.00 17.57 ? 733 HIS A N 1 ATOM 5347 C CA . HIS A 1 733 ? 11.022 27.904 59.946 1.00 17.73 ? 733 HIS A CA 1 ATOM 5348 C C . HIS A 1 733 ? 10.932 29.422 59.946 1.00 17.48 ? 733 HIS A C 1 ATOM 5349 O O . HIS A 1 733 ? 11.701 30.089 59.259 1.00 16.91 ? 733 HIS A O 1 ATOM 5350 C CB . HIS A 1 733 ? 12.207 27.507 60.821 1.00 17.83 ? 733 HIS A CB 1 ATOM 5351 C CG . HIS A 1 733 ? 12.386 26.034 60.967 1.00 18.55 ? 733 HIS A CG 1 ATOM 5352 N ND1 . HIS A 1 733 ? 12.414 25.408 62.195 1.00 18.98 ? 733 HIS A ND1 1 ATOM 5353 C CD2 . HIS A 1 733 ? 12.535 25.056 60.040 1.00 18.85 ? 733 HIS A CD2 1 ATOM 5354 C CE1 . HIS A 1 733 ? 12.588 24.110 62.017 1.00 19.12 ? 733 HIS A CE1 1 ATOM 5355 N NE2 . HIS A 1 733 ? 12.665 23.872 60.718 1.00 18.87 ? 733 HIS A NE2 1 ATOM 5356 N N . PHE A 1 734 ? 9.989 29.957 60.718 1.00 17.73 ? 734 PHE A N 1 ATOM 5357 C CA . PHE A 1 734 ? 9.944 31.388 60.999 1.00 17.42 ? 734 PHE A CA 1 ATOM 5358 C C . PHE A 1 734 ? 9.332 31.682 62.382 1.00 18.20 ? 734 PHE A C 1 ATOM 5359 O O . PHE A 1 734 ? 8.667 30.845 62.992 1.00 18.06 ? 734 PHE A O 1 ATOM 5360 C CB . PHE A 1 734 ? 9.244 32.161 59.868 1.00 16.92 ? 734 PHE A CB 1 ATOM 5361 C CG . PHE A 1 734 ? 7.746 31.963 59.799 1.00 16.86 ? 734 PHE A CG 1 ATOM 5362 C CD1 . PHE A 1 734 ? 7.203 30.824 59.212 1.00 16.38 ? 734 PHE A CD1 1 ATOM 5363 C CD2 . PHE A 1 734 ? 6.872 32.945 60.286 1.00 16.74 ? 734 PHE A CD2 1 ATOM 5364 C CE1 . PHE A 1 734 ? 5.828 30.641 59.148 1.00 16.24 ? 734 PHE A CE1 1 ATOM 5365 C CE2 . PHE A 1 734 ? 5.496 32.767 60.218 1.00 16.75 ? 734 PHE A CE2 1 ATOM 5366 C CZ . PHE A 1 734 ? 4.974 31.609 59.652 1.00 16.50 ? 734 PHE A CZ 1 ATOM 5367 N N . THR A 1 735 ? 9.639 32.867 62.885 1.00 18.80 ? 735 THR A N 1 ATOM 5368 C CA . THR A 1 735 ? 9.098 33.362 64.123 1.00 19.74 ? 735 THR A CA 1 ATOM 5369 C C . THR A 1 735 ? 8.026 34.340 63.706 1.00 19.26 ? 735 THR A C 1 ATOM 5370 O O . THR A 1 735 ? 8.280 35.228 62.891 1.00 19.41 ? 735 THR A O 1 ATOM 5371 C CB . THR A 1 735 ? 10.187 34.066 64.950 1.00 20.24 ? 735 THR A CB 1 ATOM 5372 O OG1 . THR A 1 735 ? 11.183 33.106 65.316 1.00 21.37 ? 735 THR A OG1 1 ATOM 5373 C CG2 . THR A 1 735 ? 9.599 34.689 66.215 1.00 20.94 ? 735 THR A CG2 1 ATOM 5374 N N . ALA A 1 736 ? 6.820 34.149 64.229 1.00 19.47 ? 736 ALA A N 1 ATOM 5375 C CA . ALA A 1 736 ? 5.681 34.948 63.813 1.00 19.42 ? 736 ALA A CA 1 ATOM 5376 C C . ALA A 1 736 ? 5.740 36.301 64.496 1.00 20.52 ? 736 ALA A C 1 ATOM 5377 O O . ALA A 1 736 ? 6.191 36.400 65.648 1.00 20.27 ? 736 ALA A O 1 ATOM 5378 C CB . ALA A 1 736 ? 4.385 34.239 64.149 1.00 19.02 ? 736 ALA A CB 1 ATOM 5379 N N . THR A 1 737 ? 5.324 37.334 63.762 1.00 21.18 ? 737 THR A N 1 ATOM 5380 C CA . THR A 1 737 ? 5.056 38.663 64.313 1.00 21.64 ? 737 THR A CA 1 ATOM 5381 C C . THR A 1 737 ? 3.610 38.764 64.802 1.00 22.70 ? 737 THR A C 1 ATOM 5382 O O . THR A 1 737 ? 3.284 39.621 65.627 1.00 22.45 ? 737 THR A O 1 ATOM 5383 C CB . THR A 1 737 ? 5.224 39.780 63.252 1.00 22.00 ? 737 THR A CB 1 ATOM 5384 O OG1 . THR A 1 737 ? 4.187 39.676 62.266 1.00 21.67 ? 737 THR A OG1 1 ATOM 5385 C CG2 . THR A 1 737 ? 6.599 39.731 62.569 1.00 21.93 ? 737 THR A CG2 1 ATOM 5386 N N . GLY A 1 738 ? 2.730 37.923 64.261 1.00 23.91 ? 738 GLY A N 1 ATOM 5387 C CA . GLY A 1 738 ? 1.294 37.981 64.597 1.00 24.76 ? 738 GLY A CA 1 ATOM 5388 C C . GLY A 1 738 ? 0.472 38.778 63.595 1.00 25.73 ? 738 GLY A C 1 ATOM 5389 O O . GLY A 1 738 ? -0.753 38.826 63.696 1.00 24.11 ? 738 GLY A O 1 ATOM 5390 N N . ASN A 1 739 ? 1.146 39.414 62.636 1.00 27.70 ? 739 ASN A N 1 ATOM 5391 C CA . ASN A 1 739 ? 0.471 40.089 61.542 1.00 30.57 ? 739 ASN A CA 1 ATOM 5392 C C . ASN A 1 739 ? 0.331 39.259 60.257 1.00 30.23 ? 739 ASN A C 1 ATOM 5393 O O . ASN A 1 739 ? -0.174 39.769 59.258 1.00 31.52 ? 739 ASN A O 1 ATOM 5394 C CB . ASN A 1 739 ? 1.194 41.398 61.200 1.00 33.03 ? 739 ASN A CB 1 ATOM 5395 C CG . ASN A 1 739 ? 0.385 42.273 60.256 1.00 36.62 ? 739 ASN A CG 1 ATOM 5396 O OD1 . ASN A 1 739 ? 0.847 42.649 59.166 1.00 36.28 ? 739 ASN A OD1 1 ATOM 5397 N ND2 . ASN A 1 739 ? -0.859 42.588 60.672 1.00 40.00 ? 739 ASN A ND2 1 ATOM 5398 N N . GLU A 1 740 ? 0.746 37.995 60.268 1.00 29.55 ? 740 GLU A N 1 ATOM 5399 C CA . GLU A 1 740 ? 0.767 37.201 59.030 1.00 29.62 ? 740 GLU A CA 1 ATOM 5400 C C . GLU A 1 740 ? -0.634 36.879 58.527 1.00 29.18 ? 740 GLU A C 1 ATOM 5401 O O . GLU A 1 740 ? -1.503 36.430 59.295 1.00 27.98 ? 740 GLU A O 1 ATOM 5402 C CB . GLU A 1 740 ? 1.541 35.899 59.208 1.00 30.37 ? 740 GLU A CB 1 ATOM 5403 C CG . GLU A 1 740 ? 3.045 36.096 59.367 1.00 30.78 ? 740 GLU A CG 1 ATOM 5404 C CD . GLU A 1 740 ? 3.461 36.466 60.789 1.00 29.94 ? 740 GLU A CD 1 ATOM 5405 O OE1 . GLU A 1 740 ? 2.577 36.603 61.680 1.00 26.27 ? 740 GLU A OE1 1 ATOM 5406 O OE2 . GLU A 1 740 ? 4.689 36.605 60.999 1.00 29.57 -1 740 GLU A OE2 1 ATOM 5407 N N . SER A 1 741 ? -0.833 37.125 57.232 1.00 28.65 ? 741 SER A N 1 ATOM 5408 C CA . SER A 1 741 ? -2.112 36.886 56.567 1.00 28.48 ? 741 SER A CA 1 ATOM 5409 C C . SER A 1 741 ? -1.997 35.725 55.569 1.00 27.26 ? 741 SER A C 1 ATOM 5410 O O . SER A 1 741 ? -2.629 34.677 55.751 1.00 27.75 ? 741 SER A O 1 ATOM 5411 C CB . SER A 1 741 ? -2.590 38.161 55.859 1.00 28.41 ? 741 SER A CB 1 ATOM 5412 O OG . SER A 1 741 ? -1.641 38.617 54.900 1.00 30.31 ? 741 SER A OG 1 ATOM 5413 N N . THR A 1 742 ? -1.183 35.913 54.530 1.00 24.53 ? 742 THR A N 1 ATOM 5414 C CA . THR A 1 742 ? -1.079 34.939 53.448 1.00 22.89 ? 742 THR A CA 1 ATOM 5415 C C . THR A 1 742 ? 0.340 34.480 53.207 1.00 21.88 ? 742 THR A C 1 ATOM 5416 O O . THR A 1 742 ? 1.296 35.187 53.522 1.00 21.47 ? 742 THR A O 1 ATOM 5417 C CB . THR A 1 742 ? -1.592 35.520 52.117 1.00 22.65 ? 742 THR A CB 1 ATOM 5418 O OG1 . THR A 1 742 ? -0.856 36.702 51.805 1.00 22.15 ? 742 THR A OG1 1 ATOM 5419 C CG2 . THR A 1 742 ? -3.089 35.856 52.206 1.00 22.65 ? 742 THR A CG2 1 ATOM 5420 N N . PHE A 1 743 ? 0.449 33.286 52.631 1.00 21.25 ? 743 PHE A N 1 ATOM 5421 C CA . PHE A 1 743 ? 1.715 32.726 52.182 1.00 20.73 ? 743 PHE A CA 1 ATOM 5422 C C . PHE A 1 743 ? 1.553 32.207 50.755 1.00 20.67 ? 743 PHE A C 1 ATOM 5423 O O . PHE A 1 743 ? 0.773 31.286 50.501 1.00 19.76 ? 743 PHE A O 1 ATOM 5424 C CB . PHE A 1 743 ? 2.162 31.609 53.115 1.00 20.61 ? 743 PHE A CB 1 ATOM 5425 C CG . PHE A 1 743 ? 3.349 30.823 52.610 1.00 20.36 ? 743 PHE A CG 1 ATOM 5426 C CD1 . PHE A 1 743 ? 4.633 31.351 52.683 1.00 20.28 ? 743 PHE A CD1 1 ATOM 5427 C CD2 . PHE A 1 743 ? 3.181 29.546 52.084 1.00 19.60 ? 743 PHE A CD2 1 ATOM 5428 C CE1 . PHE A 1 743 ? 5.720 30.629 52.226 1.00 19.65 ? 743 PHE A CE1 1 ATOM 5429 C CE2 . PHE A 1 743 ? 4.263 28.818 51.631 1.00 19.34 ? 743 PHE A CE2 1 ATOM 5430 C CZ . PHE A 1 743 ? 5.532 29.362 51.697 1.00 19.60 ? 743 PHE A CZ 1 ATOM 5431 N N . ALA A 1 744 ? 2.275 32.831 49.827 1.00 20.90 ? 744 ALA A N 1 ATOM 5432 C CA . ALA A 1 744 ? 2.232 32.461 48.413 1.00 20.66 ? 744 ALA A CA 1 ATOM 5433 C C . ALA A 1 744 ? 3.435 31.593 48.112 1.00 20.34 ? 744 ALA A C 1 ATOM 5434 O O . ALA A 1 744 ? 4.509 31.800 48.674 1.00 20.07 ? 744 ALA A O 1 ATOM 5435 C CB . ALA A 1 744 ? 2.253 33.703 47.538 1.00 20.86 ? 744 ALA A CB 1 ATOM 5436 N N . ILE A 1 745 ? 3.263 30.619 47.231 1.00 19.95 ? 745 ILE A N 1 ATOM 5437 C CA . ILE A 1 745 ? 4.366 29.748 46.892 1.00 19.74 ? 745 ILE A CA 1 ATOM 5438 C C . ILE A 1 745 ? 4.228 29.218 45.467 1.00 19.54 ? 745 ILE A C 1 ATOM 5439 O O . ILE A 1 745 ? 3.128 28.878 45.018 1.00 19.16 ? 745 ILE A O 1 ATOM 5440 C CB . ILE A 1 745 ? 4.519 28.620 47.950 1.00 19.59 ? 745 ILE A CB 1 ATOM 5441 C CG1 . ILE A 1 745 ? 5.784 27.791 47.689 1.00 19.41 ? 745 ILE A CG1 1 ATOM 5442 C CG2 . ILE A 1 745 ? 3.272 27.749 48.003 1.00 19.53 ? 745 ILE A CG2 1 ATOM 5443 C CD1 . ILE A 1 745 ? 6.092 26.767 48.772 1.00 19.43 ? 745 ILE A CD1 1 ATOM 5444 N N . ASP A 1 746 ? 5.365 29.170 44.771 1.00 19.49 ? 746 ASP A N 1 ATOM 5445 C CA . ASP A 1 746 ? 5.457 28.674 43.408 1.00 19.77 ? 746 ASP A CA 1 ATOM 5446 C C . ASP A 1 746 ? 6.237 27.369 43.471 1.00 18.77 ? 746 ASP A C 1 ATOM 5447 O O . ASP A 1 746 ? 7.464 27.382 43.647 1.00 18.54 ? 746 ASP A O 1 ATOM 5448 C CB . ASP A 1 746 ? 6.172 29.705 42.511 1.00 21.48 ? 746 ASP A CB 1 ATOM 5449 C CG . ASP A 1 746 ? 6.163 29.329 41.016 1.00 23.68 ? 746 ASP A CG 1 ATOM 5450 O OD1 . ASP A 1 746 ? 5.544 28.307 40.635 1.00 25.00 ? 746 ASP A OD1 1 ATOM 5451 O OD2 . ASP A 1 746 ? 6.779 30.074 40.204 1.00 25.95 -1 746 ASP A OD2 1 ATOM 5452 N N . THR A 1 747 ? 5.525 26.248 43.358 1.00 17.20 ? 747 THR A N 1 ATOM 5453 C CA . THR A 1 747 ? 6.148 24.923 43.363 1.00 16.73 ? 747 THR A CA 1 ATOM 5454 C C . THR A 1 747 ? 6.342 24.416 41.933 1.00 16.82 ? 747 THR A C 1 ATOM 5455 O O . THR A 1 747 ? 5.559 24.741 41.059 1.00 16.66 ? 747 THR A O 1 ATOM 5456 C CB . THR A 1 747 ? 5.340 23.891 44.199 1.00 16.39 ? 747 THR A CB 1 ATOM 5457 O OG1 . THR A 1 747 ? 3.969 23.856 43.786 1.00 15.59 ? 747 THR A OG1 1 ATOM 5458 C CG2 . THR A 1 747 ? 5.392 24.246 45.670 1.00 16.46 ? 747 THR A CG2 1 ATOM 5459 N N . GLN A 1 748 ? 7.404 23.639 41.705 1.00 16.88 ? 748 GLN A N 1 ATOM 5460 C CA . GLN A 1 748 ? 7.708 23.088 40.386 1.00 17.11 ? 748 GLN A CA 1 ATOM 5461 C C . GLN A 1 748 ? 8.217 21.637 40.482 1.00 16.56 ? 748 GLN A C 1 ATOM 5462 O O . GLN A 1 748 ? 9.294 21.375 41.007 1.00 16.36 ? 748 GLN A O 1 ATOM 5463 C CB . GLN A 1 748 ? 8.737 23.951 39.662 1.00 17.67 ? 748 GLN A CB 1 ATOM 5464 C CG . GLN A 1 748 ? 9.168 23.410 38.290 1.00 18.39 ? 748 GLN A CG 1 ATOM 5465 C CD . GLN A 1 748 ? 9.762 24.491 37.392 1.00 18.76 ? 748 GLN A CD 1 ATOM 5466 O OE1 . GLN A 1 748 ? 9.042 25.295 36.819 1.00 18.64 ? 748 GLN A OE1 1 ATOM 5467 N NE2 . GLN A 1 748 ? 11.083 24.514 37.280 1.00 19.23 ? 748 GLN A NE2 1 ATOM 5468 N N . GLY A 1 749 ? 7.420 20.709 39.974 1.00 15.95 ? 749 GLY A N 1 ATOM 5469 C CA . GLY A 1 749 ? 7.775 19.294 39.969 1.00 15.66 ? 749 GLY A CA 1 ATOM 5470 C C . GLY A 1 749 ? 7.670 18.618 38.621 1.00 15.43 ? 749 GLY A C 1 ATOM 5471 O O . GLY A 1 749 ? 7.891 17.407 38.534 1.00 15.82 ? 749 GLY A O 1 ATOM 5472 N N . GLY A 1 750 ? 7.374 19.380 37.566 1.00 14.93 ? 750 GLY A N 1 ATOM 5473 C CA . GLY A 1 750 ? 7.214 18.807 36.217 1.00 15.11 ? 750 GLY A CA 1 ATOM 5474 C C . GLY A 1 750 ? 5.760 18.548 35.877 1.00 14.78 ? 750 GLY A C 1 ATOM 5475 O O . GLY A 1 750 ? 4.887 18.757 36.710 1.00 15.06 ? 750 GLY A O 1 ATOM 5476 N N . SER A 1 751 ? 5.487 18.104 34.655 1.00 14.66 ? 751 SER A N 1 ATOM 5477 C CA . SER A 1 751 ? 4.097 17.940 34.186 1.00 14.56 ? 751 SER A CA 1 ATOM 5478 C C . SER A 1 751 ? 3.331 16.938 35.041 1.00 14.08 ? 751 SER A C 1 ATOM 5479 O O . SER A 1 751 ? 3.845 15.881 35.348 1.00 13.79 ? 751 SER A O 1 ATOM 5480 C CB . SER A 1 751 ? 4.065 17.487 32.724 1.00 15.02 ? 751 SER A CB 1 ATOM 5481 O OG . SER A 1 751 ? 4.621 16.190 32.570 1.00 14.89 ? 751 SER A OG 1 ATOM 5482 N N . ALA A 1 752 ? 2.100 17.294 35.409 1.00 14.06 ? 752 ALA A N 1 ATOM 5483 C CA . ALA A 1 752 ? 1.199 16.456 36.219 1.00 13.94 ? 752 ALA A CA 1 ATOM 5484 C C . ALA A 1 752 ? 1.627 16.326 37.689 1.00 14.36 ? 752 ALA A C 1 ATOM 5485 O O . ALA A 1 752 ? 1.173 15.422 38.395 1.00 14.77 ? 752 ALA A O 1 ATOM 5486 C CB . ALA A 1 752 ? 1.006 15.078 35.585 1.00 13.62 ? 752 ALA A CB 1 ATOM 5487 N N . PHE A 1 753 ? 2.472 17.240 38.162 1.00 14.43 ? 753 PHE A N 1 ATOM 5488 C CA . PHE A 1 753 ? 2.942 17.188 39.540 1.00 14.28 ? 753 PHE A CA 1 ATOM 5489 C C . PHE A 1 753 ? 1.853 17.739 40.460 1.00 15.04 ? 753 PHE A C 1 ATOM 5490 O O . PHE A 1 753 ? 0.964 18.489 40.016 1.00 14.73 ? 753 PHE A O 1 ATOM 5491 C CB . PHE A 1 753 ? 4.248 17.995 39.719 1.00 14.03 ? 753 PHE A CB 1 ATOM 5492 C CG . PHE A 1 753 ? 4.029 19.430 40.105 1.00 13.45 ? 753 PHE A CG 1 ATOM 5493 C CD1 . PHE A 1 753 ? 3.566 20.357 39.177 1.00 13.50 ? 753 PHE A CD1 1 ATOM 5494 C CD2 . PHE A 1 753 ? 4.249 19.849 41.405 1.00 13.58 ? 753 PHE A CD2 1 ATOM 5495 C CE1 . PHE A 1 753 ? 3.328 21.680 39.543 1.00 13.55 ? 753 PHE A CE1 1 ATOM 5496 C CE2 . PHE A 1 753 ? 4.027 21.174 41.778 1.00 13.28 ? 753 PHE A CE2 1 ATOM 5497 C CZ . PHE A 1 753 ? 3.569 22.087 40.845 1.00 13.28 ? 753 PHE A CZ 1 ATOM 5498 N N . GLY A 1 754 ? 1.947 17.380 41.742 1.00 15.05 ? 754 GLY A N 1 ATOM 5499 C CA . GLY A 1 754 ? 1.129 17.996 42.783 1.00 15.35 ? 754 GLY A CA 1 ATOM 5500 C C . GLY A 1 754 ? 1.956 18.411 43.993 1.00 15.34 ? 754 GLY A C 1 ATOM 5501 O O . GLY A 1 754 ? 3.098 17.971 44.167 1.00 15.89 ? 754 GLY A O 1 ATOM 5502 N N . SER A 1 755 ? 1.367 19.256 44.827 1.00 14.56 ? 755 SER A N 1 ATOM 5503 C CA . SER A 1 755 ? 2.001 19.726 46.037 1.00 14.51 ? 755 SER A CA 1 ATOM 5504 C C . SER A 1 755 ? 0.972 19.995 47.152 1.00 14.28 ? 755 SER A C 1 ATOM 5505 O O . SER A 1 755 ? -0.161 20.384 46.896 1.00 14.23 ? 755 SER A O 1 ATOM 5506 C CB . SER A 1 755 ? 2.866 20.977 45.750 1.00 14.61 ? 755 SER A CB 1 ATOM 5507 O OG . SER A 1 755 ? 2.121 22.038 45.161 1.00 14.44 ? 755 SER A OG 1 ATOM 5508 N N . SER A 1 756 ? 1.369 19.747 48.392 1.00 14.09 ? 756 SER A N 1 ATOM 5509 C CA . SER A 1 756 ? 0.513 20.015 49.538 1.00 13.83 ? 756 SER A CA 1 ATOM 5510 C C . SER A 1 756 ? 1.306 20.848 50.551 1.00 14.30 ? 756 SER A C 1 ATOM 5511 O O . SER A 1 756 ? 2.551 20.702 50.667 1.00 13.40 ? 756 SER A O 1 ATOM 5512 C CB . SER A 1 756 ? 0.022 18.709 50.164 1.00 13.73 ? 756 SER A CB 1 ATOM 5513 O OG . SER A 1 756 ? -0.673 17.895 49.215 1.00 13.52 ? 756 SER A OG 1 ATOM 5514 N N . VAL A 1 757 ? 0.588 21.720 51.276 1.00 14.31 ? 757 VAL A N 1 ATOM 5515 C CA . VAL A 1 757 ? 1.214 22.617 52.255 1.00 14.60 ? 757 VAL A CA 1 ATOM 5516 C C . VAL A 1 757 ? 0.515 22.643 53.617 1.00 14.64 ? 757 VAL A C 1 ATOM 5517 O O . VAL A 1 757 ? -0.708 22.723 53.690 1.00 14.81 ? 757 VAL A O 1 ATOM 5518 C CB . VAL A 1 757 ? 1.314 24.049 51.701 1.00 14.64 ? 757 VAL A CB 1 ATOM 5519 C CG1 . VAL A 1 757 ? 2.069 24.939 52.676 1.00 14.94 ? 757 VAL A CG1 1 ATOM 5520 C CG2 . VAL A 1 757 ? 2.031 24.045 50.361 1.00 14.63 ? 757 VAL A CG2 1 ATOM 5521 N N . TRP A 1 758 ? 1.309 22.585 54.687 1.00 14.73 ? 758 TRP A N 1 ATOM 5522 C CA . TRP A 1 758 ? 0.814 22.668 56.057 1.00 14.91 ? 758 TRP A CA 1 ATOM 5523 C C . TRP A 1 758 ? 1.550 23.754 56.830 1.00 15.91 ? 758 TRP A C 1 ATOM 5524 O O . TRP A 1 758 ? 2.747 23.979 56.605 1.00 16.44 ? 758 TRP A O 1 ATOM 5525 C CB . TRP A 1 758 ? 1.047 21.354 56.798 1.00 14.76 ? 758 TRP A CB 1 ATOM 5526 C CG . TRP A 1 758 ? 0.170 20.223 56.411 1.00 14.43 ? 758 TRP A CG 1 ATOM 5527 C CD1 . TRP A 1 758 ? -0.960 19.809 57.061 1.00 14.57 ? 758 TRP A CD1 1 ATOM 5528 C CD2 . TRP A 1 758 ? 0.370 19.308 55.325 1.00 14.19 ? 758 TRP A CD2 1 ATOM 5529 N NE1 . TRP A 1 758 ? -1.494 18.706 56.431 1.00 14.53 ? 758 TRP A NE1 1 ATOM 5530 C CE2 . TRP A 1 758 ? -0.701 18.378 55.361 1.00 14.28 ? 758 TRP A CE2 1 ATOM 5531 C CE3 . TRP A 1 758 ? 1.340 19.185 54.323 1.00 14.15 ? 758 TRP A CE3 1 ATOM 5532 C CZ2 . TRP A 1 758 ? -0.827 17.343 54.439 1.00 13.95 ? 758 TRP A CZ2 1 ATOM 5533 C CZ3 . TRP A 1 758 ? 1.216 18.149 53.395 1.00 14.20 ? 758 TRP A CZ3 1 ATOM 5534 C CH2 . TRP A 1 758 ? 0.133 17.245 53.457 1.00 14.17 ? 758 TRP A CH2 1 ATOM 5535 N N . LEU A 1 759 ? 0.844 24.405 57.750 1.00 16.83 ? 759 LEU A N 1 ATOM 5536 C CA . LEU A 1 759 ? 1.463 25.287 58.751 1.00 18.48 ? 759 LEU A CA 1 ATOM 5537 C C . LEU A 1 759 ? 1.386 24.549 60.090 1.00 18.74 ? 759 LEU A C 1 ATOM 5538 O O . LEU A 1 759 ? 0.296 24.339 60.631 1.00 18.56 ? 759 LEU A O 1 ATOM 5539 C CB . LEU A 1 759 ? 0.742 26.636 58.812 1.00 19.35 ? 759 LEU A CB 1 ATOM 5540 C CG . LEU A 1 759 ? 1.309 27.792 59.655 1.00 20.02 ? 759 LEU A CG 1 ATOM 5541 C CD1 . LEU A 1 759 ? 1.231 27.480 61.126 1.00 20.67 ? 759 LEU A CD1 1 ATOM 5542 C CD2 . LEU A 1 759 ? 2.744 28.147 59.285 1.00 20.73 ? 759 LEU A CD2 1 ATOM 5543 N N . ASN A 1 760 ? 2.544 24.158 60.615 1.00 19.26 ? 760 ASN A N 1 ATOM 5544 C CA . ASN A 1 760 ? 2.606 23.187 61.688 1.00 20.01 ? 760 ASN A CA 1 ATOM 5545 C C . ASN A 1 760 ? 1.695 21.992 61.334 1.00 19.66 ? 760 ASN A C 1 ATOM 5546 O O . ASN A 1 760 ? 1.988 21.287 60.376 1.00 19.90 ? 760 ASN A O 1 ATOM 5547 C CB . ASN A 1 760 ? 2.330 23.862 63.054 1.00 21.44 ? 760 ASN A CB 1 ATOM 5548 C CG . ASN A 1 760 ? 3.592 24.466 63.655 1.00 22.47 ? 760 ASN A CG 1 ATOM 5549 O OD1 . ASN A 1 760 ? 4.266 25.256 63.012 1.00 21.94 ? 760 ASN A OD1 1 ATOM 5550 N ND2 . ASN A 1 760 ? 3.930 24.065 64.888 1.00 25.38 ? 760 ASN A ND2 1 ATOM 5551 N N . GLY A 1 761 ? 0.586 21.787 62.037 1.00 19.63 ? 761 GLY A N 1 ATOM 5552 C CA . GLY A 1 761 ? -0.338 20.693 61.725 1.00 19.41 ? 761 GLY A CA 1 ATOM 5553 C C . GLY A 1 761 ? -1.584 21.104 60.959 1.00 19.25 ? 761 GLY A C 1 ATOM 5554 O O . GLY A 1 761 ? -2.437 20.275 60.690 1.00 19.85 ? 761 GLY A O 1 ATOM 5555 N N . THR A 1 762 ? -1.693 22.379 60.604 1.00 18.85 ? 762 THR A N 1 ATOM 5556 C CA . THR A 1 762 ? -2.868 22.889 59.911 1.00 18.49 ? 762 THR A CA 1 ATOM 5557 C C . THR A 1 762 ? -2.669 22.768 58.392 1.00 18.45 ? 762 THR A C 1 ATOM 5558 O O . THR A 1 762 ? -1.753 23.373 57.825 1.00 18.18 ? 762 THR A O 1 ATOM 5559 C CB . THR A 1 762 ? -3.126 24.361 60.291 1.00 18.23 ? 762 THR A CB 1 ATOM 5560 O OG1 . THR A 1 762 ? -3.150 24.490 61.717 1.00 18.44 ? 762 THR A OG1 1 ATOM 5561 C CG2 . THR A 1 762 ? -4.437 24.860 59.722 1.00 18.32 ? 762 THR A CG2 1 ATOM 5562 N N . TYR A 1 763 ? -3.530 21.977 57.753 1.00 18.03 ? 763 TYR A N 1 ATOM 5563 C CA . TYR A 1 763 ? -3.535 21.801 56.310 1.00 18.05 ? 763 TYR A CA 1 ATOM 5564 C C . TYR A 1 763 ? -3.954 23.110 55.655 1.00 17.91 ? 763 TYR A C 1 ATOM 5565 O O . TYR A 1 763 ? -5.031 23.606 55.936 1.00 18.36 ? 763 TYR A O 1 ATOM 5566 C CB . TYR A 1 763 ? -4.509 20.680 55.935 1.00 17.89 ? 763 TYR A CB 1 ATOM 5567 C CG . TYR A 1 763 ? -4.617 20.408 54.451 1.00 18.05 ? 763 TYR A CG 1 ATOM 5568 C CD1 . TYR A 1 763 ? -3.494 20.098 53.702 1.00 17.76 ? 763 TYR A CD1 1 ATOM 5569 C CD2 . TYR A 1 763 ? -5.850 20.469 53.794 1.00 18.68 ? 763 TYR A CD2 1 ATOM 5570 C CE1 . TYR A 1 763 ? -3.584 19.852 52.345 1.00 17.94 ? 763 TYR A CE1 1 ATOM 5571 C CE2 . TYR A 1 763 ? -5.953 20.223 52.434 1.00 18.33 ? 763 TYR A CE2 1 ATOM 5572 C CZ . TYR A 1 763 ? -4.814 19.913 51.717 1.00 18.37 ? 763 TYR A CZ 1 ATOM 5573 O OH . TYR A 1 763 ? -4.899 19.665 50.374 1.00 18.88 ? 763 TYR A OH 1 ATOM 5574 N N . LEU A 1 764 ? -3.084 23.680 54.826 1.00 17.71 ? 764 LEU A N 1 ATOM 5575 C CA . LEU A 1 764 ? -3.380 24.934 54.113 1.00 18.13 ? 764 LEU A CA 1 ATOM 5576 C C . LEU A 1 764 ? -4.046 24.706 52.765 1.00 17.46 ? 764 LEU A C 1 ATOM 5577 O O . LEU A 1 764 ? -4.920 25.469 52.382 1.00 17.24 ? 764 LEU A O 1 ATOM 5578 C CB . LEU A 1 764 ? -2.108 25.761 53.903 1.00 18.83 ? 764 LEU A CB 1 ATOM 5579 C CG . LEU A 1 764 ? -1.435 26.289 55.173 1.00 19.74 ? 764 LEU A CG 1 ATOM 5580 C CD1 . LEU A 1 764 ? -0.270 27.200 54.831 1.00 20.04 ? 764 LEU A CD1 1 ATOM 5581 C CD2 . LEU A 1 764 ? -2.440 27.029 56.050 1.00 20.06 ? 764 LEU A CD2 1 ATOM 5582 N N . GLY A 1 765 ? -3.625 23.660 52.056 1.00 17.12 ? 765 GLY A N 1 ATOM 5583 C CA . GLY A 1 765 ? -4.196 23.296 50.761 1.00 17.12 ? 765 GLY A CA 1 ATOM 5584 C C . GLY A 1 765 ? -3.241 22.484 49.885 1.00 17.61 ? 765 GLY A C 1 ATOM 5585 O O . GLY A 1 765 ? -2.125 22.145 50.286 1.00 16.61 ? 765 GLY A O 1 ATOM 5586 N N . SER A 1 766 ? -3.696 22.171 48.676 1.00 17.89 ? 766 SER A N 1 ATOM 5587 C CA . SER A 1 766 ? -2.903 21.428 47.712 1.00 17.50 ? 766 SER A CA 1 ATOM 5588 C C . SER A 1 766 ? -3.105 21.987 46.318 1.00 17.73 ? 766 SER A C 1 ATOM 5589 O O . SER A 1 766 ? -4.167 22.514 45.997 1.00 18.30 ? 766 SER A O 1 ATOM 5590 C CB . SER A 1 766 ? -3.309 19.949 47.706 1.00 17.70 ? 766 SER A CB 1 ATOM 5591 O OG . SER A 1 766 ? -3.095 19.330 48.969 1.00 17.53 ? 766 SER A OG 1 ATOM 5592 N N . TRP A 1 767 ? -2.057 21.906 45.508 1.00 17.85 ? 767 TRP A N 1 ATOM 5593 C CA . TRP A 1 767 ? -2.203 21.902 44.064 1.00 17.45 ? 767 TRP A CA 1 ATOM 5594 C C . TRP A 1 767 ? -2.375 20.442 43.650 1.00 17.46 ? 767 TRP A C 1 ATOM 5595 O O . TRP A 1 767 ? -1.436 19.644 43.742 1.00 17.57 ? 767 TRP A O 1 ATOM 5596 C CB . TRP A 1 767 ? -0.987 22.546 43.386 1.00 17.03 ? 767 TRP A CB 1 ATOM 5597 C CG . TRP A 1 767 ? -0.991 22.363 41.904 1.00 16.47 ? 767 TRP A CG 1 ATOM 5598 C CD1 . TRP A 1 767 ? -0.002 21.819 41.153 1.00 16.08 ? 767 TRP A CD1 1 ATOM 5599 C CD2 . TRP A 1 767 ? -2.059 22.682 41.000 1.00 16.39 ? 767 TRP A CD2 1 ATOM 5600 N NE1 . TRP A 1 767 ? -0.368 21.792 39.835 1.00 16.45 ? 767 TRP A NE1 1 ATOM 5601 C CE2 . TRP A 1 767 ? -1.628 22.318 39.710 1.00 16.31 ? 767 TRP A CE2 1 ATOM 5602 C CE3 . TRP A 1 767 ? -3.334 23.252 41.156 1.00 16.37 ? 767 TRP A CE3 1 ATOM 5603 C CZ2 . TRP A 1 767 ? -2.423 22.493 38.579 1.00 16.32 ? 767 TRP A CZ2 1 ATOM 5604 C CZ3 . TRP A 1 767 ? -4.122 23.439 40.032 1.00 16.25 ? 767 TRP A CZ3 1 ATOM 5605 C CH2 . TRP A 1 767 ? -3.659 23.066 38.754 1.00 16.70 ? 767 TRP A CH2 1 ATOM 5606 N N . THR A 1 768 ? -3.589 20.090 43.233 1.00 18.05 ? 768 THR A N 1 ATOM 5607 C CA . THR A 1 768 ? -3.950 18.704 42.888 1.00 17.91 ? 768 THR A CA 1 ATOM 5608 C C . THR A 1 768 ? -3.367 18.241 41.545 1.00 17.93 ? 768 THR A C 1 ATOM 5609 O O . THR A 1 768 ? -3.247 17.031 41.300 1.00 18.36 ? 768 THR A O 1 ATOM 5610 C CB . THR A 1 768 ? -5.487 18.520 42.863 1.00 18.43 ? 768 THR A CB 1 ATOM 5611 O OG1 . THR A 1 768 ? -6.093 19.599 42.144 1.00 18.62 ? 768 THR A OG1 1 ATOM 5612 C CG2 . THR A 1 768 ? -6.045 18.505 44.277 1.00 18.24 ? 768 THR A CG2 1 ATOM 5613 N N . GLY A 1 769 ? -3.016 19.187 40.676 1.00 17.63 ? 769 GLY A N 1 ATOM 5614 C CA . GLY A 1 769 ? -2.207 18.883 39.487 1.00 18.07 ? 769 GLY A CA 1 ATOM 5615 C C . GLY A 1 769 ? -2.947 18.805 38.163 1.00 18.47 ? 769 GLY A C 1 ATOM 5616 O O . GLY A 1 769 ? -4.127 18.458 38.109 1.00 19.34 ? 769 GLY A O 1 ATOM 5617 N N . LEU A 1 770 ? -2.240 19.150 37.092 1.00 18.60 ? 770 LEU A N 1 ATOM 5618 C CA . LEU A 1 770 ? -2.722 18.984 35.719 1.00 18.85 ? 770 LEU A CA 1 ATOM 5619 C C . LEU A 1 770 ? -1.541 18.609 34.833 1.00 18.84 ? 770 LEU A C 1 ATOM 5620 O O . LEU A 1 770 ? -0.401 19.030 35.084 1.00 18.77 ? 770 LEU A O 1 ATOM 5621 C CB . LEU A 1 770 ? -3.366 20.275 35.191 1.00 18.64 ? 770 LEU A CB 1 ATOM 5622 C CG . LEU A 1 770 ? -4.733 20.685 35.746 1.00 18.90 ? 770 LEU A CG 1 ATOM 5623 C CD1 . LEU A 1 770 ? -5.165 22.033 35.158 1.00 18.90 ? 770 LEU A CD1 1 ATOM 5624 C CD2 . LEU A 1 770 ? -5.792 19.615 35.503 1.00 18.87 ? 770 LEU A CD2 1 ATOM 5625 N N . TYR A 1 771 ? -1.797 17.815 33.799 1.00 19.21 ? 771 TYR A N 1 ATOM 5626 C CA . TYR A 1 771 ? -0.748 17.543 32.820 1.00 19.72 ? 771 TYR A CA 1 ATOM 5627 C C . TYR A 1 771 ? -0.193 18.861 32.258 1.00 19.07 ? 771 TYR A C 1 ATOM 5628 O O . TYR A 1 771 ? 1.008 19.010 32.088 1.00 18.35 ? 771 TYR A O 1 ATOM 5629 C CB . TYR A 1 771 ? -1.225 16.626 31.686 1.00 20.49 ? 771 TYR A CB 1 ATOM 5630 C CG . TYR A 1 771 ? -0.138 16.402 30.660 1.00 21.12 ? 771 TYR A CG 1 ATOM 5631 C CD1 . TYR A 1 771 ? 1.033 15.748 31.003 1.00 21.85 ? 771 TYR A CD1 1 ATOM 5632 C CD2 . TYR A 1 771 ? -0.259 16.893 29.367 1.00 22.07 ? 771 TYR A CD2 1 ATOM 5633 C CE1 . TYR A 1 771 ? 2.047 15.560 30.078 1.00 22.34 ? 771 TYR A CE1 1 ATOM 5634 C CE2 . TYR A 1 771 ? 0.746 16.707 28.436 1.00 22.98 ? 771 TYR A CE2 1 ATOM 5635 C CZ . TYR A 1 771 ? 1.896 16.044 28.804 1.00 22.45 ? 771 TYR A CZ 1 ATOM 5636 O OH . TYR A 1 771 ? 2.895 15.871 27.895 1.00 24.08 ? 771 TYR A OH 1 ATOM 5637 N N . ALA A 1 772 ? -1.068 19.826 32.008 1.00 19.24 ? 772 ALA A N 1 ATOM 5638 C CA . ALA A 1 772 ? -0.635 21.142 31.498 1.00 19.32 ? 772 ALA A CA 1 ATOM 5639 C C . ALA A 1 772 ? 0.197 22.012 32.472 1.00 19.40 ? 772 ALA A C 1 ATOM 5640 O O . ALA A 1 772 ? 0.737 23.016 32.052 1.00 19.60 ? 772 ALA A O 1 ATOM 5641 C CB . ALA A 1 772 ? -1.846 21.927 31.012 1.00 18.91 ? 772 ALA A CB 1 ATOM 5642 N N . ASN A 1 773 ? 0.284 21.664 33.752 1.00 19.26 ? 773 ASN A N 1 ATOM 5643 C CA . ASN A 1 773 ? 1.112 22.431 34.694 1.00 19.85 ? 773 ASN A CA 1 ATOM 5644 C C . ASN A 1 773 ? 2.376 21.692 35.134 1.00 19.27 ? 773 ASN A C 1 ATOM 5645 O O . ASN A 1 773 ? 2.300 20.615 35.706 1.00 18.41 ? 773 ASN A O 1 ATOM 5646 C CB . ASN A 1 773 ? 0.304 22.832 35.935 1.00 20.29 ? 773 ASN A CB 1 ATOM 5647 C CG . ASN A 1 773 ? -0.507 24.100 35.714 1.00 20.63 ? 773 ASN A CG 1 ATOM 5648 O OD1 . ASN A 1 773 ? -0.107 25.199 36.111 1.00 21.67 ? 773 ASN A OD1 1 ATOM 5649 N ND2 . ASN A 1 773 ? -1.642 23.955 35.072 1.00 20.73 ? 773 ASN A ND2 1 ATOM 5650 N N . SER A 1 774 ? 3.535 22.274 34.849 1.00 19.22 ? 774 SER A N 1 ATOM 5651 C CA . SER A 1 774 ? 4.786 21.805 35.443 1.00 19.54 ? 774 SER A CA 1 ATOM 5652 C C . SER A 1 774 ? 5.219 22.671 36.628 1.00 19.29 ? 774 SER A C 1 ATOM 5653 O O . SER A 1 774 ? 6.096 22.276 37.382 1.00 18.51 ? 774 SER A O 1 ATOM 5654 C CB . SER A 1 774 ? 5.897 21.711 34.391 1.00 20.03 ? 774 SER A CB 1 ATOM 5655 O OG . SER A 1 774 ? 6.056 22.935 33.710 1.00 20.54 ? 774 SER A OG 1 ATOM 5656 N N . ASP A 1 775 ? 4.617 23.851 36.787 1.00 19.98 ? 775 ASP A N 1 ATOM 5657 C CA . ASP A 1 775 ? 4.721 24.606 38.040 1.00 20.62 ? 775 ASP A CA 1 ATOM 5658 C C . ASP A 1 775 ? 3.341 25.137 38.424 1.00 20.30 ? 775 ASP A C 1 ATOM 5659 O O . ASP A 1 775 ? 2.408 25.011 37.646 1.00 20.93 ? 775 ASP A O 1 ATOM 5660 C CB . ASP A 1 775 ? 5.798 25.713 37.970 1.00 21.27 ? 775 ASP A CB 1 ATOM 5661 C CG . ASP A 1 775 ? 5.349 26.964 37.214 1.00 22.38 ? 775 ASP A CG 1 ATOM 5662 O OD1 . ASP A 1 775 ? 5.085 26.860 36.002 1.00 23.13 ? 775 ASP A OD1 1 ATOM 5663 O OD2 . ASP A 1 775 ? 5.298 28.069 37.827 1.00 22.69 -1 775 ASP A OD2 1 ATOM 5664 N N . TYR A 1 776 ? 3.198 25.672 39.632 1.00 20.19 ? 776 TYR A N 1 ATOM 5665 C CA . TYR A 1 776 ? 1.925 26.269 40.051 1.00 20.37 ? 776 TYR A CA 1 ATOM 5666 C C . TYR A 1 776 ? 2.093 27.328 41.133 1.00 19.89 ? 776 TYR A C 1 ATOM 5667 O O . TYR A 1 776 ? 2.815 27.122 42.099 1.00 19.24 ? 776 TYR A O 1 ATOM 5668 C CB . TYR A 1 776 ? 0.954 25.191 40.542 1.00 20.59 ? 776 TYR A CB 1 ATOM 5669 C CG . TYR A 1 776 ? -0.426 25.726 40.874 1.00 20.77 ? 776 TYR A CG 1 ATOM 5670 C CD1 . TYR A 1 776 ? -1.346 26.007 39.863 1.00 21.58 ? 776 TYR A CD1 1 ATOM 5671 C CD2 . TYR A 1 776 ? -0.804 25.966 42.186 1.00 21.06 ? 776 TYR A CD2 1 ATOM 5672 C CE1 . TYR A 1 776 ? -2.613 26.499 40.152 1.00 22.16 ? 776 TYR A CE1 1 ATOM 5673 C CE2 . TYR A 1 776 ? -2.065 26.461 42.492 1.00 22.15 ? 776 TYR A CE2 1 ATOM 5674 C CZ . TYR A 1 776 ? -2.969 26.724 41.472 1.00 22.42 ? 776 TYR A CZ 1 ATOM 5675 O OH . TYR A 1 776 ? -4.222 27.210 41.765 1.00 23.63 ? 776 TYR A OH 1 ATOM 5676 N N . ASN A 1 777 ? 1.396 28.450 40.960 1.00 20.36 ? 777 ASN A N 1 ATOM 5677 C CA . ASN A 1 777 ? 1.363 29.540 41.949 1.00 20.62 ? 777 ASN A CA 1 ATOM 5678 C C . ASN A 1 777 ? 0.146 29.477 42.885 1.00 20.14 ? 777 ASN A C 1 ATOM 5679 O O . ASN A 1 777 ? -0.966 29.826 42.498 1.00 19.90 ? 777 ASN A O 1 ATOM 5680 C CB . ASN A 1 777 ? 1.371 30.871 41.229 1.00 20.88 ? 777 ASN A CB 1 ATOM 5681 C CG . ASN A 1 777 ? 2.668 31.101 40.476 1.00 22.45 ? 777 ASN A CG 1 ATOM 5682 O OD1 . ASN A 1 777 ? 3.751 31.063 41.067 1.00 22.49 ? 777 ASN A OD1 1 ATOM 5683 N ND2 . ASN A 1 777 ? 2.571 31.329 39.170 1.00 22.70 ? 777 ASN A ND2 1 ATOM 5684 N N . ALA A 1 778 ? 0.362 29.028 44.115 1.00 19.09 ? 778 ALA A N 1 ATOM 5685 C CA . ALA A 1 778 ? -0.705 28.977 45.081 1.00 19.38 ? 778 ALA A CA 1 ATOM 5686 C C . ALA A 1 778 ? -0.615 30.175 46.010 1.00 19.58 ? 778 ALA A C 1 ATOM 5687 O O . ALA A 1 778 ? 0.460 30.751 46.191 1.00 19.73 ? 778 ALA A O 1 ATOM 5688 C CB . ALA A 1 778 ? -0.627 27.690 45.874 1.00 19.52 ? 778 ALA A CB 1 ATOM 5689 N N . THR A 1 779 ? -1.751 30.560 46.578 1.00 20.17 ? 779 THR A N 1 ATOM 5690 C CA . THR A 1 779 ? -1.781 31.530 47.667 1.00 21.06 ? 779 THR A CA 1 ATOM 5691 C C . THR A 1 779 ? -2.599 30.914 48.787 1.00 21.72 ? 779 THR A C 1 ATOM 5692 O O . THR A 1 779 ? -3.726 30.470 48.584 1.00 22.49 ? 779 THR A O 1 ATOM 5693 C CB . THR A 1 779 ? -2.383 32.860 47.216 1.00 21.85 ? 779 THR A CB 1 ATOM 5694 O OG1 . THR A 1 779 ? -1.635 33.352 46.101 1.00 21.42 ? 779 THR A OG1 1 ATOM 5695 C CG2 . THR A 1 779 ? -2.348 33.888 48.344 1.00 22.47 ? 779 THR A CG2 1 ATOM 5696 N N . TYR A 1 780 ? -2.014 30.839 49.966 1.00 21.80 ? 780 TYR A N 1 ATOM 5697 C CA . TYR A 1 780 ? -2.678 30.191 51.070 1.00 22.27 ? 780 TYR A CA 1 ATOM 5698 C C . TYR A 1 780 ? -2.929 31.233 52.133 1.00 23.69 ? 780 TYR A C 1 ATOM 5699 O O . TYR A 1 780 ? -2.135 32.173 52.298 1.00 23.15 ? 780 TYR A O 1 ATOM 5700 C CB . TYR A 1 780 ? -1.838 29.020 51.596 1.00 21.58 ? 780 TYR A CB 1 ATOM 5701 C CG . TYR A 1 780 ? -1.678 27.913 50.582 1.00 20.88 ? 780 TYR A CG 1 ATOM 5702 C CD1 . TYR A 1 780 ? -2.798 27.270 50.047 1.00 20.63 ? 780 TYR A CD1 1 ATOM 5703 C CD2 . TYR A 1 780 ? -0.418 27.506 50.146 1.00 20.74 ? 780 TYR A CD2 1 ATOM 5704 C CE1 . TYR A 1 780 ? -2.669 26.268 49.103 1.00 20.39 ? 780 TYR A CE1 1 ATOM 5705 C CE2 . TYR A 1 780 ? -0.279 26.491 49.201 1.00 20.07 ? 780 TYR A CE2 1 ATOM 5706 C CZ . TYR A 1 780 ? -1.405 25.875 48.686 1.00 20.05 ? 780 TYR A CZ 1 ATOM 5707 O OH . TYR A 1 780 ? -1.287 24.884 47.745 1.00 18.86 ? 780 TYR A OH 1 ATOM 5708 N N . ASN A 1 781 ? -4.054 31.073 52.819 1.00 25.10 ? 781 ASN A N 1 ATOM 5709 C CA . ASN A 1 781 ? -4.460 31.972 53.891 1.00 27.41 ? 781 ASN A CA 1 ATOM 5710 C C . ASN A 1 781 ? -4.158 31.321 55.225 1.00 27.22 ? 781 ASN A C 1 ATOM 5711 O O . ASN A 1 781 ? -4.604 30.214 55.506 1.00 26.74 ? 781 ASN A O 1 ATOM 5712 C CB . ASN A 1 781 ? -5.939 32.316 53.763 1.00 28.35 ? 781 ASN A CB 1 ATOM 5713 C CG . ASN A 1 781 ? -6.296 32.777 52.358 1.00 30.42 ? 781 ASN A CG 1 ATOM 5714 O OD1 . ASN A 1 781 ? -6.650 31.957 51.490 1.00 31.84 ? 781 ASN A OD1 1 ATOM 5715 N ND2 . ASN A 1 781 ? -6.155 34.079 52.106 1.00 30.25 ? 781 ASN A ND2 1 ATOM 5716 N N . LEU A 1 782 ? -3.370 32.018 56.032 1.00 27.34 ? 782 LEU A N 1 ATOM 5717 C CA . LEU A 1 782 ? -2.860 31.450 57.263 1.00 27.55 ? 782 LEU A CA 1 ATOM 5718 C C . LEU A 1 782 ? -3.842 31.684 58.379 1.00 26.83 ? 782 LEU A C 1 ATOM 5719 O O . LEU A 1 782 ? -4.553 32.676 58.374 1.00 26.37 ? 782 LEU A O 1 ATOM 5720 C CB . LEU A 1 782 ? -1.519 32.084 57.620 1.00 27.32 ? 782 LEU A CB 1 ATOM 5721 C CG . LEU A 1 782 ? -0.452 31.862 56.546 1.00 27.68 ? 782 LEU A CG 1 ATOM 5722 C CD1 . LEU A 1 782 ? 0.686 32.859 56.699 1.00 27.95 ? 782 LEU A CD1 1 ATOM 5723 C CD2 . LEU A 1 782 ? 0.062 30.429 56.564 1.00 27.28 ? 782 LEU A CD2 1 ATOM 5724 N N . PRO A 1 783 ? -3.883 30.771 59.355 1.00 27.72 ? 783 PRO A N 1 ATOM 5725 C CA . PRO A 1 783 ? -4.643 31.120 60.538 1.00 28.19 ? 783 PRO A CA 1 ATOM 5726 C C . PRO A 1 783 ? -3.993 32.287 61.297 1.00 28.56 ? 783 PRO A C 1 ATOM 5727 O O . PRO A 1 783 ? -2.953 32.825 60.896 1.00 26.38 ? 783 PRO A O 1 ATOM 5728 C CB . PRO A 1 783 ? -4.616 29.833 61.371 1.00 28.66 ? 783 PRO A CB 1 ATOM 5729 C CG . PRO A 1 783 ? -3.413 29.099 60.906 1.00 28.31 ? 783 PRO A CG 1 ATOM 5730 C CD . PRO A 1 783 ? -3.261 29.441 59.455 1.00 27.76 ? 783 PRO A CD 1 ATOM 5731 N N . GLN A 1 784 ? -4.643 32.674 62.382 1.00 29.53 ? 784 GLN A N 1 ATOM 5732 C CA . GLN A 1 784 ? -4.143 33.697 63.280 1.00 29.52 ? 784 GLN A CA 1 ATOM 5733 C C . GLN A 1 784 ? -2.916 33.157 64.007 1.00 27.70 ? 784 GLN A C 1 ATOM 5734 O O . GLN A 1 784 ? -3.003 32.154 64.720 1.00 26.75 ? 784 GLN A O 1 ATOM 5735 C CB . GLN A 1 784 ? -5.240 34.034 64.281 1.00 31.38 ? 784 GLN A CB 1 ATOM 5736 C CG . GLN A 1 784 ? -5.028 35.315 65.049 1.00 34.61 ? 784 GLN A CG 1 ATOM 5737 C CD . GLN A 1 784 ? -6.224 35.627 65.931 1.00 37.10 ? 784 GLN A CD 1 ATOM 5738 O OE1 . GLN A 1 784 ? -6.627 34.795 66.762 1.00 38.40 ? 784 GLN A OE1 1 ATOM 5739 N NE2 . GLN A 1 784 ? -6.801 36.820 65.759 1.00 35.64 ? 784 GLN A NE2 1 ATOM 5740 N N . LEU A 1 785 ? -1.770 33.801 63.812 1.00 25.41 ? 785 LEU A N 1 ATOM 5741 C CA . LEU A 1 785 ? -0.527 33.309 64.415 1.00 24.93 ? 785 LEU A CA 1 ATOM 5742 C C . LEU A 1 785 ? -0.199 34.027 65.732 1.00 24.42 ? 785 LEU A C 1 ATOM 5743 O O . LEU A 1 785 ? -0.566 35.179 65.928 1.00 23.25 ? 785 LEU A O 1 ATOM 5744 C CB . LEU A 1 785 ? 0.633 33.451 63.431 1.00 24.45 ? 785 LEU A CB 1 ATOM 5745 C CG . LEU A 1 785 ? 0.475 32.743 62.084 1.00 24.32 ? 785 LEU A CG 1 ATOM 5746 C CD1 . LEU A 1 785 ? 1.734 32.913 61.251 1.00 24.67 ? 785 LEU A CD1 1 ATOM 5747 C CD2 . LEU A 1 785 ? 0.149 31.266 62.256 1.00 23.69 ? 785 LEU A CD2 1 ATOM 5748 N N . GLN A 1 786 ? 0.490 33.317 66.625 1.00 25.48 ? 786 GLN A N 1 ATOM 5749 C CA . GLN A 1 786 ? 0.858 33.821 67.947 1.00 24.73 ? 786 GLN A CA 1 ATOM 5750 C C . GLN A 1 786 ? 2.196 34.531 67.871 1.00 22.91 ? 786 GLN A C 1 ATOM 5751 O O . GLN A 1 786 ? 3.204 33.902 67.565 1.00 21.20 ? 786 GLN A O 1 ATOM 5752 C CB . GLN A 1 786 ? 0.964 32.660 68.926 1.00 27.49 ? 786 GLN A CB 1 ATOM 5753 C CG . GLN A 1 786 ? -0.345 31.918 69.157 1.00 29.84 ? 786 GLN A CG 1 ATOM 5754 C CD . GLN A 1 786 ? -0.168 30.685 70.038 1.00 31.99 ? 786 GLN A CD 1 ATOM 5755 O OE1 . GLN A 1 786 ? -0.585 29.582 69.676 1.00 34.64 ? 786 GLN A OE1 1 ATOM 5756 N NE2 . GLN A 1 786 ? 0.462 30.866 71.193 1.00 33.08 ? 786 GLN A NE2 1 ATOM 5757 N N . ALA A 1 787 ? 2.203 35.835 68.156 1.00 21.40 ? 787 ALA A N 1 ATOM 5758 C CA . ALA A 1 787 ? 3.428 36.652 68.099 1.00 21.36 ? 787 ALA A CA 1 ATOM 5759 C C . ALA A 1 787 ? 4.576 36.080 68.924 1.00 19.95 ? 787 ALA A C 1 ATOM 5760 O O . ALA A 1 787 ? 4.407 35.787 70.085 1.00 19.73 ? 787 ALA A O 1 ATOM 5761 C CB . ALA A 1 787 ? 3.131 38.081 68.550 1.00 21.74 ? 787 ALA A CB 1 ATOM 5762 N N . GLY A 1 788 ? 5.743 35.929 68.318 1.00 20.04 ? 788 GLY A N 1 ATOM 5763 C CA . GLY A 1 788 ? 6.931 35.457 69.035 1.00 20.70 ? 788 GLY A CA 1 ATOM 5764 C C . GLY A 1 788 ? 7.139 33.950 69.013 1.00 21.95 ? 788 GLY A C 1 ATOM 5765 O O . GLY A 1 788 ? 8.196 33.459 69.407 1.00 21.66 ? 788 GLY A O 1 ATOM 5766 N N . LYS A 1 789 ? 6.133 33.207 68.559 1.00 23.02 ? 789 LYS A N 1 ATOM 5767 C CA . LYS A 1 789 ? 6.214 31.752 68.506 1.00 24.01 ? 789 LYS A CA 1 ATOM 5768 C C . LYS A 1 789 ? 6.783 31.313 67.157 1.00 22.71 ? 789 LYS A C 1 ATOM 5769 O O . LYS A 1 789 ? 6.710 32.046 66.163 1.00 21.77 ? 789 LYS A O 1 ATOM 5770 C CB . LYS A 1 789 ? 4.828 31.125 68.735 1.00 25.77 ? 789 LYS A CB 1 ATOM 5771 C CG . LYS A 1 789 ? 4.218 31.410 70.106 1.00 27.15 ? 789 LYS A CG 1 ATOM 5772 C CD . LYS A 1 789 ? 4.981 30.716 71.223 1.00 28.35 ? 789 LYS A CD 1 ATOM 5773 C CE . LYS A 1 789 ? 4.259 30.849 72.562 1.00 30.25 ? 789 LYS A CE 1 ATOM 5774 N NZ . LYS A 1 789 ? 4.122 32.272 73.004 1.00 31.18 ? 789 LYS A NZ 1 ATOM 5775 N N . THR A 1 790 ? 7.362 30.123 67.136 1.00 22.14 ? 790 THR A N 1 ATOM 5776 C CA . THR A 1 790 ? 7.964 29.591 65.928 1.00 23.12 ? 790 THR A CA 1 ATOM 5777 C C . THR A 1 790 ? 6.996 28.651 65.215 1.00 22.57 ? 790 THR A C 1 ATOM 5778 O O . THR A 1 790 ? 6.316 27.825 65.848 1.00 22.18 ? 790 THR A O 1 ATOM 5779 C CB . THR A 1 790 ? 9.294 28.853 66.204 1.00 24.23 ? 790 THR A CB 1 ATOM 5780 O OG1 . THR A 1 790 ? 9.034 27.642 66.914 1.00 27.06 ? 790 THR A OG1 1 ATOM 5781 C CG2 . THR A 1 790 ? 10.248 29.724 67.019 1.00 23.86 ? 790 THR A CG2 1 ATOM 5782 N N . TYR A 1 791 ? 6.944 28.798 63.893 1.00 21.49 ? 791 TYR A N 1 ATOM 5783 C CA . TYR A 1 791 ? 6.118 27.967 63.042 1.00 20.92 ? 791 TYR A CA 1 ATOM 5784 C C . TYR A 1 791 ? 6.972 27.337 61.954 1.00 20.93 ? 791 TYR A C 1 ATOM 5785 O O . TYR A 1 791 ? 8.091 27.782 61.696 1.00 20.62 ? 791 TYR A O 1 ATOM 5786 C CB . TYR A 1 791 ? 4.994 28.793 62.429 1.00 20.89 ? 791 TYR A CB 1 ATOM 5787 C CG . TYR A 1 791 ? 3.989 29.271 63.443 1.00 21.30 ? 791 TYR A CG 1 ATOM 5788 C CD1 . TYR A 1 791 ? 4.162 30.489 64.101 1.00 21.14 ? 791 TYR A CD1 1 ATOM 5789 C CD2 . TYR A 1 791 ? 2.865 28.500 63.767 1.00 21.46 ? 791 TYR A CD2 1 ATOM 5790 C CE1 . TYR A 1 791 ? 3.242 30.936 65.038 1.00 21.18 ? 791 TYR A CE1 1 ATOM 5791 C CE2 . TYR A 1 791 ? 1.937 28.944 64.699 1.00 21.22 ? 791 TYR A CE2 1 ATOM 5792 C CZ . TYR A 1 791 ? 2.140 30.158 65.331 1.00 21.33 ? 791 TYR A CZ 1 ATOM 5793 O OH . TYR A 1 791 ? 1.248 30.612 66.253 1.00 22.25 ? 791 TYR A OH 1 ATOM 5794 N N . VAL A 1 792 ? 6.445 26.283 61.340 1.00 20.62 ? 792 VAL A N 1 ATOM 5795 C CA . VAL A 1 792 ? 7.155 25.571 60.291 1.00 21.02 ? 792 VAL A CA 1 ATOM 5796 C C . VAL A 1 792 ? 6.169 25.224 59.199 1.00 21.11 ? 792 VAL A C 1 ATOM 5797 O O . VAL A 1 792 ? 5.197 24.516 59.437 1.00 21.43 ? 792 VAL A O 1 ATOM 5798 C CB . VAL A 1 792 ? 7.796 24.250 60.781 1.00 21.17 ? 792 VAL A CB 1 ATOM 5799 C CG1 . VAL A 1 792 ? 8.597 23.601 59.656 1.00 21.24 ? 792 VAL A CG1 1 ATOM 5800 C CG2 . VAL A 1 792 ? 8.691 24.493 61.978 1.00 21.36 ? 792 VAL A CG2 1 ATOM 5801 N N . ILE A 1 793 ? 6.438 25.731 58.006 1.00 20.75 ? 793 ILE A N 1 ATOM 5802 C CA . ILE A 1 793 ? 5.685 25.393 56.816 1.00 20.42 ? 793 ILE A CA 1 ATOM 5803 C C . ILE A 1 793 ? 6.264 24.102 56.225 1.00 19.81 ? 793 ILE A C 1 ATOM 5804 O O . ILE A 1 793 ? 7.434 24.069 55.816 1.00 20.57 ? 793 ILE A O 1 ATOM 5805 C CB . ILE A 1 793 ? 5.770 26.533 55.792 1.00 20.17 ? 793 ILE A CB 1 ATOM 5806 C CG1 . ILE A 1 793 ? 5.271 27.842 56.422 1.00 21.09 ? 793 ILE A CG1 1 ATOM 5807 C CG2 . ILE A 1 793 ? 4.950 26.201 54.557 1.00 20.57 ? 793 ILE A CG2 1 ATOM 5808 C CD1 . ILE A 1 793 ? 5.550 29.090 55.596 1.00 21.05 ? 793 ILE A CD1 1 ATOM 5809 N N . THR A 1 794 ? 5.478 23.028 56.209 1.00 18.41 ? 794 THR A N 1 ATOM 5810 C CA . THR A 1 794 ? 5.917 21.792 55.553 1.00 17.76 ? 794 THR A CA 1 ATOM 5811 C C . THR A 1 794 ? 5.307 21.726 54.167 1.00 17.55 ? 794 THR A C 1 ATOM 5812 O O . THR A 1 794 ? 4.102 21.915 54.011 1.00 18.25 ? 794 THR A O 1 ATOM 5813 C CB . THR A 1 794 ? 5.560 20.539 56.373 1.00 17.83 ? 794 THR A CB 1 ATOM 5814 O OG1 . THR A 1 794 ? 6.331 20.535 57.579 1.00 17.34 ? 794 THR A OG1 1 ATOM 5815 C CG2 . THR A 1 794 ? 5.869 19.260 55.595 1.00 17.84 ? 794 THR A CG2 1 ATOM 5816 N N . VAL A 1 795 ? 6.146 21.480 53.162 1.00 17.31 ? 795 VAL A N 1 ATOM 5817 C CA . VAL A 1 795 ? 5.723 21.444 51.749 1.00 16.81 ? 795 VAL A CA 1 ATOM 5818 C C . VAL A 1 795 ? 6.161 20.112 51.124 1.00 16.56 ? 795 VAL A C 1 ATOM 5819 O O . VAL A 1 795 ? 7.329 19.740 51.220 1.00 16.46 ? 795 VAL A O 1 ATOM 5820 C CB . VAL A 1 795 ? 6.330 22.618 50.950 1.00 16.37 ? 795 VAL A CB 1 ATOM 5821 C CG1 . VAL A 1 795 ? 5.886 22.575 49.504 1.00 16.32 ? 795 VAL A CG1 1 ATOM 5822 C CG2 . VAL A 1 795 ? 5.974 23.959 51.585 1.00 16.60 ? 795 VAL A CG2 1 ATOM 5823 N N . VAL A 1 796 ? 5.218 19.389 50.519 1.00 16.83 ? 796 VAL A N 1 ATOM 5824 C CA . VAL A 1 796 ? 5.507 18.109 49.855 1.00 16.40 ? 796 VAL A CA 1 ATOM 5825 C C . VAL A 1 796 ? 5.252 18.263 48.352 1.00 16.78 ? 796 VAL A C 1 ATOM 5826 O O . VAL A 1 796 ? 4.179 18.730 47.945 1.00 16.52 ? 796 VAL A O 1 ATOM 5827 C CB . VAL A 1 796 ? 4.640 16.971 50.412 1.00 16.39 ? 796 VAL A CB 1 ATOM 5828 C CG1 . VAL A 1 796 ? 4.973 15.641 49.748 1.00 16.31 ? 796 VAL A CG1 1 ATOM 5829 C CG2 . VAL A 1 796 ? 4.843 16.839 51.908 1.00 17.02 ? 796 VAL A CG2 1 ATOM 5830 N N . ILE A 1 797 ? 6.236 17.880 47.533 1.00 16.77 ? 797 ILE A N 1 ATOM 5831 C CA . ILE A 1 797 ? 6.183 18.104 46.076 1.00 17.14 ? 797 ILE A CA 1 ATOM 5832 C C . ILE A 1 797 ? 6.519 16.824 45.301 1.00 17.54 ? 797 ILE A C 1 ATOM 5833 O O . ILE A 1 797 ? 7.580 16.224 45.489 1.00 17.46 ? 797 ILE A O 1 ATOM 5834 C CB . ILE A 1 797 ? 7.172 19.207 45.630 1.00 17.17 ? 797 ILE A CB 1 ATOM 5835 C CG1 . ILE A 1 797 ? 6.946 20.520 46.401 1.00 17.13 ? 797 ILE A CG1 1 ATOM 5836 C CG2 . ILE A 1 797 ? 7.072 19.447 44.120 1.00 17.38 ? 797 ILE A CG2 1 ATOM 5837 C CD1 . ILE A 1 797 ? 8.084 21.519 46.273 1.00 16.65 ? 797 ILE A CD1 1 ATOM 5838 N N . ASP A 1 798 ? 5.619 16.426 44.410 1.00 18.41 ? 798 ASP A N 1 ATOM 5839 C CA . ASP A 1 798 ? 5.842 15.276 43.542 1.00 18.87 ? 798 ASP A CA 1 ATOM 5840 C C . ASP A 1 798 ? 6.825 15.677 42.444 1.00 19.23 ? 798 ASP A C 1 ATOM 5841 O O . ASP A 1 798 ? 6.517 16.545 41.630 1.00 19.84 ? 798 ASP A O 1 ATOM 5842 C CB . ASP A 1 798 ? 4.515 14.844 42.937 1.00 19.55 ? 798 ASP A CB 1 ATOM 5843 C CG . ASP A 1 798 ? 4.489 13.384 42.535 1.00 20.13 ? 798 ASP A CG 1 ATOM 5844 O OD1 . ASP A 1 798 ? 5.569 12.748 42.422 1.00 20.28 ? 798 ASP A OD1 1 ATOM 5845 O OD2 . ASP A 1 798 ? 3.359 12.887 42.312 1.00 20.55 -1 798 ASP A OD2 1 ATOM 5846 N N . ASN A 1 799 ? 8.029 15.104 42.464 1.00 18.95 ? 799 ASN A N 1 ATOM 5847 C CA . ASN A 1 799 ? 8.993 15.291 41.377 1.00 18.76 ? 799 ASN A CA 1 ATOM 5848 C C . ASN A 1 799 ? 8.720 14.193 40.360 1.00 17.98 ? 799 ASN A C 1 ATOM 5849 O O . ASN A 1 799 ? 8.915 13.022 40.643 1.00 17.27 ? 799 ASN A O 1 ATOM 5850 C CB . ASN A 1 799 ? 10.441 15.190 41.873 1.00 19.08 ? 799 ASN A CB 1 ATOM 5851 C CG . ASN A 1 799 ? 11.474 15.270 40.750 1.00 19.42 ? 799 ASN A CG 1 ATOM 5852 O OD1 . ASN A 1 799 ? 11.154 15.477 39.576 1.00 19.55 ? 799 ASN A OD1 1 ATOM 5853 N ND2 . ASN A 1 799 ? 12.731 15.116 41.118 1.00 20.97 ? 799 ASN A ND2 1 ATOM 5854 N N . MET A 1 800 ? 8.303 14.588 39.170 1.00 16.95 ? 800 MET A N 1 ATOM 5855 C CA . MET A 1 800 ? 7.880 13.637 38.163 1.00 17.25 ? 800 MET A CA 1 ATOM 5856 C C . MET A 1 800 ? 9.055 13.154 37.296 1.00 17.25 ? 800 MET A C 1 ATOM 5857 O O . MET A 1 800 ? 8.843 12.458 36.304 1.00 18.07 ? 800 MET A O 1 ATOM 5858 C CB . MET A 1 800 ? 6.800 14.281 37.279 1.00 17.41 ? 800 MET A CB 1 ATOM 5859 C CG . MET A 1 800 ? 5.692 14.980 38.052 1.00 17.75 ? 800 MET A CG 1 ATOM 5860 S SD . MET A 1 800 ? 4.777 13.900 39.162 1.00 17.93 ? 800 MET A SD 1 ATOM 5861 C CE . MET A 1 800 ? 3.897 12.902 37.961 1.00 18.41 ? 800 MET A CE 1 ATOM 5862 N N . GLY A 1 801 ? 10.282 13.507 37.679 1.00 16.99 ? 801 GLY A N 1 ATOM 5863 C CA . GLY A 1 801 ? 11.464 13.280 36.851 1.00 16.77 ? 801 GLY A CA 1 ATOM 5864 C C . GLY A 1 801 ? 12.022 14.566 36.265 1.00 16.31 ? 801 GLY A C 1 ATOM 5865 O O . GLY A 1 801 ? 11.328 15.583 36.188 1.00 16.14 ? 801 GLY A O 1 ATOM 5866 N N . LEU A 1 802 ? 13.281 14.511 35.845 1.00 16.34 ? 802 LEU A N 1 ATOM 5867 C CA . LEU A 1 802 ? 13.952 15.648 35.212 1.00 16.32 ? 802 LEU A CA 1 ATOM 5868 C C . LEU A 1 802 ? 13.654 15.674 33.718 1.00 15.81 ? 802 LEU A C 1 ATOM 5869 O O . LEU A 1 802 ? 13.485 14.629 33.089 1.00 14.97 ? 802 LEU A O 1 ATOM 5870 C CB . LEU A 1 802 ? 15.476 15.577 35.428 1.00 16.53 ? 802 LEU A CB 1 ATOM 5871 C CG . LEU A 1 802 ? 15.942 15.369 36.868 1.00 16.70 ? 802 LEU A CG 1 ATOM 5872 C CD1 . LEU A 1 802 ? 17.455 15.394 36.953 1.00 17.00 ? 802 LEU A CD1 1 ATOM 5873 C CD2 . LEU A 1 802 ? 15.362 16.414 37.792 1.00 16.72 ? 802 LEU A CD2 1 ATOM 5874 N N . GLU A 1 803 ? 13.638 16.878 33.156 1.00 16.13 ? 803 GLU A N 1 ATOM 5875 C CA . GLU A 1 803 ? 13.285 17.087 31.770 1.00 16.68 ? 803 GLU A CA 1 ATOM 5876 C C . GLU A 1 803 ? 14.375 16.562 30.829 1.00 17.54 ? 803 GLU A C 1 ATOM 5877 O O . GLU A 1 803 ? 15.533 16.388 31.206 1.00 17.41 ? 803 GLU A O 1 ATOM 5878 C CB . GLU A 1 803 ? 13.103 18.577 31.471 1.00 17.09 ? 803 GLU A CB 1 ATOM 5879 C CG . GLU A 1 803 ? 12.160 19.350 32.378 1.00 17.39 ? 803 GLU A CG 1 ATOM 5880 C CD . GLU A 1 803 ? 10.686 19.119 32.087 1.00 17.70 ? 803 GLU A CD 1 ATOM 5881 O OE1 . GLU A 1 803 ? 10.360 18.745 30.947 1.00 17.81 ? 803 GLU A OE1 1 ATOM 5882 O OE2 . GLU A 1 803 ? 9.848 19.335 33.003 1.00 17.90 -1 803 GLU A OE2 1 ATOM 5883 N N . GLU A 1 804 ? 13.987 16.353 29.583 1.00 18.76 ? 804 GLU A N 1 ATOM 5884 C CA . GLU A 1 804 ? 14.917 16.008 28.516 1.00 19.80 ? 804 GLU A CA 1 ATOM 5885 C C . GLU A 1 804 ? 15.752 17.225 28.075 1.00 19.46 ? 804 GLU A C 1 ATOM 5886 O O . GLU A 1 804 ? 15.573 18.337 28.592 1.00 20.74 ? 804 GLU A O 1 ATOM 5887 C CB . GLU A 1 804 ? 14.125 15.357 27.367 1.00 20.40 ? 804 GLU A CB 1 ATOM 5888 C CG . GLU A 1 804 ? 13.657 13.965 27.789 1.00 21.73 ? 804 GLU A CG 1 ATOM 5889 C CD . GLU A 1 804 ? 12.763 13.253 26.790 1.00 22.44 ? 804 GLU A CD 1 ATOM 5890 O OE1 . GLU A 1 804 ? 11.857 13.891 26.215 1.00 23.66 ? 804 GLU A OE1 1 ATOM 5891 O OE2 . GLU A 1 804 ? 12.953 12.030 26.613 1.00 22.08 -1 804 GLU A OE2 1 ATOM 5892 N N . ASN A 1 805 ? 16.690 17.004 27.159 1.00 19.25 ? 805 ASN A N 1 ATOM 5893 C CA . ASN A 1 805 ? 17.586 18.057 26.671 1.00 18.89 ? 805 ASN A CA 1 ATOM 5894 C C . ASN A 1 805 ? 17.769 17.887 25.175 1.00 19.47 ? 805 ASN A C 1 ATOM 5895 O O . ASN A 1 805 ? 18.896 17.766 24.686 1.00 19.21 ? 805 ASN A O 1 ATOM 5896 C CB . ASN A 1 805 ? 18.940 17.994 27.405 1.00 18.56 ? 805 ASN A CB 1 ATOM 5897 C CG . ASN A 1 805 ? 19.719 19.311 27.345 1.00 17.97 ? 805 ASN A CG 1 ATOM 5898 O OD1 . ASN A 1 805 ? 20.229 19.712 26.296 1.00 17.71 ? 805 ASN A OD1 1 ATOM 5899 N ND2 . ASN A 1 805 ? 19.850 19.961 28.482 1.00 17.24 ? 805 ASN A ND2 1 ATOM 5900 N N . TRP A 1 806 ? 16.652 17.869 24.453 1.00 20.56 ? 806 TRP A N 1 ATOM 5901 C CA . TRP A 1 806 ? 16.650 17.525 23.027 1.00 21.84 ? 806 TRP A CA 1 ATOM 5902 C C . TRP A 1 806 ? 17.396 18.545 22.161 1.00 21.51 ? 806 TRP A C 1 ATOM 5903 O O . TRP A 1 806 ? 18.148 18.169 21.272 1.00 21.43 ? 806 TRP A O 1 ATOM 5904 C CB . TRP A 1 806 ? 15.210 17.331 22.516 1.00 23.14 ? 806 TRP A CB 1 ATOM 5905 C CG . TRP A 1 806 ? 15.116 16.599 21.182 1.00 25.02 ? 806 TRP A CG 1 ATOM 5906 C CD1 . TRP A 1 806 ? 15.127 15.246 20.982 1.00 26.39 ? 806 TRP A CD1 1 ATOM 5907 C CD2 . TRP A 1 806 ? 14.991 17.192 19.878 1.00 25.68 ? 806 TRP A CD2 1 ATOM 5908 N NE1 . TRP A 1 806 ? 15.024 14.960 19.633 1.00 26.80 ? 806 TRP A NE1 1 ATOM 5909 C CE2 . TRP A 1 806 ? 14.944 16.137 18.938 1.00 26.02 ? 806 TRP A CE2 1 ATOM 5910 C CE3 . TRP A 1 806 ? 14.926 18.513 19.413 1.00 26.42 ? 806 TRP A CE3 1 ATOM 5911 C CZ2 . TRP A 1 806 ? 14.832 16.363 17.561 1.00 26.85 ? 806 TRP A CZ2 1 ATOM 5912 C CZ3 . TRP A 1 806 ? 14.816 18.736 18.037 1.00 26.85 ? 806 TRP A CZ3 1 ATOM 5913 C CH2 . TRP A 1 806 ? 14.774 17.664 17.132 1.00 26.59 ? 806 TRP A CH2 1 ATOM 5914 N N . THR A 1 807 ? 17.181 19.827 22.414 1.00 22.07 ? 807 THR A N 1 ATOM 5915 C CA . THR A 1 807 ? 17.829 20.884 21.644 1.00 23.07 ? 807 THR A CA 1 ATOM 5916 C C . THR A 1 807 ? 19.114 21.293 22.341 1.00 23.12 ? 807 THR A C 1 ATOM 5917 O O . THR A 1 807 ? 19.082 21.768 23.473 1.00 24.60 ? 807 THR A O 1 ATOM 5918 C CB . THR A 1 807 ? 16.910 22.115 21.486 1.00 23.76 ? 807 THR A CB 1 ATOM 5919 O OG1 . THR A 1 807 ? 15.801 21.780 20.647 1.00 25.22 ? 807 THR A OG1 1 ATOM 5920 C CG2 . THR A 1 807 ? 17.651 23.283 20.861 1.00 23.90 ? 807 THR A CG2 1 ATOM 5921 N N . VAL A 1 808 ? 20.243 21.108 21.662 1.00 23.72 ? 808 VAL A N 1 ATOM 5922 C CA . VAL A 1 808 ? 21.556 21.471 22.214 1.00 23.37 ? 808 VAL A CA 1 ATOM 5923 C C . VAL A 1 808 ? 21.624 22.982 22.343 1.00 23.56 ? 808 VAL A C 1 ATOM 5924 O O . VAL A 1 808 ? 21.202 23.721 21.449 1.00 23.35 ? 808 VAL A O 1 ATOM 5925 C CB . VAL A 1 808 ? 22.712 20.976 21.311 1.00 23.83 ? 808 VAL A CB 1 ATOM 5926 C CG1 . VAL A 1 808 ? 24.061 21.388 21.882 1.00 24.18 ? 808 VAL A CG1 1 ATOM 5927 C CG2 . VAL A 1 808 ? 22.648 19.465 21.143 1.00 23.95 ? 808 VAL A CG2 1 ATOM 5928 N N . GLY A 1 809 ? 22.139 23.440 23.471 1.00 24.97 ? 809 GLY A N 1 ATOM 5929 C CA . GLY A 1 809 ? 22.170 24.864 23.774 1.00 24.60 ? 809 GLY A CA 1 ATOM 5930 C C . GLY A 1 809 ? 21.101 25.271 24.765 1.00 24.52 ? 809 GLY A C 1 ATOM 5931 O O . GLY A 1 809 ? 21.338 26.144 25.582 1.00 24.34 ? 809 GLY A O 1 ATOM 5932 N N . GLU A 1 810 ? 19.928 24.639 24.716 1.00 24.68 ? 810 GLU A N 1 ATOM 5933 C CA . GLU A 1 810 ? 18.801 25.099 25.540 1.00 25.00 ? 810 GLU A CA 1 ATOM 5934 C C . GLU A 1 810 ? 18.904 24.689 27.018 1.00 23.84 ? 810 GLU A C 1 ATOM 5935 O O . GLU A 1 810 ? 18.272 25.317 27.881 1.00 22.68 ? 810 GLU A O 1 ATOM 5936 C CB . GLU A 1 810 ? 17.458 24.658 24.947 1.00 26.19 ? 810 GLU A CB 1 ATOM 5937 C CG . GLU A 1 810 ? 16.465 25.807 24.879 1.00 27.66 ? 810 GLU A CG 1 ATOM 5938 C CD . GLU A 1 810 ? 15.048 25.372 24.591 1.00 29.51 ? 810 GLU A CD 1 ATOM 5939 O OE1 . GLU A 1 810 ? 14.860 24.247 24.077 1.00 30.45 ? 810 GLU A OE1 1 ATOM 5940 O OE2 . GLU A 1 810 ? 14.118 26.170 24.881 1.00 31.54 -1 810 GLU A OE2 1 ATOM 5941 N N . ASP A 1 811 ? 19.699 23.648 27.300 1.00 22.58 ? 811 ASP A N 1 ATOM 5942 C CA . ASP A 1 811 ? 19.952 23.185 28.666 1.00 21.67 ? 811 ASP A CA 1 ATOM 5943 C C . ASP A 1 811 ? 18.666 22.887 29.459 1.00 20.92 ? 811 ASP A C 1 ATOM 5944 O O . ASP A 1 811 ? 18.637 23.057 30.674 1.00 21.80 ? 811 ASP A O 1 ATOM 5945 C CB . ASP A 1 811 ? 20.830 24.204 29.434 1.00 22.13 ? 811 ASP A CB 1 ATOM 5946 C CG . ASP A 1 811 ? 22.340 23.995 29.224 1.00 22.88 ? 811 ASP A CG 1 ATOM 5947 O OD1 . ASP A 1 811 ? 22.739 23.067 28.484 1.00 21.56 ? 811 ASP A OD1 1 ATOM 5948 O OD2 . ASP A 1 811 ? 23.136 24.771 29.822 1.00 23.74 -1 811 ASP A OD2 1 ATOM 5949 N N . LEU A 1 812 ? 17.615 22.415 28.795 1.00 20.48 ? 812 LEU A N 1 ATOM 5950 C CA . LEU A 1 812 ? 16.317 22.228 29.461 1.00 20.42 ? 812 LEU A CA 1 ATOM 5951 C C . LEU A 1 812 ? 16.282 21.153 30.560 1.00 19.84 ? 812 LEU A C 1 ATOM 5952 O O . LEU A 1 812 ? 15.361 21.128 31.372 1.00 20.11 ? 812 LEU A O 1 ATOM 5953 C CB . LEU A 1 812 ? 15.211 21.936 28.438 1.00 21.17 ? 812 LEU A CB 1 ATOM 5954 C CG . LEU A 1 812 ? 14.656 23.102 27.610 1.00 21.30 ? 812 LEU A CG 1 ATOM 5955 C CD1 . LEU A 1 812 ? 13.431 22.638 26.840 1.00 20.72 ? 812 LEU A CD1 1 ATOM 5956 C CD2 . LEU A 1 812 ? 14.315 24.310 28.477 1.00 21.47 ? 812 LEU A CD2 1 ATOM 5957 N N . MET A 1 813 ? 17.263 20.263 30.562 1.00 19.18 ? 813 MET A N 1 ATOM 5958 C CA . MET A 1 813 ? 17.424 19.252 31.596 1.00 19.37 ? 813 MET A CA 1 ATOM 5959 C C . MET A 1 813 ? 17.756 19.872 32.948 1.00 19.50 ? 813 MET A C 1 ATOM 5960 O O . MET A 1 813 ? 17.507 19.263 33.998 1.00 18.54 ? 813 MET A O 1 ATOM 5961 C CB . MET A 1 813 ? 18.513 18.252 31.171 1.00 19.95 ? 813 MET A CB 1 ATOM 5962 C CG . MET A 1 813 ? 18.889 17.186 32.189 1.00 19.43 ? 813 MET A CG 1 ATOM 5963 S SD . MET A 1 813 ? 20.270 17.716 33.200 1.00 19.44 ? 813 MET A SD 1 ATOM 5964 C CE . MET A 1 813 ? 19.961 16.784 34.700 1.00 18.76 ? 813 MET A CE 1 ATOM 5965 N N . LYS A 1 814 ? 18.318 21.084 32.919 1.00 20.02 ? 814 LYS A N 1 ATOM 5966 C CA . LYS A 1 814 ? 18.542 21.864 34.132 1.00 19.71 ? 814 LYS A CA 1 ATOM 5967 C C . LYS A 1 814 ? 17.263 22.472 34.729 1.00 19.07 ? 814 LYS A C 1 ATOM 5968 O O . LYS A 1 814 ? 17.322 23.077 35.791 1.00 19.53 ? 814 LYS A O 1 ATOM 5969 C CB . LYS A 1 814 ? 19.565 22.969 33.873 1.00 20.35 ? 814 LYS A CB 1 ATOM 5970 C CG . LYS A 1 814 ? 20.944 22.434 33.551 1.00 20.16 ? 814 LYS A CG 1 ATOM 5971 C CD . LYS A 1 814 ? 21.953 23.531 33.282 1.00 20.13 ? 814 LYS A CD 1 ATOM 5972 C CE . LYS A 1 814 ? 23.308 22.905 33.015 1.00 20.98 ? 814 LYS A CE 1 ATOM 5973 N NZ . LYS A 1 814 ? 24.352 23.876 32.597 1.00 21.92 ? 814 LYS A NZ 1 ATOM 5974 N N . THR A 1 815 ? 16.112 22.316 34.082 1.00 18.15 ? 815 THR A N 1 ATOM 5975 C CA . THR A 1 815 ? 14.875 22.807 34.688 1.00 17.67 ? 815 THR A CA 1 ATOM 5976 C C . THR A 1 815 ? 14.816 22.297 36.133 1.00 17.50 ? 815 THR A C 1 ATOM 5977 O O . THR A 1 815 ? 14.757 21.089 36.372 1.00 17.77 ? 815 THR A O 1 ATOM 5978 C CB . THR A 1 815 ? 13.622 22.390 33.896 1.00 17.30 ? 815 THR A CB 1 ATOM 5979 O OG1 . THR A 1 815 ? 13.772 22.797 32.535 1.00 17.62 ? 815 THR A OG1 1 ATOM 5980 C CG2 . THR A 1 815 ? 12.347 23.039 34.464 1.00 16.97 ? 815 THR A CG2 1 ATOM 5981 N N . PRO A 1 816 ? 14.849 23.220 37.108 1.00 17.30 ? 816 PRO A N 1 ATOM 5982 C CA . PRO A 1 816 ? 14.882 22.785 38.492 1.00 16.90 ? 816 PRO A CA 1 ATOM 5983 C C . PRO A 1 816 ? 13.550 22.262 39.016 1.00 16.93 ? 816 PRO A C 1 ATOM 5984 O O . PRO A 1 816 ? 12.501 22.403 38.374 1.00 15.72 ? 816 PRO A O 1 ATOM 5985 C CB . PRO A 1 816 ? 15.269 24.062 39.245 1.00 17.05 ? 816 PRO A CB 1 ATOM 5986 C CG . PRO A 1 816 ? 14.701 25.150 38.415 1.00 17.15 ? 816 PRO A CG 1 ATOM 5987 C CD . PRO A 1 816 ? 14.800 24.689 36.993 1.00 17.08 ? 816 PRO A CD 1 ATOM 5988 N N . ARG A 1 817 ? 13.640 21.690 40.215 1.00 17.66 ? 817 ARG A N 1 ATOM 5989 C CA . ARG A 1 817 ? 12.544 21.090 40.930 1.00 18.12 ? 817 ARG A CA 1 ATOM 5990 C C . ARG A 1 817 ? 12.585 21.640 42.350 1.00 18.41 ? 817 ARG A C 1 ATOM 5991 O O . ARG A 1 817 ? 13.667 21.786 42.913 1.00 19.23 ? 817 ARG A O 1 ATOM 5992 C CB . ARG A 1 817 ? 12.744 19.578 40.956 1.00 18.98 ? 817 ARG A CB 1 ATOM 5993 C CG . ARG A 1 817 ? 12.779 18.925 39.574 1.00 19.56 ? 817 ARG A CG 1 ATOM 5994 C CD . ARG A 1 817 ? 11.355 18.782 39.083 1.00 20.09 ? 817 ARG A CD 1 ATOM 5995 N NE . ARG A 1 817 ? 11.208 18.305 37.708 1.00 20.50 ? 817 ARG A NE 1 ATOM 5996 C CZ . ARG A 1 817 ? 10.979 19.077 36.649 1.00 20.31 ? 817 ARG A CZ 1 ATOM 5997 N NH1 . ARG A 1 817 ? 10.943 20.403 36.770 1.00 20.70 ? 817 ARG A NH1 1 ATOM 5998 N NH2 . ARG A 1 817 ? 10.809 18.514 35.453 1.00 19.51 ? 817 ARG A NH2 1 ATOM 5999 N N . GLY A 1 818 ? 11.416 21.923 42.930 1.00 17.45 ? 818 GLY A N 1 ATOM 6000 C CA . GLY A 1 818 ? 11.314 22.426 44.292 1.00 16.79 ? 818 GLY A CA 1 ATOM 6001 C C . GLY A 1 818 ? 10.511 23.710 44.354 1.00 16.76 ? 818 GLY A C 1 ATOM 6002 O O . GLY A 1 818 ? 9.442 23.815 43.764 1.00 16.62 ? 818 GLY A O 1 ATOM 6003 N N . ILE A 1 819 ? 11.042 24.702 45.052 1.00 17.32 ? 819 ILE A N 1 ATOM 6004 C CA . ILE A 1 819 ? 10.333 25.960 45.275 1.00 17.38 ? 819 ILE A CA 1 ATOM 6005 C C . ILE A 1 819 ? 11.067 27.063 44.525 1.00 17.91 ? 819 ILE A C 1 ATOM 6006 O O . ILE A 1 819 ? 12.263 27.277 44.722 1.00 17.56 ? 819 ILE A O 1 ATOM 6007 C CB . ILE A 1 819 ? 10.209 26.270 46.782 1.00 17.04 ? 819 ILE A CB 1 ATOM 6008 C CG1 . ILE A 1 819 ? 9.549 25.091 47.527 1.00 16.53 ? 819 ILE A CG1 1 ATOM 6009 C CG2 . ILE A 1 819 ? 9.386 27.530 47.004 1.00 17.46 ? 819 ILE A CG2 1 ATOM 6010 C CD1 . ILE A 1 819 ? 9.521 25.199 49.042 1.00 16.12 ? 819 ILE A CD1 1 ATOM 6011 N N . LEU A 1 820 ? 10.346 27.762 43.659 1.00 19.14 ? 820 LEU A N 1 ATOM 6012 C CA . LEU A 1 820 ? 10.943 28.799 42.811 1.00 20.18 ? 820 LEU A CA 1 ATOM 6013 C C . LEU A 1 820 ? 10.745 30.216 43.356 1.00 20.14 ? 820 LEU A C 1 ATOM 6014 O O . LEU A 1 820 ? 11.581 31.091 43.143 1.00 19.37 ? 820 LEU A O 1 ATOM 6015 C CB . LEU A 1 820 ? 10.342 28.721 41.414 1.00 20.83 ? 820 LEU A CB 1 ATOM 6016 C CG . LEU A 1 820 ? 10.429 27.355 40.744 1.00 21.39 ? 820 LEU A CG 1 ATOM 6017 C CD1 . LEU A 1 820 ? 9.628 27.387 39.455 1.00 22.26 ? 820 LEU A CD1 1 ATOM 6018 C CD2 . LEU A 1 820 ? 11.877 26.982 40.483 1.00 21.51 ? 820 LEU A CD2 1 ATOM 6019 N N . ASN A 1 821 ? 9.629 30.435 44.034 1.00 20.85 ? 821 ASN A N 1 ATOM 6020 C CA . ASN A 1 821 ? 9.268 31.749 44.588 1.00 21.12 ? 821 ASN A CA 1 ATOM 6021 C C . ASN A 1 821 ? 8.410 31.522 45.806 1.00 20.77 ? 821 ASN A C 1 ATOM 6022 O O . ASN A 1 821 ? 7.678 30.528 45.877 1.00 20.07 ? 821 ASN A O 1 ATOM 6023 C CB . ASN A 1 821 ? 8.438 32.577 43.592 1.00 21.62 ? 821 ASN A CB 1 ATOM 6024 C CG . ASN A 1 821 ? 9.265 33.157 42.467 1.00 22.74 ? 821 ASN A CG 1 ATOM 6025 O OD1 . ASN A 1 821 ? 10.219 33.885 42.712 1.00 24.97 ? 821 ASN A OD1 1 ATOM 6026 N ND2 . ASN A 1 821 ? 8.909 32.839 41.222 1.00 23.46 ? 821 ASN A ND2 1 ATOM 6027 N N . PHE A 1 822 ? 8.492 32.441 46.763 1.00 21.00 ? 822 PHE A N 1 ATOM 6028 C CA . PHE A 1 822 ? 7.514 32.492 47.842 1.00 21.50 ? 822 PHE A CA 1 ATOM 6029 C C . PHE A 1 822 ? 7.399 33.915 48.404 1.00 22.37 ? 822 PHE A C 1 ATOM 6030 O O . PHE A 1 822 ? 8.321 34.713 48.277 1.00 22.78 ? 822 PHE A O 1 ATOM 6031 C CB . PHE A 1 822 ? 7.856 31.476 48.948 1.00 20.83 ? 822 PHE A CB 1 ATOM 6032 C CG . PHE A 1 822 ? 9.129 31.782 49.679 1.00 20.89 ? 822 PHE A CG 1 ATOM 6033 C CD1 . PHE A 1 822 ? 10.353 31.340 49.187 1.00 20.03 ? 822 PHE A CD1 1 ATOM 6034 C CD2 . PHE A 1 822 ? 9.108 32.542 50.847 1.00 20.21 ? 822 PHE A CD2 1 ATOM 6035 C CE1 . PHE A 1 822 ? 11.523 31.638 49.859 1.00 20.18 ? 822 PHE A CE1 1 ATOM 6036 C CE2 . PHE A 1 822 ? 10.274 32.838 51.520 1.00 19.88 ? 822 PHE A CE2 1 ATOM 6037 C CZ . PHE A 1 822 ? 11.484 32.386 51.029 1.00 19.90 ? 822 PHE A CZ 1 ATOM 6038 N N . LEU A 1 823 ? 6.249 34.213 49.007 1.00 23.02 ? 823 LEU A N 1 ATOM 6039 C CA . LEU A 1 823 ? 5.983 35.491 49.641 1.00 23.52 ? 823 LEU A CA 1 ATOM 6040 C C . LEU A 1 823 ? 5.208 35.237 50.916 1.00 23.98 ? 823 LEU A C 1 ATOM 6041 O O . LEU A 1 823 ? 4.135 34.626 50.879 1.00 25.74 ? 823 LEU A O 1 ATOM 6042 C CB . LEU A 1 823 ? 5.156 36.393 48.724 1.00 24.00 ? 823 LEU A CB 1 ATOM 6043 C CG . LEU A 1 823 ? 4.872 37.797 49.269 1.00 24.60 ? 823 LEU A CG 1 ATOM 6044 C CD1 . LEU A 1 823 ? 6.183 38.550 49.415 1.00 24.39 ? 823 LEU A CD1 1 ATOM 6045 C CD2 . LEU A 1 823 ? 3.904 38.570 48.385 1.00 24.54 ? 823 LEU A CD2 1 ATOM 6046 N N . LEU A 1 824 ? 5.762 35.671 52.042 1.00 23.09 ? 824 LEU A N 1 ATOM 6047 C CA . LEU A 1 824 ? 5.032 35.699 53.293 1.00 22.69 ? 824 LEU A CA 1 ATOM 6048 C C . LEU A 1 824 ? 4.659 37.168 53.453 1.00 22.42 ? 824 LEU A C 1 ATOM 6049 O O . LEU A 1 824 ? 5.497 37.988 53.808 1.00 21.35 ? 824 LEU A O 1 ATOM 6050 C CB . LEU A 1 824 ? 5.915 35.190 54.429 1.00 22.86 ? 824 LEU A CB 1 ATOM 6051 C CG . LEU A 1 824 ? 5.297 35.091 55.821 1.00 23.18 ? 824 LEU A CG 1 ATOM 6052 C CD1 . LEU A 1 824 ? 4.105 34.139 55.862 1.00 23.40 ? 824 LEU A CD1 1 ATOM 6053 C CD2 . LEU A 1 824 ? 6.354 34.651 56.818 1.00 23.42 ? 824 LEU A CD2 1 ATOM 6054 N N . ALA A 1 825 ? 3.407 37.496 53.134 1.00 22.56 ? 825 ALA A N 1 ATOM 6055 C CA . ALA A 1 825 ? 2.992 38.889 52.907 1.00 23.13 ? 825 ALA A CA 1 ATOM 6056 C C . ALA A 1 825 ? 3.323 39.785 54.096 1.00 23.23 ? 825 ALA A C 1 ATOM 6057 O O . ALA A 1 825 ? 3.079 39.404 55.236 1.00 22.92 ? 825 ALA A O 1 ATOM 6058 C CB . ALA A 1 825 ? 1.498 38.956 52.592 1.00 23.29 ? 825 ALA A CB 1 ATOM 6059 N N . GLY A 1 826 ? 3.900 40.957 53.826 1.00 23.65 ? 826 GLY A N 1 ATOM 6060 C CA . GLY A 1 826 ? 4.274 41.898 54.889 1.00 24.01 ? 826 GLY A CA 1 ATOM 6061 C C . GLY A 1 826 ? 5.653 41.647 55.491 1.00 25.20 ? 826 GLY A C 1 ATOM 6062 O O . GLY A 1 826 ? 6.164 42.488 56.241 1.00 26.21 ? 826 GLY A O 1 ATOM 6063 N N . ARG A 1 827 ? 6.263 40.503 55.161 1.00 24.40 ? 827 ARG A N 1 ATOM 6064 C CA . ARG A 1 827 ? 7.558 40.112 55.714 1.00 23.46 ? 827 ARG A CA 1 ATOM 6065 C C . ARG A 1 827 ? 8.594 39.917 54.606 1.00 23.46 ? 827 ARG A C 1 ATOM 6066 O O . ARG A 1 827 ? 8.295 39.313 53.570 1.00 23.29 ? 827 ARG A O 1 ATOM 6067 C CB . ARG A 1 827 ? 7.452 38.790 56.483 1.00 23.00 ? 827 ARG A CB 1 ATOM 6068 C CG . ARG A 1 827 ? 6.497 38.752 57.669 1.00 22.40 ? 827 ARG A CG 1 ATOM 6069 C CD . ARG A 1 827 ? 7.087 39.298 58.957 1.00 21.72 ? 827 ARG A CD 1 ATOM 6070 N NE . ARG A 1 827 ? 8.337 38.677 59.425 1.00 21.58 ? 827 ARG A NE 1 ATOM 6071 C CZ . ARG A 1 827 ? 8.446 37.582 60.187 1.00 20.91 ? 827 ARG A CZ 1 ATOM 6072 N NH1 . ARG A 1 827 ? 7.377 36.871 60.555 1.00 21.32 ? 827 ARG A NH1 1 ATOM 6073 N NH2 . ARG A 1 827 ? 9.652 37.174 60.571 1.00 19.83 ? 827 ARG A NH2 1 ATOM 6074 N N . PRO A 1 828 ? 9.835 40.372 54.842 1.00 22.93 ? 828 PRO A N 1 ATOM 6075 C CA . PRO A 1 828 ? 10.902 39.991 53.921 1.00 22.59 ? 828 PRO A CA 1 ATOM 6076 C C . PRO A 1 828 ? 11.043 38.478 53.856 1.00 22.68 ? 828 PRO A C 1 ATOM 6077 O O . PRO A 1 828 ? 10.751 37.784 54.840 1.00 22.07 ? 828 PRO A O 1 ATOM 6078 C CB . PRO A 1 828 ? 12.148 40.597 54.559 1.00 22.78 ? 828 PRO A CB 1 ATOM 6079 C CG . PRO A 1 828 ? 11.831 40.639 56.014 1.00 22.81 ? 828 PRO A CG 1 ATOM 6080 C CD . PRO A 1 828 ? 10.367 40.953 56.088 1.00 22.87 ? 828 PRO A CD 1 ATOM 6081 N N . SER A 1 829 ? 11.509 37.981 52.718 1.00 22.73 ? 829 SER A N 1 ATOM 6082 C CA . SER A 1 829 ? 11.578 36.539 52.477 1.00 23.39 ? 829 SER A CA 1 ATOM 6083 C C . SER A 1 829 ? 12.644 35.835 53.315 1.00 22.69 ? 829 SER A C 1 ATOM 6084 O O . SER A 1 829 ? 12.528 34.622 53.568 1.00 22.51 ? 829 SER A O 1 ATOM 6085 C CB . SER A 1 829 ? 11.776 36.251 50.986 1.00 24.04 ? 829 SER A CB 1 ATOM 6086 O OG . SER A 1 829 ? 10.634 36.667 50.260 1.00 25.45 ? 829 SER A OG 1 ATOM 6087 N N . SER A 1 830 ? 13.644 36.595 53.775 1.00 21.63 ? 830 SER A N 1 ATOM 6088 C CA . SER A 1 830 ? 14.644 36.091 54.731 1.00 20.98 ? 830 SER A CA 1 ATOM 6089 C C . SER A 1 830 ? 14.042 35.696 56.092 1.00 20.29 ? 830 SER A C 1 ATOM 6090 O O . SER A 1 830 ? 14.727 35.114 56.942 1.00 20.62 ? 830 SER A O 1 ATOM 6091 C CB . SER A 1 830 ? 15.753 37.128 54.948 1.00 21.22 ? 830 SER A CB 1 ATOM 6092 O OG . SER A 1 830 ? 15.283 38.241 55.707 1.00 21.69 ? 830 SER A OG 1 ATOM 6093 N N . ALA A 1 831 ? 12.777 36.031 56.311 1.00 18.76 ? 831 ALA A N 1 ATOM 6094 C CA . ALA A 1 831 ? 12.061 35.598 57.495 1.00 18.49 ? 831 ALA A CA 1 ATOM 6095 C C . ALA A 1 831 ? 11.991 34.072 57.623 1.00 17.86 ? 831 ALA A C 1 ATOM 6096 O O . ALA A 1 831 ? 11.928 33.538 58.738 1.00 16.94 ? 831 ALA A O 1 ATOM 6097 C CB . ALA A 1 831 ? 10.647 36.179 57.481 1.00 18.58 ? 831 ALA A CB 1 ATOM 6098 N N . ILE A 1 832 ? 11.955 33.380 56.489 1.00 17.60 ? 832 ILE A N 1 ATOM 6099 C CA . ILE A 1 832 ? 11.826 31.927 56.487 1.00 18.01 ? 832 ILE A CA 1 ATOM 6100 C C . ILE A 1 832 ? 13.165 31.263 56.198 1.00 17.67 ? 832 ILE A C 1 ATOM 6101 O O . ILE A 1 832 ? 13.797 31.557 55.186 1.00 16.88 ? 832 ILE A O 1 ATOM 6102 C CB . ILE A 1 832 ? 10.781 31.446 55.462 1.00 18.63 ? 832 ILE A CB 1 ATOM 6103 C CG1 . ILE A 1 832 ? 9.418 32.075 55.769 1.00 19.21 ? 832 ILE A CG1 1 ATOM 6104 C CG2 . ILE A 1 832 ? 10.665 29.921 55.497 1.00 18.76 ? 832 ILE A CG2 1 ATOM 6105 C CD1 . ILE A 1 832 ? 8.373 31.809 54.706 1.00 19.41 ? 832 ILE A CD1 1 ATOM 6106 N N . SER A 1 833 ? 13.578 30.373 57.102 1.00 17.60 ? 833 SER A N 1 ATOM 6107 C CA . SER A 1 833 ? 14.791 29.564 56.941 1.00 17.81 ? 833 SER A CA 1 ATOM 6108 C C . SER A 1 833 ? 14.400 28.137 56.571 1.00 17.66 ? 833 SER A C 1 ATOM 6109 O O . SER A 1 833 ? 13.708 27.477 57.331 1.00 17.99 ? 833 SER A O 1 ATOM 6110 C CB . SER A 1 833 ? 15.580 29.526 58.239 1.00 17.78 ? 833 SER A CB 1 ATOM 6111 O OG . SER A 1 833 ? 15.708 30.809 58.777 1.00 18.90 ? 833 SER A OG 1 ATOM 6112 N N . TRP A 1 834 ? 14.853 27.663 55.417 1.00 17.89 ? 834 TRP A N 1 ATOM 6113 C CA . TRP A 1 834 ? 14.388 26.387 54.861 1.00 17.94 ? 834 TRP A CA 1 ATOM 6114 C C . TRP A 1 834 ? 15.343 25.203 55.083 1.00 18.76 ? 834 TRP A C 1 ATOM 6115 O O . TRP A 1 834 ? 16.561 25.338 55.074 1.00 19.26 ? 834 TRP A O 1 ATOM 6116 C CB . TRP A 1 834 ? 14.153 26.536 53.359 1.00 17.20 ? 834 TRP A CB 1 ATOM 6117 C CG . TRP A 1 834 ? 13.028 27.456 53.002 1.00 16.79 ? 834 TRP A CG 1 ATOM 6118 C CD1 . TRP A 1 834 ? 13.123 28.783 52.695 1.00 16.59 ? 834 TRP A CD1 1 ATOM 6119 C CD2 . TRP A 1 834 ? 11.637 27.113 52.885 1.00 16.03 ? 834 TRP A CD2 1 ATOM 6120 N NE1 . TRP A 1 834 ? 11.873 29.293 52.422 1.00 16.81 ? 834 TRP A NE1 1 ATOM 6121 C CE2 . TRP A 1 834 ? 10.946 28.291 52.524 1.00 16.12 ? 834 TRP A CE2 1 ATOM 6122 C CE3 . TRP A 1 834 ? 10.910 25.932 53.064 1.00 15.81 ? 834 TRP A CE3 1 ATOM 6123 C CZ2 . TRP A 1 834 ? 9.565 28.323 52.337 1.00 15.93 ? 834 TRP A CZ2 1 ATOM 6124 C CZ3 . TRP A 1 834 ? 9.529 25.959 52.884 1.00 15.74 ? 834 TRP A CZ3 1 ATOM 6125 C CH2 . TRP A 1 834 ? 8.872 27.147 52.518 1.00 15.99 ? 834 TRP A CH2 1 ATOM 6126 N N . LYS A 1 835 ? 14.762 24.033 55.274 1.00 19.83 ? 835 LYS A N 1 ATOM 6127 C CA . LYS A 1 835 ? 15.488 22.773 55.176 1.00 20.10 ? 835 LYS A CA 1 ATOM 6128 C C . LYS A 1 835 ? 14.744 21.943 54.147 1.00 18.87 ? 835 LYS A C 1 ATOM 6129 O O . LYS A 1 835 ? 13.584 22.203 53.876 1.00 18.64 ? 835 LYS A O 1 ATOM 6130 C CB . LYS A 1 835 ? 15.496 22.073 56.525 1.00 21.60 ? 835 LYS A CB 1 ATOM 6131 C CG . LYS A 1 835 ? 15.953 22.979 57.657 1.00 22.72 ? 835 LYS A CG 1 ATOM 6132 C CD . LYS A 1 835 ? 16.226 22.173 58.910 1.00 24.00 ? 835 LYS A CD 1 ATOM 6133 C CE . LYS A 1 835 ? 16.787 23.024 60.036 1.00 24.07 ? 835 LYS A CE 1 ATOM 6134 N NZ . LYS A 1 835 ? 16.908 22.158 61.235 1.00 24.92 ? 835 LYS A NZ 1 ATOM 6135 N N . LEU A 1 836 ? 15.406 20.959 53.560 1.00 17.93 ? 836 LEU A N 1 ATOM 6136 C CA . LEU A 1 836 ? 14.760 20.086 52.597 1.00 16.70 ? 836 LEU A CA 1 ATOM 6137 C C . LEU A 1 836 ? 15.326 18.692 52.686 1.00 16.28 ? 836 LEU A C 1 ATOM 6138 O O . LEU A 1 836 ? 16.434 18.487 53.201 1.00 16.13 ? 836 LEU A O 1 ATOM 6139 C CB . LEU A 1 836 ? 14.948 20.605 51.174 1.00 16.83 ? 836 LEU A CB 1 ATOM 6140 C CG . LEU A 1 836 ? 16.274 20.304 50.463 1.00 16.94 ? 836 LEU A CG 1 ATOM 6141 C CD1 . LEU A 1 836 ? 16.233 20.762 49.022 1.00 16.74 ? 836 LEU A CD1 1 ATOM 6142 C CD2 . LEU A 1 836 ? 17.449 20.941 51.198 1.00 17.16 ? 836 LEU A CD2 1 ATOM 6143 N N . THR A 1 837 ? 14.558 17.739 52.176 1.00 15.48 ? 837 THR A N 1 ATOM 6144 C CA . THR A 1 837 ? 15.071 16.422 51.927 1.00 15.22 ? 837 THR A CA 1 ATOM 6145 C C . THR A 1 837 ? 14.444 15.768 50.703 1.00 15.29 ? 837 THR A C 1 ATOM 6146 O O . THR A 1 837 ? 13.287 16.025 50.321 1.00 14.89 ? 837 THR A O 1 ATOM 6147 C CB . THR A 1 837 ? 14.929 15.488 53.140 1.00 15.13 ? 837 THR A CB 1 ATOM 6148 O OG1 . THR A 1 837 ? 15.708 14.305 52.916 1.00 15.21 ? 837 THR A OG1 1 ATOM 6149 C CG2 . THR A 1 837 ? 13.491 15.098 53.373 1.00 15.36 ? 837 THR A CG2 1 ATOM 6150 N N . GLY A 1 838 ? 15.262 14.917 50.101 1.00 15.00 ? 838 GLY A N 1 ATOM 6151 C CA . GLY A 1 838 ? 14.857 14.022 49.038 1.00 14.79 ? 838 GLY A CA 1 ATOM 6152 C C . GLY A 1 838 ? 15.159 12.651 49.591 1.00 14.14 ? 838 GLY A C 1 ATOM 6153 O O . GLY A 1 838 ? 15.175 12.471 50.796 1.00 13.32 ? 838 GLY A O 1 ATOM 6154 N N . ASN A 1 839 ? 15.425 11.702 48.705 1.00 14.32 ? 839 ASN A N 1 ATOM 6155 C CA . ASN A 1 839 ? 15.855 10.363 49.101 1.00 14.56 ? 839 ASN A CA 1 ATOM 6156 C C . ASN A 1 839 ? 17.023 10.511 50.034 1.00 15.15 ? 839 ASN A C 1 ATOM 6157 O O . ASN A 1 839 ? 17.821 11.434 49.859 1.00 14.39 ? 839 ASN A O 1 ATOM 6158 C CB . ASN A 1 839 ? 16.273 9.548 47.870 1.00 14.48 ? 839 ASN A CB 1 ATOM 6159 C CG . ASN A 1 839 ? 17.576 10.050 47.250 1.00 14.51 ? 839 ASN A CG 1 ATOM 6160 O OD1 . ASN A 1 839 ? 17.626 11.128 46.653 1.00 14.58 ? 839 ASN A OD1 1 ATOM 6161 N ND2 . ASN A 1 839 ? 18.638 9.275 47.405 1.00 14.22 ? 839 ASN A ND2 1 ATOM 6162 N N . LEU A 1 840 ? 17.133 9.606 51.008 1.00 16.03 ? 840 LEU A N 1 ATOM 6163 C CA . LEU A 1 840 ? 18.118 9.740 52.077 1.00 17.13 ? 840 LEU A CA 1 ATOM 6164 C C . LEU A 1 840 ? 19.571 9.593 51.607 1.00 18.15 ? 840 LEU A C 1 ATOM 6165 O O . LEU A 1 840 ? 19.925 8.574 51.004 1.00 18.97 ? 840 LEU A O 1 ATOM 6166 C CB . LEU A 1 840 ? 17.853 8.722 53.190 1.00 17.13 ? 840 LEU A CB 1 ATOM 6167 C CG . LEU A 1 840 ? 18.737 8.884 54.429 1.00 17.43 ? 840 LEU A CG 1 ATOM 6168 C CD1 . LEU A 1 840 ? 18.383 10.168 55.175 1.00 17.63 ? 840 LEU A CD1 1 ATOM 6169 C CD2 . LEU A 1 840 ? 18.641 7.670 55.344 1.00 17.54 ? 840 LEU A CD2 1 ATOM 6170 N N . GLY A 1 841 ? 20.401 10.596 51.933 1.00 18.17 ? 841 GLY A N 1 ATOM 6171 C CA . GLY A 1 841 ? 21.793 10.657 51.491 1.00 18.15 ? 841 GLY A CA 1 ATOM 6172 C C . GLY A 1 841 ? 21.982 11.391 50.168 1.00 18.43 ? 841 GLY A C 1 ATOM 6173 O O . GLY A 1 841 ? 23.107 11.689 49.769 1.00 19.14 ? 841 GLY A O 1 ATOM 6174 N N . GLY A 1 842 ? 20.887 11.693 49.485 1.00 18.01 ? 842 GLY A N 1 ATOM 6175 C CA . GLY A 1 842 ? 20.949 12.315 48.170 1.00 18.51 ? 842 GLY A CA 1 ATOM 6176 C C . GLY A 1 842 ? 21.790 11.502 47.208 1.00 19.14 ? 842 GLY A C 1 ATOM 6177 O O . GLY A 1 842 ? 21.487 10.333 46.911 1.00 17.93 ? 842 GLY A O 1 ATOM 6178 N N . GLU A 1 843 ? 22.867 12.116 46.730 1.00 20.17 ? 843 GLU A N 1 ATOM 6179 C CA . GLU A 1 843 ? 23.779 11.442 45.805 1.00 20.77 ? 843 GLU A CA 1 ATOM 6180 C C . GLU A 1 843 ? 24.542 10.295 46.470 1.00 21.05 ? 843 GLU A C 1 ATOM 6181 O O . GLU A 1 843 ? 24.966 9.370 45.789 1.00 20.37 ? 843 GLU A O 1 ATOM 6182 C CB . GLU A 1 843 ? 24.720 12.443 45.137 1.00 20.91 ? 843 GLU A CB 1 ATOM 6183 C CG . GLU A 1 843 ? 24.075 13.087 43.918 1.00 20.90 ? 843 GLU A CG 1 ATOM 6184 C CD . GLU A 1 843 ? 24.628 14.451 43.583 1.00 21.14 ? 843 GLU A CD 1 ATOM 6185 O OE1 . GLU A 1 843 ? 25.794 14.748 43.910 1.00 21.72 ? 843 GLU A OE1 1 ATOM 6186 O OE2 . GLU A 1 843 ? 23.893 15.230 42.956 1.00 21.21 -1 843 GLU A OE2 1 ATOM 6187 N N . ASP A 1 844 ? 24.663 10.330 47.794 1.00 21.72 ? 844 ASP A N 1 ATOM 6188 C CA . ASP A 1 844 ? 25.154 9.185 48.549 1.00 23.02 ? 844 ASP A CA 1 ATOM 6189 C C . ASP A 1 844 ? 23.993 8.262 48.902 1.00 22.52 ? 844 ASP A C 1 ATOM 6190 O O . ASP A 1 844 ? 23.713 7.964 50.056 1.00 22.01 ? 844 ASP A O 1 ATOM 6191 C CB . ASP A 1 844 ? 25.929 9.648 49.784 1.00 25.41 ? 844 ASP A CB 1 ATOM 6192 C CG . ASP A 1 844 ? 27.269 10.269 49.417 1.00 27.54 ? 844 ASP A CG 1 ATOM 6193 O OD1 . ASP A 1 844 ? 28.089 9.556 48.793 1.00 28.49 ? 844 ASP A OD1 1 ATOM 6194 O OD2 . ASP A 1 844 ? 27.496 11.461 49.736 1.00 29.30 -1 844 ASP A OD2 1 ATOM 6195 N N . TYR A 1 845 ? 23.346 7.780 47.856 1.00 22.88 ? 845 TYR A N 1 ATOM 6196 C CA . TYR A 1 845 ? 22.091 7.058 47.973 1.00 22.80 ? 845 TYR A CA 1 ATOM 6197 C C . TYR A 1 845 ? 22.291 5.726 48.697 1.00 23.62 ? 845 TYR A C 1 ATOM 6198 O O . TYR A 1 845 ? 23.366 5.129 48.658 1.00 23.97 ? 845 TYR A O 1 ATOM 6199 C CB . TYR A 1 845 ? 21.447 6.891 46.588 1.00 21.73 ? 845 TYR A CB 1 ATOM 6200 C CG . TYR A 1 845 ? 22.207 6.030 45.603 1.00 20.38 ? 845 TYR A CG 1 ATOM 6201 C CD1 . TYR A 1 845 ? 23.176 6.577 44.738 1.00 19.94 ? 845 TYR A CD1 1 ATOM 6202 C CD2 . TYR A 1 845 ? 21.945 4.668 45.517 1.00 19.93 ? 845 TYR A CD2 1 ATOM 6203 C CE1 . TYR A 1 845 ? 23.860 5.775 43.825 1.00 19.15 ? 845 TYR A CE1 1 ATOM 6204 C CE2 . TYR A 1 845 ? 22.616 3.866 44.604 1.00 19.68 ? 845 TYR A CE2 1 ATOM 6205 C CZ . TYR A 1 845 ? 23.571 4.417 43.769 1.00 18.92 ? 845 TYR A CZ 1 ATOM 6206 O OH . TYR A 1 845 ? 24.215 3.576 42.906 1.00 18.70 ? 845 TYR A OH 1 ATOM 6207 N N . GLU A 1 846 ? 21.257 5.302 49.404 1.00 24.02 ? 846 GLU A N 1 ATOM 6208 C CA . GLU A 1 846 ? 21.349 4.158 50.301 1.00 24.05 ? 846 GLU A CA 1 ATOM 6209 C C . GLU A 1 846 ? 21.260 2.826 49.569 1.00 22.65 ? 846 GLU A C 1 ATOM 6210 O O . GLU A 1 846 ? 22.015 1.921 49.860 1.00 23.00 ? 846 GLU A O 1 ATOM 6211 C CB . GLU A 1 846 ? 20.228 4.230 51.339 1.00 25.60 ? 846 GLU A CB 1 ATOM 6212 C CG . GLU A 1 846 ? 20.402 5.349 52.355 1.00 28.34 ? 846 GLU A CG 1 ATOM 6213 C CD . GLU A 1 846 ? 21.401 5.020 53.448 1.00 30.26 ? 846 GLU A CD 1 ATOM 6214 O OE1 . GLU A 1 846 ? 21.587 3.820 53.755 1.00 31.04 ? 846 GLU A OE1 1 ATOM 6215 O OE2 . GLU A 1 846 ? 21.993 5.973 54.005 1.00 34.98 -1 846 GLU A OE2 1 ATOM 6216 N N . ASP A 1 847 ? 20.320 2.701 48.638 1.00 22.14 ? 847 ASP A N 1 ATOM 6217 C CA . ASP A 1 847 ? 20.041 1.412 47.999 1.00 21.53 ? 847 ASP A CA 1 ATOM 6218 C C . ASP A 1 847 ? 20.889 1.181 46.740 1.00 20.66 ? 847 ASP A C 1 ATOM 6219 O O . ASP A 1 847 ? 20.472 1.492 45.611 1.00 20.64 ? 847 ASP A O 1 ATOM 6220 C CB . ASP A 1 847 ? 18.539 1.274 47.690 1.00 21.35 ? 847 ASP A CB 1 ATOM 6221 C CG . ASP A 1 847 ? 18.096 -0.186 47.528 1.00 20.98 ? 847 ASP A CG 1 ATOM 6222 O OD1 . ASP A 1 847 ? 18.949 -1.068 47.273 1.00 20.00 ? 847 ASP A OD1 1 ATOM 6223 O OD2 . ASP A 1 847 ? 16.882 -0.444 47.652 1.00 21.16 -1 847 ASP A OD2 1 ATOM 6224 N N . LYS A 1 848 ? 22.070 0.604 46.955 1.00 19.28 ? 848 LYS A N 1 ATOM 6225 C CA . LYS A 1 848 ? 22.984 0.265 45.870 1.00 18.71 ? 848 LYS A CA 1 ATOM 6226 C C . LYS A 1 848 ? 22.484 -0.881 44.996 1.00 17.84 ? 848 LYS A C 1 ATOM 6227 O O . LYS A 1 848 ? 22.951 -1.039 43.876 1.00 17.88 ? 848 LYS A O 1 ATOM 6228 C CB . LYS A 1 848 ? 24.385 -0.098 46.413 1.00 18.57 ? 848 LYS A CB 1 ATOM 6229 C CG . LYS A 1 848 ? 25.054 0.964 47.287 1.00 18.62 ? 848 LYS A CG 1 ATOM 6230 C CD . LYS A 1 848 ? 25.129 2.329 46.620 1.00 18.13 ? 848 LYS A CD 1 ATOM 6231 C CE . LYS A 1 848 ? 25.763 3.328 47.566 1.00 17.84 ? 848 LYS A CE 1 ATOM 6232 N NZ . LYS A 1 848 ? 25.777 4.711 47.031 1.00 17.58 ? 848 LYS A NZ 1 ATOM 6233 N N . VAL A 1 849 ? 21.583 -1.706 45.509 1.00 17.76 ? 849 VAL A N 1 ATOM 6234 C CA . VAL A 1 849 ? 21.034 -2.814 44.713 1.00 17.80 ? 849 VAL A CA 1 ATOM 6235 C C . VAL A 1 849 ? 19.935 -2.293 43.786 1.00 17.08 ? 849 VAL A C 1 ATOM 6236 O O . VAL A 1 849 ? 19.954 -2.563 42.591 1.00 17.76 ? 849 VAL A O 1 ATOM 6237 C CB . VAL A 1 849 ? 20.504 -3.959 45.604 1.00 18.20 ? 849 VAL A CB 1 ATOM 6238 C CG1 . VAL A 1 849 ? 19.776 -5.009 44.770 1.00 18.06 ? 849 VAL A CG1 1 ATOM 6239 C CG2 . VAL A 1 849 ? 21.656 -4.595 46.368 1.00 18.56 ? 849 VAL A CG2 1 ATOM 6240 N N . ARG A 1 850 ? 18.999 -1.518 44.319 1.00 16.25 ? 850 ARG A N 1 ATOM 6241 C CA . ARG A 1 850 ? 17.890 -1.024 43.498 1.00 16.24 ? 850 ARG A CA 1 ATOM 6242 C C . ARG A 1 850 ? 18.190 0.274 42.739 1.00 15.93 ? 850 ARG A C 1 ATOM 6243 O O . ARG A 1 850 ? 17.409 0.670 41.869 1.00 15.77 ? 850 ARG A O 1 ATOM 6244 C CB . ARG A 1 850 ? 16.605 -0.917 44.325 1.00 16.09 ? 850 ARG A CB 1 ATOM 6245 C CG . ARG A 1 850 ? 16.281 -2.213 45.054 1.00 16.07 ? 850 ARG A CG 1 ATOM 6246 C CD . ARG A 1 850 ? 14.926 -2.142 45.716 1.00 16.78 ? 850 ARG A CD 1 ATOM 6247 N NE . ARG A 1 850 ? 14.576 -3.367 46.429 1.00 17.44 ? 850 ARG A NE 1 ATOM 6248 C CZ . ARG A 1 850 ? 14.912 -3.661 47.683 1.00 17.36 ? 850 ARG A CZ 1 ATOM 6249 N NH1 . ARG A 1 850 ? 15.636 -2.827 48.428 1.00 16.85 ? 850 ARG A NH1 1 ATOM 6250 N NH2 . ARG A 1 850 ? 14.507 -4.823 48.195 1.00 17.46 ? 850 ARG A NH2 1 ATOM 6251 N N . GLY A 1 851 ? 19.322 0.911 43.035 1.00 15.57 ? 851 GLY A N 1 ATOM 6252 C CA . GLY A 1 851 ? 19.783 2.057 42.249 1.00 15.59 ? 851 GLY A CA 1 ATOM 6253 C C . GLY A 1 851 ? 19.349 3.419 42.779 1.00 15.75 ? 851 GLY A C 1 ATOM 6254 O O . GLY A 1 851 ? 18.569 3.494 43.717 1.00 15.81 ? 851 GLY A O 1 ATOM 6255 N N . PRO A 1 852 ? 19.840 4.510 42.152 1.00 15.78 ? 852 PRO A N 1 ATOM 6256 C CA . PRO A 1 852 ? 19.718 5.877 42.691 1.00 15.64 ? 852 PRO A CA 1 ATOM 6257 C C . PRO A 1 852 ? 18.342 6.555 42.597 1.00 15.68 ? 852 PRO A C 1 ATOM 6258 O O . PRO A 1 852 ? 18.136 7.572 43.250 1.00 14.50 ? 852 PRO A O 1 ATOM 6259 C CB . PRO A 1 852 ? 20.741 6.672 41.861 1.00 15.84 ? 852 PRO A CB 1 ATOM 6260 C CG . PRO A 1 852 ? 20.903 5.910 40.596 1.00 15.65 ? 852 PRO A CG 1 ATOM 6261 C CD . PRO A 1 852 ? 20.678 4.465 40.939 1.00 15.72 ? 852 PRO A CD 1 ATOM 6262 N N . LEU A 1 853 ? 17.427 6.004 41.796 1.00 15.70 ? 853 LEU A N 1 ATOM 6263 C CA . LEU A 1 853 ? 16.152 6.656 41.494 1.00 15.60 ? 853 LEU A CA 1 ATOM 6264 C C . LEU A 1 853 ? 14.936 6.069 42.216 1.00 15.32 ? 853 LEU A C 1 ATOM 6265 O O . LEU A 1 853 ? 13.905 6.741 42.333 1.00 14.83 ? 853 LEU A O 1 ATOM 6266 C CB . LEU A 1 853 ? 15.915 6.593 39.985 1.00 15.71 ? 853 LEU A CB 1 ATOM 6267 C CG . LEU A 1 853 ? 17.001 7.273 39.148 1.00 15.94 ? 853 LEU A CG 1 ATOM 6268 C CD1 . LEU A 1 853 ? 16.578 7.304 37.691 1.00 15.82 ? 853 LEU A CD1 1 ATOM 6269 C CD2 . LEU A 1 853 ? 17.296 8.684 39.645 1.00 16.00 ? 853 LEU A CD2 1 ATOM 6270 N N . ASN A 1 854 ? 15.067 4.822 42.680 1.00 15.06 ? 854 ASN A N 1 ATOM 6271 C CA . ASN A 1 854 ? 13.953 4.026 43.192 1.00 15.07 ? 854 ASN A CA 1 ATOM 6272 C C . ASN A 1 854 ? 13.120 4.702 44.267 1.00 16.04 ? 854 ASN A C 1 ATOM 6273 O O . ASN A 1 854 ? 11.883 4.670 44.225 1.00 17.56 ? 854 ASN A O 1 ATOM 6274 C CB . ASN A 1 854 ? 14.473 2.695 43.756 1.00 14.54 ? 854 ASN A CB 1 ATOM 6275 C CG . ASN A 1 854 ? 13.364 1.693 44.004 1.00 14.17 ? 854 ASN A CG 1 ATOM 6276 O OD1 . ASN A 1 854 ? 12.600 1.385 43.099 1.00 13.96 ? 854 ASN A OD1 1 ATOM 6277 N ND2 . ASN A 1 854 ? 13.273 1.173 45.232 1.00 14.28 ? 854 ASN A ND2 1 ATOM 6278 N N . GLU A 1 855 ? 13.791 5.293 45.241 1.00 16.55 ? 855 GLU A N 1 ATOM 6279 C CA . GLU A 1 855 ? 13.117 5.809 46.418 1.00 17.48 ? 855 GLU A CA 1 ATOM 6280 C C . GLU A 1 855 ? 13.216 7.324 46.477 1.00 17.38 ? 855 GLU A C 1 ATOM 6281 O O . GLU A 1 855 ? 14.167 7.887 45.964 1.00 17.77 ? 855 GLU A O 1 ATOM 6282 C CB . GLU A 1 855 ? 13.691 5.163 47.691 1.00 18.22 ? 855 GLU A CB 1 ATOM 6283 C CG . GLU A 1 855 ? 15.160 5.423 47.989 1.00 18.40 ? 855 GLU A CG 1 ATOM 6284 C CD . GLU A 1 855 ? 15.617 4.719 49.261 1.00 19.54 ? 855 GLU A CD 1 ATOM 6285 O OE1 . GLU A 1 855 ? 15.571 3.466 49.330 1.00 19.51 ? 855 GLU A OE1 1 ATOM 6286 O OE2 . GLU A 1 855 ? 16.024 5.418 50.209 1.00 20.31 -1 855 GLU A OE2 1 ATOM 6287 N N . GLY A 1 856 ? 12.221 7.970 47.089 1.00 17.45 ? 856 GLY A N 1 ATOM 6288 C CA . GLY A 1 856 ? 12.200 9.439 47.269 1.00 16.90 ? 856 GLY A CA 1 ATOM 6289 C C . GLY A 1 856 ? 12.310 9.787 48.749 1.00 16.55 ? 856 GLY A C 1 ATOM 6290 O O . GLY A 1 856 ? 12.849 8.994 49.517 1.00 15.81 ? 856 GLY A O 1 ATOM 6291 N N . GLY A 1 857 ? 11.772 10.944 49.155 1.00 16.48 ? 857 GLY A N 1 ATOM 6292 C CA . GLY A 1 857 ? 12.077 11.540 50.479 1.00 16.32 ? 857 GLY A CA 1 ATOM 6293 C C . GLY A 1 857 ? 11.101 11.380 51.642 1.00 16.98 ? 857 GLY A C 1 ATOM 6294 O O . GLY A 1 857 ? 11.300 11.996 52.699 1.00 16.31 ? 857 GLY A O 1 ATOM 6295 N N . LEU A 1 858 ? 10.051 10.564 51.472 1.00 17.26 ? 858 LEU A N 1 ATOM 6296 C CA . LEU A 1 858 ? 9.104 10.292 52.555 1.00 16.84 ? 858 LEU A CA 1 ATOM 6297 C C . LEU A 1 858 ? 9.793 9.567 53.713 1.00 16.93 ? 858 LEU A C 1 ATOM 6298 O O . LEU A 1 858 ? 10.703 8.760 53.503 1.00 16.82 ? 858 LEU A O 1 ATOM 6299 C CB . LEU A 1 858 ? 7.920 9.432 52.070 1.00 16.86 ? 858 LEU A CB 1 ATOM 6300 C CG . LEU A 1 858 ? 6.908 9.980 51.059 1.00 16.52 ? 858 LEU A CG 1 ATOM 6301 C CD1 . LEU A 1 858 ? 5.899 8.908 50.667 1.00 16.30 ? 858 LEU A CD1 1 ATOM 6302 C CD2 . LEU A 1 858 ? 6.194 11.200 51.615 1.00 16.51 ? 858 LEU A CD2 1 ATOM 6303 N N . TYR A 1 859 ? 9.340 9.857 54.930 1.00 16.98 ? 859 TYR A N 1 ATOM 6304 C CA . TYR A 1 859 ? 9.861 9.233 56.151 1.00 17.09 ? 859 TYR A CA 1 ATOM 6305 C C . TYR A 1 859 ? 10.050 7.715 56.044 1.00 16.89 ? 859 TYR A C 1 ATOM 6306 O O . TYR A 1 859 ? 11.123 7.192 56.351 1.00 16.10 ? 859 TYR A O 1 ATOM 6307 C CB . TYR A 1 859 ? 8.925 9.561 57.313 1.00 17.59 ? 859 TYR A CB 1 ATOM 6308 C CG . TYR A 1 859 ? 9.136 8.721 58.539 1.00 18.20 ? 859 TYR A CG 1 ATOM 6309 C CD1 . TYR A 1 859 ? 10.305 8.844 59.301 1.00 18.51 ? 859 TYR A CD1 1 ATOM 6310 C CD2 . TYR A 1 859 ? 8.165 7.812 58.956 1.00 18.63 ? 859 TYR A CD2 1 ATOM 6311 C CE1 . TYR A 1 859 ? 10.505 8.069 60.431 1.00 19.14 ? 859 TYR A CE1 1 ATOM 6312 C CE2 . TYR A 1 859 ? 8.355 7.032 60.086 1.00 19.18 ? 859 TYR A CE2 1 ATOM 6313 C CZ . TYR A 1 859 ? 9.527 7.161 60.816 1.00 19.10 ? 859 TYR A CZ 1 ATOM 6314 O OH . TYR A 1 859 ? 9.706 6.403 61.947 1.00 20.43 ? 859 TYR A OH 1 ATOM 6315 N N . ALA A 1 860 ? 8.996 7.022 55.619 1.00 17.08 ? 860 ALA A N 1 ATOM 6316 C CA . ALA A 1 860 ? 9.005 5.565 55.462 1.00 17.17 ? 860 ALA A CA 1 ATOM 6317 C C . ALA A 1 860 ? 10.049 5.083 54.461 1.00 17.61 ? 860 ALA A C 1 ATOM 6318 O O . ALA A 1 860 ? 10.691 4.050 54.679 1.00 19.07 ? 860 ALA A O 1 ATOM 6319 C CB . ALA A 1 860 ? 7.626 5.089 55.038 1.00 17.28 ? 860 ALA A CB 1 ATOM 6320 N N . GLU A 1 861 ? 10.192 5.816 53.361 1.00 17.07 ? 861 GLU A N 1 ATOM 6321 C CA . GLU A 1 861 ? 11.234 5.565 52.373 1.00 17.69 ? 861 GLU A CA 1 ATOM 6322 C C . GLU A 1 861 ? 12.651 5.848 52.933 1.00 18.02 ? 861 GLU A C 1 ATOM 6323 O O . GLU A 1 861 ? 13.577 5.048 52.721 1.00 17.90 ? 861 GLU A O 1 ATOM 6324 C CB . GLU A 1 861 ? 10.998 6.418 51.104 1.00 18.08 ? 861 GLU A CB 1 ATOM 6325 C CG . GLU A 1 861 ? 9.708 6.116 50.340 1.00 18.12 ? 861 GLU A CG 1 ATOM 6326 C CD . GLU A 1 861 ? 9.404 7.114 49.223 1.00 18.73 ? 861 GLU A CD 1 ATOM 6327 O OE1 . GLU A 1 861 ? 9.509 8.349 49.417 1.00 18.35 ? 861 GLU A OE1 1 ATOM 6328 O OE2 . GLU A 1 861 ? 9.044 6.653 48.123 1.00 20.05 -1 861 GLU A OE2 1 ATOM 6329 N N . ARG A 1 862 ? 12.815 6.975 53.640 1.00 17.62 ? 862 ARG A N 1 ATOM 6330 C CA . ARG A 1 862 ? 14.106 7.325 54.265 1.00 17.37 ? 862 ARG A CA 1 ATOM 6331 C C . ARG A 1 862 ? 14.578 6.233 55.209 1.00 17.35 ? 862 ARG A C 1 ATOM 6332 O O . ARG A 1 862 ? 15.773 5.914 55.252 1.00 16.95 ? 862 ARG A O 1 ATOM 6333 C CB . ARG A 1 862 ? 14.029 8.656 55.017 1.00 16.82 ? 862 ARG A CB 1 ATOM 6334 C CG . ARG A 1 862 ? 13.794 9.836 54.088 1.00 16.92 ? 862 ARG A CG 1 ATOM 6335 C CD . ARG A 1 862 ? 13.916 11.188 54.776 1.00 16.83 ? 862 ARG A CD 1 ATOM 6336 N NE . ARG A 1 862 ? 13.143 11.301 56.019 1.00 16.73 ? 862 ARG A NE 1 ATOM 6337 C CZ . ARG A 1 862 ? 12.044 12.045 56.211 1.00 16.50 ? 862 ARG A CZ 1 ATOM 6338 N NH1 . ARG A 1 862 ? 11.498 12.770 55.237 1.00 16.44 ? 862 ARG A NH1 1 ATOM 6339 N NH2 . ARG A 1 862 ? 11.478 12.062 57.412 1.00 16.27 ? 862 ARG A NH2 1 ATOM 6340 N N . GLN A 1 863 ? 13.630 5.666 55.947 1.00 17.20 ? 863 GLN A N 1 ATOM 6341 C CA . GLN A 1 863 ? 13.900 4.583 56.882 1.00 17.69 ? 863 GLN A CA 1 ATOM 6342 C C . GLN A 1 863 ? 14.041 3.207 56.215 1.00 17.60 ? 863 GLN A C 1 ATOM 6343 O O . GLN A 1 863 ? 14.447 2.264 56.863 1.00 18.53 ? 863 GLN A O 1 ATOM 6344 C CB . GLN A 1 863 ? 12.783 4.494 57.921 1.00 18.09 ? 863 GLN A CB 1 ATOM 6345 C CG . GLN A 1 863 ? 12.612 5.719 58.798 1.00 18.14 ? 863 GLN A CG 1 ATOM 6346 C CD . GLN A 1 863 ? 13.643 5.822 59.907 1.00 18.59 ? 863 GLN A CD 1 ATOM 6347 O OE1 . GLN A 1 863 ? 14.050 4.824 60.504 1.00 18.53 ? 863 GLN A OE1 1 ATOM 6348 N NE2 . GLN A 1 863 ? 14.047 7.049 60.212 1.00 19.71 ? 863 GLN A NE2 1 ATOM 6349 N N . GLY A 1 864 ? 13.697 3.075 54.943 1.00 17.53 ? 864 GLY A N 1 ATOM 6350 C CA . GLY A 1 864 ? 13.800 1.785 54.268 1.00 17.60 ? 864 GLY A CA 1 ATOM 6351 C C . GLY A 1 864 ? 12.674 0.786 54.518 1.00 17.38 ? 864 GLY A C 1 ATOM 6352 O O . GLY A 1 864 ? 12.843 -0.396 54.211 1.00 17.74 ? 864 GLY A O 1 ATOM 6353 N N . PHE A 1 865 ? 11.530 1.260 55.033 1.00 17.22 ? 865 PHE A N 1 ATOM 6354 C CA . PHE A 1 865 ? 10.351 0.417 55.366 1.00 16.64 ? 865 PHE A CA 1 ATOM 6355 C C . PHE A 1 865 ? 9.624 -0.188 54.150 1.00 17.02 ? 865 PHE A C 1 ATOM 6356 O O . PHE A 1 865 ? 8.726 -1.013 54.309 1.00 16.77 ? 865 PHE A O 1 ATOM 6357 C CB . PHE A 1 865 ? 9.280 1.224 56.106 1.00 16.49 ? 865 PHE A CB 1 ATOM 6358 C CG . PHE A 1 865 ? 9.673 1.753 57.474 1.00 16.78 ? 865 PHE A CG 1 ATOM 6359 C CD1 . PHE A 1 865 ? 10.766 1.281 58.178 1.00 16.64 ? 865 PHE A CD1 1 ATOM 6360 C CD2 . PHE A 1 865 ? 8.874 2.723 58.077 1.00 16.75 ? 865 PHE A CD2 1 ATOM 6361 C CE1 . PHE A 1 865 ? 11.071 1.788 59.430 1.00 16.73 ? 865 PHE A CE1 1 ATOM 6362 C CE2 . PHE A 1 865 ? 9.176 3.232 59.331 1.00 16.79 ? 865 PHE A CE2 1 ATOM 6363 C CZ . PHE A 1 865 ? 10.273 2.758 60.010 1.00 16.79 ? 865 PHE A CZ 1 ATOM 6364 N N . HIS A 1 866 ? 9.961 0.278 52.950 1.00 17.37 ? 866 HIS A N 1 ATOM 6365 C CA . HIS A 1 866 ? 9.367 -0.204 51.694 1.00 17.66 ? 866 HIS A CA 1 ATOM 6366 C C . HIS A 1 866 ? 9.992 -1.504 51.206 1.00 17.83 ? 866 HIS A C 1 ATOM 6367 O O . HIS A 1 866 ? 9.555 -2.074 50.217 1.00 18.35 ? 866 HIS A O 1 ATOM 6368 C CB . HIS A 1 866 ? 9.513 0.859 50.600 1.00 17.84 ? 866 HIS A CB 1 ATOM 6369 C CG . HIS A 1 866 ? 10.935 1.187 50.252 1.00 17.90 ? 866 HIS A CG 1 ATOM 6370 N ND1 . HIS A 1 866 ? 11.728 1.998 51.034 1.00 18.12 ? 866 HIS A ND1 1 ATOM 6371 C CD2 . HIS A 1 866 ? 11.701 0.819 49.198 1.00 18.19 ? 866 HIS A CD2 1 ATOM 6372 C CE1 . HIS A 1 866 ? 12.920 2.112 50.478 1.00 18.78 ? 866 HIS A CE1 1 ATOM 6373 N NE2 . HIS A 1 866 ? 12.924 1.419 49.353 1.00 18.39 ? 866 HIS A NE2 1 ATOM 6374 N N . GLN A 1 867 ? 11.017 -1.955 51.905 1.00 18.06 ? 867 GLN A N 1 ATOM 6375 C CA . GLN A 1 867 ? 11.705 -3.191 51.597 1.00 18.60 ? 867 GLN A CA 1 ATOM 6376 C C . GLN A 1 867 ? 11.071 -4.342 52.353 1.00 19.22 ? 867 GLN A C 1 ATOM 6377 O O . GLN A 1 867 ? 10.356 -4.121 53.335 1.00 19.50 ? 867 GLN A O 1 ATOM 6378 C CB . GLN A 1 867 ? 13.164 -3.062 52.027 1.00 18.10 ? 867 GLN A CB 1 ATOM 6379 C CG . GLN A 1 867 ? 13.872 -1.914 51.339 1.00 17.65 ? 867 GLN A CG 1 ATOM 6380 C CD . GLN A 1 867 ? 15.289 -1.768 51.805 1.00 17.45 ? 867 GLN A CD 1 ATOM 6381 O OE1 . GLN A 1 867 ? 16.199 -2.300 51.195 1.00 17.24 ? 867 GLN A OE1 1 ATOM 6382 N NE2 . GLN A 1 867 ? 15.480 -1.069 52.917 1.00 17.63 ? 867 GLN A NE2 1 ATOM 6383 N N . PRO A 1 868 ? 11.329 -5.579 51.903 1.00 19.91 ? 868 PRO A N 1 ATOM 6384 C CA . PRO A 1 868 ? 10.870 -6.788 52.588 1.00 20.19 ? 868 PRO A CA 1 ATOM 6385 C C . PRO A 1 868 ? 11.124 -6.821 54.105 1.00 20.46 ? 868 PRO A C 1 ATOM 6386 O O . PRO A 1 868 ? 12.186 -6.396 54.572 1.00 20.49 ? 868 PRO A O 1 ATOM 6387 C CB . PRO A 1 868 ? 11.681 -7.878 51.900 1.00 20.11 ? 868 PRO A CB 1 ATOM 6388 C CG . PRO A 1 868 ? 11.818 -7.389 50.505 1.00 19.94 ? 868 PRO A CG 1 ATOM 6389 C CD . PRO A 1 868 ? 11.894 -5.894 50.580 1.00 19.96 ? 868 PRO A CD 1 ATOM 6390 N N . GLU A 1 869 ? 10.142 -7.331 54.845 1.00 21.37 ? 869 GLU A N 1 ATOM 6391 C CA . GLU A 1 869 ? 10.205 -7.492 56.300 1.00 23.05 ? 869 GLU A CA 1 ATOM 6392 C C . GLU A 1 869 ? 10.480 -6.175 57.040 1.00 22.65 ? 869 GLU A C 1 ATOM 6393 O O . GLU A 1 869 ? 11.484 -6.056 57.740 1.00 21.53 ? 869 GLU A O 1 ATOM 6394 C CB . GLU A 1 869 ? 11.258 -8.537 56.685 1.00 25.85 ? 869 GLU A CB 1 ATOM 6395 C CG . GLU A 1 869 ? 11.179 -9.834 55.895 1.00 28.43 ? 869 GLU A CG 1 ATOM 6396 C CD . GLU A 1 869 ? 12.189 -10.872 56.356 1.00 30.89 ? 869 GLU A CD 1 ATOM 6397 O OE1 . GLU A 1 869 ? 12.382 -11.012 57.577 1.00 34.20 ? 869 GLU A OE1 1 ATOM 6398 O OE2 . GLU A 1 869 ? 12.790 -11.554 55.497 1.00 34.54 -1 869 GLU A OE2 1 ATOM 6399 N N . PRO A 1 870 ? 9.580 -5.181 56.893 1.00 22.47 ? 870 PRO A N 1 ATOM 6400 C CA . PRO A 1 870 ? 9.724 -3.951 57.673 1.00 22.56 ? 870 PRO A CA 1 ATOM 6401 C C . PRO A 1 870 ? 9.362 -4.204 59.142 1.00 22.00 ? 870 PRO A C 1 ATOM 6402 O O . PRO A 1 870 ? 8.759 -5.225 59.444 1.00 22.03 ? 870 PRO A O 1 ATOM 6403 C CB . PRO A 1 870 ? 8.716 -3.011 57.016 1.00 22.37 ? 870 PRO A CB 1 ATOM 6404 C CG . PRO A 1 870 ? 7.637 -3.917 56.513 1.00 22.45 ? 870 PRO A CG 1 ATOM 6405 C CD . PRO A 1 870 ? 8.266 -5.257 56.228 1.00 22.32 ? 870 PRO A CD 1 ATOM 6406 N N . PRO A 1 871 ? 9.713 -3.283 60.051 1.00 22.57 ? 871 PRO A N 1 ATOM 6407 C CA . PRO A 1 871 ? 9.388 -3.451 61.462 1.00 22.81 ? 871 PRO A CA 1 ATOM 6408 C C . PRO A 1 871 ? 7.963 -2.964 61.787 1.00 23.48 ? 871 PRO A C 1 ATOM 6409 O O . PRO A 1 871 ? 7.776 -1.995 62.524 1.00 23.04 ? 871 PRO A O 1 ATOM 6410 C CB . PRO A 1 871 ? 10.440 -2.578 62.145 1.00 22.66 ? 871 PRO A CB 1 ATOM 6411 C CG . PRO A 1 871 ? 10.590 -1.429 61.206 1.00 22.88 ? 871 PRO A CG 1 ATOM 6412 C CD . PRO A 1 871 ? 10.390 -1.993 59.811 1.00 23.08 ? 871 PRO A CD 1 ATOM 6413 N N . SER A 1 872 ? 6.977 -3.664 61.247 1.00 25.23 ? 872 SER A N 1 ATOM 6414 C CA . SER A 1 872 ? 5.583 -3.240 61.289 1.00 26.99 ? 872 SER A CA 1 ATOM 6415 C C . SER A 1 872 ? 4.795 -3.933 62.394 1.00 29.70 ? 872 SER A C 1 ATOM 6416 O O . SER A 1 872 ? 3.572 -3.734 62.520 1.00 27.54 ? 872 SER A O 1 ATOM 6417 C CB . SER A 1 872 ? 4.929 -3.561 59.945 1.00 26.63 ? 872 SER A CB 1 ATOM 6418 O OG . SER A 1 872 ? 5.131 -4.928 59.620 1.00 26.71 ? 872 SER A OG 1 ATOM 6419 N N . GLN A 1 873 ? 5.491 -4.727 63.207 1.00 32.60 ? 873 GLN A N 1 ATOM 6420 C CA . GLN A 1 873 ? 4.827 -5.619 64.157 1.00 35.03 ? 873 GLN A CA 1 ATOM 6421 C C . GLN A 1 873 ? 4.065 -4.848 65.245 1.00 32.81 ? 873 GLN A C 1 ATOM 6422 O O . GLN A 1 873 ? 3.062 -5.323 65.751 1.00 32.00 ? 873 GLN A O 1 ATOM 6423 C CB . GLN A 1 873 ? 5.836 -6.605 64.758 1.00 39.35 ? 873 GLN A CB 1 ATOM 6424 C CG . GLN A 1 873 ? 6.792 -7.189 63.712 1.00 43.69 ? 873 GLN A CG 1 ATOM 6425 C CD . GLN A 1 873 ? 7.170 -8.644 63.947 1.00 49.13 ? 873 GLN A CD 1 ATOM 6426 O OE1 . GLN A 1 873 ? 6.504 -9.378 64.687 1.00 54.56 ? 873 GLN A OE1 1 ATOM 6427 N NE2 . GLN A 1 873 ? 8.241 -9.074 63.296 1.00 50.46 ? 873 GLN A NE2 1 ATOM 6428 N N . ASN A 1 874 ? 4.522 -3.642 65.565 1.00 31.76 ? 874 ASN A N 1 ATOM 6429 C CA . ASN A 1 874 ? 3.789 -2.745 66.461 1.00 30.86 ? 874 ASN A CA 1 ATOM 6430 C C . ASN A 1 874 ? 3.077 -1.579 65.748 1.00 29.78 ? 874 ASN A C 1 ATOM 6431 O O . ASN A 1 874 ? 2.781 -0.562 66.375 1.00 29.88 ? 874 ASN A O 1 ATOM 6432 C CB . ASN A 1 874 ? 4.740 -2.204 67.535 1.00 32.23 ? 874 ASN A CB 1 ATOM 6433 C CG . ASN A 1 874 ? 5.216 -3.286 68.501 1.00 34.47 ? 874 ASN A CG 1 ATOM 6434 O OD1 . ASN A 1 874 ? 4.861 -4.472 68.378 1.00 35.41 ? 874 ASN A OD1 1 ATOM 6435 N ND2 . ASN A 1 874 ? 6.026 -2.882 69.473 1.00 35.20 ? 874 ASN A ND2 1 ATOM 6436 N N . TRP A 1 875 ? 2.798 -1.712 64.450 1.00 28.05 ? 875 TRP A N 1 ATOM 6437 C CA . TRP A 1 875 ? 2.033 -0.678 63.746 1.00 27.38 ? 875 TRP A CA 1 ATOM 6438 C C . TRP A 1 875 ? 0.544 -0.948 63.912 1.00 26.92 ? 875 TRP A C 1 ATOM 6439 O O . TRP A 1 875 ? 0.139 -2.001 64.404 1.00 26.04 ? 875 TRP A O 1 ATOM 6440 C CB . TRP A 1 875 ? 2.393 -0.605 62.260 1.00 26.74 ? 875 TRP A CB 1 ATOM 6441 C CG . TRP A 1 875 ? 3.794 -0.122 61.973 1.00 26.69 ? 875 TRP A CG 1 ATOM 6442 C CD1 . TRP A 1 875 ? 4.687 0.420 62.863 1.00 27.06 ? 875 TRP A CD1 1 ATOM 6443 C CD2 . TRP A 1 875 ? 4.447 -0.108 60.702 1.00 26.27 ? 875 TRP A CD2 1 ATOM 6444 N NE1 . TRP A 1 875 ? 5.856 0.744 62.225 1.00 26.61 ? 875 TRP A NE1 1 ATOM 6445 C CE2 . TRP A 1 875 ? 5.738 0.428 60.898 1.00 26.63 ? 875 TRP A CE2 1 ATOM 6446 C CE3 . TRP A 1 875 ? 4.073 -0.507 59.416 1.00 26.00 ? 875 TRP A CE3 1 ATOM 6447 C CZ2 . TRP A 1 875 ? 6.648 0.576 59.857 1.00 26.28 ? 875 TRP A CZ2 1 ATOM 6448 C CZ3 . TRP A 1 875 ? 4.986 -0.367 58.382 1.00 25.35 ? 875 TRP A CZ3 1 ATOM 6449 C CH2 . TRP A 1 875 ? 6.252 0.172 58.607 1.00 25.90 ? 875 TRP A CH2 1 ATOM 6450 N N . LYS A 1 876 ? -0.257 0.018 63.499 1.00 26.78 ? 876 LYS A N 1 ATOM 6451 C CA . LYS A 1 876 ? -1.718 -0.078 63.552 1.00 28.10 ? 876 LYS A CA 1 ATOM 6452 C C . LYS A 1 876 ? -2.301 -0.902 62.384 1.00 27.20 ? 876 LYS A C 1 ATOM 6453 O O . LYS A 1 876 ? -1.781 -0.866 61.270 1.00 25.90 ? 876 LYS A O 1 ATOM 6454 C CB . LYS A 1 876 ? -2.278 1.347 63.540 1.00 29.94 ? 876 LYS A CB 1 ATOM 6455 C CG . LYS A 1 876 ? -3.783 1.481 63.593 1.00 32.88 ? 876 LYS A CG 1 ATOM 6456 C CD . LYS A 1 876 ? -4.168 2.943 63.391 1.00 34.29 ? 876 LYS A CD 1 ATOM 6457 C CE . LYS A 1 876 ? -5.654 3.110 63.119 1.00 35.78 ? 876 LYS A CE 1 ATOM 6458 N NZ . LYS A 1 876 ? -5.914 4.373 62.367 1.00 37.16 ? 876 LYS A NZ 1 ATOM 6459 N N . SER A 1 877 ? -3.392 -1.626 62.652 1.00 26.83 ? 877 SER A N 1 ATOM 6460 C CA . SER A 1 877 ? -4.091 -2.428 61.640 1.00 25.56 ? 877 SER A CA 1 ATOM 6461 C C . SER A 1 877 ? -5.033 -1.583 60.795 1.00 24.71 ? 877 SER A C 1 ATOM 6462 O O . SER A 1 877 ? -6.138 -1.256 61.218 1.00 25.27 ? 877 SER A O 1 ATOM 6463 C CB . SER A 1 877 ? -4.888 -3.542 62.306 1.00 25.75 ? 877 SER A CB 1 ATOM 6464 O OG . SER A 1 877 ? -4.014 -4.405 63.002 1.00 27.57 ? 877 SER A OG 1 ATOM 6465 N N . SER A 1 878 ? -4.596 -1.231 59.597 1.00 23.30 ? 878 SER A N 1 ATOM 6466 C CA . SER A 1 878 ? -5.399 -0.402 58.715 1.00 23.13 ? 878 SER A CA 1 ATOM 6467 C C . SER A 1 878 ? -5.001 -0.671 57.287 1.00 23.01 ? 878 SER A C 1 ATOM 6468 O O . SER A 1 878 ? -3.833 -0.873 56.994 1.00 23.13 ? 878 SER A O 1 ATOM 6469 C CB . SER A 1 878 ? -5.217 1.087 59.027 1.00 23.24 ? 878 SER A CB 1 ATOM 6470 O OG . SER A 1 878 ? -6.267 1.848 58.457 1.00 23.37 ? 878 SER A OG 1 ATOM 6471 N N . SER A 1 879 ? -5.994 -0.646 56.414 1.00 23.26 ? 879 SER A N 1 ATOM 6472 C CA . SER A 1 879 ? -5.841 -0.946 55.001 1.00 23.13 ? 879 SER A CA 1 ATOM 6473 C C . SER A 1 879 ? -5.882 0.338 54.153 1.00 23.04 ? 879 SER A C 1 ATOM 6474 O O . SER A 1 879 ? -6.584 1.290 54.497 1.00 22.55 ? 879 SER A O 1 ATOM 6475 C CB . SER A 1 879 ? -6.987 -1.879 54.582 1.00 23.06 ? 879 SER A CB 1 ATOM 6476 O OG . SER A 1 879 ? -7.296 -1.744 53.214 1.00 22.59 ? 879 SER A OG 1 ATOM 6477 N N . PRO A 1 880 ? -5.163 0.358 53.014 1.00 22.92 ? 880 PRO A N 1 ATOM 6478 C CA . PRO A 1 880 ? -5.356 1.501 52.114 1.00 22.81 ? 880 PRO A CA 1 ATOM 6479 C C . PRO A 1 880 ? -6.812 1.644 51.601 1.00 22.75 ? 880 PRO A C 1 ATOM 6480 O O . PRO A 1 880 ? -7.211 2.740 51.187 1.00 23.00 ? 880 PRO A O 1 ATOM 6481 C CB . PRO A 1 880 ? -4.374 1.238 50.962 1.00 22.82 ? 880 PRO A CB 1 ATOM 6482 C CG . PRO A 1 880 ? -3.596 0.020 51.325 1.00 23.05 ? 880 PRO A CG 1 ATOM 6483 C CD . PRO A 1 880 ? -4.314 -0.693 52.426 1.00 22.82 ? 880 PRO A CD 1 ATOM 6484 N N . LEU A 1 881 ? -7.587 0.557 51.651 1.00 22.33 ? 881 LEU A N 1 ATOM 6485 C CA . LEU A 1 881 ? -9.021 0.596 51.339 1.00 22.77 ? 881 LEU A CA 1 ATOM 6486 C C . LEU A 1 881 ? -9.822 1.410 52.371 1.00 22.80 ? 881 LEU A C 1 ATOM 6487 O O . LEU A 1 881 ? -10.854 1.979 52.026 1.00 23.81 ? 881 LEU A O 1 ATOM 6488 C CB . LEU A 1 881 ? -9.616 -0.817 51.228 1.00 23.15 ? 881 LEU A CB 1 ATOM 6489 C CG . LEU A 1 881 ? -9.293 -1.676 50.001 1.00 24.30 ? 881 LEU A CG 1 ATOM 6490 C CD1 . LEU A 1 881 ? -9.794 -1.013 48.735 1.00 25.70 ? 881 LEU A CD1 1 ATOM 6491 C CD2 . LEU A 1 881 ? -7.808 -1.965 49.854 1.00 25.14 ? 881 LEU A CD2 1 ATOM 6492 N N . GLU A 1 882 ? -9.353 1.464 53.618 1.00 21.35 ? 882 GLU A N 1 ATOM 6493 C CA . GLU A 1 882 ? -9.925 2.346 54.633 1.00 21.79 ? 882 GLU A CA 1 ATOM 6494 C C . GLU A 1 882 ? -9.364 3.771 54.471 1.00 20.59 ? 882 GLU A C 1 ATOM 6495 O O . GLU A 1 882 ? -10.105 4.749 54.448 1.00 19.86 ? 882 GLU A O 1 ATOM 6496 C CB . GLU A 1 882 ? -9.670 1.767 56.038 1.00 23.85 ? 882 GLU A CB 1 ATOM 6497 C CG . GLU A 1 882 ? -10.478 0.485 56.281 1.00 26.53 ? 882 GLU A CG 1 ATOM 6498 C CD . GLU A 1 882 ? -9.990 -0.424 57.428 1.00 29.72 ? 882 GLU A CD 1 ATOM 6499 O OE1 . GLU A 1 882 ? -8.760 -0.686 57.591 1.00 29.58 ? 882 GLU A OE1 1 ATOM 6500 O OE2 . GLU A 1 882 ? -10.880 -0.922 58.155 1.00 31.63 -1 882 GLU A OE2 1 ATOM 6501 N N . GLY A 1 883 ? -8.049 3.881 54.332 1.00 19.18 ? 883 GLY A N 1 ATOM 6502 C CA . GLY A 1 883 ? -7.436 5.134 53.948 1.00 18.69 ? 883 GLY A CA 1 ATOM 6503 C C . GLY A 1 883 ? -7.436 6.199 55.021 1.00 18.07 ? 883 GLY A C 1 ATOM 6504 O O . GLY A 1 883 ? -7.419 5.897 56.209 1.00 17.40 ? 883 GLY A O 1 ATOM 6505 N N . LEU A 1 884 ? -7.448 7.454 54.590 1.00 18.24 ? 884 LEU A N 1 ATOM 6506 C CA . LEU A 1 884 ? -7.263 8.595 55.494 1.00 18.66 ? 884 LEU A CA 1 ATOM 6507 C C . LEU A 1 884 ? -8.535 9.424 55.553 1.00 19.69 ? 884 LEU A C 1 ATOM 6508 O O . LEU A 1 884 ? -9.292 9.485 54.581 1.00 19.80 ? 884 LEU A O 1 ATOM 6509 C CB . LEU A 1 884 ? -6.100 9.477 55.005 1.00 18.76 ? 884 LEU A CB 1 ATOM 6510 C CG . LEU A 1 884 ? -4.765 8.807 54.644 1.00 18.73 ? 884 LEU A CG 1 ATOM 6511 C CD1 . LEU A 1 884 ? -3.769 9.840 54.155 1.00 18.87 ? 884 LEU A CD1 1 ATOM 6512 C CD2 . LEU A 1 884 ? -4.194 8.052 55.830 1.00 18.44 ? 884 LEU A CD2 1 ATOM 6513 N N . SER A 1 885 ? -8.749 10.082 56.686 1.00 21.46 ? 885 SER A N 1 ATOM 6514 C CA . SER A 1 885 ? -9.880 10.992 56.879 1.00 22.77 ? 885 SER A CA 1 ATOM 6515 C C . SER A 1 885 ? -9.467 12.486 56.918 1.00 23.88 ? 885 SER A C 1 ATOM 6516 O O . SER A 1 885 ? -10.312 13.376 57.127 1.00 23.45 ? 885 SER A O 1 ATOM 6517 C CB . SER A 1 885 ? -10.571 10.624 58.182 1.00 23.43 ? 885 SER A CB 1 ATOM 6518 O OG . SER A 1 885 ? -9.625 10.682 59.235 1.00 24.99 ? 885 SER A OG 1 ATOM 6519 N N . GLU A 1 886 ? -8.179 12.752 56.710 1.00 24.59 ? 886 GLU A N 1 ATOM 6520 C CA . GLU A 1 886 ? -7.647 14.116 56.644 1.00 25.22 ? 886 GLU A CA 1 ATOM 6521 C C . GLU A 1 886 ? -6.492 14.147 55.641 1.00 23.43 ? 886 GLU A C 1 ATOM 6522 O O . GLU A 1 886 ? -5.920 13.093 55.312 1.00 22.53 ? 886 GLU A O 1 ATOM 6523 C CB . GLU A 1 886 ? -7.171 14.580 58.027 1.00 27.29 ? 886 GLU A CB 1 ATOM 6524 C CG . GLU A 1 886 ? -6.179 13.646 58.725 1.00 30.26 ? 886 GLU A CG 1 ATOM 6525 C CD . GLU A 1 886 ? -6.815 12.356 59.249 1.00 33.43 ? 886 GLU A CD 1 ATOM 6526 O OE1 . GLU A 1 886 ? -6.498 11.261 58.708 1.00 36.80 ? 886 GLU A OE1 1 ATOM 6527 O OE2 . GLU A 1 886 ? -7.642 12.433 60.191 1.00 35.56 -1 886 GLU A OE2 1 ATOM 6528 N N . ALA A 1 887 ? -6.152 15.336 55.146 1.00 21.03 ? 887 ALA A N 1 ATOM 6529 C CA . ALA A 1 887 ? -4.987 15.478 54.273 1.00 20.33 ? 887 ALA A CA 1 ATOM 6530 C C . ALA A 1 887 ? -3.769 14.874 54.946 1.00 20.01 ? 887 ALA A C 1 ATOM 6531 O O . ALA A 1 887 ? -3.499 15.142 56.112 1.00 20.35 ? 887 ALA A O 1 ATOM 6532 C CB . ALA A 1 887 ? -4.721 16.934 53.950 1.00 20.41 ? 887 ALA A CB 1 ATOM 6533 N N . GLY A 1 888 ? -3.053 14.023 54.227 1.00 19.12 ? 888 GLY A N 1 ATOM 6534 C CA . GLY A 1 888 ? -1.800 13.518 54.738 1.00 18.37 ? 888 GLY A CA 1 ATOM 6535 C C . GLY A 1 888 ? -1.203 12.466 53.839 1.00 17.48 ? 888 GLY A C 1 ATOM 6536 O O . GLY A 1 888 ? -1.597 12.326 52.687 1.00 16.25 ? 888 GLY A O 1 ATOM 6537 N N . ILE A 1 889 ? -0.231 11.737 54.377 1.00 16.94 ? 889 ILE A N 1 ATOM 6538 C CA . ILE A 1 889 ? 0.393 10.644 53.648 1.00 16.82 ? 889 ILE A CA 1 ATOM 6539 C C . ILE A 1 889 ? 0.568 9.447 54.580 1.00 16.46 ? 889 ILE A C 1 ATOM 6540 O O . ILE A 1 889 ? 1.166 9.564 55.652 1.00 16.73 ? 889 ILE A O 1 ATOM 6541 C CB . ILE A 1 889 ? 1.735 11.057 53.003 1.00 16.53 ? 889 ILE A CB 1 ATOM 6542 C CG1 . ILE A 1 889 ? 1.583 12.402 52.288 1.00 16.47 ? 889 ILE A CG1 1 ATOM 6543 C CG2 . ILE A 1 889 ? 2.188 9.992 52.000 1.00 16.44 ? 889 ILE A CG2 1 ATOM 6544 C CD1 . ILE A 1 889 ? 2.763 12.800 51.426 1.00 16.57 ? 889 ILE A CD1 1 ATOM 6545 N N . GLY A 1 890 ? -0.003 8.317 54.176 1.00 16.25 ? 890 GLY A N 1 ATOM 6546 C CA . GLY A 1 890 ? 0.069 7.079 54.940 1.00 16.30 ? 890 GLY A CA 1 ATOM 6547 C C . GLY A 1 890 ? 0.882 6.020 54.231 1.00 15.87 ? 890 GLY A C 1 ATOM 6548 O O . GLY A 1 890 ? 1.040 6.064 53.012 1.00 15.75 ? 890 GLY A O 1 ATOM 6549 N N . PHE A 1 891 ? 1.408 5.075 55.001 1.00 15.54 ? 891 PHE A N 1 ATOM 6550 C CA . PHE A 1 891 ? 2.260 4.020 54.465 1.00 15.52 ? 891 PHE A CA 1 ATOM 6551 C C . PHE A 1 891 ? 1.697 2.698 54.932 1.00 15.56 ? 891 PHE A C 1 ATOM 6552 O O . PHE A 1 891 ? 1.511 2.492 56.142 1.00 15.24 ? 891 PHE A O 1 ATOM 6553 C CB . PHE A 1 891 ? 3.703 4.185 54.958 1.00 15.86 ? 891 PHE A CB 1 ATOM 6554 C CG . PHE A 1 891 ? 4.652 3.127 54.452 1.00 15.88 ? 891 PHE A CG 1 ATOM 6555 C CD1 . PHE A 1 891 ? 5.263 3.258 53.220 1.00 16.60 ? 891 PHE A CD1 1 ATOM 6556 C CD2 . PHE A 1 891 ? 4.931 2.003 55.205 1.00 16.34 ? 891 PHE A CD2 1 ATOM 6557 C CE1 . PHE A 1 891 ? 6.150 2.289 52.746 1.00 16.91 ? 891 PHE A CE1 1 ATOM 6558 C CE2 . PHE A 1 891 ? 5.804 1.030 54.744 1.00 16.55 ? 891 PHE A CE2 1 ATOM 6559 C CZ . PHE A 1 891 ? 6.416 1.170 53.514 1.00 16.75 ? 891 PHE A CZ 1 ATOM 6560 N N . TYR A 1 892 ? 1.436 1.801 53.984 1.00 15.80 ? 892 TYR A N 1 ATOM 6561 C CA . TYR A 1 892 ? 0.773 0.541 54.287 1.00 16.38 ? 892 TYR A CA 1 ATOM 6562 C C . TYR A 1 892 ? 1.653 -0.632 53.892 1.00 16.41 ? 892 TYR A C 1 ATOM 6563 O O . TYR A 1 892 ? 2.235 -0.632 52.819 1.00 16.54 ? 892 TYR A O 1 ATOM 6564 C CB . TYR A 1 892 ? -0.596 0.478 53.586 1.00 16.96 ? 892 TYR A CB 1 ATOM 6565 C CG . TYR A 1 892 ? -1.564 1.605 53.982 1.00 17.25 ? 892 TYR A CG 1 ATOM 6566 C CD1 . TYR A 1 892 ? -1.515 2.855 53.354 1.00 16.97 ? 892 TYR A CD1 1 ATOM 6567 C CD2 . TYR A 1 892 ? -2.544 1.410 54.968 1.00 17.50 ? 892 TYR A CD2 1 ATOM 6568 C CE1 . TYR A 1 892 ? -2.391 3.883 53.709 1.00 17.07 ? 892 TYR A CE1 1 ATOM 6569 C CE2 . TYR A 1 892 ? -3.432 2.434 55.320 1.00 17.29 ? 892 TYR A CE2 1 ATOM 6570 C CZ . TYR A 1 892 ? -3.350 3.669 54.683 1.00 17.05 ? 892 TYR A CZ 1 ATOM 6571 O OH . TYR A 1 892 ? -4.213 4.699 55.012 1.00 17.01 ? 892 TYR A OH 1 ATOM 6572 N N . SER A 1 893 ? 1.749 -1.640 54.755 1.00 16.51 ? 893 SER A N 1 ATOM 6573 C CA . SER A 1 893 ? 2.577 -2.805 54.465 1.00 16.69 ? 893 SER A CA 1 ATOM 6574 C C . SER A 1 893 ? 1.884 -4.141 54.707 1.00 17.12 ? 893 SER A C 1 ATOM 6575 O O . SER A 1 893 ? 1.252 -4.347 55.749 1.00 16.60 ? 893 SER A O 1 ATOM 6576 C CB . SER A 1 893 ? 3.853 -2.782 55.290 1.00 16.62 ? 893 SER A CB 1 ATOM 6577 O OG . SER A 1 893 ? 4.363 -4.102 55.423 1.00 16.63 ? 893 SER A OG 1 ATOM 6578 N N . ALA A 1 894 ? 2.062 -5.052 53.754 1.00 17.13 ? 894 ALA A N 1 ATOM 6579 C CA . ALA A 1 894 ? 1.640 -6.438 53.909 1.00 17.95 ? 894 ALA A CA 1 ATOM 6580 C C . ALA A 1 894 ? 2.389 -7.367 52.964 1.00 18.10 ? 894 ALA A C 1 ATOM 6581 O O . ALA A 1 894 ? 2.941 -6.946 51.935 1.00 18.33 ? 894 ALA A O 1 ATOM 6582 C CB . ALA A 1 894 ? 0.146 -6.573 53.672 1.00 18.17 ? 894 ALA A CB 1 ATOM 6583 N N . SER A 1 895 ? 2.381 -8.639 53.325 1.00 18.12 ? 895 SER A N 1 ATOM 6584 C CA . SER A 1 895 ? 2.969 -9.685 52.512 1.00 18.61 ? 895 SER A CA 1 ATOM 6585 C C . SER A 1 895 ? 1.897 -10.635 52.045 1.00 19.54 ? 895 SER A C 1 ATOM 6586 O O . SER A 1 895 ? 0.801 -10.703 52.620 1.00 19.07 ? 895 SER A O 1 ATOM 6587 C CB . SER A 1 895 ? 4.008 -10.472 53.291 1.00 18.60 ? 895 SER A CB 1 ATOM 6588 O OG . SER A 1 895 ? 3.408 -11.232 54.308 1.00 17.95 ? 895 SER A OG 1 ATOM 6589 N N . PHE A 1 896 ? 2.222 -11.363 50.985 1.00 20.11 ? 896 PHE A N 1 ATOM 6590 C CA . PHE A 1 896 ? 1.351 -12.393 50.475 1.00 20.13 ? 896 PHE A CA 1 ATOM 6591 C C . PHE A 1 896 ? 2.195 -13.486 49.858 1.00 21.48 ? 896 PHE A C 1 ATOM 6592 O O . PHE A 1 896 ? 3.313 -13.228 49.391 1.00 21.80 ? 896 PHE A O 1 ATOM 6593 C CB . PHE A 1 896 ? 0.348 -11.811 49.472 1.00 19.82 ? 896 PHE A CB 1 ATOM 6594 C CG . PHE A 1 896 ? 0.968 -11.248 48.222 1.00 19.27 ? 896 PHE A CG 1 ATOM 6595 C CD1 . PHE A 1 896 ? 1.167 -12.056 47.104 1.00 19.30 ? 896 PHE A CD1 1 ATOM 6596 C CD2 . PHE A 1 896 ? 1.299 -9.919 48.141 1.00 18.74 ? 896 PHE A CD2 1 ATOM 6597 C CE1 . PHE A 1 896 ? 1.726 -11.543 45.943 1.00 19.30 ? 896 PHE A CE1 1 ATOM 6598 C CE2 . PHE A 1 896 ? 1.854 -9.395 46.978 1.00 19.50 ? 896 PHE A CE2 1 ATOM 6599 C CZ . PHE A 1 896 ? 2.072 -10.204 45.878 1.00 19.11 ? 896 PHE A CZ 1 ATOM 6600 N N . ASP A 1 897 ? 1.671 -14.707 49.895 1.00 22.51 ? 897 ASP A N 1 ATOM 6601 C CA . ASP A 1 897 ? 2.345 -15.857 49.312 1.00 24.15 ? 897 ASP A CA 1 ATOM 6602 C C . ASP A 1 897 ? 1.772 -16.174 47.939 1.00 22.48 ? 897 ASP A C 1 ATOM 6603 O O . ASP A 1 897 ? 0.574 -16.055 47.717 1.00 21.55 ? 897 ASP A O 1 ATOM 6604 C CB . ASP A 1 897 ? 2.209 -17.084 50.227 1.00 26.52 ? 897 ASP A CB 1 ATOM 6605 C CG . ASP A 1 897 ? 2.920 -16.904 51.569 1.00 28.97 ? 897 ASP A CG 1 ATOM 6606 O OD1 . ASP A 1 897 ? 3.704 -15.939 51.725 1.00 31.76 ? 897 ASP A OD1 1 ATOM 6607 O OD2 . ASP A 1 897 ? 2.709 -17.746 52.468 1.00 30.06 -1 897 ASP A OD2 1 ATOM 6608 N N . LEU A 1 898 ? 2.648 -16.562 47.024 1.00 22.06 ? 898 LEU A N 1 ATOM 6609 C CA . LEU A 1 898 ? 2.247 -17.129 45.742 1.00 21.51 ? 898 LEU A CA 1 ATOM 6610 C C . LEU A 1 898 ? 2.794 -18.540 45.679 1.00 22.14 ? 898 LEU A C 1 ATOM 6611 O O . LEU A 1 898 ? 3.843 -18.838 46.267 1.00 21.62 ? 898 LEU A O 1 ATOM 6612 C CB . LEU A 1 898 ? 2.815 -16.305 44.598 1.00 21.34 ? 898 LEU A CB 1 ATOM 6613 C CG . LEU A 1 898 ? 2.220 -14.904 44.396 1.00 21.43 ? 898 LEU A CG 1 ATOM 6614 C CD1 . LEU A 1 898 ? 3.054 -14.083 43.421 1.00 21.01 ? 898 LEU A CD1 1 ATOM 6615 C CD2 . LEU A 1 898 ? 0.786 -15.031 43.899 1.00 21.23 ? 898 LEU A CD2 1 ATOM 6616 N N . ASP A 1 899 ? 2.085 -19.410 44.975 1.00 23.20 ? 899 ASP A N 1 ATOM 6617 C CA . ASP A 1 899 ? 2.563 -20.768 44.706 1.00 24.36 ? 899 ASP A CA 1 ATOM 6618 C C . ASP A 1 899 ? 2.163 -21.160 43.303 1.00 23.98 ? 899 ASP A C 1 ATOM 6619 O O . ASP A 1 899 ? 1.453 -22.134 43.113 1.00 23.83 ? 899 ASP A O 1 ATOM 6620 C CB . ASP A 1 899 ? 1.981 -21.770 45.717 1.00 25.43 ? 899 ASP A CB 1 ATOM 6621 C CG . ASP A 1 899 ? 2.703 -23.125 45.696 1.00 27.09 ? 899 ASP A CG 1 ATOM 6622 O OD1 . ASP A 1 899 ? 3.937 -23.174 45.482 1.00 28.15 ? 899 ASP A OD1 1 ATOM 6623 O OD2 . ASP A 1 899 ? 2.037 -24.154 45.919 1.00 30.37 -1 899 ASP A OD2 1 ATOM 6624 N N . LEU A 1 900 ? 2.603 -20.386 42.319 1.00 24.33 ? 900 LEU A N 1 ATOM 6625 C CA . LEU A 1 900 ? 2.222 -20.639 40.932 1.00 24.94 ? 900 LEU A CA 1 ATOM 6626 C C . LEU A 1 900 ? 3.022 -21.807 40.348 1.00 25.59 ? 900 LEU A C 1 ATOM 6627 O O . LEU A 1 900 ? 4.147 -22.061 40.766 1.00 26.26 ? 900 LEU A O 1 ATOM 6628 C CB . LEU A 1 900 ? 2.377 -19.374 40.098 1.00 24.88 ? 900 LEU A CB 1 ATOM 6629 C CG . LEU A 1 900 ? 1.429 -18.247 40.530 1.00 25.69 ? 900 LEU A CG 1 ATOM 6630 C CD1 . LEU A 1 900 ? 1.661 -17.004 39.699 1.00 26.18 ? 900 LEU A CD1 1 ATOM 6631 C CD2 . LEU A 1 900 ? -0.028 -18.660 40.420 1.00 25.90 ? 900 LEU A CD2 1 ATOM 6632 N N . PRO A 1 901 ? 2.430 -22.541 39.393 1.00 26.43 ? 901 PRO A N 1 ATOM 6633 C CA . PRO A 1 901 ? 3.035 -23.792 38.933 1.00 26.33 ? 901 PRO A CA 1 ATOM 6634 C C . PRO A 1 901 ? 4.266 -23.589 38.042 1.00 25.63 ? 901 PRO A C 1 ATOM 6635 O O . PRO A 1 901 ? 4.321 -22.624 37.285 1.00 23.53 ? 901 PRO A O 1 ATOM 6636 C CB . PRO A 1 901 ? 1.896 -24.445 38.149 1.00 26.60 ? 901 PRO A CB 1 ATOM 6637 C CG . PRO A 1 901 ? 1.146 -23.282 37.591 1.00 26.86 ? 901 PRO A CG 1 ATOM 6638 C CD . PRO A 1 901 ? 1.188 -22.231 38.661 1.00 26.81 ? 901 PRO A CD 1 ATOM 6639 N N . LYS A 1 902 ? 5.236 -24.501 38.130 1.00 25.42 ? 902 LYS A N 1 ATOM 6640 C CA . LYS A 1 902 ? 6.440 -24.418 37.300 1.00 25.83 ? 902 LYS A CA 1 ATOM 6641 C C . LYS A 1 902 ? 6.120 -24.697 35.847 1.00 24.68 ? 902 LYS A C 1 ATOM 6642 O O . LYS A 1 902 ? 5.208 -25.450 35.557 1.00 25.47 ? 902 LYS A O 1 ATOM 6643 C CB . LYS A 1 902 ? 7.508 -25.397 37.784 1.00 27.54 ? 902 LYS A CB 1 ATOM 6644 C CG . LYS A 1 902 ? 8.372 -24.825 38.885 1.00 28.85 ? 902 LYS A CG 1 ATOM 6645 C CD . LYS A 1 902 ? 9.217 -25.893 39.540 1.00 30.81 ? 902 LYS A CD 1 ATOM 6646 C CE . LYS A 1 902 ? 10.078 -25.293 40.644 1.00 32.16 ? 902 LYS A CE 1 ATOM 6647 N NZ . LYS A 1 902 ? 10.629 -26.356 41.525 1.00 32.89 ? 902 LYS A NZ 1 ATOM 6648 N N . GLY A 1 903 ? 6.877 -24.088 34.941 1.00 23.91 ? 903 GLY A N 1 ATOM 6649 C CA . GLY A 1 903 ? 6.685 -24.293 33.506 1.00 23.04 ? 903 GLY A CA 1 ATOM 6650 C C . GLY A 1 903 ? 5.558 -23.475 32.898 1.00 23.14 ? 903 GLY A C 1 ATOM 6651 O O . GLY A 1 903 ? 5.124 -23.756 31.781 1.00 22.40 ? 903 GLY A O 1 ATOM 6652 N N . TRP A 1 904 ? 5.084 -22.459 33.622 1.00 22.97 ? 904 TRP A N 1 ATOM 6653 C CA . TRP A 1 904 ? 4.051 -21.550 33.111 1.00 22.85 ? 904 TRP A CA 1 ATOM 6654 C C . TRP A 1 904 ? 4.511 -20.093 33.219 1.00 22.70 ? 904 TRP A C 1 ATOM 6655 O O . TRP A 1 904 ? 5.127 -19.699 34.202 1.00 22.22 ? 904 TRP A O 1 ATOM 6656 C CB . TRP A 1 904 ? 2.728 -21.747 33.855 1.00 22.97 ? 904 TRP A CB 1 ATOM 6657 C CG . TRP A 1 904 ? 2.125 -23.062 33.571 1.00 23.68 ? 904 TRP A CG 1 ATOM 6658 C CD1 . TRP A 1 904 ? 2.432 -24.254 34.171 1.00 23.60 ? 904 TRP A CD1 1 ATOM 6659 C CD2 . TRP A 1 904 ? 1.140 -23.352 32.584 1.00 23.65 ? 904 TRP A CD2 1 ATOM 6660 N NE1 . TRP A 1 904 ? 1.696 -25.265 33.617 1.00 23.90 ? 904 TRP A NE1 1 ATOM 6661 C CE2 . TRP A 1 904 ? 0.891 -24.742 32.639 1.00 24.33 ? 904 TRP A CE2 1 ATOM 6662 C CE3 . TRP A 1 904 ? 0.431 -22.573 31.664 1.00 23.72 ? 904 TRP A CE3 1 ATOM 6663 C CZ2 . TRP A 1 904 ? -0.047 -25.370 31.810 1.00 23.77 ? 904 TRP A CZ2 1 ATOM 6664 C CZ3 . TRP A 1 904 ? -0.491 -23.199 30.833 1.00 23.75 ? 904 TRP A CZ3 1 ATOM 6665 C CH2 . TRP A 1 904 ? -0.724 -24.583 30.915 1.00 23.34 ? 904 TRP A CH2 1 ATOM 6666 N N . ASP A 1 905 ? 4.219 -19.317 32.181 1.00 22.84 ? 905 ASP A N 1 ATOM 6667 C CA . ASP A 1 905 ? 4.483 -17.885 32.146 1.00 22.82 ? 905 ASP A CA 1 ATOM 6668 C C . ASP A 1 905 ? 3.130 -17.225 32.353 1.00 22.20 ? 905 ASP A C 1 ATOM 6669 O O . ASP A 1 905 ? 2.253 -17.317 31.495 1.00 21.45 ? 905 ASP A O 1 ATOM 6670 C CB . ASP A 1 905 ? 5.086 -17.488 30.793 1.00 23.68 ? 905 ASP A CB 1 ATOM 6671 C CG . ASP A 1 905 ? 5.681 -16.083 30.788 1.00 24.94 ? 905 ASP A CG 1 ATOM 6672 O OD1 . ASP A 1 905 ? 5.611 -15.378 31.822 1.00 27.21 ? 905 ASP A OD1 1 ATOM 6673 O OD2 . ASP A 1 905 ? 6.232 -15.672 29.737 1.00 24.99 -1 905 ASP A OD2 1 ATOM 6674 N N . VAL A 1 906 ? 2.964 -16.583 33.506 1.00 21.13 ? 906 VAL A N 1 ATOM 6675 C CA . VAL A 1 906 ? 1.677 -16.043 33.917 1.00 20.95 ? 906 VAL A CA 1 ATOM 6676 C C . VAL A 1 906 ? 1.817 -14.551 34.208 1.00 20.25 ? 906 VAL A C 1 ATOM 6677 O O . VAL A 1 906 ? 2.353 -14.176 35.233 1.00 21.96 ? 906 VAL A O 1 ATOM 6678 C CB . VAL A 1 906 ? 1.175 -16.779 35.171 1.00 20.91 ? 906 VAL A CB 1 ATOM 6679 C CG1 . VAL A 1 906 ? -0.214 -16.297 35.559 1.00 21.00 ? 906 VAL A CG1 1 ATOM 6680 C CG2 . VAL A 1 906 ? 1.180 -18.278 34.925 1.00 20.93 ? 906 VAL A CG2 1 ATOM 6681 N N . PRO A 1 907 ? 1.360 -13.690 33.293 1.00 19.96 ? 907 PRO A N 1 ATOM 6682 C CA . PRO A 1 907 ? 1.515 -12.254 33.545 1.00 18.98 ? 907 PRO A CA 1 ATOM 6683 C C . PRO A 1 907 ? 0.611 -11.787 34.676 1.00 18.50 ? 907 PRO A C 1 ATOM 6684 O O . PRO A 1 907 ? -0.581 -12.067 34.635 1.00 18.30 ? 907 PRO A O 1 ATOM 6685 C CB . PRO A 1 907 ? 1.083 -11.608 32.218 1.00 18.89 ? 907 PRO A CB 1 ATOM 6686 C CG . PRO A 1 907 ? 1.132 -12.709 31.207 1.00 19.62 ? 907 PRO A CG 1 ATOM 6687 C CD . PRO A 1 907 ? 0.799 -13.958 31.955 1.00 19.73 ? 907 PRO A CD 1 ATOM 6688 N N . LEU A 1 908 ? 1.170 -11.077 35.658 1.00 17.73 ? 908 LEU A N 1 ATOM 6689 C CA . LEU A 1 908 ? 0.412 -10.604 36.802 1.00 17.50 ? 908 LEU A CA 1 ATOM 6690 C C . LEU A 1 908 ? 0.346 -9.092 36.814 1.00 17.10 ? 908 LEU A C 1 ATOM 6691 O O . LEU A 1 908 ? 1.325 -8.412 36.515 1.00 16.68 ? 908 LEU A O 1 ATOM 6692 C CB . LEU A 1 908 ? 1.035 -11.099 38.119 1.00 18.11 ? 908 LEU A CB 1 ATOM 6693 C CG . LEU A 1 908 ? 0.958 -12.590 38.481 1.00 18.59 ? 908 LEU A CG 1 ATOM 6694 C CD1 . LEU A 1 908 ? 1.475 -12.848 39.892 1.00 18.61 ? 908 LEU A CD1 1 ATOM 6695 C CD2 . LEU A 1 908 ? -0.458 -13.132 38.349 1.00 18.71 ? 908 LEU A CD2 1 ATOM 6696 N N . PHE A 1 909 ? -0.817 -8.575 37.197 1.00 16.97 ? 909 PHE A N 1 ATOM 6697 C CA . PHE A 1 909 ? -1.066 -7.138 37.218 1.00 17.23 ? 909 PHE A CA 1 ATOM 6698 C C . PHE A 1 909 ? -1.590 -6.674 38.571 1.00 17.27 ? 909 PHE A C 1 ATOM 6699 O O . PHE A 1 909 ? -2.432 -7.343 39.171 1.00 17.11 ? 909 PHE A O 1 ATOM 6700 C CB . PHE A 1 909 ? -2.110 -6.768 36.157 1.00 17.11 ? 909 PHE A CB 1 ATOM 6701 C CG . PHE A 1 909 ? -1.743 -7.176 34.765 1.00 16.72 ? 909 PHE A CG 1 ATOM 6702 C CD1 . PHE A 1 909 ? -1.884 -8.492 34.357 1.00 16.46 ? 909 PHE A CD1 1 ATOM 6703 C CD2 . PHE A 1 909 ? -1.275 -6.239 33.853 1.00 16.63 ? 909 PHE A CD2 1 ATOM 6704 C CE1 . PHE A 1 909 ? -1.544 -8.876 33.073 1.00 16.37 ? 909 PHE A CE1 1 ATOM 6705 C CE2 . PHE A 1 909 ? -0.937 -6.614 32.565 1.00 16.14 ? 909 PHE A CE2 1 ATOM 6706 C CZ . PHE A 1 909 ? -1.074 -7.934 32.175 1.00 16.32 ? 909 PHE A CZ 1 ATOM 6707 N N . LEU A 1 910 ? -1.115 -5.519 39.029 1.00 17.74 ? 910 LEU A N 1 ATOM 6708 C CA . LEU A 1 910 ? -1.770 -4.786 40.122 1.00 18.78 ? 910 LEU A CA 1 ATOM 6709 C C . LEU A 1 910 ? -2.811 -3.832 39.557 1.00 18.64 ? 910 LEU A C 1 ATOM 6710 O O . LEU A 1 910 ? -2.516 -3.086 38.622 1.00 19.34 ? 910 LEU A O 1 ATOM 6711 C CB . LEU A 1 910 ? -0.777 -3.933 40.892 1.00 20.36 ? 910 LEU A CB 1 ATOM 6712 C CG . LEU A 1 910 ? 0.296 -4.630 41.699 1.00 21.49 ? 910 LEU A CG 1 ATOM 6713 C CD1 . LEU A 1 910 ? 1.332 -3.605 42.150 1.00 21.95 ? 910 LEU A CD1 1 ATOM 6714 C CD2 . LEU A 1 910 ? -0.357 -5.340 42.875 1.00 22.45 ? 910 LEU A CD2 1 ATOM 6715 N N . ASN A 1 911 ? -4.002 -3.826 40.151 1.00 18.07 ? 911 ASN A N 1 ATOM 6716 C CA . ASN A 1 911 ? -5.108 -3.019 39.674 1.00 17.52 ? 911 ASN A CA 1 ATOM 6717 C C . ASN A 1 911 ? -5.589 -2.085 40.773 1.00 17.28 ? 911 ASN A C 1 ATOM 6718 O O . ASN A 1 911 ? -5.791 -2.511 41.897 1.00 16.77 ? 911 ASN A O 1 ATOM 6719 C CB . ASN A 1 911 ? -6.247 -3.913 39.192 1.00 17.71 ? 911 ASN A CB 1 ATOM 6720 C CG . ASN A 1 911 ? -5.823 -4.836 38.071 1.00 17.86 ? 911 ASN A CG 1 ATOM 6721 O OD1 . ASN A 1 911 ? -5.795 -4.439 36.909 1.00 18.84 ? 911 ASN A OD1 1 ATOM 6722 N ND2 . ASN A 1 911 ? -5.480 -6.071 38.415 1.00 17.70 ? 911 ASN A ND2 1 ATOM 6723 N N . ILE A 1 912 ? -5.727 -0.806 40.445 1.00 17.22 ? 912 ILE A N 1 ATOM 6724 C CA . ILE A 1 912 ? -6.237 0.192 41.377 1.00 17.82 ? 912 ILE A CA 1 ATOM 6725 C C . ILE A 1 912 ? -7.526 0.736 40.774 1.00 17.90 ? 912 ILE A C 1 ATOM 6726 O O . ILE A 1 912 ? -7.526 1.259 39.665 1.00 18.41 ? 912 ILE A O 1 ATOM 6727 C CB . ILE A 1 912 ? -5.205 1.319 41.600 1.00 17.68 ? 912 ILE A CB 1 ATOM 6728 C CG1 . ILE A 1 912 ? -3.988 0.744 42.318 1.00 18.01 ? 912 ILE A CG1 1 ATOM 6729 C CG2 . ILE A 1 912 ? -5.787 2.480 42.404 1.00 17.20 ? 912 ILE A CG2 1 ATOM 6730 C CD1 . ILE A 1 912 ? -2.841 1.727 42.441 1.00 18.43 ? 912 ILE A CD1 1 ATOM 6731 N N . GLY A 1 913 ? -8.633 0.593 41.480 1.00 18.41 ? 913 GLY A N 1 ATOM 6732 C CA . GLY A 1 913 ? -9.934 0.883 40.871 1.00 19.05 ? 913 GLY A CA 1 ATOM 6733 C C . GLY A 1 913 ? -10.191 2.362 40.632 1.00 19.44 ? 913 GLY A C 1 ATOM 6734 O O . GLY A 1 913 ? -9.735 3.222 41.398 1.00 18.93 ? 913 GLY A O 1 ATOM 6735 N N . ASN A 1 914 ? -10.927 2.648 39.565 1.00 20.18 ? 914 ASN A N 1 ATOM 6736 C CA . ASN A 1 914 ? -11.334 4.012 39.255 1.00 21.58 ? 914 ASN A CA 1 ATOM 6737 C C . ASN A 1 914 ? -12.668 4.019 38.531 1.00 23.23 ? 914 ASN A C 1 ATOM 6738 O O . ASN A 1 914 ? -12.804 4.626 37.475 1.00 23.72 ? 914 ASN A O 1 ATOM 6739 C CB . ASN A 1 914 ? -10.280 4.696 38.398 1.00 20.60 ? 914 ASN A CB 1 ATOM 6740 C CG . ASN A 1 914 ? -10.433 6.211 38.375 1.00 20.17 ? 914 ASN A CG 1 ATOM 6741 O OD1 . ASN A 1 914 ? -10.622 6.846 39.414 1.00 19.35 ? 914 ASN A OD1 1 ATOM 6742 N ND2 . ASN A 1 914 ? -10.341 6.798 37.171 1.00 19.74 ? 914 ASN A ND2 1 ATOM 6743 N N . SER A 1 915 ? -13.646 3.317 39.092 1.00 25.33 ? 915 SER A N 1 ATOM 6744 C CA . SER A 1 915 ? -14.938 3.157 38.434 1.00 27.92 ? 915 SER A CA 1 ATOM 6745 C C . SER A 1 915 ? -15.761 4.437 38.453 1.00 28.64 ? 915 SER A C 1 ATOM 6746 O O . SER A 1 915 ? -16.658 4.597 37.642 1.00 29.02 ? 915 SER A O 1 ATOM 6747 C CB . SER A 1 915 ? -15.737 2.033 39.076 1.00 28.49 ? 915 SER A CB 1 ATOM 6748 O OG . SER A 1 915 ? -16.105 2.401 40.389 1.00 31.76 ? 915 SER A OG 1 ATOM 6749 N N . THR A 1 916 ? -15.452 5.344 39.373 1.00 30.05 ? 916 THR A N 1 ATOM 6750 C CA . THR A 1 916 ? -16.174 6.607 39.489 1.00 30.56 ? 916 THR A CA 1 ATOM 6751 C C . THR A 1 916 ? -15.178 7.734 39.747 1.00 29.24 ? 916 THR A C 1 ATOM 6752 O O . THR A 1 916 ? -14.060 7.481 40.191 1.00 29.51 ? 916 THR A O 1 ATOM 6753 C CB . THR A 1 916 ? -17.252 6.525 40.606 1.00 32.75 ? 916 THR A CB 1 ATOM 6754 O OG1 . THR A 1 916 ? -18.135 7.658 40.534 1.00 35.68 ? 916 THR A OG1 1 ATOM 6755 C CG2 . THR A 1 916 ? -16.620 6.431 42.005 1.00 32.34 ? 916 THR A CG2 1 ATOM 6756 N N . THR A 1 917 ? -15.580 8.965 39.434 1.00 27.28 ? 917 THR A N 1 ATOM 6757 C CA . THR A 1 917 ? -14.734 10.139 39.628 1.00 26.20 ? 917 THR A CA 1 ATOM 6758 C C . THR A 1 917 ? -14.237 10.192 41.077 1.00 25.48 ? 917 THR A C 1 ATOM 6759 O O . THR A 1 917 ? -15.047 10.250 42.005 1.00 25.50 ? 917 THR A O 1 ATOM 6760 C CB . THR A 1 917 ? -15.491 11.435 39.283 1.00 26.87 ? 917 THR A CB 1 ATOM 6761 O OG1 . THR A 1 917 ? -15.992 11.350 37.945 1.00 26.49 ? 917 THR A OG1 1 ATOM 6762 C CG2 . THR A 1 917 ? -14.569 12.655 39.387 1.00 27.50 ? 917 THR A CG2 1 ATOM 6763 N N . PRO A 1 918 ? -12.906 10.149 41.282 1.00 23.70 ? 918 PRO A N 1 ATOM 6764 C CA . PRO A 1 918 ? -12.389 10.053 42.646 1.00 22.82 ? 918 PRO A CA 1 ATOM 6765 C C . PRO A 1 918 ? -12.005 11.412 43.224 1.00 21.09 ? 918 PRO A C 1 ATOM 6766 O O . PRO A 1 918 ? -11.980 12.403 42.502 1.00 20.13 ? 918 PRO A O 1 ATOM 6767 C CB . PRO A 1 918 ? -11.136 9.197 42.460 1.00 23.01 ? 918 PRO A CB 1 ATOM 6768 C CG . PRO A 1 918 ? -10.616 9.635 41.114 1.00 23.40 ? 918 PRO A CG 1 ATOM 6769 C CD . PRO A 1 918 ? -11.822 10.007 40.285 1.00 23.73 ? 918 PRO A CD 1 ATOM 6770 N N . SER A 1 919 ? -11.716 11.447 44.521 1.00 19.84 ? 919 SER A N 1 ATOM 6771 C CA . SER A 1 919 ? -11.053 12.594 45.115 1.00 19.31 ? 919 SER A CA 1 ATOM 6772 C C . SER A 1 919 ? -9.568 12.505 44.742 1.00 18.83 ? 919 SER A C 1 ATOM 6773 O O . SER A 1 919 ? -9.081 11.427 44.400 1.00 19.37 ? 919 SER A O 1 ATOM 6774 C CB . SER A 1 919 ? -11.242 12.610 46.637 1.00 19.50 ? 919 SER A CB 1 ATOM 6775 O OG . SER A 1 919 ? -10.778 11.411 47.245 1.00 18.52 ? 919 SER A OG 1 ATOM 6776 N N . PRO A 1 920 ? -8.853 13.635 44.788 1.00 18.25 ? 920 PRO A N 1 ATOM 6777 C CA . PRO A 1 920 ? -7.436 13.645 44.396 1.00 17.64 ? 920 PRO A CA 1 ATOM 6778 C C . PRO A 1 920 ? -6.489 12.941 45.371 1.00 17.05 ? 920 PRO A C 1 ATOM 6779 O O . PRO A 1 920 ? -6.285 13.413 46.494 1.00 16.77 ? 920 PRO A O 1 ATOM 6780 C CB . PRO A 1 920 ? -7.094 15.135 44.283 1.00 17.68 ? 920 PRO A CB 1 ATOM 6781 C CG . PRO A 1 920 ? -8.196 15.870 44.981 1.00 18.17 ? 920 PRO A CG 1 ATOM 6782 C CD . PRO A 1 920 ? -9.404 14.991 44.986 1.00 18.23 ? 920 PRO A CD 1 ATOM 6783 N N . TYR A 1 921 ? -5.921 11.814 44.937 1.00 16.23 ? 921 TYR A N 1 ATOM 6784 C CA . TYR A 1 921 ? -4.865 11.151 45.694 1.00 15.72 ? 921 TYR A CA 1 ATOM 6785 C C . TYR A 1 921 ? -3.743 10.624 44.804 1.00 15.75 ? 921 TYR A C 1 ATOM 6786 O O . TYR A 1 921 ? -3.937 10.426 43.591 1.00 15.67 ? 921 TYR A O 1 ATOM 6787 C CB . TYR A 1 921 ? -5.415 10.036 46.610 1.00 15.83 ? 921 TYR A CB 1 ATOM 6788 C CG . TYR A 1 921 ? -6.299 8.979 45.971 1.00 15.78 ? 921 TYR A CG 1 ATOM 6789 C CD1 . TYR A 1 921 ? -5.759 7.820 45.433 1.00 15.78 ? 921 TYR A CD1 1 ATOM 6790 C CD2 . TYR A 1 921 ? -7.690 9.125 45.952 1.00 16.33 ? 921 TYR A CD2 1 ATOM 6791 C CE1 . TYR A 1 921 ? -6.567 6.846 44.862 1.00 16.21 ? 921 TYR A CE1 1 ATOM 6792 C CE2 . TYR A 1 921 ? -8.510 8.153 45.393 1.00 16.42 ? 921 TYR A CE2 1 ATOM 6793 C CZ . TYR A 1 921 ? -7.946 7.025 44.842 1.00 16.46 ? 921 TYR A CZ 1 ATOM 6794 O OH . TYR A 1 921 ? -8.761 6.073 44.284 1.00 17.85 ? 921 TYR A OH 1 ATOM 6795 N N . ARG A 1 922 ? -2.571 10.423 45.422 1.00 15.32 ? 922 ARG A N 1 ATOM 6796 C CA . ARG A 1 922 ? -1.399 9.882 44.751 1.00 15.25 ? 922 ARG A CA 1 ATOM 6797 C C . ARG A 1 922 ? -0.882 8.635 45.452 1.00 15.17 ? 922 ARG A C 1 ATOM 6798 O O . ARG A 1 922 ? -0.826 8.564 46.682 1.00 14.79 ? 922 ARG A O 1 ATOM 6799 C CB . ARG A 1 922 ? -0.309 10.951 44.637 1.00 15.41 ? 922 ARG A CB 1 ATOM 6800 C CG . ARG A 1 922 ? -0.679 11.982 43.579 1.00 15.78 ? 922 ARG A CG 1 ATOM 6801 C CD . ARG A 1 922 ? 0.182 13.222 43.526 1.00 15.78 ? 922 ARG A CD 1 ATOM 6802 N NE . ARG A 1 922 ? -0.470 14.178 42.631 1.00 15.99 ? 922 ARG A NE 1 ATOM 6803 C CZ . ARG A 1 922 ? -0.006 14.591 41.452 1.00 16.04 ? 922 ARG A CZ 1 ATOM 6804 N NH1 . ARG A 1 922 ? 1.174 14.195 40.985 1.00 16.13 ? 922 ARG A NH1 1 ATOM 6805 N NH2 . ARG A 1 922 ? -0.734 15.435 40.738 1.00 16.10 ? 922 ARG A NH2 1 ATOM 6806 N N . VAL A 1 923 ? -0.515 7.644 44.656 1.00 15.07 ? 923 VAL A N 1 ATOM 6807 C CA . VAL A 1 923 ? -0.130 6.351 45.175 1.00 15.58 ? 923 VAL A CA 1 ATOM 6808 C C . VAL A 1 923 ? 1.170 5.888 44.537 1.00 15.79 ? 923 VAL A C 1 ATOM 6809 O O . VAL A 1 923 ? 1.381 6.060 43.329 1.00 15.72 ? 923 VAL A O 1 ATOM 6810 C CB . VAL A 1 923 ? -1.224 5.310 44.906 1.00 16.02 ? 923 VAL A CB 1 ATOM 6811 C CG1 . VAL A 1 923 ? -0.811 3.929 45.424 1.00 16.12 ? 923 VAL A CG1 1 ATOM 6812 C CG2 . VAL A 1 923 ? -2.536 5.778 45.527 1.00 16.49 ? 923 VAL A CG2 1 ATOM 6813 N N . GLN A 1 924 ? 2.048 5.333 45.372 1.00 15.85 ? 924 GLN A N 1 ATOM 6814 C CA . GLN A 1 924 ? 3.244 4.640 44.922 1.00 15.30 ? 924 GLN A CA 1 ATOM 6815 C C . GLN A 1 924 ? 3.139 3.243 45.497 1.00 15.05 ? 924 GLN A C 1 ATOM 6816 O O . GLN A 1 924 ? 2.783 3.092 46.662 1.00 14.60 ? 924 GLN A O 1 ATOM 6817 C CB . GLN A 1 924 ? 4.524 5.282 45.460 1.00 15.32 ? 924 GLN A CB 1 ATOM 6818 C CG . GLN A 1 924 ? 4.713 6.769 45.223 1.00 15.76 ? 924 GLN A CG 1 ATOM 6819 C CD . GLN A 1 924 ? 5.979 7.292 45.890 1.00 15.79 ? 924 GLN A CD 1 ATOM 6820 O OE1 . GLN A 1 924 ? 6.977 7.568 45.234 1.00 15.82 ? 924 GLN A OE1 1 ATOM 6821 N NE2 . GLN A 1 924 ? 5.945 7.397 47.209 1.00 16.30 ? 924 GLN A NE2 1 ATOM 6822 N N . VAL A 1 925 ? 3.470 2.232 44.694 1.00 14.87 ? 925 VAL A N 1 ATOM 6823 C CA . VAL A 1 925 ? 3.541 0.845 45.174 1.00 14.52 ? 925 VAL A CA 1 ATOM 6824 C C . VAL A 1 925 ? 4.937 0.247 44.948 1.00 14.69 ? 925 VAL A C 1 ATOM 6825 O O . VAL A 1 925 ? 5.425 0.221 43.817 1.00 15.41 ? 925 VAL A O 1 ATOM 6826 C CB . VAL A 1 925 ? 2.512 -0.056 44.461 1.00 14.22 ? 925 VAL A CB 1 ATOM 6827 C CG1 . VAL A 1 925 ? 2.495 -1.440 45.090 1.00 14.33 ? 925 VAL A CG1 1 ATOM 6828 C CG2 . VAL A 1 925 ? 1.126 0.571 44.500 1.00 14.36 ? 925 VAL A CG2 1 ATOM 6829 N N . TYR A 1 926 ? 5.566 -0.218 46.025 1.00 14.82 ? 926 TYR A N 1 ATOM 6830 C CA . TYR A 1 926 ? 6.818 -0.948 45.967 1.00 15.37 ? 926 TYR A CA 1 ATOM 6831 C C . TYR A 1 926 ? 6.545 -2.441 46.141 1.00 15.39 ? 926 TYR A C 1 ATOM 6832 O O . TYR A 1 926 ? 5.918 -2.848 47.132 1.00 15.21 ? 926 TYR A O 1 ATOM 6833 C CB . TYR A 1 926 ? 7.759 -0.509 47.093 1.00 15.92 ? 926 TYR A CB 1 ATOM 6834 C CG . TYR A 1 926 ? 8.209 0.929 47.051 1.00 15.81 ? 926 TYR A CG 1 ATOM 6835 C CD1 . TYR A 1 926 ? 7.410 1.939 47.560 1.00 16.14 ? 926 TYR A CD1 1 ATOM 6836 C CD2 . TYR A 1 926 ? 9.449 1.264 46.537 1.00 15.67 ? 926 TYR A CD2 1 ATOM 6837 C CE1 . TYR A 1 926 ? 7.830 3.261 47.537 1.00 16.48 ? 926 TYR A CE1 1 ATOM 6838 C CE2 . TYR A 1 926 ? 9.882 2.565 46.506 1.00 15.97 ? 926 TYR A CE2 1 ATOM 6839 C CZ . TYR A 1 926 ? 9.077 3.569 47.002 1.00 16.35 ? 926 TYR A CZ 1 ATOM 6840 O OH . TYR A 1 926 ? 9.520 4.875 46.956 1.00 15.90 ? 926 TYR A OH 1 ATOM 6841 N N . VAL A 1 927 ? 7.024 -3.239 45.185 1.00 15.23 ? 927 VAL A N 1 ATOM 6842 C CA . VAL A 1 927 ? 6.908 -4.706 45.225 1.00 14.99 ? 927 VAL A CA 1 ATOM 6843 C C . VAL A 1 927 ? 8.296 -5.251 45.573 1.00 14.91 ? 927 VAL A C 1 ATOM 6844 O O . VAL A 1 927 ? 9.226 -5.107 44.792 1.00 15.17 ? 927 VAL A O 1 ATOM 6845 C CB . VAL A 1 927 ? 6.428 -5.272 43.865 1.00 14.77 ? 927 VAL A CB 1 ATOM 6846 C CG1 . VAL A 1 927 ? 6.270 -6.782 43.915 1.00 15.20 ? 927 VAL A CG1 1 ATOM 6847 C CG2 . VAL A 1 927 ? 5.108 -4.647 43.459 1.00 14.74 ? 927 VAL A CG2 1 ATOM 6848 N N . ASN A 1 928 ? 8.433 -5.840 46.762 1.00 14.74 ? 928 ASN A N 1 ATOM 6849 C CA . ASN A 1 928 ? 9.714 -6.301 47.279 1.00 14.62 ? 928 ASN A CA 1 ATOM 6850 C C . ASN A 1 928 ? 10.831 -5.257 47.227 1.00 14.38 ? 928 ASN A C 1 ATOM 6851 O O . ASN A 1 928 ? 12.003 -5.596 46.996 1.00 14.18 ? 928 ASN A O 1 ATOM 6852 C CB . ASN A 1 928 ? 10.136 -7.595 46.578 1.00 15.09 ? 928 ASN A CB 1 ATOM 6853 C CG . ASN A 1 928 ? 9.180 -8.730 46.861 1.00 15.39 ? 928 ASN A CG 1 ATOM 6854 O OD1 . ASN A 1 928 ? 8.742 -8.907 47.997 1.00 16.13 ? 928 ASN A OD1 1 ATOM 6855 N ND2 . ASN A 1 928 ? 8.822 -9.480 45.833 1.00 15.41 ? 928 ASN A ND2 1 ATOM 6856 N N . GLY A 1 929 ? 10.456 -3.996 47.475 1.00 13.81 ? 929 GLY A N 1 ATOM 6857 C CA . GLY A 1 929 ? 11.392 -2.875 47.485 1.00 13.72 ? 929 GLY A CA 1 ATOM 6858 C C . GLY A 1 929 ? 11.472 -2.083 46.188 1.00 13.93 ? 929 GLY A C 1 ATOM 6859 O O . GLY A 1 929 ? 11.950 -0.951 46.203 1.00 13.71 ? 929 GLY A O 1 ATOM 6860 N N . TYR A 1 930 ? 10.999 -2.677 45.081 1.00 13.96 ? 930 TYR A N 1 ATOM 6861 C CA . TYR A 1 930 ? 11.037 -2.062 43.755 1.00 14.11 ? 930 TYR A CA 1 ATOM 6862 C C . TYR A 1 930 ? 9.755 -1.323 43.430 1.00 14.63 ? 930 TYR A C 1 ATOM 6863 O O . TYR A 1 930 ? 8.673 -1.920 43.417 1.00 15.04 ? 930 TYR A O 1 ATOM 6864 C CB . TYR A 1 930 ? 11.249 -3.132 42.700 1.00 14.04 ? 930 TYR A CB 1 ATOM 6865 C CG . TYR A 1 930 ? 12.599 -3.786 42.795 1.00 14.36 ? 930 TYR A CG 1 ATOM 6866 C CD1 . TYR A 1 930 ? 12.807 -4.911 43.606 1.00 14.48 ? 930 TYR A CD1 1 ATOM 6867 C CD2 . TYR A 1 930 ? 13.676 -3.276 42.094 1.00 14.56 ? 930 TYR A CD2 1 ATOM 6868 C CE1 . TYR A 1 930 ? 14.060 -5.493 43.704 1.00 14.60 ? 930 TYR A CE1 1 ATOM 6869 C CE2 . TYR A 1 930 ? 14.925 -3.859 42.170 1.00 14.81 ? 930 TYR A CE2 1 ATOM 6870 C CZ . TYR A 1 930 ? 15.114 -4.965 42.967 1.00 14.99 ? 930 TYR A CZ 1 ATOM 6871 O OH . TYR A 1 930 ? 16.372 -5.528 43.016 1.00 15.73 ? 930 TYR A OH 1 ATOM 6872 N N . GLN A 1 931 ? 9.866 -0.025 43.159 1.00 14.69 ? 931 GLN A N 1 ATOM 6873 C CA . GLN A 1 931 ? 8.683 0.765 42.844 1.00 14.74 ? 931 GLN A CA 1 ATOM 6874 C C . GLN A 1 931 ? 8.211 0.438 41.442 1.00 14.05 ? 931 GLN A C 1 ATOM 6875 O O . GLN A 1 931 ? 8.945 0.669 40.495 1.00 13.83 ? 931 GLN A O 1 ATOM 6876 C CB . GLN A 1 931 ? 8.951 2.265 42.988 1.00 14.92 ? 931 GLN A CB 1 ATOM 6877 C CG . GLN A 1 931 ? 7.684 3.118 42.946 1.00 15.28 ? 931 GLN A CG 1 ATOM 6878 C CD . GLN A 1 931 ? 7.504 3.874 41.641 1.00 15.77 ? 931 GLN A CD 1 ATOM 6879 O OE1 . GLN A 1 931 ? 7.824 5.079 41.535 1.00 16.89 ? 931 GLN A OE1 1 ATOM 6880 N NE2 . GLN A 1 931 ? 6.997 3.186 40.641 1.00 15.50 ? 931 GLN A NE2 1 ATOM 6881 N N . TYR A 1 932 ? 6.984 -0.086 41.320 1.00 13.61 ? 932 TYR A N 1 ATOM 6882 C CA . TYR A 1 932 ? 6.432 -0.526 40.024 1.00 13.37 ? 932 TYR A CA 1 ATOM 6883 C C . TYR A 1 932 ? 5.036 0.042 39.708 1.00 13.13 ? 932 TYR A C 1 ATOM 6884 O O . TYR A 1 932 ? 4.316 -0.481 38.854 1.00 12.56 ? 932 TYR A O 1 ATOM 6885 C CB . TYR A 1 932 ? 6.434 -2.058 39.959 1.00 13.67 ? 932 TYR A CB 1 ATOM 6886 C CG . TYR A 1 932 ? 7.551 -2.608 39.116 1.00 13.72 ? 932 TYR A CG 1 ATOM 6887 C CD1 . TYR A 1 932 ? 8.838 -2.782 39.638 1.00 13.82 ? 932 TYR A CD1 1 ATOM 6888 C CD2 . TYR A 1 932 ? 7.325 -2.945 37.787 1.00 13.85 ? 932 TYR A CD2 1 ATOM 6889 C CE1 . TYR A 1 932 ? 9.871 -3.279 38.846 1.00 13.80 ? 932 TYR A CE1 1 ATOM 6890 C CE2 . TYR A 1 932 ? 8.337 -3.448 36.993 1.00 13.81 ? 932 TYR A CE2 1 ATOM 6891 C CZ . TYR A 1 932 ? 9.597 -3.605 37.520 1.00 13.81 ? 932 TYR A CZ 1 ATOM 6892 O OH . TYR A 1 932 ? 10.553 -4.105 36.710 1.00 14.30 ? 932 TYR A OH 1 ATOM 6893 N N . ALA A 1 933 ? 4.682 1.134 40.383 1.00 12.92 ? 933 ALA A N 1 ATOM 6894 C CA . ALA A 1 933 ? 3.457 1.846 40.118 1.00 12.91 ? 933 ALA A CA 1 ATOM 6895 C C . ALA A 1 933 ? 3.516 3.244 40.720 1.00 13.01 ? 933 ALA A C 1 ATOM 6896 O O . ALA A 1 933 ? 3.820 3.392 41.885 1.00 12.65 ? 933 ALA A O 1 ATOM 6897 C CB . ALA A 1 933 ? 2.279 1.086 40.696 1.00 12.92 ? 933 ALA A CB 1 ATOM 6898 N N . LYS A 1 934 ? 3.263 4.243 39.882 1.00 13.71 ? 934 LYS A N 1 ATOM 6899 C CA . LYS A 1 934 ? 2.929 5.586 40.290 1.00 14.86 ? 934 LYS A CA 1 ATOM 6900 C C . LYS A 1 934 ? 1.540 5.916 39.714 1.00 14.46 ? 934 LYS A C 1 ATOM 6901 O O . LYS A 1 934 ? 1.293 5.751 38.509 1.00 14.48 ? 934 LYS A O 1 ATOM 6902 C CB . LYS A 1 934 ? 3.981 6.569 39.791 1.00 16.38 ? 934 LYS A CB 1 ATOM 6903 C CG . LYS A 1 934 ? 3.984 7.912 40.512 1.00 17.65 ? 934 LYS A CG 1 ATOM 6904 C CD . LYS A 1 934 ? 5.212 8.730 40.116 1.00 19.33 ? 934 LYS A CD 1 ATOM 6905 C CE . LYS A 1 934 ? 5.254 10.097 40.803 1.00 20.84 ? 934 LYS A CE 1 ATOM 6906 N NZ . LYS A 1 934 ? 6.632 10.715 40.824 1.00 21.41 ? 934 LYS A NZ 1 ATOM 6907 N N . TYR A 1 935 ? 0.637 6.362 40.586 1.00 14.26 ? 935 TYR A N 1 ATOM 6908 C CA . TYR A 1 935 ? -0.791 6.505 40.268 1.00 14.08 ? 935 TYR A CA 1 ATOM 6909 C C . TYR A 1 935 ? -1.279 7.875 40.707 1.00 13.80 ? 935 TYR A C 1 ATOM 6910 O O . TYR A 1 935 ? -1.068 8.269 41.844 1.00 13.83 ? 935 TYR A O 1 ATOM 6911 C CB . TYR A 1 935 ? -1.565 5.428 41.016 1.00 13.83 ? 935 TYR A CB 1 ATOM 6912 C CG . TYR A 1 935 ? -3.054 5.365 40.757 1.00 13.77 ? 935 TYR A CG 1 ATOM 6913 C CD1 . TYR A 1 935 ? -3.565 4.580 39.721 1.00 13.88 ? 935 TYR A CD1 1 ATOM 6914 C CD2 . TYR A 1 935 ? -3.959 6.038 41.572 1.00 13.64 ? 935 TYR A CD2 1 ATOM 6915 C CE1 . TYR A 1 935 ? -4.927 4.502 39.491 1.00 13.59 ? 935 TYR A CE1 1 ATOM 6916 C CE2 . TYR A 1 935 ? -5.330 5.955 41.352 1.00 13.64 ? 935 TYR A CE2 1 ATOM 6917 C CZ . TYR A 1 935 ? -5.804 5.188 40.304 1.00 13.75 ? 935 TYR A CZ 1 ATOM 6918 O OH . TYR A 1 935 ? -7.159 5.077 40.069 1.00 14.39 ? 935 TYR A OH 1 ATOM 6919 N N . ILE A 1 936 ? -1.900 8.606 39.797 1.00 13.57 ? 936 ILE A N 1 ATOM 6920 C CA . ILE A 1 936 ? -2.558 9.849 40.131 1.00 13.75 ? 936 ILE A CA 1 ATOM 6921 C C . ILE A 1 936 ? -4.050 9.690 39.836 1.00 14.33 ? 936 ILE A C 1 ATOM 6922 O O . ILE A 1 936 ? -4.451 9.607 38.660 1.00 14.06 ? 936 ILE A O 1 ATOM 6923 C CB . ILE A 1 936 ? -2.015 11.034 39.325 1.00 13.67 ? 936 ILE A CB 1 ATOM 6924 C CG1 . ILE A 1 936 ? -0.474 11.104 39.416 1.00 14.14 ? 936 ILE A CG1 1 ATOM 6925 C CG2 . ILE A 1 936 ? -2.616 12.324 39.860 1.00 13.48 ? 936 ILE A CG2 1 ATOM 6926 C CD1 . ILE A 1 936 ? 0.164 12.019 38.376 1.00 13.93 ? 936 ILE A CD1 1 ATOM 6927 N N . SER A 1 937 ? -4.861 9.650 40.896 1.00 14.25 ? 937 SER A N 1 ATOM 6928 C CA . SER A 1 937 ? -6.297 9.385 40.754 1.00 14.63 ? 937 SER A CA 1 ATOM 6929 C C . SER A 1 937 ? -6.960 10.331 39.767 1.00 14.55 ? 937 SER A C 1 ATOM 6930 O O . SER A 1 937 ? -7.750 9.887 38.947 1.00 15.05 ? 937 SER A O 1 ATOM 6931 C CB . SER A 1 937 ? -7.023 9.476 42.100 1.00 14.65 ? 937 SER A CB 1 ATOM 6932 O OG . SER A 1 937 ? -7.027 10.810 42.608 1.00 15.26 ? 937 SER A OG 1 ATOM 6933 N N . ASN A 1 938 ? -6.636 11.621 39.841 1.00 14.18 ? 938 ASN A N 1 ATOM 6934 C CA . ASN A 1 938 ? -7.349 12.638 39.044 1.00 14.08 ? 938 ASN A CA 1 ATOM 6935 C C . ASN A 1 938 ? -6.800 12.882 37.638 1.00 13.78 ? 938 ASN A C 1 ATOM 6936 O O . ASN A 1 938 ? -7.367 13.689 36.908 1.00 13.36 ? 938 ASN A O 1 ATOM 6937 C CB . ASN A 1 938 ? -7.451 13.995 39.782 1.00 14.24 ? 938 ASN A CB 1 ATOM 6938 C CG . ASN A 1 938 ? -6.120 14.462 40.371 1.00 14.63 ? 938 ASN A CG 1 ATOM 6939 O OD1 . ASN A 1 938 ? -5.453 13.711 41.106 1.00 15.34 ? 938 ASN A OD1 1 ATOM 6940 N ND2 . ASN A 1 938 ? -5.735 15.701 40.071 1.00 14.17 ? 938 ASN A ND2 1 ATOM 6941 N N . ILE A 1 939 ? -5.729 12.189 37.245 1.00 13.72 ? 939 ILE A N 1 ATOM 6942 C CA . ILE A 1 939 ? -5.097 12.441 35.940 1.00 13.81 ? 939 ILE A CA 1 ATOM 6943 C C . ILE A 1 939 ? -4.973 11.201 35.052 1.00 13.86 ? 939 ILE A C 1 ATOM 6944 O O . ILE A 1 939 ? -5.211 11.290 33.846 1.00 13.76 ? 939 ILE A O 1 ATOM 6945 C CB . ILE A 1 939 ? -3.738 13.144 36.115 1.00 14.06 ? 939 ILE A CB 1 ATOM 6946 C CG1 . ILE A 1 939 ? -3.935 14.447 36.887 1.00 14.31 ? 939 ILE A CG1 1 ATOM 6947 C CG2 . ILE A 1 939 ? -3.110 13.439 34.765 1.00 14.49 ? 939 ILE A CG2 1 ATOM 6948 C CD1 . ILE A 1 939 ? -2.693 15.313 37.026 1.00 14.61 ? 939 ILE A CD1 1 ATOM 6949 N N . GLY A 1 940 ? -4.588 10.059 35.624 1.00 13.85 ? 940 GLY A N 1 ATOM 6950 C CA . GLY A 1 940 ? -4.569 8.802 34.876 1.00 13.94 ? 940 GLY A CA 1 ATOM 6951 C C . GLY A 1 940 ? -3.537 8.755 33.758 1.00 14.41 ? 940 GLY A C 1 ATOM 6952 O O . GLY A 1 940 ? -2.591 9.555 33.753 1.00 14.75 ? 940 GLY A O 1 ATOM 6953 N N . PRO A 1 941 ? -3.690 7.818 32.802 1.00 14.22 ? 941 PRO A N 1 ATOM 6954 C CA . PRO A 1 941 ? -4.745 6.845 32.612 1.00 14.60 ? 941 PRO A CA 1 ATOM 6955 C C . PRO A 1 941 ? -4.498 5.459 33.213 1.00 15.24 ? 941 PRO A C 1 ATOM 6956 O O . PRO A 1 941 ? -5.362 4.609 33.111 1.00 15.69 ? 941 PRO A O 1 ATOM 6957 C CB . PRO A 1 941 ? -4.776 6.708 31.094 1.00 14.61 ? 941 PRO A CB 1 ATOM 6958 C CG . PRO A 1 941 ? -3.334 6.773 30.726 1.00 14.59 ? 941 PRO A CG 1 ATOM 6959 C CD . PRO A 1 941 ? -2.736 7.780 31.679 1.00 14.47 ? 941 PRO A CD 1 ATOM 6960 N N . GLN A 1 942 ? -3.340 5.201 33.815 1.00 15.60 ? 942 GLN A N 1 ATOM 6961 C CA . GLN A 1 942 ? -3.007 3.824 34.172 1.00 15.09 ? 942 GLN A CA 1 ATOM 6962 C C . GLN A 1 942 ? -3.718 3.373 35.449 1.00 14.95 ? 942 GLN A C 1 ATOM 6963 O O . GLN A 1 942 ? -3.590 4.008 36.493 1.00 14.42 ? 942 GLN A O 1 ATOM 6964 C CB . GLN A 1 942 ? -1.485 3.639 34.292 1.00 14.96 ? 942 GLN A CB 1 ATOM 6965 C CG . GLN A 1 942 ? -1.046 2.173 34.319 1.00 14.72 ? 942 GLN A CG 1 ATOM 6966 C CD . GLN A 1 942 ? 0.462 2.008 34.238 1.00 14.97 ? 942 GLN A CD 1 ATOM 6967 O OE1 . GLN A 1 942 ? 1.202 2.993 34.285 1.00 14.99 ? 942 GLN A OE1 1 ATOM 6968 N NE2 . GLN A 1 942 ? 0.929 0.758 34.126 1.00 14.64 ? 942 GLN A NE2 1 ATOM 6969 N N . THR A 1 943 ? -4.481 2.281 35.334 1.00 14.98 ? 943 THR A N 1 ATOM 6970 C CA . THR A 1 943 ? -5.093 1.599 36.485 1.00 15.18 ? 943 THR A CA 1 ATOM 6971 C C . THR A 1 943 ? -4.599 0.152 36.636 1.00 15.14 ? 943 THR A C 1 ATOM 6972 O O . THR A 1 943 ? -4.784 -0.465 37.693 1.00 15.05 ? 943 THR A O 1 ATOM 6973 C CB . THR A 1 943 ? -6.660 1.599 36.406 1.00 15.63 ? 943 THR A CB 1 ATOM 6974 O OG1 . THR A 1 943 ? -7.102 0.935 35.215 1.00 15.97 ? 943 THR A OG1 1 ATOM 6975 C CG2 . THR A 1 943 ? -7.212 3.020 36.389 1.00 15.66 ? 943 THR A CG2 1 ATOM 6976 N N . SER A 1 944 ? -3.965 -0.380 35.590 1.00 14.90 ? 944 SER A N 1 ATOM 6977 C CA . SER A 1 944 ? -3.443 -1.747 35.583 1.00 14.69 ? 944 SER A CA 1 ATOM 6978 C C . SER A 1 944 ? -1.904 -1.769 35.407 1.00 14.09 ? 944 SER A C 1 ATOM 6979 O O . SER A 1 944 ? -1.390 -1.323 34.389 1.00 13.86 ? 944 SER A O 1 ATOM 6980 C CB . SER A 1 944 ? -4.126 -2.527 34.462 1.00 15.04 ? 944 SER A CB 1 ATOM 6981 O OG . SER A 1 944 ? -3.449 -3.736 34.213 1.00 15.55 ? 944 SER A OG 1 ATOM 6982 N N . PHE A 1 945 ? -1.188 -2.292 36.405 1.00 14.08 ? 945 PHE A N 1 ATOM 6983 C CA . PHE A 1 945 ? 0.288 -2.203 36.489 1.00 14.12 ? 945 PHE A CA 1 ATOM 6984 C C . PHE A 1 945 ? 0.950 -3.578 36.471 1.00 14.36 ? 945 PHE A C 1 ATOM 6985 O O . PHE A 1 945 ? 0.926 -4.287 37.470 1.00 14.59 ? 945 PHE A O 1 ATOM 6986 C CB . PHE A 1 945 ? 0.710 -1.497 37.778 1.00 13.84 ? 945 PHE A CB 1 ATOM 6987 C CG . PHE A 1 945 ? 0.281 -0.072 37.852 1.00 13.49 ? 945 PHE A CG 1 ATOM 6988 C CD1 . PHE A 1 945 ? -1.009 0.252 38.240 1.00 13.38 ? 945 PHE A CD1 1 ATOM 6989 C CD2 . PHE A 1 945 ? 1.161 0.956 37.513 1.00 13.27 ? 945 PHE A CD2 1 ATOM 6990 C CE1 . PHE A 1 945 ? -1.415 1.583 38.308 1.00 13.43 ? 945 PHE A CE1 1 ATOM 6991 C CE2 . PHE A 1 945 ? 0.761 2.291 37.595 1.00 13.28 ? 945 PHE A CE2 1 ATOM 6992 C CZ . PHE A 1 945 ? -0.526 2.601 37.982 1.00 12.92 ? 945 PHE A CZ 1 ATOM 6993 N N . PRO A 1 946 ? 1.544 -3.958 35.344 1.00 14.48 ? 946 PRO A N 1 ATOM 6994 C CA . PRO A 1 946 ? 2.200 -5.271 35.331 1.00 15.07 ? 946 PRO A CA 1 ATOM 6995 C C . PRO A 1 946 ? 3.484 -5.306 36.150 1.00 15.68 ? 946 PRO A C 1 ATOM 6996 O O . PRO A 1 946 ? 4.226 -4.321 36.210 1.00 14.77 ? 946 PRO A O 1 ATOM 6997 C CB . PRO A 1 946 ? 2.516 -5.509 33.848 1.00 15.08 ? 946 PRO A CB 1 ATOM 6998 C CG . PRO A 1 946 ? 2.463 -4.139 33.214 1.00 15.02 ? 946 PRO A CG 1 ATOM 6999 C CD . PRO A 1 946 ? 1.508 -3.313 34.017 1.00 14.40 ? 946 PRO A CD 1 ATOM 7000 N N . VAL A 1 947 ? 3.728 -6.451 36.777 1.00 16.38 ? 947 VAL A N 1 ATOM 7001 C CA . VAL A 1 947 ? 4.889 -6.644 37.603 1.00 16.98 ? 947 VAL A CA 1 ATOM 7002 C C . VAL A 1 947 ? 5.454 -8.003 37.239 1.00 18.15 ? 947 VAL A C 1 ATOM 7003 O O . VAL A 1 947 ? 4.761 -9.028 37.340 1.00 18.12 ? 947 VAL A O 1 ATOM 7004 C CB . VAL A 1 947 ? 4.545 -6.630 39.095 1.00 17.26 ? 947 VAL A CB 1 ATOM 7005 C CG1 . VAL A 1 947 ? 5.815 -6.706 39.924 1.00 17.67 ? 947 VAL A CG1 1 ATOM 7006 C CG2 . VAL A 1 947 ? 3.754 -5.392 39.455 1.00 17.19 ? 947 VAL A CG2 1 ATOM 7007 N N . PRO A 1 948 ? 6.715 -8.025 36.809 1.00 18.66 ? 948 PRO A N 1 ATOM 7008 C CA . PRO A 1 948 ? 7.254 -9.241 36.227 1.00 19.04 ? 948 PRO A CA 1 ATOM 7009 C C . PRO A 1 948 ? 7.732 -10.251 37.247 1.00 19.55 ? 948 PRO A C 1 ATOM 7010 O O . PRO A 1 948 ? 8.140 -9.877 38.339 1.00 20.93 ? 948 PRO A O 1 ATOM 7011 C CB . PRO A 1 948 ? 8.441 -8.730 35.404 1.00 19.63 ? 948 PRO A CB 1 ATOM 7012 C CG . PRO A 1 948 ? 8.868 -7.475 36.082 1.00 19.34 ? 948 PRO A CG 1 ATOM 7013 C CD . PRO A 1 948 ? 7.623 -6.874 36.667 1.00 18.92 ? 948 PRO A CD 1 ATOM 7014 N N . GLU A 1 949 ? 7.700 -11.526 36.877 1.00 19.49 ? 949 GLU A N 1 ATOM 7015 C CA . GLU A 1 949 ? 8.347 -12.559 37.661 1.00 20.05 ? 949 GLU A CA 1 ATOM 7016 C C . GLU A 1 949 ? 9.822 -12.194 37.787 1.00 19.97 ? 949 GLU A C 1 ATOM 7017 O O . GLU A 1 949 ? 10.388 -11.608 36.868 1.00 19.17 ? 949 GLU A O 1 ATOM 7018 C CB . GLU A 1 949 ? 8.188 -13.924 36.992 1.00 20.54 ? 949 GLU A CB 1 ATOM 7019 C CG . GLU A 1 949 ? 8.735 -15.071 37.825 1.00 21.43 ? 949 GLU A CG 1 ATOM 7020 C CD . GLU A 1 949 ? 8.412 -16.450 37.252 1.00 22.30 ? 949 GLU A CD 1 ATOM 7021 O OE1 . GLU A 1 949 ? 7.877 -16.549 36.131 1.00 22.36 ? 949 GLU A OE1 1 ATOM 7022 O OE2 . GLU A 1 949 ? 8.705 -17.451 37.935 1.00 24.50 -1 949 GLU A OE2 1 ATOM 7023 N N . GLY A 1 950 ? 10.429 -12.528 38.929 1.00 19.69 ? 950 GLY A N 1 ATOM 7024 C CA . GLY A 1 950 ? 11.793 -12.104 39.248 1.00 19.10 ? 950 GLY A CA 1 ATOM 7025 C C . GLY A 1 950 ? 11.785 -10.938 40.230 1.00 18.89 ? 950 GLY A C 1 ATOM 7026 O O . GLY A 1 950 ? 12.531 -10.934 41.202 1.00 18.91 ? 950 GLY A O 1 ATOM 7027 N N . ILE A 1 951 ? 10.942 -9.948 39.950 1.00 18.42 ? 951 ILE A N 1 ATOM 7028 C CA . ILE A 1 951 ? 10.563 -8.927 40.919 1.00 17.79 ? 951 ILE A CA 1 ATOM 7029 C C . ILE A 1 951 ? 9.547 -9.551 41.887 1.00 17.71 ? 951 ILE A C 1 ATOM 7030 O O . ILE A 1 951 ? 9.620 -9.354 43.098 1.00 18.02 ? 951 ILE A O 1 ATOM 7031 C CB . ILE A 1 951 ? 9.915 -7.708 40.219 1.00 17.74 ? 951 ILE A CB 1 ATOM 7032 C CG1 . ILE A 1 951 ? 10.874 -7.069 39.204 1.00 17.51 ? 951 ILE A CG1 1 ATOM 7033 C CG2 . ILE A 1 951 ? 9.410 -6.689 41.239 1.00 17.75 ? 951 ILE A CG2 1 ATOM 7034 C CD1 . ILE A 1 951 ? 12.164 -6.540 39.785 1.00 17.50 ? 951 ILE A CD1 1 ATOM 7035 N N . LEU A 1 952 ? 8.581 -10.275 41.336 1.00 17.68 ? 952 LEU A N 1 ATOM 7036 C CA . LEU A 1 952 ? 7.659 -11.079 42.134 1.00 17.70 ? 952 LEU A CA 1 ATOM 7037 C C . LEU A 1 952 ? 8.237 -12.496 42.267 1.00 17.89 ? 952 LEU A C 1 ATOM 7038 O O . LEU A 1 952 ? 8.836 -13.016 41.330 1.00 18.32 ? 952 LEU A O 1 ATOM 7039 C CB . LEU A 1 952 ? 6.271 -11.139 41.470 1.00 17.46 ? 952 LEU A CB 1 ATOM 7040 C CG . LEU A 1 952 ? 5.335 -9.935 41.600 1.00 17.05 ? 952 LEU A CG 1 ATOM 7041 C CD1 . LEU A 1 952 ? 4.134 -10.108 40.684 1.00 17.26 ? 952 LEU A CD1 1 ATOM 7042 C CD2 . LEU A 1 952 ? 4.849 -9.756 43.022 1.00 17.18 ? 952 LEU A CD2 1 ATOM 7043 N N . ASN A 1 953 ? 8.066 -13.096 43.436 1.00 18.10 ? 953 ASN A N 1 ATOM 7044 C CA . ASN A 1 953 ? 8.509 -14.455 43.695 1.00 18.74 ? 953 ASN A CA 1 ATOM 7045 C C . ASN A 1 953 ? 7.295 -15.366 43.565 1.00 18.82 ? 953 ASN A C 1 ATOM 7046 O O . ASN A 1 953 ? 6.372 -15.286 44.373 1.00 18.32 ? 953 ASN A O 1 ATOM 7047 C CB . ASN A 1 953 ? 9.136 -14.523 45.093 1.00 19.10 ? 953 ASN A CB 1 ATOM 7048 C CG . ASN A 1 953 ? 10.254 -13.492 45.277 1.00 19.79 ? 953 ASN A CG 1 ATOM 7049 O OD1 . ASN A 1 953 ? 11.115 -13.355 44.409 1.00 19.45 ? 953 ASN A OD1 1 ATOM 7050 N ND2 . ASN A 1 953 ? 10.231 -12.748 46.395 1.00 19.31 ? 953 ASN A ND2 1 ATOM 7051 N N . TYR A 1 954 ? 7.277 -16.200 42.522 1.00 19.86 ? 954 TYR A N 1 ATOM 7052 C CA . TYR A 1 954 ? 6.079 -16.989 42.183 1.00 20.21 ? 954 TYR A CA 1 ATOM 7053 C C . TYR A 1 954 ? 5.913 -18.185 43.126 1.00 20.79 ? 954 TYR A C 1 ATOM 7054 O O . TYR A 1 954 ? 4.799 -18.690 43.318 1.00 20.30 ? 954 TYR A O 1 ATOM 7055 C CB . TYR A 1 954 ? 6.087 -17.434 40.710 1.00 20.18 ? 954 TYR A CB 1 ATOM 7056 C CG . TYR A 1 954 ? 5.559 -16.394 39.725 1.00 20.41 ? 954 TYR A CG 1 ATOM 7057 C CD1 . TYR A 1 954 ? 5.723 -15.028 39.950 1.00 20.09 ? 954 TYR A CD1 1 ATOM 7058 C CD2 . TYR A 1 954 ? 4.913 -16.785 38.554 1.00 20.29 ? 954 TYR A CD2 1 ATOM 7059 C CE1 . TYR A 1 954 ? 5.241 -14.087 39.052 1.00 20.08 ? 954 TYR A CE1 1 ATOM 7060 C CE2 . TYR A 1 954 ? 4.435 -15.850 37.640 1.00 20.51 ? 954 TYR A CE2 1 ATOM 7061 C CZ . TYR A 1 954 ? 4.604 -14.500 37.888 1.00 20.49 ? 954 TYR A CZ 1 ATOM 7062 O OH . TYR A 1 954 ? 4.125 -13.559 36.991 1.00 19.57 ? 954 TYR A OH 1 ATOM 7063 N N . ARG A 1 955 ? 7.010 -18.612 43.743 1.00 21.46 ? 955 ARG A N 1 ATOM 7064 C CA . ARG A 1 955 ? 6.945 -19.675 44.741 1.00 22.70 ? 955 ARG A CA 1 ATOM 7065 C C . ARG A 1 955 ? 7.585 -19.241 46.058 1.00 22.22 ? 955 ARG A C 1 ATOM 7066 O O . ARG A 1 955 ? 8.507 -19.885 46.553 1.00 24.01 ? 955 ARG A O 1 ATOM 7067 C CB . ARG A 1 955 ? 7.564 -20.963 44.176 1.00 22.76 ? 955 ARG A CB 1 ATOM 7068 C CG . ARG A 1 955 ? 6.603 -21.721 43.265 1.00 23.92 ? 955 ARG A CG 1 ATOM 7069 C CD . ARG A 1 955 ? 7.323 -22.670 42.319 1.00 25.08 ? 955 ARG A CD 1 ATOM 7070 N NE . ARG A 1 955 ? 8.256 -21.939 41.453 1.00 26.62 ? 955 ARG A NE 1 ATOM 7071 C CZ . ARG A 1 955 ? 7.950 -21.371 40.288 1.00 26.80 ? 955 ARG A CZ 1 ATOM 7072 N NH1 . ARG A 1 955 ? 6.719 -21.434 39.788 1.00 27.21 ? 955 ARG A NH1 1 ATOM 7073 N NH2 . ARG A 1 955 ? 8.892 -20.730 39.614 1.00 27.74 ? 955 ARG A NH2 1 ATOM 7074 N N . GLY A 1 956 ? 7.077 -18.146 46.617 1.00 21.29 ? 956 GLY A N 1 ATOM 7075 C CA . GLY A 1 956 ? 7.576 -17.601 47.884 1.00 20.37 ? 956 GLY A CA 1 ATOM 7076 C C . GLY A 1 956 ? 6.751 -16.438 48.430 1.00 20.59 ? 956 GLY A C 1 ATOM 7077 O O . GLY A 1 956 ? 5.587 -16.239 48.054 1.00 19.84 ? 956 GLY A O 1 ATOM 7078 N N . THR A 1 957 ? 7.365 -15.664 49.322 1.00 20.19 ? 957 THR A N 1 ATOM 7079 C CA . THR A 1 957 ? 6.696 -14.557 49.987 1.00 19.79 ? 957 THR A CA 1 ATOM 7080 C C . THR A 1 957 ? 6.971 -13.254 49.241 1.00 19.48 ? 957 THR A C 1 ATOM 7081 O O . THR A 1 957 ? 8.055 -13.077 48.694 1.00 19.95 ? 957 THR A O 1 ATOM 7082 C CB . THR A 1 957 ? 7.156 -14.449 51.452 1.00 19.43 ? 957 THR A CB 1 ATOM 7083 O OG1 . THR A 1 957 ? 6.867 -15.679 52.108 1.00 19.68 ? 957 THR A OG1 1 ATOM 7084 C CG2 . THR A 1 957 ? 6.419 -13.327 52.186 1.00 19.35 ? 957 THR A CG2 1 ATOM 7085 N N . ASN A 1 958 ? 5.983 -12.365 49.203 1.00 18.64 ? 958 ASN A N 1 ATOM 7086 C CA . ASN A 1 958 ? 6.123 -11.093 48.507 1.00 19.03 ? 958 ASN A CA 1 ATOM 7087 C C . ASN A 1 958 ? 5.654 -9.948 49.377 1.00 19.10 ? 958 ASN A C 1 ATOM 7088 O O . ASN A 1 958 ? 4.739 -10.120 50.185 1.00 18.96 ? 958 ASN A O 1 ATOM 7089 C CB . ASN A 1 958 ? 5.312 -11.098 47.220 1.00 19.09 ? 958 ASN A CB 1 ATOM 7090 C CG . ASN A 1 958 ? 5.920 -11.963 46.168 1.00 19.53 ? 958 ASN A CG 1 ATOM 7091 O OD1 . ASN A 1 958 ? 6.908 -11.577 45.525 1.00 20.09 ? 958 ASN A OD1 1 ATOM 7092 N ND2 . ASN A 1 958 ? 5.350 -13.155 45.976 1.00 19.77 ? 958 ASN A ND2 1 ATOM 7093 N N . TRP A 1 959 ? 6.261 -8.778 49.199 1.00 19.06 ? 959 TRP A N 1 ATOM 7094 C CA . TRP A 1 959 ? 5.983 -7.637 50.067 1.00 19.27 ? 959 TRP A CA 1 ATOM 7095 C C . TRP A 1 959 ? 5.479 -6.445 49.279 1.00 18.99 ? 959 TRP A C 1 ATOM 7096 O O . TRP A 1 959 ? 6.122 -6.018 48.319 1.00 19.17 ? 959 TRP A O 1 ATOM 7097 C CB . TRP A 1 959 ? 7.241 -7.279 50.858 1.00 19.96 ? 959 TRP A CB 1 ATOM 7098 C CG . TRP A 1 959 ? 7.651 -8.388 51.759 1.00 20.77 ? 959 TRP A CG 1 ATOM 7099 C CD1 . TRP A 1 959 ? 8.412 -9.481 51.433 1.00 21.68 ? 959 TRP A CD1 1 ATOM 7100 C CD2 . TRP A 1 959 ? 7.275 -8.557 53.125 1.00 21.49 ? 959 TRP A CD2 1 ATOM 7101 N NE1 . TRP A 1 959 ? 8.554 -10.302 52.524 1.00 21.84 ? 959 TRP A NE1 1 ATOM 7102 C CE2 . TRP A 1 959 ? 7.858 -9.763 53.574 1.00 21.92 ? 959 TRP A CE2 1 ATOM 7103 C CE3 . TRP A 1 959 ? 6.512 -7.803 54.017 1.00 21.94 ? 959 TRP A CE3 1 ATOM 7104 C CZ2 . TRP A 1 959 ? 7.704 -10.226 54.876 1.00 22.23 ? 959 TRP A CZ2 1 ATOM 7105 C CZ3 . TRP A 1 959 ? 6.351 -8.274 55.318 1.00 22.54 ? 959 TRP A CZ3 1 ATOM 7106 C CH2 . TRP A 1 959 ? 6.953 -9.467 55.734 1.00 22.09 ? 959 TRP A CH2 1 ATOM 7107 N N . LEU A 1 960 ? 4.310 -5.933 49.667 1.00 18.44 ? 960 LEU A N 1 ATOM 7108 C CA . LEU A 1 960 ? 3.765 -4.700 49.089 1.00 17.85 ? 960 LEU A CA 1 ATOM 7109 C C . LEU A 1 960 ? 3.920 -3.552 50.080 1.00 17.81 ? 960 LEU A C 1 ATOM 7110 O O . LEU A 1 960 ? 3.613 -3.696 51.261 1.00 17.63 ? 960 LEU A O 1 ATOM 7111 C CB . LEU A 1 960 ? 2.279 -4.831 48.752 1.00 17.57 ? 960 LEU A CB 1 ATOM 7112 C CG . LEU A 1 960 ? 1.833 -5.832 47.707 1.00 17.32 ? 960 LEU A CG 1 ATOM 7113 C CD1 . LEU A 1 960 ? 0.323 -5.815 47.643 1.00 16.86 ? 960 LEU A CD1 1 ATOM 7114 C CD2 . LEU A 1 960 ? 2.451 -5.526 46.343 1.00 17.25 ? 960 LEU A CD2 1 ATOM 7115 N N . ALA A 1 961 ? 4.377 -2.412 49.580 1.00 17.39 ? 961 ALA A N 1 ATOM 7116 C CA . ALA A 1 961 ? 4.484 -1.204 50.373 1.00 16.77 ? 961 ALA A CA 1 ATOM 7117 C C . ALA A 1 961 ? 3.752 -0.135 49.587 1.00 16.34 ? 961 ALA A C 1 ATOM 7118 O O . ALA A 1 961 ? 4.156 0.190 48.472 1.00 18.00 ? 961 ALA A O 1 ATOM 7119 C CB . ALA A 1 961 ? 5.940 -0.832 50.558 1.00 16.54 ? 961 ALA A CB 1 ATOM 7120 N N . VAL A 1 962 ? 2.669 0.387 50.138 1.00 15.12 ? 962 VAL A N 1 ATOM 7121 C CA . VAL A 1 962 ? 1.828 1.344 49.429 1.00 14.56 ? 962 VAL A CA 1 ATOM 7122 C C . VAL A 1 962 ? 1.893 2.670 50.168 1.00 14.54 ? 962 VAL A C 1 ATOM 7123 O O . VAL A 1 962 ? 1.732 2.704 51.387 1.00 13.92 ? 962 VAL A O 1 ATOM 7124 C CB . VAL A 1 962 ? 0.367 0.858 49.405 1.00 14.46 ? 962 VAL A CB 1 ATOM 7125 C CG1 . VAL A 1 962 ? -0.531 1.848 48.686 1.00 13.97 ? 962 VAL A CG1 1 ATOM 7126 C CG2 . VAL A 1 962 ? 0.268 -0.550 48.814 1.00 14.40 ? 962 VAL A CG2 1 ATOM 7127 N N . THR A 1 963 ? 2.156 3.750 49.443 1.00 14.90 ? 963 THR A N 1 ATOM 7128 C CA . THR A 1 963 ? 2.035 5.098 49.997 1.00 14.83 ? 963 THR A CA 1 ATOM 7129 C C . THR A 1 963 ? 0.778 5.737 49.436 1.00 14.86 ? 963 THR A C 1 ATOM 7130 O O . THR A 1 963 ? 0.497 5.623 48.250 1.00 15.49 ? 963 THR A O 1 ATOM 7131 C CB . THR A 1 963 ? 3.247 5.997 49.678 1.00 14.86 ? 963 THR A CB 1 ATOM 7132 O OG1 . THR A 1 963 ? 3.264 6.359 48.286 1.00 15.20 ? 963 THR A OG1 1 ATOM 7133 C CG2 . THR A 1 963 ? 4.542 5.296 50.035 1.00 14.96 ? 963 THR A CG2 1 ATOM 7134 N N . LEU A 1 964 ? 0.031 6.410 50.294 1.00 14.88 ? 964 LEU A N 1 ATOM 7135 C CA . LEU A 1 964 ? -1.213 7.033 49.912 1.00 15.01 ? 964 LEU A CA 1 ATOM 7136 C C . LEU A 1 964 ? -1.209 8.475 50.384 1.00 14.87 ? 964 LEU A C 1 ATOM 7137 O O . LEU A 1 964 ? -1.348 8.755 51.570 1.00 14.84 ? 964 LEU A O 1 ATOM 7138 C CB . LEU A 1 964 ? -2.383 6.267 50.525 1.00 15.58 ? 964 LEU A CB 1 ATOM 7139 C CG . LEU A 1 964 ? -3.782 6.873 50.416 1.00 16.10 ? 964 LEU A CG 1 ATOM 7140 C CD1 . LEU A 1 964 ? -4.089 7.241 48.980 1.00 16.47 ? 964 LEU A CD1 1 ATOM 7141 C CD2 . LEU A 1 964 ? -4.827 5.908 50.952 1.00 16.23 ? 964 LEU A CD2 1 ATOM 7142 N N . TRP A 1 965 ? -1.051 9.382 49.436 1.00 14.84 ? 965 TRP A N 1 ATOM 7143 C CA . TRP A 1 965 ? -1.053 10.816 49.695 1.00 15.13 ? 965 TRP A CA 1 ATOM 7144 C C . TRP A 1 965 ? -2.407 11.397 49.291 1.00 15.16 ? 965 TRP A C 1 ATOM 7145 O O . TRP A 1 965 ? -2.787 11.341 48.132 1.00 14.46 ? 965 TRP A O 1 ATOM 7146 C CB . TRP A 1 965 ? 0.073 11.427 48.883 1.00 15.25 ? 965 TRP A CB 1 ATOM 7147 C CG . TRP A 1 965 ? 0.220 12.894 48.903 1.00 15.55 ? 965 TRP A CG 1 ATOM 7148 C CD1 . TRP A 1 965 ? -0.409 13.804 49.710 1.00 15.37 ? 965 TRP A CD1 1 ATOM 7149 C CD2 . TRP A 1 965 ? 1.111 13.637 48.067 1.00 15.90 ? 965 TRP A CD2 1 ATOM 7150 N NE1 . TRP A 1 965 ? 0.034 15.082 49.407 1.00 15.89 ? 965 TRP A NE1 1 ATOM 7151 C CE2 . TRP A 1 965 ? 0.965 15.000 48.399 1.00 15.96 ? 965 TRP A CE2 1 ATOM 7152 C CE3 . TRP A 1 965 ? 2.026 13.277 47.065 1.00 16.03 ? 965 TRP A CE3 1 ATOM 7153 C CZ2 . TRP A 1 965 ? 1.686 16.004 47.752 1.00 15.74 ? 965 TRP A CZ2 1 ATOM 7154 C CZ3 . TRP A 1 965 ? 2.744 14.279 46.429 1.00 15.93 ? 965 TRP A CZ3 1 ATOM 7155 C CH2 . TRP A 1 965 ? 2.569 15.626 46.780 1.00 15.73 ? 965 TRP A CH2 1 ATOM 7156 N N . ALA A 1 966 ? -3.131 11.952 50.257 1.00 15.75 ? 966 ALA A N 1 ATOM 7157 C CA . ALA A 1 966 ? -4.444 12.508 50.007 1.00 15.97 ? 966 ALA A CA 1 ATOM 7158 C C . ALA A 1 966 ? -4.324 14.018 49.904 1.00 16.95 ? 966 ALA A C 1 ATOM 7159 O O . ALA A 1 966 ? -4.045 14.691 50.900 1.00 17.36 ? 966 ALA A O 1 ATOM 7160 C CB . ALA A 1 966 ? -5.391 12.113 51.128 1.00 16.15 ? 966 ALA A CB 1 ATOM 7161 N N . LEU A 1 967 ? -4.545 14.553 48.703 1.00 17.51 ? 967 LEU A N 1 ATOM 7162 C CA . LEU A 1 967 ? -4.402 15.982 48.441 1.00 18.15 ? 967 LEU A CA 1 ATOM 7163 C C . LEU A 1 967 ? -5.758 16.701 48.589 1.00 19.53 ? 967 LEU A C 1 ATOM 7164 O O . LEU A 1 967 ? -6.164 17.512 47.751 1.00 18.37 ? 967 LEU A O 1 ATOM 7165 C CB . LEU A 1 967 ? -3.816 16.204 47.041 1.00 18.02 ? 967 LEU A CB 1 ATOM 7166 C CG . LEU A 1 967 ? -2.421 15.622 46.768 1.00 17.67 ? 967 LEU A CG 1 ATOM 7167 C CD1 . LEU A 1 967 ? -2.450 14.173 46.291 1.00 17.70 ? 967 LEU A CD1 1 ATOM 7168 C CD2 . LEU A 1 967 ? -1.711 16.486 45.741 1.00 17.60 ? 967 LEU A CD2 1 ATOM 7169 N N . ASP A 1 968 ? -6.442 16.385 49.684 1.00 21.50 ? 968 ASP A N 1 ATOM 7170 C CA . ASP A 1 968 ? -7.794 16.850 49.944 1.00 22.46 ? 968 ASP A CA 1 ATOM 7171 C C . ASP A 1 968 ? -8.013 16.829 51.457 1.00 21.54 ? 968 ASP A C 1 ATOM 7172 O O . ASP A 1 968 ? -7.642 15.859 52.131 1.00 20.90 ? 968 ASP A O 1 ATOM 7173 C CB . ASP A 1 968 ? -8.800 15.936 49.254 1.00 24.74 ? 968 ASP A CB 1 ATOM 7174 C CG . ASP A 1 968 ? -10.225 16.446 49.363 1.00 27.39 ? 968 ASP A CG 1 ATOM 7175 O OD1 . ASP A 1 968 ? -10.640 17.245 48.490 1.00 30.05 -1 968 ASP A OD1 1 ATOM 7176 O OD2 . ASP A 1 968 ? -10.925 16.051 50.323 1.00 29.13 ? 968 ASP A OD2 1 ATOM 7177 N N . SER A 1 969 ? -8.637 17.878 51.991 1.00 20.47 ? 969 SER A N 1 ATOM 7178 C CA . SER A 1 969 ? -8.794 18.006 53.444 1.00 19.90 ? 969 SER A CA 1 ATOM 7179 C C . SER A 1 969 ? -9.692 16.940 54.088 1.00 19.38 ? 969 SER A C 1 ATOM 7180 O O . SER A 1 969 ? -9.674 16.780 55.305 1.00 20.50 ? 969 SER A O 1 ATOM 7181 C CB . SER A 1 969 ? -9.338 19.394 53.800 1.00 19.57 ? 969 SER A CB 1 ATOM 7182 O OG . SER A 1 969 ? -10.715 19.482 53.501 1.00 18.81 ? 969 SER A OG 1 ATOM 7183 N N . ALA A 1 970 ? -10.501 16.242 53.295 1.00 19.04 ? 970 ALA A N 1 ATOM 7184 C CA . ALA A 1 970 ? -11.301 15.132 53.814 1.00 19.00 ? 970 ALA A CA 1 ATOM 7185 C C . ALA A 1 970 ? -10.587 13.774 53.673 1.00 18.70 ? 970 ALA A C 1 ATOM 7186 O O . ALA A 1 970 ? -11.174 12.735 53.945 1.00 18.43 ? 970 ALA A O 1 ATOM 7187 C CB . ALA A 1 970 ? -12.665 15.096 53.137 1.00 18.72 ? 970 ALA A CB 1 ATOM 7188 N N . GLY A 1 971 ? -9.320 13.785 53.270 1.00 18.62 ? 971 GLY A N 1 ATOM 7189 C CA . GLY A 1 971 ? -8.546 12.559 53.165 1.00 19.19 ? 971 GLY A CA 1 ATOM 7190 C C . GLY A 1 971 ? -8.762 11.851 51.840 1.00 19.51 ? 971 GLY A C 1 ATOM 7191 O O . GLY A 1 971 ? -8.955 12.488 50.797 1.00 19.23 ? 971 GLY A O 1 ATOM 7192 N N . GLY A 1 972 ? -8.704 10.527 51.879 1.00 20.80 ? 972 GLY A N 1 ATOM 7193 C CA . GLY A 1 972 ? -8.836 9.708 50.669 1.00 21.31 ? 972 GLY A CA 1 ATOM 7194 C C . GLY A 1 972 ? -8.589 8.233 50.929 1.00 21.76 ? 972 GLY A C 1 ATOM 7195 O O . GLY A 1 972 ? -8.008 7.861 51.952 1.00 21.27 ? 972 GLY A O 1 ATOM 7196 N N . LYS A 1 973 ? -9.032 7.399 49.986 1.00 22.59 ? 973 LYS A N 1 ATOM 7197 C CA . LYS A 1 973 ? -8.880 5.947 50.073 1.00 23.33 ? 973 LYS A CA 1 ATOM 7198 C C . LYS A 1 973 ? -8.901 5.307 48.690 1.00 23.19 ? 973 LYS A C 1 ATOM 7199 O O . LYS A 1 973 ? -9.462 5.868 47.747 1.00 22.35 ? 973 LYS A O 1 ATOM 7200 C CB . LYS A 1 973 ? -9.991 5.334 50.937 1.00 23.63 ? 973 LYS A CB 1 ATOM 7201 C CG . LYS A 1 973 ? -11.390 5.756 50.528 1.00 24.77 ? 973 LYS A CG 1 ATOM 7202 C CD . LYS A 1 973 ? -12.458 5.118 51.413 1.00 26.18 ? 973 LYS A CD 1 ATOM 7203 C CE . LYS A 1 973 ? -13.801 5.106 50.699 1.00 26.96 ? 973 LYS A CE 1 ATOM 7204 N NZ . LYS A 1 973 ? -14.850 4.421 51.494 1.00 28.03 ? 973 LYS A NZ 1 ATOM 7205 N N . LEU A 1 974 ? -8.287 4.131 48.577 1.00 23.49 ? 974 LEU A N 1 ATOM 7206 C CA . LEU A 1 974 ? -8.398 3.336 47.356 1.00 24.72 ? 974 LEU A CA 1 ATOM 7207 C C . LEU A 1 974 ? -9.809 2.750 47.263 1.00 25.17 ? 974 LEU A C 1 ATOM 7208 O O . LEU A 1 974 ? -10.375 2.303 48.263 1.00 26.33 ? 974 LEU A O 1 ATOM 7209 C CB . LEU A 1 974 ? -7.355 2.204 47.322 1.00 25.08 ? 974 LEU A CB 1 ATOM 7210 C CG . LEU A 1 974 ? -5.880 2.614 47.433 1.00 25.21 ? 974 LEU A CG 1 ATOM 7211 C CD1 . LEU A 1 974 ? -4.963 1.410 47.240 1.00 25.44 ? 974 LEU A CD1 1 ATOM 7212 C CD2 . LEU A 1 974 ? -5.555 3.709 46.436 1.00 25.20 ? 974 LEU A CD2 1 ATOM 7213 N N . GLU A 1 975 ? -10.377 2.784 46.065 1.00 24.94 ? 975 GLU A N 1 ATOM 7214 C CA . GLU A 1 975 ? -11.684 2.193 45.802 1.00 25.43 ? 975 GLU A CA 1 ATOM 7215 C C . GLU A 1 975 ? -11.555 0.669 45.814 1.00 23.85 ? 975 GLU A C 1 ATOM 7216 O O . GLU A 1 975 ? -12.395 -0.035 46.364 1.00 23.98 ? 975 GLU A O 1 ATOM 7217 C CB . GLU A 1 975 ? -12.203 2.692 44.451 1.00 27.68 ? 975 GLU A CB 1 ATOM 7218 C CG . GLU A 1 975 ? -13.546 2.130 43.990 1.00 30.12 ? 975 GLU A CG 1 ATOM 7219 C CD . GLU A 1 975 ? -13.800 2.441 42.518 1.00 32.39 ? 975 GLU A CD 1 ATOM 7220 O OE1 . GLU A 1 975 ? -14.260 3.566 42.213 1.00 34.41 ? 975 GLU A OE1 1 ATOM 7221 O OE2 . GLU A 1 975 ? -13.530 1.566 41.656 1.00 32.46 -1 975 GLU A OE2 1 ATOM 7222 N N . SER A 1 976 ? -10.489 0.170 45.208 1.00 21.66 ? 976 SER A N 1 ATOM 7223 C CA . SER A 1 976 ? -10.178 -1.246 45.248 1.00 21.41 ? 976 SER A CA 1 ATOM 7224 C C . SER A 1 976 ? -8.706 -1.453 44.893 1.00 20.86 ? 976 SER A C 1 ATOM 7225 O O . SER A 1 976 ? -8.037 -0.534 44.399 1.00 19.60 ? 976 SER A O 1 ATOM 7226 C CB . SER A 1 976 ? -11.077 -2.032 44.299 1.00 21.04 ? 976 SER A CB 1 ATOM 7227 O OG . SER A 1 976 ? -10.936 -1.531 42.988 1.00 21.18 ? 976 SER A OG 1 ATOM 7228 N N . LEU A 1 977 ? -8.214 -2.654 45.175 1.00 20.04 ? 977 LEU A N 1 ATOM 7229 C CA . LEU A 1 977 ? -6.807 -2.993 44.993 1.00 20.83 ? 977 LEU A CA 1 ATOM 7230 C C . LEU A 1 977 ? -6.737 -4.496 44.820 1.00 22.02 ? 977 LEU A C 1 ATOM 7231 O O . LEU A 1 977 ? -7.070 -5.240 45.747 1.00 21.27 ? 977 LEU A O 1 ATOM 7232 C CB . LEU A 1 977 ? -5.960 -2.551 46.192 1.00 20.34 ? 977 LEU A CB 1 ATOM 7233 C CG . LEU A 1 977 ? -4.478 -2.958 46.176 1.00 20.21 ? 977 LEU A CG 1 ATOM 7234 C CD1 . LEU A 1 977 ? -3.764 -2.375 44.971 1.00 19.97 ? 977 LEU A CD1 1 ATOM 7235 C CD2 . LEU A 1 977 ? -3.789 -2.516 47.453 1.00 20.56 ? 977 LEU A CD2 1 ATOM 7236 N N . GLU A 1 978 ? -6.334 -4.931 43.626 1.00 23.43 ? 978 GLU A N 1 ATOM 7237 C CA . GLU A 1 978 ? -6.467 -6.332 43.224 1.00 25.07 ? 978 GLU A CA 1 ATOM 7238 C C . GLU A 1 978 ? -5.274 -6.816 42.403 1.00 23.37 ? 978 GLU A C 1 ATOM 7239 O O . GLU A 1 978 ? -4.720 -6.083 41.586 1.00 21.68 ? 978 GLU A O 1 ATOM 7240 C CB . GLU A 1 978 ? -7.743 -6.521 42.398 1.00 28.38 ? 978 GLU A CB 1 ATOM 7241 C CG . GLU A 1 978 ? -9.043 -6.312 43.166 1.00 31.98 ? 978 GLU A CG 1 ATOM 7242 C CD . GLU A 1 978 ? -10.275 -6.326 42.261 1.00 35.66 ? 978 GLU A CD 1 ATOM 7243 O OE1 . GLU A 1 978 ? -10.140 -6.714 41.075 1.00 36.73 ? 978 GLU A OE1 1 ATOM 7244 O OE2 . GLU A 1 978 ? -11.377 -5.938 42.737 1.00 39.77 -1 978 GLU A OE2 1 ATOM 7245 N N . LEU A 1 979 ? -4.895 -8.064 42.639 1.00 23.10 ? 979 LEU A N 1 ATOM 7246 C CA . LEU A 1 979 ? -3.916 -8.772 41.819 1.00 23.13 ? 979 LEU A CA 1 ATOM 7247 C C . LEU A 1 979 ? -4.710 -9.592 40.803 1.00 22.65 ? 979 LEU A C 1 ATOM 7248 O O . LEU A 1 979 ? -5.630 -10.294 41.191 1.00 24.02 ? 979 LEU A O 1 ATOM 7249 C CB . LEU A 1 979 ? -3.085 -9.682 42.714 1.00 23.82 ? 979 LEU A CB 1 ATOM 7250 C CG . LEU A 1 979 ? -1.767 -10.254 42.206 1.00 24.85 ? 979 LEU A CG 1 ATOM 7251 C CD1 . LEU A 1 979 ? -0.723 -9.165 42.022 1.00 25.18 ? 979 LEU A CD1 1 ATOM 7252 C CD2 . LEU A 1 979 ? -1.263 -11.290 43.193 1.00 25.75 ? 979 LEU A CD2 1 ATOM 7253 N N . SER A 1 980 ? -4.383 -9.481 39.515 1.00 21.68 ? 980 SER A N 1 ATOM 7254 C CA . SER A 1 980 ? -5.056 -10.251 38.451 1.00 20.69 ? 980 SER A CA 1 ATOM 7255 C C . SER A 1 980 ? -4.040 -10.911 37.522 1.00 20.69 ? 980 SER A C 1 ATOM 7256 O O . SER A 1 980 ? -2.843 -10.609 37.575 1.00 20.81 ? 980 SER A O 1 ATOM 7257 C CB . SER A 1 980 ? -5.961 -9.344 37.617 1.00 20.26 ? 980 SER A CB 1 ATOM 7258 O OG . SER A 1 980 ? -5.193 -8.367 36.939 1.00 19.68 ? 980 SER A OG 1 ATOM 7259 N N . TYR A 1 981 ? -4.515 -11.814 36.671 1.00 20.11 ? 981 TYR A N 1 ATOM 7260 C CA . TYR A 1 981 ? -3.644 -12.454 35.674 1.00 20.04 ? 981 TYR A CA 1 ATOM 7261 C C . TYR A 1 981 ? -4.311 -12.490 34.309 1.00 19.50 ? 981 TYR A C 1 ATOM 7262 O O . TYR A 1 981 ? -5.528 -12.393 34.213 1.00 19.04 ? 981 TYR A O 1 ATOM 7263 C CB . TYR A 1 981 ? -3.216 -13.859 36.114 1.00 19.86 ? 981 TYR A CB 1 ATOM 7264 C CG . TYR A 1 981 ? -4.313 -14.894 36.103 1.00 20.25 ? 981 TYR A CG 1 ATOM 7265 C CD1 . TYR A 1 981 ? -5.209 -15.007 37.168 1.00 20.55 ? 981 TYR A CD1 1 ATOM 7266 C CD2 . TYR A 1 981 ? -4.447 -15.779 35.037 1.00 20.74 ? 981 TYR A CD2 1 ATOM 7267 C CE1 . TYR A 1 981 ? -6.217 -15.964 37.158 1.00 21.07 ? 981 TYR A CE1 1 ATOM 7268 C CE2 . TYR A 1 981 ? -5.452 -16.735 35.009 1.00 21.20 ? 981 TYR A CE2 1 ATOM 7269 C CZ . TYR A 1 981 ? -6.331 -16.829 36.070 1.00 21.81 ? 981 TYR A CZ 1 ATOM 7270 O OH . TYR A 1 981 ? -7.323 -17.781 36.032 1.00 23.83 ? 981 TYR A OH 1 ATOM 7271 N N . THR A 1 982 ? -3.502 -12.599 33.257 1.00 19.45 ? 982 THR A N 1 ATOM 7272 C CA . THR A 1 982 ? -4.014 -12.859 31.892 1.00 19.87 ? 982 THR A CA 1 ATOM 7273 C C . THR A 1 982 ? -3.567 -14.255 31.458 1.00 19.38 ? 982 THR A C 1 ATOM 7274 O O . THR A 1 982 ? -2.893 -14.958 32.231 1.00 19.72 ? 982 THR A O 1 ATOM 7275 C CB . THR A 1 982 ? -3.548 -11.783 30.884 1.00 20.58 ? 982 THR A CB 1 ATOM 7276 O OG1 . THR A 1 982 ? -2.127 -11.590 31.003 1.00 21.24 ? 982 THR A OG1 1 ATOM 7277 C CG2 . THR A 1 982 ? -4.266 -10.454 31.153 1.00 20.48 ? 982 THR A CG2 1 ATOM 7278 N N . THR A 1 983 ? -3.962 -14.661 30.250 1.00 17.80 ? 983 THR A N 1 ATOM 7279 C CA . THR A 1 983 ? -3.780 -16.027 29.769 1.00 17.20 ? 983 THR A CA 1 ATOM 7280 C C . THR A 1 983 ? -2.452 -16.665 30.171 1.00 16.97 ? 983 THR A C 1 ATOM 7281 O O . THR A 1 983 ? -1.388 -16.211 29.754 1.00 17.33 ? 983 THR A O 1 ATOM 7282 C CB . THR A 1 983 ? -3.891 -16.098 28.227 1.00 17.48 ? 983 THR A CB 1 ATOM 7283 O OG1 . THR A 1 983 ? -4.984 -15.288 27.780 1.00 16.76 ? 983 THR A OG1 1 ATOM 7284 C CG2 . THR A 1 983 ? -4.110 -17.558 27.751 1.00 17.49 ? 983 THR A CG2 1 ATOM 7285 N N . PRO A 1 984 ? -2.500 -17.729 30.986 1.00 16.49 ? 984 PRO A N 1 ATOM 7286 C CA . PRO A 1 984 ? -1.260 -18.445 31.263 1.00 15.57 ? 984 PRO A CA 1 ATOM 7287 C C . PRO A 1 984 ? -0.711 -19.100 29.998 1.00 15.41 ? 984 PRO A C 1 ATOM 7288 O O . PRO A 1 984 ? -1.487 -19.620 29.188 1.00 13.80 ? 984 PRO A O 1 ATOM 7289 C CB . PRO A 1 984 ? -1.671 -19.518 32.275 1.00 15.88 ? 984 PRO A CB 1 ATOM 7290 C CG . PRO A 1 984 ? -3.002 -19.118 32.782 1.00 16.38 ? 984 PRO A CG 1 ATOM 7291 C CD . PRO A 1 984 ? -3.648 -18.295 31.708 1.00 16.64 ? 984 PRO A CD 1 ATOM 7292 N N . VAL A 1 985 ? 0.617 -19.052 29.843 1.00 15.75 ? 985 VAL A N 1 ATOM 7293 C CA . VAL A 1 985 ? 1.304 -19.627 28.705 1.00 15.58 ? 985 VAL A CA 1 ATOM 7294 C C . VAL A 1 985 ? 2.147 -20.811 29.145 1.00 15.72 ? 985 VAL A C 1 ATOM 7295 O O . VAL A 1 985 ? 2.940 -20.702 30.075 1.00 14.66 ? 985 VAL A O 1 ATOM 7296 C CB . VAL A 1 985 ? 2.224 -18.595 28.038 1.00 16.07 ? 985 VAL A CB 1 ATOM 7297 C CG1 . VAL A 1 985 ? 2.952 -19.217 26.849 1.00 16.00 ? 985 VAL A CG1 1 ATOM 7298 C CG2 . VAL A 1 985 ? 1.426 -17.370 27.606 1.00 16.10 ? 985 VAL A CG2 1 ATOM 7299 N N . LEU A 1 986 ? 1.974 -21.942 28.457 1.00 16.57 ? 986 LEU A N 1 ATOM 7300 C CA . LEU A 1 986 ? 2.801 -23.127 28.674 1.00 16.45 ? 986 LEU A CA 1 ATOM 7301 C C . LEU A 1 986 ? 4.117 -22.803 28.004 1.00 16.92 ? 986 LEU A C 1 ATOM 7302 O O . LEU A 1 986 ? 4.162 -22.634 26.789 1.00 16.57 ? 986 LEU A O 1 ATOM 7303 C CB . LEU A 1 986 ? 2.144 -24.356 28.051 1.00 16.53 ? 986 LEU A CB 1 ATOM 7304 C CG . LEU A 1 986 ? 2.867 -25.701 28.098 1.00 16.65 ? 986 LEU A CG 1 ATOM 7305 C CD1 . LEU A 1 986 ? 2.939 -26.233 29.523 1.00 16.96 ? 986 LEU A CD1 1 ATOM 7306 C CD2 . LEU A 1 986 ? 2.130 -26.692 27.211 1.00 16.82 ? 986 LEU A CD2 1 ATOM 7307 N N . THR A 1 987 ? 5.179 -22.690 28.795 1.00 18.07 ? 987 THR A N 1 ATOM 7308 C CA . THR A 1 987 ? 6.417 -22.057 28.326 1.00 19.26 ? 987 THR A CA 1 ATOM 7309 C C . THR A 1 987 ? 7.631 -22.968 28.365 1.00 19.43 ? 987 THR A C 1 ATOM 7310 O O . THR A 1 987 ? 7.719 -23.886 29.168 1.00 18.79 ? 987 THR A O 1 ATOM 7311 C CB . THR A 1 987 ? 6.740 -20.771 29.139 1.00 19.84 ? 987 THR A CB 1 ATOM 7312 O OG1 . THR A 1 987 ? 7.768 -20.022 28.488 1.00 19.44 ? 987 THR A OG1 1 ATOM 7313 C CG2 . THR A 1 987 ? 7.202 -21.104 30.563 1.00 20.21 ? 987 THR A CG2 1 ATOM 7314 N N . ALA A 1 988 ? 8.561 -22.672 27.470 1.00 20.96 ? 988 ALA A N 1 ATOM 7315 C CA . ALA A 1 988 ? 9.884 -23.280 27.432 1.00 22.47 ? 988 ALA A CA 1 ATOM 7316 C C . ALA A 1 988 ? 10.895 -22.530 28.302 1.00 23.94 ? 988 ALA A C 1 ATOM 7317 O O . ALA A 1 988 ? 11.984 -23.039 28.542 1.00 25.22 ? 988 ALA A O 1 ATOM 7318 C CB . ALA A 1 988 ? 10.389 -23.315 25.995 1.00 22.70 ? 988 ALA A CB 1 ATOM 7319 N N . LEU A 1 989 ? 10.564 -21.327 28.762 1.00 25.37 ? 989 LEU A N 1 ATOM 7320 C CA . LEU A 1 989 ? 11.531 -20.525 29.517 1.00 27.48 ? 989 LEU A CA 1 ATOM 7321 C C . LEU A 1 989 ? 12.071 -21.284 30.721 1.00 29.31 ? 989 LEU A C 1 ATOM 7322 O O . LEU A 1 989 ? 11.352 -22.059 31.361 1.00 28.02 ? 989 LEU A O 1 ATOM 7323 C CB . LEU A 1 989 ? 10.918 -19.222 30.017 1.00 27.63 ? 989 LEU A CB 1 ATOM 7324 C CG . LEU A 1 989 ? 10.743 -18.081 29.028 1.00 28.21 ? 989 LEU A CG 1 ATOM 7325 C CD1 . LEU A 1 989 ? 9.912 -16.987 29.688 1.00 29.34 ? 989 LEU A CD1 1 ATOM 7326 C CD2 . LEU A 1 989 ? 12.084 -17.537 28.561 1.00 28.53 ? 989 LEU A CD2 1 ATOM 7327 N N . GLY A 1 990 ? 13.344 -21.052 31.018 1.00 31.39 ? 990 GLY A N 1 ATOM 7328 C CA . GLY A 1 990 ? 13.957 -21.609 32.210 1.00 34.05 ? 990 GLY A CA 1 ATOM 7329 C C . GLY A 1 990 ? 13.436 -20.902 33.451 1.00 35.16 ? 990 GLY A C 1 ATOM 7330 O O . GLY A 1 990 ? 12.842 -19.826 33.359 1.00 35.21 ? 990 GLY A O 1 ATOM 7331 N N . GLU A 1 991 ? 13.654 -21.531 34.602 1.00 35.89 ? 991 GLU A N 1 ATOM 7332 C CA . GLU A 1 991 ? 13.371 -20.941 35.909 1.00 38.28 ? 991 GLU A CA 1 ATOM 7333 C C . GLU A 1 991 ? 13.782 -19.456 35.965 1.00 34.35 ? 991 GLU A C 1 ATOM 7334 O O . GLU A 1 991 ? 14.922 -19.108 35.637 1.00 31.74 ? 991 GLU A O 1 ATOM 7335 C CB . GLU A 1 991 ? 14.132 -21.731 36.979 1.00 43.12 ? 991 GLU A CB 1 ATOM 7336 C CG . GLU A 1 991 ? 13.538 -21.667 38.372 1.00 50.04 ? 991 GLU A CG 1 ATOM 7337 C CD . GLU A 1 991 ? 14.028 -22.812 39.253 1.00 55.92 ? 991 GLU A CD 1 ATOM 7338 O OE1 . GLU A 1 991 ? 13.169 -23.466 39.896 1.00 59.24 ? 991 GLU A OE1 1 ATOM 7339 O OE2 . GLU A 1 991 ? 15.263 -23.068 39.284 1.00 54.86 -1 991 GLU A OE2 1 ATOM 7340 N N . VAL A 1 992 ? 12.845 -18.590 36.344 1.00 30.86 ? 992 VAL A N 1 ATOM 7341 C CA . VAL A 1 992 ? 13.151 -17.175 36.542 1.00 30.24 ? 992 VAL A CA 1 ATOM 7342 C C . VAL A 1 992 ? 13.649 -16.966 37.971 1.00 29.32 ? 992 VAL A C 1 ATOM 7343 O O . VAL A 1 992 ? 12.881 -17.061 38.919 1.00 29.04 ? 992 VAL A O 1 ATOM 7344 C CB . VAL A 1 992 ? 11.928 -16.258 36.304 1.00 29.61 ? 992 VAL A CB 1 ATOM 7345 C CG1 . VAL A 1 992 ? 12.285 -14.817 36.631 1.00 29.55 ? 992 VAL A CG1 1 ATOM 7346 C CG2 . VAL A 1 992 ? 11.422 -16.369 34.873 1.00 29.25 ? 992 VAL A CG2 1 ATOM 7347 N N . GLU A 1 993 ? 14.942 -16.687 38.099 1.00 29.63 ? 993 GLU A N 1 ATOM 7348 C CA . GLU A 1 993 ? 15.587 -16.377 39.366 1.00 30.46 ? 993 GLU A CA 1 ATOM 7349 C C . GLU A 1 993 ? 15.097 -15.035 39.922 1.00 27.30 ? 993 GLU A C 1 ATOM 7350 O O . GLU A 1 993 ? 15.023 -14.038 39.200 1.00 25.67 ? 993 GLU A O 1 ATOM 7351 C CB . GLU A 1 993 ? 17.114 -16.316 39.153 1.00 36.03 ? 993 GLU A CB 1 ATOM 7352 C CG . GLU A 1 993 ? 17.971 -16.361 40.422 1.00 42.04 ? 993 GLU A CG 1 ATOM 7353 C CD . GLU A 1 993 ? 19.486 -16.261 40.159 1.00 48.19 ? 993 GLU A CD 1 ATOM 7354 O OE1 . GLU A 1 993 ? 20.272 -16.732 41.022 1.00 52.35 ? 993 GLU A OE1 1 ATOM 7355 O OE2 . GLU A 1 993 ? 19.905 -15.723 39.101 1.00 52.06 -1 993 GLU A OE2 1 ATOM 7356 N N . SER A 1 994 ? 14.779 -15.007 41.208 1.00 24.84 ? 994 SER A N 1 ATOM 7357 C CA . SER A 1 994 ? 14.432 -13.756 41.860 1.00 24.34 ? 994 SER A CA 1 ATOM 7358 C C . SER A 1 994 ? 15.634 -12.825 41.884 1.00 24.09 ? 994 SER A C 1 ATOM 7359 O O . SER A 1 994 ? 16.739 -13.237 42.235 1.00 23.69 ? 994 SER A O 1 ATOM 7360 C CB . SER A 1 994 ? 13.971 -14.010 43.278 1.00 24.22 ? 994 SER A CB 1 ATOM 7361 O OG . SER A 1 994 ? 12.837 -14.848 43.264 1.00 25.61 ? 994 SER A OG 1 ATOM 7362 N N . VAL A 1 995 ? 15.430 -11.568 41.499 1.00 22.99 ? 995 VAL A N 1 ATOM 7363 C CA . VAL A 1 995 ? 16.471 -10.575 41.728 1.00 22.54 ? 995 VAL A CA 1 ATOM 7364 C C . VAL A 1 995 ? 16.691 -10.323 43.217 1.00 22.23 ? 995 VAL A C 1 ATOM 7365 O O . VAL A 1 995 ? 15.864 -10.659 44.073 1.00 21.41 ? 995 VAL A O 1 ATOM 7366 C CB . VAL A 1 995 ? 16.208 -9.241 41.003 1.00 21.78 ? 995 VAL A CB 1 ATOM 7367 C CG1 . VAL A 1 995 ? 16.071 -9.498 39.511 1.00 21.82 ? 995 VAL A CG1 1 ATOM 7368 C CG2 . VAL A 1 995 ? 14.996 -8.523 41.569 1.00 21.60 ? 995 VAL A CG2 1 ATOM 7369 N N . ASP A 1 996 ? 17.840 -9.738 43.507 1.00 22.72 ? 996 ASP A N 1 ATOM 7370 C CA . ASP A 1 996 ? 18.194 -9.343 44.862 1.00 22.52 ? 996 ASP A CA 1 ATOM 7371 C C . ASP A 1 996 ? 17.103 -8.420 45.453 1.00 21.58 ? 996 ASP A C 1 ATOM 7372 O O . ASP A 1 996 ? 16.726 -7.407 44.852 1.00 19.04 ? 996 ASP A O 1 ATOM 7373 C CB . ASP A 1 996 ? 19.571 -8.658 44.831 1.00 23.58 ? 996 ASP A CB 1 ATOM 7374 C CG . ASP A 1 996 ? 20.236 -8.566 46.201 1.00 25.63 ? 996 ASP A CG 1 ATOM 7375 O OD1 . ASP A 1 996 ? 19.645 -9.007 47.212 1.00 25.21 ? 996 ASP A OD1 1 ATOM 7376 O OD2 . ASP A 1 996 ? 21.384 -8.040 46.259 1.00 29.07 -1 996 ASP A OD2 1 ATOM 7377 N N . GLN A 1 997 ? 16.605 -8.802 46.630 1.00 21.29 ? 997 GLN A N 1 ATOM 7378 C CA . GLN A 1 997 ? 15.555 -8.082 47.321 1.00 21.57 ? 997 GLN A CA 1 ATOM 7379 C C . GLN A 1 997 ? 16.005 -7.786 48.741 1.00 21.45 ? 997 GLN A C 1 ATOM 7380 O O . GLN A 1 997 ? 15.524 -8.397 49.681 1.00 20.94 ? 997 GLN A O 1 ATOM 7381 C CB . GLN A 1 997 ? 14.270 -8.925 47.322 1.00 21.74 ? 997 GLN A CB 1 ATOM 7382 C CG . GLN A 1 997 ? 13.607 -8.994 45.951 1.00 21.94 ? 997 GLN A CG 1 ATOM 7383 C CD . GLN A 1 997 ? 12.629 -10.150 45.792 1.00 21.72 ? 997 GLN A CD 1 ATOM 7384 O OE1 . GLN A 1 997 ? 11.976 -10.559 46.741 1.00 22.09 ? 997 GLN A OE1 1 ATOM 7385 N NE2 . GLN A 1 997 ? 12.511 -10.665 44.568 1.00 22.25 ? 997 GLN A NE2 1 ATOM 7386 N N . PRO A 1 998 ? 16.949 -6.850 48.905 1.00 22.12 ? 998 PRO A N 1 ATOM 7387 C CA . PRO A 1 998 ? 17.460 -6.557 50.244 1.00 22.17 ? 998 PRO A CA 1 ATOM 7388 C C . PRO A 1 998 ? 16.343 -6.216 51.210 1.00 22.83 ? 998 PRO A C 1 ATOM 7389 O O . PRO A 1 998 ? 15.466 -5.423 50.883 1.00 22.77 ? 998 PRO A O 1 ATOM 7390 C CB . PRO A 1 998 ? 18.363 -5.350 50.016 1.00 22.01 ? 998 PRO A CB 1 ATOM 7391 C CG . PRO A 1 998 ? 18.842 -5.518 48.615 1.00 22.03 ? 998 PRO A CG 1 ATOM 7392 C CD . PRO A 1 998 ? 17.692 -6.118 47.864 1.00 22.15 ? 998 PRO A CD 1 ATOM 7393 N N . LYS A 1 999 ? 16.372 -6.836 52.380 1.00 23.43 ? 999 LYS A N 1 ATOM 7394 C CA . LYS A 1 999 ? 15.320 -6.669 53.361 1.00 25.27 ? 999 LYS A CA 1 ATOM 7395 C C . LYS A 1 999 ? 15.577 -5.435 54.216 1.00 24.70 ? 999 LYS A C 1 ATOM 7396 O O . LYS A 1 999 ? 16.676 -4.876 54.219 1.00 24.33 ? 999 LYS A O 1 ATOM 7397 C CB . LYS A 1 999 ? 15.188 -7.936 54.224 1.00 27.92 ? 999 LYS A CB 1 ATOM 7398 C CG . LYS A 1 999 ? 16.303 -8.148 55.223 1.00 30.35 ? 999 LYS A CG 1 ATOM 7399 C CD . LYS A 1 999 ? 16.081 -9.401 56.060 1.00 34.02 ? 999 LYS A CD 1 ATOM 7400 C CE . LYS A 1 999 ? 17.006 -9.410 57.277 1.00 35.83 ? 999 LYS A CE 1 ATOM 7401 N NZ . LYS A 1 999 ? 16.895 -10.662 58.079 1.00 37.58 ? 999 LYS A NZ 1 ATOM 7402 N N . TYR A 1 1000 ? 14.555 -4.999 54.938 1.00 24.67 ? 1000 TYR A N 1 ATOM 7403 C CA . TYR A 1 1000 ? 14.704 -3.819 55.790 1.00 24.42 ? 1000 TYR A CA 1 ATOM 7404 C C . TYR A 1 1000 ? 15.845 -3.994 56.783 1.00 25.44 ? 1000 TYR A C 1 ATOM 7405 O O . TYR A 1 1000 ? 16.017 -5.051 57.375 1.00 24.98 ? 1000 TYR A O 1 ATOM 7406 C CB . TYR A 1 1000 ? 13.417 -3.488 56.552 1.00 23.39 ? 1000 TYR A CB 1 ATOM 7407 C CG . TYR A 1 1000 ? 13.662 -2.592 57.750 1.00 22.95 ? 1000 TYR A CG 1 ATOM 7408 C CD1 . TYR A 1 1000 ? 13.829 -1.214 57.597 1.00 22.23 ? 1000 TYR A CD1 1 ATOM 7409 C CD2 . TYR A 1 1000 ? 13.764 -3.131 59.029 1.00 22.50 ? 1000 TYR A CD2 1 ATOM 7410 C CE1 . TYR A 1 1000 ? 14.072 -0.399 58.692 1.00 22.77 ? 1000 TYR A CE1 1 ATOM 7411 C CE2 . TYR A 1 1000 ? 14.004 -2.326 60.127 1.00 23.23 ? 1000 TYR A CE2 1 ATOM 7412 C CZ . TYR A 1 1000 ? 14.157 -0.961 59.957 1.00 23.14 ? 1000 TYR A CZ 1 ATOM 7413 O OH . TYR A 1 1000 ? 14.398 -0.170 61.050 1.00 23.08 ? 1000 TYR A OH 1 ATOM 7414 N N . LYS A 1 1001 ? 16.617 -2.934 56.942 1.00 26.62 ? 1001 LYS A N 1 ATOM 7415 C CA . LYS A 1 1001 ? 17.632 -2.859 57.960 1.00 29.57 ? 1001 LYS A CA 1 ATOM 7416 C C . LYS A 1 1001 ? 17.689 -1.407 58.404 1.00 29.08 ? 1001 LYS A C 1 ATOM 7417 O O . LYS A 1 1001 ? 17.591 -0.499 57.574 1.00 28.74 ? 1001 LYS A O 1 ATOM 7418 C CB . LYS A 1 1001 ? 18.985 -3.298 57.402 1.00 32.17 ? 1001 LYS A CB 1 ATOM 7419 C CG . LYS A 1 1001 ? 20.040 -3.503 58.473 1.00 35.06 ? 1001 LYS A CG 1 ATOM 7420 C CD . LYS A 1 1001 ? 21.394 -3.814 57.854 1.00 37.87 ? 1001 LYS A CD 1 ATOM 7421 C CE . LYS A 1 1001 ? 22.435 -4.059 58.933 1.00 40.11 ? 1001 LYS A CE 1 ATOM 7422 N NZ . LYS A 1 1001 ? 23.810 -4.101 58.366 1.00 42.10 ? 1001 LYS A NZ 1 ATOM 7423 N N . LYS A 1 1002 ? 17.824 -1.190 59.705 1.00 29.85 ? 1002 LYS A N 1 ATOM 7424 C CA . LYS A 1 1002 ? 17.853 0.165 60.242 1.00 31.55 ? 1002 LYS A CA 1 ATOM 7425 C C . LYS A 1 1002 ? 19.017 0.955 59.625 1.00 29.09 ? 1002 LYS A C 1 ATOM 7426 O O . LYS A 1 1002 ? 20.112 0.418 59.442 1.00 27.28 ? 1002 LYS A O 1 ATOM 7427 C CB . LYS A 1 1002 ? 17.945 0.147 61.775 1.00 34.75 ? 1002 LYS A CB 1 ATOM 7428 C CG . LYS A 1 1002 ? 17.527 1.469 62.407 1.00 38.23 ? 1002 LYS A CG 1 ATOM 7429 C CD . LYS A 1 1002 ? 17.519 1.434 63.929 1.00 40.99 ? 1002 LYS A CD 1 ATOM 7430 C CE . LYS A 1 1002 ? 18.886 1.775 64.520 1.00 43.40 ? 1002 LYS A CE 1 ATOM 7431 N NZ . LYS A 1 1002 ? 18.764 2.222 65.940 1.00 44.69 ? 1002 LYS A NZ 1 ATOM 7432 N N . ARG A 1 1003 ? 18.758 2.214 59.276 1.00 26.94 ? 1003 ARG A N 1 ATOM 7433 C CA . ARG A 1 1003 ? 19.735 3.032 58.561 1.00 26.57 ? 1003 ARG A CA 1 ATOM 7434 C C . ARG A 1 1003 ? 20.302 4.098 59.472 1.00 27.76 ? 1003 ARG A C 1 ATOM 7435 O O . ARG A 1 1003 ? 19.558 4.914 60.025 1.00 25.61 ? 1003 ARG A O 1 ATOM 7436 C CB . ARG A 1 1003 ? 19.104 3.717 57.357 1.00 25.88 ? 1003 ARG A CB 1 ATOM 7437 C CG . ARG A 1 1003 ? 18.683 2.784 56.238 1.00 25.46 ? 1003 ARG A CG 1 ATOM 7438 C CD . ARG A 1 1003 ? 17.734 3.498 55.289 1.00 24.26 ? 1003 ARG A CD 1 ATOM 7439 N NE . ARG A 1 1003 ? 17.467 2.733 54.076 1.00 23.21 ? 1003 ARG A NE 1 ATOM 7440 C CZ . ARG A 1 1003 ? 17.007 3.247 52.933 1.00 22.09 ? 1003 ARG A CZ 1 ATOM 7441 N NH1 . ARG A 1 1003 ? 16.753 4.548 52.809 1.00 21.31 ? 1003 ARG A NH1 1 ATOM 7442 N NH2 . ARG A 1 1003 ? 16.816 2.448 51.894 1.00 21.78 ? 1003 ARG A NH2 1 ATOM 7443 N N . LYS A 1 1004 ? 21.627 4.102 59.587 1.00 30.33 ? 1004 LYS A N 1 ATOM 7444 C CA . LYS A 1 1004 ? 22.325 4.974 60.526 1.00 33.55 ? 1004 LYS A CA 1 ATOM 7445 C C . LYS A 1 1004 ? 22.126 6.449 60.216 1.00 31.42 ? 1004 LYS A C 1 ATOM 7446 O O . LYS A 1 1004 ? 21.954 7.248 61.129 1.00 32.10 ? 1004 LYS A O 1 ATOM 7447 C CB . LYS A 1 1004 ? 23.821 4.642 60.566 1.00 37.49 ? 1004 LYS A CB 1 ATOM 7448 C CG . LYS A 1 1004 ? 24.139 3.427 61.430 1.00 41.84 ? 1004 LYS A CG 1 ATOM 7449 C CD . LYS A 1 1004 ? 25.623 3.077 61.388 1.00 45.40 ? 1004 LYS A CD 1 ATOM 7450 C CE . LYS A 1 1004 ? 25.935 1.830 62.216 1.00 47.40 ? 1004 LYS A CE 1 ATOM 7451 N NZ . LYS A 1 1004 ? 26.047 2.132 63.673 1.00 47.92 ? 1004 LYS A NZ 1 ATOM 7452 N N . GLY A 1 1005 ? 22.114 6.792 58.932 1.00 29.63 ? 1005 GLY A N 1 ATOM 7453 C CA . GLY A 1 1005 ? 22.095 8.182 58.503 1.00 28.85 ? 1005 GLY A CA 1 ATOM 7454 C C . GLY A 1 1005 ? 20.732 8.842 58.491 1.00 28.30 ? 1005 GLY A C 1 ATOM 7455 O O . GLY A 1 1005 ? 20.616 9.979 58.062 1.00 29.12 ? 1005 GLY A O 1 ATOM 7456 N N . ALA A 1 1006 ? 19.700 8.146 58.964 1.00 28.43 ? 1006 ALA A N 1 ATOM 7457 C CA . ALA A 1 1006 ? 18.349 8.696 58.956 1.00 28.02 ? 1006 ALA A CA 1 ATOM 7458 C C . ALA A 1 1006 ? 18.232 9.858 59.932 1.00 27.96 ? 1006 ALA A C 1 ATOM 7459 O O . ALA A 1 1006 ? 19.142 10.124 60.717 1.00 27.65 ? 1006 ALA A O 1 ATOM 7460 C CB . ALA A 1 1006 ? 17.321 7.620 59.268 1.00 27.46 ? 1006 ALA A CB 1 ATOM 7461 N N . TYR A 1 1007 ? 17.104 10.551 59.878 1.00 28.49 ? 1007 TYR A N 1 ATOM 7462 C CA . TYR A 1 1007 ? 16.934 11.781 60.638 1.00 28.88 ? 1007 TYR A CA 1 ATOM 7463 C C . TYR A 1 1007 ? 16.246 11.613 62.012 1.00 32.12 ? 1007 TYR A C 1 ATOM 7464 O O . TYR A 1 1007 ? 16.059 12.597 62.721 1.00 31.60 ? 1007 TYR A O 1 ATOM 7465 C CB . TYR A 1 1007 ? 16.130 12.782 59.806 1.00 27.42 ? 1007 TYR A CB 1 ATOM 7466 C CG . TYR A 1 1007 ? 16.636 13.091 58.412 1.00 26.13 ? 1007 TYR A CG 1 ATOM 7467 C CD1 . TYR A 1 1007 ? 18.002 13.202 58.124 1.00 26.32 ? 1007 TYR A CD1 1 ATOM 7468 C CD2 . TYR A 1 1007 ? 15.734 13.331 57.384 1.00 25.46 ? 1007 TYR A CD2 1 ATOM 7469 C CE1 . TYR A 1 1007 ? 18.444 13.518 56.835 1.00 26.06 ? 1007 TYR A CE1 1 ATOM 7470 C CE2 . TYR A 1 1007 ? 16.153 13.650 56.105 1.00 25.11 ? 1007 TYR A CE2 1 ATOM 7471 C CZ . TYR A 1 1007 ? 17.502 13.750 55.820 1.00 26.00 ? 1007 TYR A CZ 1 ATOM 7472 O OH . TYR A 1 1007 ? 17.885 14.070 54.521 1.00 24.73 ? 1007 TYR A OH 1 ATOM 7473 N N . HIS A 1 1008 ? 15.889 10.385 62.388 1.00 39.03 ? 1008 HIS A N 1 ATOM 7474 C CA . HIS A 1 1008 ? 14.946 10.139 63.501 1.00 47.42 ? 1008 HIS A CA 1 ATOM 7475 C C . HIS A 1 1008 ? 15.534 10.312 64.902 1.00 51.38 ? 1008 HIS A C 1 ATOM 7476 O O . HIS A 1 1008 ? 16.748 10.420 65.089 1.00 56.22 ? 1008 HIS A O 1 ATOM 7477 C CB . HIS A 1 1008 ? 14.338 8.733 63.386 1.00 53.14 ? 1008 HIS A CB 1 ATOM 7478 C CG . HIS A 1 1008 ? 15.209 7.637 63.932 1.00 59.43 ? 1008 HIS A CG 1 ATOM 7479 N ND1 . HIS A 1 1008 ? 16.293 7.128 63.245 1.00 61.29 ? 1008 HIS A ND1 1 ATOM 7480 C CD2 . HIS A 1 1008 ? 15.137 6.936 65.092 1.00 63.85 ? 1008 HIS A CD2 1 ATOM 7481 C CE1 . HIS A 1 1008 ? 16.856 6.170 63.963 1.00 64.40 ? 1008 HIS A CE1 1 ATOM 7482 N NE2 . HIS A 1 1008 ? 16.173 6.033 65.087 1.00 63.78 ? 1008 HIS A NE2 1 HETATM 7483 C C1 . NAG B 2 . ? 31.413 29.361 35.655 1.00 67.69 ? 1156 NAG A C1 1 HETATM 7484 C C2 . NAG B 2 . ? 30.750 30.463 36.491 1.00 74.31 ? 1156 NAG A C2 1 HETATM 7485 C C3 . NAG B 2 . ? 31.088 31.816 35.855 1.00 77.82 ? 1156 NAG A C3 1 HETATM 7486 C C4 . NAG B 2 . ? 32.608 31.950 35.658 1.00 79.62 ? 1156 NAG A C4 1 HETATM 7487 C C5 . NAG B 2 . ? 33.126 30.748 34.865 1.00 78.28 ? 1156 NAG A C5 1 HETATM 7488 C C6 . NAG B 2 . ? 34.626 30.807 34.585 1.00 78.19 ? 1156 NAG A C6 1 HETATM 7489 C C7 . NAG B 2 . ? 28.694 29.666 37.639 1.00 73.27 ? 1156 NAG A C7 1 HETATM 7490 C C8 . NAG B 2 . ? 27.197 29.545 37.613 1.00 70.92 ? 1156 NAG A C8 1 HETATM 7491 N N2 . NAG B 2 . ? 29.299 30.274 36.601 1.00 74.46 ? 1156 NAG A N2 1 HETATM 7492 O O3 . NAG B 2 . ? 30.555 32.872 36.630 1.00 76.52 ? 1156 NAG A O3 1 HETATM 7493 O O4 . NAG B 2 . ? 32.939 33.149 34.984 1.00 82.78 ? 1156 NAG A O4 1 HETATM 7494 O O5 . NAG B 2 . ? 32.810 29.574 35.595 1.00 71.57 ? 1156 NAG A O5 1 HETATM 7495 O O6 . NAG B 2 . ? 35.336 30.746 35.800 1.00 79.60 ? 1156 NAG A O6 1 HETATM 7496 O O7 . NAG B 2 . ? 29.295 29.198 38.606 1.00 74.66 ? 1156 NAG A O7 1 HETATM 7497 C C1 . NAG C 2 . ? -0.781 -8.450 26.535 1.00 18.33 ? 1373 NAG A C1 1 HETATM 7498 C C2 . NAG C 2 . ? -1.942 -8.909 27.434 1.00 18.53 ? 1373 NAG A C2 1 HETATM 7499 C C3 . NAG C 2 . ? -2.948 -7.793 27.620 1.00 18.51 ? 1373 NAG A C3 1 HETATM 7500 C C4 . NAG C 2 . ? -2.245 -6.557 28.147 1.00 18.50 ? 1373 NAG A C4 1 HETATM 7501 C C5 . NAG C 2 . ? -1.022 -6.224 27.320 1.00 18.38 ? 1373 NAG A C5 1 HETATM 7502 C C6 . NAG C 2 . ? -0.226 -5.138 28.037 1.00 18.79 ? 1373 NAG A C6 1 HETATM 7503 C C7 . NAG C 2 . ? -2.483 -11.300 27.413 1.00 19.17 ? 1373 NAG A C7 1 HETATM 7504 C C8 . NAG C 2 . ? -3.313 -12.388 26.795 1.00 19.65 ? 1373 NAG A C8 1 HETATM 7505 N N2 . NAG C 2 . ? -2.666 -10.065 26.947 1.00 18.85 ? 1373 NAG A N2 1 HETATM 7506 O O3 . NAG C 2 . ? -3.900 -8.235 28.556 1.00 18.02 ? 1373 NAG A O3 1 HETATM 7507 O O4 . NAG C 2 . ? -3.113 -5.451 28.038 1.00 18.58 ? 1373 NAG A O4 1 HETATM 7508 O O5 . NAG C 2 . ? -0.188 -7.347 27.186 1.00 18.46 ? 1373 NAG A O5 1 HETATM 7509 O O6 . NAG C 2 . ? 0.389 -5.722 29.159 1.00 18.49 ? 1373 NAG A O6 1 HETATM 7510 O O7 . NAG C 2 . ? -1.683 -11.588 28.295 1.00 18.96 ? 1373 NAG A O7 1 HETATM 7511 C C1 . NAG D 2 . ? -3.557 -4.996 29.318 1.00 19.57 ? 1374 NAG A C1 1 HETATM 7512 C C2 . NAG D 2 . ? -4.197 -3.634 29.086 1.00 19.93 ? 1374 NAG A C2 1 HETATM 7513 C C3 . NAG D 2 . ? -4.980 -3.139 30.288 1.00 20.65 ? 1374 NAG A C3 1 HETATM 7514 C C4 . NAG D 2 . ? -5.893 -4.245 30.810 1.00 21.67 ? 1374 NAG A C4 1 HETATM 7515 C C5 . NAG D 2 . ? -5.033 -5.473 31.112 1.00 20.92 ? 1374 NAG A C5 1 HETATM 7516 C C6 . NAG D 2 . ? -5.805 -6.624 31.774 1.00 20.76 ? 1374 NAG A C6 1 HETATM 7517 C C7 . NAG D 2 . ? -2.942 -2.232 27.544 1.00 19.60 ? 1374 NAG A C7 1 HETATM 7518 C C8 . NAG D 2 . ? -1.815 -1.253 27.388 1.00 19.56 ? 1374 NAG A C8 1 HETATM 7519 N N2 . NAG D 2 . ? -3.166 -2.685 28.770 1.00 19.50 ? 1374 NAG A N2 1 HETATM 7520 O O3 . NAG D 2 . ? -5.717 -2.008 29.896 1.00 20.72 ? 1374 NAG A O3 1 HETATM 7521 O O4 . NAG D 2 . ? -6.491 -3.790 31.997 1.00 23.83 ? 1374 NAG A O4 1 HETATM 7522 O O5 . NAG D 2 . ? -4.464 -5.911 29.903 1.00 19.72 ? 1374 NAG A O5 1 HETATM 7523 O O6 . NAG D 2 . ? -6.951 -6.939 31.018 1.00 20.87 ? 1374 NAG A O6 1 HETATM 7524 O O7 . NAG D 2 . ? -3.584 -2.591 26.560 1.00 19.53 ? 1374 NAG A O7 1 HETATM 7525 C C1 . BMA E 3 . ? -7.915 -3.802 31.983 1.00 26.95 ? 1375 BMA A C1 1 HETATM 7526 C C2 . BMA E 3 . ? -8.388 -3.661 33.428 1.00 28.12 ? 1375 BMA A C2 1 HETATM 7527 C C3 . BMA E 3 . ? -9.897 -3.843 33.551 1.00 30.15 ? 1375 BMA A C3 1 HETATM 7528 C C4 . BMA E 3 . ? -10.557 -2.886 32.615 1.00 31.80 ? 1375 BMA A C4 1 HETATM 7529 C C5 . BMA E 3 . ? -10.039 -2.952 31.201 1.00 33.81 ? 1375 BMA A C5 1 HETATM 7530 C C6 . BMA E 3 . ? -10.644 -1.715 30.585 1.00 38.68 ? 1375 BMA A C6 1 HETATM 7531 O O2 . BMA E 3 . ? -7.980 -2.405 33.929 1.00 25.61 ? 1375 BMA A O2 1 HETATM 7532 O O3 . BMA E 3 . ? -10.423 -3.451 34.776 1.00 32.14 ? 1375 BMA A O3 1 HETATM 7533 O O4 . BMA E 3 . ? -11.929 -3.139 32.572 1.00 33.01 ? 1375 BMA A O4 1 HETATM 7534 O O5 . BMA E 3 . ? -8.619 -2.964 31.100 1.00 29.77 ? 1375 BMA A O5 1 HETATM 7535 O O6 . BMA E 3 . ? -10.472 -1.824 29.227 1.00 47.60 ? 1375 BMA A O6 1 HETATM 7536 C C1 . MAN F 4 . ? -10.920 -4.465 35.585 1.00 33.82 ? 1376 MAN A C1 1 HETATM 7537 C C2 . MAN F 4 . ? -11.768 -3.954 36.699 1.00 36.34 ? 1376 MAN A C2 1 HETATM 7538 C C3 . MAN F 4 . ? -10.791 -3.891 37.807 1.00 34.61 ? 1376 MAN A C3 1 HETATM 7539 C C4 . MAN F 4 . ? -10.271 -5.290 38.089 1.00 34.42 ? 1376 MAN A C4 1 HETATM 7540 C C5 . MAN F 4 . ? -9.549 -5.792 36.859 1.00 34.35 ? 1376 MAN A C5 1 HETATM 7541 C C6 . MAN F 4 . ? -8.974 -7.181 36.949 1.00 34.76 ? 1376 MAN A C6 1 HETATM 7542 O O2 . MAN F 4 . ? -12.742 -4.898 37.050 1.00 41.95 ? 1376 MAN A O2 1 HETATM 7543 O O3 . MAN F 4 . ? -11.489 -3.360 38.860 1.00 35.51 ? 1376 MAN A O3 1 HETATM 7544 O O4 . MAN F 4 . ? -9.322 -5.309 39.108 1.00 34.21 ? 1376 MAN A O4 1 HETATM 7545 O O5 . MAN F 4 . ? -10.384 -5.709 35.744 1.00 32.78 ? 1376 MAN A O5 1 HETATM 7546 O O6 . MAN F 4 . ? -10.008 -8.138 36.861 1.00 35.54 ? 1376 MAN A O6 1 HETATM 7547 C C1 . MAN G 4 . ? -14.054 -4.727 36.630 1.00 48.90 ? 1377 MAN A C1 1 HETATM 7548 C C2 . MAN G 4 . ? -14.829 -5.640 37.547 1.00 53.64 ? 1377 MAN A C2 1 HETATM 7549 C C3 . MAN G 4 . ? -15.068 -7.010 36.964 1.00 53.35 ? 1377 MAN A C3 1 HETATM 7550 C C4 . MAN G 4 . ? -15.851 -6.807 35.730 1.00 56.04 ? 1377 MAN A C4 1 HETATM 7551 C C5 . MAN G 4 . ? -15.108 -5.899 34.767 1.00 56.25 ? 1377 MAN A C5 1 HETATM 7552 C C6 . MAN G 4 . ? -16.000 -4.916 34.030 1.00 57.01 ? 1377 MAN A C6 1 HETATM 7553 O O2 . MAN G 4 . ? -16.092 -5.101 37.791 1.00 61.00 ? 1377 MAN A O2 1 HETATM 7554 O O3 . MAN G 4 . ? -15.813 -7.756 37.853 1.00 51.99 ? 1377 MAN A O3 1 HETATM 7555 O O4 . MAN G 4 . ? -16.035 -8.060 35.099 1.00 58.16 ? 1377 MAN A O4 1 HETATM 7556 O O5 . MAN G 4 . ? -14.043 -5.168 35.320 1.00 52.81 ? 1377 MAN A O5 1 HETATM 7557 O O6 . MAN G 4 . ? -16.595 -3.944 34.890 1.00 57.02 ? 1377 MAN A O6 1 HETATM 7558 C C1 . MAN H 4 . ? -16.060 -4.068 38.779 1.00 66.36 ? 1378 MAN A C1 1 HETATM 7559 C C2 . MAN H 4 . ? -17.373 -4.137 39.508 1.00 69.74 ? 1378 MAN A C2 1 HETATM 7560 C C3 . MAN H 4 . ? -18.469 -3.654 38.565 1.00 70.72 ? 1378 MAN A C3 1 HETATM 7561 C C4 . MAN H 4 . ? -18.171 -2.186 38.292 1.00 68.49 ? 1378 MAN A C4 1 HETATM 7562 C C5 . MAN H 4 . ? -16.861 -2.165 37.547 1.00 65.76 ? 1378 MAN A C5 1 HETATM 7563 C C6 . MAN H 4 . ? -16.450 -0.757 37.189 1.00 64.21 ? 1378 MAN A C6 1 HETATM 7564 O O2 . MAN H 4 . ? -17.272 -3.331 40.678 1.00 69.59 ? 1378 MAN A O2 1 HETATM 7565 O O3 . MAN H 4 . ? -19.766 -3.982 39.097 1.00 70.65 ? 1378 MAN A O3 1 HETATM 7566 O O4 . MAN H 4 . ? -19.138 -1.527 37.486 1.00 67.50 ? 1378 MAN A O4 1 HETATM 7567 O O5 . MAN H 4 . ? -15.868 -2.722 38.362 1.00 65.21 ? 1378 MAN A O5 1 HETATM 7568 O O6 . MAN H 4 . ? -16.883 -0.434 35.870 1.00 63.09 ? 1378 MAN A O6 1 HETATM 7569 C C1 . MAN I 4 . ? -11.515 -2.478 28.505 1.00 61.55 ? 1379 MAN A C1 1 HETATM 7570 C C2 . MAN I 4 . ? -10.948 -3.049 27.226 1.00 66.40 ? 1379 MAN A C2 1 HETATM 7571 C C3 . MAN I 4 . ? -10.977 -2.000 26.135 1.00 71.18 ? 1379 MAN A C3 1 HETATM 7572 C C4 . MAN I 4 . ? -12.412 -1.502 25.966 1.00 71.39 ? 1379 MAN A C4 1 HETATM 7573 C C5 . MAN I 4 . ? -12.820 -0.852 27.264 1.00 72.23 ? 1379 MAN A C5 1 HETATM 7574 C C6 . MAN I 4 . ? -14.201 -0.199 27.204 1.00 74.11 ? 1379 MAN A C6 1 HETATM 7575 O O2 . MAN I 4 . ? -11.726 -4.172 26.828 1.00 65.51 ? 1379 MAN A O2 1 HETATM 7576 O O3 . MAN I 4 . ? -10.464 -2.646 24.996 1.00 73.73 ? 1379 MAN A O3 1 HETATM 7577 O O4 . MAN I 4 . ? -12.546 -0.523 24.950 1.00 69.88 ? 1379 MAN A O4 1 HETATM 7578 O O5 . MAN I 4 . ? -12.806 -1.860 28.259 1.00 66.37 ? 1379 MAN A O5 1 HETATM 7579 O O6 . MAN I 4 . ? -14.319 0.846 26.223 1.00 74.50 ? 1379 MAN A O6 1 HETATM 7580 C C1 . MAN J 4 . ? -9.155 -2.161 24.695 1.00 75.70 ? 1380 MAN A C1 1 HETATM 7581 C C2 . MAN J 4 . ? -8.969 -2.337 23.184 1.00 75.13 ? 1380 MAN A C2 1 HETATM 7582 C C3 . MAN J 4 . ? -8.332 -3.666 22.813 1.00 75.72 ? 1380 MAN A C3 1 HETATM 7583 C C4 . MAN J 4 . ? -7.136 -3.974 23.688 1.00 75.12 ? 1380 MAN A C4 1 HETATM 7584 C C5 . MAN J 4 . ? -7.521 -3.916 25.160 1.00 75.59 ? 1380 MAN A C5 1 HETATM 7585 C C6 . MAN J 4 . ? -6.377 -4.284 26.080 1.00 72.10 ? 1380 MAN A C6 1 HETATM 7586 O O2 . MAN J 4 . ? -8.249 -1.276 22.569 1.00 72.76 ? 1380 MAN A O2 1 HETATM 7587 O O3 . MAN J 4 . ? -7.931 -3.693 21.439 1.00 74.60 ? 1380 MAN A O3 1 HETATM 7588 O O4 . MAN J 4 . ? -6.834 -5.294 23.301 1.00 74.00 ? 1380 MAN A O4 1 HETATM 7589 O O5 . MAN J 4 . ? -8.047 -2.610 25.505 1.00 77.19 ? 1380 MAN A O5 1 HETATM 7590 O O6 . MAN J 4 . ? -6.574 -5.572 26.664 1.00 69.88 ? 1380 MAN A O6 1 HETATM 7591 C C1 . NAG K 2 . ? 20.973 -19.164 -6.556 1.00 49.07 ? 1478 NAG A C1 1 HETATM 7592 C C2 . NAG K 2 . ? 22.057 -18.479 -7.392 1.00 53.01 ? 1478 NAG A C2 1 HETATM 7593 C C3 . NAG K 2 . ? 23.231 -19.432 -7.607 1.00 54.47 ? 1478 NAG A C3 1 HETATM 7594 C C4 . NAG K 2 . ? 23.774 -19.859 -6.249 1.00 56.31 ? 1478 NAG A C4 1 HETATM 7595 C C5 . NAG K 2 . ? 22.639 -20.440 -5.405 1.00 55.92 ? 1478 NAG A C5 1 HETATM 7596 C C6 . NAG K 2 . ? 23.124 -20.771 -3.996 1.00 56.36 ? 1478 NAG A C6 1 HETATM 7597 C C7 . NAG K 2 . ? 21.552 -16.679 -8.991 1.00 52.69 ? 1478 NAG A C7 1 HETATM 7598 C C8 . NAG K 2 . ? 20.945 -16.331 -10.321 1.00 51.40 ? 1478 NAG A C8 1 HETATM 7599 N N2 . NAG K 2 . ? 21.515 -17.973 -8.647 1.00 52.39 ? 1478 NAG A N2 1 HETATM 7600 O O3 . NAG K 2 . ? 24.253 -18.789 -8.327 1.00 55.01 ? 1478 NAG A O3 1 HETATM 7601 O O4 . NAG K 2 . ? 24.838 -20.784 -6.405 1.00 58.02 ? 1478 NAG A O4 1 HETATM 7602 O O5 . NAG K 2 . ? 21.550 -19.529 -5.312 1.00 51.69 ? 1478 NAG A O5 1 HETATM 7603 O O6 . NAG K 2 . ? 22.275 -21.746 -3.432 1.00 55.74 ? 1478 NAG A O6 1 HETATM 7604 O O7 . NAG K 2 . ? 22.049 -15.786 -8.297 1.00 52.05 ? 1478 NAG A O7 1 HETATM 7605 C C1 . NAG L 2 . ? -3.198 -16.836 21.675 1.00 22.20 ? 1622 NAG A C1 1 HETATM 7606 C C2 . NAG L 2 . ? -4.265 -15.795 21.990 1.00 22.86 ? 1622 NAG A C2 1 HETATM 7607 C C3 . NAG L 2 . ? -4.887 -15.264 20.695 1.00 22.36 ? 1622 NAG A C3 1 HETATM 7608 C C4 . NAG L 2 . ? -3.787 -14.722 19.802 1.00 21.53 ? 1622 NAG A C4 1 HETATM 7609 C C5 . NAG L 2 . ? -2.678 -15.756 19.638 1.00 21.87 ? 1622 NAG A C5 1 HETATM 7610 C C6 . NAG L 2 . ? -1.533 -15.210 18.800 1.00 22.05 ? 1622 NAG A C6 1 HETATM 7611 C C7 . NAG L 2 . ? -5.582 -15.837 24.121 1.00 25.84 ? 1622 NAG A C7 1 HETATM 7612 C C8 . NAG L 2 . ? -6.772 -16.467 24.807 1.00 24.94 ? 1622 NAG A C8 1 HETATM 7613 N N2 . NAG L 2 . ? -5.325 -16.286 22.860 1.00 25.47 ? 1622 NAG A N2 1 HETATM 7614 O O3 . NAG L 2 . ? -5.778 -14.194 20.967 1.00 22.95 ? 1622 NAG A O3 1 HETATM 7615 O O4 . NAG L 2 . ? -4.379 -14.509 18.551 1.00 21.14 ? 1622 NAG A O4 1 HETATM 7616 O O5 . NAG L 2 . ? -2.195 -16.216 20.888 1.00 21.15 ? 1622 NAG A O5 1 HETATM 7617 O O6 . NAG L 2 . ? -0.654 -16.271 18.551 1.00 22.97 ? 1622 NAG A O6 1 HETATM 7618 O O7 . NAG L 2 . ? -4.916 -14.981 24.739 1.00 24.86 ? 1622 NAG A O7 1 HETATM 7619 C C1 . NAG M 2 . ? -4.371 -13.132 18.128 1.00 20.50 ? 1623 NAG A C1 1 HETATM 7620 C C2 . NAG M 2 . ? -4.592 -13.109 16.611 1.00 20.16 ? 1623 NAG A C2 1 HETATM 7621 C C3 . NAG M 2 . ? -4.767 -11.685 16.109 1.00 20.53 ? 1623 NAG A C3 1 HETATM 7622 C C4 . NAG M 2 . ? -5.829 -10.957 16.922 1.00 21.58 ? 1623 NAG A C4 1 HETATM 7623 C C5 . NAG M 2 . ? -5.476 -11.048 18.404 1.00 21.61 ? 1623 NAG A C5 1 HETATM 7624 C C6 . NAG M 2 . ? -6.538 -10.416 19.272 1.00 22.79 ? 1623 NAG A C6 1 HETATM 7625 C C7 . NAG M 2 . ? -3.444 -14.938 15.436 1.00 18.91 ? 1623 NAG A C7 1 HETATM 7626 C C8 . NAG M 2 . ? -2.171 -15.420 14.824 1.00 19.29 ? 1623 NAG A C8 1 HETATM 7627 N N2 . NAG M 2 . ? -3.446 -13.712 15.962 1.00 19.83 ? 1623 NAG A N2 1 HETATM 7628 O O3 . NAG M 2 . ? -5.144 -11.737 14.772 1.00 19.82 ? 1623 NAG A O3 1 HETATM 7629 O O4 . NAG M 2 . ? -5.872 -9.592 16.535 1.00 22.38 ? 1623 NAG A O4 1 HETATM 7630 O O5 . NAG M 2 . ? -5.356 -12.383 18.805 1.00 19.99 ? 1623 NAG A O5 1 HETATM 7631 O O6 . NAG M 2 . ? -6.085 -10.487 20.600 1.00 25.43 ? 1623 NAG A O6 1 HETATM 7632 O O7 . NAG M 2 . ? -4.406 -15.681 15.419 1.00 17.88 ? 1623 NAG A O7 1 HETATM 7633 C C1 . BMA N 3 . ? -7.217 -9.138 16.317 1.00 22.93 ? 1624 BMA A C1 1 HETATM 7634 C C2 . BMA N 3 . ? -7.215 -7.644 16.045 1.00 23.66 ? 1624 BMA A C2 1 HETATM 7635 C C3 . BMA N 3 . ? -8.595 -7.135 15.618 1.00 24.99 ? 1624 BMA A C3 1 HETATM 7636 C C4 . BMA N 3 . ? -9.190 -8.064 14.553 1.00 23.77 ? 1624 BMA A C4 1 HETATM 7637 C C5 . BMA N 3 . ? -9.163 -9.511 15.015 1.00 23.00 ? 1624 BMA A C5 1 HETATM 7638 C C6 . BMA N 3 . ? -9.763 -10.496 14.014 1.00 22.73 ? 1624 BMA A C6 1 HETATM 7639 O O2 . BMA N 3 . ? -6.271 -7.411 15.000 1.00 22.86 ? 1624 BMA A O2 1 HETATM 7640 O O3 . BMA N 3 . ? -8.490 -5.801 15.076 1.00 28.87 ? 1624 BMA A O3 1 HETATM 7641 O O4 . BMA N 3 . ? -10.538 -7.716 14.261 1.00 22.99 ? 1624 BMA A O4 1 HETATM 7642 O O5 . BMA N 3 . ? -7.799 -9.836 15.219 1.00 23.10 ? 1624 BMA A O5 1 HETATM 7643 O O6 . BMA N 3 . ? -9.479 -10.099 12.664 1.00 22.33 ? 1624 BMA A O6 1 HETATM 7644 C C1 . MAN O 4 . ? -8.312 -10.739 12.144 1.00 22.20 ? 1625 MAN A C1 1 HETATM 7645 C C2 . MAN O 4 . ? -7.798 -9.919 10.970 1.00 22.81 ? 1625 MAN A C2 1 HETATM 7646 C C3 . MAN O 4 . ? -8.808 -9.916 9.838 1.00 23.43 ? 1625 MAN A C3 1 HETATM 7647 C C4 . MAN O 4 . ? -9.161 -11.357 9.486 1.00 23.84 ? 1625 MAN A C4 1 HETATM 7648 C C5 . MAN O 4 . ? -9.617 -12.082 10.746 1.00 24.31 ? 1625 MAN A C5 1 HETATM 7649 C C6 . MAN O 4 . ? -9.952 -13.537 10.493 1.00 25.27 ? 1625 MAN A C6 1 HETATM 7650 O O2 . MAN O 4 . ? -6.599 -10.479 10.501 1.00 22.21 ? 1625 MAN A O2 1 HETATM 7651 O O3 . MAN O 4 . ? -8.244 -9.271 8.730 1.00 24.61 ? 1625 MAN A O3 1 HETATM 7652 O O4 . MAN O 4 . ? -10.202 -11.349 8.556 1.00 23.78 ? 1625 MAN A O4 1 HETATM 7653 O O5 . MAN O 4 . ? -8.595 -12.045 11.719 1.00 22.51 ? 1625 MAN A O5 1 HETATM 7654 O O6 . MAN O 4 . ? -10.851 -13.899 11.522 1.00 26.37 ? 1625 MAN A O6 1 HETATM 7655 C C1 . MAN P 4 . ? -9.025 -8.134 8.283 1.00 27.73 ? 1626 MAN A C1 1 HETATM 7656 C C2 . MAN P 4 . ? -8.493 -7.732 6.915 1.00 28.37 ? 1626 MAN A C2 1 HETATM 7657 C C3 . MAN P 4 . ? -7.083 -7.161 7.068 1.00 29.43 ? 1626 MAN A C3 1 HETATM 7658 C C4 . MAN P 4 . ? -7.132 -5.962 8.022 1.00 30.41 ? 1626 MAN A C4 1 HETATM 7659 C C5 . MAN P 4 . ? -7.690 -6.473 9.352 1.00 30.59 ? 1626 MAN A C5 1 HETATM 7660 C C6 . MAN P 4 . ? -7.669 -5.404 10.445 1.00 31.33 ? 1626 MAN A C6 1 HETATM 7661 O O2 . MAN P 4 . ? -9.393 -6.777 6.401 1.00 28.88 ? 1626 MAN A O2 1 HETATM 7662 O O3 . MAN P 4 . ? -6.503 -6.869 5.816 1.00 29.08 ? 1626 MAN A O3 1 HETATM 7663 O O4 . MAN P 4 . ? -5.856 -5.405 8.225 1.00 30.37 ? 1626 MAN A O4 1 HETATM 7664 O O5 . MAN P 4 . ? -8.999 -6.991 9.137 1.00 27.70 ? 1626 MAN A O5 1 HETATM 7665 O O6 . MAN P 4 . ? -8.976 -5.057 10.821 1.00 32.78 ? 1626 MAN A O6 1 HETATM 7666 C C1 . MAN Q 4 . ? -8.846 -4.785 16.025 1.00 33.03 ? 1627 MAN A C1 1 HETATM 7667 C C2 . MAN Q 4 . ? -8.983 -3.426 15.352 1.00 36.08 ? 1627 MAN A C2 1 HETATM 7668 C C3 . MAN Q 4 . ? -7.658 -3.003 14.761 1.00 35.37 ? 1627 MAN A C3 1 HETATM 7669 C C4 . MAN Q 4 . ? -6.635 -2.879 15.880 1.00 35.79 ? 1627 MAN A C4 1 HETATM 7670 C C5 . MAN Q 4 . ? -6.633 -4.123 16.797 1.00 35.16 ? 1627 MAN A C5 1 HETATM 7671 C C6 . MAN Q 4 . ? -5.985 -3.793 18.140 1.00 35.89 ? 1627 MAN A C6 1 HETATM 7672 O O2 . MAN Q 4 . ? -9.290 -2.467 16.340 1.00 42.03 ? 1627 MAN A O2 1 HETATM 7673 O O3 . MAN Q 4 . ? -7.805 -1.739 14.177 1.00 35.17 ? 1627 MAN A O3 1 HETATM 7674 O O4 . MAN Q 4 . ? -5.364 -2.613 15.310 1.00 34.78 ? 1627 MAN A O4 1 HETATM 7675 O O5 . MAN Q 4 . ? -7.918 -4.666 17.083 1.00 32.61 ? 1627 MAN A O5 1 HETATM 7676 O O6 . MAN Q 4 . ? -5.844 -4.979 18.899 1.00 37.97 ? 1627 MAN A O6 1 HETATM 7677 C C1 . MAN R 4 . ? -10.681 -2.075 16.379 1.00 50.60 ? 1628 MAN A C1 1 HETATM 7678 C C2 . MAN R 4 . ? -10.835 -0.829 17.267 1.00 52.96 ? 1628 MAN A C2 1 HETATM 7679 C C3 . MAN R 4 . ? -10.439 -1.190 18.705 1.00 51.85 ? 1628 MAN A C3 1 HETATM 7680 C C4 . MAN R 4 . ? -11.152 -2.448 19.211 1.00 52.00 ? 1628 MAN A C4 1 HETATM 7681 C C5 . MAN R 4 . ? -11.268 -3.568 18.168 1.00 52.14 ? 1628 MAN A C5 1 HETATM 7682 C C6 . MAN R 4 . ? -12.357 -4.569 18.572 1.00 51.96 ? 1628 MAN A C6 1 HETATM 7683 O O2 . MAN R 4 . ? -12.169 -0.352 17.281 1.00 58.25 ? 1628 MAN A O2 1 HETATM 7684 O O3 . MAN R 4 . ? -10.708 -0.118 19.586 1.00 49.14 ? 1628 MAN A O3 1 HETATM 7685 O O4 . MAN R 4 . ? -10.444 -2.972 20.316 1.00 49.53 ? 1628 MAN A O4 1 HETATM 7686 O O5 . MAN R 4 . ? -11.555 -3.089 16.856 1.00 50.85 ? 1628 MAN A O5 1 HETATM 7687 O O6 . MAN R 4 . ? -11.949 -5.887 18.259 1.00 50.85 ? 1628 MAN A O6 1 HETATM 7688 C C1 . MAN S 4 . ? -12.553 0.527 16.196 1.00 62.08 ? 1629 MAN A C1 1 HETATM 7689 C C2 . MAN S 4 . ? -13.938 1.083 16.564 1.00 64.17 ? 1629 MAN A C2 1 HETATM 7690 C C3 . MAN S 4 . ? -15.016 -0.010 16.454 1.00 65.59 ? 1629 MAN A C3 1 HETATM 7691 C C4 . MAN S 4 . ? -14.946 -0.754 15.111 1.00 66.12 ? 1629 MAN A C4 1 HETATM 7692 C C5 . MAN S 4 . ? -13.509 -1.208 14.838 1.00 65.32 ? 1629 MAN A C5 1 HETATM 7693 C C6 . MAN S 4 . ? -13.356 -1.907 13.481 1.00 64.04 ? 1629 MAN A C6 1 HETATM 7694 O O2 . MAN S 4 . ? -14.268 2.219 15.783 1.00 60.79 ? 1629 MAN A O2 1 HETATM 7695 O O3 . MAN S 4 . ? -16.303 0.527 16.693 1.00 64.20 ? 1629 MAN A O3 1 HETATM 7696 O O4 . MAN S 4 . ? -15.780 -1.895 15.143 1.00 65.13 ? 1629 MAN A O4 1 HETATM 7697 O O5 . MAN S 4 . ? -12.614 -0.098 14.921 1.00 64.35 ? 1629 MAN A O5 1 HETATM 7698 O O6 . MAN S 4 . ? -13.016 -3.268 13.664 1.00 61.75 ? 1629 MAN A O6 1 HETATM 7699 C C1 . MAN T 4 . ? -11.451 -15.153 11.201 1.00 27.94 ? 1630 MAN A C1 1 HETATM 7700 C C2 . MAN T 4 . ? -12.626 -15.442 12.136 1.00 28.95 ? 1630 MAN A C2 1 HETATM 7701 C C3 . MAN T 4 . ? -12.114 -15.652 13.553 1.00 28.06 ? 1630 MAN A C3 1 HETATM 7702 C C4 . MAN T 4 . ? -11.190 -16.856 13.504 1.00 27.53 ? 1630 MAN A C4 1 HETATM 7703 C C5 . MAN T 4 . ? -10.034 -16.566 12.538 1.00 27.79 ? 1630 MAN A C5 1 HETATM 7704 C C6 . MAN T 4 . ? -9.116 -17.769 12.346 1.00 27.37 ? 1630 MAN A C6 1 HETATM 7705 O O2 . MAN T 4 . ? -13.187 -16.672 11.726 1.00 29.97 ? 1630 MAN A O2 1 HETATM 7706 O O3 . MAN T 4 . ? -13.181 -15.892 14.432 1.00 27.22 ? 1630 MAN A O3 1 HETATM 7707 O O4 . MAN T 4 . ? -10.696 -17.111 14.791 1.00 27.73 ? 1630 MAN A O4 1 HETATM 7708 O O5 . MAN T 4 . ? -10.496 -16.190 11.252 1.00 27.03 ? 1630 MAN A O5 1 HETATM 7709 O O6 . MAN T 4 . ? -7.945 -17.255 11.767 1.00 28.15 ? 1630 MAN A O6 1 HETATM 7710 C C1 . MAN U 4 . ? -14.344 -16.547 10.883 1.00 31.13 ? 1631 MAN A C1 1 HETATM 7711 C C2 . MAN U 4 . ? -15.069 -17.895 10.925 1.00 30.74 ? 1631 MAN A C2 1 HETATM 7712 C C3 . MAN U 4 . ? -14.254 -18.971 10.186 1.00 32.30 ? 1631 MAN A C3 1 HETATM 7713 C C4 . MAN U 4 . ? -13.905 -18.486 8.785 1.00 32.84 ? 1631 MAN A C4 1 HETATM 7714 C C5 . MAN U 4 . ? -13.186 -17.133 8.882 1.00 33.68 ? 1631 MAN A C5 1 HETATM 7715 C C6 . MAN U 4 . ? -12.837 -16.563 7.509 1.00 34.84 ? 1631 MAN A C6 1 HETATM 7716 O O2 . MAN U 4 . ? -16.348 -17.732 10.366 1.00 29.70 ? 1631 MAN A O2 1 HETATM 7717 O O3 . MAN U 4 . ? -14.892 -20.234 10.120 1.00 31.00 ? 1631 MAN A O3 1 HETATM 7718 O O4 . MAN U 4 . ? -13.094 -19.462 8.170 1.00 33.80 ? 1631 MAN A O4 1 HETATM 7719 O O5 . MAN U 4 . ? -13.992 -16.180 9.562 1.00 31.53 ? 1631 MAN A O5 1 HETATM 7720 O O6 . MAN U 4 . ? -11.500 -16.104 7.507 1.00 37.35 ? 1631 MAN A O6 1 HETATM 7721 C C1 . NAG V 2 . ? -1.804 43.398 59.925 1.00 45.27 ? 1739 NAG A C1 1 HETATM 7722 C C2 . NAG V 2 . ? -3.286 43.028 60.116 1.00 45.78 ? 1739 NAG A C2 1 HETATM 7723 C C3 . NAG V 2 . ? -4.234 44.022 59.441 1.00 45.74 ? 1739 NAG A C3 1 HETATM 7724 C C4 . NAG V 2 . ? -3.824 45.466 59.717 1.00 48.11 ? 1739 NAG A C4 1 HETATM 7725 C C5 . NAG V 2 . ? -2.344 45.675 59.405 1.00 50.46 ? 1739 NAG A C5 1 HETATM 7726 C C6 . NAG V 2 . ? -1.885 47.091 59.749 1.00 52.16 ? 1739 NAG A C6 1 HETATM 7727 C C7 . NAG V 2 . ? -3.841 40.619 60.368 1.00 44.52 ? 1739 NAG A C7 1 HETATM 7728 C C8 . NAG V 2 . ? -4.100 39.303 59.681 1.00 45.00 ? 1739 NAG A C8 1 HETATM 7729 N N2 . NAG V 2 . ? -3.560 41.686 59.600 1.00 45.53 ? 1739 NAG A N2 1 HETATM 7730 O O3 . NAG V 2 . ? -5.555 43.797 59.883 1.00 42.14 ? 1739 NAG A O3 1 HETATM 7731 O O4 . NAG V 2 . ? -4.597 46.331 58.915 1.00 50.33 ? 1739 NAG A O4 1 HETATM 7732 O O5 . NAG V 2 . ? -1.547 44.770 60.148 1.00 48.91 ? 1739 NAG A O5 1 HETATM 7733 O O6 . NAG V 2 . ? -0.582 47.297 59.243 1.00 51.90 ? 1739 NAG A O6 1 HETATM 7734 O O7 . NAG V 2 . ? -3.896 40.653 61.590 1.00 41.11 ? 1739 NAG A O7 1 HETATM 7735 C C1 . NAG W 2 . ? 5.141 24.498 65.577 1.00 28.42 ? 1760 NAG A C1 1 HETATM 7736 C C2 . NAG W 2 . ? 5.073 24.985 67.021 1.00 30.00 ? 1760 NAG A C2 1 HETATM 7737 C C3 . NAG W 2 . ? 6.437 25.045 67.724 1.00 31.36 ? 1760 NAG A C3 1 HETATM 7738 C C4 . NAG W 2 . ? 7.181 23.736 67.549 1.00 32.49 ? 1760 NAG A C4 1 HETATM 7739 C C5 . NAG W 2 . ? 7.349 23.552 66.051 1.00 32.17 ? 1760 NAG A C5 1 HETATM 7740 C C6 . NAG W 2 . ? 8.167 22.310 65.740 1.00 32.27 ? 1760 NAG A C6 1 HETATM 7741 C C7 . NAG W 2 . ? 3.176 26.393 67.645 1.00 28.77 ? 1760 NAG A C7 1 HETATM 7742 C C8 . NAG W 2 . ? 2.578 27.762 67.693 1.00 28.37 ? 1760 NAG A C8 1 HETATM 7743 N N2 . NAG W 2 . ? 4.388 26.266 67.104 1.00 29.32 ? 1760 NAG A N2 1 HETATM 7744 O O3 . NAG W 2 . ? 6.224 25.280 69.091 1.00 32.09 ? 1760 NAG A O3 1 HETATM 7745 O O4 . NAG W 2 . ? 8.423 23.716 68.235 1.00 34.31 ? 1760 NAG A O4 1 HETATM 7746 O O5 . NAG W 2 . ? 6.070 23.427 65.445 1.00 30.19 ? 1760 NAG A O5 1 HETATM 7747 O O6 . NAG W 2 . ? 8.124 22.064 64.352 1.00 33.79 ? 1760 NAG A O6 1 HETATM 7748 O O7 . NAG W 2 . ? 2.532 25.458 68.108 1.00 29.43 ? 1760 NAG A O7 1 HETATM 7749 C C1 . NAG X 2 . ? 3.730 31.569 38.375 1.00 24.37 ? 1777 NAG A C1 1 HETATM 7750 C C2 . NAG X 2 . ? 3.679 31.330 36.871 1.00 24.71 ? 1777 NAG A C2 1 HETATM 7751 C C3 . NAG X 2 . ? 5.064 31.586 36.295 1.00 24.61 ? 1777 NAG A C3 1 HETATM 7752 C C4 . NAG X 2 . ? 5.490 32.982 36.709 1.00 25.34 ? 1777 NAG A C4 1 HETATM 7753 C C5 . NAG X 2 . ? 5.524 33.074 38.227 1.00 25.64 ? 1777 NAG A C5 1 HETATM 7754 C C6 . NAG X 2 . ? 6.007 34.450 38.711 1.00 26.32 ? 1777 NAG A C6 1 HETATM 7755 C C7 . NAG X 2 . ? 2.046 29.664 36.119 1.00 25.48 ? 1777 NAG A C7 1 HETATM 7756 C C8 . NAG X 2 . ? 1.764 28.208 35.903 1.00 25.50 ? 1777 NAG A C8 1 HETATM 7757 N N2 . NAG X 2 . ? 3.253 29.969 36.601 1.00 24.56 ? 1777 NAG A N2 1 HETATM 7758 O O3 . NAG X 2 . ? 5.022 31.518 34.898 1.00 23.93 ? 1777 NAG A O3 1 HETATM 7759 O O4 . NAG X 2 . ? 6.740 33.316 36.155 1.00 26.65 ? 1777 NAG A O4 1 HETATM 7760 O O5 . NAG X 2 . ? 4.196 32.871 38.653 1.00 24.72 ? 1777 NAG A O5 1 HETATM 7761 O O6 . NAG X 2 . ? 5.375 35.475 37.969 1.00 25.78 ? 1777 NAG A O6 1 HETATM 7762 O O7 . NAG X 2 . ? 1.165 30.494 35.860 1.00 26.50 ? 1777 NAG A O7 1 HETATM 7763 C C1 . NAG Y 2 . ? -10.437 8.230 36.944 1.00 19.95 ? 1914 NAG A C1 1 HETATM 7764 C C2 . NAG Y 2 . ? -9.166 8.609 36.159 1.00 19.95 ? 1914 NAG A C2 1 HETATM 7765 C C3 . NAG Y 2 . ? -9.098 10.097 35.850 1.00 20.31 ? 1914 NAG A C3 1 HETATM 7766 C C4 . NAG Y 2 . ? -10.444 10.558 35.277 1.00 20.55 ? 1914 NAG A C4 1 HETATM 7767 C C5 . NAG Y 2 . ? -11.580 10.049 36.169 1.00 20.15 ? 1914 NAG A C5 1 HETATM 7768 C C6 . NAG Y 2 . ? -12.982 10.527 35.797 1.00 19.97 ? 1914 NAG A C6 1 HETATM 7769 C C7 . NAG Y 2 . ? -7.201 7.175 36.322 1.00 18.06 ? 1914 NAG A C7 1 HETATM 7770 C C8 . NAG Y 2 . ? -6.053 6.701 37.154 1.00 17.91 ? 1914 NAG A C8 1 HETATM 7771 N N2 . NAG Y 2 . ? -7.991 8.098 36.848 1.00 19.09 ? 1914 NAG A N2 1 HETATM 7772 O O3 . NAG Y 2 . ? -8.038 10.296 34.935 1.00 19.79 ? 1914 NAG A O3 1 HETATM 7773 O O4 . NAG Y 2 . ? -10.489 11.965 35.268 1.00 22.61 ? 1914 NAG A O4 1 HETATM 7774 O O5 . NAG Y 2 . ? -11.563 8.646 36.190 1.00 19.67 ? 1914 NAG A O5 1 HETATM 7775 O O6 . NAG Y 2 . ? -13.333 9.989 34.551 1.00 19.56 ? 1914 NAG A O6 1 HETATM 7776 O O7 . NAG Y 2 . ? -7.362 6.718 35.203 1.00 17.57 ? 1914 NAG A O7 1 HETATM 7777 C C1 . NAG Z 2 . ? -10.328 12.536 33.962 1.00 25.15 ? 1915 NAG A C1 1 HETATM 7778 C C2 . NAG Z 2 . ? -10.866 13.964 33.992 1.00 27.26 ? 1915 NAG A C2 1 HETATM 7779 C C3 . NAG Z 2 . ? -10.574 14.682 32.676 1.00 29.12 ? 1915 NAG A C3 1 HETATM 7780 C C4 . NAG Z 2 . ? -9.123 14.512 32.232 1.00 30.55 ? 1915 NAG A C4 1 HETATM 7781 C C5 . NAG Z 2 . ? -8.768 13.017 32.256 1.00 28.64 ? 1915 NAG A C5 1 HETATM 7782 C C6 . NAG Z 2 . ? -7.337 12.727 31.790 1.00 28.08 ? 1915 NAG A C6 1 HETATM 7783 C C7 . NAG Z 2 . ? -12.893 14.277 35.370 1.00 27.64 ? 1915 NAG A C7 1 HETATM 7784 C C8 . NAG Z 2 . ? -14.394 14.258 35.440 1.00 27.88 ? 1915 NAG A C8 1 HETATM 7785 N N2 . NAG Z 2 . ? -12.308 13.981 34.206 1.00 27.32 ? 1915 NAG A N2 1 HETATM 7786 O O3 . NAG Z 2 . ? -10.853 16.039 32.861 1.00 29.61 ? 1915 NAG A O3 1 HETATM 7787 O O4 . NAG Z 2 . ? -9.015 15.006 30.916 1.00 33.44 ? 1915 NAG A O4 1 HETATM 7788 O O5 . NAG Z 2 . ? -8.976 12.541 33.569 1.00 26.86 ? 1915 NAG A O5 1 HETATM 7789 O O6 . NAG Z 2 . ? -6.395 13.483 32.529 1.00 26.52 ? 1915 NAG A O6 1 HETATM 7790 O O7 . NAG Z 2 . ? -12.279 14.564 36.379 1.00 28.49 ? 1915 NAG A O7 1 HETATM 7791 C C1 . BMA AA 3 . ? -8.081 16.097 30.781 1.00 39.73 ? 1916 BMA A C1 1 HETATM 7792 C C2 . BMA AA 3 . ? -7.772 16.201 29.293 1.00 41.93 ? 1916 BMA A C2 1 HETATM 7793 C C3 . BMA AA 3 . ? -6.800 17.321 28.952 1.00 44.05 ? 1916 BMA A C3 1 HETATM 7794 C C4 . BMA AA 3 . ? -7.313 18.624 29.566 1.00 44.06 ? 1916 BMA A C4 1 HETATM 7795 C C5 . BMA AA 3 . ? -7.837 18.520 31.014 1.00 44.97 ? 1916 BMA A C5 1 HETATM 7796 C C6 . BMA AA 3 . ? -8.733 19.733 31.325 1.00 46.34 ? 1916 BMA A C6 1 HETATM 7797 O O2 . BMA AA 3 . ? -9.007 16.456 28.634 1.00 41.73 ? 1916 BMA A O2 1 HETATM 7798 O O3 . BMA AA 3 . ? -6.665 17.390 27.505 1.00 46.41 ? 1916 BMA A O3 1 HETATM 7799 O O4 . BMA AA 3 . ? -6.240 19.568 29.597 1.00 45.27 ? 1916 BMA A O4 1 HETATM 7800 O O5 . BMA AA 3 . ? -8.595 17.329 31.289 1.00 41.73 ? 1916 BMA A O5 1 HETATM 7801 O O6 . BMA AA 3 . ? -8.602 20.187 32.681 1.00 46.40 ? 1916 BMA A O6 1 HETATM 7802 C C1 . MAN BA 4 . ? -5.355 17.648 26.972 1.00 49.68 ? 1917 MAN A C1 1 HETATM 7803 C C2 . MAN BA 4 . ? -5.360 17.508 25.444 1.00 52.10 ? 1917 MAN A C2 1 HETATM 7804 C C3 . MAN BA 4 . ? -5.334 16.040 25.046 1.00 49.59 ? 1917 MAN A C3 1 HETATM 7805 C C4 . MAN BA 4 . ? -4.136 15.404 25.694 1.00 48.13 ? 1917 MAN A C4 1 HETATM 7806 C C5 . MAN BA 4 . ? -4.207 15.546 27.194 1.00 47.34 ? 1917 MAN A C5 1 HETATM 7807 C C6 . MAN BA 4 . ? -2.997 14.905 27.839 1.00 44.90 ? 1917 MAN A C6 1 HETATM 7808 O O2 . MAN BA 4 . ? -4.212 18.021 24.794 1.00 57.26 ? 1917 MAN A O2 1 HETATM 7809 O O3 . MAN BA 4 . ? -5.191 15.819 23.646 1.00 48.56 ? 1917 MAN A O3 1 HETATM 7810 O O4 . MAN BA 4 . ? -4.085 14.042 25.347 1.00 47.36 ? 1917 MAN A O4 1 HETATM 7811 O O5 . MAN BA 4 . ? -4.296 16.909 27.572 1.00 48.71 ? 1917 MAN A O5 1 HETATM 7812 O O6 . MAN BA 4 . ? -3.245 14.811 29.190 1.00 43.20 ? 1917 MAN A O6 1 HETATM 7813 C C1 . MAN CA 4 . ? -3.867 19.377 24.825 1.00 65.05 ? 1918 MAN A C1 1 HETATM 7814 C C2 . MAN CA 4 . ? -2.898 19.573 23.686 1.00 67.99 ? 1918 MAN A C2 1 HETATM 7815 C C3 . MAN CA 4 . ? -1.555 19.024 24.117 1.00 66.76 ? 1918 MAN A C3 1 HETATM 7816 C C4 . MAN CA 4 . ? -1.062 19.762 25.352 1.00 66.83 ? 1918 MAN A C4 1 HETATM 7817 C C5 . MAN CA 4 . ? -2.018 19.408 26.447 1.00 65.92 ? 1918 MAN A C5 1 HETATM 7818 C C6 . MAN CA 4 . ? -1.781 20.161 27.745 1.00 66.75 ? 1918 MAN A C6 1 HETATM 7819 O O2 . MAN CA 4 . ? -2.666 20.949 23.466 1.00 74.38 ? 1918 MAN A O2 1 HETATM 7820 O O3 . MAN CA 4 . ? -0.627 19.229 23.087 1.00 66.00 ? 1918 MAN A O3 1 HETATM 7821 O O4 . MAN CA 4 . ? 0.287 19.438 25.709 1.00 65.60 ? 1918 MAN A O4 1 HETATM 7822 O O5 . MAN CA 4 . ? -3.265 19.883 26.018 1.00 65.90 ? 1918 MAN A O5 1 HETATM 7823 O O6 . MAN CA 4 . ? -0.700 21.076 27.705 1.00 64.63 ? 1918 MAN A O6 1 HETATM 7824 C C1 . MAN DA 4 . ? -3.881 21.752 23.257 1.00 79.47 ? 1919 MAN A C1 1 HETATM 7825 C C2 . MAN DA 4 . ? -3.496 22.877 22.355 1.00 81.07 ? 1919 MAN A C2 1 HETATM 7826 C C3 . MAN DA 4 . ? -2.819 23.889 23.260 1.00 79.07 ? 1919 MAN A C3 1 HETATM 7827 C C4 . MAN DA 4 . ? -3.957 24.647 23.917 1.00 79.26 ? 1919 MAN A C4 1 HETATM 7828 C C5 . MAN DA 4 . ? -4.542 23.597 24.865 1.00 81.79 ? 1919 MAN A C5 1 HETATM 7829 C C6 . MAN DA 4 . ? -5.951 23.942 25.303 1.00 83.50 ? 1919 MAN A C6 1 HETATM 7830 O O2 . MAN DA 4 . ? -4.716 23.295 21.743 1.00 86.46 ? 1919 MAN A O2 1 HETATM 7831 O O3 . MAN DA 4 . ? -1.757 24.582 22.636 1.00 79.62 ? 1919 MAN A O3 1 HETATM 7832 O O4 . MAN DA 4 . ? -3.704 25.890 24.569 1.00 74.36 ? 1919 MAN A O4 1 HETATM 7833 O O5 . MAN DA 4 . ? -4.762 22.336 24.255 1.00 79.53 ? 1919 MAN A O5 1 HETATM 7834 O O6 . MAN DA 4 . ? -6.623 24.654 24.268 1.00 88.29 ? 1919 MAN A O6 1 HETATM 7835 CL CL . CL EA 5 . ? 14.150 9.924 58.641 1.00 23.57 ? 2001 CL A CL 1 HETATM 7836 O OH2 . 1PE FA 6 . ? 10.290 12.514 24.318 1.00 44.52 ? 3001 1PE A OH2 1 HETATM 7837 C C12 . 1PE FA 6 . ? 9.995 13.578 23.443 1.00 46.88 ? 3001 1PE A C12 1 HETATM 7838 C C22 . 1PE FA 6 . ? 10.449 13.245 22.043 1.00 49.79 ? 3001 1PE A C22 1 HETATM 7839 O OH3 . 1PE FA 6 . ? 11.307 14.205 21.445 1.00 52.38 ? 3001 1PE A OH3 1 HETATM 7840 C C13 . 1PE FA 6 . ? 11.540 16.475 20.706 1.00 55.06 ? 3001 1PE A C13 1 HETATM 7841 C C23 . 1PE FA 6 . ? 10.639 15.253 20.768 1.00 54.12 ? 3001 1PE A C23 1 HETATM 7842 O OH4 . 1PE FA 6 . ? 10.867 17.610 21.202 1.00 56.83 ? 3001 1PE A OH4 1 HETATM 7843 C C14 . 1PE FA 6 . ? 10.989 19.859 22.092 1.00 61.05 ? 3001 1PE A C14 1 HETATM 7844 C C24 . 1PE FA 6 . ? 11.721 18.721 21.405 1.00 59.26 ? 3001 1PE A C24 1 HETATM 7845 O OH5 . 1PE FA 6 . ? 10.804 19.661 23.504 1.00 65.09 ? 3001 1PE A OH5 1 HETATM 7846 C C15 . 1PE FA 6 . ? 10.016 21.930 23.507 1.00 68.76 ? 3001 1PE A C15 1 HETATM 7847 C C25 . 1PE FA 6 . ? 10.753 20.850 24.283 1.00 66.58 ? 3001 1PE A C25 1 HETATM 7848 O OH6 . 1PE FA 6 . ? 9.397 22.847 24.371 1.00 71.06 ? 3001 1PE A OH6 1 HETATM 7849 C C16 . 1PE FA 6 . ? 7.261 22.700 25.414 1.00 68.48 ? 3001 1PE A C16 1 HETATM 7850 C C26 . 1PE FA 6 . ? 7.997 22.944 24.134 1.00 69.77 ? 3001 1PE A C26 1 HETATM 7851 O OH7 . 1PE FA 6 . ? 7.619 23.677 26.369 1.00 67.61 ? 3001 1PE A OH7 1 HETATM 7852 C C1 . GAL GA 7 . ? 12.811 10.238 19.486 1.00 34.22 ? 4001 GAL A C1 1 HETATM 7853 C C2 . GAL GA 7 . ? 14.069 10.059 20.369 1.00 32.02 ? 4001 GAL A C2 1 HETATM 7854 C C3 . GAL GA 7 . ? 14.001 8.844 21.311 1.00 31.43 ? 4001 GAL A C3 1 HETATM 7855 C C4 . GAL GA 7 . ? 12.617 8.764 21.930 1.00 32.29 ? 4001 GAL A C4 1 HETATM 7856 C C5 . GAL GA 7 . ? 11.672 8.636 20.741 1.00 33.52 ? 4001 GAL A C5 1 HETATM 7857 C C6 . GAL GA 7 . ? 10.314 8.036 21.097 1.00 33.11 ? 4001 GAL A C6 1 HETATM 7858 O O1 . GAL GA 7 . ? 12.691 11.568 18.997 1.00 39.49 ? 4001 GAL A O1 1 HETATM 7859 O O2 . GAL GA 7 . ? 15.209 9.897 19.557 1.00 29.77 ? 4001 GAL A O2 1 HETATM 7860 O O3 . GAL GA 7 . ? 14.989 8.854 22.322 1.00 29.29 ? 4001 GAL A O3 1 HETATM 7861 O O4 . GAL GA 7 . ? 12.324 9.947 22.649 1.00 31.11 ? 4001 GAL A O4 1 HETATM 7862 O O5 . GAL GA 7 . ? 11.600 9.926 20.170 1.00 33.30 ? 4001 GAL A O5 1 HETATM 7863 O O6 . GAL GA 7 . ? 9.364 9.040 21.290 1.00 35.39 ? 4001 GAL A O6 1 HETATM 7864 C C1 . GAL HA 7 . ? 10.501 13.943 15.094 1.00 57.61 ? 4002 GAL A C1 1 HETATM 7865 C C2 . GAL HA 7 . ? 10.933 13.035 13.923 1.00 59.00 ? 4002 GAL A C2 1 HETATM 7866 C C3 . GAL HA 7 . ? 11.856 11.868 14.287 1.00 59.83 ? 4002 GAL A C3 1 HETATM 7867 C C4 . GAL HA 7 . ? 12.441 11.984 15.697 1.00 60.24 ? 4002 GAL A C4 1 HETATM 7868 C C5 . GAL HA 7 . ? 11.304 12.207 16.699 1.00 59.10 ? 4002 GAL A C5 1 HETATM 7869 C C6 . GAL HA 7 . ? 11.842 12.170 18.142 1.00 52.65 ? 4002 GAL A C6 1 HETATM 7870 O O1 . GAL HA 7 . ? 11.357 15.071 15.089 1.00 54.50 ? 4002 GAL A O1 1 HETATM 7871 O O2 . GAL HA 7 . ? 9.806 12.503 13.260 1.00 55.97 ? 4002 GAL A O2 1 HETATM 7872 O O3 . GAL HA 7 . ? 12.884 11.699 13.333 1.00 58.70 ? 4002 GAL A O3 1 HETATM 7873 O O4 . GAL HA 7 . ? 13.403 13.015 15.792 1.00 61.60 ? 4002 GAL A O4 1 HETATM 7874 O O5 . GAL HA 7 . ? 10.515 13.368 16.407 1.00 57.68 ? 4002 GAL A O5 1 HETATM 7875 O O . HOH IA 8 . ? -1.379 -7.939 8.104 1.00 18.26 ? 5001 HOH A O 1 HETATM 7876 O O . HOH IA 8 . ? -4.726 -5.601 34.817 1.00 26.07 ? 5002 HOH A O 1 HETATM 7877 O O . HOH IA 8 . ? -12.873 -0.745 41.788 1.00 24.39 ? 5003 HOH A O 1 HETATM 7878 O O . HOH IA 8 . ? 3.237 -9.082 4.712 1.00 23.21 ? 5004 HOH A O 1 HETATM 7879 O O . HOH IA 8 . ? 15.306 1.638 47.704 1.00 14.49 ? 5005 HOH A O 1 HETATM 7880 O O . HOH IA 8 . ? 19.052 22.840 40.120 1.00 12.54 ? 5006 HOH A O 1 HETATM 7881 O O . HOH IA 8 . ? 6.789 5.650 -1.404 1.00 8.06 ? 5007 HOH A O 1 HETATM 7882 O O . HOH IA 8 . ? 16.693 8.132 33.735 1.00 21.08 ? 5008 HOH A O 1 HETATM 7883 O O . HOH IA 8 . ? 9.657 10.794 8.977 1.00 25.73 ? 5009 HOH A O 1 HETATM 7884 O O . HOH IA 8 . ? -1.597 -24.017 7.275 1.00 21.48 ? 5010 HOH A O 1 HETATM 7885 O O . HOH IA 8 . ? -1.068 -18.632 17.767 1.00 27.34 ? 5011 HOH A O 1 HETATM 7886 O O . HOH IA 8 . ? 16.562 7.199 45.507 1.00 19.43 ? 5012 HOH A O 1 HETATM 7887 O O . HOH IA 8 . ? 1.533 13.358 60.682 1.00 23.05 ? 5013 HOH A O 1 HETATM 7888 O O . HOH IA 8 . ? -8.826 6.419 41.432 1.00 16.66 ? 5014 HOH A O 1 HETATM 7889 O O . HOH IA 8 . ? 7.983 4.429 38.659 1.00 14.33 ? 5015 HOH A O 1 HETATM 7890 O O . HOH IA 8 . ? 4.096 -11.216 36.009 1.00 12.51 ? 5016 HOH A O 1 HETATM 7891 O O . HOH IA 8 . ? 2.359 25.689 44.530 1.00 20.54 ? 5017 HOH A O 1 HETATM 7892 O O . HOH IA 8 . ? 12.567 -1.934 26.362 1.00 16.05 ? 5018 HOH A O 1 HETATM 7893 O O . HOH IA 8 . ? 23.966 5.623 5.072 1.00 17.47 ? 5019 HOH A O 1 HETATM 7894 O O . HOH IA 8 . ? 24.325 13.679 13.962 1.00 16.65 ? 5020 HOH A O 1 HETATM 7895 O O . HOH IA 8 . ? 2.019 -8.377 21.210 1.00 13.01 ? 5021 HOH A O 1 HETATM 7896 O O . HOH IA 8 . ? 11.069 -19.302 15.596 1.00 17.63 ? 5022 HOH A O 1 HETATM 7897 O O . HOH IA 8 . ? 7.365 18.807 32.494 1.00 17.16 ? 5023 HOH A O 1 HETATM 7898 O O . HOH IA 8 . ? 36.039 -0.473 12.201 1.00 17.99 ? 5024 HOH A O 1 HETATM 7899 O O . HOH IA 8 . ? 6.520 -11.392 3.449 1.00 25.45 ? 5025 HOH A O 1 HETATM 7900 O O . HOH IA 8 . ? 16.178 15.383 62.526 1.00 17.30 ? 5026 HOH A O 1 HETATM 7901 O O . HOH IA 8 . ? 7.831 -3.066 52.988 1.00 16.41 ? 5027 HOH A O 1 HETATM 7902 O O . HOH IA 8 . ? -7.259 -2.070 36.405 1.00 23.20 ? 5028 HOH A O 1 HETATM 7903 O O . HOH IA 8 . ? 2.670 9.821 43.008 1.00 36.66 ? 5029 HOH A O 1 HETATM 7904 O O . HOH IA 8 . ? 22.243 7.598 29.208 1.00 16.15 ? 5030 HOH A O 1 HETATM 7905 O O . HOH IA 8 . ? 27.470 21.010 20.455 1.00 14.79 ? 5031 HOH A O 1 HETATM 7906 O O . HOH IA 8 . ? 16.031 -14.564 12.882 1.00 17.63 ? 5032 HOH A O 1 HETATM 7907 O O . HOH IA 8 . ? 15.015 7.687 51.044 1.00 11.64 ? 5033 HOH A O 1 HETATM 7908 O O . HOH IA 8 . ? 9.384 6.261 44.174 1.00 26.33 ? 5034 HOH A O 1 HETATM 7909 O O . HOH IA 8 . ? -4.816 -20.954 0.254 1.00 19.93 ? 5035 HOH A O 1 HETATM 7910 O O . HOH IA 8 . ? 22.232 21.862 26.133 1.00 17.04 ? 5036 HOH A O 1 HETATM 7911 O O . HOH IA 8 . ? 5.646 -4.528 53.166 1.00 21.76 ? 5037 HOH A O 1 HETATM 7912 O O . HOH IA 8 . ? 23.669 1.262 39.393 1.00 15.77 ? 5038 HOH A O 1 HETATM 7913 O O . HOH IA 8 . ? 24.024 9.813 17.087 1.00 17.18 ? 5039 HOH A O 1 HETATM 7914 O O . HOH IA 8 . ? 4.615 21.807 59.135 1.00 15.00 ? 5040 HOH A O 1 HETATM 7915 O O . HOH IA 8 . ? 24.840 -1.269 39.587 1.00 25.70 ? 5041 HOH A O 1 HETATM 7916 O O . HOH IA 8 . ? -12.386 1.422 49.941 1.00 23.47 ? 5042 HOH A O 1 HETATM 7917 O O . HOH IA 8 . ? -4.296 -5.585 59.336 1.00 16.20 ? 5043 HOH A O 1 HETATM 7918 O O . HOH IA 8 . ? 23.171 -4.093 5.952 1.00 18.84 ? 5044 HOH A O 1 HETATM 7919 O O . HOH IA 8 . ? 12.965 8.480 -2.518 1.00 17.39 ? 5045 HOH A O 1 HETATM 7920 O O . HOH IA 8 . ? 21.834 23.062 40.560 1.00 25.92 ? 5046 HOH A O 1 HETATM 7921 O O . HOH IA 8 . ? -1.519 2.926 29.046 1.00 9.34 ? 5047 HOH A O 1 HETATM 7922 O O . HOH IA 8 . ? 0.554 -7.967 2.836 1.00 26.85 ? 5048 HOH A O 1 HETATM 7923 O O . HOH IA 8 . ? 20.129 12.962 53.611 1.00 17.71 ? 5049 HOH A O 1 HETATM 7924 O O . HOH IA 8 . ? -7.510 -10.662 -7.146 1.00 20.44 ? 5050 HOH A O 1 HETATM 7925 O O . HOH IA 8 . ? 31.197 16.133 10.953 1.00 24.34 ? 5051 HOH A O 1 HETATM 7926 O O . HOH IA 8 . ? 33.560 5.128 39.057 1.00 17.70 ? 5052 HOH A O 1 HETATM 7927 O O . HOH IA 8 . ? 0.868 -3.372 30.321 1.00 17.97 ? 5053 HOH A O 1 HETATM 7928 O O . HOH IA 8 . ? 4.024 -1.605 36.454 1.00 10.29 ? 5054 HOH A O 1 HETATM 7929 O O . HOH IA 8 . ? 2.364 -15.142 15.627 1.00 20.56 ? 5055 HOH A O 1 HETATM 7930 O O . HOH IA 8 . ? 15.263 -10.312 8.620 1.00 15.77 ? 5056 HOH A O 1 HETATM 7931 O O . HOH IA 8 . ? 10.221 -19.475 37.077 1.00 16.32 ? 5057 HOH A O 1 HETATM 7932 O O . HOH IA 8 . ? 14.743 19.009 34.694 1.00 18.02 ? 5058 HOH A O 1 HETATM 7933 O O . HOH IA 8 . ? 8.260 9.527 39.066 1.00 30.71 ? 5059 HOH A O 1 HETATM 7934 O O . HOH IA 8 . ? 2.593 -6.138 68.255 1.00 22.52 ? 5060 HOH A O 1 HETATM 7935 O O . HOH IA 8 . ? 1.825 8.464 47.476 1.00 9.40 ? 5061 HOH A O 1 HETATM 7936 O O . HOH IA 8 . ? 15.633 12.779 45.729 1.00 18.82 ? 5062 HOH A O 1 HETATM 7937 O O . HOH IA 8 . ? -3.418 25.177 46.145 1.00 25.57 ? 5063 HOH A O 1 HETATM 7938 O O . HOH IA 8 . ? 5.986 1.730 -3.917 1.00 17.74 ? 5064 HOH A O 1 HETATM 7939 O O . HOH IA 8 . ? 18.709 -8.327 -7.399 1.00 22.63 ? 5065 HOH A O 1 HETATM 7940 O O . HOH IA 8 . ? 28.157 13.772 25.305 1.00 16.61 ? 5066 HOH A O 1 HETATM 7941 O O . HOH IA 8 . ? -1.272 -38.382 4.201 1.00 28.61 ? 5067 HOH A O 1 HETATM 7942 O O . HOH IA 8 . ? 31.125 10.444 34.112 1.00 13.91 ? 5068 HOH A O 1 HETATM 7943 O O . HOH IA 8 . ? -2.030 -15.563 24.917 1.00 21.94 ? 5069 HOH A O 1 HETATM 7944 O O . HOH IA 8 . ? -1.774 0.842 0.220 1.00 15.17 ? 5070 HOH A O 1 HETATM 7945 O O . HOH IA 8 . ? -3.863 2.231 1.324 1.00 22.92 ? 5071 HOH A O 1 HETATM 7946 O O . HOH IA 8 . ? -5.164 1.679 9.454 1.00 18.85 ? 5072 HOH A O 1 HETATM 7947 O O . HOH IA 8 . ? 16.895 9.770 3.718 1.00 17.06 ? 5073 HOH A O 1 HETATM 7948 O O . HOH IA 8 . ? -4.949 15.404 31.311 1.00 23.58 ? 5074 HOH A O 1 HETATM 7949 O O . HOH IA 8 . ? 14.665 28.511 44.767 1.00 20.03 ? 5075 HOH A O 1 HETATM 7950 O O . HOH IA 8 . ? 10.374 -31.176 -1.865 1.00 27.15 ? 5076 HOH A O 1 HETATM 7951 O O . HOH IA 8 . ? 20.312 -2.353 49.229 1.00 20.37 ? 5077 HOH A O 1 HETATM 7952 O O . HOH IA 8 . ? 9.391 21.418 34.674 1.00 14.05 ? 5078 HOH A O 1 HETATM 7953 O O . HOH IA 8 . ? -4.371 -9.674 24.875 1.00 18.47 ? 5079 HOH A O 1 HETATM 7954 O O . HOH IA 8 . ? 24.439 6.603 21.987 1.00 14.88 ? 5080 HOH A O 1 HETATM 7955 O O . HOH IA 8 . ? 15.092 3.249 38.997 1.00 17.45 ? 5081 HOH A O 1 HETATM 7956 O O . HOH IA 8 . ? 1.015 24.270 46.440 1.00 20.92 ? 5082 HOH A O 1 HETATM 7957 O O . HOH IA 8 . ? 17.649 -13.021 10.895 1.00 26.87 ? 5083 HOH A O 1 HETATM 7958 O O . HOH IA 8 . ? -4.536 -6.606 -0.548 1.00 19.22 ? 5084 HOH A O 1 HETATM 7959 O O . HOH IA 8 . ? -2.098 -8.155 -5.083 1.00 25.58 ? 5085 HOH A O 1 HETATM 7960 O O . HOH IA 8 . ? -0.734 -28.480 29.435 1.00 13.35 ? 5086 HOH A O 1 HETATM 7961 O O . HOH IA 8 . ? 15.209 -18.001 7.318 1.00 13.34 ? 5087 HOH A O 1 HETATM 7962 O O . HOH IA 8 . ? -4.167 -10.349 -6.110 1.00 23.81 ? 5088 HOH A O 1 HETATM 7963 O O . HOH IA 8 . ? 14.131 -6.898 58.083 1.00 18.53 ? 5089 HOH A O 1 HETATM 7964 O O . HOH IA 8 . ? 20.869 8.207 4.372 1.00 18.83 ? 5090 HOH A O 1 HETATM 7965 O O . HOH IA 8 . ? 6.254 -3.091 25.217 1.00 12.42 ? 5091 HOH A O 1 HETATM 7966 O O . HOH IA 8 . ? -7.776 8.807 32.656 1.00 18.98 ? 5092 HOH A O 1 HETATM 7967 O O . HOH IA 8 . ? -6.665 -0.678 32.092 1.00 15.41 ? 5093 HOH A O 1 HETATM 7968 O O . HOH IA 8 . ? 22.974 -18.722 19.699 1.00 34.67 ? 5094 HOH A O 1 HETATM 7969 O O . HOH IA 8 . ? 14.114 -17.481 18.802 1.00 19.00 ? 5095 HOH A O 1 HETATM 7970 O O . HOH IA 8 . ? 20.882 6.440 6.372 1.00 18.09 ? 5096 HOH A O 1 HETATM 7971 O O . HOH IA 8 . ? 6.083 -2.202 14.905 1.00 18.74 ? 5097 HOH A O 1 HETATM 7972 O O . HOH IA 8 . ? 12.713 -16.907 6.567 1.00 13.87 ? 5098 HOH A O 1 HETATM 7973 O O . HOH IA 8 . ? -2.295 13.782 58.179 1.00 21.21 ? 5099 HOH A O 1 HETATM 7974 O O . HOH IA 8 . ? 7.822 -3.921 48.868 1.00 14.42 ? 5100 HOH A O 1 HETATM 7975 O O . HOH IA 8 . ? 8.257 36.831 51.894 1.00 24.49 ? 5101 HOH A O 1 HETATM 7976 O O . HOH IA 8 . ? 22.002 -12.709 14.088 1.00 17.98 ? 5102 HOH A O 1 HETATM 7977 O O . HOH IA 8 . ? -1.112 22.867 63.923 1.00 26.85 ? 5103 HOH A O 1 HETATM 7978 O O . HOH IA 8 . ? 39.106 -3.630 21.063 1.00 26.70 ? 5104 HOH A O 1 HETATM 7979 O O . HOH IA 8 . ? 1.229 2.944 63.368 1.00 16.51 ? 5105 HOH A O 1 HETATM 7980 O O . HOH IA 8 . ? 13.507 -11.442 -6.985 1.00 23.74 ? 5106 HOH A O 1 HETATM 7981 O O . HOH IA 8 . ? 0.554 20.163 37.802 1.00 16.93 ? 5107 HOH A O 1 HETATM 7982 O O . HOH IA 8 . ? 16.712 33.202 56.727 1.00 21.21 ? 5108 HOH A O 1 HETATM 7983 O O . HOH IA 8 . ? -6.905 -9.126 0.826 1.00 20.04 ? 5109 HOH A O 1 HETATM 7984 O O . HOH IA 8 . ? 3.560 -0.155 34.241 1.00 13.86 ? 5110 HOH A O 1 HETATM 7985 O O . HOH IA 8 . ? 6.590 10.927 35.806 1.00 18.03 ? 5111 HOH A O 1 HETATM 7986 O O . HOH IA 8 . ? 1.073 5.395 35.770 1.00 13.63 ? 5112 HOH A O 1 HETATM 7987 O O . HOH IA 8 . ? -0.123 0.858 29.838 1.00 14.84 ? 5113 HOH A O 1 HETATM 7988 O O . HOH IA 8 . ? 16.656 -20.122 2.942 1.00 17.05 ? 5114 HOH A O 1 HETATM 7989 O O . HOH IA 8 . ? 1.636 6.167 62.578 1.00 20.24 ? 5115 HOH A O 1 HETATM 7990 O O . HOH IA 8 . ? 1.573 37.118 55.684 1.00 18.89 ? 5116 HOH A O 1 HETATM 7991 O O . HOH IA 8 . ? 7.018 -2.575 17.555 1.00 16.82 ? 5117 HOH A O 1 HETATM 7992 O O . HOH IA 8 . ? 18.784 -23.609 18.370 1.00 23.31 ? 5118 HOH A O 1 HETATM 7993 O O . HOH IA 8 . ? 24.656 23.272 44.371 1.00 25.17 ? 5119 HOH A O 1 HETATM 7994 O O . HOH IA 8 . ? 19.020 -11.917 8.563 1.00 15.30 ? 5120 HOH A O 1 HETATM 7995 O O . HOH IA 8 . ? 7.772 12.303 55.296 1.00 13.29 ? 5121 HOH A O 1 HETATM 7996 O O . HOH IA 8 . ? -8.123 12.003 48.187 1.00 25.50 ? 5122 HOH A O 1 HETATM 7997 O O . HOH IA 8 . ? -4.711 -5.183 14.414 1.00 28.12 ? 5123 HOH A O 1 HETATM 7998 O O . HOH IA 8 . ? -5.981 -30.401 25.445 1.00 29.49 ? 5124 HOH A O 1 HETATM 7999 O O . HOH IA 8 . ? 5.787 -15.483 34.631 1.00 12.63 ? 5125 HOH A O 1 HETATM 8000 O O . HOH IA 8 . ? 26.772 5.796 41.901 1.00 20.84 ? 5126 HOH A O 1 HETATM 8001 O O . HOH IA 8 . ? 13.753 10.372 39.065 1.00 20.79 ? 5127 HOH A O 1 HETATM 8002 O O . HOH IA 8 . ? 18.383 6.981 49.310 1.00 15.50 ? 5128 HOH A O 1 HETATM 8003 O O . HOH IA 8 . ? 12.524 12.061 9.795 1.00 24.27 ? 5129 HOH A O 1 HETATM 8004 O O . HOH IA 8 . ? 4.452 0.407 0.803 1.00 14.54 ? 5130 HOH A O 1 HETATM 8005 O O . HOH IA 8 . ? 7.850 4.546 5.329 1.00 24.63 ? 5131 HOH A O 1 HETATM 8006 O O . HOH IA 8 . ? 19.074 12.201 44.520 1.00 11.98 ? 5132 HOH A O 1 HETATM 8007 O O . HOH IA 8 . ? 6.021 -16.418 27.052 1.00 15.55 ? 5133 HOH A O 1 HETATM 8008 O O . HOH IA 8 . ? 16.753 -17.447 19.901 1.00 13.19 ? 5134 HOH A O 1 HETATM 8009 O O . HOH IA 8 . ? 16.679 29.054 53.811 1.00 16.50 ? 5135 HOH A O 1 HETATM 8010 O O . HOH IA 8 . ? -0.112 12.108 57.154 1.00 20.05 ? 5136 HOH A O 1 HETATM 8011 O O . HOH IA 8 . ? 33.531 11.951 34.645 1.00 18.07 ? 5137 HOH A O 1 HETATM 8012 O O . HOH IA 8 . ? 11.182 34.556 61.261 1.00 13.57 ? 5138 HOH A O 1 HETATM 8013 O O . HOH IA 8 . ? 9.034 9.100 46.746 1.00 19.09 ? 5139 HOH A O 1 HETATM 8014 O O . HOH IA 8 . ? 16.049 2.959 59.243 1.00 25.20 ? 5140 HOH A O 1 HETATM 8015 O O . HOH IA 8 . ? 10.513 10.073 37.336 1.00 19.07 ? 5141 HOH A O 1 HETATM 8016 O O . HOH IA 8 . ? 0.631 2.308 -11.166 1.00 18.17 ? 5142 HOH A O 1 HETATM 8017 O O . HOH IA 8 . ? -3.274 14.633 42.768 1.00 13.23 ? 5143 HOH A O 1 HETATM 8018 O O . HOH IA 8 . ? 22.929 -14.485 6.675 1.00 25.20 ? 5144 HOH A O 1 HETATM 8019 O O . HOH IA 8 . ? -3.840 11.333 57.781 1.00 22.09 ? 5145 HOH A O 1 HETATM 8020 O O . HOH IA 8 . ? -0.504 -21.790 21.036 1.00 13.19 ? 5146 HOH A O 1 HETATM 8021 O O . HOH IA 8 . ? 5.817 2.283 -1.115 1.00 15.89 ? 5147 HOH A O 1 HETATM 8022 O O . HOH IA 8 . ? 2.033 -14.999 18.459 1.00 17.52 ? 5148 HOH A O 1 HETATM 8023 O O . HOH IA 8 . ? -1.184 -12.090 16.421 1.00 17.83 ? 5149 HOH A O 1 HETATM 8024 O O . HOH IA 8 . ? 27.185 4.729 44.178 1.00 15.49 ? 5150 HOH A O 1 HETATM 8025 O O . HOH IA 8 . ? 15.981 11.965 38.403 1.00 20.44 ? 5151 HOH A O 1 HETATM 8026 O O . HOH IA 8 . ? -3.796 19.116 31.867 1.00 18.38 ? 5152 HOH A O 1 HETATM 8027 O O . HOH IA 8 . ? 26.665 -17.903 15.587 1.00 25.45 ? 5153 HOH A O 1 HETATM 8028 O O . HOH IA 8 . ? -3.852 17.469 57.676 1.00 18.06 ? 5154 HOH A O 1 HETATM 8029 O O . HOH IA 8 . ? 35.045 2.036 11.034 1.00 23.76 ? 5155 HOH A O 1 HETATM 8030 O O . HOH IA 8 . ? 19.539 10.494 4.021 1.00 18.48 ? 5156 HOH A O 1 HETATM 8031 O O . HOH IA 8 . ? 30.703 13.181 25.988 1.00 18.29 ? 5157 HOH A O 1 HETATM 8032 O O . HOH IA 8 . ? 6.209 6.020 37.214 1.00 20.50 ? 5158 HOH A O 1 HETATM 8033 O O . HOH IA 8 . ? 16.242 20.645 40.693 1.00 17.44 ? 5159 HOH A O 1 HETATM 8034 O O . HOH IA 8 . ? 23.191 22.018 53.392 1.00 16.52 ? 5160 HOH A O 1 HETATM 8035 O O . HOH IA 8 . ? 0.815 -17.525 15.721 1.00 25.07 ? 5161 HOH A O 1 HETATM 8036 O O . HOH IA 8 . ? 11.186 11.330 40.311 1.00 11.74 ? 5162 HOH A O 1 HETATM 8037 O O . HOH IA 8 . ? -5.848 21.983 43.692 1.00 20.01 ? 5163 HOH A O 1 HETATM 8038 O O . HOH IA 8 . ? 0.288 -10.993 -0.065 1.00 28.09 ? 5164 HOH A O 1 HETATM 8039 O O . HOH IA 8 . ? 16.924 3.235 40.709 1.00 7.07 ? 5165 HOH A O 1 HETATM 8040 O O . HOH IA 8 . ? -6.024 -14.027 5.346 1.00 26.86 ? 5166 HOH A O 1 HETATM 8041 O O . HOH IA 8 . ? 24.056 24.299 35.706 1.00 27.42 ? 5167 HOH A O 1 HETATM 8042 O O . HOH IA 8 . ? 7.865 9.241 43.093 1.00 23.54 ? 5168 HOH A O 1 HETATM 8043 O O . HOH IA 8 . ? 21.735 10.649 41.290 1.00 13.33 ? 5169 HOH A O 1 HETATM 8044 O O . HOH IA 8 . ? 17.418 -9.911 7.252 1.00 15.43 ? 5170 HOH A O 1 HETATM 8045 O O . HOH IA 8 . ? 7.497 -11.266 -1.084 1.00 24.78 ? 5171 HOH A O 1 HETATM 8046 O O . HOH IA 8 . ? 17.482 21.302 25.806 1.00 16.17 ? 5172 HOH A O 1 HETATM 8047 O O . HOH IA 8 . ? 17.829 -0.195 54.733 1.00 21.13 ? 5173 HOH A O 1 HETATM 8048 O O . HOH IA 8 . ? 18.506 4.573 47.442 1.00 36.10 ? 5174 HOH A O 1 HETATM 8049 O O . HOH IA 8 . ? -6.350 -9.561 44.818 1.00 18.42 ? 5175 HOH A O 1 HETATM 8050 O O . HOH IA 8 . ? -1.488 36.216 62.277 1.00 23.77 ? 5176 HOH A O 1 HETATM 8051 O O . HOH IA 8 . ? 1.793 -16.244 -6.517 1.00 19.15 ? 5177 HOH A O 1 HETATM 8052 O O . HOH IA 8 . ? 14.441 30.800 43.048 1.00 24.42 ? 5178 HOH A O 1 HETATM 8053 O O . HOH IA 8 . ? 22.901 12.216 15.854 1.00 20.93 ? 5179 HOH A O 1 HETATM 8054 O O . HOH IA 8 . ? 6.139 -27.553 27.980 1.00 18.36 ? 5180 HOH A O 1 HETATM 8055 O O . HOH IA 8 . ? 20.973 1.364 -1.525 1.00 18.51 ? 5181 HOH A O 1 HETATM 8056 O O . HOH IA 8 . ? 21.205 10.103 38.786 1.00 15.17 ? 5182 HOH A O 1 HETATM 8057 O O . HOH IA 8 . ? 19.958 9.812 43.430 1.00 20.04 ? 5183 HOH A O 1 HETATM 8058 O O . HOH IA 8 . ? 4.051 6.643 29.743 1.00 17.91 ? 5184 HOH A O 1 HETATM 8059 O O . HOH IA 8 . ? 3.602 -22.729 19.529 1.00 25.68 ? 5185 HOH A O 1 HETATM 8060 O O . HOH IA 8 . ? -4.807 5.496 -4.302 1.00 14.26 ? 5186 HOH A O 1 HETATM 8061 O O . HOH IA 8 . ? -7.268 -12.514 37.268 1.00 19.35 ? 5187 HOH A O 1 HETATM 8062 O O . HOH IA 8 . ? 21.231 1.989 32.554 1.00 12.83 ? 5188 HOH A O 1 HETATM 8063 O O . HOH IA 8 . ? -7.243 8.883 7.392 1.00 25.29 ? 5189 HOH A O 1 HETATM 8064 O O . HOH IA 8 . ? 9.473 -16.702 40.642 1.00 14.91 ? 5190 HOH A O 1 HETATM 8065 O O . HOH IA 8 . ? 18.339 15.366 20.502 1.00 25.34 ? 5191 HOH A O 1 HETATM 8066 O O . HOH IA 8 . ? -5.929 2.948 25.159 1.00 23.85 ? 5192 HOH A O 1 HETATM 8067 O O . HOH IA 8 . ? 16.685 -12.913 -3.237 1.00 24.43 ? 5193 HOH A O 1 HETATM 8068 O O . HOH IA 8 . ? 1.666 36.213 50.423 1.00 21.68 ? 5194 HOH A O 1 HETATM 8069 O O . HOH IA 8 . ? 11.470 20.706 63.564 1.00 21.87 ? 5195 HOH A O 1 HETATM 8070 O O . HOH IA 8 . ? 19.724 18.153 18.772 1.00 27.38 ? 5196 HOH A O 1 HETATM 8071 O O . HOH IA 8 . ? -9.157 -2.673 40.955 1.00 25.79 ? 5197 HOH A O 1 HETATM 8072 O O . HOH IA 8 . ? 18.117 -23.144 2.794 1.00 28.61 ? 5198 HOH A O 1 HETATM 8073 O O . HOH IA 8 . ? 32.827 -8.298 6.860 1.00 27.16 ? 5199 HOH A O 1 HETATM 8074 O O . HOH IA 8 . ? 9.096 6.640 35.895 1.00 16.37 ? 5200 HOH A O 1 HETATM 8075 O O . HOH IA 8 . ? -4.234 0.810 32.794 1.00 8.17 ? 5201 HOH A O 1 HETATM 8076 O O . HOH IA 8 . ? 12.849 19.168 27.835 1.00 23.14 ? 5202 HOH A O 1 HETATM 8077 O O . HOH IA 8 . ? 12.023 26.590 35.405 1.00 18.22 ? 5203 HOH A O 1 HETATM 8078 O O . HOH IA 8 . ? 25.787 12.657 24.580 1.00 18.05 ? 5204 HOH A O 1 HETATM 8079 O O . HOH IA 8 . ? 3.018 1.617 -12.174 1.00 16.24 ? 5205 HOH A O 1 HETATM 8080 O O . HOH IA 8 . ? -10.179 -4.415 46.521 1.00 18.58 ? 5206 HOH A O 1 HETATM 8081 O O . HOH IA 8 . ? 17.856 11.769 35.753 1.00 28.97 ? 5207 HOH A O 1 HETATM 8082 O O . HOH IA 8 . ? -6.322 23.485 48.210 1.00 15.29 ? 5208 HOH A O 1 HETATM 8083 O O . HOH IA 8 . ? -1.525 -3.724 17.751 1.00 23.89 ? 5209 HOH A O 1 HETATM 8084 O O . HOH IA 8 . ? -2.035 -5.103 15.378 1.00 17.17 ? 5210 HOH A O 1 HETATM 8085 O O . HOH IA 8 . ? 3.482 25.273 34.055 1.00 13.13 ? 5211 HOH A O 1 HETATM 8086 O O . HOH IA 8 . ? 5.618 12.166 7.999 1.00 30.66 ? 5212 HOH A O 1 HETATM 8087 O O . HOH IA 8 . ? -1.168 6.998 34.900 1.00 9.32 ? 5213 HOH A O 1 HETATM 8088 O O . HOH IA 8 . ? 13.821 18.541 25.269 1.00 26.70 ? 5214 HOH A O 1 HETATM 8089 O O . HOH IA 8 . ? 7.780 8.081 32.588 1.00 16.12 ? 5215 HOH A O 1 HETATM 8090 O O . HOH IA 8 . ? -10.462 5.132 34.629 1.00 21.47 ? 5216 HOH A O 1 HETATM 8091 O O . HOH IA 8 . ? 13.576 13.204 7.465 1.00 28.97 ? 5217 HOH A O 1 HETATM 8092 O O . HOH IA 8 . ? 18.901 11.626 38.312 1.00 15.50 ? 5218 HOH A O 1 HETATM 8093 O O . HOH IA 8 . ? 8.338 7.581 29.818 1.00 23.12 ? 5219 HOH A O 1 HETATM 8094 O O . HOH IA 8 . ? -2.485 6.851 37.173 1.00 13.31 ? 5220 HOH A O 1 HETATM 8095 O O . HOH IA 8 . ? 26.129 26.856 31.107 1.00 33.28 ? 5221 HOH A O 1 HETATM 8096 O O . HOH IA 8 . ? 4.353 19.153 27.705 1.00 27.17 ? 5222 HOH A O 1 HETATM 8097 O O . HOH IA 8 . ? 6.199 7.604 28.080 1.00 22.59 ? 5223 HOH A O 1 HETATM 8098 O O . HOH IA 8 . ? 7.059 8.427 36.616 1.00 19.34 ? 5224 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 MET 1 1 ? ? ? A . n A 1 2 LYS 2 2 ? ? ? A . n A 1 3 LEU 3 3 ? ? ? A . n A 1 4 SER 4 4 ? ? ? A . n A 1 5 SER 5 5 ? ? ? A . n A 1 6 ALA 6 6 ? ? ? A . n A 1 7 CYS 7 7 ? ? ? A . n A 1 8 ALA 8 8 ? ? ? A . n A 1 9 ILE 9 9 ? ? ? A . n A 1 10 ALA 10 10 ? ? ? A . n A 1 11 LEU 11 11 ? ? ? A . n A 1 12 LEU 12 12 ? ? ? A . n A 1 13 ALA 13 13 ? ? ? A . n A 1 14 ALA 14 14 ? ? ? A . n A 1 15 GLN 15 15 ? ? ? A . n A 1 16 ALA 16 16 ? ? ? A . n A 1 17 ALA 17 17 ? ? ? A . n A 1 18 GLY 18 18 ? ? ? A . n A 1 19 ALA 19 19 ? ? ? A . n A 1 20 SER 20 20 ? ? ? A . n A 1 21 ILE 21 21 ? ? ? A . n A 1 22 LYS 22 22 ? ? ? A . n A 1 23 HIS 23 23 ? ? ? A . n A 1 24 ARG 24 24 ? ? ? A . n A 1 25 ILE 25 25 ? ? ? A . n A 1 26 ASN 26 26 ? ? ? A . n A 1 27 GLY 27 27 ? ? ? A . n A 1 28 PHE 28 28 ? ? ? A . n A 1 29 THR 29 29 ? ? ? A . n A 1 30 LEU 30 30 ? ? ? A . n A 1 31 THR 31 31 ? ? ? A . n A 1 32 GLU 32 32 ? ? ? A . n A 1 33 HIS 33 33 ? ? ? A . n A 1 34 SER 34 34 ? ? ? A . n A 1 35 ASP 35 35 ? ? ? A . n A 1 36 PRO 36 36 ? ? ? A . n A 1 37 ALA 37 37 ? ? ? A . n A 1 38 LYS 38 38 ? ? ? A . n A 1 39 ARG 39 39 ? ? ? A . n A 1 40 GLU 40 40 ? ? ? A . n A 1 41 LEU 41 41 41 LEU LEU A . n A 1 42 LEU 42 42 42 LEU LEU A . n A 1 43 GLN 43 43 43 GLN GLN A . n A 1 44 LYS 44 44 44 LYS LYS A . n A 1 45 TYR 45 45 45 TYR TYR A . n A 1 46 VAL 46 46 46 VAL VAL A . n A 1 47 THR 47 47 47 THR THR A . n A 1 48 TRP 48 48 48 TRP TRP A . n A 1 49 ASP 49 49 49 ASP ASP A . n A 1 50 ASP 50 50 50 ASP ASP A . n A 1 51 LYS 51 51 51 LYS LYS A . n A 1 52 SER 52 52 52 SER SER A . n A 1 53 LEU 53 53 53 LEU LEU A . n A 1 54 PHE 54 54 54 PHE PHE A . n A 1 55 ILE 55 55 55 ILE ILE A . n A 1 56 ASN 56 56 56 ASN ASN A . n A 1 57 GLY 57 57 57 GLY GLY A . n A 1 58 GLU 58 58 58 GLU GLU A . n A 1 59 ARG 59 59 59 ARG ARG A . n A 1 60 ILE 60 60 60 ILE ILE A . n A 1 61 MET 61 61 61 MET MET A . n A 1 62 ILE 62 62 62 ILE ILE A . n A 1 63 PHE 63 63 63 PHE PHE A . n A 1 64 SER 64 64 64 SER SER A . n A 1 65 GLY 65 65 65 GLY GLY A . n A 1 66 GLU 66 66 66 GLU GLU A . n A 1 67 PHE 67 67 67 PHE PHE A . n A 1 68 HIS 68 68 68 HIS HIS A . n A 1 69 PRO 69 69 69 PRO PRO A . n A 1 70 PHE 70 70 70 PHE PHE A . n A 1 71 ARG 71 71 71 ARG ARG A . n A 1 72 LEU 72 72 72 LEU LEU A . n A 1 73 PRO 73 73 73 PRO PRO A . n A 1 74 VAL 74 74 74 VAL VAL A . n A 1 75 LYS 75 75 75 LYS LYS A . n A 1 76 GLU 76 76 76 GLU GLU A . n A 1 77 LEU 77 77 77 LEU LEU A . n A 1 78 GLN 78 78 78 GLN GLN A . n A 1 79 LEU 79 79 79 LEU LEU A . n A 1 80 ASP 80 80 80 ASP ASP A . n A 1 81 ILE 81 81 81 ILE ILE A . n A 1 82 PHE 82 82 82 PHE PHE A . n A 1 83 GLN 83 83 83 GLN GLN A . n A 1 84 LYS 84 84 84 LYS LYS A . n A 1 85 VAL 85 85 85 VAL VAL A . n A 1 86 LYS 86 86 86 LYS LYS A . n A 1 87 ALA 87 87 87 ALA ALA A . n A 1 88 LEU 88 88 88 LEU LEU A . n A 1 89 GLY 89 89 89 GLY GLY A . n A 1 90 PHE 90 90 90 PHE PHE A . n A 1 91 ASN 91 91 91 ASN ASN A . n A 1 92 CYS 92 92 92 CYS CYS A . n A 1 93 VAL 93 93 93 VAL VAL A . n A 1 94 SER 94 94 94 SER SER A . n A 1 95 PHE 95 95 95 PHE PHE A . n A 1 96 TYR 96 96 96 TYR TYR A . n A 1 97 VAL 97 97 97 VAL VAL A . n A 1 98 ASP 98 98 98 ASP ASP A . n A 1 99 TRP 99 99 99 TRP TRP A . n A 1 100 ALA 100 100 100 ALA ALA A . n A 1 101 LEU 101 101 101 LEU LEU A . n A 1 102 VAL 102 102 102 VAL VAL A . n A 1 103 GLU 103 103 103 GLU GLU A . n A 1 104 GLY 104 104 104 GLY GLY A . n A 1 105 LYS 105 105 105 LYS LYS A . n A 1 106 PRO 106 106 106 PRO PRO A . n A 1 107 GLY 107 107 107 GLY GLY A . n A 1 108 GLU 108 108 108 GLU GLU A . n A 1 109 TYR 109 109 109 TYR TYR A . n A 1 110 ARG 110 110 110 ARG ARG A . n A 1 111 ALA 111 111 111 ALA ALA A . n A 1 112 ASP 112 112 112 ASP ASP A . n A 1 113 GLY 113 113 113 GLY GLY A . n A 1 114 ILE 114 114 114 ILE ILE A . n A 1 115 PHE 115 115 115 PHE PHE A . n A 1 116 ASP 116 116 116 ASP ASP A . n A 1 117 LEU 117 117 117 LEU LEU A . n A 1 118 GLU 118 118 118 GLU GLU A . n A 1 119 PRO 119 119 119 PRO PRO A . n A 1 120 PHE 120 120 120 PHE PHE A . n A 1 121 PHE 121 121 121 PHE PHE A . n A 1 122 ASP 122 122 122 ASP ASP A . n A 1 123 ALA 123 123 123 ALA ALA A . n A 1 124 ALA 124 124 124 ALA ALA A . n A 1 125 SER 125 125 125 SER SER A . n A 1 126 GLU 126 126 126 GLU GLU A . n A 1 127 ALA 127 127 127 ALA ALA A . n A 1 128 GLY 128 128 128 GLY GLY A . n A 1 129 ILE 129 129 129 ILE ILE A . n A 1 130 TYR 130 130 130 TYR TYR A . n A 1 131 LEU 131 131 131 LEU LEU A . n A 1 132 LEU 132 132 132 LEU LEU A . n A 1 133 ALA 133 133 133 ALA ALA A . n A 1 134 ARG 134 134 134 ARG ARG A . n A 1 135 PRO 135 135 135 PRO PRO A . n A 1 136 GLY 136 136 136 GLY GLY A . n A 1 137 PRO 137 137 137 PRO PRO A . n A 1 138 TYR 138 138 138 TYR TYR A . n A 1 139 ILE 139 139 139 ILE ILE A . n A 1 140 ASN 140 140 140 ASN ASN A . n A 1 141 ALA 141 141 141 ALA ALA A . n A 1 142 GLU 142 142 142 GLU GLU A . n A 1 143 SER 143 143 143 SER SER A . n A 1 144 SER 144 144 144 SER SER A . n A 1 145 GLY 145 145 145 GLY GLY A . n A 1 146 GLY 146 146 146 GLY GLY A . n A 1 147 GLY 147 147 147 GLY GLY A . n A 1 148 PHE 148 148 148 PHE PHE A . n A 1 149 PRO 149 149 149 PRO PRO A . n A 1 150 GLY 150 150 150 GLY GLY A . n A 1 151 TRP 151 151 151 TRP TRP A . n A 1 152 LEU 152 152 152 LEU LEU A . n A 1 153 GLN 153 153 153 GLN GLN A . n A 1 154 ARG 154 154 154 ARG ARG A . n A 1 155 VAL 155 155 155 VAL VAL A . n A 1 156 ASN 156 156 156 ASN ASN A . n A 1 157 GLY 157 157 157 GLY GLY A . n A 1 158 THR 158 158 158 THR THR A . n A 1 159 LEU 159 159 159 LEU LEU A . n A 1 160 ARG 160 160 160 ARG ARG A . n A 1 161 SER 161 161 161 SER SER A . n A 1 162 SER 162 162 162 SER SER A . n A 1 163 ASP 163 163 163 ASP ASP A . n A 1 164 LYS 164 164 164 LYS LYS A . n A 1 165 ALA 165 165 165 ALA ALA A . n A 1 166 TYR 166 166 166 TYR TYR A . n A 1 167 LEU 167 167 167 LEU LEU A . n A 1 168 ASP 168 168 168 ASP ASP A . n A 1 169 ALA 169 169 169 ALA ALA A . n A 1 170 THR 170 170 170 THR THR A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 ASN 172 172 172 ASN ASN A . n A 1 173 TYR 173 173 173 TYR TYR A . n A 1 174 VAL 174 174 174 VAL VAL A . n A 1 175 SER 175 175 175 SER SER A . n A 1 176 HIS 176 176 176 HIS HIS A . n A 1 177 VAL 177 177 177 VAL VAL A . n A 1 178 ALA 178 178 178 ALA ALA A . n A 1 179 ALA 179 179 179 ALA ALA A . n A 1 180 THR 180 180 180 THR THR A . n A 1 181 ILE 181 181 181 ILE ILE A . n A 1 182 ALA 182 182 182 ALA ALA A . n A 1 183 LYS 183 183 183 LYS LYS A . n A 1 184 TYR 184 184 184 TYR TYR A . n A 1 185 GLN 185 185 185 GLN GLN A . n A 1 186 ILE 186 186 186 ILE ILE A . n A 1 187 THR 187 187 187 THR THR A . n A 1 188 ASN 188 188 188 ASN ASN A . n A 1 189 GLY 189 189 189 GLY GLY A . n A 1 190 GLY 190 190 190 GLY GLY A . n A 1 191 PRO 191 191 191 PRO PRO A . n A 1 192 ILE 192 192 192 ILE ILE A . n A 1 193 ILE 193 193 193 ILE ILE A . n A 1 194 LEU 194 194 194 LEU LEU A . n A 1 195 TYR 195 195 195 TYR TYR A . n A 1 196 GLN 196 196 196 GLN GLN A . n A 1 197 PRO 197 197 197 PRO PRO A . n A 1 198 GLU 198 198 198 GLU GLU A . n A 1 199 ASN 199 199 199 ASN ASN A . n A 1 200 GLU 200 200 200 GLU GLU A . n A 1 201 TYR 201 201 201 TYR TYR A . n A 1 202 THR 202 202 202 THR THR A . n A 1 203 SER 203 203 203 SER SER A . n A 1 204 GLY 204 204 204 GLY GLY A . n A 1 205 CYS 205 205 205 CYS CYS A . n A 1 206 CYS 206 206 206 CYS CYS A . n A 1 207 GLY 207 207 207 GLY GLY A . n A 1 208 VAL 208 208 208 VAL VAL A . n A 1 209 GLU 209 209 209 GLU GLU A . n A 1 210 PHE 210 210 210 PHE PHE A . n A 1 211 PRO 211 211 211 PRO PRO A . n A 1 212 ASP 212 212 212 ASP ASP A . n A 1 213 PRO 213 213 213 PRO PRO A . n A 1 214 VAL 214 214 214 VAL VAL A . n A 1 215 TYR 215 215 215 TYR TYR A . n A 1 216 MET 216 216 216 MET MET A . n A 1 217 GLN 217 217 217 GLN GLN A . n A 1 218 TYR 218 218 218 TYR TYR A . n A 1 219 VAL 219 219 219 VAL VAL A . n A 1 220 GLU 220 220 220 GLU GLU A . n A 1 221 ASP 221 221 221 ASP ASP A . n A 1 222 GLN 222 222 222 GLN GLN A . n A 1 223 ALA 223 223 223 ALA ALA A . n A 1 224 ARG 224 224 224 ARG ARG A . n A 1 225 ASN 225 225 225 ASN ASN A . n A 1 226 ALA 226 226 226 ALA ALA A . n A 1 227 GLY 227 227 227 GLY GLY A . n A 1 228 VAL 228 228 228 VAL VAL A . n A 1 229 VAL 229 229 229 VAL VAL A . n A 1 230 ILE 230 230 230 ILE ILE A . n A 1 231 PRO 231 231 231 PRO PRO A . n A 1 232 LEU 232 232 232 LEU LEU A . n A 1 233 ILE 233 233 233 ILE ILE A . n A 1 234 ASN 234 234 234 ASN ASN A . n A 1 235 ASN 235 235 235 ASN ASN A . n A 1 236 ASP 236 236 236 ASP ASP A . n A 1 237 ALA 237 237 237 ALA ALA A . n A 1 238 SER 238 238 238 SER SER A . n A 1 239 ALA 239 239 239 ALA ALA A . n A 1 240 SER 240 240 240 SER SER A . n A 1 241 GLY 241 241 241 GLY GLY A . n A 1 242 ASN 242 242 242 ASN ASN A . n A 1 243 ASN 243 243 243 ASN ASN A . n A 1 244 ALA 244 244 244 ALA ALA A . n A 1 245 PRO 245 245 245 PRO PRO A . n A 1 246 GLY 246 246 246 GLY GLY A . n A 1 247 THR 247 247 247 THR THR A . n A 1 248 GLY 248 248 248 GLY GLY A . n A 1 249 LYS 249 249 249 LYS LYS A . n A 1 250 GLY 250 250 250 GLY GLY A . n A 1 251 ALA 251 251 251 ALA ALA A . n A 1 252 VAL 252 252 252 VAL VAL A . n A 1 253 ASP 253 253 253 ASP ASP A . n A 1 254 ILE 254 254 254 ILE ILE A . n A 1 255 TYR 255 255 255 TYR TYR A . n A 1 256 GLY 256 256 256 GLY GLY A . n A 1 257 HIS 257 257 257 HIS HIS A . n A 1 258 ASP 258 258 258 ASP ASP A . n A 1 259 SER 259 259 259 SER SER A . n A 1 260 TYR 260 260 260 TYR TYR A . n A 1 261 PRO 261 261 261 PRO PRO A . n A 1 262 LEU 262 262 262 LEU LEU A . n A 1 263 GLY 263 263 263 GLY GLY A . n A 1 264 PHE 264 264 264 PHE PHE A . n A 1 265 ASP 265 265 265 ASP ASP A . n A 1 266 CYS 266 266 266 CYS CYS A . n A 1 267 ALA 267 267 267 ALA ALA A . n A 1 268 ASN 268 268 268 ASN ASN A . n A 1 269 PRO 269 269 269 PRO PRO A . n A 1 270 THR 270 270 270 THR THR A . n A 1 271 VAL 271 271 271 VAL VAL A . n A 1 272 TRP 272 272 272 TRP TRP A . n A 1 273 PRO 273 273 273 PRO PRO A . n A 1 274 SER 274 274 274 SER SER A . n A 1 275 GLY 275 275 275 GLY GLY A . n A 1 276 ASP 276 276 276 ASP ASP A . n A 1 277 LEU 277 277 277 LEU LEU A . n A 1 278 PRO 278 278 278 PRO PRO A . n A 1 279 THR 279 279 279 THR THR A . n A 1 280 ASN 280 280 280 ASN ASN A . n A 1 281 PHE 281 281 281 PHE PHE A . n A 1 282 ARG 282 282 282 ARG ARG A . n A 1 283 THR 283 283 283 THR THR A . n A 1 284 LEU 284 284 284 LEU LEU A . n A 1 285 HIS 285 285 285 HIS HIS A . n A 1 286 LEU 286 286 286 LEU LEU A . n A 1 287 GLU 287 287 287 GLU GLU A . n A 1 288 GLN 288 288 288 GLN GLN A . n A 1 289 SER 289 289 289 SER SER A . n A 1 290 PRO 290 290 290 PRO PRO A . n A 1 291 THR 291 291 291 THR THR A . n A 1 292 THR 292 292 292 THR THR A . n A 1 293 PRO 293 293 293 PRO PRO A . n A 1 294 TYR 294 294 294 TYR TYR A . n A 1 295 ALA 295 295 295 ALA ALA A . n A 1 296 ILE 296 296 296 ILE ILE A . n A 1 297 VAL 297 297 297 VAL VAL A . n A 1 298 GLN 298 298 298 GLN GLN A . n A 1 299 PHE 299 299 299 PHE PHE A . n A 1 300 GLN 300 300 300 GLN GLN A . n A 1 301 GLY 301 301 301 GLY GLY A . n A 1 302 GLY 302 302 302 GLY GLY A . n A 1 303 SER 303 303 303 SER SER A . n A 1 304 TYR 304 304 304 TYR TYR A . n A 1 305 ASP 305 305 305 ASP ASP A . n A 1 306 PRO 306 306 306 PRO PRO A . n A 1 307 TRP 307 307 307 TRP TRP A . n A 1 308 GLY 308 308 308 GLY GLY A . n A 1 309 GLY 309 309 309 GLY GLY A . n A 1 310 PRO 310 310 310 PRO PRO A . n A 1 311 GLY 311 311 311 GLY GLY A . n A 1 312 PHE 312 312 312 PHE PHE A . n A 1 313 ALA 313 313 313 ALA ALA A . n A 1 314 ALA 314 314 314 ALA ALA A . n A 1 315 CYS 315 315 315 CYS CYS A . n A 1 316 SER 316 316 316 SER SER A . n A 1 317 GLU 317 317 317 GLU GLU A . n A 1 318 LEU 318 318 318 LEU LEU A . n A 1 319 LEU 319 319 319 LEU LEU A . n A 1 320 ASN 320 320 320 ASN ASN A . n A 1 321 ASN 321 321 321 ASN ASN A . n A 1 322 GLU 322 322 322 GLU GLU A . n A 1 323 PHE 323 323 323 PHE PHE A . n A 1 324 GLU 324 324 324 GLU GLU A . n A 1 325 ARG 325 325 325 ARG ARG A . n A 1 326 VAL 326 326 326 VAL VAL A . n A 1 327 PHE 327 327 327 PHE PHE A . n A 1 328 TYR 328 328 328 TYR TYR A . n A 1 329 LYS 329 329 329 LYS LYS A . n A 1 330 ASN 330 330 330 ASN ASN A . n A 1 331 ASP 331 331 331 ASP ASP A . n A 1 332 PHE 332 332 332 PHE PHE A . n A 1 333 SER 333 333 333 SER SER A . n A 1 334 PHE 334 334 334 PHE PHE A . n A 1 335 GLN 335 335 335 GLN GLN A . n A 1 336 ILE 336 336 336 ILE ILE A . n A 1 337 ALA 337 337 337 ALA ALA A . n A 1 338 ILE 338 338 338 ILE ILE A . n A 1 339 MET 339 339 339 MET MET A . n A 1 340 ASN 340 340 340 ASN ASN A . n A 1 341 LEU 341 341 341 LEU LEU A . n A 1 342 TYR 342 342 342 TYR TYR A . n A 1 343 MET 343 343 343 MET MET A . n A 1 344 ILE 344 344 344 ILE ILE A . n A 1 345 PHE 345 345 345 PHE PHE A . n A 1 346 GLY 346 346 346 GLY GLY A . n A 1 347 GLY 347 347 347 GLY GLY A . n A 1 348 THR 348 348 348 THR THR A . n A 1 349 ASN 349 349 349 ASN ASN A . n A 1 350 TRP 350 350 350 TRP TRP A . n A 1 351 GLY 351 351 351 GLY GLY A . n A 1 352 ASN 352 352 352 ASN ASN A . n A 1 353 LEU 353 353 353 LEU LEU A . n A 1 354 GLY 354 354 354 GLY GLY A . n A 1 355 TYR 355 355 355 TYR TYR A . n A 1 356 PRO 356 356 356 PRO PRO A . n A 1 357 ASN 357 357 357 ASN ASN A . n A 1 358 GLY 358 358 358 GLY GLY A . n A 1 359 TYR 359 359 359 TYR TYR A . n A 1 360 THR 360 360 360 THR THR A . n A 1 361 SER 361 361 361 SER SER A . n A 1 362 TYR 362 362 362 TYR TYR A . n A 1 363 ASP 363 363 363 ASP ASP A . n A 1 364 TYR 364 364 364 TYR TYR A . n A 1 365 GLY 365 365 365 GLY GLY A . n A 1 366 SER 366 366 366 SER SER A . n A 1 367 ALA 367 367 367 ALA ALA A . n A 1 368 VAL 368 368 368 VAL VAL A . n A 1 369 THR 369 369 369 THR THR A . n A 1 370 GLU 370 370 370 GLU GLU A . n A 1 371 SER 371 371 371 SER SER A . n A 1 372 ARG 372 372 372 ARG ARG A . n A 1 373 ASN 373 373 373 ASN ASN A . n A 1 374 ILE 374 374 374 ILE ILE A . n A 1 375 THR 375 375 375 THR THR A . n A 1 376 ARG 376 376 376 ARG ARG A . n A 1 377 GLU 377 377 377 GLU GLU A . n A 1 378 LYS 378 378 378 LYS LYS A . n A 1 379 TYR 379 379 379 TYR TYR A . n A 1 380 SER 380 380 380 SER SER A . n A 1 381 GLU 381 381 381 GLU GLU A . n A 1 382 LEU 382 382 382 LEU LEU A . n A 1 383 LYS 383 383 383 LYS LYS A . n A 1 384 LEU 384 384 384 LEU LEU A . n A 1 385 LEU 385 385 385 LEU LEU A . n A 1 386 GLY 386 386 386 GLY GLY A . n A 1 387 ASN 387 387 387 ASN ASN A . n A 1 388 PHE 388 388 388 PHE PHE A . n A 1 389 ALA 389 389 389 ALA ALA A . n A 1 390 LYS 390 390 390 LYS LYS A . n A 1 391 VAL 391 391 391 VAL VAL A . n A 1 392 SER 392 392 392 SER SER A . n A 1 393 PRO 393 393 393 PRO PRO A . n A 1 394 GLY 394 394 394 GLY GLY A . n A 1 395 TYR 395 395 395 TYR TYR A . n A 1 396 LEU 396 396 396 LEU LEU A . n A 1 397 THR 397 397 397 THR THR A . n A 1 398 ALA 398 398 398 ALA ALA A . n A 1 399 SER 399 399 399 SER SER A . n A 1 400 PRO 400 400 400 PRO PRO A . n A 1 401 GLY 401 401 401 GLY GLY A . n A 1 402 ASN 402 402 402 ASN ASN A . n A 1 403 LEU 403 403 403 LEU LEU A . n A 1 404 THR 404 404 404 THR THR A . n A 1 405 THR 405 405 405 THR THR A . n A 1 406 SER 406 406 406 SER SER A . n A 1 407 GLY 407 407 407 GLY GLY A . n A 1 408 TYR 408 408 408 TYR TYR A . n A 1 409 ALA 409 409 409 ALA ALA A . n A 1 410 ASP 410 410 410 ASP ASP A . n A 1 411 THR 411 411 411 THR THR A . n A 1 412 THR 412 412 412 THR THR A . n A 1 413 ASP 413 413 413 ASP ASP A . n A 1 414 LEU 414 414 414 LEU LEU A . n A 1 415 THR 415 415 415 THR THR A . n A 1 416 VAL 416 416 416 VAL VAL A . n A 1 417 THR 417 417 417 THR THR A . n A 1 418 PRO 418 418 418 PRO PRO A . n A 1 419 LEU 419 419 419 LEU LEU A . n A 1 420 LEU 420 420 420 LEU LEU A . n A 1 421 GLY 421 421 421 GLY GLY A . n A 1 422 ASN 422 422 422 ASN ASN A . n A 1 423 SER 423 423 423 SER SER A . n A 1 424 THR 424 424 424 THR THR A . n A 1 425 GLY 425 425 425 GLY GLY A . n A 1 426 SER 426 426 426 SER SER A . n A 1 427 PHE 427 427 427 PHE PHE A . n A 1 428 PHE 428 428 428 PHE PHE A . n A 1 429 VAL 429 429 429 VAL VAL A . n A 1 430 VAL 430 430 430 VAL VAL A . n A 1 431 ARG 431 431 431 ARG ARG A . n A 1 432 HIS 432 432 432 HIS HIS A . n A 1 433 SER 433 433 433 SER SER A . n A 1 434 ASP 434 434 434 ASP ASP A . n A 1 435 TYR 435 435 435 TYR TYR A . n A 1 436 SER 436 436 436 SER SER A . n A 1 437 SER 437 437 437 SER SER A . n A 1 438 GLU 438 438 438 GLU GLU A . n A 1 439 GLU 439 439 439 GLU GLU A . n A 1 440 SER 440 440 440 SER SER A . n A 1 441 THR 441 441 441 THR THR A . n A 1 442 SER 442 442 442 SER SER A . n A 1 443 TYR 443 443 443 TYR TYR A . n A 1 444 LYS 444 444 444 LYS LYS A . n A 1 445 LEU 445 445 445 LEU LEU A . n A 1 446 ARG 446 446 446 ARG ARG A . n A 1 447 LEU 447 447 447 LEU LEU A . n A 1 448 PRO 448 448 448 PRO PRO A . n A 1 449 THR 449 449 449 THR THR A . n A 1 450 SER 450 450 450 SER SER A . n A 1 451 ALA 451 451 451 ALA ALA A . n A 1 452 GLY 452 452 452 GLY GLY A . n A 1 453 SER 453 453 453 SER SER A . n A 1 454 VAL 454 454 454 VAL VAL A . n A 1 455 THR 455 455 455 THR THR A . n A 1 456 ILE 456 456 456 ILE ILE A . n A 1 457 PRO 457 457 457 PRO PRO A . n A 1 458 GLN 458 458 458 GLN GLN A . n A 1 459 LEU 459 459 459 LEU LEU A . n A 1 460 GLY 460 460 460 GLY GLY A . n A 1 461 GLY 461 461 461 GLY GLY A . n A 1 462 THR 462 462 462 THR THR A . n A 1 463 LEU 463 463 463 LEU LEU A . n A 1 464 THR 464 464 464 THR THR A . n A 1 465 LEU 465 465 465 LEU LEU A . n A 1 466 ASN 466 466 466 ASN ASN A . n A 1 467 GLY 467 467 467 GLY GLY A . n A 1 468 ARG 468 468 468 ARG ARG A . n A 1 469 ASP 469 469 469 ASP ASP A . n A 1 470 SER 470 470 470 SER SER A . n A 1 471 LYS 471 471 471 LYS LYS A . n A 1 472 ILE 472 472 472 ILE ILE A . n A 1 473 HIS 473 473 473 HIS HIS A . n A 1 474 VAL 474 474 474 VAL VAL A . n A 1 475 THR 475 475 475 THR THR A . n A 1 476 ASP 476 476 476 ASP ASP A . n A 1 477 TYR 477 477 477 TYR TYR A . n A 1 478 ASN 478 478 478 ASN ASN A . n A 1 479 VAL 479 479 479 VAL VAL A . n A 1 480 SER 480 480 480 SER SER A . n A 1 481 GLY 481 481 481 GLY GLY A . n A 1 482 THR 482 482 482 THR THR A . n A 1 483 ASN 483 483 483 ASN ASN A . n A 1 484 ILE 484 484 484 ILE ILE A . n A 1 485 ILE 485 485 485 ILE ILE A . n A 1 486 TYR 486 486 486 TYR TYR A . n A 1 487 SER 487 487 487 SER SER A . n A 1 488 THR 488 488 488 THR THR A . n A 1 489 ALA 489 489 489 ALA ALA A . n A 1 490 GLU 490 490 490 GLU GLU A . n A 1 491 VAL 491 491 491 VAL VAL A . n A 1 492 PHE 492 492 492 PHE PHE A . n A 1 493 THR 493 493 493 THR THR A . n A 1 494 TRP 494 494 494 TRP TRP A . n A 1 495 LYS 495 495 495 LYS LYS A . n A 1 496 LYS 496 496 496 LYS LYS A . n A 1 497 PHE 497 497 497 PHE PHE A . n A 1 498 ALA 498 498 498 ALA ALA A . n A 1 499 ASP 499 499 499 ASP ASP A . n A 1 500 GLY 500 500 500 GLY GLY A . n A 1 501 LYS 501 501 501 LYS LYS A . n A 1 502 VAL 502 502 502 VAL VAL A . n A 1 503 LEU 503 503 503 LEU LEU A . n A 1 504 VAL 504 504 504 VAL VAL A . n A 1 505 LEU 505 505 505 LEU LEU A . n A 1 506 TYR 506 506 506 TYR TYR A . n A 1 507 GLY 507 507 507 GLY GLY A . n A 1 508 GLY 508 508 508 GLY GLY A . n A 1 509 ALA 509 509 509 ALA ALA A . n A 1 510 GLY 510 510 510 GLY GLY A . n A 1 511 GLU 511 511 511 GLU GLU A . n A 1 512 HIS 512 512 512 HIS HIS A . n A 1 513 HIS 513 513 513 HIS HIS A . n A 1 514 GLU 514 514 514 GLU GLU A . n A 1 515 LEU 515 515 515 LEU LEU A . n A 1 516 ALA 516 516 516 ALA ALA A . n A 1 517 ILE 517 517 517 ILE ILE A . n A 1 518 SER 518 518 518 SER SER A . n A 1 519 THR 519 519 519 THR THR A . n A 1 520 LYS 520 520 520 LYS LYS A . n A 1 521 SER 521 521 521 SER SER A . n A 1 522 ASN 522 522 522 ASN ASN A . n A 1 523 VAL 523 523 523 VAL VAL A . n A 1 524 THR 524 524 524 THR THR A . n A 1 525 VAL 525 525 525 VAL VAL A . n A 1 526 ILE 526 526 526 ILE ILE A . n A 1 527 GLU 527 527 527 GLU GLU A . n A 1 528 GLY 528 528 528 GLY GLY A . n A 1 529 SER 529 529 529 SER SER A . n A 1 530 GLU 530 530 530 GLU GLU A . n A 1 531 SER 531 531 531 SER SER A . n A 1 532 GLY 532 532 532 GLY GLY A . n A 1 533 ILE 533 533 533 ILE ILE A . n A 1 534 SER 534 534 534 SER SER A . n A 1 535 SER 535 535 535 SER SER A . n A 1 536 LYS 536 536 536 LYS LYS A . n A 1 537 GLN 537 537 537 GLN GLN A . n A 1 538 THR 538 538 538 THR THR A . n A 1 539 SER 539 539 539 SER SER A . n A 1 540 SER 540 540 540 SER SER A . n A 1 541 SER 541 541 541 SER SER A . n A 1 542 VAL 542 542 542 VAL VAL A . n A 1 543 VAL 543 543 543 VAL VAL A . n A 1 544 VAL 544 544 544 VAL VAL A . n A 1 545 GLY 545 545 545 GLY GLY A . n A 1 546 TRP 546 546 546 TRP TRP A . n A 1 547 ASP 547 547 547 ASP ASP A . n A 1 548 VAL 548 548 548 VAL VAL A . n A 1 549 SER 549 549 549 SER SER A . n A 1 550 THR 550 550 550 THR THR A . n A 1 551 THR 551 551 551 THR THR A . n A 1 552 ARG 552 552 552 ARG ARG A . n A 1 553 ARG 553 553 553 ARG ARG A . n A 1 554 ILE 554 554 554 ILE ILE A . n A 1 555 ILE 555 555 555 ILE ILE A . n A 1 556 GLN 556 556 556 GLN GLN A . n A 1 557 VAL 557 557 557 VAL VAL A . n A 1 558 GLY 558 558 558 GLY GLY A . n A 1 559 ASP 559 559 559 ASP ASP A . n A 1 560 LEU 560 560 560 LEU LEU A . n A 1 561 LYS 561 561 561 LYS LYS A . n A 1 562 ILE 562 562 562 ILE ILE A . n A 1 563 LEU 563 563 563 LEU LEU A . n A 1 564 LEU 564 564 564 LEU LEU A . n A 1 565 LEU 565 565 565 LEU LEU A . n A 1 566 ASP 566 566 566 ASP ASP A . n A 1 567 ARG 567 567 567 ARG ARG A . n A 1 568 ASN 568 568 568 ASN ASN A . n A 1 569 SER 569 569 569 SER SER A . n A 1 570 ALA 570 570 570 ALA ALA A . n A 1 571 TYR 571 571 571 TYR TYR A . n A 1 572 ASN 572 572 572 ASN ASN A . n A 1 573 TYR 573 573 573 TYR TYR A . n A 1 574 TRP 574 574 574 TRP TRP A . n A 1 575 VAL 575 575 575 VAL VAL A . n A 1 576 PRO 576 576 576 PRO PRO A . n A 1 577 GLN 577 577 577 GLN GLN A . n A 1 578 LEU 578 578 578 LEU LEU A . n A 1 579 ALA 579 579 579 ALA ALA A . n A 1 580 THR 580 580 580 THR THR A . n A 1 581 ASP 581 581 581 ASP ASP A . n A 1 582 GLY 582 582 582 GLY GLY A . n A 1 583 THR 583 583 583 THR THR A . n A 1 584 SER 584 584 584 SER SER A . n A 1 585 PRO 585 585 585 PRO PRO A . n A 1 586 GLY 586 586 586 GLY GLY A . n A 1 587 PHE 587 587 587 PHE PHE A . n A 1 588 SER 588 588 588 SER SER A . n A 1 589 THR 589 589 589 THR THR A . n A 1 590 PRO 590 590 590 PRO PRO A . n A 1 591 GLU 591 591 591 GLU GLU A . n A 1 592 LYS 592 592 592 LYS LYS A . n A 1 593 VAL 593 593 593 VAL VAL A . n A 1 594 ALA 594 594 594 ALA ALA A . n A 1 595 SER 595 595 595 SER SER A . n A 1 596 SER 596 596 596 SER SER A . n A 1 597 ILE 597 597 597 ILE ILE A . n A 1 598 ILE 598 598 598 ILE ILE A . n A 1 599 VAL 599 599 599 VAL VAL A . n A 1 600 LYS 600 600 600 LYS LYS A . n A 1 601 ALA 601 601 601 ALA ALA A . n A 1 602 GLY 602 602 602 GLY GLY A . n A 1 603 TYR 603 603 603 TYR TYR A . n A 1 604 LEU 604 604 604 LEU LEU A . n A 1 605 VAL 605 605 605 VAL VAL A . n A 1 606 ARG 606 606 606 ARG ARG A . n A 1 607 THR 607 607 607 THR THR A . n A 1 608 ALA 608 608 608 ALA ALA A . n A 1 609 TYR 609 609 609 TYR TYR A . n A 1 610 LEU 610 610 610 LEU LEU A . n A 1 611 LYS 611 611 611 LYS LYS A . n A 1 612 GLY 612 612 612 GLY GLY A . n A 1 613 SER 613 613 613 SER SER A . n A 1 614 GLY 614 614 614 GLY GLY A . n A 1 615 LEU 615 615 615 LEU LEU A . n A 1 616 TYR 616 616 616 TYR TYR A . n A 1 617 LEU 617 617 617 LEU LEU A . n A 1 618 THR 618 618 618 THR THR A . n A 1 619 ALA 619 619 619 ALA ALA A . n A 1 620 ASP 620 620 620 ASP ASP A . n A 1 621 PHE 621 621 621 PHE PHE A . n A 1 622 ASN 622 622 622 ASN ASN A . n A 1 623 ALA 623 623 623 ALA ALA A . n A 1 624 THR 624 624 624 THR THR A . n A 1 625 THR 625 625 625 THR THR A . n A 1 626 SER 626 626 626 SER SER A . n A 1 627 VAL 627 627 627 VAL VAL A . n A 1 628 GLU 628 628 628 GLU GLU A . n A 1 629 VAL 629 629 629 VAL VAL A . n A 1 630 ILE 630 630 630 ILE ILE A . n A 1 631 GLY 631 631 631 GLY GLY A . n A 1 632 VAL 632 632 632 VAL VAL A . n A 1 633 PRO 633 633 633 PRO PRO A . n A 1 634 SER 634 634 634 SER SER A . n A 1 635 THR 635 635 635 THR THR A . n A 1 636 ALA 636 636 636 ALA ALA A . n A 1 637 LYS 637 637 637 LYS LYS A . n A 1 638 ASN 638 638 638 ASN ASN A . n A 1 639 LEU 639 639 639 LEU LEU A . n A 1 640 PHE 640 640 640 PHE PHE A . n A 1 641 ILE 641 641 641 ILE ILE A . n A 1 642 ASN 642 642 642 ASN ASN A . n A 1 643 GLY 643 643 643 GLY GLY A . n A 1 644 ASP 644 644 644 ASP ASP A . n A 1 645 LYS 645 645 645 LYS LYS A . n A 1 646 THR 646 646 646 THR THR A . n A 1 647 SER 647 647 647 SER SER A . n A 1 648 HIS 648 648 648 HIS HIS A . n A 1 649 THR 649 649 649 THR THR A . n A 1 650 VAL 650 650 650 VAL VAL A . n A 1 651 ASP 651 651 651 ASP ASP A . n A 1 652 LYS 652 652 652 LYS LYS A . n A 1 653 ASN 653 653 653 ASN ASN A . n A 1 654 GLY 654 654 654 GLY GLY A . n A 1 655 ILE 655 655 655 ILE ILE A . n A 1 656 TRP 656 656 656 TRP TRP A . n A 1 657 SER 657 657 657 SER SER A . n A 1 658 ALA 658 658 658 ALA ALA A . n A 1 659 THR 659 659 659 THR THR A . n A 1 660 VAL 660 660 660 VAL VAL A . n A 1 661 ASP 661 661 661 ASP ASP A . n A 1 662 TYR 662 662 662 TYR TYR A . n A 1 663 ASN 663 663 663 ASN ASN A . n A 1 664 ALA 664 664 664 ALA ALA A . n A 1 665 PRO 665 665 665 PRO PRO A . n A 1 666 ASP 666 666 666 ASP ASP A . n A 1 667 ILE 667 667 667 ILE ILE A . n A 1 668 SER 668 668 668 SER SER A . n A 1 669 LEU 669 669 669 LEU LEU A . n A 1 670 PRO 670 670 670 PRO PRO A . n A 1 671 SER 671 671 671 SER SER A . n A 1 672 LEU 672 672 672 LEU LEU A . n A 1 673 LYS 673 673 673 LYS LYS A . n A 1 674 ASP 674 674 674 ASP ASP A . n A 1 675 LEU 675 675 675 LEU LEU A . n A 1 676 ASP 676 676 676 ASP ASP A . n A 1 677 TRP 677 677 677 TRP TRP A . n A 1 678 LYS 678 678 678 LYS LYS A . n A 1 679 TYR 679 679 679 TYR TYR A . n A 1 680 VAL 680 680 680 VAL VAL A . n A 1 681 ASP 681 681 681 ASP ASP A . n A 1 682 THR 682 682 682 THR THR A . n A 1 683 LEU 683 683 683 LEU LEU A . n A 1 684 PRO 684 684 684 PRO PRO A . n A 1 685 GLU 685 685 685 GLU GLU A . n A 1 686 ILE 686 686 686 ILE ILE A . n A 1 687 GLN 687 687 687 GLN GLN A . n A 1 688 SER 688 688 688 SER SER A . n A 1 689 SER 689 689 689 SER SER A . n A 1 690 TYR 690 690 690 TYR TYR A . n A 1 691 ASP 691 691 691 ASP ASP A . n A 1 692 ASP 692 692 692 ASP ASP A . n A 1 693 SER 693 693 693 SER SER A . n A 1 694 LEU 694 694 694 LEU LEU A . n A 1 695 TRP 695 695 695 TRP TRP A . n A 1 696 PRO 696 696 696 PRO PRO A . n A 1 697 ALA 697 697 697 ALA ALA A . n A 1 698 ALA 698 698 698 ALA ALA A . n A 1 699 ASP 699 699 699 ASP ASP A . n A 1 700 LEU 700 700 700 LEU LEU A . n A 1 701 LYS 701 701 701 LYS LYS A . n A 1 702 GLN 702 702 702 GLN GLN A . n A 1 703 THR 703 703 703 THR THR A . n A 1 704 LYS 704 704 704 LYS LYS A . n A 1 705 ASN 705 705 705 ASN ASN A . n A 1 706 THR 706 706 706 THR THR A . n A 1 707 LEU 707 707 707 LEU LEU A . n A 1 708 ARG 708 708 708 ARG ARG A . n A 1 709 SER 709 709 709 SER SER A . n A 1 710 LEU 710 710 710 LEU LEU A . n A 1 711 THR 711 711 711 THR THR A . n A 1 712 THR 712 712 712 THR THR A . n A 1 713 PRO 713 713 713 PRO PRO A . n A 1 714 THR 714 714 714 THR THR A . n A 1 715 SER 715 715 715 SER SER A . n A 1 716 LEU 716 716 716 LEU LEU A . n A 1 717 TYR 717 717 717 TYR TYR A . n A 1 718 SER 718 718 718 SER SER A . n A 1 719 SER 719 719 719 SER SER A . n A 1 720 ASP 720 720 720 ASP ASP A . n A 1 721 TYR 721 721 721 TYR TYR A . n A 1 722 GLY 722 722 722 GLY GLY A . n A 1 723 PHE 723 723 723 PHE PHE A . n A 1 724 HIS 724 724 724 HIS HIS A . n A 1 725 THR 725 725 725 THR THR A . n A 1 726 GLY 726 726 726 GLY GLY A . n A 1 727 TYR 727 727 727 TYR TYR A . n A 1 728 LEU 728 728 728 LEU LEU A . n A 1 729 LEU 729 729 729 LEU LEU A . n A 1 730 TYR 730 730 730 TYR TYR A . n A 1 731 ARG 731 731 731 ARG ARG A . n A 1 732 GLY 732 732 732 GLY GLY A . n A 1 733 HIS 733 733 733 HIS HIS A . n A 1 734 PHE 734 734 734 PHE PHE A . n A 1 735 THR 735 735 735 THR THR A . n A 1 736 ALA 736 736 736 ALA ALA A . n A 1 737 THR 737 737 737 THR THR A . n A 1 738 GLY 738 738 738 GLY GLY A . n A 1 739 ASN 739 739 739 ASN ASN A . n A 1 740 GLU 740 740 740 GLU GLU A . n A 1 741 SER 741 741 741 SER SER A . n A 1 742 THR 742 742 742 THR THR A . n A 1 743 PHE 743 743 743 PHE PHE A . n A 1 744 ALA 744 744 744 ALA ALA A . n A 1 745 ILE 745 745 745 ILE ILE A . n A 1 746 ASP 746 746 746 ASP ASP A . n A 1 747 THR 747 747 747 THR THR A . n A 1 748 GLN 748 748 748 GLN GLN A . n A 1 749 GLY 749 749 749 GLY GLY A . n A 1 750 GLY 750 750 750 GLY GLY A . n A 1 751 SER 751 751 751 SER SER A . n A 1 752 ALA 752 752 752 ALA ALA A . n A 1 753 PHE 753 753 753 PHE PHE A . n A 1 754 GLY 754 754 754 GLY GLY A . n A 1 755 SER 755 755 755 SER SER A . n A 1 756 SER 756 756 756 SER SER A . n A 1 757 VAL 757 757 757 VAL VAL A . n A 1 758 TRP 758 758 758 TRP TRP A . n A 1 759 LEU 759 759 759 LEU LEU A . n A 1 760 ASN 760 760 760 ASN ASN A . n A 1 761 GLY 761 761 761 GLY GLY A . n A 1 762 THR 762 762 762 THR THR A . n A 1 763 TYR 763 763 763 TYR TYR A . n A 1 764 LEU 764 764 764 LEU LEU A . n A 1 765 GLY 765 765 765 GLY GLY A . n A 1 766 SER 766 766 766 SER SER A . n A 1 767 TRP 767 767 767 TRP TRP A . n A 1 768 THR 768 768 768 THR THR A . n A 1 769 GLY 769 769 769 GLY GLY A . n A 1 770 LEU 770 770 770 LEU LEU A . n A 1 771 TYR 771 771 771 TYR TYR A . n A 1 772 ALA 772 772 772 ALA ALA A . n A 1 773 ASN 773 773 773 ASN ASN A . n A 1 774 SER 774 774 774 SER SER A . n A 1 775 ASP 775 775 775 ASP ASP A . n A 1 776 TYR 776 776 776 TYR TYR A . n A 1 777 ASN 777 777 777 ASN ASN A . n A 1 778 ALA 778 778 778 ALA ALA A . n A 1 779 THR 779 779 779 THR THR A . n A 1 780 TYR 780 780 780 TYR TYR A . n A 1 781 ASN 781 781 781 ASN ASN A . n A 1 782 LEU 782 782 782 LEU LEU A . n A 1 783 PRO 783 783 783 PRO PRO A . n A 1 784 GLN 784 784 784 GLN GLN A . n A 1 785 LEU 785 785 785 LEU LEU A . n A 1 786 GLN 786 786 786 GLN GLN A . n A 1 787 ALA 787 787 787 ALA ALA A . n A 1 788 GLY 788 788 788 GLY GLY A . n A 1 789 LYS 789 789 789 LYS LYS A . n A 1 790 THR 790 790 790 THR THR A . n A 1 791 TYR 791 791 791 TYR TYR A . n A 1 792 VAL 792 792 792 VAL VAL A . n A 1 793 ILE 793 793 793 ILE ILE A . n A 1 794 THR 794 794 794 THR THR A . n A 1 795 VAL 795 795 795 VAL VAL A . n A 1 796 VAL 796 796 796 VAL VAL A . n A 1 797 ILE 797 797 797 ILE ILE A . n A 1 798 ASP 798 798 798 ASP ASP A . n A 1 799 ASN 799 799 799 ASN ASN A . n A 1 800 MET 800 800 800 MET MET A . n A 1 801 GLY 801 801 801 GLY GLY A . n A 1 802 LEU 802 802 802 LEU LEU A . n A 1 803 GLU 803 803 803 GLU GLU A . n A 1 804 GLU 804 804 804 GLU GLU A . n A 1 805 ASN 805 805 805 ASN ASN A . n A 1 806 TRP 806 806 806 TRP TRP A . n A 1 807 THR 807 807 807 THR THR A . n A 1 808 VAL 808 808 808 VAL VAL A . n A 1 809 GLY 809 809 809 GLY GLY A . n A 1 810 GLU 810 810 810 GLU GLU A . n A 1 811 ASP 811 811 811 ASP ASP A . n A 1 812 LEU 812 812 812 LEU LEU A . n A 1 813 MET 813 813 813 MET MET A . n A 1 814 LYS 814 814 814 LYS LYS A . n A 1 815 THR 815 815 815 THR THR A . n A 1 816 PRO 816 816 816 PRO PRO A . n A 1 817 ARG 817 817 817 ARG ARG A . n A 1 818 GLY 818 818 818 GLY GLY A . n A 1 819 ILE 819 819 819 ILE ILE A . n A 1 820 LEU 820 820 820 LEU LEU A . n A 1 821 ASN 821 821 821 ASN ASN A . n A 1 822 PHE 822 822 822 PHE PHE A . n A 1 823 LEU 823 823 823 LEU LEU A . n A 1 824 LEU 824 824 824 LEU LEU A . n A 1 825 ALA 825 825 825 ALA ALA A . n A 1 826 GLY 826 826 826 GLY GLY A . n A 1 827 ARG 827 827 827 ARG ARG A . n A 1 828 PRO 828 828 828 PRO PRO A . n A 1 829 SER 829 829 829 SER SER A . n A 1 830 SER 830 830 830 SER SER A . n A 1 831 ALA 831 831 831 ALA ALA A . n A 1 832 ILE 832 832 832 ILE ILE A . n A 1 833 SER 833 833 833 SER SER A . n A 1 834 TRP 834 834 834 TRP TRP A . n A 1 835 LYS 835 835 835 LYS LYS A . n A 1 836 LEU 836 836 836 LEU LEU A . n A 1 837 THR 837 837 837 THR THR A . n A 1 838 GLY 838 838 838 GLY GLY A . n A 1 839 ASN 839 839 839 ASN ASN A . n A 1 840 LEU 840 840 840 LEU LEU A . n A 1 841 GLY 841 841 841 GLY GLY A . n A 1 842 GLY 842 842 842 GLY GLY A . n A 1 843 GLU 843 843 843 GLU GLU A . n A 1 844 ASP 844 844 844 ASP ASP A . n A 1 845 TYR 845 845 845 TYR TYR A . n A 1 846 GLU 846 846 846 GLU GLU A . n A 1 847 ASP 847 847 847 ASP ASP A . n A 1 848 LYS 848 848 848 LYS LYS A . n A 1 849 VAL 849 849 849 VAL VAL A . n A 1 850 ARG 850 850 850 ARG ARG A . n A 1 851 GLY 851 851 851 GLY GLY A . n A 1 852 PRO 852 852 852 PRO PRO A . n A 1 853 LEU 853 853 853 LEU LEU A . n A 1 854 ASN 854 854 854 ASN ASN A . n A 1 855 GLU 855 855 855 GLU GLU A . n A 1 856 GLY 856 856 856 GLY GLY A . n A 1 857 GLY 857 857 857 GLY GLY A . n A 1 858 LEU 858 858 858 LEU LEU A . n A 1 859 TYR 859 859 859 TYR TYR A . n A 1 860 ALA 860 860 860 ALA ALA A . n A 1 861 GLU 861 861 861 GLU GLU A . n A 1 862 ARG 862 862 862 ARG ARG A . n A 1 863 GLN 863 863 863 GLN GLN A . n A 1 864 GLY 864 864 864 GLY GLY A . n A 1 865 PHE 865 865 865 PHE PHE A . n A 1 866 HIS 866 866 866 HIS HIS A . n A 1 867 GLN 867 867 867 GLN GLN A . n A 1 868 PRO 868 868 868 PRO PRO A . n A 1 869 GLU 869 869 869 GLU GLU A . n A 1 870 PRO 870 870 870 PRO PRO A . n A 1 871 PRO 871 871 871 PRO PRO A . n A 1 872 SER 872 872 872 SER SER A . n A 1 873 GLN 873 873 873 GLN GLN A . n A 1 874 ASN 874 874 874 ASN ASN A . n A 1 875 TRP 875 875 875 TRP TRP A . n A 1 876 LYS 876 876 876 LYS LYS A . n A 1 877 SER 877 877 877 SER SER A . n A 1 878 SER 878 878 878 SER SER A . n A 1 879 SER 879 879 879 SER SER A . n A 1 880 PRO 880 880 880 PRO PRO A . n A 1 881 LEU 881 881 881 LEU LEU A . n A 1 882 GLU 882 882 882 GLU GLU A . n A 1 883 GLY 883 883 883 GLY GLY A . n A 1 884 LEU 884 884 884 LEU LEU A . n A 1 885 SER 885 885 885 SER SER A . n A 1 886 GLU 886 886 886 GLU GLU A . n A 1 887 ALA 887 887 887 ALA ALA A . n A 1 888 GLY 888 888 888 GLY GLY A . n A 1 889 ILE 889 889 889 ILE ILE A . n A 1 890 GLY 890 890 890 GLY GLY A . n A 1 891 PHE 891 891 891 PHE PHE A . n A 1 892 TYR 892 892 892 TYR TYR A . n A 1 893 SER 893 893 893 SER SER A . n A 1 894 ALA 894 894 894 ALA ALA A . n A 1 895 SER 895 895 895 SER SER A . n A 1 896 PHE 896 896 896 PHE PHE A . n A 1 897 ASP 897 897 897 ASP ASP A . n A 1 898 LEU 898 898 898 LEU LEU A . n A 1 899 ASP 899 899 899 ASP ASP A . n A 1 900 LEU 900 900 900 LEU LEU A . n A 1 901 PRO 901 901 901 PRO PRO A . n A 1 902 LYS 902 902 902 LYS LYS A . n A 1 903 GLY 903 903 903 GLY GLY A . n A 1 904 TRP 904 904 904 TRP TRP A . n A 1 905 ASP 905 905 905 ASP ASP A . n A 1 906 VAL 906 906 906 VAL VAL A . n A 1 907 PRO 907 907 907 PRO PRO A . n A 1 908 LEU 908 908 908 LEU LEU A . n A 1 909 PHE 909 909 909 PHE PHE A . n A 1 910 LEU 910 910 910 LEU LEU A . n A 1 911 ASN 911 911 911 ASN ASN A . n A 1 912 ILE 912 912 912 ILE ILE A . n A 1 913 GLY 913 913 913 GLY GLY A . n A 1 914 ASN 914 914 914 ASN ASN A . n A 1 915 SER 915 915 915 SER SER A . n A 1 916 THR 916 916 916 THR THR A . n A 1 917 THR 917 917 917 THR THR A . n A 1 918 PRO 918 918 918 PRO PRO A . n A 1 919 SER 919 919 919 SER SER A . n A 1 920 PRO 920 920 920 PRO PRO A . n A 1 921 TYR 921 921 921 TYR TYR A . n A 1 922 ARG 922 922 922 ARG ARG A . n A 1 923 VAL 923 923 923 VAL VAL A . n A 1 924 GLN 924 924 924 GLN GLN A . n A 1 925 VAL 925 925 925 VAL VAL A . n A 1 926 TYR 926 926 926 TYR TYR A . n A 1 927 VAL 927 927 927 VAL VAL A . n A 1 928 ASN 928 928 928 ASN ASN A . n A 1 929 GLY 929 929 929 GLY GLY A . n A 1 930 TYR 930 930 930 TYR TYR A . n A 1 931 GLN 931 931 931 GLN GLN A . n A 1 932 TYR 932 932 932 TYR TYR A . n A 1 933 ALA 933 933 933 ALA ALA A . n A 1 934 LYS 934 934 934 LYS LYS A . n A 1 935 TYR 935 935 935 TYR TYR A . n A 1 936 ILE 936 936 936 ILE ILE A . n A 1 937 SER 937 937 937 SER SER A . n A 1 938 ASN 938 938 938 ASN ASN A . n A 1 939 ILE 939 939 939 ILE ILE A . n A 1 940 GLY 940 940 940 GLY GLY A . n A 1 941 PRO 941 941 941 PRO PRO A . n A 1 942 GLN 942 942 942 GLN GLN A . n A 1 943 THR 943 943 943 THR THR A . n A 1 944 SER 944 944 944 SER SER A . n A 1 945 PHE 945 945 945 PHE PHE A . n A 1 946 PRO 946 946 946 PRO PRO A . n A 1 947 VAL 947 947 947 VAL VAL A . n A 1 948 PRO 948 948 948 PRO PRO A . n A 1 949 GLU 949 949 949 GLU GLU A . n A 1 950 GLY 950 950 950 GLY GLY A . n A 1 951 ILE 951 951 951 ILE ILE A . n A 1 952 LEU 952 952 952 LEU LEU A . n A 1 953 ASN 953 953 953 ASN ASN A . n A 1 954 TYR 954 954 954 TYR TYR A . n A 1 955 ARG 955 955 955 ARG ARG A . n A 1 956 GLY 956 956 956 GLY GLY A . n A 1 957 THR 957 957 957 THR THR A . n A 1 958 ASN 958 958 958 ASN ASN A . n A 1 959 TRP 959 959 959 TRP TRP A . n A 1 960 LEU 960 960 960 LEU LEU A . n A 1 961 ALA 961 961 961 ALA ALA A . n A 1 962 VAL 962 962 962 VAL VAL A . n A 1 963 THR 963 963 963 THR THR A . n A 1 964 LEU 964 964 964 LEU LEU A . n A 1 965 TRP 965 965 965 TRP TRP A . n A 1 966 ALA 966 966 966 ALA ALA A . n A 1 967 LEU 967 967 967 LEU LEU A . n A 1 968 ASP 968 968 968 ASP ASP A . n A 1 969 SER 969 969 969 SER SER A . n A 1 970 ALA 970 970 970 ALA ALA A . n A 1 971 GLY 971 971 971 GLY GLY A . n A 1 972 GLY 972 972 972 GLY GLY A . n A 1 973 LYS 973 973 973 LYS LYS A . n A 1 974 LEU 974 974 974 LEU LEU A . n A 1 975 GLU 975 975 975 GLU GLU A . n A 1 976 SER 976 976 976 SER SER A . n A 1 977 LEU 977 977 977 LEU LEU A . n A 1 978 GLU 978 978 978 GLU GLU A . n A 1 979 LEU 979 979 979 LEU LEU A . n A 1 980 SER 980 980 980 SER SER A . n A 1 981 TYR 981 981 981 TYR TYR A . n A 1 982 THR 982 982 982 THR THR A . n A 1 983 THR 983 983 983 THR THR A . n A 1 984 PRO 984 984 984 PRO PRO A . n A 1 985 VAL 985 985 985 VAL VAL A . n A 1 986 LEU 986 986 986 LEU LEU A . n A 1 987 THR 987 987 987 THR THR A . n A 1 988 ALA 988 988 988 ALA ALA A . n A 1 989 LEU 989 989 989 LEU LEU A . n A 1 990 GLY 990 990 990 GLY GLY A . n A 1 991 GLU 991 991 991 GLU GLU A . n A 1 992 VAL 992 992 992 VAL VAL A . n A 1 993 GLU 993 993 993 GLU GLU A . n A 1 994 SER 994 994 994 SER SER A . n A 1 995 VAL 995 995 995 VAL VAL A . n A 1 996 ASP 996 996 996 ASP ASP A . n A 1 997 GLN 997 997 997 GLN GLN A . n A 1 998 PRO 998 998 998 PRO PRO A . n A 1 999 LYS 999 999 999 LYS LYS A . n A 1 1000 TYR 1000 1000 1000 TYR TYR A . n A 1 1001 LYS 1001 1001 1001 LYS LYS A . n A 1 1002 LYS 1002 1002 1002 LYS LYS A . n A 1 1003 ARG 1003 1003 1003 ARG ARG A . n A 1 1004 LYS 1004 1004 1004 LYS LYS A . n A 1 1005 GLY 1005 1005 1005 GLY GLY A . n A 1 1006 ALA 1006 1006 1006 ALA ALA A . n A 1 1007 TYR 1007 1007 1007 TYR TYR A . n A 1 1008 HIS 1008 1008 1008 HIS HIS A . n A 1 1009 HIS 1009 1009 ? ? ? A . n A 1 1010 HIS 1010 1010 ? ? ? A . n A 1 1011 HIS 1011 1011 ? ? ? A . n A 1 1012 HIS 1012 1012 ? ? ? A . n A 1 1013 HIS 1013 1013 ? ? ? 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 1156 1156 NAG NAG A . C 2 NAG 1 1373 1373 NAG NAG A . D 2 NAG 2 1374 1374 NAG NAG A . E 3 BMA 3 1375 1375 BMA BMA A . F 4 MAN 4 1376 1376 MAN MAN A . G 4 MAN 5 1377 1377 MAN MAN A . H 4 MAN 6 1378 1378 MAN MAN A . I 4 MAN 7 1379 1379 MAN MAN A . J 4 MAN 8 1380 1380 MAN MAN A . K 2 NAG 1 1478 1478 NAG NAG A . L 2 NAG 1 1622 1622 NAG NAG A . M 2 NAG 2 1623 1623 NAG NAG A . N 3 BMA 3 1624 1624 BMA BMA A . O 4 MAN 4 1625 1625 MAN MAN A . P 4 MAN 5 1626 1626 MAN MAN A . Q 4 MAN 6 1627 1627 MAN MAN A . R 4 MAN 7 1628 1628 MAN MAN A . S 4 MAN 8 1629 1629 MAN MAN A . T 4 MAN 9 1630 1630 MAN MAN A . U 4 MAN 10 1631 1631 MAN MAN A . V 2 NAG 1 1739 1739 NAG NAG A . W 2 NAG 1 1760 1760 NAG NAG A . X 2 NAG 1 1777 1777 NAG NAG A . Y 2 NAG 1 1914 1914 NAG NAG A . Z 2 NAG 2 1915 1915 NAG NAG A . AA 3 BMA 3 1916 1916 BMA BMA A . BA 4 MAN 4 1917 1917 MAN MAN A . CA 4 MAN 5 1918 1918 MAN MAN A . DA 4 MAN 6 1919 1919 MAN MAN A . EA 5 CL 1 2001 2001 CL CL A . FA 6 1PE 1 3001 3001 1PE 1PE A . GA 7 GAL 1 4001 4001 GAL GAL A . HA 7 GAL 2 4002 4002 GAL GAL A . IA 8 HOH 1 5001 187 HOH HOH A . IA 8 HOH 2 5002 182 HOH HOH A . IA 8 HOH 3 5003 186 HOH HOH A . IA 8 HOH 4 5004 67 HOH HOH A . IA 8 HOH 5 5005 25 HOH HOH A . IA 8 HOH 6 5006 147 HOH HOH A . IA 8 HOH 7 5007 40 HOH HOH A . IA 8 HOH 8 5008 168 HOH HOH A . IA 8 HOH 9 5009 218 HOH HOH A . IA 8 HOH 10 5010 21 HOH HOH A . IA 8 HOH 11 5011 202 HOH HOH A . IA 8 HOH 12 5012 60 HOH HOH A . IA 8 HOH 13 5013 189 HOH HOH A . IA 8 HOH 14 5014 95 HOH HOH A . IA 8 HOH 15 5015 132 HOH HOH A . IA 8 HOH 16 5016 163 HOH HOH A . IA 8 HOH 17 5017 151 HOH HOH A . IA 8 HOH 18 5018 160 HOH HOH A . IA 8 HOH 19 5019 143 HOH HOH A . IA 8 HOH 20 5020 167 HOH HOH A . IA 8 HOH 21 5021 158 HOH HOH A . IA 8 HOH 22 5022 45 HOH HOH A . IA 8 HOH 23 5023 41 HOH HOH A . IA 8 HOH 24 5024 191 HOH HOH A . IA 8 HOH 25 5025 175 HOH HOH A . IA 8 HOH 26 5026 36 HOH HOH A . IA 8 HOH 27 5027 80 HOH HOH A . IA 8 HOH 28 5028 17 HOH HOH A . IA 8 HOH 29 5029 224 HOH HOH A . IA 8 HOH 30 5030 112 HOH HOH A . IA 8 HOH 31 5031 68 HOH HOH A . IA 8 HOH 32 5032 205 HOH HOH A . IA 8 HOH 33 5033 78 HOH HOH A . IA 8 HOH 34 5034 91 HOH HOH A . IA 8 HOH 35 5035 79 HOH HOH A . IA 8 HOH 36 5036 170 HOH HOH A . IA 8 HOH 37 5037 173 HOH HOH A . IA 8 HOH 38 5038 203 HOH HOH A . IA 8 HOH 39 5039 150 HOH HOH A . IA 8 HOH 40 5040 194 HOH HOH A . IA 8 HOH 41 5041 104 HOH HOH A . IA 8 HOH 42 5042 124 HOH HOH A . IA 8 HOH 43 5043 71 HOH HOH A . IA 8 HOH 44 5044 126 HOH HOH A . IA 8 HOH 45 5045 83 HOH HOH A . IA 8 HOH 46 5046 184 HOH HOH A . IA 8 HOH 47 5047 1 HOH HOH A . IA 8 HOH 48 5048 211 HOH HOH A . IA 8 HOH 49 5049 84 HOH HOH A . IA 8 HOH 50 5050 139 HOH HOH A . IA 8 HOH 51 5051 107 HOH HOH A . IA 8 HOH 52 5052 23 HOH HOH A . IA 8 HOH 53 5053 174 HOH HOH A . IA 8 HOH 54 5054 14 HOH HOH A . IA 8 HOH 55 5055 209 HOH HOH A . IA 8 HOH 56 5056 102 HOH HOH A . IA 8 HOH 57 5057 200 HOH HOH A . IA 8 HOH 58 5058 146 HOH HOH A . IA 8 HOH 59 5059 222 HOH HOH A . IA 8 HOH 60 5060 77 HOH HOH A . IA 8 HOH 61 5061 18 HOH HOH A . IA 8 HOH 62 5062 166 HOH HOH A . IA 8 HOH 63 5063 62 HOH HOH A . IA 8 HOH 64 5064 92 HOH HOH A . IA 8 HOH 65 5065 161 HOH HOH A . IA 8 HOH 66 5066 152 HOH HOH A . IA 8 HOH 67 5067 133 HOH HOH A . IA 8 HOH 68 5068 94 HOH HOH A . IA 8 HOH 69 5069 51 HOH HOH A . IA 8 HOH 70 5070 154 HOH HOH A . IA 8 HOH 71 5071 156 HOH HOH A . IA 8 HOH 72 5072 110 HOH HOH A . IA 8 HOH 73 5073 144 HOH HOH A . IA 8 HOH 74 5074 65 HOH HOH A . IA 8 HOH 75 5075 157 HOH HOH A . IA 8 HOH 76 5076 66 HOH HOH A . IA 8 HOH 77 5077 118 HOH HOH A . IA 8 HOH 78 5078 46 HOH HOH A . IA 8 HOH 79 5079 125 HOH HOH A . IA 8 HOH 80 5080 155 HOH HOH A . IA 8 HOH 81 5081 171 HOH HOH A . IA 8 HOH 82 5082 195 HOH HOH A . IA 8 HOH 83 5083 192 HOH HOH A . IA 8 HOH 84 5084 47 HOH HOH A . IA 8 HOH 85 5085 162 HOH HOH A . IA 8 HOH 86 5086 85 HOH HOH A . IA 8 HOH 87 5087 29 HOH HOH A . IA 8 HOH 88 5088 164 HOH HOH A . IA 8 HOH 89 5089 131 HOH HOH A . IA 8 HOH 90 5090 142 HOH HOH A . IA 8 HOH 91 5091 53 HOH HOH A . IA 8 HOH 92 5092 39 HOH HOH A . IA 8 HOH 93 5093 57 HOH HOH A . IA 8 HOH 94 5094 225 HOH HOH A . IA 8 HOH 95 5095 135 HOH HOH A . IA 8 HOH 96 5096 183 HOH HOH A . IA 8 HOH 97 5097 115 HOH HOH A . IA 8 HOH 98 5098 145 HOH HOH A . IA 8 HOH 99 5099 76 HOH HOH A . IA 8 HOH 100 5100 159 HOH HOH A . IA 8 HOH 101 5101 138 HOH HOH A . IA 8 HOH 102 5102 121 HOH HOH A . IA 8 HOH 103 5103 43 HOH HOH A . IA 8 HOH 104 5104 127 HOH HOH A . IA 8 HOH 105 5105 10 HOH HOH A . IA 8 HOH 106 5106 28 HOH HOH A . IA 8 HOH 107 5107 140 HOH HOH A . IA 8 HOH 108 5108 16 HOH HOH A . IA 8 HOH 109 5109 3 HOH HOH A . IA 8 HOH 110 5110 6 HOH HOH A . IA 8 HOH 111 5111 38 HOH HOH A . IA 8 HOH 112 5112 149 HOH HOH A . IA 8 HOH 113 5113 111 HOH HOH A . IA 8 HOH 114 5114 26 HOH HOH A . IA 8 HOH 115 5115 49 HOH HOH A . IA 8 HOH 116 5116 93 HOH HOH A . IA 8 HOH 117 5117 82 HOH HOH A . IA 8 HOH 118 5118 190 HOH HOH A . IA 8 HOH 119 5119 201 HOH HOH A . IA 8 HOH 120 5120 109 HOH HOH A . IA 8 HOH 121 5121 54 HOH HOH A . IA 8 HOH 122 5122 179 HOH HOH A . IA 8 HOH 123 5123 193 HOH HOH A . IA 8 HOH 124 5124 137 HOH HOH A . IA 8 HOH 125 5125 24 HOH HOH A . IA 8 HOH 126 5126 120 HOH HOH A . IA 8 HOH 127 5127 114 HOH HOH A . IA 8 HOH 128 5128 42 HOH HOH A . IA 8 HOH 129 5129 217 HOH HOH A . IA 8 HOH 130 5130 8 HOH HOH A . IA 8 HOH 131 5131 176 HOH HOH A . IA 8 HOH 132 5132 31 HOH HOH A . IA 8 HOH 133 5133 22 HOH HOH A . IA 8 HOH 134 5134 34 HOH HOH A . IA 8 HOH 135 5135 32 HOH HOH A . IA 8 HOH 136 5136 204 HOH HOH A . IA 8 HOH 137 5137 136 HOH HOH A . IA 8 HOH 138 5138 37 HOH HOH A . IA 8 HOH 139 5139 122 HOH HOH A . IA 8 HOH 140 5140 87 HOH HOH A . IA 8 HOH 141 5141 198 HOH HOH A . IA 8 HOH 142 5142 50 HOH HOH A . IA 8 HOH 143 5143 141 HOH HOH A . IA 8 HOH 144 5144 227 HOH HOH A . IA 8 HOH 145 5145 88 HOH HOH A . IA 8 HOH 146 5146 130 HOH HOH A . IA 8 HOH 147 5147 52 HOH HOH A . IA 8 HOH 148 5148 101 HOH HOH A . IA 8 HOH 149 5149 97 HOH HOH A . IA 8 HOH 150 5150 108 HOH HOH A . IA 8 HOH 151 5151 105 HOH HOH A . IA 8 HOH 152 5152 216 HOH HOH A . IA 8 HOH 153 5153 226 HOH HOH A . IA 8 HOH 154 5154 74 HOH HOH A . IA 8 HOH 155 5155 197 HOH HOH A . IA 8 HOH 156 5156 177 HOH HOH A . IA 8 HOH 157 5157 129 HOH HOH A . IA 8 HOH 158 5158 221 HOH HOH A . IA 8 HOH 159 5159 153 HOH HOH A . IA 8 HOH 160 5160 86 HOH HOH A . IA 8 HOH 161 5161 210 HOH HOH A . IA 8 HOH 162 5162 116 HOH HOH A . IA 8 HOH 163 5163 58 HOH HOH A . IA 8 HOH 164 5164 73 HOH HOH A . IA 8 HOH 165 5165 4 HOH HOH A . IA 8 HOH 166 5166 48 HOH HOH A . IA 8 HOH 167 5167 181 HOH HOH A . IA 8 HOH 168 5168 223 HOH HOH A . IA 8 HOH 169 5169 44 HOH HOH A . IA 8 HOH 170 5170 55 HOH HOH A . IA 8 HOH 171 5171 185 HOH HOH A . IA 8 HOH 172 5172 13 HOH HOH A . IA 8 HOH 173 5173 119 HOH HOH A . IA 8 HOH 174 5174 213 HOH HOH A . IA 8 HOH 175 5175 64 HOH HOH A . IA 8 HOH 176 5176 70 HOH HOH A . IA 8 HOH 177 5177 180 HOH HOH A . IA 8 HOH 178 5178 196 HOH HOH A . IA 8 HOH 179 5179 75 HOH HOH A . IA 8 HOH 180 5180 72 HOH HOH A . IA 8 HOH 181 5181 134 HOH HOH A . IA 8 HOH 182 5182 165 HOH HOH A . IA 8 HOH 183 5183 169 HOH HOH A . IA 8 HOH 184 5184 35 HOH HOH A . IA 8 HOH 185 5185 178 HOH HOH A . IA 8 HOH 186 5186 5 HOH HOH A . IA 8 HOH 187 5187 206 HOH HOH A . IA 8 HOH 188 5188 30 HOH HOH A . IA 8 HOH 189 5189 113 HOH HOH A . IA 8 HOH 190 5190 199 HOH HOH A . IA 8 HOH 191 5191 106 HOH HOH A . IA 8 HOH 192 5192 33 HOH HOH A . IA 8 HOH 193 5193 208 HOH HOH A . IA 8 HOH 194 5194 100 HOH HOH A . IA 8 HOH 195 5195 99 HOH HOH A . IA 8 HOH 196 5196 212 HOH HOH A . IA 8 HOH 197 5197 61 HOH HOH A . IA 8 HOH 198 5198 228 HOH HOH A . IA 8 HOH 199 5199 56 HOH HOH A . IA 8 HOH 200 5200 98 HOH HOH A . IA 8 HOH 201 5201 2 HOH HOH A . IA 8 HOH 202 5202 214 HOH HOH A . IA 8 HOH 203 5203 59 HOH HOH A . IA 8 HOH 204 5204 148 HOH HOH A . IA 8 HOH 205 5205 89 HOH HOH A . IA 8 HOH 206 5206 96 HOH HOH A . IA 8 HOH 207 5207 188 HOH HOH A . IA 8 HOH 208 5208 103 HOH HOH A . IA 8 HOH 209 5209 20 HOH HOH A . IA 8 HOH 210 5210 7 HOH HOH A . IA 8 HOH 211 5211 9 HOH HOH A . IA 8 HOH 212 5212 220 HOH HOH A . IA 8 HOH 213 5213 15 HOH HOH A . IA 8 HOH 214 5214 123 HOH HOH A . IA 8 HOH 215 5215 19 HOH HOH A . IA 8 HOH 216 5216 11 HOH HOH A . IA 8 HOH 217 5217 219 HOH HOH A . IA 8 HOH 218 5218 81 HOH HOH A . IA 8 HOH 219 5219 172 HOH HOH A . IA 8 HOH 220 5220 27 HOH HOH A . IA 8 HOH 221 5221 128 HOH HOH A . IA 8 HOH 222 5222 215 HOH HOH A . IA 8 HOH 223 5223 69 HOH HOH A . IA 8 HOH 224 5224 207 HOH HOH A . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _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,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 9840 ? 1 MORE 111 ? 1 'SSA (A^2)' 32920 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2017-04-19 2 'Structure model' 1 1 2017-06-28 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 2 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category citation # loop_ _pdbx_audit_revision_item.ordinal _pdbx_audit_revision_item.revision_ordinal _pdbx_audit_revision_item.data_content_type _pdbx_audit_revision_item.item 1 2 'Structure model' '_citation.journal_volume' 2 2 'Structure model' '_citation.page_first' 3 2 'Structure model' '_citation.page_last' # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? refinement ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0049 1 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS ? ? ? . 2 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.5.21 3 ? phasing ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? 11.4.04 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 OE2 A GLU 861 ? ? OH A TYR 926 ? ? 2.18 2 1 O2 A MAN 1376 ? ? O5 A MAN 1377 ? ? 2.18 # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 CD _pdbx_validate_rmsd_bond.auth_asym_id_1 A _pdbx_validate_rmsd_bond.auth_comp_id_1 GLU _pdbx_validate_rmsd_bond.auth_seq_id_1 198 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 OE2 _pdbx_validate_rmsd_bond.auth_asym_id_2 A _pdbx_validate_rmsd_bond.auth_comp_id_2 GLU _pdbx_validate_rmsd_bond.auth_seq_id_2 198 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.179 _pdbx_validate_rmsd_bond.bond_target_value 1.252 _pdbx_validate_rmsd_bond.bond_deviation -0.073 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.011 _pdbx_validate_rmsd_bond.linker_flag 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 49 ? ? -141.14 -158.41 2 1 LEU A 72 ? ? -157.01 77.13 3 1 PRO A 73 ? ? -90.80 51.12 4 1 GLU A 103 ? ? -141.23 55.10 5 1 ASN A 140 ? ? 60.70 -100.00 6 1 GLU A 198 ? ? 64.46 -166.31 7 1 THR A 202 ? ? -139.24 -36.79 8 1 ASN A 268 ? ? -119.73 72.07 9 1 SER A 289 ? ? -162.84 61.48 10 1 LEU A 319 ? ? -97.25 54.42 11 1 TYR A 359 ? ? -116.43 -164.00 12 1 ASN A 422 ? ? -88.21 -104.15 13 1 ALA A 451 ? ? -95.66 30.90 14 1 SER A 480 ? ? 39.57 64.03 15 1 ASP A 499 ? ? -108.67 60.26 16 1 ALA A 601 ? ? -150.50 -132.46 17 1 ASN A 760 ? ? 47.13 -111.39 18 1 ASP A 899 ? ? -142.20 58.42 19 1 ASN A 914 ? ? -149.66 50.41 20 1 LEU A 967 ? ? -94.10 46.94 21 1 THR A 983 ? ? -38.87 115.48 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A MET 1 ? A MET 1 2 1 Y 1 A LYS 2 ? A LYS 2 3 1 Y 1 A LEU 3 ? A LEU 3 4 1 Y 1 A SER 4 ? A SER 4 5 1 Y 1 A SER 5 ? A SER 5 6 1 Y 1 A ALA 6 ? A ALA 6 7 1 Y 1 A CYS 7 ? A CYS 7 8 1 Y 1 A ALA 8 ? A ALA 8 9 1 Y 1 A ILE 9 ? A ILE 9 10 1 Y 1 A ALA 10 ? A ALA 10 11 1 Y 1 A LEU 11 ? A LEU 11 12 1 Y 1 A LEU 12 ? A LEU 12 13 1 Y 1 A ALA 13 ? A ALA 13 14 1 Y 1 A ALA 14 ? A ALA 14 15 1 Y 1 A GLN 15 ? A GLN 15 16 1 Y 1 A ALA 16 ? A ALA 16 17 1 Y 1 A ALA 17 ? A ALA 17 18 1 Y 1 A GLY 18 ? A GLY 18 19 1 Y 1 A ALA 19 ? A ALA 19 20 1 Y 1 A SER 20 ? A SER 20 21 1 Y 1 A ILE 21 ? A ILE 21 22 1 Y 1 A LYS 22 ? A LYS 22 23 1 Y 1 A HIS 23 ? A HIS 23 24 1 Y 1 A ARG 24 ? A ARG 24 25 1 Y 1 A ILE 25 ? A ILE 25 26 1 Y 1 A ASN 26 ? A ASN 26 27 1 Y 1 A GLY 27 ? A GLY 27 28 1 Y 1 A PHE 28 ? A PHE 28 29 1 Y 1 A THR 29 ? A THR 29 30 1 Y 1 A LEU 30 ? A LEU 30 31 1 Y 1 A THR 31 ? A THR 31 32 1 Y 1 A GLU 32 ? A GLU 32 33 1 Y 1 A HIS 33 ? A HIS 33 34 1 Y 1 A SER 34 ? A SER 34 35 1 Y 1 A ASP 35 ? A ASP 35 36 1 Y 1 A PRO 36 ? A PRO 36 37 1 Y 1 A ALA 37 ? A ALA 37 38 1 Y 1 A LYS 38 ? A LYS 38 39 1 Y 1 A ARG 39 ? A ARG 39 40 1 Y 1 A GLU 40 ? A GLU 40 41 1 Y 1 A HIS 1009 ? A HIS 1009 42 1 Y 1 A HIS 1010 ? A HIS 1010 43 1 Y 1 A HIS 1011 ? A HIS 1011 44 1 Y 1 A HIS 1012 ? A HIS 1012 45 1 Y 1 A HIS 1013 ? A HIS 1013 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 ALPHA-D-MANNOSE MAN 5 'CHLORIDE ION' CL 6 'PENTAETHYLENE GLYCOL' 1PE 7 BETA-D-GALACTOSE GAL 8 water HOH #